ID A0AJD2_LISW6 Unreviewed; 617 AA. AC A0AJD2; DT 28-NOV-2006, integrated into UniProtKB/TrEMBL. DT 28-NOV-2006, sequence version 1. DT 27-MAY-2015, entry version 61. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=lwe1696 {ECO:0000313|EMBL:CAK21114.1}; OS Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / OS SLCC5334). OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=386043 {ECO:0000313|EMBL:CAK21114.1, ECO:0000313|Proteomes:UP000000779}; RN [1] {ECO:0000313|EMBL:CAK21114.1, ECO:0000313|Proteomes:UP000000779} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35897 / DSM 20650 / SLCC5334 RC {ECO:0000313|Proteomes:UP000000779}; 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., Karst U., Goesmann A., Bekel T., RA Bartels D., Kaiser O., Meyer F., Ohler A.P., 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; CAK21114.1; -; Genomic_DNA. DR RefSeq; WP_011702478.1; NC_008555.1. DR RefSeq; YP_849893.1; NC_008555.1. DR ProteinModelPortal; A0AJD2; -. DR STRING; 386043.lwe1696; -. DR EnsemblBacteria; CAK21114; CAK21114; lwe1696. DR KEGG; lwe:lwe1696; -. DR PATRIC; 20330543; VBILisWel39304_1706. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; LWEL386043:GI5X-1718-MONOMER; -. DR Proteomes; UP000000779; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000779}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 617 AA; 68714 MW; 23B122505EC143C7 CRC64; MNLRKDLSEK VLIADGAMGT LLYSYGVDRS FEELNLSHPE DIVAIHKAYI GAGADIIQTN TYGANYIKLA RYGLEDEVKR INQAAIRLAK EAARGTGTYI FGTIGGINGA VDARLPAAPL EEIKRSFREQ LYCFLLDGVD AILLETYYDL DELKTVLKIL RETTDLPVVA NVSMHEPGIL QNGKKLPDAL EELITLGADV VGINCRLGPY HMARALETVP LYEKAYLAVY PNASLPEMQD GKVIYQSDTD YFAHYGEVFR QEGARIIGGC CGTTPDHIRA LRQGLETTKP ILEKEVRPIL ELVPEEVVDE EAGERLLDKV KERLTILVEL DPPRTFDTTK FFEGAEALNN AGVDAITISD NSLATPRISN MALASILKHE YGIKPLIHLT TRDHNLVGMH SHVMGFHKLG LHDVLAITGD PTKVGDFPGA SSVFDLRSVE LVQLIKKFND GISYTGKSLK EKARFHVGAA FNPNALNLEK AVRLIERKVE YGADYIITQP IYDVNKAVLL KEALQKANID VPLFIGVMPL LSSRNAEFLH NEVPGIRLTE EVRERMREAE EHGYANEEGM AIARELIDAI CEHFQGIYII TPFLRYDLSV ELAKYIQKKQ QVEIISK // ID A0APQ0_DROME Unreviewed; 331 AA. AC A0APQ0; DT 28-NOV-2006, integrated into UniProtKB/TrEMBL. DT 28-NOV-2006, sequence version 1. DT 27-MAY-2015, entry version 31. DE SubName: Full=CG10623 protein {ECO:0000313|EMBL:CAL25772.1}; GN Name=CG10623 {ECO:0000313|EMBL:CAL25772.1}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000313|EMBL:CAL25772.1}; RN [1] {ECO:0000313|EMBL:CAL25772.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ZBMEL82 {ECO:0000313|EMBL:CAL25772.1}; RX PubMed=16951084; DOI=10.1534/genetics.106.058008; RA Proeschel M., Zhang Z., Parsch J.; RT "Widespread adaptive evolution of Drosophila genes with sex-biased RT expression."; RL Genetics 174:893-900(2006). RN [2] {ECO:0000313|EMBL:CAL25772.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ZBMEL82 {ECO:0000313|EMBL:CAL25772.1}; RA Proeschel M., Zhang Z., Parsch J.; RT "Widespread adaptive evolution of Drosophila genes with sex-biased RT expression."; RL Genetics 0:0-0(0). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM294638; CAL25772.1; -; Genomic_DNA. DR ProteinModelPortal; A0APQ0; -. DR PaxDb; A0APQ0; -. DR PRIDE; A0APQ0; -. DR eggNOG; COG2040; -. DR Bgee; A0APQ0; -. DR ExpressionAtlas; A0APQ0; differential. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 331 AA; 36682 MW; 9BA713AE7BB95F26 CRC64; MEVNQKWNWD TKPILVKCGG FSSQLAKNVS EKVDGDPLWG SRFDATNPEA VIQTHLDFLR NGADIILTNT YQSSVEGFVK YLGVTRERGV ELIQKSVQLA KQAKEQYLSE IGSEAESALP LIMGSIGPYG AYLHDGSEYT GNYADKMSKE ELRAWHKTRI EICLAAGVDG LALETLPCLM EAEAVTELVL DKFPDAKFWV SLQCMDEKHM ASGENFAEAA LSLWRLVQSR KAENRLLGIG LNCVNPLFVT PLLSSLTKVA GSDRIPLVVY SNRGEIYDVE QGDWTGTGEE VVKFVPEWIQ LGVRIVGGCC RVYPTDVLAI RKYVDGLNIK P // ID A0APQ1_DROME Unreviewed; 331 AA. AC A0APQ1; DT 28-NOV-2006, integrated into UniProtKB/TrEMBL. DT 28-NOV-2006, sequence version 1. DT 27-MAY-2015, entry version 35. DE SubName: Full=CG10623 protein {ECO:0000313|EMBL:CAL25773.1}; GN Name=CG10623 {ECO:0000313|EMBL:CAL25773.1}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000313|EMBL:CAL25773.1}; RN [1] {ECO:0000313|EMBL:CAL25773.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ZBMEL377 {ECO:0000313|EMBL:CAL25781.1}, and RC ZBMEL84 {ECO:0000313|EMBL:CAL25773.1}; RX PubMed=16951084; DOI=10.1534/genetics.106.058008; RA Proeschel M., Zhang Z., Parsch J.; RT "Widespread adaptive evolution of Drosophila genes with sex-biased RT expression."; RL Genetics 174:893-900(2006). RN [2] {ECO:0000313|EMBL:CAL25773.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ZBMEL377 {ECO:0000313|EMBL:CAL25781.1}, and RC ZBMEL84 {ECO:0000313|EMBL:CAL25773.1}; RA Proeschel M., Zhang Z., Parsch J.; RT "Widespread adaptive evolution of Drosophila genes with sex-biased RT expression."; RL Genetics 0:0-0(0). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM294639; CAL25773.1; -; Genomic_DNA. DR EMBL; AM294647; CAL25781.1; -; Genomic_DNA. DR ProteinModelPortal; A0APQ1; -. DR PRIDE; A0APQ1; -. DR Bgee; A0APQ1; -. DR ExpressionAtlas; A0APQ1; differential. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 331 AA; 36664 MW; CA56E2AD2EEABFFC CRC64; MEVNQKWNWD TKPILVKCGG FSSQLAKNVT EKVDGDPLWG SRFDATNPEA VIQTHLDFLR NGADIILTNT YQSSVEGFVK YLGVTRERGV ELIQKSVQLA KQAKEQYLSE IGSEAESALP LIMGSIGPYG AYLHDGSEYT GNYADKLSKE ELRAWHKTRI EICLAAGVDG LALETLPCLM EAEAVTELVL DNFPDAKFWV SLQCMDEKHM ASGENFAEAA LSLWRLVQSR KAENRLLGIG LNCVNPLFVT PLLSSLTKVA GSDRIPLVVY SNRGEIYDVE QGDWTGTGEE VVKFVPEWIQ LGVRIVGGCC RVYPTDVLAI RKYVDGLNIK P // ID A0APQ2_DROME Unreviewed; 331 AA. AC A0APQ2; DT 28-NOV-2006, integrated into UniProtKB/TrEMBL. DT 28-NOV-2006, sequence version 1. DT 27-MAY-2015, entry version 38. DE SubName: Full=CG10623 protein {ECO:0000313|EMBL:CAL25774.1}; DE SubName: Full=CG10623-PA {ECO:0000313|EMBL:CAR93710.1}; GN Name=CG10623 {ECO:0000313|EMBL:CAL25774.1}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000313|EMBL:CAL25774.1}; RN [1] {ECO:0000313|EMBL:CAL25774.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ZBMEL145 {ECO:0000313|EMBL:CAL25776.1}, RC ZBMEL186 {ECO:0000313|EMBL:CAL25778.1}, and RC ZBMEL95 {ECO:0000313|EMBL:CAL25774.1}; RX PubMed=16951084; DOI=10.1534/genetics.106.058008; RA Proeschel M., Zhang Z., Parsch J.; RT "Widespread adaptive evolution of Drosophila genes with sex-biased RT expression."; RL Genetics 174:893-900(2006). RN [2] {ECO:0000313|EMBL:CAR93710.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MEL01 {ECO:0000313|EMBL:CAR93710.1}, and RC MEL19 {ECO:0000313|EMBL:CAR93719.1}; RX PubMed=19126864; DOI=10.1093/molbev/msn297; RA Parsch J., Zhang Z., Baines J.F.; RT "The influence of demography and weak selection on the McDonald- RT Kreitman test: an empirical study in Drosophila."; RL Mol. Biol. Evol. 26:691-698(2009). RN [3] {ECO:0000313|EMBL:CAL25774.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ZBMEL145 {ECO:0000313|EMBL:CAL25776.1}, RC ZBMEL186 {ECO:0000313|EMBL:CAL25778.1}, and RC ZBMEL95 {ECO:0000313|EMBL:CAL25774.1}; RA Proeschel M., Zhang Z., Parsch J.; RT "Widespread adaptive evolution of Drosophila genes with sex-biased RT expression."; RL Genetics 0:0-0(0). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM294640; CAL25774.1; -; Genomic_DNA. DR EMBL; AM294642; CAL25776.1; -; Genomic_DNA. DR EMBL; AM294644; CAL25778.1; -; Genomic_DNA. DR EMBL; FM245784; CAR93710.1; -; Genomic_DNA. DR EMBL; FM245793; CAR93719.1; -; Genomic_DNA. DR ProteinModelPortal; A0APQ2; -. DR PRIDE; A0APQ2; -. DR Bgee; A0APQ2; -. DR ExpressionAtlas; A0APQ2; differential. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 331 AA; 36696 MW; CAE154AE79EFEEFD CRC64; MEVNQKWNWD TKPILVKCGG FSSQLAKNVT EKVDGDPLWG SRFDATNPEA VIQTHLDFLR NGADIILTNT YQSSVEGFVK YLGVTRERGV ELIQKSVQLA KQAKEQYLSE IGSEAESALP LIMGSIGPYG AYLHDGSEYT GNYADKMSKE ELRAWHKTRI EICLAAGVDG LALETLPCLM EAEAVTELVL DKFPDAKFWV SLQCMDEKHM ASGENFAEAA LSLWRLVQSR KAENRLLGIG LNCVNPLFVT PLLSSLTKVA GSDRIPLVVY SNRGEIYDVE QGDWTGTGEE VVKFVPEWIQ LGVRIVGGCC RVYPTDVLAI RKYVDGLNIK P // ID A0APR0_DROME Unreviewed; 331 AA. AC A0APR0; DT 28-NOV-2006, integrated into UniProtKB/TrEMBL. DT 28-NOV-2006, sequence version 1. DT 27-MAY-2015, entry version 30. DE SubName: Full=CG10623 protein {ECO:0000313|EMBL:CAL25782.1}; GN Name=CG10623 {ECO:0000313|EMBL:CAL25782.1}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000313|EMBL:CAL25782.1}; RN [1] {ECO:0000313|EMBL:CAL25782.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ZBMEL384 {ECO:0000313|EMBL:CAL25782.1}; RX PubMed=16951084; DOI=10.1534/genetics.106.058008; RA Proeschel M., Zhang Z., Parsch J.; RT "Widespread adaptive evolution of Drosophila genes with sex-biased RT expression."; RL Genetics 174:893-900(2006). RN [2] {ECO:0000313|EMBL:CAL25782.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ZBMEL384 {ECO:0000313|EMBL:CAL25782.1}; RA Proeschel M., Zhang Z., Parsch J.; RT "Widespread adaptive evolution of Drosophila genes with sex-biased RT expression."; RL Genetics 0:0-0(0). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM294648; CAL25782.1; -; Genomic_DNA. DR ProteinModelPortal; A0APR0; -. DR PRIDE; A0APR0; -. DR Bgee; A0APR0; -. DR ExpressionAtlas; A0APR0; differential. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 331 AA; 36697 MW; 27B35D56DE5CDADD CRC64; MEVNQEWNWD TKPILVKCGG FSSQLAKNVT EKVDGDPLWG SRFDATNPEA VIQTHLDFLR NGADIILTNT YQSSVEGFVK YLGVTRERGV ELIQKSVQLA KQAKEQYLSE IGSEAESALP LIMGSIGPYG AYLHDGSEYT GNYADKMSKE ELRAWHKTRI EICLAAGVDG LALETLPCLM EAEAVTELVL DKFPDAKFWV SLQCMDEKHM ASGENFAEAA LSLWRLVQSR KAENRLLGIG LNCVNPLFVT PLLSSLTKVA GSDRIPLVVY SNRGEIYDVE QGDWTGTGEE VVKFVPEWIQ LGVRIVGGCC RVYPTDVLAI RKYVDGLNIK P // ID A0APR1_DROME Unreviewed; 331 AA. AC A0APR1; DT 28-NOV-2006, integrated into UniProtKB/TrEMBL. DT 28-NOV-2006, sequence version 1. DT 27-MAY-2015, entry version 30. DE SubName: Full=CG10623 protein {ECO:0000313|EMBL:CAL25783.1}; GN Name=CG10623 {ECO:0000313|EMBL:CAL25783.1}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000313|EMBL:CAL25783.1}; RN [1] {ECO:0000313|EMBL:CAL25783.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ZBMEL398 {ECO:0000313|EMBL:CAL25783.1}; RX PubMed=16951084; DOI=10.1534/genetics.106.058008; RA Proeschel M., Zhang Z., Parsch J.; RT "Widespread adaptive evolution of Drosophila genes with sex-biased RT expression."; RL Genetics 174:893-900(2006). RN [2] {ECO:0000313|EMBL:CAL25783.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ZBMEL398 {ECO:0000313|EMBL:CAL25783.1}; RA Proeschel M., Zhang Z., Parsch J.; RT "Widespread adaptive evolution of Drosophila genes with sex-biased RT expression."; RL Genetics 0:0-0(0). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM294649; CAL25783.1; -; Genomic_DNA. DR ProteinModelPortal; A0APR1; -. DR PRIDE; A0APR1; -. DR Bgee; A0APR1; -. DR ExpressionAtlas; A0APR1; differential. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 331 AA; 36691 MW; 0883D21C9E5BBFE5 CRC64; MEVNQKWNWD TKPILVKCGG FSSQLAKNVT EKVDGDPLWG SRFDATNPEA VIQTHLDFLR NGADIILTNT YQSSVEGFVK YLGVTRERGV ELIQKSVQLA KQAKEQYLSE IGSEAESALP LIMGSIGPYG AYLHDGSEYT GNYADKMSKE ELRAWHKTRI EICLAAGVDG LALETLPCLM EAEAVTELVL DNFPDAKFWV SLQCMDEKHM ASGENFAEAA LSLWRLVQSR KAENRLLGIG LNCVNPLFVT PLLSSLTKVA GSDRIPLVVY SNRGEIYDVE QGDWTGTGEE VVKFVPEWIH LGVRIVGGCC RVYPTDVLAI RKYVDGLNIK P // ID A0K132_ARTS2 Unreviewed; 1216 AA. AC A0K132; DT 12-DEC-2006, integrated into UniProtKB/TrEMBL. DT 12-DEC-2006, sequence version 1. DT 27-MAY-2015, entry version 75. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABK05002.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABK05002.1}; GN OrderedLocusNames=Arth_3627 {ECO:0000313|EMBL:ABK05002.1}; OS Arthrobacter sp. (strain FB24). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Micrococcaceae; Arthrobacter. OX NCBI_TaxID=290399 {ECO:0000313|EMBL:ABK05002.1, ECO:0000313|Proteomes:UP000000754}; RN [1] {ECO:0000313|EMBL:ABK05002.1, ECO:0000313|Proteomes:UP000000754} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FB24 {ECO:0000313|EMBL:ABK05002.1, RC ECO:0000313|Proteomes:UP000000754}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000454; ABK05002.1; -; Genomic_DNA. DR RefSeq; WP_011693452.1; NC_008541.1. DR RefSeq; YP_833102.1; NC_008541.1. DR ProteinModelPortal; A0K132; -. DR STRING; 290399.Arth_3627; -. DR EnsemblBacteria; ABK05002; ABK05002; Arth_3627. DR KEGG; art:Arth_3627; -. DR PATRIC; 21002747; VBIArtSp72239_4051. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; ASP290399:GHIF-3702-MONOMER; -. DR Proteomes; UP000000754; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000754}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABK05002.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000754}; KW Transferase {ECO:0000313|EMBL:ABK05002.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 240 240 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 770 770 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1216 AA; 131567 MW; C9E78551435876F2 CRC64; MPRFALDIES VPRPVRAQEL LDAVNTRVVI ADGAMGTMLQ GRELSLEKDF LGLEGCNEIL NDTRPDVLAD IHDAYFATGI DAVETNTFGA NWSNLSDYGI DDRIEELARK GAAIARERAE AAEKTDGRMR WVLGSMGPGT KLPSLGHTTY DYLKQTFALQ AEGLIDGGAD AFLIETSQDL LQTKAAVNGC KQAIVTRGIR LPIFVEVTVE TTGTMLMGSE IGAALTALEP LGVDAIGLNC ATGPDEMSEH LRHLSKQSSV AIACMPNAGL PVLGPNGAHY PLSPSELATA HEQFVREFGL GLVGGCCGTT PEHMAAVVER LAPLRASAAV TSGGRGADGS RVPTEREAGI ASLYHHVPFD QESAYLAIGE RTNANGSKAF RQAMLEERWD DCVDIAREQV RVGAHLLDVC IDYVGRDGVA DIKEIVSRFA SASTLPLVID STEPPVLQAG LELIGGRPVV NSVNYEDGDG PNSRFARIMP LVKEHGTAVI ALTIDEQGQA RTTEGKVAIA SRLVDALVGE WGMRVEDIIV DALTFPVATG QEETRRDGIE TIEAIRQITT KYPGINTTLG VSNVSFGLNP AARVVLNSVF LHEAVQAGLS SGIIDAAKIV PLASLPEEQR KVALDLVYDR REYDADGNVT YDPLAIMLDL FAGVDTAALK DQRAAELAAL PTGERLQRRI IDGEGKGLEA DLDLARSEGM TPLGIINDQL LEGMKVVGER FGAGEMQLPF VLQSAEVMKN AVALLEPHME KSDSSGKGTM VIATVRGDVH DIGKNLVDII LTNNGYKVVN IGIKQGIAEI MAAAEEHNAD VIGMSGLLVK STVVMKENLA ELQSRGLAKK WPIILGGAAL TRAYVEQDLA EQFEGTVRYA KDAFEGLALM EPLVQVARGA DPDAVGLPPL KKRIHKGGPK FTVTEPEAMP GRSDVASDNL VPSPPFWGTR IVRGVALHDY AALLDERATF MGQWGLKPGR GDDGASYEEL VELEGRPRLR YWLDRILAEG MLDASVAYGY FPVVSEGEQV VVLHHGEDHD GVLGTPGLLA PDGGSGGPIG TERLRFDFPR QRRDRHLCLA DFVRSRESGQ VDVLPVQLVT AGSKIDEVTS ELFKGNHYRD YYELNGLVMQ LTEALAEFWH ARIRSELGFA AEEPKDKAGY FKLDYRGARF SLGYPACPDM EDRRKVTELL KPERMGVVLS DELMLHPEQS TDAFVFHHPE AKYFKV // ID A0KAY7_BURCH Unreviewed; 355 AA. AC A0KAY7; DT 12-DEC-2006, integrated into UniProtKB/TrEMBL. DT 12-DEC-2006, sequence version 1. DT 27-MAY-2015, entry version 53. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABK09664.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABK09664.1}; GN OrderedLocusNames=Bcen2424_2916 {ECO:0000313|EMBL:ABK09664.1}; OS Burkholderia cenocepacia (strain HI2424). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=331272 {ECO:0000313|EMBL:ABK09664.1, ECO:0000313|Proteomes:UP000000776}; RN [1] {ECO:0000313|Proteomes:UP000000776} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HI2424 {ECO:0000313|Proteomes:UP000000776}; 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 ----------------------------------------------------------------------- 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; ABK09664.1; -; Genomic_DNA. DR RefSeq; WP_011546326.1; NC_008542.1. DR RefSeq; YP_836557.1; NC_008542.1. DR STRING; 331272.Bcen2424_2916; -. DR EnsemblBacteria; ABK09664; ABK09664; Bcen2424_2916. DR KEGG; bch:Bcen2424_2916; -. DR PATRIC; 19063305; VBIBurCen15205_2987. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; BCEN331272:GHR7-2987-MONOMER; -. DR Proteomes; UP000000776; Chromosome 1. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000776}; KW Methyltransferase {ECO:0000313|EMBL:ABK09664.1}; KW Transferase {ECO:0000313|EMBL:ABK09664.1}. SQ SEQUENCE 355 AA; 38251 MW; 7BD91FA896F82429 CRC64; MSAIPLAASV PLDARYTRGA ALPALLKSRI LILDGAMGTM IQRYKLDEAA YRGERFKDFP RDIKGNNELL SLTQPQIIRE IHDQYFAAGA DIVETNTFGA TTVAQADYGM EDLVVEMNVA SAKLARESAA KYATPDKPRF VAGAIGPTPK TASISPDVND PGARNVTFDE LRTSYYQQAK ALLDGGVDLF LVETIFDTLN AKAALFALDE LFEDTGERLP IMISGTVTDA SGRILSGQTV EAFWNSLRHA KPLTFGLNCA LGAALMRPYI AELAKLCDTY VSCYPNAGLP NPMSDTGFDE TPDVTSGLLK EFAQAGLVNL AGGCCGTTPE HIAEIAKALA DVKPRRWPNQ YSDNA // ID A0KFD9_AERHH Unreviewed; 1227 AA. AC A0KFD9; DT 12-DEC-2006, integrated into UniProtKB/TrEMBL. DT 12-DEC-2006, sequence version 1. DT 27-MAY-2015, entry version 69. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABK39635.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABK39635.1}; GN Name=metH {ECO:0000313|EMBL:ABK39635.1}; GN OrderedLocusNames=AHA_0432 {ECO:0000313|EMBL:ABK39635.1}; OS Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / OS JCM 1027 / KCTC 2358 / NCIMB 9240). OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales; OC Aeromonadaceae; Aeromonas. OX NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK39635.1, ECO:0000313|Proteomes:UP000000756}; RN [1] {ECO:0000313|EMBL:ABK39635.1, ECO:0000313|Proteomes:UP000000756} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240 RC {ECO:0000313|Proteomes:UP000000756}; 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.H., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000462; ABK39635.1; -; Genomic_DNA. DR RefSeq; WP_011704406.1; NC_008570.1. DR RefSeq; YP_854961.1; NC_008570.1. DR ProteinModelPortal; A0KFD9; -. DR SMR; A0KFD9; 657-1226. DR STRING; 380703.AHA_0432; -. DR EnsemblBacteria; ABK39635; ABK39635; AHA_0432. DR GeneID; 4488402; -. DR KEGG; aha:AHA_0432; -. DR PATRIC; 20778352; VBIAerHyd135212_0421. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; AHYD380703:GH2M-433-MONOMER; -. DR Proteomes; UP000000756; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000756}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABK39635.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000756}; KW Transferase {ECO:0000313|EMBL:ABK39635.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 251 251 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 315 315 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 762 762 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135105 MW; 87996AA086223C8D CRC64; MSNKKSDVTN KLEACLKERI LIIDGAMGTM IQGYKLGEAD YRGARFADWH TDIKGNNDLL VLTRPAVIRE IHEQYCAAGA DILETNTFNA TRIAMADYEM EEFSAEINCE AARLARAVAD EWTAKEPHKP RFVAGVLGPT NRTASISPDV NDPGKRNVTY DQLVAAYTES THALIEGGAD IILIETIFDT LNAKAAAFAV EGVFEALGYS LPVMISGTIT DASGRTLSGQ TTEAFYHSLR HVKPVSFGLN CALGPDELRQ YVEELSRISE THVSAHPNAG LPNAFGEYDL DAVEMAEHIR EWAASGFLNL VGGCCGTTPT HIRAMADAVA GIKPRALPEL PVACRLSGLE PLIITPESMF VNVGERTNVT GSAKFKRLIK EGLYDEALDV AKQQVESGAQ IIDINMDEGM LDAEAAMVRF LNLIAGEPDI ARVPVMIDSS KWEVLEAGLK CVQGKPVVNS ISMKEGEEKF IQQARLLRRY GAAVIVMAFD EVGQADTRAR KFEICQRAYR ILVDRVGFPP EDIIFDPNIF AVATGIDEHN NYAVDFIDAV KDIKQNLPHA MISGGVSNVS FSFRGNEPVR EAIHAVFLYH AIQNGMDMGI VNAGQLAIYE DIPSDLKEKV EAVVLNLNPD ATEALLAIAE RYRGGGAQTE DPRDQAWRSW PVGKRLEHAL VKGITDFIEE DTEEARSKAE KPLHVIEGPL MDGMNVVGDL FGAGKMFLPQ VVKSARVMKR AVAYLQPYIE AEKSGGSSNG KIVMATVKGD VHDIGKNIVG VVLQCNNYEI VDLGVMVSCE TILKTAREVN ADIIGLSGLI TPSLDEMVHV AKEMERQGFK LPLLIGGATT SKAHTAVKIE QNYSEPVVYV SNASRAVGVA QSLLSPELKP AFVARIDKEY EIAREQHARK QPRSKPVSLA HARANRHQLD WVGYQPPKPR EPGVQTFEDV PVSVLRPYID WTPFFLSWEL AGKFPRILED EVVGEEATRL YADANAMLDQ LEQDRSVRCA GIIGLFPANA VGDSIEVYTD ESRREVRKVL HHLRQQSEKQ GFPNYCLADY VAPKESGKPD WIGAFAVTGG IGEEAIAKAY KAEHDDYNAI LIQAVCDRLA EAFAEYLHEQ VRKVHWGYAP NEALSNEELI RENYRGIRPA PGYPACPEHT EKGSIWELLG VEQAIGMKLT ESYAMWPGAA VSGWYFSHPD SKYFAVAQIQ QDQVEDYAQR KGMTLAEAER WLGPNLH // ID A0KM11_AERHH Unreviewed; 300 AA. AC A0KM11; DT 12-DEC-2006, integrated into UniProtKB/TrEMBL. DT 12-DEC-2006, sequence version 1. DT 27-MAY-2015, entry version 46. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABK39829.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ABK39829.1}; GN OrderedLocusNames=AHA_2807 {ECO:0000313|EMBL:ABK39829.1}; OS Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / OS JCM 1027 / KCTC 2358 / NCIMB 9240). OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales; OC Aeromonadaceae; Aeromonas. OX NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK39829.1, ECO:0000313|Proteomes:UP000000756}; RN [1] {ECO:0000313|EMBL:ABK39829.1, ECO:0000313|Proteomes:UP000000756} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240 RC {ECO:0000313|Proteomes:UP000000756}; 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.H., 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; ABK39829.1; -; Genomic_DNA. DR RefSeq; WP_011706612.1; NC_008570.1. DR RefSeq; YP_857312.1; NC_008570.1. DR ProteinModelPortal; A0KM11; -. DR STRING; 380703.AHA_2807; -. DR EnsemblBacteria; ABK39829; ABK39829; AHA_2807. DR GeneID; 4488157; -. DR KEGG; aha:AHA_2807; -. DR PATRIC; 20783238; VBIAerHyd135212_2816. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; PYVDVWL; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; AHYD380703:GH2M-2807-MONOMER; -. DR Proteomes; UP000000756; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000756}; KW Methyltransferase {ECO:0000313|EMBL:ABK39829.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000756}; KW Transferase {ECO:0000313|EMBL:ABK39829.1}. SQ SEQUENCE 300 AA; 32018 MW; 4C1281A2DAD3CF2B CRC64; MDTKDLWVLD GGMGRELARR GAPFRQPEWS ALALMEAPET VREVHQAYVA SGARVITTNS YALVPFHIGD ARFVAEGEGL AALAGQLARE VAEEQPGRVQ VAGSLPPLFG SYRADLFDAG RVSELATPLI RALSPHVDLW LAETMSLIAE PLAIRALLPE DGKPFWVSFT LEDEAPGGEP TLRSGERVAD AVTALASAGV DAILFNCCQP EVIEGALKVA GAALQTLDRS DIRLGAYANA FPPQPKEATA NDGLDEIRTD LGPLDYLGWA ERWRGVGANL IGGCCGIGPE HIQALSSRLR // ID A0L0D7_SHESA Unreviewed; 1244 AA. AC A0L0D7; DT 12-DEC-2006, integrated into UniProtKB/TrEMBL. DT 12-DEC-2006, sequence version 1. DT 01-APR-2015, entry version 66. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABK49506.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABK49506.1}; GN OrderedLocusNames=Shewana3_3282 {ECO:0000313|EMBL:ABK49506.1}; OS Shewanella sp. (strain ANA-3). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=94122 {ECO:0000313|EMBL:ABK49506.1, ECO:0000313|Proteomes:UP000002589}; RN [1] {ECO:0000313|Proteomes:UP000002589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ANA-3 {ECO:0000313|Proteomes:UP000002589}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000469; ABK49506.1; -; Genomic_DNA. DR RefSeq; WP_011718089.1; NC_008577.1. DR RefSeq; YP_870912.1; NC_008577.1. DR ProteinModelPortal; A0L0D7; -. DR SMR; A0L0D7; 668-1244. DR STRING; 94122.Shewana3_3282; -. DR EnsemblBacteria; ABK49506; ABK49506; Shewana3_3282. DR KEGG; shn:Shewana3_3282; -. DR PATRIC; 23574548; VBISheSp134792_3640. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SSP94122:GJ9K-3396-MONOMER; -. DR Proteomes; UP000002589; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002589}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABK49506.1}; KW Transferase {ECO:0000313|EMBL:ABK49506.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 258 258 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 774 774 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1244 AA; 138321 MW; BC4DC91CAF2FE414 CRC64; MAISLHRASQ TLADIRNQLS KRILILDGAM GTMIQGYKLE EEDYRGERFK DWHTDVKGNN DLLVLTQPHI IKQIHIDYLK AGADIIETNT FNATTIAMAD YDMQSLSAEI NREGARLARE ACDEIEQATG KPRYVAGVLG PTNRTCSISP DVNDPGYRNI HFDELVTAYC ESTRALIEGG ADIIMVETIF DTLNAKAALF AIETVFDELF GPNSPARLPV MISGTITDAS GRTLTGQTTE AFYNSLRHIK PLSIGLNCAL GPKELRPYVE ELSRIAECYV SAHPNAGLPN EFGGYDETPE DMASVIQEWA REGMLNIIGG CCGSTPEHIK VIREAVEPFA PRVLPEIPVA CRLSGLEPLT IDAQTLFVNV GERTNVTGSA KFLKLIKEGK FEQALDVARE QVESGAQIID INMDEGMLDG VEVMHKFLNL IASEPDISRV PIMIDSSKWE VIEAGLKCIQ GKGIVNSISL KEGEEKFIEQ ATLVKRYGAA AIIMAFDEQG QADTKARKVE ICTRAYRVLV DKVGFPPEDI IFDPNIFAIA TGIDEHDNYA VDFIEAIKEI KATLPHAMIS GGVSNVSFSF RGNNPVREAI HAVFLYHAIK VGMDMGIVNA GQLAIYDDID PELKDKVENV VLNLHCPVED SNNTEQLLEI AEKFRGDGSS SAKKEDLEWR SWPVNQRLAH ALVKGITEFI DEDTEAARQL ASRPLDVIEG PLMDGMNIVG DLFGSGKMFL PQVVKSARVM KKAVAYLNPF IEQEKVEGQS NGRILMVTVK GDVHDIGKNI VGVVLACNGF EVFDLGVMVS VERILEAVKE HNIDIIGMSG LITPSLDEMV HNVKTFHREG LTIPAIIGGA TCSKIHTAVK IAPHYPHGAI YIADASRAVP MVSKLVSNET RQATIDETYA EYEEMRIKRL SQTKRKEIVS LEAARENRCQ HDWANYTPFK PNVLGRQVFD DYPLTDLVDR IDWTPFFRAW ELHGHYPEIL TDKVVGVEAQ KLFADGQAML KKIIDEKWLT AKGVIGLFPA NTVGFDDIEL YTDETRTEVE MTTHHLRMQL ERVGNDNFCL ADFVAPKDSG VADYMGGFAV TAGHGIDEHI ARFEANHDDY NAIMLKCLAD RLAEAFAERM HERVRKEFWG YAADEQLDNE ALIREKYKGI RPAPGYPACP DHTEKGLLWD LLKPNETIDL NITESYAMFP TAAVSGWYFA HPKSRYFGVT NIGRDQVEDY AKRKGMTVAE TEKWLAPVLD YDPE // ID A0LDY2_MAGSM Unreviewed; 1220 AA. AC A0LDY2; DT 12-DEC-2006, integrated into UniProtKB/TrEMBL. DT 12-DEC-2006, sequence version 1. DT 27-MAY-2015, entry version 68. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABK46175.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABK46175.1}; GN OrderedLocusNames=Mmc1_3690 {ECO:0000313|EMBL:ABK46175.1}; OS Magnetococcus sp. (strain MC-1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Magnetococcales; OC Magnetococcaceae; Magnetococcus. OX NCBI_TaxID=156889 {ECO:0000313|EMBL:ABK46175.1, ECO:0000313|Proteomes:UP000002586}; RN [1] {ECO:0000313|EMBL:ABK46175.1, ECO:0000313|Proteomes:UP000002586} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC-1 {ECO:0000313|EMBL:ABK46175.1, RC ECO:0000313|Proteomes:UP000002586}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000471; ABK46175.1; -; Genomic_DNA. DR RefSeq; WP_011715228.1; NC_008576.1. DR RefSeq; YP_867581.1; NC_008576.1. DR ProteinModelPortal; A0LDY2; -. DR SMR; A0LDY2; 654-903. DR STRING; 156889.Mmc1_3690; -. DR EnsemblBacteria; ABK46175; ABK46175; Mmc1_3690. DR KEGG; mgm:Mmc1_3690; -. DR PATRIC; 22434115; VBIMagSp23654_3775. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; MSP156889:GH36-3745-MONOMER; -. DR Proteomes; UP000002586; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002586}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABK46175.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002586}; KW Transferase {ECO:0000313|EMBL:ABK46175.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 251 251 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 315 315 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 767 767 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1220 AA; 132400 MW; E47CB69377F50841 CRC64; MSAMANQRTE QFRTLLQQRI LILDGAMGTM IQRLGLEEAD YRGSRFADHP AELHGANDLL VLTKPQVIRN IHTAYLEAGA DIVETNTFNG NAPSLGDYGL EALVYEVNLE GARVARQACD AVMAQQPGRI CFVAGVLGPT NRTCSISPDV NNPGFRNIDF DALVADYANG TRGLLDGGAD ILLVETVFDT LNCKAALFAV RQVLEQRQLD LPLMISFTIT DQSGRTLTGQ TVEAFWNSVS HARPDTIGMN CALGADQLRP HLETLAEIAA TRISVHPNAG LPNAFGEYDE TPAMMADKVV AFAQGGLINI VGGCCGTSPD HIRAIAQRVA GLAPRQIPTL KPACHLSGLE PLTIDADSLF VNVGERTNVA GSARFARLIR EGQYETALAV AREQVESGAQ IVDVNMDDAM LDAQSAMVTF LNLMAAEPEI SRVPVMIDSS EWRVLEAGLK CVQGKCIINS LSLKEGDEPF LKQAHLARRY GAAVIVMAFD EQGQADSYQR RIDICQRAYD LLVHTVGMEP NDIIFDPNIF AVATGIEEHN NYAVEFIQAT RWIKQNLPGA RISGGVSNVS FSFRGNNPVR EAMHAVFLYH AIAAGMDMGI VNAGQLAVYE EIPVDLRERV EDVILNRRSD ATDRLLEVAD HYRQSGVTED KADAAWRSEP VQARLRHAMI KGITEFIDAD VEEARSLAAH PLEVVEGPLM AGMNAVGDLF GEGKMFLPQV VKSARVMKQA VAYLVPHIEE ANRQGGIENR ASGAGKILLA TVKGDVHDIG KNIVKVVLQC NNFEVEDLGV MVAVETILDR AQESGAQIIG LSGLITPSLQ QMTHVAKEMQ RRGMQHIPLL IGGATTSKAH TAVKIAPVTE GCVVQVKDAS RSVGVAAALL SARERDDFMA ACVAEHEKYR AIHEQRSTRK PLLSMQEARA RAFATPAAVT QAAQPGVHVL ADYDLATLVP YIDWTPFFRT WELHGRYPEI LSDSKVGQAA TRLFEDAQQM LQEIIAQGSL KANGVLGLFN ASRVGDDIEL ADGLGTIHTL RQQRDGGEAP CYALADFVGQ GDTIGMFAVT AGIGVAELVA HHQAAHDDYR AIMVEALADR LAEAFAEHIH ERARREFWGY AGDEALSKGD LIAERYVGIR PAPGYPACPD HTEKALLFKC LNAQEHAGMA LTESFAMTPA ASVSGYLFAH PQARYFSVGR IGGDQLEAYA KRKGMSVEEM AKWLAPNLDS // ID A0LU36_ACIC1 Unreviewed; 1158 AA. AC A0LU36; DT 12-DEC-2006, integrated into UniProtKB/TrEMBL. DT 12-DEC-2006, sequence version 1. DT 27-MAY-2015, entry version 68. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABK52946.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABK52946.1}; GN OrderedLocusNames=Acel_1174 {ECO:0000313|EMBL:ABK52946.1}; OS Acidothermus cellulolyticus (strain ATCC 43068 / 11B). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Frankineae; Acidothermaceae; Acidothermus. OX NCBI_TaxID=351607 {ECO:0000313|EMBL:ABK52946.1, ECO:0000313|Proteomes:UP000008221}; RN [1] {ECO:0000313|Proteomes:UP000008221} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43068 / 11B {ECO:0000313|Proteomes:UP000008221}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000481; ABK52946.1; -; Genomic_DNA. DR RefSeq; WP_011720009.1; NC_008578.1. DR RefSeq; YP_872932.1; NC_008578.1. DR ProteinModelPortal; A0LU36; -. DR STRING; 351607.Acel_1174; -. DR EnsemblBacteria; ABK52946; ABK52946; Acel_1174. DR KEGG; ace:Acel_1174; -. DR PATRIC; 20672816; VBIAciCel132453_1244. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; ACEL351607:GIXW-1200-MONOMER; -. DR Proteomes; UP000008221; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008221}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABK52946.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008221}; KW Transferase {ECO:0000313|EMBL:ABK52946.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 231 231 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 297 297 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 298 298 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 741 741 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1158 AA; 125465 MW; B372914B16D70131 CRC64; MTTRAALLRR ELARRVLVAD GAMGTMLQAA RLGPADFTLP DIGVLEGCNE VLSLTRPDVV AAVHDAYLAA GCDAIETNTF GANLGNLGEY GIADRIEELA AAGARIAREV ADRWSTPSEP RFVLGSVGPG TKLPSLGHVT FAELRDAYQR QVTGLINGGV DAVLVETAQD LLQAKAAVIG AKRARAAAGV DIPIFASVTV ETTGTMLLGS EIGAALTSLE ALGIEMIGLN CATGPAEMSE HVRYLAAHAA VAVSCLPNAG LPILGPDGAQ YPLTPGELAD ALEEYAAQFG LALVGGCCGT TPEHLRLVAE RLRHRPIGSR RAETVPAVSS LYQTVPLRQQ TAFLAVGERT NANGSKAFRE AMLAGRYEDC VELARGAARD GSHLIDVCVD YVGRDGVRDM RELARRLATA TTLPVMLDST EPAVIEAGLE CLGGRCIVNS VNFEDGDGPQ SRISRLMPIV REHGAAVVAL TIDETGQART AEHKVSVAER LIDTLTNRWG MRETDILVDT LTFTLGTGQE ESRRDGIATI EAIREVKTRH PDVHTILGIS NISFGLNPAA RAVLNSVFLA ECLRAGLDAA IVHPAKILPM SRIPEDQQAV ALDVIYDRRR PDYDPLVRLM ELFAGVTAAA SQKSRAAELA AMPLAERLHR RIVDGERNGL EADLDEALTT RRALDIINEI LLPAMKEVGD LFGRGDMQLP FVLQSAEVMK AAVAYLEPHM EKSNRSGKGT IVLATVKGDV HDIGKNLVDI ILSNNGYRVV NLGIKQPITA ILEAAERHDA DAIGMSGLLV KSTVVMRENL QEISSRGLAK RWPVLLGGAA LTRAYVEDDL ASEFDGTVRY AKDAFEGLRL MDTLMAIKRG EPGASLPPLR RRRIAQSATA VSEPASRSDV ATDIPIPTPP FLGDRVVKGI PLGDYLGYLD EKALFAGRWG LRSRPNGPSY AEIVEAEGRP RLRQWLDRLQ AENLLAAGVV YGYYRCVSEG DDLIILADDG RTERCRFRFP RQQRGRRLCI ADFFRPAGSG ETDVVAFQLV TIGARVSAFT ARLFADGAFR DYLEVHGLSV QLAEALAEFW HRRIREELGI ADADHPELRE ILDHQGYRGS RYSFGYPACP DLEDRAKIVQ LLKPERIGVR LSEEYQLDPE QSTDALIVHH PEAKYFSV // ID A0LY73_GRAFK Unreviewed; 348 AA. AC A0LY73; DT 12-DEC-2006, integrated into UniProtKB/TrEMBL. DT 12-DEC-2006, sequence version 1. DT 27-MAY-2015, entry version 53. DE SubName: Full=Complete circular genome {ECO:0000313|EMBL:CAL65318.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAL65318.1}; GN OrderedLocusNames=GFO_0332 {ECO:0000313|EMBL:CAL65318.1}; OS Gramella forsetii (strain KT0803). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Gramella. OX NCBI_TaxID=411154 {ECO:0000313|EMBL:CAL65318.1, ECO:0000313|Proteomes:UP000000755}; RN [1] {ECO:0000313|EMBL:CAL65318.1, ECO:0000313|Proteomes:UP000000755} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KT0803 {ECO:0000313|EMBL:CAL65318.1, RC ECO:0000313|Proteomes:UP000000755}; RX PubMed=17107561; DOI=10.1111/j.1462-2920.2006.01152.x; RA Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E., RA Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K., RA Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I., RA Gloeckner F.O.; RT "Whole genome analysis of the marine Bacteroidetes'Gramella forsetii' RT reveals adaptations to degradation of polymeric organic matter."; RL Environ. Microbiol. 8:2201-2213(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; CU207366; CAL65318.1; -; Genomic_DNA. DR RefSeq; WP_011708256.1; NC_008571.1. DR RefSeq; YP_860386.1; NC_008571.1. DR ProteinModelPortal; A0LY73; -. DR STRING; 411154.GFO_0332; -. DR EnsemblBacteria; CAL65318; CAL65318; GFO_0332. DR KEGG; gfo:GFO_0332; -. DR PATRIC; 22069535; VBIGraFor5527_0326. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; GFOR411154:GI79-332-MONOMER; -. DR Proteomes; UP000000755; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000755}; KW Methyltransferase {ECO:0000313|EMBL:CAL65318.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000755}; KW Transferase {ECO:0000313|EMBL:CAL65318.1}. SQ SEQUENCE 348 AA; 37861 MW; BD5E114ADED7AC11 CRC64; MSKIEELLSQ KILILDGAMG TMLQEYKFSE EDFRGKRFAD WPVSLQGNND LLSITQPEAI ATIHRKYFDA GADIVETNTF SGTTIAMADY KMEDLVYELN YESARIAKKV AEEVTAENPS KPRFVAGAIG PTNKTASMSP DVNDPGYRAI SFDELRKAYK QQAKALIDGG ADILLVETVF DTLNAKAALF AIDELKEELG ITIPVMISGT ITDASGRTLS GQTAEAFLIS VSHIPLLSIG FNCALGAKQL TPHLEVLNRY ANSGVSAYPN AGLPNAFGEY DQDAAEMASQ IEEYLEKSLV NILGGCCGTT PKHIKAIAEV AKNYKPREIN LQDHAELVSA SQQSDHKI // ID A0NU21_LABAI Unreviewed; 342 AA. AC A0NU21; DT 09-JAN-2007, integrated into UniProtKB/TrEMBL. DT 09-JAN-2007, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=Methionine synthase I {ECO:0000313|EMBL:EAV43930.1}; GN ORFNames=SIAM614_12418 {ECO:0000313|EMBL:EAV43930.1}; OS Labrenzia aggregata (strain ATCC 25650 / DSM 13394 / JCM 20685 / NBRC OS 16684 / NCIMB 2208 / IAM 12614) (Stappia aggregata). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Labrenzia. OX NCBI_TaxID=384765 {ECO:0000313|EMBL:EAV43930.1}; RN [1] {ECO:0000313|EMBL:EAV43930.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=IAM 12614 {ECO:0000313|EMBL:EAV43930.1}; 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. {ECO:0000313|EMBL:EAV43930.1}. 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; AAUW01000008; EAV43930.1; -; Genomic_DNA. DR RefSeq; WP_006935147.1; NZ_AAUW01000008.1. DR ProteinModelPortal; A0NU21; -. DR EnsemblBacteria; EAV43930; EAV43930; SIAM614_12418. DR PATRIC; 30165501; VBILabAgg74751_2668. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 342 AA; 35597 MW; BDA25E9F5241E16E CRC64; MSKLEELLAE RGALLADGAT GTNLFEMGLV SGDAPELWNT DEPEKITALH KSFVDAGSDI ILTNTFGCNR HRLKLHKAED RVRELNIAAV KLARDVAEAS GRTVLIGGSV GPTGELFQPL GALSYEEGVA AFKEQMAGLV EGGADILWVE TMSAVEEMKA AAEAAQNFDV PLVITASFDT AGKTMMGLSP KGLGDLQAQF ACTPVAIGSN CGVGASDLLA AIMDITEAYP DAIVVAKANC GIPQIKGDEV IYTGTPELMA KYAHMALDAG ARIVGGCCGT SPVHLAAMRA AVDAHQAGVR PTLDEVIAEI GPLVSPPNKE ADAARAENDG SGSGRRRGRR RG // ID A0P2G4_LABAI Unreviewed; 1242 AA. AC A0P2G4; DT 09-JAN-2007, integrated into UniProtKB/TrEMBL. DT 09-JAN-2007, sequence version 1. DT 27-MAY-2015, entry version 51. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EAV40828.1}; GN ORFNames=SIAM614_17489 {ECO:0000313|EMBL:EAV40828.1}; OS Labrenzia aggregata (strain ATCC 25650 / DSM 13394 / JCM 20685 / NBRC OS 16684 / NCIMB 2208 / IAM 12614) (Stappia aggregata). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Labrenzia. OX NCBI_TaxID=384765 {ECO:0000313|EMBL:EAV40828.1}; RN [1] {ECO:0000313|EMBL:EAV40828.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=IAM 12614 {ECO:0000313|EMBL:EAV40828.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EAV40828.1}. 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; AAUW01000026; EAV40828.1; -; Genomic_DNA. DR RefSeq; WP_006939533.1; NZ_AAUW01000026.1. DR ProteinModelPortal; A0P2G4; -. DR SMR; A0P2G4; 654-901. DR EnsemblBacteria; EAV40828; EAV40828; SIAM614_17489. DR PATRIC; 30171399; VBILabAgg74751_5579. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 249 249 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 764 764 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1242 AA; 136061 MW; B733EBD524E84725 CRC64; MIKSDAFERL RDLAKTRILV LDGAMGTEIQ LLKLDEAAYR GDRFKDWPSD IKGNNDLLSL TQPDAIRKIH VDYLEAGADI VETNTFSSTT IAQADYGMEE LAYELNFESA KLAREACDKV MAQDPSRPRF VAGALGPTNR TASISPDVNN PGYRAVSFDD LRIAYAEATR GLIAGGADII LVETIFDTLN AKAALFAVDE VFEETGKILP VMISGTITDL SGRTLSGQTP EAFWNSVRHT NPLTIGLNCA LGAKEMRAHV DELGRVADTL VCAYPNAGLP NEFGEYDESP EHMAGLIEEF ASAGLVNVVG GCCGTTPAHI KAIAEAVSDK KPREIPEIDV HMRLSGLEPF VVTKETNFVN VGERTNVTGS ARFRKLIKEG DYPTALEVAR QQVENGAQII DINMDEGLLD SEEAMVTFLN LVAAEPDIAK VPIMIDSSKW TVIEAGLKCI QGKGVVNSIS MKEGEEAFIE QAKKVRRYGA AVVVMAFDEK GQADTFERKT EICARSYKIL TEKVGFPPED IIFDPNIFAV ATGIEEHNNY GVDFIEATGW IRENLPHAHV SGGVSNLSFS FRGNEAVREA MHSVFLYHAI KRGMDMGIVN AGQLAVYNDL ETELRELCED VVLNRRKDST DRMLEAAERW KGEGGKKREA DLTWRTLGVA KRLEHALVHG IADYVEEDTE EARQAFDRPL HVIEGPLMDG MNVVGDLFGS GQMFLPQVVK SARVMKKAVA YLMPFMEKEK EELGQTGHSS AGKILMATVK GDVHDIGKNI VGVVLQCNNF EVIDLGVMVP AAKILDTARQ EKVDMIGLSG LITPSLDEMC HVAAELEREG LDVPLLIGGA TTSKIHTAVK IHPNYARGQA IYVTDAGRAV GVASKLMSEG GRAPYYADVR AEYADIAEKH AAGRGAQQRT SLKAARDNAF KADFQGKQPV APKKPGTTVF DAFPLEELVP FIDWTPFFST WEIKGRYPAV LTDNRYGPAA RALFDDARRM LDEIVEKKLL TARGVASLWP ANAVGDDVRV FTDESRSDTL ATFHTLRQQM TRSAGGRANI ALSDFVAPVD SGISDWIGGF AVTAGHGEDE LAARYARESD DYNKILSQAL ADRLAEAFAE KLHQIVRTEL WGYAADESLS IEDIIAEKYQ GIRPAPGYPA QPDHTEKDTL FQLLDAERLT GIQLTESKAM LPGSSVSGLY FGHADSHYFG VGKIEKDQVE DYAARKGWDL AYAERWLAPI LNYDPARMVA AE // ID A0PL93_MYCUA Unreviewed; 1277 AA. AC A0PL93; DT 09-JAN-2007, integrated into UniProtKB/TrEMBL. DT 09-JAN-2007, sequence version 1. DT 01-APR-2015, entry version 63. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase, MetH {ECO:0000313|EMBL:ABL03112.1}; GN Name=metH {ECO:0000313|EMBL:ABL03112.1}; GN OrderedLocusNames=MUL_0395 {ECO:0000313|EMBL:ABL03112.1}; OS Mycobacterium ulcerans (strain Agy99). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=362242 {ECO:0000313|EMBL:ABL03112.1, ECO:0000313|Proteomes:UP000000765}; RN [1] {ECO:0000313|EMBL:ABL03112.1, ECO:0000313|Proteomes:UP000000765} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Agy99 {ECO:0000313|EMBL:ABL03112.1, RC ECO:0000313|Proteomes:UP000000765}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000325; ABL03112.1; -; Genomic_DNA. DR RefSeq; WP_011738737.1; NC_008611.1. DR RefSeq; YP_904583.1; NC_008611.1. DR ProteinModelPortal; A0PL93; -. DR SMR; A0PL93; 689-1276. DR STRING; 362242.MUL_0395; -. DR EnsemblBacteria; ABL03112; ABL03112; MUL_0395. DR GeneID; 4553946; -. DR KEGG; mul:MUL_0395; -. DR PATRIC; 18167338; VBIMycUlc37413_0545. DR GenoList; MUL_0395; -. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; QPFFNAW; -. DR OrthoDB; EOG6091CH; -. DR Proteomes; UP000000765; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000765}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABL03112.1}; KW Transferase {ECO:0000313|EMBL:ABL03112.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 349 349 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 350 350 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 806 806 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1277 AA; 139772 MW; 6EEF8BFD2B11B2E9 CRC64; MWVERRCNGS PVPRRYPPRS AESRTPSATE GINVSAFEPN IRPDCTDALT ATLGQRIMVI DGAMGTAIQR DRPDEAGYRG ERFKDWPSDL VGNNDLLSLT QPQIIEGIHR EYLQAGADIL ETNTFNANAV SLSDYDMAEL AYELNYAGAA LARAAADEFS TPEKPRYVAG ALGPTTRTAS ISPDVNDPGA RNVSYDQLVA AYLEAANGLV DGGADIIIIE TIFDSLNAKA AVFAVETLFE DRGRRWPVII SGTITDASGR TLSGQVTEAF WNAIRHAKPI AVGLNCALGA PEMRPYIAEM ARIADTFVSC YPNAGLPNAF GEYDETPEHQ AGYIAEFADA GLVNLVGGCC GTAPPHIAEI AKVVEGKAPR ELPEIPVATR LSGLEPLNIT DDSLFENIGE RTNITGSARF RNLIKAEDYD TALSVALQQV EVGAQVIDIN MDEGMIDGVA AMDRFTKLIA AEPDISRVPV MIDSSKWEVI EAGLKNVQGK PIVNSISMKE GEEKFVREAR LCRKYGAAVV VMAFDEKGQA DNLERRKEIC GRAYRILTEE VGFPAEDIIF DPNCFALATG IEEHATYGID FIEACAWIKE NLPGVHISGG ISNVSFSFRG NNPVREAIHA VFLFHAIKAG LDMGIVNAGA LVPYDSIDPE LRERIEDVVL NRREDAAERL LEIAERFNTK GKPEDPAAAE WRSLPVRERI THALVKGIDA HVDADTEELR AEIAAAGGRL IEVIEGPLMD GMNVVGDLFG AGKMFLPQVV KSARVMKKAV AYLLPFIEAE KAQSGSTEQD KTNGIIIMAT VKGDVHDIGK NIVGVVLQCN NYTVVDLGVM VPAEKILAAA REYDADIIGL SGLITPSLDE MVNFAAAMER EGMQIPLLIG GATTSRAHTA VKVAPRRSGP VVWVKDASRS VPVAAALLDD KQRPGLLEAT AADYAALRER HSQKNERPML TLEKARANRT PIDWDGYTPP LPAQGLGVRE FHDYDLAELR EYIDWQPFFN AWEMKGRFPD ILNNPATGEA ARKLYNDAQE MLDTLIREKW LTANGVIGFF PANAVGDDIE VYTDETRAEV LTTLHNLRQQ GEHRAGIPNR SLGDFIAPKD TGLADYVGAF AVTAGLGSQT KIVEFKEALD DYSAILLESI ADRLAEAFAE RMHQRVREEF WGYQPDEQLD NEALIGERYV GIRPAPGYPA CPEHTEKTTL FELMDVTKRT GIELTESMAM WPGAAVSGWY FSHPQSQYFV VGRMAQDQVA DYAKRKGWTL PEAERWLGPN LGYNPED // ID A0Q0N0_CLONN Unreviewed; 808 AA. AC A0Q0N0; DT 09-JAN-2007, integrated into UniProtKB/TrEMBL. DT 09-JAN-2007, sequence version 1. DT 27-MAY-2015, entry version 57. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase, putative {ECO:0000313|EMBL:ABK61675.1}; GN OrderedLocusNames=NT01CX_2109 {ECO:0000313|EMBL:ABK61675.1}; OS Clostridium novyi (strain NT). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=386415 {ECO:0000313|EMBL:ABK61675.1, ECO:0000313|Proteomes:UP000008220}; RN [1] {ECO:0000313|EMBL:ABK61675.1, ECO:0000313|Proteomes:UP000008220} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NT {ECO:0000313|EMBL:ABK61675.1, RC ECO:0000313|Proteomes:UP000008220}; 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; ABK61675.1; -; Genomic_DNA. DR RefSeq; WP_011722182.1; NC_008593.1. DR RefSeq; YP_878182.1; NC_008593.1. DR ProteinModelPortal; A0Q0N0; -. DR STRING; 386415.NT01CX_2109; -. DR EnsemblBacteria; ABK61675; ABK61675; NT01CX_2109. DR KEGG; cno:NT01CX_2109; -. DR PATRIC; 19479888; VBICloNov112828_1214. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CNOV386415:GH98-1241-MONOMER; -. DR Proteomes; UP000008220; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008220}; KW Methyltransferase {ECO:0000313|EMBL:ABK61675.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008220}; KW Transferase {ECO:0000313|EMBL:ABK61675.1}. SQ SEQUENCE 808 AA; 88803 MW; 38A03891E12F0F58 CRC64; MHERMINMNV LQYIKDNILI FDGAMGTMLQ KSGLNLGESP EKLNFSHENL IIDIHKKYIE AGANVITTNT FGANELKLKN TSFSVEDVIY KAVSLAIKAK EDTNCFIALD IGPIGQLLEP MGTLKFEDAI NIFKRQIKAG VKAGVDLILI ETMTDLYEMK AAILAAKETC DLPIFATMSF ENDGRTFTGC LPESMAVTLE ALGVTAVGVN CSLGPKELKP IVKKTLEHTN LPVIVQPNAG LPTIVNGQSL YTITPEEFCN YVESLIDMGV SIIGGCCGTT PDFIKCLKSM SHHKKVLKRD PIKKSFLTTP SKILELNEVR IIGEKINPSG KKNLKEAIIN DDMDYILKQA ITQLNGGADI LDINVGLPEI NEANILENTI KEIQSRIDIP LSIDSSNLEA IERALRIYNG KPIVNSVNGE NSSLETILPL VKKYGASVIG LTLDNKGIPK TAGERFEIGK KILNTALEYG IKKEDVYIDC LTLTVSAQQK EVMETLKALK MVKENLGVKT LLGISNISFG LPNRDIINET FLSLALGAGL DLPIMNPNNE NMINIINAFK VLNNNDKNAK HYIETYKDKK ISTTIVTNNN SSNESLNPAF KNEASLENSI LQGLKSNTKD LVKELLKTNN ELNIINDYLI PALDRVGDRY ESGEIFLPQL IQAAETVKIA FDLIKENLNR NNKKEITKGT IMLATVKGDV HDIGKNIVKV ILENYGYEIL DLGKDVPIER IVKEAIENDI KLVGLSALMT TTVKSMEDTI TALKKANFKG KIMASGAVIT KDYSIKMGAD FCAKDAKDSV EIAKLVFG // ID A0QZX6_MYCS2 Unreviewed; 1246 AA. AC A0QZX6; DT 09-JAN-2007, integrated into UniProtKB/TrEMBL. DT 09-JAN-2007, sequence version 1. DT 27-MAY-2015, entry version 76. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABK73783.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABK73783.1}; DE SubName: Full=Methionine synthase (5-methyltetrahydrofolate--homocysteine methyltransferase) (Methionine synthase, vitamin-B12 dependent) (MS) {ECO:0000313|EMBL:AFP40545.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AFP40545.1}; DE SubName: Full=Mycobacterium smegmatis str. MC2 155, complete genome {ECO:0000313|EMBL:AIU09280.1}; GN Name=metH {ECO:0000313|EMBL:ABK73783.1}; GN OrderedLocusNames=MSMEG_4185 {ECO:0000313|EMBL:ABK73783.1}, GN MSMEI_4087 {ECO:0000313|EMBL:AFP40545.1}; GN ORFNames=LJ00_20750 {ECO:0000313|EMBL:AIU09280.1}; OS Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=246196 {ECO:0000313|EMBL:ABK73783.1, ECO:0000313|Proteomes:UP000000757}; RN [1] {ECO:0000313|EMBL:AFP40545.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC2 155 {ECO:0000313|EMBL:AFP40545.1}; RX PubMed=16381882; DOI=10.1093/nar/gkj060; RA Perrodou E., Deshayes C., Muller J., Schaeffer C., Van Dorsselaer A., RA Ripp R., Poch O., Reyrat J.M., Lecompte O.; RT "ICDS database: interrupted CoDing sequences in prokaryotic genomes."; RL Nucleic Acids Res. 34:D338-D343(2006). RN [2] {ECO:0000313|EMBL:ABK73783.1, ECO:0000313|Proteomes:UP000000757} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700084 / mc(2)155 {ECO:0000313|Proteomes:UP000000757}, and RC MC2 155 {ECO:0000313|EMBL:ABK73783.1}; 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 [3] {ECO:0000313|EMBL:AFP40545.1, ECO:0000313|Proteomes:UP000006158} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700084 / mc(2)155 {ECO:0000313|Proteomes:UP000006158}, and RC MC2 155 {ECO:0000313|EMBL:AFP40545.1}; 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 [4] {ECO:0000313|EMBL:AFP40545.1, ECO:0000313|Proteomes:UP000006158} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700084 / mc(2)155, and MC2 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). RN [5] {ECO:0000313|EMBL:AIU09280.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC2 155 {ECO:0000313|EMBL:AIU09280.1}; RX PubMed=25657281; RA Mohan A., Padiadpu J., Baloni P., Chandra N.; RT "Complete Genome Sequences of a Mycobacterium smegmatis Laboratory RT Strain (MC2 155) and Isoniazid-Resistant (4XR1/R2) Mutant Strains."; RL Genome Announc. 3:0-0(2015). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000480; ABK73783.1; -; Genomic_DNA. DR EMBL; CP001663; AFP40545.1; -; Genomic_DNA. DR EMBL; CP009494; AIU09280.1; -; Genomic_DNA. DR RefSeq; WP_011729624.1; NC_018289.1. DR RefSeq; YP_006568840.1; NC_018289.1. DR RefSeq; YP_888464.1; NC_008596.1. DR ProteinModelPortal; A0QZX6; -. DR SMR; A0QZX6; 661-1245. DR STRING; 246196.MSMEG_4185; -. DR EnsemblBacteria; ABK73783; ABK73783; MSMEG_4185. DR EnsemblBacteria; AFP40545; AFP40545; MSMEI_4087. DR EnsemblBacteria; AIU09280; AIU09280; LJ00_20750. DR GeneID; 4536551; -. DR KEGG; msm:MSMEG_4185; -. DR PATRIC; 18080727; VBIMycSme59918_4106. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; QPFFNAW; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; MSME246196:GJ4Y-4184-MONOMER; -. DR Proteomes; UP000000757; Chromosome. DR Proteomes; UP000006158; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000757}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABK73783.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000757}; KW Transferase {ECO:0000313|EMBL:ABK73783.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 258 258 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 775 775 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1246 AA; 136998 MW; 03D0F9D60821F8D4 CRC64; MNAVRSETLA PNIRPDCTDA LTAALRQRIL VIDGAMGTAI QRDRPDEAGY RGERFKDWPS DLVGNNDLLN LTQPHIIEAI HREYLDAGAD LLETNTFNAN AVSLSDYGMQ ELAYELNYAG AALARAACDE YSTPDKPRYV AGALGPTTRT ASISPDVNDP GARNVSYDQL AEAYLEAARG LVDGGADLII VETIFDTLNA KAAIFAIETL FEERGRRWPV IISGTITDAS GRTLSGQVTE AFWNSIRHAQ PLAVGLNCAL GAPEMRPYIA EMSRIADTFV SCYPNAGLPN AFGEYDESPK RQASYVEEFA EAGFVNLVGG CCGTTPAHIA EIAKVVEGKP PRQVPEIPVA TRLSGLEPLN IDEDSLFVNI GERTNITGSA RFRNLIKAED YDTALSVALQ QVEVGAQVID INMDEGMIDG VAAMDRFTKL IASEPDISRV PVMIDSSKWE VIEAGLKNVQ GKPIVNSISL KEGEEKFVRE ARLCRKYGAA VVVMAFDEQG QADNLERRKQ ICGRAYKTLT EEVGFPAEDI IFDPNCFALA TGIEEHATYG IDFIEACRWI KENLPGVHIS GGISNVSFSF RGNNPVREAI HAVFLFHAIK AGLDMGIVNA GALVPYDSID PELRERIEDV VLNRREDAAE RLLEIAERFN SKDKGEDPAA AEWRSLPVRE RITHALVKGI DAHVDDDTEE LRAEIAAAGG RPIEVIEGPL MDGMNVVGDL FGSGKMFLPQ VVKSARVMKK AVAYLLPYIE AEKKPGDAER SNGTIIMATV KGDVHDIGKN IVGVVLQCNN YTVIDLGVMV PAQKILDAAK EHNADIIGLS GLITPSLDEM VNFAAEMERE GMDIPLLIGG ATTSRAHTAV KVAPRRSGPV VWVKDASRSV PVAAALLDDK QRPALLEATE KDYASLRERH AQKNERPMVT LEKARANRTP IDWDGYTPPV PAQGLGIREF ENYDLSELRQ YIDWQPFFNA WEMKGKFPDI LNNPASGEAA RKLYEEAQEM LDTLIKEKWL TANGVIGFFP ANAVGDDIEV YTDDTRTEVL TTLRNLRQQG EHRDGIPNRS LGDFIAPKET GLADYIGAFA VTAGLGSAEK IAEFKADHDD YSAILLESLA DRLAEAFAER MHQRVRTELW AYQPDEELDN EALIAERYRG IRPAPGYPAC PEHTEKATLF KLLDVTERTG IELTESMAMW PGAAVSGWYF SHPQSQYFVV GRLAQDQVAD YARRKGWTLQ EAERWLAPNL GYNPED // ID A0RIN1_BACAH Unreviewed; 1133 AA. AC A0RIN1; DT 09-JAN-2007, integrated into UniProtKB/TrEMBL. DT 09-JAN-2007, sequence version 1. DT 27-MAY-2015, entry version 69. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABK87074.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABK87074.1}; GN Name=metH {ECO:0000313|EMBL:ABK87074.1}; GN OrderedLocusNames=BALH_3850 {ECO:0000313|EMBL:ABK87074.1}; OS Bacillus thuringiensis (strain Al Hakam). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=412694 {ECO:0000313|EMBL:ABK87074.1, ECO:0000313|Proteomes:UP000000761}; RN [1] {ECO:0000313|EMBL:ABK87074.1, ECO:0000313|Proteomes:UP000000761} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Al Hakam {ECO:0000313|EMBL:ABK87074.1, RC ECO:0000313|Proteomes:UP000000761}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000485; ABK87074.1; -; Genomic_DNA. DR RefSeq; WP_011733324.1; NC_008600.1. DR RefSeq; YP_896581.1; NC_008600.1. DR ProteinModelPortal; A0RIN1; -. DR STRING; 412694.BALH_3850; -. DR EnsemblBacteria; ABK87074; ABK87074; BALH_3850. DR KEGG; btl:BALH_3850; -. DR PATRIC; 19000543; VBIBacThu63319_4271. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; BTHU412694:GH1W-3767-MONOMER; -. DR Proteomes; UP000000761; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000761}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABK87074.1}; KW Transferase {ECO:0000313|EMBL:ABK87074.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 223 223 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 287 287 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 719 719 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1133 AA; 126118 MW; 61A3A43CF1AE6599 CRC64; MMKCIEEKLQ NSILLLDGAM GTMIQQEDLT AEDFGGEEYE GCNEYLVETR PDVILKIHKA YIEAGADIIE TNTFGATNIV LSDYELSHLD EELNEKAARL AKQAVKESGK EVYVAGAMGP TTKAISVTGG VTFEELIEAY TRQARGLLKG EVDVLLVETS QDMRNVKAAY IGIQAAFDEL KKIVPIMISG TIEPMGTTLA GQTIEAFYLS VEHMKPLSVG LNCATGPEFM RDHIRSLSDL SECYISCYPN AGLPDEDGHY HESPSSLAEK VKRFAEEGWV NIIGGCCGTT PEHIKAMKEA LASLKPREHH EREGHGVSGL EALQYDDSMR PLFVGERTNV IGSRKFKRLV AEGKFEEAAE VARAQVKKNA HIIDICMADP DRDEIEDMEN FLAEVTKVLK VPIMIDSTDE HVMERALTYI QGKAVINSIN LEDGEERFIK VTPLLQKYGA AIVVGTIDED GMAVSAERKL EIAKRSYELL TTKYGIRPSD IIFDALVFPV GTGDEEYIGS AAATIEGIRL IKEALPECLT ILGVSNISFG LPPAGREVLN SVFLYHATKA GLDYAIVNTE KLERYASIPD EEKRLADALL FETTQETLEE FTNFYRVAKK KDVVVQETLT LDERLANYIV EGTKQGLHED LSLALTEGRK PLDIINGPLM TGMDEVGRLF NNNELIVAEV LQSAESMKAA VSYLEPHMES SDSAKKGKVL LATVKGDVHD IGKNLVEIIL ANNGYEIINL GINVRSDRIV QEVQEKKPDI IGLSGLLVKS AQQMVTTAED LKAADIDIPI VVGGAALTRK FTDNRISPSY KGLVCYASDA MTGLDIINKL QKEEEREKMK QDKKERHLHI VTKEEKKVEI PAVIEPLPKS EVMVPDSTKR IVLRDVPALH LVPFLNRQML LGHHLGLKGS VKKLLKEGDK RAHELNDLID ELLQEGQSWL KPKAVYQFFP AQSDGQNIVI YDPEDHTRVI ERFTFPRQGR APYRTLGDYL RPIGDEMDYV AFLSVTVGEG VRDIAEEWKA KGDYLRSHAI QSLALELAEG LAEKTHMLIR DRWGIPDSPE LTMEERFRTK YRGIRVSFGY PACPELADQE KLFRLIHPEE IGISLTEGFM MEPEASVTAM VFSHPEARYF SVL // ID A0RIN2_BACAH Unreviewed; 610 AA. AC A0RIN2; DT 09-JAN-2007, integrated into UniProtKB/TrEMBL. DT 09-JAN-2007, sequence version 1. DT 27-MAY-2015, entry version 58. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN Name=metE {ECO:0000313|EMBL:ABK87075.1}; GN OrderedLocusNames=BALH_3851 {ECO:0000313|EMBL:ABK87075.1}; OS Bacillus thuringiensis (strain Al Hakam). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=412694 {ECO:0000313|EMBL:ABK87075.1, ECO:0000313|Proteomes:UP000000761}; RN [1] {ECO:0000313|EMBL:ABK87075.1, ECO:0000313|Proteomes:UP000000761} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Al Hakam {ECO:0000313|EMBL:ABK87075.1, RC ECO:0000313|Proteomes:UP000000761}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ABK87075.1; -; Genomic_DNA. DR RefSeq; WP_000770338.1; NC_008600.1. DR RefSeq; YP_896582.1; NC_008600.1. DR ProteinModelPortal; A0RIN2; -. DR STRING; 412694.BALH_3851; -. DR EnsemblBacteria; ABK87075; ABK87075; BALH_3851. DR KEGG; btl:BALH_3851; -. DR PATRIC; 19000545; VBIBacThu63319_4272. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; BTHU412694:GH1W-3768-MONOMER; -. DR Proteomes; UP000000761; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000761}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ABK87075.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:ABK87075.1}. SQ SEQUENCE 610 AA; 67264 MW; 00A5EA30497F636A CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNISDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTE INRAAVKLAK ASVTDRNAIL GTIGGMKHIG AVTTTDMERE FMLLEQASAL LEEQVDGLLL ETFYDEFELL HAVQVLRKET NIPIVAQLAL HEAGTTQNGN DVNEILKQLL DYGANVVGLN CQLGPLHMTE ALKMISIPKN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPKFIEQGI RLLGGCCGTT PEHIESMKRA TLNVTPVIEK DTIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRISNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIA LIEEVYEATK HLEQPIFIGI MPLISKRNAD FLHFEVPGIT LPEAVRERMD GHETKEAAIE EGIRISQELI DETMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID A0RW49_CENSY Unreviewed; 317 AA. AC A0RW49; DT 09-JAN-2007, integrated into UniProtKB/TrEMBL. DT 09-JAN-2007, sequence version 1. DT 27-MAY-2015, entry version 41. DE SubName: Full=Methionine synthase I (Cobalamin-dependent), methyltransferase domain {ECO:0000313|EMBL:ABK77566.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABK77566.1}; GN OrderedLocusNames=CENSYa_0934 {ECO:0000313|EMBL:ABK77566.1}; OS Cenarchaeum symbiosum (strain A). OC Archaea; Thaumarchaeota; Cenarchaeales; Cenarchaeaceae; Cenarchaeum. OX NCBI_TaxID=414004 {ECO:0000313|EMBL:ABK77566.1, ECO:0000313|Proteomes:UP000000758}; RN [1] {ECO:0000313|EMBL:ABK77566.1, ECO:0000313|Proteomes:UP000000758} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A {ECO:0000313|Proteomes:UP000000758}; RX PubMed=17114289; DOI=10.1073/pnas.0608549103; RA Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y., RA Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.; RT "Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum RT symbiosum."; RL Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(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; DP000238; ABK77566.1; -; Genomic_DNA. DR RefSeq; WP_013482192.1; NC_014820.1. DR RefSeq; YP_875870.1; NC_014820.1. DR ProteinModelPortal; A0RW49; -. DR EnsemblBacteria; ABK77566; ABK77566; CENSYa_0934. DR GeneID; 6371114; -. DR KEGG; csy:CENSYa_0934; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR Proteomes; UP000000758; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000758}; KW Methyltransferase {ECO:0000313|EMBL:ABK77566.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000758}; KW Transferase {ECO:0000313|EMBL:ABK77566.1}. SQ SEQUENCE 317 AA; 33421 MW; 56F87F9C0B1494A2 CRC64; MGRRVTFLEA ARGRVLLFDG AMGTEIQALD PGPEDFPDGK EGFNDGLVLS RPEWISKIHR SYIEAGADCI ETNSFGSNKI KLDEYGFGER TVEINEKAAS LAAAEAGRVE RDVYVVGSMG PTGYLPSSND PDLGQIPLDT IQDAFALQAE GLVRGGADAL IIETSQDILE VKLAIEGAHA AMEKSGSSVP LIANTTLDRY GKMLLGTTVQ AAYTTVSDMG IDFFGLNCST GPREMAPSVR WLSGQGHGLL VVPNAGMPEN DGGRSVYGMT PDDMAGVLGG FISEYPQVRM VGGCCGTTPA HISALRRAID GAQAGGR // ID A0XXK5_9GAMM Unreviewed; 356 AA. AC A0XXK5; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 27-MAY-2015, entry version 31. DE SubName: Full=Putative B12-dependent homocysteine-N5-methyltetrahydrofolate transmethylase (N terminal) {ECO:0000313|EMBL:EAW29208.1}; GN ORFNames=ATW7_10328 {ECO:0000313|EMBL:EAW29208.1}; OS Alteromonadales bacterium TW-7. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales. OX NCBI_TaxID=156578 {ECO:0000313|EMBL:EAW29208.1}; RN [1] {ECO:0000313|EMBL:EAW29208.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TW-7 {ECO:0000313|EMBL:EAW29208.1}; 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. {ECO:0000313|EMBL:EAW29208.1}. 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; AAVS01000002; EAW29208.1; -; Genomic_DNA. DR RefSeq; WP_006791479.1; NZ_AAVS01000002.1. DR ProteinModelPortal; A0XXK5; -. DR EnsemblBacteria; EAW29208; EAW29208; ATW7_10328. DR PATRIC; 24461917; VBIAltBac127053_0323. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EAW29208.1}; KW Transferase {ECO:0000313|EMBL:EAW29208.1}. SQ SEQUENCE 356 AA; 38817 MW; 25DB256237F866EC CRC64; MPNNTAANKQ AELSEALKER ILILDGAMGT MIQTHKLEEE DYRGERFKDW HVLIKGNNDL LSLTKPELIA DIHRGFLTAG ADIIETNTFN STTISMEDYD MASISREVNL ESAKLARSIC DEFTAKNPEK PRYVAGVLGP TSKTCSISPD VNDPGYRNVT FDKLVTAYVE STLALMEGGA DLILIETIFD TLNAKAASFA VEEAFEQAGR TLPVMISGTI TDASGRTLSG QTTEAFYNSI RHIKPISIGL NCALGPDLLR QYVEELSRVC ETFTSVHPNA GLPNEFGEYD LEAGDMAAEI IDWGKSGFIN IVGGCCGTTP EHIRAFAKGL EGVKPRALPE LDVRMRLSGL EACNLN // ID A0YB18_9GAMM Unreviewed; 1229 AA. AC A0YB18; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 01-APR-2015, entry version 51. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EAW31748.1}; GN ORFNames=GP2143_04840 {ECO:0000313|EMBL:EAW31748.1}; OS marine gamma proteobacterium HTCC2143. OC Bacteria; Proteobacteria; Gammaproteobacteria; OMG group; BD1-7 clade. OX NCBI_TaxID=247633 {ECO:0000313|EMBL:EAW31748.1}; RN [1] {ECO:0000313|EMBL:EAW31748.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2143 {ECO:0000313|EMBL:EAW31748.1}; 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 (DEC-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EAW31748.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2143 {ECO:0000313|EMBL:EAW31748.1}; RX PubMed=20601481; DOI=10.1128/JB.00683-10; RA Oh H.M., Kang I., Ferriera S., Giovannoni S.J., Cho J.C.; RT "Genome sequence of the oligotrophic marine Gammaproteobacterium RT HTCC2143, isolated from the Oregon Coast."; RL J. Bacteriol. 192:4530-4531(2010). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EAW31748.1}. 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; AAVT01000002; EAW31748.1; -; Genomic_DNA. DR RefSeq; WP_007224696.1; NZ_AAVT01000002.1. DR ProteinModelPortal; A0YB18; -. DR SMR; A0YB18; 654-1228. DR EnsemblBacteria; EAW31748; EAW31748; GP2143_04840. DR PATRIC; 25933838; VBIMarGam125067_1343. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1229 AA; 135967 MW; EB2A87018E01F16E CRC64; MTSRTNRISA LKELISQRIL IIDGAMGSMI QTYGLQEDDY RGDLLQDHHL DIKGNNDILS ITKPSIIEEI HNAYLDAGAD IIETNSFNAT RVAQGDYQLE SFSYEINVAS AKIARAAADR ATLKNPNKPR FVAGVLGPTP RTASISPDVN DPSARNTSFD QLSDDYYQST KGLIEGDVDI ILIETIFDTL NAKAAIFAVK RCFRDLGIEL PIMITVTFPD MSGRILSGQS PEGFWNSIAH AKPLIVGTNC GRRFKEIRPF IEELANVADC YFSGHFNAGL PNAFGEYDET PEDMFDDLKG FADRGFLNLV GGCCGTTPEH IAEIAKIADL CSPREIPLKP IACRLSGLEP FTISKESLFV NVGERCNVTG SAKFKRLIIE EDFDTALDVA REQVENGAQI IDINMDEGML DAQSAMVKFL KLIASEPDIS RVPIMVDSSK WEIIEAGLKC IQGKPIVNSI SLKEGENEFL EKAQLCLDYG AAVVVMAFDE KGQADTLERK MAICQRSYNL LVQQLDFPPQ DIIFDPNIFA VATGIEEHNN YAVDFIEATR FIKNTLPHAL VSGGVSNVSF SFRGNNPVRE AIHSVFLYYA IKAGLDMGIV NAGQLAIYDD LPQTLKDRVE DIVLNQRDDS TERLLDIAAD YVGDGAKKQA DNLEWRELPV EKRIEHALVK GITNFIIEDT EQARLIADRP ISVIEGPLMD GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AYLQPFIEDE KEEDAKANGK IIMATVKGDV HDIGKNIVGV VLQCNNYEVI DLGVMVSCSE ILRAAKEQNA DIIGLSGLIT PSLDEMVHVA KEMTREGFSI PLMIGGATTS KAHTAVKIEP QYDKAPIVYV PDASRSVSVA STLLNPESSI EFWKQRKEEY AVVRERIKNR KPKVKSLRYA AAAANRPTID WDNFNATKPM FEGTRVFENY SLSALVDTID WTPFFMSWEL AGKYPKILDD EVVGEAARNL FADAQMMLEK IINENLLMAK AVIGFWPANS INNDDIELYS GDETIATLHH IRQQTAKPNG KPNLSLADFI APAETGKQDY IGGFVVTAGI GAEQLAKSYE EANDDYSAIM VKALADRLAE SFAEHMHMRV RKEFWSYAAA EDLSNTELIK EKYRGIRPAP GYPACPDHTE KATLFKLLSP EDNIGVELTE NFAMSPAAAV SGFYYSHPQS SYFATGKISK DQVKSLAERK ALSVSEMERW LAPVLDYDN // ID A0YFF1_9GAMM Unreviewed; 306 AA. AC A0YFF1; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EAW30365.1}; GN ORFNames=GP2143_09175 {ECO:0000313|EMBL:EAW30365.1}; OS marine gamma proteobacterium HTCC2143. OC Bacteria; Proteobacteria; Gammaproteobacteria; OMG group; BD1-7 clade. OX NCBI_TaxID=247633 {ECO:0000313|EMBL:EAW30365.1}; RN [1] {ECO:0000313|EMBL:EAW30365.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2143 {ECO:0000313|EMBL:EAW30365.1}; 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 (DEC-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EAW30365.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2143 {ECO:0000313|EMBL:EAW30365.1}; RX PubMed=20601481; DOI=10.1128/JB.00683-10; RA Oh H.M., Kang I., Ferriera S., Giovannoni S.J., Cho J.C.; RT "Genome sequence of the oligotrophic marine Gammaproteobacterium RT HTCC2143, isolated from the Oregon Coast."; RL J. Bacteriol. 192:4530-4531(2010). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAW30365.1}. 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; AAVT01000008; EAW30365.1; -; Genomic_DNA. DR RefSeq; WP_007226228.1; NZ_AAVT01000008.1. DR ProteinModelPortal; A0YFF1; -. DR EnsemblBacteria; EAW30365; EAW30365; GP2143_09175. DR PATRIC; 25937206; VBIMarGam125067_3007. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 209 209 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 280 280 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 281 281 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 306 AA; 33016 MW; 46A7B3286B4BA1EB CRC64; MVMSKVVLLD GGMGQELLRR SSQKPHSMWS ARVLLEEPEI VEAVHRDYIE AGARVITLNN YSATPERMAR EGHPELFDIL QKKAIDIAKR ARDNSPRARD HDIKIAGCLP PLFASYKPEL APNFEECLER YRVIADIQKA DVDLFICETM SSIKEGTASA VAAASTGLPV WLGLTLEDNL EGRLRSGETL ADAMAPIVDL GVEALLLNCS MPESINAAIG TLINGYDTVG AYANGFTSIA ALKPGGTVEE LQARQDLSPN GYAKFALSWV DSGAKIIGGC CEVGPAHIAE LEQQLLAKGH EICSAL // ID A0YZR2_LYNSP Unreviewed; 1191 AA. AC A0YZR2; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 27-MAY-2015, entry version 53. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EAW33490.1}; GN ORFNames=L8106_04161 {ECO:0000313|EMBL:EAW33490.1}; OS Lyngbya sp. (strain PCC 8106) (Lyngbya aestuarii (strain CCY9616)). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Lyngbya. OX NCBI_TaxID=313612 {ECO:0000313|EMBL:EAW33490.1}; RN [1] {ECO:0000313|EMBL:EAW33490.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PCC 8106 {ECO:0000313|EMBL:EAW33490.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EAW33490.1}. 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; AAVU01000075; EAW33490.1; -; Genomic_DNA. DR RefSeq; WP_009787947.1; NZ_AAVU01000075.1. DR ProteinModelPortal; A0YZR2; -. DR EnsemblBacteria; EAW33490; EAW33490; L8106_04161. DR PATRIC; 30997321; VBILynSp34733_5914. DR OMA; DYNSIMV; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EAW33490.1}; KW Transferase {ECO:0000313|EMBL:EAW33490.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 228 228 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 737 737 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1191 AA; 132598 MW; 57D1F7F8DE8AF9CF CRC64; MKSLFLERLH SPERPVLVFD GAMGTNLQVQ NLTAEDFGGK EYEGCNEYLV HTKPEAVKTV HRGFLEAGSD VIETDTFGAT SIVLAEYDLA DIAYDLNKAA AQLAKAVTAE YSTPEKPRFV AGSIGPGTKL PTLGHIDYDT LEAAFTEQAE GLFDGDVDLF IVETCQDVLQ IKAALNGIEN VFKKKCERRP IMVSVTVEAF GTMLVGSEIS AALTILEPYS IDILGLNCAT GPDLMKEHIR YLSEYSPFVV SCIPNAGLPE NVGGQAHYKL TPTELKMALM HFIEDLGVQV IGGCCGTRPD HIKALAEIAQ TLKPKQRQTQ LIPSAASIYG TQTYEQENSF LIIGERLNAS GSKKCRTLLN EEDWDGLVAL AKSQVKEGAQ ILDVNVDYVG RDGVRDMHEL VSRLVTNVNL PLMLDSTEWE KMEAGLKVAG GKCLLNSTNY EDGEERFFKV LELAKKYGAG VVVGTIDEEG MARTAQKKFE IAKRAYHDAI NYGIPAHEIF FDTLALPIST GIEEDRENGK ATVESIRMIR AELPGCHIAL GVSNISFGLN PAARQVLNSV FLHECMAVGL DAAIVSASKI LPLAKIEPEH QEICRRLIYD QRQFDGEICV DDPLTKLTQL FEGKTTKKDR AATENLPIEE RLKQHIIDGE RIGLEDALVV ALEKYPPLDI INIYLLDGMK VVGELFGSGQ MQLPFVLQSA QTMKAAVAYL EPYMEKDDSN GSGKGTFLIA TVKGDVHDIG KNLVDIILSN NGYKVVNLGI KQPVDNIISA YREHHADCIA MSGLLVKSTA FMKDNLEAFN KEGISVPVIL GGAALTPKFV YDDCQNAYKG KVVYGKDAFS DLNFMEQLMP AKTSKKWDDC QGFLEEYAKE NNFFGNGKIK SETTTSEKSK SEEKDKEPAK PVEVDTRRSE VVEVDIERPT PPFWGTKVLQ PEDIPLDEVF WYLDLQALFA GQWQFRKPKD QSREEYDAFL AETVYPILAE WKQRILEENL LHPQAVYGYF PCQAEGNKLL IYDPEVMSSG EVKPTEPVEI IEFPRQLSGK RLCIADFFAP KESGIIDVFP MHAVTVGEIA TEIAQKLFAE DDYTNYLYFH GMAVQTAEAM AEWLHARVRQ ELGFGGEDAD NIKDILRQRY RGSRYSFGYP ACPNMQDQYK QLDLLKTDRI AMYMDESEQL YPEQSTTAIM TYHPIAKYFN T // ID A0Z3S4_9GAMM Unreviewed; 339 AA. AC A0Z3S4; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 27-MAY-2015, entry version 31. DE SubName: Full=Methionine synthase I {ECO:0000313|EMBL:EAW41464.1}; GN ORFNames=MGP2080_02031 {ECO:0000313|EMBL:EAW41464.1}; OS marine gamma proteobacterium HTCC2080. OC Bacteria; Proteobacteria; Gammaproteobacteria; OMG group; OM60 clade. OX NCBI_TaxID=247639 {ECO:0000313|EMBL:EAW41464.1}; RN [1] {ECO:0000313|EMBL:EAW41464.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2080 {ECO:0000313|EMBL:EAW41464.1}; 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 (APR-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EAW41464.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2080 {ECO:0000313|EMBL:EAW41464.1}; RX PubMed=20472793; DOI=10.1128/JB.00511-10; RA Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L., RA Giovannoni S.J.; RT "Genome sequences of strains HTCC2148 and HTCC2080, belonging to the RT OM60/NOR5 clade of the Gammaproteobacteria."; RL J. Bacteriol. 192:3842-3843(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. {ECO:0000313|EMBL:EAW41464.1}. 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; AAVV01000004; EAW41464.1; -; Genomic_DNA. DR RefSeq; WP_007234470.1; NZ_AAVV01000004.1. DR ProteinModelPortal; A0Z3S4; -. DR EnsemblBacteria; EAW41464; EAW41464; MGP2080_02031. DR PATRIC; 25926737; VBIMarGam104700_1229. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 339 AA; 35478 MW; 67882942A85FC226 CRC64; MENPISALIA DKGWCVADGA TGSNFFGRGL EAGYPPELWC LEKPEDVLWL HGEFLSAGSD LILTNSFGGN ALRLKLHQAE NRVRELNIAA ANLARQAVEA HAQKTGRKAL VAGSIGPTGE LFEPMGALTY EAAVTCFTEQ AEALAEGGAD VLWIETMSAN EEVAAAAEAG KKTGLPVCAT MTFDTAKRSM MGITPTDFVQ CAEELGLSVM GANCGVGPAE LMHSTREMLA TNSVIPVAAK GNCGIPEYVD GAIHYHGSPE LMAQYAVFAR DAGATVIGGC CGTTPEHVAA MVEALNSTSK GTFDAAAMDL ALGVAWKNLP DPNAADSETS SRRGRRKRA // ID A0Z416_9GAMM Unreviewed; 713 AA. AC A0Z416; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 27-MAY-2015, entry version 47. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EAW41053.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EAW41053.1}; DE Flags: Fragment; GN Name=metH {ECO:0000313|EMBL:EAW41053.1}; GN ORFNames=MGP2080_09408 {ECO:0000313|EMBL:EAW41053.1}; OS marine gamma proteobacterium HTCC2080. OC Bacteria; Proteobacteria; Gammaproteobacteria; OMG group; OM60 clade. OX NCBI_TaxID=247639 {ECO:0000313|EMBL:EAW41053.1}; RN [1] {ECO:0000313|EMBL:EAW41053.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2080 {ECO:0000313|EMBL:EAW41053.1}; 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 (APR-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EAW41053.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2080 {ECO:0000313|EMBL:EAW41053.1}; RX PubMed=20472793; DOI=10.1128/JB.00511-10; RA Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L., RA Giovannoni S.J.; RT "Genome sequences of strains HTCC2148 and HTCC2080, belonging to the RT OM60/NOR5 clade of the Gammaproteobacteria."; RL J. Bacteriol. 192:3842-3843(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. {ECO:0000313|EMBL:EAW41053.1}. 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; AAVV01000005; EAW41053.1; -; Genomic_DNA. DR RefSeq; WP_007234562.1; NZ_AAVV01000005.1. DR EnsemblBacteria; EAW41053; EAW41053; MGP2080_09408. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EAW41053.1}; KW Transferase {ECO:0000313|EMBL:EAW41053.1}. FT NON_TER 713 713 {ECO:0000313|EMBL:EAW41053.1}. SQ SEQUENCE 713 AA; 78202 MW; 1EB42009D71C5C8E CRC64; MLTSRFPKYS KASALTLIDA LEQQILLIDG AMGTMIQEQV LTEADYRGER FKDHPSDLKG NNDLLSLTRP NLISTIHETY LAAGADLIET NTFNATATAQ ADYQLETIIW DLNLEGARLA RGAADKFIQK TPEKPRFVAG VLGPTPRTAS ISPDVNDPGA RNITFDELRA DYQLATEALI EGGVDILMVE TVFDTLNAKA ALFGCREAMD KLGVELPIMV SATFPDTSGR LLSGQTGEAF WHAIAHARPL IVGSNCGRRF REVKPFLEEL AKVSSCYFSA HLNAGLPNAF GDYDETPQDM ATDFDTFAAQ GYLNLAGGCC GTTPEHIRSI ATSVADHQPR KLPALPQDTY LSGLESFSFT GKNFVNVGER CNVTGSARFK SLILDDQYEA ALDVARKQVE DGAQIIDINM DEGMLDAEAA MVRFLNLIAS EPDIARVPIM VDSSKWSVIE AGLKCIPGKS IVNSISLKAG EAEFLQQASL CQRYGASVVI MAFDEDGQAD TFERRKKICR RSYDLLRSEL DFNPFDIMFD PNIFAIGTGI EVHNNHAVDF IETARWIKEN LPGARISGGV SNVSFSFRGN NPVREAIHSV FLYHAIGAGL DMGIVNAGQL AVYDDLPANL KNAVEDLVLN RKDDATERLL ELAEEYRGSG SRSRVEDLTW REGPVANRLQ HALLKGITQF IEEDAEEARQ LSKRPIDVIE GPLMDGMNTV GDR // ID A0Z513_9GAMM Unreviewed; 306 AA. AC A0Z513; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EAW40907.1}; GN ORFNames=MGP2080_00490 {ECO:0000313|EMBL:EAW40907.1}; OS marine gamma proteobacterium HTCC2080. OC Bacteria; Proteobacteria; Gammaproteobacteria; OMG group; OM60 clade. OX NCBI_TaxID=247639 {ECO:0000313|EMBL:EAW40907.1}; RN [1] {ECO:0000313|EMBL:EAW40907.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2080 {ECO:0000313|EMBL:EAW40907.1}; 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 (APR-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EAW40907.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2080 {ECO:0000313|EMBL:EAW40907.1}; RX PubMed=20472793; DOI=10.1128/JB.00511-10; RA Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L., RA Giovannoni S.J.; RT "Genome sequences of strains HTCC2148 and HTCC2080, belonging to the RT OM60/NOR5 clade of the Gammaproteobacteria."; RL J. Bacteriol. 192:3842-3843(2010). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAW40907.1}. 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; AAVV01000006; EAW40907.1; -; Genomic_DNA. DR RefSeq; WP_007234909.1; NZ_AAVV01000006.1. DR ProteinModelPortal; A0Z513; -. DR EnsemblBacteria; EAW40907; EAW40907; MGP2080_00490. DR PATRIC; 25927679; VBIMarGam104700_1697. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 206 206 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 277 277 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 278 278 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 306 AA; 32451 MW; DBC89BE0D8B6C634 CRC64; MTTAITLLDG GMGQELIRRS SAAKPHPLWS LQVMMDEPEL VANVHRDFCL AGARVICLNT YSVTRHRLQM GNELPDLPEL LKHAGDLARA GIQASGLHGI DVVASLPPLT ASYLKQSPLS PTQMKDEYKE LMELQRHHVD GFLAETLSSV AEGEAVLRAA QEAGTGVHLA FTVQDEDGTL LRSGELLEDA LRACVPLKPL SVILNCSIPE AIDQGLPLVA QATEIFGAYA NGFHSVTALK PGGTVDVLTA REDLTPAAYT DMSLQWLELG ASILGGCCEV GPAHIEALAQ GIIGKGRQLS GLPAAA // ID A0ZGY7_NODSP Unreviewed; 1184 AA. AC A0ZGY7; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 27-MAY-2015, entry version 53. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AHJ27499.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AHJ27499.1}; GN ORFNames=NSP_11580 {ECO:0000313|EMBL:AHJ27499.1}; OS Nodularia spumigena CCY9414. OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nodularia. OX NCBI_TaxID=313624 {ECO:0000313|EMBL:AHJ27499.1, ECO:0000313|Proteomes:UP000019325}; RN [1] {ECO:0000313|EMBL:AHJ27499.1, ECO:0000313|Proteomes:UP000019325} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCY9414 {ECO:0000313|EMBL:AHJ27499.1}; RX PubMed=23555932; RA Voss B., Bolhuis H., Fewer D.P., Kopf M., Moke F., Haas F., RA El-Shehawy R., Hayes P., Bergman B., Sivonen K., Dittmann E., RA Scanlan D.J., Hagemann M., Stal L.J., Hess W.R.; RT "Insights into the physiology and ecology of the brackish-water- RT adapted Cyanobacterium Nodularia spumigena CCY9414 based on a genome- RT transcriptome analysis."; RL PLoS ONE 8:E60224-E60224(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; CP007203; AHJ27499.1; -; Genomic_DNA. DR RefSeq; WP_006197004.1; NZ_AAVW01000042.1. DR ProteinModelPortal; A0ZGY7; -. DR EnsemblBacteria; EAW44838; EAW44838; N9414_16539. DR PATRIC; 25519025; VBINodSpu128623_2714. DR Proteomes; UP000019325; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000019325}; KW Methyltransferase {ECO:0000313|EMBL:AHJ27499.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000019325}; KW Transferase {ECO:0000313|EMBL:AHJ27499.1}. SQ SEQUENCE 1184 AA; 131687 MW; 7E234B3DA32CEDD7 CRC64; MTHPFLEHLH SPNRPVIVFD GAMGTNLQSQ NLTAEDFGGP QYEGCNEYLV HTNPEAVAKV HRDFLAAGAD VIETDTFGAT SIVLAEYDLA DQTYYLNKTA VEIAKRVAAE FSTPEKPRFV AGSLGPTTKL PTLGHIDFDT LKANFAEQAE ALFDGGVDLF LVETCQDVLQ IKAALNGIEE VFAKKGDRRP LMVSVTMESM GTMLVGSEIN AVLTILAPYP IDILGLNCAT GPDLMKPHIK YLSEHSPFIV SCIPNAGLPE NVGGQAHYRL TPMELRMALM HFVEDLGVQV IGGCCGTRPE HIQQLAEISK TLKPKIRQHS LEPAAASIYS TQPYDQDNSF LIVGERLNAS GSKKCRDLLN AEDWDGLVSM ARAQVKEGAH ILDVNVDYVG RNGVRDMHEL VSRIVNNVTL PLMLDSTEWE KMEAGLKVAG GKCLLNSTNY EDGEPRFLKV LDLAKTHGAG IVIGTIDEDG MARTAERKFQ IAQRAYRQAV EHGIPPTEIF FDTLALPIST GIEEDRANGK ATVESIRRIR QELPGCHVIL GISNISFGLN PASRVVLNSM FLHEAMQAGM DAAIVSPNKI LPLSKIEEKH QKVCLDLIYD RRKFDGDVCV YDPLGELTTL FEGVTTKRDK GVDESLPLEE RLKRHIIDGE RIGLEKLLTT ALEQYPPLQI INTFLLDGMK VVGELFGSGQ MQLPFVLQSA ETMKTAVAYL EPFMEKSETD SNGKGTFIIA TVKGDVHDIG KNLVDIILTN NGYRVINLGI KQPVENIIQA YEEHKADCIA MSGLLVKSTA FMKDNLQAFN EKGITVPVIL GGAALTPKFV HQDCQNTYKG KVVYGKDAFS DLHFMDKLMP AKAGNNWDDL QGFLDEVVAD EAEITSEVIT EEAPTAQTPV PIDTRRSEAV AIDIQRPTPP FWGTQLLTPG DIPIEEVLWH LDLQALIAGQ WQFRKPKEQS KEEYQAFLAE TVYPILESWK QRVIEENLLH PQVVYGYFPC QSEGNTLYVY ETFAERARSA YRQVAKDAKV RASFEFPRQR SLRRLCIADY FAPKESGVID VFPMQAVTVG DIATEFAQKL FADNQYTDYL YFHGLAVQVA EALAEWTHAR IRRELGFGAD EPDNIRDILA QRYQGSRYSF GYPACPNIQD QYKQLELLEA DRINLYMDES EQIYPEQSTT AIIAYHPVAK YFSA // ID A1A234_BIFAA Unreviewed; 81 AA. AC A1A234; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 27-MAY-2015, entry version 33. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:BAF39767.1}; GN Name=mmuM {ECO:0000313|EMBL:BAF39767.1}; GN OrderedLocusNames=BAD_0986 {ECO:0000313|EMBL:BAF39767.1}; OS Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC OS 11814 / E194a). OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=367928 {ECO:0000313|EMBL:BAF39767.1, ECO:0000313|Proteomes:UP000008702}; RN [1] {ECO:0000313|EMBL:BAF39767.1, ECO:0000313|Proteomes:UP000008702} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a RC {ECO:0000313|Proteomes:UP000008702}; 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 ----------------------------------------------------------------------- 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; BAF39767.1; -; Genomic_DNA. DR RefSeq; WP_011743350.1; NC_008618.1. DR RefSeq; YP_909849.1; NC_008618.1. DR STRING; 367928.BAD_0986; -. DR EnsemblBacteria; BAF39767; BAF39767; BAD_0986. DR KEGG; bad:BAD_0986; -. DR eggNOG; COG2040; -. DR KO; K00547; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; BADO367928:GHPT-1033-MONOMER; -. DR Proteomes; UP000008702; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008702}; KW Methyltransferase {ECO:0000313|EMBL:BAF39767.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008702}; KW Transferase {ECO:0000313|EMBL:BAF39767.1}. SQ SEQUENCE 81 AA; 8767 MW; 612F7EC3D85B141B CRC64; MLPAIRAIRQ VTDKPIIVYP NNGDIYDPKT KTWSPNPTGS EPAFAHLVPQ WIDAGARLIG GCCRTTPDDI RTIAHAASAN V // ID A1AKP7_PELPD Unreviewed; 615 AA. AC A1AKP7; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 29-APR-2015, entry version 63. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; DE Flags: Precursor; GN OrderedLocusNames=Ppro_0283 {ECO:0000313|EMBL:ABK97917.1}; OS Pelobacter propionicus (strain DSM 2379). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Pelobacteraceae; Pelobacter. OX NCBI_TaxID=338966 {ECO:0000313|EMBL:ABK97917.1, ECO:0000313|Proteomes:UP000006732}; RN [1] {ECO:0000313|EMBL:ABK97917.1, ECO:0000313|Proteomes:UP000006732} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2379 {ECO:0000313|EMBL:ABK97917.1, RC ECO:0000313|Proteomes:UP000006732}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Note=FAD.; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {ECO:0000256|RuleBase:RU004255}. CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ABK97917.1; -; Genomic_DNA. DR RefSeq; WP_011734231.1; NC_008609.1. DR RefSeq; YP_899975.1; NC_008609.1. DR ProteinModelPortal; A1AKP7; -. DR STRING; 338966.Ppro_0283; -. DR EnsemblBacteria; ABK97917; ABK97917; Ppro_0283. DR KEGG; ppd:Ppro_0283; -. DR PATRIC; 22893593; VBIPelPro64470_0438. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; PPRO338966:GHL0-283-MONOMER; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000006732; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004255}; KW Complete proteome {ECO:0000313|Proteomes:UP000006732}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ABK97917.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000006732}; KW Transferase {ECO:0000313|EMBL:ABK97917.1}. SQ SEQUENCE 615 AA; 64692 MW; BE0CFD9BB87BD80F CRC64; MNILERLKGE VLTGDGALGT MLYARGVGLD SSFEQLNLTR PALVRELADD YVAAGAQVIE TNTFGANYTR LAALGLEQRV WEINLAGARI ARQAADQGRD VLVAGSVGPL PRIRGDEAES DQERMAELFR VQCQALAEGG VDLLLLETFS SLTQLAAAVQ AARCTGLTVA ASMAFLEGGR SADGATVEEF CAAMERAGAD LVGANCGAGP LELVKVVRRL AAVTHKPITA YANSGFPEYH DGRFIYRATP EYLATMAGEL VAAGASLVGG CCGTTPEHIA AISRALSGRC PASRAGAAAV RVGEPEQRPS SSGGSFLDAW GRRKLITVEL DPPKGLDCSR IIEGCRRLKR AGVDAINLAE NPLARPRMGN IALGSLIQQQ VGIPVIIHVT GRDRNLIGMQ SDLMGASLLG IRSVLAVTGD PATMGDHAGA TSVFDLHSLT LIKLLADLNR GVNAMGNPIG GGAGFTIGAA FNPNARDMAG QASRLRKKVA NGAMFAQTQP IYDAGLFFQA LELTADCAIP LIPGIMPLVS QRNADYLHNE VPGISIPETV LARMCGLEKE AGVAEGLAIA REFIDASFHS SGGYYLMPPF GKVELALDLI EYIHTKEREP SCGES // ID A1ANV9_PELPD Unreviewed; 806 AA. AC A1ANV9; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 27-MAY-2015, entry version 59. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABK99029.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABK99029.1}; GN OrderedLocusNames=Ppro_1413 {ECO:0000313|EMBL:ABK99029.1}; OS Pelobacter propionicus (strain DSM 2379). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Pelobacteraceae; Pelobacter. OX NCBI_TaxID=338966 {ECO:0000313|EMBL:ABK99029.1, ECO:0000313|Proteomes:UP000006732}; RN [1] {ECO:0000313|EMBL:ABK99029.1, ECO:0000313|Proteomes:UP000006732} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2379 {ECO:0000313|EMBL:ABK99029.1, RC ECO:0000313|Proteomes:UP000006732}; 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; ABK99029.1; -; Genomic_DNA. DR RefSeq; WP_011735322.1; NC_008609.1. DR RefSeq; YP_901087.1; NC_008609.1. DR ProteinModelPortal; A1ANV9; -. DR STRING; 338966.Ppro_1413; -. DR EnsemblBacteria; ABK99029; ABK99029; Ppro_1413. DR KEGG; ppd:Ppro_1413; -. DR PATRIC; 22895905; VBIPelPro64470_1569. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PPRO338966:GHL0-1438-MONOMER; -. DR Proteomes; UP000006732; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006732}; KW Methyltransferase {ECO:0000313|EMBL:ABK99029.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006732}; KW Transferase {ECO:0000313|EMBL:ABK99029.1}. SQ SEQUENCE 806 AA; 86169 MW; B947BCE22347A7A5 CRC64; MTPFLEAIQE RVLILDGAMG TMLQERGLRP GQSPEELNLT MPDVVASVHR EYIEAGADII ITNSFGGSRF KLAHFGLEGR LAEINARAVE IARGEARGRA YVGGSMGPTG QFVEPLGEVS FDRMKESFRE QAEALVSAGV DLISLETFLD IKECRAAVIA IREVSPTIPI IAMMTFDDNG RSVLGTPPEA AAITLAAAGV DIVGSNCGLG VEGIHDILVR MRRVTSLPLI SQANAGLPIL KDGITVFPGT PREMTDYHDR LISLGVRVIG GCCGTTPAHI RAMKEALAGR QQVWQEPTHL EGMTLLSCRG GWTAVGPGQK TAIIGERINP TGKKLYSKEL QEGKVSYIRR EAMEQAQLGA TLLDLNVGAP GIDEPVAMER AVFCASGAVG VPLVLDSSSP AALEAGLKAA DGKVLINSVS GEAKSLSRVL PLAKKYGAAL IGLTLDAKGI PDSAEGRLAI ARRIRNAARR QGIPDQDIII DCLTLTVSAE QKRAAETLRT IRLVKEKLGL STVLGVSNIS FGLPQRPLIS SSFFSMAMAA GLDAAIINPR EKAMMDAWRS AMVLLNRDPR AEAFIQTYRD EQAVATPAAP VSDAPQEIRQ RLGQAVINGD RDGIIGLVEE ALAQGLAPLQ ISNEGFLPGL EEVGRRFEKN IFFLPQVMQS ADTMHAGFAR LKEEMKGQPL ESRGRILMAT VEGDIHDIGK NIVCTLLENH GFEVFDIGKN VSAATIVAKA REFGVDAVGL SALMTTTMAE MDTVLKKLKA VGIKAFTMIG GAVVTQEYAD RIGADIYARD AMEAVAKVKK LLQIAD // ID A1B3D4_PARDP Unreviewed; 1250 AA. AC A1B3D4; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 27-MAY-2015, entry version 63. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABL70028.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABL70028.1}; GN OrderedLocusNames=Pden_1935 {ECO:0000313|EMBL:ABL70028.1}; OS Paracoccus denitrificans (strain Pd 1222). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Paracoccus. OX NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL70028.1, ECO:0000313|Proteomes:UP000000361}; RN [1] {ECO:0000313|Proteomes:UP000000361} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000489; ABL70028.1; -; Genomic_DNA. DR RefSeq; WP_011748225.1; NC_008686.1. DR RefSeq; YP_915724.1; NC_008686.1. DR ProteinModelPortal; A1B3D4; -. DR SMR; A1B3D4; 669-1241. DR STRING; 318586.Pden_1935; -. DR EnsemblBacteria; ABL70028; ABL70028; Pden_1935. DR KEGG; pde:Pden_1935; -. DR PATRIC; 22854985; VBIParDen97112_1870. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PDEN318586:GCVQ-1965-MONOMER; -. DR Proteomes; UP000000361; Chromosome 1. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000361}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABL70028.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000361}; KW Transferase {ECO:0000313|EMBL:ABL70028.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 259 259 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 777 777 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1250 AA; 135996 MW; D2ED6A49A2E927B2 CRC64; MILPLSPVFD AMRAAARDRI LILDGAMGTQ IQQLGLSETD FAGHGTGCAC GCHPPAPGEH PQQGNNDLLN LTQPKAIEEI HYRYAKAGAD IVETNTFSST TIAQADYGME AAVYDLNFHG ARIARQALDR ATAEDGRPRW VAGALGPTNR TASISPDVNN PGYRAVTFDD LRIAYAEQIR GLIDGGADLI LIETIFDTLN AKAAIFACEE VFQDKGQRLP VMISGTITDL SGRTLSGQTP TAFWYSMRHA APITVGLNCA LGAAAMRPHL AELSTVADTL ICAYPNAGLP NEMGQYDETP EEMAAQVAEF AREGLVNVVG GCCGSTPEHI AAIARAVADL PPRAIPEIEP RLRLSGLEPF VKTDDIPFVN VGERTNVTGS ARFRKLITNG DYAAALDVAR DQVENGAQII DVNMDEGLID SKQAMIDYLN LIAAEPDIAR VPVMIDSSKW EVIEAGLKCV QGKAIVNSIS LKEGEEGFLN QARLCRRYGA AVVVMAFDET GQADTENRKV EICSRAYDLL VNAVGFPPED IIFDPNIFAV ATGIEEHDNY GVDFIGATRR ITQALPHVHV SGGVSNLSFS FRGNEPVREA MHAVFLYHAI QAGMDMGIVN AGQLAVYDQI DAGLREACED VVLNRQPKAG GTATENMLEI AERFRGEGGA KAREKDLTWR TWPVAKRLEH ALVNGITEYI DEDTEEARLS VERPLHVIEG PLMAGMNVVG DLFGSGKMFL PQVVKSARVM KQAVAHLLPY MEAEKAGSGA SSSAGKVLMA TVKGDVHDIG KNIVGVVLAC NNYEIIDLGV MVPATKILET AKAENVDIIG LSGLITPSLD EMVHVASEME REGFDIPLLI GGATTSRVHT AVKIHPRYGR GQAVYVTDAS RAVGVVGSLL SGQKNAYVEN IRSEYMDVAN KHARAEADKK RLPLATARDN AVRIDWTGFQ AKAPEFLGSR VIEDFDLAEI ARYIDWTPFF QTWELKGVYP RILDDEKQGE VARQLFADAQ AMLTRIIDEQ WFKPRAVIGF WPANRVGDDI RLFTAEDRAA ELATLHTLRQ QVTKRDGRPN VALADFVAPE GHRDYVGGFV VTAGGEEQQI ADRFKAAHDD FSAILVQALA DRFAEALAEM MHERVRRQYW GYADEAFSPE ELIAEPYAGI RPAPGYPAQP DHTEKVTLFR LLDATAATGV ELTESMAMWP GASVSGLYIG HPDAYYFGVA KVEHDQVLDY ADRKGMPVSQ VERWLAPILN YTPQAAVAAE // ID A1B924_PARDP Unreviewed; 319 AA. AC A1B924; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 27-MAY-2015, entry version 45. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABL72018.1}; GN OrderedLocusNames=Pden_3952 {ECO:0000313|EMBL:ABL72018.1}; OS Paracoccus denitrificans (strain Pd 1222). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Paracoccus. OX NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL72018.1, ECO:0000313|Proteomes:UP000000361}; RN [1] {ECO:0000313|Proteomes:UP000000361} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; ABL72018.1; -; Genomic_DNA. DR RefSeq; WP_011750185.1; NC_008687.1. DR RefSeq; YP_917714.1; NC_008687.1. DR ProteinModelPortal; A1B924; -. DR STRING; 318586.Pden_3952; -. DR EnsemblBacteria; ABL72018; ABL72018; Pden_3952. DR KEGG; pde:Pden_3952; -. DR PATRIC; 22859056; VBIParDen97112_3883. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265278; -. DR OMA; GTNLFAM; -. DR OrthoDB; EOG693GKH; -. DR BioCyc; PDEN318586:GCVQ-3995-MONOMER; -. DR Proteomes; UP000000361; Chromosome 2. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000361}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ABL72018.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000361}; KW Transferase {ECO:0000313|EMBL:ABL72018.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 212 212 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 278 278 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 279 279 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 319 AA; 33352 MW; 40904D12670BCA68 CRC64; MPDQLSRMLG ERPWLLADGA TGTNLYNMGL APGQAPDLWC ETHPEKVREL HRQMIASGAD IILTNSFGAN ASRLRLAKAQ DKVAQLNRAA ARLAREAAAE VGRAVVVAGS IGPIGEIMAP MGRLTEAEAA AMFTEQAQAL KEGGADLLWV ETISAVEEMR AAAKAAQAVG MPWCGMMSFE PGGRSMMGVT PPQLASLIDR LSHPPIAYGA NCGTGPAELL LAVAGFAASG NERPLIAKPN AGVPRYQDGG LIYDATPEVM AEFAVLARDL GVRIVGGCCG TTPEHLAAMR DALVAAPRGP RPSPERISAR IAEVMGPGE // ID A1BI87_CHLPD Unreviewed; 1249 AA. AC A1BI87; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 29-APR-2015, entry version 66. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABL66114.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABL66114.1}; GN OrderedLocusNames=Cpha266_2102 {ECO:0000313|EMBL:ABL66114.1}; OS Chlorobium phaeobacteroides (strain DSM 266). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Chlorobium. OX NCBI_TaxID=290317 {ECO:0000313|EMBL:ABL66114.1, ECO:0000313|Proteomes:UP000008701}; RN [1] {ECO:0000313|EMBL:ABL66114.1, ECO:0000313|Proteomes:UP000008701} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 266 {ECO:0000313|EMBL:ABL66114.1, RC ECO:0000313|Proteomes:UP000008701}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000492; ABL66114.1; -; Genomic_DNA. DR RefSeq; WP_011745916.1; NC_008639.1. DR RefSeq; YP_912538.1; NC_008639.1. DR ProteinModelPortal; A1BI87; -. DR SMR; A1BI87; 648-894. DR STRING; 290317.Cpha266_2102; -. DR EnsemblBacteria; ABL66114; ABL66114; Cpha266_2102. DR KEGG; cph:Cpha266_2102; -. DR PATRIC; 21392696; VBIChlPha122104_2508. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CPHA290317:GHX4-2143-MONOMER; -. DR Proteomes; UP000008701; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008701}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABL66114.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008701}; KW Transferase {ECO:0000313|EMBL:ABL66114.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1249 AA; 137726 MW; 3454F407A7B1561E CRC64; MKNSLINLLE TRILVLDGAM GTMIQRHKLQ EEDYRGTRFA SHSHPLIGNN DMLVLTQPDI IHAIHCDFLD AGSDIIETNT FNANPISQAD YHAEHLVREL NVEAAKLARK AADAFTARNP EKPRFVAGSI GPTNKTLSLS PDVNNPGYRA VTFRNVVDNY IMQLEGLMEG GVDLLLVETV FDTLNCKAAL FAIEEFFNRI GKHIPVMVSG TVVDASGRTL SGQTTEAFWI SIAHMPDLLS VGLNCALGSK QMRPFIESLS GIAESYVSVY PNAGLPNEFG EYDDSPAYMA EQIAGFATSG FVNIVGGCCG TTPQHIEAIA EAVQALEPRK RPHREHELKL SGLEPLVVNS TTGFINVGER TNVTGSKKFA RLVKEGNYDE ALSIARQQVE SGAQVIDVNV DEGMLDSEKV MREFLNLIGS EPEISRVPIM IDSSKWSVIE NGLQCVQGKS IVNSISLKEG EDLFRERAQK VLQYGAAAIV MAFDEQGQAD SYARRIEICK RAYDLLTMEV GFPPEDIIFD PNVLTVATGI DEHNNYAVDF IETVRWIKEN LPYAKVSGGI SNVSFSFRGN EPVREAMHAA FLYHAIRAGL DMGIVNAGQL AIYEDIDPEL LERVEDVLLN RRPDATERLV SFAETIQGDG EKTEAKAAEW RSFPVEERLR HALIKGIVEY IEEDTEEARL LYPSPLQVIE GPLMNGMNAI GDLFAVGKMF LPQVVKSARV MKRSVACLIP WIEKEKAANK DTRAAAKVLL ATVKGDVHDI GKNIVAVVLA CNNYDVVDIG VMMPCEKILE AAEREKADLI GLSGLITPSL DEMVHVAREM ERLGMTIPLL IGGATTSRIH TAVKIAPVYS GPVIQVLDAS RSVPVVSSLL NPALSETYIG QLKKEQAELR EGHAARAAGN KYLSLPDARK NRAKLQWDDT TVYNPLKPGI TLIEDATVEA LRPYIDWTPL FLTWELHGRY PQIFDHKEYG NEAKKLFDDA NKLLDRIEKE KLLGLRGVAG IFPASSNGDD IDVFTDESRS TVLTTFHTLR QQQEKKAGEP NLALADFIAP EKSGIKDYIG CFAVTAGLGI ERTLKQFSEE QDDYHRIMTQ ALADRLAEAF AEMLHEKVRK ELWGYAPDRC VKNNIPCACH PVPAGKTEHE ALGIEALLAE KYQGIRPASG YPACPDHTEK AELFTLLNAE TSTGITLTET FAMNPAASVS GLYFAHPAAK YFVLGKIGRD QVEDYAVRKG MSVEQAERWL APALNYDPE // ID A1C5J4_ASPCL Unreviewed; 342 AA. AC A1C5J4; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 27-MAY-2015, entry version 37. DE SubName: Full=Homocysteine S-methyltransferase, putative {ECO:0000313|EMBL:EAW14962.1}; GN ORFNames=ACLA_003750 {ECO:0000313|EMBL:EAW14962.1}; 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 {ECO:0000313|Proteomes:UP000006701}; RN [1] {ECO:0000313|Proteomes:UP000006701} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 RC {ECO:0000313|Proteomes:UP000006701}; 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; DS027004; EAW14962.1; -; Genomic_DNA. DR RefSeq; XP_001276388.1; XM_001276387.1. DR ProteinModelPortal; A1C5J4; -. DR STRING; 5057.CADACLAP00000163; -. DR EnsemblFungi; CADACLAT00000167; CADACLAP00000163; CADACLAG00000167. DR GeneID; 4708421; -. DR KEGG; act:ACLA_003750; -. DR EuPathDB; FungiDB:ACLA_003750; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000006701; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006701}; KW Methyltransferase {ECO:0000313|EMBL:EAW14962.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006701}; KW Transferase {ECO:0000313|EMBL:EAW14962.1}. SQ SEQUENCE 342 AA; 37408 MW; 8210AE444DE8BFEE CRC64; MASIEILDGG LGTSLQDQHG VTFDSSTPLW ASHLLVSDPT TLLACQRNFI NADTDVLLTA TYQVSIEGFE RTKTVDYPTG IPRNAIAKYL RTAIDIAEQA KGNSTAKIAL SLGPYGACMI PGQEYSGKYD AEHDTEEKLF QWHLERLRLF QEADERLSER VQYVAFETLP RLDEIRAVKR AIHAAGLNVP FWVACVFPGE QAALPDGSSV EEVVTAALAE MPDQSVPWGI GINCTKIHKL NGLMRNFGEK IASAMAAGRV STVPTLVLYP DGTNGEVYNT TTQTWEKPEG YTNDDARPWE KQLGQIVNDA GANGPFTSFL VGGCCKASHN DIRKLAEQLK SQ // ID A1CCT5_ASPCL Unreviewed; 308 AA. AC A1CCT5; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 27-MAY-2015, entry version 35. DE SubName: Full=Homocysteine S-methyltransferase, putative {ECO:0000313|EMBL:EAW12342.1}; GN ORFNames=ACLA_063090 {ECO:0000313|EMBL:EAW12342.1}; 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 {ECO:0000313|Proteomes:UP000006701}; RN [1] {ECO:0000313|Proteomes:UP000006701} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 RC {ECO:0000313|Proteomes:UP000006701}; 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; DS027050; EAW12342.1; -; Genomic_DNA. DR RefSeq; XP_001273768.1; XM_001273767.1. DR ProteinModelPortal; A1CCT5; -. DR STRING; 5057.CADACLAP00005617; -. DR EnsemblFungi; CADACLAT00005754; CADACLAP00005617; CADACLAG00005754. DR GeneID; 4706051; -. DR KEGG; act:ACLA_063090; -. DR EuPathDB; FungiDB:ACLA_063090; -. DR HOGENOM; HOG000179103; -. DR OMA; CCGTDHR; -. DR OrthoDB; EOG7XH70V; -. DR Proteomes; UP000006701; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006701}; KW Methyltransferase {ECO:0000313|EMBL:EAW12342.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006701}; KW Transferase {ECO:0000313|EMBL:EAW12342.1}. SQ SEQUENCE 308 AA; 33640 MW; 2BEE39E743C50A28 CRC64; MTLPQLFSPK LFLAECGTDT MLVYKDKIPL PCFSSLPLVN TEPGRKIILH YYKVYIEIAT ANGTGIVLDT RTWRGAAPWA QALGLSVAQL LELNRGAVRL AKEARRAATV PVAISGTMGP LRDAYEDTTD LLTLEEARAG YREQVYVLAD AGVDLLTLLT MTNLCEIIAV VELAREVGLP VVVSFMVQED GRMLGGQSLE SAIRTVDDRT GGYVSYYGVN CVHPLRIVNA LRDMPEDVRS RIGMIKGNAS MKSHHELDNT DTLDRGDIAV FTAGVEQVLA YVPNLRVLGG CCGTDEEHLE AVAKRCIK // ID A1D0G5_NEOFI Unreviewed; 343 AA. AC A1D0G5; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 29-APR-2015, entry version 36. DE SubName: Full=Homocysteine S-methyltransferase, putative {ECO:0000313|EMBL:EAW24485.1}; GN ORFNames=NFIA_040610 {ECO:0000313|EMBL:EAW24485.1}; 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 {ECO:0000313|Proteomes:UP000006702}; RN [1] {ECO:0000313|Proteomes:UP000006702} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181 RC {ECO:0000313|Proteomes:UP000006702}; 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; DS027686; EAW24485.1; -; Genomic_DNA. DR RefSeq; XP_001266382.1; XM_001266381.1. DR STRING; 36630.CADNFIAP00003656; -. DR EnsemblFungi; CADNFIAT00003745; CADNFIAP00003656; CADNFIAG00003745. DR GeneID; 4592494; -. DR KEGG; nfi:NFIA_040610; -. DR EuPathDB; FungiDB:NFIA_040610; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; NCTKIYK; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000006702; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006702}; KW Methyltransferase {ECO:0000313|EMBL:EAW24485.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006702}; KW Transferase {ECO:0000313|EMBL:EAW24485.1}. SQ SEQUENCE 343 AA; 37164 MW; C1943C90CDFCD9BA CRC64; MASIQILDGG LGTSLQDQHG VTFDSSTPLW ASHLLVSDPT TLLACQRDFI TAGSDILLTA TYQVSIEGFA RTKTPEFPDG IPRPAIGKYL RTALAVAEQA RVCPSAAKIA LSLGPYGACM IPGQEYSGKY DAEHDSEETL FQWHLERLRL FLEADEKLAE RVQYVAFETL PRLDEIRAVR RAIRAAGLDV PFWVACVFPG EGATLPDGSS IGQIVQAALA EMDGAAVPWG LGINCTKIYK LDGLVREFGE EVASAVGKGQ VGAVPSLVLY PDGTNGEVYN TTTQTWEKRE RYTSDERGPW EAQLAHVVTN ARATGPFTSF LVGGCCKASH NDIRKLAEQL KSE // ID A1DJI9_NEOFI Unreviewed; 313 AA. AC A1DJI9; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 29-APR-2015, entry version 35. DE SubName: Full=Homocysteine S-methyltransferase, putative {ECO:0000313|EMBL:EAW16878.1}; GN ORFNames=NFIA_002280 {ECO:0000313|EMBL:EAW16878.1}; 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 {ECO:0000313|Proteomes:UP000006702}; RN [1] {ECO:0000313|Proteomes:UP000006702} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181 RC {ECO:0000313|Proteomes:UP000006702}; 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; DS027697; EAW16878.1; -; Genomic_DNA. DR RefSeq; XP_001258775.1; XM_001258774.1. DR STRING; 36630.CADNFIAP00000468; -. DR EnsemblFungi; CADNFIAT00000477; CADNFIAP00000468; CADNFIAG00000477. DR GeneID; 4585314; -. DR KEGG; nfi:NFIA_002280; -. DR EuPathDB; FungiDB:NFIA_002280; -. DR HOGENOM; HOG000179103; -. DR OMA; CCGTDHR; -. DR OrthoDB; EOG7XH70V; -. DR Proteomes; UP000006702; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006702}; KW Methyltransferase {ECO:0000313|EMBL:EAW16878.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006702}; KW Transferase {ECO:0000313|EMBL:EAW16878.1}. SQ SEQUENCE 313 AA; 33731 MW; 5823CF1EC6B00556 CRC64; MALPQLLSPK PFLTECGMET CLVYKDKVHL PCFSSLPLVD SDSSRKLISH YYDSYISVAA TNGTGIVLDT RTWRGATPWA QPMGLSADKL LELNHAAVRL AKEARNKAVG GENNIPVVIS GTMGPLRDAY EDTSESITLE DAREGYREQV EVLADAGVDM LAIMTVTNLN EAIAVVELAK EVRLPVVVSF SIESDGRLLG GRSLESAIRT VDEKTGGYVV YYGVNCAHPV RISAALRDVP EDVRGRIGLI KGNASLKSHD ELDNSGTLDR GDISAFTDGF EGVLPLVPNV KVIGGCCGTD EEHLEAIAKR CIK // ID A1JRW4_YERE8 Unreviewed; 1231 AA. AC A1JRW4; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 27-MAY-2015, entry version 64. DE SubName: Full=5-Methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:CAL13894.1}; GN Name=metH {ECO:0000313|EMBL:CAL13894.1}; GN OrderedLocusNames=YE3875 {ECO:0000313|EMBL:CAL13894.1}; 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 {ECO:0000313|EMBL:CAL13894.1, ECO:0000313|Proteomes:UP000000642}; RN [1] {ECO:0000313|EMBL:CAL13894.1, ECO:0000313|Proteomes:UP000000642} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC 13174 / 8081 {ECO:0000313|Proteomes:UP000000642}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AM286415; CAL13894.1; -; Genomic_DNA. DR RefSeq; WP_011817311.1; NC_008800.1. DR RefSeq; YP_001008020.1; NC_008800.1. DR ProteinModelPortal; A1JRW4; -. DR SMR; A1JRW4; 655-1231. DR STRING; 393305.YE3875; -. DR EnsemblBacteria; CAL13894; CAL13894; YE3875. DR GeneID; 4714710; -. DR KEGG; yen:YE3875; -. DR PATRIC; 18567580; VBIYerEnt11519_4122. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR Proteomes; UP000000642; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000642}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAL13894.1}; KW Transferase {ECO:0000313|EMBL:CAL13894.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 252 252 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 315 315 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 316 316 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 763 763 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1231 AA; 136353 MW; 003D94500C756736 CRC64; MVDTVTNNKV KELHQQLAQR ILVLDGGMGT MIQSYRLEEA DYRGVRFADW PSDLKGNNDL LVLSKPEVIT AIHNAYLEAG ADILETNTFN STSIAMADYQ MESLSAEINY EAARLARICA DEWTARTPDK PRYVAGVLGP TNRTASISPK VNDPAFRNVS FDQLVEAYRE STRALIEGGV DLIMIETVFD TLNAKAATFA VESEFEAMGV LLPVMISGTI TDASGRTLSG QTTEAFYNSL RHVKPLSFGL NCALGPDELR QYVAELSRIS EYYVSAHPNA GLPNAFGEYD LEAKEMAEQI GEWARAGFLN IVGGCCGTTP RHIAAMVKAV AGVAPRPLPE IPVACRLAGL EPLTIDANTL FVNVGERTNV TGSARFKRLI KEEKYGEALD VARQQVESGA QIIDINMDEG MLDAEAAMVR FLNLIAGEPD IARVPIMIDS SKWDVIEKGL KCIQGKGIVN SISMKEGVDA FIHHAKLVRR YGAAMVVMAF DEQGQADTRA RKIEICRRAY KILTETVGFP PEDIIFDPNI FAVATGIEEH NNYAVDFIEA CADIKAELPH AMISGGVSNV SFSFRGNDPV REAIHAVFLY YAIRNGMDMG IVNAGQLAIY DDLSDELRNA VEDVILNRRD DSTERLLDLA EKYRGSKSDE VAVQQAEWRG WPVKKRLEYS LVKGITEFIE LDTEEARQQA DRPIEVIEGP LMAGMNVVGD LFGEGKMFLP QVVKSARVMK QAVAYLEPYI EASKQKGTTA GKILLATVKG DVHDIGKNIV GVVLQCNNYE IIDLGVMVPT EKILRTAREE KVDIIGLSGL ITPSLDEMVN VAKEMERQGF NLPLLIGGAT TSKAHTAVKI EQNYSGSTTY VSNASRSVGV VSALLSDTQR DDFVAKIRKE YETVRIQHAR KKPRTPPVSL QAARDNPTVI DWESYTPPVA HKLGVQTVEA SIETLRNYID WTPFFMTWSL AGKYPRILED EVVGEEAKRL FADANEMLDK LSAEGLLHPK GVVGLFPANS VGDDIEIYRD ERRDEVLVVS HHLRQQTEKT DFPNYCLADY VAPKSSGKAD YYGAFAVTGG LEEDALADAY DAQHDDYNKI MIKALSDRLA EAFAEYLHER VRKVYWGFAP NENLSNEELV RENYQGIRPA PGYPACPEHT EKSQIWQLLD VETHTGMKLT ESYAMWPGAS VSGWYFSHPD SKYFAVAQIQ RDQVEDYAAR KGMPVAEVER WLAPNLGYDA D // ID A1KBY6_AZOSB Unreviewed; 1233 AA. AC A1KBY6; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 29-APR-2015, entry version 64. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CAL96342.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAL96342.1}; GN Name=metH {ECO:0000313|EMBL:CAL96342.1}; GN OrderedLocusNames=azo3726 {ECO:0000313|EMBL:CAL96342.1}; OS Azoarcus sp. (strain BH72). OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Rhodocyclaceae; Azoarcus. OX NCBI_TaxID=62928 {ECO:0000313|EMBL:CAL96342.1, ECO:0000313|Proteomes:UP000002588}; RN [1] {ECO:0000313|EMBL:CAL96342.1, ECO:0000313|Proteomes:UP000002588} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BH72 {ECO:0000313|EMBL:CAL96342.1, RC ECO:0000313|Proteomes:UP000002588}; 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., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AM406670; CAL96342.1; -; Genomic_DNA. DR RefSeq; WP_011767448.1; NC_008702.1. DR RefSeq; YP_935228.1; NC_008702.1. DR ProteinModelPortal; A1KBY6; -. DR SMR; A1KBY6; 658-905. DR STRING; 62928.azo3726; -. DR EnsemblBacteria; CAL96342; CAL96342; azo3726. DR KEGG; azo:azo3726; -. DR PATRIC; 21015894; VBIAzoSp26047_3765. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR Proteomes; UP000002588; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002588}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAL96342.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002588}; KW Transferase {ECO:0000313|EMBL:CAL96342.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 769 769 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1233 AA; 134014 MW; FF7EF774251E4F05 CRC64; MQADRSEELR QQLAQRILIL DGAMGTMIQQ YKLGEADYRG TRFLEHPKDL KGNNDLLVLT RPDVVGEIHR AYLDAGADII ETCSFNATRV SQAEYGMADI AYELNVASAR LVRELCDEFT ARNPAKPRYC AGVLGPTSRT LSISPDVNDP GYRNIEFDAL VEDYYESAKG LMEGGADLLL IETIFDTLNA KAAVFAVEKL FDDLDRRLPV MISGTITDAS GRTLSGQTAE AFWNSLAHAR PISFGLNCAL GAKELRAYVD ELSNVCDTFV SAHPNAGLPN PLAPTGYDET PEQLAEAVVE WAQSGLVNIL GGCCGTTPAH IAAIAQAVAQ VPPRRVPDIE KKLRLSGLEP FNVGADSLFV NVGERTNVTG SKAFARMILE GRFDDALAVA RQQVENGAQV IDINMDEAML DSVAAMERFL KLIASEPDIS RVPIMIDSSK WEVIEAGLKC IQGKGIVNSI SMKEGEESFL RQARLARRYG AAVIVMAFDE KGQADTYARK IEICARAYEL LVGIGFPPED IIFDPNIFAI ATGIEEHDNY AVDFIQSVAW IKANLPHAKT SGGVSNVSFS FRGNEPVREA IHTVFLYHAI KAGLTMGIVN AGMLGVYDDL DPVLREKVED VVLNRKPASG QNPGEALVEL AQTVKEGKAK DTGPDLAWRE WSVEERLKHA LVKGITEFVV ADTEEVRARL ESEGKPPLAV IEGPLMAGMD VVGDLFGAGK MFLPQVVKSA RVMKQAVAHL IPYIEAEKAR TGATSKGRIV IATVKGDVHD IGKNIVGVVL GCNGYEVIDL GVMVPTDKIL NAAREHGAQA IGLSGLITPS LEEMSHVAAE MQRQGFDVPL LIGGATTSRA HTAIKIAPHY QQPVVYVPDA SRAVGVVTAL LSEGGAGDFK AQLAADYDKI RAQHANKKGV QLVSLEAARA NAYNPLSVEG YEPVEPNTLG VMALDVDLDE LRDYIDWGPF FQTWDLAGSF PKILDDEVVG ETARNVFNDA QAMLEDLIAG EWVQAKAVFG LFPANSVGDD IAFYADESRD EPMMTWHGLR QQHERPAGKP HWCLADFVAP KASGVRDWCG AFAVTAGLGI EHKLAEFEAA HDDYRAIMLK SLADRLAEAT AEWLHERVRK EYWGYAADEQ LDNAALIKEQ YKGIRPAPGY PACPDHTVKA ALFQLLDAPT NAGMGLTESM AMTPAASVSG FYFAHPESHY FAISKIGRDQ VTDWAQRTGL TEEAAARWLA PLL // ID A1KC77_AZOSB Unreviewed; 313 AA. AC A1KC77; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 29-APR-2015, entry version 39. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CAL96433.1}; GN OrderedLocusNames=azo3817 {ECO:0000313|EMBL:CAL96433.1}; OS Azoarcus sp. (strain BH72). OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Rhodocyclaceae; Azoarcus. OX NCBI_TaxID=62928 {ECO:0000313|EMBL:CAL96433.1, ECO:0000313|Proteomes:UP000002588}; RN [1] {ECO:0000313|EMBL:CAL96433.1, ECO:0000313|Proteomes:UP000002588} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BH72 {ECO:0000313|EMBL:CAL96433.1, RC ECO:0000313|Proteomes:UP000002588}; 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., 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 ----------------------------------------------------------------------- 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; CAL96433.1; -; Genomic_DNA. DR RefSeq; WP_011767539.1; NC_008702.1. DR RefSeq; YP_935319.1; NC_008702.1. DR STRING; 62928.azo3817; -. DR EnsemblBacteria; CAL96433; CAL96433; azo3817. DR KEGG; azo:azo3817; -. DR PATRIC; 21016078; VBIAzoSp26047_3856. DR eggNOG; COG2040; -. DR HOGENOM; HOG000179103; -. DR OMA; CCGTDHR; -. DR OrthoDB; EOG6R5C46; -. DR Proteomes; UP000002588; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002588}; KW Reference proteome {ECO:0000313|Proteomes:UP000002588}. SQ SEQUENCE 313 AA; 33838 MW; 629F597A09677587 CRC64; MSLYRHRLPQ LAGAAFVSDG GMETTLIYHH GRELPHFAAF TLMDDAEGRR LLTDYYRRYI DIALRHRRGL LLETPTWRAS ADWGARLGYD AAALARVNRD SVALLDALRA THQRAGTPMV ISGAIGPRGD GYVADAGMSA TEAADYHGEQ IATLASTRCD LVTAFTLNYV DEAIGIVRAA QHETMPVVIS FTLETDGRLP SGQALGDAIR ETDAATAAGA TYYMINCAHP THFDHVLDGA GDWRHRIRGL RANASCRSHA ELDAATELDA GDPIDLGARY RALRPQLPGL AVIGGCCGTD HRHVEAICAA YDG // ID A1R978_ARTAT Unreviewed; 317 AA. AC A1R978; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 27-MAY-2015, entry version 49. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABM08173.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ABM08173.1}; GN Name=mmuM {ECO:0000313|EMBL:ABM08173.1}; GN OrderedLocusNames=AAur_3089 {ECO:0000313|EMBL:ABM08173.1}; OS Arthrobacter aurescens (strain TC1). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Micrococcaceae; Arthrobacter. OX NCBI_TaxID=290340 {ECO:0000313|EMBL:ABM08173.1, ECO:0000313|Proteomes:UP000000637}; RN [1] {ECO:0000313|EMBL:ABM08173.1, ECO:0000313|Proteomes:UP000000637} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TC1 {ECO:0000313|EMBL:ABM08173.1, RC ECO:0000313|Proteomes:UP000000637}; 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.M., 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 ----------------------------------------------------------------------- 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; ABM08173.1; -; Genomic_DNA. DR RefSeq; WP_011775725.1; NC_008711.1. DR RefSeq; YP_948790.1; NC_008711.1. DR STRING; 290340.AAur_3089; -. DR EnsemblBacteria; ABM08173; ABM08173; AAur_3089. DR KEGG; aau:AAur_3089; -. DR PATRIC; 20981672; VBIArtAur67810_3140. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; AAUR290340:GI59-3088-MONOMER; -. DR Proteomes; UP000000637; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000637}; KW Methyltransferase {ECO:0000313|EMBL:ABM08173.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000637}; KW Transferase {ECO:0000313|EMBL:ABM08173.1}. SQ SEQUENCE 317 AA; 33511 MW; 18FA5302BBF9D0E6 CRC64; MPQNTTLSTH LATGKDLVLD GALATELEAH GCDLEDPLWS AKVLLEQPHL IKQVHRDYFD AGASVAITAS YQATPQGFAR RGLGAEESLE LVALSVRLAD EARREALADG TANGPLLVAG SVGPYGAYLA DGSEYRGDYT LSAAEFRDFH RPRIAALVET GADFLACETL PSYAEAEALV ALVAEFDVES WFTFTLRDSG HISDGTPIGD VAVLLSAEPR VTAVGVNCVP LELVTDALGT LHRFSNKPLV AYPNSGESYD AVTKTWAPSA GVQGSGTLAG NAPDWQDRGA RLIGGCCRTT PRDIEGLAAN MTPREPA // ID A1S2M1_SHEAM Unreviewed; 314 AA. AC A1S2M1; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 27-MAY-2015, entry version 44. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABL98627.1}; GN OrderedLocusNames=Sama_0417 {ECO:0000313|EMBL:ABL98627.1}; OS Shewanella amazonensis (strain ATCC BAA-1098 / SB2B). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=326297 {ECO:0000313|EMBL:ABL98627.1, ECO:0000313|Proteomes:UP000009175}; RN [1] {ECO:0000313|EMBL:ABL98627.1, ECO:0000313|Proteomes:UP000009175} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1098 / SB2B {ECO:0000313|Proteomes:UP000009175}; 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; ABL98627.1; -; Genomic_DNA. DR RefSeq; WP_011758537.1; NC_008700.1. DR RefSeq; YP_926297.1; NC_008700.1. DR ProteinModelPortal; A1S2M1; -. DR STRING; 326297.Sama_0417; -. DR DNASU; 4602672; -. DR EnsemblBacteria; ABL98627; ABL98627; Sama_0417. DR KEGG; saz:Sama_0417; -. DR PATRIC; 23449393; VBISheAma74963_0431. DR eggNOG; COG2040; -. DR HOGENOM; HOG000179103; -. DR KO; K00547; -. DR OMA; CCGTDHR; -. DR OrthoDB; EOG6R5C46; -. DR BioCyc; SAMA326297:GH0T-446-MONOMER; -. DR Proteomes; UP000009175; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009175}; KW Methyltransferase {ECO:0000313|EMBL:ABL98627.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000009175}; KW Transferase {ECO:0000313|EMBL:ABL98627.1}. SQ SEQUENCE 314 AA; 34112 MW; 82D62FE8AFC34DD3 CRC64; MGIYRTQLPQ LDGGVFLTDG GIETTLIFHE GFELPYFAAF ELLKTPQGRD ALTHYFVTYV KLAGLFDTGF ILESPTWRAS SDWGALLGYT KETLAQANRE AIALLEVIRE AHSGRLPVVV SGCIGPRFDG YLPDKSMTAE DARHYHSIQI ETLASTSADM ICALTLNRVE EAIGIVEAAR EAAMPVVISF TLETDGRLPT GQSLGDAVVQ VDEATAGYAA YFMINCAHPS HLETVPQDAP WLARVKGFRA NASSLSHAEL NDATTLDDGD PHQLGQQYAS LMSTRLKGLN VLGGCCGTDH RHLEQIAKAC IKPR // ID A1S3K9_SHEAM Unreviewed; 1246 AA. AC A1S3K9; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 27-MAY-2015, entry version 65. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABL98965.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABL98965.1}; GN OrderedLocusNames=Sama_0758 {ECO:0000313|EMBL:ABL98965.1}; OS Shewanella amazonensis (strain ATCC BAA-1098 / SB2B). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=326297 {ECO:0000313|EMBL:ABL98965.1, ECO:0000313|Proteomes:UP000009175}; RN [1] {ECO:0000313|EMBL:ABL98965.1, ECO:0000313|Proteomes:UP000009175} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1098 / SB2B {ECO:0000313|Proteomes:UP000009175}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000507; ABL98965.1; -; Genomic_DNA. DR RefSeq; WP_011758875.1; NC_008700.1. DR RefSeq; YP_926635.1; NC_008700.1. DR ProteinModelPortal; A1S3K9; -. DR STRING; 326297.Sama_0758; -. DR EnsemblBacteria; ABL98965; ABL98965; Sama_0758. DR KEGG; saz:Sama_0758; -. DR PATRIC; 23450109; VBISheAma74963_0788. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SAMA326297:GH0T-788-MONOMER; -. DR Proteomes; UP000009175; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000009175}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABL98965.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000009175}; KW Transferase {ECO:0000313|EMBL:ABL98965.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 259 259 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 776 776 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1246 AA; 137870 MW; 20E51CEF438EDBB6 CRC64; MATPVLSQAT KALAQSRQQR LNEDLSTRIL ILDGAMGTMI QGHKLEEEHY RGSRFADWHC DVKGNNDLLV LTQPEIIKGI HREYLLAGAD IIETNTFNAT TVAMADYDMQ SLSAEINLVG ARIAREVADE VEAQTGIPRY VAGVLGPTNR TCSISPDVND PGYRNIHFDD LVTAYRESTA ALIEGGADII MVETIFDTLN AKAALFAIES IFDEVGLRLP VMISGTITDA SGRTLTGQTT EAFYNSLRHI KPISMGLNCA LGPKELRPYV EELSRISECY VSAHPNAGLP NEFGGYDETP KEMADIIVQW AIEGMLNIVG GCCGTTPDHI RVIREAVEKH APRKLPELPV ACRLAGLEPL TISADSLFVN VGERTNVTGS AKFLKLIKEG QYETALDVAR DQVENGAQII DINMDEGMLD GEEVMTTFLN LVASEPEISK VPIMIDSSKW EVIEAGLKCV QGKCIVNSIS LKEGEAKFIE QATLVKRYGA AAIIMAFDET GQADTRARKI EICTRAYRIL VDKVGFPPED IIFDPNIFAV ATGIEEHDNY AVDFIEAVRD IKATLPHAMI SGGVSNVSFS FRGNNPVREA IHAVFLYHAI KEGMDMGIVN AGQLAIYDDI PAELKERVEA VVLNLPCPVE DSTNTEQLLE IAEKYRGGGG SGAGKKEDLQ WRSLPVNKRL EHALVKGITE FIDADTEEAR QQATRPLDVI EGPLMDGMNV VGDLFGEGKM FLPQVVKSAR VMKKAVAYLN PFIEAEKVAG QSNGKVLMVT VKGDVHDIGK NIVGVVLACN GYEVIDLGVM VPVEKIVEVA KKEQVDIIGM SGLITPSLDE MVHNVKTFER EGLTLPAIIG GATCSKIHTA VKIAPHYPHG AIYIPDASRA VPMVSKLINE ETRAATIKAT YDEYDVMREK RLSQAKRKEI ISIEAARENR CQLDWANYQP KVPNKLGIQV FEDYPLDDLV DRIDWTPFFR AWELHGHFPR ILEDEVVGEE ARKLFADAKA MLQTIIDEKW LTAKGVIGLF PANTVNHDDI ELYTDESRSQ VLMTTHHLRM QIERVGNDNF CLSDFVAPKD SGVVDYTGGF AVCAGHGIDE HLARFEANHD DYNAIMLKVL ADRLAEAFAE RMHERVRKEF WGYASDENLD NEALIREKYR GIRPAPGYPA CPDHTEKGLL WDLLKPNECI DLNITESFAM YPTAAVSGWY FAHPEARYFG VTNIGRDQVE DYARRKGMTV AETEKWLAPI LDYDPE // ID A1SJZ9_NOCSJ Unreviewed; 1244 AA. AC A1SJZ9; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 01-APR-2015, entry version 65. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABL82134.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABL82134.1}; GN OrderedLocusNames=Noca_2631 {ECO:0000313|EMBL:ABL82134.1}; OS Nocardioides sp. (strain BAA-499 / JS614). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Nocardioidaceae; Nocardioides. OX NCBI_TaxID=196162 {ECO:0000313|EMBL:ABL82134.1, ECO:0000313|Proteomes:UP000000640}; RN [1] {ECO:0000313|Proteomes:UP000000640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000509; ABL82134.1; -; Genomic_DNA. DR RefSeq; WP_011756074.1; NC_008699.1. DR RefSeq; YP_923821.1; NC_008699.1. DR ProteinModelPortal; A1SJZ9; -. DR SMR; A1SJZ9; 657-910. DR STRING; 196162.Noca_2631; -. DR EnsemblBacteria; ABL82134; ABL82134; Noca_2631. DR KEGG; nca:Noca_2631; -. DR PATRIC; 22747313; VBINocSp122728_2891. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; QPFFNAW; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; NSP196162:GH4V-2675-MONOMER; -. DR Proteomes; UP000000640; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000640}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABL82134.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000640}; KW Transferase {ECO:0000313|EMBL:ABL82134.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 252 252 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 315 315 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 316 316 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 774 774 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1244 AA; 136394 MW; D0B493617BB12261 CRC64; MSWSPQQRPD LTDQLTRALE QRILVLDGAM GTAIQRDRPD EAGYRGERFA DWPSDLVGNN DLLTITRPEI IAGIHREYLL AGADIIETNT FNANAVSLSD YGMQELAYEI NYEAAQLARR EVDAVSTQEH PRYVAGALGP TTRTASISPD VNDPGARNVT YDQLVAAYLD AARGLVDGGA DLLVIETIFD TLNAKAAIFA VETLFAENQR RWPVIISGTI TDASGRTLSG QVTEAFWNSV RHARPLAVGL NCALGAKEMR PYIAEIARIA DTFVSCYPNA GLPNAFGEYD EAAEETAAII EEFAASGFVN LVGGCCGTTP AHVAAIAKAV EGKTRRPVPE LTPALRLAGL EPFAVTDKSL FVNVGERTNI TGSARFRKLI KDGDYDTALS VAAQQVENGA QVIDINMDEG MIDGVAAMDR FTRLIASEPD ISRVPVMVDS SKWEVIQAGL KNIQGKPIVN SISMKEGEDT FREQARLCRQ YGAAAVVMAF DEDGQADNLE RRKAICERAY RILVDEVGFP PEDIIFDPNV FAVATGIEEH ASYGLDFIEA TRWIKQNLPG AKVSGGISNV SFSFRGNNPV REAIHAVFLY HAIGAGLDMG IVNAGALVVY DQVEPELRER IEDVILNRRP DAAERLLEIA EAHNRAGETT EAAAAEEWRA LPVEERITHA LVKGIDAHVE PDTEELRQLI AARGGRPIEV IEGPLMDGMN VVGDLFGAGK MFLPQVVKSA RVMKKAVAYL IPFIEQEKLD NPELATAKET NGTIVMATVK GDVHDIGKNI VGVVLQCNNY EVIDLGVMVP TQKLLDTALE VGADAVGVSG LITPSLDEMV GVAAEMQRRG MEIPLLVGGA TTSRAHTAVK VDGKYDGPVV WVKDASRSVP TLATLLNPAQ RPRLMAEIKE DYDSLRARHA TKHDRPMLTL EQARDNRTPI DWSTYAPPAP RTPGIHVLED YDLAELRDFI DWQPFFNAWE LKGKFPDILN SPTTGETARG LYDDAQAMLD RVIEEKWLRA NAVFGLFPAN AVGDDVEVYT DDSRTEVLTT LHNLRQQGDH RDGIPNRSLG DFVAPRATGL PDHVGAFAVT AGLGAEARIL EFKEQLDDYS AIMLEALADR LAEAFAERLH QRVRTEFWAH APEEDLDNQA LIAERYDGIR PAPGYPACPE HTEKRTLWRL LDVTARTGIE LTDGMAMWPG AAVSGWYYSH PQSQYFVLGR IGRDQVADYA ERKGWTLTEA ERWLSPNLGY DPDD // ID A1SR72_PSYIN Unreviewed; 1227 AA. AC A1SR72; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 27-MAY-2015, entry version 64. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABM01987.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABM01987.1}; GN OrderedLocusNames=Ping_0113 {ECO:0000313|EMBL:ABM01987.1}; OS Psychromonas ingrahamii (strain 37). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Psychromonadaceae; Psychromonas. OX NCBI_TaxID=357804 {ECO:0000313|EMBL:ABM01987.1, ECO:0000313|Proteomes:UP000000639}; RN [1] {ECO:0000313|EMBL:ABM01987.1, ECO:0000313|Proteomes:UP000000639} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=37 {ECO:0000313|EMBL:ABM01987.1, RC ECO:0000313|Proteomes:UP000000639}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000510; ABM01987.1; -; Genomic_DNA. DR RefSeq; WP_011768546.1; NC_008709.1. DR RefSeq; YP_941586.1; NC_008709.1. DR ProteinModelPortal; A1SR72; -. DR SMR; A1SR72; 655-1226. DR STRING; 357804.Ping_0113; -. DR EnsemblBacteria; ABM01987; ABM01987; Ping_0113. DR KEGG; pin:Ping_0113; -. DR PATRIC; 23064894; VBIPsyIng103130_0121. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PING357804:GJBJ-122-MONOMER; -. DR Proteomes; UP000000639; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000639}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABM01987.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000639}; KW Transferase {ECO:0000313|EMBL:ABM01987.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 249 249 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135882 MW; F1EBB47A1C2DED79 CRC64; MVVNDRSALI KAQLEKHILL IDGAMGTMIQ SYKFEEEDYR GERFADWSCD VKGNNDLLVL SQPRVIADIH REYLDAGADI LETNTFNATT IAMADYQMQS LSAEINREAA RLARQEADQK TAETPERPRF VAGVLGPTNR TCSISPDVND PAFRNVSFDE LVEAYTESTR ALIEGGCDLI LIETIFDTLN AKAAVFAVSG VFDELGYKLP VMISGTITDA SGRTLTGQTT EAFYNSLRHI EPISFGLNCA LGPEELRQYV QEISKISETY VSAHPNAGLP NAFGEYDLEA DEMAAHIKEW AESGFLNLVG GCCGTTPAHI KAMADAVAGV KPRALPEIEI ACRLSGLEAL TIRKDSLFQN VGERTNVTGS ARFKRLIMDE LYDQALEVAL HQVTAGANII DINMDEAMLD SLYAMKRFLN LCASEPDISR VPIMIDSSKW EILEEGMKCV QGKGIVNSIS MKEGVDNFIA QAKLIRRYGF AVIVMAFDED GQADTRARKF DICKRSYDIL VNQVGFPPED IIFDPNIFAV ATGISDHNNY AVDFIEAVKD IKTNLPHVMI SGGVSNVSFS FRGNNPVREA IHAVFLYHCI QNGMDMGIVN AAQLAIYDDI PKELKEAVEA IILNTSPDAT DNLLELAEKY RDSGSEKVDD GKSLEWRNLP VNERIAHSLV KGITEFIVED TEEARVNAEM PIDVIEGPLM DGMNIVGDLF GDGKMFLPQV VKSARVMKQA VAYLNPYIEE TKAVGATNGK IVMATVKGDV HDIGKNIVGV ILQCNNYEII DLGVMVPTEK IIKTAIAEKA DIIGLSGLIT PSLDEMVYVA KEMQRQGLKL PLLIGGATTS KAHTAVKIEQ NYDQPVVYVS NASRAVGVCQ KLLNPVHKLE FVKKLDEDYV RVREQYANRR PRSAPVSLQR ARANAAKIDW ANYQPPVPNQ LGVQVIKKMS IKILREYIDW TPFFLTWGLA GKYPRILEDE VVGEEAKRLF ADALAMLDVV EAQGEISASG MVGIFPANSV GDDIEIYTDQ TRSKILQMSH HLRQQSEKKP PFVNHCLADY IAPKSLGIAD YIGAFAVTGG IGEKEVAERY KAELDDYNAI LVQAICDRLA EAFAEYLHQK TRKEYWGFAA NETLECDDLI REKYQGIRPA PGYAACPEHT EKQVIWDLMD VEQQIGMQLT SSYAMFPGAA VSGWIFSHPE SRYFAVAHIQ QDQLEDYAGR KGWDLLTAER WLGPNLS // ID A1SWN6_PSYIN Unreviewed; 310 AA. AC A1SWN6; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 27-MAY-2015, entry version 45. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABM03901.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ABM03901.1}; GN OrderedLocusNames=Ping_2160 {ECO:0000313|EMBL:ABM03901.1}; OS Psychromonas ingrahamii (strain 37). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Psychromonadaceae; Psychromonas. OX NCBI_TaxID=357804 {ECO:0000313|EMBL:ABM03901.1, ECO:0000313|Proteomes:UP000000639}; RN [1] {ECO:0000313|EMBL:ABM03901.1, ECO:0000313|Proteomes:UP000000639} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=37 {ECO:0000313|EMBL:ABM03901.1, RC ECO:0000313|Proteomes:UP000000639}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; ABM03901.1; -; Genomic_DNA. DR RefSeq; WP_011770461.1; NC_008709.1. DR RefSeq; YP_943500.1; NC_008709.1. DR ProteinModelPortal; A1SWN6; -. DR STRING; 357804.Ping_2160; -. DR EnsemblBacteria; ABM03901; ABM03901; Ping_2160. DR KEGG; pin:Ping_2160; -. DR PATRIC; 23069575; VBIPsyIng103130_2389. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; QPEVMAA; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; PING357804:GJBJ-2246-MONOMER; -. DR Proteomes; UP000000639; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000639}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ABM03901.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000639}; KW Transferase {ECO:0000313|EMBL:ABM03901.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 215 215 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 296 296 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 310 AA; 33828 MW; C0779A503865BEB5 CRC64; MDNRLNITMK SQFRLPIILD GGMGRELKRI GAPFQQPEWS AQALIESPHF ISEVHKSFIE AGAEVITTNT YALVPFHIGE KRFNEQGADL IKLAARLARE CVKENSAVLV AGCIPPVLGS YRPDLFSVEK AKPVLELLIK NQEADVDIWL AETISSIAEA AMIKARTVVT NKPTWIAFTI KDEITTEPAL RSGESVYDAV SQIAGQNVSA ILFNCSGVEV METALITAKQ ALLDKEIEDQ VQLGVYANNF PPIGELHQAN QDHGVSGIRD DVPPEKYHEF GLSWINAGAS IIGGCCGVSP AHIKKLAELK // ID A1TAR9_MYCVP Unreviewed; 1251 AA. AC A1TAR9; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 27-MAY-2015, entry version 65. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABM14269.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABM14269.1}; GN OrderedLocusNames=Mvan_3474 {ECO:0000313|EMBL:ABM14269.1}; OS Mycobacterium vanbaalenii (strain DSM 7251 / PYR-1). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=350058 {ECO:0000313|EMBL:ABM14269.1, ECO:0000313|Proteomes:UP000009159}; RN [1] {ECO:0000313|EMBL:ABM14269.1, ECO:0000313|Proteomes:UP000009159} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 7251 / PYR-1 {ECO:0000313|Proteomes:UP000009159}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000511; ABM14269.1; -; Genomic_DNA. DR RefSeq; WP_011780673.1; NC_008726.1. DR RefSeq; YP_954275.1; NC_008726.1. DR ProteinModelPortal; A1TAR9; -. DR SMR; A1TAR9; 661-1250. DR STRING; 350058.Mvan_3474; -. DR EnsemblBacteria; ABM14269; ABM14269; Mvan_3474. DR KEGG; mva:Mvan_3474; -. DR PATRIC; 18185251; VBIMycVan31953_3542. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; QPFFNAW; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; MVAN350058:GIWR-3499-MONOMER; -. DR Proteomes; UP000009159; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000009159}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABM14269.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000009159}; KW Transferase {ECO:0000313|EMBL:ABM14269.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 258 258 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 778 778 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1251 AA; 137087 MW; 81E2F9F3C4E2F40F CRC64; MNSADPNIWE PNIRPDCTDE LKVALGRRIV VIDGAMGTAI QRDRPDEAGY RGERFKDWPS DLVGNNDLLT LTQPQIIEGI HREYLEAGAD ILETNTFNAN AVSLSDYGME KLSYELNYAG AALARKACDE FSTPDKPRYV AGALGPTTRT ASISPDVNDP GARNVSYDQL VAAYLDAASG LVDGGADLLI VETIFDTLNA KAAVFAIETL FEDRGRRWPV IISGTITDAS GRTLSGQVTE AFWNSVRHAR PLAVGLNCAL GAPEMRPYLA EMSRIADTFV SCYPNAGLPN AFGEYDESPT RQAGYVAEFA EAGLVNLVGG CCGTTPAHIA EIARVVDGKP PRKVPEIPVA TRLAGLEPLN ITDDSLFVNI GERTNITGSA RFRNLIKAED YDTALSVALQ QVEVGAQVID INMDEGMIDG VAAMDRFTKL IAAEPDISRV PVMIDSSKWE VIEAGLKNVQ GKPIVNSISM KEGEEKFIRE ARLCRKYGAA VVVMAFDEQG QADNLERRKQ ICGRAYRILT EEVGFPAEDI IFDPNCFALA TGIEEHASYG IDFIEACAWI KENLPGVHIS GGISNVSFSF RGNNPVREAI HAVFLFHAIK AGLDMGIVNA GALVPYDSID PELRDRIEDV VLNRREDAAE RLLEIAERFN SKGETEDAGV AEWRSLPVRE RITHALVKGI DAHVDDDTEE LRAEIADAGG RPIEVIEGPL MDGMNVVGDL FGAGKMFLPQ VVKSARVMKK AVAYLLPFIE AEKAENGTSD SKDTNGTIVM ATVKGDVHDI GKNIVGVVLQ CNNFEVIDLG VMVPAQKILD AAKEHNADII GLSGLITPSL DEMANFAVEM EREGLEIPLL IGGATTSRAH TAVKIAPRRG GPVVWVKDAS RSVPVAAALL DDRQRPALLE ATEADYASLR ERHAQKNERP MLTLEKARAN RTPVEWDGYT PPVPAQGLGV REFKDYDLAE LREYIDWQPF FNAWEMKGRF PDILNNPATG EAARKLYDDA QEMLDTLIKE KWLTANGVIG FFPANASPGG DDIVVYTDDT RTEVLTTLHN LRQQGEHRSG IPNRSLGDFI APKESGLRDY IGAFAVTAGL GSQDKIMEFK AALDDYSAIL LESLADRLAE AFAERMHERV RKEFWGYQPD EQLDNDALIG EKYVGIRPAP GYPACPEHTE KATLWKLMDV KERTGIELTE SMAMWPGAAV SGWYFSHPQS QYFVVGRLAQ DQVADYAKRK GWTLAEAERW LAPNLGYNPE D // ID A1TIJ8_ACIAC Unreviewed; 354 AA. AC A1TIJ8; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 27-MAY-2015, entry version 52. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABM30786.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABM30786.1}; GN OrderedLocusNames=Aave_0174 {ECO:0000313|EMBL:ABM30786.1}; OS Acidovorax citrulli (strain AAC00-1) (Acidovorax avenae subsp. OS citrulli). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Acidovorax. OX NCBI_TaxID=397945 {ECO:0000313|EMBL:ABM30786.1, ECO:0000313|Proteomes:UP000002596}; RN [1] {ECO:0000313|Proteomes:UP000002596} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AAC00-1 {ECO:0000313|Proteomes:UP000002596}; 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; ABM30786.1; -; Genomic_DNA. DR RefSeq; WP_011793364.1; NC_008752.1. DR RefSeq; YP_968560.1; NC_008752.1. DR ProteinModelPortal; A1TIJ8; -. DR STRING; 397945.Aave_0174; -. DR EnsemblBacteria; ABM30786; ABM30786; Aave_0174. DR KEGG; aav:Aave_0174; -. DR PATRIC; 20675353; VBIAciCit38535_0184. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; ACIT397945:GI5W-174-MONOMER; -. DR Proteomes; UP000002596; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002596}; KW Methyltransferase {ECO:0000313|EMBL:ABM30786.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002596}; KW Transferase {ECO:0000313|EMBL:ABM30786.1}. SQ SEQUENCE 354 AA; 38289 MW; 8DB3E2EC13BC4F88 CRC64; MQPLHYTRAR QLPGILAERI AILDGAMGTM IQRFKLGEAQ YRGEGYSGPD GAGDRFKDFP RDVKGNNELL SLTRPDVIRD IHERYLAAGA DLIETNTFGA TTIAQEDYHM ADLAREMNLA SARLARAACD KYSTPDKPRF VAGALGPTPK TASISPDVND PGARNVDFEQ LRAAYYEQTQ ALVEGGADVL LVETIFDTLN AKAALFAIDE YFEASGERLP LIISGTVTDA SGRILSGQTV TAFWHSVRHA RPLAIGLNCA LGATLMRPYI QELNRVAEDT FISCYPNAGL PNPMSDTGFD ETPEVTSRLV HEFAAEGLVN IVGGCCGTTP DHIAAIGRAV APVPTRKLFY PEAA // ID A1U0U1_MARHV Unreviewed; 1232 AA. AC A1U0U1; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 27-MAY-2015, entry version 66. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABM18610.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABM18610.1}; GN OrderedLocusNames=Maqu_1526 {ECO:0000313|EMBL:ABM18610.1}; OS Marinobacter hydrocarbonoclasticus (strain ATCC 700491 / DSM 11845 / OS VT8). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Marinobacter. OX NCBI_TaxID=351348 {ECO:0000313|EMBL:ABM18610.1, ECO:0000313|Proteomes:UP000000998}; RN [1] {ECO:0000313|Proteomes:UP000000998} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700491 / DSM 11845 / VT8 RC {ECO:0000313|Proteomes:UP000000998}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000514; ABM18610.1; -; Genomic_DNA. DR RefSeq; WP_011785012.1; NC_008740.1. DR RefSeq; YP_958797.1; NC_008740.1. DR ProteinModelPortal; A1U0U1; -. DR SMR; A1U0U1; 654-1229. DR STRING; 351348.Maqu_1526; -. DR EnsemblBacteria; ABM18610; ABM18610; Maqu_1526. DR KEGG; maq:Maqu_1526; -. DR PATRIC; 22458324; VBIMarAqu65105_1929. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; MHYD351348:GHYZ-1558-MONOMER; -. DR Proteomes; UP000000998; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000998}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABM18610.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000998}; KW Transferase {ECO:0000313|EMBL:ABM18610.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1232 AA; 137209 MW; 972CB3C3B9B305FE CRC64; MTDRNTRLEQ LHQALKERIV ILDGGMGTMI QNQKLDEAAF RGDRFKDYER EVQGNNDLLN LTQPALLRNI HAEYLDAGAD IIETNTFNST KLSQADYGLE ELARELNVAA AKLAREIADE FTARNPDKPR FVAGAVGPTS RTASISPDVN NPGYRNVDFQ TLVDNYYEAV SGLVEGGSDL ILIETIFDTL NAKAAIYATQ QFFIDSGIEL PIMISGTITD ASGRTLSGQT TEAFYNSVAH AKPISVGLNC ALGADALRPY VEELSNKAET YVSAHPNAGL PNEFGEYDQT PEEMAEIIEG FAKDGFLNII GGCCGSRPDH IEAIARAVAK YPPRQIPDRP KALRLSGLEP FTGDENTLFI NVGERTNVTG SKRFLRLIKE EQYEEALSVA RDQVENGAQI IDINMDEGML DSREVMVRFL NLVASEPDIS RVPIMIDSSK WDVIEAGLRC IQGKAVVNSI SLKEGEEEFI KRARDCMRYG AAVVVMAFDE DGQADTFERK TEICKRSYDV LTGIGFNPAD IIFDPNIFAI ATGIEEHNNY AVDFINATRW IKENLPHASI SGGVSNVSFS FRGNDAVREA IHSVFLYHAI KAGMNMGIVN PGQLVIYDEI EPDLKELVED VVLNRREDST DRLLEAAEKF KSKGGQTKEE DLAWREWPVE KRLEHALVKG ITNFIIEDTE ACRLNASHPI EVIEGPLMDG MNVVGDLFGD GKMFLPQVVK SARVMKQAVA HLIPYIEAEK SEDQQAKGKI LMATVKGDVH DIGKNIVGVV LQCNNYEVID LGVMVPCEKI LETARKENVD MIGLSGLITP SLDEMVHVAR EMQRLDFNIP LMIGGATTSK AHTAVKIEPQ YKNDIALYVS DASRCVNVAS QLLSKTAKPA FVEAARTEYD EIRERRKNRG DRTKLVSLKE ARARAPEIDF ENYQPPKPAF TGVRVFEEYD LNELVDYIDW TPFFISWDIA GKYPAIFDDP KRGDAARTLF DDAQKLLKQM IGEKRISARG VIGFWPANRR GDDIVVYTDE SRTEELTTLH HLRQQDEKAP GKPMMALSDF VAPESLHLGD YVGGFAVTTG IGVDELTTEF KNAHDDYSAI MVQALADRLA EAFAERMHER VRKEFWGYAT DEQMANEDLI KERYRGIRPA PGYPACPDHT EKATLFKLLD ATANTSLQLT EHFAMYPTAA VSGWYFAHPE AKYFAVGKIG VDQVEDYAER KGLTKAEAER WLMPSLAYDP AE // ID A1UHU7_MYCSK Unreviewed; 1264 AA. AC A1UHU7; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 27-MAY-2015, entry version 65. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABL92405.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABL92405.1}; GN OrderedLocusNames=Mkms_3211 {ECO:0000313|EMBL:ABL92405.1}; OS Mycobacterium sp. (strain KMS). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=189918 {ECO:0000313|EMBL:ABL92405.1, ECO:0000313|Proteomes:UP000000638}; RN [1] {ECO:0000313|EMBL:ABL92405.1, ECO:0000313|Proteomes:UP000000638} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KMS {ECO:0000313|EMBL:ABL92405.1, RC ECO:0000313|Proteomes:UP000000638}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000518; ABL92405.1; -; Genomic_DNA. DR RefSeq; WP_011768279.1; NC_008705.1. DR RefSeq; YP_939195.1; NC_008705.1. DR ProteinModelPortal; A1UHU7; -. DR SMR; A1UHU7; 676-1263. DR STRING; 189918.Mkms_3211; -. DR EnsemblBacteria; ABL92405; ABL92405; Mkms_3211. DR KEGG; mkm:Mkms_3211; -. DR PATRIC; 18105406; VBIMycSp70743_3734. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; QPFFNAW; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; MSP189918:GH4X-3234-MONOMER; -. DR Proteomes; UP000000638; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000638}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABL92405.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000638}; KW Transferase {ECO:0000313|EMBL:ABL92405.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 273 273 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 336 336 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 337 337 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 793 793 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1264 AA; 138594 MW; 026D2BDEF504D512 CRC64; MNSPEPKIPE PKIPGPKNPG PENFEPNIRP DCTDELTTAL NSRIMVIDGA MGTAIQRDRP DEAGYRGERF TEWPTALQGN NDLLNLTQPQ IIEAIHREYL EAGADILETN TFNANAISLA DYDMADLSYE LNYAGAALAR KAADEYSTAE KPRYVAGAIG PTTRTASISP DVNDPGARNV SYDQLVAAYL EAANGLVDGG ADLIIIETIF DSLNAKAAVF AVETLFEDRG RRWPVIISGT ITDASGRTLS GQVTEAFWNA IRHAKPIAVG LNCALGAPEM RPYIAEMARI ADTFVSCYPN AGLPNAFGEY DESPERQAGY IADFAEAGLV NLVGGCCGTA PPHIAEIAKA VEGKPPREVP EIPVATRLSG LEPLNITDDS LFVNIGERTN ITGSARFRNL IKAEDYDTAL SVALQQVEVG AQVIDINMDE GMIDGVAAMD RFTKLIAAEP DISRVPVMID SSKWEVIEAG LKNVQGKPIV NSISMKEGEE KFIREARLCR KYGAAVVVMA FDEQGQADNL ERRKEICGRA YRILTEEVGF PAEDIIFDPN CFALATGIEE HATYGIDFIE ACAWIKENLP GVHISGGISN VSFSFRGNNP VREAIHSVFL FHAIKAGLDM GIVNAGALVP YDSIDPELRD RIEDVVLNRR EDAAERLLEI AERFNKSEKA DDPAAAEWRS LPVRERITHA LVKGIDAHVD ADTEELRAEI AAAGGRPIEV IEGPLMDGMN VVGDLFGAGK MFLPQVVKSA RVMKKAVAYL LPYIEAEKEQ NGTTASKDTN GTIIMATVKG DVHDIGKNIV GVVLQCNNFE VIDLGVMVPA QKILDAAKEH DADIIGLSGL ITPSLDEMVN FAAEMEREGL EIPLLIGGAT TSRAHTAVKV APRRSGPVVW VKDASRSVPV AAALLDDKQR PALLEATAKD YASLRERHAQ KNERPMLTLE KARANRTPIE WDGYTPPVPA QGVGVREFLD YDLAELREYI DWQPFFNAWE MKGRFPDILN NPVSGEAARK LYDDAQEMLD TLIKEKWLTA NGVIGFFPAN AVGDDIEVYT DDTRTEVLTT LHNLRQQGEH RDGIPNRSLG DFIAPRETGL RDYVGAFAVT AGLGSQDRIV EFKAANDDYS AILLESLADR LAEAFAERMH QRVRKEFWGY QPDEQLDNEA LIGEKYSGIR PAPGYPACPE HTEKATLWEL MDVQERTGIE LTESMAMWPG AAVSGWYFSH PQSQYFVVGR LAQDQVADYA KRKGWTLPEA ERWLAPNLGY NPED // ID A1VIG2_POLNA Unreviewed; 351 AA. AC A1VIG2; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 27-MAY-2015, entry version 52. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABM35440.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABM35440.1}; GN OrderedLocusNames=Pnap_0115 {ECO:0000313|EMBL:ABM35440.1}; OS Polaromonas naphthalenivorans (strain CJ2). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Polaromonas. OX NCBI_TaxID=365044 {ECO:0000313|EMBL:ABM35440.1, ECO:0000313|Proteomes:UP000000644}; RN [1] {ECO:0000313|Proteomes:UP000000644} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CJ2 {ECO:0000313|Proteomes:UP000000644}; 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 ----------------------------------------------------------------------- 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; ABM35440.1; -; Genomic_DNA. DR RefSeq; WP_011799550.1; NC_008781.1. DR RefSeq; YP_980361.1; NC_008781.1. DR ProteinModelPortal; A1VIG2; -. DR STRING; 365044.Pnap_0115; -. DR EnsemblBacteria; ABM35440; ABM35440; Pnap_0115. DR KEGG; pna:Pnap_0115; -. DR PATRIC; 22944705; VBIPolNap76733_0923. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; PNAP365044:GJ8X-115-MONOMER; -. DR Proteomes; UP000000644; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000644}; KW Methyltransferase {ECO:0000313|EMBL:ABM35440.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000644}; KW Transferase {ECO:0000313|EMBL:ABM35440.1}. SQ SEQUENCE 351 AA; 38083 MW; A3E8BD52FEB5B46A CRC64; MHAMKPITYT RAQQLPALLA QRILILDGAM GTMIQRFRLN EAQYRGERFK DFHKDVKGNN ELLSLTRPDM IRDIHEGYLA AGADMIETNT FGATTVAQAD YDMADLAVEM NYESARIARA ACDKFSTPEK PRFVVGALGP TPKTASISPD VNDAGARNTS FEELRKAYYE QTEALVKGGA DVLLVETIFD TLNAKAALFA IDEYFENSGE RLPLIISGTV TDASGRILSG QTVTAFWHSV RHAEPLAVGL NCALGAALMR PYIQELAKAA PDTFISCYPN AGLPNPMSDT GFDETPDVTS RLLHEFAAEG LVNIVGGCCG TTPEHIAAIA QAVAPMDGRR LQRNGFYAQA A // ID A1W263_ACISJ Unreviewed; 366 AA. AC A1W263; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 27-MAY-2015, entry version 54. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABM40338.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABM40338.1}; GN OrderedLocusNames=Ajs_0083 {ECO:0000313|EMBL:ABM40338.1}; OS Acidovorax sp. (strain JS42). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Acidovorax. OX NCBI_TaxID=232721 {ECO:0000313|EMBL:ABM40338.1, ECO:0000313|Proteomes:UP000000645}; RN [1] {ECO:0000313|Proteomes:UP000000645} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JS42 {ECO:0000313|Proteomes:UP000000645}; 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; ABM40338.1; -; Genomic_DNA. DR RefSeq; WP_011803553.1; NC_008782.1. DR RefSeq; YP_984414.1; NC_008782.1. DR ProteinModelPortal; A1W263; -. DR STRING; 232721.Ajs_0083; -. DR EnsemblBacteria; ABM40338; ABM40338; Ajs_0083. DR KEGG; ajs:Ajs_0083; -. DR PATRIC; 20685370; VBIAciSp27161_0244. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; ASP232721:GHWE-83-MONOMER; -. DR Proteomes; UP000000645; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000645}; KW Methyltransferase {ECO:0000313|EMBL:ABM40338.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000645}; KW Transferase {ECO:0000313|EMBL:ABM40338.1}. SQ SEQUENCE 366 AA; 39427 MW; 0F1AF52A9A9D71C1 CRC64; MAQSPLLCAR HRGRRRLPTI GPMTLPHYTR AQALPAILEQ RIAILDGAMG TMIQRFKLTE AQYRGERFKD FARDVKGNNE LLSLTRPDVI RDIHEGYLAA GADLIETNTF GATSIAQDDY GLAELAYEMN LESAKLARAA CDKFSTPDKP RFVAGALGPT PKTASISPDV NDPGARNVTF EQLRAAYHEQ ARGLIEGGAD VLLVETIFDT LNAKAALFAI DEVFEETGEC LPIMISGTVT DASGRILSGQ TVTAFWHSVR HARPLSVGLN CALGATLMRP YIQELAKAAP DTFISCYPNA GLPNPMSDTG FDETPEVTSR LVHEFAAEGL VNIVGGCCGT TPDHIGAIAR AVAPVGTRRL FQTEAA // ID A1WH59_VEREI Unreviewed; 370 AA. AC A1WH59; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 27-MAY-2015, entry version 51. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABM56966.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABM56966.1}; GN OrderedLocusNames=Veis_1195 {ECO:0000313|EMBL:ABM56966.1}; OS Verminephrobacter eiseniae (strain EF01-2). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Verminephrobacter. OX NCBI_TaxID=391735 {ECO:0000313|EMBL:ABM56966.1, ECO:0000313|Proteomes:UP000000374}; RN [1] {ECO:0000313|Proteomes:UP000000374} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EF01-2 {ECO:0000313|Proteomes:UP000000374}; 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; ABM56966.1; -; Genomic_DNA. DR RefSeq; WP_011808977.1; NC_008786.1. DR RefSeq; YP_995984.1; NC_008786.1. DR ProteinModelPortal; A1WH59; -. DR STRING; 391735.Veis_1195; -. DR EnsemblBacteria; ABM56966; ABM56966; Veis_1195. DR KEGG; vei:Veis_1195; -. DR PATRIC; 24015867; VBIVerEis120356_1332. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; VEIS391735:GHY5-1206-MONOMER; -. DR Proteomes; UP000000374; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000374}; KW Methyltransferase {ECO:0000313|EMBL:ABM56966.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000374}; KW Transferase {ECO:0000313|EMBL:ABM56966.1}. SQ SEQUENCE 370 AA; 40285 MW; EC7AC31E322FF012 CRC64; MWLRPTGPDG ASYNRAMQAL HYTRAARLPD ILAQRIVILD GAMGTMLQRL RLGEAQYRGA GYAGPDGAGE RFKDFARDLK GNNELLSITR PDLISDIHEH YLAAGADLIE TNTFGATRVA QEDYRMAPLA REMNLRSAQL ARAACDKYSR PDKPRFVAGA LGPTPKTASI SPDVNDPGAR NIDFEQLRAA YYEQTEALLE GGADILLVET IFDTLNAKAA LFAIDECFEH SGERLPIIIS GTVTDASGRI LSGQTVTAFW HSVRHARPLA IGLNCALGAT LMRPYIQELH RAARDCFISC YPNAGLPNPM SDTGFDETPQ ITSRLLHEFA AEGLVNILGG CCGTTPEHIG AIAKAVENQP ARQRFYPAEA // ID A1WU24_HALHL Unreviewed; 305 AA. AC A1WU24; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 27-MAY-2015, entry version 45. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABM61186.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ABM61186.1}; GN OrderedLocusNames=Hhal_0392 {ECO:0000313|EMBL:ABM61186.1}; 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 {ECO:0000313|EMBL:ABM61186.1, ECO:0000313|Proteomes:UP000000647}; RN [1] {ECO:0000313|Proteomes:UP000000647} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 244 / SL1 {ECO:0000313|Proteomes:UP000000647}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; ABM61186.1; -; Genomic_DNA. DR RefSeq; WP_011813209.1; NC_008789.1. DR RefSeq; YP_001001988.1; NC_008789.1. DR ProteinModelPortal; A1WU24; -. DR STRING; 349124.Hhal_0392; -. DR EnsemblBacteria; ABM61186; ABM61186; Hhal_0392. DR KEGG; hha:Hhal_0392; -. DR PATRIC; 22095063; VBIHalHal112047_0399. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; PYVDVWL; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; HHAL349124:GI3I-401-MONOMER; -. DR Proteomes; UP000000647; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000647}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ABM61186.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000647}; KW Transferase {ECO:0000313|EMBL:ABM61186.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 209 209 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 280 280 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 281 281 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 305 AA; 32083 MW; 94C4230325FBC934 CRC64; MTQERDVVLL DGGMGQELRR RSSQPVTPLW SAQVMLDEPD LVTAAHRDFI QAGARVITAN TYSATPQRLA RDGAPELFDS LHAAALDAAR QARDASGQQD VRIAGCLPPL VASYRPDVAP NDADCLEGYR RMVEAQAQAQ GVDLFICETM SLAREARAAT EAAVESNLPV WVAFTVDDGD GTRLRSGESL IQAAQAVVAA GAERVLVNCA IPEAVTTAMG ELTGLGVPFG GYANAFTSVA ALQPGGTVDV LESRTDLDPA AYAEHALHWV EQGATLVGGC CEVGPAHIAE LAERLTAAGY RVVSS // ID A1WZ06_HALHL Unreviewed; 1228 AA. AC A1WZ06; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 01-APR-2015, entry version 61. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABM62918.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABM62918.1}; GN OrderedLocusNames=Hhal_2154 {ECO:0000313|EMBL:ABM62918.1}; 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 {ECO:0000313|EMBL:ABM62918.1, ECO:0000313|Proteomes:UP000000647}; RN [1] {ECO:0000313|Proteomes:UP000000647} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 244 / SL1 {ECO:0000313|Proteomes:UP000000647}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000544; ABM62918.1; -; Genomic_DNA. DR RefSeq; WP_011814940.1; NC_008789.1. DR RefSeq; YP_001003720.1; NC_008789.1. DR ProteinModelPortal; A1WZ06; -. DR SMR; A1WZ06; 651-1227. DR STRING; 349124.Hhal_2154; -. DR EnsemblBacteria; ABM62918; ABM62918; Hhal_2154. DR KEGG; hha:Hhal_2154; -. DR PATRIC; 22098613; VBIHalHal112047_2132. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; HHAL349124:GI3I-2206-MONOMER; -. DR Proteomes; UP000000647; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000647}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABM62918.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000647}; KW Transferase {ECO:0000313|EMBL:ABM62918.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 246 246 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 757 757 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1228 AA; 136680 MW; 346F0CD1E50FAED0 CRC64; MTDRSQQIRD QLAQRILILD CGMGTEIQKY PLEEADFRGE RFSDHPSELK GNNDLLVLTR PDIIRDITRQ NLDAGVDIVE TNTFNSQVLS QADYGTEHLV DELNIEAAKL ARAVCDEVEQ ETGIPRFVAG TMGPTGKTAS ISPDVNNPGH RDITFDQLFE AYAQQARGLL EGGADLILIE TVFDTLNAKA AIYALEEVFE ESGRRLPVMI SGTITDASGR TLSGQTAAAF WNSVRHARPI SIGLNCALGA EDLRPHLQEL SKIADTHIST HPNAGLPNEF GEYDQSPEEM AKIVRTFAEE GLINIIGGCC GTSPAHIAAI REQVKDFAPR QVPDLAPDVT RLSGLEPCNI GKDSLFVNIG ERANVTGSAR FRRLIKEGDY ETALEVAKEQ VENGAQIIDI NMDEGMLDSK DAMIDFLNLV GSEPDISRVP IMIDSSKWDI IEEGLKRIQG KGLVNSISLK EGEEAFLQQA RKLKRYGAAA VVMCFDEKGQ ADTYERRLEI AERAYNALVN DGFEPADIVF DLNIFAVATG IEEHNNYAVD FIEATRWVKE NLPHAKVSGG LSNLSFSFRG NEPVREAMHS VFLYHAIKAG LDMAIVNAGQ IEVYDEIDKE LRELCEDVIL NRHEDATDRL LELAERYKGQ GGKKKEEDLA WREEPVEKRL EHALIKGITD YIDVDVEEAR QKHDRPIQVI EGPLMDGMNT VGDLFGEGKM FLPQVVKSAR VMKQAVSHLL PYIEAEKSGD DEPAGRVLIA TVKGDVHDIG KNIVAVVLQC NNFEVHDIGV MVPTETILQK AKEVKADIIG LSGLITPSLD EMIGVAQEME RQGFTCPLLI GGATTSRVHT AVKIAPNYSA PSIYVKDASR AVGVASKLVS ETQAEPYKQE LAAEYQQVRE QHEARQKKTK WVTFEQAKQN ATPIDWSAHQ PIQPQKPGVQ VLDDYPLEDL VERIDWTPFF AAWQMRGQYP KILDDEKQGE EARKLFDDAQ AMLRRIIDEK WLSARAVFGL FPANSTGEDT EVYADEQRSE VLATLCHLRQ QTEKGEGKPH QSLADFIAPK DSGVLDWMGA FAVTAGVGID EHVRRFEEAG DDYSAIMLKA LADRLAEAFA ESLHEQVRKD HWGYAADENL SNEDMIKERY QGIRPAPGYP ACPDHTEKDR LWEILNVEEN IGLTLTESRA MVPTAAVSGW YFAHPEARYF GVGKIFQDQV EDYAKRKGMS RKEAERWLGP NLGYEPED // ID A1YL83_HOMAM Unreviewed; 165 AA. AC A1YL83; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 29-OCT-2014, entry version 20. DE SubName: Full=Betaine homocysteine methyl transferase-like protein {ECO:0000313|EMBL:ABL75448.1}; DE Flags: Fragment; GN Name=BHMT {ECO:0000313|EMBL:ABL75448.1}; OS Homarus americanus (American lobster). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Malacostraca; OC Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Astacidea; OC Nephropoidea; Nephropidae; Homarus. OX NCBI_TaxID=6706 {ECO:0000313|EMBL:ABL75448.1}; RN [1] {ECO:0000313|EMBL:ABL75448.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Hepatopancreas {ECO:0000313|EMBL:ABL75448.1}; RA Horst M.N., Walker A.N., Bush P., Wilson T., Chang E.S., Miller T., RA Larkin P.; RT "Pesticide induced alterations in gene expression in the lobster, RT Homarus americanus."; RL Comp. Biochem. Physiol. Part D Genomics Proteomics 2:44-52(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; EF095140; ABL75448.1; -; mRNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 2: Evidence at transcript level; KW Transferase {ECO:0000313|EMBL:ABL75448.1}. FT NON_TER 1 1 {ECO:0000313|EMBL:ABL75448.1}. SQ SEQUENCE 165 AA; 18667 MW; DD3C6223B7645D87 CRC64; HLIAQPLALH TPDAHKQGFI DLPEFPFGLE PRICTRWDMH KYAREAYDLG VRYIGGCCGF EAYHIRAVAE ELATERGRKP KASEKHDMWA GGLKMHTKPW VRARASKEYW QSLKPSSGRP FCSSMSQPDK WGVTAGDSTL KQKTAITTDE EIAELAKPRR VMNGK // ID A1ZT30_9BACT Unreviewed; 1250 AA. AC A1ZT30; DT 20-FEB-2007, integrated into UniProtKB/TrEMBL. DT 20-FEB-2007, sequence version 1. DT 27-MAY-2015, entry version 47. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EAY26420.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EAY26420.1}; GN ORFNames=M23134_07015 {ECO:0000313|EMBL:EAY26420.1}; OS Microscilla marina ATCC 23134. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae; OC Microscilla. OX NCBI_TaxID=313606 {ECO:0000313|EMBL:EAY26420.1}; RN [1] {ECO:0000313|EMBL:EAY26420.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 23134 {ECO:0000313|EMBL:EAY26420.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EAY26420.1}. 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; AAWS01000034; EAY26420.1; -; Genomic_DNA. DR RefSeq; WP_002700937.1; NZ_AAWS01000034.1. DR ProteinModelPortal; A1ZT30; -. DR SMR; A1ZT30; 645-895, 901-1249. DR EnsemblBacteria; EAY26420; EAY26420; M23134_07015. DR PATRIC; 26280695; VBIMicMar10703_5451. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EAY26420.1}; KW Transferase {ECO:0000313|EMBL:EAY26420.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 242 242 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1250 AA; 139096 MW; 5EA5B76C994BFF53 CRC64; MMIEQLLKKR IFVLDGAMGT MIQRYKFTEE DYRGERFKDY EHPLQGNNDL LSITQPEAIK TIHGKFLEAG ADILETNTFS ATTIAMADYH MEDLVYELNY ESAKIAKEVA TEFTNKNPNK PRFVAGSIGP TNRSASLSPD VNDPGLRNIT FDQLVVAYYE QAKALVEGGV DILLVETIFD TLNAKAALFA IDKYYEDTNK RLPIMVSGTI TDAAGRTLSG QTIEAFLYSV SHMPILTVGV NCALGADLMR PYIQSLAKNA PFLVSAHPNA GLPNEFGEYD QTPEEMGAII KEFLESGFLN VVGGCCGTTP EHIAEITKIA AEYSPRVIPE QERLATYSGM EPLKVTKAIN FVNIGERTNV AGSAKFRKLI KNEQYEDALA IALHQVEGGA QVIDVNMDEG MIDSEEVMTI FLNLIASEPD IARLPIMIDS SKWTVIEAGL KVVQGKSIVN SISLKEGEEN FKNQANLVRR YGAAVVVMAF DEVGQADSYE RRIEICERAY RILVDEVKFP PEDIIFDPNI LTVATGMEEH NNYAVDFINA TRWIKENLPY AKVSGGVSNI SFSFRGNNVI REAMHSAFLY HAIKAGLDMG IVNAGMIEVY EDIPKDMLTL IEDVLLNRNA DATDKLITFA EQVKGKGKVQ VKDTKWRENP VEERLKHALL KGITEFIDED TEEARLKYDR PLHVIEGPLM DGMSVVGDLF GQGKMFLPQV VKSARVMKKS VAHLMPFMEK EKEEAVARGE LNTKGVGKIL MATVKGDVHD IGKNIVGVVL GCNNYEVIDL GVMVPAQKIL DTAIKEKVDV IGLSGLITPS LDEMVNVANE MERLGLDIPL LIGGATTSRI HTAVKIEPKY KGSVIHVLDA SRSVPVVSNL LSDNNREKFA QDIKDEYARM REGHANRKQN KKFLTAGAAR KNKFAINWDE TNVVRPQFLG TKVFEDYPLE EIVDYIDWTP FFQTWELHGK YPKILTDEVV GEEATRLFAD AKEMLQKIVT EKWLTAKSVF GFFPANTIND DDIAVYAYQK NTVEALANGN ATNTNDWGFA EDRTQTIALS HALRQQAQKA NTVPNIALSD FIAPAETGIQ DYLGGFAVSV FGAEAIAKKF EEDHDDFNSI MVKALADRMA EAFAELLHEK VRKDYWGYDQ SETLSNEELI KERYKGIRPA PGYPACPDHT EKVTLFKLLD APNSTGVALT ESLAMTPAAS VSGWYFSHPQ SKYFGLGKIE KDQVESYAER KGISVEEAEK WLSPNLNYDR // ID A2AXF3_STRCM Unreviewed; 1167 AA. AC A2AXF3; DT 20-FEB-2007, integrated into UniProtKB/TrEMBL. DT 20-FEB-2007, sequence version 1. DT 27-MAY-2015, entry version 51. DE SubName: Full=Putative methionine synthase {ECO:0000313|EMBL:CAL34092.1}; GN Name=fnq14 {ECO:0000313|EMBL:CAL34092.1}; OS Streptomyces cinnamonensis. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1900 {ECO:0000313|EMBL:CAL34092.1}; RN [1] {ECO:0000313|EMBL:CAL34092.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 1042 {ECO:0000313|EMBL:CAL34092.1}; RX PubMed=17103476; DOI=10.1002/cbic.200600338; RA Haagen Y., Gluck K., Fay K., Kammerer B., Gust B., Heide L.; RT "A gene cluster for prenylated naphthoquinone and prenylated phenazine RT biosynthesis in Streptomyces cinnamonensis DSM 1042."; RL ChemBioChem 7:2016-2027(2006). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AM384985; CAL34092.1; -; Genomic_DNA. DR ProteinModelPortal; A2AXF3; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 231 231 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 297 297 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 298 298 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 742 742 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1167 AA; 126426 MW; 19820B5F28EEE202 CRC64; MSSTPQQRAD ALRQALATRV VVADGAMGTM LQAQDPTLDD FQQLEGCNEV LNVTRPDIVR SVHQEYFAAG VDCVETNTFG ANHAALGEYD IAHRIFELSQ AGARIAREVA EEFTASSGRP RWVLGSIGPG TKLPTLGHTD FTTLRDGFQA NAEGLIAGGA DALIVETTQD LLQTKASLLG ARRALSSAGL DLPLVCSLAF ETTGTMLLGS EIGAALTALE PLGIDMIGLN CSTGPAEMTE HLRYLARHCR VPLLCMPNAG LPVLTKDGAH FPLDAAGLAD AQESFVREYG LSLVGGCCGT TPEHLRQVVQ RVSGLTPPAR TPHPEPGAAS LYQTVPFRQD TAYMAIGERT NANGSKKFRE AMLEGRWDDC VEIAREQIRE GAHMLDLCVD YVGRDGVADM AELAGRFATA STLPIVLDST ELPVLQAGLE KLGGRAVINS VNYEDGDGPE SRFAKVTALA KEHGAALIAL TIDEEGQART AEHKVAIAER LIEDLTGNWG IHEADILIDT LTFTICTGQE ESRGDGIATI EAIRELKKRH PDVQTTLGLS NISFGLNPAA RVLLNSVFLD ECVKAGLDSA IVHASKILPI ARFDDEQVST ALDLIYDRRA EGYDPLQKLM ELFEGVSTKS MKAGKAEELL ALPLEERLQR RIIDGEKNGL EADLDEALQT TPALDIVNNT LLEGMKVVGE LFGSGQMQLP FVLQSAEVMK SAVAHLEPHM EKVEGAEGKG TIVLATVRGD VHDIGKNLVD IILSNNGYNV VNLGIKQPVA AILDAAAEHK ADVIGMSGLL VKSTVIMKEN LEELNQRKMA ADYPVILGGA ALTRAYVEQD LHEIYEGEVR YARDAFEGLR LMDALIAVKR GVPGASLPEL KQRRVPKRDT PVSVEEPEGP SRSDVAVDNP VPTPPFWGTR VIKGIQLKEY ASWLDEGALF KGQWGLKQAR TGTGPTYEEL VEREGRPRLR GLLDELQTKN LLEAAVVYGY FRCVSKGEDL ILLDEAGAEL TRFTFPRQPR GRRLCLADFF RPEESGETDV VGLQVVTVGS KIGEAAAELF AADSYRDYLE LHGLSVQLAE ALAEYWHARV RAELGIAGAD PDTPEGMFRT QYQGCRYSLG YPACPDLADR AKIAALLRPE RIGVQLSEEF QLHPEQSTDA IVLHHPQASY FNAGGRP // ID A2BR57_PROMS Unreviewed; 1188 AA. AC A2BR57; DT 20-FEB-2007, integrated into UniProtKB/TrEMBL. DT 20-FEB-2007, sequence version 1. DT 27-MAY-2015, entry version 68. DE SubName: Full=Putative methionine synthase {ECO:0000313|EMBL:ABM70268.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABM70268.1}; GN Name=metH {ECO:0000313|EMBL:ABM70268.1}; GN OrderedLocusNames=A9601_09841 {ECO:0000313|EMBL:ABM70268.1}; OS Prochlorococcus marinus (strain AS9601). OC Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae; OC Prochlorococcus. OX NCBI_TaxID=146891 {ECO:0000313|EMBL:ABM70268.1, ECO:0000313|Proteomes:UP000002590}; RN [1] {ECO:0000313|EMBL:ABM70268.1, ECO:0000313|Proteomes:UP000002590} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AS9601 {ECO:0000313|EMBL:ABM70268.1, RC ECO:0000313|Proteomes:UP000002590}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000551; ABM70268.1; -; Genomic_DNA. DR RefSeq; WP_011818423.1; NC_008816.1. DR RefSeq; YP_001009375.1; NC_008816.1. DR ProteinModelPortal; A2BR57; -. DR STRING; 146891.A9601_09841; -. DR EnsemblBacteria; ABM70268; ABM70268; A9601_09841. DR GeneID; 4717694; -. DR KEGG; pmb:A9601_09841; -. DR PATRIC; 22983465; VBIProMar75723_0989. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PMAR146891:GH90-1003-MONOMER; -. DR Proteomes; UP000002590; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002590}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABM70268.1}; KW Transferase {ECO:0000313|EMBL:ABM70268.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 746 746 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1188 AA; 132537 MW; BBE95C01F35BFA11 CRC64; MESFRTYLNR DEKPLIIFDG GTGTSFQNLN LTPDDFGGKE LEGCNENLVL SSPEVVEKVH NSFLEAGCHV IETNTFGASS IVLDEYDIAD KAYEINKNAA FIAKKAAHKY SSVDKPRFVA GSIGPTTKLP TLGHIDFDEL KQSYKEQIYG LIDGGVDILL IETCQDVLQI KSALLASKEI LESKNIDIPL MVSITMETTG TMLVGSDIAS ALTILEPFNI DILGLNCATG PEQMKEHIKY LSENSPFAIS CIPNAGLPEN IGGVAHYRLK PIELKMQLMN FIYDFNVQLI GGCCGTTPEH IKYLSSIIDE IIDIERTHNN GKKNSSGFIP SASSIYNSVP YKQDNSILIV GERLNASGSK KVRELLNNDD WDGLVAIAKQ QQKENAHVLD VNVDYVGRDG VKDMKEITSR LVTNINLPLM IDSTDADKME SGLKSAGGKC IINSTNYEDG NERFDQVLNL ALGYGSGLVV GTIDEDGMAR NSEKKYKIVK RAINRTRECG LSDYELFFDP LALPISTGIE EDRLNAKETI SAILKIRENF PDIHIILGIS NISFGLSPLS RINLNSIFLD ECIKAGLDSA IIAPNKILPL SKISEETKKL CLDLIYDKRK FEDDICIYDP LVELTKAFQD LSIQDFKKAS SENKNQTLEE SLKNHIIDGE KIGLEDQLNK ALKKYKPLEI INTFLLDGMK VVGDLFGSGQ MQLPFVLQSA ETMKFAVSIL EPHMETVDEN ISNGKLLIAT VKGDVHDIGK NLVDIILTNN GYDVINLGIK QDVSAIIDAQ KKYNADCIAM SGLLVKSTAF MKDNLEAFNN ENISVPVILG GAALTPKFVN EDCSKIYKGK ILYGKDAFTD LKFMNEYMDN KKKGNWSNTE GFINNEGINI NLASSKSNSQ AVKKSISINT DTSKFNLKEN FIRSKFINEE DPIQAPFLGT KVLNDVDIDL NKLIFYLDTK ALFSGQWQIK KGKNQSVDEY NNYLNSYAKP LLDKWLEIII EKKLISPKAV YGYFRCGRKD NSIFLFDEKS LNKISQFNFP RQKSGNNLCI ADFYCDLKND KPIDIFPMQA VTMGDIASEY SQKLFKEDKY SDYLLFHGLT VQLAEALAEY VHALIRIECG FRSEEPYKNR EILAQKYRGA RYSFGYPACP KVSDSNIQLS LLDAKRINLT MDESEQLHPE QSTTAIISLH SKAKYFSA // ID A2BWK5_PROM5 Unreviewed; 1187 AA. AC A2BWK5; DT 20-FEB-2007, integrated into UniProtKB/TrEMBL. DT 20-FEB-2007, sequence version 1. DT 27-MAY-2015, entry version 66. DE SubName: Full=Putative methionine synthase {ECO:0000313|EMBL:ABM72166.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABM72166.1}; GN Name=metH {ECO:0000313|EMBL:ABM72166.1}; GN OrderedLocusNames=P9515_09591 {ECO:0000313|EMBL:ABM72166.1}; OS Prochlorococcus marinus (strain MIT 9515). OC Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae; OC Prochlorococcus. OX NCBI_TaxID=167542 {ECO:0000313|EMBL:ABM72166.1, ECO:0000313|Proteomes:UP000001589}; RN [1] {ECO:0000313|EMBL:ABM72166.1, ECO:0000313|Proteomes:UP000001589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MIT 9515 {ECO:0000313|EMBL:ABM72166.1, RC ECO:0000313|Proteomes:UP000001589}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000552; ABM72166.1; -; Genomic_DNA. DR RefSeq; WP_011820268.1; NC_008817.1. DR RefSeq; YP_001011273.1; NC_008817.1. DR ProteinModelPortal; A2BWK5; -. DR STRING; 167542.P9515_09591; -. DR EnsemblBacteria; ABM72166; ABM72166; P9515_09591. DR KEGG; pmc:P9515_09591; -. DR PATRIC; 23015520; VBIProMar113831_0985. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PMAR167542:GI3N-986-MONOMER; -. DR Proteomes; UP000001589; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001589}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABM72166.1}; KW Transferase {ECO:0000313|EMBL:ABM72166.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 746 746 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1187 AA; 132380 MW; 97F6B83233967603 CRC64; MVSFRDYLNR DDKPIIIFDG GTGTSFQNLN LSSNHFGGDE LEGCNENLVL SSPNIVEQVH NSFLEAGCHV IETNTFGASS IVLDEYNIAS KAYDINKKAA QIAQKSVNSF SSVNSPRFVA GSIGPTTKLP TLGHIEFDKL KESYEEQIHG LIDGGIDLLL IETCQDVLQI KSALFASQEV IKNKNIDLPI MISITMETTG TMLVGSDIAS ALTILEPYKI DILGLNCATG PVQMKDHIKY LSENSPFAIS CIPNAGLPEN VGGVAHYKLT PIELKMQLMN FIYDYNVQLI GGCCGTTPEH IKYLSSIIDE IVDKKKINTK SSTEKNSFIP SAASIYNSVP YKQDNSILIV GERLNASGSK KVRELLNKDD WDGLVSIAKQ QQKENAHILD VNVDYVGRDG VKDMKEITSR LVTNINLPLM IDSTEADKME SGLKTAGGKC IINSTNYEDG DDRFNQVLKL ALDYGSGIVI GTIDEDGMAR TSDKKYNIAK RALIQTRSSG LEDYEVFFDP LALPISTGIE EDRLNAKATI EAILKIRKSF PDIHIILGIS NISFGLSPLS RINLNSIFLD ECIKAGLDSA IIAPNKILPL SKISEDTKKL CLDLIYDRRN FKNKICVYDP LVELTKAFQD LTISDFKKAS TSNKKLSLEE KLKNHIVDGE KIGLEENLNN ALKKYNPLEI INTYLLDGMK VVGELFGSGQ MQLPFVLQSA ETMKFAVSVL EPHMETVDEK VSNGKLLIAT VKGDVHDIGK NLVDIILSNN GFDVINLGIK QDVSAIIEAQ KIHKADCIAM SGLLVKSTAF MKDNLEAFNN AEINVPVILG GAALTPKFVN EDCSQIYKGK ILYGKDAFTD LQFMNEFMES KKNGNWSNEN GFINEDDIQI KLASPRSTDK NRYLNKNIKN TEKIKIIENF ERSSFVDEEK PIKAPFIGTR VLQNVDIDIE KLLFYLDKKA LFSGQWQIKK NKGQSVEEYN KYLESYANPL LQKWIDIILD KELISPKAVY GYFNCGRKDN SIYLFDNKSH KKISEFNFPR QKSGNNLCIA DFYCDLKNNQ PLDIFPMQAV TMGAIASEYS QELFKADKYS DYLIFHGLTV QLAEALAEYV HSLVRIECGF KKFEPTNNRE ILAQKYRGAR YSFGYPACPK VSDSNIQLSL LDAKRINLTM DESEQLHPEQ STTAIISLHS KAKYFSA // ID A2C254_PROM1 Unreviewed; 1182 AA. AC A2C254; DT 20-FEB-2007, integrated into UniProtKB/TrEMBL. DT 20-FEB-2007, sequence version 1. DT 27-MAY-2015, entry version 67. DE SubName: Full=Putative methionine synthase {ECO:0000313|EMBL:ABM75564.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABM75564.1}; GN Name=metH {ECO:0000313|EMBL:ABM75564.1}; GN OrderedLocusNames=NATL1_10061 {ECO:0000313|EMBL:ABM75564.1}; OS Prochlorococcus marinus (strain NATL1A). OC Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae; OC Prochlorococcus. OX NCBI_TaxID=167555 {ECO:0000313|EMBL:ABM75564.1, ECO:0000313|Proteomes:UP000002592}; RN [1] {ECO:0000313|Proteomes:UP000002592} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NATL1A {ECO:0000313|Proteomes:UP000002592}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000553; ABM75564.1; -; Genomic_DNA. DR RefSeq; WP_011823689.1; NC_008819.1. DR RefSeq; YP_001014829.1; NC_008819.1. DR ProteinModelPortal; A2C254; -. DR STRING; 167555.NATL1_10061; -. DR EnsemblBacteria; ABM75564; ABM75564; NATL1_10061. DR KEGG; pme:NATL1_10061; -. DR PATRIC; 23019607; VBIProMar31285_1030. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PMAR167555:GI3K-1028-MONOMER; -. DR Proteomes; UP000002592; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002592}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABM75564.1}; KW Transferase {ECO:0000313|EMBL:ABM75564.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 226 226 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 292 292 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 744 744 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1182 AA; 131435 MW; 75B9FBE84730F716 CRC64; MTHFLDYLNS EKRPIIVFDG ATGTSLQDQQ LTADDYGGAS LEGCNENLVL SSVSSVEKVH QSFLEAGCDV IETNTFGATS IVLDEYGIGN KAYEINFKAA QIARRIANKY QTPEKPRFVA GSIGPTTKLP TLGHISFDEL KKSYLEQAKA LIEGGIDLFL IETCQDVLQI KAALQSVNEA IGDGIKIPVM VSVTMETTGQ MLIGSDISSI TTILEPFSID ILGLNCATGP EEMKDHIKYL SEHSPFHISC IPNAGLPENV GGKAHYRLTP MELKFQLSHF INDLGVQLIG GCCGTRPEHI KQLSDLSLEL LSSDRRLINL SKKRSIIPAA SSIYESIPYE QDNSFLIVGE RLNASGSKKV RELLNIEDWD GLVGIAKSQL KENAHVLDVN VDFVGRNGIE DMSNLVKRLV NNINLPLMLD STDYEKMESG LKRAGGKCIL NSTNYEDGQD RFHKVIDLAK EHGSAVVIGT IDEDGMARAA EKKAEIATRA FKDATNSGLK PYEIFYDPLA LPISTGLEED RKNGFETIKA IKLIKDRHPQ VHLILGISNV SFGLSSSARV VLNSIFLNEA IKAGLDSAIV SPSKILPLNK ISEEEIKICL DLIYDKRIID NSVCTYDPLT TLTSYFDDSK KTLNNSSIDE DINLPIEDKL KNHIIDGEKT NLHSNLNLAL NKYKPLIIIN EYLLDGMKVV GELFGSGQMQ LPFVLQSAET MKYAVSYLED FMDKSEVNQS KGKFIIATVK GDVHDIGKNL VDIILSNNGY DVINLGIKQD VNAIIKAQKE HHADCIAMSG LLVKSTAFMK DNLKALNEED IDVPIILGGA ALTPKFVNQD CASVYKGKVI YGRDAFTDLK FMDAYMKAKL ANNWNNKTGF SEGAPEGITI GTYKSSNSDP KVIKESLEVK KVNDNSRSKD ISSVKSIKPP FLGPKVLLEK DIDLSNVYKF LDRNALFAGQ WQMKRSKDMS ASDYKEFLKQ KAEPKLDYWM NKIINDNLIS PSLVYGYFPC GREGNYLNVY DTDHKSLLGK FLLPRQRSGK RYCIADFYND LVDNHPSDYL PMQAVTMGEK ASDYSHKLFS QDSYSDYLYF HGLTVQLAEA LAEYIHSIIR IECGFKYEEP DNIKDILDVK YRGCRYSFGY PACPEVSDSR KQLDWLDADK INISMDESEQ LHPEQSTTAI VALHPVAKYF GI // ID A2C9S5_PROM3 Unreviewed; 1214 AA. AC A2C9S5; DT 20-FEB-2007, integrated into UniProtKB/TrEMBL. DT 20-FEB-2007, sequence version 1. DT 27-MAY-2015, entry version 65. DE SubName: Full=Putative methionine synthase {ECO:0000313|EMBL:ABM78235.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABM78235.1}; GN Name=metH {ECO:0000313|EMBL:ABM78235.1}; GN OrderedLocusNames=P9303_14891 {ECO:0000313|EMBL:ABM78235.1}; OS Prochlorococcus marinus (strain MIT 9303). OC Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae; OC Prochlorococcus. OX NCBI_TaxID=59922 {ECO:0000313|EMBL:ABM78235.1, ECO:0000313|Proteomes:UP000002274}; RN [1] {ECO:0000313|EMBL:ABM78235.1, ECO:0000313|Proteomes:UP000002274} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MIT 9303 {ECO:0000313|EMBL:ABM78235.1, RC ECO:0000313|Proteomes:UP000002274}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000554; ABM78235.1; -; Genomic_DNA. DR RefSeq; WP_011826128.1; NC_008820.1. DR RefSeq; YP_001017500.1; NC_008820.1. DR ProteinModelPortal; A2C9S5; -. DR STRING; 59922.P9303_14891; -. DR EnsemblBacteria; ABM78235; ABM78235; P9303_14891. DR KEGG; pmf:P9303_14891; -. DR PATRIC; 23000458; VBIProMar17757_1540. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PMAR59922:GH54-1580-MONOMER; -. DR Proteomes; UP000002274; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002274}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABM78235.1}; KW Transferase {ECO:0000313|EMBL:ABM78235.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 242 242 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 766 766 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1214 AA; 134420 MW; 42430907FCA358CB CRC64; MRDRMTAGPL DITRPESAFL ARLHSSERPV LVFDGATGTS LQKQDLSADD FGGALLEGCN ENLVITRPDA VREVHRQFLE SGCDVIETNS FGAASIVLAE YGLEDQAFEL NRQAAQLAKA MAAQYSTKDQ PRFVAGSIGP TTKLPTLGHI AFDTMRDSFQ EQAEGLLAGD IDLFIVETCQ DVLQIKAALQ GIESAFLKAG ERRPIMVSVT METTGTMLLG SDIASVVTIL EPFPIDILGL NCATGPEQMK DHIRYLSEHS PFTISCIPNA GLPENIGGVA HYRLKPLELK MQLMHFVEDL GVQVIGGCCG TTPEHTSALA ELAKEMRAAE RACRQGEKEH QRQLFGYEPS AASIYGITPY HQDNSFLIIG ERLNASGSKK VRELLNSEDW DGLVALARGQ IKENAHVLDV NVDYVGRDGE KDMNQLVSRL VTNINLPLML DSTEWQKMEA GLKVSGGKCI LNSTNYEDGE ERFFKVLDLA KKYGAGLVIG TIDENGMART AMQKVAIAKR AYRDATEYGI PAHEIFYDPL ALPISTGIEE DRRNGLETIE AIRIIREELQ GVHVVLGVSN VSFGLSPAAR ITLNSVFLHD CTDAGMDAAI VSPAKILPLN KVSDEQQKIC RDLINDQRRF ENDICIYDPL TKLTSLFEGV SAKEARASGP SLADLPVEDR LKQHIIDGER IGLNEALDEG LESYKPLQLV NTFLLDGMKV VGELFGSGKM QLPFVLQSAQ TMKAAVAYLE PYMEKSEGDN SSKAKFLIAT VKGDVHDIGK NLVDIILTNN GYEVINLGIK QDAASIINAQ KTHQADCIAM SGLLVKSTAF MKNNLQEFND SGISVPVILG GAALTPRFVN HDCSEVYKGK LIYGKDAFTD LRFMDAYVKA LSNDRWDDCR GFLDGTPDGL TLGGQSTESD SPPSNKEEQP QEENEKNIQH INLPVNTSRS EKVTQEDAVT PPFLGSKHLK LDKIPLDEII QYLDRNALFS GQWQIRKRKD QSREQYDQYI NDEIEPILQH WLQRIRNESL LHPGVAYGYF PCGRKDNDLL VFNNEGNSLL GQFNLPRQKS GNRYCIADFY RDLEEGLPKD ILPMQAVTMG ENASIFAQKL FESDAYTDYL FFHGLSVQLA EALAEWTHSR IRCECGFKSD EPKTLQDVLA QRYRGSRFSF GYPACPNVGD SRQQLKWLKA DSIGLTMDPN DQLHPEQSTT ALVTLHSKAR YFSA // ID A2R696_ASPNC Unreviewed; 353 AA. AC A2R696; DT 06-MAR-2007, integrated into UniProtKB/TrEMBL. DT 06-MAR-2007, sequence version 1. DT 27-MAY-2015, entry version 41. DE SubName: Full=Aspergillus niger contig An15c0240, genomic contig {ECO:0000313|EMBL:CAK48546.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:CAK48546.1}; GN ORFNames=An15g07110 {ECO:0000313|EMBL:CAK48546.1}; 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 {ECO:0000313|Proteomes:UP000006706}; RN [1] {ECO:0000313|EMBL:CAK48546.1, ECO:0000313|Proteomes:UP000006706} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS 513.88 / FGSC A1513 {ECO:0000313|Proteomes:UP000006706}; 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., van den Berg M., RA Breestraat S., Caddick M.X., Contreras R., Cornell M., Coutinho P.M., RA Danchin E.G., Debets A.J., Dekker P., van Dijck P.W., van Dijk A., RA Dijkhuizen L., Driessen A.J., d'Enfert C., Geysens S., Goosen C., RA Groot G.S., de Groot P.W., Guillemette T., Henrissat B., Herweijer M., RA van den Hombergh J.P., van den Hondel C.A., van der Heijden R.T., 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., Meulenberg R., RA Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., RA Pal K., van Peij N.N., Ram A.F., Rinas U., Roubos J.A., Sagt C.M., RA Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., RA van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P., RA van Ooyen A.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; AM270351; CAK48546.1; -; Genomic_DNA. DR RefSeq; XP_001397238.1; XM_001397201.2. DR ProteinModelPortal; A2R696; -. DR STRING; 5061.CADANGAP00012156; -. DR EnsemblFungi; CADANGAT00012390; CADANGAP00012156; CADANGAG00012390. DR GeneID; 4988312; -. DR KEGG; ang:ANI_1_1740134; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000006706; Chromosome 3R. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006706}; KW Methyltransferase {ECO:0000313|EMBL:CAK48546.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006706}; KW Transferase {ECO:0000313|EMBL:CAK48546.1}. SQ SEQUENCE 353 AA; 38706 MW; A8683A4387D7B785 CRC64; MAKTPILILD GGLGTSLQDH YNITFSSSTT PLWSSHLMIS DPSTLLSCQR DFTTTAAVDV LLTATYQVSP EGFQRTKTPS HPTGIPRESI AGYLRTALDV AGQAVQNTSA SVALSLGPYG ACMIPGQEYS GKYDGEHDTE EKLWRWHTDR LGLFNDEAME GMRLGERVKY IAMETVPRID EVRAVRRAVG SSRFCEGIPF WVACVFPIED KDTLPDGSTV DEVVEAALLP IEGGATPWGI GINCTKLHKL PRLVKLFGDA VERLLRDGRI QERPALVLYP DGTQGEVYNT ATQTWEKVQD KSGAADSRPW EVQLAQVVND ASATGQFSSI LVGGCCKASF NDIKRLREQL RPQ // ID A2S5V9_BURM9 Unreviewed; 359 AA. AC A2S5V9; DT 06-MAR-2007, integrated into UniProtKB/TrEMBL. DT 06-MAR-2007, sequence version 1. DT 27-MAY-2015, entry version 48. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABN03249.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABN03249.1}; GN OrderedLocusNames=BMA10229_A1345 {ECO:0000313|EMBL:ABN03249.1}; OS Burkholderia mallei (strain NCTC 10229). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=412022 {ECO:0000313|EMBL:ABN03249.1, ECO:0000313|Proteomes:UP000002283}; RN [1] {ECO:0000313|EMBL:ABN03249.1, ECO:0000313|Proteomes:UP000002283} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC 10229 {ECO:0000313|EMBL:ABN03249.1, RC ECO:0000313|Proteomes:UP000002283}; 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; ABN03249.1; -; Genomic_DNA. DR RefSeq; WP_004204527.1; NC_008836.1. DR RefSeq; YP_001027328.1; NC_008836.1. DR ProteinModelPortal; A2S5V9; -. DR STRING; 412022.BMA10229_A1345; -. DR EnsemblBacteria; ABN03249; ABN03249; BMA10229_A1345. DR KEGG; bml:BMA10229_A1345; -. DR PATRIC; 19133650; VBIBurMal46188_3544. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; BMAL412022:GJI8-1345-MONOMER; -. DR Proteomes; UP000002283; Chromosome I. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002283}; KW Methyltransferase {ECO:0000313|EMBL:ABN03249.1}; KW Transferase {ECO:0000313|EMBL:ABN03249.1}. SQ SEQUENCE 359 AA; 38459 MW; 1013B7D60E53B797 CRC64; MSEPTPIAPF ASSAAPAAPY TRGAALPQLL RQRILILDGA MGTMIQRYKL DEAAYRGERF KDFPRDVKGN NELLSITQPR IIREIHDQYF AAGADIVETN TFGATAVAQA DYGMEALVVE MNVASAALAR ESAAKYATPE KPRFVAGAIG PTPKTASISP DVNDPGARNV TFDELRDAYY QQAKALLDGG VDLFLVETIF DTLNAKAALF ALDQLFDDTG ERLPIMISGT VTDASGRILS GQTVEAFWNS LRHAKPLTFG LNCALGAALM RPYIAELAKL CDTYVSCYPN AGLPNPMSDT GFDETPDVTS GLLKEFAQAG LVNLAGGCCG TTPEHIAAIA KALAEVKPRR WPSQYSEAA // ID A2SC39_METPP Unreviewed; 357 AA. AC A2SC39; DT 06-MAR-2007, integrated into UniProtKB/TrEMBL. DT 06-MAR-2007, sequence version 1. DT 27-MAY-2015, entry version 56. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABM93128.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABM93128.1}; GN OrderedLocusNames=Mpe_A0166 {ECO:0000313|EMBL:ABM93128.1}; OS Methylibium petroleiphilum (strain PM1). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Methylibium. OX NCBI_TaxID=420662 {ECO:0000313|EMBL:ABM93128.1, ECO:0000313|Proteomes:UP000000366}; RN [1] {ECO:0000313|EMBL:ABM93128.1, ECO:0000313|Proteomes:UP000000366} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PM1 {ECO:0000313|EMBL:ABM93128.1, RC ECO:0000313|Proteomes:UP000000366}; RX PubMed=17158667; DOI=10.1128/JB.01259-06; RA Kane S.R., Chakicherla A.Y., Chain P.S.G., 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; ABM93128.1; -; Genomic_DNA. DR RefSeq; WP_011827767.1; NC_008825.1. DR RefSeq; YP_001019363.1; NC_008825.1. DR STRING; 420662.Mpe_A0166; -. DR EnsemblBacteria; ABM93128; ABM93128; Mpe_A0166. DR KEGG; mpt:Mpe_A0166; -. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; MPET420662:GHBE-166-MONOMER; -. DR Proteomes; UP000000366; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000366}; KW Methyltransferase {ECO:0000313|EMBL:ABM93128.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000366}; KW Transferase {ECO:0000313|EMBL:ABM93128.1}. SQ SEQUENCE 357 AA; 38603 MW; 24236CB41E0082DC CRC64; MSALPYTRAA QLPELLKQRI LILDGAMGTM IQRYKLGEAD YRGERFKDHG KDLKGNNELL QFTRPDVITE IHEGYLAAGA DLIETNTFGA TTIAQEDYGL APLAREMNVV AARLARAACD KFSTPDKPRF VAGAFGPTPR TASISPDVND PAARNVSFDE LRAAYYEQGE GLLEGGADLF LVETIFDTLN AKAAIFAIDE LFENTGERLP VIISGTVTDA SGRILSGQTV SAFWHSVRHA HPVAVGLNCA LGATLMRPYI EELCKAAPDT FISCYPNAGL PNPMSDTGFD ETPAITGGLV EEFARAGFLN IAGGCCGTTP DHIAEIARRV SAYRPRARQE RWISELSEEA DGDLQTA // ID A2TF10_PAROL Unreviewed; 400 AA. AC A2TF10; DT 06-MAR-2007, integrated into UniProtKB/TrEMBL. DT 06-MAR-2007, sequence version 1. DT 04-MAR-2015, entry version 30. DE SubName: Full=Betaine homocysteine S-methyltansferase {ECO:0000313|EMBL:ABM88795.1}; DE EC=2.1.1.5 {ECO:0000313|EMBL:ABM88795.1}; GN Name=BHMT {ECO:0000313|EMBL:ABM88795.1}; OS Paralichthys olivaceus (Bastard halibut) (Hippoglossus olivaceus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Carangaria; Pleuronectiformes; Pleuronectoidei; Paralichthyidae; OC Paralichthys. OX NCBI_TaxID=8255 {ECO:0000313|EMBL:ABM88795.1}; RN [1] {ECO:0000313|EMBL:ABM88795.1} RP NUCLEOTIDE SEQUENCE. RA Zhang F.T., Zhang Y.B., Gui J.F.; RT "Gene cloning and characterization of Paralichthys olivaceus betaine RT homocysteine S-methyltansferase."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EF198069; ABM88795.1; -; mRNA. DR ProteinModelPortal; A2TF10; -. DR SMR; A2TF10; 7-393. DR HOVERGEN; HBG080367; -. DR UniPathway; UPA00051; UER00083. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000313|EMBL:ABM88795.1}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000313|EMBL:ABM88795.1}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 212 212 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 400 AA; 44252 MW; 341AA4485FF1994E CRC64; MAPAGAKRGV LERLDAGEVV IGDGGFVFAL EKRGYVKAGP WTPEAAAENP EAVRQLHREF LRAGSTVMQT FTFYASDDKL VNRGHTQRFT GQQINEAACD LAREVANEGD ALVAGGISQT PAYLSRKNEG EVKAIFKKQI DVFIQKNVDF LIAEYFEHVE EAEWAVQVLR TTGKPVAATL CIGPEGDLNG VSPGDCAVKL VKAGAHIVGI NCHFDPETCV KTVKMMKAGV EKAGLKAHYM SQPLAFHTPD CNRQGFIDLP EFPFSLEPRI LIRWDMQRYA REAYIAGIRY IGGCCGFEPY HIRALAEELA PERGFLPVGS EKHGNWGSGL EMHTKPWVRA RARRDYWEKQ KPASGRPYCP SMSSPDGWGV TKGHADLMQQ KEATSKEQLK VLFDKANKCH // ID A2TZV1_9FLAO Unreviewed; 334 AA. AC A2TZV1; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 27-MAY-2015, entry version 39. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EAQ42273.1}; GN ORFNames=MED152_06125 {ECO:0000313|EMBL:EAQ42273.1}; OS Polaribacter sp. MED152. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Polaribacter. OX NCBI_TaxID=313598 {ECO:0000313|EMBL:EAQ42273.1, ECO:0000313|Proteomes:UP000006470}; RN [1] {ECO:0000313|EMBL:EAQ42273.1, ECO:0000313|Proteomes:UP000006470} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MED152 {ECO:0000313|EMBL:EAQ42273.1}; 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP004349; EAQ42273.1; -; Genomic_DNA. DR RefSeq; WP_015480985.1; NC_020830.1. DR RefSeq; YP_007671242.1; NC_020830.1. DR EnsemblBacteria; EAQ42273; EAQ42273; MED152_06125. DR KEGG; pom:MED152_06125; -. DR PATRIC; 31152470; VBIPolSp11901_1216. DR KO; K00548; -. DR Proteomes; UP000006470; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006470}; KW Methyltransferase {ECO:0000313|EMBL:EAQ42273.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006470}; KW Transferase {ECO:0000313|EMBL:EAQ42273.1}. SQ SEQUENCE 334 AA; 36730 MW; EB294E8151B6C227 CRC64; MSNIYKALQE RILVLDGAMG TMLQAYKFTE EDFRGERFKE YPTPLQGNND LLSLTQPEAI KTIHAKYFEA GADIIETNTF SGTTIAMADY QMEDLVYELN YQSAKIAKEV ALEFTAKEPN KPRFVAGSIG PTNRTASMSP DVNDPGYRAV TFDELRVAYK QQVEALLDGG ADILLVETVF DTLNAKAALF AIEQVKEERK MDIPVMLSGT ITDASGRTLS GQTAEAFLIS VSHIPLLSVG FNCALGANLL QPHLEAIANK TEFAISAHPN AGLPNAFGEY DETPEEMGEQ IEEYLKKNLI NIIGGCCGTS PEHIRVIANI AAKYKPRKIL EKVH // ID A2VKI0_MYCTX Unreviewed; 302 AA. AC A2VKI0; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Homocysteine S-methyltransferase mmuM {ECO:0000313|EMBL:EAY60661.1}; GN ORFNames=TBCG_02399 {ECO:0000313|EMBL:EAY60661.1}; OS Mycobacterium tuberculosis C. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=348776 {ECO:0000313|EMBL:EAY60661.1}; RN [1] {ECO:0000313|EMBL:EAY60661.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C {ECO:0000313|EMBL:EAY60661.1}; 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 ----------------------------------------------------------------------- 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; EAY60661.1; -; Genomic_DNA. DR RefSeq; WP_003899329.1; NZ_CH482373.1. DR ProteinModelPortal; A2VKI0; -. DR SMR; A2VKI0; 2-300. DR EnsemblBacteria; EAY60661; EAY60661; TBCG_02399. DR PATRIC; 26049204; VBIMycTub57268_2714. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EAY60661.1}; KW Transferase {ECO:0000313|EMBL:EAY60661.1}. SQ SEQUENCE 302 AA; 31532 MW; D819AB178F9A551D CRC64; MELVSDSVLI SDGGLATELE ARGHDLSDPL WSARLLVDAP HAITAVHTAY FRAGAQIATT ASYQASFEGF AARGIGHDDA TVLLRRSVEL AQAARDEVGV GGLSVAASVG PYGAALADGS EYRGCYGLSV AALMKWHLPR LEVLVDAGAD MLALKTIPDI DEAEALVNLV RRLATPAWLS YTINGTRTRA GQPLTDAFAV AAGVPEIVAV GVNCCAPDDV LPAIAFAVAH TGKPVIVYPN SGEGWDGRRR AWVGPRRFSG SSGQLAREWV AAGARIVGGC CRVRPIDIAE IGRALTTAPP RG // ID A2VV10_9BURK Unreviewed; 355 AA. AC A2VV10; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 27-MAY-2015, entry version 30. DE SubName: Full=Methionine synthase I (Cobalamin-dependent) {ECO:0000313|EMBL:EAY63556.1}; GN ORFNames=BCPG_01842 {ECO:0000313|EMBL:EAY63556.1}; OS Burkholderia cenocepacia PC184. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=350702 {ECO:0000313|EMBL:EAY63556.1}; RN [1] {ECO:0000313|EMBL:EAY63556.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PC184 {ECO:0000313|EMBL:EAY63556.1}; 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; CH482377; EAY63556.1; -; Genomic_DNA. DR RefSeq; WP_006477666.1; NZ_CH482377.1. DR EnsemblBacteria; EAY63556; EAY63556; BCPG_01842. DR PATRIC; 26850642; VBIBurCen79288_2031. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 355 AA; 38239 MW; 6857B74674E6F938 CRC64; MSATPLAASV PLDARYTRGA ALPALLKSRI LILDGAMGTM IQRYKLDEAA YRGERFKDFP RDIKGNNELL SLTQPQIIRE IHDQYFAAGA DIVETNTFGA TTVAQADYGM EDLVVEMNVA SAKLARESAA KYATPDKPRF VAGAIGPTPK TASISPDVND PGARNVTFDE LRTSYYQQAK ALLDGGVDLF LVETIFDTLN AKAALFALDE LFEDTGERLP IMISGTVTDA SGRILSGQTV EAFWNSLRHA KPLTFGLNCA LGAALMRPYI AELAKLCDTY VSCYPNAGLP NPMSDTGFDE TPDVTSGLLK EFAQAGLVNL AGGCCGTTPE HIAEIAKALA DVKPRRWPNQ YSDNA // ID A2W726_9BURK Unreviewed; 356 AA. AC A2W726; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 27-MAY-2015, entry version 30. DE SubName: Full=Methionine synthase I (Cobalamin-dependent) {ECO:0000313|EMBL:EAY67772.1}; GN ORFNames=BDAG_00463 {ECO:0000313|EMBL:EAY67772.1}; OS Burkholderia dolosa AUO158. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=350701 {ECO:0000313|EMBL:EAY67772.1}; RN [1] {ECO:0000313|EMBL:EAY67772.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AUO158 {ECO:0000313|EMBL:EAY67772.1}; 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; EAY67772.1; -; Genomic_DNA. DR RefSeq; WP_006763267.1; NZ_CH482380.1. DR EnsemblBacteria; EAY67772; EAY67772; BDAG_00463. DR PATRIC; 26860979; VBIBurDol134514_1487. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 356 AA; 38137 MW; F08C341A6907176E CRC64; MSATPSAASA APLDAHYTRG AELPALLNSR ILILDGAMGT MIQRYKLDEA AYRGERFKDF PRDVKGNNEL LSITQPQVIR EIHDQYFAAG ADIVETNTFG ATSVAQADYG MEDLVVEMNV ASAKLARESA AKYATPDKPR FVAGAIGPTP KTASISPDVN DPGARNVTFD ELRDAYYTQA KALLDGGVDL FLVETIFDTL NAKAALFALD QLFEDTGERL PIMISGTVTD ASGRILSGQT VEAFWNSLRH AKPLTFGLNC ALGAALMRPY IAELAKLCDT YVSCYPNAGL PNPMADTGFD ETPDVTSGLL KEFAQAGLVN LAGGCCGTTP EHIAEIAKAL ADVKPRRWPS QYSEAA // ID A2Z7F0_ORYSI Unreviewed; 335 AA. AC A2Z7F0; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 04-MAR-2015, entry version 35. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EAY78534.1}; GN ORFNames=OsI_33628 {ECO:0000313|EMBL:EAY78534.1}; 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 {ECO:0000313|EMBL:EAY78534.1, ECO:0000313|Proteomes:UP000007015}; RN [1] {ECO:0000313|EMBL:EAY78534.1, ECO:0000313|Proteomes:UP000007015} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. 93-11 {ECO:0000313|Proteomes:UP000007015}; 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). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000135; EAY78534.1; -; Genomic_DNA. DR ProteinModelPortal; A2Z7F0; -. DR STRING; 39947.LOC_Os10g28630.1; -. DR EnsemblPlants; BGIOSGA032938-TA; BGIOSGA032938-PA; BGIOSGA032938. DR Gramene; A2Z7F0; -. DR HOGENOM; HOG000265278; -. DR OMA; QCKDENT; -. DR Proteomes; UP000007015; Chromosome 10. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007015}; KW Reference proteome {ECO:0000313|Proteomes:UP000007015}. SQ SEQUENCE 335 AA; 36508 MW; 067B43F2E99A4D75 CRC64; MSQQGEYHAD MMAEFLRGSG GAAVIDGGLA TELEANGADL KDALWSARCL FTCPDLIRKV HLDYLEAGAS VLITGSYQAT IQGFLSKGFS QEESESFLRR SVELACEARA IYLEKCSNGS DEAKDVTKYR KRPILIAASV GSYGAYLADG SEYSGDYGNE GTLEFLKNFH LRRLQVLAEA GPDVIVFETI PNKIETQAYV ELLEECKLRI PAWFGFTSKD GVNVVSGDSL IECASIADSC KEVAAVGINC TPPRFIHELV LSIRKVTSKP ILIYPNSGES YDPIRKEWVE CSGISNEDFV SYVKKWHEAG ASLIGGCCRT SPDTIRGISK ALHGV // ID A2ZMI7_ORYSI Unreviewed; 342 AA. AC A2ZMI7; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 27-MAY-2015, entry version 37. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EAY83821.1}; GN ORFNames=OsI_39039 {ECO:0000313|EMBL:EAY83821.1}; 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 {ECO:0000313|EMBL:EAY83821.1, ECO:0000313|Proteomes:UP000007015}; RN [1] {ECO:0000313|EMBL:EAY83821.1, ECO:0000313|Proteomes:UP000007015} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. 93-11 {ECO:0000313|Proteomes:UP000007015}; 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). CC ----------------------------------------------------------------------- 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; EAY83821.1; -; Genomic_DNA. DR ProteinModelPortal; A2ZMI7; -. DR STRING; 39946.BGIOSIBCE037264; -. DR EnsemblPlants; BGIOSGA037758-TA; BGIOSGA037758-PA; BGIOSGA037758. DR Gramene; A2ZMI7; -. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; SEWCKDG; -. DR Proteomes; UP000007015; Chromosome 12. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007015}; KW Reference proteome {ECO:0000313|Proteomes:UP000007015}. SQ SEQUENCE 342 AA; 36846 MW; DBDB39AD0D3652C5 CRC64; MVGKSGVAEE GGAAAAAAVR RWVEAGGGRL VMDGGLATEL EANGADLNDP LWSAKCLLSS PHLVRKVHLD YLEAGANIII TASYQATIQG FESKGFSKEQ SEDLLAKSVE IAREARDMFL KEHSDRPIQH PILVAASIGS YGAYLADGSE YSGDYGEAGT LEFLKDFHKR RLEVLAEAGP DLIAFETIPN KLEAQAYVEL LDECNISIPA WFSFNSKDGV HIVSGDSLIE CATIANGCSK VGAVGINCTP PRFIHGLILS IRKVTDKPML IYPNSGERYD AEKKEWVEST GVSDGDFVSY VNEWCKDGAV LIGGCCRTTP NTIKAISRSL NQRHSSLHLP VA // ID A3CMV4_STRSV Unreviewed; 315 AA. AC A3CMV4; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 27-MAY-2015, entry version 49. DE SubName: Full=Methyltransferase, putative {ECO:0000313|EMBL:ABN44509.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ABN44509.1}; GN Name=mmuM {ECO:0000313|EMBL:ABN44509.1}; GN OrderedLocusNames=SSA_1096 {ECO:0000313|EMBL:ABN44509.1}; OS Streptococcus sanguinis (strain SK36). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=388919 {ECO:0000313|EMBL:ABN44509.1, ECO:0000313|Proteomes:UP000002148}; RN [1] {ECO:0000313|EMBL:ABN44509.1, ECO:0000313|Proteomes:UP000002148} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SK36 {ECO:0000313|EMBL:ABN44509.1, RC ECO:0000313|Proteomes:UP000002148}; RX PubMed=17277061; DOI=10.1128/JB.01808-06; RA Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., RA Manque P., Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., RA Chaplin M.D., Akan D., Paik S., Peterson D.L., Macrina F.L., RA Buck G.A.; RT "Genome of the opportunistic pathogen Streptococcus sanguinis."; RL J. Bacteriol. 189:3166-3175(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; CP000387; ABN44509.1; -; Genomic_DNA. DR RefSeq; WP_011836916.1; NC_009009.1. DR RefSeq; YP_001035059.1; NC_009009.1. DR STRING; 388919.SSA_1096; -. DR EnsemblBacteria; ABN44509; ABN44509; SSA_1096. DR GeneID; 4806957; -. DR KEGG; ssa:SSA_1096; -. DR PATRIC; 19769164; VBIStrSan33173_1043. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; SSAN388919:GHEN-1081-MONOMER; -. DR Proteomes; UP000002148; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002148}; KW Methyltransferase {ECO:0000313|EMBL:ABN44509.1}; KW Transferase {ECO:0000313|EMBL:ABN44509.1}. SQ SEQUENCE 315 AA; 34853 MW; 03D3D1D0C22670A1 CRC64; MGKFKDLLDK QEIIILDGAL GTELESLGYD VSGKLWSAQY LLDQPQIIQN VHESYVRAGS DIITTSSYQA SIPAFVEAGL TPEKSYDLLK ETVFLARKAI ENTWQALSPE EKNQRPRLLV AGSVGPYAAY LADGSEYTGD YQLSEEEFQD FHRPRIQALL EAGSDLLAIE TIPNGAEAEA ILRLLAEEFP QAEAYLSFVA QSENAISDGT KIEELGNLAQ ESPQVLTVGF NCTAPHLIAP LLDGLRQVCN KPFLTYPNSG ETYNGLTKIW HNDPEQERSL LENSKLWQNQ GVRLFGGCCR TQPEDIAQLA RGLKD // ID A3D758_SHEB5 Unreviewed; 300 AA. AC A3D758; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 27-MAY-2015, entry version 44. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABN62571.1}; GN OrderedLocusNames=Sbal_3090 {ECO:0000313|EMBL:ABN62571.1}; OS Shewanella baltica (strain OS155 / ATCC BAA-1091). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=325240 {ECO:0000313|EMBL:ABN62571.1, ECO:0000313|Proteomes:UP000001557}; RN [1] {ECO:0000313|EMBL:ABN62571.1, ECO:0000313|Proteomes:UP000001557} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OS155 / ATCC BAA-1091 {ECO:0000313|Proteomes:UP000001557}; 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; ABN62571.1; -; Genomic_DNA. DR RefSeq; WP_011847414.1; NC_009052.1. DR RefSeq; YP_001051440.1; NC_009052.1. DR ProteinModelPortal; A3D758; -. DR STRING; 325240.Sbal_3090; -. DR EnsemblBacteria; ABN62571; ABN62571; Sbal_3090. DR KEGG; sbl:Sbal_3090; -. DR PATRIC; 37185339; VBISheBal55297_3453. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; PYVDVWL; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; SBAL325240:GCTA-3179-MONOMER; -. DR Proteomes; UP000001557; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001557}; KW Methyltransferase {ECO:0000313|EMBL:ABN62571.1}; KW Transferase {ECO:0000313|EMBL:ABN62571.1}. SQ SEQUENCE 300 AA; 32032 MW; A324F9DF1AF2B070 CRC64; MDKQQLWVLD GGMGRELARR GAPFRQPEWS ALALIEAPQT VTEVHQAYVA SGAKVITTNS YALVPFHIGD ERFAAEGEAL AALAGKLARD VADEHANAVR VAGSLPPLFG SYRADLFEAA RVSELALPLI RALSPSVDLW LAETMSLIAE PLAIKALLPE DGKPFWVSFT LEDETLGSEP TLRSGERVAD AIDALVAVGV DAILFNCCQP EVIEAALQVA SDRLSALGRA DIRLGAYANA FPPQPKEATA NDGLDEIRAD LGPLDYLGWA ERWRAAGASL IGGCCGIGPE HIQALSTRLR // ID A3D7Y2_SHEB5 Unreviewed; 1233 AA. AC A3D7Y2; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 27-MAY-2015, entry version 65. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABN62845.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABN62845.1}; GN OrderedLocusNames=Sbal_3368 {ECO:0000313|EMBL:ABN62845.1}; OS Shewanella baltica (strain OS155 / ATCC BAA-1091). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=325240 {ECO:0000313|EMBL:ABN62845.1, ECO:0000313|Proteomes:UP000001557}; RN [1] {ECO:0000313|EMBL:ABN62845.1, ECO:0000313|Proteomes:UP000001557} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OS155 / ATCC BAA-1091 {ECO:0000313|Proteomes:UP000001557}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000563; ABN62845.1; -; Genomic_DNA. DR RefSeq; WP_011847606.1; NC_009052.1. DR RefSeq; YP_001051714.1; NC_009052.1. DR ProteinModelPortal; A3D7Y2; -. DR SMR; A3D7Y2; 657-897. DR STRING; 325240.Sbal_3368; -. DR EnsemblBacteria; ABN62845; ABN62845; Sbal_3368. DR KEGG; sbl:Sbal_3368; -. DR PATRIC; 37185962; VBISheBal55297_3746. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SBAL325240:GCTA-3475-MONOMER; -. DR Proteomes; UP000001557; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001557}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABN62845.1}; KW Transferase {ECO:0000313|EMBL:ABN62845.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 763 763 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1233 AA; 136912 MW; 043421534CD184E3 CRC64; MADIRKQLAE RILILDGAMG TMIQDHKLEE EDYRGERFKD WHTDVKGNND LLVLSQPHII KKIHTDYLNA GADIIETNTF NATTIAMADY DMQSLSAEIN LAGARLAREA CDEVFAATGI PRYVAGVLGP TNRTCSISPD VNDPGYRNVS FDELVSAYRE STKALIEGGA DIIMVETIFD TLNAKAALFA IESVFDDLFG QHSKDRLPIM ISGTITDASG RTLTGQTTEA FYNSLRHIKP LSIGLNCALG PKELRPYVEE LSRIAECYVS AHPNAGLPNE FGGYDETPED MANVIEDWAR EGMLNIIGGC CGSTPEHIRV IREAVDRHNP RVLPNIPVAC RLAGLEPLTI DAQSLFVNVG ERTNVTGSAK FLKLIKDGKF EQALDVAREQ VESGAQIIDI NMDEGMLDGA EIMHKFLNLI ASEPDISRVP IMIDSSKWEV IEAGLKCIQG KGIVNSISLK EGEAKFIEQA TLVKRYGAAA IIMAFDEQGQ ADTKARKIEI CTRAYRVLVD KVGFPPEDII FDPNIFAIAT GIDEHDNYAV DFIDAIKAIK ATLPHAMISG GVSNVSFSFR GNNPVREAIH AVFLYHAIKV GMDMGIVNAG QLAIYDDIDP ELKVRVENVV LNLPCPVEGS SNTEQLLEIA EKFRGDGAQV GKKEDLEWRS WPVSQRLSHA LVKGITEFID EDTEAARQEA KRPLDVIEGA LMDGMNVVGD LFGSGKMFLP QVVKSARVMK KAVAYLNPYI ELEKVEGQSN GKILMVTVKG DVHDIGKNIV GVVLACNGFE VFDLGVMVSV ERILDAVKEH NIDIIGMSGL ITPSLDEMVH NVKTFHREGL TIPAIIGGAT CSKIHTAVKI APHYPHGAIY IADASRAVPM VSKLINNETR QATIDETYAE YDDMRTKRLS QAKRKEIVSL EAARENRCQH DWANYTPFTP NVLGRQVFNN YPLEDLVERI DWTPFFRSWE LHGHYPEILT DKVVGEEAQK LFADGQAMLK QIIEEKWLTA KAVIGLFPAN TVNYDDIELY TDESRTTVEM TTHHLRMQLE RVGNDNFCLS DFVAPKDSGV ADYMGGFAVT TGHGIDEHVA RFEANHDDYN AIMLKCLADR LAEAFAERMH ERVRKEFWGY AADEQLSNEA LIREKYKGIR PAPGYPACPD HTEKGLLWDL LKPDETIDLN ITESYAMFPT AAVSGWYFAH PKSRYFGVSN IGRDQVEDYA KRKGMTVAET EKWLAPVLDY DPE // ID A3DD51_CLOTH Unreviewed; 804 AA. AC A3DD51; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 27-MAY-2015, entry version 59. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABN51880.1}; GN OrderedLocusNames=Cthe_0645 {ECO:0000313|EMBL:ABN51880.1}; OS Clostridium thermocellum (strain ATCC 27405 / DSM 1237 / NBRC 103400 / OS NCIMB 10682 / NRRL B-4536 / VPI 7372) (Ruminiclostridium OS thermocellum). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminiclostridium. OX NCBI_TaxID=203119 {ECO:0000313|EMBL:ABN51880.1, ECO:0000313|Proteomes:UP000002145}; RN [1] {ECO:0000313|Proteomes:UP000002145} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 RC / VPI 7372 {ECO:0000313|Proteomes:UP000002145}; 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 ----------------------------------------------------------------------- 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; ABN51880.1; -; Genomic_DNA. DR RefSeq; WP_003516591.1; NC_009012.1. DR RefSeq; YP_001037073.1; NC_009012.1. DR ProteinModelPortal; A3DD51; -. DR STRING; 203119.Cthe_0645; -. DR EnsemblBacteria; ABN51880; ABN51880; Cthe_0645. DR KEGG; cth:Cthe_0645; -. DR PATRIC; 19514965; VBICloThe47081_0674. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CTHE203119:GIW8-666-MONOMER; -. DR Proteomes; UP000002145; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002145}; KW Methyltransferase {ECO:0000313|EMBL:ABN51880.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002145}; KW Transferase {ECO:0000313|EMBL:ABN51880.1}. SQ SEQUENCE 804 AA; 87325 MW; 08DB3DE1D405FBA6 CRC64; MNKKDFLDFL NQNILILDGA TGTELQKRGM PGGVCPEMWV IENPDVIMDI QKDYINAGSN AVYTCTFGGN RIKLSEFGLG DKVVEINKKL AQLSRKAAGE KGLVAGDLAP TGRFVRPFGD MPFEEAVDVY KEQVKGLLEG GVDFFVIETM MDIQEARAAL LAVKESCDLP VCVSMTFDES GRTLTGTDSV SALIILQSLG ADVVGCNCST GPQDMIKIIR EMKPYAKVPL LAKPNAGLPK LIDGKTRFDM EPEEFGSYIK EFVEAGVNLL GGCCGTSPVY IEQIRKNIEG LKPIPPQPKE ICAVASARKT VFVDANEPVV VVGERINPTG KKKLQEELRQ GMTSLVRQFA VEQVEKGADI LDVNVGMPGI DEKETMVKVV ELLSSITDAP LCLDSSSPEV LEAALRIYPG RALINSISAE KVKIEKLLPI AAKYGAAFIL LPLGDAGVPK SAGERCKIVE EVFNEASKWG YTKKDVIVDG LVMTVSADQE AAVETLKVIE WCTQSFGCGT IVGLSNVSFG MPERAWINSA FLAMAIGYGL TMAILNPSSD TLMSIKMASD VLKVKDRNSK KYIEHFAALK SDKPQVVEKK DTASPVEKVY DAVVKGDREN IRKYIDDALK DGTEPSIIVD KYLIPAITHV GDLYDRKEYF LPQLIQSAET MKEAFGILEP LLKKEPVDEK GNKVKVILAT VKGDIHDIGK NIVGLMLRNY GFEVYDLGKD VSAEEIVKKA KETNAPIIGL SALMTTTMLE MREVVSLVRQ EGLNAKIMIG GAVVNADYAK EIGADGYSED AYGAVKLASK LAGI // ID A3I2Z5_9BACT Unreviewed; 350 AA. AC A3I2Z5; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 38. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EAZ79194.1}; GN ORFNames=ALPR1_14024 {ECO:0000313|EMBL:EAZ79194.1}; OS Algoriphagus machipongonensis. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cyclobacteriaceae; OC Algoriphagus. OX NCBI_TaxID=388413 {ECO:0000313|EMBL:EAZ79194.1, ECO:0000313|Proteomes:UP000003919}; RN [1] {ECO:0000313|EMBL:EAZ79194.1, ECO:0000313|Proteomes:UP000003919} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PR1 {ECO:0000313|EMBL:EAZ79194.1}; 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. {ECO:0000313|EMBL:EAZ79194.1}. 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; AAXU02000001; EAZ79194.1; -; Genomic_DNA. DR RefSeq; WP_008201423.1; NZ_CM001023.1. DR ProteinModelPortal; A3I2Z5; -. DR EnsemblBacteria; EAZ79194; EAZ79194; ALPR1_14024. DR Proteomes; UP000003919; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000003919}; KW Reference proteome {ECO:0000313|Proteomes:UP000003919}. SQ SEQUENCE 350 AA; 38194 MW; 00DAA7E22ABEB31C CRC64; MQNRTELLLQ QIQKRILILD GAMGTMIQRY KLTEEDFRTP ELKNYAKDLK GNNDLLSLSK PEIIKAIHRE YLDAGSDIIE TNTFSATTIA QADYGLEHLA YAINFESAKL AREVAEEYSA NNPDKPRFVA GAIGPTNRTA SLSPDVNDPG YRAVTFDQLA EAYSEQVRGL LDGGSDILLV ETIFDTLNAK AALYAIQDVF EERNLPLDPR EGGIPIMVSG TITDASGRTL SGQTTEAFLI SISHVPLLSV GLNCALGAKE LRPYLKVLAQ KSPFYVSAYP NAGLPNEFGA YDQGADEMAG QVRDFLKEGM LNILGGCCGT TPEHIAALAN LSEGFAPRKL NQLEVEETLD // ID A3I968_9BACI Unreviewed; 304 AA. AC A3I968; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 35. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EAZ85750.1}; DE Flags: Fragment; GN ORFNames=BB14905_06954 {ECO:0000313|EMBL:EAZ85750.1}; OS Bacillus sp. B14905. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=388400 {ECO:0000313|EMBL:EAZ85750.1}; RN [1] {ECO:0000313|EMBL:EAZ85750.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=B14905 {ECO:0000313|EMBL:EAZ85750.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAZ85750.1}. 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; AAXV01000010; EAZ85750.1; -; Genomic_DNA. DR RefSeq; WP_008176888.1; NZ_AAXV01000010.1. DR EnsemblBacteria; EAZ85750; EAZ85750; BB14905_06954. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; FT NON_TER 304 304 {ECO:0000313|EMBL:EAZ85750.1}. SQ SEQUENCE 304 AA; 32784 MW; 50A36AE258C41598 CRC64; MAKHLIEEQL DKRILILDGA MGTMLQNENL SADDFGGEDL DGCNENLVLT RPDVIEKIHH KYLEAGADII CTNTFGGTPL VLNEYNLGAK AEEINKRAVE IARQAVDNYT TSDWPRFVAG AMGPTTKTLS VTGGITFDEL EENFFVQAKA LIEAGADVLL LETSQDMLNV KAGTLGVTRA FEVTGKELPV MISGTIEPMG TTLAGQTIDA FYISIEHIQP LSVGLNCATG PEFMTDHIRS LAELSTGYIS CYPNAGLPDE EGCYHESPES LSQKLKGFAE KGWLNIVGGC CGTTPAHIAA IREI // ID A3I969_9BACI Unreviewed; 615 AA. AC A3I969; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 07-JAN-2015, entry version 41. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=BB14905_06959 {ECO:0000313|EMBL:EAZ85751.1}; OS Bacillus sp. B14905. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=388400 {ECO:0000313|EMBL:EAZ85751.1}; RN [1] {ECO:0000313|EMBL:EAZ85751.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=B14905 {ECO:0000313|EMBL:EAZ85751.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAZ85751.1}. 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; AAXV01000010; EAZ85751.1; -; Genomic_DNA. DR RefSeq; WP_008176889.1; NZ_AAXV01000010.1. DR ProteinModelPortal; A3I969; -. DR EnsemblBacteria; EAZ85751; EAZ85751; BB14905_06959. DR PATRIC; 25221450; VBIBacSp135347_1936. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EAZ85751.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862, KW ECO:0000313|EMBL:EAZ85751.1}; KW Transferase {ECO:0000313|EMBL:EAZ85751.1}. SQ SEQUENCE 615 AA; 67453 MW; F21125C04D11BD74 CRC64; MGLLEKLKTH VLTADGAIGT VLYGYGLEYC HEEMNVQRPE LIEKIHREYI AAGADIIQTN TYGANAIKLA RYGLESSVQQ FNEAAITIAK RAAADGGQFV LGTIGGIRGI RKSDATLDDI LVTVEEQASV LLAGNPDGLL LETYYDFEEL TATLNMLRAK TNIPIIAQVS MHEPGVLQNG MSLNNALHEL EILGADIVGV NCRLGPYHTI QAFEAVELPA KAFMSAYPNA SLLDLEDGRV VYESEADYFG RAAVELRDQG VRLIGGCCGT TPKHIAAAKK YLEELSPVSE KHAKPEKIEI VRDAEPAKFE PLHEKVKRER SVIVELDTPR HLEIDGFLEG AKQLYEAGAD VVMMADNSLA SPRISNIAMG ALLKSTNGVR PLTHITCRDR NLIGLQSHLM GLNALGIHDV LAVTGDPTKV GDFPGATSVY DVSSMELIQL IKQLNEGVSF SGKPLRKKAN FSVAAAFNPN VRVLDRAVAR LEKKIEHGAD YFISQPVYTK EKIIEIYEAT KHLQAPIYIG IMPVTSYKSA EFLHHEVPGI KLSEDALSRM KACGEDKERA TLEGIAIAKE LVEVAAQYFH GIYLITPFLR YDVTLELMKY IEQLDEQKKG VSING // ID A3IWD3_9CHRO Unreviewed; 1193 AA. AC A3IWD3; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 50. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EAZ89246.1}; GN ORFNames=CY0110_06834 {ECO:0000313|EMBL:EAZ89246.1}; OS Cyanothece sp. CCY0110. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Cyanothece. OX NCBI_TaxID=391612 {ECO:0000313|EMBL:EAZ89246.1}; RN [1] {ECO:0000313|EMBL:EAZ89246.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCY0110 {ECO:0000313|EMBL:EAZ89246.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EAZ89246.1}. 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; AAXW01000050; EAZ89246.1; -; Genomic_DNA. DR RefSeq; WP_008277689.1; NZ_AAXW01000050.1. DR ProteinModelPortal; A3IWD3; -. DR EnsemblBacteria; EAZ89246; EAZ89246; CY0110_06834. DR PATRIC; 27731097; VBICyaSp137568_4428. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EAZ89246.1}; KW Transferase {ECO:0000313|EMBL:EAZ89246.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 228 228 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 739 739 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1193 AA; 133435 MW; C30DA55888CCE27B CRC64; MNSTFLNHLK SPKRPVLVFD GATGTSLQSQ NLTAEDFGGP EYEGCNEYLV HTKPEAVEKV HRGFLEVGAD VIETDTFGGT SIVLAEYDLA DKAYYLNKRA TEIAKKMAAE YSTPEKPRFV AGSMGPGTKL PTLGHIDFDT LRDAYVEQAE GLYDGGADLL IIETCQDVLQ IKAALNAVEA VFEKKGNRLP IMVSITMETM GTMLVGTEIS AALTILEPYK IDILGLNCAT GPEQMKEHIK YLSEHSPFIV SCIPNAGLPE NVGGQAHYRL TPVELKMALM HFIEDLGVQI IGGCCGTRPD HIKSLSELSQ ELKPKERHPE YEPSAASIYS TQPYIQDNSF LIVGERLNAS GSKKCRKLLD AEDWDSLVSL AKSQVKEGAH VLDVNVDYVG RDGVRDMHEL ASRLVNNITL PLMLDSTEWQ KMESGLKVAG GKCILNSTNY EDGEERFLKV LELAKKYGAG VVVGTIDEEG MGRTADKKFQ IAKRAYDAAI NYGIPAHEIF FDPLALPIST GIEEDRENGK ATVEAIKRIR EELPGCHILL GISNISFGLN PAARQVLNSV FLYETMQVGL DGAIVSASKI LPLAKIEEDH QKVCRDLIYD LREFDGDICT YDPLTKLTEL FAGKTTKKDP SKTANLPIEE RLKQHIIDGE RLGLEDALAE ALKQYPPLDI INVFLLDGMK IVGELFGSGQ MQLPFVLQSA QTMKAAVAYL EPFMDKEEGE ENDSGKGKFL IATVKGDVHD IGKNLVDIIL SNNGYKVINL GIKQPVENII KAYEEHQPDC IAMSGLLVKS TAFMKDNLEV FNERGIDVPV ILGGAALTPK FVYEDCQNTY KGKVVYGKDA FSDLHFMDQL MPAKSAENWD NLQGFLGEFI DNNSLFQEER GEKAAQKAIE KNGKSTTPEI PKVIDTKRSE AVEIMEPATP PFWGTKILKP NEFDLNEIFW YLDLQALIAG QWQFRKPKEQ SREEYEAFLA EKVYPILEEW KQRVVRENLL HPTVIYGYFP CQSQDNSLLV YHPETVKNAN NKIPEDVKPI WEIDFPRQKS GRRLCIADFF SPKESGKIDV FPMQAVTVGE IATEYAQKLF AANDYTNYLY YHGMAVQTAE ALAEWTHTKI RRELGFSDQE PDNIREMLQQ HYQGSRYSFG YPACPNIQDQ YKQLEVMGCD RINMYMDESE QIYPEQSTTA IITYHPVAKY FSA // ID A3J2B1_9FLAO Unreviewed; 330 AA. AC A3J2B1; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=Methionine synthase I, homocysteine S-methyltransferase {ECO:0000313|EMBL:EAZ96466.1}; GN ORFNames=FBBAL38_03565 {ECO:0000313|EMBL:EAZ96466.1}; OS Flavobacteria bacterium BAL38. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales. OX NCBI_TaxID=391598 {ECO:0000313|EMBL:EAZ96466.1}; RN [1] {ECO:0000313|EMBL:EAZ96466.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BAL38 {ECO:0000313|EMBL:EAZ96466.1}; 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 (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. {ECO:0000313|EMBL:EAZ96466.1}. 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; AAXX01000001; EAZ96466.1; -; Genomic_DNA. DR RefSeq; WP_008254731.1; NZ_AAXX01000001.1. DR ProteinModelPortal; A3J2B1; -. DR EnsemblBacteria; EAZ96466; EAZ96466; FBBAL38_03565. DR PATRIC; 27381136; VBIFlaBac114234_0688. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EAZ96466.1}; KW Transferase {ECO:0000313|EMBL:EAZ96466.1}. SQ SEQUENCE 330 AA; 36464 MW; 9B10DF6E763BD234 CRC64; MSKIQEEIKK RILVLDGAMG TMLQRYKFEE EDFRGERFKD FPHPLKGNND LLSITQPEAV KSVHRAYFEA GADIVETNTF SGTTIGMADY YLEDLVYELN FQSAKIAREV ADEFTDKSRF VAGSIGPTNR TASMSPDVND PGFRAVSFDD LKIAYKQQVE ALIDGGCDLL LVETIFDTLN AKAALFAIEE VKEERNIDIP VMVSGTITDA SGRTLSGQTV EAFLISISHI PLLSVGFNCA LGADQLKPYL KALGNNTLLN ISAHPNAGLP NAFGQYDQTP EEMQQLIREY LQENLVNIIG GCCGTTPDHI QLIAEVAKEF KPRTQQLKSV // ID A3JFK5_9ALTE Unreviewed; 303 AA. AC A3JFK5; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EAZ99145.1}; GN ORFNames=MELB17_06204 {ECO:0000313|EMBL:EAZ99145.1}; OS Marinobacter sp. ELB17. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Marinobacter. OX NCBI_TaxID=270374 {ECO:0000313|EMBL:EAZ99145.1}; RN [1] {ECO:0000313|EMBL:EAZ99145.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ELB17 {ECO:0000313|EMBL:EAZ99145.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAZ99145.1}. 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; AAXY01000010; EAZ99145.1; -; Genomic_DNA. DR RefSeq; WP_007350798.1; NZ_AAXY01000010.1. DR ProteinModelPortal; A3JFK5; -. DR EnsemblBacteria; EAZ99145; EAZ99145; MELB17_06204. DR PATRIC; 31003324; VBIMarSp19762_2719. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 200 200 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 271 271 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 272 272 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 303 AA; 32224 MW; 90ABB6CFF163C383 CRC64; MRPVVLLDGG LGQEIYRRAA NVSSALWSVA VMHEQPDVVT AVHSDFIRAG AKTLSLNTYA ATPSRLLRHG QLEQLAAIHQ NAFELLGQAV KATGACVDIA GCLPPLAGSY QGQPARSFED LRDEYSVLVK QQAVADVLLI ETMTNTLEAC AACAAASELG KPYGVAFRLE ADGKLMSGET LAEAVAAVSP YSPTAVMLNC CDPELISAAM PELVRLHPCV GGYANAFKSV EALAQGGSVD ALEARADISP QAYVAHVRQW LDDGATVIGG CCEITPEHVR HIVETLADDY EFIRFSQRSV PNS // ID A3JG88_9ALTE Unreviewed; 1232 AA. AC A3JG88; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 48. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EAZ98734.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EAZ98734.1}; GN Name=metH {ECO:0000313|EMBL:EAZ98734.1}; GN ORFNames=MELB17_13841 {ECO:0000313|EMBL:EAZ98734.1}; OS Marinobacter sp. ELB17. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Marinobacter. OX NCBI_TaxID=270374 {ECO:0000313|EMBL:EAZ98734.1}; RN [1] {ECO:0000313|EMBL:EAZ98734.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ELB17 {ECO:0000313|EMBL:EAZ98734.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EAZ98734.1}. 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; AAXY01000013; EAZ98734.1; -; Genomic_DNA. DR RefSeq; WP_007351031.1; NZ_AAXY01000013.1. DR ProteinModelPortal; A3JG88; -. DR EnsemblBacteria; EAZ98734; EAZ98734; MELB17_13841. DR PATRIC; 31003793; VBIMarSp19762_2951. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EAZ98734.1}; KW Transferase {ECO:0000313|EMBL:EAZ98734.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1232 AA; 136586 MW; 9D4D88484983AAED CRC64; MTDRTTRLKQ LHQALKERIV ILDGGMGTMI QQLKLDESAF RGERFANYAS DLQGNNDLLN LTQPALMRNI HADYMDAGAD IIETNTFNSS RLSQADYGLE DIAKELNVAA ARMAREIADE FTAKNPAKPR FVAGAVGPTS RTASLSPDVN NPGYRNVDFQ ALVDNYYEAV EGLVEGGCDL ILIETIFDTL NAKAAIYATQ QYFEDSGIEL PIMISGTITD ASGRTLSGQT TEAFWNSIAH AKPISVGLNC ALGADALRPY IEELSAKADT YVSAHPNAGL PNEFGEYDQT PEEMAEIIEG FARDGFLNII GGCCGSRPDH IEAIANAVAK YPPRKIAQPK PALRLSGLEP FTGDEHTLFI NVGERTNVTG SKRFLRLIKE ERYEEALSVA RDQVENGAQI IDINMDEGLL DSKEVMVTFL NLVASEPDIC RVPIMIDSSK WEVIEAGLRC IQGKAVVNSI SLKEGEEEFF KRARDCMRYG AAVVVMAFDE KGQADTFKRK TEICKRSYDA LMSIGFKPGD IIFDPNIFAI ATGIEEHNNY AVDFINGCRW IRANLPHASI SGGVSNVSFS FRGNDVVRET IHSVFLYHAI KAGLNMGIVN PGQLVIYDDI EAELKEAVED VVLNRREDST DRLLELAERF KGQGVKTPEE DLAWRDLPVK KRLEHALVKG ITSHIIEDTE ACRQEADRPI HVIEGPLMDG MNVVGDLFGD GKMFLPQVVK SARVMKQAVA HLIPFIEAEK SGGQQAKGKI LMATVKGDVH DIGKNIVGVV LQCNNYEVID MGVMVPCDKI LAAAKEHNVD IIGLSGLITP SLDEMVHVAR EMQRLDFHLP LMIGGATTSK AHTAVKIEPH YKNDIALYVS DASRCVNVAS KLLSKTAKPD LVKAARAEYD EIRERRKNRS ERTKLVSLKE ARDRAPEIDF DNYVPPKPAF LGARLFEEYD LNELVPYIDW TPFFISWDIA GKYPQIFDDP KRGEVAKTLF DEAQVILRKM IDEKRVTACG IAGFWPANRR GDDVVVYTDE SRTEELAVLH HLRQQDEKAP GKPMMALSDF VAAKGYEHPD YVGGFAVTTG IGAEEMSNEY RDANDDYNAI MVKALADRLA EAFAERLHER VRTEFWGYAS DESMDTAALI KERYQGIRPA PGYPACPDHI EKATLFTLLD ATAKTGITLT EHFAMFPAAA VSGWYFSHPQ SKYFAVGRIG VDQVEDYADR TGQTKAEAER WLQPSLAYDP AE // ID A3JP99_9RHOB Unreviewed; 337 AA. AC A3JP99; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 34. DE SubName: Full=Methionine synthase I {ECO:0000313|EMBL:EBA03589.1}; GN ORFNames=RB2150_03798 {ECO:0000313|EMBL:EBA03589.1}; OS Rhodobacteraceae bacterium HTCC2150. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae. OX NCBI_TaxID=388401 {ECO:0000313|EMBL:EBA03589.1}; RN [1] {ECO:0000313|EMBL:EBA03589.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2150 {ECO:0000313|EMBL:EBA03589.1}; 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] {ECO:0000313|EMBL:EBA03589.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2150 {ECO:0000313|EMBL:EBA03589.1}; 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. {ECO:0000313|EMBL:EBA03589.1}. 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; AAXZ01000002; EBA03589.1; -; Genomic_DNA. DR RefSeq; WP_008183637.1; NZ_AAXZ01000002.1. DR ProteinModelPortal; A3JP99; -. DR EnsemblBacteria; EBA03589; EBA03589; RB2150_03798. DR PATRIC; 28462842; VBIRhoBac104552_0988. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 337 AA; 35393 MW; 403D14357CDB1974 CRC64; MSNLLEKLLV ERDWLLADGA TGTNLFNMGL TAGDAPELWN DTAPEKIRKL YSGAVDSGSD IFLTNTFGGN ASRMKLHDAQ SRVFELNKKG AEIGREIADA SGRQVVVAGS VGPTGDIMAP MGSLTFDSAV EMFHEQAEGL KAGGADVAWV ETISAPEEFQ AAARAFELAE LPWAGTMSFD TAGRTMMGMT SRDMVAMVEK LPNAPLAFGA NCGVGASDLL RTVLGFAAST PQLPVIAKGN AGIPKYVDGH IHYDGTPELM GQYAVLARNC GAKIIGGCCG TMPEHLVAMR AALENTPKSA APSLDEITAV LGGFSSASDG LGDNEPAPTR RNRRKRA // ID A3JQP4_9RHOB Unreviewed; 308 AA. AC A3JQP4; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EBA04084.1}; GN ORFNames=RB2150_06273 {ECO:0000313|EMBL:EBA04084.1}; OS Rhodobacteraceae bacterium HTCC2150. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae. OX NCBI_TaxID=388401 {ECO:0000313|EMBL:EBA04084.1}; RN [1] {ECO:0000313|EMBL:EBA04084.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2150 {ECO:0000313|EMBL:EBA04084.1}; 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] {ECO:0000313|EMBL:EBA04084.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2150 {ECO:0000313|EMBL:EBA04084.1}; 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. {ECO:0000313|EMBL:EBA04084.1}. 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; AAXZ01000002; EBA04084.1; -; Genomic_DNA. DR RefSeq; WP_008184418.1; NZ_AAXZ01000002.1. DR ProteinModelPortal; A3JQP4; -. DR EnsemblBacteria; EBA04084; EBA04084; RB2150_06273. DR PATRIC; 28463833; VBIRhoBac104552_1478. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EBA04084.1}; KW Transferase {ECO:0000313|EMBL:EBA04084.1}. SQ SEQUENCE 308 AA; 34057 MW; B20A1AE8976359DF CRC64; MDMIKRQLPH QTDNVFLAYV GMETDIIFNM GIDLPGFAAY PLLENQEGRE IIKKYHRDFI KLAQSKNLGA ILETPTWVAN RSRAESLGYT PDQLRLINAD AVQVLSEVRA EFESSTIILS ANLGPRDDAY APSEQMSTDE AKTYHMEQLA IFVDGEVDLV SGYTIAYTAE ATGMVLAAKA LDLPIIISFT IETDGRLPTG ATLEEAISEV DEATDGYADY FMINCAHPDH FTSILKSAPW MSRIKGVVAN ASRCSHAELD NAEDLDAGDP VEFGQQLREI RRNFPQINIL GGCCGTDMRH MQSIADNL // ID A3JRH5_9RHOB Unreviewed; 292 AA. AC A3JRH5; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EBA04365.1}; GN ORFNames=RB2150_07678 {ECO:0000313|EMBL:EBA04365.1}; OS Rhodobacteraceae bacterium HTCC2150. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae. OX NCBI_TaxID=388401 {ECO:0000313|EMBL:EBA04365.1}; RN [1] {ECO:0000313|EMBL:EBA04365.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2150 {ECO:0000313|EMBL:EBA04365.1}; 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] {ECO:0000313|EMBL:EBA04365.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2150 {ECO:0000313|EMBL:EBA04365.1}; 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. {ECO:0000313|EMBL:EBA04365.1}. 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; AAXZ01000002; EBA04365.1; -; Genomic_DNA. DR RefSeq; WP_008184838.1; NZ_AAXZ01000002.1. DR ProteinModelPortal; A3JRH5; -. DR EnsemblBacteria; EBA04365; EBA04365; RB2150_07678. DR PATRIC; 28464389; VBIRhoBac104552_1753. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EBA04365.1}; KW Transferase {ECO:0000313|EMBL:EBA04365.1}. SQ SEQUENCE 292 AA; 30643 MW; 6BE59EAC98CCA2BF CRC64; MSITLLDGGM GQELISRAGK ATGLWSVQAL LDAPEIIRNV HDDYFAAGAE VATTNSYSVL PDRLIAHGIG DRLEELARLA CQIAVDARDA NGSGIVLGSL GPQGFSYQPD LSPPADEAAE AYASLARIHA EYVDAHICET MSSVDQARGG LMGAGVTGKP VWLALSVNDE DGTKLRSGED LTDVLPLLEQ YQPAGVLLNC SIPEAITQGL SVLAKQSIPF GGYANGFTKI VSDFSKIGAT VDMLTARQDL GPDAYADFAA KWIAEGATLI GGCCEVGPAH IVELHKRFKG AE // ID A3JU33_9RHOB Unreviewed; 314 AA. AC A3JU33; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EBA02749.1}; GN ORFNames=RB2150_17882 {ECO:0000313|EMBL:EBA02749.1}; OS Rhodobacteraceae bacterium HTCC2150. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae. OX NCBI_TaxID=388401 {ECO:0000313|EMBL:EBA02749.1}; RN [1] {ECO:0000313|EMBL:EBA02749.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2150 {ECO:0000313|EMBL:EBA02749.1}; 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] {ECO:0000313|EMBL:EBA02749.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2150 {ECO:0000313|EMBL:EBA02749.1}; 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. {ECO:0000313|EMBL:EBA02749.1}. 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; AAXZ01000006; EBA02749.1; -; Genomic_DNA. DR RefSeq; WP_008186546.1; NZ_AAXZ01000006.1. DR ProteinModelPortal; A3JU33; -. DR EnsemblBacteria; EBA02749; EBA02749; RB2150_17882. DR PATRIC; 28466200; VBIRhoBac104552_2643. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EBA02749.1}; KW Transferase {ECO:0000313|EMBL:EBA02749.1}. SQ SEQUENCE 314 AA; 34088 MW; FD39F0ABC9D98E3D CRC64; MTQSSPQLPH QTKEIFLTDG GTETWLMYKR GFELPEFSAF HLLNNQQSTA ALKEYYTAFA DVAMQLGTPF IFDSLTYRAS RDWGALLGYS SEGLADMNHK CFDLYRECAT KASLTAQNTI ISGCIGPKGD AYQTNKTLNA QSAEAYHAEQ IETFKNAGVD IITALTLNTT DEAIGIARAS AKAGIPSVIA FTIEKNRKLR SGETLKQAIE AVDAATADAP AYYMINCSHP VDFGPALTSE PWANRIRGLR ANASSLDHGT LCQLGHLEEG DPDELAQQYV DIRSSHPKMN VFGGCCGTDY AHVEKIGQAL LAAG // ID A3K3T6_9RHOB Unreviewed; 296 AA. AC A3K3T6; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EBA08200.1}; GN ORFNames=SSE37_11669 {ECO:0000313|EMBL:EBA08200.1}; OS Sagittula stellata E-37. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Sagittula. OX NCBI_TaxID=388399 {ECO:0000313|EMBL:EBA08200.1}; RN [1] {ECO:0000313|EMBL:EBA08200.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=E-37 {ECO:0000313|EMBL:EBA08200.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EBA08200.1}. 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; AAYA01000006; EBA08200.1; -; Genomic_DNA. DR RefSeq; WP_005859086.1; NZ_AAYA01000006.1. DR ProteinModelPortal; A3K3T6; -. DR EnsemblBacteria; EBA08200; EBA08200; SSE37_11669. DR PATRIC; 29860320; VBISagSte54459_2450. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EBA08200.1}; KW Transferase {ECO:0000313|EMBL:EBA08200.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 200 200 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 273 273 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 274 274 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 296 AA; 31441 MW; 0DA084DA916CB97C CRC64; MKVTLLDGGM GQELIHRAGD RPTPLWSTQV MIDRPGLVQE IHADYFAAGA TVATANSYAV LRDRLIPAGI KDRYEELVEA AMAEATQARD AFGGGKIAGS TAPLGATYRT DKHPDLHEAI PLYAEKARLM APRADLILIE TAASLLTCRA ALEGVLQAGR PVWLSISVDD EDGSRLRSGE KVADVLPIAR DGAAAVLINC SAPEAMPAAL DILARVDLPI GAYANAFTRI TKDFLKDQPT VDSLEARRDM GPETYAGHAM SWLDHGATIL GGCCETGPAH IAEIASRLRA AGHEIA // ID A3K6H6_9RHOB Unreviewed; 363 AA. AC A3K6H6; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=Methionine synthase I {ECO:0000313|EMBL:EBA07326.1}; GN ORFNames=SSE37_06804 {ECO:0000313|EMBL:EBA07326.1}; OS Sagittula stellata E-37. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Sagittula. OX NCBI_TaxID=388399 {ECO:0000313|EMBL:EBA07326.1}; RN [1] {ECO:0000313|EMBL:EBA07326.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=E-37 {ECO:0000313|EMBL:EBA07326.1}; 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. {ECO:0000313|EMBL:EBA07326.1}. 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; AAYA01000010; EBA07326.1; -; Genomic_DNA. DR RefSeq; WP_005860955.1; NZ_AAYA01000010.1. DR ProteinModelPortal; A3K6H6; -. DR EnsemblBacteria; EBA07326; EBA07326; SSE37_06804. DR PATRIC; 29862271; VBISagSte54459_3416. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 363 AA; 38444 MW; F44D8C36637C0817 CRC64; MMQIMSLRHG YNYETRDAIS EGDDRMSDAL TKALAERDWL LADGATGTNL FNMGLMSGDA PEFWNETEQD KIRALYKGSV DAGSDLFLTN SFGANASRLK LHDAAHRAYE LSKRAAELGR EVADAAGRQI IVAGSVGPTG EIMGAAGNLS HERAVEMFEE TARGLMDGGA DVLWVETISA PEEFRAAAAA FDNIGAPWCG TMSFDTAGRT MMGVTSQDMV ALVDSLPNPP IAFGANCGVG ASDLMRTVLG FAATGTDRPI IAKGNAGIPK YVDGHIHYDG TPELMADYAC LARDAGARII GGCCGTMSVH LAAMRAALET RAPQPRPTLE VIAEKLGGFS SASDGTGEDE GAGRERRGRR RRG // ID A3LQC9_PICST Unreviewed; 337 AA. AC A3LQC9; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 2. DT 01-APR-2015, entry version 43. DE SubName: Full=AdoMet-homocysteine methyltransferase {ECO:0000313|EMBL:ABN65186.2}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ABN65186.2}; GN Name=SAM4 {ECO:0000313|EMBL:ABN65186.2}; GN ORFNames=PICST_30270 {ECO:0000313|EMBL:ABN65186.2}; 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 {ECO:0000313|EMBL:ABN65186.2, ECO:0000313|Proteomes:UP000002258}; RN [1] {ECO:0000313|EMBL:ABN65186.2, ECO:0000313|Proteomes:UP000002258} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545 RC {ECO:0000313|Proteomes:UP000002258}; 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; CP000496; ABN65186.2; -; Genomic_DNA. DR RefSeq; XP_001383215.2; XM_001383178.1. DR STRING; 4924.PICST_30270; -. DR GeneID; 4837518; -. DR KEGG; pic:PICST_30270; -. DR InParanoid; A3LQC9; -. DR KO; K00547; -. DR OMA; WESAINI; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000002258; Chromosome 2. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002258}; KW Methyltransferase {ECO:0000313|EMBL:ABN65186.2}; KW Reference proteome {ECO:0000313|Proteomes:UP000002258}; KW Transferase {ECO:0000313|EMBL:ABN65186.2}. SQ SEQUENCE 337 AA; 38610 MW; 98894FBDCF017C41 CRC64; MLSLKEALSK NRLVLDGAMG TELEACIPKD SKIQPRKHPL WSGLVLLNEP NLIKNVHYNY LEQADVDALI SSTYQISYPS LKEHTDLDDE QIRGIWKKSI DVVEDAILQY RSKNSNSKKK IYIIGSIGPY ATYLADGSEY TGDYKNASDS DIESYHQPLL EYFLGDDRVD TIGFETIPSF QEVKVVLKLL SHLFAEQEKR KYYYISFNFD EATITDGTPT EVVISYIDSF LDKYPFLRKY MVGLGLNCID YHKIGSIVAK INDSQTSAQK PLFPLIVYPN FTIKYVPEED DYRAYKDIEK WKELVSEWVT IPNVRMIGGC CSTSPKEIKE VRRIIGT // ID A3M360_ACIBT Unreviewed; 292 AA. AC A3M360; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 2. DT 27-MAY-2015, entry version 41. DE SubName: Full=Putative homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:ABO11354.2}; GN OrderedLocusNames=A1S_0922 {ECO:0000313|EMBL:ABO11354.2}; OS Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / OS NCDC KC755 / 5377). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=400667 {ECO:0000313|EMBL:ABO11354.2, ECO:0000313|Proteomes:UP000006737}; RN [1] {ECO:0000313|EMBL:ABO11354.2, ECO:0000313|Proteomes:UP000006737} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377 RC {ECO:0000313|Proteomes:UP000006737}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; ABO11354.2; -; Genomic_DNA. DR STRING; 400667.A1S_0922; -. DR EnsemblBacteria; ABO11354; ABO11354; A1S_0922. DR PATRIC; 20718041; VBIAciBau103176_0935. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; ABAU400667:GI0Q-910-MONOMER; -. DR Proteomes; UP000006737; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006737}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ABO11354.2}; KW Transferase {ECO:0000313|EMBL:ABO11354.2}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 202 202 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 275 275 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 276 276 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 292 AA; 32078 MW; EB1EA2EE4F96D60A CRC64; MKILDGGLGR ELARRGAPFR QPEWSALALI EAPETVKEVH LDFINAGAEV ITTNNYAVVP FHIGQERFET DGVRLIKVAI EQAKNAVKES GKNVKIAGCL PPLFGSYRAD LFQPEQAKNL AEPIINTLAP EVDFWLAETQ SCLKEVETVH ALLPQDGKDY WVSFTLQDEI KQEQALLRSG ENMQQVADFI KQSNAKAVLF NCCQPEVILQ AINEIKGLIP ESVQIGAYAN AFPPQDESAT ANDGLDEIRK DLDAPAYLAF AKQWQQAGAS LVGGCCGIGP EHIAELSQFF KE // ID A3M3A9_ACIBT Unreviewed; 1228 AA. AC A3M3A9; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 2. DT 29-APR-2015, entry version 66. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABO11403.2}; GN OrderedLocusNames=A1S_0971 {ECO:0000313|EMBL:ABO11403.2}; OS Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / OS NCDC KC755 / 5377). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=400667 {ECO:0000313|EMBL:ABO11403.2, ECO:0000313|Proteomes:UP000006737}; RN [1] {ECO:0000313|EMBL:ABO11403.2, ECO:0000313|Proteomes:UP000006737} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377 RC {ECO:0000313|Proteomes:UP000006737}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000521; ABO11403.2; -; Genomic_DNA. DR STRING; 400667.A1S_0971; -. DR EnsemblBacteria; ABO11403; ABO11403; A1S_0971. DR PATRIC; 20718144; VBIAciBau103176_0986. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; ABAU400667:GI0Q-959-MONOMER; -. DR Proteomes; UP000006737; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006737}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1228 AA; 135789 MW; C2C77AD11982DA91 CRC64; MSTLATLKAL LAKRILIIDG AMGTMIQRHK LEEADYRGER FADWAHDLKG NNDLLVLTQP QIIQGIHEAY LDAGADIIET NSFNGTRVSM SDYHMEDLVP EINREAARLA KAACEKYSTP DKPRFVAGVL GPTSRTCSIS PDVNNPAFRN ISFDELKENY IEATHALIEG GADIILIETV FDTLNCKAAI FAVKEVFKQI GRELPIMISG TITDASGRTL TGQTAEAFWN SVRHGDLLSI GFNCALGADA MRPHVKTISD VADTFVSAHP NAGLPNAFGE YDETPEQTAA FLKEFAESGL INITGGCCGT TPDHIRAIAN AVKDIAPRQV PETVPACRLS GLEPFNIYDD SLFVNVGERT NVTGSKKFLR LIREENFAEA LEVAQQQVEA GAQIIDINMD EGMLDSQNAM VHFLNLVASE PDISRVPIMI DSSKWEIIEA GLKCVQGKPV VNSISLKEGY DEFVEKARLC RQYGAAIIVM AFDEVGQADT AERKREICKR SYDILVNEVG FPAEDIIFDP NVFAVATGIE EHNNYAVDFI EATGWIKQNL PHAMISGGVS NVSFSFRGNE PVREAIHSVF LYHAIKQGMT MGIVNAGQMA IYDDIPTELK EAVEDVILNQ NQGESGQAAT EKLLEVAEKY RGQGGATKEA ENLEWRNESV EKRLEYALVK GITTYIDQDT EEARLKSKRP LDVIEGPLMD GMNVVGDLFG SGKMFLPQVV KSARVMKQAV AWLNPYIEAE KTEGQSKGKV LMATVKGDVH DIGKNIVGVV LGCNGYDIVD LGVMVPCEKI LQTAIDEKCD IIGLSGLITP SLDEMVFVAK EMQRKGFNIP LLIGGATTSK AHTAVKIDPQ YQNDAVIYVA DASRAVGVAT TLLSKEMRGA FIEEHRAEYA KIRERLANKQ PKAAKLTYKE SVENGFKIDE SYVPPKPNLL GTQVLKNYPL ATLVDYFDWT PFFISWSLTG KFPKILEDEV VGEAATDLYN QAQAMLKDII DNNRFDARAV FGMFPAQRTD ADTVSVFDEA GQNVTHTFEH LRQQSDKVTG KPNLSLADYI RADREQQDYL GGFTVSIFGA EELANEYKAK GDDYSAILVQ SLADRFAEAF AEHLHERIRK EFWGYKADEQ LSNEELIKEK YVGIRPAPGY PACPEHSEKA VLFDWLGSTD KIGTKLTEHF AMMPPSSVSG FYYSHPQSEY FNVGKISQDQ LEDYAKRKGW TLDEAKRWLA PNLDDSIA // ID A3N187_ACTP2 Unreviewed; 297 AA. AC A3N187; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 46. DE SubName: Full=Homocysteine/selenocysteine methylase {ECO:0000313|EMBL:ABN74173.1}; GN OrderedLocusNames=APL_1081 {ECO:0000313|EMBL:ABN74173.1}; OS Actinobacillus pleuropneumoniae serotype 5b (strain L20). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=416269 {ECO:0000313|EMBL:ABN74173.1, ECO:0000313|Proteomes:UP000001432}; RN [1] {ECO:0000313|EMBL:ABN74173.1, ECO:0000313|Proteomes:UP000001432} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=L20 {ECO:0000313|EMBL:ABN74173.1, RC ECO:0000313|Proteomes:UP000001432}; 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.E.; 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; ABN74173.1; -; Genomic_DNA. DR RefSeq; WP_009875349.1; NC_009053.1. DR RefSeq; YP_001053778.1; NC_009053.1. DR ProteinModelPortal; A3N187; -. DR STRING; 416269.APL_1081; -. DR EnsemblBacteria; ABN74173; ABN74173; APL_1081. DR GeneID; 4849266; -. DR KEGG; apl:APL_1081; -. DR PATRIC; 20747074; VBIActPle94089_1129. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; PYVDVWL; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; APLE416269:GHV7-1094-MONOMER; -. DR Proteomes; UP000001432; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001432}; KW Methyltransferase {ECO:0000313|EMBL:ABN74173.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001432}; KW Transferase {ECO:0000313|EMBL:ABN74173.1}. SQ SEQUENCE 297 AA; 32264 MW; EEC46D6FC0882E41 CRC64; MTITILDGGM SRELMRLNAP FKQPEWSALS LYEKPSAVQQ VHEDFIANGA EVITTNSYAV VPFHIGEQRF SADGKMLADL AGRLAKQAVK NSGKSAKIAG SLPPMFGSYR ADLIQADRFA EIAQPIIDGL APYVDIWLCE TQSAIIEPTS IKPLLPKDDR PLWVSFTLTD DEPTPEPQLR SGEPVALAIE KMVELGVDAI LFNCCQPEVI EQALAITQSI LKAKNATHIQ TGAYANAFAP QPKDATANDG LDEVRKDLDP EAYLAWAQKW TAQGATIVGG CCGIGIEYIN TLAKHLK // ID A3N546_BURP6 Unreviewed; 359 AA. AC A3N546; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 47. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABN83023.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABN83023.1}; GN Name=metH {ECO:0000313|EMBL:ABN83023.1}; GN OrderedLocusNames=BURPS668_0414 {ECO:0000313|EMBL:ABN83023.1}; OS Burkholderia pseudomallei (strain 668). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=320373 {ECO:0000313|EMBL:ABN83023.1, ECO:0000313|Proteomes:UP000002153}; RN [1] {ECO:0000313|EMBL:ABN83023.1, ECO:0000313|Proteomes:UP000002153} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=668 {ECO:0000313|EMBL:ABN83023.1, RC ECO:0000313|Proteomes:UP000002153}; 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; ABN83023.1; -; Genomic_DNA. DR RefSeq; WP_004204527.1; NC_009074.1. DR RefSeq; YP_001057467.1; NC_009074.1. DR ProteinModelPortal; A3N546; -. DR STRING; 320373.BURPS668_0414; -. DR EnsemblBacteria; ABN83023; ABN83023; BURPS668_0414. DR KEGG; bpd:BURPS668_0414; -. DR PATRIC; 19246831; VBIBurPse82117_0391. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; BPSE320373:GJ9C-413-MONOMER; -. DR Proteomes; UP000002153; Chromosome I. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002153}; KW Methyltransferase {ECO:0000313|EMBL:ABN83023.1}; KW Transferase {ECO:0000313|EMBL:ABN83023.1}. SQ SEQUENCE 359 AA; 38459 MW; 1013B7D60E53B797 CRC64; MSEPTPIAPF ASSAAPAAPY TRGAALPQLL RQRILILDGA MGTMIQRYKL DEAAYRGERF KDFPRDVKGN NELLSITQPR IIREIHDQYF AAGADIVETN TFGATAVAQA DYGMEALVVE MNVASAALAR ESAAKYATPE KPRFVAGAIG PTPKTASISP DVNDPGARNV TFDELRDAYY QQAKALLDGG VDLFLVETIF DTLNAKAALF ALDQLFDDTG ERLPIMISGT VTDASGRILS GQTVEAFWNS LRHAKPLTFG LNCALGAALM RPYIAELAKL CDTYVSCYPN AGLPNPMSDT GFDETPDVTS GLLKEFAQAG LVNLAGGCCG TTPEHIAAIA KALAEVKPRR WPSQYSEAA // ID A3NQU6_BURP0 Unreviewed; 359 AA. AC A3NQU6; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 47. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase domain protein {ECO:0000313|EMBL:ABN91314.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABN91314.1}; GN Name=metH {ECO:0000313|EMBL:ABN91314.1}; GN OrderedLocusNames=BURPS1106A_0434 {ECO:0000313|EMBL:ABN91314.1}; OS Burkholderia pseudomallei (strain 1106a). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=357348 {ECO:0000313|EMBL:ABN91314.1, ECO:0000313|Proteomes:UP000006738}; RN [1] {ECO:0000313|EMBL:ABN91314.1, ECO:0000313|Proteomes:UP000006738} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1106a {ECO:0000313|EMBL:ABN91314.1, RC ECO:0000313|Proteomes:UP000006738}; 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; ABN91314.1; -; Genomic_DNA. DR RefSeq; WP_004204527.1; NC_009076.1. DR RefSeq; YP_001064717.1; NC_009076.1. DR ProteinModelPortal; A3NQU6; -. DR STRING; 357348.BURPS1106A_0434; -. DR EnsemblBacteria; ABN91314; ABN91314; BURPS1106A_0434. DR KEGG; bpl:BURPS1106A_0434; -. DR PATRIC; 19219446; VBIBurPse14980_0409. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; BPSE357348:GHVF-433-MONOMER; -. DR Proteomes; UP000006738; Chromosome I. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006738}; KW Methyltransferase {ECO:0000313|EMBL:ABN91314.1}; KW Transferase {ECO:0000313|EMBL:ABN91314.1}. SQ SEQUENCE 359 AA; 38459 MW; 1013B7D60E53B797 CRC64; MSEPTPIAPF ASSAAPAAPY TRGAALPQLL RQRILILDGA MGTMIQRYKL DEAAYRGERF KDFPRDVKGN NELLSITQPR IIREIHDQYF AAGADIVETN TFGATAVAQA DYGMEALVVE MNVASAALAR ESAAKYATPE KPRFVAGAIG PTPKTASISP DVNDPGARNV TFDELRDAYY QQAKALLDGG VDLFLVETIF DTLNAKAALF ALDQLFDDTG ERLPIMISGT VTDASGRILS GQTVEAFWNS LRHAKPLTFG LNCALGAALM RPYIAELAKL CDTYVSCYPN AGLPNPMSDT GFDETPDVTS GLLKEFAQAG LVNLAGGCCG TTPEHIAAIA KALAEVKPRR WPSQYSEAA // ID A3PCY0_PROM0 Unreviewed; 1188 AA. AC A3PCY0; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 66. DE SubName: Full=Putative methionine synthase {ECO:0000313|EMBL:ABO17605.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABO17605.1}; GN Name=metH {ECO:0000313|EMBL:ABO17605.1}; GN OrderedLocusNames=P9301_09821 {ECO:0000313|EMBL:ABO17605.1}; OS Prochlorococcus marinus (strain MIT 9301). OC Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae; OC Prochlorococcus. OX NCBI_TaxID=167546 {ECO:0000313|EMBL:ABO17605.1, ECO:0000313|Proteomes:UP000001430}; RN [1] {ECO:0000313|EMBL:ABO17605.1, ECO:0000313|Proteomes:UP000001430} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MIT 9301 {ECO:0000313|EMBL:ABO17605.1, RC ECO:0000313|Proteomes:UP000001430}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000576; ABO17605.1; -; Genomic_DNA. DR RefSeq; WP_011862952.1; NC_009091.1. DR RefSeq; YP_001091206.1; NC_009091.1. DR ProteinModelPortal; A3PCY0; -. DR STRING; 167546.P9301_09821; -. DR EnsemblBacteria; ABO17605; ABO17605; P9301_09821. DR GeneID; 4911448; -. DR KEGG; pmg:P9301_09821; -. DR PATRIC; 22995539; VBIProMar103344_0955. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PMAR167546:GH1Y-1008-MONOMER; -. DR Proteomes; UP000001430; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001430}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABO17605.1}; KW Transferase {ECO:0000313|EMBL:ABO17605.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 746 746 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1188 AA; 132406 MW; 3F9C10E3AEFEB9D0 CRC64; MESFRTYLNR DEKPLIIFDG GTGTSFQNLN LTADDFGGKE LEGCNENLVL SSPKIVEKVH NSFLEAGCHV IETNTFGASS IVLDEYDIKN KAYEINKNAA LIAKKAAAKY TSVDKPRFVA GSIGPTTKLP TLGHINFDEL KESYKEQIYG LTDGGVDLLL IETCQDVLQI KSALLASKEV LDSKNIDIPI MVSITMETTG TMLVGSDIAS ALTILEPFNI DILGLNCATG PEQMKEHIKY LSENSPFAIS CIPNAGLPEN IGGVAHYRLK PIELKMQLMN FIYDFNVQLI GGCCGTTPEH IKYLSSIIDE IIDKEMPNKN GKNNLSGYIP SASSIYNSVP YKQDNSILIV GERLNASGSK KVRELLNNDD WDGLVSIAKQ QQKENAHVLD VNVDYVGRDG VKDMKEITSR LVTNINLPLM IDSTDADKME SGLKSAGGKC IINSTNYEDG NERFDQVLNL ALGYGSGLVV GTIDEDGMAR NADKKYDIAK RAINRTRECG LSDYELFFDP LALPISTGIE EDRLNAKETI TAISKIRENF PEIHIILGIS NISFGLSPLS RINLNSIFLD ECIKAGLDSA IIAPNKILPL SKISEETKKL CLDLIYDKRK FEDDICIYDP LVELTKAFQD LSIQDFKKAS SENKNLTLEE SLKNHIIDGE KIGLEDQLNK ALKKYKPLEI INTFLLDGMK VVGDLFGSGQ MQLPFVLQSA ETMKFAVSIL EPHMETVEEN ISNGKLLIAT VKGDVHDIGK NLVDIILTNN GYEVINLGIK QDVSAIIDAQ KKHNADCIAM SGLLVKSTAF MKDNLEAFNN QDISVPVILG GAALTPKFVN EDCSQIYKGK ILYGKDAFTD LKFMNEYMDN KKKGNWSNTE GFINNEGIDI NLASSKSNSQ AVKKSISIDI ETSKFNLKEN FIRSKFINEE EPIQAPFLGT KVLNEIDIDL NKLIFYLDTK ALFSGQWQIK KGKNQSVDEY NNYLDSYAKP LLDRWLETIV EKKLISPKAV YGYFRCGRKD NSIFLFDDKS LNKISEFNFP RQKSGNNLCI ADFYCDLKKD KPIDIFPMQA VTMGDIASEY SQKLFKEDKY SDYLLFHGLT VQLAEALAEY VHALIRIECG FRTEEPDKNR EILAQKYRGA RYSFGYPACP KVSDSNIQLS LLDAKRISLT MDESEQLHPE QSTTAIISLH SKAKYFSA // ID A3PHU4_RHOS1 Unreviewed; 335 AA. AC A3PHU4; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 46. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABN75910.1}; GN OrderedLocusNames=Rsph17029_0799 {ECO:0000313|EMBL:ABN75910.1}; OS Rhodobacter sphaeroides (strain ATCC 17029 / ATH 2.4.9). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=349101 {ECO:0000313|EMBL:ABN75910.1, ECO:0000313|Proteomes:UP000002606}; RN [1] {ECO:0000313|Proteomes:UP000002606} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17029 / ATH 2.4.9 {ECO:0000313|Proteomes:UP000002606}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; ABN75910.1; -; Genomic_DNA. DR RefSeq; WP_011337253.1; NC_009049.1. DR RefSeq; YP_001042682.1; NC_009049.1. DR ProteinModelPortal; A3PHU4; -. DR STRING; 349101.Rsph17029_0799; -. DR EnsemblBacteria; ABN75910; ABN75910; Rsph17029_0799. DR KEGG; rsh:Rsph17029_0799; -. DR PATRIC; 23169269; VBIRhoSph114483_0948. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265278; -. DR KO; K00548; -. DR OMA; GTNLFAM; -. DR OrthoDB; EOG693GKH; -. DR BioCyc; RSPH349101:GHC8-815-MONOMER; -. DR Proteomes; UP000002606; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002606}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ABN75910.1}; KW Transferase {ECO:0000313|EMBL:ABN75910.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 212 212 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 278 278 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 279 279 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 335 AA; 35341 MW; 251001B86A6FA50E CRC64; MTDALSRLLR TRDWLMADGA TGTNLFNMGL SSGEPPELWT VDRPDNIRSL YRAAVEAGSD IFLTNSFGGN AARLKLHEAQ GRVGELNRIA AELGREVADA AGRPVVVAGS MGPTGEIFEP MGTLTHRMAV EIFHEQAEAL KAGGADVLWV ETISAAEEFK AAAEAARLAG MPWCGTMSFD TAGRTMMGIT AAALVDLVTK LPNPPLAFGA NCGVGASDLL RTVLGFAAQG IEVPIIAKGN AGIPKYHDGH IHYDGTPELM AEYAVLARDA GARIIGGCCG TMPEHLKAMR AALEGRPRGP RPSLETISET LGGFSSASDG SDDAGPTRER RRRRS // ID A3PP33_RHOS1 Unreviewed; 359 AA. AC A3PP33; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 49. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABN78099.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABN78099.1}; GN OrderedLocusNames=Rsph17029_2998 {ECO:0000313|EMBL:ABN78099.1}; OS Rhodobacter sphaeroides (strain ATCC 17029 / ATH 2.4.9). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=349101 {ECO:0000313|EMBL:ABN78099.1, ECO:0000313|Proteomes:UP000002606}; RN [1] {ECO:0000313|Proteomes:UP000002606} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17029 / ATH 2.4.9 {ECO:0000313|Proteomes:UP000002606}; 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; ABN78099.1; -; Genomic_DNA. DR RefSeq; WP_011842013.1; NC_009050.1. DR RefSeq; YP_001044871.1; NC_009050.1. DR ProteinModelPortal; A3PP33; -. DR STRING; 349101.Rsph17029_2998; -. DR EnsemblBacteria; ABN78099; ABN78099; Rsph17029_2998. DR KEGG; rsh:Rsph17029_2998; -. DR PATRIC; 23173931; VBIRhoSph114483_3251. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; RSPH349101:GHC8-3042-MONOMER; -. DR Proteomes; UP000002606; Chromosome 2. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002606}; KW Methyltransferase {ECO:0000313|EMBL:ABN78099.1}; KW Transferase {ECO:0000313|EMBL:ABN78099.1}. SQ SEQUENCE 359 AA; 38164 MW; 43C505E9659650D9 CRC64; MEPFPLWSPL LLLIRPDSML TFSLPPSRAV PALEALVRQR ILILDGAMGT QIQALGLSEE DYAGCGCRHH AERPQKGNND LLILTQPQAI EEIHFRYAMA GADIVETNTF SATTIAQADY GMESAVEDLN REGARIVRRA LDRATALDGR PRFVAGAVGP TNRTASISPD VNDPGYRAVS FDDLRVAYAT QVRALIAGGA DLILIETIFD TLNAKAAIFA CFEAFAEAGR RLPLMISGTI TDASGRTLSG QTPTAFWHSV RHARPFTVGL NCALGAAAMR PHLAELAGVA DAAICAYPNA GLPNAFGQYD EGPDETAAQV ARFAREGLVN VVGGCCGTTP DHVRAIACAV ADLPPRTLA // ID A3QAT4_SHELP Unreviewed; 1240 AA. AC A3QAT4; DT 17-APR-2007, integrated into UniProtKB/TrEMBL. DT 17-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 63. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABO22582.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABO22582.1}; GN OrderedLocusNames=Shew_0710 {ECO:0000313|EMBL:ABO22582.1}; OS Shewanella loihica (strain ATCC BAA-1088 / PV-4). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=323850 {ECO:0000313|EMBL:ABO22582.1, ECO:0000313|Proteomes:UP000001558}; RN [1] {ECO:0000313|EMBL:ABO22582.1, ECO:0000313|Proteomes:UP000001558} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1088 / PV-4 {ECO:0000313|Proteomes:UP000001558}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000606; ABO22582.1; -; Genomic_DNA. DR RefSeq; WP_011864516.1; NC_009092.1. DR RefSeq; YP_001092841.1; NC_009092.1. DR ProteinModelPortal; A3QAT4; -. DR SMR; A3QAT4; 665-1239. DR STRING; 323850.Shew_0710; -. DR EnsemblBacteria; ABO22582; ABO22582; Shew_0710. DR KEGG; slo:Shew_0710; -. DR PATRIC; 23513187; VBISheLoi132094_0712. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SLOI323850:GHQJ-732-MONOMER; -. DR Proteomes; UP000001558; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001558}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABO22582.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001558}; KW Transferase {ECO:0000313|EMBL:ABO22582.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 255 255 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 318 318 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 319 319 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 771 771 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1240 AA; 137436 MW; F51E0EE3C7C9E7AD CRC64; MATQSPVRNV RQINDAIRAR LNKEILILDG AMGTMIQNHK LEEADFRGER FKQWPCDLKG NNDLLVLTQP ELIKQIHRDY LLAGADIIET NTFNATQVAM ADYEMQELSR EINLEGARLA RTACDEVAAE SGRQCYVAGV LGPTNRTCSI SPDVNDPGYR NIHFDDLVEA YIESTQALIE GGADIIMVET IFDTLNAKAA LFAIETLFDQ LGQRLPVMIS GTITDASGRT LTGQTTEAFY NSLRHVKPLS IGLNCALGPQ ELRPYVEELS KIAECYVSAH PNAGLPNEFG GYDETPEQMA EVIGPWAEEG LLNIIGGCCG TTPDHIKAIR AAVIKHGARE LPDLPVACRL SGLEPLTIDA DSLFVNVGER TNVTGSAKFL RLIKTGEYEE ALSVARDQVE NGAQIIDINM DEGMLDGVEV MQKFLNLIAS EPDISRVPIM IDSSKWEVIE AGLKCIQGKG VVNSISLKEG EAKFIEQATL VKRYGAAAII MAFDEVGQAD TMARKIEICT RAYRVLVDKV GFPPEDIIFD PNIFAIATGI DEHDNYAVDF IEATREIKRT LPHAMISGGV SNVSFSFRGN NPVREAIHAV FLYHAIQAGM DMGIVNAGQL AIYDDIDPDL KARVEAVVQN LPCPVQGSNN TEQLLEIAEQ YRGDGAAGAK KEDLEWRSWP VNKRLEHALV KGITEFIDQD TEEARQLASR PLDVIEGPLM DGMNVVGDLF GSGKMFLPQV VKSARVMKKA VAYLNPYIEA EKVEGESNGK ILMVTVKGDV HDIGKNIVGV VLACNGYEVV DLGVMVPVEK IIEVAKAEKV DIIGMSGLIT PSLDEMVHNV KAFHKAGLNI PSIIGGATCS KIHTAVKIAP HAPEGAIYIA DASRAVPMVA KLINKETRQA TIDAAYEEYR VMRDKRNSQA KRKQIVSLEA ARENRCQQDW NAHTPFVPNQ LGRQVFDDYP LEDLVDRIDW TPFFRSWELH GHFPKILDDE VVGEEARKLY QDAKAMLKTI IDEKWLTAKA VIGLFPANTV NYDDIEIYTD ESRSKVEMTT HHLRMQIERV GNDNFCLADF VAPKDSGVAD YMGGFAVTAG HGIDEHVARF EANHDDYSAI MLKCLADRLV EAFAERMHER VRKEFWGYAA DENLDNEALI REKYKGIRPA PGYPACPDHT EKGLLWELLK PDETIDLKIT ESYAMFPTAA VSGWYFAHPQ SRYFGVTNIG RDQVEDYAKR KGMSVEETER WLAPVLDYDV // ID A3RWY3_RALSL Unreviewed; 346 AA. AC A3RWY3; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase homocysteine-binding subunit {ECO:0000313|EMBL:EAP71977.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EAP71977.1}; GN ORFNames=RRSL_01650 {ECO:0000313|EMBL:EAP71977.1}; OS Ralstonia solanacearum UW551. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=342110 {ECO:0000313|EMBL:EAP71977.1, ECO:0000313|Proteomes:UP000005933}; RN [1] {ECO:0000313|EMBL:EAP71977.1, ECO:0000313|Proteomes:UP000005933} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UW551 {ECO:0000313|EMBL:EAP71977.1}; 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. {ECO:0000313|EMBL:EAP71977.1}. 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; AAKL01000038; EAP71977.1; -; Genomic_DNA. DR RefSeq; WP_003264556.1; NZ_AAKL01000038.1. DR EnsemblBacteria; EAP71977; EAP71977; RRSL_01650. DR PATRIC; 38544487; VBIRalSol34715_3189. DR Proteomes; UP000005933; Unassembled WGS sequence. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005933}; KW Methyltransferase {ECO:0000313|EMBL:EAP71977.1}; KW Transferase {ECO:0000313|EMBL:EAP71977.1}. SQ SEQUENCE 346 AA; 37450 MW; EB55394ED0AB16DC CRC64; MTAPLPYTRA ANLPALLRQR ILILDGAMGT MIQRYKLTEA QYRGERFAGH PVDVKGNNEL LLLTAPEVIR EIHEQYLAAG ADLIETNTFG ATTVAQEDYK MAELAYEMNV VAARLAREAC DKYSTPDKPR FVAGAFGPTP KTASISPDVN DPGARNINFD QLRDAYYEQG KALLEGGADV FLVETIFDTL NAKAALFAID QLFEDLGERV PVMISGTVTD ASGRILSGQT VEAFWNSLRH AKPITFGLNC ALGAALMRPY IAELAKICDT AVSCYPNAGL PNPMSDTGFD ETPDVTSSLV DEFAAAGLVN LVGGCCGTTP EHIQAIAERV AQRKPRAWPG QYREAA // ID A3SM60_9RHOB Unreviewed; 299 AA. AC A3SM60; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EAP78441.1}; GN ORFNames=ISM_09090 {ECO:0000313|EMBL:EAP78441.1}; OS Roseovarius nubinhibens ISM. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseovarius. OX NCBI_TaxID=89187 {ECO:0000313|EMBL:EAP78441.1}; RN [1] {ECO:0000313|EMBL:EAP78441.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ISM {ECO:0000313|EMBL:EAP78441.1}; 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. {ECO:0000313|EMBL:EAP78441.1}. 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; AALY01000001; EAP78441.1; -; Genomic_DNA. DR RefSeq; WP_009813840.1; NZ_CH724156.1. DR ProteinModelPortal; A3SM60; -. DR PRIDE; A3SM60; -. DR EnsemblBacteria; EAP78441; EAP78441; ISM_09090. DR PATRIC; 28129163; VBIRosNub115512_1810. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EAP78441.1}; KW Transferase {ECO:0000313|EMBL:EAP78441.1}. SQ SEQUENCE 299 AA; 32299 MW; 4FA4AB1E6A9CB209 CRC64; MAEITLLDGS IGQELMKRSG DAPTTIWSIQ VMRHHPGMVR EVHEAYFRAG ATIASTNTYC VHRDRLEKVD LDPELMPDLV KSALAEAEEA RAAHGGGRIA GSLGPLEASY RPDIRITPET AARKFAELVA LMRDRVDLFL IETVASLEHA EGALRGVASA GKPVWLAVTV DDEDGTRLRS GEAVADLAPL IERFAPEAVL INCSRPEAVA DGLRVIREFG RPFGAYANGF TRISEDFLKA KPTVDVLTAR RDLDPAAYAG FAMGWVGQGA TILGGCCEVG PEHIAHLAKR LRAEGHEIV // ID A3SN37_9RHOB Unreviewed; 337 AA. AC A3SN37; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EAP75877.1}; GN ORFNames=ISM_13465 {ECO:0000313|EMBL:EAP75877.1}; OS Roseovarius nubinhibens ISM. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseovarius. OX NCBI_TaxID=89187 {ECO:0000313|EMBL:EAP75877.1}; RN [1] {ECO:0000313|EMBL:EAP75877.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ISM {ECO:0000313|EMBL:EAP75877.1}; 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. {ECO:0000313|EMBL:EAP75877.1}. 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; AALY01000002; EAP75877.1; -; Genomic_DNA. DR RefSeq; WP_009814702.1; NZ_CH724156.1. DR ProteinModelPortal; A3SN37; -. DR EnsemblBacteria; EAP75877; EAP75877; ISM_13465. DR PATRIC; 28130933; VBIRosNub115512_2684. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EAP75877.1}; KW Transferase {ECO:0000313|EMBL:EAP75877.1}. SQ SEQUENCE 337 AA; 36118 MW; D1B5AB030CF3435A CRC64; MTTVFSDFLN SRDWLLADGA TGTNLFNMGL QSGDAPEMWN VEHPEKITRL YQMAVDAGSD LFLTNSFGGT AARLKLHGAE KRVRELSRVA AELGREVADK TDRRVIVAGS VGPTGEIMAP MGALTHEIAV EMFHEQADGL KEGGADVLWL ETISAPEEYR AAAEAFKLAD MPWCGTMSFD TAGRTMMGFT SADMAEMVEK LDPAPLAYGA NCGVGASDLM RTVLGFVTQG SERPIIAKGN AGIPKYVDGH IHYDGTPDLM AEYACLARDA GAKIIGGCCG TMPEHLSKMR EALETRPRGD IPTLEQIAEA LGGFSSEADG TGDDTPPARP RRGRRRG // ID A3SWC5_9RHOB Unreviewed; 337 AA. AC A3SWC5; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=Methionine synthase I {ECO:0000313|EMBL:EAP80826.1}; GN ORFNames=NAS141_05793 {ECO:0000313|EMBL:EAP80826.1}; OS Sulfitobacter sp. NAS-14.1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Sulfitobacter. OX NCBI_TaxID=314267 {ECO:0000313|EMBL:EAP80826.1}; RN [1] {ECO:0000313|EMBL:EAP80826.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NAS-14.1 {ECO:0000313|EMBL:EAP80826.1}; 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. {ECO:0000313|EMBL:EAP80826.1}. 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; AALZ01000003; EAP80826.1; -; Genomic_DNA. DR RefSeq; WP_005853702.1; NZ_CH959312.1. DR ProteinModelPortal; A3SWC5; -. DR EnsemblBacteria; EAP80826; EAP80826; NAS141_05793. DR PATRIC; 28308521; VBISulSp100835_0180. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 337 AA; 35411 MW; 172A60386B40B0B9 CRC64; MSNPLTDLLA EKGTLLADGA TGTNLFNMGL MSGDAPEMWN TEQPQNIIKL YQGAVQSGSD IFLTNSFGAN ASRLKLHNAE KRAHELSRVS AELAREVADK AGRKVIVAGS VGPTGEIMEP VGPLTHALAV EMFHETADGL KAGGADVGWL ETISAPEEYR AAAEGFKLAG LDWVGTMSFD TAGRTMMGMT SEAMVDMVHD LDYGPLAYGA NCGTGASDVL RTVLGFASKG MPTPIVSKGN AGIPKYVEGH IHYDGTPELM ADYAEMARNC GASIIGGCCG TMPEHLVHMR AALDSRPKGD APTLEQIVEA LGPFSSASDG TDGEGPTRAP RRGRRRG // ID A3TGH3_9MICO Unreviewed; 305 AA. AC A3TGH3; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:EAP99933.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EAP99933.1}; GN Name=mmuM {ECO:0000313|EMBL:EAP99933.1}; GN ORFNames=JNB_07179 {ECO:0000313|EMBL:EAP99933.1}; OS Janibacter sp. HTCC2649. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Intrasporangiaceae; Janibacter. OX NCBI_TaxID=313589 {ECO:0000313|EMBL:EAP99933.1}; RN [1] {ECO:0000313|EMBL:EAP99933.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2649 {ECO:0000313|EMBL:EAP99933.1}; RX PubMed=21075932; DOI=10.1128/JB.01298-10; RA Thrash J.C., Cho J.C., Bertagnolli A.D., Ferriera S., Johnson J., RA Vergin K.L., Giovannoni S.J.; RT "Genome sequence of the marine Janibacter sp. strain HTCC2649."; RL J. Bacteriol. 193:584-585(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. {ECO:0000313|EMBL:EAP99933.1}. 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; AAMN01000001; EAP99933.1; -; Genomic_DNA. DR RefSeq; WP_009775740.1; NZ_CH672413.1. DR ProteinModelPortal; A3TGH3; -. DR EnsemblBacteria; EAP99933; EAP99933; JNB_07179. DR PATRIC; 27560866; VBIJanSp77695_1370. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EAP99933.1}; KW Transferase {ECO:0000313|EMBL:EAP99933.1}. SQ SEQUENCE 305 AA; 31535 MW; D4288B2F91D9F0AA CRC64; MALAGQCDDV AMTIDALLHT GPVVLDGGFS TALEARGHDL SGRLWSARLL RQAPSEVVAA HRTFVDAGAE IVISASYQAS HAGYVAAGLT EEECDADLDA SIELARQGAD GRALVAASVG PYGAHLADGS EYTGYPAVSR ATLREFHSRR LERLIAAGPD LVAVETIPEV AEAEVVVELL TEIAPDLPYW VSFSATGGGR LTGGAPFAEA IGVVRGAAIA VGVNCTAPRH IDELLEAGGP NVPYVIYPNA GATYDPGSKT WTEDGSAHFA PTTVQRWNDL GARFIGGCCG IGADGIREIA GAVRA // ID A3TL58_9MICO Unreviewed; 1266 AA. AC A3TL58; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 01-APR-2015, entry version 50. DE SubName: Full=MetH {ECO:0000313|EMBL:EAP99113.1}; GN ORFNames=JNB_03055 {ECO:0000313|EMBL:EAP99113.1}; OS Janibacter sp. HTCC2649. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Intrasporangiaceae; Janibacter. OX NCBI_TaxID=313589 {ECO:0000313|EMBL:EAP99113.1}; RN [1] {ECO:0000313|EMBL:EAP99113.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2649 {ECO:0000313|EMBL:EAP99113.1}; RX PubMed=21075932; DOI=10.1128/JB.01298-10; RA Thrash J.C., Cho J.C., Bertagnolli A.D., Ferriera S., Johnson J., RA Vergin K.L., Giovannoni S.J.; RT "Genome sequence of the marine Janibacter sp. strain HTCC2649."; RL J. Bacteriol. 193:584-585(2011). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EAP99113.1}. 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; AAMN01000002; EAP99113.1; -; Genomic_DNA. DR RefSeq; WP_009774922.1; NZ_CH672413.1. DR ProteinModelPortal; A3TL58; -. DR SMR; A3TL58; 656-909. DR EnsemblBacteria; EAP99113; EAP99113; JNB_03055. DR PATRIC; 27559226; VBIJanSp77695_0564. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 253 253 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 316 316 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 773 773 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1266 AA; 138716 MW; CCDFBEB5A251D499 CRC64; MDTAVDHRPD ATAALTAALT ERVLVLDGAM GTMIQREGLS EEDYRGERFA DWPSDLRGNN DLLSLTNPSI IEGIHRAYLL AGADLVETNT FNAQRISLAD YDMADIAYEM NLEAARLARR ACDEVAAETG RPRWVMGALG PTTRTASISP DVNDPGARNV SFDQLVEAYL EQARGLVDGG ADALIIETIF DTLNAKAAIF AVETLFDDLG RRWPVIISGT ITDASGRTLS GQVTEAFWNS VRHARPLVVG LNCALGPDEL RPYIAELSRI AGCFVSAYPN AGLPNAFGEY DETPDQMASV VGEFATSGLV NILGGCCGTT PEHIEAIAEA AAKGNPRVPS EVPGALRLSG LEPLTVDESS LFVNVGERTN ITGSARFRRL IKEEDYPAAL SVARQQVEAG AQVIDINMDE GMIDGVAAMD RFVKLIGSEP DICRVPLMID SSKWEVIEAG LKCSQGKPIV NSISMKEGVE PFLEHARLCH KYGAAVVVMA FDEEGQADSL ERRKVICQRA YDLLTQEVGM DPHDIIFDPN IFAVATGIEE HAAYGTDFIE ATRWIKENLP GALVSGGVSN VSFSFRGNNP VREAIHAVFL YNAIQAGMDM GIVNAGALVV LDDVDPELRE RIEDVVLNRR PDSTERLVEI ADRFNNTGEA APEVTEAEWR GLPVRERITH SLVKGIDDFV VEDTELLRQE IEAADGKPIE VIEGPLMDGM GVVGDLFGAG KMFLPQVVKS ARVMKKAVAH LIPYIEAEKE RSGVSTQNSK GLIVMATVKG DVHDIGKNIV GVVLQCNNYD VIDLGVMVPT QKILDTAKEK GADIIGLSGL ITPSLDEMVR VAQEMERQGF TIPLLIGGAT TSRAHTAVKV DGQYSGPVVW VKDASRSVPV ASQLLSATQR EPLLQTIKAD YDSMRARHAA KSTERPLVSI DAARKAHTPI DWTAYRPVRP HLLAQQSKDV WSGKADTKWH RAAAQFTREF ISYPIEELRR YIDWTPFFQA WEMKGRYPDI LSNPATGETA RKLFEDANAM LDRIIEEKWL TAKAVIGLFP ANAVGDDIEV YADESRETVL TTIHGLRQQG QHREGVPNRC LSDFIAPKET GLRDYVGGFA VTAGHGTHER IKAFQEELDD YSGILLEALA DRLAEAFAER LHERVRREFW GHAGDEHLSN EDLISEKYAG IRPAPGYPAC PDHTEKETLF KLLGAAERAG MELTESMAMQ PGASVSGWYF SHPQSQYFVV GRLGRDQVED YAARKGWTLA EAERWLGPNL GYQPED // ID A3TMD5_9MICO Unreviewed; 309 AA. AC A3TMD5; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 01-OCT-2014, entry version 21. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EAP99540.1}; GN ORFNames=JNB_05190 {ECO:0000313|EMBL:EAP99540.1}; OS Janibacter sp. HTCC2649. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Intrasporangiaceae; Janibacter. OX NCBI_TaxID=313589 {ECO:0000313|EMBL:EAP99540.1}; RN [1] {ECO:0000313|EMBL:EAP99540.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2649 {ECO:0000313|EMBL:EAP99540.1}; RX PubMed=21075932; DOI=10.1128/JB.01298-10; RA Thrash J.C., Cho J.C., Bertagnolli A.D., Ferriera S., Johnson J., RA Vergin K.L., Giovannoni S.J.; RT "Genome sequence of the marine Janibacter sp. strain HTCC2649."; RL J. Bacteriol. 193:584-585(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. {ECO:0000313|EMBL:EAP99540.1}. 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; AAMN01000002; EAP99540.1; -; Genomic_DNA. DR RefSeq; WP_009775348.1; NZ_CH672413.1. DR EnsemblBacteria; EAP99540; EAP99540; JNB_05190. DR PATRIC; 27560072; VBIJanSp77695_0979. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 309 AA; 32085 MW; 71A8B79B77C119BA CRC64; MTDGGLETDL IFHHGVDLPG FAAYPLLETA EGRALLSQYY AGFAQVASRA GAGLLLETPT WRASADWVVA LGGVRSDVRR INLESVLFLA GLAENLISDG VSPGGAAGFD GSGRGPDVRV CGVLGPRGDG YIAGDPTSAD EFGDYHWAQI AAFAQSGVAR VTAYTLTTVA EAVGVVQAAR AQGVAVAVSF TVETDGRLPD GTPLGEAIES LRLQAAPDDL LVNCAHPSHI AAALTPEAAW TDHVTGLRVN ASRQSHAELD DAAELDEGDI VDLVTEHERL AARLPRLDIV GGCCGTDVRH VAALWGVDV // ID A3TX97_OCEBH Unreviewed; 339 AA. AC A3TX97; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=Methionine synthase I {ECO:0000313|EMBL:EAQ03457.1}; GN ORFNames=OB2597_02517 {ECO:0000313|EMBL:EAQ03457.1}; OS Oceanicola batsensis (strain ATCC BAA-863 / DSM 15984 / HTCC2597). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Oceanicola. OX NCBI_TaxID=252305 {ECO:0000313|EMBL:EAQ03457.1}; RN [1] {ECO:0000313|EMBL:EAQ03457.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2597 {ECO:0000313|EMBL:EAQ03457.1}; 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. {ECO:0000313|EMBL:EAQ03457.1}. 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; AAMO01000004; EAQ03457.1; -; Genomic_DNA. DR RefSeq; WP_009804757.1; NZ_CH724131.1. DR ProteinModelPortal; A3TX97; -. DR EnsemblBacteria; EAQ03457; EAQ03457; OB2597_02517. DR PATRIC; 28490793; VBIOceBat2886_2223. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 339 AA; 35787 MW; E5EB23E587664312 CRC64; MADALSKLLE TRDWLMADGA TGTNLFNMGL SSGDAPELWN VDQPEKIRTL YSYAVNAGSD IFLTNTFGGN ASRLKLHDAQ DRVRELNRIG AELGREVADA SGRTVVVAGS VGPTGDIMAP MGSLTHELAV EMFHEQAEGL KEGGADILWL ETISAPEEYK AAAEAFAMAG MPWCGTMSFD TAGRTMMGVT SEAMVSMVEK LPNPPLAYGA NCGVGAADLL RTVLGFAAQG VERPIIAKGN AGIPKYEDGH IHYDGTPELM ADYAVMARDC GATVIGGCCG TMPEHLGKMR EALETRPRGP RPTLDTIAAT LGGFSSATDG TGDDADAPKR SRGGRRRRG // ID A3UED1_9RHOB Unreviewed; 353 AA. AC A3UED1; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 33. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EAP91612.1}; GN ORFNames=OA2633_05521 {ECO:0000313|EMBL:EAP91612.1}; OS Oceanicaulis sp. HTCC2633. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Hyphomonadaceae; Oceanicaulis. OX NCBI_TaxID=314254 {ECO:0000313|EMBL:EAP91612.1}; RN [1] {ECO:0000313|EMBL:EAP91612.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2633 {ECO:0000313|EMBL:EAP91612.1}; 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. {ECO:0000313|EMBL:EAP91612.1}. 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; AAMQ01000001; EAP91612.1; -; Genomic_DNA. DR RefSeq; WP_009801507.1; NZ_CH672428.1. DR EnsemblBacteria; EAP91612; EAP91612; OA2633_05521. DR PATRIC; 25534344; VBIOceAle934_1917. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 353 AA; 37921 MW; 21A705432F35C6D2 CRC64; MTKAERRAAL DALALERILI LDGAMGTQIQ TLKLDEAGYR GERFADWSCP IQGNNDILNL STPDAVRAIH KEYFDAGADL VETNTFSATQ IAQADYKMED LAAQIASEGA RLAREAADAA EAETGSPKAV LGAIGPTNKT LSLSPNVEDP GFREVTFDQV REAYAEQVEA MAEHVDFFLI ETIFDTLNAK AAIKAILDLR NEGRIDADIP IILSGTITDA SGRTLSGQTT EAFYNSIRHA QPWAVGLNCA LGGKQLRPYV AELARIAECH VLAYPNAGLP NAFGEYDETP DETAAFIADW AQSGLINIAG GCCGTTPAHI AAIARDARAG APRKRDDRPR AMRLSGLEPF ELA // ID A3UPV1_VIBSP Unreviewed; 299 AA. AC A3UPV1; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EAP95504.1}; GN ORFNames=V12B01_17716 {ECO:0000313|EMBL:EAP95504.1}; OS Vibrio splendidus 12B01. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=314291 {ECO:0000313|EMBL:EAP95504.1}; RN [1] {ECO:0000313|EMBL:EAP95504.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=12B01 {ECO:0000313|EMBL:EAP95504.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAP95504.1}. 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; AAMR01000006; EAP95504.1; -; Genomic_DNA. DR RefSeq; WP_004732341.1; NZ_CH724170.1. DR ProteinModelPortal; A3UPV1; -. DR EnsemblBacteria; EAP95504; EAP95504; V12B01_17716. DR PATRIC; 25652136; VBIVibSpl92012_0704. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EAP95504.1}; KW Transferase {ECO:0000313|EMBL:EAP95504.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 204 204 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 279 279 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 280 280 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 299 AA; 32541 MW; 3854BDF9C0A236A9 CRC64; MKTLTILDGG MGRELKEIDA PFSQPLWSAQ ALIEAPEFVS QAHQNFVDAG AEILITNSYA CVPFHLGEEL FEQRGFELAA QSGELAKAVA DNAPHTVKVA GAIPPPFGSY RPDLFKVEEA APIIQTLYDA QDPNIDLWIA ETICSLQEFE SIHAVLKQSS KPCYYAFSLE DTKGDSANIR SGESVTDSIK LACQSNATGI MFNCSVPEVM DQAIIDAKKV IDELGSDLDI GVYANNFAPI SSEHEANDMF QEMRELDGQG YLAYAKRWHA LGANIIGGCC GIGPKHIKAL ADWKHSIQS // ID A3UZX7_VIBSP Unreviewed; 1225 AA. AC A3UZX7; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 46. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EAP91932.1}; GN ORFNames=V12B01_10607 {ECO:0000313|EMBL:EAP91932.1}; OS Vibrio splendidus 12B01. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=314291 {ECO:0000313|EMBL:EAP91932.1}; RN [1] {ECO:0000313|EMBL:EAP91932.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=12B01 {ECO:0000313|EMBL:EAP91932.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EAP91932.1}. 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; AAMR01000077; EAP91932.1; -; Genomic_DNA. DR RefSeq; WP_004735983.1; NZ_CH724177.1. DR ProteinModelPortal; A3UZX7; -. DR SMR; A3UZX7; 654-1224. DR EnsemblBacteria; EAP91932; EAP91932; V12B01_10607. DR PATRIC; 25658213; VBIVibSpl92012_4168. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EAP91932.1}; KW Transferase {ECO:0000313|EMBL:EAP91932.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1225 AA; 136211 MW; 95A6030A607B7751 CRC64; MGSNVRQKID ALLKQRILLI DGGMGTMIQD YKLEEQDYRG ERFADWHSDL KGNNDLLVLT QPKLIKDIHM EYLEAGADIL ETNTFNSTTI AMADYDMESL SEEINFTAAK LAREAADEWT AKTPDKPRFV AGVLGPTNRT CSISPDVNDP GYRNVSFDEL VEAYSESTRA LIKGGSDLIL IETIFDTLNA KACSFAVESV FEEVGITLPV MISGTITDAS GRTLSGQTTE AFYNALRHVK PISFGLNCAL GPDELREYVG EMSRISECNV SAHPNAGLPN AFGEYDLSPE DMAEHVKEWA DSGFLNLIGG CCGTTPEHIR HMAEAVEGVT PRQLPDLPVS CRLSGLEPLT IAKESLFVNV GERTNVTGSA RFKRLIKEEL YDEALSVARE QVENGAQIID INMDEGMLDA EACMVKFLNL CASEPEISKV PVMVDSSKWE VIEAGLKCIQ GKGIVNSISL KEGKEKFVEQ AKLVRRYGAA VIVMAFDELG QADTRERKVE ICTNAYNILV DEVGFPPEDI IFDPNIFAVA TGIDEHNNYA VDFIEAVGDI KRDLPHAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK NGMDMGIVNA GQLEIYDNVP EDLREAVEDV VLNRRDDSTE RLLDIATEYL ERAVGKVEDK SALEWRTWPV EKRLEHSLVK GITDFIVEDT EEARVNASRP IEVIEGPLMD GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AHLEPFINAT KDVGATNGKI LLATVKGDVH DIGKNIVGVV LQCNNYEIID LGVMVSCEKI LKVAKEENVD IIGLSGLITP SLDEMVHVAK EMERQGFKLP LLIGGATTSK AHTAVKIEQN YSEPVVYVNN ASRAVGVCTS LLSNELKPAF VEKLDIDYDR VRDQHNRKKP RTKPVSLERA RANKVAIDWN AYTPPAPAKP GVHIFKDFDV ATLRQYIDWT PFFMTWSLVG KYPAIFDHEE VGEEAKRLFK DANDLLDRVE REKLLEARGM CAMFPANSVG DDIEVYTDES RTEVLKVLHN LRQQTEKPKG FNYCLSDYIA PKDSGKADWI GGFAVTGGIG ERELADEYKA NGDDYNAIMI QAVADRLAEA FAEYLHKEVR KDIWGYSPDE NLSNDDLIRE KYQGIRPAPG YPACPEHTEK GTLWELMDVE KAIDMSLTTS YAMWPGASVS GMYFSHPDAR YFAIAQIQQD QVDSYADRKG WDMLEAEKWL GPNIN // ID A3V0V3_9RHOB Unreviewed; 282 AA. AC A3V0V3; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EAQ08081.1}; GN ORFNames=SKA53_10164 {ECO:0000313|EMBL:EAQ08081.1}; OS Loktanella vestfoldensis SKA53. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Loktanella. OX NCBI_TaxID=314232 {ECO:0000313|EMBL:EAQ08081.1}; RN [1] {ECO:0000313|EMBL:EAQ08081.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SKA53 {ECO:0000313|EMBL:EAQ08081.1}; 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. {ECO:0000313|EMBL:EAQ08081.1}. 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; AAMS01000001; EAQ08081.1; -; Genomic_DNA. DR RefSeq; WP_007205983.1; NZ_CH672414.1. DR ProteinModelPortal; A3V0V3; -. DR EnsemblBacteria; EAQ08081; EAQ08081; SKA53_10164. DR PATRIC; 30247519; VBILokVes90427_0361. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EAQ08081.1}; KW Transferase {ECO:0000313|EMBL:EAQ08081.1}. SQ SEQUENCE 282 AA; 29405 MW; 1C02706EDBA8746F CRC64; MTKITLLDGG MGQELIRRSG EAPTPLWSTQ VMIDHPGMVA AVHADYRAAG ATVHTTNTYA IHRDRLEGTG LEDRFADLTA AASTEAQGSG RIAGSIGPLI ASYRPDIHPA HDIAVPAYAE VAALIAPRVD LFLCETVASV AHARAVLAAT LPLGKPVWLS VTLDDEDGSR LRSGEPVADV LEAAQGASAL LANCSAPEAM AAAMAAFAKG NLPFGAYANG FTQITKDFLK SKPTVDALSA RRDLGPDAYA HFALGWIDQG PPSSVAAARS APPISRGWRS NC // ID A3V5M8_9RHOB Unreviewed; 1254 AA. AC A3V5M8; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 47. DE SubName: Full=Probable 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EAQ06946.1}; GN ORFNames=SKA53_15401 {ECO:0000313|EMBL:EAQ06946.1}; OS Loktanella vestfoldensis SKA53. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Loktanella. OX NCBI_TaxID=314232 {ECO:0000313|EMBL:EAQ06946.1}; RN [1] {ECO:0000313|EMBL:EAQ06946.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SKA53 {ECO:0000313|EMBL:EAQ06946.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EAQ06946.1}. 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; AAMS01000004; EAQ06946.1; -; Genomic_DNA. DR RefSeq; WP_007207019.1; NZ_CH672414.1. DR ProteinModelPortal; A3V5M8; -. DR EnsemblBacteria; EAQ06946; EAQ06946; SKA53_15401. DR PATRIC; 30249583; VBILokVes90427_1379. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EAQ06946.1}; KW Transferase {ECO:0000313|EMBL:EAQ06946.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 261 261 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 325 325 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 777 777 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1254 AA; 136233 MW; D6EAE969667DEA1E CRC64; MTTILPKSPA FDRIAAAAAD RILILDGAMG TQIQALGFAE GDFTAHGAGC ACHPQFFSDD PLPQQGNNDL LILTQPQAIE DIHYTYAMAG ADIVETNTFS STSIAQADYG LEHLVYDLNF HGARLVRQAL DRATAQDGRM RFVAGALGPT NRTASMSPDV NNPGYRAVTF DQLRVAYVEQ LRGLIDGGAD LILIETIFDT LNAKAAIFAC EEIFAANGLR LPVMISGTIT DRSGRTLSGQ TPTAFWHAVR HADPLTIGLN CALGAAEMRA HLAELSGVAD TLICAYPNAG LPNEFGAYDE SPAFMAEQIA AFAKEGLVNI VGGCCGSTPD HIRAIAAAVA GHKPRAIPAQ TPLMRLSGLE PFTLTRDIAF VNVGERTNVT GSAKFRKLIT ARDYAAAVDV AREQVENGAQ IIDVNMDEGL IDSKQAMIDY LNLIAAEPDI ARVPVMIDSS KWEVIEAGLQ CVQGKPIVNS ISMKEGEEAF LHQARLCRAY GAAVVVMAFD EAGQADTEDR KVAICTRAYQ LLTQKVGFPP EDIIFDPNVF AVATGIEEHD NYGVDFINAT RRIKADLPHV HVSGGVSNLS FSFRGNDPVR EAMHAVFLYH AIQAGMDMGI VNAGQLAVYD SIDPDLRDAC EDVVLNRTPD ATENMLVIAE RFKSTGAREA KERDLAWREW SVEKRLEHAL VNGITEFIDA DTDEARLRAD RPLHVIEGPL MAGMNVVGDL FGAGKMFLPQ VVKSARVMKQ AVAVLLPYME EEKRLNGGTG RESAGKVLMA TVKGDVHDIG KNIVGVVLAC NNYDIIDLGV MVPAAKILEV AKAENVDIIG LSGLITPSLD EMVHVAAEME RAGMDIPLLI GGATTSRVHT AVKIHPNYAR GQTLYVTDAS RAVGVVSALL SPDQKAGYIA TIRAEYEKVA DQHARSELAK KRLPLAAARA NALKIDWQDY KVPAPSFLGT KVYEDWDLAE LARYIDWTPF FQTWELKGIY PKILQDEKQG QAARALFADA QEMLHQIIAE KWFRPRAVVG FWPANAVGDD IRLFSDDSRK TELAMLHTLR QQVSKRDGRP NVALSDFVAP VGMADYVGGF VVTAGIEEVA IAERFAAAGD DFNAILVKAL ADRFAEAFAE RMHEMVRRDL WGYAPDEDLA PTDLIGEPYR GIRPAPGYPA QPDHTEKTTL FQLLDAQAAT GVTLTESMAM WPGSSVSGLY IGHPDAYYFG VAKVEQDQVL DYAARKGMDL AEVERWLGPI LNYVPQQKAA LAAE // ID A3V8J6_9RHOB Unreviewed; 339 AA. AC A3V8J6; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=Methionine synthase I {ECO:0000313|EMBL:EAQ05427.1}; GN ORFNames=SKA53_03424 {ECO:0000313|EMBL:EAQ05427.1}; OS Loktanella vestfoldensis SKA53. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Loktanella. OX NCBI_TaxID=314232 {ECO:0000313|EMBL:EAQ05427.1}; RN [1] {ECO:0000313|EMBL:EAQ05427.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SKA53 {ECO:0000313|EMBL:EAQ05427.1}; 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. {ECO:0000313|EMBL:EAQ05427.1}. 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; AAMS01000009; EAQ05427.1; -; Genomic_DNA. DR RefSeq; WP_007204641.1; NZ_CH672414.1. DR ProteinModelPortal; A3V8J6; -. DR EnsemblBacteria; EAQ05427; EAQ05427; SKA53_03424. DR PATRIC; 30244895; VBILokVes90427_1948. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 339 AA; 35027 MW; 2EB3173A4E842C5A CRC64; MTNALSKLLE TRDWLMADGA TGTNLFNMGL MSGDAPEMWN IDEPAKIRAL YKGAADAGSD IFLTNSFGGN ASRMKLHGAE GQVHELNKVA AALGRDIADA SGRTIVVAGS VGPTGEIMSP MGTLTHERAV EMFHEQAEGL KAGGADVLWV ETISAAEEFA AAAEAFALAG MPWCGTMSFD TAGRTMMGLT SADMVKKVGK LAHQPLAFGA NCGTGASDLL RTVLGFAAAG PTLPLIAKGN AGIPKYHDGH IHYDGTPELM ADYAVLARDS GATIIGGCCG TTPDHLRAMR HALETRPKGT APTLDAITAA LGGFSSASDG TDGAGPEAAP RRGRRAKRD // ID A3VAK3_9RHOB Unreviewed; 349 AA. AC A3VAK3; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 32. DE SubName: Full=Methionine synthase, 5-methyltetrahydrofolate--homocysteinemethyltransferase {ECO:0000313|EMBL:EAQ14944.1}; GN ORFNames=RB2654_20213 {ECO:0000313|EMBL:EAQ14944.1}; OS Maritimibacter alkaliphilus HTCC2654. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Maritimibacter. OX NCBI_TaxID=314271 {ECO:0000313|EMBL:EAQ14944.1}; RN [1] {ECO:0000313|EMBL:EAQ14944.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2654 {ECO:0000313|EMBL:EAQ14944.1}; 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. {ECO:0000313|EMBL:EAQ14944.1}. 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; AAMT01000001; EAQ14944.1; -; Genomic_DNA. DR RefSeq; WP_008334931.1; NZ_CH902578.1. DR ProteinModelPortal; A3VAK3; -. DR EnsemblBacteria; EAQ14944; EAQ14944; RB2654_20213. DR PATRIC; 28480191; VBIRhoBac6565_3019. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EAQ14944.1}; KW Transferase {ECO:0000313|EMBL:EAQ14944.1}. SQ SEQUENCE 349 AA; 37506 MW; 12F66123841AAD89 CRC64; MRAFNIPPTD TEAALKRAAR ERILILDGAM GTQIQSLGLD EDAFLGHGGH SCAYHSDHPQ KGNNDLLILT QPDEIERIHY DFAMAGADIV ETNTFSSTTI AQADYAMEEA VHDLNAQGAR IARRAMDRAT AEDGKPRWVA GAVGPTNRTA SISPDVNDPG YRAVTFDDLR RAYGQQIRGL IAGGADLILI ETIFDTLNAK AAIFACFEAF AEHGKRLPVM ISGTITDASG RTLSGQTPTA FWHSVRHARP FTVGLNCALG ANAMRPHLKE LSDVADALIC AYPNAGLPNA FGEYDEGPDD TAPQVEQFAR EGLVNVVGGC CGTTPDHIRA IAEAVAKYEP RKLPSYTDA // ID A3VJZ9_9RHOB Unreviewed; 338 AA. AC A3VJZ9; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 31. DE SubName: Full=Methionine synthase I {ECO:0000313|EMBL:EAQ11505.1}; GN ORFNames=RB2654_02050 {ECO:0000313|EMBL:EAQ11505.1}; OS Maritimibacter alkaliphilus HTCC2654. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Maritimibacter. OX NCBI_TaxID=314271 {ECO:0000313|EMBL:EAQ11505.1}; RN [1] {ECO:0000313|EMBL:EAQ11505.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2654 {ECO:0000313|EMBL:EAQ11505.1}; 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. {ECO:0000313|EMBL:EAQ11505.1}. 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; AAMT01000015; EAQ11505.1; -; Genomic_DNA. DR RefSeq; WP_008328220.1; NZ_CH902578.1. DR ProteinModelPortal; A3VJZ9; -. DR EnsemblBacteria; EAQ11505; EAQ11505; RB2654_02050. DR PATRIC; 28473292; VBIRhoBac6565_2547. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 338 AA; 35605 MW; 374BEFC97AA6C1A7 CRC64; MSQDALSTLL SERDWLLADG ATGTTLFNMG LTSGDAPEMW NVDHPDRVRA LYQGPVDAGS DIFLTNSFGG TASRLKLHNA QDRVGELNRI AAELGREVAD KAGRTVIVAG SMGPTGEIME PMGPLSFDAA VEMFHEQAEA LKAGGVDVLW VETISSPDEY KAAARAAALA DMPWCGTMSF DTAGRTMMGV TSAAMAKLVE TLPNPPIGFG ANCGVGASDL LRTILGFKQT GTERPVIAKG NAGIPKYVHG HIHYDGTPEL MADYAVMARD CGARIIGGCC GTTPEHLVAM REALETRAPG AAPALERIAE TLGAFSSTSD GTDDKGPAPR ERRGRRRG // ID A3VWD1_9RHOB Unreviewed; 336 AA. AC A3VWD1; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 31. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EAQ26761.1}; GN ORFNames=ROS217_19582 {ECO:0000313|EMBL:EAQ26761.1}; OS Roseovarius sp. 217. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseovarius. OX NCBI_TaxID=314264 {ECO:0000313|EMBL:EAQ26761.1}; RN [1] {ECO:0000313|EMBL:EAQ26761.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=217 {ECO:0000313|EMBL:EAQ26761.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAQ26761.1}. 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; AAMV01000001; EAQ26761.1; -; Genomic_DNA. DR RefSeq; WP_009818730.1; NZ_CH902584.1. DR ProteinModelPortal; A3VWD1; -. DR EnsemblBacteria; EAQ26761; EAQ26761; ROS217_19582. DR PATRIC; 28139095; VBIRosSp94902_1921. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 212 212 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 278 278 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 279 279 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 336 AA; 35626 MW; A6502C8969461C32 CRC64; MPNALTKMLA TRDWILADGA TGTNLFNMGL QSGDAPEMWN DQHPDRIKRL YTEAVDAGSD LFLTNSFGGN AARLKLHGAQ GRARELSRIS AEIGRDVADR YDRPVIVAGS VGPTGEIMAP MGALTHALAV EIFHEQAEGL KEGGADVLWL ETISAPEEYK AAAEAFKLAD MPWCGTMSFD TAGRTMMGLT SSDMATMVEK LGNPPLAFGA NCGVGASDLL RTILGFVAQG SDRPIVAKGN AGIPKYHDGH IHYDGTPDLM ADYAVLARDA GATIIGGCCG TMPEHLSKMR AALESRPRGP RPTLDEITEA LGAFSSGGDG TGDDTAAPRR PRRRRA // ID A3VZD0_9RHOB Unreviewed; 298 AA. AC A3VZD0; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EAQ26204.1}; GN ORFNames=ROS217_13546 {ECO:0000313|EMBL:EAQ26204.1}; OS Roseovarius sp. 217. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseovarius. OX NCBI_TaxID=314264 {ECO:0000313|EMBL:EAQ26204.1}; RN [1] {ECO:0000313|EMBL:EAQ26204.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=217 {ECO:0000313|EMBL:EAQ26204.1}; 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. {ECO:0000313|EMBL:EAQ26204.1}. 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; AAMV01000002; EAQ26204.1; -; Genomic_DNA. DR RefSeq; WP_009817539.1; NZ_CH902584.1. DR ProteinModelPortal; A3VZD0; -. DR EnsemblBacteria; EAQ26204; EAQ26204; ROS217_13546. DR PATRIC; 28136669; VBIRosSp94902_0488. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EAQ26204.1}; KW Transferase {ECO:0000313|EMBL:EAQ26204.1}. SQ SEQUENCE 298 AA; 30890 MW; B7ED4C8C8562E892 CRC64; MTEITLLDGS IGQELVKRSG DRATPLWSTQ VMIDHPEIVR AVHDNYFAVG ATVASTNTYA VLRDRLARVG LQDEVARLTD VAVRAAVAAR GAHGSGRVAG AIGPLVQSYR PDLCPPAAEA AALYAENVAL LKDRVDLILL ETMSSVDQAR GGLMAAGLSG LPVWLGVTVM DDDGTRLRSG EALGDLAGLV AEFAPDAVLI NCTRPESVAT GLEIVRGFGR PFGAYANGFT CISAGFLGAA PTVDALEQRG DLSPAAYAGF AMGWVAQGAS IVGGCCEVGP AHIAELARRL RAAGHDIV // ID A3WED3_9SPHN Unreviewed; 348 AA. AC A3WED3; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 34. DE SubName: Full=Methionine synthase I cobalamin-binding domain protein {ECO:0000313|EMBL:EAQ28014.1}; GN ORFNames=NAP1_10483 {ECO:0000313|EMBL:EAQ28014.1}; OS Erythrobacter sp. NAP1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Erythrobacteraceae; Erythrobacter. OX NCBI_TaxID=237727 {ECO:0000313|EMBL:EAQ28014.1}; RN [1] {ECO:0000313|EMBL:EAQ28014.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NAP1 {ECO:0000313|EMBL:EAQ28014.1}; 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] {ECO:0000313|EMBL:EAQ28014.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NAP1 {ECO:0000313|EMBL:EAQ28014.1}; 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. {ECO:0000313|EMBL:EAQ28014.1}. 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; AAMW01000002; EAQ28014.1; -; Genomic_DNA. DR RefSeq; WP_007165220.1; NZ_CH672390.1. DR ProteinModelPortal; A3WED3; -. DR EnsemblBacteria; EAQ28014; EAQ28014; NAP1_10483. DR PATRIC; 30316878; VBIErySp29781_2083. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 348 AA; 37207 MW; 32BD47023706E75C CRC64; MNARDRLNEA AKERVLIFDG AFGTQIQERK LTEEDYAGDL GLKADQKGNN DILALTRPDV IKDITRSYLD AGSDVVSTNT FSANSISQAD YAAEDQVAAI NIASGKIARE LADEYEAKDG RPRFVAGAIG PTNKTLSLSP DVEDPGFREI DFDELTAVYK EQAAALVEGG VDFILIETVF DTLNAKAGIM AVKQLEQELG REVPLMISMT LTDLSGRNLS GHTVEAFWYA VRHAKPVTIG LNCSFGADQL RPHIQALSGI ADTLLMAYPN AGLPNELGEY DEIPDTTAGL VKLWAQNGQA NILGGCCGSS PAHIKAIAEA VEGLPPRAVP TPETAMRLSG LEAFVVAA // ID A3WRU5_9BRAD Unreviewed; 1321 AA. AC A3WRU5; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 01-APR-2015, entry version 46. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EAQ37294.1}; GN ORFNames=NB311A_03264 {ECO:0000313|EMBL:EAQ37294.1}; OS Nitrobacter sp. Nb-311A. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Nitrobacter. OX NCBI_TaxID=314253 {ECO:0000313|EMBL:EAQ37294.1}; RN [1] {ECO:0000313|EMBL:EAQ37294.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Nb-311A {ECO:0000313|EMBL:EAQ37294.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EAQ37294.1}. 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; AAMY01000001; EAQ37294.1; -; Genomic_DNA. DR RefSeq; WP_009798360.1; NZ_CH672416.1. DR ProteinModelPortal; A3WRU5; -. DR SMR; A3WRU5; 686-1269. DR EnsemblBacteria; EAQ37294; EAQ37294; NB311A_03264. DR PATRIC; 25476361; VBINitSp102674_0128. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EAQ37294.1}; KW Transferase {ECO:0000313|EMBL:EAQ37294.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 281 281 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 344 344 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 345 345 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 801 801 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1321 AA; 144354 MW; 1F3E534A4A85B388 CRC64; MPPGRRRDLN PPPKDTDARD KRGRDDRRMT RVTNSSNPIA DKFRALARER ILVLDGAMGT MIQDRGFDEA AFRGERFKDF HRDVRGNNDL LILTQPQAIE DIHTQYLRAG ADLVATNTFS STSIAQADYD MADLVYDLNR EGARLARSAA EKVSAEDGKP RFVVGAIGPT NRTASISPDV ANPGYRAVTF DDLRKAYGEQ INGLLDGGAD LLLVETIFDT LNAKAALYAI AEIGEQRGID IPVMISGTIT DKSGRLLSGQ LPEAFWHSVR HAGPITIGFN CALGAEDLRA HVAEIGRVAD TLVCAYPNAG LPNEFGQYDE SPDYMARLIG EFAQTGLVNV VGGCCGTTPD HIAAIAAAVA PHKPRVVPVI APRLRLSGLE PFSLTSDIPF VNVGERTNVT GSARFRNLIK AGDYAAALDV ARNQVENGAQ IIDVNMDEGL LDSEAAMVTF LNLIAAEPDI ARVPVMVDSS KFSVIEAGLK CLQGKPVVNS ISLKEGEEKF LHEARIARRH GAAVVVMAFD ETGQADTCQR KMEICKRAYD ILVEQVGFPP EDIIFDPNVF AIATGLEEHN NYGVDFIEAT RWIRQNLPHA HISGGVSNLS FSFRGNEPVR EAMHSVFLYH AIKAGMDMGI VNAGQMVIYD DIDPELRQVC EDVVLNRDPD AGERLLNLAE KFRGQGRQAK EADLSWREWP VEKRLSHALV NGITEYIEQD TEEARQSADR PLSVIEGPLM AGMNVVGDLF GDGKMFLPQV VKSARVMKQA VAYLMPFMEE EKARNQAAGI EGAGSTSAGK ILLATVKGDV HDIGKNIVGI VLQCNNYEVI DLGVMVPAAK IIETAKAEKA DIVGLSGLIT PSLDEMGYFA AELERQGLNL PLLIGGATTS RVHTAVKIDP NYRNGPVIHV NDASRAVGVV ASLMSPERRE AYAAGVRAEY AKISAAHFRA QQDKKRLPLA TARANAVPID WSSYRPVKPT FLGTKAFTDY PLEELVEVID WTPFFQVWEL AGRFPAILDD KVVGETARAL YDDARKMLDR IVTEKWFTAS GVIGFWPANR IGDDIAVYGD ESRTTQIATY HTLRQQLEKR EGRHNAALAD FIAPKETGIA DYIGGFAVTA GLGEDEIAAR FKNANDDYSS ILVKALADRL AEAFAERMHQ RVRTEFWGYA PDEALTNDQL IREEYVGIRP APGYPAQPDH TEKATLFRLL DATRATGVEL TESFAMWPGS SVSGLYYSHP ESQYFGVGKI ERDQVEDYAA RKGMEVAEIE RWLASILNYI PGQDLSGQSG QPAATPVPAP ANDVSAEAAD HPPGCQCAVH MQLRKTTARA S // ID A3X6T6_9RHOB Unreviewed; 297 AA. AC A3X6T6; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 01-OCT-2014, entry version 18. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EAQ46471.1}; GN ORFNames=MED193_14787 {ECO:0000313|EMBL:EAQ46471.1}; OS Roseobacter sp. MED193. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseobacter. OX NCBI_TaxID=314262 {ECO:0000313|EMBL:EAQ46471.1}; RN [1] {ECO:0000313|EMBL:EAQ46471.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MED193 {ECO:0000313|EMBL:EAQ46471.1}; 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. {ECO:0000313|EMBL:EAQ46471.1}. 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; AANB01000002; EAQ46471.1; -; Genomic_DNA. DR RefSeq; WP_009810463.1; NZ_CH902583.1. DR EnsemblBacteria; EAQ46471; EAQ46471; MED193_14787. DR PATRIC; 28113303; VBIRosSp92751_0666. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EAQ46471.1}; KW Transferase {ECO:0000313|EMBL:EAQ46471.1}. SQ SEQUENCE 297 AA; 31938 MW; EB4936B3DA7AA909 CRC64; MQITLLDGSI GQEIVKRSGD RPTPLWSTSV MIEQPELVGA VHGDYFTVGA TVATTNTYAV HRDRLVRAGM EDRFEELLEV AMRQAEMARD AHGSGRIAAA LGPIGASYRP DLDIPLEKAK TLFSELVRLM EPKADLFLLE TVSSVDHARG ALMGCAETEK PVWLAVSVND DDGRLLRSGE PVQDLAPVIE EFQPAAVLIN CSRPEAIAAG LQIIKGFGRR FGAYANGFTG ITEGFLDEAP TVEALEQRRD LGPVEYAAFV MGWVAGGASI VGGCCEVGPA HIAEVARQLR EAGHEII // ID A3XF76_9RHOB Unreviewed; 185 AA. AC A3XF76; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 29-OCT-2014, entry version 20. DE SubName: Full=Methionine synthase I {ECO:0000313|EMBL:EAQ43526.1}; DE Flags: Fragment; GN ORFNames=MED193_02685 {ECO:0000313|EMBL:EAQ43526.1}; OS Roseobacter sp. MED193. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseobacter. OX NCBI_TaxID=314262 {ECO:0000313|EMBL:EAQ43526.1}; RN [1] {ECO:0000313|EMBL:EAQ43526.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MED193 {ECO:0000313|EMBL:EAQ43526.1}; 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. {ECO:0000313|EMBL:EAQ43526.1}. 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; AANB01000015; EAQ43526.1; -; Genomic_DNA. DR RefSeq; WP_009808072.1; NZ_CH902583.1. DR EnsemblBacteria; EAQ43526; EAQ43526; MED193_02685. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; FT NON_TER 185 185 {ECO:0000313|EMBL:EAQ43526.1}. SQ SEQUENCE 185 AA; 19828 MW; 4FB59162BA7460D5 CRC64; MTTFFADFLA EKDVLLADGA TGTNLFNMGL QSGDAPELWN TDEPKKIMAL YQGSVDAGSD LFLTNSFGGT AARLKLHDAQ GRVRELNRAA AELGREVADK MDRKIAVAGS VGPTGEIMLP VGELSHELAV EMFHEQAEAL KEGGVDVLWV ETISAPEEFR AAAEAFALAD MPWCGTMSFD TAGRT // ID A3XKL4_LEEBM Unreviewed; 318 AA. AC A3XKL4; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 33. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EAQ49903.1}; GN ORFNames=MED217_02095 {ECO:0000313|EMBL:EAQ49903.1}; 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 {ECO:0000313|EMBL:EAQ49903.1}; RN [1] {ECO:0000313|EMBL:EAQ49903.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MED217 {ECO:0000313|EMBL:EAQ49903.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAQ49903.1}. 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; AANC01000003; EAQ49903.1; -; Genomic_DNA. DR RefSeq; WP_009778814.1; NZ_CH672395.1. DR ProteinModelPortal; A3XKL4; -. DR EnsemblBacteria; EAQ49903; EAQ49903; MED217_02095. DR PATRIC; 29225442; VBILeeBla91056_1953. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EAQ49903.1}; KW Transferase {ECO:0000313|EMBL:EAQ49903.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 318 AA; 34722 MW; B9C82446AEBFC83C CRC64; MLQRYKFTEE DFRGEKFKDW SSPVQGNNDM LSITQPEAIA EVHANYFEAG ADIVETNTFS GTTIAMADYG MEDYVYELNY ESAKIAKKVA QEFTEKEPEK PRFVAGAMGP TNKTASMSPD VNDPGFRAIS FDELRTAYKQ QAKALLDGGV DLLLVETIFD TLNAKAALFA IEEIKEERNI EIPVMVSGTI TDASGRTLSG QTAEAFLISV EHMPLLSVGF NCALGAKQLT PYLEVVSGKS NFAVSAYPNA GLPNAFGEYD ETADEMAAQI KTYLDKQLIN IVGGCCGTTP EHIHAIAKLV EGYAPRPLPE LKKTEAAL // ID A3Y840_9GAMM Unreviewed; 1245 AA. AC A3Y840; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 01-APR-2015, entry version 47. DE SubName: Full=B12-dependent homocysteine-N5-methyltetrahydrofolate transmethylase,repressor of metE and metF {ECO:0000313|EMBL:EAQ66667.1}; GN ORFNames=MED121_12105 {ECO:0000313|EMBL:EAQ66667.1}; OS Marinomonas sp. MED121. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Marinomonas. OX NCBI_TaxID=314277 {ECO:0000313|EMBL:EAQ66667.1}; RN [1] {ECO:0000313|EMBL:EAQ66667.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MED121 {ECO:0000313|EMBL:EAQ66667.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EAQ66667.1}. 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; AANE01000002; EAQ66667.1; -; Genomic_DNA. DR RefSeq; WP_009831615.1; NZ_CH672429.1. DR ProteinModelPortal; A3Y840; -. DR SMR; A3Y840; 654-1241. DR EnsemblBacteria; EAQ66667; EAQ66667; MED121_12105. DR PATRIC; 28813609; VBIMarSp20187_0094. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EAQ66667.1}; KW Transferase {ECO:0000313|EMBL:EAQ66667.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 249 249 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 765 765 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1245 AA; 137687 MW; 417575913A7C7A97 CRC64; MVKSKSYSLI EERLAQNILV LDGAMGTMIQ AYKLTEDDFR GDRFADWPSD VQGNNDLLSL TQAKIIKDIH KAYLAAGSDI VETNTFNANA ISMLDYGMQS LSYELNFESA RLAREACDEF TKQNPDKPRF VAGAVGPTSR TCSISPDVND PGYRNIEFDE LVVAYTEAVD GLIKGGSDLI LIETIFDTLN AKAAIYAVLE YFETTGVRYP VMISGTITDA SGRTLSGQTT EAFWNSVSHA NPISVGLNCA LGPKDLRQYV EEISRVADVN VSAHPNAGLP NAFGEYDETP EEMLEEMQEW VNSGFLNIIG GCCGTEPSHI KAFADAVANA KPRAIPEIPK ACRLSGLEPF NIDENTLFVN VGERTNVTGS AIFKRLIKEG DFDSALTVAR QQVENGAQII DINMDEGMLD SEAAMVRFLK LIASEPDISR VPIMLDSSKW EILEAGLKCI QGKGVVNSIS MKEGVENFTE QARKLRKYGA AVIVMAFDEV GQADTRERKI EICRRSYQIL VEEVGFPPED IIFDPNIFAI ATGIEEHNRY ALDFIEATGD IKRELPHALI SGGVSNVSFS FRGNNPVREA IHAVFLYHAI QQGMTMGIVN AGQLALYDDI PAKLRDAVED AVLNRTDNAT DTLLDIATEF LGTGSNDNEV QVQEWRSLAV NERLSHALVK GITEFIDEDT EEARLAHTRP LEVIEGPLMD GMGIVGDLFG SGKMFLPQVV KSARVMKKAV AYLMPFIEEE KARNQDMASS SNGKIVMATV KGDVHDIGKN IVGVVLQCNN YEVIDLGVMV PAEKILRTAR EENANLIGLS GLITPSLDEM VHVAKEMERQ EFDIPVLIGG ATTSKAHTAV KIEQGYKRSQ VVHVTNASRS VGVASNLLSK DTEKRQAFID DIKLDYEKTR KRYKERSKAG RRVSLDKARQ NKAPIDWTLP IPKPKKLGVT VFTEKDIDLA ELKNYIDWTP FFMTWELAGA YPRILTDEVV GVEATKLYKD ALVMLDKVID EKLLEAKAIV GIFPANQVNH DDIEIYTDET RSEVKETLSF LRLQNELTAP GKYNNCLADF VAPKETGVAD YMGAFACATG FGIDPLVAAY EADHDDYNSI MIKAMADRLA EACAEYLHEK VRKEIWAYVP NESLSNEELI KEKYQGMRPA PGYPACPDHT EKDKLWSLMN IEENTGISIT ESYAMLPTAA VSGWYFANPE SSYFGVGKIG PDQVEDYANR KGMSKDDAER WLAPNLGYDP EDDKV // ID A3YZM5_9SYNE Unreviewed; 1221 AA. AC A3YZM5; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 55. DE SubName: Full=Putative methionine synthase {ECO:0000313|EMBL:EAQ74518.1}; GN ORFNames=WH5701_13030 {ECO:0000313|EMBL:EAQ74518.1}; OS Synechococcus sp. WH 5701. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechococcus. OX NCBI_TaxID=69042 {ECO:0000313|EMBL:EAQ74518.1}; RN [1] {ECO:0000313|EMBL:EAQ74518.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=WH 5701 {ECO:0000313|EMBL:EAQ74518.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EAQ74518.1}. 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; AANO01000007; EAQ74518.1; -; Genomic_DNA. DR RefSeq; WP_006171470.1; NZ_CH724159.1. DR ProteinModelPortal; A3YZM5; -. DR EnsemblBacteria; EAQ74518; EAQ74518; WH5701_13030. DR PATRIC; 29896209; VBISynSp31756_0141. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 243 243 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 771 771 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1221 AA; 132701 MW; 50CFC00D07BA0C8C CRC64; MTALVGSAAA ARTGTGRIGF LEHLHGPGRP VVVFDGATGT SLQQMDLSAE DFGGAALEGC NENLVFTRPD AVQAVHAQFL EAGCDVIETD TFGAASIVLA EYGLEDQAFA LNQRAAELAR EMADRYSTPT KPRFVAGSMG PTTKLPTLGH IDFDTMKASF REQAAGLLAG DVDLFIVETC QDVLQIKAAL QGLEEAFEAA GERRPLMVSV TMETTGTMLV GSDIAAVVSI LEPFAIDVLG LNCATGPEQM KEHIRYLSEH SPFVISCIPN AGLPENVGGV AHYRLTPLEL RLQLLHFVED LGVQVIGGCC GTTPSHIAAL AELAVDLHPS PRPVRLPQHR LKRPALQWEP AAASIYGVTP YHQDNSFLII GERLNASGSR KVRDLLNAED WDGLVALARG QIKENAHVLD VNVDYVGRDG EKDMHDLVSR LVTNVNLPLM LDSTEWQKME AGLKVAGGKC ILNSTNYEDG DERFFKVLEL ARRYGAGVVV GTIDEEGMAR TAERKFAIAQ RAYRDALEYG IPAHEIFYDP LALPISTGIE EDRRNAAATI EAIRLIRENL PGVHVVLGVS NVSFGLSPAA RIVLNSVFLH ECCEAGLDAA IVSPAKILPL AKITEEHQQV CRDLIEDRRR FESEAEAAIC TYDPLTVLTS LFEGVSAKEA RASGPSLADL PVEQRLRQHI IDGERIGLEP ALQEALASYP PLQIINTFLL DGMKVVGELF GSGQMQLPFV LQSAETMKAA VAFLEPHMEK VDGVSSAKAK FLIATVKGDV HDIGKNLVDI ILTNNGYEVI NLGIKQGVEA IIEAQHLHQA DCIAMSGLLV KSTAFMKDNL QAFNEAGITA PVILGGAALT PRFVQKDCRS VYNGQVIYGR DAFADLRFMD ALSEARKAGQ WDDRLGFLAG APAGLGLEAE PEPAAEPRAA GAEAASPDDQ ATPATASAPE VTSHRSAVVP EEPAVEPPFL GSCLIQEGEI PLDEVFAYLD RNALFAGQWQ LRKSQDQSRQ AYEAMLAEKA EPVLQSWIER CRQEVLLTPR VAYGYFPCGR DGNALVVFDP EGSERELGRF ELPRQRGGNR YCIADFFRDL SDGRPSDVLP MQAVTMGERA SAYARELFAA DRYTDYLYFH GLGVQMAEAL AEWTHARIRR ELGFAAEEPA ALRDVLAQRY RGSRYSFGYP ACPNVADSRQ QLAWLDTGRI GLTMDESDQL DPEQSTTALV ALHSLARYFS A // ID A3Z6R5_9SYNE Unreviewed; 1208 AA. AC A3Z6R5; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 51. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EAQ69306.1}; GN ORFNames=RS9917_12720 {ECO:0000313|EMBL:EAQ69306.1}; OS Synechococcus sp. RS9917. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechococcus. OX NCBI_TaxID=221360 {ECO:0000313|EMBL:EAQ69306.1}; RN [1] {ECO:0000313|EMBL:EAQ69306.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=RS9917 {ECO:0000313|EMBL:EAQ69306.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EAQ69306.1}. 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; AANP01000003; EAQ69306.1; -; Genomic_DNA. DR RefSeq; WP_007102491.1; NZ_CH724158.1. DR ProteinModelPortal; A3Z6R5; -. DR EnsemblBacteria; EAQ69306; EAQ69306; RS9917_12720. DR PATRIC; 29893090; VBISynSp107221_2482. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EAQ69306.1}; KW Transferase {ECO:0000313|EMBL:EAQ69306.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 238 238 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1208 AA; 132010 MW; 0117F84A4553DB11 CRC64; MQAELVAPTP VVSRFLSRLH SPERPVLVFD GATGTSLQQL NLTAADFGGP ELEGCNENLV VTRPDAVQAV HRQFLEAGCD VIETDTFGAA SVVLAEYGLQ DQAFALNKRA AELARTVAQE YSTAEKPRFV AGSMGPTTKL PTLGHIGFDT LKEAYREQAA GLLAGDVDLF IIETCQDVLQ IKAALQGVEA AFADAGERRP LMVSVTMETT GTMLVGSDIA AVVAILEPFA IDILGLNCAT GPEQMKDHIR YLAEHSPFVV SCIPNAGLPE NVGGVAHYRL QPLELKMQLM HFVEDLGVQV IGGCCGTTPA HIQALAELSE ELKPAQRPCR TEHRQRVQLS YDPAAASIYG ATSYHQDNSF LIIGERLNAS GSKKVRDLLN AEDWDGLVAV ARGQVKENAH VLDVNVDYVG RDGEKDMHEL VTRVVTNINL PLMLDSTEWQ KMEAGLKVAG GKCILNSTNY EDGDERFFKV LELARRYGAG VVVGTIDEEG MARTAEKKLA IAKRAYRDAV EFGIPAREIF YDPLALPIST GIEEDRRNGL ETIEAIRRIR DELPGVHVVL GVSNVSFGLS PAARISLNSV FLHDCCEAGM DAAIVSPAKI LPLMKIAEEH QQVCRDLIFD RRRFDGDVCT YDPLTELTTL FEGVSAKEAR QSGPSLADLP VEERLKQHII DGERIGLEEA LREGLQSYPP LEIVNTFLLD GMKVVGDLFG SGQMQLPFVL QSAETMKAAV AFLEPHMEKS DGKRSAKAKF LIATVKGDVH DIGKNLVDII LTNNGYEVIN LGIKQEVGAI IAAQQEHQAD CIAMSGLLVK STAFMKDNLQ AFNDAGISVP VVLGGAALTP RFVNKDCSEV YEGKVIYGRD AFTDLRFMDA YVKARAEERW DDRRGFLDGT PEGLSIGGED PASGEAVTGE ATAEASEATP QAAASLPVSS ERSEAVPAEA PIQPPFLGAS LLEGPEAIPL EDVIAYLDRQ ALFAGQWQMR KTREQTREAY EAELQEKAEP ILQSWLERVR SEQLLRPAVA YGYFPCGRGG NDLVVFSTDG AVELGRFSLP RQRSGNRYCI ADFFADLRDG QPTDVLPMQA VTMGEEASRF AQDLFQRDAY SDYLFFHGLA VQMAEALAEW THARIRRECG FPDPEGLPIR DVLAQRYRGS RYSFGYPACP NVGDSRQQLA WLGAERIGLE MDESEQLHPE QSTTALVALH SKARYFSA // ID A3ZUI9_9PLAN Unreviewed; 1239 AA. AC A3ZUI9; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 46. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EAQ79899.1}; GN ORFNames=DSM3645_22204 {ECO:0000313|EMBL:EAQ79899.1}; OS Blastopirellula marina DSM 3645. OC Bacteria; Planctomycetes; Planctomycetia; Planctomycetales; OC Planctomycetaceae; Blastopirellula. OX NCBI_TaxID=314230 {ECO:0000313|EMBL:EAQ79899.1}; RN [1] {ECO:0000313|EMBL:EAQ79899.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 3645 {ECO:0000313|EMBL:EAQ79899.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EAQ79899.1}. 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; AANZ01000012; EAQ79899.1; -; Genomic_DNA. DR RefSeq; WP_002652340.1; NZ_CH672376.1. DR ProteinModelPortal; A3ZUI9; -. DR SMR; A3ZUI9; 659-895. DR EnsemblBacteria; EAQ79899; EAQ79899; DSM3645_22204. DR PATRIC; 36949617; VBIBlaMar90471_1359. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EAQ79899.1}; KW Transferase {ECO:0000313|EMBL:EAQ79899.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 252 252 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 315 315 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 316 316 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 769 769 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1239 AA; 136673 MW; 095AEB93C58D5197 CRC64; MAIATPNDSK HLVIQELDKR ILILDGAMGT MVQKYKLDEN AVRGPKFDGF HKDLKNFTDI LCLTRPEIVE QIHREFLEAG ADILETNTFG ATPVAMEEFD LAHLATDVNV AAIQLARKVV DEFNERTPHK PRFVAGSIGP TSRTASMSPK VEDPGFRNVT FQQLVDSYLV QIAAMVEAGA DLLFPETTFD TLNLKACLFA IEKYFRDNNV VLPVMASVTI TDESGRTLSG QTVEAFWNSV AHFPLLSVGV NCALGADKMR PYVQELASIS PAYISCHPNA GLPNEFGEYD ETPEQMAATL TTFADSGWLN IVGGCCGTSP AHIKAIAEAV EHKAPRIRAT PPDFTRLSGQ QSLTILPTSN FTMIGERTNV TGSRRFARLV REELYEEAIA VALEQVNNGA NVIDINMDDA LLDGEAAMAR YLNLIAAEPD ICKAPIMIDS SKWSVIEAGL RCVQGKPIVN SISLKEGEAD FLAKARLVRS YGAAVVVMAF DETGQAVEKD PKVQICKRAY DLLVNEVGFP PSDIIFDPNI LTVATGIEEH NNYAINFIEA CREIKQVCPG AKISGGVSNV SFSFRGNDFI REAIHAVFLF HAIKAGLDMG IVNAGQLAVY DDVAPELREL IEDVLFNRRD DSTERLVDYA ETVKDRKAGG SAVTEDLSWR EGSVQERLSH ALVKGIDKFV VEDTQEARQH YDRCLRIIEG PLMDGMNIVG DLFGAGKMFL PQVVKSARVM KKAVAYLLPI MEEEKVALGE VAQDVRGTIL MATVKGDVHD IGKNIVGVVL GCNNYSVIDL GVMVSCDKIL AAAKKHGVDA IGLSGLITPS LDEMVHVAKE MEAAGFTIPL LIGGATTSAK HTAVKIAPAY SGTTVHVLDA SRSVGVVDRL LSDEMREEFL VKNKKLQDDL VASYKKRQEV KLVSMEHARR NKFATDWSTV DIRTPSFLGV RTLPKVSLTE LREYIDWTPF FMSWELKGKY PKIFEDSFVG EEAKKLFNDA NALLDKIIAE ELLTANGVYA FWPANSDGDD IVLYSDESRQ TEIGRMHTLR QQWERKGQKD FRALADYIAP IDSGRKDYLG GFAVTTGIGC QELATKFDAD FDDYNSIMTK ALADRLAEAF AEWLHARARL DWGFGADENL SKEELIAEKY RGIRPAAGYP AQPDHTEKRQ LFDLLKAEDN AGIELTESLA MFPAASVSGL YFGHPQSRYF AVDRMTHEQV ADYAKRKGCT LAEMERWLAP NLGYDPDEK // ID A4A4H1_9GAMM Unreviewed; 1221 AA. AC A4A4H1; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 56. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:EAQ99100.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EAQ99100.1}; GN ORFNames=KT71_15561 {ECO:0000313|EMBL:EAQ99100.1}; OS Congregibacter litoralis KT71. OC Bacteria; Proteobacteria; Gammaproteobacteria; OMG group; OM60 clade; OC Congregibacter. OX NCBI_TaxID=314285 {ECO:0000313|EMBL:EAQ99100.1, ECO:0000313|Proteomes:UP000019205}; RN [1] {ECO:0000313|EMBL:EAQ99100.1, ECO:0000313|Proteomes:UP000019205} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KT71 {ECO:0000313|EMBL:EAQ99100.1}; RX PubMed=17299055; DOI=10.1073/pnas.0608046104; RA Fuchs B.M., Spring S., Teeling H., Quast C., Wulf J., RA Schattenhofer M., Yan S., Ferriera S., Johnson J., Glockner F.O., RA Amann R.; RT "Characterization of a marine gammaproteobacterium capable of aerobic RT anoxygenic photosynthesis."; RL Proc. Natl. Acad. Sci. U.S.A. 104:2891-2896(2007). RN [2] {ECO:0000313|EMBL:EAQ99100.1, ECO:0000313|Proteomes:UP000019205} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KT71 {ECO:0000313|EMBL:EAQ99100.1}; RX PubMed=19287491; DOI=10.1371/journal.pone.0004866; RA Spring S., Lunsdorf H., Fuchs B.M., Tindall B.J.; RT "The photosynthetic apparatus and its regulation in the aerobic RT gammaproteobacterium Congregibacter litoralis gen. nov., sp. nov."; RL PLoS ONE 4:E4866-E4866(2009). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EAQ99100.1}. 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; AAOA02000001; EAQ99100.1; -; Genomic_DNA. DR RefSeq; WP_008295544.1; NZ_CM002299.1. DR ProteinModelPortal; A4A4H1; -. DR SMR; A4A4H1; 656-1220. DR EnsemblBacteria; EAQ99100; EAQ99100; KT71_15561. DR PATRIC; 29068761; VBIConLit32816_2636. DR Proteomes; UP000019205; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000019205}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EAQ99100.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000019205}; KW Transferase {ECO:0000313|EMBL:EAQ99100.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1221 AA; 134525 MW; 1A6CF236B4982F32 CRC64; MTAFFPVTGP LADALSERIL IIDGAMGTMI QAEGLAEADY RGERFAKHGG DLKGNNDLLS ITRPDVIENI HRAYLQAGAD IIETNTFNST AVALEDYGLQ AIARELNETS ARIARKAADE VSAETPDKPR FVAGVLGPTP RTASISPDVN DPGARNIDYQ TLSEDYAEAT RGLLDGNVDL LMIETIFDTL NAKAAIFAIE KVFEERGVRI PVMLSVTFPD VSGRNLSGQS PEAFWFSIAH ARPLVVGSNC GRRFQEVRPF LEELSKATDG YFSAHLNAGL PNAFGEYDEA PEVMAMEFKD FAERGFVNLV GGCCGTTPAH IRAIANAVHG IPPRPLPDNP KACQLSGLEP FTFSADSLFV NVGERCNVTG SARFKKLILS GDYEAALDVA RTQVEDGAQI IDVNMDEGML DAKEAMVTFL NLIASEPDIS RVPIMIDSSR WEVIEAGLRC VQGKAVVNSI SLKAGEEEFL EQAALCQRYG AAVVVMAFDE DGQADTVARR REICQRSWDL LRNRLDFNPD DIIFDPNIFA IGTGIEAHNS YAVDFIEATR WIKENLPGAK VSGGVSNVSF SFRGNNPVRE AIHSVFLYHA IRAGMDMGIV NAGQLAVYDE LPAELRDAVE DVVLNRRDDS TERLLDLASK YHADGPASVR VEDLAWRDEP VKKRLEYALV KGINGYIEED AEEARQQADR PIEVIEGPLM DGMNVVGDLF GQGKMFLPQV VKSARVMKQA VAYLQPYIEE EKAEGSTNGK ILMATVKGDV HDIGKNIVGV VLQCNNYEVI DLGVMVHCEE ILRVAREENV DVIGLSGLIT PSLDEMVHVA SEMQRTGFSV PLMIGGATTS KAHTAVKIEP NYTNDLVVYV PDASRSVSVA SQLLGEQKEG FVSERREEYL QVRERMASRK PKAKRLSYEE ALANRAVFDW SAYTPPTPTF TGVRVFKDIS LADLVETIDW TPFFITWELA GKYPRILNDD IVGEQARDLF ADAQAMLKKI VDENWLEARA AVGFWPAHSD GEDVLLDIDG APEPTRLHHL RQQTEKANGD PNFSLSDFIA PENDFIGGFC VTTGHGVAKR AAAFEAAHDD YSSIMLKALA DRLAEALAEH MHRRVRQEFW AYARDEELTN EDLIKERYRG IRPAPGYPAC PDHTEKRTLF DLLDAESLCG VSLSDNYAME PASSVSGWYF SHPEARYFAV GKIGEDQLES MAARKNSKTA ELARWLAPNL D // ID A4ATR1_MARSH Unreviewed; 330 AA. AC A4ATR1; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 44. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EAR00831.1}; GN OrderedLocusNames=FB2170_17141 {ECO:0000313|EMBL:EAR00831.1}; OS Maribacter sp. (strain HTCC2170 / KCCM 42371). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Maribacter. OX NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00831.1, ECO:0000313|Proteomes:UP000001602}; RN [1] {ECO:0000313|EMBL:EAR00831.1, ECO:0000313|Proteomes:UP000001602} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602}; RX PubMed=21037013; DOI=10.1128/JB.01207-10; RA Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J., RA Cho J.C.; RT "Complete genome sequence of strain HTCC2170, a novel member of the RT genus Maribacter in the family Flavobacteriaceae."; RL J. Bacteriol. 193:303-304(2011). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002157; EAR00831.1; -; Genomic_DNA. DR RefSeq; WP_013304634.1; NC_014472.1. DR RefSeq; YP_003860865.1; NC_014472.1. DR ProteinModelPortal; A4ATR1; -. DR EnsemblBacteria; EAR00831; EAR00831; FB2170_17141. DR KEGG; fbc:FB2170_17141; -. DR PATRIC; 42329859; VBIFlaBac16383_0209. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR BioCyc; MSP313603:GH3X-208-MONOMER; -. DR Proteomes; UP000001602; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001602}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EAR00831.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001602}; KW Transferase {ECO:0000313|EMBL:EAR00831.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 243 243 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 330 AA; 36143 MW; A87956A9353B4BE0 CRC64; MKEIKDILKE RVLILDGATG TMLQRYKFTE EDFRGERFKE WPLSLQGNND LLSLTQPEAI AIIHAKYLEA GADIIETNTF SGTTIAMADY QMEELVYELN YESARIARKV ADEFTVKNPD KPRFVAGSIG PTNKTASMSP DVNDPGFRAV SFDELRIAYK QQVEALIDGG VDLLLVETIF DTLNAKAALF AIEEVKEERN MDIPIMVSGT ITDASGRTLS GQTAEAFLIS ISHIPILSVG FNCALGASQL VPHLEVLSAK TDFAVSAHPN AGLPNAFGEY DETPEQMASQ IKEYLEKGLV NIVGGCCGTT PEHISAMADL VKDFEPRNSL // ID A4BC32_9GAMM Unreviewed; 1227 AA. AC A4BC32; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 47. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EAR10517.1}; GN ORFNames=MED297_01810 {ECO:0000313|EMBL:EAR10517.1}; OS Reinekea blandensis MED297. OC Bacteria; Proteobacteria; Gammaproteobacteria; Reinekea. OX NCBI_TaxID=314283 {ECO:0000313|EMBL:EAR10517.1}; RN [1] {ECO:0000313|EMBL:EAR10517.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MED297 {ECO:0000313|EMBL:EAR10517.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EAR10517.1}. 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; AAOE01000004; EAR10517.1; -; Genomic_DNA. DR RefSeq; WP_008046855.1; NZ_CH724153.1. DR ProteinModelPortal; A4BC32; -. DR SMR; A4BC32; 653-1224. DR EnsemblBacteria; EAR10517; EAR10517; MED297_01810. DR PATRIC; 28434721; VBIReiBla99298_3214. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EAR10517.1}; KW Transferase {ECO:0000313|EMBL:EAR10517.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136056 MW; 1D4708155C88190B CRC64; MSHREQRIKN LHQAIRERIL ILDGAMGSLI QSYQLEEQDY RGERFADWPS DLKGNNDLLT LTRPDVIEAI YTAYLEAGSD IIETNTFNST AVSQDDYGMQ SLAYELNREG AALARRACDA MTAKTPEKPR WVTGVIGPTS KTLSLSPDVN NPGYRAITFE ALVEDYKTAT RGLIDGGADL LLIETIFDTL NAKAAIFAIH SVFDEVGFEL PIMISGTITD ASGRTLSGQT TEAFYYSVKH AKPLTVGLNC ALGADELRPY VETLSSIADC YVSVHPNAGL PNEFGEYDES PEEMTSVVDE FAASGFVNII GGCCGTTPKH IELINAAMQK HSPRQPAADP HRMALSGLEP FVLTDELNFV NVGERTNVTG SAKFRRLIKE ELYDEALDVA REQVENGAQI IDVNMDEGML DSADAMTTFL NLIASEPDIA RVPIMVDSSK WDVIEAGLRC VQGKAIVNSI SLKEGEANFL HQAKLCQRYG AAVVIMAFDE TGQADTRERK IEICQRSYDL LTAHGFPPED IIFDPNIFAV ATGIDEHNNY ALDFIEATDH IRRNMPYASV SGGVSNVSFS FRGNNPVREA IHSVFLYHAS KVGMNMGIVN AGQLVIYDDI PDELRERVED VILNRRNDAT DRLLEIAEKY RGDGKTEVKE DLEWRSLPVN KRIEHALVKG ITAHIIDDTE EARQQATAPI DVIEGPLMDG MNVVGDLFGA GKMFLPQVVK SARVMKQAVA HLIPFIEAEK SADAKPKGKV LMATVKGDVH DIGKNIVGVV LACNNFDVID LGVMVPAEKI LKVAREENVD VIGLSGLITP SLDEMVHIAR EMQRQDFHLP LMIGGATTSK AHTAVKIDPQ YHNDATIYVT DASRAVSVVQ SLLNPKQKPI FVAERQAEYE TVRERNKNRK SKALHPYPQA CENAESFDWD SYTPPVPAFT GTQVFDNYSV KELRDYIDWT PFFNTWDLHG KYPKILSDEK VGETATSLFQ DAQAMLDRII DENWLTPKAV VGFWPAARTS ADTIQVQEDH GTTDLEHLRQ QSIKPDQQPN YSLADFIAPD GHGSDYLGGF VVTTGHGVDE RANAYEQAGD DYNSIMLKAL ADRLAEAFAE RMHERVRKEF WGYDRDESLS NDELIKERYQ GIRPAPGYPA CPDHTEKAKL FDLLNATDAT GVALTDSFAM MPAASVSGWY FSHPQSKYFG VGKISRDQVE DYAQRKGMTM EEAERWLSPN LAYEPTA // ID A4BNK6_9GAMM Unreviewed; 1233 AA. AC A4BNK6; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 45. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EAR22805.1}; GN ORFNames=NB231_10143 {ECO:0000313|EMBL:EAR22805.1}; OS Nitrococcus mobilis Nb-231. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Nitrococcus. OX NCBI_TaxID=314278 {ECO:0000313|EMBL:EAR22805.1}; RN [1] {ECO:0000313|EMBL:EAR22805.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Nb-231 {ECO:0000313|EMBL:EAR22805.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EAR22805.1}. 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; AAOF01000002; EAR22805.1; -; Genomic_DNA. DR RefSeq; WP_005002169.1; NZ_CH672427.1. DR ProteinModelPortal; A4BNK6; -. DR SMR; A4BNK6; 651-1230. DR EnsemblBacteria; EAR22805; EAR22805; NB231_10143. DR PATRIC; 25484981; VBINitMob112042_1579. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EAR22805.1}; KW Transferase {ECO:0000313|EMBL:EAR22805.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1233 AA; 136611 MW; F1834B9E68513488 CRC64; MTDSTNRLQE ELEHRVLLLD SATGTMIQRY RLAEEDFRGD RFRDHGCNLQ GNNDLLVCTR PDIVAEIHRS NLQAGADIIE TNTFNATTPS QADYATEHLV PEINLTAARI ARKCADEFSR ATPQQPRFVA GVLGPTSKTA SLSPDVNNPG YRNTSFTQLV EAYTEAAQGL ISGGVDLLLV ETIFDTLNAK ACLFALDGLF QQLGTKVPVM VSGTITDASG RTLSGQTTEA FWNSVRHAQP FAIGLNCALG AEDLRPYIKE LSQIAECYVS THPNAGLPNE MGEYEQSPHA MAQLLREFVE SGYVNIAGGC CGTTPEHIAA IREAIAGLPP RQRPERPRAL RLSGLEPLTL GTDSLFANIG ERTNVTGSAR FRRLIKEDDF EAALEVGRDQ VESGAQIIDV NMDEGLLDSK ECMVRFLNLA AGEPDIARVP FMVDSSKWEV IEAGLQCIQG KAIVNSISLK EGEEDFIAKA GLVRRYGAAA VIMAFDEQGQ ADTLERRVAI AERAYRILTE EVGFPPEDII LDLNIFAIAT GLEEHNNYAV DFIDATREVK TRLPHVKVSG GLSNLSFSFR GNEPVRRAMH SAFLYHAIQA GMDMAIVNAG QLEVYDDIPK DLLERVEDVL LNRRDDATER LVEYAEQFKG QGAKSKEEDL EWRTRSVAKR LEHALVKGIV EYIETDTEEA RTQHAQPIEV IEGPLMDGMN VVGDLFGSGK MFLPQVVKSA RVMKKAVAYL LPFIEAEKAK HGNSEPNARI VMATVKGDVH DIGKNIVGVV LQCNNFEVTD LGVMVPNEKT LAIALEQKAD IVGLSGLITP SLDEMVGMAK EMERQGLDIP LLIGGATTSR VHTAVKIAPQ YSGDVIYVKD ASRAVGVCSK LMSTTQRAAY VQSIKEEYEG VRQQRAKRQR KQKWLRITEA RANRYPIDWT TYEPPQPQQP GLHVLDEVAL ETLEPYIDWT PFFSAWQLAG RFPKLLDDAL VGEAARKLYA DARAMLTQII EEQWLQARGV CGLFPANAVG EDTEVYTDES RTQVRLVTHH LRQQTEKPAG RPNMSLADFV APKETGLPDW LGAFAVTTGI GIEAHIRRFE AEHDDYNAIL LKALADRLAE ACAEMLHHRV RTEYWGYTTG EALDNEALIQ ERYQGIRPAP GYPACPDHTE KALVWELLDA ERNAAITLTE SWAMVPTAAV SGWYFAHPNA RYFGLGQIYR DQVEDYAKRK GMSLKEAERW LTPNLGYDPE ELA // ID A4C928_9GAMM Unreviewed; 353 AA. AC A4C928; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 31. DE SubName: Full=Putative B12-dependent homocysteine-N5-methyltetrahydrofolate transmethylase (N terminal) {ECO:0000313|EMBL:EAR29093.1}; GN ORFNames=PTD2_08614 {ECO:0000313|EMBL:EAR29093.1}; OS Pseudoalteromonas tunicata D2. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=87626 {ECO:0000313|EMBL:EAR29093.1}; RN [1] {ECO:0000313|EMBL:EAR29093.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=D2 {ECO:0000313|EMBL:EAR29093.1}; 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. {ECO:0000313|EMBL:EAR29093.1}. 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; AAOH01000003; EAR29093.1; -; Genomic_DNA. DR RefSeq; WP_009838354.1; NZ_AAOH01000003.1. DR ProteinModelPortal; A4C928; -. DR EnsemblBacteria; EAR29093; EAR29093; PTD2_08614. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EAR29093.1}; KW Transferase {ECO:0000313|EMBL:EAR29093.1}. SQ SEQUENCE 353 AA; 38615 MW; 883DD1E9E598F8AF CRC64; MPNKDKSAQL KAALQQRILI LDGAMGTMIQ QHKLEEEDYR GERFADWHIL IKGNNDLLTL TQPEIIAKIH RDYLLAGADI IETNTFNSTT ISMEDYEMGH LSREINLESA KLARKVCDEI EALDPSRPRY VAGVLGPTSK TCSISPDVND PGFRNVTFDA LVAAYVESTL ALMEGGADII LIETIFDTLN SKAASFAVEE AFEQAGRTLP VMISGTITDA SGRTLSGQTT EAFYNSIRHI KPIAIGLNCA LGPDLLRQYV EELSRVCETY TSVHPNAGLP NEFGEYDLEA PEMAAEIIDW GKTGFINIVG GCCGTTPLHI KAFADGLANV PPRPLPELEV RMRLSGLEAC NLN // ID A4CPQ9_ROBBH Unreviewed; 1228 AA. AC A4CPQ9; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 01-APR-2015, entry version 57. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EAR14380.1}; GN OrderedLocusNames=RB2501_03110 {ECO:0000313|EMBL:EAR14380.1}; OS Robiginitalea biformata (strain ATCC BAA-864 / HTCC2501 / KCTC 12146). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Robiginitalea. OX NCBI_TaxID=313596 {ECO:0000313|EMBL:EAR14380.1, ECO:0000313|Proteomes:UP000009049}; RN [1] {ECO:0000313|EMBL:EAR14380.1, ECO:0000313|Proteomes:UP000009049} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-864 / HTCC2501 / KCTC 12146 RC {ECO:0000313|Proteomes:UP000009049}; RX PubMed=19767438; DOI=10.1128/JB.01191-09; RA Oh H.M., Giovannoni S.J., Lee K., Ferriera S., Johnson J., Cho J.C.; RT "Complete genome sequence of Robiginitalea biformata HTCC2501."; RL J. Bacteriol. 191:7144-7145(2009). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001712; EAR14380.1; -; Genomic_DNA. DR RefSeq; WP_015755816.1; NC_013222.1. DR RefSeq; YP_003196842.1; NC_013222.1. DR ProteinModelPortal; A4CPQ9; -. DR SMR; A4CPQ9; 648-889. DR STRING; 313596.RB2501_03110; -. DR EnsemblBacteria; EAR14380; EAR14380; RB2501_03110. DR KEGG; rbi:RB2501_03110; -. DR PATRIC; 23337745; VBIRobBif55773_3117. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; RBIF313596:GH7G-3218-MONOMER; -. DR Proteomes; UP000009049; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000009049}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EAR14380.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000009049}; KW Transferase {ECO:0000313|EMBL:EAR14380.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 243 243 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 757 757 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1228 AA; 135635 MW; 54A3024FEE84A17F CRC64; MHNLSDLLTE RILVLDGAMG TMLQRYGFTE ADYRGDRFAD WPQPLQGNND LLSLTQPKAL GEIHRAYLEA GADILETNTF SATSVGMADY GMQEFVYEIN RAAAEIAKRE AEAATRANPA KPRFVAGSLG PTNKTASMSP DVNDPGYRAI DFEALRLAYR EQAAGLLDGG VDLFLVETVF DTLNAKAALF AIEELKSERG IDTPVMVSGT ITDASGRTLS GQTAEAFLVS VSHIPMLSIG LNCALGASQL VPHLEVLSAR AGVAVSAHPN AGLPNAFGEY DQNPAQMARQ VREYLEKGLV NIVGGCCGTT PDHIRALAEL VAEYKPRQIP DGRPRQLKLA GLEPLVITPE SNFVNVGERT NVAGSRKFLR LVKEGNFEEA LEIARDQVDG GAQIIDVNMD DGLIDGKAAM VKYLNLMLAE PDIARVPVMI DSSKWDIIEA GLQVVQGKSV VNSISLKEGE AVFLEQARKI LLYGAAVIVM AFDETGQADN FERRIEIAER SYRLLTEQAG FPPEDIIFDL NIFPVATGME EHRRNALDFI EATRWVRDNL PHCSVSGGVS NVSFSFRGNT PVREAMHSAF LYHAIRAGMN MGIVNPTLLE VYDDIPKELL GYVEDVLLDR REEATERLLE YAETVQGTQK DRKTDMSWRE APLQDRITRA LVKGIDQFIE ADVEEARQAA GKPIEVIEGH LMTGMNVVGD LFGSGKMFLP QVVKSARVMK KAVAYLTPFI EEAKAAQPGS KQAAGKVLMA TVKGDVHDIG KNIVSVVLAC NNYEIVDLGV MVPPERIIEK AREEDVDIIG LSGLITPSLD EMVFLAREME RQGFRVPLLI GGATTSKAHT AVKIDPQYSA AVVHVNDASR AVTVVGDLLQ EERSQEYKKA VKLDYESFRE KFLKRGKIRE YLPLEAARAN RLGLEFGPDQ VHVPRQLGVQ VIESIDLRKL EPFIDWSPFF RSWDLHGKFP DILEDAVVGQ QATALYRDAR EMLKKIFREK SLTARAVFGL FPAVSTRRDD IVIRRDDNRE FSFRTLRQQT KKKQGVPNIA LADFIAPEDS GISDFMGCFC VSAGFGAAEL AREYEDRLDD YNSILVKALA DRLAEAAAEY LHREVRVLHW GYAPGETLDN DALIREAYKG IRPAPGYPAC PDHLEKQTIW EVLQVEETIG VELTESLAMW PAASVSGYYF AHPGARYFGL GKITRDQLED YADRKGIPLE TAEKWLQPNL AEAAATVQ // ID A4CUH0_SYNPV Unreviewed; 1205 AA. AC A4CUH0; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 01-APR-2015, entry version 54. DE SubName: Full=Putative methionine synthase {ECO:0000313|EMBL:EAR18685.1}; GN ORFNames=WH7805_02582 {ECO:0000313|EMBL:EAR18685.1}; OS Synechococcus sp. (strain WH7805). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechococcus. OX NCBI_TaxID=59931 {ECO:0000313|EMBL:EAR18685.1}; RN [1] {ECO:0000313|EMBL:EAR18685.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=WH 7805 {ECO:0000313|EMBL:EAR18685.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EAR18685.1}. 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; AAOK01000003; EAR18685.1; -; Genomic_DNA. DR RefSeq; WP_006041332.1; NZ_CH724168.1. DR ProteinModelPortal; A4CUH0; -. DR EnsemblBacteria; EAR18685; EAR18685; WH7805_02582. DR PATRIC; 29900706; VBISynSp124776_1215. DR PhylomeDB; A4CUH0; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 238 238 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1205 AA; 131827 MW; 0F1BDFF8433C019F CRC64; MQAVQSKPGT ATSRFLQRLH DPSKPVLVFD GATGTSLQQM DLTADDFGGE ALEGCNENLV ITRPDAVQAV HRLFLDAGCD VIETDTFGAA SVVLAEYGLE NQAFELNRRA AELAREMADQ YSSERKPRFV AGSMGPTTKL PTLGHIDFDT LRDSFKEQAA GLLAGDVDLF IIETCQDVLQ IKAALQGVEA AFHASGQRRP LMVSVTMETT GTMLVGSDIA AVVSILEPFP IDVLGLNCAT GPEQMKEHIK YLSEYSPFVV SCIPNAGLPE NIGGVAHYRL TPLELKMQLM HFVEDLGVQV IGGCCGTTPA HIKALSEISE ELKPAQRDVR TRHLERQQLR YEPAASSIYG ATPYFQDNSF LIIGERLNAS GSKKVRELLN EEDWDGLIAV ARGQVKENAH VLDVNVDYVG RDGEKDMHEL VTRVVTNVNL PLMLDSTEWQ KMEAGLKVAG GKCILNSTNY EDGDERFFKV LELARRYGAG VVIGTIDEDG MARTAEKKVA IAKRAYRDAV EFGIPAREIF YDPLALPIST GIEEDRRNGA ETIAAIRRIR SELPGVHVVL GVSNVSFGLS PAARITLNSV FLHDCCEAGM DAAIVSPAKI LPLVKIDADH QQVCRDLIND TRRFDGDACI YDPLTKLTTL FEGVSAKDAR ASGPSLADLP VEERLKQHII DGERIGLEDA LNEGLQTYPP LDIVNTFLLD GMKVVGELFG SGQMQLPFVL QSAETMKAAV AFLEPHMEKS EGKRSAKAKF LIATVKGDVH DIGKNLVDII LTNNGYEVIN LGIKQDVGAI ISAQQKHGAD CIAMSGLLVK STAFMKDNLQ AFNDAGIDVP VVLGGAALTP RFVNKDCSDV YNGKVIYGRD AFTDLRFMDA FVDARKQGHW DNLKGFLNGT PEGISLGGEN EPSSEESSNE GGPASASEEA AALSVTDERS DVVPEEPPLR PEFLGSKVLQ GAEQIPLREV IAYLDRQALF AGQWQMRKAK DQSREDYEAD LKAKAEPILQ TWLERSLNED LLQPAVAYGY FPCGRDGNAV AVFDPDSNDE LGRFALPRQR SGNRYCIADF YRDLSSGHPT DVLPMQAVTM GEKASVFAQK LFEADSYSDY LFFHGLAVQM AEALAEWTHA RIRRECGFAD PDGMPLRDVL AQRYRGSRYS FGYPACPNVA DSRQQLLWLG AERIGLSMDE SDQLHPEQST TALVALHSVA RYFSA // ID A4E8K1_9ACTN Unreviewed; 849 AA. AC A4E8K1; DT 17-APR-2007, integrated into UniProtKB/TrEMBL. DT 17-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 41. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EBA40217.1}; GN ORFNames=COLAER_00742 {ECO:0000313|EMBL:EBA40217.1}; OS Collinsella aerofaciens ATCC 25986. OC Bacteria; Actinobacteria; Coriobacteridae; Coriobacteriales; OC Coriobacterineae; Coriobacteriaceae; Collinsella. OX NCBI_TaxID=411903 {ECO:0000313|EMBL:EBA40217.1}; RN [1] {ECO:0000313|EMBL:EBA40217.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 25986 {ECO:0000313|EMBL:EBA40217.1}; 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] {ECO:0000313|EMBL:EBA40217.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 25986 {ECO:0000313|EMBL:EBA40217.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EBA40217.1}. 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; AAVN02000002; EBA40217.1; -; Genomic_DNA. DR RefSeq; WP_006234686.1; NZ_AAVN02000002.1. DR ProteinModelPortal; A4E8K1; -. DR EnsemblBacteria; EBA40217; EBA40217; COLAER_00742. DR PATRIC; 31035129; VBIColAer81217_0653. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EBA40217.1}; KW Transferase {ECO:0000313|EMBL:EBA40217.1}. SQ SEQUENCE 849 AA; 90010 MW; 8F79CFC8D0360F8D CRC64; MFTPLITHDS DGTALAAPVD AVRRNGATYK TRTIDDLRIK DDRLRAAIEG TGHLLFDGGM GTMLQAAGMK AGALPELLNF EEPQVITDIQ RQYVEAGCDV ITANTFGANA HKLDGAATVA DVFAAAVTCA RAAGAHYVAG DIGPIGALLR PLGTLSFDEA YDLFAEEVRA GVAAGVDLFI IETMTDLAEI KAAVLACREN SDLPVFATMT FEEDGRTFLG TSPEVAAITL DAIGADVLGI NCSQGPAELR GLAARMLTVT DKPVMVQANA GLPHVDDDGN TVFDIQAPEY AEAVAGMIAD GVSVVGGCCG TTPAHMAALR TLIDNHTPSP RHRKPSMSVT SAQTVVDLPC DGHKIAVIGE RINPTGKKRL QQALRDGDLD YVVSQGISQQ EQGADILDVN VGLPEIDEVK IIQQATEQLQ GSTLLPLQID STDPAAVEAA VRRYAGKPII NSVNGKQQIM DEIFPLVAHY GTNVVGLTLD EGGIPDTAEA RFAIAEHIVA EAARYGIGPD RILIDCLVMT ASTNQRQAEQ ILRAMSLCKE RLGVKCALGV SNISFGLPAR PLLGSVFLAA AFGAGLDAPI MNPGSKRFMD TVYSYRVLSV EDEGSTGYIE RYAGWTDPYK IAANPAAAQA ASTDTVPAAG TAGTDDPIRR MVVSGRKGEI AAETERLLAD HDAMDLINNH FIPALDEVGV LFDQGKFFLP QLMASAEAAR VGFDTIKRLM PAGEIADKGK ICVATVKGDI HDIGKNIVKM LLDNYGYTVF DLGRDVDPQE VLKTVKERDI KLVGLSALMT TTVVAMEETI KLLHAEVPGV KIIVGGAVLT PEYAKQIGAD YYAKDAAESA RIAEEVFGQ // ID A4EBI1_9ACTN Unreviewed; 297 AA. AC A4EBI1; DT 17-APR-2007, integrated into UniProtKB/TrEMBL. DT 17-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase protein {ECO:0000313|EMBL:EBA39185.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EBA39185.1}; GN ORFNames=COLAER_01799 {ECO:0000313|EMBL:EBA39185.1}; OS Collinsella aerofaciens ATCC 25986. OC Bacteria; Actinobacteria; Coriobacteridae; Coriobacteriales; OC Coriobacterineae; Coriobacteriaceae; Collinsella. OX NCBI_TaxID=411903 {ECO:0000313|EMBL:EBA39185.1}; RN [1] {ECO:0000313|EMBL:EBA39185.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 25986 {ECO:0000313|EMBL:EBA39185.1}; 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] {ECO:0000313|EMBL:EBA39185.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 25986 {ECO:0000313|EMBL:EBA39185.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EBA39185.1}. 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; AAVN02000007; EBA39185.1; -; Genomic_DNA. DR RefSeq; WP_006235725.1; NZ_AAVN02000007.1. DR ProteinModelPortal; A4EBI1; -. DR EnsemblBacteria; EBA39185; EBA39185; COLAER_01799. DR PATRIC; 31037038; VBIColAer81217_1581. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EBA39185.1}; KW Transferase {ECO:0000313|EMBL:EBA39185.1}. SQ SEQUENCE 297 AA; 31469 MW; AEA8BACC7EC7FE15 CRC64; MDTSYYNRFG AEELTRRLSS ETLLAQGPMG SVLLSEYDAA DIPPAFWNLA EPQTVSRIHR LYVAAGAQVL ITNTFQASSY ALKHDQIAPS VAEVNRGAVD DARQAHPQLL LGSMGPIGIE WFAEDSVEYR EIRGIAREQA HALLNAGVDG LLIETVTSIR NLQPMLAGAR DAADGMPVLV SFVVDDKGDL LGDGLNIEAA VLYAEKHGAN SVGVNCCSLA AANAAVPRMV ASATTPVTVR PNVGDPVQTQ DGPVWHENPE AFARACIEWR HAGAAMVGSC CGTTAITTAA MAEALDI // ID A4EF94_9RHOB Unreviewed; 292 AA. AC A4EF94; DT 17-APR-2007, integrated into UniProtKB/TrEMBL. DT 17-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Homocysteine S-methyltransferase, putative {ECO:0000313|EMBL:EBA13566.1}; GN ORFNames=RCCS2_06754 {ECO:0000313|EMBL:EBA13566.1}; OS Roseobacter sp. CCS2. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseobacter. OX NCBI_TaxID=391593 {ECO:0000313|EMBL:EBA13566.1}; RN [1] {ECO:0000313|EMBL:EBA13566.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCS2 {ECO:0000313|EMBL:EBA13566.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EBA13566.1}. 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; AAYB01000001; EBA13566.1; -; Genomic_DNA. DR RefSeq; WP_008231313.1; NZ_AAYB01000001.1. DR ProteinModelPortal; A4EF94; -. DR EnsemblBacteria; EBA13566; EBA13566; RCCS2_06754. DR PATRIC; 28093964; VBIRosSp4847_0689. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EBA13566.1}; KW Transferase {ECO:0000313|EMBL:EBA13566.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 194 194 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 267 267 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 268 268 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 292 AA; 29945 MW; BA7F248196A5406B CRC64; MTDIILLDGG MGQELVHRAG DRPTPLWSTQ VMIDHPGLVA KVHADYAAAG ATVHTTNTYA ILHDRLDGTG MEDQFAALYT AALKEAEGAG VLAGAIGPLG ASYRPDLMPA HDVAVATYTE VANLLAPKVD LIICETVASV AHARAILEAT VATAKPVWLA LTVDDADGTK LRSGEPLADV FAVAGAADAI LANCSSPEAI SAAIDVLATG DKPFGGYANG FTQISEGFLG DKPTVDALTA RHDLGPDEYA AFAMQWVAQG ATIVGGCCEV GPAHIAKLAD SITAAGHRIV AP // ID A4EKV4_9RHOB Unreviewed; 339 AA. AC A4EKV4; DT 17-APR-2007, integrated into UniProtKB/TrEMBL. DT 17-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=Methionine synthase I {ECO:0000313|EMBL:EBA11851.1}; GN ORFNames=RCCS2_18021 {ECO:0000313|EMBL:EBA11851.1}; OS Roseobacter sp. CCS2. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseobacter. OX NCBI_TaxID=391593 {ECO:0000313|EMBL:EBA11851.1}; RN [1] {ECO:0000313|EMBL:EBA11851.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCS2 {ECO:0000313|EMBL:EBA11851.1}; 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. {ECO:0000313|EMBL:EBA11851.1}. 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; AAYB01000003; EBA11851.1; -; Genomic_DNA. DR ProteinModelPortal; A4EKV4; -. DR EnsemblBacteria; EBA11851; EBA11851; RCCS2_18021. DR PATRIC; 28097886; VBIRosSp4847_2625. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 339 AA; 35156 MW; 6214B79C8DC71893 CRC64; MMTNALSNLL KTRDWLMADG ATGTNLFNMG LMSGDAPEMW NVDETAKIIA LYKGAADAGS DIFLTNSFGA NASRLKLHGA EGRVKELNKA AAELGREVAD ASERVIVVAG SVGPTGEIMA PMGSLTHEIA VEMFHEQAEG LKAGGADVLW VETISAPEEF AAASEAFALA DMPWCGTMSF DTAGRTMMGL TSADMVKKVG KLAHQPFGFG ANCGVGASDL LRTVLGFAAA DPTLPIIAKG NAGIPKYHDG HIHYDGTPAL MADYAVLARD CGATIIGGCC GTTPEHLRAM REALETRPKG ASPSLEAIAQ ALGGFSSASD GTDGAGPAAS PRRGRRRRA // ID A4EQS6_9RHOB Unreviewed; 340 AA. AC A4EQS6; DT 17-APR-2007, integrated into UniProtKB/TrEMBL. DT 17-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Methionine synthase I {ECO:0000313|EMBL:EBA17632.1}; GN ORFNames=RSK20926_17877 {ECO:0000313|EMBL:EBA17632.1}; OS Roseobacter sp. SK209-2-6. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseobacter. OX NCBI_TaxID=388739 {ECO:0000313|EMBL:EBA17632.1}; RN [1] {ECO:0000313|EMBL:EBA17632.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK209-2-6 {ECO:0000313|EMBL:EBA17632.1}; 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. {ECO:0000313|EMBL:EBA17632.1}. 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; AAYC01000002; EBA17632.1; -; Genomic_DNA. DR RefSeq; WP_008204415.1; NZ_AAYC01000002.1. DR ProteinModelPortal; A4EQS6; -. DR EnsemblBacteria; EBA17632; EBA17632; RSK20926_17877. DR PATRIC; 28117809; VBIRosSp102653_0708. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 340 AA; 36115 MW; 3A592A84E6E0FF7A CRC64; MTNTFKTLLA EKDALLADGA TGTNLFKMGL QSGDAPELWN TDEPKKIMAL YQGSVDAGSD LFLTNSFGGT AARLKLHDAQ KRVRELNQAA AELGREVADK SERKIAVAGS VGPTGEIFEP VGPMTHALAV EMFHEQAEAL KEGGADVLWL ETISAPEEFR AAAEAFKLAD MTWCGTMSFD TAGRTMMGVT SADLAQLVEE FDNAPVAFGA NCGTGASDIL RTVLGFAAQG TERPIISKGN AGIPKYVDGH IHYDGTPELM GEYAVMARDS GAKIIGGCCG TMPEHLSSMR EALDTRPRGE RPALEKIVEV LGPFTSASDG TGEDAAEGAE RRRGRGRRRG // ID A4FGI6_SACEN Unreviewed; 297 AA. AC A4FGI6; DT 17-APR-2007, integrated into UniProtKB/TrEMBL. DT 17-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 42. DE SubName: Full=MmuM protein {ECO:0000313|EMBL:CAM03161.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:CAM03161.1}; GN Name=mmuM {ECO:0000313|EMBL:CAM03161.1}; GN OrderedLocusNames=SACE_3890 {ECO:0000313|EMBL:CAM03161.1}; OS Saccharopolyspora erythraea (strain NRRL 23338). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Pseudonocardineae; Pseudonocardiaceae; Saccharopolyspora. OX NCBI_TaxID=405948 {ECO:0000313|EMBL:CAM03161.1, ECO:0000313|Proteomes:UP000006728}; RN [1] {ECO:0000313|EMBL:CAM03161.1, ECO:0000313|Proteomes:UP000006728} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL 23338 {ECO:0000313|Proteomes:UP000006728}; 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 ----------------------------------------------------------------------- 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; CAM03161.1; -; Genomic_DNA. DR RefSeq; WP_009947861.1; NZ_ABFV01000045.1. DR RefSeq; YP_001106086.1; NC_009142.1. DR ProteinModelPortal; A4FGI6; -. DR STRING; 405948.SACE_3890; -. DR EnsemblBacteria; CAM03161; CAM03161; SACE_3890. DR KEGG; sen:SACE_3890; -. DR PATRIC; 23415204; VBISacEry28377_3896. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR Proteomes; UP000006728; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006728}; KW Methyltransferase {ECO:0000313|EMBL:CAM03161.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006728}; KW Transferase {ECO:0000313|EMBL:CAM03161.1}. SQ SEQUENCE 297 AA; 31088 MW; 986D932351323972 CRC64; MPFPDLCSSA PLVLDGGLAT ELEARGHDLS DELWSARLLH DAPEEIVAAH EAFFRAGAVI ATTASYQASF PGFGARGIGR GDAAALMRRS VELARQAAER LEPDRPRWVA ASVGPYGATL ADGSEYRGRY GLTVSDLVGF HRPRLEVLAG AGPDVLALET VPDLDEAIAL VEAVDGIGVP AWLSYTVADG RTRAGQPLAE AFEVARDHED IVAVGVNCCS PAEVAPALAI ARQVTGKPVV AYPNSGEDWD AHCRTWTGAS RFPGTAASAW AHEGAAVIGG CCRVRPDDIA DLAATLP // ID A4FGJ4_SACEN Unreviewed; 1189 AA. AC A4FGJ4; DT 17-APR-2007, integrated into UniProtKB/TrEMBL. DT 17-APR-2007, sequence version 1. DT 27-MAY-2015, entry version 65. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CAM03169.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAM03169.1}; GN Name=metH {ECO:0000313|EMBL:CAM03169.1}; GN OrderedLocusNames=SACE_3898 {ECO:0000313|EMBL:CAM03169.1}; OS Saccharopolyspora erythraea (strain NRRL 23338). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Pseudonocardineae; Pseudonocardiaceae; Saccharopolyspora. OX NCBI_TaxID=405948 {ECO:0000313|EMBL:CAM03169.1, ECO:0000313|Proteomes:UP000006728}; RN [1] {ECO:0000313|EMBL:CAM03169.1, ECO:0000313|Proteomes:UP000006728} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL 23338 {ECO:0000313|Proteomes:UP000006728}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AM420293; CAM03169.1; -; Genomic_DNA. DR RefSeq; WP_009947851.1; NZ_ABFV01000045.1. DR RefSeq; YP_001106094.1; NC_009142.1. DR ProteinModelPortal; A4FGJ4; -. DR STRING; 405948.SACE_3898; -. DR EnsemblBacteria; CAM03169; CAM03169; SACE_3898. DR KEGG; sen:SACE_3898; -. DR PATRIC; 23415220; VBISacEry28377_3904. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR Proteomes; UP000006728; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006728}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAM03169.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006728}; KW Transferase {ECO:0000313|EMBL:CAM03169.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 229 229 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 296 296 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 739 739 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1189 AA; 130546 MW; 1ABA9CEA47A0176B CRC64; MADRKNDPSG FLAAIGERVL VADGGMGTAL QAYDLSLDDF ANLEGCNEIL NETRPDVVSS VYRGFLEAGS DAIETNTFGT NLANLGEYGI PERIRDLAEK GTRLAREAAD EYSTPDKPRF VLGSMGPGTK LPTLGHAPYA DLRDAYVENV LGMIDGGIDV VLVETSQDLL QTKAAIVAAK RAMEQTGRWL PIIAQVTVEQ TGTMLVGSEI GAALTALEPL GIDMIGMNCA TGPAEMSEHL RVLSQHARVP ISVMPNAGLP ELGPNGAVYP LKADELAEAL AGFVTNFGAR LVGGCCGTTG EHVRAVSEAV ASLTPPERTP EVIPSVSSMY QTVPFEQDAS ILNVGERTNA NGSKAFREAM LEERYEDCVE IAKAQTREGA HMLDLCVDYV GRDGTKDMRE LASRLATAST LPIMVDSTEP DVIQAGLEHL GGRCAVNSVN YEDGTEPGGR FQRVMEMVRE HGATVVVTCI DEEGQARTRD WKLRVAERMI EDLTTNWGLE KSAIIIDCLV FPITTGQEEV RKDGIETIEA IRELKKRHPD VQTTLGLSNV SFGLNPAARQ VLNSVFLNEC REAGLDSAIV NSSKILPMTK IDEEPRKVAL DLVYDRRSEG YDPLQKLMEL FEGQTAKSSS ASRAEELAKL PLFERLEKRI VDGERNGLEA DLEAAMQEKP PLEIINQNLL GGMKIVGDLF GSGQMQLPFV LQSAEVMKAA VAHLEPHMEK DDSGGKGRLL LATVKGDVHD IGKNLVDIIV SNNGYEVVNI GIKQPINAIL DAAEEHKVDA IGMSGLLVKS TVIMKENLEE MNSRGIAEKY PVMLGGAALT RSYVENDLDE VYQGDVRYAK DAFEGLHLMD RMMAVKRGET PEEDEAEAAK KAERKARRER SLRIAEKRKA AEGDIPDLYD ESTRSDVDAD APVPAPPFWG SKVIKGVPVA DYLALLDERA TFFGQWGLRG SKKGEGPTYE ELVESEGRPR LRYWIDELAT AGILQHAAVV YGYFPVISEG NSLIVLDKEE PDAPERTRFT FPRQQRDRRL CLADFFRSRE KAEQTGQVDV LPMQLVTMGQ PIADYANELF AKNSYRDYLE IHGMGVQLTE ALAEYWHRRI RRELQFSGGA SAADQDPADV LEFFKLGYRG ARFSFGYGAC PEIEDRAKIV ELLESERIGV VLSEEFQLHP EQSTDAIVCH HPEAKYFNT // ID A4G1H3_HERAR Unreviewed; 1252 AA. AC A4G1H3; DT 17-APR-2007, integrated into UniProtKB/TrEMBL. DT 17-APR-2007, sequence version 1. DT 29-APR-2015, entry version 66. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CAL60360.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAL60360.1}; GN Name=metH {ECO:0000313|EMBL:CAL60360.1}; GN OrderedLocusNames=HEAR0124 {ECO:0000313|EMBL:CAL60360.1}; OS Herminiimonas arsenicoxydans. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae; Herminiimonas. OX NCBI_TaxID=204773 {ECO:0000313|EMBL:CAL60360.1, ECO:0000313|Proteomes:UP000006697}; RN [1] {ECO:0000313|EMBL:CAL60360.1, ECO:0000313|Proteomes:UP000006697} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ULPAs1 {ECO:0000313|Proteomes:UP000006697}; 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 N., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CU207211; CAL60360.1; -; Genomic_DNA. DR RefSeq; WP_011869709.1; NC_009138.1. DR RefSeq; YP_001098489.1; NC_009138.1. DR ProteinModelPortal; A4G1H3; -. DR SMR; A4G1H3; 660-918. DR STRING; 204773.HEAR0124; -. DR EnsemblBacteria; CAL60360; CAL60360; HEAR0124. DR KEGG; har:HEAR0124; -. DR PATRIC; 22110448; VBIHerArs17568_0124. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; HARS204773:GJCA-121-MONOMER; -. DR Proteomes; UP000006697; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006697}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAL60360.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006697}; KW Transferase {ECO:0000313|EMBL:CAL60360.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 255 255 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 320 320 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 778 778 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1252 AA; 137886 MW; DC216FFA6FCDDE5D CRC64; MKRDAISPTE TLLRDLMARR ILILDGAMGT MIQQYKLTEE DYRGTRFADF AVPGKEVFVK GNNELLSLTQ PHVISEIHEK YLAAGADLIE SNTFGATTVA QDDYHMGHLA YEMNVASARL ARAACDKYST PDKPRFVAGA LGPTPKTASI SPDVNDPAAR NVTFDQLVAS YLEQTRGLVE GGADVLLVET IFDTLNCKAA LFAIDQFFEE SGQRLPIMIS GTVTDASGRI LSGQTVPAFW HSIRHARPLT VGLNCALGAA LMRPYAEELS KIADTFVCIY PNAGLPNPMS DTGFDETPDV TSSLLKDFAE SGFVNIAGGC CGTTPDHIKA IADTVANIAP RIVPTIEPTM KLSGLEPFII DDNSLFVNVG ERTNVTGSKA FARLIINEKY DEALTVARQQ VENGAQIIDI NMDEAMLDSE AAMTRFLNSV ASEPDIARVP IMIDSSKWSV IEAGLKCVQG KAIVNSISMK EGEEKFLHDA KLCRRYGAAV IVMAFDEKGQ ADTFERKIEI CERAYWLLVN EVDFPPEDII FDPNIFAIAT GIEEHNNYAV DFINSVRWIK ENLPHAKISG GVSNVSFSFR GNDPAREAIH TVFLYHAIKA GMTMGIVNAG MVGVYDNLPA ELKECVEDVV LNRREDATER MIEIAATLKA GDKKEEATLE WRSGTVQQRL AHALVQGITQ WIVEDTEEAR QELLKNGGRP IHVIEGPLMD GMNIVGDLFG QGKMFLPQVV KSARVMKQAV AHLIPFIEEE KRLLQEQTGI VSKPKGKIVI ATVKGDVHDI GKNIVSVVLQ CNNFEVVNMG VMVPCSEILA RAKAENADII GLSGLITPSL EEMAYVAKEM QRDEYFRGLK TPLLIGGATT SRAHTAVKIA HNYDGPVVYV PDASRSVSVA QSLLTPESRD QYIADIATDY ERIRVQHANK KTLPMLSLEQ ARANKMQVEF TGKYAPVKPK FIGRRVFKNV DLATIAQYID WGPFFQTWDL AGPYPAILTD EVVGDAATKV FAEGQALLKK IIEGRWLTAN GVIALLPANT VNDDDIEVYT DETRTQVAFT YYGVRQQTVK PIIDGVQRPN QCLADFIAPK SSGIADYIGL FAVTAGLGIE KYEKRFEDAY DDYSSIMLKS LADRLAEAFA EQLHERVRTD LWGYVPDEAL SNEAMIKEEY LGIRPAPGYP ACPEHTVKAE MFKTLQAEEI GMMLTDSFAM FPGAAVSGFY FAHPEAKYFV VGKIGEDQVK DMVLRRGVSQ EDIERWLAPN LS // ID A4H4V2_LEIBR Unreviewed; 1249 AA. AC A4H4V2; DT 01-MAY-2007, integrated into UniProtKB/TrEMBL. DT 01-MAY-2007, sequence version 1. DT 29-APR-2015, entry version 60. DE SubName: Full=Complete genome, chromosome 7 {ECO:0000313|EMBL:CAM41620.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAM41620.1}; GN ORFNames=LBRM_07_0090 {ECO:0000313|EMBL:CAM41620.1}; OS Leishmania braziliensis. OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; OC Leishmaniinae; Leishmania; Leishmania braziliensis species complex. OX NCBI_TaxID=5660 {ECO:0000313|Proteomes:UP000007258}; RN [1] {ECO:0000313|EMBL:CAM41620.1, ECO:0000313|Proteomes:UP000007258} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM41620.1, RC ECO:0000313|Proteomes:UP000007258}; RX PubMed=17572675; DOI=10.1038/ng2053; RA Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A., RA Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A., RA Fraser A., Rajandream M.A., Carver T., Norbertczak H., RA Chillingworth T., Hance Z., Jagels K., Moule S., Ormond D., Rutter S., RA Squares R., Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., RA Thurston S., Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., RA Depledge D.P., Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R., RA Barrell B., Cruz A.K., Mottram J.C., Smith D.F., Berriman M.; RT "Comparative genomic analysis of three Leishmania species that cause RT diverse human disease."; RL Nat. Genet. 39:839-847(2007). RN [2] {ECO:0000313|EMBL:CAM41620.1, ECO:0000313|Proteomes:UP000007258} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM41620.1, RC ECO:0000313|Proteomes:UP000007258}; RX PubMed=22038252; DOI=10.1101/gr.122945.111; RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A., RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D., RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F., RA Hertz-Fowler C., Mottram J.C.; RT "Chromosome and gene copy number variation allow major structural RT change between species and strains of Leishmania."; RL Genome Res. 21:2129-2142(2011). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; FR798981; CAM41620.1; -; Genomic_DNA. DR RefSeq; XP_001562504.1; XM_001562454.2. DR ProteinModelPortal; A4H4V2; -. DR SMR; A4H4V2; 661-912. DR GeneID; 5412880; -. DR KEGG; lbz:LBRM_07_0090; -. DR InParanoid; A4H4V2; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR Proteomes; UP000007258; Chromosome 7. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007258}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAM41620.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007258}; KW Transferase {ECO:0000313|EMBL:CAM41620.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 251 251 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 315 315 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 779 779 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1249 AA; 138231 MW; 23835D37B78CEA61 CRC64; MRGERSPAFE ELEELFQKRI LILDGGMGTM LQRYKLEEAD FRGEEFKNAT KEVKGNNDLL CLTQPVKVWD VHYKYAVAGA DILGTNTFNA QAVSQSDYET QHLVRRINLA AAKICRDAAD QASCETGRRI FVAGVLGPLN RTASISPSVE RPDYRNITYD EIVAAYTEQA TALLEGGVDV LMVETIFDSL NAKAALFALN TLFDDAGYTR VPIMVSGTIT DLSGRTLSGQ TVEAFYLSMR HGNIISIGLN CALGCREMRP YIQRLAQISE GYVTCYPNAG LPNAMGGYDE PPEDMARDMN DFATNGWVNL VGGCCGTTPD HIHAMAMAVK SIPPRPKGQR STTLAISGLE PLYFTNHIGF CNIGERCNLS GSLKFKRLVK EGKWEECLEV ARKQVEEGAM VLDVNMDDGL IDGVAAMTRF LNLLASDPDV ARVPVMIDSS KFHVIEAGLK CTQGTPIVNS ISLKVGKEEF LRQARLIRRY GAAVVVMAFD ENGQASDYDS KIRICKRAYD MLVADGFPAE NIVFDPNVLT ICTGMEEHNN YAVDFMNAAA WIKANLPGAK VSGGISNLSF SFRGFEVIRM AMHSAFLKKM IADGSLDMAI VNAGALPVYT DIEPGLLQLV EDAIYNRTPD SSERILEYAD RLKAEAAARG GAEEAKVTKV DEWRNAPVEE RLLHALIKGI VEFIENDVEE ARTCGKYERP LHIIEGPLMD GMGKVGELFG SGKMFLPQVI KSARVMKKAV AVLVPYMEAE KLALIDSPKG KSVSRSKRVL MATVKGDVHD IGKNIVGVVL GCNSYEVIDL GVMVSCEKIL AAAKEYDVDV IGLSGLITPS LDEMVHVAKE MKKMGFKIPL MVGGATTSKQ HTAVKIQPHY HKTVHVLDAS KSVVTVANML GSNNEEFWEE VHETYQEIAE DYLANQKDRV YKPLAFCREN ALKIDFVANP PAPRPRKLGT ITISDYPLEK IVSRIDWSPF FSVWQVRGTY PNRGFPKLFN CPTVGVEAKR LFDDAQEMIK DIIATRSFRA KAVVKLMPVN SVGDDIEVYE DDTRVEKIAT FFGLRQQAEK ERGEPYLCIS DFIAPKGVAP DYLGSLVVGI FGADKMSEQY EKDNDGYRSI MIKALADRFA EAFTEEVHRI IRTDLWGFVE RETSETADLI QMQYQGIRPA PGYPSQPDHT EMATIWRLGE VEERTGVKLS ESYAMMPAAS VSALVFAHAQ SKYFAVGKIQ KDQAKDYAAR KGWYLDRVES QLSSSLAYD // ID A4HQE8_LEIBR Unreviewed; 320 AA. AC A4HQE8; DT 01-MAY-2007, integrated into UniProtKB/TrEMBL. DT 01-MAY-2007, sequence version 1. DT 29-APR-2015, entry version 43. DE SubName: Full=Complete genome, chromosome 36 {ECO:0000313|EMBL:CAM44414.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:CAM44414.1}; GN ORFNames=LBRM_35_6610 {ECO:0000313|EMBL:CAM44414.1}; OS Leishmania braziliensis. OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; OC Leishmaniinae; Leishmania; Leishmania braziliensis species complex. OX NCBI_TaxID=5660 {ECO:0000313|Proteomes:UP000007258}; RN [1] {ECO:0000313|EMBL:CAM44414.1, ECO:0000313|Proteomes:UP000007258} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM44414.1, RC ECO:0000313|Proteomes:UP000007258}; RX PubMed=17572675; DOI=10.1038/ng2053; RA Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A., RA Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A., RA Fraser A., Rajandream M.A., Carver T., Norbertczak H., RA Chillingworth T., Hance Z., Jagels K., Moule S., Ormond D., Rutter S., RA Squares R., Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., RA Thurston S., Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., RA Depledge D.P., Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R., RA Barrell B., Cruz A.K., Mottram J.C., Smith D.F., Berriman M.; RT "Comparative genomic analysis of three Leishmania species that cause RT diverse human disease."; RL Nat. Genet. 39:839-847(2007). RN [2] {ECO:0000313|EMBL:CAM44414.1, ECO:0000313|Proteomes:UP000007258} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM44414.1, RC ECO:0000313|Proteomes:UP000007258}; RX PubMed=22038252; DOI=10.1101/gr.122945.111; RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A., RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D., RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F., RA Hertz-Fowler C., Mottram J.C.; RT "Chromosome and gene copy number variation allow major structural RT change between species and strains of Leishmania."; RL Genome Res. 21:2129-2142(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; FR799010; CAM44414.1; -; Genomic_DNA. DR RefSeq; XP_001569273.1; XM_001569223.1. DR GeneID; 5420257; -. DR KEGG; lbz:LBRM_35_6610; -. DR InParanoid; A4HQE8; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR Proteomes; UP000007258; Chromosome 36. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007258}; KW Methyltransferase {ECO:0000313|EMBL:CAM44414.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007258}; KW Transferase {ECO:0000313|EMBL:CAM44414.1}. SQ SEQUENCE 320 AA; 34491 MW; 20CA841D3CB6E7FA CRC64; MEAYLADPKH VVMLDGGLGT ELEARGCNLL DPLWSGEVLL KSPQKIQDVE LAYLQAGARC LITASYQITP KSLMEHRLLT EEAAVAVIEE SVRIAQVVRE RYVKENPQAE PVFVAGSVGP YGAYLADGSE YRGDYVRSAE EFKEFHRARI AALLRAGVDV LAIETQASAA EVHAIVALLQ EEHPNCRAWV SFTTSRTSPV KAISDDTTWA EIIPFLEMSP QVVAVGVNCI PMAEASAVLA HLHTLTTMPL VVYTNSGESY NPATKTWHPI AMADGTTLSL AALAPEWASQ GARIIGGCCR TRPSDIAGAA AALRSACFIE // ID A4HT60_LEIIN Unreviewed; 1252 AA. AC A4HT60; DT 01-MAY-2007, integrated into UniProtKB/TrEMBL. DT 01-MAY-2007, sequence version 1. DT 29-APR-2015, entry version 60. DE SubName: Full=Putative cobalamin-dependent methionine synthase {ECO:0000313|EMBL:CAM65605.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAM65605.1}; GN ORFNames=LINJ_07_0240 {ECO:0000313|EMBL:CAM65605.1}; OS Leishmania infantum. OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; OC Leishmaniinae; Leishmania. OX NCBI_TaxID=5671 {ECO:0000313|Proteomes:UP000008153}; RN [1] {ECO:0000313|EMBL:CAM65605.1, ECO:0000313|Proteomes:UP000008153} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JPCM5 {ECO:0000313|EMBL:CAM65605.1, RC ECO:0000313|Proteomes:UP000008153}; RX PubMed=17572675; DOI=10.1038/ng2053; RA Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A., RA Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A., RA Fraser A., Rajandream M.A., Carver T., Norbertczak H., RA Chillingworth T., Hance Z., Jagels K., Moule S., Ormond D., Rutter S., RA Squares R., Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., RA Thurston S., Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., RA Depledge D.P., Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R., RA Barrell B., Cruz A.K., Mottram J.C., Smith D.F., Berriman M.; RT "Comparative genomic analysis of three Leishmania species that cause RT diverse human disease."; RL Nat. Genet. 39:839-847(2007). RN [2] {ECO:0000313|EMBL:CAM65605.1, ECO:0000313|Proteomes:UP000008153} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JPCM5 {ECO:0000313|EMBL:CAM65605.1, RC ECO:0000313|Proteomes:UP000008153}; RX PubMed=22038252; DOI=10.1101/gr.122945.111; RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A., RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D., RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F., RA Hertz-Fowler C., Mottram J.C.; RT "Chromosome and gene copy number variation allow major structural RT change between species and strains of Leishmania."; RL Genome Res. 21:2129-2142(2011). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; FR796439; CAM65605.1; -; Genomic_DNA. DR RefSeq; XP_001463251.1; XM_001463214.1. DR ProteinModelPortal; A4HT60; -. DR SMR; A4HT60; 664-915. DR STRING; 5671.LinJ07.0400; -. DR GeneID; 5066609; -. DR KEGG; lif:LINJ_07_0240; -. DR eggNOG; COG1410; -. DR InParanoid; A4HT60; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR Proteomes; UP000008153; Chromosome 7. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008153}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAM65605.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008153}; KW Transferase {ECO:0000313|EMBL:CAM65605.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 254 254 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 318 318 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 782 782 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1252 AA; 138719 MW; 2EC6F3557BC7ECEA CRC64; MSAMHGERSP VFEELEEIFQ KRILVLDGGM GTMLQRYKLE EKDFRGEEFK NATKDLKGNN DLLCLTQPAK VQDVHYKYAI AGADVMETNT FNSQAVSQSD YETQHLVRRI NLAAAKICRD AAEQASRETG RRIFVAGVLG PLNRTASISP SVERPDYRNI TYDEIVAAYT EQATALLDGG VDVLLIETIF DSLNAKAALF AVNTLFEDKG YTRVPIMVSG TITDLSGRTL SGQTVDAFYS SMRHGNIISI GLNCALGCRE MRPYVERLAE ISEAYVTCHP NAGLPNAMGE YDELPEDMAR DIRDFAVNGW VNLVGGCCGT TPDHIRAIAT AVKGIPPRLR GQPSETMVIS GLEALYFTHH IGFCNIGERC NISGSLKFKR LVKEGKWEEC LAVARQQVEE GAMVLDVNMD DGLIDGVTAM TRFLNMIASD PEVARVPVMI DSSKFHVIEA GLKCTQGTPI VNSISLKVGE EEFLRQARLI RRYGAAVVVM AFDENGQAAD YASKTRICKR AYDMLVADGF PPENIVFDPN VLTICTGMEE HNNYAIDFMN AAAWIKANLP RAKVSGGISN LSFSFRGFEA IRMAMHSAFL KKMIADGSLD MAIVNAGALP VYTDIEPDLL QLVEDAIYNR TPHSSERILE YAERLKAEKA SGGGAEEAKV SKVDEWRNAS VEERLSHALI KGIVEFIEDD VEEARTCGKY ERPLHIIEGP LMDGMGKVGE LFGSGKMFLP QVIKSARVMK KAVAVLVPYM EAEKAALMAD TNGASTSRAK RVLMATVKGD VHDIGKNIVG VVLGCNSYEV IDLGVMVSCE KILAAAKEHD VHVIGLSGLI TPSLDEMVHV AKEMKRMGFG IPLMVGGATT SKQHTAVKIQ PHYNKTVHVL DASKAVVTVS NMLGSSEEEF WEEVRETYQE IAEDYLANLK DRVYKPLAFC RENALKIDFV ANPPAPRPRK LGTITISDYS LEMIATRIDW NPFFSVWQVR GTYPNRGFPK LFNCPTVGAE AKRLFDDAQE MLKDIIATRS FRAKAVVTLM PVNSVGDDIE VYKDDTRNEK IATFFGLRQQ SEKERGEPYL CISDFIAPKG VAPDYLGSLA VGIFGADKMS EQYEKDNDSY RSIMIKALAD RFAEAFTEEM HRIIRTDLWG YAEKETAETV DLIRMQYQGI RPAPGYPSQP DHTEMDTMWR IGEVEERTGV RLSESYAMMP AASVSALVFA HAQSKYFAVG KIQKDQVKDY AERKGWNLDR AESQLSSSLA YN // ID A4IE37_LEIIN Unreviewed; 199 AA. AC A4IE37; DT 01-MAY-2007, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 2. DT 29-APR-2015, entry version 38. DE SubName: Full=Putative homocysteine S-methyltransferase {ECO:0000313|EMBL:CAM73127.2}; DE EC=2.1.1.10 {ECO:0000313|EMBL:CAM73127.2}; DE Flags: Fragment; GN ORFNames=LINJ_36_6570 {ECO:0000313|EMBL:CAM73127.2}; OS Leishmania infantum. OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; OC Leishmaniinae; Leishmania. OX NCBI_TaxID=5671 {ECO:0000313|Proteomes:UP000008153}; RN [1] {ECO:0000313|EMBL:CAM73127.2, ECO:0000313|Proteomes:UP000008153} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JPCM5 {ECO:0000313|EMBL:CAM73127.2, RC ECO:0000313|Proteomes:UP000008153}; RX PubMed=17572675; DOI=10.1038/ng2053; RA Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A., RA Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A., RA Fraser A., Rajandream M.A., Carver T., Norbertczak H., RA Chillingworth T., Hance Z., Jagels K., Moule S., Ormond D., Rutter S., RA Squares R., Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., RA Thurston S., Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., RA Depledge D.P., Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R., RA Barrell B., Cruz A.K., Mottram J.C., Smith D.F., Berriman M.; RT "Comparative genomic analysis of three Leishmania species that cause RT diverse human disease."; RL Nat. Genet. 39:839-847(2007). RN [2] {ECO:0000313|EMBL:CAM73127.2, ECO:0000313|Proteomes:UP000008153} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JPCM5 {ECO:0000313|EMBL:CAM73127.2, RC ECO:0000313|Proteomes:UP000008153}; RX PubMed=22038252; DOI=10.1101/gr.122945.111; RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A., RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D., RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F., RA Hertz-Fowler C., Mottram J.C.; RT "Chromosome and gene copy number variation allow major structural RT change between species and strains of Leishmania."; RL Genome Res. 21:2129-2142(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; FR796468; CAM73127.2; -; Genomic_DNA. DR RefSeq; XP_001470006.2; XM_001469969.2. DR STRING; 5671.LinJ36.6760; -. DR GeneID; 5074118; -. DR KEGG; lif:LINJ_36_6570; -. DR eggNOG; COG2040; -. DR InParanoid; A4IE37; -. DR KO; K00547; -. DR Proteomes; UP000008153; Chromosome 36. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008153}; KW Methyltransferase {ECO:0000313|EMBL:CAM73127.2}; KW Reference proteome {ECO:0000313|Proteomes:UP000008153}; KW Transferase {ECO:0000313|EMBL:CAM73127.2}. FT NON_TER 199 199 {ECO:0000313|EMBL:CAM73127.2}. SQ SEQUENCE 199 AA; 21661 MW; A0A8B7D2BB1202F6 CRC64; MECSSLFVSH LPHPTGIGCN PVSTVVAGTR AARARTHFTH MENHHFLCWG LLANWKVGGM EAYLADPNQV VMLDGGLATE LETRGCDLLD PLWSGKVLLE SPQRIRDVAL AYLRAGARCI ITASYQITPQ SLMEHRGLTE DAAVAAIEES VRIAQSVRER HLKEKPQAAP VFVAGSVGPY GAYLADGSEY RGDYVRSAE // ID A4IKZ9_GEOTN Unreviewed; 1136 AA. AC A4IKZ9; DT 01-MAY-2007, integrated into UniProtKB/TrEMBL. DT 01-MAY-2007, sequence version 1. DT 27-MAY-2015, entry version 65. DE SubName: Full=5-methyltetrahydrofolate S-homocysteine methyltransferase {ECO:0000313|EMBL:ABO66003.1}; GN Name=metH {ECO:0000313|EMBL:ABO66003.1}; GN OrderedLocusNames=GTNG_0621 {ECO:0000313|EMBL:ABO66003.1}; OS Geobacillus thermodenitrificans (strain NG80-2). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=420246 {ECO:0000313|EMBL:ABO66003.1, ECO:0000313|Proteomes:UP000001578}; RN [1] {ECO:0000313|EMBL:ABO66003.1, ECO:0000313|Proteomes:UP000001578} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NG80-2 {ECO:0000313|EMBL:ABO66003.1, RC ECO:0000313|Proteomes:UP000001578}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000557; ABO66003.1; -; Genomic_DNA. DR RefSeq; WP_008879056.1; NC_009328.1. DR RefSeq; YP_001124748.1; NC_009328.1. DR ProteinModelPortal; A4IKZ9; -. DR STRING; 420246.GTNG_0621; -. DR EnsemblBacteria; ABO66003; ABO66003; GTNG_0621. DR KEGG; gtn:GTNG_0621; -. DR PATRIC; 21977535; VBIGeoThe136879_0652. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; GTHE420246:GIXT-693-MONOMER; -. DR Proteomes; UP000001578; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001578}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABO66003.1}; KW Transferase {ECO:0000313|EMBL:ABO66003.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 724 724 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1136 AA; 125283 MW; 62D2CE76885A0456 CRC64; MANITLEQQL QRKILVIDGA MGTMIQSANL SASDFGGEAY EGCNEYLTLT APHVIRHIHE AYLEAGADII ETNTFGATRI VLDEYGLGHL ALELNIEAAK LAKQAAELFS TPDWPRFVAG SMGPTTKTLS VTGGATFDEL VTAYEEQARG LLLGGVDLLL LETCQDTLNV KAGFIGISKA FEAVGRRVPL MISGTIEPMG TTLAGQAIDS FFISIRHMNP IAVGLNCATG PEFMTDHLRT LSTLADTAVS CYPNAGLPDE EGHYHETPDM LAEKIRRFAE KGWINIVGGC CGTTPDHIRA IAEAVRDLPP RVIPSSFDIH AVSGIEALMY DETMRPLFVG ERTNVIGSRK FKRLIAEGKY EEAAEIARAQ VKNGAHVIDI CLADPDRDER YDMEQFVRHV IKKVKVPLVI DSTDERVIEC ALTYSQGKAI INSINLEDGE ERFAKIAPLL HQYGAAVVVG TIDEQGMAIT AERKLEIALR SYDLLVNRYG VPAQDIIFDP LVFPVGTGDE QYIGAAKETI EGIRLIKERL PDCLTMLGIS NVSFGLPPAG REVLNSVFLY HCTQAGLDYA IVNTEKLERF ASIPENEVRM AEALLFDTSD ETLNAFIEFY RSKITTAKPV ETNLSLEERL ARYVIEGSKD GLIPDLEQAL ETYSDPLSII NGPLMAGMDE VGRLFNNNQL IVAEVLQSAE VMKAAVAFLE PYMEKKEGST KGKVLLATVK GDVHDIGKNL VDIILSNNGY EVVDLGIKVA PQQLIEAARQ HEPDIIGLSG LLVKSAQQMV VTAQDLRQAG ISTPILVGGA ALTRKFTENK IAPEYDGIVL YAKDAMDGLA LANQIQQGTI DYMKKERVEN EPARAVGAAT AVKSNVSTDV PVYIPADLDR HVLRDVPLGH VLPYVNWQMV LGHHLGLKGK VKRLLEEKDE KALALKAVVD ELLAEVQERG WIQPAGVYRF FPAQSDGNRV YIYDPVDRQT VLETFDFPRQ PRAPFLCLAD YLKSKESGEI DYVGFFAVTA GGGIRELAQR WKDEGEFLKS HAIQALALEI AEGFAERIHQ IMRDRWGFPD DPDFTMEERF AAKYQGQRYS FGYPACPNLE DQEKLFRLLH PEDIGIRLTD GYMMEPEASV SAIVFAHPEA RYFNVL // ID A4IL00_GEOTN Unreviewed; 616 AA. AC A4IL00; DT 01-MAY-2007, integrated into UniProtKB/TrEMBL. DT 01-MAY-2007, sequence version 1. DT 01-APR-2015, entry version 58. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=GTNG_0622 {ECO:0000313|EMBL:ABO66004.1}; OS Geobacillus thermodenitrificans (strain NG80-2). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=420246 {ECO:0000313|EMBL:ABO66004.1, ECO:0000313|Proteomes:UP000001578}; RN [1] {ECO:0000313|EMBL:ABO66004.1, ECO:0000313|Proteomes:UP000001578} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NG80-2 {ECO:0000313|EMBL:ABO66004.1, RC ECO:0000313|Proteomes:UP000001578}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ABO66004.1; -; Genomic_DNA. DR RefSeq; WP_011886902.1; NC_009328.1. DR RefSeq; YP_001124749.1; NC_009328.1. DR ProteinModelPortal; A4IL00; -. DR STRING; 420246.GTNG_0622; -. DR EnsemblBacteria; ABO66004; ABO66004; GTNG_0622. DR KEGG; gtn:GTNG_0622; -. DR PATRIC; 21977537; VBIGeoThe136879_0653. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; GTHE420246:GIXT-694-MONOMER; -. DR Proteomes; UP000001578; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001578}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 616 AA; 67558 MW; 5D52F6676D2850DC CRC64; MGLLDELKQR VLIADGAMGT LLYSHGIDRC FEELNLSKPE EIVHIHEAYI AAGADVIQTN TYGANYVKLA RYGLEDEVPS INRAAVRLAK QAANGRTHVL GTIGGLRTLN KSAVPLEEVK RTFREQLFVL LAEGVDGVLL ETYYDLEELE TVLTIARKET TLPIIAHVSL HEVGVLQDGT PLADALARLE ALGADVVGLN CRLGPYHMLQ SLEEVPLPTR AFLSAYPNAS LPDYRDGRLV YETNAEYFEE TAKAFRDQGV RLIGGCCGTT PKHIEAMARA LQDRKPVTKK TVKRRAVSVS VQADNPSAVT PLSELARTRR SVIVELDPPK QLGIDKFLVG AKALHDAGID ALTLADNSLA TPRISNVAVG SIVKEQLGVR PLIHITCRDR NLIGLQSHLM GLHTLGITDV LAITGDPSKI GDFPGATSVY DLSSFDLIRL ISQFNEGLSY SGKPLGQKTN FSIGAAFNPN VRHLDKAVER MEKKIQCGAH YFLTQPVYSE EKIVEVYEAT KHLHTPIYIG IMPLVSARNA DFLHHEVPGI TLSDEIRARM AACGNDPVQA TREGIAIAKA LIDAAFDLFN GIYLITPFLR YDMTVELIRY IHEKEAAAKE RKVVHG // ID A4J5C2_DESRM Unreviewed; 598 AA. AC A4J5C2; DT 01-MAY-2007, integrated into UniProtKB/TrEMBL. DT 01-MAY-2007, sequence version 1. DT 29-APR-2015, entry version 54. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=Dred_1750 {ECO:0000313|EMBL:ABO50275.1}; OS Desulfotomaculum reducens (strain MI-1). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfotomaculum. OX NCBI_TaxID=349161 {ECO:0000313|EMBL:ABO50275.1, ECO:0000313|Proteomes:UP000001556}; RN [1] {ECO:0000313|EMBL:ABO50275.1, ECO:0000313|Proteomes:UP000001556} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MI-1 {ECO:0000313|EMBL:ABO50275.1, RC ECO:0000313|Proteomes:UP000001556}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ABO50275.1; -; Genomic_DNA. DR RefSeq; WP_011878089.1; NC_009253.1. DR RefSeq; YP_001113100.1; NC_009253.1. DR ProteinModelPortal; A4J5C2; -. DR STRING; 349161.Dred_1750; -. DR EnsemblBacteria; ABO50275; ABO50275; Dred_1750. DR KEGG; drm:Dred_1750; -. DR PATRIC; 21729691; VBIDesRed82656_1919. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00548; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; DRED349161:GHP6-1805-MONOMER; -. DR Proteomes; UP000001556; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001556}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000001556}. SQ SEQUENCE 598 AA; 66682 MW; D39623C99B2F5AA0 CRC64; MIREYLKNNI LITDGAMGTY YAQITGKYNV FPEFANINEP EIIERIHTEY INAGAKLIKT NTFSANSRVL KIPKSEVKKI VLAGLDLANK VAQGKSIFIA ASIGPIPEMF DKMETDQENS LDEYKFIVDI FLNSDIKIFM FETFSDVSDL LEITKYIKVK DSSAFIVTQF ATTPEGFTRK GLSNKHIIAE VKKSKSIDAY GFNCGVGPTH LFNSLKKLNF ADDMVAAAPN AGYPEIVHER MVYIQNPNYF AEKMKDISGL GVKILGGCCG TTPIHIEKMS ELIQSYLNAP IPKQQISAKP KVIIDREKTD GFFEKMRKGK FVIAVELDPP FNADTDLILQ NAWICKDHGV DAITIADSPM ARARADSIMI AAKIKREVGI EVLPHLCCRD KNLNALKSAL LAGYIENIRN VLAITGDPVA IADKNDIKGV FNLNSMKLIQ LISTMNKELF PEDPINVGGA LNLNLLKPEA ELAKMVKKIN SGATFFLTQP IFEDYVINIL RLINKNDGIK ILGGIMPLVS YKNALFLNNE VAGIKIPERI INKYNSNMGK DEAEIIGIEI AVEIANKIKE SVDGFYFITP FNRVEMIMKI IKKLKCFH // ID A4J6L9_DESRM Unreviewed; 800 AA. AC A4J6L9; DT 01-MAY-2007, integrated into UniProtKB/TrEMBL. DT 01-MAY-2007, sequence version 1. DT 27-MAY-2015, entry version 57. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABO50722.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABO50722.1}; GN OrderedLocusNames=Dred_2207 {ECO:0000313|EMBL:ABO50722.1}; OS Desulfotomaculum reducens (strain MI-1). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfotomaculum. OX NCBI_TaxID=349161 {ECO:0000313|EMBL:ABO50722.1, ECO:0000313|Proteomes:UP000001556}; RN [1] {ECO:0000313|EMBL:ABO50722.1, ECO:0000313|Proteomes:UP000001556} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MI-1 {ECO:0000313|EMBL:ABO50722.1, RC ECO:0000313|Proteomes:UP000001556}; 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 ----------------------------------------------------------------------- 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; ABO50722.1; -; Genomic_DNA. DR RefSeq; WP_011878524.1; NC_009253.1. DR RefSeq; YP_001113547.1; NC_009253.1. DR ProteinModelPortal; A4J6L9; -. DR STRING; 349161.Dred_2207; -. DR EnsemblBacteria; ABO50722; ABO50722; Dred_2207. DR KEGG; drm:Dred_2207; -. DR PATRIC; 21730721; VBIDesRed82656_2422. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; DRED349161:GHP6-2273-MONOMER; -. DR Proteomes; UP000001556; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001556}; KW Methyltransferase {ECO:0000313|EMBL:ABO50722.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001556}; KW Transferase {ECO:0000313|EMBL:ABO50722.1}. SQ SEQUENCE 800 AA; 85898 MW; 4305D247220B3C5A CRC64; MSFRKRVKKE VLIIDGAMGT LLQQRGLPGG WCPEEWNLSH PEAVKEIHKL YLEAGADIIT TNTFGAIQLK LADYHLGDQV KEINQAAVKL AKEVAQPYGA MVAGSVGPLG KFLQPLGTMT FEEAYQQFYE QCAAMVEAGV DLILFETFGD IGEMRAALIA AADAGDVPVV ASFTFDETGR TFTGTDPETA AVVAERLGIA AIGVNCSVGP RQLEGVVRKL TESTNLPVLV SPNAGMPEII GGKTVFRETP EIMAEYAQRF VDYGASILGG CCGTTPKHIQ AIYQQVKKLK PKCRNKRFGL RVASRVKTVT IQPSGVPVAI GERLNPTGKK ALQAEIREGK TEITRRDALT QVQAGAEILD VNVGVGGVDQ VAAMERAVQA VQVLVEAPLC IDSTDPTVIE HALKLYHGKA LINSVNGEEN SIETILPLAK RYGAALIGLT LDDEGIPPTA AGRLAVARRL VERTEAMGIP RDDLMMDCLV LTVSAQPEGV PETLEAIRLV KQKLQITTSL GVSNVSFGLP NRVLINAAFF AMALNAGLDA AILNPQDQRM METLRASAVL TGRDVRAEKY IAIEQQTHNG SKMETTGEQM KASTPLDILY QAVLSGDKDN IVSYINEALK TGLSPMELLD KALIPGIEEV GRRYGAGIYF LPQLMMAGET MTKSFERLRP ELAKGPAKKA GTVVLATVKG DIHDIGKNIV SVMLANHGFE VIDLGKNVAN EEILRVAAEQ KANIIGLSAL MTTTMVHMQE IIKLVKEQGL NCKVMVGGAA VTEHYAREIG ADGYAIDAVE AVNVAKKLAS // ID A4JI99_BURVG Unreviewed; 355 AA. AC A4JI99; DT 01-MAY-2007, integrated into UniProtKB/TrEMBL. DT 01-MAY-2007, sequence version 1. DT 27-MAY-2015, entry version 49. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABO56002.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABO56002.1}; GN OrderedLocusNames=Bcep1808_3011 {ECO:0000313|EMBL:ABO56002.1}; 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 {ECO:0000313|EMBL:ABO56002.1, ECO:0000313|Proteomes:UP000002287}; RN [1] {ECO:0000313|Proteomes:UP000002287} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G4 / LMG 22486 {ECO:0000313|Proteomes:UP000002287}; 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 PDB data bank. CC ----------------------------------------------------------------------- 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; ABO56002.1; -; Genomic_DNA. DR RefSeq; WP_011886164.1; NC_009256.1. DR RefSeq; YP_001120837.1; NC_009256.1. DR STRING; 269482.Bcep1808_3011; -. DR EnsemblBacteria; ABO56002; ABO56002; Bcep1808_3011. DR KEGG; bvi:Bcep1808_3011; -. DR PATRIC; 19324678; VBIBurVie89221_7281. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; BVIE269482:GJNA-3084-MONOMER; -. DR Proteomes; UP000002287; Chromosome 1. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002287}; KW Methyltransferase {ECO:0000313|EMBL:ABO56002.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002287}; KW Transferase {ECO:0000313|EMBL:ABO56002.1}. SQ SEQUENCE 355 AA; 38065 MW; 94FF207EA5D29FB9 CRC64; MSASPLAASA PPDARYTRGA ELPALLKSRI LILDGAMGTM IQRYKLDEAA YRGERFKDFP RDVKGNNELL SLTQPQIISE IHDQYFAAGA DIVETNTFGA TTVAQADYGM EDLVVEMNVE SARLARESAA RHATPGKPRF VAGAIGPTPK TASISPDVND PGARNITFDE LHAAYYQQAK ALLDGGVDLF LVETIFDTLN AKAALFALDE LFEDTGERLP IMVSGTVTDA SGRILSGQTV EAFWNSLRHA KPLTFGLNCA LGAALMRPYI AEIAKLCDTY VSCYPNAGLP NPMSDTGFDE TPDVTSGLLK EFAQAGLVNL AGGCCGTTPE HIAEIAKALA DVKPRRWPSQ YSEAA // ID A4QE93_CORGB Unreviewed; 1221 AA. AC A4QE93; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 27-MAY-2015, entry version 68. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:BAF54559.1}; GN OrderedLocusNames=cgR_1567 {ECO:0000313|EMBL:BAF54559.1}; OS Corynebacterium glutamicum (strain R). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=340322 {ECO:0000313|EMBL:BAF54559.1, ECO:0000313|Proteomes:UP000006698}; RN [1] {ECO:0000313|Proteomes:UP000006698} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R {ECO:0000313|Proteomes:UP000006698}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP009044; BAF54559.1; -; Genomic_DNA. DR RefSeq; WP_011897261.1; NC_009342.1. DR RefSeq; YP_001138461.1; NC_009342.1. DR STRING; 340322.cgR_1567; -. DR EnsemblBacteria; BAF54559; BAF54559; cgR_1567. DR KEGG; cgt:cgR_1567; -. DR PATRIC; 21507724; VBICorGlu58097_1615. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CGLU340322:GJBE-1639-MONOMER; -. DR Proteomes; UP000006698; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006698}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 239 239 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 772 772 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1221 AA; 133380 MW; 7642F6130A526A71 CRC64; MSTSVTSPAH NNAHSSEFLD ALANHVLIGD GAMGTQLQGF DLDVEKDFLD LEGCNEILND TRPDVLRQIH RAYFEAGADL VETNTFGCNL PNLADYDIAD RCRELAYKGT AVAREVADEM GPGRNGMRRF VVGSLGPGTK LPSLGHAPYA DLRGHYKEAA LGIIDGGGDA FLIETAQDLL QVKAAVHGVQ DAMAELDTFL PIICHVTVET TGTMLMGSEI GAALTALQPL GIDMIGLNCA TGPDEMSEHL RYLSKHADIP VSVMPNAGLP VLGKNGAEYP LEAEDLAQAL AGFVSEYGLS MVGGCCGTTP EHIRAVRDAV VGVPEQETST LTKIPAGPVE QASREVEEED SVASLYTSVP LSQETGISMI GERTNSNGSK AFREAMLSGD WETCVDIAKQ QTRDGAHMLD LCVDYVGRDG TADMATLAAL LATSSTLPIM IDSTEPEVIR TGLEHLGGRS IVNSVNFEDG DGPDSRYQRI MKLVKQHGAA VVALTIDEEG QARTAEHKVR IAKRLIDDIT GSYGLDIKDI VVDCLTFPIS TGQEETRRDG IETIEAIREL KKLYPEIHTT LGLSNISFGL NPAARQVLNS VFLNECIEAG LDSAIAHSSK ILPMNRIDDR QREVALDMVY DRRTEDYDPL QEFMQLFEGV SAADAKDARA EQLAAMPLFE RLAQRIIDGD KNGLEDDLEA GMKEKSPIAI INEDLLNGMK TVGELFGSGQ MQLPFVLQSA ETMKTAVAYL EPFMEEEAEA TGSAQAEGKG KIVVATVKGD VHDIGKNLVD IILSNNGYEV VNLGIKQPLS AMLEAAEEHK ADVIGMSGLL VKSTVVMKEN LEEMNNAGAS NYPVILGGAA LTRTYVENDL NEVYTGEVYY ARDAFEGLRL MDEVMAEKRG EGLDPNSPEA IEQAKKKAER KARNERSRKI AAERKANAAP VIVPERSDVS TDTPTAAPPF WGTRIVKGLP LAEFLGNLDE RALFMGQWGL KSTRGNEGPS YEDLVETEGR PRLRYWLDRL KSEGILDHVA LVYGYFPAVA EGDDVVILES PDPHAAERMR FSFPRQQRGR FLCIADFIRP REQAVKDGQV DVMPFQLVTM GNPIADFANE LFAANEYREY LEVHGIGVQL TEALAEYWHS RVRSELKLND GGSVADFDPE DKTKFFDLDY RGARFSFGYG SCPDLEDRAK LVELLEPGRI GVELSEELQL HPEQSTDAFV LYHPEAKYFN V // ID A4RUZ2_OSTLU Unreviewed; 1252 AA. AC A4RUZ2; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 01-APR-2015, entry version 59. DE SubName: Full=B12 dependent methionine synthase {ECO:0000313|EMBL:ABO95339.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABO95339.1}; GN Name=metH {ECO:0000313|EMBL:ABO95339.1}; GN ORFNames=OSTLU_45056 {ECO:0000313|EMBL:ABO95339.1}; OS Ostreococcus lucimarinus (strain CCE9901). OC Eukaryota; Viridiplantae; Chlorophyta; prasinophytes; Mamiellophyceae; OC Mamiellales; Bathycoccaceae; Ostreococcus. OX NCBI_TaxID=436017 {ECO:0000313|EMBL:ABO95339.1, ECO:0000313|Proteomes:UP000001568}; RN [1] {ECO:0000313|EMBL:ABO95339.1, ECO:0000313|Proteomes:UP000001568} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCE9901 {ECO:0000313|EMBL:ABO95339.1, RC ECO:0000313|Proteomes:UP000001568}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000583; ABO95339.1; -; Genomic_DNA. DR RefSeq; XP_001417046.1; XM_001417009.1. DR ProteinModelPortal; A4RUZ2; -. DR SMR; A4RUZ2; 664-909, 918-1251. DR STRING; 436017.A4RUZ2; -. DR EnsemblPlants; ABO95339; ABO95339; OSTLU_45056. DR GeneID; 5000739; -. DR KEGG; olu:OSTLU_45056; -. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR Proteomes; UP000001568; Chromosome 3. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001568}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABO95339.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001568}; KW Transferase {ECO:0000313|EMBL:ABO95339.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 238 238 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 301 301 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 302 302 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 777 777 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1252 AA; 137902 MW; CA0552DB4CF809F7 CRC64; MQKRVMVIDG AMGTAVQKYK LSEDDFRGDR YKNHTHDLKG NNDILVLTKP EVISEIHEAY LAAGADIIET NTFSSTMIAQ ADYELDKKEE VRDMNLAAAR LAKAACVKFT EQNPAKPRFA AGAIGPTNRT LSVSPSVENP AFRACTFDEI VDAYYEQIEA LVEGGVDLIL VETIFDTLNA KAAIFAIEKF FEAYGTRLPL FISGTIVDNS GRTLSGQTNE AFWNSVSHAK PMAVGLNCAL GAKDMVPYIE NLSKCADCWV FAYPNAGLPN AMGGYDQKGA EMAEDCRVFL EKGLLNGIGG CCGTTDDHIG ALAQMVAPYT PRKKHDVPEI MRISGLEPFN YVPNENDYRK TFINLGERCN VAGSSIFKKA IVDGNFEKAL AIALKQVEHG AHVIDINMDD GLIDGETAMS RFVNLLVSEP DASKVPFMID SSKFHVVEAG LKCSQGKCIM NSISLKGGEE EFLHHAKIVK RHGAAVVVMA FDEEGQAATE AEKVRICCRA YKLLVEQLGF NPQDIIFDPN ILTIGTGMEE HNNYGVDFIN ATREIKRLCP GCKISGGVSN LAFSFRGNEP VRRAFHSAFL YHACKAGMDM GIVNAAQVEE DVYEKMDKEL LEYVEDVLLN RCTNATERML EFAATLDPKS TPCNLRKKGA AGGGAVKAAG SGKEWRNQPC EKRLEYALIK GIDEFCIADT EECRVGDKYK SCLEVIEGPL MDGMNVVGDL FGAGKMFLPQ VIKSARVMKK AVGHLIPFMD AEKALTGSTE ASTAGTFLIA TVKGDVHDIG KNIVAVVLGC NNFKVIDIGV MCPCEKILDA VRESKADILG LSGLITPSLD EMVTVAKEME KAGMRIPLLI GGATTSKMHT AVKLTPNYSG GVIHVLDASR AVPVAQTLLD KRKHADFMDD INETYAEMRD EFYAGLEDRK YLTLQKARAT VKPVDFTAAP NVPVTPKFCG AKAMEVSIDD VLPYIDWNPF FQVWQLRGRY PNRGYPKIFN DETVGPEAKK LFDEANAMIT KIKQNKRLTL KGIYGFYPAN SVGDDIVVYT DESRTTTHHT FYTLRQQAEK DTDEPYMALS DFIAPKDSGV KDYLGMFVCS AGFGLDELTA EFKAANDDYS YIMAEALADR LAEAFAELLH ERVRKDDWGY AKDESFNCED LLKVKYQGIR PAPGYPSQPD HTEKATMWDL MKVKEEIGVE LTETFAMLPS ASVSGLYFAG ACSEYFNVGK LTSDQVEEYA GRKKMELSEV QRWLGPNLSY EP // ID A4SD45_PROVI Unreviewed; 1224 AA. AC A4SD45; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 29-APR-2015, entry version 63. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABP36404.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABP36404.1}; GN OrderedLocusNames=Cvib_0382 {ECO:0000313|EMBL:ABP36404.1}; 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 {ECO:0000313|EMBL:ABP36404.1, ECO:0000313|Proteomes:UP000006700}; RN [1] {ECO:0000313|EMBL:ABP36404.1, ECO:0000313|Proteomes:UP000006700} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 265 {ECO:0000313|EMBL:ABP36404.1, RC ECO:0000313|Proteomes:UP000006700}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000607; ABP36404.1; -; Genomic_DNA. DR RefSeq; WP_011889633.1; NC_009337.1. DR RefSeq; YP_001129906.1; NC_009337.1. DR ProteinModelPortal; A4SD45; -. DR SMR; A4SD45; 648-893. DR STRING; 290318.Cvib_0382; -. DR EnsemblBacteria; ABP36404; ABP36404; Cvib_0382. DR KEGG; pvi:Cvib_0382; -. DR PATRIC; 21395108; VBIChlPha132153_0408. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CPHA290318:GHNQ-391-MONOMER; -. DR Proteomes; UP000006700; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006700}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABP36404.1}; KW Transferase {ECO:0000313|EMBL:ABP36404.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1224 AA; 134489 MW; E72D635B60516012 CRC64; MKATLPELLQ QRILVLDGAM GTMIQRHKFQ EEDYRGERFK DHAHPLLGNN DLLVLTQPEV IYAIHCDFLE AGSDIIETNT FNANPISQGD YGAESLVIEI NHEAAKLARK AADAYTAKTP GKPRFVAGSI GPTNKTLSLS PDVNRPGYRA VSFQEVVNNY TMQLEGLMEG GVDLLLVETV FDTLNCKAAL FAIEEFFNRS GHRVPVMVSG TVVDASGRTL SGQTTEAFWI SIAHMPDLLS VGLNCALGSK QMRPFIEAVS TVAESFVSVY PNAGLPNEFG EYDDSPDYMA GQIADFAQSG FVNIVGGCCG TTPGHIKAIA EAVSAIPPRR RPEKKNELQL SGLEPLIVNE TTGFINVGER TNVTGSKKFA RLIKEGNYDE ALSIARQQVE NGAQVIDVNV DEGMLDSEQV MQEFLNLIAS EPEISRVPVM IDSSKWSVIE KGLQCVQGKS IVNSISLKEG EEPFRQRAGK ILEYGAAAVV MAFDEEGQAD SLERRKEICG RAYRILTREV GFPPEDIIFD PNVLTVATGI EEHDNYAVDF IESVRWIKEN LPHAKVSGGI SNVSFSFRGN EPVREAMHAA FLYHAIRAGL DMGIVNAGQL AIYQDIEPEL LLRVEDVLLN RRPDATERLV SFAETIREGG EKLEAKAARW RSLPVEERLQ HALIKGIVEY IDEDTEEARK NYPSPLQVIE GPLMNGMNTI GDLFAEGKMF LPQVVKSARV MKRSVAWLIP FIEEEKARQK DTSAAAKILL ATVKGDVHDI GKNIVSVVLS CNNYEVVDIG VMMPCDKILE AVEREKPDIL GLSGLITPSL DEMVHVASEM ERLGMKIPLL IGGATTSKIH TAVKIAPVYS GPVVQVLDAS RSVPIAGNLL NPEKSSAYRA ELKAEQAGMR KNHEERGAAA TLLTLEEARA NRLAIDWSSS TVPAPRNPGI TVLDSVTIAA LRPYIDWTPF FLTWELHGRY PEIFEDTKVG EEARTLFNDA EALLNRIEKG QLLGMRGVAG LFPANSTGDD IEVYSDESRT APLCVFHTLR QQKQQPKGKP NLALSDFIAP KESGVGDYIG GFALTTGLRI QNLLDQFQKE HDDYHRIMAL ALADRLAEAF AEMLHEKVRR ELWGYAPGEI LGTGELLSEK YQGIRPAPGY PACPDHTEKG ALFNLLNAEA NTGITLTETF AMNPAASVSG LYFAHPESHY FVLGKINGEQ TEDYARRKGM SSAEAAKWLS PNLQ // ID A4SL41_AERS4 Unreviewed; 300 AA. AC A4SL41; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 27-MAY-2015, entry version 44. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABO89613.1}; GN OrderedLocusNames=ASA_1525 {ECO:0000313|EMBL:ABO89613.1}; OS Aeromonas salmonicida (strain A449). OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales; OC Aeromonadaceae; Aeromonas. OX NCBI_TaxID=382245 {ECO:0000313|EMBL:ABO89613.1, ECO:0000313|Proteomes:UP000000225}; RN [1] {ECO:0000313|Proteomes:UP000000225} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A449 {ECO:0000313|Proteomes:UP000000225}; 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; ABO89613.1; -; Genomic_DNA. DR RefSeq; WP_005320139.1; NC_009348.1. DR RefSeq; YP_001141361.1; NC_009348.1. DR STRING; 382245.ASA_1525; -. DR EnsemblBacteria; ABO89613; ABO89613; ASA_1525. DR GeneID; 4997031; -. DR KEGG; asa:ASA_1525; -. DR PATRIC; 20789421; VBIAerSal2987_1514. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; PYVDVWL; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; ASAL382245:GJJN-1516-MONOMER; -. DR Proteomes; UP000000225; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000225}; KW Methyltransferase {ECO:0000313|EMBL:ABO89613.1}; KW Transferase {ECO:0000313|EMBL:ABO89613.1}. SQ SEQUENCE 300 AA; 31800 MW; 067E4E413E19BBEF CRC64; METQALWVLD GGMGRELARR GAPFRQPEWS ALALMEAPQT VREVHQAYVA SGARVITTNS YALVPFHIGA ERFAAEGEAL AALAGQLARE VANEQPGSVQ VAGSLPPLFG SYRADLFEAD RVGELATPLI RALTPHVDIW LAETMSLIAE PLALKALLPQ DGKPFWVSFT LEDEAPGSEP ALRSGERVAD AVTALASAGV DAILFNCCQP EVIEAALTVA GDSLQALGRG DIRLGAYANA FPPQPKEATA NDGLDEIRAD LGPLDYLGWA ERWRAVGASL IGGCCGIGPE HIQALASRLR // ID A4SSJ3_AERS4 Unreviewed; 1226 AA. AC A4SSJ3; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 29-APR-2015, entry version 67. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABO91865.1}; GN Name=metH {ECO:0000313|EMBL:ABO91865.1}; GN OrderedLocusNames=ASA_3912 {ECO:0000313|EMBL:ABO91865.1}; OS Aeromonas salmonicida (strain A449). OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales; OC Aeromonadaceae; Aeromonas. OX NCBI_TaxID=382245 {ECO:0000313|EMBL:ABO91865.1, ECO:0000313|Proteomes:UP000000225}; RN [1] {ECO:0000313|Proteomes:UP000000225} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A449 {ECO:0000313|Proteomes:UP000000225}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000644; ABO91865.1; -; Genomic_DNA. DR RefSeq; WP_005316300.1; NC_009348.1. DR RefSeq; YP_001143613.1; NC_009348.1. DR STRING; 382245.ASA_3912; -. DR EnsemblBacteria; ABO91865; ABO91865; ASA_3912. DR GeneID; 4998640; -. DR KEGG; asa:ASA_3912; -. DR PATRIC; 20794254; VBIAerSal2987_3877. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; ASAL382245:GJJN-3899-MONOMER; -. DR Proteomes; UP000000225; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000225}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 254 254 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 318 318 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 765 765 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1226 AA; 134878 MW; B9D35B1059BB2C65 CRC64; MNEKPSIKSD ITKKLESCLK ERILIIDGAM GTMIQGYKLG EADYRGERFA DWHTDIKGNN DLLVLTRPGI IREIHDQYCA AGADILETNT FNATRIAMAD YEMEDLSAEI NREAARLARA VADEWTARNP ARPRFVAGVL GPTNRTCSIS PDVNDPGKRN VTYDQLVAAY TESTHALIEG GADLILIETI FDTLNAKAAA FAVEGVFEAL GYSLPVMISG TITDASGRTL SGQTTEAFYH SLRHVKPISF GLNCALGPDE LRQYVEELSR ISETFVSAHP NAGLPNAFGE YDLDAGEMAD HIREWAQSGF LNMVGGCCGT TPTHIRAMSD AVAGIKPRTL PTLPVACRLS GLEPLIITAD SMFVNVGERT NVTGSAKFKR LIKEGLYDEA LDVAKQQVES GAQIIDINMD EGMLDAEAAM VRFLNLIAGE PDIARVPVMI DSSKWEVLEA GLKCVQGKPV VNSISMKEGE EKFIQQAKLL RRYGAAVIVM AFDEVGQADT RTRKFEICQR AYRILVDQVG FPPEDIIFDP NIFAVATGID EHNNYAVDFI EAVKDIKTHL PHAMISGGVS NVSFSFRGNE PVREAIHAVF LYHAIQNGMD MGIVNAGQLA IYEDIPAELK AKVEAVVLNL SDSATEDLLA IAEKYRGAGA QAEDPRDQEW RSWPVGKRLE HALVKGITDF IEEDTEEARA GAEKPLHVIE GPLMDGMNVV GDLFGAGKMF LPQVVKSARV MKRAVAYLQP YIEAEKQGGY SNGKIVLATV KGDVHDIGKN IVGVVLQCNN YEIVDLGVMV SCETILKTAR EVGADIIGLS GLITPSLDEM VHVAKEMERQ GFKLPLLIGG ATTSKAHTAV KIEQNYSEPV VYVSNASRAV GVAQSLLNPE LKPAFVARID KEYEVARDQH ARKQPRSKPV SLAHARANRQ QLDWVNYQPP APRELGVQTF ENVHVSVLRP YIDWTPFFLS WELAGKYPRI LEDEIIGEEA TKLFADANAM LDKLEQDESV RCAGIIGLFP ANTIGDSIEV YTDESRSKVR KVLHHLRQQS EKQGFPNYCL ADYVAPKESG KPDWIGAFAV TGGIGEEAIA TAYKADHDDY NAILIQAVCD RLAEYLHEQV RKVHWGYAAD EALSNEDLIR ENYRGIRPAP GYPACPEHTE KGSIWELLGV EQAIGMKLTE SYAMWPGAAV SGWYFSHPDS KYFAVAQIQQ DQVEDYAARK GMTLAEAERW LGPNLN // ID A4T0C8_POLSQ Unreviewed; 354 AA. AC A4T0C8; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 27-MAY-2015, entry version 46. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABP35192.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABP35192.1}; GN OrderedLocusNames=Pnuc_1980 {ECO:0000313|EMBL:ABP35192.1}; 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 {ECO:0000313|EMBL:ABP35192.1, ECO:0000313|Proteomes:UP000000231}; RN [1] {ECO:0000313|EMBL:ABP35192.1, ECO:0000313|Proteomes:UP000000231} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18221 / CIP 109841 / QLW-P1DMWA-1 RC {ECO:0000313|Proteomes:UP000000231}; 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 ----------------------------------------------------------------------- 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; ABP35192.1; -; Genomic_DNA. DR RefSeq; WP_011903815.1; NC_009379.1. DR ProteinModelPortal; A4T0C8; -. DR STRING; 312153.Pnuc_1980; -. DR EnsemblBacteria; ABP35192; ABP35192; Pnuc_1980. DR KEGG; pnu:Pnuc_1980; -. DR PATRIC; 22968485; VBIPolNec12025_2046. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; PNEC312153:GH50-2023-MONOMER; -. DR Proteomes; UP000000231; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000231}; KW Methyltransferase {ECO:0000313|EMBL:ABP35192.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000231}; KW Transferase {ECO:0000313|EMBL:ABP35192.1}. SQ SEQUENCE 354 AA; 38207 MW; 4F3720D08B2B5F92 CRC64; MQFNGLSQPY TRGQALPELL KQRILILDGA MGTMIQQYKL GEADYRGLPT NTRFAGHPGD IKGNNELLVL TQPQIISKIH EQYLDAGADI IETNTFGATS VAQEDYKMAG LAREMNEVSA KLARAACEKY STPDKPRFAA GAIGPTPKTA SISPDVNDPG ARNVTFDALR ASYREQIEGL FAGGVDLFLV ETIFDTLNAK AALFALDEFF EETGERLPVM ISGTVTDASG RILSGQTVEA FWNSLRHIKP LTFGLNCALG AALMRPYIAE LSRICDAAVS CYPNAGLPNP MSDTGFDETP DITSSLVDGF AKDGLVNLVG GCCGTTPDHI RAIANAVAKR KPRAFYRENT EESV // ID A4TB79_MYCGI Unreviewed; 1251 AA. AC A4TB79; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 27-MAY-2015, entry version 65. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABP45530.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABP45530.1}; GN OrderedLocusNames=Mflv_3053 {ECO:0000313|EMBL:ABP45530.1}; 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 {ECO:0000313|EMBL:ABP45530.1, ECO:0000313|Proteomes:UP000000232}; RN [1] {ECO:0000313|Proteomes:UP000000232} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PYR-GCK {ECO:0000313|Proteomes:UP000000232}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000656; ABP45530.1; -; Genomic_DNA. DR RefSeq; WP_011893930.1; NC_009338.1. DR RefSeq; YP_001134318.1; NC_009338.1. DR ProteinModelPortal; A4TB79; -. DR SMR; A4TB79; 663-1250. DR STRING; 350054.Mflv_3053; -. DR EnsemblBacteria; ABP45530; ABP45530; Mflv_3053. DR KEGG; mgi:Mflv_3053; -. DR PATRIC; 18034254; VBIMycGil17082_3108. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; QPFFNAW; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; MGIL350054:GHK8-3089-MONOMER; -. DR Proteomes; UP000000232; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000232}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABP45530.1}; KW Transferase {ECO:0000313|EMBL:ABP45530.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 260 260 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 780 780 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1251 AA; 137214 MW; 2E9B7F2B323D54A2 CRC64; MEGAHVNAVE FEPNIRPDCT EELTAALRER IMVIDGAMGT AIQRDRPDEA GYRGDRFTEW PTALQGNNDL LNLTQPQIIE AIHREYLDAG ADILETNTFN ANAISLSDYD MTDLAYELNY AGAALARKAA DEYSTADKPR YVAGAIGPTT RTASISPDVN DPGARNVSYD QLVAAYLEAA NGLVDGGSDL IMIETIFDSL NAKAAVFAVE TLFEERGRRW PVIISGTITD ASGRTLSGQV TEAFWNAIRH AKPLAVGLNC ALGAPEMRPY IAEVARIADT FVSCYPNAGL PNAFGEYDES PERQASYIAE FAEAGLVNLV GGCCGTAPPH IAEIAKVVDG KTPRELPQIP VATRLSGLEP LNINDESLFV NIGERTNITG SARFRNLIKA EDYDTALSVA LQQVEVGAQV IDINMDEGMI DGVAAMDRFT KLIASEPDIS RVPVMIDSSK WEVIEAGLKN VQGKPIVNSI SMKEGEEKFI REAQLCRKYG AAVVVMAFDE QGQADNLERR KEICGRAYRI LTEKVGFPAE DIIFDPNCFA LATGIEEHAT YGIDFIEACA WIKENLPGVH ISGGISNVSF SFRGNNPVRE AIHAVFLFHA IKAGLDMGIV NAGALVPYDS IDPELRDRIE DVVLNRRADA AERLLEIAER FNKADKGEDP QAAEWRSLPV RERITHALVK GIDAHVDDDT EELRAEIEAA GGRPIEVIEG PLMDGMNVVG DLFGSGKMFL PQVVKSARVM KKAVAYLLPY IEAEKADAGT TGSKDTNGTI VMATVKGDVH DIGKNIVGVV LQCNNFEVID LGVMVPAQKI LDAAREHDAD IIGLSGLITP SLDEMSNFAV EMERAGLEIP LLIGGATTSR AHTAVKISPR RSGPVVWVKD ASRSVPVAAA LLDDKQRPAL LEATEKDYAS LRERHAQKND RPMLTLEKAR ANRTPIEWDG YTPPVPAQGV GVREFIDYDL AELREYIDWQ PFFNAWEMKG RFPDILNNPA TGEAARKLYN DAQEMLDTLI KEKWLTANGV IGFFCANAVG DDIEVYTDDT RTEVLTTLYN LRQQGEHRDG IPNRSQGDFI APKETGLRDY IGAFAVTAGL GSQAKIMEFK AALDDYSAIL LESLADRLAE AFAERMHERV RTEFWGYQPD EQLDNNALIA ERYVGIRPAP GYPSCPEHTE KATLFGLLDA TERTGIELTE SMAMWPGAAV SGWYFSHPQS QYFVVGRLAQ DQVADYARRK GWTLQEAERW LAPNLGYNPE D // ID A4U3E9_9PROT Unreviewed; 1158 AA. AC A4U3E9; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 29-APR-2015, entry version 46. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:CAM77406.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAM77406.1}; GN Name=metH {ECO:0000313|EMBL:CAM77406.1}; GN ORFNames=MGR_2923 {ECO:0000313|EMBL:CAM77406.1}; OS Magnetospirillum gryphiswaldense. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Magnetospirillum. OX NCBI_TaxID=55518 {ECO:0000313|EMBL:CAM77406.1}; RN [1] {ECO:0000313|EMBL:CAM77406.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MSR-1 {ECO:0000313|EMBL:CAM77406.1}; 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 implicated in magnetosome RT biomineralization and function."; RL J. Bacteriol. 189:4899-4910(2007). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CU459003; CAM77406.1; -; Genomic_DNA. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAM77406.1}; KW Transferase {ECO:0000313|EMBL:CAM77406.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 287 287 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 730 730 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1158 AA; 125562 MW; AF1AC14AD093BADC CRC64; MTNILDHLHQ RVLLCDGGTG ALVQAMNLSV DKDFMGLENC TDILVESRPD VVRNIAMQYF NAGADMVETN TFGASPITLA EFGIADKAFD LNKRAAEIAR EAAEEFSDGR ARFVLGSVGP GTKLPSLGHI GYDELEAAYV VQCAGQIAGG ADAILIETCQ DPLQIKAAVN GAKIAREQAG KDTPIFVQVT VETTGTMLVG ADIAAAATVV HSLGVPSLGL NCAAGPQEML EHVKYLVENW PDLISLQPNA GLPELVDGQT RYPLLPEELA VWHERFVGMG VNLLGGCCGT TPAHIGATHQ MLQRIGSGYR PNPVKRSVHW VPAVASLYSQ VTLRQENAFL AIGERCNANG SKKFRDLQDA EDWDGIVAMA REQVKEGSHT LDVCTAFVGR KEVADMTQVV TRLRGAVTTP LVIDSTELPV LEAALKLYGG KAILNSINFE NGEEDAADRL KLAKKFGAAV VALTIDEEGM AKDCAAKLRI AHRLYDFAVN QHGLPAGDLL FDPLTFTICT GNEDDRKLGL ETLDAIEALA RELPECGIVL GLSNISFGLK PAARQVLNSV FNDYAVKRGM TGAIVHVSKI LPLHSIPADE VKAAEDLIFD RRSPGIDPLQ AFIALFGDRK AAENKKELPA KIEDRLKQRI VDGDRTGLDD DLAAAMAEGW APLAIINDLL LDGMKVVGEL FGSGKMQLPF VLQSAETMKA AVAYLEPHME KSDGSAKATM VLATVKGDVH DIGKNLVDII LTNNGYKVVN IGIKQPVGEI IKAAKEHKAD AVGMSGLLVK STVIMKDNLE EMRAQGLDVP VLLGGAALTR KFVEEDCLNA YGGSGVAYAR DAFDGLDLMA KVADGSFDTY VQARSKAPKS GNSKRIGQPA EASTLRPVDW DEVTMRRAEL HRDVPPPVPP FWGAKLIENV PLQNLAGFLN ETMLYQFHWG YRKQGKSIDE FKAWASKELK PIALNMLKRC SQEGILHAQG VYGYWKAAAD GDSVVVFDTD GSTELARFGF PRQARDGGLC IADFFRPISD PVRDVIGLQV VTMGQKASDV ARQWFEANKY QDYLYLHGLS VEMAEAMAEY VHKRIRAELG FAAQDAAEMD KLLKQNYQGS RYSFGYPACP NVEDQKQLLA LLGADRVGIT LSDEFQLEPE QSTSAIVCVH PQAKYFTV // ID A4VLN1_PSEU5 Unreviewed; 1230 AA. AC A4VLN1; DT 29-MAY-2007, integrated into UniProtKB/TrEMBL. DT 29-MAY-2007, sequence version 1. DT 01-APR-2015, entry version 60. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABP79882.1}; GN Name=metH {ECO:0000313|EMBL:ABP79882.1}; GN OrderedLocusNames=PST_2223 {ECO:0000313|EMBL:ABP79882.1}; OS Pseudomonas stutzeri (strain A1501). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=379731 {ECO:0000313|EMBL:ABP79882.1, ECO:0000313|Proteomes:UP000000233}; RN [1] {ECO:0000313|Proteomes:UP000000233} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A1501 {ECO:0000313|Proteomes:UP000000233}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000304; ABP79882.1; -; Genomic_DNA. DR RefSeq; WP_011913349.1; NC_009434.1. DR RefSeq; YP_001172724.1; NC_009434.1. DR STRING; 379731.PST_2223; -. DR EnsemblBacteria; ABP79882; ABP79882; PST_2223. DR KEGG; psa:PST_2223; -. DR PATRIC; 19964936; VBIPseStu31643_2231. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PSTU379731:GJER-2218-MONOMER; -. DR Proteomes; UP000000233; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000233}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000233}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1230 AA; 134793 MW; 5EFD7EA2D631F04E CRC64; MSARNARLQA LQHALSQRIL ILDGGMGTMI QSYKLEESDY RGERFTDWPS DVKGNNDLLL LSRPDVIQAI EKAYLDAGAD ILETNTFNAT RVSQADYGME ELVYELNVEG ARLAREVADA KTAETPDRPR FVAGVLGPTS RTCSISPDVN NPGYRNVTFD LLVENYTEAT RGLIEGGADL ILIETIFDTL NAKAAIFAVQ QVFEEDGVEL PIMISGTITD ASGRTLSGQT TEAFWNSVRH AKPISVGLNC ALGAKDLRPY LEELANKADT HVSAHPNAGL PNAFGEYDET PAEMAAVVEE FAASGFLNII GGCCGTTPAH IQAIAEAVAK YPPRVIPDIP KACRLSGLEP FTIDRSSLFV NVGERTNITG SAKFARLIRE ENYTEALEVA LQQVEAGAQV IDINMDEGML DSKAAMVTFL NLIAGEPDIS RVPIMIDSSK WEVIEAGLKC IQGKGIVNSI SMKEGVEQFK HHAHLCKRYG AAVVVMAFDE AGQADTAARK REICQRSYDI LVNEVGFPPE DIIFDPNIFA IATGIEEHNN YAVDFIEACA FIRDNLPYAL TSGGVSNVSF SFRGNNPVRE AIHSVFLFHA IKAGLTMGIV NAGQLEIYDE IPKELRDAVE DVVLNRCAGG TEALLEIADK YKGDGSVKEA ETEEWRNLPV DKRLEHALVK GITAFIVEDT EECRQQCARP IEVIEGPLMS GMNVVGDLFG AGKMFLPQVV KSARVMKQAV AHLIPFIEAE KGGKPEAKGK ILMATVKGDV HDIGKNIVGV VLGCNGYDVV DMGVMVPAEK ILQTAIAEKC DIIGLSGLIT PSLDEMVHVA KEMQRQGFSL PLMIGGATTS KAHTAVKIDP QYSNDAVVYV TDASRAVGVA TTLLSKELKP AFVDKTREEY AMIRERTANR SARTERLSYL DAIANKPPFD WSGYAPVKPS FTGRQVLEDI DLRTLVDYID WTPFFIAWDL AGKYPRILED EVVGEAATSL FNDAQAMLKK LVDEKLIRAR AVFGFWPANQ VQDDDLEVYG DNGEKLATLH HLRQQTIKAD AKPNLSLADF VAPKSTGITD YVGGFICTAG IGAEELAKAY QDKGDDYNSI MVKALADRLA EACAEWLHEQ VRKHYWGYAP DERLSNEELI REQYKGIRPA PGYPACPDHT EKGTLFQLLD ADGISQVTLT EHYAMLPTAA VSGWYFAHPE AQYFAVGKID KDQVESYSQR KGQELAISER WLMPNLGYDN // ID A4VY01_STRSY Unreviewed; 315 AA. AC A4VY01; DT 29-MAY-2007, integrated into UniProtKB/TrEMBL. DT 29-MAY-2007, sequence version 1. DT 27-MAY-2015, entry version 43. DE SubName: Full=Putative methyltransferase {ECO:0000313|EMBL:ABP90990.1}; GN OrderedLocusNames=SSU05_2024 {ECO:0000313|EMBL:ABP90990.1}; OS Streptococcus suis (strain 05ZYH33). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=391295 {ECO:0000313|EMBL:ABP90990.1, ECO:0000313|Proteomes:UP000000243}; RN [1] {ECO:0000313|EMBL:ABP90990.1, ECO:0000313|Proteomes:UP000000243} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=05ZYH33 {ECO:0000313|EMBL:ABP90990.1, RC ECO:0000313|Proteomes:UP000000243}; 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 ----------------------------------------------------------------------- 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; ABP90990.1; -; Genomic_DNA. DR RefSeq; WP_012027907.1; NC_009442.1. DR RefSeq; YP_001199390.1; NC_009442.1. DR STRING; 391295.SSU05_2024; -. DR EnsemblBacteria; ABP90990; ABP90990; SSU05_2024. DR GeneID; 5099476; -. DR KEGG; ssu:SSU05_2024; -. DR PATRIC; 19775802; VBIStrSui128929_1993. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; YGRSVTK; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; SSUI391295:GHI8-2084-MONOMER; -. DR Proteomes; UP000000243; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000243}; KW Methyltransferase {ECO:0000313|EMBL:ABP90990.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000243}; KW Transferase {ECO:0000313|EMBL:ABP90990.1}. SQ SEQUENCE 315 AA; 34941 MW; C91D1BB78C13069C CRC64; MGRFKELLEQ KEYIILHGAL GTELEFRGHD VSGKLWSAKY LLENPQYIKD IHKDYIRAGA DLVTTSTYQA TFEGLAEVGL SQAEAEELIR WTVDLAKEAR DEVWAELSEA EKVQRTYPLI SGDVGPYAAY LANGAEYTGD YGNISLSELK DFHRRRIELL LEQEAELLAL ETIPNVLEAQ ALVELLAEDF PEAEAYISFT SQDGQSISDG TSIEKIAELV NSSEQILAVG LNCTAPSLYP AFLSQLREKT DKPFVTYPNS GEVYDGATQT WKEKADDSHS LLDNTLEWHE LGAKVVGGCC RTRPADIADL VAGLK // ID A4W5D2_ENT38 Unreviewed; 1227 AA. AC A4W5D2; DT 29-MAY-2007, integrated into UniProtKB/TrEMBL. DT 29-MAY-2007, sequence version 1. DT 01-APR-2015, entry version 62. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABP58912.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABP58912.1}; GN OrderedLocusNames=Ent638_0222 {ECO:0000313|EMBL:ABP58912.1}; OS Enterobacter sp. (strain 638). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Enterobacter. OX NCBI_TaxID=399742 {ECO:0000313|EMBL:ABP58912.1, ECO:0000313|Proteomes:UP000000230}; RN [1] {ECO:0000313|Proteomes:UP000000230} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=638 {ECO:0000313|Proteomes:UP000000230}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000653; ABP58912.1; -; Genomic_DNA. DR RefSeq; WP_011915485.1; NC_009436.1. DR RefSeq; YP_001174963.1; NC_009436.1. DR STRING; 399742.Ent638_0222; -. DR EnsemblBacteria; ABP58912; ABP58912; Ent638_0222. DR KEGG; ent:Ent638_0222; -. DR PATRIC; 20409970; VBIEntSp101211_0350. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; ESP399742:GJ0E-232-MONOMER; -. DR Proteomes; UP000000230; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000230}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABP58912.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000230}; KW Transferase {ECO:0000313|EMBL:ABP58912.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135825 MW; B854E3F77F2B41E7 CRC64; MSSKIEQLRA QLNERILVLD GGMGTMIQSY RLSEDDFRGE RFADWPCDLK GNNDLLVLSK PDVIAAIHHA YFEAGADIVE TNTFNSTTIA MADYQMESLS AEINFTAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNVTFDQLV AAYRESTKAL VEGGSDLIMI ETVFDTLNAK AAIFAVKEEM EALGVDLPIM VSGTITDASG RTLSGQTTEA FYNSLRHADA LTFGLNCALG PDELRQYVQE LSRIADCYVT AHPNAGLPNA FGEYDLDAVT MAAQIREWAE SGFLNIVGGC CGTTPEHIAA MSHAVAGLPP RKLPDLPVAC RLAGLEPLTI SKESLFVNVG ERTNVTGSAK FKRLIKEEKY NEALDVARQQ VESGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVEPFIHHA KKVRRYGAAV VVMAFDEVGQ ADTRERKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELREGVEDVI LNRRDDATER MLDLAEKYRG SKADESVNIQ QAEWRAWDVK KRLEYSLVKG ITEFIELDTE EARQQAARPI EVIEGPLMDG MNVVGDLFSE GKMFLPQVVK SARVMKQAVA YLEPYIEASK EKSSSNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIIDL GVMVPADKIL KTAREVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVSAL LSDTQRDDFV ARTRKEYDTV RIQHARKKPR TPPVTLAAAR ENDLAFDWSS YTPPVAHRLG VQDVTASIET LRNYIDWTPF FMTWSLAGKY PRILEDDVVG EEAQRLFKDA NDMLDQLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT NVLAVSRHLR QQTEKVGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA ISDRLAEAFA EYLHERVRKV HWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKGT IWQLLDVETH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYALRKGMS VSEVERWLAP NLGYDAD // ID A4W733_ENT38 Unreviewed; 311 AA. AC A4W733; DT 29-MAY-2007, integrated into UniProtKB/TrEMBL. DT 29-MAY-2007, sequence version 1. DT 01-APR-2015, entry version 45. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABP59513.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ABP59513.1}; GN OrderedLocusNames=Ent638_0828 {ECO:0000313|EMBL:ABP59513.1}; OS Enterobacter sp. (strain 638). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Enterobacter. OX NCBI_TaxID=399742 {ECO:0000313|EMBL:ABP59513.1, ECO:0000313|Proteomes:UP000000230}; RN [1] {ECO:0000313|Proteomes:UP000000230} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=638 {ECO:0000313|Proteomes:UP000000230}; 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 ----------------------------------------------------------------------- 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; ABP59513.1; -; Genomic_DNA. DR RefSeq; WP_012016234.1; NC_009436.1. DR RefSeq; YP_001175564.1; NC_009436.1. DR STRING; 399742.Ent638_0828; -. DR EnsemblBacteria; ABP59513; ABP59513; Ent638_0828. DR KEGG; ent:Ent638_0828; -. DR PATRIC; 20411230; VBIEntSp101211_0964. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; ESP399742:GJ0E-854-MONOMER; -. DR Proteomes; UP000000230; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000230}; KW Methyltransferase {ECO:0000313|EMBL:ABP59513.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000230}; KW Transferase {ECO:0000313|EMBL:ABP59513.1}. SQ SEQUENCE 311 AA; 33598 MW; D14DCB65DA3EBB01 CRC64; MSLNNPLTAL LETQPFIVLD GAMATELEAR GCNLADSLWS AKVLVENPDL IRDVHLDYFR AGAQVAITAS YQATPAGFAA RGLDEAQSRA LIGKSVELAR KAREAYLAEN AHAGTLLVAG SVGPYGAYLA DGSEYRGDYL RSAQEFTEFH RPRVEALLDA GADLLACETL PSFAEIKALA ALLSEYPRAR AWFSFTLRES EHLSDGTPLR EVVAALADYP QIVALGINCI ALENTTAALE HLHSLTALPL VVYPNSGEHY DAVTKTWHHH GEACETLSGY LPHWLAAGAK LIGGCCRTTP KDIAELNAQR R // ID A4WQF1_RHOS5 Unreviewed; 357 AA. AC A4WQF1; DT 29-MAY-2007, integrated into UniProtKB/TrEMBL. DT 29-MAY-2007, sequence version 1. DT 29-APR-2015, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ABP69615.1}; GN OrderedLocusNames=Rsph17025_0709 {ECO:0000313|EMBL:ABP69615.1}; OS Rhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=349102 {ECO:0000313|EMBL:ABP69615.1, ECO:0000313|Proteomes:UP000000234}; RN [1] {ECO:0000313|EMBL:ABP69615.1, ECO:0000313|Proteomes:UP000000234} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17025 / ATH 2.4.3 {ECO:0000313|Proteomes:UP000000234}; 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 ----------------------------------------------------------------------- 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; ABP69615.1; -; Genomic_DNA. DR RefSeq; WP_011907762.1; NC_009428.1. DR RefSeq; YP_001166920.1; NC_009428.1. DR STRING; 349102.Rsph17025_0709; -. DR EnsemblBacteria; ABP69615; ABP69615; Rsph17025_0709. DR KEGG; rsq:Rsph17025_0709; -. DR PATRIC; 23159567; VBIRhoSph94549_0721. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265278; -. DR KO; K00548; -. DR OMA; GTNLFAM; -. DR OrthoDB; EOG693GKH; -. DR BioCyc; RSPH349102:GHE1-2038-MONOMER; -. DR Proteomes; UP000000234; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000234}. SQ SEQUENCE 357 AA; 37832 MW; B160934CE4E46A1B CRC64; MAELRAHGPH SLRAVPDLSE DKMTDALSRM LQTREWLMAD GATGTNLFNM GLSSGEPPEL WNIDRPDNIR ALYRAAVEAG SDIFLTNSFG GNAARLKLHE AQGRVGELNR TAAELGREVA DASGRTVVVA GSMGPTGEIF EPMGTLTHRM AVEIFHEQAE ALKAGGADVL WVETISAAEE FKAAAEAARL AGMPWCGTMS FDTAGRTMMG LTPAALVDLV TKLPNPPLAF GANCGVGASD LLRTVLGFTA QGVELPVIAK GNAGIPKYHD GHIHYDGTPD LMAEYAVLAR DAGARVIGGC CGTMPEHLRA MRAALETRPK GPRPSLETIS EVLGGFSSAS DGSDDAGPTR ERRRRRS // ID A4WYR1_RHOS5 Unreviewed; 342 AA. AC A4WYR1; DT 29-MAY-2007, integrated into UniProtKB/TrEMBL. DT 29-MAY-2007, sequence version 1. DT 27-MAY-2015, entry version 46. DE SubName: Full=Plasmid pRSPA01, complete sequence {ECO:0000313|EMBL:ABP72525.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABP72525.1}; GN OrderedLocusNames=Rsph17025_3657 {ECO:0000313|EMBL:ABP72525.1}; OS Rhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3). OG Plasmid pRSPA01 {ECO:0000313|EMBL:ABP72525.1, OG ECO:0000313|Proteomes:UP000000234}. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=349102 {ECO:0000313|EMBL:ABP72525.1, ECO:0000313|Proteomes:UP000000234}; RN [1] {ECO:0000313|EMBL:ABP72525.1, ECO:0000313|Proteomes:UP000000234} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17025 {ECO:0000313|EMBL:ABP72525.1}; 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., 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; ABP72525.1; -; Genomic_DNA. DR RefSeq; WP_011910570.1; NC_009429.1. DR RefSeq; YP_001169830.1; NC_009429.1. DR STRING; 349102.Rsph17025_3657; -. DR EnsemblBacteria; ABP72525; ABP72525; Rsph17025_3657. DR KEGG; rsq:Rsph17025_3657; -. DR PATRIC; 23165787; VBIRhoSph94549_3791. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; RSPH349102:GHE1-971-MONOMER; -. DR Proteomes; UP000000234; Plasmid pRSPA01. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000234}; KW Methyltransferase {ECO:0000313|EMBL:ABP72525.1}; KW Plasmid {ECO:0000313|EMBL:ABP72525.1}; KW Transferase {ECO:0000313|EMBL:ABP72525.1}. SQ SEQUENCE 342 AA; 36222 MW; A1D382E126C1A096 CRC64; MLPFSLPPSP VFPVLDALAR ERILILDGAM GTQIQQLGLA EEDYAGDCAC RHHSDHPQKG NNDLLILTQP QAIEEIHFRY AMAGADIVET NTFSATTIAQ ADYGMESAVR DLNVEGARIV RRALDRATAI DGKPRFVAGA VGPTNRTASI SPDVNDPGFR AVTFDDLRTA YSQQVRGLIE GGADLILIET IFDTLNAKAA IFACFEAFAE AGRRLPLMIS GTITDASGRT LSGQTPTAFW HSVRHARPFT VGLNCALGAA AMRPHLAELA GVADSFTCAY PNAGLPNAFG QYDEGPEDTA AQVARFAREG LVNVVGGCCG TTPDHICAIA DAVAGLAPRA VK // ID A4X6X2_SALTO Unreviewed; 1167 AA. AC A4X6X2; DT 29-MAY-2007, integrated into UniProtKB/TrEMBL. DT 29-MAY-2007, sequence version 1. DT 27-MAY-2015, entry version 67. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABP54622.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABP54622.1}; GN OrderedLocusNames=Strop_2171 {ECO:0000313|EMBL:ABP54622.1}; OS Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micromonosporineae; Micromonosporaceae; Salinispora. OX NCBI_TaxID=369723 {ECO:0000313|EMBL:ABP54622.1, ECO:0000313|Proteomes:UP000000235}; RN [1] {ECO:0000313|Proteomes:UP000000235} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440 RC {ECO:0000313|Proteomes:UP000000235}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000667; ABP54622.1; -; Genomic_DNA. DR RefSeq; WP_011906052.1; NC_009380.1. DR RefSeq; YP_001159000.1; NC_009380.1. DR STRING; 369723.Strop_2171; -. DR EnsemblBacteria; ABP54622; ABP54622; Strop_2171. DR GeneID; 5058634; -. DR KEGG; stp:Strop_2171; -. DR PATRIC; 23443372; VBISalTro43511_2228. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; STRO369723:GI49-2205-MONOMER; -. DR Proteomes; UP000000235; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000235}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABP54622.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000235}; KW Transferase {ECO:0000313|EMBL:ABP54622.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 219 219 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 730 730 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1167 AA; 126678 MW; 04BF2C1449430335 CRC64; MLDALTDRIL VADGAMGTML HAADLTLDDF DGLEGCNEIL NVTRPDVVRG VHEAYLAVGA DCVETNTFGA NLANLAEYGI EGRIRELSEA GAQLARAAAD AYATPEQPRF VLGSIGPGTK LPTLGHAAYT TLRDAYQENA VGLIAGGSDA LIIETCQDLL QVKAAVIGSK RAMAELGRSV PIICHMAVET TGTMLLGSEI GAALTAIEPL GIDLIGLNCS TGPAEMGEHL RYLSQHSQIP VSVMPNAGLP VLTSDGAYFP LTPDEMGDAL EQFVTDYGVA LVGGCCGTTP EHIRVLAERM RGRPPVVREP RPEPGASSIY HHVPFAQDAS VLMVGERTNA NGSKAFREAM LAGDWQACVE IARSQARDGS HLLDLCVDYV GRDGTQDMRE LASRFATAST LPIMLDSTEP GVIEAGLETL GGRCVVNSVN FEDGDGPDSR YARLMPVVKE HGAGVVALLI DEEGQARTQD WKVRVAARLI DDLTGRWGMA RSDILIDALT FPIATGQEET RRDGIETIEA IREIAARYPG VNFTLGISNV SFGLNPAARQ VLNSVFLHEC VQAGLTSAIV HASKILPMSK IPDEQREIAL DLVYDRRREG YDPVQRFIEA FEGVDAASAR ASRAEELAAL PLEERLKRRI IDGERNGLEA DLDAALATGL AAMAVINDIL LDGMKVVGEL FGAGQMQLPF VLQSAEVMKS AVAYLEPHLE KADDGGKGRI VLATVKGDVH DIGKNLVDII LSNNGYEVVN IGIKQPINAI LDAAEQNRAD AIGMSGLLVK STVIMKENLV EMATRGVAER WPVLLGGAAL TRAYVEDDLR SMFPGQVHYA RDAFEGLSLM DRVMAAKRGG AQVVDPEREA ALAARRERRA RQRAIVSESL PELNDSSVRS DVATDVEVPT PPFFGTRVVK GLPLADYAAL LDERATFLGQ WGLRGTRGGK GPTYEELVET EGRPRLRYWL DRLIADQVLE AAVVYGYFPA YSDGNDLVVL DENGHAERAR FTFPRQRQER RLCLADFFRP RGGELDVVTL QLVTVGQPIS EYTAKLFARN EYRDYLEVHG LSVQLTEALA EYWHQRVRAE LRLPEDRTVA TADPADLAGL LRTEYRGCRY AFGYPACPDL EDRAKLVDLL GAERIGVQLS EEFQLVPEQA TDAIVVHHPE ASYFNAK // ID A4XIN4_CALS8 Unreviewed; 411 AA. AC A4XIN4; DT 29-MAY-2007, integrated into UniProtKB/TrEMBL. DT 29-MAY-2007, sequence version 1. DT 27-MAY-2015, entry version 36. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABP66769.1}; GN OrderedLocusNames=Csac_1164 {ECO:0000313|EMBL:ABP66769.1}; OS Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903 / OS Tp8T 6331). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacterales Family III. Incertae Sedis; OC Caldicellulosiruptor. OX NCBI_TaxID=351627 {ECO:0000313|EMBL:ABP66769.1, ECO:0000313|Proteomes:UP000000256}; RN [1] {ECO:0000313|Proteomes:UP000000256} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43494 / DSM 8903 {ECO:0000313|Proteomes:UP000000256}; 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 ----------------------------------------------------------------------- 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; ABP66769.1; -; Genomic_DNA. DR RefSeq; WP_011916708.1; NC_009437.1. DR RefSeq; YP_001179960.1; NC_009437.1. DR STRING; 351627.Csac_1164; -. DR EnsemblBacteria; ABP66769; ABP66769; Csac_1164. DR KEGG; csc:Csac_1164; -. DR PATRIC; 21251984; VBICalSac56748_1307. DR eggNOG; COG0646; -. DR HOGENOM; HOG000269747; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CSAC351627:GJ17-1192-MONOMER; -. DR Proteomes; UP000000256; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000256}; KW Methyltransferase {ECO:0000313|EMBL:ABP66769.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000256}; KW Transferase {ECO:0000313|EMBL:ABP66769.1}. SQ SEQUENCE 411 AA; 45508 MW; CA3A5E019DD2B7AA CRC64; MFKNEVYKKV LVFDGAMGTQ LIQNGLKENE CPDLWSVTRP EVIAKIHRDY FEAGSDCVET NTFGANREKL KKYGLENEVE KINKAAILLA KDVAKEYGGY VGLSVGPTGR LMRPSGDLDF DEAESVFYEQ ILAGIEAGAD FISIETMSDI KEAKAAFLAY KRAKENANKD VACLVSLTFE ENKRLLMGTP PEVAAYFFSF IGADLVGANC SGGAKQLLDV IKSMNGFSFV PLSTKPNAGL PKMIDGKVVY EDCIADFESS TEEFIQSGVR LYGGCCGTNP EYIKAIAKLV KGKEALFESR AEKRFITSIY SILDVSTKFS VYEFKLTNDF SQESIFELVG IEEDGILVDI GENVDQEILK NFLLESQDFS KKPYIFNIKT KEQADLIDRY YFGIYGTVSS LCGSSGIKVE I // ID A4XIN5_CALS8 Unreviewed; 604 AA. AC A4XIN5; DT 29-MAY-2007, integrated into UniProtKB/TrEMBL. DT 29-MAY-2007, sequence version 1. DT 27-MAY-2015, entry version 50. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=Csac_1165 {ECO:0000313|EMBL:ABP66770.1}; OS Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903 / OS Tp8T 6331). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacterales Family III. Incertae Sedis; OC Caldicellulosiruptor. OX NCBI_TaxID=351627 {ECO:0000313|EMBL:ABP66770.1, ECO:0000313|Proteomes:UP000000256}; RN [1] {ECO:0000313|Proteomes:UP000000256} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43494 / DSM 8903 {ECO:0000313|Proteomes:UP000000256}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ABP66770.1; -; Genomic_DNA. DR RefSeq; WP_011916709.1; NC_009437.1. DR RefSeq; YP_001179961.1; NC_009437.1. DR ProteinModelPortal; A4XIN5; -. DR STRING; 351627.Csac_1165; -. DR EnsemblBacteria; ABP66770; ABP66770; Csac_1165. DR KEGG; csc:Csac_1165; -. DR PATRIC; 21251986; VBICalSac56748_1308. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; CSAC351627:GJ17-1193-MONOMER; -. DR Proteomes; UP000000256; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000256}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ABP66770.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000000256}; KW Transferase {ECO:0000313|EMBL:ABP66770.1}. SQ SEQUENCE 604 AA; 67055 MW; 64498533BE655CCC CRC64; MKSFREFLSQ QDIVLFDGAM GTELLNRGYN KDFPLEWANI SNPDLVKSIH SDYILAGSQC IETNTFGANE CRLNLYGFEG QVEKINRNAV KIAKEVAGQT AYVIGSVGPL GKPVGSGFEI DDKRAKEVYK KQLYFLLDEG VDAILFETAA STHEVLIAIE ALKELDSNFP YIVQFSFTRD LTTIYGEDIY KVIEFLKGID ADVVGLNCGN GPHQTLEALK IFSQHLKGPF SVQPNAGYPQ LVQGRLVYST SANYFASFVD EYVKYGAKII GGCCGTTPEH IKAIKERIKT ISKSVEIEVI EKKEEQKSIL KDTPSELSQK LGKKFVFTVE ISPPKGIELE KTKEGVKLLK EAGADTVNIA DSPMARVRIS PIALAHILKE ELGVESILHF TCRDRNLISL QSELLGAAAL GVKNVLALTG DPPSIGDYPQ AKPVFDVNSE GLVLILNKLN SGTDYMGNPI GKATNFTIGV ALNLNADDLD KEIERLKRKI ENGAHFIETQ PIYEVEALEK FFEKVDFKLP PILGGILPLR SSRHAEFLHN EVPGITIPDK IRERMKNSKD PVKEGIEIAC EIVDRIKEMV SGIYIMPPFE KYEMAAEIIK RFRV // ID A4XUA3_PSEMY Unreviewed; 1236 AA. AC A4XUA3; DT 29-MAY-2007, integrated into UniProtKB/TrEMBL. DT 29-MAY-2007, sequence version 1. DT 29-APR-2015, entry version 61. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABP84919.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABP84919.1}; GN OrderedLocusNames=Pmen_2159 {ECO:0000313|EMBL:ABP84919.1}; OS Pseudomonas mendocina (strain ymp). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=399739 {ECO:0000313|EMBL:ABP84919.1, ECO:0000313|Proteomes:UP000000229}; RN [1] {ECO:0000313|EMBL:ABP84919.1, ECO:0000313|Proteomes:UP000000229} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ymp {ECO:0000313|Proteomes:UP000000229}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000680; ABP84919.1; -; Genomic_DNA. DR RefSeq; WP_012018564.1; NC_009439.1. DR RefSeq; YP_001187651.1; NC_009439.1. DR STRING; 399739.Pmen_2159; -. DR EnsemblBacteria; ABP84919; ABP84919; Pmen_2159. DR GeneID; 5109499; -. DR KEGG; pmy:Pmen_2159; -. DR PATRIC; 19910851; VBIPseMen131592_2184. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PMEN399739:GHR6-2199-MONOMER; -. DR Proteomes; UP000000229; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000229}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABP84919.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000229}; KW Transferase {ECO:0000313|EMBL:ABP84919.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1236 AA; 135474 MW; 3143A793D51D4888 CRC64; MSDRSARLQA LQQALKERIL ILDGGMGTMI QSYKLEEADY RGERFADWPS DVKGNNDLLL LTQPQIIAAI EKAYLDAGAD ILETNTFNAT RVSQADYDME ELVYELNLAG ARVAREVADA KTLETPDRPR FVAGVLGPTS RTCSISPDVN DPGYRNVTFD ELVENYTEAT RGLIEGGADL ILIETIFDTL NAKAAIFAVQ QVFEEDGIEL PIMISGTITD ASGRTLSGQT TEAFWNSVRH AKPISVGLNC ALGAKDLRPY LEELANKADT HVSAHPNAGL PNAFGEYDES PAEMAAVVEE FAASGFLNII GGCCGTTPAH IQAIAEAVAK YPPRVIPDIP KACRLSGLEP FTIDRNSLFV NVGERTNITG SAKFARLIRE ENYTEALEVA LQQVEAGAQV IDINMDEGML DSKAAMVRFL NLIAGEPDIS RVPIMIDSSK WEVIEAGLKC IQGKGIVNSI SMKEGVEQFK HHARLCKRYG AAVVVMAFDE VGQADTAARK KEICQRSYDI LVNEVGFPPE DIIFDPNIFA VATGIEEHNN YAVDFIEACA YIREHLPFAL SSGGVSNVSF SFRGNNPVRE AIHSVFLYYA IQNGLTMGIV NAGQLEIYDE IPKELRDAVE DVVLNRNDGA TEALLAIADK YKGDGAAKEV ENEEWRSLPV DKRLEHALVK GITAFIVEDT EECRQQCARP IEVIEGPLMA GMNVVGDLFG SGKMFLPQVV KSARVMKQAV AHLIPFIEAE KGDKPEAKGK ILMATVKGDV HDIGKNIVGV VLGCNGYDIV DLGVMVPAEK ILQTARDEKC DIIGLSGLIT PSLDEMVHVA KEMQRQGFTL PLMIGGATTS KAHTAVKIDP QYSNDAVVYV TDASRAVGVA TQLLSKELKA DFVQKTREEY VVVRERTSAR ASRTERLGYA DAIANKPAFD WNGYIAPKPS FTGAQVLDDI DLATLAEYID WTPFFISWDL AGKYPRILTD EIVGEAATSL FNDAQAMLKK LIDEKLIRAR AVFGFWPANQ VAHDDIEVYG DDGKPLAKLH HLRQQTIKPD GKPNLSLADF VAPKESGVTD YVGGFITTAG IGAEELAKAY EANGDDYNSI MVKALADRLA EACAEWLHER VRKEYWGYAA DEQLDNEALI REQYKGIRPA PGYPACPDHT EKATLFKLLD PEADYNKAGR SGVFLTEHYA MFPAAAVSGW YFAHPEAQYF AVGKVDKDQI EQYSKRKGQD IAVSERWLAP NLGYDD // ID A4Y9P7_SHEPC Unreviewed; 1244 AA. AC A4Y9P7; DT 29-MAY-2007, integrated into UniProtKB/TrEMBL. DT 29-MAY-2007, sequence version 1. DT 27-MAY-2015, entry version 62. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABP76680.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABP76680.1}; GN OrderedLocusNames=Sputcn32_2965 {ECO:0000313|EMBL:ABP76680.1}; OS Shewanella putrefaciens (strain CN-32 / ATCC BAA-453). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=319224 {ECO:0000313|EMBL:ABP76680.1, ECO:0000313|Proteomes:UP000006699}; RN [1] {ECO:0000313|EMBL:ABP76680.1, ECO:0000313|Proteomes:UP000006699} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CN-32 / ATCC BAA-453 {ECO:0000313|Proteomes:UP000006699}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000681; ABP76680.1; -; Genomic_DNA. DR RefSeq; WP_011919838.1; NC_009438.1. DR RefSeq; YP_001184479.1; NC_009438.1. DR STRING; 319224.Sputcn32_2965; -. DR EnsemblBacteria; ABP76680; ABP76680; Sputcn32_2965. DR KEGG; spc:Sputcn32_2965; -. DR PATRIC; 23554932; VBIShePut135485_3100. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SPUT319224:GHAP-3070-MONOMER; -. DR Proteomes; UP000006699; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006699}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABP76680.1}; KW Transferase {ECO:0000313|EMBL:ABP76680.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 258 258 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 774 774 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1244 AA; 137969 MW; B5D3E6CE01D98893 CRC64; MTIPSTKAGQ ILADIRKQLA ERILILDGAM GTMIQGYKLE EEDYRGERFK DWHTDVKGNN DLLVLTQPHI IKQIHTDYLN AGADIIETNT FNATTIAMAD YDMQSLSAEI NREGARLARE ACDEAFAATG IPRYVAGVLG PTNRTCSISP DVNDPGYRNV SFDELVTAYK ESTKALIEGG ADIIMVETIF DTLNAKAALF AIESVFDDLF GQHSKDRLPI MISGTITDAS GRTLTGQTTE AFYNSLRHIK PLSIGLNCAL GPKELRPYVE ELSRISECYV SAHPNAGLPN EFGGYDETPE DMANVIEDWA REGMLNIIGG CCGSTPEHIR VIRQAVEKYD PRVLPDIPVA CRLAGLEPLT IDAQTLFVNV GERTNVTGSA KFLKLIKEGK FEQALDVARE QVESGAQIID INMDEGMLDG VEIMHKFLNL IASEPDISRV PIMIDSSKWE VIEAGLKCIQ GKGIVNSISL KEGEAKFIEQ ATLVKRYGAA AIIMAFDEQG QADTKARKIE ICTRAYRVLV DKVGFPPEDI IFDPNIFAIA TGIDEHDNYA VDFIDAIKAI KATLPHAMIS GGVSNVSFSF RGNNPVREAI HAVFLYHAIK VGMDMGIVNA GQLAIYDDID PELKVRVENV VLNLPCPVEG SSNTEQLLEI AEKFRGDGAQ VGKKEDLEWR SWPVNQRLAH ALVKGITEFI DEDTEAARQV ASRPLDVIEG PLMDGMNVVG DLFGSGKMFL PQVVKSARVM KKAVAYLNPF IEKEKVAGQS NGKILMVTVK GDVHDIGKNI VGVVLACNGF EVFDLGVMVS VERILDAVKE HNIDIIGMSG LITPSLDEMV HNVKTFHREG LTIPAIIGGA TCSKIHTAVK IAPHYPHGAI YIADASRAVP MVSKLVNNET RQATIDETYA EYDDMRTKRL SQAKRKEIVS LEAARENRCQ HDWASYTPFK PNVLGRQVFD DYPLEDLVER IDWTPFFRSW ELHGHYPEIL SDKVVGVEAQ KLFADGQAML KKIIEEKWLT AKAVIGLFPA NTVNYDDIEL YTDESRTTVE MTTHHLRMQL ERVGNDNFCL SDFVAPKDSG VADYMGGFAV TAGHGIDEHV ARFEANHDDY NAIMLKCLAD RLAEAFAERM HERVRKEFWG YAADEQLSNE ALIREKYKGI RPAPGYPACP DHTEKGLLWD LLKPDETIDL NITESYAMFP TAAVSGWYFA HPKSRYFGVS NIGRDQVEDY AKRKGMTVAE TEKWLAPVLD YDPE // ID A4YC88_SHEPC Unreviewed; 300 AA. AC A4YC88; DT 29-MAY-2007, integrated into UniProtKB/TrEMBL. DT 29-MAY-2007, sequence version 1. DT 27-MAY-2015, entry version 41. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABP77571.1}; GN OrderedLocusNames=Sputcn32_3865 {ECO:0000313|EMBL:ABP77571.1}; OS Shewanella putrefaciens (strain CN-32 / ATCC BAA-453). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=319224 {ECO:0000313|EMBL:ABP77571.1, ECO:0000313|Proteomes:UP000006699}; RN [1] {ECO:0000313|EMBL:ABP77571.1, ECO:0000313|Proteomes:UP000006699} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CN-32 / ATCC BAA-453 {ECO:0000313|Proteomes:UP000006699}; 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 ----------------------------------------------------------------------- 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; ABP77571.1; -; Genomic_DNA. DR RefSeq; WP_011920266.1; NC_009438.1. DR RefSeq; YP_001185370.1; NC_009438.1. DR STRING; 319224.Sputcn32_3865; -. DR EnsemblBacteria; ABP77571; ABP77571; Sputcn32_3865. DR KEGG; spc:Sputcn32_3865; -. DR PATRIC; 23556838; VBIShePut135485_4032. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; DVITANS; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; SPUT319224:GHAP-3991-MONOMER; -. DR Proteomes; UP000006699; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006699}; KW Methyltransferase {ECO:0000313|EMBL:ABP77571.1}; KW Transferase {ECO:0000313|EMBL:ABP77571.1}. SQ SEQUENCE 300 AA; 31838 MW; FC0C633C1622A7DF CRC64; MKKQALWVLD GGMGRELARR GAPFRQPEWS ALALMEAPQT VREVHQAYAA SGARVITTNS YALVPFHIGA ERFAAEGEAL AVLAGQLARE VANEQPGSVQ VAGSLPPLFG SYRADLFEAD RVGELATPLI QALAPHVDIW LAETMSLIAE PLALKALLPQ DGKPFWVSFT LEDEAPGSEP ALRSGERVAD AVTALAAVGV DAILFNCCQP EVIEAALTVA GDSLQALDRG DIRLGAYANA FPPQPKEATA NDGLDEIRAD LGPLDYLGWA ERWRAVGASL IGGCCGIGPE HIQALASRLR // ID A4YLY3_BRASO Unreviewed; 1284 AA. AC A4YLY3; DT 29-MAY-2007, integrated into UniProtKB/TrEMBL. DT 29-MAY-2007, sequence version 1. DT 29-APR-2015, entry version 61. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CAL74909.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAL74909.1}; GN Name=metH {ECO:0000313|EMBL:CAL74909.1}; GN OrderedLocusNames=BRADO0994 {ECO:0000313|EMBL:CAL74909.1}; OS Bradyrhizobium sp. (strain ORS278). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=114615 {ECO:0000313|EMBL:CAL74909.1, ECO:0000313|Proteomes:UP000001994}; RN [1] {ECO:0000313|EMBL:CAL74909.1, ECO:0000313|Proteomes:UP000001994} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ORS278 {ECO:0000313|EMBL:CAL74909.1, RC ECO:0000313|Proteomes:UP000001994}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CU234118; CAL74909.1; -; Genomic_DNA. DR RefSeq; WP_011924160.1; NC_009445.1. DR RefSeq; YP_001203146.1; NC_009445.1. DR STRING; 114615.BRADO0994; -. DR EnsemblBacteria; CAL74909; CAL74909; BRADO0994. DR KEGG; bra:BRADO0994; -. DR PATRIC; 21218217; VBIBraSp122330_0937. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; BSP114615:GJN5-947-MONOMER; -. DR Proteomes; UP000001994; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001994}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAL74909.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001994}; KW Transferase {ECO:0000313|EMBL:CAL74909.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 767 767 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1284 AA; 139431 MW; 000BDAAF53401664 CRC64; MSSPVSTARS AFLAAAAKRI LILDGAMGTM IQALQFDEAA FRSERFKDFH RDLRGNNDLL ILTQPDAIED IHAQYLRAGA DIVATNTFSA TSIAQADYDL SDIIYELNRE GARLARNAAT RVAAEDGKPR FVAGAMGPTN RTASISPDVS NPGYRAVTFD DLRLAYGEQA RGLLDGGADI LLVETIFDTL NAKAALYAIA ELCEARGIDV PVMISGTITD KSGRLLSGQM PEAFWNSVRH AKPLTIGFNC ALGAEDLRAH VADIGRVADT LVCAYPNAGL PNEFGQYDET PAYMARLIGE FARDGLVNIV GGCCGTTPDH IAAIAAAVAP HKPRIVLDIA PRLRLSGLEP FELTPEIPFV NVGERTNVTG SAKFRKLITA GDYTAALQVA RDQVENGAQV IDVNMDEGLL DSEAAMRTFL NLVAAEPDIA RVPVMVDSSK FHVIEAGLKC VQGKPVVNSI SLKEGEEKFI HEAQIARRHG AAVVVMAFDE TGQADTYQRK TEICARAYKI LVETVGFPPE DIIFDPNIFA IATGIEEHDN YGVDFIEATR WIRQNLPHAH VSGGVSNLSF SFRGNEPVRE AMHSVFLYHA IKAGMDMGIV NAGQMIVYDD IDPELRQVCE DVVLNRDPGA SERLLALAEK FRGQGKQTKE ADLAWREWPV EKRLSHALVH GITEFIDVDT EEARAKSTRP LDVIEGPLMA GMNVVGDLFG DGKMFLPQVV KSARVMKQAV AYLMPFMEAE KAANKGRANE RSNAGKIVLA TVKGDVHDIG KNIVGIVLQC NNFEVIDLGV MVPAAKIIDT AKAENADIIG LSGLITPSLD EMAYLASEME RQGLNVPLLI GGATTSRVHT AVKIDPNYQG GPVVHVNDAS RAVGVASSLL SPERKDAYAA DIRTEYQKIA AAHLRGQADK KRLSLADARA NAPKIDFANA RPVKPTFLGT KTFVDYDLAE LVPYIDWTPF FQTWELAGRF PAILDDAKVG EAARALYDDA QKMLKQIVDE KWFTARAAIG FWPANAVGDD IVLYADDSRT KTVATMHTLR QQLEKREGRF NTALSDFVAP MDSGVPDYVG GFVVTTGLGE DAVADRFKNA NDDYSSILVK ALADRLAEAF AERLHARVRR EFWAYAPDEA LSADDLILEK YQGIRPAPGY PAQPDHTEKA TLFKLLDAET SAGVRLTESF AMWPGSSVSG LYFASPESFY FGVGKIERDQ VEDYAARKGM TVAEVERWLA PILNYIPARG GQAAQTPRAA ATLAPANDAE LASHPPGCAC AVHLAWRKKA VGAK // ID A5CB34_VITVI Unreviewed; 347 AA. AC A5CB34; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 01-OCT-2014, entry version 19. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:CAN82018.1}; GN ORFNames=VITISV_003417 {ECO:0000313|EMBL:CAN82018.1}; 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 {ECO:0000313|EMBL:CAN82018.1}; RN [1] {ECO:0000313|EMBL:CAN82018.1} RP NUCLEOTIDE SEQUENCE. RA Velasco R., Zharkikh A., Troggio M., Cartwright D.A., Cestaro A., RA Pruss D., Pindo M., FitzGerald L.M., Vezzulli S., Reid J., RA Malacarne G., Iliev D., Coppola G., Wardell B., Micheletti D., RA Macalma T., Facci M., Mitchell J.T., Perazzolli M., Eldredge G., RA Gatto P., Oyzerski R., Moretto M., Gutin N., Stefanini M., Chen Y., RA Segala C., Davenport C., Dematte L., Mraz A., Battilana J., Stormo K., RA Costa F., Tao Q., Si-Ammour A., Harkins T., Lackey A., Perbost C., RA Taillon B., Stella A., Solovyev V., Fawcett J.A., Sterck L., RA Vandepoele K., Grando S.M., Toppo S., Moser C., Lanchbury J., RA Bogden R., Skolnick M., Sgaramella V., Bhatnagar S.K., Fontana P., RA Gutin A., Van de Peer Y., Salamini F., Viola R.; RT "The first genome sequence of an elite grapevine cultivar (Pinot noir RT Vitis vinifera L.): coping with a highly heterozygous genome."; RL PLoS ONE 2:e1326-e1326(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; AM488721; CAN82018.1; -; Genomic_DNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 347 AA; 38501 MW; 5C7D2E7AB5737047 CRC64; MGHVDLQPSS FISDFLLQTG GVAVIDGGLA TELERHGADL NDPLWSAKCL LSSPHLIRTG SRFVNLGWYS LRLLGVKNQN VAVWEFKMVH LDYLEAGADI IITASYQVNS AYIYVNRLLF RGLKLEASLE EKVKPCLGKS VEIACEARKM YYDRCIEFAC DDXEDGRILK HRPILVAASV GSYGAYLADG SEYSGIYGDE ITVETLKDFH RRRVQILADA GADLIAFETV PNKLEAQAYA ELLEEENIKI PAWFSFNSKD GVHVVSGDSL LECVSIAESC KKVVSVGINC TPPRFIHGLI LSIKKVTTKP ILIYPNSGES YDPEQKEWVV LSSITRNQCL GKLFLSF // ID A5CUX7_CLAM3 Unreviewed; 301 AA. AC A5CUX7; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 27-MAY-2015, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CAN02915.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:CAN02915.1}; GN OrderedLocusNames=CMM_2830 {ECO:0000313|EMBL:CAN02915.1}; OS Clavibacter michiganensis subsp. michiganensis (strain NCPPB 382). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Microbacteriaceae; Clavibacter. OX NCBI_TaxID=443906 {ECO:0000313|EMBL:CAN02915.1, ECO:0000313|Proteomes:UP000001564}; RN [1] {ECO:0000313|EMBL:CAN02915.1, ECO:0000313|Proteomes:UP000001564} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCPPB 382 {ECO:0000313|EMBL:CAN02915.1, RC ECO:0000313|Proteomes:UP000001564}; RX PubMed=18192381; DOI=10.1128/JB.01595-07; RA Gartemann K.H., Abt B., Bekel T., Burger A., Engemann J., Flugel M., RA Gaigalat L., Goesmann A., Grafen I., Kalinowski J., Kaup O., RA Kirchner O., Krause L., Linke B., McHardy A., Meyer F., Pohle S., RA Ruckert C., Schneiker S., Zellermann E.M., Puhler A., Eichenlaub R., RA 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; CAN02915.1; -; Genomic_DNA. DR RefSeq; WP_012039518.1; NC_009480.1. DR RefSeq; YP_001223575.1; NC_009480.1. DR STRING; 443906.CMM_2830; -. DR EnsemblBacteria; CAN02915; CAN02915; CMM_2830. DR KEGG; cmi:CMM_2830; -. DR PATRIC; 21456525; VBIClaMic82482_2956. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; CMIC443906:GCI2-2916-MONOMER; -. DR Proteomes; UP000001564; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001564}; KW Methyltransferase {ECO:0000313|EMBL:CAN02915.1}; KW Transferase {ECO:0000313|EMBL:CAN02915.1}. SQ SEQUENCE 301 AA; 31275 MW; DA2A477694F23E15 CRC64; MTRPLPLPDR PLVLDGGLGT LLEARGHDLS DPLWSARVLA DEPDAVRAAH AEFFRAGADV AITASYQVGF EAFAARGLGT ADTEALLRAS VRLAAEARDE VAREDAAGAG RDRWIAASVG PYGATLGDGS EYAGSSGLTR DELRRWHAPR FAVLADAGAD LLACETIPSL DEGRALVDLA RGSGASAWLA FTVEGGRLRS GEPMAEGFAL ADEADEVVAV GINCAHPEEV PAAIAAARSV TDRPVVVYPN SGERWDAVAR AWGGDPALPA VDAWIRAGAS LVGGCCQVGP DEIARMRDAL G // ID A5CWS5_VESOH Unreviewed; 1226 AA. AC A5CWS5; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 27-MAY-2015, entry version 63. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:BAF61585.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:BAF61585.1}; GN Name=metH {ECO:0000313|EMBL:BAF61585.1}; GN OrderedLocusNames=COSY_0466 {ECO:0000313|EMBL:BAF61585.1}; OS Vesicomyosocius okutanii subsp. Calyptogena okutanii (strain HA). OC Bacteria; Proteobacteria; Gammaproteobacteria; OC sulfur-oxidizing symbionts. OX NCBI_TaxID=412965 {ECO:0000313|EMBL:BAF61585.1, ECO:0000313|Proteomes:UP000000247}; RN [1] {ECO:0000313|EMBL:BAF61585.1, ECO:0000313|Proteomes:UP000000247} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HA {ECO:0000313|EMBL:BAF61585.1, RC ECO:0000313|Proteomes:UP000000247}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP009247; BAF61585.1; -; Genomic_DNA. DR RefSeq; WP_011929855.1; NC_009465.1. DR RefSeq; YP_001219309.1; NC_009465.1. DR ProteinModelPortal; A5CWS5; -. DR SMR; A5CWS5; 658-898. DR STRING; 412965.COSY_0466; -. DR EnsemblBacteria; BAF61585; BAF61585; COSY_0466. DR KEGG; vok:COSY_0466; -. DR PATRIC; 32020771; VBICanVes128383_0465. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CVES412965:GHZZ-465-MONOMER; -. DR Proteomes; UP000000247; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000247}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAF61585.1}; KW Transferase {ECO:0000313|EMBL:BAF61585.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 253 253 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 316 316 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 766 766 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1226 AA; 136982 MW; A9F1757FA21B9821 CRC64; MLYTCIMLIM NIKQILKSLL NKRILVLDGA MGTMIQQHKL TEQEYRGDRF KDWHVLVQGN NDLLSLTQPQ IIKNIHKDYL KVGADIIETN TFNATRTSMS DYKMEKLAYE INLKSAKIAR QAADEFSNTK KPRFVAGVIG PTSRTCSLSP DVNDPGFRNI TFDELVDVYI ESTRGLIKGG VDIILIETIF DTLNAKAAIF AIEQVFEDDG IELPIMISGT ITDASGRTLS GQMTEAFYNS LRHAKPISIG LNCALGPDLL RQYVAEMSRV ADTYVSAHPN AGLPNEFGEY DLNALTMSEQ VSEWARSGLV NILGGCCGST PDHIRAIADS INRIPPRKIP TIKPECRLSA LEAFNIGNDS LFVNIGERAN ITGSAKFKRL ILNQEYEKAL DICRTQVEEG AQMIDINMDE GMLDGKTAMI RFINLIASEP DIAKVPLIVD SSKWEIIEAG LKCTQGKPIV NSISLKEGKT KFIQYARLCK RYGAAIIVMA FDESGQADTQ ARKIEICTKA YYILVNNVNF PPEDIIFDPN IFAIATGIEE HNNYGIDFIE ATRAIKKNLP YAKISGGVSN VSFSFRGNNT VREAIHSVFL YHTVKAGMTM GIVNAGQLMV YNDIDPELKK AVEDVVLNIN KQAGERLVDI ALKFSNTFEQ KNNKQNLEWR TWAVERRLEH ALVKGITTYI NKDTQEAFDK LGRPILVIEG PLMSGMNVVG DLFSAGKMFL PQVVKSARVM KKSVAYLDPF LENEKENCVT SSQGKILMAT VKGDVHDIGK NIVSVVLSCN NYKIIDLGVM VPTETILETA RKENVDIIGL SGLITPSLDE MVFVAKEMTR QGLKLPLMIG GATTSKAHTA VKIEPEYDHG VFYVKDASKS VGVATALLSK TLKQQLLIDT KIDYENVRKR RINKGKSKLI SLEKARANRP NISFNSIVKP KKLGIHVFKN YNLAEIFEFI DWVPFFQTWE LTGKFPDILT DEIVGESASI LFNDAKVLFK KVINERLLTA NAVIGIFPAN SINEDIELYD ENNEVIITLN HLRQQLDKKG NTPNFCLSDF IASKDSGIND YMGAFAVTTG INIELLITTF KADHDDYNSI MIKAIADRLV EGFTELMHFK LRTKLWGYSF ERFDNNQFIQ EKFDGIRPAP GYPSCPEHSE KEKLWTLLDV KNNTGMILTS SYAMLPTASV SGWYFANPDA RYFGVAKINQ SQLNNYAKRK NISLEQAEKL LSPNLE // ID A5DCB0_PICGU Unreviewed; 313 AA. AC A5DCB0; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 22-JUL-2008, sequence version 2. DT 07-JAN-2015, entry version 36. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EDK36817.2}; GN ORFNames=PGUG_00915 {ECO:0000313|EMBL:EDK36817.2}; 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 {ECO:0000313|EMBL:EDK36817.2, ECO:0000313|Proteomes:UP000001997}; RN [1] {ECO:0000313|Proteomes:UP000001997} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL RC Y-324 {ECO:0000313|Proteomes:UP000001997}; 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; CH408155; EDK36817.2; -; Genomic_DNA. DR RefSeq; XP_001487538.1; XM_001487488.1. DR STRING; 4929.A5DCB0; -. DR GeneID; 5128722; -. DR KEGG; pgu:PGUG_00915; -. DR InParanoid; A5DCB0; -. DR KO; K00547; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000001997; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001997}; KW Reference proteome {ECO:0000313|Proteomes:UP000001997}. SQ SEQUENCE 313 AA; 35157 MW; C9B340C7295A55D9 CRC64; MYGGKPLVLD GGLGIQLETL AEKRNFAVKN DPLWSGRALI EAPDLIEDVH KSFLEAGCDI VTTSTYQISR ASLKKYTDFT DAQIEELWAK SVDVCWQACK FHESKARVCG AIGPYGGFLA NYAEYTGEYG LITNHKLEQY HLPLATFLNN NPKVDILAFE TIPNYKELKV IVNLVCKMSA TGPLKPFYLS MNFRNSSQMS DGTPIEKIMG YLNGKLNKNR TLRKRLIAIG CNCTELKDAT HVLKNIETYN YHNIPTIVYP NVFADHNDTK IDQKWSQSVD EWLKIGASII GGCCGTGPKQ IAQIRFKVDH MIY // ID A5DTG6_LODEL Unreviewed; 326 AA. AC A5DTG6; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 07-JAN-2015, entry version 39. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EDK42474.1}; GN ORFNames=LELG_00652 {ECO:0000313|EMBL:EDK42474.1}; 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; OC Candida/Lodderomyces clade; Lodderomyces. OX NCBI_TaxID=379508 {ECO:0000313|EMBL:EDK42474.1, ECO:0000313|Proteomes:UP000001996}; RN [1] {ECO:0000313|Proteomes:UP000001996} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239 RC {ECO:0000313|Proteomes:UP000001996}; 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; CH981524; EDK42474.1; -; Genomic_DNA. DR RefSeq; XP_001528132.1; XM_001528082.1. DR STRING; 36914.A5DTG6; -. DR GeneID; 5235056; -. DR KEGG; lel:LELG_00652; -. DR InParanoid; A5DTG6; -. DR KO; K00547; -. DR OMA; SYIGKWR; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000001996; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001996}; KW Reference proteome {ECO:0000313|Proteomes:UP000001996}. SQ SEQUENCE 326 AA; 36653 MW; AB0813C386702A68 CRC64; MSQNIFNKKV VLDGALGTAL EDLIDPSAPY LPSKSPLWSG QVLLDAPELI QKVHEMYIGA GSEVIFTSTY QLSYDSLRKH TTLSDEQILE VWQRSIDLVR AAALSIDETA RYTKEKESRG EPGKVHIAGS IGPYAAYLAN GSEYTGDYGN VTDEQLEAFH TPMLEFFTEN EAVDLIAFET IPNFQELKAV TKLVKRLNCK KPVLFSITCQ NLDNLTDGTP LLEVKKYLDF CLPKEQKILG INCVEYTLVQ GIMSHFAGFK FYVYPNLGFE YDLEKHQFVI KEGRSEDDWR LFVENLASKE AVIGIGGCCN TGVKEIEQIS QVMYKE // ID A5ES00_BRASB Unreviewed; 1287 AA. AC A5ES00; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 29-APR-2015, entry version 62. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABQ38944.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABQ38944.1}; GN Name=metH {ECO:0000313|EMBL:ABQ38944.1}; GN OrderedLocusNames=BBta_7061 {ECO:0000313|EMBL:ABQ38944.1}; OS Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=288000 {ECO:0000313|EMBL:ABQ38944.1, ECO:0000313|Proteomes:UP000000246}; RN [1] {ECO:0000313|EMBL:ABQ38944.1, ECO:0000313|Proteomes:UP000000246} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BTAi1 / ATCC BAA-1182 {ECO:0000313|Proteomes:UP000000246}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000494; ABQ38944.1; -; Genomic_DNA. DR RefSeq; WP_012046873.1; NC_009485.1. DR RefSeq; YP_001242850.1; NC_009485.1. DR ProteinModelPortal; A5ES00; -. DR SMR; A5ES00; 655-1235. DR STRING; 288000.BBta_7061; -. DR EnsemblBacteria; ABQ38944; ABQ38944; BBta_7061. DR KEGG; bbt:BBta_7061; -. DR PATRIC; 21214779; VBIBraSp29847_7039. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; BSP288000:GJBR-6775-MONOMER; -. DR Proteomes; UP000000246; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000246}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABQ38944.1}; KW Transferase {ECO:0000313|EMBL:ABQ38944.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 767 767 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1287 AA; 140039 MW; 9CB9E124B3ABA33A CRC64; MSAPVSPART AFLTAARERI LILDGAMGTM IQALQFDEAA FRSERFKDFH RDLRGNNDLL ILTQPEAIED IHAQYLRAGA DIVATNTFSA TSIAQADYDL SDIIYELNRE GARLARNAAT RVAAEDGKQR FVAGAMGPTN RTASISPDVS NPGYRAVTFD DLRIAYGEQA RGLLDGGADL LLVETIFDTL NAKAALYAIA ELCEARGIDV PVMISGTITD KSGRLLSGQM PEAFWNSVRH AKPLTIGFNC ALGAEDLRAH VADIGRVADT LVCAYPNAGL PNEFGQYDET PAYMARLIGE FARDGLVNIV GGCCGTTPDH IAAIAAAVAP HKPRAVPEIA PRLRLSGLEP FELTPEIPFV NVGERTNVTG SAKFRKLITA GDYTAALQVA RDQVENGAQV IDVNMDEGLL DSEAAMRTFL NLVAAEPDIA RVPVMVDSSK FHVIEAGLKC VQGKPVVNSI SLKEGEEKFI HEAKIARRHG AAVVVMAFDE TGQADTYKRK TEICARAYKI LVEQIGFPPE DIIFDPNIFA IATGIEEHNN YGVDFIEATR WIRSNLPHAH VSGGVSNLSF SFRGNEPVRE AMHSVFLYHA IKAGMDMGIV NAGQMIVYDD IDPELRQVCE DVVLNRDPGA SERLLALAEK FRGQGKQTKE ADLAWRDWPV DKRLSHALVH GITEFIEVDT EEARAASTRP LDVIEGPLMA GMNVVGDLFG DGKMFLPQVV KSARVMKQAV AYLMPFMEAE KAANKGRANE RSNAGKIVLA TVKGDVHDIG KNIVGIVLQC NNFEVIDLGV MVPAAKIIET AKTENADIIG LSGLITPSLD EMAYLASEME RQGLNMPLLI GGATTSRVHT AVKIDPNYQS GPVVHVNDAS RAVGVASSLL SAERKDAYAA EIRTEYQKIA AAHLRGQADK KRLKLSDARA NAPKIDFAKA RPVKPTFLGV KTFADYDLAE LVPYIDWTPF FQTWELAGRF PAILDDAKVG EAARALYDDA LKMLKRIVDE KWFTARAAIG FWPANAEGDD IVLYADDSRT ERIATLHTLR QQLEKREGRF NTALSDFVAP VGSSVPDYVG GFVVTAGLGE DAVADRFKNA NDDYSSILVK ALADRLAEAF AERLHARVRR EFWAYAPDEA LSPDDLILEK YQGIRPAPGY PAQPDHTEKA TLFELLDAEN NAGVRLTESF AMWPGSSVSG LYFASPESFY FGVGKIERDQ VEDYATRKGM TVAEVERWLA PILNYIPARG GQEAETSRAT TAPAPANDTA PAELAGHPPG CTCAVHLAWR KKAVGAK // ID A5FJS2_FLAJ1 Unreviewed; 334 AA. AC A5FJS2; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 27-MAY-2015, entry version 47. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABQ04540.1}; GN OrderedLocusNames=Fjoh_1508 {ECO:0000313|EMBL:ABQ04540.1}; OS Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / UW101) OS (Cytophaga johnsonae). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=376686 {ECO:0000313|EMBL:ABQ04540.1, ECO:0000313|Proteomes:UP000006694}; RN [1] {ECO:0000313|EMBL:ABQ04540.1, ECO:0000313|Proteomes:UP000006694} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17061 / DSM 2064 / UW101 RC {ECO:0000313|Proteomes:UP000006694}; 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; ABQ04540.1; -; Genomic_DNA. DR RefSeq; WP_012023586.1; NC_009441.1. DR RefSeq; YP_001193859.1; NC_009441.1. DR STRING; 376686.Fjoh_1508; -. DR EnsemblBacteria; ABQ04540; ABQ04540; Fjoh_1508. DR KEGG; fjo:Fjoh_1508; -. DR PATRIC; 21897357; VBIFlaJoh53613_1554. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; FJOH376686:GIXN-1538-MONOMER; -. DR Proteomes; UP000006694; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006694}; KW Methyltransferase {ECO:0000313|EMBL:ABQ04540.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006694}; KW Transferase {ECO:0000313|EMBL:ABQ04540.1}. SQ SEQUENCE 334 AA; 36705 MW; A6064797A5C7BDE6 CRC64; MAITIQEAIK KNILILDGAM GTMLQRYNFS EEDFRGERFK DFPHPLKGNN DLLSLTQPQA IRDVHAAYYE AGADIVETNT FSGTTIGMAD YHMEDLVYEL NYESAKIARQ VADEFTAKNP EKPRFVAGSI GPTNRTASMS PDVNDPGYRA VTFDDLRIAY KQQAEALMDG GCDLLLVETI FDTLNAKAAL FAIEEVKEER NIDIPIMVSG TITDASGRTL SGQTVEAFLI SVSHIPLLSV GFNCALGADL LKPYLKTLAH NTSFNVSAHP NAGLPNAFGQ YDETPEQTQV FIKEYLEDNL INIIGGCCGT TPDHIRLMAE VAKDYKPRIA PVIA // ID A5FZ72_ACICJ Unreviewed; 1171 AA. AC A5FZ72; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 27-MAY-2015, entry version 65. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABQ30904.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABQ30904.1}; GN OrderedLocusNames=Acry_1700 {ECO:0000313|EMBL:ABQ30904.1}; OS Acidiphilium cryptum (strain JF-5). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acidiphilium. OX NCBI_TaxID=349163 {ECO:0000313|EMBL:ABQ30904.1, ECO:0000313|Proteomes:UP000000245}; RN [1] {ECO:0000313|EMBL:ABQ30904.1, ECO:0000313|Proteomes:UP000000245} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JF-5 {ECO:0000313|EMBL:ABQ30904.1, RC ECO:0000313|Proteomes:UP000000245}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000697; ABQ30904.1; -; Genomic_DNA. DR RefSeq; WP_011942428.1; NC_009484.1. DR RefSeq; YP_001234823.1; NC_009484.1. DR ProteinModelPortal; A5FZ72; -. DR STRING; 349163.Acry_1700; -. DR EnsemblBacteria; ABQ30904; ABQ30904; Acry_1700. DR KEGG; acr:Acry_1700; -. DR PATRIC; 20648434; VBIAciCry6074_2198. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; ACRY349163:GHET-1726-MONOMER; -. DR Proteomes; UP000000245; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000245}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABQ30904.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000245}; KW Transferase {ECO:0000313|EMBL:ABQ30904.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 234 234 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 301 301 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 742 742 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1171 AA; 129357 MW; 319E0AADB56C3057 CRC64; MWRASYIPTT MSRPSLLEAL RHRVLLCDGG MGSRVQALTL DTERDFWGKE NCTEVLNLSR PDLVREIHRG YYEAGADMVE TNSFGGSPIT LAEFELGDRA REINRVAAEL AREAAETFAD GRDRYVIGSV GPGTKLPTLG NIEYDPLEAG LAEQCRGLIE GGVDAILIET CQDTLQIKAA VNGARIARAE QKRDTPIFVQ VTVETTGTLL VGPDIAAAAT VIQALDVPLI GLNCATGPQE MAEHVRYLAQ NWPGLISVQP NAGLPELVDG KTHYPLTPDE LATWLERFIR EDGINLIGGC CGTSTPHIAA LDAMLRRLGE VRPAPVPRKP VWIPSVASLY GSTPLRQENA YFSIGERCNA NGSKKWRELQ ERHDWDGCIA MGREQVAEAS NALDICTAFV GRDELGEMSE IITRFTSSVN APLVIDSTET PVIEAALKLH GGKPIINSIN FEDGEHIAEE RMLLARKFGA AVIALTIDET GMAKEPAQKL EIATRLVDFA CRKHGLPQSD LLIDPLTFTI ATGNEDDRKL GLWTLEGIRL IRDAFPDIQI ILGLSNISFG LNPAARAVLN SVFLDHAVKA GMTGAIVHVS KIRPLHLIPL EEVQVMEDLI FDRRREDYDP LQRVLEMFAD RKAADAVKKA RADTVEGRLR DRIVDGDRKG LADDLDEAMK THAPLDIINN LLLDGMKTVG ELFGAGKMQL PFVLQSAETM KAAVAYLEPY MERVEGQQKG TIVLATVKGD VHDIGKNLVD IILTNNGYRV VNLGIKVPLA DMVAAAREHR AHAIGMSGLL VKSTVVMREN LEEMSRQGLD IPVLLGGAAL TRNYVEEDCV AAYASGRVAY ARDAFDGLHL MDRVTGNGFD DYLAALQSKR RGKARNTKRT LGQADARGFA PVDISAAQAR RRRLTRETPV PTPPFWGARI IEAPQKALVP YINERSLFQF QWGFRKQGKS LEDFMGWARQ ELRPVMKRML DLCAADSILK PQAIYGYWKA AGQGNDLILF AEDGATELAR FTLPRQPRDD GDCIADFFRD VDDAERDVIG LQVVTMGAKA SETARAWFEE NRYQDYLYLH GLSVEMAEAM AEYTHKRIRA ELGFAAEDDR DMEKMLAQSY RGSRYSFGYP ACPNLEDQIL LLRLLDAERI GVSLSDEHQL HPEQSTSAIV VLNPHAKYFS V // ID A5GBX1_GEOUR Unreviewed; 604 AA. AC A5GBX1; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 29-APR-2015, entry version 60. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=Gura_0708 {ECO:0000313|EMBL:ABQ24918.1}; OS Geobacter uraniireducens (strain Rf4) (Geobacter uraniumreducens). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=351605 {ECO:0000313|EMBL:ABQ24918.1, ECO:0000313|Proteomes:UP000006695}; RN [1] {ECO:0000313|EMBL:ABQ24918.1, ECO:0000313|Proteomes:UP000006695} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Rf4 {ECO:0000313|EMBL:ABQ24918.1, RC ECO:0000313|Proteomes:UP000006695}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Note=FAD.; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {ECO:0000256|RuleBase:RU004255}. CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ABQ24918.1; -; Genomic_DNA. DR RefSeq; WP_011937642.1; NC_009483.1. DR RefSeq; YP_001229491.1; NC_009483.1. DR ProteinModelPortal; A5GBX1; -. DR STRING; 351605.Gura_0708; -. DR EnsemblBacteria; ABQ24918; ABQ24918; Gura_0708. DR KEGG; gur:Gura_0708; -. DR PATRIC; 22031314; VBIGeoUra13052_0750. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; GURA351605:GI6A-717-MONOMER; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000006695; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004255}; KW Complete proteome {ECO:0000313|Proteomes:UP000006695}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ABQ24918.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000006695}; KW Transferase {ECO:0000313|EMBL:ABQ24918.1}. SQ SEQUENCE 604 AA; 64355 MW; 1C72796D9590884D CRC64; MNFSDRLRHE VLVGDGAIGT MLYAKGVSLD ANFEHLNLVR PELVLGLHQE YVAAGAQVIE TNTFGANYPK LHAIGLGNKV HDINLKGALL ARRAAEGRDA FVAGSIGPLV KLKGEERDLG EREMLEIFRA QVTALTEGGV DLFILETFSD LRQIEIALQV AKETGLPVVA NMAFGENSRI AGGIEAEAVA ERLAAAGADV VGANCGAGPL EILRTVKRMG AVIELPIAAY PNSGFPEYVD GRYIYRATPE YFAGMAAEMV AVGAALVGGC CGTTPAHIMR IAEKVRGLKP VPRAPAPPVH AVERGGVREG TGPGFLAGWG KEKIVTVELD PPKGLDCSKV LIGSRILKDA GADAINLAEN PLARVRMGNI ALASLIQKEV GIEVIVHITC RDRNLLGLQS DLMGASLLGI RSILAVTGDP ASLGEQAGAS SVFDLNSFTL IKLLNGLNGG VNALGNPIGS GTRFTIGAAF NPNTQRMDVQ AGRLAKKVVN GACFAQTQPI YDVQRLDEMI EQTAHLDIPI LPGILPLVSE RNAEFLHNEV PGIIIPEEIR MRMRGKEKDE GVREGLAIAR EFIAAVRERV GGFYLIPPFG RYEIAAELVK YIKG // ID A5GCJ3_GEOUR Unreviewed; 804 AA. AC A5GCJ3; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 27-MAY-2015, entry version 56. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABQ24704.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABQ24704.1}; GN OrderedLocusNames=Gura_0489 {ECO:0000313|EMBL:ABQ24704.1}; OS Geobacter uraniireducens (strain Rf4) (Geobacter uraniumreducens). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=351605 {ECO:0000313|EMBL:ABQ24704.1, ECO:0000313|Proteomes:UP000006695}; RN [1] {ECO:0000313|EMBL:ABQ24704.1, ECO:0000313|Proteomes:UP000006695} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Rf4 {ECO:0000313|EMBL:ABQ24704.1, RC ECO:0000313|Proteomes:UP000006695}; 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; ABQ24704.1; -; Genomic_DNA. DR RefSeq; WP_011937429.1; NC_009483.1. DR RefSeq; YP_001229277.1; NC_009483.1. DR ProteinModelPortal; A5GCJ3; -. DR STRING; 351605.Gura_0489; -. DR EnsemblBacteria; ABQ24704; ABQ24704; Gura_0489. DR KEGG; gur:Gura_0489; -. DR PATRIC; 22030858; VBIGeoUra13052_0524. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; GURA351605:GI6A-496-MONOMER; -. DR Proteomes; UP000006695; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006695}; KW Methyltransferase {ECO:0000313|EMBL:ABQ24704.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006695}; KW Transferase {ECO:0000313|EMBL:ABQ24704.1}. SQ SEQUENCE 804 AA; 84973 MW; 24C9490D42E03DD5 CRC64; MKQPFLQAMK ERVLVLDGAM GTMLQERGLK PGQSPEELNL TMPDVVAGVH REYIEAGADI IVTNTFGGNR AKLAHHGLAA KVREINARAV EIARKVAGEH AYVAASIAPT GRFVEPVGDA SFDEMCDIFR EQAQALIDAG VDAISFETFL DIKEIRAGII AVREIAPAIP IIAMLTFDDK GRSVLGTPPE SAAITLEAVG ADIVGSNCGL GVEGIYEILS AMRRVTRLPL ISQANAGLPV LKDGKTIFPA TPAEMTAYHD RMLELGVRII GGCCGTTPAH IRAIKAALAE KDQSVRAGGP AEGITWLSSR GGFTALGKGR PVAVIGERIN PTGKKGFAAE LREGKVSYIR REALDQVAAG ATLLDVNVGA PGIDEPAAME RAVFCAGSAV SVPLVLDSSS PEALERGLKA ADGKVLINSV NGEEKSLARV LPLAKKYGAA VIGLTLDEKG IPETAEERTA VAQKIAERAL SLGISRKNVV IDCLTLAVSA EQKRAMETLS AIRLVKGRLG LNTVLGVSNI SFGLPCRPLI SSAFFAMAME AGLDAAIVNP KEQAMMDVWR SVMVLLNRDP NAAAYIDAYK GAVATLAGTQ VQEPPQDIKG RLAKAVIDGD VENIVALVET AFAEGLSPLD ISNGGLLPGL EEVGRRFEKN IVFLPQVMLS AETMKTAFAR LKQEMKGMSL ESQGKILMAT VEGDIHDIGK NIVCTLLENH GFEVIDLGKN VPAARIIAEA KAHDVDAVGL SALMTTTMSE MENVVRQLKA AGVKTFTMVG GAVLTQEYAT EIGADLYAKD AMEAVARIKA ILGK // ID A5GL88_SYNPW Unreviewed; 1205 AA. AC A5GL88; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 29-APR-2015, entry version 59. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CAK23703.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAK23703.1}; GN Name=metH {ECO:0000313|EMBL:CAK23703.1}; GN OrderedLocusNames=SynWH7803_1277 {ECO:0000313|EMBL:CAK23703.1}; OS Synechococcus sp. (strain WH7803). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechococcus. OX NCBI_TaxID=32051 {ECO:0000313|EMBL:CAK23703.1, ECO:0000313|Proteomes:UP000001566}; RN [1] {ECO:0000313|Proteomes:UP000001566} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WH7803 {ECO:0000313|Proteomes:UP000001566}; RG Genoscope; RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CT971583; CAK23703.1; -; Genomic_DNA. DR RefSeq; WP_011933183.1; NC_009481.1. DR RefSeq; YP_001225000.1; NC_009481.1. DR ProteinModelPortal; A5GL88; -. DR STRING; 32051.SynWH7803_1277; -. DR EnsemblBacteria; CAK23703; CAK23703; SynWH7803_1277. DR KEGG; syx:SynWH7803_1277; -. DR PATRIC; 23828698; VBISynSp43824_1310. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR Proteomes; UP000001566; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001566}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAK23703.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001566}; KW Transferase {ECO:0000313|EMBL:CAK23703.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 238 238 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1205 AA; 131810 MW; EB2DB1C39AEA33B9 CRC64; MQAVQSKSGP ATSRFLARLH DPCKPVLVFD GATGTSLQQM DLTAEDFGGE ALEGCNENLV VTRPDAVQAV HRLFLDAGCD VIETDTFGAA SVVLAEYGLE DQAFELNRRA AELAREMADH YSNDTKPRFV AGSMGPTTKL PTLGHIDFDT LRDSFQEQAA GLLAGDVDLF IIETCQDVLQ IKAALQGVEA AFEASGQRRP LMVSVTMETT GTMLVGSDIA AVVSILEPFP IDVLGLNCAT GPEQMKEHIK YLSEYSPFVV SCIPNAGLPE NIGGVAHYRL TPLELKMQLM HFVEDLGVQV IGGCCGTTPA HIKALSEISE ELTPATRDVR TLHLERQQLS YEPSASSIYG STPYFQDNSF LIIGERLNAS GSKKVRELLN EEDWDGLVAV ARGQVKENAH VLDVNVDYVG RDGEKDMHEL VTRVVTNVNL PLMLDSTEWQ KMEAGLKVAG GKCILNSTNY EDGDERFFKV LELARRFGAG VVIGTIDEDG MARTAEKKLA IAKRAYRDAV EFGIPAREIF YDPLALPIST GIEEDRRNGA ETIEAIRRIR SELPGVHVVL GVSNVSFGLS PAARITLNSV FLHDCCEAGM DAAIVSPAKI LPLIKIDDDH QQVCRDLISD ARRFEGDVCV YDPLTELTTL FEGVSTKDAR ASGPSLADLP VEERLKQHII DGERIGLEDA LNEGLQSYPP LDIVNTFLLD GMKVVGELFG SGQMQLPFVL QSAETMKAAV AFLEPHMEKS DGKRSAKAKF LIATVKGDVH DIGKNLVDII LTNNGYEVIN LGIKQDVGAI IAAQQEHEAD CIAMSGLLVK STAFMKDNLQ AFNEAGINVP VVLGGAALTP RFVNKDCSDV YNGKVIYGRD AFTDLRFMDA FVEARKDGSW DNLKGFINGN PEGVSVGGDF ESASDETTDV GASTPESEQQ ANLQVTDERS DAVPEEAALR PDFLGSKVLQ GVEQIPLNEV IAYLDRQALF AGQWQMRKAK DQTREDYEAD LKTKAEPILQ TWLERSLNED LLQPAVAYGY FPCGRDGNAV AVFDPDSNQE LGRFALPRQR SGNRYCIADF YRDLSSGQPT DVLPMQAVTM GEKASVFAQK LFEADSYSDY LFFHGLAVQM AEALAEWTHA RIRRECGFAD PDGMPLRDVL AQRYRGSRYS FGYPACPNVA DSRQQLLWLG AERIGLSMDE SDQLHPEQST TALVALHSAA RYFSA // ID A5GTA3_SYNR3 Unreviewed; 1196 AA. AC A5GTA3; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 27-MAY-2015, entry version 63. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CAK28112.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAK28112.1}; GN Name=metH {ECO:0000313|EMBL:CAK28112.1}; GN OrderedLocusNames=SynRCC307_1209 {ECO:0000313|EMBL:CAK28112.1}; OS Synechococcus sp. (strain RCC307). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechococcus. OX NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK28112.1, ECO:0000313|Proteomes:UP000001115}; RN [1] {ECO:0000313|Proteomes:UP000001115} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115}; RG Genoscope; RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CT978603; CAK28112.1; -; Genomic_DNA. DR RefSeq; WP_011935626.1; NC_009482.1. DR RefSeq; YP_001227465.1; NC_009482.1. DR ProteinModelPortal; A5GTA3; -. DR STRING; 316278.SynRCC307_1209; -. DR EnsemblBacteria; CAK28112; CAK28112; SynRCC307_1209. DR KEGG; syr:SynRCC307_1209; -. DR PATRIC; 23823313; VBISynSp108374_1211. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR Proteomes; UP000001115; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001115}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAK28112.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001115}; KW Transferase {ECO:0000313|EMBL:CAK28112.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 228 228 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 752 752 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1196 AA; 130910 MW; 08D8FC560DD0DD4D CRC64; MMHRFLERLH APERPVLVFD GATGTSLQQM DLGPDDFGGA ALEGCNENLV VTRPDAVQEV HRQFLEAGCD VIETDTFGAT SLVLAEYDLQ DQTYELNVKA AQLAREMADR YSTPEKPRFV AGSMGPTTKL PTLGHVGFDA MRDSFAEQAR GLLAGNVDLF IIETCQDPLQ IKAALAGLEQ AFAAAGERRP VMVSVTMETT GTMLVGSDIA AVVAILEPFP IDVLGLNCAT GPEQMKEHVR YLSAHAPFVV SCIPNAGLPE NVGGVAHYRL TPVEMKMAMH HFIEDLGVQV IGGCCGTTPA HIAALAELAQ EMTPAERPVR TPQAQLQRPL LGAEASAASI YGTTPYHQDN SFLIIGERLN ASGSKKVREL LNSEDWDGLV AVARGQVKEN AHVLDVNVDY VGRDGEKDMH DLVSRLVTNV NLPLMLDSTE WQKMEAGLKV AGGKCLLNST NYEDGDERFF KVLELARTYG AGVVVGTIDE EGMARTADRK FAIAQRAYRD AVEFGIPAHE IFYDPLALPI STGIEEDRRN GCETIEAIRR IITDLPGVHV VLGVSNISFG LSPAARITLN SVFLHDCCEA GMDAAIVSPA KILPLMKISD EHQQVCRDLI NDNRRFEGSV CIYDPLTELT TMFEGVSTKE ARASGPSLAD LPVEERLKQH IIDGERIGLE PALDEGLQNY KPLQIVNTFL LDGMKVVGEL FGSGQMQLPF VLQSAETMKS AVAYLEPHME KTEGESSGKA KFLIATVKGD VHDIGKNLVD IILTNNGYEV VNLGIKQSVD AIIEAQQTHQ ADCIAMSGLL VKSTAFMKDN LQAFNDAGIS VPVILGGAAL TPRFVQKDCR EVYNGQVIYG RDAFADLRFM DALVDAKKGG EWSDTEGFLG AVPEGLGLNG DAHSDSASSD GAASEPTEEK PSLPVSLERS AAVPEEPALE PPFWGTKVLS EQDMDLEEVF GYLDRNALFA GQWQMRKSKD QSREEYEQQL RDKAEPVLQE WLQRARSEKL LTPRVAYGYF PCGRDGNAVV VFDPNDTTRE LGRFELPRQR SGNTYCIADF YRDLSSNGEP TDMLPMQAVT MGEKASAFAK ELFQADRYSD YLYFHGLGVQ MAEALAEWTH ARIRAELGFA ADEPEALRDV LAQRYRGSRY SFGYPACPNV ADSRPQLDWL EADRIGLSMD DSDQLEPEQS TTALVALHSQ ARYFSA // ID A5I293_CLOBH Unreviewed; 792 AA. AC A5I293; A7G3Z3; DT 26-JUN-2007, integrated into UniProtKB/TrEMBL. DT 26-JUN-2007, sequence version 1. DT 27-MAY-2015, entry version 67. DE SubName: Full=Putative methionine synthase {ECO:0000313|EMBL:CAL83158.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAL83158.1}; GN Name=metH {ECO:0000313|EMBL:CAL83158.1}; GN OrderedLocusNames=CBO1623 {ECO:0000313|EMBL:CAL83158.1}; OS Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=441771 {ECO:0000313|Proteomes:UP000001986}; RN [1] {ECO:0000313|EMBL:CAL83158.1, ECO:0000313|Proteomes:UP000001986} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A [Sanger] RC {ECO:0000313|Proteomes:UP000001986}; RX PubMed=17519437; DOI=10.1101/gr.6282807; RA Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T., 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., 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). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM412317; CAL83158.1; -; Genomic_DNA. DR RefSeq; WP_011949155.1; NC_009698.1. DR RefSeq; YP_001254125.1; NC_009495.1. DR RefSeq; YP_001387508.1; NC_009698.1. DR ProteinModelPortal; A5I293; -. DR STRING; 413999.CBO1623; -. DR EnsemblBacteria; ABS36462; ABS36462; CLC_1650. DR GeneID; 5185878; -. DR GeneID; 5399477; -. DR KEGG; cbh:CLC_1650; -. DR KEGG; cbo:CBO1623; -. DR PATRIC; 19365307; VBICloBot22612_1597. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CBOT413999:GJ72-1678-MONOMER; -. DR BioCyc; CBOT441771:GIWX-1618-MONOMER; -. DR Proteomes; UP000001986; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001986}; KW Methyltransferase {ECO:0000313|EMBL:CAL83158.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001986}; KW Transferase {ECO:0000313|EMBL:CAL83158.1}. SQ SEQUENCE 792 AA; 87938 MW; 96B510D117168060 CRC64; MNIKDYIKEN VLIFDGAMGT MLQKLGLKIS DLPEELNILE PEKIINIHRK YIEAGAKVIT TNTFGANEIK LKQSKFSLES IIDKAIDNVK KAGKNKEILI ALDIGPIGQL LEPMGTLKFE EAYEIFKRQI VQGQKSGADI ILIETMTDLY EAKAAILAAK ENTNLPVFCT MTFEKNKRTF TGCTPLSMVL TLEGLGVDAL GVNCSLGPNE LGDIVDEIIK YSSIPIMVQP NAGLPTIKAG RTIYNIEPKE FADFQRSIVE KGVRIVGGCC GTTDEFIREI VYSLKDIKIK KLKENNIYGV CSSTKSVLIE GVKIIGERIN PTGKKLFKEA LRNNDTDYIL KEAISQVECG ADILDVNVGL PEIDEEETMK KVIKEIQSII DTPLQIDSNN PKVIEKALRV YNGKAIVNSV NGEEKILDSV LPLIKKYGAS VVGLTLDDKG IPKKAEERLK IAEKIVNKAL DYGIKRKDIF IDCLVLTASA QQEDVRETLK AVTLVKEKLN VKTILGVSNI SFGLPNRELI NKTFLAMSLQ SGLDLPILNP NNKEMINIIN AYKVLNNEDK RAANYIERYT NEISNSREVK IPKNDLTLKE IVMKGIKEES YSKTKDLLKD RGELSIINEE LIPALDEVGD KYEKGIIFLP QLIQSAETVK KAFTAIKEKL REDNSPKINK GKILMATVKG DIHDIGKNIV KVILENYGFD IIDLGKDVEA EKIVEEVKKN NIKLVGLSAL MTTTVNSMRD TIKILKESGM DCKVFVGGAV LNEEYAKMIN ADYYAKDAKE AVDIAKGFFG GF // ID A5IKF3_THEP1 Unreviewed; 768 AA. AC A5IKF3; DT 26-JUN-2007, integrated into UniProtKB/TrEMBL. DT 26-JUN-2007, sequence version 1. DT 27-MAY-2015, entry version 56. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABQ46676.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABQ46676.1}; GN OrderedLocusNames=Tpet_0656 {ECO:0000313|EMBL:ABQ46676.1}; OS Thermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=390874 {ECO:0000313|EMBL:ABQ46676.1, ECO:0000313|Proteomes:UP000006558}; RN [1] {ECO:0000313|Proteomes:UP000006558} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RKU-1 / ATCC BAA-488 / DSM 13995 RC {ECO:0000313|Proteomes:UP000006558}; 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., Tapia R., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., RA Noll K., Richardson P.; RT "Complete sequence of Thermotoga petrophila RKU-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; CP000702; ABQ46676.1; -; Genomic_DNA. DR RefSeq; WP_011943266.1; NC_009486.1. DR ProteinModelPortal; A5IKF3; -. DR SMR; A5IKF3; 1-565. DR STRING; 390874.Tpet_0656; -. DR EnsemblBacteria; ABQ46676; ABQ46676; Tpet_0656. DR KEGG; tpt:Tpet_0656; -. DR PATRIC; 23944076; VBIThePet65348_0663. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; TPET390874:GHJI-672-MONOMER; -. DR Proteomes; UP000006558; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006558}; KW Methyltransferase {ECO:0000313|EMBL:ABQ46676.1}; KW Transferase {ECO:0000313|EMBL:ABQ46676.1}. SQ SEQUENCE 768 AA; 85826 MW; D813CEDA8A3B863B CRC64; MRNRREVSKL LSERVLLLDG AYGTEFMKYG YDDLPEELNI KAPDVVLKVH RSYIESGSDV ILTNTFGATR MKLRKHGLED KLDPIVRNAV RIARRAAGEK LVFGDIGPTG ELPYPLGNTL FEEFYENFRE TVKIMVEEGV DGIIFETFSD ILELKAAVLA AREVSRDVFL IAHMTFDEKG RSLTGTDPAN FAITFDELDV DALGINCSLG PEEILPIFQE LSQYTDKFLV VEPNAGKPIV ENGKTVYPLK PHDFAVHIDS YYELGVNIFG GCCGTTPEHV KLFRKVLGNR KPLKRKKKRI FAVSSPSKLV TFDHFVVIGE RINPAGRKKL WAEMQKGNEE IVINEAKTQV EKGAEVLDVN FGIESQIDVR YVEKIVQALP YVSNVPLSLD IQSVDLTEKA LRTYPGRPLF NSSKVDEEEL EKKINLLKKY GGTLIVLLMG KDVPKSFEER KEYFEKALKI LERHNFSDRV IFDPGVLPLG AEGKPVEVLK TIEFISNRGF NTTVGLSNLS FGLPDRSYYN TAFLVLGISK GLSSAIMNPL DEILMKTLNA TLVILEKKEL PRAEVKEEKL VEIILSGNRS ELERLVEDFL KEKDPLSIIE EQLRPAMERI GELYDKGKIF LPQLILAAQT VKPAFDKLTS MLPSDSQGET FVIATVKGDV HDIGKNIVAS VIRSSGYRVV DLGKDVETSK ILETVEKERP VALGLSAMMT TTVGRIKEVV EKLKEKNLKI PVIVGGASLN EKLAKELGAD YYARNASEAV KILKSLGR // ID A5K8K1_PLAVS Unreviewed; 508 AA. AC A5K8K1; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 39. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDL44147.1}; GN ORFNames=PVX_100640 {ECO:0000313|EMBL:EDL44147.1}; OS Plasmodium vivax (strain Salvador I). OC Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium). OX NCBI_TaxID=126793 {ECO:0000313|Proteomes:UP000008333}; RN [1] {ECO:0000313|EMBL:EDL44147.1, ECO:0000313|Proteomes:UP000008333} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Salvador I {ECO:0000313|EMBL:EDL44147.1, RC ECO:0000313|Proteomes:UP000008333}; 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., 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., Korsinczky M., Meyer E.V., Nene V., Paulsen I., RA White O., Ralph S.A., Ren Q., Sargeant T.J., Salzberg S.L., RA Stoeckert C.J., Sullivan S.A., Yamamoto M.M., Hoffman S.L., RA Wortman J.R., Gardner M.J., Galinski M.R., Barnwell J.W., RA 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. {ECO:0000313|EMBL:EDL44147.1}. 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; AAKM01000010; EDL44147.1; -; Genomic_DNA. DR RefSeq; XP_001613874.1; XM_001613824.1. DR ProteinModelPortal; A5K8K1; -. DR GeneID; 5473155; -. DR KEGG; pvx:PVX_100640; -. DR EuPathDB; PlasmoDB:PVX_100640; -. DR HOGENOM; HOG000283439; -. DR InParanoid; A5K8K1; -. DR Proteomes; UP000008333; Chromosome 14. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 4. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 4. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008333}; KW Reference proteome {ECO:0000313|Proteomes:UP000008333}. SQ SEQUENCE 508 AA; 56609 MW; 3CB63EF233DFFE4C CRC64; MAKEVFTLDG GKISELERLG VGNFDFLSCH DEGDEEQMVS TLENIHLSYL LAGCNVISTN TFQVNLHSLQ EKGISVQDGE GIVDRYIDIA HRALLRYEGI KRSEDFPLFH LCPLEDSSPY EHLEGFQQMR NHLGIVHPKD SVNTREYVDS FDLSPGGWGG SPIRRCPGRY VAFATGGYSA AFRDFSEYSG VMRKGGAPGK AAPLGNAMTS CKPQNQQYDI FISTPTLHAD DQPPSIKMIP VSSRESGRER GGPSREAAPN RHLFNYGLEY YVDVGDEEII SNCNFKLGAY KRNEEKLHLF SLLTSSNVRE VLTLYSHLVK CGGHFDTNVV VSFYCNDGQH IGCCGYSFVD VVLILLYLDS RNRFIKAIGL NCVSIDSVRE LFAPLTRCIS SDGTVDVDAY GSPSGELSGL TKTILKGLKK NRFLGDIHFF ASPNKSLNRV TYDYEGREVH FETTQERHKH VCNYVGEWLH VGLSGFGGCC YYNPYDISLL DYKLGQLAGG VAVREKQR // ID A5KL27_9FIRM Unreviewed; 826 AA. AC A5KL27; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 42. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EDK24665.1}; GN ORFNames=RUMTOR_00931 {ECO:0000313|EMBL:EDK24665.1}; OS Ruminococcus torques ATCC 27756. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Blautia. OX NCBI_TaxID=411460 {ECO:0000313|EMBL:EDK24665.1}; RN [1] {ECO:0000313|EMBL:EDK24665.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27756 {ECO:0000313|EMBL:EDK24665.1}; 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 (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EDK24665.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27756 {ECO:0000313|EMBL:EDK24665.1}; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Ruminococcus torques (ATCC 27756)."; 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. {ECO:0000313|EMBL:EDK24665.1}. 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; AAVP02000003; EDK24665.1; -; Genomic_DNA. DR RefSeq; WP_004844944.1; NZ_DS264344.1. DR ProteinModelPortal; A5KL27; -. DR EnsemblBacteria; EDK24665; EDK24665; RUMTOR_00931. DR PATRIC; 31168055; VBIRumTor82068_0040. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDK24665.1}; KW Transferase {ECO:0000313|EMBL:EDK24665.1}. SQ SEQUENCE 826 AA; 90755 MW; A9D2C7AB0EC769C4 CRC64; MIRQRLGKDL LFFDGGMGTL LQEKGLAPGE LPETWNLTHS EEIYKIHRQY IEAGSDIILT NTFGANALKF HDDSCSLEEI IKAAVSHVKK AEREALLQTG DERKIYTALD VGPTGKLLKP MGDLEFETAY EAFKEVVILG EQAGADLIHI ETMSDTYELK AAVLAAKENT SLPVFATVIF DERKKLLTGA DVSSVVALLE GLGVDALGIN CAMGPKEMLP VLEELIKYSS VPIIVKPNAG LPKQRDGKTY YDVTEDEFAA YMEQIVRMGA CVIGGCCGTT PEHIRAMRKR CENAELVPVT EKEFTVVSSY GQSVILGEGS KIIGERINPT GKKRFKQALK EHDLDYILRE GITQQDQGAH ILDVNVGLPD IDEPALMEEV VQELQSVVNI PLQIDTVDEK AMEKALRIYN GKAMVNSVSG KKESMEKVFP LVKKYGGVVI GLTLDEDGIP ADADGRVRIA EKIIKTAEKF GIKKKDIVID ALAMTISSEP EGAKVTLETL RRLRDEIGVN TVLGVSNISF GLPCRPIVNA AFYTMAMLNG LSAGIINPSS EDMMKSWYAY HALMNLDNNC EQYIQKYANS VVSTNIMKTS ELSETKLKGE NDRSRKSSSK MTLQEAIEKG LRDDAGKITT DMIATEAPLD IINEELIPAL NHVGDGFEKG TVFLPQLLMS AEAAKSAFSV LKEKMEKSGE IREKKGRVIL ATVKGDIHDI GKNIVKVLLE NYSFDVIDLG KDVSPEKIVE TACEKQVPLV GLSALMTTTV VSMEETIKML REKKPDCKVM VGGAVLNQEY ADMIGADFYG KDAMQSVHYA EKIFKDALQK SADKKE // ID A5KUF8_VIBBS Unreviewed; 299 AA. AC A5KUF8; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EDK31116.1}; GN ORFNames=VSWAT3_13627 {ECO:0000313|EMBL:EDK31116.1}; OS Vibrionales bacterium (strain SWAT-3). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC unclassified Vibrionales. OX NCBI_TaxID=391574 {ECO:0000313|EMBL:EDK31116.1}; RN [1] {ECO:0000313|EMBL:EDK31116.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SWAT-3 {ECO:0000313|EMBL:EDK31116.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDK31116.1}. 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; AAZW01000001; EDK31116.1; -; Genomic_DNA. DR RefSeq; WP_008216021.1; NZ_AAZW01000001.1. DR ProteinModelPortal; A5KUF8; -. DR EnsemblBacteria; EDK31116; EDK31116; VSWAT3_13627. DR PATRIC; 25660200; VBIVibBac109234_0292. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EDK31116.1}; KW Transferase {ECO:0000313|EMBL:EDK31116.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 204 204 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 279 279 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 280 280 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 299 AA; 32584 MW; 52DADE9700296712 CRC64; MKTLTILDGG MGRELKEIGA PFSQPLWSAQ ALIEAPDFVS QAHQNFIDAG AEIIITNSYA CVPFHLGEEL FAQRGFELAA LSGELARAVA DQASQAVKVA GSIPPPFGSY RPDLFKIEQA ASIIQTLYDA QEPNIDLWLV ETLCSVQEFE SIHGVLKQST KPCYYAFSLE DTKGDSASIR SGESVKEAVK LVCQSNATGI MFNCSVPEVM DQAIIDTKQV MDELGQDLEI GVYANNFAPI SSEHEANDML QEMRELDGQG YLTYAKRWHA LGANIIGGCC GIGPKHIKAL SDWKRSTQS // ID A5L291_VIBBS Unreviewed; 574 AA. AC A5L291; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 35. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EDK28222.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EDK28222.1}; GN Name=metH {ECO:0000313|EMBL:EDK28222.1}; GN ORFNames=VSWAT3_10188 {ECO:0000313|EMBL:EDK28222.1}; OS Vibrionales bacterium (strain SWAT-3). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC unclassified Vibrionales. OX NCBI_TaxID=391574 {ECO:0000313|EMBL:EDK28222.1}; RN [1] {ECO:0000313|EMBL:EDK28222.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SWAT-3 {ECO:0000313|EMBL:EDK28222.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDK28222.1}. 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; AAZW01000024; EDK28222.1; -; Genomic_DNA. DR EnsemblBacteria; EDK28222; EDK28222; VSWAT3_10188. DR PATRIC; 25665531; VBIVibBac109234_2929. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDK28222.1}; KW Transferase {ECO:0000313|EMBL:EDK28222.1}. SQ SEQUENCE 574 AA; 62893 MW; AA2D5745FBEA38B1 CRC64; MGSNVRQKID ALLKKRILLI DGGMGTMIQD YKLDEQDYRG ERFADWHSDL KGNNDLLVLT QPKLIKDIHS QYLEAGADIL ETNTFNATTI AMADYDMESL SEEINFAAAK LAREAADEWT AKTPEKPRFV AGVLGPTNRT CSISPDVNDP GYRNVSFDEL VEAYSESTRA LIKGGSDLIL IETIFDTLNA KACAFAVESV FEEVGITLPV MISGTITDAS GRTLSGQTTE AFYNALRHVK PISFGLNCAL GPDELREYVG EMSRISESYV SAHPNAGLPN AFGEYDLSPE DMAEHVKEWA ESGFLNLIGG CCGTTPEHIR QMAEAVEGVT PRQLPDLPVS CRLSGLEPLT IAKESLFVNV GERTNVTGSA RFKRLIKEEL YDEALSVARE QVENGAQIID INMDEGMLDA EACMVKFLNL CASEPEISKV PVMVDSSKWE VIEAGLKCIQ GKGIVNSISL KEGKDKFVEQ AKLVRRYGAA VIVMAFDEVG QADTRERKVE ICTNAYNILV DEVGFPPEDI IFDPNIFAVA TGIEEHNNYA VDFIEAVGDI KRDLPHAMIS GGGGGIERVI LIPR // ID A5MZH5_CLOK5 Unreviewed; 313 AA. AC A5MZH5; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 48. DE SubName: Full=Predicted homocysteine S-methyltransferase {ECO:0000313|EMBL:EDK34271.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EDK34271.1}; GN OrderedLocusNames=CKL_2259 {ECO:0000313|EMBL:EDK34271.1}; OS Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=431943 {ECO:0000313|EMBL:EDK34271.1, ECO:0000313|Proteomes:UP000002411}; RN [1] {ECO:0000313|EMBL:EDK34271.1, ECO:0000313|Proteomes:UP000002411} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680 RC {ECO:0000313|Proteomes:UP000002411}; RX PubMed=18218779; DOI=10.1073/pnas.0711093105; RA Seedorf H., Fricke W.F., Veith B., Brueggemann 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; EDK34271.1; -; Genomic_DNA. DR RefSeq; WP_012102601.1; NC_009706.1. DR RefSeq; YP_001395642.1; NC_009706.1. DR ProteinModelPortal; A5MZH5; -. DR STRING; 431943.CKL_2259; -. DR EnsemblBacteria; EDK34271; EDK34271; CKL_2259. DR KEGG; ckl:CKL_2259; -. DR PATRIC; 19466031; VBICloKlu111549_2350. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; CKLU431943:GJF1-2252-MONOMER; -. DR Proteomes; UP000002411; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002411}; KW Methyltransferase {ECO:0000313|EMBL:EDK34271.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002411}; KW Transferase {ECO:0000313|EMBL:EDK34271.1}. SQ SEQUENCE 313 AA; 34832 MW; 58D558CB1DDCB0B2 CRC64; MNPLKHILKD FKVIILDGAL ATELEKIGCN IDDSLWSAKI LYEDPKIIEG VHYDYFVSGA DCAITSSYQA TIRGFMEKGF KEDEAIELIR LSVQVAKKAR DRFWKNPLNR INRPKPLIAG SIGPYGAYLA DGSEYIGHYN ISEEELMEFH RPRMKILIEE GVDILACETI PSLVEAQAIL KLLEEFPSVC SWISFSAKDE LNISEGTSLA KCAKYLDSNR QVAAIGVNCT PPKYINSLIE QISKNSSKPI IVYPNSGEEY DGITKTWHGD SSSKAFSCSA KEWFDGGARL IGGCCRTTPE DIKSTCKVLK NNL // ID A5N6T7_CLOK5 Unreviewed; 801 AA. AC A5N6T7; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 61. DE SubName: Full=MetH1 {ECO:0000313|EMBL:EDK33018.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EDK33018.1}; GN Name=metH1 {ECO:0000313|EMBL:EDK33018.1}; GN OrderedLocusNames=CKL_0976 {ECO:0000313|EMBL:EDK33018.1}; OS Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=431943 {ECO:0000313|EMBL:EDK33018.1, ECO:0000313|Proteomes:UP000002411}; RN [1] {ECO:0000313|EMBL:EDK33018.1, ECO:0000313|Proteomes:UP000002411} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680 RC {ECO:0000313|Proteomes:UP000002411}; RX PubMed=18218779; DOI=10.1073/pnas.0711093105; RA Seedorf H., Fricke W.F., Veith B., Brueggemann 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; EDK33018.1; -; Genomic_DNA. DR RefSeq; WP_012101348.1; NC_009706.1. DR RefSeq; YP_001394366.1; NC_009706.1. DR ProteinModelPortal; A5N6T7; -. DR STRING; 431943.CKL_0976; -. DR EnsemblBacteria; EDK33018; EDK33018; CKL_0976. DR KEGG; ckl:CKL_0976; -. DR PATRIC; 19463395; VBICloKlu111549_1032. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CKLU431943:GJF1-976-MONOMER; -. DR Proteomes; UP000002411; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002411}; KW Methyltransferase {ECO:0000313|EMBL:EDK33018.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002411}; KW Transferase {ECO:0000313|EMBL:EDK33018.1}. SQ SEQUENCE 801 AA; 87798 MW; C9F79F51DFEF6D92 CRC64; MNFKNLVDKF NNRFIFFDGA MGTMLQKAGL KLGELPEVLN ITNPEIISGI HRKYLDAGAD IITTNTFGAN ELKYDSSDYT IEDVISAGVK LAKQEAGDKL VALDIGPIGK IMEPTGNLSF ESAYKLFKNQ IVIGEKSGAD VVLIETMTDL YEAKAAVLAA KENSNIPIFC TMTFQEDGRT LMGTDAKTMV FVLEALGVDV LGVNCSLGPK ELQGIVEEIL KYSSIPVMVQ PNAGLPRYDG ENTIYDISPE DFAENVLTMA QKGIRVLGGC CGTTPEFIRM CRKDLEGLTP LNIEEKHYTA VCSATDTVIV GEKIKIIGER INPTGRSIYK KELKEGSINY IQKEAIMQKE EGANILGVNV GLPEINEVEI MKKAIRAVQK VVQLPLSIDS PDPQVLETGI RMYNGKPVIN SVNGSKKSME EVFPIVKKYG GCVIALTIDE KGIPHTAEGR VKIAEKIIKT ASIYGINKKN IIIDCLTLTV SAQQKEVLET IKAIKMVTEK FGVKTVLGVS NISFGLPNRS ILNRTFLAMA LQAGLNLPIM NPADESMKEV IAAFQVLTNI DKEGKEYVIK YGNKSKDEKP KGEGNSPLKN ADNNLKDLKQ LIIDGIEDEA EAMTTELLKN KKALEIVNSY IIPALDEVGK QYELQDIFLP QLIQSAETVK KSFEIIKDNM LSSGQKSLEK GTIVLATVKG DIHDIGKNIV KVLLENYGFE VIDLGRDVDI DNIVNTIRDN NIKLVGLSAL MTTTVASMKK TIEAIRENNL NCKIVVGGAV LNQNYADMIG ADYYAKDARE AVKIAEEVFL I // ID A5N923_CLOK5 Unreviewed; 590 AA. AC A5N923; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 60. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN Name=metH2 {ECO:0000313|EMBL:EDK33804.1}; GN OrderedLocusNames=CKL_1762 {ECO:0000313|EMBL:EDK33804.1}; OS Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=431943 {ECO:0000313|EMBL:EDK33804.1, ECO:0000313|Proteomes:UP000002411}; RN [1] {ECO:0000313|EMBL:EDK33804.1, ECO:0000313|Proteomes:UP000002411} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680 RC {ECO:0000313|Proteomes:UP000002411}; RX PubMed=18218779; DOI=10.1073/pnas.0711093105; RA Seedorf H., Fricke W.F., Veith B., Brueggemann 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; EDK33804.1; -; Genomic_DNA. DR RefSeq; WP_012102157.1; NC_009706.1. DR RefSeq; YP_001395152.1; NC_009706.1. DR ProteinModelPortal; A5N923; -. DR STRING; 431943.CKL_1762; -. DR EnsemblBacteria; EDK33804; EDK33804; CKL_1762. DR KEGG; ckl:CKL_1762; -. DR PATRIC; 19464997; VBICloKlu111549_1833. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00548; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; CKLU431943:GJF1-1762-MONOMER; -. DR Proteomes; UP000002411; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002411}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EDK33804.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000002411}; KW Transferase {ECO:0000313|EMBL:EDK33804.1}. SQ SEQUENCE 590 AA; 66365 MW; D248E82F8DC700B5 CRC64; MNIKEKPLIF DGAMGTYYPR ISKDPLPKCE LANIYDRNTI LKIHREYIEA GCMAIKTNTF GANKVSLESD FNKVKEVIIN GYEIAKEAAK DTEVLVFADI GPIPFLESMD LYEGYKEIVD LFLELGAKYF IFETFSSDEY LREISEYIKG KDPEAYILME FAVSPEGYTR VGKSGKKLIE NILKIPTIDA CGFNCFSGPY HLLQYIKTFN IGNETISVMP NSGYPTVIDN RTFFDNTKEY FAQRMLEIAK QGVSILGGCC GTTPEFIRET VIKLKKLSKS EIVLKKQAEK IHTEKPVVKN VLLEKINKGK KIIAVELDPP IDTEVDFFLN SARTLKEQEI DAITIADCPI ARARVDSSLL ACKLKRELDI TTIPHMTCRD RNINATKALL LGLNIEGVNN VLVVTGDPIP SAERDEVKAM FSFNSAILAN YITNLNDTIF SSPFNICGAL NVNSRNFNTE LKRAKTKIEN GIAVFLTQPI LTEEALENLK LARRELTARI LGGIIPVVSY RNACFMNNEI SGIRVSEEII KQYKDVSKEE AVKLAVKIST DIAEQIYPYV DGYYLITPFK RIDIISEIIN NIKAKNTITI // ID A5PAW3_9SPHN Unreviewed; 348 AA. AC A5PAW3; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 31. DE SubName: Full=Methionine synthase I cobalamin-binding domain {ECO:0000313|EMBL:EDL49368.1}; GN ORFNames=ED21_21849 {ECO:0000313|EMBL:EDL49368.1}; OS Erythrobacter sp. SD-21. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Erythrobacteraceae; Erythrobacter. OX NCBI_TaxID=161528 {ECO:0000313|EMBL:EDL49368.1}; RN [1] {ECO:0000313|EMBL:EDL49368.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SD-21 {ECO:0000313|EMBL:EDL49368.1}; 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. {ECO:0000313|EMBL:EDL49368.1}. 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; ABCG01000003; EDL49368.1; -; Genomic_DNA. DR RefSeq; WP_006833289.1; NZ_ABCG01000003.1. DR ProteinModelPortal; A5PAW3; -. DR EnsemblBacteria; EDL49368; EDL49368; ED21_21849. DR PATRIC; 30322178; VBIErySp11529_1519. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 348 AA; 37512 MW; EE0062171F1D7C31 CRC64; MSKRQEFEAA AATRILIKDG PYGTEIQRAK LAAGDYAGDT GLKDDQKGNN DLVNLTQPQV IRKICDSYID AGAHILATNT FNANRISQAD YGAEHLVHEI NVSAAKIIRE AIDEATAKDG VPRFVAGAMG PTNKTLSLSP NVEDPGFREV SFDEIVEVYV EQARGLIEGG ADFILIETVF DTLNCKAAVM AVKQLERELG QDIPLMISLT LTDLSGRNLS GHTVEAFWHT VRHAKPLTMG LNCSFGAEQL RPHVQILSDI ADCYLMAYPN AGLPNDLGEY DELPETTAAL TRVWADNGRI NALGGCCGST PAHIAAMAKK VEGVAPRALP TVDQHMRLAG LEPFTIAA // ID A5TSW8_FUSNP Unreviewed; 1082 AA. AC A5TSW8; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 50. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EDK87993.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EDK87993.1}; GN Name=metH {ECO:0000313|EMBL:EDK87993.1}; GN ORFNames=FNP_0176 {ECO:0000313|EMBL:EDK87993.1}; OS Fusobacterium nucleatum subsp. polymorphum ATCC 10953. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=393480 {ECO:0000313|EMBL:EDK87993.1, ECO:0000313|Proteomes:UP000001921}; RN [1] {ECO:0000313|EMBL:EDK87993.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 10953 {ECO:0000313|EMBL:EDK87993.1}; RA Qin X., Weinstock G.M.; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EDK87993.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 10953 {ECO:0000313|EMBL:EDK87993.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CM000440; EDK87993.1; -; Genomic_DNA. DR RefSeq; WP_005895537.1; NZ_CM000440.1. DR ProteinModelPortal; A5TSW8; -. DR EnsemblBacteria; EDK87993; EDK87993; FNP_0176. DR PATRIC; 30264071; VBIFusNuc113593_2159. DR Proteomes; UP000001921; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001921}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EDK87993.1}; KW Transferase {ECO:0000313|EMBL:EDK87993.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 723 723 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1082 AA; 120764 MW; 7E35C57AE5D37AA2 CRC64; MFEFEKELKE RILVLDGAMG TVLQKYELTP EDFNGAKGCY EILNETRPDI IFEVHKKYIE AGADIIETNS FNCNAISLKD YHLEDKVYDL AKKSAEIARD AVKESGKKVY VFGSIGPTNK SLSFPVGDVP YKRAVSFDEM KEVIKVQVAG LIDGGVDGIL LETIFDGLTA KAALLATEEV FEEKNVKLPI SISATVNRQG KLLTGQSMES LIAALDRDSV TSFGFNCSFG AKDLVPLVIK IKELTTKFVS LHANAGLPNQ NGDYVETAQK MRDDLLPLIE NQAINILGGC CGTSYDHIRA IAEMVKGQKP RVLPKENLLE TCLSGNEIYN FNDKFTWVGE RNNISGSKLF RTMIEEHNYL KALEVARQQI DAGAKVLDIN VDDGILDSVE EMKNFLRVLQ NDSFIAKVPI MIDSSDFAVI EEGLKNTSGK AIVNSISLKE GTEEFLRKAK IIRKYGASIV VMAFDEKGQG VSAERKIEIC QRAYDLLKSI GVKNSDIVFD PNILSVGTGQ EADRYHAREF IKTIDYIHEN LKGCGVVGGL SNLSFAFRGN NVLRAAFHHI FLEEAVPRGF NFAILNPKEK APQWTDEERE KIKSFIFGDS TDMEALLSLN LVKKKEDAQI FAETPEDKIR KALIQGGSES LQEVIGDLLK KYKALEILEN ILMSAMQEIG RLFEQGELYL PQLIRSASVM NNCVDILTPY LEKVDKTSSK GKILMATVDG DVHDIGKNIV GTVLECNGYE VIDLGVMVPR EKIVETAKEI NADVVTLSGL ISPSLKEMER VADLFQKVGM QVPVLIAGAA TSKLHTGLKV LPNYDYSLHV TDAMDTITVV SQLLSTKRKD FLETKQTQLR KIAKRYMDNN SNQPEEKKVL PEVKKTVSYI PKVLGKQFLS LPVEIFKDTL KWDIALYALR VRNTPEEEKT LNDLKKIYEK LIEEKVEFRA AYGYFRCKKT ETFLEMEGMT FEVSPNLAQY IEKEDYVGGF VISVGSKIFK DDKYLGLLET LLCNAIAETA SEYMETRVTE DIVPTFLRPA VGYPILPDHS LKKVVFDLID GERTGAKLSP AFAMSPLSTV CGFYLCNDNA KY // ID A5U4F0_MYCTA Unreviewed; 1192 AA. AC A5U4F0; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 63. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocystein methyltransferase {ECO:0000313|EMBL:ABQ73900.1}; GN Name=metH {ECO:0000313|EMBL:ABQ73900.1}; GN OrderedLocusNames=MRA_2139 {ECO:0000313|EMBL:ABQ73900.1}; OS Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=419947 {ECO:0000313|EMBL:ABQ73900.1, ECO:0000313|Proteomes:UP000001988}; RN [1] {ECO:0000313|EMBL:ABQ73900.1, ECO:0000313|Proteomes:UP000001988} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25177 / H37Ra {ECO:0000313|Proteomes:UP000001988}; RX PubMed=18584054; DOI=10.1371/journal.pone.0002375; RA Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L., RA Wang H., Wang S., Zhao G., Zhang Y.; RT "Genetic basis of virulence attenuation revealed by comparative RT genomic analysis of Mycobacterium tuberculosis strain H37Ra versus RT H37Rv."; RL PLoS ONE 3:E2375-E2375(2008). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000611; ABQ73900.1; -; Genomic_DNA. DR RefSeq; WP_003900472.1; NC_009525.1. DR RefSeq; YP_001283462.1; NC_009525.1. DR ProteinModelPortal; A5U4F0; -. DR SMR; A5U4F0; 16-621, 637-1192. DR STRING; 419947.MRA_2139; -. DR EnsemblBacteria; ABQ73900; ABQ73900; MRA_2139. DR KEGG; mra:MRA_2139; -. DR PATRIC; 18144397; VBIMycTub106795_2401. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; MTUB419947:GJ8N-2206-MONOMER; -. DR Proteomes; UP000001988; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001988}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABQ73900.1}; KW Transferase {ECO:0000313|EMBL:ABQ73900.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 231 231 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 297 297 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 298 298 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 742 742 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1192 AA; 130323 MW; 820450DCE77BE15B CRC64; MTAADKHLYD TDLLDVLSQR VMVGDGAMGT QLQAADLTLD DFRGLEGCNE ILNETRPDVL ETIHRNYFEA GADAVETNTF GCNLSNLGDY DIADRIRDLS QKGTAIARRV ADELGSPDRK RYVLGSMGPG TKLPTLGHTE YAVIRDAYTE AALGMLDGGA DAILVETCQD LLQLKAAVLG SRRAMTRAGR HIPVFAHVTV ETTGTMLLGS EIGAALTAVE PLGVDMIGLN CATGPAEMSE HLRHLSRHAR IPVSVMPNAG LPVLGAKGAE YPLLPDELAE ALAGFIAEFG LSLVGGCCGT TPAHIREVAA AVANIKRPER QVSYEPSVSS LYTAIPFAQD ASVLVIGERT NANGSKGFRE AMIAEDYQKC LDIAKDQTRD GAHLLDLCVD YVGRDGVADM KALASRLATS STLPIMLDST ETAVLQAGLE HLGGRCAINS VNYEDGDGPE SRFAKTMALV AEHGAAVVAL TIDEEGQART AQKKVEIAER LINDITGNWG VDESSILIDT LTFTIATGQE ESRRDGIETI EAIRELKKRH PDVQTTLGLS NISFGLNPAA RQVLNSVFLH ECQEAGLDSA IVHASKILPM NRIPEEQRNV ALDLVYDRRR EDYDPLQELM RLFEGVSAAS SKEDRLAELA GLPLFERLAQ RIVDGERNGL DADLDEAMTQ KPPLQIINEH LLAGMKTVGE LFGSGQMQLP FVLQSAEVMK AAVAYLEPHM ERSDDDSGKG RIVLATVKGD VHDIGKNLVD IILSNNGYEV VNIGIKQPIA TILEVAEDKS ADVVGMSGLL VKSTVVMKEN LEEMNTRGVA EKFPVLLGGA ALTRSYVEND LAEIYQGEVH YARDAFEGLK LMDTIMSAKR GEAPDENSPE AIKAREKEAE RKARHQRSKR IAAQRKAAEE PVEVPERSDV AADIEVPAPP FWGSRIVKGL AVADYTGLLD ERALFLGQWG LRGQRGGEGP SYEDLVETEG RPRLRYWLDR LSTDGILAHA AVVYGYFPAV SEGNDIVVLT EPKPDAPVRY RFHFPRQQRG RFLCIADFIR SRELAAERGE VDVLPFQLVT MGQPIADFAN ELFASNAYRD YLEVHGIGVQ LTEALAEYWH RRIREELKFS GDRAMAAEDP EAKEDYFKLG YRGARFAFGY GACPDLEDRA KMMALLEPER IGVTLSEELQ LHPEQSTDAF VLHHPEAKYF NV // ID A5U5F4_MYCTA Unreviewed; 302 AA. AC A5U5F4; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:ABQ74254.1}; GN Name=mmuM {ECO:0000313|EMBL:ABQ74254.1}; GN OrderedLocusNames=MRA_2484 {ECO:0000313|EMBL:ABQ74254.1}; OS Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=419947 {ECO:0000313|EMBL:ABQ74254.1, ECO:0000313|Proteomes:UP000001988}; RN [1] {ECO:0000313|EMBL:ABQ74254.1, ECO:0000313|Proteomes:UP000001988} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25177 / H37Ra {ECO:0000313|Proteomes:UP000001988}; RX PubMed=18584054; DOI=10.1371/journal.pone.0002375; RA Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L., RA Wang H., Wang S., Zhao G., Zhang Y.; RT "Genetic basis of virulence attenuation revealed by comparative RT genomic analysis of Mycobacterium tuberculosis strain H37Ra versus RT H37Rv."; RL PLoS ONE 3:E2375-E2375(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; CP000611; ABQ74254.1; -; Genomic_DNA. DR RefSeq; WP_003911868.1; NZ_AAYK01000261.1. DR RefSeq; YP_001283816.1; NC_009525.1. DR ProteinModelPortal; A5U5F4; -. DR SMR; A5U5F4; 2-300. DR STRING; 419947.MRA_2484; -. DR EnsemblBacteria; ABQ74254; ABQ74254; MRA_2484. DR KEGG; mra:MRA_2484; -. DR PATRIC; 18145196; VBIMycTub106795_2796. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; YGRSVTK; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; MTUB419947:GJ8N-2565-MONOMER; -. DR Proteomes; UP000001988; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001988}; KW Methyltransferase {ECO:0000313|EMBL:ABQ74254.1}; KW Transferase {ECO:0000313|EMBL:ABQ74254.1}. SQ SEQUENCE 302 AA; 31593 MW; 721C9D2DDF7F29CC CRC64; MELVSDSVLI SDGGLATELE ARGHDLSDPL WSARLLVDAP HAITAVHTAY FRAGAQIATT ASYQASFEGF AARGIGHDDA TVLLRRSVEL AQAARDEVGV GGLSVAASVG PYGAALADGS EYRGYYGLSV AALMKWHLPR LEVLVDAGAD MLALETIPDI DEAEALVNLV RRLATPAWLS YTINGTRTRA GQPLTDAFAV AAGVPEIVAV GVNCCAPDDV LPAIAFAVAH TGKPVIVYPN SGEGWDGRRR AWVGPRRFSG SSGQLAREWV AAGARIVGGC CRVRPIDIAE IGRALTTAPP RG // ID A5UPF4_ROSS1 Unreviewed; 1254 AA. AC A5UPF4; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 64. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABQ88507.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABQ88507.1}; GN OrderedLocusNames=RoseRS_0064 {ECO:0000313|EMBL:ABQ88507.1}; OS Roseiflexus sp. (strain RS-1). OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Roseiflexineae; OC Roseiflexaceae; Roseiflexus. OX NCBI_TaxID=357808 {ECO:0000313|EMBL:ABQ88507.1, ECO:0000313|Proteomes:UP000006554}; RN [1] {ECO:0000313|Proteomes:UP000006554} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RS-1 {ECO:0000313|Proteomes:UP000006554}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000686; ABQ88507.1; -; Genomic_DNA. DR RefSeq; WP_011954867.1; NC_009523.1. DR RefSeq; YP_001274457.1; NC_009523.1. DR ProteinModelPortal; A5UPF4; -. DR STRING; 357808.RoseRS_0064; -. DR EnsemblBacteria; ABQ88507; ABQ88507; RoseRS_0064. DR KEGG; rrs:RoseRS_0064; -. DR PATRIC; 23347981; VBIRosSp109359_0071. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; RSP357808:GH5Z-64-MONOMER; -. DR Proteomes; UP000006554; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 2. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006554}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABQ88507.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006554}; KW Transferase {ECO:0000313|EMBL:ABQ88507.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 277 277 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 343 343 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 344 344 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 816 816 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1254 AA; 138139 MW; B799E41C3424F3A3 CRC64; MRLPEPHAGA WGFLLHKRES AIIAPASPII TCRQFGYEVS RGVSLKKPTY LEALRERVLI YDGAMGTSID TFHLTAADYG GENTFGARDY LVMTRPDVIE QIHTSFLEAG ADVLETCTFQ STRIRLEEWG LADQTHAINV AAARLARRVA DAFEARDGRP RYVAGSMGPT GKLPSSDDPS LSDITFDQLS DIFYEQAVAL IEGGVDVLLV ETSVDILEVK AALDGIRRAK ADLNRPDVAV QAQVFLDLSG KMLLGTEVPA LVATLEAMPV DVIGLNCSTG PEHMREAIRY MTRHSRKPIS CIPNAGLPIE VNGETVYPME PEPFARILGE YVHEYGVAVV GGCCGTRPAH IRRLRQVVGA ATPPKVRDIE YIPSVSSGVR AAALRQEGTL TIIGERVNTL GSRKVKRLLL NDDYDGVLEV AREQVDSGSH ILDVCVAMTE RSDEREMMVR LLKKLTMNIE LPLAIDTTEA DVLNAALAIY PGRAIVNSVS LEGGRGDKID RTMPLVARYG AATIAMTIDE EGMAHTAERK LAIARRIAQI AQDEYGVPPE ALIFDVLTFP ITTGQPELRR AAIETIEGIR LVKQHIPGCF TTLGVSNLSF GVAPYARAAL NSVFLKHAVD AGLDTAIINP AHVMPYAEIP PEQIRVCEDL IFDRDEQALA RFIQFFEEHG SAAKTERVDP TEGMTAAQRV HWKIVHRKKE GIEQDIDTVI AERIREAEMR AGIHDSALDP AHPSREAIFA SPFRNSAAVD VLNTVLLPAM KEVGDLFGAG QLILPFVLQS AEVMKKAVAH LEQYLEKLEG VTKGKIVLAT VYGDVHDIGK NLVHTILANN GYTVYDLGKQ VPINTIIEKA VEVNADAIGL SALLVSTSKQ MPLCVQELHR RGLKFPVLVG GAAINKQYGQ RILFVDDHTP YEPGVFYCKD AFEGLETVDA LVDPSTRATF IERTKAEAAE ALGKKQRGRV ALAELGRATL SDTAKVRSAV RTDVPVPTPP FWGARVLTRI KLADVVECLD RNALYRLQWG AKNAKGEEWE HLKADFDAKV RDLIREAERD GWLEPKVVYG YYPCQSDGHE VIVYDPPSVL NGAQPRELTR FVFPRQPERE RLCLADYFRS RESGEYDVVG LQIVTMGRKV DDLTETLQQS GDYSRAYFIH GLGVSLAEAL AEYTNRLIRR QLGLKGTQGK RYSWGYPACP DLEEHEKLFR VLPAAEIGVT LTEAWQLVPE QSTAAIVIHH PEAKYFSIGS ARERAEEDVA ETLA // ID A5V8Z3_SPHWW Unreviewed; 353 AA. AC A5V8Z3; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 49. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABQ68759.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABQ68759.1}; GN OrderedLocusNames=Swit_2400 {ECO:0000313|EMBL:ABQ68759.1}; OS Sphingomonas wittichii (strain RW1 / DSM 6014 / JCM 10273). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingomonas. OX NCBI_TaxID=392499 {ECO:0000313|EMBL:ABQ68759.1, ECO:0000313|Proteomes:UP000001989}; RN [1] {ECO:0000313|Proteomes:UP000001989} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RW1 / DSM 6014 / JCM 10273 {ECO:0000313|Proteomes:UP000001989}; 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; ABQ68759.1; -; Genomic_DNA. DR RefSeq; WP_012048616.1; NC_009511.1. DR RefSeq; YP_001262897.1; NC_009511.1. DR ProteinModelPortal; A5V8Z3; -. DR STRING; 392499.Swit_2400; -. DR EnsemblBacteria; ABQ68759; ABQ68759; Swit_2400. DR KEGG; swi:Swit_2400; -. DR PATRIC; 23683939; VBISphWit55028_2924. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; SWIT392499:GHZK-2423-MONOMER; -. DR Proteomes; UP000001989; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001989}; KW Methyltransferase {ECO:0000313|EMBL:ABQ68759.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001989}; KW Transferase {ECO:0000313|EMBL:ABQ68759.1}. SQ SEQUENCE 353 AA; 38119 MW; BC0060E6FDC8BB78 CRC64; MTLHRSEAAA IFRDQAKQRI LLTDGAFGTM IQSYKLQEAD YRGSYELPSD QKGNNDLLVL TRPDVIDAIT RQYLDAGSDI VSTNTFNANI ISQEDYDAVH LVREINLAAA RIARTAADDY AARDGRPRFV AGAIGPTNKT LSLSPDVNDP GYRAVDFDTM RDVYQDQTAA LLDGGCDFIL IETIFDTLNA KAAIMAVLDE QAKRGVEIPM MISMTITDMS GRNLSGHSVE AFWHAVRHAH PLTIGLNCAF GADLLRPHVQ VLSGLADALV MIYPNAGLPN DLGQYDEQPA TTGGFIRDWA DQGLVNIVGG CCGSTPAHIA AMADAVAGKP ARALHAHDHR TRLAGLDPMI MAA // ID A5VKC8_LACRD Unreviewed; 310 AA. AC A5VKC8; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 48. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABQ83302.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ABQ83302.1}; GN OrderedLocusNames=Lreu_1042 {ECO:0000313|EMBL:ABQ83302.1}; OS Lactobacillus reuteri (strain DSM 20016). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=557436 {ECO:0000313|EMBL:ABQ83302.1, ECO:0000313|Proteomes:UP000001991}; RN [1] {ECO:0000313|Proteomes:UP000001991} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20016 {ECO:0000313|Proteomes:UP000001991}; 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 ----------------------------------------------------------------------- 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; ABQ83302.1; -; Genomic_DNA. DR RefSeq; WP_003667059.1; NC_009513.1. DR RefSeq; YP_001271639.1; NC_009513.1. DR ProteinModelPortal; A5VKC8; -. DR STRING; 557436.Lreu_1042; -. DR EnsemblBacteria; ABQ83302; ABQ83302; Lreu_1042. DR GeneID; 5189060; -. DR KEGG; lre:Lreu_1042; -. DR PATRIC; 22255276; VBILacReu87937_1051. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; LREU557436:GC7Y-1102-MONOMER; -. DR Proteomes; UP000001991; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001991}; KW Methyltransferase {ECO:0000313|EMBL:ABQ83302.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001991}; KW Transferase {ECO:0000313|EMBL:ABQ83302.1}. SQ SEQUENCE 310 AA; 33808 MW; DE82383D6DDE118D CRC64; MTKITAELTK PLLIDGAMST ALEQLGADTN NSLWTASVLA NQPALVKKVH QEYFKAGDRL AITDTYQANV PAFIKNGYSK QEAHSLIQRA VVLAKEARDE YQQETGIYNY VAGALGPYGA YLANGSEYSG AYHLSTIEYQ QFHRPRLTDI LTVGVDVIAI ETQPRLDEVL AELDLVKELA PDTLCYVSFS LKDSTHLPDG TPLAVAARTV AKYTNVFAVG VNCIPLEEVT AAIETVHQVT EKPVIAYPNS SATYDPTTKT WSYPHGRRGL VDYLPQWIAA GLIIVGGCCT TTPQDIAALH EYLKGGAYHD // ID A5VY96_PSEP1 Unreviewed; 311 AA. AC A5VY96; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 39. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABQ76856.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ABQ76856.1}; GN OrderedLocusNames=Pput_0692 {ECO:0000313|EMBL:ABQ76856.1}; OS Pseudomonas putida (strain F1 / ATCC 700007). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=351746 {ECO:0000313|EMBL:ABQ76856.1, ECO:0000313|Proteomes:UP000006553}; RN [1] {ECO:0000313|EMBL:ABQ76856.1, ECO:0000313|Proteomes:UP000006553} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F1 / ATCC 700007 {ECO:0000313|Proteomes:UP000006553}; 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 ----------------------------------------------------------------------- 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; ABQ76856.1; -; Genomic_DNA. DR RefSeq; WP_012051142.1; NC_009512.1. DR RefSeq; YP_001266040.1; NC_009512.1. DR STRING; 351746.Pput_0692; -. DR EnsemblBacteria; ABQ76856; ABQ76856; Pput_0692. DR KEGG; ppf:Pput_0692; -. DR PATRIC; 19917377; VBIPsePut56420_0690. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; PYVDVWL; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; PPUT351746:GI26-717-MONOMER; -. DR Proteomes; UP000006553; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006553}; KW Methyltransferase {ECO:0000313|EMBL:ABQ76856.1}; KW Transferase {ECO:0000313|EMBL:ABQ76856.1}. SQ SEQUENCE 311 AA; 33363 MW; 8145A9F198309BD5 CRC64; MNFIHKNLQR SYMAERTMVI LDGGMGRELQ RSGAPFRQPE WSALALSEAP EAVVGVHAAF IEAGAQVITS NSYAVVPFHI GEERFAAEGR QLAHIAGQLA RHAADSGAHP VRVAGSLPPL FGSYRPDLFQ PERVAEVLTP LLQGLAPHVD LWLAETQSSV AEVRAIHSHL PADGRPFWVS FTLQDEDVDD VPRLRSGEPV ADAIEAAVSL GVAAVLFNCS QPEVIGAAID VARSVIERHN AEIAIGAYAN AFPPQPKEAT ANDGLDELRE DLDPPGYLAW AKGWRARGAS MVGGCCGIGP EHIAELKRNL A // ID A5W5N6_PSEP1 Unreviewed; 1235 AA. AC A5W5N6; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 59. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABQ79446.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABQ79446.1}; GN OrderedLocusNames=Pput_3320 {ECO:0000313|EMBL:ABQ79446.1}; OS Pseudomonas putida (strain F1 / ATCC 700007). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=351746 {ECO:0000313|EMBL:ABQ79446.1, ECO:0000313|Proteomes:UP000006553}; RN [1] {ECO:0000313|EMBL:ABQ79446.1, ECO:0000313|Proteomes:UP000006553} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F1 / ATCC 700007 {ECO:0000313|Proteomes:UP000006553}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000712; ABQ79446.1; -; Genomic_DNA. DR RefSeq; WP_004573789.1; NC_009512.1. DR RefSeq; YP_001268630.1; NC_009512.1. DR ProteinModelPortal; A5W5N6; -. DR SMR; A5W5N6; 654-1235. DR STRING; 351746.Pput_3320; -. DR EnsemblBacteria; ABQ79446; ABQ79446; Pput_3320. DR KEGG; ppf:Pput_3320; -. DR PATRIC; 19922783; VBIPsePut56420_3373. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PPUT351746:GI26-3371-MONOMER; -. DR Proteomes; UP000006553; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006553}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABQ79446.1}; KW Transferase {ECO:0000313|EMBL:ABQ79446.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1235 AA; 135452 MW; D6809C101A291CCF CRC64; MSDRSARLQA LQNALKERIL ILDGGMGTMI QSYRLEEHDY RGTRFADWPS DVKGNNDLLL LSRPDVIAAI EKAYLDAGAD ILETNTFNAT QISQADYGME SLVYELNVEG ARIARQVADA KTLETPDKPR FVAGVLGPTS RTCSISPDVN DPGFRNVTFD ELVENYIEAT RGLIEGGADL ILIETIFDTL NAKAAIFAVQ QVFEDDNVEL PIMISGTITD ASGRTLSGQT TEAFWNSVRH AKPISVGLNC ALGAKDLRPY LEELATKADT HVSAHPNAGL PNAFGEYDET PAEMAAVVEE FAASGFLNII GGCCGTTPGH IQAIAEAVAK YKPREIPEIA KACRLSGLEP FTIDRQSLFV NVGERTNITG SAKFARLIRE ENYTEALEVA LQQVEAGAQV IDINMDEGML DSQAAMVRFL NLIAGEPDIS RVPIMIDSSK WEVIEAGLKC IQGKGIVNSI SMKEGVEQFK HHARLCKRYG AAVVVMAFDE VGQADTAARK KEICQRSYDI LVNEVGFPPE DIIFDPNIFA VATGIEEHNN YAVDFIEACA YIRDHLPHAL SSGGVSNVSF SFRGNNPVRE AIHSVFLYHA IQNGLTMGIV NAGQLEIYDE IPAQLREKVE DVVLNRTPHG TDALLAIADD YKGGGATKEV ENEEWRSLPV EKRLEHALVK GITAFIVEDT EECRQQCARP IEVIEGPLMN GMNVVGDLFG AGKMFLPQVV KSARVMKQAV AHLIPFIEAE KGDKPEAKGK ILMATVKGDV HDIGKNIVGV VLGCNGYDIV DLGVMVPAEK ILQTAREQKC DIIGLSGLIT PSLDEMVHVA REMQRQGFEL PLMIGGATTS KAHTAVKIEP KYSNDAVIYV TDASRAVGVA TQLLSKELKP GFVEKTRLEY VDVRERTANR SARTERLSYA QAIAAKPQYD WASYQPAVPS FTGVKVLEDI DLRTLAEYID WTPFFISWDL AGKFPRILTD EVVGEAATAL YKDAREMLDK LIDEKLISAR AVFGFWPANQ VADDDIEVYG EDGQALATLH HLRQQTIKPD GKPNWSLADF VAPKDSGVTD YVGGFITTAG IGAEEVAKAY QDKGDDYSSI MVKALADRLA EACAEWLHEQ VRKEHWGYAR DEHLDNEALI KEQYSGIRPA PGYPACPDHT EKETLFRLLD GTAIGETGPS GVYLTEHFAM FPAAAVSGWY FAHPQAKYFA VGKVDKDQIE RYSARKGQDI SVSERWLAPN LGYDS // ID A5WD09_PSYWF Unreviewed; 1272 AA. AC A5WD09; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 01-APR-2015, entry version 62. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABQ93550.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABQ93550.1}; GN OrderedLocusNames=PsycPRwf_0595 {ECO:0000313|EMBL:ABQ93550.1}; OS Psychrobacter sp. (strain PRwf-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Psychrobacter. OX NCBI_TaxID=349106 {ECO:0000313|EMBL:ABQ93550.1, ECO:0000313|Proteomes:UP000001993}; RN [1] {ECO:0000313|EMBL:ABQ93550.1, ECO:0000313|Proteomes:UP000001993} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PRwf-1 {ECO:0000313|EMBL:ABQ93550.1, RC ECO:0000313|Proteomes:UP000001993}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000713; ABQ93550.1; -; Genomic_DNA. DR RefSeq; WP_011959876.1; NC_009524.1. DR RefSeq; YP_001279500.1; NC_009524.1. DR ProteinModelPortal; A5WD09; -. DR SMR; A5WD09; 699-937. DR STRING; 349106.PsycPRwf_0595; -. DR EnsemblBacteria; ABQ93550; ABQ93550; PsycPRwf_0595. DR KEGG; prw:PsycPRwf_0595; -. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PPRW349106:GHZF-605-MONOMER; -. DR Proteomes; UP000001993; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001993}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABQ93550.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001993}; KW Transferase {ECO:0000313|EMBL:ABQ93550.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 352 352 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 353 353 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 804 804 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1272 AA; 140989 MW; EF63F634CBFEEDAB CRC64; MANCSHPEHN TKKDLPETAI KKGHNPDNFN LVPPAKFPFK EQQLTARQRI VEQLNQRILM LDGAMGTQIQ TFKLGESDYR GERFADFTQD VQGNNDLLVL TQPELIKSIH RDHLTAGADI IETNSFNGTQ ISMADYAMEH LVPEINKEAA RLAREVADEF TAQNPDKPRF VAGVIGPTSR TCSLSPDVND PAYRNVTFDE LVDNYTEALF ALIEGGIDLV LIETIFDTLN AKAAIFAVTG VFETIGFELP IMISGTITDA SGRTLSGQTA EAFYNSIRHA KPLSVGFNCA LGADALKPHI QTLSDIADTY ISAHPNAGLP NEFGEYDETP EQTAALLDGF GKSGLLNIVG GCCGTRPEHI KAIHDVMQKY PPRQIPTIAP ACRLSGLEPF TITKDSLFVN VGERTNVTGS KKFLRLIKTG EFTEALDVAR NQVDGGAQIV DINMDEGMLD SKGAMIHFLN LVAGEPDISR VPLMIDSSKW DIIEEGLKRT QGKSVVNSIS LKEGYDEFVK HAKLCMRYGA AVIVMAFDED GQADSYERKI QICQRSYDIL VNEVGFPSED IIFDPNIFAV ATGITEHNNY GADFINATRW ITDNLPNAMV SGGVSNVSFS FRGNPIREAI NAVFLYHAIQ AGLTMGIVNP AMLEVYDEIP KEARDAIEDV MLNRNQGESG QEATERLMTI AEAYVAGGKK NDGTIDLSWR EQSVEKRIEH ALVKGITTYI DEDTEEARLK YPKPLHVIEG PLMDGMNVVG DLFGAGKMFL PQVVKSARVM KRAVAVLNPY IEAEKVEGEV KGKVVMATVK GDVHDIGKNI VGVVLGCNGY DVVDLGVMVP CDKILDTAIA EKADIIGLSG LITPSLDEMV YVAKQMQERG MTLPLMIGGA TTSKAHTAVK IEPNYQNDAV IYVSDASRSV GVVTKLLSQE HRVELLRETR EEYQKVRERL ANRKPKAAKL SYQESIEQGF KFDWDNYTPP VPNEQGQIIF DNYPIENLLP YIDWTPFFVS WGLVGKYPKI FDDEVVGAEA KDLFANAKAL MQTFIDEQLV TPKGVFKIMP ARRTDHDTVT VYDKEPSAGG QPTHVFEHLR QQSDKASGKP NYSLADFISP SEDYDDYLGG FTVSIVGAQE LSDSYKEAGD DYNAIMVQAL CDRLAEAFAE HLHELIRTKY WGYQPTEQLT NEELIKEKYV GIRPAPGYPA CPEHTEKGKL FDWLDTTNAI GTYLTESFAM WPASSVSGFY YSHPESTYFN VGKIDRDQLE DYAKRKDWDI KTAEKWLNPN LT // ID A5WFJ9_PSYWF Unreviewed; 310 AA. AC A5WFJ9; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 41. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABQ94440.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ABQ94440.1}; GN OrderedLocusNames=PsycPRwf_1497 {ECO:0000313|EMBL:ABQ94440.1}; OS Psychrobacter sp. (strain PRwf-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Psychrobacter. OX NCBI_TaxID=349106 {ECO:0000313|EMBL:ABQ94440.1, ECO:0000313|Proteomes:UP000001993}; RN [1] {ECO:0000313|EMBL:ABQ94440.1, ECO:0000313|Proteomes:UP000001993} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PRwf-1 {ECO:0000313|EMBL:ABQ94440.1, RC ECO:0000313|Proteomes:UP000001993}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; ABQ94440.1; -; Genomic_DNA. DR RefSeq; WP_011960724.1; NC_009524.1. DR RefSeq; YP_001280390.1; NC_009524.1. DR ProteinModelPortal; A5WFJ9; -. DR STRING; 349106.PsycPRwf_1497; -. DR EnsemblBacteria; ABQ94440; ABQ94440; PsycPRwf_1497. DR KEGG; prw:PsycPRwf_1497; -. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; PYVDVWL; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; PPRW349106:GHZF-1523-MONOMER; -. DR Proteomes; UP000001993; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001993}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ABQ94440.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001993}; KW Transferase {ECO:0000313|EMBL:ABQ94440.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 210 210 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 310 AA; 33642 MW; 377B2A53FDFA3BD5 CRC64; MSVKAITIID GGMGRELAKR GAPFRQPEWS ALAMIEAPEI VRDVHRDFIR SGAGVITTNS YALLPFHIGE VRFAKHAQDL AASAGEMARA AVELENTPTK VAGSIPPLFG SYRADLFQAE QVEDIATPLI TGLRPYVDFW LAETQSLIAE SVAVRKLLTK LDTDNKPVWV SFTLEDSEHL DVPRLRSGET VVEAVTTLAG LNVEAILFNC CQPEVIEQAL EVAQSVLQHK DAAHIKLGAY ANAFPPQPKD ATANDGLDEV REDLTPPAYL DWAKKWQAQG VSLIGGGCGI GPEHINELSG YFTKAGTTQR // ID A5Z3E1_9FIRM Unreviewed; 824 AA. AC A5Z3E1; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 39. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EDM52536.1}; GN ORFNames=EUBVEN_00187 {ECO:0000313|EMBL:EDM52536.1}; OS Eubacterium ventriosum ATCC 27560. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium. OX NCBI_TaxID=411463 {ECO:0000313|EMBL:EDM52536.1}; RN [1] {ECO:0000313|EMBL:EDM52536.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27560 {ECO:0000313|EMBL:EDM52536.1}; 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 (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EDM52536.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27560 {ECO:0000313|EMBL:EDM52536.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDM52536.1}. 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; AAVL02000022; EDM52536.1; -; Genomic_DNA. DR RefSeq; WP_005361830.1; NZ_DS264279.1. DR ProteinModelPortal; A5Z3E1; -. DR EnsemblBacteria; EDM52536; EDM52536; EUBVEN_00187. DR PATRIC; 31246667; VBIEubVen137708_1406. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDM52536.1}; KW Transferase {ECO:0000313|EMBL:EDM52536.1}. SQ SEQUENCE 824 AA; 89278 MW; 523D40A770B7E7CA CRC64; MLKAVTYVIL EKNVPLERME KTVANKNIFD KDFILLDGAM GTMLQQKGME LGTVPETLNI TKPDWIIDIH KQYIDAGSDV VYANTFGANR YKMANTGYSV DELIGAAINN AKEAAKGTET LVALDMGPIG QLLEPTGSLS FEEAYDIFKE EVIAGRNAGA DIIVIETMTD LMETKAAILA AKENSDLQVM CTMTFEDNKR TFTGCSVSAM CLTVQGLGVD ALGVNCSLGP KELMPIVEEI SKWTTVPIVV KANAGLPDPV TNTYNVLPDE FADTCKEMVK YGAKVLGGCC GTTPAYVAKL KEMVATVNAS VVKKKPRQLA VCTPLKTVVV DQPRIVGERI NPTGKKRFKQ ALRDNDMNYI LSQAIEQIDA GADILDVNVG SPDIDEKEMM VKVIKALQAI VDVPLQIDST KPEVLEAALR VYNGKPIVNS VNGEEEVLDT ILPIVAKYGG AVIGLALDEN GIPPTAEGRV EIAKRIRDKA MSYGIPKEDI IIDCLTLTVS AEQKAAAETL KAMNIVKNEL GLRTVLGVSN ISFGLPNREI INKTFLTIAM ANGLDLPIIN PNVPSMVWAV KAYKVLAAID ENSMDFIDYS SKVQPEVTTT KTEVVKSNDS TVSLGSELAD KILKAMETGM KDDGRSYTSQ LLKEKEAMEI INQILIPALD VVGDKFEKGT IFLPQLILAA DVAKECFDEI KNYLADSGDS SESKGKIIVA TVKGDIHDIG KNIVKVILEN YGYNVIDLGR DVDCMEVVNA AIENDVHLVG LSALMTTTLG SMEETIKLLR EHNVDCKIMV GGAVLTEDYA MKIGADYYAK DAKMSADIAK KVLG // ID A5ZH15_9BACE Unreviewed; 915 AA. AC A5ZH15; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 01-APR-2015, entry version 44. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EDM20724.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EDM20724.1}; GN Name=metH {ECO:0000313|EMBL:EDM20724.1}; GN ORFNames=BACCAC_02187 {ECO:0000313|EMBL:EDM20724.1}; OS Bacteroides caccae ATCC 43185. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=411901 {ECO:0000313|EMBL:EDM20724.1}; RN [1] {ECO:0000313|EMBL:EDM20724.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43185 {ECO:0000313|EMBL:EDM20724.1}; 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 (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EDM20724.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43185 {ECO:0000313|EMBL:EDM20724.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EDM20724.1}. 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; AAVM02000004; EDM20724.1; -; Genomic_DNA. DR ProteinModelPortal; A5ZH15; -. DR SMR; A5ZH15; 651-895. DR EnsemblBacteria; EDM20724; EDM20724; BACCAC_02187. DR PATRIC; 28982928; VBIBacCac10171_2053. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EDM20724.1}; KW Transferase {ECO:0000313|EMBL:EDM20724.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 915 AA; 100056 MW; 1CDF89E4DDC3787C CRC64; MKKTISQIVS DRILILDGAM GTMIQQYNLT EEDFRGERFA HIPGQLKGNN DLLCLTRPDV IQDIHRKYLE AGADIIETNT FSSTTVSMAD YHVEEYVREI NLAAVKLARE LADEYTAKNP DKPRFVAGSV GPTNKTCSMS PDVNNPAYRA LTYDELAAAY QQQMEAMLEG GVDAILIETI FDTLNAKTAI FAAEQAMKVT GVEVPVMLSV TVSDVGGRTL SGQTLDAFLA SVQHANIFSV GLNCSFGARQ LKPFLEQLAV RAPYYISAYP NAGLPNSLGK YDQTPADMAH EVKEYIQEGL INIIGGCCGT TDAYIAEYPA LVEGARPHIP APKPDCMWLS GLELLEVKPE INFVNVGERC NVAGSRKFLR LINEKKYDEA LSIARQQVED GALVIDVNMD DGLLDAKAEM TTFLNLIMSE PEIARVPVMI DSSKWEVIEA GLKCLQGKSI VNSISLKEGE DKFLEHARII KQYGAAAVVM AFDEKGQADT AARKIEVCER AYRLLVDEIG FNPHDIIFDP NVLAVATGIE EHNNYAVDFI EATGWIKKNL PGAHVSGGVS NLSFSFRGNN YIREAMHAVF LYHAIQQGMD MGIVNPGTSV LYSDIPVDIL EKIEDVVLNR RPDAAERLIE LAEALKATSG EAAGQQAVKH DAWRDESVQE RLKYALMKGI GDYLEQDLAE ALPLYDKAVN VIEGPLMDGM NYVGELFGAG KMFLPQVVKT ARTMKKAVAI LQPIIESEKV EGTTSAGKVL LATVKGDVHD IGKNIVAVVM ACNGYEIVDL GVMVPAETIV QRAIEEKVDM IGLSGLITPS LEEMAHVAIE LEKAGLDIPL LIGGATTSKM HTALKIAPVY HAPVVHLKDA SQNASVASRL LNPQLKAELV NELEAEYEAL REKSGLLRRE TVSLEEAQKN KLNLF // ID A5ZUF2_9FIRM Unreviewed; 289 AA. AC A5ZUF2; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EDM86732.1}; GN ORFNames=RUMOBE_02637 {ECO:0000313|EMBL:EDM86732.1}; OS Ruminococcus obeum ATCC 29174. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Blautia. OX NCBI_TaxID=411459 {ECO:0000313|EMBL:EDM86732.1}; RN [1] {ECO:0000313|EMBL:EDM86732.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29174 {ECO:0000313|EMBL:EDM86732.1}; 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 (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EDM86732.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29174 {ECO:0000313|EMBL:EDM86732.1}; 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. {ECO:0000313|EMBL:EDM86732.1}. 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; AAVO02000012; EDM86732.1; -; Genomic_DNA. DR RefSeq; WP_005422212.1; NZ_DS264297.1. DR ProteinModelPortal; A5ZUF2; -. DR EnsemblBacteria; EDM86732; EDM86732; RUMOBE_02637. DR PATRIC; 29795280; VBIRumObe16879_0331. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDM86732.1}; KW Transferase {ECO:0000313|EMBL:EDM86732.1}. SQ SEQUENCE 289 AA; 30660 MW; 75F440942BCCA00E CRC64; MTKEEFRKLT ENILILDGAT GSNLMASGMP RGICTETWVI DHKDIIQDLQ RAYIQAGSQV IYAPTFGGNS INLEKHGLRD KIEEINRTLV GYSKELAGSG IYVAGDITTS GSFITADGDY TYTEAYNMYQ EQIRILADAG IDLIAAETMI NIEETLAAVD AAASVCDLPI MCTMTVEADG SIFSGGNAVE AAVSLEAAGA DAVGINCSVG PDQLVSVVRN IKENVSIPVI AKPNAGMPVI DEKGNAVYSM NAEEFAHHMK VLIENGASVV GGCCGTTPSF IKALHDTIR // ID A6ARL1_VIBCY Unreviewed; 1226 AA. AC A6ARL1; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 43. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EDL68647.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EDL68647.1}; GN Name=metH {ECO:0000313|EMBL:EDL68647.1}; GN ORFNames=A1Q_4802 {ECO:0000313|EMBL:EDL68647.1}; OS Vibrio campbellii (strain HY01). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=410291 {ECO:0000313|EMBL:EDL68647.1}; RN [1] {ECO:0000313|EMBL:EDL68647.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HY01 {ECO:0000313|EMBL:EDL68647.1}; RA Heidelberg J., Sebastian Y.; RT "Annotation of Vibrio harveyi HY01."; RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EDL68647.1}. 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; AAWP01000028; EDL68647.1; -; Genomic_DNA. DR RefSeq; WP_005432817.1; NZ_DS179593.1. DR ProteinModelPortal; A6ARL1; -. DR SMR; A6ARL1; 654-1224. DR EnsemblBacteria; EDL68647; EDL68647; A1Q_4802. DR PATRIC; 31189610; VBIVibHar127108_4144. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EDL68647.1}; KW Transferase {ECO:0000313|EMBL:EDL68647.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1226 AA; 136638 MW; F3A74818E134FB57 CRC64; MGSNVRQQIE AQLKQRILLI DGGMGTMIQG YKLEEQDYRG ERFADWHCDL KGNNDLLVLT QPQLIKEIHS AYLEAGADIL ETNTFNATTI AMADYEMESL SEEINFAAAK LAREAADEWT AKTPERPRYV AGVLGPTNRT CSISPDVNDP GYRNVSFDEL VEAYSESTRA LIKGGSDLIL IETIFDTLNA KACAFAVDSV FEELGIELPV MISGTITDAS GRTLSGQTTE AFYNSLRHVN PISFGLNCAL GPDELRPYVE ELSRISESFV STHPNAGLPN AFGEYDLSPE DMAEHVKEWA ESGFLNLIGG CCGTTPEHIR HMAMAVEGVK PRDLPELTVA CRLSGLEPLT IEKETLFINV GERTNVTGSA RFKRLIKEEL YDEALEVARQ QVENGAQIID INMDEGMLDA EACMVRFLNL CASEPEISKV PIMVDSSKWE VIEAGLKCIQ GKGIVNSISL KEGKEKFVEQ AKLIRRYGAA VIVMAFDEVG QAETRERKLE ICTNAYRILV DEVGFPPEDI IFDPNIFAVA TGIEEHNNYA VDFIEAVADI KRDLPHAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK NGMDMGIVNA GQLEIYDNVP DKLREAVEDV VLNRRDDSTE RLLDIAAEYA GKGVGKEEDA SALEWRTWTV EKRLEHALVK GITEFIVEDT EEARLNASKP LEVIEGPLMD GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AHLEPFINKE KQAGSSNGKI LLATVKGDVH DIGKNIVGVV LQCNNYEIID LGVMVPCEKI LKVAKEENVD IIGLSGLITP SLDEMVHVAK EMERLDFDLP LLIGGATTSK AHTAVKIEQN YKHPVVYVNN ASRAVGVCTS LLSDELRPGF VEKLDVDYER VRDQHNRKKP RTKPVTLEEA RANKVAIDWD KYTPPAPVKP GIHIFDDFEV STLRKYIDWT PFFMTWSLVG KYPTIFDHEE VGEEAQRLYK DANELLDRVE REGLLKARGM CGLFPAASVG DDIEVYTDES RTEVAKVLHN LRQQTEKPKG FNYCLSDYVA PKESGKRDWV GAFAVTGGIG ERELADEYKA QGDDYNAIMI QAVADRLAEA FAEYLHERVR KEIWGYAANE ALSNEELIRE KYQGIRPAPG YPACPEHTEK GPLWDLMNVE ENIGMSLTSS YAMYPGASVS GWYFSHPDSR YFAIAQIQED QLQSYADRKG WDRIEAEKWL GPNING // ID A6B8R4_VIBPQ Unreviewed; 1226 AA. AC A6B8R4; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 51. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EDM57440.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EDM57440.1}; GN Name=metH {ECO:0000313|EMBL:EDM57440.1}; GN ORFNames=A79_3620 {ECO:0000313|EMBL:EDM57440.1}; OS Vibrio parahaemolyticus serotype O3:K6 (strain AQ3810). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=419109 {ECO:0000313|EMBL:EDM57440.1}; RN [1] {ECO:0000313|EMBL:EDM57440.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AQ3810 {ECO:0000313|EMBL:EDM57440.1}; 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. {ECO:0000313|EMBL:EDM57440.1}. 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; AAWQ01000177; EDM57440.1; -; Genomic_DNA. DR RefSeq; WP_005453805.1; NZ_KK073774.1. DR ProteinModelPortal; A6B8R4; -. DR SMR; A6B8R4; 654-1224. DR PRIDE; A6B8R4; -. DR EnsemblBacteria; EDM57440; EDM57440; A79_3620. DR EnsemblBacteria; EXF67522; EXF67522; D030_4642. DR PATRIC; 38610672; VBIVibPar22798_0028. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDM57440.1}; KW Transferase {ECO:0000313|EMBL:EDM57440.1}. SQ SEQUENCE 1226 AA; 136218 MW; 2F7A3269FB7C20A9 CRC64; MGSKVRQQIE AQLKQRILLI DGGMGTMIQG YKLEEQDYRG ERFANWHCDL KGNNDLLVLS QPQLIKEIHS AYLEAGADIL ETNTFNATTI AMADYEMESL SEEINFAAAK LAREVADEWT AKTPDKPRYV AGVLGPTNRT CSISPDVNDP GYRNVSFDEL VEAYSESTRA LIRGGADLIL IETIFDTLNA KACAFAVDSV FEELGVALPV MISGTITDAS GRTLSGQTTE AFYNSLRHVR PLSFGLNCAL GPDELRPYVE ELSRISESFV SAHPNAGLPN AFGEYDLSPE DMAEHVKEWA SSGFLNLIGG CCGTTPEHIR QMAQAVEGVT PRALPDLPVA CRLSGLEPLT IEKETLFINV GERTNVTGSA RFKRLIKEEQ YDEALEVARQ QVENGAQIID INMDEGMLDA QACMVRFLNL CASEPEISKV PIMVDSSKWE VIEAGLKCIQ GKGIVNSISL KEGKEKFVEQ AKLIRRYGAA VIVMAFDEVG QAETRTRKLE ICTNAYRILV DEVGFPPEDI IFDPNIFAVA TGIDEHNNYA VDFIEAVADI KRDLPHAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK NGMDMGIVNA GQLEIYDNVP EKLREAVEDV VLNRRDDATE RLLDIAAEYA DKGVGKEEDA SALEWRTWPV AKRLEHALVK GITEFIVADT EEARVNAVKP LEVIEGPLMD GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AHLEPFINAE KQSGSSNGKI LLATVKGDVH DIGKNIVGVV LQCNNYEIID LGVMVPCEKI LKVAIEENVD IIGLSGLITP SLDEMVHVAK EMERLNFDLP LLIGGATTSK AHTAVKIEQN YKNPVVYVNN ASRAVGVCSS LLSDERRPAF IEKLDADYER VRDQHNRKKP RTKPVTLEQA RANKVAIDWD AYTPPVPAKP GLHIFDDFDV ATLRKYIDWT PFFMTWSLVG KYPTIFKHEE VGEEAQRLFH DANELLDRVE REGLLKARGI CGLFPAASVG DDIEVYTDES RTEVAKVLRN LRQQTEKPKG FNYCLSDYIA PKESGKQDWV GAFAVTGGIG ERELADEYKA QGDDYNAIMI QAVADRLAEA FAEYLHERVR KEIWGYAADE NLSNDELIRE KYQGIRPAPG YPACPEHTEK GPLWELLNVE ENIGMSLTTS YAMYPGASVS GWYFSHPDSR YFAIAQIQDD QLESYADRKG WDRIEAEKWL GPNING // ID A6B9U9_VIBPQ Unreviewed; 597 AA. AC A6B9U9; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 36. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EDM57054.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EDM57054.1}; GN ORFNames=A79_5262 {ECO:0000313|EMBL:EDM57054.1}; OS Vibrio parahaemolyticus serotype O3:K6 (strain AQ3810). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=419109 {ECO:0000313|EMBL:EDM57054.1}; RN [1] {ECO:0000313|EMBL:EDM57054.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AQ3810 {ECO:0000313|EMBL:EDM57054.1}; 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. {ECO:0000313|EMBL:EDM57054.1}. 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; AAWQ01000290; EDM57054.1; -; Genomic_DNA. DR RefSeq; WP_005468954.1; NZ_DS180860.1. DR EnsemblBacteria; EDM57054; EDM57054; A79_5262. DR PATRIC; 38622719; VBIVibPar22798_5536. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDM57054.1}; KW Transferase {ECO:0000313|EMBL:EDM57054.1}. SQ SEQUENCE 597 AA; 65934 MW; D1B935673402279D CRC64; MGSKVRQQIE AQLKQRILLI DGGMGTMIQG YKLEEQDYRG ERFANWHCDL KGNNDLLVLS QPQLIKEIHS AYLEAGADIL ETNTFNATTI AMADYEMESL SEEINFAAAK LAREVADEWT AKTPDKPRYV AGVLGPTNRT CSISPDVNDP GYRNVSFDEL VEAYSESTRA LIRGGADLIL IETIFDTLNA KACAFAVDSV FEELGVALPV MISGTITDAS GRTLSGQTTE AFYNSLRHVR PLSFGLNCAL GPDELRPYVE ELSRISESFV SAHPNAGLPN AFGEYDLSPE DMAEHVKEWA SSGFLNLIGG CCGTTPEHIR QMAQAVEGVT PRALPDLPVA CRLSGLEPLT IEKETLFINV GERTNVTGSA RFKRLIKEEQ YDEALEVARQ QVENGAQIID INMDEGMLDA QACMVRFLNL CASEPEISKV PIMVDSSKWE VIEAGLKCIQ GKGIVNSISL KEGKEKFVEQ AKLIRRYGAA VIVMAFDEVG QAETRTRKLE ICTNAYRILV DEVGFPPEDI IFDPNIFAVA TGIDEHNNYA VDFIEAVADI KRDLPHAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK TVWTWAL // ID A6B9Z6_VIBPQ Unreviewed; 200 AA. AC A6B9Z6; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EDM57007.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EDM57007.1}; DE Flags: Fragment; GN ORFNames=A79_5518 {ECO:0000313|EMBL:EDM57007.1}; OS Vibrio parahaemolyticus serotype O3:K6 (strain AQ3810). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=419109 {ECO:0000313|EMBL:EDM57007.1}; RN [1] {ECO:0000313|EMBL:EDM57007.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AQ3810 {ECO:0000313|EMBL:EDM57007.1}; 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. {ECO:0000313|EMBL:EDM57007.1}. 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; AAWQ01000315; EDM57007.1; -; Genomic_DNA. DR RefSeq; WP_005461634.1; NZ_DS180239.1. DR EnsemblBacteria; EDM57007; EDM57007; A79_5518. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDM57007.1}; KW Transferase {ECO:0000313|EMBL:EDM57007.1}. FT NON_TER 200 200 {ECO:0000313|EMBL:EDM57007.1}. SQ SEQUENCE 200 AA; 22128 MW; 1B40E7A656DC4A89 CRC64; MGSKVRQQIE AQLKQRILLI DGGMGTMIQG YKLEEQDYRG ERFANWHCDL KGNNDLLVLS QPQLIKEIHS AYLEAGADIL ETNTFNATTI AMADYEMESL SEEINFAAAK LAREVADEWT AKTPDKPRYV AGVLGPTNRT CSISPDVNDP GYRNVSFDEL VEAYSESTRA LIRGGADLIL IETIFDTLNA KACAFAVDSV // ID A6BDT3_9FIRM Unreviewed; 796 AA. AC A6BDT3; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 39. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EDM63772.1}; GN ORFNames=DORLON_00449 {ECO:0000313|EMBL:EDM63772.1}; OS Dorea longicatena DSM 13814. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Dorea. OX NCBI_TaxID=411462 {ECO:0000313|EMBL:EDM63772.1}; RN [1] {ECO:0000313|EMBL:EDM63772.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 13814 {ECO:0000313|EMBL:EDM63772.1}; 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 (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EDM63772.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 13814 {ECO:0000313|EMBL:EDM63772.1}; 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. {ECO:0000313|EMBL:EDM63772.1}. 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; AAXB02000002; EDM63772.1; -; Genomic_DNA. DR RefSeq; WP_006426473.1; NZ_DS264392.1. DR ProteinModelPortal; A6BDT3; -. DR EnsemblBacteria; EDM63772; EDM63772; DORLON_00449. DR PATRIC; 36985413; VBIDorLon81175_0403. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDM63772.1}; KW Transferase {ECO:0000313|EMBL:EDM63772.1}. SQ SEQUENCE 796 AA; 86575 MW; F010E235FE8F62A7 CRC64; MLLERLGKEL LYFDGGMGTL LQSKGLQPGE LPEVWNLEHA EEIIDIHKAY FEAGSDIVLS NTFGANAIKF HDSKYGLKEI VTAGIQNAKK AAERGVHDGR KTYVALDVGP TGKLLKPMGD LSFEDAYDAF KETMIYGEQA GADLIHIETM SDSYEVKAAV LAAKENTSLP VFATMIFDEK GKLLTGGDVP AVVTMLEGLR VDALGINCGM GPEQMLPILE DILKYASVPI IVKPNAGLPK QRDGEVYYDV EPEQFAGYMA KIVEMGAHVI GGCCGTTPAH IQKMVETTRE MSVKPATKKD ITMVSSYGHA VILGGKPMII GERINPTGKK KFKQALKDHD MDYILKEGIT QQDKGAHILD VNVGLPDIDE PAMMKEVIME LQSVSSLPLQ IDTVDITAME AAMRIYNGKP MVNSVNGKQE NMDAVFPLIK RYGGVVIGLT IDEDGIPATA DGRVRVAGKI IEEAKKYGID KKDIVIDVLA MTISSEPEGA KVTLEALKKV RETYGVCTVL GVSNISFGLP YRPAVNSNFY TMAMQNGLSA GIINPSSEDM MCSYYSFCAL MNYDKNCEDY IRVYGSQKAG TPAPAAKAEL TLKEAIEKGL KEEAHHATGE LLKEQAPLEI INEHLIPALD TVGKGFEKGT VFLPQLLMSA DAAKIAFAVI KDVLAQEGGE VQAKNKVILA TVKGDIHDIG KNIVKVLLEN YSFDVIDLGK DVPPEVIVDT AVEQDIRLVG LSALMTTTVV SMEETIKLLR ERKPECKVMV GGAVLNQDYA DMIGADFYGK DAMQSVYYAQ RVFGEE // ID A6BZ53_9PLAN Unreviewed; 1234 AA. AC A6BZ53; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 48. DE SubName: Full=Peptidase S26A, signal peptidase I {ECO:0000313|EMBL:EDL62348.1}; GN ORFNames=PM8797T_28509 {ECO:0000313|EMBL:EDL62348.1}; OS Planctomyces maris DSM 8797. OC Bacteria; Planctomycetes; Planctomycetia; Planctomycetales; OC Planctomycetaceae; Planctomyces. OX NCBI_TaxID=344747 {ECO:0000313|EMBL:EDL62348.1}; RN [1] {ECO:0000313|EMBL:EDL62348.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 8797 {ECO:0000313|EMBL:EDL62348.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EDL62348.1}. 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; ABCE01000001; EDL62348.1; -; Genomic_DNA. DR RefSeq; WP_002643675.1; NZ_ABCE01000001.1. DR EnsemblBacteria; EDL62348; EDL62348; PM8797T_28509. DR PATRIC; 30923292; VBIPlaMar116015_0161. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 763 763 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1234 AA; 137067 MW; 38E56A7FA4B71585 CRC64; MSDRAARIEA LYSAVQKRIL ILDGAMGTMI QNHKLKEADY RGSRFADYHM DIAGNNDLLS LTQPEIIRGI HREYLEAGAD IIETNTFNGT RLSQSDYQME SLVHELNLES ARLAREVADE ITAENPDKPR WVAGILGPTS RTCSISPDVN DPGARNVTYD ELVENYLESI DGLVKGGADL ILIETIFDTL NAKAAVFAVK TYFQRENLEL PIMISGTITD ASGRTLSGQT TEAFWNSLSH AKPFSIGLNC ALGAQELRQY VKELSRVADT YVSAHPNAGL PNEFGEYDQS AAEMAEIVDE FASSGFLNIL GGCCGTTPAH IKAIAEAMEK HYPRPIPEIE PALRLSGLEP FNVTKDSLFV NVGERCNVTG SARFKRLIKE DDYDTALEVA LEQVQNGAHV MDVNMDEGML DAVKAMTLFL NLVATEPEIA RVPVMVDSSK WEVIVAGLKC IQGKPIVNSI SLKEGEAEFL ERARLCQMYG AAVVIMAFDE EGQADTQQRK TEICARSYKL LVEQLDFPPQ DIIFDPNIFA VATGIDEHNN YAVDFIEATR WIRQNLPYAS VSGGVSNVSF SFRGNNPVRE AIHSVFLYYA IQAGMNMGIV NATQLAVYDD LPAKLKDRVE DVILNRTPEG TEALLAIAEE YRGDGKAGSS KMEDLSWREL PVTKRIEHAL VKGISTYIIE DAELARQELP RPLDVIEGPL MDGMNVVGDL FGAGKMFLPQ VVKSARVMKQ AVAYLQPYIE MEKQEESKPN GRILMATVKG DVHDIGKNIV GVVLQCNNFE VIDLGVMVPC ETILKTAREK QCDVIGLSGL ITPSLDEMVT VAAEMERLGM DLPLMIGGAT TSKAHTAVKI EPQYTRNQVV YVPDASRAVG VAAALISDEQ HDDYVAKIKA EYVTVRERVA NRKPQGTPVP YAEAVTQGLQ IDWEKYTPPK PSFTGTQVLD DYPLEKLVDY IDWTPFFISW NLVGKYPRIL EDDVVGEAAR DLFESGQAML KKIIDEKLLK ARAVIGFWPA NRMQGDDIEV YADENRGEVI ANLHHIRQQV RKRGQEEKPL MSLADFIAPK ESGQQDYIGG FVVTAGIGAE ELAKSYEAEH DDYSSIMVKA LADRLAEAFA EHLHARVRRE FWGYAADESL SNDALIKEEY QGIRPAPGYP SCPDHTEKAT LFKMLNAEQE IGVNLTEHFA MYPTAAVSGW YFSAPESRYF HTGKIDRDQL ESLAERKKMS LEDMERWLRP VLMD // ID A6D2I5_9VIBR Unreviewed; 298 AA. AC A6D2I5; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EDL53208.1}; GN ORFNames=VSAK1_01497 {ECO:0000313|EMBL:EDL53208.1}; OS Vibrio shilonii AK1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=391591 {ECO:0000313|EMBL:EDL53208.1}; RN [1] {ECO:0000313|EMBL:EDL53208.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AK1 {ECO:0000313|EMBL:EDL53208.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDL53208.1}. 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; ABCH01000020; EDL53208.1; -; Genomic_DNA. DR RefSeq; WP_006072293.1; NZ_ABCH01000020.1. DR ProteinModelPortal; A6D2I5; -. DR EnsemblBacteria; EDL53208; EDL53208; VSAK1_01497. DR PATRIC; 28383916; VBIVibShi100628_2747. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EDL53208.1}; KW Transferase {ECO:0000313|EMBL:EDL53208.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 204 204 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 279 279 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 280 280 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 298 AA; 32415 MW; 5469FBB9F150EA5A CRC64; MNPLTILDGG MGRELKRMGA PFSQPYWSAQ ALIEAPHFVE QAHQQFIDSG ADIITTNSYA CVPFHLGDVL YHERGTELAG LAAKLAKNAV SHSNRAVTIA GSLPPAFGSY RPDLFMAERG AQVWQDLMQA QDAYVDIWLV ETLSSIEEAQ VVSQVLAEST KPKYYAYTLL DDVSQLGKLR SGETVVDAVQ SLLKHNPDGI LFNCSIPEVI EAALAATAKV LESHHSSICL GAFANSFTPI QSGHKANDAV QELREVSPQE YLLFAKKWQQ HGANIIGGCC GIGPEHIEVL AKWKASVK // ID A6D961_9VIBR Unreviewed; 1225 AA. AC A6D961; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 43. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EDL50860.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EDL50860.1}; GN Name=metH {ECO:0000313|EMBL:EDL50860.1}; GN ORFNames=VSAK1_04630 {ECO:0000313|EMBL:EDL50860.1}; OS Vibrio shilonii AK1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=391591 {ECO:0000313|EMBL:EDL50860.1}; RN [1] {ECO:0000313|EMBL:EDL50860.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AK1 {ECO:0000313|EMBL:EDL50860.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EDL50860.1}. 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; ABCH01000093; EDL50860.1; -; Genomic_DNA. DR RefSeq; WP_006075527.1; NZ_ABCH01000093.1. DR ProteinModelPortal; A6D961; -. DR SMR; A6D961; 654-1224. DR EnsemblBacteria; EDL50860; EDL50860; VSAK1_04630. DR PATRIC; 28388630; VBIVibShi100628_5016. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EDL50860.1}; KW Transferase {ECO:0000313|EMBL:EDL50860.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1225 AA; 136173 MW; ACE4B7C5FB7DBA66 CRC64; MGSNVRQQIE SQLRQRILLI DGGMGTMIQG YKLEEEDYRG ERFADWPSDL KGNNDLLVLT QPALIKEIHS AYLEAGADIL ETNTFNATTI AMADYDMESL SEEINYQAAK LAREAADEWT TKTPDRPRYV AGVLGPTNRT CSISPDVNDP GYRNVTFDEL VEAYSESTHA LIKGGSDLIL IETIFDTLNA KACAFAVESV FEELGYELPV MISGTITDAS GRTLSGQTTE AFYNALRHVR PLSFGLNCAL GPDELRQYVE EMSRIGESFV SAHPNAGLPN AFGEYDLSPE DMAEHIGEWA RSGFLNLVGG CCGTTPEHIR QMANAVEGVT PRPLPELPVA CRLSGLEPLT IEKDSLFINV GERTNVTGSA RFKRLIKEEQ YDEALEVARQ QVENGAQIID INMDEGMLDA EACMVRFLNL CASEPEISKV PIMVDSSKWE VIEAGLKCIQ GKGIVNSISM KEGKEKFVEQ AKLIRRYGAA VIVMAFDEIG QAETRERKLE ICTNAYNILV DEVGFPPEDI IFDPNIFAVA TGIEEHNNYA VDFIEAVADI KRDLPHAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK NGMDMGIVNA GQLEIYDNVP EKLREAVEDV VLNRRDDGTE RLLDIAAEYA NKGVGKEEDA SALEWRTWPV SKRLEHALVK GITEFIVEDT EEARVNASKP LEVIEGPLMD GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AHLEPFINAE KQAGSSNGKI LLATVKGDVH DIGKNIVGVV LQCNNYEIID LGVMVPCETI LKVAKEENVD IIGLSGLITP SLDEMVHVAK EMERQGFTLP LLIGGATTSK AHTAVKIEQN YSEPVVYVNN ASRAVGVCTS LLSEELKPAF IEKLDIDYER VRDQHNRKKP RTKPVTLEEA RANKVAIDWQ NYTPPIPAKS GVHVFENFEV ATLRNYIDWT PFFMTWSLVG KYPAILEHEE VGEEAKRLFH DANELLDRVE REGLLKASGM CALFPAASVG DDIEVYTDET RTQVRKVLHN LRQQTEKPKG FNYCLSDYVA PKESGKQDWI GAFAVTGGIG ERELADEYKA QGDDYNAIMI QAVADRLAEA FAEYMHEKVR KEIWGYSADE ALSNDDLIRE KYQGIRPAPG YPACPEHTEK GALWELLEVE QTIGMSLTSS YAMWPGASVS GWYFSHPDSR YFAIAQIQQD QVDSYADRKG WDQTEAEKWL GPNIN // ID A6DGP4_9BACT Unreviewed; 1204 AA. AC A6DGP4; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 46. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EDM29361.1}; GN ORFNames=LNTAR_23264 {ECO:0000313|EMBL:EDM29361.1}; OS Lentisphaera araneosa HTCC2155. OC Bacteria; Lentisphaerae; Lentisphaeria; Lentisphaerales; OC Lentisphaeraceae; Lentisphaera. OX NCBI_TaxID=313628 {ECO:0000313|EMBL:EDM29361.1}; RN [1] {ECO:0000313|EMBL:EDM29361.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2155 {ECO:0000313|EMBL:EDM29361.1}; 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] {ECO:0000313|EMBL:EDM29361.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2155 {ECO:0000313|EMBL:EDM29361.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EDM29361.1}. 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; ABCK01000002; EDM29361.1; -; Genomic_DNA. DR RefSeq; WP_007277081.1; NZ_ABCK01000002.1. DR ProteinModelPortal; A6DGP4; -. DR EnsemblBacteria; EDM29361; EDM29361; LNTAR_23264. DR PATRIC; 29240755; VBILenAra45852_0542. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EDM29361.1}; KW Transferase {ECO:0000313|EMBL:EDM29361.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 256 256 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 790 790 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1204 AA; 133459 MW; A23A3A2406A90054 CRC64; MKFLDALKEQ ILVLDGAMGS MVQLLKLPDS AYGGEEYAML SDLLVFSRPD QVRDNIHLEY LKAGANILET NTFGASPLRL QEFDFSKMDL SDFADLPEGL DFLENDYYAL THYFNIRGIE LAQDAIEKYK KMDEYDGRPL FVAGSIGPSN WVISSTAANL NKTDFATIKQ NFYLQVKAMM QANVDVLLFE TQQDMLELKA SIAGAHQAAE ELGFKVPIMA QVTVDQFNKM QIFNTDMEAA YAAVGGIGID VFGINCTLGP ELMQKVIPAL AQMSELPISV VPNAGQPISV NGETVYPLAP EKMGEYMRDY EAENGINIVG GCCGTTPAHI AEITKHLGGK KPKVREVKRR NLISGPQNAF ELDASEGLIQ IGERLNVRGS KKVRDAVEVE DNIDNDALEE VVNEQNRDLG IDILDVCMDS NIVNTEKVLP KVIYDMTMDF GGAFCIDSFA VDALEVAIDV YPGRPIINSI ALEEHSPGVS KIDAIVPLTK HHNPVYIALV TDGDGPALTA DKKLELAEKI VAESAKHGVT PDQLMIDINA FPIGAESIEG MNFALESLNS LKPIKAIHPE IMTSIGVGNL TNGLAKKPYM RVVLTSVFLD EGYKRGLDAA IVNPNHFIPV ESIEPYDYEL GKKVIFDRDM DAFEELETIA ESRRGIVKEK KCSYDDMPVE EAICEKIKDG YKEKSEGSFE KNEFTYEYKD AIALSMKDIV DVHQPLDFIN DYLMEAMREL GDGFGRGEVS LPHLLKSADV MKHCMNFLEA YMKNMSGESL DGKRTFKGTV IIGTVYQDVH SIGKDLAKTL LENYGYRVID LGVQVPLEKF IDTAIAENAD AIGMSALLVQ TSNHMITVQQ MCQEKGVDFP LLIGGAPVNS RHAAYVSMYG QDDFAAMNGK VFYCQSGMDG VNIMNTLMDS GKRDGLIADN TKKLEQFYRL AIKQAEAREK HESGLDDRKI DLSDWKAPEG KAIRLADYNV SITDLKQHFD LRTLYGLNWD FGGKKAWAKK GVTEDDLNRM RDEWVQKSDE NNWIDPISRF ALLPAQSLDE NTVAVYNPDD LNEELAQFTF NHVAGRKDRW SVPQYIHSKK SGEFDLIGIQ ISSGGAKTEE VINEMREAGE LEDCFLLQGL SDRVAEDMAD QAHCSARKLA GVDLSQGCRY SPGYPAMEDM ANNKIIFDLL KADEMGISMT DADEFAPTST TAAFVVFNPD ATYQ // ID A6DZN2_9RHOB Unreviewed; 336 AA. AC A6DZN2; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EDM31805.1}; GN ORFNames=RTM1035_07729 {ECO:0000313|EMBL:EDM31805.1}; OS Roseovarius sp. TM1035. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseovarius. OX NCBI_TaxID=391613 {ECO:0000313|EMBL:EDM31805.1}; RN [1] {ECO:0000313|EMBL:EDM31805.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TM1035 {ECO:0000313|EMBL:EDM31805.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDM31805.1}. 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; ABCL01000004; EDM31805.1; -; Genomic_DNA. DR RefSeq; WP_008280813.1; NZ_ABCL01000004.1. DR ProteinModelPortal; A6DZN2; -. DR EnsemblBacteria; EDM31805; EDM31805; RTM1035_07729. DR PATRIC; 28156155; VBIRosSp37286_1744. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EDM31805.1}; KW Transferase {ECO:0000313|EMBL:EDM31805.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 212 212 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 278 278 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 279 279 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 336 AA; 35771 MW; 824FA1E76CD3879A CRC64; MTNALTKMLA TRDWILADGA TGTNLFNMGL QSGDAPEMWN DQHPDRIKRL YTEAVDAGSD LFLTNSFGGN AARLKLHGAQ GRARELSRIS AEIGRDVADR YDRTVIVAGS VGPTGEIMAP MGALTHELAV EIFHEQAEGL KEGGADVLWL ETISAPEEYK AAAEAFKLAD MPWCGTMSFD TAGRTMMGVT SSDMATMVEK LGNPPMAYGA NCGVGASDLL RTILGFVAQG SERPIIAKGN AGIPKYHDGH IHYDGTPELM AEYAVLARDS GATIIGGCCG TMPEHLSKMR AALENRPRGA RPTLEEITEA LGGFSSGGDG TGDDTAAPRR PRRRRG // ID A6E2N9_9RHOB Unreviewed; 298 AA. AC A6E2N9; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EDM31420.1}; GN ORFNames=RTM1035_02985 {ECO:0000313|EMBL:EDM31420.1}; OS Roseovarius sp. TM1035. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseovarius. OX NCBI_TaxID=391613 {ECO:0000313|EMBL:EDM31420.1}; RN [1] {ECO:0000313|EMBL:EDM31420.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TM1035 {ECO:0000313|EMBL:EDM31420.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDM31420.1}. 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; ABCL01000006; EDM31420.1; -; Genomic_DNA. DR RefSeq; WP_008281905.1; NZ_ABCL01000006.1. DR ProteinModelPortal; A6E2N9; -. DR EnsemblBacteria; EDM31420; EDM31420; RTM1035_02985. DR PATRIC; 28158325; VBIRosSp37286_2807. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EDM31420.1}; KW Transferase {ECO:0000313|EMBL:EDM31420.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 202 202 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 275 275 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 276 276 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 298 AA; 31017 MW; 08D480EF55BE58BD CRC64; MTEITLLDGS IGQELVKRSG DRATPLWSTQ VMIDHPGIVR LVHDDYFAVG ATVASTNTYA VLRDRLARVG LQDEVARLTD VAVGAAVAAR DAHGSGRVAG AIGPLVQSYR PDLCPPASEA AALYAENVAL LKDRVDLILL ETMSSVDQAR GGLMAAGLSG LPVWLGVTVM DDDGTRLRSG EALGDLAALV AEFGPEAVLI NCTRPESVAA GLEIVKGFGL PFGAYANGFT CISAGFLGAA PTVDALEQRH DLTPAAYAEF AMGWVDQGAS IVGGCCEVGP AHIEELARRL RAAGHDIV // ID A6EBG1_9SPHI Unreviewed; 1219 AA. AC A6EBG1; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 01-APR-2015, entry version 47. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EDM37060.1}; GN ORFNames=PBAL39_04658 {ECO:0000313|EMBL:EDM37060.1}; OS Pedobacter sp. BAL39. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Pedobacter. OX NCBI_TaxID=391596 {ECO:0000313|EMBL:EDM37060.1}; RN [1] {ECO:0000313|EMBL:EDM37060.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BAL39 {ECO:0000313|EMBL:EDM37060.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EDM37060.1}. 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; ABCM01000005; EDM37060.1; -; Genomic_DNA. DR RefSeq; WP_008240366.1; NZ_ABCM01000005.1. DR ProteinModelPortal; A6EBG1; -. DR SMR; A6EBG1; 645-892, 898-1219. DR EnsemblBacteria; EDM37060; EDM37060; PBAL39_04658. DR PATRIC; 31337856; VBIPedSp63332_1733. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 242 242 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 757 757 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1219 AA; 135536 MW; B701D8C17821022A CRC64; MDIRAELEKR ILIIDGAMGT MIQRYNLTEE DFRGERFKDH PCDVKGNNDL LNLTRPDIIK EIHTEYLRAG TDIIETNTFS TQRISLADYQ MEELDYEMSF EGARVARHAV DDFMAAHPDR KCFVAGAVGP TNRTLSISPD VNDPGFRALT FDELVDAYDQ QVRGLVDGGA DLLLIETIFD TLNAKAAIFS IKKYEAIIGR KIEIMISGTI TDASGRTLSG QTVEAFLNSI IHAKPLSIGF NCALGAKEMR PHIEELAAKA PCYVSAYPNA GLPNEFGAYD EMPHETAHLV EDFIQHGFVN IVGGCCGTTP EHIGCIAEKA RGITPRKIAE LKPFMRLSGL EPVTITPESI FVNIGERTNI TGSPKFSKLI LSGDYEAALT VARQQVEGGA QVIDVNMDEG MIDSEAAMTK FLNLIASEPD ISKLPIMVDS SKWSVIEAGL KCLQGKGIVN SISLKEGEDK FRESALKIMD YGAAVVVMAF DEKGQADNYE RRKEICGRSY NILVHEIGFP PEDIIFDPNI LTVATGMDEH NNYAVDFINA TRWIKENLPH AKVSGGVSNI SFSFRGNNTV REAMHSAFLY HAIGAGMDMG IVNAGMLEVY QEIPPELLER VEDVLLNRRD DATERLVEFA DTIKSKGKEV VRDEEWRKGS VEERLSHALV KGIIEYLDAD VEEARQRYAR PIQVIEGPLM DGMNIVGDLF GAGKMFLPQV VKSARVMKKA VAYLLPFIEQ EKLDNPDGDQ SSSAGRVLMA TVKGDVHDIG KNIVGVVLAC NNFEIVDMGV MVPAQEIIKK AREINADIIG LSGLITPSLD EMVHFAKEME REGFTIPLII GGATTSRIHA AVKVAPNYSG PAIHVLDASR SVTVCSTLMN KETRDDYING IRAEYDKARE AHLNKRSDKR FKSLDVAREN KFKIDLDQVA PAPSFTGTKV FEDYPLEELV PYIDWTPFFH TWELRGSYPR IFEDKLAGDE ARKLFDDAQV LLKRIIDEKL LTAKGVIGFW PANTVGDDII LDVEGKEVTI HTLRQQAEKV DGQPYYALSD FVAPKESGVA DYFGGFAVTT GIGCDELVAE FEANYDDYNS IMAKALADRL AEAFAERMHE LVRKDYWGYA QDEHLSNEAL IKEEYAGIRP APGYPACPEH TEKGTLFELL DAENRIGLRL TESYAMYPTA AVSGFYFAHP QSRYFGLGKI LKDQIEEYAL RKDMPVEEVE RWLSPNLAY // ID A6EME1_9BACT Unreviewed; 332 AA. AC A6EME1; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=Methionine synthase I, homocysteine S-methyltransferase {ECO:0000313|EMBL:EDM45741.1}; GN ORFNames=SCB49_08027 {ECO:0000313|EMBL:EDM45741.1}; OS unidentified eubacterium SCB49. OC Bacteria; Bacteroidetes; environmental samples. OX NCBI_TaxID=50743 {ECO:0000313|EMBL:EDM45741.1}; RN [1] {ECO:0000313|EMBL:EDM45741.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SCB49 {ECO:0000313|EMBL:EDM45741.1}; 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. {ECO:0000313|EMBL:EDM45741.1}. 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; ABCO01000001; EDM45741.1; -; Genomic_DNA. DR EnsemblBacteria; EDM45741; EDM45741; SCB49_08027. DR PATRIC; 30959922; VBIUniEub121565_0497. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDM45741.1}; KW Transferase {ECO:0000313|EMBL:EDM45741.1}. SQ SEQUENCE 332 AA; 35989 MW; 68636CE6E712D1E8 CRC64; MKNTKTLKEA LQNKILILDG AMGTMLQRYN FSEEDFRSTR FADFHTSVKG NNDLLSITQP EAIAEVHAKY FEAGADIVET NTFSGTTIAM ADYDMEALVY EINFESAKIA REVADKFTAL QPEKPRFVAG AMGPTNKTAS MSPDVNDPGF RAVSFEELRL AYKQQAEALL DGGVDVLLVE TVFDTLNAKA ALFAIEEIKE ERKIDVPIMI SGTITDASGR TLSGQTAEAF LISISHIPLL SVGFNCALGA KQLTPHLEVI SQKSTAAISA HPNAGLPNAF GEYDQSPEQM AEQIEAYLDK KLINIIGGCC GTTPAHIKAI AAVAKGYDPR PF // ID A6EVN6_9ALTE Unreviewed; 1235 AA. AC A6EVN6; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 44. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EDM49073.1}; GN ORFNames=MDG893_06745 {ECO:0000313|EMBL:EDM49073.1}; OS Marinobacter algicola DG893. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Marinobacter. OX NCBI_TaxID=443152 {ECO:0000313|EMBL:EDM49073.1}; RN [1] {ECO:0000313|EMBL:EDM49073.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DG893 {ECO:0000313|EMBL:EDM49073.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EDM49073.1}. 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; ABCP01000002; EDM49073.1; -; Genomic_DNA. DR RefSeq; WP_007152087.1; NZ_ABCP01000002.1. DR ProteinModelPortal; A6EVN6; -. DR SMR; A6EVN6; 657-1232. DR EnsemblBacteria; EDM49073; EDM49073; MDG893_06745. DR PATRIC; 28805951; VBIMarAlg30321_0450. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EDM49073.1}; KW Transferase {ECO:0000313|EMBL:EDM49073.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 253 253 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 316 316 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 763 763 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1235 AA; 137170 MW; CCB439EE94D0C9A4 CRC64; MTDRNARLDR LEQLGNALKE RIIVLDGGMG TMIQNLKLDE AAFRGDRFAD YDREVQGNND LLNLTQPALL RNIHADYLEA GADIIETNTF NSTQLSQADY GLESIAKELN VEAAKLARQI ADEFTARNPE KPRFVAGAVG PTSRTASISP DVNNPGYRNV DFQTLVDNYY EAVEGLVQGG SDLILIETIF DTLNAKAAIY ATQQYFIDSG IELPIMISGT ITDASGRTLS GQTTEAFWNS VSHARPVSVG LNCALGADAL RPYVEELSNK STTYVSAHPN AGLPNEFGEY DQTPEEMAEI IEGFARDGFL NIIGGCCGSR PDHIEAIADA VAKYPPRKIP NQKPALRLSG LEPFTGDENT LFINVGERTN VTGSKRFLRL IKEEQYEEAL SVARDQVENG AQIIDINMDE GMLDSKDVMV TFLNLVASEP DISRVPIMID SSKWEVIEAG LRCIQGKAVV NSISLKEGEE EFLKRARDCM RYGAAVVVMA FDEDGQADTF ERKTEICKRS YDLLVGIGFT AGDIIFDPNI FAIATGIEEH NNYAVDFINA SRWIRDNLPH ASISGGVSNV SFSFRGNDAV REAIHSVFLY HAIKAGMNMG IVNPGQLVIY DEIDPELKGL VEDVVLNRRD DATDRLLEIA ERYRSKGGKT QEEDLAWREW PVEKRVEHAL VKGITNYIIE DTEACRQRAA RPIEVIEGPL MDGMNVVGDL FGDGKMFLPQ VVKSARVMKQ AVAHLIPYIE AEKSGDQQAK GKILMATVKG DVHDIGKNIV GVVLQCNNYE VIDLGVMVPC DKILDVAKKE NVDIIGLSGL ITPSLDEMVH VAKEMQRLDF NIPLMIGGAT TSKAHTAVKI EPQYKNDIAL YVSDASRCVN VASQLLSKTA KPALVEGART EYDEIRERRK NRGERTKLVS LKEARDRAPN IRFDGYQPPK PAFTGVRSFE TYDLEKLVDY IDWTPFFISW DMSGKYPAIF DDPKRGEAAR TLFDDGQQIL QQMINEKRVS AKAAIGFWPA NRRGDDIVLY TDETREKELT TLHHLRQQDD KAPGKPMMTL SDFVAPEGDG PVDYMGGFAV TTGIGAEEFS LEFKDRNDDY NAIMVKALAD RLAEAFAEHL HERVRKEFWG YAEDEALRND DLIRERYRGI RPAPGYPACP DHTEKATLFD LLDAPANAGL ELTEHFAMFP TAAVSGWYFS HPESKYFAVG KIGVDQVEDY ATRKGISKAE AERWLAPSLA YDPAE // ID A6FBJ5_9GAMM Unreviewed; 1239 AA. AC A6FBJ5; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 01-APR-2015, entry version 47. DE SubName: Full=Methionine synthase I {ECO:0000313|EMBL:EDM67469.1}; GN ORFNames=PE36_00549 {ECO:0000313|EMBL:EDM67469.1}; OS Moritella sp. PE36. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Moritellaceae; Moritella. OX NCBI_TaxID=58051 {ECO:0000313|EMBL:EDM67469.1}; RN [1] {ECO:0000313|EMBL:EDM67469.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PE36 {ECO:0000313|EMBL:EDM67469.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EDM67469.1}. 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; ABCQ01000012; EDM67469.1; -; Genomic_DNA. DR RefSeq; WP_006031757.1; NZ_ABCQ01000012.1. DR ProteinModelPortal; A6FBJ5; -. DR SMR; A6FBJ5; 653-1239. DR EnsemblBacteria; EDM67469; EDM67469; PE36_00549. DR PATRIC; 25979572; VBIMorSp76677_1814. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 249 249 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1239 AA; 137633 MW; D48EC23237BB5285 CRC64; MATIKNKQQL EQQLKQRIML IDGGMGTMIQ DYKLQEADYR GERFADWHCD VKGNNDLLVL SKPQLIADIH KEYLDAGADI LETNTFNATT IAMADYDMES LSAEINREAA RIARQVADEK TAENPDRPRF VAGVLGPTNR TCSISPDVND PAFRNTSFDL MVEAYIESTK ALIEGGSDII LIETIFDTLN AKAAVFAVKT VFEELGFELP IMISGTITDA SGRTLTGQTT EAFYNSLRHA EPITFGLNCA LGPDELRQYV DELSRISESY VTAHPNAGLP NAFGEYDLSP EDMAVHIKEW AEAGFLNMVG GCCGTTPEHI KAMADAVEGV KPRQLPEIEI ACRLSGLEPL TIKKDSLFVN VGERTNVTGS ARFKRLIKEE NYDEALHVAL QQVESGAQII DINMDEGMLD SLHCMERFLN LVASEPDISK VPIMIDSSKW EIIEAGLKCV QGKAIVNSIS LKEGEDNFRH QAKLIRRYGA AMIVMAFDED GQADTQERKF QICKRSYDIL VNEVNFPPED IIFDPNIFAV ATGIDEHNNY AVDFIEAVKD IKRELPHAMI SGGVSNVSFS FRGNNPLREA IHAVFLYYCI REGMDMGIVN AGQLAIYDDL PKDLLDGVED VILNRNDNAT EALLALAEKY RDSGVEVEAE TQEWRSFEVN KRLEYALIKG ITEFIEEDTE EARQQATLPL EVIEGPLMDG MNAVGDLFGA GKMFLPQVVK SARVMKRAVS YLNPYIEASK QKSSSNGRIL LATVKGDVHD IGKNIVGVVL QCNNYEIVDM GVMVSCDDIL KKAVEENCDI IGLSGLITPS LDEMVHVAKE CQRKGFKLPI LIGGATTSKA HTAVKIEQNY DEPVIYVSNA SRAVGVVAAL LSETKKPELV ARMAKEYEVA REQHARKRPR SAPVTLEVAR ANKAPIDWVN YTPPVPKTLG VKKYISYSIA ELRKYIDWTP FFMTWTLAGK YPRILTDEVV GVEATSLFND ANDMLDRLEE GGAGLEGVPD DYKISVNGVI GLFPANTVND DTIEVYTDET RSQVLTKLEH LRQQTKKKPG QYNNSLADFV APKDSGKFDY IGAFAVTGGI GEDDVANYFK GIEDDYNAIL IQSVCDRLAE AMAERLHELV RKEEWGFTQT EEWSNDDLIR EKYQGIRPAP GYAACPEHTE KGTIWELLDP DSIGMKLTSS YAMWPGAAVS GLIFSHPESR YFAVASIQED QVKDYAERKN MTLEEAERWL GPNLGYAPD // ID A6FS57_9RHOB Unreviewed; 338 AA. AC A6FS57; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EDM71023.1}; GN ORFNames=RAZWK3B_16540 {ECO:0000313|EMBL:EDM71023.1}; OS Roseobacter sp. AzwK-3b. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseobacter. OX NCBI_TaxID=351016 {ECO:0000313|EMBL:EDM71023.1}; RN [1] {ECO:0000313|EMBL:EDM71023.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AzwK-3b {ECO:0000313|EMBL:EDM71023.1}; 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. {ECO:0000313|EMBL:EDM71023.1}. 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; ABCR01000006; EDM71023.1; -; Genomic_DNA. DR RefSeq; WP_007815632.1; NZ_ABCR01000006.1. DR ProteinModelPortal; A6FS57; -. DR EnsemblBacteria; EDM71023; EDM71023; RAZWK3B_16540. DR PATRIC; 28089546; VBIRosSp9675_2528. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDM71023.1}; KW Transferase {ECO:0000313|EMBL:EDM71023.1}. SQ SEQUENCE 338 AA; 35984 MW; 10BC61B56C7DFDEF CRC64; MTNALSKLLK TRDWLLADGA TGTNLFNMGL ESGDAPEMWN DEHPDRITRL YTMAVDAGSD IFLTNSFGGN AARLKLHGAE KRARELSRIS AEIGREVADK RDRTVIVAGS VGPTGEIMAP MGALTHELAV EIFHEQAEGL KEGGADVLWL ETISAPEEYK AAAEAFKLAG MPWCGTMSFD TAGRTMMGLT SADMVNVVEG LANPPLGYGA NCGVGASDLL RTVLGFAAQG TDRPIIAKGN AGIPKYHDGH IHYDGTPELM ADYAVLARDS GATIIGGCCG TTAEHLEKMH EALSTRPRGE RPTLEQITEA LGPFSSAADG TGDDDDGPKR ERRGRRRG // ID A6FTJ3_9RHOB Unreviewed; 299 AA. AC A6FTJ3; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 01-OCT-2014, entry version 16. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EDM70616.1}; GN ORFNames=RAZWK3B_05707 {ECO:0000313|EMBL:EDM70616.1}; OS Roseobacter sp. AzwK-3b. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseobacter. OX NCBI_TaxID=351016 {ECO:0000313|EMBL:EDM70616.1}; RN [1] {ECO:0000313|EMBL:EDM70616.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AzwK-3b {ECO:0000313|EMBL:EDM70616.1}; 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. {ECO:0000313|EMBL:EDM70616.1}. 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; ABCR01000008; EDM70616.1; -; Genomic_DNA. DR RefSeq; WP_007816530.1; NZ_ABCR01000008.1. DR EnsemblBacteria; EDM70616; EDM70616; RAZWK3B_05707. DR PATRIC; 28090458; VBIRosSp9675_2981. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDM70616.1}; KW Transferase {ECO:0000313|EMBL:EDM70616.1}. SQ SEQUENCE 299 AA; 30917 MW; 17E32E61770E324D CRC64; MTTITLLDGS IGQELVRRAG DAPTPLWSTQ TMLDHPDLVR EVHDAYFSAG ATVATTNTYA LLEDRLARVG LEARMTDLTQ TAVMAARAAR DAAGGGRVAG VVGPLIASYR PDICPAPDIA AGLYDRPVGL LADAGVDLLL LETMSSVAQA DGALRAACGR GLPVWLALTV DDADGTCLRS GEPLGAIAPL IDRFAPDALL INCSRPEAIA PALDILGTFG LPFGAYANGF TEISAGFLTD APTVDALDAR TDLGPARYAD AAMGWLSQGA TILGGCCEIG PAHIAELARR LTAAGHRLQ // ID A6FWT9_9DELT Unreviewed; 1251 AA. AC A6FWT9; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 43. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EDM81763.1}; GN ORFNames=PPSIR1_04833 {ECO:0000313|EMBL:EDM81763.1}; OS Plesiocystis pacifica SIR-1. OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Nannocystineae; Nannocystaceae; Plesiocystis. OX NCBI_TaxID=391625 {ECO:0000313|EMBL:EDM81763.1}; RN [1] {ECO:0000313|EMBL:EDM81763.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SIR-1 {ECO:0000313|EMBL:EDM81763.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EDM81763.1}. 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; ABCS01000001; EDM81763.1; -; Genomic_DNA. DR RefSeq; WP_006968938.1; NZ_ABCS01000001.1. DR ProteinModelPortal; A6FWT9; -. DR SMR; A6FWT9; 660-902. DR EnsemblBacteria; EDM81763; EDM81763; PPSIR1_04833. DR PATRIC; 29488906; VBIPlePac99763_0046. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EDM81763.1}; KW Transferase {ECO:0000313|EMBL:EDM81763.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 249 249 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 767 767 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1251 AA; 136875 MW; 64D76A3208E8BDE7 CRC64; MTDSTQTTRD RLQALMRERI VMLDGAMGTM LQGYSLGEED FRGERFADHP SPLAGNNDLL SLTRPDIVRE VHRIYFESGA DIVETNTFSS TSIAQADYNL EHLARELNVA SARLAREAAD AVATPERPRF VAGAIGPTNR TLSLSPDVED PAYRAIDFAT LRDAYAEQID GLIEGGVDLL LIETIFDTLN AKAAIMAMFE VFERRGVEIP LMISVTVTDR SGRTLSGQTI GAFWRSVAHA KPLSVGLNCA LGASAMRPYV AELAELAGCA VSCYPNAGLP NAFGEYDELP EQTAAELGEF VSSNLVNIVG GCCGTSPQHI ETIAEFVEGK APRAIPEVDG ARERNYEASH FSGLEPLTID GNTGFVMVGE RTNVTGSRKF CKLIKANDYD RALSVAVQQV RSGANILDVN MDEGMLDSEQ AMRTFLNLIA SEPEVARVPI MIDSSKWSVI EAGLECVQGK AIVNSLSLKE GEADFLAKAA VVQRHGAGLV VMAFDETGQA ESAARKLEIC SRAYTLLRER LDFEPTDIIF DPNVLAVATG IEEHDRFALE FIEACRGIKQ ACPGARISGG ISNLSFSFRG NNLVREAIHS AFLYHAIAAG LDMGIVNAGQ LEVYAEIEPE LRERVEDVLF VRRPDATDRL IELAEGLKGK KKERKIDLSW REQSVGARMA HALVHGITDF IEDDTEEARQ TLGRPLEVIE GPLMDGMKVV GDLFGAGKMF LPQVVKSARV MKRAVAYLTP YMEDEQGEGE LEPQGRVVLA TVKGDVHDIG KNIVAVVLRC NNYEVHDLGV MVPADKILES AKENRADIIG LSGLITPSLD EMVHVAKEMQ RLDFATPLLI GGATTSRQHT AVKIAPHFGE PTVHVLDASR VVNVVSDLMD PGRRETLDAR NRKEQASLRE LHEHKRKNPI TPLIRTRRQG PKLDHGVDTV ATPDFLGARV ISDVSLAEIA EYIDWTFFFT SWGLRGVFPG ILQHPKYGEA ARELYDTGRR MLDELVAKDQ LGVRAVQGFW PAHADGDDLV LWEPGAVGER ERARFHMLRQ QQVRGPKSAN REQRPVYRSL ADFVAPLSSY GESGLVDYVG AFACTTGVGA DELAARYEAA HDDYSAIMVK ALADRLAEAY AELLHERARQ SWYARGEALS KAELIKEKYR GIRPAFGYPA CPDHTEKGAL FDLLGAPAQG ITLTESYAMQ PGAAVSGIYL GHPSSRYFTV GRLGRDQIED YARRKGMSVS EAERWLAPNL GYDDGSAGAA A // ID A6G2A6_9DELT Unreviewed; 322 AA. AC A6G2A6; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Homocysteine S-methyltransferase, putative {ECO:0000313|EMBL:EDM80075.1}; GN ORFNames=PPSIR1_20649 {ECO:0000313|EMBL:EDM80075.1}; OS Plesiocystis pacifica SIR-1. OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Nannocystineae; Nannocystaceae; Plesiocystis. OX NCBI_TaxID=391625 {ECO:0000313|EMBL:EDM80075.1}; RN [1] {ECO:0000313|EMBL:EDM80075.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SIR-1 {ECO:0000313|EMBL:EDM80075.1}; 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. {ECO:0000313|EMBL:EDM80075.1}. 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; ABCS01000014; EDM80075.1; -; Genomic_DNA. DR RefSeq; WP_006970855.1; NZ_ABCS01000014.1. DR EnsemblBacteria; EDM80075; EDM80075; PPSIR1_20649. DR PATRIC; 29492857; VBIPlePac99763_1993. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDM80075.1}; KW Transferase {ECO:0000313|EMBL:EDM80075.1}. SQ SEQUENCE 322 AA; 34226 MW; 2DC7231AF775F23C CRC64; MPEPSAPLLL DGALATELRR RGFELEAPLF AARALLEAPD LLVEIHRDYA LAGAQVLSTN SFGLHAATLA RAGMAERQAE LAARSVELTF LARQLVRQSG SERTSFRVAA SVPPPPPSPS EGDAPELTRA ALRSLASALV DAGADLVLFE TFAKPEHIRA ALEVAGALEV PVWLSVVGDA RPGHRGQLLG GVPFDALAAL LREPGLRRPD ALLLNCTQID AVPRALDALL QTARAAGLEG VDLGLYPHLG RARHDGEWID RILEAEVYAG QIEAWMAARP ALSIAGACCG STPAYVEALA RRLHPDAAAR ERANVRLAHR LP // ID A6G853_9DELT Unreviewed; 325 AA. AC A6G853; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:EDM77894.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EDM77894.1}; GN Name=mmuM {ECO:0000313|EMBL:EDM77894.1}; GN ORFNames=PPSIR1_01704 {ECO:0000313|EMBL:EDM77894.1}; OS Plesiocystis pacifica SIR-1. OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Nannocystineae; Nannocystaceae; Plesiocystis. OX NCBI_TaxID=391625 {ECO:0000313|EMBL:EDM77894.1}; RN [1] {ECO:0000313|EMBL:EDM77894.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SIR-1 {ECO:0000313|EMBL:EDM77894.1}; 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. {ECO:0000313|EMBL:EDM77894.1}. 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; ABCS01000038; EDM77894.1; -; Genomic_DNA. DR RefSeq; WP_006972898.1; NZ_ABCS01000038.1. DR ProteinModelPortal; A6G853; -. DR EnsemblBacteria; EDM77894; EDM77894; PPSIR1_01704. DR PATRIC; 29497067; VBIPlePac99763_4063. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDM77894.1}; KW Transferase {ECO:0000313|EMBL:EDM77894.1}. SQ SEQUENCE 325 AA; 34454 MW; CFA96D98F769A49F CRC64; MSAEADGMDA LDRLLAREPF AVLDGGLATS LEACGCDLDD PLWSARLLLD DPEALRTVHR RWRDAGADIL ATASYQASLP GLRAKGLSEA RAKALLRESV TLTRAAADEA NAPRPLIAAS VGSYGAYLAD GSEYRGGYGL SVEALADFHR PRLLELAAAG PDLIAFETFP DAVELAALAE LLTELLTELG DTLPRAWISA SLSPPGPDRS VRLADGTPLT KALAPLTDHP KVAALGVNCV GPREVAPALE VLAACTDRPL VAYPNSGERW IDRGWSGAAL EPNKFAALAE RWFELGARLI GGCCRTNYAH IQALVKLRER IAAAT // ID A6GN35_9BURK Unreviewed; 1264 AA. AC A6GN35; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 01-APR-2015, entry version 44. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EDM84591.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EDM84591.1}; GN Name=metH {ECO:0000313|EMBL:EDM84591.1}; GN ORFNames=LMED105_03550 {ECO:0000313|EMBL:EDM84591.1}; OS Limnobacter sp. MED105. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Limnobacter. OX NCBI_TaxID=391597 {ECO:0000313|EMBL:EDM84591.1}; RN [1] {ECO:0000313|EMBL:EDM84591.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MED105 {ECO:0000313|EMBL:EDM84591.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EDM84591.1}. 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; ABCT01000002; EDM84591.1; -; Genomic_DNA. DR RefSeq; WP_008248361.1; NZ_ABCT01000002.1. DR ProteinModelPortal; A6GN35; -. DR SMR; A6GN35; 679-936. DR EnsemblBacteria; EDM84591; EDM84591; LMED105_03550. DR PATRIC; 27461967; VBILimSp111806_0781. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EDM84591.1}; KW Transferase {ECO:0000313|EMBL:EDM84591.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 263 263 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 328 328 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 329 329 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 796 796 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1264 AA; 138795 MW; B1E6B824A5EB4A1D CRC64; MNTRPASSPA EHNSLVVNGA AVEAQLRELL QKRILILDGA TGTMIQQYKL TEAQYRGERF ADFHRDIKGN NELLVLTQPA IMTEIHEQYL AAGADILETN TFGATTVAQA DYDMEHLVDE MNREAARLCK EACIKYSTPD KPRFAAGALG PTPKTASISP DVNDPGARNI TFDELVATYY QQTKGLVEGG VDLLLVETIF DTLNAKAALF AIDQYFEDSG NKLPIMISGT VTDASGRVLS GQTVEAFWNS VRHAKPITIG LNCALGASLM RPYVAELSKI CDVPICVYPN AGLPNPMSDT GFDETPEITS SLVKEFAAAG FLNVAGGCCG TTPDHIAAIA KALENQKPRT IPTVEPKCRL SGLEPLNIDD NSLFINVGER TNVTGSKAFA RMILNEQYDE ALSVARQQVE NGAQIVDVNM DEAMLDSKAA MVKFLNLMAS EPDISRVPVM IDSSKWDVIE AGLKCVQGKA VVNSISMKEG VEEFKRQAKL CKRYGAAVIV MAFDEKGQAD TYARKIEICE RAYNILVNEV GFPAEDIIFD PNIFAIATGI EEHDNYGNDF IEATGWIKKN LPHAKISGGV SNVSFSFRGN EPAREAIHTV FLYHAIKNGM TMGIVNAGMM GVYDELEPEL KARVEDIVLN RQPNLPANDP DFGKSATERM IEFAGTLKAG GKKLEENLEW RNQPVQKRLA HALVHGITNF IVEDTEECRA EIAANGGRPI NVIEGPLMDG MNVVGDLFGA GKMFLPQVVK SARVMKQAVA HLIPYIEEEK KQLVAAGGDA KAKGKILIAT VKGDVHDIGK NIVTVVLQCN NFEVENMGVM VPAEQILAKA KEINADIIGL SGLITPSLEE MAYVASEMQR DPYFRDRGIP LLIGGATTSR VHTAVKIAPH YEGPTVYVSD ASRSVGVASN LLSDESADTF KADLKTEYER VREQHANKKA QPLISIEAAR ANKQKIDWAN YTPPKPKFIG KRYFKNYDLA DIAQYIDWTP FFQTWDLHGG YPRVLEDELV GEAARKVFED GQAMLKKCIE GRWLQANAAV AFYPANTVSD DHIEVYADES RSQVLFTYSP LRQQGEKREG IANKSLADFI APKGAGADYI GMFAVTAGLG VEKKEKEFQA AHDDYSSIMF KAIADRMAEA FAECLHQRVR KDLWGYVADE TLSNEELIAE KYQGIRPAPG YPACPEHTIK RNMFEVMQCE EIGMTLTESL AMNPAASVSG FYFANPESDY FNVGPVGQDQ FKALLDYSGR SEEDLRRALS TNLT // ID A6L3C1_BACV8 Unreviewed; 917 AA. AC A6L3C1; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 60. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|EMBL:ABR40185.1}; GN OrderedLocusNames=BVU_2528 {ECO:0000313|EMBL:ABR40185.1}; OS Bacteroides vulgatus (strain ATCC 8482 / DSM 1447 / NCTC 11154). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=435590 {ECO:0000313|EMBL:ABR40185.1, ECO:0000313|Proteomes:UP000002861}; RN [1] {ECO:0000313|EMBL:ABR40185.1, ECO:0000313|Proteomes:UP000002861} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8482 / DSM 1447 / NCTC 11154 RC {ECO:0000313|Proteomes:UP000002861}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000139; ABR40185.1; -; Genomic_DNA. DR RefSeq; WP_005847467.1; NC_009614.1. DR RefSeq; YP_001299807.1; NC_009614.1. DR ProteinModelPortal; A6L3C1; -. DR SMR; A6L3C1; 652-894. DR STRING; 435590.BVU_2528; -. DR EnsemblBacteria; ABR40185; ABR40185; BVU_2528. DR GeneID; 5303492; -. DR KEGG; bvu:BVU_2528; -. DR PATRIC; 21070008; VBIBacVul85104_2609. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; BVUL435590:GH96-2523-MONOMER; -. DR Proteomes; UP000002861; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002861}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABR40185.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002861}; KW Transferase {ECO:0000313|EMBL:ABR40185.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 243 243 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 917 AA; 100856 MW; E91AC6CE0F06EA5A CRC64; MATLKQLIDE RVLILDGAMG TMIQRYNLSE QDFRGERFAE MPGQMKGNND LLCLTRPDVI KDIHHKYLEA GADIIETNTF NAQRVSMADY HMQDLCREIN LAAAGLAREM ADEYTAKTPH KPRFVAGSVG PTNKTCSMSP DVNNPALRAL TYDELAAAYQ EQMEALLEGG VDALLIETIF DSLNAKAAIY AAETAMKKIG REVPLMLSVT VSDIAGRTLS GQTLDAFLAS VQHAPIFSIG LNCSFGAKQL KPFLEGLAAR APYYISAYPN AGLPNSLGQY DQTPEEMASE VKEYIDEGLV NIIGGCCGTT EEYIAKYQEL IVSGSAWVSP HIPATTPERL WLSGLELLEQ TPEMNFINVG ERCNVAGSRK FLRLINEKKY EEALSIARKQ VEDGALVIDV NMDDGLLDAR EEMTTFLNLV MSEPDIARVP VMIDSSKWEV IEAGLKCLQG KSIVNSISLK EGEEIFIEHA RLIKKLGAAV VVMAFDEKGQ ADTFERKIEV CARAYKILTE QVDFNPHDII FDPNVLAVAT GIEEHDNYAV DFIKATGWIK KNLPGAHVSG GVSNLSFSFR GNNYIREAMH AVFLYHAIRQ GMDMGIVNPA ASVLYTDIPA DVLERIEDVV LNRRPDAAER LIETAEALKN TATGTEAVKQ DVWREEPMVE KRLQYALIKG IGDHLEEDLA EAVKLYPKAV DIIEGPLMEG MNKVGELFGA GKMFLPQVVK TARTMKKAVA ILQPLIEADK QEGVRSAGKV LMATVKGDVH DIGKNIVSVV MACNNYEIID LGVMVPAEMI VRKAIEEKVD IIGLSGLITP SLEEMAHVAV ELKRAGLDIP IMIGGATTSK LHTALKIAPV YGGPVIHMKD ASQNALVAAR LLNPESSFEF VERLNKEYED LRLKNSAKQV KTVSLEEAQK NKLNLWS // ID A6L929_PARD8 Unreviewed; 1230 AA. AC A6L929; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 61. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:ABR42193.1}; GN OrderedLocusNames=BDI_0415 {ECO:0000313|EMBL:ABR42193.1}; OS Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / NCTC OS 11152). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Parabacteroides. OX NCBI_TaxID=435591 {ECO:0000313|EMBL:ABR42193.1, ECO:0000313|Proteomes:UP000000566}; RN [1] {ECO:0000313|EMBL:ABR42193.1, ECO:0000313|Proteomes:UP000000566} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8503 / DSM 20701 / NCTC 11152 RC {ECO:0000313|Proteomes:UP000000566}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000140; ABR42193.1; -; Genomic_DNA. DR RefSeq; WP_008780887.1; NC_009615.1. DR RefSeq; YP_001301815.1; NC_009615.1. DR ProteinModelPortal; A6L929; -. DR SMR; A6L929; 650-895. DR STRING; 435591.BDI_0415; -. DR EnsemblBacteria; ABR42193; ABR42193; BDI_0415. DR GeneID; 5305570; -. DR KEGG; pdi:BDI_0415; -. DR PATRIC; 22843980; VBIParDis29947_0404. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PDIS435591:GCNH-415-MONOMER; -. DR Proteomes; UP000000566; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000566}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABR42193.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000566}; KW Transferase {ECO:0000313|EMBL:ABR42193.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1230 AA; 136496 MW; 29C6AB3EDEF7E578 CRC64; MNKERFLRLL NERILILDGG MGTMIQSFKL NEQDYRGERF ADFPGQLKGN NDLLCITRPD VIQSIHRQYL DAGADIFATN TFNANAISMA DYAMEAYVRE INLAAGRLSR EVADTYMAEH PDRTIFVAGS IGPTNKTASM SPDVSDPAYR AVTYKDLYNA YKEQVEGLVD GGVDIILFET TFDTLNVKAG LEAAEVVLKE KEKDLPIMLS LTLSAQGGRT FSGQTLLAFL ASIQHTHIVS VGLNCSFGAA DMKPYLQELA KYAPYYISAY PNAGLPNSFG TYDETPDKMA QHVKPFVEEG LVNIIGGCCG TTPAHISRYP ELVKGAKPHI PALKPDCLWL SGLELLEVKP ENNFVNVGER CNVAGSRKFL RLIKEGSYEE ALTIARKQVE DGAQVIDINM DDGMLDAVKE MKTFLNLIAS EPDIARVPVM IDSSKWEVIE EGLMCVQGKS IVNSISLKEG EEVFLKHAAR IKQLGAAAVV MAFDEKGQAD TYERKIEICE RAYRLLIEKI DFNPQDIIFD PNVLAIATGM EEHNGYGLAF IRAVEWIKKN LPGAKVSGGV SNLSFSFRGN NHVREAMHSV FLYHAIGKGM DMGIVNPSTS VLYEDIEPEF RTLLEDVILA RRPEAAEELI TYAQNLHVQA SGETPEKHEA WRELSLKERL EHALIKGIGD YLEDDLQEAL RTYSHAVDII DGPLMSGMNK VGELFGAGKM FLPQVVKTAR TMKKAVAILQ PAIESEKKAS GSAKAGKVIF ATVKGDVHDI GKNIVSIVLS CNNYEVIDLG VMVPADVIIK KAIEEKPDLV CLSGLITPSL EEMAHVADEM QKAGLTIPMM VGGATTSKLH TAVKIAPHYD YPVIHVLDAS QNPLIAAKLL NPDTRDAYIR ELEQEQEALR ASLGQKKETL ASLSEARKHP IEIDWTGYTP VVPARMGVHV IPYIPLEEVI PYIHWTFFFS AWKLNGRFSE ISQIHGCDSC RASWLAGFPE KDRAKATEAM QLYKDAVRLL DRLVNMKVEY CKAIYGFFSA NSEGDTIRMG DIALPLLRQQ VKKEENIYKC LSDYVIPVSE ERTDYVGAFV VTAGAGADCL KDKFEEEGDT YNSMLLQTLT DRLAEATAEY LHEKVRKEYW GYAKDESLSI PDLYKVKYQG IRPAIGYPSL PDQLLNFTLD GLLDMSRIGV SLTENGAMYP TASVSGIYIA HPSSQYFMIG SIDEEQMRDY ASRRNLTEEQ ARKLLSKNIG // ID A6LKZ2_THEM4 Unreviewed; 781 AA. AC A6LKZ2; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 55. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABR30593.1}; GN OrderedLocusNames=Tmel_0729 {ECO:0000313|EMBL:ABR30593.1}; OS Thermosipho melanesiensis (strain BI429 / DSM 12029). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermosipho. OX NCBI_TaxID=391009 {ECO:0000313|EMBL:ABR30593.1, ECO:0000313|Proteomes:UP000001110}; RN [1] {ECO:0000313|EMBL:ABR30593.1, ECO:0000313|Proteomes:UP000001110} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BI429 / DSM 12029 {ECO:0000313|Proteomes:UP000001110}; 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., Mikhailova N., Nelson K., Gogarten J.P., Noll K., RA Richardson P.; RT "Complete sequence of Thermosipho melanesiensis BI429."; 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; CP000716; ABR30593.1; -; Genomic_DNA. DR RefSeq; WP_012056954.1; NC_009616.1. DR RefSeq; YP_001305978.1; NC_009616.1. DR ProteinModelPortal; A6LKZ2; -. DR STRING; 391009.Tmel_0729; -. DR EnsemblBacteria; ABR30593; ABR30593; Tmel_0729. DR KEGG; tme:Tmel_0729; -. DR PATRIC; 23922661; VBITheMel19269_0758. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; TMEL391009:GHM1-775-MONOMER; -. DR Proteomes; UP000001110; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001110}; KW Methyltransferase {ECO:0000313|EMBL:ABR30593.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001110}; KW Transferase {ECO:0000313|EMBL:ABR30593.1}. SQ SEQUENCE 781 AA; 87740 MW; 67FD635A5223DEC5 CRC64; MYGRMVVILE RKEFLELLNE RIYFLDGAYG TEFFKLGFKE VIETLNVTNS EMVYALQKAY VDAGVDFLLT NTFSANRLKL SSLKVKYNLK DINYNAVKIA KKARKDKKVY ILGDISSTGY LISPLGELTF DEAYEVFKEQ GEILLNSGID GFILETMSDL KELKAAILAL RDLSKDVPII VQMTFDEDGV AVTGTSVEIF STLMNDLDVD VVGINCTLEP EKLLPVFKQL SNYSRKPISV EPNAGKPKLL RDGSIVYNTS PEKFALYMED FVEFGANIVG GCCGTSPEHI RLMVEFLKEK KPKKREIVKE EFVSSRTKLK KMKPFLIIGE RINAAGKKKF QQKIRERNYN KIVELAILQE KEGAHVLDLN LGIEKLLDKT HFSQVVNTLD KISSLPLSLD IQEFEFMEMA LKEYVGRPII NSSTAKRENL DKAIYLLKRY GGILILLTMK DKIPESAKER FDIALEAIRY LEKHDIEKER VIVDPLVLPL GAKKDPAVTI KTIELLSKEG INTSIGLSNL SFGMPNREAL NSSFLALCID KGLTAAILNT SEKCTMNAVF GSLTLKGVDF EKKEIIRNEP MIEMILNKKE DELKREIEKL LEEYTPLQIS QDILSKKMEY IGELYSKGEI YLPQLILAAE TVTPIFEYLN SLIESNAREK LGTVVLATVE GDVHDIGKRI VGTVLKSSGI NVIDLGKDVP AKEILKAVKE YKPDIVGLSA MMTTTIGRIK EVKDLFVDNN VDIPIISGGA SMNKEIADNF GVYYAKNASQ ALKLVKKILK R // ID A6LTA0_CLOB8 Unreviewed; 801 AA. AC A6LTA0; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 58. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABR33580.1}; GN OrderedLocusNames=Cbei_1402 {ECO:0000313|EMBL:ABR33580.1}; OS Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium OS acetobutylicum). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=290402 {ECO:0000313|EMBL:ABR33580.1, ECO:0000313|Proteomes:UP000000565}; RN [1] {ECO:0000313|EMBL:ABR33580.1, ECO:0000313|Proteomes:UP000000565} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51743 / NCIMB 8052 {ECO:0000313|Proteomes:UP000000565}; 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; ABR33580.1; -; Genomic_DNA. DR RefSeq; WP_011968734.1; NC_009617.1. DR RefSeq; YP_001308536.1; NC_009617.1. DR ProteinModelPortal; A6LTA0; -. DR STRING; 290402.Cbei_1402; -. DR EnsemblBacteria; ABR33580; ABR33580; Cbei_1402. DR KEGG; cbe:Cbei_1402; -. DR PATRIC; 19346794; VBICloBei69853_1443. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EINIESA; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CBEI290402:GHL5-1474-MONOMER; -. DR Proteomes; UP000000565; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000565}; KW Methyltransferase {ECO:0000313|EMBL:ABR33580.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000565}; KW Transferase {ECO:0000313|EMBL:ABR33580.1}. SQ SEQUENCE 801 AA; 88332 MW; DA7418AC2CD467E9 CRC64; MGLREYIKNN ILIFDGAMGT MLQKKGLKLG ENPEILNLKE PYIIEEIHRE YISSGANVIT TNTFGANELK LKLCGLVVEE AIDAAVNIAK KTKGNSETYI ALDVGPIGEL LETMGTLSFD RAYEIFKRQI IQGVKSGVDI ILIETMTDLY ELKAAVLAAK ENSSLPIFCT MTFEENLRTF TGCTPEAMVL VLEGLGVDAL GVNCSLGPKQ LKPIVEKICS LSHIPVMVQP NAGLPTLSIG NETKYDVTKE EFADTLCGFI DLGVRVIGGC CGTSPEYIEE LYKITRNKKL VFMEKEYYSA VCTPSKVVRI DGVRIIGERI NPTGKKIFKE ALKNGDLDYI LNQAVSQIEV GAHILDVNVG LPEIDEADMM HKVIREIQGI MDTPLQIDSS DHKAIETGLR YYNGKPILNS VNGEDEVLDR ILPIVKKYGA SVVGLTLDER GIPAKAEERF EIAEKIISKA AEYGIRKEDV FIDCLVLTVS AQQKEVQETL KAVRMVKEKL GVKTVLGVSN ISFGLPNREL INETFLVLAL ANGLDLPIIN PNVNGMTRVI DSYNVLYNYD KGAESYINNY ANVELSREVT IKGNGAAKIN SNINTVHDLK YIVVKGLKEE AKQATVELLK EKKELEIVNE YLIPALDMVG EKYEKGELFL PQLIQAAETV KNSFTILKEE ISRTNSQTIS KGKIIVATVK GDIHDIGKNI VKVILENYGY EMIDLGKDVP IKTVVEEAKK HNASLIGLSA LMTTTLKSME ETIKALREDG YNGKIFVGGA VLTKDTAERI GADFYAKDAK ESVEIARRVL S // ID A6LUG9_CLOB8 Unreviewed; 593 AA. AC A6LUG9; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 53. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=Cbei_1828 {ECO:0000313|EMBL:ABR33999.1}; OS Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium OS acetobutylicum). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=290402 {ECO:0000313|EMBL:ABR33999.1, ECO:0000313|Proteomes:UP000000565}; RN [1] {ECO:0000313|EMBL:ABR33999.1, ECO:0000313|Proteomes:UP000000565} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51743 / NCIMB 8052 {ECO:0000313|Proteomes:UP000000565}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ABR33999.1; -; Genomic_DNA. DR RefSeq; WP_011969151.1; NC_009617.1. DR RefSeq; YP_001308955.1; NC_009617.1. DR ProteinModelPortal; A6LUG9; -. DR STRING; 290402.Cbei_1828; -. DR EnsemblBacteria; ABR33999; ABR33999; Cbei_1828. DR KEGG; cbe:Cbei_1828; -. DR PATRIC; 19347694; VBICloBei69853_1886. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; CBEI290402:GHL5-1907-MONOMER; -. DR Proteomes; UP000000565; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000565}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ABR33999.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000000565}; KW Transferase {ECO:0000313|EMBL:ABR33999.1}. SQ SEQUENCE 593 AA; 66495 MW; B753C80DB09F85B2 CRC64; MIKELLKNDI LICDGAMGTY YSEVTGNDVS YCEFGNLNDK ETIKRIHKEY IEAGAKLIRT NTFSANTYDL GVSLETLMDI IKSGINLAKE VTRNTSVLIG ASIGPIKTDN LDEFSNEVLE EYKYIVDCFL KNGIDIFIFE TFSNYNCLKK ISEYIKYKNI DSFILTQFAV KPDGFTRDGL SAAKLIKEVR NTKYIDAFGF NCGSGPAHIL EMVKKINIEN EIVSVLPNAG YPEIIHERTV YPNNPVYFAK KVNEIRSFGV SIIGGCCGTN PSYIKQLTQI VNENSKVVNA NAKAEPKVKS FEKKAKNTFK DKLENGEFVV AIELSAPIDT DISRIIDGAK ICKENNIDLV TVPDSPMSKV RADSTIISSK IKREIGIEAM PHVCCRDKNT NAIRSSLIGS HIENIRNILA ITGDPISDAS KVETKSVFNL NSFRLIELIE SMNEEIFKED SIYVGGALNL NVLNKEVEYN RMMKKIEKGA KFFLTQPIYD DNAIEFLKMI KERTNVKILA GLLPVVSYRN AMFLNNELPG VTIPDKYVQM FSENMSKEEA QEIGVKITVE IGKKLKGIAD GLYFITPFNR VNMLIEIIKQ INA // ID A6LWW4_CLOB8 Unreviewed; 310 AA. AC A6LWW4; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 38. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABR34844.1}; GN OrderedLocusNames=Cbei_2691 {ECO:0000313|EMBL:ABR34844.1}; OS Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium OS acetobutylicum). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=290402 {ECO:0000313|EMBL:ABR34844.1, ECO:0000313|Proteomes:UP000000565}; RN [1] {ECO:0000313|EMBL:ABR34844.1, ECO:0000313|Proteomes:UP000000565} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51743 / NCIMB 8052 {ECO:0000313|Proteomes:UP000000565}; 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; ABR34844.1; -; Genomic_DNA. DR RefSeq; WP_012058899.1; NC_009617.1. DR RefSeq; YP_001309800.1; NC_009617.1. DR STRING; 290402.Cbei_2691; -. DR EnsemblBacteria; ABR34844; ABR34844; Cbei_2691. DR KEGG; cbe:Cbei_2691; -. DR PATRIC; 19349524; VBICloBei69853_2792. DR eggNOG; COG2040; -. DR HOGENOM; HOG000179103; -. DR OMA; CCGTDHR; -. DR OrthoDB; EOG6R5C46; -. DR BioCyc; CBEI290402:GHL5-2779-MONOMER; -. DR Proteomes; UP000000565; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000565}; KW Methyltransferase {ECO:0000313|EMBL:ABR34844.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000565}; KW Transferase {ECO:0000313|EMBL:ABR34844.1}. SQ SEQUENCE 310 AA; 34899 MW; 1078BA9B2E71D2E7 CRC64; MDFQTCFDKS SSILMEGALG ERLKREFNII FDDKVAMAGL VYDSDSRQAM CSIYKEYLKT AEKYKFPFIV TTPTRRANKE RVLESEFTEK IIEDNVRFLQ GIKSNAKIDM FVGGLMGCKG DAYKACDVLS IDDAKEFHSW QANLFKESGV DFLFAGIMPA LPEAIGMAKA MESTELPYII SFMIRDDGRL IDGTTINDAI LHIDNATIKK PICYMVNCVH PAILKKSLSY SFNKTKLVKE RFHGIQANTS PLSPEELDNS SDLKFSDGIS LADDMMELYK YFVPKILGGC CGTDNTHIEE IAKRLKGRKV // ID A6LY07_CLOB8 Unreviewed; 1213 AA. AC A6LY07; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 01-APR-2015, entry version 65. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABR35237.1}; GN OrderedLocusNames=Cbei_3100 {ECO:0000313|EMBL:ABR35237.1}; OS Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium OS acetobutylicum). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=290402 {ECO:0000313|EMBL:ABR35237.1, ECO:0000313|Proteomes:UP000000565}; RN [1] {ECO:0000313|EMBL:ABR35237.1, ECO:0000313|Proteomes:UP000000565} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51743 / NCIMB 8052 {ECO:0000313|Proteomes:UP000000565}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000721; ABR35237.1; -; Genomic_DNA. DR RefSeq; WP_012059289.1; NC_009617.1. DR RefSeq; YP_001310193.1; NC_009617.1. DR ProteinModelPortal; A6LY07; -. DR SMR; A6LY07; 647-886. DR STRING; 290402.Cbei_3100; -. DR EnsemblBacteria; ABR35237; ABR35237; Cbei_3100. DR KEGG; cbe:Cbei_3100; -. DR PATRIC; 19350390; VBICloBei69853_3217. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CBEI290402:GHL5-3195-MONOMER; -. DR Proteomes; UP000000565; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000565}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000565}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 242 242 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 754 754 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1213 AA; 135427 MW; DEE370E31E5BE4CD CRC64; MNLQIKELLE KRILVLDGAM GTCIQNYKLE EKDYRGNLNI SCNQKGNNDI LNLTNPNIIR EIHEAYLESG ADIIETNTFN STSISQKDYE MEDKIYELNF EGAKLAKEAA DKFTAENPDK PRFVAGSLGP TNKTASLSPD VENPGYRNIS FDELAEAYKE QVLGLIDGGV DLILIETIFD ALNARAALMG AKQGFLEKGK DLPVIISGTI ADKSGRILSG QTLEAFANTM VDESIIAIGL NCSFGAKDLI PFVKYLSRTQ NRYISVYPNA GLPNSFGEYD EKPEETAALI KSLAEDGCLN IVGGCCGTTP DHIKAVSEAI KDISPRKIPD IETETVYCGL EALRANKENN FINIGERTNV AGSAKFARLI REKNYEEALS IAKDQVENGA QIVDINFDDA LLDAKEEMDK FLKLLASEPE ISKVPVMIDS SKFEVLVTGL KAIQGKPIVN SISLKVGEEE FKRQASIIRD FGAAVVVMAF DENGQADSYE KKISICKRAY DILVNEVNFP PQNIVFDPNI LTIATGIEEH NNYAVDFINA TKWIKENLPY AKVSGGVSNL SFAFRGNNVI REAMHSVFLY HAIKNGMDMG IVNPGMIQIY DEIDKGLLEK VEAVIFNKSE NAADELLEFA ANFNKVDNKL EENKEAWRNE NVKERLKTAL VKGIDKYIKE DVEEVRAEYS KSLEVIEGPL MDGMNEVGKL FGDGKMFLPQ VVKSARVMKK AVEVLRPYLE EEKSSSGSIS AGKVVFATVK GDVHDIGKNI VSVVLSCNNF EVIDLGVMVP TEIILETAKK ENADIIALSG LITPSLEEMS NVAEEMEKQG FKIPLMVGGA TTSKAHTAIK IAPKYSGGVI HTTDASKAVE AAKLLLNKDK KAEYLNKIES EYETLRETFN KVPRKFVTLD YARENNFKKE WDKEQIEKPK MLGIKKFIDF PIGKLRKYID WSFFFIAWDM GMTYPQILED AKYGEEAKKL LADAEKMLDK MESENILKAN AAFGLFEANS VGDNIEVYND SEMINFNLLR QQEVKKDNTY MCLSDFIAPK DTGIKDYIGA FITTGGIGAK EYADKLKASG DDYGATMVIL LADRLAEAFA EYVHEKVRKE YWAYSPDENL FIEEIFKGKY RGIRPAIGYP SLRDHSEKVK LFNLLDKEGE LNVKLTESYM MSPTASTCGL YFGNKDAKYF DINKIHQDQF NDYAQRNGRD KGELKKLMYT IID // ID A6MZX1_ORYSI Unreviewed; 119 AA. AC A6MZX1; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 29-OCT-2014, entry version 27. DE SubName: Full=Homocysteine s-methyltransferase 3 {ECO:0000313|EMBL:ABR25541.1}; DE Flags: Fragment; 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 {ECO:0000313|EMBL:ABR25541.1}; RN [1] {ECO:0000313|EMBL:ABR25541.1} RP NUCLEOTIDE SEQUENCE. RA Kumari S., Panjabi V., Singla-Pareek S.L., Sopory S.K., Pareek A.; RT "A comparative transcriptome map of early and late salinity stress RT responses in contrasting genotypes of Oryza sativa L."; 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; EF575953; ABR25541.1; -; mRNA. DR Gramene; A6MZX1; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Methyltransferase {ECO:0000313|EMBL:ABR25541.1}; KW Transferase {ECO:0000313|EMBL:ABR25541.1}. FT NON_TER 1 1 {ECO:0000313|EMBL:ABR25541.1}. SQ SEQUENCE 119 AA; 12845 MW; DE60BD0A7AC2635A CRC64; ARGSLIECAT IANGCSKVGA VGINCTPPRF IHGLILSIRK VTDKPILIYP NSGERYDAEK KEWVESTGVS DGDFVSYVNE WCKDGAVLIG GCCRTTPNTI KAISRSLNQR HSSLHLPVA // ID A6NZH5_9FIRM Unreviewed; 799 AA. AC A6NZH5; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 27-MAY-2015, entry version 42. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EDM98824.1}; GN ORFNames=BACCAP_03626 {ECO:0000313|EMBL:EDM98824.1}; OS Pseudoflavonifractor capillosus ATCC 29799. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Pseudoflavonifractor. OX NCBI_TaxID=411467 {ECO:0000313|EMBL:EDM98824.1}; RN [1] {ECO:0000313|EMBL:EDM98824.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29799 {ECO:0000313|EMBL:EDM98824.1}; 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 (APR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EDM98824.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29799 {ECO:0000313|EMBL:EDM98824.1}; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Pseudoflavonifractor capillosus ATCC RT 29799."; 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. {ECO:0000313|EMBL:EDM98824.1}. 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; AAXG02000032; EDM98824.1; -; Genomic_DNA. DR RefSeq; WP_006574130.1; NZ_AAXG02000032.1. DR ProteinModelPortal; A6NZH5; -. DR EnsemblBacteria; EDM98824; EDM98824; BACCAP_03626. DR PATRIC; 31031907; VBIBacCap83047_2759. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDM98824.1}; KW Transferase {ECO:0000313|EMBL:EDM98824.1}. SQ SEQUENCE 799 AA; 84775 MW; 54998EA9850C9F52 CRC64; MSFLEKLGRE RLFFDGGTGT LLQAQGLKGG ELPETWNLRY PERIQAVHKA YLEAGSHVIC TNTFGANALN FPDGGEWDLD ELVRAAVDNA KKARAEAGRE NDAYIALDLG PTGRLLRPMG DLDFEDAVAL FARVVRVGAQ AGADLVLIET MSDGYEAKAA VLAAKENSDL PVVVTTVYDE NGKMLTGGTI ASTVALLEGL RVDALGVNCG MGPEQMLPLA EELVKLASVP VVVNPNAGLP RREGDKTVFD VDPERFAAVM ERIAKLGVWG LGGCCGTTPD HIRALTAACR NIPVTPPERK RRTVVSSFSQ AVEIGPKPVI IGERINPTGK KRFKEALRGH DLEYILNEGF AQEEAGAHIL DVNVGLPEID EPAMLEEAVC ALQSVIPLPL QIDTSDTEAM ARAMRRYNGK PMINSVSGKA ESMAAVFPLV RKYGGVVVGL ALDEGGIPET AEGRLAVARK IYNTAAEYGI PSEDIVIDGL TLTVSSEPKA AVVTLETLRR VRDELGGHTI LGVSNVSFGL PRRDIINANF FAMALEAGLS CAIINPLAEG MMGAWRSYCA LAGLDNQCGG YIGAYSGQTA APAVPASGTE LSLEECVTRG MQEGAAQSAR TALDKGAQPL ELVNSALIPA LDKVGQGFEK KTLFLPQLLM SAEAAKAAFE VVKAAMASEP QEKQGKVVLA TVKGDIHDIG KNIVKVLLEN YGFEVIDLGK DVAPEKIVAA AAAPDIQLVG LSALMTTTVV SMEETIKALR ESGSGVKVVV GGAVLTQEYA DSIDADCYAR DAMATVRYAK EVYGTEEKP // ID A6P195_9FIRM Unreviewed; 386 AA. AC A6P195; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDM97787.1}; GN ORFNames=BACCAP_04262 {ECO:0000313|EMBL:EDM97787.1}; OS Pseudoflavonifractor capillosus ATCC 29799. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Pseudoflavonifractor. OX NCBI_TaxID=411467 {ECO:0000313|EMBL:EDM97787.1}; RN [1] {ECO:0000313|EMBL:EDM97787.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29799 {ECO:0000313|EMBL:EDM97787.1}; 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 (APR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EDM97787.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29799 {ECO:0000313|EMBL:EDM97787.1}; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Pseudoflavonifractor capillosus ATCC RT 29799."; 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. {ECO:0000313|EMBL:EDM97787.1}. 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; AAXG02000047; EDM97787.1; -; Genomic_DNA. DR RefSeq; WP_006574738.1; NZ_AAXG02000047.1. DR ProteinModelPortal; A6P195; -. DR EnsemblBacteria; EDM97787; EDM97787; BACCAP_04262. DR PATRIC; 31032844; VBIBacCap83047_3203. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 386 AA; 41604 MW; 3D39A258D1B93818 CRC64; MDIPLPLPLL IGGAEDDGNR ESTWLPGHRE KLSLIQRSWV TAGCNAVVAP TFRGNRFRLP RRDGEEDVRG YNRTLVELTR RSAGERVLVA GGIGPAGQEL EPFGDVTFEE LVTAYAEQAA ALAEAGVDLF LLGEGMTMAE ERAAMLAVRQ ASSRPVVVLA RCDEEGRTES GTDVLAALIV MQGMGAAAFG LSTGEGAEVL LEQLQRLTPY AAIPLAAVVS EPEQELQDLA EAGVKLFACG GALSGDGPSL LARDLALVDF SRFVPPEHDP DVIPCASEKE ARFITPDVDV GETIECTSDL MEEILEAEET CPQGSLKIAI LEEDDVAIFA ENQYAVRDAL CLWSDVPELL EQALRVYQGR AFWDGTGDLE PEFLAEMAKK YGLVLL // ID A6Q2F4_NITSB Unreviewed; 1148 AA. AC A6Q2F4; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 27-MAY-2015, entry version 62. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:BAF69663.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:BAF69663.1}; GN Name=metH {ECO:0000313|EMBL:BAF69663.1}; GN OrderedLocusNames=NIS_0549 {ECO:0000313|EMBL:BAF69663.1}; OS Nitratiruptor sp. (strain SB155-2). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Nitratiruptor. OX NCBI_TaxID=387092 {ECO:0000313|EMBL:BAF69663.1, ECO:0000313|Proteomes:UP000001118}; RN [1] {ECO:0000313|EMBL:BAF69663.1, ECO:0000313|Proteomes:UP000001118} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SB155-2 {ECO:0000313|EMBL:BAF69663.1, RC ECO:0000313|Proteomes:UP000001118}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP009178; BAF69663.1; -; Genomic_DNA. DR RefSeq; WP_012081926.1; NC_009662.1. DR RefSeq; YP_001356020.1; NC_009662.1. DR ProteinModelPortal; A6Q2F4; -. DR STRING; 387092.NIS_0549; -. DR EnsemblBacteria; BAF69663; BAF69663; NIS_0549. DR KEGG; nis:NIS_0549; -. DR PATRIC; 22683138; VBINitSp82229_0583. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; NSP387092:GHA5-577-MONOMER; -. DR Proteomes; UP000001118; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001118}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAF69663.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001118}; KW Transferase {ECO:0000313|EMBL:BAF69663.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 218 218 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 722 722 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1148 AA; 128009 MW; 4DD42575DB720FE9 CRC64; MIKRLLRERI LIIDGAMGTQ LQAKANEISA DVWEGKEGCN ELLNRTAPKV IKSIHEAYAK VGADIIKTNT FGSMPWVLDE YDLASEAYDL TKRGCELVKE VCETYSTPEK PRFVACSLGP GTKLPSLGHI DYDAMYVGYS EAARGAKDGG ADIFLLETCQ DPLQIKAAMH ACQDTAPEIP IMVSVTIEQN GTMLIGTDAA TIATILEPFD IISLGFNCGT GPDMVEKHVR VLSEVWDRPI SVHANAGLPQ NRGGYTYYPM GPKEFTELEA KFTSIDGVAL LGGCCGTTPQ HIKALVDAVE GKKPLPPKGK QPRSIASLFE SRTLMQDPAP FLMGERSNAT GSKAFRELLL KSDYEGTLSV AQQQVRSGAH GIDVSVGFAG RDETKDMHEV IKLYNEKISI PLMPDSTQVP AIEVALKHIG GRPIINSANL EDGVEKFDKI CSLAKRYGAA LVLLAIDEEG MAKTKEKKLA VAERMYERAV NKHGLNPGDL VFDLLTFTVG SGDEEYQTAA IETIEAIREL RRRHPEVGAV LGVSNISFGL DKHAREYLNS VFLHHCVEAG LTMAIVNVKN LIPYHKISEE DRKVCEDLLF NRRENGDPLF AFIEHFSKAD KKEAASDDEL SKLPLEEQIH KLLIDGDKER MMPLLEKAKD EIDPEKIINE ILIGAMKEVG DLFGSGQMQL PFVLQSAEVM KAAVDYLNQF LPKTDKQSQT TLILGTVKGD VHDVGKNLVD ILLTNNGFKV INLGIKVELE EFIKAYKEHN AQAIGMSGLL VKSTQVMLEN LKEMKQKGID APILLGGAAL TKKFVDEFCR PSYDGPIFYC RDAFDGIVAM SRIEEGNFDT RLGSDSDEEE IVEIKPKEEV KIDPANIILP KPAHVPTPPF WGRKTLEIDP DIAYEWINKR LLFKQRWGYK SKGLSKEEYQ KQLDEKVIPA FNRLRSELGD IFEPTILYGY WPARAVDNEL YVFGEEFGWQ RDEDANREPI ENIIGDAIEI FTFPRQSKPP HRCIADYFHD ERMDVSAFTC VSAGNRFSEY EGELFKAGKY HEYHLVHGLS VELAEALAEI AHKQIRIELG ILRNEKPDLG DVKMVGYQGA RYSPGYPACP DLELNRHIFN LLQPEEFGIT LSETFQIHPE QSTCAIVVHH PEAKYFNI // ID A6QBA6_SULNB Unreviewed; 1169 AA. AC A6QBA6; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 27-MAY-2015, entry version 63. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:BAF72765.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:BAF72765.1}; GN Name=metH {ECO:0000313|EMBL:BAF72765.1}; GN OrderedLocusNames=SUN_1818 {ECO:0000313|EMBL:BAF72765.1}; OS Sulfurovum sp. (strain NBC37-1). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Sulfurovum. OX NCBI_TaxID=387093 {ECO:0000313|EMBL:BAF72765.1, ECO:0000313|Proteomes:UP000006378}; RN [1] {ECO:0000313|EMBL:BAF72765.1, ECO:0000313|Proteomes:UP000006378} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBC37-1 {ECO:0000313|EMBL:BAF72765.1, RC ECO:0000313|Proteomes:UP000006378}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP009179; BAF72765.1; -; Genomic_DNA. DR RefSeq; WP_012083578.1; NC_009663.1. DR RefSeq; YP_001359122.1; NC_009663.1. DR ProteinModelPortal; A6QBA6; -. DR STRING; 387093.SUN_1818; -. DR EnsemblBacteria; BAF72765; BAF72765; SUN_1818. DR KEGG; sun:SUN_1818; -. DR PATRIC; 23776665; VBISulSp49917_1845. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SSP387093:GH25-1849-MONOMER; -. DR Proteomes; UP000006378; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006378}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAF72765.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006378}; KW Transferase {ECO:0000313|EMBL:BAF72765.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 230 230 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 296 296 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 297 297 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 732 732 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1169 AA; 130757 MW; 6D8D3F3398E1A968 CRC64; MSITETIKSL LEKRILVIDG AMGTQIQDLD VPKEAWIDHS GKEQEGCNEL LNDTAADLIK RIHKRYAMAG ADLIKTNTFG TMPWVLDEYQ MGERAYELSK KGAELVKEIC AEYSTKISPK FVLGSIGPGT KLPSLGHIHY DEMYEGYKTV ALGLIDGGCD VFLLETCQDP LQIKAALHAC QDANKERGVE LPVMVSVTIE LSGSMLIGTD ATTIVTIMEP FDILSLGFNC GTGPDQVKKH LKTLSELCSI PISVHANAGL PQNRGGYTYY PMGPDEFTQK QLEFTEFDGV SFLGGCCGTT PQHIQALKKA VETIKPKKPT GSIEPSIASL FTTTELFQKP APLLIGERSN ATGSKAFREL IIAGDYEGTL TVGQAQVRDG AHCLDVNVEF AGRNGATDMS AVMELYNQKI PLPLMPDATR VGTMEAALKC IGGKPIINSV NLEDGEGKLD AICQLAKKYG TALVCLTIDE TGMAKTTEEK LRVAERIYDL CVNRHGIDPR NLIFDMLTFT VGSGDLEYRD AAIQTLEAIR ELHKRHPEVG STLGLSNISF GLDKNARIYL NSVFLHHCIQ AGMTSVIINV KHIVPLAKMS QEDIDICEEL LFRPDDNSLF RFIEHFSDKT VDDSGTDEEY EAMNSEEKIA KLLLDGDKER MIPLVEEARK EIDPDRIVNE ILIDAMKVVG ELFGSGQMQL PFVLQSAETM KATVDYLNPY LTKQEKETDT TLVIGTVKGD VHDVGKNLVD IILSNNGFKV INVGIKTDLD TYLEAHKEHK VQAIGMSGLL VKSTAVMKDN LETMAEMGMT IPVLLGGAAL TRSFVDDFCR PIYKGPIFYC RDAFDGVIVM SRIEKYNEDP SVGLDTRLAG DMVKREEKKE KKEVVIPPFE EIQMPEPVDI PTPPFWGRRV LQKKDLDLNM VFDWVNQKTV IKMHWGYKSK GMTKEAYQKL LDETVYPAYE RLKKEFIEKD LFDPTIIYGY YPVRSNDREL LVFSESEGWN VDENADREPF KEVVGRAEYA FSFPRQRRKP YRALSDFFRH ERHDVLGITC VSAGSKFSAY EKELYDAGKY LEYNMVHGFS VELAEALAEV AHKQIRMDLG ILKEDEGATL RDVRMNRYRG ARYSFGYAAC PDLEQSRIIF DLLKPEEFGI ELSETFQIHP EQSTTALVVH HPKATYYAI // ID A6SU92_JANMA Unreviewed; 1252 AA. AC A6SU92; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 01-APR-2015, entry version 60. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:ABR88494.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABR88494.1}; GN Name=metH {ECO:0000313|EMBL:ABR88494.1}; GN OrderedLocusNames=mma_0149 {ECO:0000313|EMBL:ABR88494.1}; OS Janthinobacterium sp. (strain Marseille) (Minibacterium massiliensis). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae; Janthinobacterium. OX NCBI_TaxID=375286 {ECO:0000313|EMBL:ABR88494.1, ECO:0000313|Proteomes:UP000006388}; RN [1] {ECO:0000313|EMBL:ABR88494.1, ECO:0000313|Proteomes:UP000006388} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Marseille {ECO:0000313|EMBL:ABR88494.1, RC ECO:0000313|Proteomes:UP000006388}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000269; ABR88494.1; -; Genomic_DNA. DR RefSeq; WP_011979375.1; NC_009659.1. DR RefSeq; YP_001351839.1; NC_009659.1. DR ProteinModelPortal; A6SU92; -. DR SMR; A6SU92; 660-918. DR STRING; 375286.mma_0149; -. DR EnsemblBacteria; ABR88494; ABR88494; mma_0149. DR KEGG; mms:mma_0149; -. DR PATRIC; 22152695; VBIJanSp106498_0153. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; JSP375286:GJ8U-149-MONOMER; -. DR Proteomes; UP000006388; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006388}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABR88494.1}; KW Transferase {ECO:0000313|EMBL:ABR88494.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 255 255 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 320 320 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 778 778 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1252 AA; 137927 MW; C9078E56E7D86172 CRC64; MKRDALCPTE VLLRDLMARR ILILDGAMGT MIQQYKLTEE DYRGTRFADF AVPGKEIFVK GNNELLSLTR PDVISQIHEQ YLAAGADLIE SNTFGATTVA QDDYHMGHLA YEMNVASARL ARAACDKYST PDKPRFVAGA LGPTPKTASI SPDVNDPAAR NVTFDQLVAA YLDQTRGLVE GGADVLLVET IFDTLNCKAA LFAIDQFFEE SGKRFPIMIS GTVTDASGRI LSGQTVPAFW HSIRHARPLT VGLNCALGAA LMRPYAEELS KIADTYVCIY PNAGLPNPMS DTGFDETPDV TSSLLKDFAE SGFVNVAGGC CGTTPDHIKA IAETVKTIAP RVIPTVEPTL KLSGLEPFII DDQSLFVNVG ERTNVTGSKA FARLIINEQY DEALAVARQQ VENGAQIIDI NMDEAMLDSQ AAMSRFLNLV ASEPDIARVP IMIDSSKWSV IEAGLKCVQG KAIVNSISMK EGEEKFLHEA KLCRRYGAAV IVMAFDEKGQ ADTFERKIEI CERAYWLLVN EVAFPPEDII FDPNIFAIAT GIEEHNNYAV DFINSVRWIK ENLPHAKISG GVSNVSFSFR GNDPAREAIH TVFLYHAIKA GMTMGIVNAG MVGVYDNLPE ELRERVEDVV LNRREDATER MIEIASTLKA GDKKEEATLE WRSGTVQQRL AHALVQGITQ WIVEDTEEAR QELLGNGGRP IHVIEGPLMD GMNIVGDLFG QGKMFLPQVV KSARVMKQAV AHLIPFIEEE KRLLQEQTGI VSKPKGKIVI ATVKGDVHDI GKNIVSVVLQ CNNFEVVNMG VMVPCSEILA KAKEENADII GLSGLITPSL EEMAYVAKEM QRDEYFRGLK TPLLIGGATT SRAHTAVKIA HNYDGPVVYV PDASRSVSVA QSLLTPEQRD AYIAEIAADY ERIREQHANK KAVPMLTLAE ARANKMKLEF TGKYAPVKPK FIGRRVFKNV DLATIAQYID WGPFFQTWDL AGPYPAILKD EVVGEAATKV FAEGQALLKK VIEGRWLQAN GVIALLPANT VNDDDIEIYT DETRSKVAFT YYGVRQQTVK PVIDGVARPN QCLTDFIAPK SSGVADYIGL FAVTAGLGIE KYEKRFEDAH DDYSSIMLKS LADRLAEAFA EHLHERVRKD LWGYAADEKL TNEALIKEEY SGIRPAPGYP ACPEHTVKKE MFQTLQAEEI GMMLTDSYAM FPGAAVSGFY FAHPEAKYFV VGKIGDDQVV DMAERRGATK EDVERWLAPN LS // ID A6T591_KLEP7 Unreviewed; 310 AA. AC A6T591; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 27-MAY-2015, entry version 38. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:ABR75762.1}; GN Name=mmuM {ECO:0000313|EMBL:ABR75762.1}; GN ORFNames=KPN_00310 {ECO:0000313|EMBL:ABR75762.1}; OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH OS 78578). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=272620 {ECO:0000313|EMBL:ABR75762.1, ECO:0000313|Proteomes:UP000000265}; RN [1] {ECO:0000313|EMBL:ABR75762.1, ECO:0000313|Proteomes:UP000000265} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700721 / MGH 78578 {ECO:0000313|Proteomes:UP000000265}; 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 ----------------------------------------------------------------------- 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; ABR75762.1; -; Genomic_DNA. DR RefSeq; WP_004147274.1; NC_009648.1. DR RefSeq; YP_001333992.1; NC_009648.1. DR STRING; 272620.KPN_00310; -. DR EnsemblBacteria; ABR75762; ABR75762; KPN_00310. DR KEGG; kpn:KPN_00310; -. DR PATRIC; 20454813; VBIKlePne13394_0313. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; KPNE272620:GKDC-310-MONOMER; -. DR Proteomes; UP000000265; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000265}; KW Methyltransferase {ECO:0000313|EMBL:ABR75762.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000265}; KW Transferase {ECO:0000313|EMBL:ABR75762.1}. SQ SEQUENCE 310 AA; 33199 MW; 62AADDC7709E38C3 CRC64; MSQTNPFTAL LDAQPFVLLD GAMATELEAR GCDLADSLWS AKVLLENPQL IRDVHLDYFR AGAQVAITAS YQATPAGFAA RGLDEAQSRA LIGKSVELAR KAREAYLAEN PQAGTLLVAG SVGPYGAFLA DGSEYRGDYQ RSAAEFQAFH RPRVEALLDA GADLLACETL PSFAEIQALA ALLQEYPRAR AWYSFTLRDA EHLSDGTPLR EVMAALADNP QVVAVGINCI ALENTPAALA HLHSLTALPL VVYPNSGEHY DAVSKTWHHH GEACASLADY LPQWLAAGAK LIGGCCRTTP KDIAALNAKR // ID A6TGS0_KLEP7 Unreviewed; 1227 AA. AC A6TGS0; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 27-MAY-2015, entry version 59. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:ABR79754.1}; GN Name=metH {ECO:0000313|EMBL:ABR79754.1}; GN ORFNames=KPN_04399 {ECO:0000313|EMBL:ABR79754.1}; OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH OS 78578). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=272620 {ECO:0000313|EMBL:ABR79754.1, ECO:0000313|Proteomes:UP000000265}; RN [1] {ECO:0000313|EMBL:ABR79754.1, ECO:0000313|Proteomes:UP000000265} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700721 / MGH 78578 {ECO:0000313|Proteomes:UP000000265}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000647; ABR79754.1; -; Genomic_DNA. DR RefSeq; WP_015959249.1; NC_009648.1. DR RefSeq; YP_001338021.1; NC_009648.1. DR ProteinModelPortal; A6TGS0; -. DR SMR; A6TGS0; 651-1227. DR STRING; 272620.KPN_04399; -. DR EnsemblBacteria; ABR79754; ABR79754; KPN_04399. DR KEGG; kpn:KPN_04399; -. DR PATRIC; 20463258; VBIKlePne13394_4443. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; KPNE272620:GKDC-4436-MONOMER; -. DR Proteomes; UP000000265; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000265}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000265}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135755 MW; 215BF175FF006791 CRC64; MSSKVEQLHQ QLKERILVLD GGMGTMIQGY RLSEQDFRGE RFADWPCDLK GNNDLLVLSK PEVIREIHDA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARASADAWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTRAL AEGGVDLILI ETVFDTLNAK AAIYAVKEEL EALGVDLPLM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LSFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MATQIREWAE AGFLNIVGGC CGTTPEHIAA MSRAVAGLPP RQLPEIAVAC RLAGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VESGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVESFIHHA KLVRRYGAAV VVMAFDEVGQ ADTRERKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPG ELRDAVEDVI LNRRDDSTER LLELAEKYRG SKADDGANAQ QAEWRTWEVK KRLEYSLVKG ITEFIEQDTE EARQQAARPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGSSNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIIDL GVMVPADKIL KTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVSAL LSDTQRDEFV ARTRKEYETV RIQHGRKKPR TPPVTLAAAR ENDLAFDWES YTPPVAHRLG VQTVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG EEAQRLFKDA NELLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVLTVSHHLR QQTEKVGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAYEAQH DDYNKIMIKA IADRLAEAFA EYLHEKVRKV YWGYAANENL SNEELIRENY QGIRPAPGYP ACPEHTEKGT IWQLLDVEAH TGMKLTESFA MWPGASVSGW YFSHPDSKYF AVAQIQRDQV EDYALRKGMT PAEVERWLAP NLGYDAD // ID A6TTI3_ALKMQ Unreviewed; 789 AA. AC A6TTI3; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 27-MAY-2015, entry version 53. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABR49501.1}; GN OrderedLocusNames=Amet_3373 {ECO:0000313|EMBL:ABR49501.1}; OS Alkaliphilus metalliredigens (strain QYMF). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Alkaliphilus. OX NCBI_TaxID=293826 {ECO:0000313|EMBL:ABR49501.1, ECO:0000313|Proteomes:UP000001572}; RN [1] {ECO:0000313|Proteomes:UP000001572} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=QYMF {ECO:0000313|Proteomes:UP000001572}; 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 ----------------------------------------------------------------------- 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; ABR49501.1; -; Genomic_DNA. DR RefSeq; WP_012064464.1; NC_009633.1. DR RefSeq; YP_001321160.1; NC_009633.1. DR ProteinModelPortal; A6TTI3; -. DR STRING; 293826.Amet_3373; -. DR EnsemblBacteria; ABR49501; ABR49501; Amet_3373. DR KEGG; amt:Amet_3373; -. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; AMET293826:GI5P-3426-MONOMER; -. DR Proteomes; UP000001572; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001572}; KW Methyltransferase {ECO:0000313|EMBL:ABR49501.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001572}; KW Transferase {ECO:0000313|EMBL:ABR49501.1}. SQ SEQUENCE 789 AA; 85731 MW; B0412D170E26EF8C CRC64; MNFLRDCKEG MLIFDGAMGT MLQKSGLKVG ALPEIYNIEH PELIQQIHER FVRAGAQVVT TNTFQANELK LKDSIYSLEE IIEGGIKVAK ASGAPYVALD IGPLGQMMKP LGEISFDRAY DIFKRQVQAG VKAGADCILI ETISDLYEAK AAILAAKENS DLPVLCTMTF QEDGRTFTGT DPMTATLVLQ SLGVDALGVN CSLGPKEMLP ILSDILKYAK VPVMVQSNAG LPRLEGDDTI FPASPEEFAL YGREMAELGV GILGGCCGTT PEHIQALKKA VFQINSPERK VERVTCACSP TKTVILDGRT TVIGERINPT GKKRLKEALR NNQLEVLVAE AIDQSNAGAQ VLDVNVGLPE IDEVAVLKEV IMGIQEVVDT PLQIDSVNVE AMEAAARIYN GKPIINSVNG KEAVMAAVFP IAKKYGATLI GLTLDDKGIP ETAEERIQIA KTIMERAKAY GIPKEDLIID CLVMTASAQQ SVVKETIKAV SLVKSELGLK TSLGVSNVSF GLPNRELLNR TFLATALAAG LDAPIMDPLS KEMMDTIEAF RVLNNEDQEA MAFIRRFKNN TKSIEAPVQS SKDLKTMIIE GRKTEVAAAV DLLLQNESPF EIIETYFIPA LDQVGKEYEV GDLFLPQLLR AAETVKAGLA VIKASSFEKM PELDRGSILL ATVKGDIHDI GKNIVKMLME NYGFQIIDLG RDVDPQLIVE TIKKNNIRLV GLSALMTTTV KNMQLTIKMI KEEAPHCKVM VGGAVLNEEY AQMIGADYYT VDGQAGIRIA KAFFKGSLI // ID A6TYK9_STAA2 Unreviewed; 613 AA. AC A6TYK9; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 27-MAY-2015, entry version 54. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=SaurJH1_0415 {ECO:0000313|EMBL:ABR51277.1}; OS Staphylococcus aureus (strain JH1). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=359787 {ECO:0000313|EMBL:ABR51277.1, ECO:0000313|Proteomes:UP000001109}; RN [1] {ECO:0000313|EMBL:ABR51277.1, ECO:0000313|Proteomes:UP000001109} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JH1 {ECO:0000313|EMBL:ABR51277.1, RC ECO:0000313|Proteomes:UP000001109}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ABR51277.1; -; Genomic_DNA. DR RefSeq; WP_000077317.1; NC_009632.1. DR RefSeq; YP_001315564.1; NC_009632.1. DR ProteinModelPortal; A6TYK9; -. DR SMR; A6TYK9; 3-567. DR STRING; 359787.SaurJH1_0415; -. DR EnsemblBacteria; ABR51277; ABR51277; SaurJH1_0415. DR KEGG; sah:SaurJH1_0415; -. DR PATRIC; 19532625; VBIStaAur98826_0443. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; SAUR359787:GCG4-415-MONOMER; -. DR Proteomes; UP000001109; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001109}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ABR51277.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:ABR51277.1}. SQ SEQUENCE 613 AA; 68430 MW; 913D89847AF5FD02 CRC64; MSQFLTQLKD NVLVADGAIG TILYSEGLDT CPEAYNLSHP DKVERIHRSY IEAGADVIQT NTYGANFEKL KRFGLEDKVK AIHQAAVRIA KKAANKDTYI LGTVGGFRGI KQEDISLQTI LYHTEIQIDT LIEEGVDALL FETYYDLEEL TNVISRTRKK YDIPIIAQLT ASNTNYLVNG QAINEGLKQL VQCGANIVGL NCHHGPHHMQ ESFTHIELPE HAFLSCYPNA SLLDIENSEF KYSDNAQYFG QVAQNLIREG VRLIGGCCGT TPEHIKFIKE SIQTLKPVND KKVIPIPTKA LFNPSQNKVR QSLTSKVQER PTVIIELDTP KHLDTDRFFE NIAKLDKANV DAVTLADNSL ATVRISNIAA ASLIKQYYNI EPLVHITCRD RNLIGLQSHL LGLSLIGVNE ILAITGDPSK VGHLPGATNV YDVNSKGLTE LALRFNQGIN TDGDALKKRT HFNIAGAFNP NVRKLDGAVK RLEKKIESGM SYFITQPVYS KEKIIEIYHA TKHLNKPFFI GIMPIASYKN ALFLHNEVPG IKMSDEILQQ FEAVKDDKAK TRELSLKLSK DLIDTVHEYF NGLYIITPFQ NVEDSLELAA YSKSITAHKE AIL // ID A6U723_SINMW Unreviewed; 322 AA. AC A6U723; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 27-MAY-2015, entry version 35. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABR59453.1}; GN OrderedLocusNames=Smed_0597 {ECO:0000313|EMBL:ABR59453.1}; OS Sinorhizobium medicae (strain WSM419) (Ensifer medicae). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=366394 {ECO:0000313|EMBL:ABR59453.1, ECO:0000313|Proteomes:UP000001108}; RN [1] {ECO:0000313|Proteomes:UP000001108} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WSM419 {ECO:0000313|Proteomes:UP000001108}; 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; ABR59453.1; -; Genomic_DNA. DR RefSeq; WP_011974799.1; NC_009636.1. DR RefSeq; YP_001326288.1; NC_009636.1. DR ProteinModelPortal; A6U723; -. DR STRING; 366394.Smed_0597; -. DR EnsemblBacteria; ABR59453; ABR59453; Smed_0597. DR GeneID; 5321433; -. DR KEGG; smd:Smed_0597; -. DR PATRIC; 23620058; VBISinMed134228_3691. DR eggNOG; COG2040; -. DR HOGENOM; HOG000179103; -. DR OMA; CCGTDHR; -. DR OrthoDB; EOG6R5C46; -. DR BioCyc; SMED366394:GJAL-606-MONOMER; -. DR Proteomes; UP000001108; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001108}; KW Methyltransferase {ECO:0000313|EMBL:ABR59453.1}; KW Transferase {ECO:0000313|EMBL:ABR59453.1}. SQ SEQUENCE 322 AA; 35658 MW; 5CCF83E6AF64CCC8 CRC64; MEENLARYRH DLPLVRGGMF LSDGGMETAL IFHEGVDLPH FASFVLLSSA EGRRQLLRYY TRYLEIARRH ATGFVLDTAT WRANADWGEK LGFDAEALKK VNRDAVYLLT GLRSEYERPE APVVLNGVIG PRGDGYRAGR MTAIEAEDYH SAQIAALSGS EADMITAVTM TNTEEAIGIV RSARNHDMPC AISFTVETDG RLITGRPLEH AIETVDAETD GYPLYYMINC AHPSHFENML DRQSAWVRRI GGIRANASTK SHAELDESET LDAGDVCDLA ERYRSLTRHL PHLRVLGGCC GTDHRHITAI CEACLPHAAL SA // ID A6UAC6_SINMW Unreviewed; 337 AA. AC A6UAC6; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 27-MAY-2015, entry version 42. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABR60606.1}; GN OrderedLocusNames=Smed_1771 {ECO:0000313|EMBL:ABR60606.1}; OS Sinorhizobium medicae (strain WSM419) (Ensifer medicae). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=366394 {ECO:0000313|EMBL:ABR60606.1, ECO:0000313|Proteomes:UP000001108}; RN [1] {ECO:0000313|Proteomes:UP000001108} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WSM419 {ECO:0000313|Proteomes:UP000001108}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; ABR60606.1; -; Genomic_DNA. DR RefSeq; WP_011975909.1; NC_009636.1. DR RefSeq; YP_001327441.1; NC_009636.1. DR ProteinModelPortal; A6UAC6; -. DR STRING; 366394.Smed_1771; -. DR EnsemblBacteria; ABR60606; ABR60606; Smed_1771. DR GeneID; 5322629; -. DR KEGG; smd:Smed_1771; -. DR PATRIC; 23622547; VBISinMed134228_4912. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265278; -. DR KO; K00548; -. DR OMA; GTNLFAM; -. DR OrthoDB; EOG693GKH; -. DR BioCyc; SMED366394:GJAL-1802-MONOMER; -. DR Proteomes; UP000001108; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001108}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ABR60606.1}; KW Transferase {ECO:0000313|EMBL:ABR60606.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 215 215 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 281 281 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 282 282 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 337 AA; 35183 MW; 487D0D74370313CC CRC64; MSVAPHALAD LLAQKGVLLA DGATGTSLFA MGLEAGEAPE IWNETKPENI TKLHQDFVDA GADIILTNSF GGTRHRLKLH QAEDRVHQLN KRAAEIARAV ADKAPRKVIT AGSVGPTGEL LIPLGALSYE DAVAAFVEQI EGLKAGGAEV AWIETMSSAD EIRAAAEAAV KVGLPYVYTG SFDTAGKTMM GLHPKDIHGV AADIGEGPVA VGANCGVGAS DILSSLLDMT AESPDATIVV KGNCGIPEFR GSEIHYSGTP PLMAEYARLA MDAGARIIGG CCGTSCNHLA AMRLAIDNHI KGERPTLETI VEKIGPLRNK SANEGPAAPA RERRRRA // ID A6UDH0_SINMW Unreviewed; 1257 AA. AC A6UDH0; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 01-APR-2015, entry version 58. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABR61700.1}; GN OrderedLocusNames=Smed_2870 {ECO:0000313|EMBL:ABR61700.1}; OS Sinorhizobium medicae (strain WSM419) (Ensifer medicae). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=366394 {ECO:0000313|EMBL:ABR61700.1, ECO:0000313|Proteomes:UP000001108}; RN [1] {ECO:0000313|Proteomes:UP000001108} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WSM419 {ECO:0000313|Proteomes:UP000001108}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000738; ABR61700.1; -; Genomic_DNA. DR RefSeq; WP_012067083.1; NC_009636.1. DR RefSeq; YP_001328535.1; NC_009636.1. DR ProteinModelPortal; A6UDH0; -. DR SMR; A6UDH0; 668-1247. DR STRING; 366394.Smed_2870; -. DR EnsemblBacteria; ABR61700; ABR61700; Smed_2870. DR GeneID; 5323746; -. DR KEGG; smd:Smed_2870; -. DR PATRIC; 23624923; VBISinMed134228_6083. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SMED366394:GJAL-2919-MONOMER; -. DR Proteomes; UP000001108; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001108}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 262 262 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 325 325 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 326 326 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 779 779 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1257 AA; 138093 MW; CD68D082962292F4 CRC64; MSASDDLFGH VSPKPDGSEI FRQLAQAAAE RILIMDGAMG TEIQQLGFVE DHFRGERFGA CNCHQQGNND LLTLTQPKAI EEIHYHYAIA GADILETNTF SSTRIAQADY GMEDMVYDLN RDGARLARRA ARRAEAEDGR RRFVAGALGP TNRTASISPD VNNPGYRAVS FDDLRLAYSE QVRGLIDGGA DIILIETIFD TLNAKAAIFA TQEVFAEKAV HLPIMISGTI TDLSGRTLSG QTPTAFWYSV RHASPFTIGL NCALGANAMR AHIDELSAIA DTLVCAYPNA GLPNEFGQYD ESPEQMAAQI EGFARDGLVN VVGGCCGSTP AHIRAIAEAV AKYPPRRVPE TERLMRLSGL EPFTLTDEIP FVNVGERTNV TGSAKFRKLI TAGDYAAALE VARDQVANGA QIIDVNMDEG LIDSKQVMVE FLNLVASEPD IARVPVMIDS SKWEVIEAGL KCVQGKALVN SISLKEGEEA FLYHARLVRA YGAAVVVMAF DEKGQADTKT RKVEICRRAY RLLTEEVGFP PEDIIFDPNI FAVATGIEEH DNYGVDFIEA THEIVAALPH VHISGGVSNL SFSFRGNEPV REAMHAVFLY HAIQAGMDMG IVNAGQLAVY DAIDAELREA CEDVVLNRRS DGTERLLEIA ERYRGQGGSQ GREKDLAWRE WPVEKRLEHA LVYGITEFIE ADTEEARLSA ERPLHVIEGP LMAGMNVVGD LFGSGKMFLP QVVKSARVMK QAVAVLLPHM EAEKRANGGG EARESAGKIL MATVKGDVHD IGKNIVGVVL ACNNYEIIDL GVMVSSARIL EVAREQKVDI IGLSGLITPS LDEMAHVASE LEREGFDLPL LIGGATTSRV HTAVKINPRY SLGQTVYVTD ASRAVGVVSS LLSPEVRDGY KETIRAEYLK VAEAHARNEA EKRRLPLSQA RANAVKIDWE AHRPKVPSFL GTRVFDGWDL AELARYIDWT PFFQTWEMKG VYPRILDDEH QGAAARQLFE DAQAMLAQIV AEKWFAPKAV VGFWPAGSVG DDVRLFTDET RKGELATLFT LRQQLVKRDG RPNVALADFV APAESGKRDY AGAFVVTAGI EEVAIAERFE RANDDYSSIM VKALADRFAE AFAERMHEYV RKELWGYAAD EAFTPQELIG EPYAGIRPAP GYPAQPDHTE KETLFRLLNA EAAIGVKLTE SYAMWPGSSV SGLYIGHPDS YYFGVAKIER DQVEDYAERK QMSVREVERW LSPVLNYVPA PEAEAAE // ID A6UMQ0_SINMW Unreviewed; 307 AA. AC A6UMQ0; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 27-MAY-2015, entry version 32. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABR64930.1}; GN OrderedLocusNames=Smed_6335 {ECO:0000313|EMBL:ABR64930.1}; OS Sinorhizobium medicae (strain WSM419) (Ensifer medicae). OG Plasmid pSMED03 {ECO:0000313|EMBL:ABR64930.1, OG ECO:0000313|Proteomes:UP000001108}. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=366394 {ECO:0000313|EMBL:ABR64930.1, ECO:0000313|Proteomes:UP000001108}; RN [1] {ECO:0000313|Proteomes:UP000001108} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WSM419 {ECO:0000313|Proteomes:UP000001108}; 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 pSMED03."; 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; CP000741; ABR64930.1; -; Genomic_DNA. DR RefSeq; WP_011971140.1; NC_009622.1. DR RefSeq; YP_001314863.1; NC_009622.1. DR ProteinModelPortal; A6UMQ0; -. DR STRING; 366394.Smed_6335; -. DR EnsemblBacteria; ABR64930; ABR64930; Smed_6335. DR GeneID; 5320638; -. DR KEGG; smd:Smed_6335; -. DR PATRIC; 23618374; VBISinMed134228_2859. DR eggNOG; COG2040; -. DR HOGENOM; HOG000179103; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; SMED366394:GJAL-6397-MONOMER; -. DR Proteomes; UP000001108; Plasmid pSMED03. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001108}; KW Methyltransferase {ECO:0000313|EMBL:ABR64930.1}; KW Plasmid {ECO:0000313|EMBL:ABR64930.1}; KW Transferase {ECO:0000313|EMBL:ABR64930.1}. SQ SEQUENCE 307 AA; 33444 MW; B46C0EC9C57A47B8 CRC64; MGILDRLFSS PDPFISDGGM ETDLIFHEGA EMPLFASFVL LDSPEGCEML RRYAVSYFDL AQVASRGFVM GTPTWRANGG WGPKLGLDDA GIRDVNRRAI AFARDLRSAH PWRDHILIEG VLGPAGDGYA PEQLLTPTEA ARLHSAQLET FAEEDVDIAS AFTITHPGEA IGMVNRARDL GLPFALSFTV ETDGRLPTGQ DLDCALDEVE AATGGYVRYY GINCAHPEHF GEQLPSRWLN RIGVVRPNAS RRSHAELDEA TELDDGDPQE FGALYAEMAE KLPRLRVVGG CCGSDMRHIK ALIAAGV // ID A6V6X4_PSEA7 Unreviewed; 1234 AA. AC A6V6X4; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 27-MAY-2015, entry version 60. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABR85511.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABR85511.1}; GN Name=metH {ECO:0000313|EMBL:ABR85511.1}; GN OrderedLocusNames=PSPA7_3449 {ECO:0000313|EMBL:ABR85511.1}; OS Pseudomonas aeruginosa (strain PA7). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=381754 {ECO:0000313|EMBL:ABR85511.1, ECO:0000313|Proteomes:UP000001582}; RN [1] {ECO:0000313|EMBL:ABR85511.1, ECO:0000313|Proteomes:UP000001582} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PA7 {ECO:0000313|EMBL:ABR85511.1, RC ECO:0000313|Proteomes:UP000001582}; RA Dodson R.J., Harkins D., Paulsen I.T.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000744; ABR85511.1; -; Genomic_DNA. DR RefSeq; WP_012076145.1; NC_009656.1. DR RefSeq; YP_001348809.1; NC_009656.1. DR ProteinModelPortal; A6V6X4; -. DR SMR; A6V6X4; 658-1233. DR STRING; 381754.PSPA7_3449; -. DR EnsemblBacteria; ABR85511; ABR85511; PSPA7_3449. DR KEGG; pap:PSPA7_3449; -. DR PATRIC; 19828550; VBIPseAer80442_3287. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PAER381754:GHMY-3449-MONOMER; -. DR Proteomes; UP000001582; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001582}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABR85511.1}; KW Transferase {ECO:0000313|EMBL:ABR85511.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 254 254 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 318 318 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 765 765 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1234 AA; 135199 MW; 1CB3B8E76E7291C2 CRC64; MSSPLTDRSA RLQALQHALR ERILILDGGM GTMIQSYRLE EADYRGERFA DWPSDVKGNN DLLLLSRPDV IQAIEKAYLD AGADILETNT FNATQVSQAD YGMQALAYEL NVEGARLARQ VADAKTAQTP DKPRFVAGVL GPTSRTCSIS PDVNNPGYRN VTFDELVENY VEATRGLIEG GADLILIETI FDTLNAKAAI FAVQGVFEEL GVELPIMISG TITDASGRTL SGQTTEAFWN SVRHARPISV GLNCALGAKE LRPYIEELST KADTHVSAHP NAGLPNAFGE YDESPAEMAV VVEEFAAAGF LNIVGGCCGT TPAHIEAIAK AVAKYPPRAI PEIPRACRLS GLEPFTIDRS SLFVNVGERT NITGSARFAR LIREENYAEA LEVAQQQVEA GAQVIDINMD EGMLDSKAAM VTFLNLIASE PDISRVPIMI DSSKWEVIEA GLKCIQGKGI VNSISMKEGV EAFKHHARLC KRYGAAVVVM AFDEDGQADT QARKEEICKR SYDILVDEVG FPPEDIIFDA NIFAIATGIE EHNNYAVDFI NACAYIRDNL PYALSSGGVS NVSFSFRGNN PVREAIHSVF LYYAIRNGLT MGIVNAGQLE IYDEIPKALR DRVEDVVLNR TPEATEALLA IADDYKGGGA VKEAEDEEWR SYSVEKRLEH ALVKGITTWI VEDTEECRQR CARPIEVIEG PLMAGMNVVG DLFGAGKMFL PQVVKSARVM KQAVAHLIPF IEAEKGDKPE AKGKILMATV KGDVHDIGKN IVGVVLGCNG YDVVDLGVMV PAEKILQTAI AEKCDIIGLS GLITPSLDEM VHVAKEMQRQ NFQLPLMIGG ATTSKAHTAV KIDPQYSNDA VVYVTDASRA VGVATSLLSK ELKADYVART RADYAVVRER TANRSARTER LSYEQAIANK PAFDWAGYQA PTPSFTGVRV LDEIDLAVLA EYIDWTPFFI SWDLAGKYPR ILTDEVVGEA ATSLFNDARA MLKKLIDEKL IKARAVFGFW PANQVEHDDL EVYDADGETL ATLHHLRQQT IKPDGKPNLS LADFVAPKDS GVRDYIGGFI TTAGIGAEEV AKAYEAKGDD YNSIMVKALA DRLAEACAEW LHERVRKEYW GYARDEHLDN EALIKEQYIG IRPAPGYPAC PDHTEKGTLF ELLDPQGLSG VSLTEHYAMF PAAAVSGWYF AHPQAQYFAV GKIDKDQVQR YSQRKGQEAS VSERWLAPNL GYDD // ID A6VP77_ACTSZ Unreviewed; 297 AA. AC A6VP77; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 27-MAY-2015, entry version 38. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABR74774.1}; GN OrderedLocusNames=Asuc_1415 {ECO:0000313|EMBL:ABR74774.1}; OS Actinobacillus succinogenes (strain ATCC 55618 / 130Z). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=339671 {ECO:0000313|EMBL:ABR74774.1, ECO:0000313|Proteomes:UP000001114}; RN [1] {ECO:0000313|Proteomes:UP000001114} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 55618 / 130Z {ECO:0000313|Proteomes:UP000001114}; RX PubMed=21118570; DOI=10.1186/1471-2164-11-680; RA McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A., RA Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L., RA Burkhart K.B., Harkins V., Vieille C.; RT "A genomic perspective on the potential of Actinobacillus succinogenes RT for industrial succinate production."; RL BMC Genomics 11:680-680(2010). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; ABR74774.1; -; Genomic_DNA. DR RefSeq; WP_012073151.1; NC_009655.1. DR RefSeq; YP_001344709.1; NC_009655.1. DR STRING; 339671.Asuc_1415; -. DR EnsemblBacteria; ABR74774; ABR74774; Asuc_1415. DR KEGG; asu:Asuc_1415; -. DR PATRIC; 20761204; VBIActSuc117883_1478. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; PYVDVWL; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; ASUC339671:GHDX-1483-MONOMER; -. DR Proteomes; UP000001114; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001114}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ABR74774.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001114}; KW Transferase {ECO:0000313|EMBL:ABR74774.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 204 204 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 281 281 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 282 282 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 297 AA; 32693 MW; C06286A9B71D484D CRC64; MQVTILDGGM SRELMRLNAP FKQPEWSALS LYEKPSAVQQ VHEDYIASGA DVITTNSYAV VPFHIGERRF HADGKMLADL AGRLAQSAVK NSGKPVKIAG SLPPMFGSYR ADLIEKDRFR EIAQPIIDGL SPYADIWLCE TQSAIIEPVS IKPLLPKDER PLWVSFTLID DEPTAEPQLR SGESVKSAVK KMIELGVDAI LFNCCQPEVI ERALDVTRKI LNENQAAHIK MGAYANAFAP QPKDATANDG LDEVRKDLDP QAYLRWAQKW KAQGAAIIGG CCGIGIDHIR VLADNLN // ID A6VXB2_MARMS Unreviewed; 1245 AA. AC A6VXB2; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 27-MAY-2015, entry version 62. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABR71091.1}; GN OrderedLocusNames=Mmwyl1_2169 {ECO:0000313|EMBL:ABR71091.1}; OS Marinomonas sp. (strain MWYL1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Marinomonas. OX NCBI_TaxID=400668 {ECO:0000313|EMBL:ABR71091.1, ECO:0000313|Proteomes:UP000001113}; RN [1] {ECO:0000313|EMBL:ABR71091.1, ECO:0000313|Proteomes:UP000001113} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MWYL1 {ECO:0000313|EMBL:ABR71091.1, RC ECO:0000313|Proteomes:UP000001113}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000749; ABR71091.1; -; Genomic_DNA. DR RefSeq; WP_012069870.1; NC_009654.1. DR STRING; 400668.Mmwyl1_2169; -. DR EnsemblBacteria; ABR71091; ABR71091; Mmwyl1_2169. DR KEGG; mmw:Mmwyl1_2169; -. DR PATRIC; 22467707; VBIMarSp124341_2241. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; MSP400668:GHKD-2192-MONOMER; -. DR Proteomes; UP000001113; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001113}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001113}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 249 249 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 764 764 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1245 AA; 137751 MW; D66EC008429EF302 CRC64; MVKSDSYSII EKRLAENVLI LDGAMGTMIQ GYKLEEKDYR GERFAEWNSD LKGNNDLLSL TQPKIIKDIY SSYLAAGADI IETNTFNANY ISMLDYHMEG LSYELNFESA RLAREAADEF TKQNPNKPRF VAGAVGPTSR TCTISPDVND PGFRNVHFDE LVDAYTTAVD GLIKGGVDII LIETIFDTLN AKAAIYAVLD YFEKTGVRYP IMISGTITDA SGRTLSGQTT EAFWNSISHA KPISVGLNCA LGPKELRQYV EELSRIADTH VSAHPNAGLP NAFGEYDESP EEMLEEIQGW VDSGFLNIIG GCCGTSPEHI ATFAKAFADS TPRVIPEIEK ACRLSGLEPF NIDGNSLFVN VGERTNVTGS AMFKRLIKEG DFDTALDVAR QQVENGAQII DINMDEGMLD SQAAMERFLK LIASEPDISR VPIMLDSSKW EILEAGLKWI QGKGVVNSIS MKEGEDKFRE QARKLMKYGA AVIVMAFDEV GQADTRARKI EICRRSYHIL VDEVGFPPED IIFDPNIFAI ATGIEEHNRY ALDFIEATGD ITRELPYAKV SGGVSNVSFS FRGNNPVREA IHAVFLYHAI KQGMTMGIVN AGQLALYEDI PTKLRNAVED AVLNRTPDAT DNLLAIAGEF AGTGEVAEKE TQEWRGLPVS ERLSHALVKG ITEFIDEDTE EARQAFARPL EVIEGPLMDG MGIVGDLFGS GKMFLPQVVK SARVMKKAVA YLMPFIEEEK RLNMDTASSS NGKIVMATVK GDVHDIGKNI VGVVLQCNNF EVIDLGVMVP AEKILRTAKE EGADMIGLSG LITPSLDEMV HVAKEMERQG FDLPVMIGGA TTSKAHTAVK IEQNYKRNQV VHVTNASRSV GVASALLSKD KERRQKFVDE IKADYEKTRI RYKDRAKAGR RVSLDKARQN KAPIVFDGSN VVQPKKLGIT VLTENDIDLN LVKDYIDWTP FFQTWELAGA YPRILTDDVV GVEATRVFED ALKMLDEVIA TKSLQARAVV GLFPANQVNH DDIEIYADGS RSEVVERLSF LRIQNELTAP GKYNHSLADF VAPKESGVAD YIGAFACAAG FGIDPLVAKY EADHDDYNSI MIKAVADRLA EATAEYLHEK VRKEFWGYAE AEELTNEQLI KEKYQGIRPA PGYPACPDHT EKAKLWSLLD VKEKIDMEIT ENFAMLPTAA VSGWYFAHPD TTYFGIGKIG PDQVDDYAER KGMSKDDAER WLAPNLGYDP EDDRI // ID A6VZG2_MARMS Unreviewed; 303 AA. AC A6VZG2; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 27-MAY-2015, entry version 39. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABR71841.1}; GN OrderedLocusNames=Mmwyl1_2930 {ECO:0000313|EMBL:ABR71841.1}; OS Marinomonas sp. (strain MWYL1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Marinomonas. OX NCBI_TaxID=400668 {ECO:0000313|EMBL:ABR71841.1, ECO:0000313|Proteomes:UP000001113}; RN [1] {ECO:0000313|EMBL:ABR71841.1, ECO:0000313|Proteomes:UP000001113} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MWYL1 {ECO:0000313|EMBL:ABR71841.1, RC ECO:0000313|Proteomes:UP000001113}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; ABR71841.1; -; Genomic_DNA. DR RefSeq; WP_012070617.1; NC_009654.1. DR ProteinModelPortal; A6VZG2; -. DR STRING; 400668.Mmwyl1_2930; -. DR EnsemblBacteria; ABR71841; ABR71841; Mmwyl1_2930. DR KEGG; mmw:Mmwyl1_2930; -. DR PATRIC; 22469359; VBIMarSp124341_3031. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; PYVDVWL; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; MSP400668:GHKD-2992-MONOMER; -. DR Proteomes; UP000001113; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001113}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ABR71841.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001113}; KW Transferase {ECO:0000313|EMBL:ABR71841.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 208 208 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 303 AA; 32916 MW; A4E1362A2DA49E24 CRC64; MTSFTILDGG MGRELERRGA PFKQPEWSAL AMMEAPNIVK EVHQSYIQSG SRVITTNSYA LVPFHIGEEA FKKQGRALAV LSGKVAREAA DESGTNTKVA GSLAPLFGSY RADLYQADRV EELAVPLIES LNPYVDLWLS ETQSLIDEVT RVKALVDKID TDKKPFWVSF TLEDLEPTTE PLLRSGETVA EAVKAMQAIG VNAILFNCSQ PEIIGKAIQV TQTTLSSLNA NSIQIGAYAN AFPPQPKNAT ANDGLDEIRT DLTPPAYLAW VKQWVEDGAT LIGGCCGIGP EHITAMNEFN KAN // ID A6WVC4_OCHA4 Unreviewed; 1263 AA. AC A6WVC4; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 27-MAY-2015, entry version 62. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABS12928.1}; GN OrderedLocusNames=Oant_0197 {ECO:0000313|EMBL:ABS12928.1}; OS Ochrobactrum anthropi (strain ATCC 49188 / DSM 6882 / NCTC 12168). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Ochrobactrum. OX NCBI_TaxID=439375 {ECO:0000313|EMBL:ABS12928.1, ECO:0000313|Proteomes:UP000002301}; RN [1] {ECO:0000313|EMBL:ABS12928.1, ECO:0000313|Proteomes:UP000002301} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49188 / DSM 6882 / NCTC 12168 RC {ECO:0000313|Proteomes:UP000002301}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000758; ABS12928.1; -; Genomic_DNA. DR RefSeq; WP_011982388.1; NC_009667.1. DR RefSeq; YP_001368757.1; NC_009667.1. DR ProteinModelPortal; A6WVC4; -. DR SMR; A6WVC4; 669-922. DR STRING; 439375.Oant_0197; -. DR EnsemblBacteria; ABS12928; ABS12928; Oant_0197. DR GeneID; 5380230; -. DR KEGG; oan:Oant_0197; -. DR PATRIC; 20465359; VBIOchAnt73124_0208. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; OANT439375:GJIT-199-MONOMER; -. DR Proteomes; UP000002301; Chromosome 1. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002301}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002301}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 263 263 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 326 326 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 327 327 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 784 784 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1263 AA; 138309 MW; A6C6178D16DFBE8F CRC64; MASSLDGLFG ATAAQPDGSE VLAALTKAAR ERILILDGAM GTQIQGLGFH EEHFRGERFG ACDCQLQGNN DLLTLTQPKA IEEIHYAYAI AGADILETNT FSSTTIAQAD YGMEEQVYEL NRDGARLARR AALRAEQKDG RRRFVAGALG PTNRTASLSP DVNNPGYRAV TFDDLRIAYA EQIRGLIDGG SDIILIETIF DTLNAKAAVF ASEQVFEEKG IFLPVMISGT ITDLSGRTLS GQTPTAFWHS LRHAKPFTIG LNCALGANAM RAHLDELSTI ADTFICAYPN AGLPNEFGQY DETPEAMAAQ IEGFARDGMV NVVGGCCGST PEHIRAIAEA VAKHPPRKPA KVAPLMRLSG LEPFTLTEDI PFVNVGERTN VTGSARFRKL IKAGDFAAAL DVARDQVVNG AQIIDINMDE GLIDSEKAMV EFLNLIAAEP DIARVPIMID SSKWEVIEAG LKCVQGKAVV NSISMKEGEE AFIHHAKLVR AYGAAVVVMA FDETGQADTE ARKIEICTRA YKILTEQVGF APEDIIFDPN IFAVATGIEE HNNYGVDFIE ATRKIMATLP HVHVSGGVSN LSFSFRGNEP VREAMHAVFL YHAIQAGMDM GIVNAGQLAV YDAIDPELRE ACEDVVLNRR SDATERLLEI AERFRDSGSK EAKVQDLTWR EWPVAKRLEH ALVNGITEYI EADTEEARQS AERPLHVIEG PLMAGMNVVG DLFGAGKMFL PQVVKSARVM KQAVAVLLPY MEEEKRLNAE KGIGGGERQS AGKVLMATVK GDVHDIGKNI VGVVLACNNY EIIDLGVMVP SQKILQVARD EKVDIIGLSG LITPSLDEMA HVAAEMEREG FDIPLLIGGA TTSRVHTAVK IHPRYERGQA VYVIDASRAV GVVSSLLSPE GKQAYVDGLR GEYAKVAAAH ARNEAEKQRL PIARARANAH KLDWDNFVPA KPTFTGTKTF DDYDLAEIAR YIDWTPFFQT WELKGRYPAI LEDEKQGEAA RQLWDDAQAM LKKIIDEKWF TPKAVVGFWP ANAVGDDIRL FTDESRNEEL ATFFTLRQQL SKRDGRPNVA MSDFVAPAES GKQDYVGGFV VTAGIGEVAI AERFERANDD YSAILVKALA DRFAEAFAEL MHERVRKEFW AYAANETYSP EELIGEPYQG IRPAPGYPAQ PDHTEKTTLF RLLDATANTG VELTESYAMW PGSSVSGLYI GHPESYYFGV AKVERDQVED YASRKGMTIE EVERWLAPIL NYTPGAAPEE AAA // ID A6ZN38_YEAS7 Unreviewed; 112 AA. AC A6ZN38; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=Conserved protein {ECO:0000313|EMBL:EDN64262.1}; GN ORFNames=SCY_4504 {ECO:0000313|EMBL:EDN64262.1}; OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=307796 {ECO:0000313|EMBL:EDN64262.1, ECO:0000313|Proteomes:UP000007060}; RN [1] {ECO:0000313|EMBL:EDN64262.1, ECO:0000313|Proteomes:UP000007060} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YJM789 {ECO:0000313|EMBL:EDN64262.1, RC ECO:0000313|Proteomes:UP000007060}; 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. {ECO:0000313|EMBL:EDN64262.1}. 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; AAFW02000021; EDN64262.1; -; Genomic_DNA. DR ProteinModelPortal; A6ZN38; -. DR OrthoDB; EOG7X9GHR; -. DR Proteomes; UP000007060; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007060}. SQ SEQUENCE 112 AA; 12436 MW; F01DDDA7CEAF4926 CRC64; MEEIAQVIKD LGDKINPNFS FLGINCVSFN QSPDILESLH QALPNMALLA YPNSGEVYDT EKKIWLPNSD KLNSWDTVVK QYISSGARII GGCCRTSPKD IQEISAAVKK YT // ID A6ZVW8_YEAS7 Unreviewed; 261 AA. AC A6ZVW8; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=AdoMet-homocysteine methyltransferase {ECO:0000313|EMBL:EDN61326.1}; GN Name=SAM4 {ECO:0000313|EMBL:EDN61326.1}; GN ORFNames=SCY_5445 {ECO:0000313|EMBL:EDN61326.1}; OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=307796 {ECO:0000313|EMBL:EDN61326.1, ECO:0000313|Proteomes:UP000007060}; RN [1] {ECO:0000313|EMBL:EDN61326.1, ECO:0000313|Proteomes:UP000007060} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YJM789 {ECO:0000313|EMBL:EDN61326.1, RC ECO:0000313|Proteomes:UP000007060}; 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. {ECO:0000313|EMBL:EDN61326.1}. 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; AAFW02000132; EDN61326.1; -; Genomic_DNA. DR ProteinModelPortal; A6ZVW8; -. DR OrthoDB; EOG7X9GHR; -. DR Proteomes; UP000007060; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007060}; KW Methyltransferase {ECO:0000313|EMBL:EDN61326.1}; KW Transferase {ECO:0000313|EMBL:EDN61326.1}. SQ SEQUENCE 261 AA; 29529 MW; 033A9E74EBAE569C CRC64; MFNDFLNAGA EILMTTTYQT SYKSVSENTP IRTLSEYNNL LNRIVDFSRN CIGEDKYLIG CIGPWGAHIC REFTGDYGAE PENIDFYQYF KPQLENFNKN DKLDLIGFET IPNIHELKAI LSWDESILSR PFYIGLSVHE HGVLRDGTTM EEIAQVIKDL GDKINPNFSF LGINCVSFNQ SPDILESLHQ ALPNMALLAY PNSGEVYDTE KKIWLPNSDK LNSWDTVVKQ YISSGARIIG GCCRTSPKDI QEISAAVKKY T // ID A6ZVY3_YEAS7 Unreviewed; 325 AA. AC A6ZVY3; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=AdoMet-homocysteine methyltransferase {ECO:0000313|EMBL:EDN60875.1}; GN Name=SAM4 {ECO:0000313|EMBL:EDN60875.1}; GN ORFNames=SCY_5460 {ECO:0000313|EMBL:EDN60875.1}; OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=307796 {ECO:0000313|EMBL:EDN60875.1, ECO:0000313|Proteomes:UP000007060}; RN [1] {ECO:0000313|EMBL:EDN60875.1, ECO:0000313|Proteomes:UP000007060} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YJM789 {ECO:0000313|EMBL:EDN60875.1, RC ECO:0000313|Proteomes:UP000007060}; 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. {ECO:0000313|EMBL:EDN60875.1}. 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; AAFW02000135; EDN60875.1; -; Genomic_DNA. DR ProteinModelPortal; A6ZVY3; -. DR Proteomes; UP000007060; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007060}; KW Methyltransferase {ECO:0000313|EMBL:EDN60875.1}; KW Transferase {ECO:0000313|EMBL:EDN60875.1}. SQ SEQUENCE 325 AA; 36678 MW; 4CC68E458A051B5D CRC64; MARLPLKQFL ADNPKKVLVL DGGQGTELEN RGIKVANPVW STIPFISESF WSDESSANRK IVKEMFNDFL HAGAEILMTT TYQTSYKSVS ENTPIRTLSE YNNLLNRIVD FSRNCIGEDK YLIGCIGPWG AHICREFTGD YGAEPENIDF YQYFKPQLEN FNKNDKLDLI GFETIPNIHE LKAILSWDES VLSRPFYIGL SVHEHGVLRD GTTMEEIAQV IKDLGDKINP NFSFLGINCV SFNQSPDILE SLHQALPNMA LLAYPNSGEV YDTEKKIWLP NSDKLNSWDT VVKQYISSGA RIIGGCCRTS PKDIQEISAA VKKYT // ID A7A0J9_YEAS7 Unreviewed; 324 AA. AC A7A0J9; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=S-Methylmethionine Homocysteine methylTransferase {ECO:0000313|EMBL:EDN59490.1}; GN Name=MHT1 {ECO:0000313|EMBL:EDN59490.1}; GN ORFNames=SCY_3523 {ECO:0000313|EMBL:EDN59490.1}; OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=307796 {ECO:0000313|EMBL:EDN59490.1, ECO:0000313|Proteomes:UP000007060}; RN [1] {ECO:0000313|EMBL:EDN59490.1, ECO:0000313|Proteomes:UP000007060} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YJM789 {ECO:0000313|EMBL:EDN59490.1, RC ECO:0000313|Proteomes:UP000007060}; 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. {ECO:0000313|EMBL:EDN59490.1}. 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; AAFW02000167; EDN59490.1; -; Genomic_DNA. DR ProteinModelPortal; A7A0J9; -. DR OrthoDB; EOG7X9GHR; -. DR Proteomes; UP000007060; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007060}; KW Methyltransferase {ECO:0000313|EMBL:EDN59490.1}; KW Transferase {ECO:0000313|EMBL:EDN59490.1}. SQ SEQUENCE 324 AA; 36729 MW; AD4F03CA4CC76284 CRC64; MKRIPIKELI IEHPGKVLIL DGGQGTELEN RGININSPVW SAAPFTSESF WEPSSQERKV VEEMYRDFMI AGANILMTIT YQANFQSISE NTSIKTLAAY KRFLDKIVSF TREFIGEERY LIGSIGPWAA HVSCEYTGDY GPHPENIDYY GFFKPQLENF NQNRDIDLIG FETIPNFHEL KAILSWDEDI ISKPFYIGLS VDDNSLLRDG TTLEEISVHI KGLGNKINKN LLLMGVNCVS FNQSALILKM LHEHLPGMPL LVYPNSGEIY NPKEKTWHRP TNKLDDWETT VKKFVDNGAR IIGGCCRTSP KDIAEIASAV DKYS // ID A7AL74_9PORP Unreviewed; 1231 AA. AC A7AL74; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 27-MAY-2015, entry version 46. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EDN84746.1}; GN Name=metH {ECO:0000313|EMBL:EDN84746.1}; GN ORFNames=PARMER_04199 {ECO:0000313|EMBL:EDN84746.1}; OS Parabacteroides merdae ATCC 43184. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Parabacteroides. OX NCBI_TaxID=411477 {ECO:0000313|EMBL:EDN84746.1, ECO:0000313|Proteomes:UP000004276}; RN [1] {ECO:0000313|EMBL:EDN84746.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43184 {ECO:0000313|EMBL:EDN84746.1}; 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 (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EDN84746.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43184 {ECO:0000313|EMBL:EDN84746.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EDN84746.1}. 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; AAXE02000112; EDN84746.1; -; Genomic_DNA. DR RefSeq; WP_005641530.1; NZ_DS264546.1. DR ProteinModelPortal; A7AL74; -. DR SMR; A7AL74; 649-892. DR EnsemblBacteria; EDN84746; EDN84746; PARMER_04199. DR PATRIC; 25877209; VBIParMer55919_3463. DR Proteomes; UP000004276; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000004276}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EDN84746.1}; KW Transferase {ECO:0000313|EMBL:EDN84746.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1231 AA; 135935 MW; 977E9548D4151ADC CRC64; MDKEIFLNLL KERILILDGG MGTMVQGFKL TEKDYRGKQF ADWMSDLKGN NDLLCITRPD VIKSIHRQYL DAGADIFATN TFNANAISME DYGMQGQVRN INLAAGKLAR EVADGFMKEH PDRTIFVAGS VGPTNKTASM SPDVSDPAYR AVTYLDLYSA YKEQVDALVD GGVDIVLFET TFDTLNVKAG LEAAEAVLKE KGKDLPIMLS LTLSAQGGRT FSGQTLLAFL ASVQHTNIVS VGLNCSFGAA DMKPFLAELA KHAPYYISAY PNAGLPNSFG SYDETPEKMA VHVKSFIDEG LVNILGGCCG TTPAHIAKYP ELVKGAKPHV PAPRPDCLWL SGLELLEVKP ENNFVNVGER CNVAGSRKFL RLIKEENYEE ALTIARKQVE DGAQVIDINM DDGMLDAVKE MTTFLNLIAS EPDISRVPVM IDSSKWEVIE KGLMCVQGKS IVNSISLKEG EEVFLQHAAR IKQLGAATVV MAFDEKGQAD TFERKIEVCG RAYRLLREKV DFDPNGIIFD PNVLAIATGM EEHNGYGLDF IRAVEWIKKN LPGAKVSGGV SNLSFSFRGN NYVREAMHSV FLYHAINKGM DMGIVNPSSS VLYEDIEPAF RMLLEDVILA CRPEAAEELI AYAQNLHVKA QEGEGEKQEV WREYPLKERL ENALIKGVGD HLEEDLKEAL KEYPRAVDII DGPLMGGMNK VGELFGAGKM FLPQVVKTAR TMKKAVAILQ PAIEAEKVSS DSAKAGKVLF ATVKGDVHDI GKNIVSIVLA CNNYEVIDLG VMVPADVIVK KAIEEKPDLV CLSGLITPSL EEMVHVTDEM QKAGLSIPIM VGGATTSKLH TAIKIAPHYD YPVIHVLDAS QNPLIAAKLL NPDTRDAYIA QLNSEYEALR ASVNKKKEIL VPLAEARTNR PVIDWASYNP VVPARNGVQV IPSIPLEEII PYIHWTFFFS AWKLNGRFSE IAQIHGCDAC RAAWLAEFSE ADRTKASEAM QLYKDAVKLL DRLVEMKAEY CKAVYGFFPA NGDGDNIRVG EVLLPVLRQQ AKKEEGIYKS LADYVMPVSE GRTDYVGAFV VTAGTGAESL KERFEQEGDT YNSMLLQTLT DRLAEATAEY LHEKVRKEYW GYAPDESLSI SDLYKVKYQG IRPAIGYPSL PDQLLNYTLD KLLNMSQIGV RLTENGAMYP TATVSGIYIA HPDSQYFMIG NIDEEQMKDY ACRRNLSEAE VKKLLNKNIS N // ID A7AYB8_RUMGN Unreviewed; 805 AA. AC A7AYB8; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 27-MAY-2015, entry version 38. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EDN79286.1}; GN ORFNames=RUMGNA_00283 {ECO:0000313|EMBL:EDN79286.1}; OS Ruminococcus gnavus ATCC 29149. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Blautia. OX NCBI_TaxID=411470 {ECO:0000313|EMBL:EDN79286.1}; RN [1] {ECO:0000313|EMBL:EDN79286.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29149 {ECO:0000313|EMBL:EDN79286.1}; 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 (APR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EDN79286.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29149 {ECO:0000313|EMBL:EDN79286.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDN79286.1}. 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; AAYG02000003; EDN79286.1; -; Genomic_DNA. DR RefSeq; WP_004840267.1; NZ_AAYG02000003.1. DR ProteinModelPortal; A7AYB8; -. DR EnsemblBacteria; EDN79286; EDN79286; RUMGNA_00283. DR PATRIC; 29782801; VBIRumGna65643_0227. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDN79286.1}; KW Transferase {ECO:0000313|EMBL:EDN79286.1}. SQ SEQUENCE 805 AA; 87774 MW; B3EA9C7D1967E8FD CRC64; MILERLGKEL LFFDGGMGTL LQAKGLLPGE LPETWNLTHA EAVRQIHRSY FEAGSDIVLT NTFGANALKF HDESCSLKEI IFSAVSHVKE AAKQGVRDNR EVYTALDIGP TGKLLKPMGD LEFETAYEAF KEVMIYGEQA GADLIHIETM SDTYELKAAV LAAKENTTLP VFVTTIFDER GKLLTGADVP SVVALLEGLR VDALGINCGM GPEQMMPILH EILEYTSLPV IVKPNAGLPK QRDGETYYDV EPEQFAKTME MIVETGACVI GGCCGTTPDH IRAMIAQCKD LLIKTPEKKV HTIVSSYGQA VMLGTGSRII GERINPTGKK KFKQALKDHD LDYILKEGIM QQDNGAHILD VNVGLPDIDE VSMMKEVITE LQSVTSLPLQ IDTVDIQAME QAMRIYNGKS MVNSVSGKQE SMDAVFPLIQ KYGGVVIGLT LDEDGIPETA DGRVAIAEKI IREAAKYGID KKDLVIDVLA MTVSSEPEGA KITLEALHRV RYDLGVNTVL GVSNISFGLP GRPIINANFY TMAMFQGLSA GIINPASEDM MRSYYAYHVL MNLDPNCENY IGRYGSANVE FASAPGSITT GAGRTAGGMM TLQAAIEKGL KEEAHQITNV LMQEKKPLDI INEHLIPALD TVGKGFEKGT VFLPQLLMSA EAAKTAFAVL KEGLENSGDV QEKKEKIVLA TVKGDIHDIG KNIVKVLLEN YSFEVVDLGK DVPPETIVDT VVAQQIRLVG LSALMTTTVV SMEETIRQLR EKAPWCKVMV GGAVLNQEYA DMIGADFYGK DAMQSVYYAQ GLLQQ // ID A7C1C8_9GAMM Unreviewed; 157 AA. AC A7C1C8; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=5-methyltetrahydrofolate--homocysteine S-methyltransferase {ECO:0000313|EMBL:EDN67406.1}; GN ORFNames=BGP_4439 {ECO:0000313|EMBL:EDN67406.1}; OS Beggiatoa sp. PS. OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Thiotrichaceae; Beggiatoa. OX NCBI_TaxID=422289 {ECO:0000313|EMBL:EDN67406.1}; RN [1] {ECO:0000313|EMBL:EDN67406.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PS {ECO:0000313|EMBL:EDN67406.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDN67406.1}. 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; ABBZ01001377; EDN67406.1; -; Genomic_DNA. DR ProteinModelPortal; A7C1C8; -. DR EnsemblBacteria; EDN67406; EDN67406; BGP_4439. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDN67406.1}; KW Transferase {ECO:0000313|EMBL:EDN67406.1}. SQ SEQUENCE 157 AA; 17742 MW; 82708F464D1ED768 CRC64; MSTTDTIQSL LEQRILILDG AMGTMIQQHK LEEEDYRGER FKKWTCDLKG NNDLLSLTQP HIIKEIHTQY LEAGADIIET NTFNATRIAM ADYRMEELVY ELNVAGAKLA REAADEMAQK HQTNHALSPV CWAQPIALAP CLLMSITRLF AILPLIS // ID A7EH16_SCLS1 Unreviewed; 369 AA. AC A7EH16; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 27-MAY-2015, entry version 38. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EDO02132.1}; GN ORFNames=SS1G_04608 {ECO:0000313|EMBL:EDO02132.1}; 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 {ECO:0000313|Proteomes:UP000001312}; RN [1] {ECO:0000313|Proteomes:UP000001312} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312}; 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; CH476625; EDO02132.1; -; Genomic_DNA. DR RefSeq; XP_001594800.1; XM_001594750.1. DR ProteinModelPortal; A7EH16; -. DR STRING; 665079.A7EH16; -. DR EnsemblFungi; EDO02132; EDO02132; SS1G_04608. DR GeneID; 5490382; -. DR KEGG; ssl:SS1G_04608; -. DR EuPathDB; FungiDB:SS1G_04608; -. DR eggNOG; COG2040; -. DR InParanoid; A7EH16; -. DR KO; K00547; -. DR OMA; WHHERIS; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000001312; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001312}; KW Reference proteome {ECO:0000313|Proteomes:UP000001312}. SQ SEQUENCE 369 AA; 40844 MW; 8C88DE59211F3DDA CRC64; MSSECKIHLL DGGLGTTLGD SHQVQFTEKE PLWSSQLLIP THPHGPNTLL ATQKSFVDAG ADILLTATYQ ASYEGFGRSG YAVHSHSSSG FEKEDGDKEE VNEIMRSAVD IASNAFSVKK DSNGKIALSL GAYGAIMTPG QEYTGKYDDQ HKSSEHLSSW HHERISVFSR DPKSWDRVDY VAFETIPLLE EIEGVRKSMG EIERSNGGKT GSKPFWVTCV FPGEGNGLPD GSSVQQIVQA MLSKKEGSPV PFGVGLNCTK VGKVEALILD FEREVRSLIE KGDVSEWPSL VVYPDGTIKG EVYNTSTKVW EIREPPGKED LQWDEAVLEI VRRTRDRGLW KEIIVGGCCK TTPREIGKLR ERIDRLIKE // ID A7FDG4_YERP3 Unreviewed; 1230 AA. AC A7FDG4; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 27-MAY-2015, entry version 61. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABS46120.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABS46120.1}; GN Name=metH {ECO:0000313|EMBL:ABS46120.1}; GN OrderedLocusNames=YpsIP31758_0298 {ECO:0000313|EMBL:ABS46120.1}; OS Yersinia pseudotuberculosis serotype O:1b (strain IP 31758). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=349747 {ECO:0000313|EMBL:ABS46120.1, ECO:0000313|Proteomes:UP000002412}; RN [1] {ECO:0000313|EMBL:ABS46120.1, ECO:0000313|Proteomes:UP000002412} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IP 31758 {ECO:0000313|EMBL:ABS46120.1, RC ECO:0000313|Proteomes:UP000002412}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000720; ABS46120.1; -; Genomic_DNA. DR RefSeq; WP_012104349.1; NC_009708.1. DR RefSeq; YP_001399292.1; NC_009708.1. DR ProteinModelPortal; A7FDG4; -. DR SMR; A7FDG4; 654-1230. DR STRING; 349747.YpsIP31758_0298; -. DR EnsemblBacteria; ABS46120; ABS46120; YpsIP31758_0298. DR KEGG; ypi:YpsIP31758_0298; -. DR PATRIC; 18629116; VBIYerPse15693_0524. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; YPSE349747:GH71-312-MONOMER; -. DR Proteomes; UP000002412; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002412}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABS46120.1}; KW Transferase {ECO:0000313|EMBL:ABS46120.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 251 251 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 315 315 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 762 762 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1230 AA; 136029 MW; F82851B068DF2531 CRC64; MDTVIDNKVK ELHQQLAQRI LVLDGGMGTM IQSYRLEEAD YRGARFADWA SDLKGNNDLL VLSKPEVITA IHNAYLEAGA DILETNTFNS TSIAMADYQM ASLSAEINYE AARLARVCAD EWSARTPEKP RYVAGVLGPT NRTASISPKV NDPAFRNVSF DQLVEAYRES TRALIEGGVD LIMIETVFDT LNAKAATFAV ESEFEAMGVL LPVMISGTIT DASGRTLSGQ TTEAFYNSLR HVKPLSFGLN CALGPDELRQ YVAELSRISE YYVSAHPNAG LPNAFGEYDL EAKEMAEQIG EWARAGFLNI VGGCCGTTPR HIAAMVNAVA GVPPRPLPDI PVACRLAGLE PLTIDANTLF VNVGERTNVT GSARFKRLIK EEKYGEALDV ARQQVESGAQ IIDINMDEGM LDAEAAMVRF LNLIAGEPDI ARVPIMIDSS RWDVIEKGLK CIQGKGIVNS ISMKEGVDAF IHHAKLVRRY GAAMVVMAFD ETGQADTRAR KIEICRRAYK ILTETVGFPP EDIIFDPNIF AVATGIEEHN NYAVDFIEAC ADIKAELPHA LISGGVSNVS FSFRGNDPVR EAIHAVFLYY AIRNGMDMGI VNAGQLAIYD DLSDELRDAV EDVILNRRDD STERLLDLAE KYRDSKSGEV AIQQAEWRGW SVVKRLEYSL VKGITEFIEL DTEEARQQAD RPIEVIEGPL MSGMNVVGDL FGEGKMFLPQ VVKSARVMKQ AVAYLEPYIE ASKQKGTTAG KILLATVKGD VHDIGKNIVG VVLQCNNYEI IDLGVMVPTE KILRTAREEK VDIIGLSGLI TPSLDEMVNV AKEMERQGFT LPLLIGGATT SKAHTAVKIE QNYSGSTTYV SNASRSVGVV SALLSDTQRE AFVAKTRKEY ETVRIQHARK KPRTPPVSLQ AARNNPTVID WENYTPPVAH KLGVQVVEAS IETLRNYIDW TPFFMTWSLA GKYPRILEDE VVGEEAKRLL ADANALLDKL SAEDLLHPKG VVGLFPANSV GDDIEIYRDE RRDEVLAISY HLRQQTEKTD FPNYCLADYV APKSSGKADY FGAFAVTGGL EEDALADAYD AQRDDYNKIM IKALSDRLAE AFAEYLHERV RKVYWGFAPN ENLSNEELVR ENYQGIRPAP GYPACPEHTE KGQIWQLLDV ETHTGMKLTE SYAMWPGASV SGWYFSHPDS KYFAVAQIQR DQVEDYAARK GMPIAEVERW LAPNLGYDAD // ID A7GDV1_CLOBL Unreviewed; 792 AA. AC A7GDV1; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 27-MAY-2015, entry version 51. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:ABS41889.1}; GN OrderedLocusNames=CLI_1701 {ECO:0000313|EMBL:ABS41889.1}; OS Clostridium botulinum (strain Langeland / NCTC 10281 / Type F). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=441772 {ECO:0000313|EMBL:ABS41889.1, ECO:0000313|Proteomes:UP000002410}; RN [1] {ECO:0000313|Proteomes:UP000002410} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Langeland / NCTC 10281 / Type F RC {ECO:0000313|Proteomes:UP000002410}; 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 ----------------------------------------------------------------------- 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; ABS41889.1; -; Genomic_DNA. DR RefSeq; WP_012099714.1; NC_009699.1. DR RefSeq; YP_001390961.1; NC_009699.1. DR ProteinModelPortal; A7GDV1; -. DR STRING; 441772.CLI_1701; -. DR EnsemblBacteria; ABS41889; ABS41889; CLI_1701. DR KEGG; cbf:CLI_1701; -. DR PATRIC; 19426357; VBICloBot15611_1620. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CBOT441772:GJIE-1677-MONOMER; -. DR Proteomes; UP000002410; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002410}; KW Methyltransferase {ECO:0000313|EMBL:ABS41889.1}; KW Transferase {ECO:0000313|EMBL:ABS41889.1}. SQ SEQUENCE 792 AA; 87762 MW; 0471361B51A7703D CRC64; MNIKDYIKEN VLIFDGAMGT MLQKLGLKIS DLPEELNILE PEKIINIHRK YIEAGAKVIT TNTFGANEIK LKQSKFSLET IIDKAIDNVK KAGKNEEILI ALDIGPIGQL LEPMGTLRFE EAYEIFKRQI VQGQKSGADI VLIETMTDLY EAKAAILAAK ENTNLPVFCT MTFEKNKRTF TGCTPLSMVL TLEGLGVDAL GVNCSLGPNE LGDIVDEIIK YSSIPIMVQP NAGLPTIKAG RTIYNIKPKE FADFQRSIVE KGVRIVGGCC GTTDEFIREI VYSLKDAKIK KLKEKNICGV CSSTKSVLIE GVKIIGERIN PTGKKLFKEA LRNNDTDYIL KEAISQVECG ADILDVNVGL PEINEEETMK KVIKEIQSII DTPLQIDSNN SKVIEKALRI YNGKAIVNSV NGEEEVLDSV LPLIKKYGAA VVGLTLDDKG IPKKAEERLK VAEKIVNKAL EYGIRREDVF IDCLVLTASA QQEDVTETLK AVNLVKEKLN VKTILGVSNI SFGLPNRELI NKTFLAMSLQ SGLDLPILNP NNKEMINIIN AYKVLNNEDK GAANYIERYT NEISNSREVK IKKNDLTLKE IVIKGIKEES YSKTKDLLKY RGELSIINEE LIPALDEVGD KYEKGIIFLP QLIQSAETVK KAFTAIKEKL REDNSPKISK GKILMATVKG DIHDIGKNIV KVILENYGFD IIDLGKDVES EKVVEEVKKN NIKLVGLSAL MTTTVNSMRD TIKILKESGM DCKVFVGGAV LNEEYAKMIN ADYYAKDAKE AVDIAKGFFG GF // ID A7GSV2_BACCN Unreviewed; 1132 AA. AC A7GSV2; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 27-MAY-2015, entry version 66. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABS23210.1}; GN OrderedLocusNames=Bcer98_2983 {ECO:0000313|EMBL:ABS23210.1}; OS Bacillus cereus subsp. cytotoxis (strain NVH 391-98). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=315749 {ECO:0000313|EMBL:ABS23210.1, ECO:0000313|Proteomes:UP000002300}; RN [1] {ECO:0000313|EMBL:ABS23210.1, ECO:0000313|Proteomes:UP000002300} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NVH 391-98 {ECO:0000313|EMBL:ABS23210.1, RC ECO:0000313|Proteomes:UP000002300}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000764; ABS23210.1; -; Genomic_DNA. DR RefSeq; WP_012095445.1; NC_009674.1. DR RefSeq; YP_001376205.1; NC_009674.1. DR ProteinModelPortal; A7GSV2; -. DR STRING; 315749.Bcer98_2983; -. DR EnsemblBacteria; ABS23210; ABS23210; Bcer98_2983. DR KEGG; bcy:Bcer98_2983; -. DR PATRIC; 18934586; VBIBacCyt128034_3137. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; BCYT315749:GH2A-3091-MONOMER; -. DR Proteomes; UP000002300; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002300}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002300}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 126437 MW; F7517D9934A2F8CB CRC64; MRRIEERLQQ EILILDGAMG TMIQQADLTA DDFGGEEYEG CNEYLVKTRP DLILNIHKAY IDAGADIIET NTFGATNIVL SDYKLSHLDE ELNERAALLA RQAVKESQKE VYVAGAMGPT TKAISVTGGV TFDELMEAYT RQARGLLRGG VDLLLIETSQ DMRNVKAAYL GIQNAFEQLH QTVPLMISGT IEPMGTTLAG QTIEAFYLSV EHMNPLSVGL NCATGPEFMR EHIRSLSELS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KSFAEEGWIN IIGGCCGTTP EHIRAIKETL ASCKPRQYDE RAGHGISGLE ALQYDDSMRP LFVGERTNVI GSRKFKRLVA EGNFEEAAEI ARAQVKKNAH IIDICMADPD RDEVEDMENF LAEVTKVLKV PIMIDSTDEK VMAKALTYIQ GKGVINSINL ENGEERFEQV TPLIRKYGAA IVVGTIDEEG MAVRAERKLE IAKRSYELLT KKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPEE EKKLADALLF ETSKETLEEF TNFYRSAKKK DVLVQETLTL DERLANYIVE GTKQGLQDDI SCALKEGRKP LDIINGPLMA GMDEVGRLFN NNELIVAEVL QSAESMKAAV AYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVDIILS NNGYEIINLG INVRSDRIVQ EVKEKKPDII GLSGLLVKSA QQMVKTAEDL KAANINIPIV VGGAALTRKF TDNRISPSYD GLVLYASDAM TGLDIMNRLQ KEEEREKMKQ NKKERHLHVV KQEEKKVEIP AVIEPLSKAK VMVPDSTKRV VLRDIPVSHL SPFLNRQMLI GHHLGLRGNV KKLLREGDKR AHELNDLIDE LLQEEQSWLR PKAIYQFFPA QSDGQTIIIY DPEDHTRVLE RFSFPRQMKA PYRTLGDYLR PVGEEMDYVA FLSVTVGEGV RNVAEEWKRK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDAPEM TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID A7GSV3_BACCN Unreviewed; 614 AA. AC A7GSV3; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 27-MAY-2015, entry version 55. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=Bcer98_2984 {ECO:0000313|EMBL:ABS23211.1}; OS Bacillus cereus subsp. cytotoxis (strain NVH 391-98). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=315749 {ECO:0000313|EMBL:ABS23211.1, ECO:0000313|Proteomes:UP000002300}; RN [1] {ECO:0000313|EMBL:ABS23211.1, ECO:0000313|Proteomes:UP000002300} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NVH 391-98 {ECO:0000313|EMBL:ABS23211.1, RC ECO:0000313|Proteomes:UP000002300}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ABS23211.1; -; Genomic_DNA. DR RefSeq; WP_012095447.1; NC_009674.1. DR RefSeq; YP_001376206.1; NC_009674.1. DR ProteinModelPortal; A7GSV3; -. DR STRING; 315749.Bcer98_2984; -. DR EnsemblBacteria; ABS23211; ABS23211; Bcer98_2984. DR KEGG; bcy:Bcer98_2984; -. DR PATRIC; 18934588; VBIBacCyt128034_3138. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; BCYT315749:GH2A-3092-MONOMER; -. DR Proteomes; UP000002300; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002300}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ABS23211.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000002300}; KW Transferase {ECO:0000313|EMBL:ABS23211.1}. SQ SEQUENCE 614 AA; 67690 MW; F063756F49C1BD0C CRC64; MKLLDLLSKG IVIGDGAIGT LLHSHGLQSS FEELNISDPD LIVSIHKQYV AAGADVIQTN TYGANEAKLR TYGLENQVVQ INRAAVKLAK AAAKEQNAIL GTIGGMKHIG AVTTTNIERE FMLLEQAGAL IEEEVDGLLL ETFYDEFELI HAIKVLRKQT DIPIVAQLAL HEAGTTQNGN DVNEILAQLI HNGANVVGLN CQLGPLPMTE ALKMISIPKD GYLSAYPNAG LPNYIEGRYI YEGSPAYFET MTPKFIEQGV RLLGGCCGTT PAHIERMKRA IANQVPVIEK TVVSRPPILH THSERFRTHS TLAEKAKKQT TVVVELDPPK TLDTQRFFEG AKALKRAGAD AITLADNSLA SPRISNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSVLGMEEVL ALTGDPARVG DFPGATSVYD VSSIELIKMI QEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIAAGAEY FLTQPIYDKA LIYEVYKETK HLEQPIFIGI MPLVSKRNAD FLHFEVPGIT LPDQVRERMR EHETEADAIE EGISIAQELI DEALKYFRGI YLITPFLKYE ITEHLVKYIK EKQEVREEVT NETN // ID A7H6G1_ANADF Unreviewed; 1149 AA. AC A7H6G1; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 27-MAY-2015, entry version 63. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABS24307.1}; GN OrderedLocusNames=Anae109_0087 {ECO:0000313|EMBL:ABS24307.1}; OS Anaeromyxobacter sp. (strain Fw109-5). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter. OX NCBI_TaxID=404589 {ECO:0000313|EMBL:ABS24307.1, ECO:0000313|Proteomes:UP000006382}; RN [1] {ECO:0000313|Proteomes:UP000006382} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Fw109-5 {ECO:0000313|Proteomes:UP000006382}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000769; ABS24307.1; -; Genomic_DNA. DR RefSeq; WP_011984413.1; NC_009675.1. DR RefSeq; YP_001377291.1; NC_009675.1. DR ProteinModelPortal; A7H6G1; -. DR STRING; 404589.Anae109_0087; -. DR EnsemblBacteria; ABS24307; ABS24307; Anae109_0087. DR KEGG; afw:Anae109_0087; -. DR PATRIC; 20925215; VBIAnaSp113478_0095. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; ASP404589:GHMT-89-MONOMER; -. DR Proteomes; UP000006382; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006382}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006382}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 733 733 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1149 AA; 124197 MW; 1E7B4EAE7F697A08 CRC64; MTFREAIDRR PLVFDGAMGT QIQRHQLTAA EFGGKDGAND LLTLTRPDLV EDIHARYFAV GCDVVETNTF GSSRLKLDEY GLGHRTYEVN FRAAILARRA AERFATPDHP RFVAGSMGPT GMLPSSSDPA LGNITSDALE RIFFEQAKGL IEGGVDALII ETQQDMLELR AAVLAADACR KEFLRDVFII AQPTLIDANG RMLLGTDVAS ALATLERLPV DAVGLNCSTG PAEMRAAVRT LAEKSSHYVS VLPNAGMPEN EDGRAVYKLS PAALADALAG FVAEYGVELV GGCCGTTPEH MRAVVERVRG LRAPRRARPA PAPELSSAMK AVPLAMEPRP LIVGERLNSQ GSKKVKELLL ADDYAGLLQI ARGQVDAGAH VLDVCVALNE RDDEGAQMRT LAKLLAQAVD APLMIDSTEA DVVEGALKVY PGRCIVNSVN LEKSGERVRK ILPLVRRYGA AVVAMTIDEK GMAQTAERKA EIARRTVAIA RDHGIPPDSL VFDALTFTLA TGGEEYRKSA IETLEGIRRI KAENPGVLTT LGVSNVSFGL AKSAREVVNS VFLYHAVQAG LDLAIVNPKD IRPYPAIAEE ERVLAEDLLL DRRPDALARL IAHFGAKGAP EKAAVDPLAA AGGKSAEERI HLQILHRRPE GIEALIDDAL TRRSAVEVLN QVLLPAMKDV GDRFGAGELI LPFVLQSAEV MKKAVAHLEQ FLEKKEGATK GTVVLATVYG DVHDIGKNLV KTILANNGFT VHDLGKQVPI ATVIEKAVAA NADAIGLSAL LVSTSKQMPF CVEELARRNL SFPVIIGGAA INRRFGYRAL FTQGGAPYPG GVFYAKDAFE GLEVVEALVD PARREGLKQG VLQKAIANRD MPASPVPPPA PARRSGVAPA LRIPSPPFWG ARVVPAGEIA LAELWPLLDL PELFKLQWGV KAKGEEYERL IREQFGPKLE ELKAEAQANG WLVPKVVYGY FPCHAEGNDL VVLDPTHRKA EVARLVLPRQ PDDRNLCMAD WFREERGSDV CALQVVTVGD QATHLAEAAQ ERGDYSRGLF VHGLAVEAAE ALAEYWHRRV RAELGVPEGQ GKRYSPGYPS WPELADQRQV WKLLEPDRTI GVSLTEANQM VPEASTSAIV LHHPDAIYFV VRGATAAAV // ID A7HBZ7_ANADF Unreviewed; 280 AA. AC A7HBZ7; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 27-MAY-2015, entry version 38. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABS26243.1}; GN OrderedLocusNames=Anae109_2040 {ECO:0000313|EMBL:ABS26243.1}; OS Anaeromyxobacter sp. (strain Fw109-5). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter. OX NCBI_TaxID=404589 {ECO:0000313|EMBL:ABS26243.1, ECO:0000313|Proteomes:UP000006382}; RN [1] {ECO:0000313|Proteomes:UP000006382} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Fw109-5 {ECO:0000313|Proteomes:UP000006382}; 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 ----------------------------------------------------------------------- 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; ABS26243.1; -; Genomic_DNA. DR RefSeq; WP_012096821.1; NC_009675.1. DR RefSeq; YP_001379227.1; NC_009675.1. DR ProteinModelPortal; A7HBZ7; -. DR STRING; 404589.Anae109_2040; -. DR EnsemblBacteria; ABS26243; ABS26243; Anae109_2040. DR KEGG; afw:Anae109_2040; -. DR PATRIC; 20929335; VBIAnaSp113478_2141. DR eggNOG; NOG330803; -. DR HOGENOM; HOG000265278; -. DR KO; K00548; -. DR OMA; VLTCTFN; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; ASP404589:GHMT-2055-MONOMER; -. DR Proteomes; UP000006382; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006382}; KW Methyltransferase; KW Reference proteome {ECO:0000313|Proteomes:UP000006382}; Transferase. SQ SEQUENCE 280 AA; 27644 MW; 4D0AB15FB76857B6 CRC64; MTSLHEAPGA PTLLDGGMGT ALVARGLPQG ALPEEWLLAR PDAIAEVHAD HARAGAEIVL TCTFNLAAPR LAQRLDPPRV EELAAIAVRL ARGAAPGARV AGALGPTGLA APGRPAPIRS LAAGYGRAAR ALAAAGADLL WLETQHDRAE ARLALVAARA TGLDAVVTFT ALGDGATLSD GTSVEEALLA MASLGASAVG VNCGAPGAAL GALAAWAKAT LPVPFVAKPS PGLPGAVRSP DAFAAELRPA LAAGVALVGG CCGASGDHLR ALAAGWRAPR // ID A7HL42_FERNB Unreviewed; 780 AA. AC A7HL42; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 27-MAY-2015, entry version 53. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABS60625.1}; GN OrderedLocusNames=Fnod_0772 {ECO:0000313|EMBL:ABS60625.1}; OS Fervidobacterium nodosum (strain ATCC 35602 / DSM 5306 / Rt17-B1). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; OC Fervidobacterium. OX NCBI_TaxID=381764 {ECO:0000313|EMBL:ABS60625.1, ECO:0000313|Proteomes:UP000002415}; RN [1] {ECO:0000313|EMBL:ABS60625.1, ECO:0000313|Proteomes:UP000002415} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35602 / DSM 5306 / Rt17-B1 RC {ECO:0000313|Proteomes:UP000002415}; 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., Mikhailova N., Nelson K., Gogarten J.P., Noll K., RA Richardson P.; RT "Complete sequence of Fervidobacterium nodosum Rt17-B1."; 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; CP000771; ABS60625.1; -; Genomic_DNA. DR RefSeq; WP_011993942.1; NC_009718.1. DR RefSeq; YP_001410282.1; NC_009718.1. DR ProteinModelPortal; A7HL42; -. DR STRING; 381764.Fnod_0772; -. DR EnsemblBacteria; ABS60625; ABS60625; Fnod_0772. DR KEGG; fno:Fnod_0772; -. DR PATRIC; 21882997; VBIFerNod12464_0809. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; FNOD381764:GC5M-792-MONOMER; -. DR Proteomes; UP000002415; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002415}; KW Methyltransferase {ECO:0000313|EMBL:ABS60625.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002415}; KW Transferase {ECO:0000313|EMBL:ABS60625.1}. SQ SEQUENCE 780 AA; 86388 MW; 8633BAEBE6093050 CRC64; MTRSEFHVLI SERVLFLDGA YGTEFFKRGY IKGKEPIEIL NVKAPEKVLE LQSEYVKAGV DFLLTNTFSG NRHKLKKLGY ENYFEQINSE AVRIAKEAAK HSEKKVYILG DMSSVGEMIQ PIGDLDSKYV YNIFKEQAKV LIESGVDGII IETMSDLKEL KLAYLAVRDV SEDIPLFVSM TFEENSVAVT GTSLEVYVSL FNDLDVDAIG INCTLTPDKM VPLVKKLSIF SKKPIFAEPN AGKPTLSADG RLIYKTTPEE FTVYIEDYVE LGANIVGGCC GTGPDHIRYM TKLIGERKPK ARKTEELNVI TNRTYMVEVS PFLVIGERIN AAAKKKLHAQ IREFNFENVL KLAKDQEKEG AQVLDVNLGL ESVLSDEHFR RIIVELDRIV SLPLSLDIQF NEYLEVALFE YPGRAIINSA KAIKEDLDAK IRMLKRYGGI LIILAMGKEI PNSPEERYKT AKDAVEYAEK NGIDRSRIFV DPLVLPLGAN QDYNVTLETI KLLNKEGIKT SIGLSNFSFG MPNREQLNAS FLALAMHYGL SGAILNTSEV TTVNILSGMK KILKKESTNV SVEDVDNDLA KLLLAGDGVN AEKQIMAYLD SMKPIEVAQN VLTKSMEVIG NLYAQNKIFL PHLILAAETV KPIFNKLLSM IEEKDSAKLG RVLLATVEGD IHDIGKKIVA TVLESAGFEV IDIGKDVPAK AILEKVKEFN PDIVGLSAMM TTTVVQVGEV VKTLRNNGVT VPVIAGGASM NEDLAKRFGS LYAKDAQQAV EICKELVSKT // ID A7HS45_PARL1 Unreviewed; 313 AA. AC A7HS45; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 27-MAY-2015, entry version 34. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABS62728.1}; GN OrderedLocusNames=Plav_1107 {ECO:0000313|EMBL:ABS62728.1}; OS Parvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhodobiaceae; Parvibaculum. OX NCBI_TaxID=402881 {ECO:0000313|EMBL:ABS62728.1, ECO:0000313|Proteomes:UP000006377}; RN [1] {ECO:0000313|Proteomes:UP000006377} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DS-1 / DSM 13023 / NCIMB 13966 RC {ECO:0000313|Proteomes:UP000006377}; 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; ABS62728.1; -; Genomic_DNA. DR RefSeq; WP_012109984.1; NC_009719.1. DR RefSeq; YP_001412385.1; NC_009719.1. DR ProteinModelPortal; A7HS45; -. DR STRING; 402881.Plav_1107; -. DR EnsemblBacteria; ABS62728; ABS62728; Plav_1107. DR KEGG; pla:Plav_1107; -. DR PATRIC; 22863800; VBIParLav90819_1140. DR eggNOG; COG2040; -. DR HOGENOM; HOG000179103; -. DR OMA; CCGTDHR; -. DR OrthoDB; EOG6R5C46; -. DR BioCyc; PLAV402881:GHQA-1120-MONOMER; -. DR Proteomes; UP000006377; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006377}; KW Methyltransferase {ECO:0000313|EMBL:ABS62728.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006377}; KW Transferase {ECO:0000313|EMBL:ABS62728.1}. SQ SEQUENCE 313 AA; 33996 MW; FD24EB5DBB80A39C CRC64; MTKYRNRLPQ TQGGLFLSDG GIETTLIFED GFELPYFAAF HLLQDQAGTE GLRAYFRRHA KIAVDARTGF ILESPTWRAS PDWGQKLGYT LEALDAANRV ALRLMHELRA EFETPSSPMV ISGCVGPRGD GYIAGEAMSP EEAEAYHARQ IRLYAEEGAD MATAITMTNV NEAVGVTRAA KAAGLPVAIS FTVETDGTLP AGDRLGDAIA AVDAATGRTP AYYMINCAHP DHFDAVLKGE WVKRIGGIRA NASRCSHAEL NEAEELDFGN PQELGQQYRD LRARFPQINV MGGCCGTDHR HIEAISSACL ETA // ID A7HVS8_PARL1 Unreviewed; 353 AA. AC A7HVS8; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 27-MAY-2015, entry version 41. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABS64011.1}; GN OrderedLocusNames=Plav_2402 {ECO:0000313|EMBL:ABS64011.1}; OS Parvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhodobiaceae; Parvibaculum. OX NCBI_TaxID=402881 {ECO:0000313|EMBL:ABS64011.1, ECO:0000313|Proteomes:UP000006377}; RN [1] {ECO:0000313|Proteomes:UP000006377} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DS-1 / DSM 13023 / NCIMB 13966 RC {ECO:0000313|Proteomes:UP000006377}; 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; ABS64011.1; -; Genomic_DNA. DR RefSeq; WP_012111320.1; NC_009719.1. DR RefSeq; YP_001413668.1; NC_009719.1. DR ProteinModelPortal; A7HVS8; -. DR STRING; 402881.Plav_2402; -. DR EnsemblBacteria; ABS64011; ABS64011; Plav_2402. DR KEGG; pla:Plav_2402; -. DR PATRIC; 22866513; VBIParLav90819_2479. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; PLAV402881:GHQA-2429-MONOMER; -. DR Proteomes; UP000006377; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006377}; KW Methyltransferase {ECO:0000313|EMBL:ABS64011.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006377}; KW Transferase {ECO:0000313|EMBL:ABS64011.1}. SQ SEQUENCE 353 AA; 38076 MW; E0664DAE7F6E445F CRC64; MTREERIEKL KALSKERILV LDGAMGTMIQ GYKLTEADYR GELLKDHASD VKGDNELISL AQPDILREIH LKYYRAGADF AETNTFGATS IAQADYHLEH LAYQMNVESA RIAREAADIA ESETPGRVCF VAGVLGPTNR TASISPKVND PGFRNVNFDQ LVESYKEATK GLIEGGADTI LVETIFDTLN AKAALFAIEE VFDELGFELP IMISGTITDM SGRLLSGQTP EAFWNSVRHV KPFSIGLNCA LGAKEMRPHV ATLSRIADAG VSAHPNAGLP NEMGEYDQDA AQMSALVGEF AKSGLVNIVG GCCGTTPEHI HAIAEAVKGA TPRAKPEIEP RLRLSGLEAF TAA // ID A7IJ79_XANP2 Unreviewed; 1271 AA. AC A7IJ79; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 27-MAY-2015, entry version 58. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABS68072.1}; GN OrderedLocusNames=Xaut_2832 {ECO:0000313|EMBL:ABS68072.1}; OS Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Xanthobacteraceae; Xanthobacter. OX NCBI_TaxID=78245 {ECO:0000313|EMBL:ABS68072.1, ECO:0000313|Proteomes:UP000002417}; RN [1] {ECO:0000313|EMBL:ABS68072.1, ECO:0000313|Proteomes:UP000002417} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1158 / Py2 {ECO:0000313|Proteomes:UP000002417}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000781; ABS68072.1; -; Genomic_DNA. DR RefSeq; WP_012114823.1; NC_009720.1. DR RefSeq; YP_001417729.1; NC_009720.1. DR ProteinModelPortal; A7IJ79; -. DR SMR; A7IJ79; 684-1263. DR STRING; 78245.Xaut_2832; -. DR EnsemblBacteria; ABS68072; ABS68072; Xaut_2832. DR KEGG; xau:Xaut_2832; -. DR PATRIC; 24047763; VBIXanAut29526_3166. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; XAUT78245:GHS6-2860-MONOMER; -. DR Proteomes; UP000002417; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002417}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002417}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 278 278 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 341 341 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 342 342 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 794 794 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1271 AA; 138317 MW; 60B55C654EDBEA9E CRC64; MSCFRPATDV HLFHRGCPKP RALRTSAMTE TRAADTFSAL AQAASERILV LDGAMGTMIQ GLKLDEAGYR GARFADWPRD VKGNNDLLSL TQPDAVRAIH LEYFRAGADM VETNTFSGTS IAQADYGMEE LVYELNFESA RLAREAGDIA QAEDGRPRFV AGAFGPTNRT ASISPDVNDP GFRAVTFDDL AGAYHEQARG LVDGGADILL VETIFDTLNA KAAIFAIEQL FAERGIRLPV MISGTITDLS GRTLSGQTPA AFWYSLQHAR PFSIGLNCAL GAREMRAHVA EIGRVADTLV CAYPNAGLPN EFGMYDESPQ AMAELVGEFA ASGLVNIVGG CCGTTPAHIR AIAEAVKGKA PRVVPQIEPR LRLSGLEPFE LTPEIPFVNV GERTNVTGSA RFRKLITTGD FAAALAVARD QVESGAQVID INMDEGLLDS EAAMVTFLNL VAAEPDIAKV PVMVDSSKWE IIEQGLKRLQ GKGIVNSISM KEGEDAFREK ARLVRSYGAA VVVMAFDEEG QADTFERKTQ ICARAYRILT EELAFPPEDI IFDPNIFAVA TGIEEHAGYG VAFIEATRWI RQNLPHAHVS GGVSNLSFSF RGNEPVREAM HAVFLYHAIQ AGMDMGIVNA GQLAVYDEIE PGLREACEDV VLNRRPDATE RLLEIAEGFK GAAGKEKKEA DLAWRSWPVD KRLAHALVNG ITDFVEADTE EARQSVARPL HVIEGPLMAG MNVVGDLFGA GKMFLPQVVK SARVMKQAVA YLMPFMEKEK EEMGVTSASA AGKVLMATVK GDVHDIGKNI VGVVLQCNNY EVIDLGVMVP MAKILETAKA EKVDVIGLSG LITPSLDEMV NVAAEMEREG FSLPLLIGGA TTSRVHTAVK ISPRYERGQA VYVTDASRAV GVVSSLLNKD TRGAYVADIR AEYRKLAEAH ARADANKQRV PLAKARDNAL KLDFSAYEVP RPGFLGTQMI EDHDLADLVP FIDWTPFFQS WELTGRYPAI LEDQVVGEPA RALFADAQAM LEKMVAEKWV SARAVVGFWP ANAMGDDIVL FRDDTRKTPL ATLHTLRQQL AKRDGRFNLA LSDFVAPLET GVADYVGGFA VTTGIGEEER VAAFKAANDD YSAILLKALC DRLAEAFAER LHHLVRTRLW GYAADEALAN DDLIAERYRG IRPAPGYPAQ PDHTEKATIF RLLDATHKAG IQLTESFAMW PGAAVSGLYF AHPESAYFGV GRIERDQVED YAARKGWSVE EAEKWLAPIL NYDPAQVAAA E // ID A7LTW4_BACO1 Unreviewed; 915 AA. AC A7LTW4; DT 02-OCT-2007, integrated into UniProtKB/TrEMBL. DT 02-OCT-2007, sequence version 1. DT 27-MAY-2015, entry version 45. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EDO13020.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EDO13020.1}; GN Name=metH {ECO:0000313|EMBL:EDO13020.1}; GN ORFNames=BACOVA_01260 {ECO:0000313|EMBL:EDO13020.1}; 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 {ECO:0000313|EMBL:EDO13020.1}; RN [1] {ECO:0000313|EMBL:EDO13020.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 8483 {ECO:0000313|EMBL:EDO13020.1}; 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 (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EDO13020.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 8483 {ECO:0000313|EMBL:EDO13020.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EDO13020.1}. 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; AAXF02000042; EDO13020.1; -; Genomic_DNA. DR RefSeq; WP_004296934.1; NZ_DS264560.1. DR ProteinModelPortal; A7LTW4; -. DR SMR; A7LTW4; 650-895. DR EnsemblBacteria; EDO13020; EDO13020; BACOVA_01260. DR PATRIC; 27040071; VBIBacOva42630_1143. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EDO13020.1}; KW Transferase {ECO:0000313|EMBL:EDO13020.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 915 AA; 100049 MW; A52BB64348C516CF CRC64; MKKTISQIVS ERILILDGAM GTMIQQYNLK EEDFRGERFA HIPGQLKGNN DLLCLTRPDV IQDIHRKYLE VGADIIETNT FSSTTVSMAD YHVEEYVREM NLAAVKLARD LADEYTAKNP DKPRFVAGSV GPTNKTCSMS PDVNNPAYRA LSYDELAASY QQQMEAMLEG GVDAILIETI FDTLNAKAAI FAAEQAMKMT GIEVPIMLSV TVSDIGGRTL SGQTLDAFLA SVQHANIFSV GLNCSFGARQ LKPFLEQLAS RAPYYISAYP NAGLPNNLGK YDQTPADMAH EVREYIEEGL INIIGGCCGT TDAYIAEYPA LVEGAKPHVP ASAPDCMWLS GLELLEVKPE INFVNVGERC NVAGSRKFLR LINEKKYDEA LSIARQQVED GALVVDVNMD DGLLDAKTEM TIFLNLIMSE PEIARVPIMI DSSKWEVIEA GLKCLQGKSI VNSISLKEGE EVFLEHARII RQYGAAAVVM AFDEKGQADT AARKIEVCQR AYRLLVDKIG FNPHDIIFDP NVLAVATGIE EHNNYAVDFI EATAWIKKNL PGAHISGGVS NLSFSFRGNN YIREAMHAVF LYHAIQQGMD MGIVNPGTSV LYTDIPADVL EKIEDVVLNR RPDAAERLIE LAESLKANMS ETAGQPAVKQ DAWREGTVQE RLKYALMKGI GDFLEQDLAE ALPLYDKAVD VIEGPLMDGM NHVGELFGAG KMFLPQVVKT ARTMKKAVAI LQPIIESEKV EGSASAGKVL LATVKGDVHD IGKNIVAVVM ACNGYDIVDL GVMVPAETIV QRAIEEKVDM IGLSGLITPS LEEMAHVAVE LEKAGLDIPL LIGGATTSKM HTALKIAPVY HAPVVHLKDA SQNASVASKL LNPQAKAELV NELETEYEAL REKSGLMKRE TVSLEEAQKN KLNLF // ID A7MLT2_CROS8 Unreviewed; 310 AA. AC A7MLT2; DT 02-OCT-2007, integrated into UniProtKB/TrEMBL. DT 02-OCT-2007, sequence version 1. DT 29-APR-2015, entry version 39. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ABU78172.1}; GN OrderedLocusNames=ESA_02943 {ECO:0000313|EMBL:ABU78172.1}; OS Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Cronobacter. OX NCBI_TaxID=290339 {ECO:0000313|EMBL:ABU78172.1, ECO:0000313|Proteomes:UP000000260}; RN [1] {ECO:0000313|EMBL:ABU78172.1, ECO:0000313|Proteomes:UP000000260} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-894 {ECO:0000313|EMBL:ABU78172.1, RC ECO:0000313|Proteomes:UP000000260}; 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 ----------------------------------------------------------------------- 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; ABU78172.1; -; Genomic_DNA. DR RefSeq; WP_012125536.1; NC_009778.1. DR RefSeq; YP_001439008.1; NC_009778.1. DR STRING; 290339.ESA_02943; -. DR EnsemblBacteria; ABU78172; ABU78172; ESA_02943. DR GeneID; 5548570; -. DR KEGG; esa:ESA_02943; -. DR PATRIC; 20397723; VBICroSak107175_2633. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; CSAK290339:GJ80-2933-MONOMER; -. DR Proteomes; UP000000260; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000260}; KW Reference proteome {ECO:0000313|Proteomes:UP000000260}. SQ SEQUENCE 310 AA; 33242 MW; 9443E31F6B6C4C67 CRC64; MLLNNPLTPL LSQQPFVVLD GALATELEAR GCNLADSLWS AKVLMEQPEL IYAVHLDYFR AGAQCAITAS YQATPAGFAA RGLDEAQSRA LIARSVELAR QARDDYYHEQ PDAGPLLVAG SVGPYGAYLA DGSEYRGDYA LSAAEFADFH RPRVEALLEA GVDLLACETL PSLPEALALA ALLESYPQAR AWFTFTLRDS DHISDGTPLS DVAAALAPYT QIVALGINCV ALEKTTAALA RLHDATRLPL VVYPNSGEQY DAVSKTWRHD GHACQTLAHY LGEWRAAGAA LIGGCCRTTP ADIAALRAQR // ID A7MPE0_CROS8 Unreviewed; 1211 AA. AC A7MPE0; DT 02-OCT-2007, integrated into UniProtKB/TrEMBL. DT 02-OCT-2007, sequence version 1. DT 01-APR-2015, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ABU75363.1}; GN OrderedLocusNames=ESA_00058 {ECO:0000313|EMBL:ABU75363.1}; OS Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Cronobacter. OX NCBI_TaxID=290339 {ECO:0000313|EMBL:ABU75363.1, ECO:0000313|Proteomes:UP000000260}; RN [1] {ECO:0000313|EMBL:ABU75363.1, ECO:0000313|Proteomes:UP000000260} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-894 {ECO:0000313|EMBL:ABU75363.1, RC ECO:0000313|Proteomes:UP000000260}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000783; ABU75363.1; -; Genomic_DNA. DR RefSeq; WP_012123599.1; NC_009778.1. DR RefSeq; YP_001436199.1; NC_009778.1. DR ProteinModelPortal; A7MPE0; -. DR SMR; A7MPE0; 635-1211. DR STRING; 290339.ESA_00058; -. DR EnsemblBacteria; ABU75363; ABU75363; ESA_00058. DR KEGG; esa:ESA_00058; -. DR PATRIC; 20392447; VBICroSak107175_0051. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CSAK290339:GJ80-55-MONOMER; -. DR Proteomes; UP000000260; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000260}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000260}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 231 231 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 743 743 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1211 AA; 134051 MW; 08BF33B9A0F3DCED CRC64; MVLDGGMGTM IQSYRLDEED FRGERFADWQ CDLKGNNDLL VLTKPDIIAA IHYAYFEAGA DIIETNTFNS TTIAMADYQM ESLSAEINYE AAKLARACAD EWTARTPEKP RYVAGVLGPT NRTASISPDV NDPAFRNITF DQLVEAYRES TRALIEGGAD LILIETVFDT LNAKAAIFAV KAEFEALGVE LPIMISGTIT DASGRTLSGQ TTEAFYNSLR HADALTFGLN CALGPDELRQ YVAELSRIAE CYVTAHPNAG LPNAFGEYDL DADVMAAQIR EWAQSGFLNI VGGCCGTTPE HIAAMSRAVD GLPPRKLPDI PVACRLAGLE PLNIGDDSLF VNVGERTNVT GSAKFKRLIK EEKYSEALDV ARQQVENGAQ IIDINMDEGM LDAEAAMVRF LNLIAGEPDI ARVPIMIDSS KWDVIEKGLK CIQGKGIVNS ISMKEGVEAF VHHAKLVRRY GAAVVVMAFD EVGQADTRER KIEICRRAYK ILTEEVGFPP EDIIFDPNIF AVATGIDEHN NYAQDFIGAC EDIKRELPHA LISGGVSNVS FSFRGNDPVR EAIHAVFLYY AIRNGMDMGI VNAGQLAIYD DLPTELRDAV EDVILNRRAD GTERLLALAE KYRGSKADNA ADAQQAEWRT WDVKKRLEYS LVKGITEFIE QDTEEARQQA ARPIEVIEGP LMDGMNVVGD LFGEGKMFLP QVVKSARVMK QAVAYLEPYI QASKEVGKSN GKIVLATVKG DVHDIGKNIV GVVLQCNNYE IIDLGVMVPT DKILKTAREV NADIIGLSGL ITPSLDEMVN VAKEMERQGF TLPLLIGGAT TSKAHTAVKI EQNYSGPTVY VQNASRTVGV VSALLSDTLR DDFVARTRKE YETVRIQHGR KKPRTPPVTL AAARENDLAF DWESYTPPAA HRLGVEEVTA SIETLRNYID WTPFFMTWSL AGKYPRILED EVVGEEAQRL FKDANEMLDK LSAEKSLTPR GVVGLFPANR VGDDIEIYRD ETRTHVLSVS HHLRQQTEKV GFANYCLADF VAPKHSGKAD YLGAFAVTGG QEEDALAEAF DAQHDDYNKI MVKAVADRLA EAFAEYLHER VRKVLWGYAP YENLSNEELI RENYQGIRPA PGYPACPEHT EKSVIWDLLD VENRIGMKLT ESYAMWPGAS VSGWYFSHPE SKYFAVAQIQ RDQVEDYAQR KGMSVSEVER WLAANLGYDA D // ID A7MU58_VIBCB Unreviewed; 1226 AA. AC A7MU58; DT 02-OCT-2007, integrated into UniProtKB/TrEMBL. DT 02-OCT-2007, sequence version 1. DT 27-MAY-2015, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ABU72626.1}; GN OrderedLocusNames=VIBHAR_03712 {ECO:0000313|EMBL:ABU72626.1}; OS Vibrio campbellii (strain ATCC BAA-1116 / BB120). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=338187 {ECO:0000313|EMBL:ABU72626.1, ECO:0000313|Proteomes:UP000008152}; RN [1] {ECO:0000313|EMBL:ABU72626.1, ECO:0000313|Proteomes:UP000008152} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1116 / BB120 {ECO:0000313|Proteomes:UP000008152}; 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 ----------------------------------------------------------------------- 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; ABU72626.1; -; Genomic_DNA. DR RefSeq; WP_012129016.1; NC_022269.1. DR RefSeq; YP_008527219.1; NC_022269.1. DR ProteinModelPortal; A7MU58; -. DR SMR; A7MU58; 654-1224. DR STRING; 338187.VIBHAR_03712; -. DR EnsemblBacteria; ABU72626; ABU72626; VIBHAR_03712. DR EnsemblBacteria; AGU95231; AGU95231; M892_12650. DR KEGG; vca:M892_12650; -. DR KEGG; vha:VIBHAR_03712; -. DR PATRIC; 20134032; VBIVibHar24526_3512. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; VHAR338187:GJCH-3699-MONOMER; -. DR Proteomes; UP000008152; Chromosome I. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008152}. SQ SEQUENCE 1226 AA; 136844 MW; 280A1C5042D70BFA CRC64; MGSNVRQQIE AQLKQRILLI DGGMGTMIQG YKLEEQDYRG ERFADWHCDL KGNNDLLVLT QPQLIKEIHS AYLEAGADIL ETNTFNATTI AMADYEMESL SEEINYAAAK LAREAADEWT AKTPERPRYV AGVLGPTNRT CSISPDVNDP GYRNVSFDEL VEAYSESTRA LIKGGSDLIL IETIFDTLNA KACAFAVDSV FEELSIELPV MISGTITDAS GRTLSGQTTE AFYNSLRHVN PISFGLNCAL GPDELRPYVE ELSRISESFV STHPNAGLPN AFGEYDLSPE DMAEHVKEWA ESGFLNLIGG CCGTTPEHIR HMAMAVEGVK PRDLPELTVA CRLSGLEPLT IEKETLFINV GERTNVTGSA RFKRLIKEEL YDEALEVARQ QVENGAQIID INMDEGMLDA EACMVRFLNL CASEPEISKV PIMVDSSKWE VIEAGLKCIQ GKGIVNSISL KEGKEKFVEQ AKLIRRYGAA VIVMAFDEVG QAETRERKLE ICTNAYRILV DEVGFPPEDI IFDPNIFAVA TGIEEHNNYA VDFIEAVADI KRDLPHAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK NGMDMGIVNA GQLEIYDNVP DKLREAVEDV ILNRRHDSTE RLLDIAAEYA GKGVGKEEDA SALEWRTWEV EKRLEHALVK GITEFIVEDT EEARLNASKP LEVIEGPLMD GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AHLEPFINKE KQTGSSNGKI LLATVKGDVH DIGKNIVGVV LQCNNYEIID LGVMVPCEKI LKVAKEENVD IIGLSGLITP SLDEMVHLAK EMERLDFDLP LLIGGATTSK AHTAVKIEQN YKHPVVYVNN ASRAVGVCTS LLSDELRPGF VEKLDVDYER VREQHNRKKP RTKPVTLEEA RANKVAIDWD KYTPPAPAKP GIHIFDDFEV STLRKYIDWT PFFMTWSLVG KYPTIFDHEE VGEEAQRLYK DANELLDRVE REGLLKARGM CGLFPAASVG DDIEVYTDES RTEVAKVLHN LRQQTEKPKG FNYCLSDYVA PKESGKHDWV GAFAVTGGIG ERELADEYKA QGDDYNAIMI QAVADRLAEA FAEYLHERVR KEIWGYAADE DLSNEELIRE KYQGIRPAPG YPACPEHTEK GPLWELMNVE ENIGMSLTSS YAMYPGASVS GWYFSYPDSR YFAIAQIQED QLQSYADRKG WDRIEAEKWL GPNING // ID A7N4Y4_VIBCB Unreviewed; 301 AA. AC A7N4Y4; DT 02-OCT-2007, integrated into UniProtKB/TrEMBL. DT 02-OCT-2007, sequence version 1. DT 27-MAY-2015, entry version 41. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ABU73715.1}; GN OrderedLocusNames=VIBHAR_05821 {ECO:0000313|EMBL:ABU73715.1}; OS Vibrio campbellii (strain ATCC BAA-1116 / BB120). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=338187 {ECO:0000313|EMBL:ABU73715.1, ECO:0000313|Proteomes:UP000008152}; RN [1] {ECO:0000313|EMBL:ABU73715.1, ECO:0000313|Proteomes:UP000008152} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1116 / BB120 {ECO:0000313|Proteomes:UP000008152}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; ABU73715.1; -; Genomic_DNA. DR RefSeq; WP_012129404.1; NC_009784.1. DR STRING; 338187.VIBHAR_05821; -. DR EnsemblBacteria; ABU73715; ABU73715; VIBHAR_05821. DR KEGG; vha:VIBHAR_05821; -. DR PATRIC; 20136004; VBIVibHar24526_4482. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; VHAR338187:GJCH-4806-MONOMER; -. DR Proteomes; UP000008152; Chromosome II. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008152}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 208 208 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 301 AA; 33258 MW; 27FF08EB132F896E CRC64; MKKLTILDGG MGRELKRMSA PFSQPLWSAQ ALIESPEFVY QAHDNFIQAG AEIIIANSYA CVPFHLGQEL YDQQGSKLAR FAAKIARECA DKSDTPVRVA GCIPPAFGSY RPDLFEPIQG EAIFQTLFEA QVEYVDLWIA ETIGSLKELK CLQRVFATSA KPTAYAFSLS DDSLETALLR SGETVTQAIE QLTQSKQTEH SISIYFNCSV PEVMAKAVSD TKTVLDQHNL DIEIGVYANN FTAIKSNHEA NSALQSMREL TPEKYLAFAQ DWYLRGASIV GGCCGIGPEH IKALSDWKRS L // ID A7NQR8_ROSCS Unreviewed; 1208 AA. AC A7NQR8; DT 02-OCT-2007, integrated into UniProtKB/TrEMBL. DT 02-OCT-2007, sequence version 1. DT 27-MAY-2015, entry version 62. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABU59914.1}; GN OrderedLocusNames=Rcas_3878 {ECO:0000313|EMBL:ABU59914.1}; OS Roseiflexus castenholzii (strain DSM 13941 / HLO8). OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Roseiflexineae; OC Roseiflexaceae; Roseiflexus. OX NCBI_TaxID=383372 {ECO:0000313|EMBL:ABU59914.1, ECO:0000313|Proteomes:UP000000263}; RN [1] {ECO:0000313|EMBL:ABU59914.1, ECO:0000313|Proteomes:UP000000263} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13941 / HLO8 {ECO:0000313|Proteomes:UP000000263}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000804; ABU59914.1; -; Genomic_DNA. DR RefSeq; WP_012122337.1; NC_009767.1. DR RefSeq; YP_001433932.1; NC_009767.1. DR ProteinModelPortal; A7NQR8; -. DR STRING; 383372.Rcas_3878; -. DR EnsemblBacteria; ABU59914; ABU59914; Rcas_3878. DR KEGG; rca:Rcas_3878; -. DR PATRIC; 23346598; VBIRosCas91182_4339. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; RCAS383372:GH89-3928-MONOMER; -. DR Proteomes; UP000000263; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000263}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 233 233 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 769 769 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1208 AA; 132844 MW; 7F68721E69D9FBA0 CRC64; MKKPTYLEAL CERVLIYDGA MGTSIDTFHL TAADYGGEQT FGARDYLVIT RPDVIEQIHA SFLEAGADVL ETCTFQSTRP RLEEWGLADQ THAINVAAAR LARRVADAFE ARDGRPRYVA GSMGPTGKLP SSDDPALSDV TFDQLSDIFY EQATALIEGG VDVLLVETSV DILEVKAALD GIRRAKADLN RPDVAVQAQV FLDLSGKMLL GTEVPAIIAT LEAMPVDVIG LNCSTGPEHM REAIRYMTRH SRKPISCIPN AGLPIEVNGE TVYPMEPEPF ARILGEYVHE YGVAVVGGCC GTRPAHIRRL REVVGFVPPK VRDIEYIPSV SSGVRAAALR QEGTLTIIGE RVNTLGSRKV KRLLLNEDYD GVLEVAREQV DSGAHLLDVC VAMTERSDER EMMVKLVKKL TMNVELPLVI DTTEADVLEA ALAIYPGRAV VNSVSLEGGR GDKIDRTMPL VARYGAATIA MTIDEEGMAH TAERKLAIAQ RIAQIAQDEY GVPNEALIFD VLTFPITTGQ AELRRAAIET IEGIRLVKQH IPGCFTTLGV SNLSFGVAPH ARATLNSVFL KHAVDAGLDT AIINPAHVTP YAEIPPEHIK VCEDLIFDRD DQALARFIQF FEEHAADAKT ERADPTEGMT AAQRIHWKIV HRKKEGIEAD IDQVIAERIG DMEARAGNGV SNPDRRSHES LVASPFRNAA AVDVLNTVLL PAMKEVGDLF GAGQLILPFV LQSAEVMKRA VAHLEQYLEK LEGVTKGKIV LATVYGDVHD IGKNLVHTIL ANNGYTVYDL GKQVPINTII EKAVEVNADA IGLSALLVST SKQMPLCVQE LYRRGLKFPV LVGGAAINKQ YGQRILFVDD NTPYEPGVFY CKDAFEGLET VDALADPTTR AAFVERTKAE AAEALGKKQR GRVALAELGR ATLSDAAKVR SAVRTDVPVP TPPFWGAKVV RRIKLADVVE CLDRNALYRL QWGAKNAKGE EWERLKAEFD AKVRDLVREA ERDGWLEPQV VYGYYPCQSD GHEVIVYDPP STLNGAQPRE LTRFVFPRQP ERERLCLADY FRSRESGEYD VVALQIVTMG RKVDDLTETL QHAGDYARAY FIHGLGVSLA EALAEYTNRL IRQQLGLKGT QGKRYSWGYP ACPDLEEHEK LFRVLPADQI GVSLTEAWQL VPEQSTAAIV IHHPEAKYFS IGSARERAEE DVAETLSI // ID A7RIN5_NEMVE Unreviewed; 374 AA. AC A7RIN5; DT 02-OCT-2007, integrated into UniProtKB/TrEMBL. DT 02-OCT-2007, sequence version 1. DT 04-MAR-2015, entry version 42. DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EDO48828.1}; GN ORFNames=v1g178461 {ECO:0000313|EMBL:EDO48828.1}; OS Nematostella vectensis (Starlet sea anemone). OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria; OC Edwardsiidae; Nematostella. OX NCBI_TaxID=45351 {ECO:0000313|Proteomes:UP000001593}; RN [1] {ECO:0000313|EMBL:EDO48828.1, ECO:0000313|Proteomes:UP000001593} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593}; RX PubMed=17615350; DOI=10.1126/science.1139158; RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., RA Salamov A., Terry A., Shapiro H., Lindquist E., Kapitonov V.V., RA Jurka J., Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., RA Finnerty J.R., Technau U., Martindale M.Q., Rokhsar D.S.; RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and RT genomic organization."; RL Science 317:86-94(2007). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS469512; EDO48828.1; -; Genomic_DNA. DR RefSeq; XP_001640891.1; XM_001640841.1. DR UniGene; Nve.355; -. DR ProteinModelPortal; A7RIN5; -. DR SMR; A7RIN5; 5-359. DR STRING; 45351.JGI178461; -. DR EnsemblMetazoa; EDO48828; EDO48828; NEMVEDRAFT_v1g178461. DR GeneID; 5521003; -. DR KEGG; nve:NEMVE_v1g178461; -. DR eggNOG; COG0646; -. DR HOGENOM; HOG000231636; -. DR InParanoid; A7RIN5; -. DR OMA; CKELNER; -. DR OrthoDB; EOG79GT7C; -. DR Proteomes; UP000001593; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001593}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000001593}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 210 210 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 292 292 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 374 AA; 41757 MW; 49333FE83EE00449 CRC64; MPFKQGILER LNDGEVIIGD GGMTHALEKR CYVKAGVWTP ECVVEHPEAV RQLHREFLRA GADVIQAFTF AMQDKPLVSA GYSYKWDEIS HAGSILAKEV SDEGEFALSS GSLCETGSLF IKGLASKEEI KQRFRDQVKI FVDTGMDLLI AEYISHVQEA EWMVEVMKES GKPVAVTMAI SREGDRHGVL PGECAVRLVR AGADIIGVNC RFDPERSLDT IALMQEAIQR EGLKTHWMVQ PLGYWCPDAG PSGFTSIPEC TLALEPRVLT RIEAHKFARK AYNMGVRYIG GCCGFEPYHI RALAKELSKE RGRLPPGSDK SCLWGEALVH HAEAQVARRA TREYWEKLVP ATGRPFSPAF AVHEDTWKTE KKHE // ID A7RIN6_NEMVE Unreviewed; 434 AA. AC A7RIN6; DT 02-OCT-2007, integrated into UniProtKB/TrEMBL. DT 02-OCT-2007, sequence version 1. DT 27-MAY-2015, entry version 42. DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EDO48829.1}; GN ORFNames=v1g197687 {ECO:0000313|EMBL:EDO48829.1}; OS Nematostella vectensis (Starlet sea anemone). OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria; OC Edwardsiidae; Nematostella. OX NCBI_TaxID=45351 {ECO:0000313|Proteomes:UP000001593}; RN [1] {ECO:0000313|EMBL:EDO48829.1, ECO:0000313|Proteomes:UP000001593} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593}; RX PubMed=17615350; DOI=10.1126/science.1139158; RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., RA Salamov A., Terry A., Shapiro H., Lindquist E., Kapitonov V.V., RA Jurka J., Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., RA Finnerty J.R., Technau U., Martindale M.Q., Rokhsar D.S.; RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and RT genomic organization."; RL Science 317:86-94(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; DS469512; EDO48829.1; -; Genomic_DNA. DR RefSeq; XP_001640892.1; XM_001640842.1. DR UniGene; Nve.24305; -. DR ProteinModelPortal; A7RIN6; -. DR STRING; 45351.JGI197687; -. DR EnsemblMetazoa; EDO48829; EDO48829; NEMVEDRAFT_v1g197687. DR GeneID; 5521004; -. DR KEGG; nve:NEMVE_v1g197687; -. DR eggNOG; COG0646; -. DR HOGENOM; HOG000231636; -. DR InParanoid; A7RIN6; -. DR OrthoDB; EOG79GT7C; -. DR Proteomes; UP000001593; Unassembled WGS sequence. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001593}; KW Reference proteome {ECO:0000313|Proteomes:UP000001593}. SQ SEQUENCE 434 AA; 48844 MW; D0337D55FF4984CF CRC64; MHDVIRIKHI LGILERLNNG EVIIGDGGMS HALEKRCYVK IGVWTPECVV EHPEAVRQLH SEFLRAGADV IQAFTFAMQD KPLVSAGYSY KWDEISRAGS ILAKEVSDKG EFALSSGSLC ETGSLFIKGL ATKEEIKQRF RDQVKIFVDT GMDLLIAEYI SHVQEAEWMV EVMKESGKPV AVTMAISREG DRHGVLPGEC AVRLVRAGAD IIGVNYRFDP ERSLDTIALM QEAIQREGLK THWMVQPLGY WCPDAGPSGI TSIPECSLAL DPRVLTRIEA HKFARKAYNM GVRYIGGCCG FEPYHIRALA EELANERGRF PPGSDKSCLW GKALVHHTEP QIARRANREY WENLVPATVF LLFMFPDSPF LVLVIAIWLS SQSTETNILR PRVERKIDLY VGVAYNVKNI LMNLIKCKIS YLVMEFVDIF IENL // ID A7RIN7_NEMVE Unreviewed; 365 AA. AC A7RIN7; DT 02-OCT-2007, integrated into UniProtKB/TrEMBL. DT 02-OCT-2007, sequence version 1. DT 04-MAR-2015, entry version 42. DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EDO48830.1}; DE Flags: Fragment; GN ORFNames=v1g83002 {ECO:0000313|EMBL:EDO48830.1}; OS Nematostella vectensis (Starlet sea anemone). OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria; OC Edwardsiidae; Nematostella. OX NCBI_TaxID=45351 {ECO:0000313|Proteomes:UP000001593}; RN [1] {ECO:0000313|EMBL:EDO48830.1, ECO:0000313|Proteomes:UP000001593} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593}; RX PubMed=17615350; DOI=10.1126/science.1139158; RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., RA Salamov A., Terry A., Shapiro H., Lindquist E., Kapitonov V.V., RA Jurka J., Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., RA Finnerty J.R., Technau U., Martindale M.Q., Rokhsar D.S.; RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and RT genomic organization."; RL Science 317:86-94(2007). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS469512; EDO48830.1; -; Genomic_DNA. DR RefSeq; XP_001640893.1; XM_001640843.1. DR ProteinModelPortal; A7RIN7; -. DR STRING; 45351.JGI83002; -. DR GeneID; 5521086; -. DR KEGG; nve:NEMVE_v1g83002; -. DR eggNOG; COG0646; -. DR HOGENOM; HOG000231636; -. DR InParanoid; A7RIN7; -. DR OrthoDB; EOG79GT7C; -. DR Proteomes; UP000001593; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001593}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000001593}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 202 202 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT NON_TER 1 1 {ECO:0000313|EMBL:EDO48830.1}. SQ SEQUENCE 365 AA; 40591 MW; C2F9F8FB020D7F08 CRC64; ERLNNEEVII GDGGMTYALE RRGYVKAGVW TPECVMENPE AVQQLHREFL RAGADVIQAF TFAMQDKPLV SAGYSYKWNE ISHAGSLLAK GVSGEGEFAL ASGSLCETGS LFRKGLASKE EIQQRFRDQV QIFVDTGMDL IIAEYISHVQ EAEWMVEVIK ESGMPTAVSL AISREGDHHG VLPGECALRL VRAGADIIGV NCRFDPERSL DTIALMQEAI QREGLKTHWM VQPVGYWVPD AGPSGFTSIP ENPLALEPRL MTRIEAHKFA RKAYNMGVRY IGGCCGFEPY HIRAVAEELA KERGRFPPGS DKSCLWGKAL VHHAEPQIAR RANREYWENL EPATGRPFSA AYATTEDTWK TSQDD // ID A7RLS1_NEMVE Unreviewed; 398 AA. AC A7RLS1; DT 02-OCT-2007, integrated into UniProtKB/TrEMBL. DT 02-OCT-2007, sequence version 1. DT 04-MAR-2015, entry version 44. DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EDO47743.1}; GN ORFNames=v1g236455 {ECO:0000313|EMBL:EDO47743.1}; OS Nematostella vectensis (Starlet sea anemone). OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria; OC Edwardsiidae; Nematostella. OX NCBI_TaxID=45351 {ECO:0000313|Proteomes:UP000001593}; RN [1] {ECO:0000313|EMBL:EDO47743.1, ECO:0000313|Proteomes:UP000001593} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593}; RX PubMed=17615350; DOI=10.1126/science.1139158; RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., RA Salamov A., Terry A., Shapiro H., Lindquist E., Kapitonov V.V., RA Jurka J., Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., RA Finnerty J.R., Technau U., Martindale M.Q., Rokhsar D.S.; RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and RT genomic organization."; RL Science 317:86-94(2007). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS469518; EDO47743.1; -; Genomic_DNA. DR RefSeq; XP_001639806.1; XM_001639756.1. DR UniGene; Nve.29; -. DR ProteinModelPortal; A7RLS1; -. DR SMR; A7RLS1; 4-391. DR STRING; 45351.JGI236455; -. DR PRIDE; A7RLS1; -. DR EnsemblMetazoa; EDO47743; EDO47743; NEMVEDRAFT_v1g236455. DR GeneID; 5519847; -. DR KEGG; nve:NEMVE_v1g236455; -. DR eggNOG; COG0646; -. DR HOGENOM; HOG000231636; -. DR InParanoid; A7RLS1; -. DR KO; K00544; -. DR OMA; WGVTKGT; -. DR OrthoDB; EOG79GT7C; -. DR Proteomes; UP000001593; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001593}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000001593}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 211 211 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 398 AA; 44123 MW; 466FA90EB44E3497 CRC64; MGPKRGFLER LEAGETIIGD GGFVFALEKR GYVKAGPWTP EATVENPEAV RQLHREFLRA GSDVMQTFTF YASDDKLQNR GNEASKKFGC AAINEAACDL AREVADEGDA LVAGGVCQTP TYLSGKGKEA CQAEFQKQVD VFIKKDVDFI IAEYYEHVEE AVWAVELLKK TGKPIAASLC IGPEGDMHGV SAGDCAVRLA EAGADCIGVN CHYGPIKSLE TMRLMKAGLD AAGYKKHLMI QPLGYHTPDC GKQGFIDLPE FPFGLEPRIC TRWDMHKYAR EAYDMGIRFI GGCCGFEPYH IRALSEELAK ERGKFPKGSE KHGLWGDGLR QHTKPWVRSR ARRDYWEKLN PSSGRPFSAS CSKPDNWGIT AGHDYLKQHA EDTSDKELKE IMEVAQSR // ID A7S7I8_NEMVE Unreviewed; 265 AA. AC A7S7I8; DT 02-OCT-2007, integrated into UniProtKB/TrEMBL. DT 02-OCT-2007, sequence version 1. DT 07-JAN-2015, entry version 37. DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EDO40315.1}; DE Flags: Fragment; GN ORFNames=v1g107735 {ECO:0000313|EMBL:EDO40315.1}; OS Nematostella vectensis (Starlet sea anemone). OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria; OC Edwardsiidae; Nematostella. OX NCBI_TaxID=45351 {ECO:0000313|Proteomes:UP000001593}; RN [1] {ECO:0000313|EMBL:EDO40315.1, ECO:0000313|Proteomes:UP000001593} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593}; RX PubMed=17615350; DOI=10.1126/science.1139158; RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., RA Salamov A., Terry A., Shapiro H., Lindquist E., Kapitonov V.V., RA Jurka J., Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., RA Finnerty J.R., Technau U., Martindale M.Q., Rokhsar D.S.; RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and RT genomic organization."; RL Science 317:86-94(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; DS469593; EDO40315.1; -; Genomic_DNA. DR RefSeq; XP_001632378.1; XM_001632328.1. DR STRING; 45351.JGI107735; -. DR EnsemblMetazoa; EDO40315; EDO40315; NEMVEDRAFT_v1g107735. DR GeneID; 5512035; -. DR KEGG; nve:NEMVE_v1g107735; -. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR InParanoid; A7S7I8; -. DR KO; K00547; -. DR OMA; AINTHNE; -. DR OrthoDB; EOG7GQXW0; -. DR Proteomes; UP000001593; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001593}; KW Reference proteome {ECO:0000313|Proteomes:UP000001593}. FT NON_TER 1 1 {ECO:0000313|EMBL:EDO40315.1}. FT NON_TER 265 265 {ECO:0000313|EMBL:EDO40315.1}. SQ SEQUENCE 265 AA; 29548 MW; C73DA6A7B6A8FE3B CRC64; FFMQGDPLWS ARVLVENPEA VKQVHKSFLT HGSDIITTAT YQASISGFCK HLGVTADEAR KLIQRGVHIA RESVDEFWDK HSNSPQVAGS VCPYGTCQSD GSEYHGNYVD TMTIKNLMDW HRPQIQALVE TGLDLLAFET IPAQKEGEAL VQLLKEFPGT KAWLSYSCKD GSHTSHNEDF VSAIMAAVAD SEQIIAVGNN CCSPVYVTSL IRRLKPKTTL PIVIYPNKGE EWIDRRYSEW QDTGNVPPVV SYLDEWIDSG AQWIG // ID A7SKT1_NEMVE Unreviewed; 1178 AA. AC A7SKT1; DT 02-OCT-2007, integrated into UniProtKB/TrEMBL. DT 02-OCT-2007, sequence version 1. DT 27-MAY-2015, entry version 55. DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EDO35691.1}; GN ORFNames=v1g245922 {ECO:0000313|EMBL:EDO35691.1}; OS Nematostella vectensis (Starlet sea anemone). OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria; OC Edwardsiidae; Nematostella. OX NCBI_TaxID=45351 {ECO:0000313|Proteomes:UP000001593}; RN [1] {ECO:0000313|EMBL:EDO35691.1, ECO:0000313|Proteomes:UP000001593} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593}; RX PubMed=17615350; DOI=10.1126/science.1139158; RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., RA Salamov A., Terry A., Shapiro H., Lindquist E., Kapitonov V.V., RA Jurka J., Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., RA Finnerty J.R., Technau U., Martindale M.Q., Rokhsar D.S.; RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and RT genomic organization."; RL Science 317:86-94(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; DS469691; EDO35691.1; -; Genomic_DNA. DR RefSeq; XP_001627791.1; XM_001627741.1. DR UniGene; Nve.5609; -. DR ProteinModelPortal; A7SKT1; -. DR SMR; A7SKT1; 577-835, 841-1176. DR STRING; 45351.JGI245922; -. DR EnsemblMetazoa; EDO35691; EDO35691; NEMVEDRAFT_v1g245922. DR GeneID; 5507102; -. DR KEGG; nve:NEMVE_v1g245922; -. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR InParanoid; A7SKT1; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG7TF786; -. DR Proteomes; UP000001593; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001593}; KW Reference proteome {ECO:0000313|Proteomes:UP000001593}. SQ SEQUENCE 1178 AA; 131055 MW; 2017C6BEE18DB8FB CRC64; MIFDGGMGTM IQKLHLEEAD FRGEEFKNHP KSLKGNNDLL SITKPDAILD IHKGYLEAGA DFVETNTFSG TKIAQADYGL EDAAYRLNRA SAEVAKRAAY EVTASTGVEK FVAGAMGPTN RTLSISPTVE CPGFRNVTFD ELVDAYTEQA RGLLDGGVDV LLVETIFDTA NAKAALFAID QLFEKEYSPV PVFVSGTIVD KSGRTLSGQT TESFVISVSH SSPMCIGLNC ALGAVEMRPF IEAVGMNTEA YTICYPNAGL PNTFGDYDET PETMAKHLKA RCCGTTPEHI RAIAEAVRPY KPRMRPEDLH SDALSLCGLE SMRINPSVLF VNIGERCNVA GSRMFCKLIK NGKFQVPLCI DSSNFDVIEA GLKCAQGKCI VNSISLKNGE EDFLDKARII KRYGAAVVVM AFDEQGQAAD CERKVEICTR SYNLLVKEAH FEPNDIIFDP NILTVATGME EHNNYGKYFI QATRIIKETL PGARVSGGLS NFSFSFRGMD AIREAMHSVF LYHAIKAGLD MAIVNAGALP VYDDIEKNLL ELCEDLLWNR DPEATEKLLQ LAQSMGPGAK KVTITDEWRH GNVEERLEFA LVKGIDKYVI EDTEEARVNT DRYPRPLNVI EGPLMKGMGV VGDLFGAGKM FLPQVIKSAR VMKKAVGHLI PFMEEERQMR LANGGGVGDS SLKNKYNGTI VLATVKGDVH DIGKNIVGVV LGCNNYRVID LGVMTACEKI LQTAIEEEAD IIGLSGLITP SLDEMIHVAK EMERQGLKIP LLIGGATTSR THTAVKIAPR YSEPTIHVLD ASKSVVVCSA LMDKGARDDF VEEVSEEYEE IREDHYDSLK ERRYLSIEKA REKKAFVDFV DFRPVKPTFL GIKVFEDYDL EKIIPYIDWK PFFDVWQLRG KYPNRGYPKI FNDKTVGEEA RRVYNDAQTM LNNVLRDKTL RAVGELAFFP ANSEGDDVYV FDEDDNRTGE PRAVFCGLRQ QAEKEHGVTD PYYCISDFIA PRDSGIKDYV GCFAVTCLGA EALAEEYQNE LDDYSVIMVK ALADRIVEAF AEELHEQVRK HYWGYCGEES LDTKDLHRIR YQGIRPAFGY PSQPDHTEKL TMWGLMNCEE STGIKLTESL AMDPAASVSG LYFSHPESCY FAVGKICQDQ IQEYANRKDK PVQVMEKWLS SALSYDAE // ID A7T8D2_NEMVE Unreviewed; 156 AA. AC A7T8D2; DT 02-OCT-2007, integrated into UniProtKB/TrEMBL. DT 02-OCT-2007, sequence version 1. DT 27-MAY-2015, entry version 34. DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EDO27759.1}; GN ORFNames=v1g223749 {ECO:0000313|EMBL:EDO27759.1}; OS Nematostella vectensis (Starlet sea anemone). OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria; OC Edwardsiidae; Nematostella. OX NCBI_TaxID=45351 {ECO:0000313|Proteomes:UP000001593}; RN [1] {ECO:0000313|EMBL:EDO27759.1, ECO:0000313|Proteomes:UP000001593} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593}; RX PubMed=17615350; DOI=10.1126/science.1139158; RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., RA Salamov A., Terry A., Shapiro H., Lindquist E., Kapitonov V.V., RA Jurka J., Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., RA Finnerty J.R., Technau U., Martindale M.Q., Rokhsar D.S.; RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and RT genomic organization."; RL Science 317:86-94(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; DS472641; EDO27759.1; -; Genomic_DNA. DR RefSeq; XP_001619859.1; XM_001619809.1. DR ProteinModelPortal; A7T8D2; -. DR STRING; 45351.JGI223749; -. DR EnsemblMetazoa; EDO27759; EDO27759; NEMVEDRAFT_v1g223749. DR GeneID; 5498090; -. DR KEGG; nve:NEMVE_v1g223749; -. DR eggNOG; COG2040; -. DR InParanoid; A7T8D2; -. DR OrthoDB; EOG7GQXW0; -. DR Proteomes; UP000001593; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 2. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001593}; KW Reference proteome {ECO:0000313|Proteomes:UP000001593}. SQ SEQUENCE 156 AA; 17268 MW; 7A5FE6226FD7EB15 CRC64; MALQKPPPPN FRPGDIYQHK KNLMDWHRPQ IQALVETGLD LLAFETIPAQ KEGEALVQLL KEFPGTKAWL SYSCKDGSHT SHNEDFVSAI MAAVADSEQV RYGWQDTGNV PPVVSYLDEW IDSGAQWIGG CCRTSLTDIS ETRAAIARRT SKPGIG // ID A7TSR2_VANPO Unreviewed; 323 AA. AC A7TSR2; DT 02-OCT-2007, integrated into UniProtKB/TrEMBL. DT 02-OCT-2007, sequence version 1. DT 27-MAY-2015, entry version 30. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EDO14697.1}; GN ORFNames=Kpol_1068p7 {ECO:0000313|EMBL:EDO14697.1}; 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 {ECO:0000313|Proteomes:UP000000267}; RN [1] {ECO:0000313|EMBL:EDO14697.1, ECO:0000313|Proteomes:UP000000267} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 22028 / DSM 70294 {ECO:0000313|Proteomes:UP000000267}; 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; DS480521; EDO14697.1; -; Genomic_DNA. DR RefSeq; XP_001642555.1; XM_001642505.1. DR STRING; 436907.A7TSR2; -. DR GeneID; 5542720; -. DR KEGG; vpo:Kpol_1068p7; -. DR eggNOG; COG2040; -. DR InParanoid; A7TSR2; -. DR OrthoDB; EOG79SF86; -. DR PhylomeDB; A7TSR2; -. DR Proteomes; UP000000267; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000267}; KW Reference proteome {ECO:0000313|Proteomes:UP000000267}. SQ SEQUENCE 323 AA; 36388 MW; E33892C10032BCD5 CRC64; MRVPIEELIR NQPDEVLVSD GGLGTLLESR GINVSSPLWS TVPFLKDDFW DSETKTSDRN IIEGIYRDYI TSGSRILSTI TYQTSFALIS THTEVKTIEG YKQLIRNITS FCRSAIGEDN YLIGSIGPFG ARLGAEYTGN YGDSPSNINY LEYFKPQLEE FNNNDDIDII GFETVPNKYE LEAILSWDKS VISKPYYVSL SLLDNGGLRD GTSFEEIATI FKKYSNNDNL ILTGANCISF KYASENISKL HQAIPTLPLI VYPNSGEIYD PLTKKWTIDQ TFGLTWEDLI KELRTSNVRI VGGCCRTTPD DINKIKDMIT KVK // ID A7VAJ5_BACUN Unreviewed; 921 AA. AC A7VAJ5; DT 23-OCT-2007, integrated into UniProtKB/TrEMBL. DT 23-OCT-2007, sequence version 1. DT 01-APR-2015, entry version 41. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EDO52072.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EDO52072.1}; GN Name=metH {ECO:0000313|EMBL:EDO52072.1}; GN ORFNames=BACUNI_04626 {ECO:0000313|EMBL:EDO52072.1}; OS Bacteroides uniformis ATCC 8492. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=411479 {ECO:0000313|EMBL:EDO52072.1}; RN [1] {ECO:0000313|EMBL:EDO52072.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 8492 {ECO:0000313|EMBL:EDO52072.1}; 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 (JUN-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EDO52072.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 8492 {ECO:0000313|EMBL:EDO52072.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EDO52072.1}. 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; AAYH02000049; EDO52072.1; -; Genomic_DNA. DR ProteinModelPortal; A7VAJ5; -. DR SMR; A7VAJ5; 657-899. DR EnsemblBacteria; EDO52072; EDO52072; BACUNI_04626. DR PATRIC; 27181325; VBIBacUni30129_4018. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EDO52072.1}; KW Transferase {ECO:0000313|EMBL:EDO52072.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 243 243 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 765 765 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 921 AA; 100969 MW; E4C7D93423962C06 CRC64; MSKLGSLVRE RILILDGAMG TMIQQYNLTE EDFRDERFSQ IPGQMKGNND LLCLTRPDVI QDIHRKYLAA GADIIETNTF SSTRVSMADY HVQDYVREMN LAAVRLARKV ADEFTSLTPD KPRFVAGSVG PTNKTCSMSP DVNNPAFRAL SYDELADAYR EQMEALLEGG VDALLIETIF DTLNAKAAIF AAGQAMETVG VHVPLMLSVT VSDIGGRTLS GQTLDAFLAS VQHADIFSVG LNCSFGARQL KPFLEQLAVR APYYISAYPN AGLPNSLGTY DQTPADMAHE VKEYIHEGLV NIIGGCCGTT DAYIAEYSSL IAGATPHQPV PRPENLWLSG LELLEVKPEN NFVNVGERCN VAGSRKFLRL INEKKYDEAL SIARQQVEDG AQVIDINMDD GLLDAQVEMT AFLHLIASEP EIARVPVMID SSKWEVIVAG LKCLQGKSIV NSISLKEGED KFLEHARTIK QYGAAAVVMA FDEKGQADTY ERKIEVCERA YRLLVDKIGF NPHDIIFDPN VLAVATGMDE HNNYAVDFIR ATGWIRKNLP GAHVSGGVSN LSFSFRGNNY IREAMHAVFL YYAIREGMDM GIVNPATSVL YTDIPADILE RIEDVVLNRR PDAAERLIET AERLKAEAEA AKTSGGERQA AAHSQLAWRE GTPVEERLKY ALTKGIGDYL EEDLAEALKL YPKAVSIIEG PLMAGMNHVG DLFGAGKMFL PQVVKTARTM KRAVAILQPV IESEKEEGAT AAGKVLLATV KGDVHDIGKN IVSVVMACNG YDIVDLGVMV PAETIVQHAI EEKVDMIGLS GLITPSLDEM VHVAIELEKA GLDVPLLIGG ATTSPLHTAL KIAPVYHAPV IHLKDASQNA TVAAKLMNPK TKEELEEELH EKYRQLCEKN REKQVTTVSL EEARKNKLNL F // ID A7VBG6_9CLOT Unreviewed; 807 AA. AC A7VBG6; DT 23-OCT-2007, integrated into UniProtKB/TrEMBL. DT 23-OCT-2007, sequence version 1. DT 27-MAY-2015, entry version 34. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EDO59169.1}; GN ORFNames=CLOL250_00227 {ECO:0000313|EMBL:EDO59169.1}; OS Clostridium sp. L2-50. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=411489 {ECO:0000313|EMBL:EDO59169.1}; RN [1] {ECO:0000313|EMBL:EDO59169.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=L2-50 {ECO:0000313|EMBL:EDO59169.1}; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Clostridium sp. L2-50."; RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EDO59169.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=L2-50 {ECO:0000313|EMBL:EDO59169.1}; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., 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. {ECO:0000313|EMBL:EDO59169.1}. 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; AAYW02000002; EDO59169.1; -; Genomic_DNA. DR RefSeq; WP_008400900.1; NZ_DS480316.1. DR ProteinModelPortal; A7VBG6; -. DR EnsemblBacteria; EDO59169; EDO59169; CLOL250_00227. DR PATRIC; 27241612; VBICloSp41567_0824. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDO59169.1}; KW Transferase {ECO:0000313|EMBL:EDO59169.1}. SQ SEQUENCE 807 AA; 88065 MW; 43BD5A1B61AEEF3B CRC64; MNKHEFRQLF DEKILILDGA TGTNLMNAGM PLGVCPEKYI LEHKEVMLEL QTSYLNAGTD ILYAPTFTCN RLKLREYGLE NNLYQMNMDL VALSKQAVAE CGHGYVAGDL TMTGEMLYPM GKLQFEELVD IYKEQIKVLV EAGCDLLVVE TMMSLAETRA AVIAANEICD LPVMASLTFN EDGRTLYGTD PVTAVNVLQN LGVDAIGVNC STGPDKMTEL VAAMKEVAFV PVFAKPNAGM PELVDGKSVY AMTPETFAED MKMIIEAGAG MVGGCCGTTP AHIKALSDMA KTMDIPEISD KKERLLSSER MTRQISLDGP FMVVGERINP TGKKKLQAEL REGVLDTVMT MAEEQMEKGA SILDINVGMN GIDEKEMMVR VVYEVSQAVN LPLCIDSSNP AVIEAALRIY PGRALVNSVS LEKVKMQEIL PLVSKYGAMF ILLPLSDEGL PKDSDEKENI IHTVLDAAYK MGFQKEDVVV DGLVATVGAE KAAAVNCLKT IRYCHDMGLA TICGLSNISF GLPERMFVNA AFLTMAIQNG LTMAIANPSQ TMLMNMAYAS DMLLNKDEGD IRYIQNVKPL GITTAAPVQN GGSQEDEKEK SVIYTDVVKG NKRNISEDVK KELEQGIDPQ KIIDDELIPA INRVGKLFEQ KKYFLPQLIA SAETMELAIN QITPLIVRED DGKAMPAIVV ATVEGDIHDI GKNLVVLMLR NYGFPVIDLG KDVPADVIVD AAIENDAKVI GLSALMTTTM MKMVDVVELV KEKNLDIKVV IGGAVITESF AEEIHADGYS EDAAECVQVV KRLLDIE // ID A7VDU6_9CLOT Unreviewed; 600 AA. AC A7VDU6; DT 23-OCT-2007, integrated into UniProtKB/TrEMBL. DT 23-OCT-2007, sequence version 1. DT 07-JAN-2015, entry version 33. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=CLOL250_01084 {ECO:0000313|EMBL:EDO58358.1}; OS Clostridium sp. L2-50. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=411489 {ECO:0000313|EMBL:EDO58358.1}; RN [1] {ECO:0000313|EMBL:EDO58358.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=L2-50 {ECO:0000313|EMBL:EDO58358.1}; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Clostridium sp. L2-50."; RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EDO58358.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=L2-50 {ECO:0000313|EMBL:EDO58358.1}; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Hodges J., RA Shah N., Mardis E.R., Wilson R.K.; RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDO58358.1}. 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; AAYW02000007; EDO58358.1; -; Genomic_DNA. DR RefSeq; WP_008401807.1; NZ_DS480321.1. DR ProteinModelPortal; A7VDU6; -. DR EnsemblBacteria; EDO58358; EDO58358; CLOL250_01084. DR PATRIC; 27243171; VBICloSp41567_1572. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EDO58358.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EDO58358.1}. SQ SEQUENCE 600 AA; 66342 MW; 8A542749A31E8C40 CRC64; MRLKEYIQTK RIIADGAFGT YYMSLYGDGS KPEKGLAISN LPELANITAP ERVIGIHTEY IEAGAQLIRT NTFASNTKSL LSDTEAVKEN IRAAVTCAKA AAEKAEHEIY IAGDIGPIPA EGVPHSDNLT KEYIMIGETF IEQGIDILLF ETFPELETIL PAIAYLKETH DCTILVHFSV NQFGYSNTGL SAKRLIADAE ACRYIDGTGL NCGVGPGHMK KLIRKISADD ATFLSVFPNS GYPKYLNNRL TFTDNAEYFA EKISEIAESG ICIFGGCCGT TPDYIRKIAA GISLDYPVGS RETVAEVTVS SEKPAYGFME RRVKDPSHKL VAVELVPPLN ADDEKLLDAA HILKNAEVDV VTFPDSPSGR TRADSVLMAE KIRLETGLCV MPHICCRDKN AIAIRSTILG ASLNHITNFL LLTGDPVPVL FRQTTKSVFN FDSVGMMKIV QEMNSDTFSE HPVTYGGAIN HNRMNTKAET ERIRRKMAAG ATFFMTQPIF SAEQAEIIRQ MKKETGATIL VGLMPLVSRK NAVFMKNEMT GIEIPDSVID RYREDMNREE GENCGIRLAR EFMAMTDDFA DGYYFSFPFN RVHMLKKILG // ID A7VPD0_9FIRM Unreviewed; 600 AA. AC A7VPD0; DT 23-OCT-2007, integrated into UniProtKB/TrEMBL. DT 23-OCT-2007, sequence version 1. DT 27-MAY-2015, entry version 34. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=CLOLEP_00406 {ECO:0000313|EMBL:EDO62817.1}; OS [Clostridium] leptum DSM 753. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminiclostridium. OX NCBI_TaxID=428125 {ECO:0000313|EMBL:EDO62817.1}; RN [1] {ECO:0000313|EMBL:EDO62817.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 753 {ECO:0000313|EMBL:EDO62817.1}; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Clostridium leptum (DSM 753)."; RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EDO62817.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 753 {ECO:0000313|EMBL:EDO62817.1}; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Wang C., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDO62817.1}. 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; ABCB02000012; EDO62817.1; -; Genomic_DNA. DR RefSeq; WP_003527756.1; NZ_DS480341.1. DR ProteinModelPortal; A7VPD0; -. DR EnsemblBacteria; EDO62817; EDO62817; CLOLEP_00406. DR PATRIC; 30581937; VBICloLep22705_0324. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EDO62817.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EDO62817.1}. SQ SEQUENCE 600 AA; 66500 MW; 39CFD669610D0B29 CRC64; MNLDTLLKQK RPVITDGAMG TYFTQKTGFS IHECEWANIS RPELISEIHR EYVKAGAQFL RTNTFSANTK SLGRPLADVL EIVRAGYRLA KEAAGCQAVA AADMTAIYPR GDEETDLLPE YLAIADAFLS EGAEVFLFET LTELSPFDQI ADYLKKKKPE CKVLISFTVS PEGITRLGVP LRRLLDEVKP HRELFDGIGL NCGCGPAHIL KFARELLSYS RQYLSLPVLV MPNAGYPAME ENRTVFDTSP EYFSHQAVRI AELGVDMIGG CCGTTPKHLQ LLSRLIQKKR EPLAAVTTTV TAVGSLEKSA PQESRFAQKL RKGDFVMAAE LDPPYGSRVD KLLTACRVLQ NSGVDIVTIS DSPMARVKLD PVVCGAKLQR ETGMEVLPHF CCRDRNVNAL RAMLLGAQCE NIRTILAVTG DHVPELDRGY IKPVFNVTSA KLMEMISQMN QDVFADSPFT IGGAFNPNVA NPKAELARLE KKLKAGAVFF LTQPVFDEGR ISTVKEAREM GAKMLLGIMP LVSYRNAVYM NNEVPGIQIP TAYVNRFSPE MSREEAQRTG IEIALEIAES LRPHADGFYF MTPFNRAEIV AELIEKCREM // ID A7VWF8_9FIRM Unreviewed; 408 AA. AC A7VWF8; DT 23-OCT-2007, integrated into UniProtKB/TrEMBL. DT 23-OCT-2007, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EDO60105.1}; GN ORFNames=CLOLEP_02923 {ECO:0000313|EMBL:EDO60105.1}; OS [Clostridium] leptum DSM 753. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminiclostridium. OX NCBI_TaxID=428125 {ECO:0000313|EMBL:EDO60105.1}; RN [1] {ECO:0000313|EMBL:EDO60105.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 753 {ECO:0000313|EMBL:EDO60105.1}; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Clostridium leptum (DSM 753)."; RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EDO60105.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 753 {ECO:0000313|EMBL:EDO60105.1}; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Wang C., RA 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. {ECO:0000313|EMBL:EDO60105.1}. 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; ABCB02000020; EDO60105.1; -; Genomic_DNA. DR RefSeq; WP_003532436.1; NZ_DS480349.1. DR ProteinModelPortal; A7VWF8; -. DR EnsemblBacteria; EDO60105; EDO60105; CLOLEP_02923. DR PATRIC; 30585903; VBICloLep22705_2263. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDO60105.1}; KW Transferase {ECO:0000313|EMBL:EDO60105.1}. SQ SEQUENCE 408 AA; 43986 MW; C3690FF866D88CBE CRC64; MSFPFHLPLI LDGATGTNLI AAGMPSGVCV EQWILEHPEK LLALQRAFLE AGSNAVMAPT FGANREKLAA YGLQDQVEEI NLKLVALSKE AAEPFHALVG GDVSPAGVMI EPYGDLTFDE LYDIYLEQIR ALKKAGVDFI ALETQMSLAD LRAGVLAAKE AGLPVFATIT VEDNGRTIMG TKFLPVLITL QALGAAAVGL NCSTGPEVME ELLEGAVSHA QVPLIAKPNA GKPSQEDPAV YPLSPAEFAE KMESLLAAGA QIVGGCCGST PEHIRELAQT VENTYRELAP QEPDHFAAAI ESESFFLGDD ISLSEPLECS YDLGDDLIDI EDEQVNAALV EVNSIDDAKL LIENASMTRL PIVVRIHNLD VLEYTLRNFQ GRLIVDSACD LEEEEMRPIV DYYGAILY // ID A7XLV2_PERFV Unreviewed; 401 AA. AC A7XLV2; DT 23-OCT-2007, integrated into UniProtKB/TrEMBL. DT 23-OCT-2007, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=Betaine homocysteine S-methyltansferase {ECO:0000313|EMBL:ABU63967.1}; OS Perca flavescens (American yellow perch) (Morone flavescens). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Percoidei; Percidae; Percinae; Perca. OX NCBI_TaxID=8167 {ECO:0000313|EMBL:ABU63967.1}; RN [1] {ECO:0000313|EMBL:ABU63967.1} RP NUCLEOTIDE SEQUENCE. RA Goetz F.W., Shepherd B., Rise M.; RT "Genes derived from estrogen stimulated yellow perch."; RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EU081830; ABU63967.1; -; mRNA. DR ProteinModelPortal; A7XLV2; -. DR SMR; A7XLV2; 5-395. DR HOVERGEN; HBG080367; -. DR UniPathway; UPA00051; UER00083. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 210 210 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 292 292 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 401 AA; 44252 MW; BF2DA33CDE017D29 CRC64; MAPGKKGIIE RLNAGEVVIG DGGFVFALEK RGYVKAGPWT PEASVTHPEA VRQLHREFLR AGSNVMQTFT FYASDDKLEN RGQNLRLSGV QINEAACDLA REVASEGDAM VAGGVCQTPS YLSCKSEIEV KAIFKKQLEV FMKKNVDFLI AEYFEHVEEA EWAVQVLKTS GKPVAASLCI GPEGDMHGVS PGECAVRLVK AGAQIVGVNC HFDPMTCVKT VKMMKEGVEK AGLKAHYMVQ PLAYHTPDCN CQGFIDLPEF PFALEPRILT RWDMHTYARV AYKAGIRFIG GCCGFEPYHI RAIAEELSIE RGIMPPASEK HGMWGAGLEM HTKPWVRARA RRDYWEHLSP ASGRPTCPSM STPEGWGVTK GHADLLQHKE ATSTQEMKHV LEMQKKAKSS A // ID A7Z101_BACA2 Unreviewed; 315 AA. AC A7Z101; DT 23-OCT-2007, integrated into UniProtKB/TrEMBL. DT 23-OCT-2007, sequence version 1. DT 27-MAY-2015, entry version 41. DE SubName: Full=YbgG {ECO:0000313|EMBL:ABS72677.1}; GN Name=ybgG {ECO:0000313|EMBL:ABS72677.1}; GN OrderedLocusNames=RBAM_002780 {ECO:0000313|EMBL:ABS72677.1}; OS Bacillus amyloliquefaciens subsp. plantarum (strain DSM 23117 / BGSC OS 10A6 / FZB42). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=326423 {ECO:0000313|EMBL:ABS72677.1, ECO:0000313|Proteomes:UP000001120}; RN [1] {ECO:0000313|EMBL:ABS72677.1, ECO:0000313|Proteomes:UP000001120} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 23117 / BGSC 10A6 / FZB42 RC {ECO:0000313|Proteomes:UP000001120}; 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 ----------------------------------------------------------------------- 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; ABS72677.1; -; Genomic_DNA. DR RefSeq; WP_011996257.1; NC_009725.1. DR RefSeq; YP_001419908.1; NC_009725.1. DR ProteinModelPortal; A7Z101; -. DR STRING; 326423.RBAM_002780; -. DR EnsemblBacteria; ABS72677; ABS72677; RBAM_002780. DR KEGG; bay:RBAM_002780; -. DR PATRIC; 18745459; VBIBacAmy31356_0242. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; BAMY326423:GCM4-276-MONOMER; -. DR Proteomes; UP000001120; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001120}. SQ SEQUENCE 315 AA; 34381 MW; 953EC1AB0B927D50 CRC64; MNPITQILNE YPVMIIDGAM ATELERMGCD LHDDLWSAKI LLERPELIKQ VHAEYFAAGA DCAITASYQS TIEGFAARGI PETDAIRLIQ TSVELAAQAR DEFWAHEENR LHRPKPLVAA SIGPYGASLA DGSEYRGHYG LTEDELISFH RPRMKALIES GADLLACETI PCLSEAKAIT RLLEEFPGTY AWISFSAKDG RHISEGTPIS ECAALLDSCS QIAAIGINCT PIEHIPPLIE EIKRAASKPI IAYPNSGEQY DPVTKTWKGA ACENNFGKSA QGWYENGVSL IGGCCRTKPA DIQAIADWAK TLKTT // ID A7Z390_BACA2 Unreviewed; 613 AA. AC A7Z390; DT 23-OCT-2007, integrated into UniProtKB/TrEMBL. DT 23-OCT-2007, sequence version 1. DT 27-MAY-2015, entry version 54. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN Name=yitJ {ECO:0000313|EMBL:ABS73466.1}; GN OrderedLocusNames=RBAM_011020 {ECO:0000313|EMBL:ABS73466.1}; OS Bacillus amyloliquefaciens subsp. plantarum (strain DSM 23117 / BGSC OS 10A6 / FZB42). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=326423 {ECO:0000313|EMBL:ABS73466.1, ECO:0000313|Proteomes:UP000001120}; RN [1] {ECO:0000313|EMBL:ABS73466.1, ECO:0000313|Proteomes:UP000001120} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 23117 / BGSC 10A6 / FZB42 RC {ECO:0000313|Proteomes:UP000001120}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ABS73466.1; -; Genomic_DNA. DR RefSeq; WP_012117262.1; NC_009725.1. DR RefSeq; YP_001420697.1; NC_009725.1. DR ProteinModelPortal; A7Z390; -. DR STRING; 326423.RBAM_011020; -. DR EnsemblBacteria; ABS73466; ABS73466; RBAM_011020. DR KEGG; bay:RBAM_011020; -. DR PATRIC; 18747193; VBIBacAmy31356_1075. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; BAMY326423:GCM4-1100-MONOMER; -. DR Proteomes; UP000001120; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001120}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 613 AA; 68361 MW; 47478D320614B447 CRC64; MGLLQDLKER ILIGDGAMGT LLYSYGIDRC FEELNVSKPE EIKRIHKAYV EAGADIIQTN TYGANFIKLS RYGLEDETKK INQEAVRIAR ASSDGAYVLG TMGGIRTFNK NAYSLEEIKR SFREQLYLLL HEEPDGLLLE TYYDLEEARE VLKIARKETE LPIMLNVSMH EQGVLQDGTP LWEALRSIAD LGADIAGINC RLGPYHMIEA LTEVPIFRDA YLSVYPNSSL PSLEEGRLVY DTDDAYFRES AVQFRTQGAR IIGGCCGTTP NHIRAMAEAV RGLSPVTEKE VKIRREEEVI SVSNERTEPG LNEIAAQKRS IIVELDPPKK LNFDKFLQAA AELKETGIEA LTLADNSLAT PRISNAACGS LLKERLDIRS LVHITCRDRN IIGLQSHLMG LDTLGLTDIL AITGDPSKIG DFPGATSVYD LTSFDLIRLI KQFNEGISLS GKPLGKKTNF SVAGAFNPNV RHLDKAVKRL EKKIECGADY FVSQPVYSEQ QLIDIHHETK HLKTPVYIGI MPLTSSRNAE FIHHEIPGIK LSDSIREKMA LAGEDKRKQK AEGLAIAKSL LDTACELFNG IYLITPFLRS DLTSELAAYI KQKDEKRADV YLH // ID A7ZUN3_ECO24 Unreviewed; 1227 AA. AC A7ZUN3; DT 23-OCT-2007, integrated into UniProtKB/TrEMBL. DT 23-OCT-2007, sequence version 1. DT 27-MAY-2015, entry version 62. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABV17810.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABV17810.1}; GN Name=metH {ECO:0000313|EMBL:ABV17810.1}; GN OrderedLocusNames=EcE24377A_4563 {ECO:0000313|EMBL:ABV17810.1}; OS Escherichia coli O139:H28 (strain E24377A / ETEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=331111 {ECO:0000313|EMBL:ABV17810.1, ECO:0000313|Proteomes:UP000001122}; RN [1] {ECO:0000313|Proteomes:UP000001122} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=E24377A / ETEC {ECO:0000313|Proteomes:UP000001122}; 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 ----------------------------------------------------------------------- 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; ABV17810.1; -; Genomic_DNA. DR RefSeq; WP_000096011.1; NC_009801.1. DR RefSeq; YP_001465512.1; NC_009801.1. DR ProteinModelPortal; A7ZUN3; -. DR SMR; A7ZUN3; 6-639, 651-1227. DR STRING; 331111.EcE24377A_4563; -. DR EnsemblBacteria; ABV17810; ABV17810; EcE24377A_4563. DR KEGG; ecw:EcE24377A_4563; -. DR PATRIC; 18298392; VBIEscCol31211_4772. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; ECOL331111:GH7P-4545-MONOMER; -. DR Proteomes; UP000001122; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001122}; KW Methyltransferase {ECO:0000313|EMBL:ABV17810.1}; KW Transferase {ECO:0000313|EMBL:ABV17810.1}. SQ SEQUENCE 1227 AA; 135997 MW; 91F0CAA1E9127D9A CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAD // ID A8AKB5_CITK8 Unreviewed; 310 AA. AC A8AKB5; DT 23-OCT-2007, integrated into UniProtKB/TrEMBL. DT 23-OCT-2007, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ABV13928.1}; GN OrderedLocusNames=CKO_02822 {ECO:0000313|EMBL:ABV13928.1}; OS Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Citrobacter. OX NCBI_TaxID=290338 {ECO:0000313|EMBL:ABV13928.1, ECO:0000313|Proteomes:UP000008148}; RN [1] {ECO:0000313|EMBL:ABV13928.1, ECO:0000313|Proteomes:UP000008148} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696 RC {ECO:0000313|Proteomes:UP000008148}; 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 ----------------------------------------------------------------------- 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; ABV13928.1; -; Genomic_DNA. DR RefSeq; WP_012133641.1; NC_009792.1. DR STRING; 290338.CKO_02822; -. DR EnsemblBacteria; ABV13928; ABV13928; CKO_02822. DR KEGG; cko:CKO_02822; -. DR PATRIC; 20388323; VBICitKos71230_2361. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; CKOS290338:GJ8L-2815-MONOMER; -. DR Proteomes; UP000008148; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008148}; KW Reference proteome {ECO:0000313|Proteomes:UP000008148}. SQ SEQUENCE 310 AA; 33439 MW; FCAB55305A9B1954 CRC64; MSQHNPLSAI LDKQDFLLLD GAMATELEAR GCDLADSLWS AKVLVENPAL IREVHLDYYR AGAQCAITAS YQATPAGLAA RGFDEAQSKA LIGKSVELAR KAREAYLAEN PQAGTLLVAG SVGPYGAYLA DGAEYRGDYV CTPETFQAFH RPRVEALLDA GVDLLACETL PNFIEIKALA ELLTEYPRAR AWFSFTLRDS EHLSDGTPLR DVAAFLNACP QVVATGVNCI ALENVTAALQ HLHGLTALPL VVYPNSGERY DAVSKTWHHH GEACATLAEY LPQWLAAGAK LIGGCCRTTP KDIAELNAQR // ID A8ANB5_CITK8 Unreviewed; 1247 AA. AC A8ANB5; DT 23-OCT-2007, integrated into UniProtKB/TrEMBL. DT 23-OCT-2007, sequence version 1. DT 27-MAY-2015, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ABV14978.1}; GN OrderedLocusNames=CKO_03902 {ECO:0000313|EMBL:ABV14978.1}; OS Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Citrobacter. OX NCBI_TaxID=290338 {ECO:0000313|EMBL:ABV14978.1, ECO:0000313|Proteomes:UP000008148}; RN [1] {ECO:0000313|EMBL:ABV14978.1, ECO:0000313|Proteomes:UP000008148} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696 RC {ECO:0000313|Proteomes:UP000008148}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000822; ABV14978.1; -; Genomic_DNA. DR RefSeq; WP_012134672.1; NC_009792.1. DR ProteinModelPortal; A8ANB5; -. DR SMR; A8ANB5; 671-1247. DR STRING; 290338.CKO_03902; -. DR EnsemblBacteria; ABV14978; ABV14978; CKO_03902. DR KEGG; cko:CKO_03902; -. DR PATRIC; 20390198; VBICitKos71230_3270. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CKOS290338:GJ8L-3893-MONOMER; -. DR Proteomes; UP000008148; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008148}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008148}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 267 267 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 330 330 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 331 331 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 779 779 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1247 AA; 138342 MW; 492E2D1A5BC1266C CRC64; MPVWFVGLFS VQVECCREQV VSSKVEQLRA QLDERILVLD GGMGTMIQSY RLSEEDFRGE RFADWPCDLK GNNDLLVLSK PEVITAIHHA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFTAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNISFDQLV AAYRESTKAL VEGGSDLILI ETVFDTLNAK AAVFAVKEEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LARIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE SGFLNIVGGC CGTTPEHIAA MSRAVDGLAP RKLPDIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VESGAQIIDI NMDEGMLDAE VAMVRFLNLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVETFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYNILTK EVGFPPEDII FDPNIFAVAT GIDEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDSTER LLALAEKYRG SKADDSANAQ QAEWRSWEVK KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGSSNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIIDL GVMVPAEKIL KTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSETQHDEFV ARTRKEYETV RIQHARKKPR TPPVTLAAAR DNDLAFDWES YTPPVAHRLG VQDVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG EEAKRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVLAVSHHLR QQTEKVGFAN YCLSDFVAPK QSGKEDYIGA FAVTGGLEED ALAEAFEAQH DDYNKIMVKA IADRLAEAFA EYLHERVRKV YWGYAANENL SNEELIRENY QGIRPAPGYP ACPEHTEKGT IWQLLDVEKH TGMKLTESYA MWPGASVSGW YFSHPDSKYY TVAQIQRDQV EDYAQRKGMT VAEVERWLAS NLGYDAD // ID A8DVQ8_NEMVE Unreviewed; 314 AA. AC A8DVQ8; DT 13-NOV-2007, integrated into UniProtKB/TrEMBL. DT 13-NOV-2007, sequence version 1. DT 27-MAY-2015, entry version 43. DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EDO25701.1}; DE Flags: Fragment; GN ORFNames=v1g156669 {ECO:0000313|EMBL:EDO25701.1}; OS Nematostella vectensis (Starlet sea anemone). OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria; OC Edwardsiidae; Nematostella. OX NCBI_TaxID=45351 {ECO:0000313|Proteomes:UP000001593}; RN [1] {ECO:0000313|EMBL:EDO25701.1, ECO:0000313|Proteomes:UP000001593} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593}; RX PubMed=17615350; DOI=10.1126/science.1139158; RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., RA Salamov A., Terry A., Shapiro H., Lindquist E., Kapitonov V.V., RA Jurka J., Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., RA Finnerty J.R., Technau U., Martindale M.Q., Rokhsar D.S.; RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and RT genomic organization."; RL Science 317:86-94(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; DS478507; EDO25701.1; -; Genomic_DNA. DR RefSeq; XP_001617801.1; XM_001617751.1. DR STRING; 45351.JGI156669; -. DR EnsemblMetazoa; EDO25701; EDO25701; NEMVEDRAFT_v1g156669. DR GeneID; 5495977; -. DR KEGG; nve:NEMVE_v1g156669; -. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR InParanoid; A8DVQ8; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG7TF786; -. DR Proteomes; UP000001593; Unassembled WGS sequence. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001593}; KW Reference proteome {ECO:0000313|Proteomes:UP000001593}. FT NON_TER 314 314 {ECO:0000313|EMBL:EDO25701.1}. SQ SEQUENCE 314 AA; 34567 MW; 346327004FFB5CCF CRC64; MKEIQSILKE RILVLDGAMG TMIQRHALEE EDFRRGWFEN HHKPLKGNND LLSLTRPDII KEIHSLYFEA GADIAETNTF SGTTIAQADY DLEDAVYDIN FHSAKIAREV ADEFTAREPH KPRFVAGSMG PTNRTASISP DVNDPGYRAI TFNELVTAYK QQANALIDGG VDLLLVETVF DTLNAKAALF AIDEVYEERN VNLPIMVSGT ITDQSGRTLT GQTTEAFLIS ISHMNLLTVG LNCALGASMM RPYLQILDKK APFGVSAHPN AGLPNEFGEY DETAEMMAEQ IKEFLEEGLV NIIGGCCGTT PAHI // ID A8DW65_NEMVE Unreviewed; 142 AA. AC A8DW65; DT 13-NOV-2007, integrated into UniProtKB/TrEMBL. DT 13-NOV-2007, sequence version 1. DT 07-JAN-2015, entry version 34. DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EDO25545.1}; DE Flags: Fragment; GN ORFNames=v1g157096 {ECO:0000313|EMBL:EDO25545.1}; OS Nematostella vectensis (Starlet sea anemone). OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria; OC Edwardsiidae; Nematostella. OX NCBI_TaxID=45351 {ECO:0000313|Proteomes:UP000001593}; RN [1] {ECO:0000313|EMBL:EDO25545.1, ECO:0000313|Proteomes:UP000001593} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593}; RX PubMed=17615350; DOI=10.1126/science.1139158; RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., RA Salamov A., Terry A., Shapiro H., Lindquist E., Kapitonov V.V., RA Jurka J., Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., RA Finnerty J.R., Technau U., Martindale M.Q., Rokhsar D.S.; RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and RT genomic organization."; RL Science 317:86-94(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; DS479194; EDO25545.1; -; Genomic_DNA. DR RefSeq; XP_001617645.1; XM_001617595.1. DR STRING; 45351.JGI157096; -. DR EnsemblMetazoa; EDO25545; EDO25545; NEMVEDRAFT_v1g157096. DR GeneID; 5495801; -. DR KEGG; nve:NEMVE_v1g157096; -. DR eggNOG; COG0646; -. DR InParanoid; A8DW65; -. DR OMA; EVANEFT; -. DR OrthoDB; EOG7TF786; -. DR Proteomes; UP000001593; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001593}; KW Reference proteome {ECO:0000313|Proteomes:UP000001593}. FT NON_TER 142 142 {ECO:0000313|EMBL:EDO25545.1}. SQ SEQUENCE 142 AA; 16007 MW; AAC8D7F468AA9F2D CRC64; MSNIYQELQK RILVLDGAMG TMLQEFKFTE EDFRGERFKE YSTPLQGNND LLSITQPEAV KEVHRKYFAA GADIVETNTF SGTTIAMADY QLEELVYELN YQSAKIAKEV ANEFTAKEPH KPRFVAGSIG PTNRTASMSP DV // ID A8ER28_ARCB4 Unreviewed; 1159 AA. AC A8ER28; DT 13-NOV-2007, integrated into UniProtKB/TrEMBL. DT 13-NOV-2007, sequence version 1. DT 27-MAY-2015, entry version 64. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:ABV66402.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABV66402.1}; GN Name=metH {ECO:0000313|EMBL:ABV66402.1}; GN OrderedLocusNames=Abu_0117 {ECO:0000313|EMBL:ABV66402.1}; OS Arcobacter butzleri (strain RM4018). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Arcobacter. OX NCBI_TaxID=367737 {ECO:0000313|EMBL:ABV66402.1, ECO:0000313|Proteomes:UP000001136}; RN [1] {ECO:0000313|EMBL:ABV66402.1, ECO:0000313|Proteomes:UP000001136} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RM4018 {ECO:0000313|EMBL:ABV66402.1, RC ECO:0000313|Proteomes:UP000001136}; RX PubMed=18159241; DOI=10.1371/journal.pone.0001358; RA Miller W.G., Parker C.T., Rubenfield M., Mendz G.L., Woesten M.M.S.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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000361; ABV66402.1; -; Genomic_DNA. DR RefSeq; WP_012012017.1; NC_009850.1. DR RefSeq; YP_001489071.1; NC_009850.1. DR ProteinModelPortal; A8ER28; -. DR STRING; 367737.Abu_0117; -. DR EnsemblBacteria; ABV66402; ABV66402; Abu_0117. DR KEGG; abu:Abu_0117; -. DR PATRIC; 20961592; VBIArcBut20197_0117. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; ABUT367737:GHWO-117-MONOMER; -. DR Proteomes; UP000001136; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001136}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABV66402.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001136}; KW Transferase {ECO:0000313|EMBL:ABV66402.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 223 223 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 728 728 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1159 AA; 129402 MW; B99C017968DBD748 CRC64; MEELIKNLID KRVLIIDGAM GTQLQIADIK KEEWFFEDLD LEGCNELLNL TAPHILETIH DNYAKAGADL ISTNTFGSMP WVLDEYNIGH MSYELSKLGA SLVKKSCEKF STPEKPRFCL ASIGPGTKLP SLGHIKYDEM YEGYKIMAKG LVDGGTDIFL LETCQDPLQI KAALHALNDV APNIPIMVSV TIELSGTMLI GTDAMTIAAI MAPFNILSLG FNCGTGPVQV HKHVKTLSQV CKFPISVHSN AGLPQNRGGK TYYPMQPEEF TALQKEFLKI NGVSFLGGCC GTTPEHIEAL AKAVENEIPL KPCGFLKASL ASLFNIVPLK QEPAPLLIGE RSNATGSKAF RELLKANDYE GTLSVAQQQV RAGAHVIDVS VGFAGRDERF DMDEVVSLYS QKIALPLMPD STQILALEAA LKQIGGRCII NSVNLEDGIE KFDAVCSLAK KFGAALVCLV IDEIGMAKSK ERKLEVAERI FDLCVNRHGF DPADLVFDML TFTIGSGDDE YRTAGIETLE AIREFEIRHP EVGTTLGLSN ISFGLATNAR IYLNSIYLDH CVKAGLTSAI VNVKHILPLN KISEEDKKAC DNLIFNIWEN GADPLFAFIE HFSNVEGQEE QSDEEYQKLE PIEKVKKLLL DGDKERLIPL ALELRHTISP EIIVNEWLID GMKVIGELFG SGQMQLPFVL QSAETMKACV DSLNPYLPKQ EKASETTLIL GTVKGDVHDV GKNLVDIILS NNGFKVVNVG IKADLGQFVE ELNKHNAHAI GMSGLLVKST AVMKENLEEL QKLGIKVPVL LGGAALTKNF VDEYCRTIYD GPIFYCRDAF DGVVSMQRIE KGDENNTALA ADLIERIDTS DRVEKEEIEI PSYEEISMPE RGKFVFPPIW DRVTKRGEKL NKELIFKWIN HRVLFRQRWG YKRGKQTPEA FMKYERDVVE PTYEALKAEL VDKDIFDPIA IYAYYPCISH DNKLYIFDKK YLFNSLEESK NIPPLSEAIK VLEFPRQKRK PFRCIPDFFA NDRLDVVAFT LASAGLKITD YERSLYDNGE FTKYYQVHGL GVELAEALAE VLHKQIRLDL DIVPNEGHTL NDVQMKQYVG CRYSPGYAAC PDLAMNRDIF DLLNPEEFGI ELSETFQMHP EQTTCAIVVT NPEANYYNV // ID A8F6Y8_THELT Unreviewed; 773 AA. AC A8F6Y8; DT 13-NOV-2007, integrated into UniProtKB/TrEMBL. DT 13-NOV-2007, sequence version 1. DT 27-MAY-2015, entry version 52. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABV33922.1}; GN OrderedLocusNames=Tlet_1365 {ECO:0000313|EMBL:ABV33922.1}; OS Thermotoga lettingae (strain ATCC BAA-301 / DSM 14385 / TMO). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=416591 {ECO:0000313|EMBL:ABV33922.1, ECO:0000313|Proteomes:UP000002016}; RN [1] {ECO:0000313|EMBL:ABV33922.1, ECO:0000313|Proteomes:UP000002016} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-301 / DSM 14385 / TMO RC {ECO:0000313|Proteomes:UP000002016}; 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., Bruce D., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nelson K., RA Gogarten J.P., Noll K., Richardson P.; RT "Complete sequence of Thermotoga lettingae TMO."; 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; CP000812; ABV33922.1; -; Genomic_DNA. DR RefSeq; WP_012003398.1; NC_009828.1. DR RefSeq; YP_001470986.1; NC_009828.1. DR ProteinModelPortal; A8F6Y8; -. DR STRING; 416591.Tlet_1365; -. DR EnsemblBacteria; ABV33922; ABV33922; Tlet_1365. DR KEGG; tle:Tlet_1365; -. DR PATRIC; 23933365; VBITheLet125395_1431. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; TLET416591:GI64-1396-MONOMER; -. DR Proteomes; UP000002016; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002016}; KW Methyltransferase {ECO:0000313|EMBL:ABV33922.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002016}; KW Transferase {ECO:0000313|EMBL:ABV33922.1}. SQ SEQUENCE 773 AA; 85937 MW; F7A2C2069D46345C CRC64; MRRNEFFQLL QERVLFLDGA YGTEFFKRGV NGLIELLNIE DPEEVQKLHR EYIEAGSDII LTNTFSANRL KLRAYNLEKD LERININAVK IAKSVSGGKF VFGDISSTGN FISPLGNLDF EEAYEVFKEQ ASLLIEAGVD GIILETMSDL KELKAAIIAV RDLSHEIPLI AHMTFEADGK TVSGTSIEIF ATLMNDLDVD VVGINCSLEP DEMLPVFTKL SELSMKPLCV EPNAGKPILE KGRLSYKTAP KEFAVYMADF IELGANIVGG CCGTGPEHIK VMCKYIGNQK PRKRQVKREQ YLSSRTILRP TDTFLVIGER INASGRKKLQ TKIQQMDFSQ VVELSQLQEQ EGCDAIDLNF GIEKLLTHDH FRRAIVELDK RSSLPVSFDI QNLQFLESAM REYAGRGLIN SAFAREDHLE ERIRLLKKYG GMLIVLAMEK HVPETAQQRF KIAMKAAEIL KDHDVDLERV YFDPLVLPAG AKNDYHTTLK AIELMNRAGL KTSIGLSNLS FGLANRESVN AAFLALCIEK GLSAAILNSA EATTMNVLRG ALQLKGKEPA KTEQVIEDEL VKLIVSGQKE KLMNFVKDSL KEKEPLYISQ NMLARAMEQI GTLYSRGIIY LPHLILASET VQPAFDYLNN LLGEAQTKLG KVLLATVQGD IHDIGKRIVA TVLKSGGFEV YDVGKDVPAQ KILSECERLK PDIVGLSAMM TTTVGQVKEV SDLLKKNNVR VVVIAGGASM NEQLANQFGV LYAKDALKAL EICKKIVGKE NER // ID A8F9K6_BACP2 Unreviewed; 312 AA. AC A8F9K6; DT 13-NOV-2007, integrated into UniProtKB/TrEMBL. DT 13-NOV-2007, sequence version 1. DT 27-MAY-2015, entry version 41. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABV60923.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ABV60923.1}; GN Name=mmuM {ECO:0000313|EMBL:ABV60923.1}; GN OrderedLocusNames=BPUM_0224 {ECO:0000313|EMBL:ABV60923.1}; OS Bacillus pumilus (strain SAFR-032). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=315750 {ECO:0000313|EMBL:ABV60923.1, ECO:0000313|Proteomes:UP000001355}; RN [1] {ECO:0000313|EMBL:ABV60923.1, ECO:0000313|Proteomes:UP000001355} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SAFR-032 {ECO:0000313|EMBL:ABV60923.1, RC ECO:0000313|Proteomes:UP000001355}; 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; ABV60923.1; -; Genomic_DNA. DR RefSeq; WP_012008799.1; NC_009848.1. DR RefSeq; YP_001485483.1; NC_009848.1. DR ProteinModelPortal; A8F9K6; -. DR STRING; 315750.BPUM_0224; -. DR EnsemblBacteria; ABV60923; ABV60923; BPUM_0224. DR GeneID; 5619451; -. DR KEGG; bpu:BPUM_0224; -. DR PATRIC; 18964185; VBIBacPum16546_0228. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; BPUM315750:GH6N-241-MONOMER; -. DR Proteomes; UP000001355; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001355}; KW Methyltransferase {ECO:0000313|EMBL:ABV60923.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001355}; KW Transferase {ECO:0000313|EMBL:ABV60923.1}. SQ SEQUENCE 312 AA; 34292 MW; 4FC95053B58763A8 CRC64; MNPIQSRLQA HAPLILDGAL ATELERKGCN LNDSLWSAKI LIEQPELIQQ VHLDYFQAGA DCATTASYQT TIDGFAEKGY SKEEAIELMK RSVTLAKEAR DLFWQDEASR NGRTKPFVAG SVGPFGAYLS DGSEYKGNYG LTEQALIDFH RPRIQALVEA GADILACETI PCLIEAIAIA KLLQDEFSGV SAWITFSAKD DLHISEGDLL RECVQALEPY EQIAAVGVNC TPPQYISSLI QEMKKGTSKP IVVYPNSGEL YDPEDKVWSG DTPQHTFGEC AHQWYQDGAH IIGGCCRTTP EDITDILKLT TS // ID A8FBU3_BACP2 Unreviewed; 1142 AA. AC A8FBU3; DT 13-NOV-2007, integrated into UniProtKB/TrEMBL. DT 13-NOV-2007, sequence version 1. DT 27-MAY-2015, entry version 60. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABV61710.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABV61710.1}; GN OrderedLocusNames=BPUM_1026 {ECO:0000313|EMBL:ABV61710.1}; OS Bacillus pumilus (strain SAFR-032). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=315750 {ECO:0000313|EMBL:ABV61710.1, ECO:0000313|Proteomes:UP000001355}; RN [1] {ECO:0000313|EMBL:ABV61710.1, ECO:0000313|Proteomes:UP000001355} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SAFR-032 {ECO:0000313|EMBL:ABV61710.1, RC ECO:0000313|Proteomes:UP000001355}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000813; ABV61710.1; -; Genomic_DNA. DR RefSeq; WP_012009525.1; NC_009848.1. DR RefSeq; YP_001486270.1; NC_009848.1. DR ProteinModelPortal; A8FBU3; -. DR STRING; 315750.BPUM_1026; -. DR EnsemblBacteria; ABV61710; ABV61710; BPUM_1026. DR GeneID; 5620292; -. DR KEGG; bpu:BPUM_1026; -. DR PATRIC; 18965887; VBIBacPum16546_1041. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; BPUM315750:GH6N-1080-MONOMER; -. DR Proteomes; UP000001355; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001355}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABV61710.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001355}; KW Transferase {ECO:0000313|EMBL:ABV61710.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 225 225 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 722 722 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1142 AA; 126855 MW; 24322A34559712D0 CRC64; MSTITEQLKK RILVLDGAMG TMIQNANLTA EDFGGEEYEG CNEYLNVTAP HIIRTIHKEY LEASADLIET NTFGATKLVL DEYGLGHLAY ELNVRAAQLA KDEAKRFSTP EQPRFVVGAM GPTTKTLSVT GGTTFDELVR NYEEQARALI DGKCDALLLE TSQDMLNVKA GFKGIQEAFQ QTGIELPLMV SGTIEPMGTT LAGQDIEAFY ISLEHMKPMS VGLNCATGPE FMTDHIRTLS SIAKSAVSCY PNAGLPDEEG QYHESPASLA KKISAFAKEG WLNIVGGCCG TTPAHIQALS DEVRTIQPRH ITHESSQHTV SGIEPLIYDE SMRPLFVGER TNVIGSRKFK RLIAEQKFEE ASEIARAQVK NGAHVIDVCL ADPDRDEIAD MEGFLQEAMK KVKAPFVIDS TDKHVIEKAL TYSQGKAIIN SINLEDGEER FEEILPLVKL YGGALVVGTI DETGMAVTAE RKLEIAVRSH DLLTKKYGIP ASDIIFDPLV FPVGTGDEQY IGAAEETIKG IKMIKEKLPE CLTILGISNV SFGLPPLGRE ILNAVYLYHC VQAGLDYAIV NTEKLERFAS IPKEEIKLAE TLLYETNDQT LAEFTQFYRG KKKTEKKPKV SLPLDERLAL YVVEGTKEGL IDDLSLALEQ YESPLHIING PLMQGMAEVG RLFNQNELIV AEVLQSAEVM KASVSYLEQY MEKQHASGKG KILLATVKGD VHDIGKNLVD IILSNNGFQV VDLGIKVTPQ TLIEAVQKEK PDMIGLSGLL VKSAQQMVLT AQDLQKANIS VPILVGGAAL SRKFTKMKIS PHYDGPVLYA KDAMDGLSLA NELKANPLQF QIKPDEEPVA PVKEKETKQP QAVIELLEKR AALPEAPIFT PENTARHYVK DIDLHHIMPY VNEQMLIGHH LGLKGKVKKL LAEQHPKALE LKQLVTDLLN EGREKNWFAP AFVYQFYPAS SNGNDLHIYD PEVPDRIIET FQFPRQEKLP YRSISDYVRG SGEKEKDYIA LFAVTAGARI REVAQQFKQE GDYLKMHAVQ ALALELAEGL AERTHQVIRD KWGFPDPVDF TMEKRFQAKY QGQRYSFGYP ACPNLEDQEK LFKLLQPEKI GIHLTEGFMM EPEASVTAIV VSHPEARYFN VH // ID A8FBU4_BACP2 Unreviewed; 613 AA. AC A8FBU4; DT 13-NOV-2007, integrated into UniProtKB/TrEMBL. DT 13-NOV-2007, sequence version 1. DT 27-MAY-2015, entry version 49. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN Name=yitJ {ECO:0000313|EMBL:ABV61711.1}; GN OrderedLocusNames=BPUM_1027 {ECO:0000313|EMBL:ABV61711.1}; OS Bacillus pumilus (strain SAFR-032). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=315750 {ECO:0000313|EMBL:ABV61711.1, ECO:0000313|Proteomes:UP000001355}; RN [1] {ECO:0000313|EMBL:ABV61711.1, ECO:0000313|Proteomes:UP000001355} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SAFR-032 {ECO:0000313|EMBL:ABV61711.1, RC ECO:0000313|Proteomes:UP000001355}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ABV61711.1; -; Genomic_DNA. DR RefSeq; WP_012009526.1; NC_009848.1. DR RefSeq; YP_001486271.1; NC_009848.1. DR ProteinModelPortal; A8FBU4; -. DR STRING; 315750.BPUM_1027; -. DR EnsemblBacteria; ABV61711; ABV61711; BPUM_1027. DR GeneID; 5620293; -. DR KEGG; bpu:BPUM_1027; -. DR PATRIC; 18965889; VBIBacPum16546_1042. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; BPUM315750:GH6N-1081-MONOMER; -. DR Proteomes; UP000001355; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001355}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ABV61711.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862, KW ECO:0000313|EMBL:ABV61711.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001355}; KW Transferase {ECO:0000313|EMBL:ABV61711.1}. SQ SEQUENCE 613 AA; 68266 MW; AA5ECE43AB0CE516 CRC64; MGLLQDLQNR VLIADGAMGT LLYSYGIDRC FEELNLSKED EVKRVHEAYV QAGADIIQTN TYGANYIKLS RYGLEEETKR INTKAVQIAK AAAGSAYVLG TIGGIRTFNK NAYTIEEIKR SFREQLYILL NEEPDGILLE TYYDMEEAKA VLQIARKETT LPIVMNVSMH EQGVLQDGTP LRDGLSELSS LGADVVGINC RLGPYHMIQA LEGVPILENS HLSVYPNSSL PSLEEGRLVY DTDNDYFRKS ALEFRNQGAR IIGGCCGTTP QHIHAMAEAV KDLAPITEKE VKVLKEEIIS IQDQRTEPGL DELATKKRTI IVELDPPKKL NFEKFLVAAK ELKNAGIDAL TLADNSLATP RISNVACGAL LKQQLDMRSL VHITCRDRNL IGLQSHLMGL DTLGLTDILA ITGDPSKIGD FPGATSVYDL TSFDLIRLIK QFNEGLSFSG KPLGKKTNFS VAGAFNPNVR HIDKAVKRLE KKIEYGADYF ISQPVYSEEQ LVKIHEESRH LDKPIYIGIM PLTSSRNAEF IHHEIPGIKL SDSIRDIMAR AGEDKEKQRA EGLAIARSLL DTACELFNGI YLITPFLRSD LTAELTTYIH QKEKESNIHV NYH // ID A8FZS0_SHESH Unreviewed; 1252 AA. AC A8FZS0; DT 13-NOV-2007, integrated into UniProtKB/TrEMBL. DT 13-NOV-2007, sequence version 1. DT 27-MAY-2015, entry version 58. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABV38343.1}; GN OrderedLocusNames=Ssed_3739 {ECO:0000313|EMBL:ABV38343.1}; OS Shewanella sediminis (strain HAW-EB3). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV38343.1, ECO:0000313|Proteomes:UP000002015}; RN [1] {ECO:0000313|EMBL:ABV38343.1, ECO:0000313|Proteomes:UP000002015} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV38343.1, RC ECO:0000313|Proteomes:UP000002015}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000821; ABV38343.1; -; Genomic_DNA. DR RefSeq; WP_012144073.1; NC_009831.1. DR RefSeq; YP_001475471.1; NC_009831.1. DR ProteinModelPortal; A8FZS0; -. DR SMR; A8FZS0; 672-1252. DR STRING; 425104.Ssed_3739; -. DR EnsemblBacteria; ABV38343; ABV38343; Ssed_3739. DR KEGG; sse:Ssed_3739; -. DR PATRIC; 23565332; VBISheSed62411_3966. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SSED425104:GH7Q-3873-MONOMER; -. DR Proteomes; UP000002015; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002015}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 257 257 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 320 320 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 778 778 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1252 AA; 138458 MW; C75D2A0ECB9036B5 CRC64; MATGTLSNSK KIRDIGPQIS QQLKDSILIL DGAMGTMIQD RKFEEADFRG ERFNEWPCDV KGNNDLLVLT QSAAIKQIHK DYLLAGADII ETNTFNATRI AMADYDMQEL SAEINLNGAR LAREAADEVE AETGRACYVA GVLGPTNRTC SISPDVNDPG FRNVSFDELV EAYIESIDAL IEGGSDIIMV ETIFDTLNAK AALFAIETVF ENLGTRLPIM ISGTITDASG RTLTGQTTEA FYNSLRHVKP LSIGLNCALG PKELRAYVEE LSKISECYVS AHPNAGLPNE FGGYDETPAE MAEVIGQWAE EGFLNIVGGC CGTTPDHIRA IREAVIKHPA RALPDIPVAC RLSGLEPLTI DANSLFLNVG ERTNVTGSAK FLRLIKTGEY EEALSVARDQ VENGAQIIDI NMDEGMLDGV EMMHKFLNLI ASEPDISRVP IMIDSSKWEV IEAGLKCIQG KGIVNSISLK EGEEKFIQQA KLVKRYGAAA IIMAFDEEGQ ADTKARKIEI CTRAYRVLVD KVGFPPEDII FDPNIFAIAT GIDEHDNYAV DFIEATREIK RTLPHAMISG GVSNVSFSFR GNNPVREAIH AVFLYHAIQA GMDMGIVNAG QLAIYDDIDA ELKERVEAIV QNLPCTALGS DGSETNNTEL LLEVAERFRG DGSQTAKKED LEWRSWDVNK RLAHALVKGI TDFIDEDTEE ARANASRPLD VIEGPLMDGM NIVGDLFGSG KMFLPQVVKS ARVMKKAVAY LNPYIEKEKV PGQSNGKILM VTVKGDVHDI GKNIVGVVLA CNGYEVIDLG VMVPVEKIIE VAKAENVDII GMSGLITPSL DEMVHNVKSF HKAGLTIPSI IGGATCSKIH TAVKIAPHSP EGAIYIADAS RAVPMVSKLI NNETRQATID EAYQEYDIMR EKRLSQAKRK EITTIAAARD NRCQHDWENY TPFVPNQLGR QVFDDYPLED LVDRIDWTPF FRSWELHGHF PRILDDEVVG AEARKLFHDG KAMLEKIIDE KWLTAKAVIG LFPANTVNHD DIELYSCDGT DETREKPIMT THHLRMQIER VGNDNFCLAD FVAPKDSGVA DYMGGFAVTA GHGIDEHIER FEADHDDYNA IMLKSLADRL AEAFAERMHE RVRKEFWGYA SDEALDNEAL IREKYKGIRP APGYPACPDH TEKGLLWDLL KPDETIDLNI TESYAMFPTA AVSGWYFAHP KSRYFGVTNI GRDQVEDYAA RKGMSVAETE RWLAPVLDYD PE // ID A8G4U9_PROM2 Unreviewed; 1189 AA. AC A8G4U9; DT 13-NOV-2007, integrated into UniProtKB/TrEMBL. DT 13-NOV-2007, sequence version 1. DT 27-MAY-2015, entry version 58. DE SubName: Full=Putative methionine synthase {ECO:0000313|EMBL:ABV50630.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABV50630.1}; GN Name=metH {ECO:0000313|EMBL:ABV50630.1}; GN OrderedLocusNames=P9215_10151 {ECO:0000313|EMBL:ABV50630.1}; OS Prochlorococcus marinus (strain MIT 9215). OC Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae; OC Prochlorococcus. OX NCBI_TaxID=93060 {ECO:0000313|EMBL:ABV50630.1, ECO:0000313|Proteomes:UP000002014}; RN [1] {ECO:0000313|EMBL:ABV50630.1, ECO:0000313|Proteomes:UP000002014} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MIT 9215 {ECO:0000313|EMBL:ABV50630.1, RC ECO:0000313|Proteomes:UP000002014}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000825; ABV50630.1; -; Genomic_DNA. DR RefSeq; WP_012007717.1; NC_009840.1. DR RefSeq; YP_001484216.1; NC_009840.1. DR ProteinModelPortal; A8G4U9; -. DR STRING; 93060.P9215_10151; -. DR EnsemblBacteria; ABV50630; ABV50630; P9215_10151. DR KEGG; pmh:P9215_10151; -. DR PATRIC; 22991526; VBIProMar119824_1035. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PMAR93060:GI08-1046-MONOMER; -. DR Proteomes; UP000002014; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002014}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABV50630.1}; KW Transferase {ECO:0000313|EMBL:ABV50630.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 228 228 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 747 747 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1189 AA; 132448 MW; 2A0C29FF4195D8E8 CRC64; MMESFRTYLN RDEKPLIIFD GGTGTSFQNL NLTADDFGGK ELEGCNENLV LSSPNVVERV HTSFLEAGCH VIETNTFGAS SIVLDEYDIA DKAYEINKNA ALIAKKAAAK YKSVKKPRFV AGSIGPTTKL PTLGHIDFDE LKQSYKEQIY GLTDGGVDLL LIETCQDVLQ IKSALLASKE VLDSKNIDIP IMVSITMETT GTMLVGSDIA SALTILEPFN IDILGLNCAT GPEQMKEHIK YLSENSPFAI SCIPNAGLPE NIGGVAHYRL KPIELKMQLM NFIYDFNVQL IGGCCGTTPE HIKYLSSIID EIIHKERSSK NGNNNLSGYI PSASSIYNSV PYKQDNSILI VGERLNASGS KKVRELLNND DWDGLVSIAK QQQKENAHVL DVNVDYVGRD GVKDMKEITS RLVTNINLPL MIDSTDADKM ESGLKSAGGK CIINSTNYED GNERFDQVLN LALGYGSGLV VGTIDEDGMA RDADKKYNIV KRAINRTREC GLSDYELFFD PLALPISTGI EEDRLNAKET INAISTIRKN FPDIHIILGI SNISFGLSPL SRINLNSIFL DECIKAGLDS AIIAPNKILP LSKISKETKK LCLDLIYDKR EFEDDICIYD PLVELTKAFQ DLSIQDFKKA SSENKNLTLE ESLKNHIIDG EKIGLEDQLN KALKKYKPLE IINNFLLDGM KVVGDLFGSG QMQLPFVLQS AETMKFAVSI LEPYMETVDE SISNGKLLIA TVKGDVHDIG KNLVDIILTN NGYDVINLGI KQDVSAIINA QKKHNADCIA MSGLLVKSTA FMKDNLEAFN NENISVPVIL GGAALTPKFV NEDCSKIYKG KILYGKDAFT DLKFMNEYMD NKKKGNWSNT EGFINNEGIN INLASSKANS RAVKKSISIH TQTSKLNLKE NFIRSKFIKE EEPIQAPFLG TKVLKGFDID LKKLIFYLDT KALFSGQWQI KKGKNQSVDE YNNYLDSYAK PLLDRWLETI IEKKLISPRA VYGYFRCGRK DNSIFLFDDK SLNKISQFNF PRQKSGNNLC IADFYCDLKN DKPIDIFPMQ AVTMGDIASE YSQKLFKEDK YSDYLLFHGL TVQLAEALAE YVHALIRVEC GFSTEEPDKN REILAQKYRG ARYSFGYPAC PKVSDSNIQL SLLDAKRINL TMDESEQLHP EQSTTAIISL HSKAKYFSA // ID A8GHH9_SERP5 Unreviewed; 312 AA. AC A8GHH9; DT 13-NOV-2007, integrated into UniProtKB/TrEMBL. DT 13-NOV-2007, sequence version 1. DT 27-MAY-2015, entry version 42. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABV42569.1}; GN OrderedLocusNames=Spro_3471 {ECO:0000313|EMBL:ABV42569.1}; OS Serratia proteamaculans (strain 568). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Serratia. OX NCBI_TaxID=399741 {ECO:0000313|EMBL:ABV42569.1, ECO:0000313|Proteomes:UP000007074}; RN [1] {ECO:0000313|EMBL:ABV42569.1, ECO:0000313|Proteomes:UP000007074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=568 {ECO:0000313|EMBL:ABV42569.1, RC ECO:0000313|Proteomes:UP000007074}; 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 ----------------------------------------------------------------------- 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; ABV42569.1; -; Genomic_DNA. DR RefSeq; WP_012146183.1; NC_009832.1. DR RefSeq; YP_001479697.1; NC_009832.1. DR ProteinModelPortal; A8GHH9; -. DR STRING; 399741.Spro_3471; -. DR EnsemblBacteria; ABV42569; ABV42569; Spro_3471. DR KEGG; spe:Spro_3471; -. DR PATRIC; 32419744; VBISerPro44537_3529. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; SPRO399741:GI55-3546-MONOMER; -. DR Proteomes; UP000007074; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007074}; KW Methyltransferase {ECO:0000313|EMBL:ABV42569.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007074}; KW Transferase {ECO:0000313|EMBL:ABV42569.1}. SQ SEQUENCE 312 AA; 33593 MW; 320B076F9CA6813F CRC64; MSVNNPVATL LSAHPTLILD GALATELEAR GCDLSDPLWS AKVLIENPEL IYQVHLDYFN AGAQCAITAS YQATPQGFLR RGLDQAQSLA LIAKSVQLAQ QARRDYLAQH PQAAPLLIAG SVGPYGAYLA DGSEYRGDYS LPQEEMIAFH RPRISALAEA GVDLLACETL PSFSELQALL TLLEEFPTLG AWFAFTLRDS QHLSDGTPLT EVMAALHANP QVLAIGINCI ALENVAPALQ QFAALADKPL LVYPNSGEHY DAVSKTWHAC GGAHGSLIDQ IGEWQRIGAR LIGGCCRTTP QDIHQIATRC RA // ID A8GKE4_SERP5 Unreviewed; 1209 AA. AC A8GKE4; DT 13-NOV-2007, integrated into UniProtKB/TrEMBL. DT 13-NOV-2007, sequence version 1. DT 27-MAY-2015, entry version 60. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABV43584.1}; GN OrderedLocusNames=Spro_4490 {ECO:0000313|EMBL:ABV43584.1}; OS Serratia proteamaculans (strain 568). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Serratia. OX NCBI_TaxID=399741 {ECO:0000313|EMBL:ABV43584.1, ECO:0000313|Proteomes:UP000007074}; RN [1] {ECO:0000313|EMBL:ABV43584.1, ECO:0000313|Proteomes:UP000007074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=568 {ECO:0000313|EMBL:ABV43584.1, RC ECO:0000313|Proteomes:UP000007074}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000826; ABV43584.1; -; Genomic_DNA. DR RefSeq; WP_012147184.1; NC_009832.1. DR RefSeq; YP_001480712.1; NC_009832.1. DR ProteinModelPortal; A8GKE4; -. DR SMR; A8GKE4; 633-1209. DR STRING; 399741.Spro_4490; -. DR EnsemblBacteria; ABV43584; ABV43584; Spro_4490. DR KEGG; spe:Spro_4490; -. DR PATRIC; 32421796; VBISerPro44537_4544. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SPRO399741:GI55-4577-MONOMER; -. DR Proteomes; UP000007074; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007074}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007074}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 230 230 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 741 741 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1209 AA; 133858 MW; 91405A58534F4390 CRC64; MLDGGMGTMI QSYRLEESDF RGERFADWQS DLKGNNDLLV LTKPEVITAI HYGYLEAGAD ILETNTFNST SIAMADYHME SLSAEINYQA ACLARACADE WTARTPEQPR YVAGVLGPTN RTASISPNVN DPAFRNVSFD ELVEAYREST RALVEGGVDL IMIETIFDTL NAKAAAFAVE TEFEALGVAL PIMISGTITD ASGRTLSGQT TEAFYNSMRH VKPLSFGLNC ALGPDELRQY VSELSRISES YVTAHPNAGL PNAFGEYDLD AQEMAKQVGE WANAGFLNII GGCCGTTPEH IAAMVKAVAG VPPRQLPAIP VACRLAGLEP LNIDAKTLFV NVGERTNVTG SARFKRLIKE EKYSEALAVA RQQVESGAQI IDINMDEGML DAEAAMVRFL NLIAGEPDIA RVPIMIDSSK WSVIEKGLKC IQGKGIVNSI SMKEGEEAFI HHAKLVRRYG AAVVVMAFDE AGQADTRERK FEICRRAYKI LTERVGFPPE DIIFDPNIFA VATGIDEHNN YAVDFIEACA DIKTHLPHAM ISGGVSNVSF SFRGNDPVRE AIHAVFLYHA IRNGMDMGIV NAGQLAIYDD LSAELRDAVE DVILNRRDDG TERLLELAEK YRGSKDNEVA VQQAEWRGWP VEKRLEYSLV KGITEFIELD TEEARQRADR PIEVIEGPLM AGMNVVGDLF GEGKMFLPQV VKSARVMKQA VAYLEPYIEA SKEKGTTAGK ILLATVKGDV HDIGKNIVGV VLQCNNYEIV DLGVMVPTEK ILKTAREQNV DIIGLSGLIT PSLDEMVNVA KEMERQGFTL PLLIGGATTS KAHTAVKIEQ NYSGSTTYVQ NASRTVGVVS ALLSATQRDD FVARTRKEYE TVRIQHARKK PRTPPVDLQK ARDNAMVLDW ESYQPPVPKR LGVYPVEAGI ETLRHYIDWT PFFMTWSLAG KYPRILEDEV VGEEAKRLFA DANQMLDMLA ANGSLNPRGV YGLFPANRVG DDVEVYRDEN RDEVLVVSRH LRQQTEKTDF PNYCLADFVA PKSSGKADYF GAFAVTGGLE EDDLAAAYDA QHDDYNKIMV KALSDRLAEA FAEYLHEQVR KLHWGFAAEE NLSNEELIRE NYQGIRPAPG YPACPEHTEK AEIWRLLDVN RHTGMVLTES FAMWPGAAVS GWYFSHPQSK YFAVAQLQRD QVEDYAARKG MSVSEVERWL APNLGYDAD // ID A8H811_SHEPA Unreviewed; 1210 AA. AC A8H811; DT 13-NOV-2007, integrated into UniProtKB/TrEMBL. DT 13-NOV-2007, sequence version 1. DT 29-APR-2015, entry version 57. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABV88698.1}; GN OrderedLocusNames=Spea_3384 {ECO:0000313|EMBL:ABV88698.1}; OS Shewanella pealeana (strain ATCC 700345 / ANG-SQ1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=398579 {ECO:0000313|EMBL:ABV88698.1, ECO:0000313|Proteomes:UP000002608}; RN [1] {ECO:0000313|EMBL:ABV88698.1, ECO:0000313|Proteomes:UP000002608} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700345 / ANG-SQ1 {ECO:0000313|Proteomes:UP000002608}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000851; ABV88698.1; -; Genomic_DNA. DR RefSeq; WP_012156597.1; NC_009901.1. DR RefSeq; YP_001503233.1; NC_009901.1. DR ProteinModelPortal; A8H811; -. DR SMR; A8H811; 634-1208. DR STRING; 398579.Spea_3384; -. DR EnsemblBacteria; ABV88698; ABV88698; Spea_3384. DR KEGG; spl:Spea_3384; -. DR PATRIC; 23536911; VBIShePea72822_3534. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SPEA398579:GHG5-3548-MONOMER; -. DR Proteomes; UP000002608; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002608}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002608}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 224 224 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 287 287 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 740 740 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1210 AA; 134125 MW; CE6B8F6C057FD695 CRC64; MGTMIQDRKF EELDFRGQQF KDWHCDVKGN NDMLVLTQPE AIKQIHKDYL LAGSDIIETN TFNATRIAMA DYDMQAHSAE INLVGARLAR EAANEVEAET GRQCYVAGVL GPTNRTCSIS PDVNDPGFRN VSFDELVEAY IESINALVAG GSDIIMVETI FDTLNAKAAL FAIETVYDTQ GFRLPIMISG TITDASGRTL TGQTTEAFYN SLRHVKPLSI GLNCALGPKE LRPYVEELSK ISECYVSAHP NAGLPNEFGG YDETPEQMAE IIEEWAQEGF LNIIGGCCGT TPDHIRVIRE AVIKHSARPL PDIPVACRLS GLEPLTIDEN SLFLNVGERT NVTGSAKFLR LIKTGEYEEA LSVAREQVEN GAQIIDINMD EGMLDGAETM HKFLNLIASE PDISRVPIMI DSSKWEVIEA GLKCIQGKGI VNSISLKEGE EKFIEQAKLV KRYGAAAIVM AFDEVGQADT KARKVEICTR AYNVLVDKVG FPPEDIIFDP NIFAIATGIE EHDNYAVDFI EATAEIKRTL PHAMISGGVS NVSFSFRGNN PVREAIHAVF LYHAIQAGMD MGIVNAGQLA IYDDIDPELK ERVEAIVQNL PCKVADTNNT ELLLEVAEKF RGDGSQTAKK EDLEWRSKPV NERLAHALVK GITEFIDEDT EEARQQATRP LDVIEGPLMD GMNIVGDLFG SGKMFLPQVV KSARVMKKAV AYLNPYIELE KVAGQSNGKI LMVTVKGDVH DIGKNIVGVV LACNGYEVID LGVMVPVEKI IEVAIAENVD IIGMSGLITP SLDEMVHNVK SFHKAGLTIP SIIGGATCSK IHTAVKIAPH SPEGAIYIAD ASRAVPMVSK LINDATRQAT IDQAYAEYDV MREKRLSQTK RKVITSIAAA RENSCQHDWQ NYTPFVPNQL GRQVFDDYPL EDLVERIDWT PFFRSWELHG HFPRILEDEV VGIEARKLFS DGKAMLDKII SEKWLTAKAV IGLFPANTVN HDDIELYTDE TRSELELTTH HLRMQIERVG NDNFCLADFV APKNSGVADY MGGFAVTAGH GIDEHVARFE ADHDDYSAIM LKCLADRLAE AFAERMHERV RKEFWGYASD EVLDNEALIR EKYKGIRPAP GYPACPDHTE KGLLWDLLKP DETIGLKITE SYAMFPTAAV SGWYFAHPKS RYFGVTNIGR DQVEDYATRK GMSIEETERW LAPVLDYDPQ // ID A8HVP5_AZOC5 Unreviewed; 1248 AA. AC A8HVP5; DT 04-DEC-2007, integrated into UniProtKB/TrEMBL. DT 04-DEC-2007, sequence version 1. DT 27-MAY-2015, entry version 58. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|EMBL:BAF90339.1}; GN OrderedLocusNames=AZC_4341 {ECO:0000313|EMBL:BAF90339.1}; OS Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / OS NBRC 14845 / NCIMB 13405 / ORS 571). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Xanthobacteraceae; Azorhizobium. OX NCBI_TaxID=438753 {ECO:0000313|EMBL:BAF90339.1, ECO:0000313|Proteomes:UP000000270}; RN [1] {ECO:0000313|Proteomes:UP000000270} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / NBRC 14845 / NCIMB 13405 / RC ORS 571 {ECO:0000313|Proteomes:UP000000270}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP009384; BAF90339.1; -; Genomic_DNA. DR RefSeq; WP_012172861.1; NC_009937.1. DR RefSeq; YP_001527257.1; NC_009937.1. DR ProteinModelPortal; A8HVP5; -. DR SMR; A8HVP5; 661-909. DR STRING; 438753.AZC_4341; -. DR EnsemblBacteria; BAF90339; BAF90339; AZC_4341. DR KEGG; azc:AZC_4341; -. DR PATRIC; 21025599; VBIAzoCau17976_4528. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; ACAU438753:GJF3-4397-MONOMER; -. DR Proteomes; UP000000270; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000270}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAF90339.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000270}; KW Transferase {ECO:0000313|EMBL:BAF90339.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 255 255 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 318 318 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 319 319 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 771 771 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1248 AA; 135791 MW; 8258859FED72196B CRC64; MTTAPAKTGQ TEPRSALLAA ARDRILVLDG AMGTMIQGLK LDEAGYRGAR FADWPQDIKG NNDILNLTRP DDVRAIHLKY FLAGADIVET NTFSSTTIAQ ADYAMEALAY ELNVEGARLA KEAAIEAEKQ DGRPRFVAGA IGPTNRTASI SPDVNNPGFR ATSFDELATA YAEQTRGLIA GGSDIILIET IFDTLNAKAA VFAAETVFEE IGRRLPVMIS GTITDLSGRT LSGQTPSAFW YSLRHAQPFS IGLNCALGAK EMRAHIAELG RVADTFVCAY PNAGLPNEFG LYDESPEAMA ELVGEFAASG LVNIVGGCCG TTPDHIGAIA KAVAGKAPRA IPTLEPRLRL SGLEPFELTR EIPFVNVGER TNVTGSARFR KLITNGDFTA ALDVARDQVE SGAQVIDVNM DEGLLDSHAA MVTFLNLVAA EPDIARVPVM VDSSKWDIIE AGLKCIQGKG IVNSISMKEG EDAFRHYARL VRRYGAAVVV MAFDEKGQAD TYERKIEICA RAYKILTEEI GFPPEDIIFD PNVFAVATGI EEHAPYGVNF IEATRWIRQN LPHAHISGGV SNLSFSFRGN EPVREAMHAV FLYHAIQAGM DMGIVNAGQL AVYDEIPAEL REACEDVVLN RNADATERLL SLAEGFKGGA GKEKREADLT WRTWDVEKRL AHALINGITE YVEADTEEAR AAAARPLHVI EGPLMSGMNI VGDLFGAGKM FLPQVVKSAR VMKQAVAYLM PFMEKEKEEM GLTEASAAGK ILMATVKGDV HDIGKNIVGV VLQCNNYEVI DLGVMVPAAK ILEVAKAEKV DVIGLSGLIT PSLDEMVTVA SEMEREGFHV PLLIGGATTS RVHTAVKIAP QYHRGQAVYV TDASRAVGVV SNLLSPDTRE TYVADIRAEY SKLAEAHARA DANKQRVPLK SARDNALKLD FKASAPVKPT FLGTKVFEDY DLADLVPFID WSPFFASWEL TGKYPQILQD ETVGEAARNL FSDAQAMLKK IIDEKWVTAK AVVGFWPANA VGDDILLFRD EGRMTPLATL HTLRQQLARR EGRSNLALAD FVAPVESGVH DYVGGFAVTA GIGEEERTTA FKAANDDYSA ILLKALCDRL AEAFAERMHQ RVRTEFWGYA DDEGLSNEDL IAEKYRGIRP APGYPAQPDH TEKGTLFTLL DATDKIGLEL TESFAMWPGA AVSGLYFAHP ESAYFGVGRI ERDQVEDYAA RKGWTVEQAE RWLAPILNYD PTRRAAAE // ID A8HYR2_CHLRE Unreviewed; 1242 AA. AC A8HYR2; DT 04-DEC-2007, integrated into UniProtKB/TrEMBL. DT 04-DEC-2007, sequence version 1. DT 29-APR-2015, entry version 51. DE SubName: Full=Cobalamin-dependent methionine synthase {ECO:0000313|EMBL:EDP08397.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EDP08397.1}; GN Name=METH1 {ECO:0000313|EMBL:EDP08397.1}; GN ORFNames=CHLREDRAFT_76715 {ECO:0000313|EMBL:EDP08397.1}; OS Chlamydomonas reinhardtii (Chlamydomonas smithii). OC Eukaryota; Viridiplantae; Chlorophyta; Chlorophyceae; OC Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas. OX NCBI_TaxID=3055 {ECO:0000313|Proteomes:UP000006906}; RN [1] {ECO:0000313|EMBL:EDP08397.1, ECO:0000313|Proteomes:UP000006906} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CC-503 {ECO:0000313|Proteomes:UP000006906}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; DS496110; EDP08397.1; -; Genomic_DNA. DR RefSeq; XP_001696420.1; XM_001696368.1. DR UniGene; Cre.7863; -. DR ProteinModelPortal; A8HYR2; -. DR SMR; A8HYR2; 645-898, 907-1241. DR STRING; 3055.JGI76715; -. DR PRIDE; A8HYR2; -. DR ProMEX; A8HYR2; -. DR EnsemblPlants; EDP08397; EDP08397; CHLREDRAFT_76715. DR GeneID; 5722204; -. DR KEGG; cre:CHLREDRAFT_76715; -. DR eggNOG; COG1410; -. DR InParanoid; A8HYR2; -. DR KO; K00548; -. DR Proteomes; UP000006906; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006906}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EDP08397.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006906}; KW Transferase {ECO:0000313|EMBL:EDP08397.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 237 237 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 301 301 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1242 AA; 137039 MW; C2223A05CE9980A5 CRC64; MRERIIFIDG AMGTQIQKFT LEEEDFRGER YAKHSHELKG NNDLLVITRP DVISKIHTAY LEAGADIIET NTFNGTWISQ SDYELQADVA LINRTAAQLA KKCVADFLAK NPGSGPRFVA GAIGPTNKTL SVSPSVENPA FRGITYDEVV DAYYKQAEAL VEGGVDMFLV ETIFDTLNAK AAMYALEKFF SDKGMRLPVF VSGTIVDNSG RTLSGQTNEA FWNSIRHAKP MAVGLNCALG AKDMLKYVAN LAACADCYVF CYPNAGLPNA MGGYDQKGDE MAEEIRPFCE GNLVNAIGGC CGTGPEHIAA IKKMASAYKP RKPVTVPPLM RLSGLEPLNY TPDASNMRRT FLNIGERCNV AGSILFKKAI VNNDFDTAVA IALKQVQQGA DVLDINMDDG LIEGVGAMTR FVNLLVSDPE ISRVPFMIDS SKFHIVEAGL KCSQGKCIVN SISLKEGEAA FRHQAEVVRR HGAAVVVMAF DEQGQAASYE EKIRICSRAY RILVEEVGFD PQDIIFDPNI LTIGTGLPEH NNYAVDFIRA TREIKRLCPG SKVSGGVSNI AFSFRGNEAV RRAFHSAFLH HACLAGMDMG IVNAAQVKED EYSKIDKELL EFVEDVLLNR CENATERMLE YAASLDPKSK PTAKEESWRD LPVEKRIEYA LIKGIDEFAV VDTEEARSSG RYTKPLQVIE GPLMDGMNVV GDLFGAGKMF LPQVIKSARV MKKAVAHLIP FIEEEKRLSG NVGENSNAGC FLIATVKGDV HDIGKNIVSV VLGCNNFKVI DMGVMTPWEK ILDAAVEHKA DIIGLSGLIT PSLDEMVTVA KKMEERGMKT PLLIGGATTS KMHTAVKIAP VYSGPVVHVL DASRSVPVCQ AFVDKNDKQR QVRDSYIEEV SEQYADLREE FYASLEDRKY LSLADARKRA LAVDWKDPVN QPVKPKVLGN KVIRAFPIED VLDYIDWNPF FQVWQLRGRY PNRGFPRIFN DATVGSEAKK LYEEAQAMLR DFVVNKRVTL NAVMGLYPAA AVGDDIEVYA DDSRAKVVAR LAGLRQQAEK DGGEPFYCIS DFVAPKGSGV PDYVGMFACS AGHGLEKVIE GYKAAGDDYS YIMAEALADR LAEALAEKLH ELVRREYWGY APDEKLSVDD MLKVKYQGIR PAPGYPSQPD HTEKRTMWEL LDAEAATDIK LTESLAMWPA ASVSGLYFGG KCSSYFAVGK ITREQVEDYA ARKKMDIKDA ERWLSTMLNY EP // ID A8JJT1_CHLRE Unreviewed; 1297 AA. AC A8JJT1; DT 04-DEC-2007, integrated into UniProtKB/TrEMBL. DT 04-DEC-2007, sequence version 1. DT 07-JAN-2015, entry version 38. DE SubName: Full=Cobalamin-dependent methionine synthase {ECO:0000313|EMBL:EDO95867.1}; DE Flags: Fragment; GN Name=METH2 {ECO:0000313|EMBL:EDO95867.1}; GN ORFNames=CHLREDRAFT_195332 {ECO:0000313|EMBL:EDO95867.1}; OS Chlamydomonas reinhardtii (Chlamydomonas smithii). OC Eukaryota; Viridiplantae; Chlorophyta; Chlorophyceae; OC Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas. OX NCBI_TaxID=3055 {ECO:0000313|Proteomes:UP000006906}; RN [1] {ECO:0000313|EMBL:EDO95867.1, ECO:0000313|Proteomes:UP000006906} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CC-503 {ECO:0000313|Proteomes:UP000006906}; 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; DS496807; EDO95867.1; -; Genomic_DNA. DR RefSeq; XP_001702462.1; XM_001702410.1. DR PRIDE; A8JJT1; -. DR EnsemblPlants; EDO95867; EDO95867; CHLREDRAFT_195332. DR GeneID; 5728003; -. DR KEGG; cre:CHLREDRAFT_195332; -. DR InParanoid; A8JJT1; -. DR KO; K00548; -. DR Proteomes; UP000006906; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.20; -; 3. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF00809; Pterin_bind; 2. DR Pfam; PF02574; S-methyl_trans; 2. DR SUPFAM; SSF51717; SSF51717; 2. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 2. DR PROSITE; PS50972; PTERIN_BINDING; 3. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006906}; KW Reference proteome {ECO:0000313|Proteomes:UP000006906}. FT NON_TER 1297 1297 {ECO:0000313|EMBL:EDO95867.1}. SQ SEQUENCE 1297 AA; 141583 MW; 77A57BE5FE30E646 CRC64; MDDGLIEGVG AMTRFVNLLV SDPEISRVPF MIDSSKFHIV EAGLKCSQGK CIVNSISLKE GEAAFRHQAE VVRRHGAAVV VMAFDEQGQA ASYEEKIRIC SRAYRILVEE VGFDPQDIIF DPNILTIGTG LPEHNNYAVD FIRATREIKR LCPGSKVSGG VSNIAFSFRG NEAVRRAFHS AFLHHACLAG MDMGIVNAAQ VKEDEYSKID KELLEFVEDV LLNRRQDSTE RMLEYAATLD PKSKPTAVVR LGGASSGPKI TPRLNPIPAG KDQLAPDAKP APVPKYKAWK DGVKPTAAFV PLDKLMRERI IFIDGAMGTQ IQKFTLEEED FRGERYAKHS HEIPGNNDLL VITRPDVISK IHTAYLEAGA DIIETNTFNG TWISQSDYEL QADEEVALIN RTAAQLAKKC VADFLAKNPG SGPRFVAGAI GPTNKTLSVS PSVENPAFRG ITYDEVVDAY YKQAEALVEG GVDMFLVETI FDTLNAKAAM YALEKFFSDK GMRLPVFVSG TIVDNSGRTL SGQTNEAFWN SIRHAKPMAV GLNCALGAKD MLNILFKKAI INNDFDTAVA IALKQVQQGA DVLDINMDDG LIEGVGAMTR FVNLLVSDPE ISRVPFMIDS SKFHIVEAGL KCSQGKCIVN SISLKEGEAA FKHQAEEVKR HGAAVVVMAF DEQGQAASYE EKVRICSRAY RILVKEVGFD PQDIIFDPNI LTIGTGLPEH NNYAVDFIRA TREIKRLCPG SKVSGGVSNI AFSFRGNEAV RRAFHSAFLH HACLAGMDMG IVNAAQVKED EYSKIDKELL EFVEDVLLNR CENATERMLE FAATLDPKSK PTAVVKIASA PAGPKITPRL NPIPAGKDQL APDAKPAPVP KYKAWKDGVK PTAAFVPLDK LMRERIIFID GAMGTQIQKF TLEEEDFRGE RYAKHSHELK GNNDLLVITR PDVIGKIHTA YLEAGADIIE TNTFNGTWIS QSDYELQADE EVALINRTAA QLAKKCVADF LAKNPGSGPR FVAGAIGPTN KTLSVSPSVE NPAFRGITYD EVVDAYYKQA EALVEGGVDM FLVETIFDTL NAKAAMYALE KFFSDKGMRL PVFVSGTIVD NSGRTLSGQT NEAFWNSIRH AKPMAVGLNC ALGAKDMLKY VANLAACADC YVFCYPNAGL PNAMGGYDQK GDEMAEEIRP FCEGNLVNAI GGCCGTGPEH IAAIKKMASA YKPRKPVTVP PLMRLSGLEP LNYTPDASNM RRTFLNIGER CNVAGSILFK KAIVNNDFDT AVAIALKQVQ QGADVLDINM DDGLIEG // ID A8KB71_DANRE Unreviewed; 311 AA. AC A8KB71; DT 04-DEC-2007, integrated into UniProtKB/TrEMBL. DT 04-DEC-2007, sequence version 1. DT 27-MAY-2015, entry version 44. DE SubName: Full=Zgc:171603 protein {ECO:0000313|EMBL:AAI53991.1}; GN ORFNames=zgc:171603 {ECO:0000313|EMBL:AAI53991.1}, GN zgc:172121 {ECO:0000313|ZFIN:ZDB-GENE-030131-9545}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|EMBL:AAI53991.1}; RN [1] {ECO:0000313|EMBL:AAI53991.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Ovary {ECO:0000313|EMBL:AAI53991.1}; RG NIH - Zebrafish Gene Collection (ZGC) 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; BC153990; AAI53991.1; -; mRNA. DR RefSeq; NP_001108386.1; NM_001114914.1. DR UniGene; Dr.115279; -. DR ProteinModelPortal; A8KB71; -. DR GeneID; 337599; -. DR ZFIN; ZDB-GENE-030131-9545; zgc:172121. DR eggNOG; COG2040; -. DR HOVERGEN; HBG062720; -. DR PhylomeDB; A8KB71; -. DR NextBio; 20812327; -. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IBA:GO_Central. DR GO; GO:0032259; P:methylation; IBA:GOC. DR GO; GO:0033528; P:S-methylmethionine cycle; IBA:GO_Central. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; SQ SEQUENCE 311 AA; 34223 MW; 2D0131FEE15E5310 CRC64; MAAEMDSSPF ILDGGLATEL EASGFLLQGD PLWSARVLHT DPQAIKDVHY RYLQSGSDVI TTATYQASIE GFVKYLGVQP EEAQHMMMSA VQLAKETVSE FISQSPMSDR REPLVAGSVG PYGSFLHDGS EYTGAYEDKM TVEELKDWHR PQIQCLVKAG ADLVAMETIP GLKEAEALVE VLKEFPETKA WLSFSCKDNN SISSGRRFSE AVEMACRSTQ LVAVGVNCCP APLVKPLLES AKSHKRADLS WVVYPNSGEG WDVTTGWKTE MRTSFANLSL EWKAQGALWI GGCCRVRPAD ITELKQLHVQ P // ID A8LCR3_FRASN Unreviewed; 1262 AA. AC A8LCR3; DT 04-DEC-2007, integrated into UniProtKB/TrEMBL. DT 04-DEC-2007, sequence version 1. DT 01-APR-2015, entry version 57. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABW11081.1}; GN OrderedLocusNames=Franean1_1643 {ECO:0000313|EMBL:ABW11081.1}; OS Frankia sp. (strain EAN1pec). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Frankineae; Frankiaceae; Frankia. OX NCBI_TaxID=298653 {ECO:0000313|EMBL:ABW11081.1, ECO:0000313|Proteomes:UP000001313}; RN [1] {ECO:0000313|Proteomes:UP000001313} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EAN1pec {ECO:0000313|Proteomes:UP000001313}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000820; ABW11081.1; -; Genomic_DNA. DR RefSeq; WP_020459254.1; NC_009921.1. DR RefSeq; YP_001505987.1; NC_009921.1. DR ProteinModelPortal; A8LCR3; -. DR SMR; A8LCR3; 681-931. DR STRING; 298653.Franean1_1643; -. DR EnsemblBacteria; ABW11081; ABW11081; Franean1_1643. DR KEGG; fre:Franean1_1643; -. DR PATRIC; 21936144; VBIFraSp51419_1685. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; QPFFNAW; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; FSP298653:GHPI-1659-MONOMER; -. DR Proteomes; UP000001313; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001313}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001313}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 277 277 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 340 340 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 341 341 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 796 796 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1262 AA; 134703 MW; 65DC5EB183134594 CRC64; MAGSGSLDEV SVPAGTVGGE QAEAGAGARP EPGGAVRPAA AGSEQALREL LEQRVVVLDG AWGTMLQNAG LTPADYRTER FADHPKDVTG DPDLLNLTRP DVILDVHRQY LAAGADITTT NTFTATSIAQ ADYGLQSLVR EMNVRGAQLA RQAADEAGGR RFVAGSIGPL NVALSLSPRV EDPAYRAATF DEVRDSYAEQ IEALAEGGVD LLLIETIFDT LNAKAAIAAA REVAPQLPLW ISVTIVDLSG RTLSGQTVEA FWSSIAHANP LVVGVNCSLG ADEMRPHVAD LARLAGTYTA CHPNAGLPNA FGGYDQSPEE AGRLIGEFAE AGMVNIVGGC CGTTPAHIAR IAAAVAGAAP RPVPALPPRT RFSGLEPFEI GPDTGFVMIG ERTNVTGSAR FRRLIEGNDF QGAIDVALEQ VRGGANLLDV NMDADLLDSE RAMTTFLNLL ATEPEAARLP IMIDSSRWTV LEAGLRCVQG KGVVNSISLK EGEEPFLEQA RRIRDFGAGV VVMAFDEQGQ AETAERKVAI CGRAYDLLTQ RVGFPAEDIV FDPNVLAVAT GIAEHNGYAK AFLDALPLIK QRCPGVHISG GISNLSFSFR GNDVVREAMH SAFLFYAVQA GLDMGIVNAG QLAVYQDIPA DLLELVEDVL FDRRDDATDR LVSFAETVTG SGTKRVVDLS WREGPVEQRL SHALVHGIVD FIEADTEEAR ASAARALDVI EGPLMDGMKI VGDLFGSGKM FLPQVVKSAR VMKRSVAYLE PFMEAEKQQA LLDGTASSDR SGNGKVVLAT VKGDVHDIGK NIVGVVLGCN NYEVIDLGVM VPAKVILDTA VAESADAIGL SGLITPSLDE MVSVATEMQR RGLKLPLLIG GATTSRQHTA VRIAPAYDAT TVHVLDASRV VGVVSDLLDS DRAADLAVRN RDEQQHLREQ HEKRQQQPLL TLAQARANRE RVSFDELPTP AFTGIRVVTP ELSALREMID WQFFFLAWEL KGKYPAILDQ PVARELFDEG NALLDQIIAD GSLRAEGVYG FWPANSDGDD ILIDVGAGDG GGDAGAGLGA DAAGRLRVPM LRQQTAKPTG RPNRSLADYV APAGDHLGGF AVAIHGADTL AAAFEARQDD YRSIMVKALA DRLAEAFAEY VHLEARRAWF EPGSEPALAD LHAERFRGIR PAFGYPASPD HSEKQALFDL LDAGQVGLGL TESFAMTPAA AVSGLIFASP ASRYFTVGRI GRDQVEDYAA RRGLTVGDVE RWLRPNLAYD PE // ID A8LSK2_DINSH Unreviewed; 341 AA. AC A8LSK2; DT 04-DEC-2007, integrated into UniProtKB/TrEMBL. DT 04-DEC-2007, sequence version 1. DT 27-MAY-2015, entry version 44. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABV92816.1}; GN OrderedLocusNames=Dshi_1074 {ECO:0000313|EMBL:ABV92816.1}; OS Dinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Dinoroseobacter. OX NCBI_TaxID=398580 {ECO:0000313|EMBL:ABV92816.1, ECO:0000313|Proteomes:UP000006833}; RN [1] {ECO:0000313|Proteomes:UP000006833} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16493 / NCIMB 14021 / DFL 12 RC {ECO:0000313|Proteomes:UP000006833}; 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; ABV92816.1; -; Genomic_DNA. DR RefSeq; WP_012177747.1; NC_009952.1. DR RefSeq; YP_001532417.1; NC_009952.1. DR ProteinModelPortal; A8LSK2; -. DR STRING; 398580.Dshi_1074; -. DR EnsemblBacteria; ABV92816; ABV92816; Dshi_1074. DR KEGG; dsh:Dshi_1074; -. DR PATRIC; 21814731; VBIDinShi9476_1119. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265278; -. DR KO; K00548; -. DR OMA; GTNLFAM; -. DR OrthoDB; EOG693GKH; -. DR BioCyc; DSHI398580:GKEL-1092-MONOMER; -. DR Proteomes; UP000006833; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006833}; KW Methyltransferase {ECO:0000313|EMBL:ABV92816.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006833}; KW Transferase {ECO:0000313|EMBL:ABV92816.1}. SQ SEQUENCE 341 AA; 35599 MW; 3FA5ECCFE69E9F16 CRC64; MARDPLTPLL AERGILLTDG ATGTTLFNMG LSSGDAPELW NTDHPDRIAA LYQGAVDAGS DLFLTNSFGG NASRLKLHAA QDRVRELNRL AAEIGRGVAD KADRKVLVAG SMGPTGEIMA PMGPLTHDIA VEMFHEQAEG LKEGGADILW VETISAPEEY AAAAEAAARA DMPWCGTMSF DTAGRTMMGT TSATMARMVE KLAHPPVAFG ANCGVGASDL LRTVLGFAAA GTERPIIAKG NAGIPKYVDG HIHYDGTPDL MAQYAILARA SGASVIGGCC GTTFEHLRHM RAALDASAAD MPRPSLDEIT EALGGFSSAA DGTEAGGPKP ADRPRRRRRA S // ID A8LTT9_DINSH Unreviewed; 308 AA. AC A8LTT9; DT 04-DEC-2007, integrated into UniProtKB/TrEMBL. DT 04-DEC-2007, sequence version 1. DT 27-MAY-2015, entry version 37. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABV95656.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ABV95656.1}; GN Name=mmuM {ECO:0000313|EMBL:ABV95656.1}; GN OrderedLocusNames=Dshi_3928 {ECO:0000313|EMBL:ABV95656.1}; OS Dinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12). OG Plasmid pDSHI02 {ECO:0000313|EMBL:ABV95656.1, OG ECO:0000313|Proteomes:UP000006833}. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Dinoroseobacter. OX NCBI_TaxID=398580 {ECO:0000313|EMBL:ABV95656.1, ECO:0000313|Proteomes:UP000006833}; RN [1] {ECO:0000313|Proteomes:UP000006833} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16493 / NCIMB 14021 / DFL 12 RC {ECO:0000313|Proteomes:UP000006833}; 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; CP000832; ABV95656.1; -; Genomic_DNA. DR RefSeq; WP_012187314.1; NC_009956.1. DR RefSeq; YP_001542137.1; NC_009956.1. DR ProteinModelPortal; A8LTT9; -. DR STRING; 398580.Dshi_3928; -. DR EnsemblBacteria; ABV95656; ABV95656; Dshi_3928. DR KEGG; dsh:Dshi_3928; -. DR PATRIC; 21820669; VBIDinShi9476_4061. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; QPEVMAA; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; DSHI398580:GKEL-3965-MONOMER; -. DR Proteomes; UP000006833; Plasmid pDSHI02. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006833}; KW Methyltransferase {ECO:0000313|EMBL:ABV95656.1}; KW Plasmid {ECO:0000313|EMBL:ABV95656.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006833}; KW Transferase {ECO:0000313|EMBL:ABV95656.1}. SQ SEQUENCE 308 AA; 31931 MW; 9031C101D7A42C85 CRC64; MDITLLDGGL GQELVRRAGR ATPLWSMEAL LNAPDLVRAV HDDFFAAGAE VATTNTYAVL PDRLAAFDMA DQLAPLTERA CGIAAAARDA AGGGLVAGAL GPLGFSYQPD KAPPPEQAAE IYAEVARLQA RIVDVLVLET MSSVDQARGG MMGAQVAGKP VWLALSVDDA DGTKLRSGEP LAAISPVLET FSPDRVLINC ARPEAVSQAM PILAGLHPRI GGYANGFTRI ESGFNRIGAT VDLLQARQDI GPAAYAAFAQ AWVAAGATTV GGCCEIGPAH IEELARVLKT PVKETIPAGL SAREVAPD // ID A8M0Q1_SALAI Unreviewed; 307 AA. AC A8M0Q1; DT 04-DEC-2007, integrated into UniProtKB/TrEMBL. DT 04-DEC-2007, sequence version 1. DT 27-MAY-2015, entry version 36. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABV98061.1}; GN OrderedLocusNames=Sare_2200 {ECO:0000313|EMBL:ABV98061.1}; OS Salinispora arenicola (strain CNS-205). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micromonosporineae; Micromonosporaceae; Salinispora. OX NCBI_TaxID=391037 {ECO:0000313|EMBL:ABV98061.1, ECO:0000313|Proteomes:UP000001153}; RN [1] {ECO:0000313|EMBL:ABV98061.1, ECO:0000313|Proteomes:UP000001153} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CNS-205 {ECO:0000313|EMBL:ABV98061.1, RC ECO:0000313|Proteomes:UP000001153}; 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; ABV98061.1; -; Genomic_DNA. DR RefSeq; WP_012182363.1; NC_009953.1. DR RefSeq; YP_001537052.1; NC_009953.1. DR STRING; 391037.Sare_2200; -. DR EnsemblBacteria; ABV98061; ABV98061; Sare_2200. DR GeneID; 5708195; -. DR KEGG; saq:Sare_2200; -. DR PATRIC; 23432920; VBISalAre38676_2226. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; QPEVMAA; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; SARE391037:GH66-2232-MONOMER; -. DR Proteomes; UP000001153; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001153}; KW Methyltransferase {ECO:0000313|EMBL:ABV98061.1}; KW Transferase {ECO:0000313|EMBL:ABV98061.1}. SQ SEQUENCE 307 AA; 32785 MW; D7279E476E6200CD CRC64; MDRRSGSRPL ILDGGLGTEL QRRGRSVTAP WWTAHCLRDA DGRRLIAQIH AEYVTAGADV ITADTFRTTP RAAHRAGIAG HTVAADLVRT AVALAREAAD TVRRRVLVAG SVAPVEDCYR PDLVPNDGVL RREHAWLAEQ LARTSVDLVL VETMNTAREA VAATRAVCAE GLPAWVSFVC TNDARLLSGT DVVAAAAAVR AAGADMVLVN CTDPAGTDGA LRRLRRPDVG PLGAYPNLED RRGLPPAAAV DRYLPPRLTP DAFAELCAGW YYLDVVGGCC GSTPTHIATL RGRFPVDDRG VRPRESG // ID A8M267_SALAI Unreviewed; 1171 AA. AC A8M267; DT 04-DEC-2007, integrated into UniProtKB/TrEMBL. DT 04-DEC-2007, sequence version 1. DT 27-MAY-2015, entry version 61. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABV98183.1}; GN OrderedLocusNames=Sare_2325 {ECO:0000313|EMBL:ABV98183.1}; OS Salinispora arenicola (strain CNS-205). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micromonosporineae; Micromonosporaceae; Salinispora. OX NCBI_TaxID=391037 {ECO:0000313|EMBL:ABV98183.1, ECO:0000313|Proteomes:UP000001153}; RN [1] {ECO:0000313|EMBL:ABV98183.1, ECO:0000313|Proteomes:UP000001153} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CNS-205 {ECO:0000313|EMBL:ABV98183.1, RC ECO:0000313|Proteomes:UP000001153}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000850; ABV98183.1; -; Genomic_DNA. DR RefSeq; WP_012182484.1; NC_009953.1. DR RefSeq; YP_001537174.1; NC_009953.1. DR ProteinModelPortal; A8M267; -. DR STRING; 391037.Sare_2325; -. DR EnsemblBacteria; ABV98183; ABV98183; Sare_2325. DR KEGG; saq:Sare_2325; -. DR PATRIC; 23433184; VBISalAre38676_2358. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SARE391037:GH66-2357-MONOMER; -. DR Proteomes; UP000001153; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001153}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 223 223 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 734 734 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1171 AA; 126894 MW; 30ABFE26E25F3609 CRC64; MVISVLDALT DRILVADGAM GTMLHAADLT LDDFDGLEGC NEILNVTRPD AVRSVHEAYL AVGADCVETN TFGANLPNLA EYGIEGRIRE LSEAGARLAR TAADAYATPE QPRFVLGSIG PGTKLPTLGH ASYASLRDAY RENAAGLIAG GSDALIIETC QDLLQVKAAV IGSKRAMAEL GRTVPIICHV AVETTGTMLL GSEIGAALAA IEPLGIDLIG LNCSTGPAEM GEHLRYLSQH SRIPVSVMPN AGLPVLTSDG AYFPLTPDEM ADALERFVTD YGVALVGGCC GSTPEHIRVL AERLRGRSPV AREPRPEPGA SSIYHQVPFA QDASVLMVGE RTNANGSKAF REAMLAGDWQ ACVEIARGQA RDGSHLLDLC VDYVGRDGTQ DMRELAGRFA TASTLPIMLD STEPGVIEAG LETLGGRCVV NSVNFEDGDG PDSRYARLMP VVKEHGAAVV ALLIDEEGQA RTKDWKVRVA TRLIDDLTGR WGMARSDILI DALTFPIATG QEETRRDGIE TIEAIREIAA RYPGVNFTLG ISNVSFGLNP AARQVLNSVF LHECVQAGLT SAIVHASKIL PIAKIPSEQR EIALDLVYDR RREGYDPVQR FIETFEGVDA ASARASRAEE LAALPLNERL KRRIIDGERN GLEADLDAAL AAGMTALVVI NDILLDGMKV VGELFGAGQM QLPFVLQSAE VMKSAVAYLE PHLEKADDGG KGRIVLATVK GDVHDIGKNL VDIILSNNGY EVVNIGIKQP INAILDAAEQ HRADAIGMSG LLVKSTVIMK ENLVEMATRG VAERWPVLLG GAALTRAYVE DDLRSMFPGQ VHYARDAFEG LSLMDRVMAA KRGGAPVVDA EREAALAARR ARRERQRAVV SESLPELHDA SVRSDVATDV DLPTPPFFGT RVIKGLPLAD YAALLDERAT FLGQWGLRGA RGGKGPSYEE LVETEGRPRL RYWLDRLAAD QVLEAAVVYG YFPAYSDGND LVVLDENGHA ERARFTFPRQ RQERRLCLAD FFRPRGAELD VVALQLVTVG QPISEYTAKL FARNEYRDYL EVHGLSVQLT EALAEYWHRR IRTELTLPGD RTVAVDDPAD LAGLLRNDYR GCRYAFGYPA CPDLTDRAKL VELLGAERIG VHLSEEFQLV PEQATDAIVV HHPEASYFNA K // ID A8MFL1_ALKOO Unreviewed; 792 AA. AC A8MFL1; DT 04-DEC-2007, integrated into UniProtKB/TrEMBL. DT 04-DEC-2007, sequence version 1. DT 27-MAY-2015, entry version 47. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABW17650.1}; GN OrderedLocusNames=Clos_0080 {ECO:0000313|EMBL:ABW17650.1}; OS Alkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii OS (strain OhILAs)). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Alkaliphilus. OX NCBI_TaxID=350688 {ECO:0000313|EMBL:ABW17650.1, ECO:0000313|Proteomes:UP000000269}; RN [1] {ECO:0000313|Proteomes:UP000000269} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OhILAs {ECO:0000313|Proteomes:UP000000269}; 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 ----------------------------------------------------------------------- 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; ABW17650.1; -; Genomic_DNA. DR RefSeq; WP_012157965.1; NC_009922.1. DR RefSeq; YP_001511646.1; NC_009922.1. DR ProteinModelPortal; A8MFL1; -. DR STRING; 350688.Clos_0080; -. DR EnsemblBacteria; ABW17650; ABW17650; Clos_0080. DR KEGG; aoe:Clos_0080; -. DR PATRIC; 20865232; VBIAlkOre124042_0087. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; AORE350688:GHBG-95-MONOMER; -. DR Proteomes; UP000000269; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000269}; KW Methyltransferase {ECO:0000313|EMBL:ABW17650.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000269}; KW Transferase {ECO:0000313|EMBL:ABW17650.1}. SQ SEQUENCE 792 AA; 86413 MW; DDDC298761F28783 CRC64; MKIVNRLKDG TLIFDGAMGT MLQNRGLKLG ELPEMLNFSA PEIVIEIHKS YVDAGADVVT TNTFGANELK LAGSPYTVEE VIHKAVVNAR TACEGTDTYV ALDIGPIGEL LAPMGTLSFQ EAYEIFKRQV VQGVKSGADL ILIETMTDLY EAKAAVLAAK ENANVPVFCT MSFEANGRTF TGCTPEAMVL VLEGLGVNAL GVNCSLGPKE LGPIVDHILK IATVPVMVQA NAGLPTVVEG RTVFNVLPED FARHGCNFVE KGVKIVGGCC GTTDRYIEGL KEVLKDRQPG KIEAATLTGV CTPTKVVEIQ GVRVIGERIN PTGKKLLKEA LRSGNLDYIL REAIAQVDAG AHILDVNVGL PEINEEEIME KIVQEIQSIL DVPLQIDSTN PKAIEKGLRI YNGKAIVNSV NGEDKVLERI LPIVKKYGAA VVGLTLDERG IPKTAEARFE IAEKIVDRAL SYGIKREDVY IDCLTLTAAA QQEEVQETLK TIQLVKKHLN VKTVLGVSNV SFGLPNRDLL NRTFLAASIF AGLDLPIINP LDQGMMETIV ASQVLWNQDK SAEAYLKYHQ NQPKTEVGSK PKMAQSQEDL FNMIIKGIRD EAKIATENLL QEKAPLDIVN QYIVPALDFV GERYEKGDLF LPQLIQSAET VKSAFEVIKK KLKENAHSDI SNGKILLATV KGDIHDIGKN IVKVLLENYN YEIIDLGRDV PKEKIVEEVV KNKIKLVGLS ALMTTTVKNM EETIEALKKM DPECIVMVGG AVLNPEYAEM IKADYYAKDA KDAVAIAKNI LG // ID A8N5L5_COPC7 Unreviewed; 355 AA. AC A8N5L5; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EAU91638.1}; GN ORFNames=CC1G_09320 {ECO:0000313|EMBL:EAU91638.1}; 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 {ECO:0000313|EMBL:EAU91638.1, ECO:0000313|Proteomes:UP000001861}; RN [1] {ECO:0000313|Proteomes:UP000001861} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003 RC {ECO:0000313|Proteomes:UP000001861}; 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., Canback 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., Kues 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. {ECO:0000313|EMBL:EAU91638.1}. 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; AACS01000040; EAU91638.1; -; Genomic_DNA. DR RefSeq; XP_001830160.1; XM_001830108.1. DR ProteinModelPortal; A8N5L5; -. DR GeneID; 6006599; -. DR KEGG; cci:CC1G_09320; -. DR EuPathDB; FungiDB:CC1G_09320; -. DR InParanoid; A8N5L5; -. DR KO; K00547; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000001861; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 2. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001861}; KW Reference proteome {ECO:0000313|Proteomes:UP000001861}. SQ SEQUENCE 355 AA; 38870 MW; 8F162F9EDE9BE23A CRC64; MPKPKIAILD GGLGTHLENI IGDEVSKGPL WSTQAVISHP LSVLKTHRNF INAGATIIET ATYQASLPGL IKSGLQEYEA RELMWKAVSL AKEAAADSDA SIALSLGPFG ATLRPTQEFE GFYPPPYGPK AYHPEGPNTQ AFDSNEAEAR AIGALAQFHL DRLLVFSQNS AVWDSIQYLA FETLLLPREV IAIRKAVGLL RTHLFKEHRS FDKSWWISFV VPSDATNPSV LPLVSSALCE GHDLPSAIGI NCTSFGTLLP RTLELCRLVP RFRPLSQLGL VLYPNGGTYD TTNQRWLPDP VDADRQWGLA LRDVLTGVLS ETGAEGWREL IAGGCCRTGP SHISQFAELL REFQE // ID A8Q150_BRUMA Unreviewed; 328 AA. AC A8Q150; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 2. DT 04-MAR-2015, entry version 27. DE SubName: Full=Protein Bm10931, isoform c {ECO:0000313|EMBL:CDQ00485.1}; GN Name=Bm10931 {ECO:0000313|EMBL:CDQ00485.1}; GN ORFNames=BM_Bm10931c {ECO:0000313|EMBL:CDQ00485.1}; OS Brugia malayi (Filarial nematode worm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Spirurida; OC Filarioidea; Onchocercidae; Brugia. OX NCBI_TaxID=6279 {ECO:0000313|EMBL:CDQ00485.1, ECO:0000313|Proteomes:UP000026912}; RN [1] {ECO:0000313|Proteomes:UP000026912} RP NUCLEOTIDE SEQUENCE. RA Ghedin E.; RL Submitted (NOV-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; HF575360; CDQ00485.1; -; Genomic_DNA. DR InParanoid; A8Q150; -. DR OMA; YGRSVTK; -. DR Proteomes; UP000026912; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000026912}; KW Reference proteome {ECO:0000313|Proteomes:UP000026912}. SQ SEQUENCE 328 AA; 36352 MW; A05FE4C5B3E80EE3 CRC64; MARNFAELSR SKGMDAHFTC EKIQILDGGF GTELEAVGYN IENNSLWSCA ALFDNPDLIL QVHKRFIEAG SDIILTNSYQ ACINTMMSSH GMTKNAAESS LKKLVSLAEQ AINECSVREK VKIVGSVGPY GVIFNDGSEY NGYYVDEIEQ QVLVDYHMQQ TIPLLQAGLK VIAYETVPSY KEALAILKAA DAIGYSYNFW ISFSCKNDKQ TNHNEDFCKS VEKIAHHPSI LGIGINCTSP NYITPLLQSA STSVNSLPFI VYPNSGEVYE HSTKKWRIGK CRFPDIEQLI EWKDLGVKVV GGCCRVGAEK IKELSILVAK LNSGYSML // ID A8S298_CLOBW Unreviewed; 821 AA. AC A8S298; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 27-MAY-2015, entry version 36. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDP13445.1}; GN ORFNames=CLOBOL_06010 {ECO:0000313|EMBL:EDP13445.1}; OS Clostridium bolteae (strain ATCC BAA-613 / WAL 16351). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=411902 {ECO:0000313|EMBL:EDP13445.1, ECO:0000313|Proteomes:UP000005396}; RN [1] {ECO:0000313|EMBL:EDP13445.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-613 {ECO:0000313|EMBL:EDP13445.1}; 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 (AUG-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EDP13445.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-613 {ECO:0000313|EMBL:EDP13445.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDP13445.1}. 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; ABCC02000047; EDP13445.1; -; Genomic_DNA. DR RefSeq; WP_007038127.1; NZ_DS480702.1. DR ProteinModelPortal; A8S298; -. DR EnsemblBacteria; EDP13445; EDP13445; CLOBOL_06010. DR PATRIC; 36972467; VBICloBol101009_5029. DR Proteomes; UP000005396; Unassembled WGS sequence. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005396}. SQ SEQUENCE 821 AA; 88124 MW; 2DA6F9984738B704 CRC64; MMMTILEEMK VRRLFCDGGM GSLLQAQGLK PGELPETWNL TRRDVLISIH RSYLEAGADI MTTNTFGANR LKFKDDLESI VTAAVENART AVREAGHGYV ALDLGPTGRL LKPLGDLDFE DAVKLYKEVV SIGARAGADL VLIETMSDSY ELKAAVLAAR EAGFRPDTGE RLPVFATVIF DEKGKLLTGG NVESTVALLE GLRVDALGIN CGLGPVQMKG ILEEILRVSS LPVLVNPNAG LPRSENGKTV YDIDAEGFAL VMEEIAAMGA VVVGGCCGTT PEHIRLMTQR CKDMPVVWPE KKHRTVVSSY AKAVTAGRKT IIIGERINPT GKSKFKQALR DHNLEYILKE GVSQQDNGAD VLDVNVGLPE IHEPSMMEEA VRELQAIIDL PLQIDTSDME AMERAMRIYN GKPLINSVNG KEESMSRIFP LMAKYGGVAV GLCLDESGIP DTADGRLAVG RKIIERAAVY GIGPEDIILD GLCMTVSSDS KGALTTLETL RRIRDELGVG TVLGVSNISF GLPQREIINA AFFTMAMECG LGAAIINPNS EAMMRAYYSF NALMDRDPQC GQYISVYSGQ SAGLGQTIGK SGSQNGIKAD NHFGSGEDQG GGSQGPALTA AIERGLKEAA HNAVTELLKE REPLDIINSE MIPALDRVGK GFEKGTVFLP QLLMSAEAAK AAFEVIKAAM DGSGQAQEKK GTIILATVKG DIHDIGKNIV KVLLENYSYE VIDLGRDVPS EVIVKEAVER QVALVGLSAL MTTTVPSMEE TIRQLRAASV TVKVMVGGAV LTEDYARTIG ADAYCRDAMA SVNYAEQVFG A // ID A8SCX4_9FIRM Unreviewed; 605 AA. AC A8SCX4; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 27-MAY-2015, entry version 37. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=FAEPRAM212_02090 {ECO:0000313|EMBL:EDP21362.1}; OS Faecalibacterium prausnitzii M21/2. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Faecalibacterium. OX NCBI_TaxID=411485 {ECO:0000313|EMBL:EDP21362.1}; RN [1] {ECO:0000313|EMBL:EDP21362.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M21/2 {ECO:0000313|EMBL:EDP21362.1}; 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] {ECO:0000313|EMBL:EDP21362.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M21/2 {ECO:0000313|EMBL:EDP21362.1}; 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 (SEP-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDP21362.1}. 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; ABED02000027; EDP21362.1; -; Genomic_DNA. DR RefSeq; WP_005925170.1; NZ_DS483502.1. DR ProteinModelPortal; A8SCX4; -. DR EnsemblBacteria; EDP21362; EDP21362; FAEPRAM212_02090. DR PATRIC; 30687704; VBIFaePra13114_1864. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EDP21362.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EDP21362.1}. SQ SEQUENCE 605 AA; 65129 MW; F7C9184A7CFD5219 CRC64; MKSFYRKGKV SMLDVRKLLA QRPLLFDGGM GTYYKAKPGQ ECEQANLTDP EGILAVHRAY LAAGADAIKT NTFSLPRLAA AQQPGWEQLA DAGWQLAVKA AGETGAAVFA DLGPAPDTEN LPAEQVYLAV AKRFALLGAR NFLFETLSAE DGVLEAIRAL KQTVPEAFVL VSFAVLPDGY TREGRYCAEL VRRVAQSGVV DAVGLNCVSA PGAMRALVQQ LGDAGLPLSV MPNAGYPVVA RAQVRYQGKP EYFARELSRL ASEGVRILGG CCGTTPQHIA ALRTALDALP EVLPAAPAAK PAVAAKPAVE TDDAFLRKLR AGQRVIAVEL DSPKDADLTA YLEGARRLQA AGADLLTIAD CPIARARMDS SLVACRVHRE LGMNVLPHMT CRDRNLNATK ALLLGLYAEG VREVLAITGD PIPTAERDEV KNVYQFNSRK LAQYIVSLAG EGREMPSPIT VFGALNLNAR NFEVELRRAA EKLENGMSGF LTQPVLSAQA VENLKKTRET LGERAKILAG ILPVVSQRNA IFMENEVNGI HVDDAIIQRF EGLDRAAGEE LGLEVSVQAA KAAAPYVDGF YLMTPFNRVA LMERLIARLR TEVTG // ID A8SDR3_9FIRM Unreviewed; 805 AA. AC A8SDR3; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 27-MAY-2015, entry version 36. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EDP20974.1}; GN ORFNames=FAEPRAM212_02302 {ECO:0000313|EMBL:EDP20974.1}; OS Faecalibacterium prausnitzii M21/2. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Faecalibacterium. OX NCBI_TaxID=411485 {ECO:0000313|EMBL:EDP20974.1}; RN [1] {ECO:0000313|EMBL:EDP20974.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M21/2 {ECO:0000313|EMBL:EDP20974.1}; 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] {ECO:0000313|EMBL:EDP20974.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M21/2 {ECO:0000313|EMBL:EDP20974.1}; 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 (SEP-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. {ECO:0000313|EMBL:EDP20974.1}. 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; ABED02000028; EDP20974.1; -; Genomic_DNA. DR RefSeq; WP_005920806.1; NZ_DS483482.1. DR ProteinModelPortal; A8SDR3; -. DR EnsemblBacteria; EDP20974; EDP20974; FAEPRAM212_02302. DR PATRIC; 30684436; VBIFaePra13114_0292. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDP20974.1}; KW Transferase {ECO:0000313|EMBL:EDP20974.1}. SQ SEQUENCE 805 AA; 85032 MW; AEE2318A50D68E75 CRC64; MNELFRQSNT ILLDGGMGTM LQAAGLKLGA RPEELNITDP ALIEGIHGQY AAAGSRIVNA NTFGASAHKL AGSTYTLEQV ITAGIENCKR ACAPYGALTA LDVGPLGELL EPSGTLAFED AVAEYARIVK AGEAAGADLI FFETYTDLYE LKAALLAAKE NTRLPILASM SFEAGGRTFT GCTVESFAAT ARGLGADAVG INCSLGPKEI FPMAKRLAEA VPGNFPVFVK PNAGLPRADG SGYDITPQLF ALQMKPYREL HLFAAGGCCG TTPEFIKLLN GTFAGCTPGR PAHRMPSVLC TPVDTVTVDG ITVVGERINP TGKKRFQQAL REGDMNYVLE QAVSQAEAGA QILDVNVGAP GVDEPVLMEQ VVKALQSVTS LPLQLDSSNV EALARGLRVY NGKPIVNSTN GEPEKLAAIL PLCKKYGAAI VGLAIDEKGI QPKAADRVAI ARRITEAALA AGIPREDIYI DCLTLTASAQ QEDVLATVQA LEACKKELGV RTVLGVSNIS FGLPCRTYLN TTFLTMAMYA GLDLAIMNPS SEEMMAAVYA YNVLTNRDKQ STKYIERFAD RVPASTALAQ AAKAAPAASA AEAELTGPYA ALMKAVEKGL KGDAAAHTRA LLAEKQPLEV VDEALIPALD IVGAKYEKGT LFLPQLLQAA SAAQSAFEEI KTAIAQKGEG SASKGRIVLA TVKGDVHDIG KNIVRVILEN YGFEVLDLGR DVPVETVVDT VREKDVHLVG LSALMTTTLK SMEETIAALR AAKLDCKIMV GGAVLTPEYA EKIGADWYAK DAKRSADIAK EFFGV // ID A8SP62_9FIRM Unreviewed; 808 AA. AC A8SP62; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 27-MAY-2015, entry version 35. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EDP27475.1}; GN ORFNames=COPEUT_00184 {ECO:0000313|EMBL:EDP27475.1}; OS Coprococcus eutactus ATCC 27759. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Coprococcus. OX NCBI_TaxID=411474 {ECO:0000313|EMBL:EDP27475.1}; RN [1] {ECO:0000313|EMBL:EDP27475.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27759 {ECO:0000313|EMBL:EDP27475.1}; 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] {ECO:0000313|EMBL:EDP27475.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27759 {ECO:0000313|EMBL:EDP27475.1}; 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 (SEP-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. {ECO:0000313|EMBL:EDP27475.1}. 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; ABEY02000003; EDP27475.1; -; Genomic_DNA. DR RefSeq; WP_004850896.1; NZ_DS483529.1. DR ProteinModelPortal; A8SP62; -. DR EnsemblBacteria; EDP27475; EDP27475; COPEUT_00184. DR PATRIC; 29079291; VBICopEut84706_1084. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDP27475.1}; KW Transferase {ECO:0000313|EMBL:EDP27475.1}. SQ SEQUENCE 808 AA; 86965 MW; 4104AB57863D8845 CRC64; MNKTEFRKLF DDKILILDGA TGTNLMDAGM PLGVCPEQWI LEHKQIMIDL QTAYLNAGTD ILYAPTFTCN RIKLNEYGLA DNLVSMNSEL VKLSQKAVEN AGHGLVAGDI TMTGEMLYPM GKLQFEELVD VYKEQIKVLD ESGCDLLVVE TMMSLAETRA AVIAANEVSK LPIIASLTFN EDGRTLYGTD PVTAVNVLQN LGVAAIGVNC STGPDKMVEL VKQMKSIAFI PVFAKPNAGM PELVDDKSVY KMTPEEFAAD MKLIIEAGAG MVGGCCGTRP DHIKALSDMA ATVPVPKISS EHVRCISSER SSLVIDLDAP FKVVGERINP TGKKKLQAEL REGSLELVMN MAEEQVEKGA SILDINVGMN GIDEREMMLK VVYQVSQAVN LPLCLDSSSP EVIEAALRIY PGRALVNSVS LEKVKMEEIL PLVRKYGAMF ILLPLSDKGL PESSQEKEDI INTVLGTAYD LGFTKKDVVV DGLVATIGAQ KDAAVNCLRT INYCYSNGLA TICGLSNISF GLPERMFVNT AFLTMAIERG LTMAIANPSQ TMLMNAAYAS DMLLFKEDSD VRYIENVKAL DIAAPGAGAS GGKAGADLEG KSQIYIDVLK GNKRTILDDV NAVLASGADP QSIIDDDLIS AINEVGKLFE KKKYFLPQLI SSAETMEMAI GVISPLVLKG KDSSNMPTIV VATVEGDIHD IGKNLVVLML RNYGFNVIDL GKDVPCDVII QAAKENNASI IGLSALMTTT MVKMKDVVEA VRENGLDSKV IIGGAVITES YAEEIGADGY SEDAADCVVL VKELLGIE // ID A8SPV0_9FIRM Unreviewed; 606 AA. AC A8SPV0; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 27-MAY-2015, entry version 35. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=COPEUT_00890 {ECO:0000313|EMBL:EDP27369.1}; OS Coprococcus eutactus ATCC 27759. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Coprococcus. OX NCBI_TaxID=411474 {ECO:0000313|EMBL:EDP27369.1}; RN [1] {ECO:0000313|EMBL:EDP27369.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27759 {ECO:0000313|EMBL:EDP27369.1}; 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] {ECO:0000313|EMBL:EDP27369.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27759 {ECO:0000313|EMBL:EDP27369.1}; 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 (SEP-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDP27369.1}. 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; ABEY02000006; EDP27369.1; -; Genomic_DNA. DR RefSeq; WP_004852224.1; NZ_DS483532.1. DR ProteinModelPortal; A8SPV0; -. DR EnsemblBacteria; EDP27369; EDP27369; COPEUT_00890. DR PATRIC; 29080564; VBICopEut84706_1718. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EDP27369.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EDP27369.1}. SQ SEQUENCE 606 AA; 66622 MW; F9C1F6921423C90D CRC64; MNILESLRDK LLVADGAFGT CYAGMYGERG TVAPELANMR HPERVLEIHK EYVKAGAGII RTNTFAANTA SLDADMDYVI SNVRAAVKLA KQAVAETGAP GIDRKKAYVA GDIGPIPADA GLTLNERVSQ YKLLGEAMQD MGVDIIWFET FPEFNVLEPV VKQLKARKDT PVMVSFCVNQ FGYSNCGFSA RALLSQAAAN SDVDCVGLNC GVGPYHMLQL LKKLDIDCGK PVSIMPNAGY PKFTQSRLVF NDNKEGFIDK IQDIAALGAD IIGGCCGTNP EYIRQIKESV KKGDIVKAAK VHVEKQQFDN APKDNFLKGR LKSGKAAVKN AGGHKLIAVE LAPPVDVNDQ KLLDAAHILK QSHVDVVTFP DSPSGRTRAD SILMAEKVHK ETGLRVMPHL CCRDKNAIAI RGSVLGAQLN GIKDFLVITG DPVPVMFRQT TRSVFNFDSV GMMKLLQTMN EEVFIGDKIT YGGAINQNRI NTKFEIDRIK RKLEAGAEFF LSQPVFSREQ AQILRDMKAE TGATILVGIM PLVSRRNALF MKNEMTGIEI PDEIIERYGE NATRQEGEDC GIQIAREILD YTADFADGYY FSFPFNRVHM LAHIVD // ID A8T0K2_9VIBR Unreviewed; 310 AA. AC A8T0K2; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EDP60788.1}; GN ORFNames=AND4_07709 {ECO:0000313|EMBL:EDP60788.1}; OS Vibrio sp. AND4. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=314289 {ECO:0000313|EMBL:EDP60788.1}; RN [1] {ECO:0000313|EMBL:EDP60788.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AND4 {ECO:0000313|EMBL:EDP60788.1}; 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] {ECO:0000313|EMBL:EDP60788.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AND4 {ECO:0000313|EMBL:EDP60788.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDP60788.1}. 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; ABGR01000001; EDP60788.1; -; Genomic_DNA. DR RefSeq; WP_009841245.1; NZ_ABGR01000001.1. DR ProteinModelPortal; A8T0K2; -. DR EnsemblBacteria; EDP60788; EDP60788; AND4_07709. DR PATRIC; 28390037; VBIVibSp137788_0442. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EDP60788.1}; KW Transferase {ECO:0000313|EMBL:EDP60788.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 212 212 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 287 287 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 310 AA; 33930 MW; 61E435ACF8AD8B1D CRC64; MDLSMKKLTI LDGGMGRELK RIGAPFSQPL WSAQALIESP QFVYQAHNNF IQAGAEIITA NSYACVPFHL GQDGYEQKGR DLACFAAKIA RECADNALAS VQVAGCLPPA FGSYRPDLFD PNQGEAIFRT LFEAQDEYVD LWIAETICSL KELDGLQSVF KSCNKPTAYA FSLSDDSMEH ALLRSGETVR QAIEHLVANE DTGNTISVYF NCSVPEVMTK AIIATKAVLE SHNVDIEIGV YANNFTAIKS NHEANRSLQS MRELSPEEYL AFAKEWHHNG ATVIGGCCGI GPEHIAVLSE WKCGVSHGCK // ID A8T919_9VIBR Unreviewed; 1226 AA. AC A8T919; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 01-APR-2015, entry version 44. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EDP58113.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EDP58113.1}; GN Name=metH {ECO:0000313|EMBL:EDP58113.1}; GN ORFNames=AND4_13170 {ECO:0000313|EMBL:EDP58113.1}; OS Vibrio sp. AND4. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=314289 {ECO:0000313|EMBL:EDP58113.1}; RN [1] {ECO:0000313|EMBL:EDP58113.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AND4 {ECO:0000313|EMBL:EDP58113.1}; 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] {ECO:0000313|EMBL:EDP58113.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AND4 {ECO:0000313|EMBL:EDP58113.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EDP58113.1}. 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; ABGR01000014; EDP58113.1; -; Genomic_DNA. DR RefSeq; WP_009843529.1; NZ_ABGR01000014.1. DR ProteinModelPortal; A8T919; -. DR SMR; A8T919; 654-1224. DR EnsemblBacteria; EDP58113; EDP58113; AND4_13170. DR PATRIC; 28394659; VBIVibSp137788_2708. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EDP58113.1}; KW Transferase {ECO:0000313|EMBL:EDP58113.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1226 AA; 136512 MW; CAC149B0F097401C CRC64; MGSNVRQQIE AQLKQRILLI DGGMGTMIQG YQLEEQDYRG ERFADWHSDL KGNNDLLVLT QPQLIKEIHS AYLEAGADIL ETNTFNATTI AMADYEMESL SEEINFAAAK LAREAVDEWT SKTPDRPRYV AGVLGPTNRT CSISPDVNDP GYRNVSFDEL VEAYSESTRA LIRGGSDLIL IETIFDTLNA KACAFAVDSV FEELEITLPV MISGTITDAS GRTLSGQTTE AFYNSLRHVN PISFGLNCAL GPDELRPYVE ELSRISESFI STHPNAGLPN AFGEYDLSPE EMANHVKEWA ESGFLNLIGG CCGTTPEHIR HMAMAVEGMK PRELPDLTVA CRLSGLEPLT IEKESLFINV GERTNVTGSA RFKRLIKEEL YDEALEVARQ QVENGAQIID INMDEGMLDA EACMVRFLHL CASEPEISKV PIMVDSSKWE VIEAGLKCIQ GKGIVNSISL KEGKEKFIEQ AKLIRRYGAA VIVMAFDELG QAETRERKLE ICTNAYRILV DEVGFPAEDI IFDPNIFAVA TGIEEHNNYA VDFIEAVADI KRDLPHAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK NGMDMGIVNA GQLEIYDNVP DKLREAVEDV VLNRRDDSTE RLLDIAAEYA GKGVGKEEDA SAQEWRTWAV EKRLEHALVK GITEFIVEDT EEARLNASKP LEVIEGPLMD GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AHLEPFINEE KQAGSSNGKI LLATVKGDVH DIGKNIVGVV LQCNNYEIID LGVMVPCDKI LKVAKEENVD IIGLSGLITP SLDEMVHVAK EMERLDFDVP LLIGGATTSK AHTAVKIEQN YKNPVVYVNN ASRAVGVCSS LLSDERRPGF VEKLDADYER VREQHHRKKP RTKPVTLEAA RANKVAIDWG AYTPPIPAKP GIHVFDDFEV STLRKYIDWT PFFMTWSLVG KYPTIFKHSE VGEEAQRLYK DANDLLERIE SEGLLKARGM CGLFPAASVG DDIEVYTDES RTEVARVLLN LRQQTEKPKG FNYCLSDYIA PKESGKKDWI GAFAVTGGIG ERELADEYKA QGDDYNAIMI QAVADRLAEA FAECLHERVR KEIWGYAVEE DLSNEELIRE KYQGIRPAPG YPACPEHTEK GPIWDLMNVE ENIGMSLTSS YAMYPGASVS GWYFSHPDSR YFAIAQIQED QLLSYADRKG WDRIEAEKWL GPNING // ID A8TIL6_9PROT Unreviewed; 344 AA. AC A8TIL6; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Methionine synthase I {ECO:0000313|EMBL:EDP66509.1}; GN ORFNames=BAL199_15648 {ECO:0000313|EMBL:EDP66509.1}; OS alpha proteobacterium BAL199. OC Bacteria; Proteobacteria; Alphaproteobacteria. OX NCBI_TaxID=331869 {ECO:0000313|EMBL:EDP66509.1}; RN [1] {ECO:0000313|EMBL:EDP66509.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BAL199 {ECO:0000313|EMBL:EDP66509.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDP66509.1}. 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; ABHC01000001; EDP66509.1; -; Genomic_DNA. DR RefSeq; WP_007668209.1; NZ_ABHC01000001.1. DR ProteinModelPortal; A8TIL6; -. DR EnsemblBacteria; EDP66509; EDP66509; BAL199_15648. DR PATRIC; 30872163; VBIAlpPro7182_0087. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 344 AA; 35513 MW; 0D00E46966EF8F76 CRC64; MADCLTDLLA ERGHLIADGA MGTNLFALGL ETGDSPELWN VEHPDRVATV HRDFLEAGSD IVLTNSFGGS SFRLKLHHAQ DRVRELNAAA AGIARREVDA HAASTGRRTL VAGSIGPTGE LFIPLGALTA EAAADAFAEQ AAGLAEGGAD VLWIETMSAP EEVLAAVAGG ARTGLPIVVT MTFDTNARTM MGVTPVEFAN FAQALEHTPV AIGANCGVGP AELVDTILGI TAAAPGAVVI AKGNCGIPQY VEGAIVYNGS PEAMAAYAQL VRDAGARIVG GCCGSTAIHV KAIAEALDGY VPGSRPDLAR VTEVLGAPWV KPGRLADSDP RADSEPRRPR RRRA // ID A8TSY9_9PROT Unreviewed; 315 AA. AC A8TSY9; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 01-OCT-2014, entry version 14. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EDP64386.1}; GN ORFNames=BAL199_09193 {ECO:0000313|EMBL:EDP64386.1}; OS alpha proteobacterium BAL199. OC Bacteria; Proteobacteria; Alphaproteobacteria. OX NCBI_TaxID=331869 {ECO:0000313|EMBL:EDP64386.1}; RN [1] {ECO:0000313|EMBL:EDP64386.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BAL199 {ECO:0000313|EMBL:EDP64386.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDP64386.1}. 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; ABHC01000009; EDP64386.1; -; Genomic_DNA. DR RefSeq; WP_007674271.1; NZ_ABHC01000009.1. DR EnsemblBacteria; EDP64386; EDP64386; BAL199_09193. DR PATRIC; 30877637; VBIAlpPro7182_2799. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDP64386.1}; KW Transferase {ECO:0000313|EMBL:EDP64386.1}. SQ SEQUENCE 315 AA; 33916 MW; A27EF4F2F716BF5F CRC64; MKSYREHLPQ LADRIFLTDG GIETTLIYLE GLDLPYFAAF RLLQDETGRE TLRRYYRRHA EIARLNGVGF ILESATWRAS ADWADKVGVS LTALDETNRM AIDLLHGLRA ELQTEGSPMV VSGCVGPRGD GYDPGKVMTA AEAQAYHGRQ IAVFATAGAD MVTAITMTNT PEAVGVALAA KSRGMPVAIS FTVETNGRLP TGQPLQDAIA AVDAATGAAP AYYMINCAHP THFAEQLVAG QPWVSRIRGV RANASRCSHA ELDRATELDA GDPVELGALY RDLRARLGHI SVLGGCCGTD HRHIEQIAGQ CRKAA // ID A8TTR6_9PROT Unreviewed; 354 AA. AC A8TTR6; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EDP64190.1}; GN ORFNames=BAL199_06329 {ECO:0000313|EMBL:EDP64190.1}; OS alpha proteobacterium BAL199. OC Bacteria; Proteobacteria; Alphaproteobacteria. OX NCBI_TaxID=331869 {ECO:0000313|EMBL:EDP64190.1}; RN [1] {ECO:0000313|EMBL:EDP64190.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BAL199 {ECO:0000313|EMBL:EDP64190.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDP64190.1}. 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; ABHC01000010; EDP64190.1; -; Genomic_DNA. DR RefSeq; WP_007674678.1; NZ_ABHC01000010.1. DR ProteinModelPortal; A8TTR6; -. DR EnsemblBacteria; EDP64190; EDP64190; BAL199_06329. DR PATRIC; 30878082; VBIAlpPro7182_3021. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 354 AA; 37994 MW; 12CEABAE27D7F8F7 CRC64; MTRSDRLDAL DQLAKQCVVV LDGAMGTMIQ NLKFNEAEFR GERFKDHGSE LQGDNDILNL SKPEAIEEIH HAYLDAGADI IQTNTFNATS ISQADYALQD LAREINRVGA EIARRAADAH TAKTGRPAFV GGGLGPTNRT ASISPDVNNP GARNVRFDEL REAYHDATMG LIEGGADLIM VETIFDTLNA KAALVAVREA FDEAKVELPI IISGTITDRS GRTLSGQTPE AFWNSVRHAR PFAVGFNCAL GAKELRAHVA ELSRVADVKV SAYPNAGLPN EFGGYDETPD QTASHLGRWA ADGLINLVGG CCGTTPDHIR AIAEAVKASG PRVVPSVPRR LRLSGLEPFE IQAA // ID A8TTR7_9PROT Unreviewed; 317 AA. AC A8TTR7; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EDP64191.1}; GN ORFNames=BAL199_06334 {ECO:0000313|EMBL:EDP64191.1}; OS alpha proteobacterium BAL199. OC Bacteria; Proteobacteria; Alphaproteobacteria. OX NCBI_TaxID=331869 {ECO:0000313|EMBL:EDP64191.1}; RN [1] {ECO:0000313|EMBL:EDP64191.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BAL199 {ECO:0000313|EMBL:EDP64191.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDP64191.1}. 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; ABHC01000010; EDP64191.1; -; Genomic_DNA. DR RefSeq; WP_007674679.1; NZ_ABHC01000010.1. DR ProteinModelPortal; A8TTR7; -. DR EnsemblBacteria; EDP64191; EDP64191; BAL199_06334. DR PATRIC; 30878084; VBIAlpPro7182_3022. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDP64191.1}; KW Transferase {ECO:0000313|EMBL:EDP64191.1}. SQ SEQUENCE 317 AA; 32855 MW; DFBE3197DC0B09A7 CRC64; MTRADLIAAA RGAPLLVSGG LAEPLAGHGA ACLEVLNLEQ PRDVRAAHAG YLAAGARVIR TNTAGASPER LDRYRMHDEA FIVSYMAAEH AVQSARISTD ETGVTRWVLG VARMESRIRQ LGFLPLERVE SAARTMASGL AGGGVDAIVV ETNQDGARLA AAFDGVRRGM SDAGRSVPVL LTLRYDALFA TPHRDRVTEE LAGAAAAAAG LGVAALGIAN TDLADGWAAT LRAVARAFPG PLMVEAAPTS RDLTAILNDP ILWFRLALVG GGASPQDTKL LSERLGALQG GDEVGNLHAA AANDPAAVPA RRPKGKL // ID A8UF05_9FLAO Unreviewed; 333 AA. AC A8UF05; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=Methionine synthase I, homocysteine S-methyltransferase {ECO:0000313|EMBL:EDP72564.1}; GN ORFNames=FBALC1_15722 {ECO:0000313|EMBL:EDP72564.1}; OS Flavobacteriales bacterium ALC-1. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales. OX NCBI_TaxID=391603 {ECO:0000313|EMBL:EDP72564.1}; RN [1] {ECO:0000313|EMBL:EDP72564.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ALC-1 {ECO:0000313|EMBL:EDP72564.1}; 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 (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. {ECO:0000313|EMBL:EDP72564.1}. 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; ABHI01000001; EDP72564.1; -; Genomic_DNA. DR RefSeq; WP_008269657.1; NZ_ABHI01000001.1. DR ProteinModelPortal; A8UF05; -. DR EnsemblBacteria; EDP72564; EDP72564; FBALC1_15722. DR PATRIC; 27398677; VBIFlaBac8923_0732. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDP72564.1}; KW Transferase {ECO:0000313|EMBL:EDP72564.1}. SQ SEQUENCE 333 AA; 36656 MW; BAF9065ABAB051C7 CRC64; MHNIYKEIQK RILVLDGAMG TMLQQYNFSE GDFRGERFAA YPSPLKGNND LLSLTQPKAI AEVHAKYFEA GADIVETNTF SGTTIAMADY DMEDLVYELN FESAKIAKEV ADKFTKANPE QPRFVAGSIG PTNKTASLSP DVNRPEYRAI TFNELRIAYK QQVEALIDGG VDVLLVETIF DTLNAKAALF AIEEVKDERN IDIPIMVSGT ITDASGRTLS GQTVEAFLTS ISHIPLLSVG FNCALGAEQL KPYLQRLSNE TEFYTSAHPN AGLPNAFGEY DESPKQMQSY IEDYLKDGLI NIIGGCCGTS PAHINAIAEV AKNYQPRLIQ KFA // ID A8WG15_DANRE Unreviewed; 307 AA. AC A8WG15; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 27-MAY-2015, entry version 39. DE SubName: Full=Zgc:172121 protein {ECO:0000313|EMBL:AAI54543.1}; GN ORFNames=zgc:172121 {ECO:0000313|EMBL:AAI54543.1, GN ECO:0000313|ZFIN:ZDB-GENE-030131-9545}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|EMBL:AAI54543.1}; RN [1] {ECO:0000313|EMBL:AAI54543.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Whole {ECO:0000313|EMBL:AAI54543.1}; RG NIH - Zebrafish Gene Collection (ZGC) project; 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; BC154542; AAI54543.1; -; mRNA. DR RefSeq; NP_001108360.1; NM_001114888.1. DR UniGene; Dr.115279; -. DR ProteinModelPortal; A8WG15; -. DR GeneID; 337599; -. DR ZFIN; ZDB-GENE-030131-9545; zgc:172121. DR HOGENOM; HOG000265278; -. DR HOVERGEN; HBG062720; -. DR NextBio; 20812327; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; SQ SEQUENCE 307 AA; 33850 MW; 5EB5B0F422BBEBE1 CRC64; MDSSPFILDG GLATELEASG FQLQGDPLWS ARVLHTDPQA IKDVHYRYLQ SGSDVITTAT YQASIEGFVK YLGVQPEEAQ HMMMSAVQLA KETVSEFISQ SPMSDRREPL VAGSVGPYGS FLHDGSEYTG AYEDKMTVEE LKDWHRPQIQ CLVKAGADLV AMETIPGLKE AEALVKVLKE FPETKAWLSF SCKDNNSISS GRRFSEAVEM ACRSTQLVAV GVNCCPALLV KPLLESAKSH KRADLSWVVY PNSGEGWDVT TGWKTEMRTS FANLSLEWKA QGALWIGGCC RVRPADITEL KQLHVQP // ID A8XME5_CAEBR Unreviewed; 247 AA. AC A8XME5; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 2. DT 07-JAN-2015, entry version 40. DE SubName: Full=Protein CBG15622 {ECO:0000313|EMBL:CAP33820.2}; GN ORFNames=CBG15622 {ECO:0000313|EMBL:CAP33820.2, GN ECO:0000313|WormBase:CBG15622}, GN CBG_15622 {ECO:0000313|EMBL:CAP33820.2}; OS Caenorhabditis briggsae. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP33820.2, ECO:0000313|Proteomes:UP000008549}; RN [1] {ECO:0000313|EMBL:CAP33820.2, ECO:0000313|Proteomes:UP000008549} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AF16 {ECO:0000313|EMBL:CAP33820.2, RC ECO:0000313|Proteomes:UP000008549}; RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045; RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N., RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., RA D'Eustachio P., Fitch D.H.A., Fulton L.A., Fulton R.E., RA Griffiths-Jones S., Harris T.W., Hillier L.W., Kamath R., RA Kuwabara P.E., Mardis E.R., Marra M.A., Miner T.L., Minx P., RA Mullikin J.C., Plumb R.W., Rogers J., Schein J.E., Sohrmann M., RA Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K., Durbin R.M., RA Waterston R.H.; RT "The genome sequence of Caenorhabditis briggsae: a platform for RT comparative genomics."; RL PLoS Biol. 1:166-192(2003). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=AF16; RG WormBase Consortium; 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; HE601374; CAP33820.2; -; Genomic_DNA. DR EnsemblMetazoa; CBG15622; CBG15622; CBG15622. DR WormBase; CBG15622; CBP33137; WBGene00035790; -. DR InParanoid; A8XME5; -. DR OMA; YEGIRIF; -. DR OrthoDB; EOG7GQXW0; -. DR Proteomes; UP000008549; Chromosome IV. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008549}; KW Reference proteome {ECO:0000313|Proteomes:UP000008549}. SQ SEQUENCE 247 AA; 28222 MW; E603EC81CB6941BC CRC64; MVRLMDGSMS VQLKQFGYDC NALENKPHWS FPANSDMHLM EQVYRSFLDL GSKIITTNTY HFGSTLDRKL DKNEENFEKT CNLLVNLAKE YEGIRIFGSV GTLATFYHDL SEYSGKYMDL PDAETTAFNY FHKILTIFQG KTKIRNLIFE TIPSALEATV ALDVLEQFPE MKAIFSFTFK ENAHLRHGEH IETILVKLKK SKQIFGIGIN CTDPENVLSV LKSVKNLGFP EIFVYPNMGD SRFLSGK // ID A8YJN6_MICAE Unreviewed; 1117 AA. AC A8YJN6; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 27-MAY-2015, entry version 44. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CAO87653.1}; GN Name=metH {ECO:0000313|EMBL:CAO87653.1}; GN ORFNames=IPF_4230 {ECO:0000313|EMBL:CAO87653.1}; OS Microcystis aeruginosa PCC 7806. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Microcystis. OX NCBI_TaxID=267872 {ECO:0000313|EMBL:CAO87653.1}; RN [1] {ECO:0000313|EMBL:CAO87653.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PCC 7806 {ECO:0000313|EMBL:CAO87653.1}; RA Frangeul L.; RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AM778951; CAO87653.1; -; Genomic_DNA. DR ProteinModelPortal; A8YJN6; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 228 228 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 737 737 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1117 AA; 123678 MW; C6EE310A05C07DE2 CRC64; MNSPFLDYLN GPKHPVLVFD GAMGTSLQSQ NLTAEDFGGA EYEGCNEYLV HTKPSAVAKV HEAFLAVGAD VIETDTFGGT SIVLAEYDLA DQAYYLNKSA AELAKACANK YSTPEKPRFV AGSMGPGTKL PTLGHIDFDT LKNAYVEQVE GLYDGGADLL LVETCQDVLQ IKAALNAIEE VFQKKGQRLP LMVSVTMETM GTMLVGTEIN AVVSILQPYK IDILGLNCAT GPDLMKPHIK YLSENSPFIV SCIPNAGLPE NVGGQAHYRL TPVELKMALM HFIEDLGVQI IGGCCGTRPD HIQALAELSQ GLTPKSRHYH YEPSAASIYS TQPYIQDNSF LIVGEKLNAS GSKKCRELLN VEDWDSLVSM AKAQVKEGAH ILDVNVDYVG RDGVRDMHQL ASRLVNNVTL PLMLDSTEWE KMEAGLKVAG GKCILNSTNY EDGESRFYQV LDLAKKYGAG VVIGTIDEEG MGRTAEKKFQ IAKRAYYAAI EYGIPPYEIF FDPLALPIST GIEEDRENGK ATIEAMGRIR QELPECHILL GVSNISFGLN PAARQVLNSV FLNEAMQVGM DGAIVSANKI LPLAKIEPEY QQICRDLIYD NRRFDGDICV YDPLTKLTEL FAGKTTKKDP STNANLPVEE RLKQHIIDGE RLGLEEALKQ ALQDYPPLDI INIFLLDGMK VVGELFGSGQ MQLPFVLQSA QTMKAAVAFL EPFMEKKEGD NNAKGTFIIA TVKGDVHDIG KNLVDIILTN NGYRVINLGI KQPVENIIEA YQEHKADCIA MSGLLVKSTA FMKENLEVFN EKGITVPVIL GGAALTPKFV HDDCQKTYKG QVIYGKDAFS DLHFMDKLMP AKAGGQWDDS EGFLGKFAEA EKTPVVAEEL KVNPDTIFTD GSVNQELVID TRRSEAVAVD ISRPTPPFWG TKILTAAEIP IEEVFWYLDL QALFVGQWQF RKPKSQSKQE YDQFLQEKVH PILAAWKEKI VKENLLNPTL IYGYFPCQSS GNSLLIYDPE SIQAGEKPEN LQPIAIFEFP RQKSGRRLCI ADFFAPQESG IIDVFPMQAV TVGEIATEYA KSLFDANERI YRIPLLSRYG CANRRSHGRM DPHPHPSRVR FRRVRSR // ID A8YVC8_LACH4 Unreviewed; 331 AA. AC A8YVC8; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABX27215.1}; GN OrderedLocusNames=lhv_1172 {ECO:0000313|EMBL:ABX27215.1}; OS Lactobacillus helveticus (strain DPC 4571). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=405566 {ECO:0000313|EMBL:ABX27215.1, ECO:0000313|Proteomes:UP000000790}; RN [1] {ECO:0000313|EMBL:ABX27215.1, ECO:0000313|Proteomes:UP000000790} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DPC 4571 {ECO:0000313|EMBL:ABX27215.1, RC ECO:0000313|Proteomes:UP000000790}; RX PubMed=17993529; DOI=10.1128/JB.01295-07; RA Callanan M., Kaleta P., O'Callaghan J., O'Sullivan O., Jordan K., RA McAuliffe O., Sangrador-Vegas A., Slattery L., Fitzgerald G.F., RA Beresford T., Ross R.P.; RT "Genome sequence of Lactobacillus helveticus: an organism RT distinguished by selective gene loss and IS element expansion."; RL J. Bacteriol. 190:727-735(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; CP000517; ABX27215.1; -; Genomic_DNA. DR RefSeq; WP_012211892.1; NC_010080.1. DR RefSeq; YP_001577506.1; NC_010080.1. DR ProteinModelPortal; A8YVC8; -. DR STRING; 405566.lhv_1172; -. DR EnsemblBacteria; ABX27215; ABX27215; lhv_1172. DR KEGG; lhe:lhv_1172; -. DR PATRIC; 22234568; VBILacHel91643_1235. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; QCKDENT; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; LHEL405566:GJEN-1067-MONOMER; -. DR Proteomes; UP000000790; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000790}; KW Methyltransferase {ECO:0000313|EMBL:ABX27215.1}; KW Transferase {ECO:0000313|EMBL:ABX27215.1}. SQ SEQUENCE 331 AA; 37462 MW; 6D7A771E085118B1 CRC64; MDKLKVVTRS TRPFGDGCFL FLLKNEKEVL MMNLISRAKK GIVLDGAMSD ELERQGVKTN NKLWTATALI NELDKIYQAH WDYFTAGAEL VITDTYQANV QAFTQAGYSE QEAEKFIRDA VKVAKKARDD YEQKTGKHNY VAGTVGSYSA YLADGNEYRG DYELSELEYL AFHLPRLRQI LAEKPDLIAL ETQPKLDEPL AVLNWLKENA SDYPVYVSFT LKDATHISDG TTLEQAVSAV DKFEQVFAIG INCISPDLVA PALKEIGKYT FKPLVLYPNL GASYDPKIKQ WREFKEKFDF NKLTKKWYQE GARLIGGCCT TGPTEIKQML V // ID A9A1I5_NITMS Unreviewed; 320 AA. AC A9A1I5; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 27-MAY-2015, entry version 46. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABX13164.1}; GN OrderedLocusNames=Nmar_1268 {ECO:0000313|EMBL:ABX13164.1}; OS Nitrosopumilus maritimus (strain SCM1). OC Archaea; Thaumarchaeota; Nitrosopumilales; Nitrosopumilaceae; OC Nitrosopumilus. OX NCBI_TaxID=436308 {ECO:0000313|EMBL:ABX13164.1, ECO:0000313|Proteomes:UP000000792}; RN [1] {ECO:0000313|EMBL:ABX13164.1, ECO:0000313|Proteomes:UP000000792} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SCM1 {ECO:0000313|EMBL:ABX13164.1, RC ECO:0000313|Proteomes:UP000000792}; 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 Lykidis A., Stahl D., Richardson P.; RT "Complete sequence of Nitrosopumilus maritimus SCM1."; 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; CP000866; ABX13164.1; -; Genomic_DNA. DR RefSeq; WP_012215651.1; NC_010085.1. DR RefSeq; YP_001582602.1; NC_010085.1. DR ProteinModelPortal; A9A1I5; -. DR STRING; 436308.Nmar_1268; -. DR EnsemblBacteria; ABX13164; ABX13164; Nmar_1268. DR GeneID; 5773358; -. DR KEGG; nmr:Nmar_1268; -. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR BioCyc; NMAR436308:GI3J-1301-MONOMER; -. DR Proteomes; UP000000792; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000792}; KW Methyltransferase {ECO:0000313|EMBL:ABX13164.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000792}; KW Transferase {ECO:0000313|EMBL:ABX13164.1}. SQ SEQUENCE 320 AA; 35335 MW; 2A24AFF6E3AF9392 CRC64; MTEKEPFLDA LQNRVLLFDG AMGTEIQKFN PKPEDFPNNQ DGFNDGLVVT RPDWIKQIHR HYLDAGADCI ETNSFGSNKI KLDEYGFGDQ TIEFNKKIAQ LASEVCQEYS DRPRYVIGSM GPSGFLPSSN DPDLGQKPLD EIKEAFELQA EGLILGGVDA LLIETSQDIL EVKLVIEACH QAMEKTGKKI PIIANTTLDQ YGKMLLGTNI QAAYTTVSDM GIDVFGMNCS TGPIEMTPSV RWLDEQNEHN ILVVPNAGMP ENEGGQAVYK MTPEKMGDAL GDFLNQYKKV RIIGGCCGTN PEHIKVLRKV IDEKANSVEG // ID A9AE61_BURM1 Unreviewed; 367 AA. AC A9AE61; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 27-MAY-2015, entry version 44. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABX14083.1}; DE Flags: Precursor; GN OrderedLocusNames=Bmul_0388 {ECO:0000313|EMBL:ABX14083.1}; OS Burkholderia multivorans (strain ATCC 17616 / 249). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=395019 {ECO:0000313|EMBL:ABX14083.1, ECO:0000313|Proteomes:UP000007064}; RN [1] {ECO:0000313|Proteomes:UP000007064} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17616 / 249 {ECO:0000313|Proteomes:UP000007064}; 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. CC ----------------------------------------------------------------------- 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; ABX14083.1; -; Genomic_DNA. DR RefSeq; WP_012212623.1; NC_010084.1. DR RefSeq; YP_001578580.1; NC_010084.1. DR STRING; 395019.Bmul_0388; -. DR EnsemblBacteria; ABX14083; ABX14083; Bmul_0388. DR KEGG; bmu:Bmul_0388; -. DR PATRIC; 19173991; VBIBurMul17996_0521. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR Proteomes; UP000007064; Chromosome 1. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007064}; KW Methyltransferase {ECO:0000313|EMBL:ABX14083.1}; KW Signal {ECO:0000313|EMBL:ABX14083.1}; KW Transferase {ECO:0000313|EMBL:ABX14083.1}. FT SIGNAL 1 22 Potential. {ECO:0000313|EMBL:ABX14083.1}. FT CHAIN 23 367 Potential. {ECO:0000313|EMBL:ABX14083.1}. FT /FTId=PRO_5000285039. SQ SEQUENCE 367 AA; 39477 MW; AC17AAAF0542206A CRC64; MSVSRLRRSF AMSATPTAAS AAPLDASYTR GAELPALLKS RILILDGAMG TMIQRYKLDE AAYRGERFKD FPRDVKGNNE LLSITQPQVI REIHDQYFAA GADIVETNTF GATTVAQADY GMEDLVVEMN VESAKLARAS AAQYATPDKP RFVAGAIGPT PKTASISPDV NDPGARNVTF DELRDAYYMQ AKALLDGGVD LFLVETIFDT LNAKAALFAL DQLFEDTGER LPIMISGTVT DASGRILSGQ TVEAFWNSLR HAKPLTFGLN CALGAALMRP YIAELAKLCD TFVSCYPNAG LPNPMAETGF DETPDVTSGL LREFAQAGLV NLAGGCCGTT PEHIAEIAKA LADVKPRRWP SQYSEAA // ID A9B073_HERA2 Unreviewed; 1180 AA. AC A9B073; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 27-MAY-2015, entry version 63. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABX05182.1}; GN OrderedLocusNames=Haur_2544 {ECO:0000313|EMBL:ABX05182.1}; OS Herpetosiphon aurantiacus (strain ATCC 23779 / DSM 785). OC Bacteria; Chloroflexi; Chloroflexia; Herpetosiphonales; OC Herpetosiphonaceae; Herpetosiphon. OX NCBI_TaxID=316274 {ECO:0000313|EMBL:ABX05182.1, ECO:0000313|Proteomes:UP000000787}; RN [1] {ECO:0000313|Proteomes:UP000000787} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23779 / DSM 785 {ECO:0000313|Proteomes:UP000000787}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000875; ABX05182.1; -; Genomic_DNA. DR RefSeq; WP_012190084.1; NC_009972.1. DR RefSeq; YP_001545310.1; NC_009972.1. DR ProteinModelPortal; A9B073; -. DR STRING; 316274.Haur_2544; -. DR EnsemblBacteria; ABX05182; ABX05182; Haur_2544. DR KEGG; hau:Haur_2544; -. DR PATRIC; 22122169; VBIHerAur93466_2612. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; HAUR316274:GHYA-2572-MONOMER; -. DR Proteomes; UP000000787; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000787}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000787}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 235 235 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 301 301 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 302 302 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 750 750 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1180 AA; 129663 MW; 9150226864B9FC8E CRC64; MTSIKPYIAE LAKRVLIYDG AMGTSLDLYD LKPEDFGGEQ YFGARDYLAL TRPDIIEQIH SSFMEAGVDV LETNTFQSTR IRLHEWGLAD KTYEQNFKAA QLARKVADRY QAQDGRKRFV AGSMGPTGFL PSSDDPTLSN ITWDALSDTF KEQTIALVEG GVDVLLVETS VDILEVKAAI DGIRRGLAEL KRPDIAIQAQ VFLDLSGRML LGTDIQATMV TLEALADVDV IGLNCSTGPE HMRPAITYLA ANSKLPISCI PNAGLPMEVN GETVFPLEPA GFAKSLTEFV QDLGVRVVGG CCGTTPAHLR ALVDSIGNNC PPKPNQAPIV PQVSSAMRSL ALHQDPGPFI IGERVNSVGS RKVKKLLLKD DYDGVLQIAR EQADSGSHAL DVCVAMTERP DEKEQMQKLL KKLTMGVELP LVIDSTEYEV IDAALQIYPG RAIINSTSLE GGREQKFDKT MPLVARYGAA IIALTIDEEG MAHTAEAKVA IAKRMAEMGR QEYGVQNDAW LFDALTFPLT TGQAELRESA KETMEGIRRI KAEIPGAMTV LGVSNLSFGI QPHARSALNS VFLYHAVKAG LDAAIINPTH VMPFAEISAE TRKVCEDVIF NSDEEALPRF IQYFEANTAV AGEAKVDPTA TMNAEERIHW KILHRKKDGI EADIDESRAW REAGGQTQGE AAIDILNGVM LPAMKEVGDK FGAGELILPY VLQSAEVMKR AVAHLEQFLD RVEGTTKGKV VLATVYGDVH DIGKNLVYTI LSNNGYTVYD LGKQVPVNTI IEKALEVGAD AIGLSALLVS TSKQMPLCVQ ELHKRNLAFP VLVGGAAINR QYGQRILFPE PEVAYTGGVF YCKDAFEGLE TMDKLSDPTV REEYLSVMED AARESLKAPE RGRTLLEKLG KNNPSGVRST TRNDNPVPTP PFWGVQVAKK IRLDDVTPYL DLNTLWRLGW GIKNLKGAEY DRVVNDEFKP RLRRMIDDAK RNGWLQPQAV YGYFPAQAAG EELVVYDPKD RKTVLTRFAF PRQPSRERLC LADYFRPVES GEFDVVGLQI VTMGHVAAER VESLQKANDY SESFFSHGLS TTYAEALAEF TNKIISQGLG LSYQAKRYSW GYPACPDLEE HTKLFSVLPA KEIDVSLTSA FQLDPEQSTA AIVVHHPDAK YFSIGSVAER AESDVAELTS // ID A9B657_HERA2 Unreviewed; 617 AA. AC A9B657; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 27-MAY-2015, entry version 53. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=Haur_3632 {ECO:0000313|EMBL:ABX06268.1}; OS Herpetosiphon aurantiacus (strain ATCC 23779 / DSM 785). OC Bacteria; Chloroflexi; Chloroflexia; Herpetosiphonales; OC Herpetosiphonaceae; Herpetosiphon. OX NCBI_TaxID=316274 {ECO:0000313|EMBL:ABX06268.1, ECO:0000313|Proteomes:UP000000787}; RN [1] {ECO:0000313|Proteomes:UP000000787} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23779 / DSM 785 {ECO:0000313|Proteomes:UP000000787}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ABX06268.1; -; Genomic_DNA. DR RefSeq; WP_012191162.1; NC_009972.1. DR RefSeq; YP_001546396.1; NC_009972.1. DR ProteinModelPortal; A9B657; -. DR STRING; 316274.Haur_3632; -. DR EnsemblBacteria; ABX06268; ABX06268; Haur_3632. DR KEGG; hau:Haur_3632; -. DR PATRIC; 22124433; VBIHerAur93466_3735. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; HAUR316274:GHYA-3671-MONOMER; -. DR Proteomes; UP000000787; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000787}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ABX06268.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000000787}; KW Transferase {ECO:0000313|EMBL:ABX06268.1}. SQ SEQUENCE 617 AA; 66736 MW; CFB30D5318E52AFC CRC64; MANPFLEQLG QRALLCDGAM GTQLYGRGID FDECFDALNL TQPDVVREIH QSYIEAGADI IETNTYGANR FKLEPFGLAD KVRQINHRGM KLAREAREIA GTNTLIAGAV GPLGVLLQPY GPLTEQAAHE AFAEQIGTLL EQGADLLMFE TFSDLREMLI AVKAAKQVGD LPIVAQMTFA EDGRTVLGNT PEEVVRKLVE LGVAVVGVNC SVGSQRVFRV VQSMRAVNPT IPISAQPNAG WPTERHNRVF YPSSPEYMAD YARRMVEELN VQIVGGCCGT TPQHISNMHS ALQDLNPAST LNITIVDDEV PSVQLPSKSA ETTQLGRMLA DGAFVTSVEI DPPKGHNPRR CLEGARQMQA AGVNFINVAD SPMARVRMSA LPMCNLIQQQ VGMETILHFT TRDRSLMGLQ SDLLGAHALG VRNILALKGD PPSFGAYPGT SGVFDVDTIG LVKVIAGMNS GVDTAGNDIG TPTNFLIGVA LNINAEDPDW EIDRLHQKVA AGAHYAMTQI SYDATELDRF LDKLGPLPIP IILGLMPVQS YRHASFLHNE VPGITLPKDV LERMKEAGAN GRAVGVQVSQ EILAAAYDRI QGVYIMPSFG RYEMAAEVLE VLKAANA // ID A9BAF6_PROM4 Unreviewed; 1191 AA. AC A9BAF6; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 27-MAY-2015, entry version 61. DE SubName: Full=Putative methionine synthase {ECO:0000313|EMBL:ABX08818.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABX08818.1}; GN Name=metH {ECO:0000313|EMBL:ABX08818.1}; GN OrderedLocusNames=P9211_08871 {ECO:0000313|EMBL:ABX08818.1}; OS Prochlorococcus marinus (strain MIT 9211). OC Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae; OC Prochlorococcus. OX NCBI_TaxID=93059 {ECO:0000313|EMBL:ABX08818.1, ECO:0000313|Proteomes:UP000000788}; RN [1] {ECO:0000313|EMBL:ABX08818.1, ECO:0000313|Proteomes:UP000000788} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MIT 9211 {ECO:0000313|Proteomes:UP000000788}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000878; ABX08818.1; -; Genomic_DNA. DR RefSeq; WP_012195440.1; NC_009976.1. DR RefSeq; YP_001550772.1; NC_009976.1. DR ProteinModelPortal; A9BAF6; -. DR STRING; 93059.P9211_08871; -. DR EnsemblBacteria; ABX08818; ABX08818; P9211_08871. DR KEGG; pmj:P9211_08871; -. DR PATRIC; 22987334; VBIProMar136502_0945. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; ILESWIT; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PMAR93059:GHJV-912-MONOMER; -. DR Proteomes; UP000000788; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000788}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABX08818.1}; KW Transferase {ECO:0000313|EMBL:ABX08818.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 225 225 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 292 292 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 743 743 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1191 AA; 132032 MW; 70BF35D686176A61 CRC64; MDFINHLKKR NTILVFDGGM GTALQLQELS KEDFGGSQFE GCNEYLLISN PKSVEKVHRS YLEVGCDVIE TNTFGATSVV LAEYGLENKA YQLNLAASKM AKTLAKEYST INKPRYAAGS IGPTTKLPTL GHIDFDDLTN SYQEQVEALI TGGIDLVLVE TCQDVLQIKS ALLAISLAEK SLGIKIPVMV SITMETTGTM LIGTEISAAL TILEPFNIDI LGLNCATGPE EMKSHIQYLS SHSPFITSCI PNAGLPENIG GKAHYRLTPI ELKMQLMHFI KDLGVKVIGG CCGTTPEHIK GLTQLVEEIT NSNDQNLPSI KKIATQPSAS SIYEKISYQQ DNSFLIVGER LNASGSKKVR ELLNKDDWDG LVSLAKGQLK ENAHILDVNV DYVGRDGVAD MSRLVSKLVT NVNIPLMLDS TDYEKMESGL KKAGGKCILN STNFEDGPDR FFQVLQLCKS HGSSVVIGTI DEEGMARTAS KKLDITKRSY KEATCFGLKD SDIFFDPLVL PITTGIEDDR LNAKETILAI KNIKSLYPSV HLILGISNVS FGLNPAARVT LNSVFLNECI NSGLDSAIIS PSKILPLSKV SEDNLKICLD LIYDKRKYRD HICIYDPLTQ LTKAFEGVSA KSKSSSDDLS KLPIEKRLKS HIIEGEKEKL RENLLIALEG YKPLHIVNTF LLDGMKVVGE LFGSGQMQLP FVLQSAETMK YAVSILEPFM EKTSDSKSSK GKFIIATVKG DVHDIGKNLV DIILTNNGYE VFNLGIKQDV NSIIKAQEGI QADCIAMSGL LVKSTAFMKD NLQALNEANI QVPVILGGAA LTPRFVNTDC SQVYNGMVIY GKDAFTDLRF MDAYMEAKIN NRWDNKLGFL DGNPDNLSIP NPSASKNPDY INDNKTIKIT TNSLKTKGTL QANTSRSNTI LKEKPIVPPF KGNRILNSQQ LDLSQYSFYL DRNALFSGQW QFKKKKEQSR EDYEQDLIDT AEPILESWIT RIQEQNLISP SLVYGYFPCA RVGNSLKIYS LTSHQYLGTF TFPRQRSGNK LCISDYFNDL ENDRPIDYLP MQAVTMGEEA SMFAHKLYKE DKYTDYLFFH GLIVQLAEAL AEYSHSIIRT ECGFAGLEPK NIKDILAQRY RGCRYSFGYP ACPNVGDSRL QLKWLEGSRI GLSMDDSDQL HPEQSTTAII ALHSQAKYFS A // ID A9BIZ3_PETMO Unreviewed; 774 AA. AC A9BIZ3; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 27-MAY-2015, entry version 49. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABX32481.1}; GN OrderedLocusNames=Pmob_1792 {ECO:0000313|EMBL:ABX32481.1}; OS Petrotoga mobilis (strain DSM 10674 / SJ95). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Petrotoga. OX NCBI_TaxID=403833 {ECO:0000313|EMBL:ABX32481.1, ECO:0000313|Proteomes:UP000000789}; RN [1] {ECO:0000313|EMBL:ABX32481.1, ECO:0000313|Proteomes:UP000000789} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 10674 / SJ95 {ECO:0000313|Proteomes:UP000000789}; 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., Kuske C.R., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Noll K., Richardson P.; RT "Complete sequence of Petroga mobilis SJ95."; 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; CP000879; ABX32481.1; -; Genomic_DNA. DR RefSeq; WP_012209578.1; NC_010003.1. DR RefSeq; YP_001568804.1; NC_010003.1. DR ProteinModelPortal; A9BIZ3; -. DR STRING; 403833.Pmob_1792; -. DR EnsemblBacteria; ABX32481; ABX32481; Pmob_1792. DR KEGG; pmo:Pmob_1792; -. DR PATRIC; 22921414; VBIPetMob40494_1919. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PMOB403833:GH51-1839-MONOMER; -. DR Proteomes; UP000000789; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000789}; KW Methyltransferase {ECO:0000313|EMBL:ABX32481.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000789}; KW Transferase {ECO:0000313|EMBL:ABX32481.1}. SQ SEQUENCE 774 AA; 86432 MW; 0BFEACE338ED9E28 CRC64; MNRKEFAEIL NEKILILDGG YGTEFIKRGY KNIPAEILNI EYPEVVYNLQ SEYVKSGADI LLTNTFSGNR RKLKELNYEE AFEKVNVKAV EIAKQASKGK ALVFGDLSSL GEYPKPMGAL EMDEAIEEYY QQAKVLFESG VDGFIVETMT DIKELKAAVY GIRKVTEDLP LIAHMTFEEN GRSVTGTSVE IFANVFNDLD VDVLGINCTL GPEDLLKVFE RLSLSTNKFL SVEPNAGKPI FDGKNLEYKM TPEIFGMFVE DYLDLGVNII GGCCGTSPEH IKVIRNMVKR RPKKIVKEIP IMYSSRTILN KFHPFTVIGE RINPAGNKKF QNEIEEFNFD NVIKRANNQK NAKAHAIDVN LGIEKILNEE HFKKIIIELD KHSSLPISFD IQNIGFLESA LKEYPGRPII NSSKLSKKDL DRKLELIKKY GGLLIVLALE KEILESAEER LQLMLRKWPY IESKGISKDR IIVDPLVLSL AANNDPNITL ETVKLLSQNG FNTTMGLSNL SFGLPNRNYI NAAFLSRAKS KGLTSAILNP EDEFLMNTLN GNLLLDKNIV IPTKVEKQDE LTEKILQGEE GEVKRIIENQ LKEKSPLEVS QDVLGKAMEK IGDLYAQGNI YLPELLLAAE TVKPIFDYLN NLIPESQNDK KAKVVLATVE GDIHDIGKNI VAAVLRSANF KIIDLGKDVE TSIIIDAVQK EKPNILGLSA MMTTTVGKIE DVVNELKKLS LNVKVIAGGA SMNRKLAETF GCDAYAKDAS EGLKICKSWV NLNS // ID A9BPE8_DELAS Unreviewed; 368 AA. AC A9BPE8; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 27-MAY-2015, entry version 42. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABX32815.1}; GN OrderedLocusNames=Daci_0169 {ECO:0000313|EMBL:ABX32815.1}; OS Delftia acidovorans (strain DSM 14801 / SPH-1). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Delftia. OX NCBI_TaxID=398578 {ECO:0000313|EMBL:ABX32815.1, ECO:0000313|Proteomes:UP000000784}; RN [1] {ECO:0000313|Proteomes:UP000000784} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784}; 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; ABX32815.1; -; Genomic_DNA. DR RefSeq; WP_012202108.1; NC_010002.1. DR RefSeq; YP_001561200.1; NC_010002.1. DR ProteinModelPortal; A9BPE8; -. DR STRING; 398578.Daci_0169; -. DR PRIDE; A9BPE8; -. DR EnsemblBacteria; ABX32815; ABX32815; Daci_0169. DR KEGG; dac:Daci_0169; -. DR PATRIC; 21634135; VBIDelAci41351_0173. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; DACI398578:GHK3-169-MONOMER; -. DR Proteomes; UP000000784; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000784}; KW Methyltransferase {ECO:0000313|EMBL:ABX32815.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000784}; KW Transferase {ECO:0000313|EMBL:ABX32815.1}. SQ SEQUENCE 368 AA; 39415 MW; 6B2FF2D662C4111F CRC64; MPGTAAPEFL QSLPMSLPQY TRAKELPAIL AKRLVILDGA MGTMIQRFKL GEAQYRGQGY TGPGSVGDRF KDFPHDVKGN NELLSLTRPD VIRDIHDKYL AAGADLIETN TFGATTIAQD DYHMADLARE MNLKSAQLAR AACDKYSTPG HPRYVAGALG PTPKTASISP DVNDPGARNV NFEQLRQAYL EQTLALIEGG ADVILVETIF DTLNAKAALF AVDEAFEQSG ECLPIMISGT VTDASGRILS GQTVTAFWHS VRHANPLSIG LNCALGAALM RPYVQELNKA APETFISCYP NAGLPNPMSD TGFDETPEVT SRLVHEFASE GLVNIVGGCC GTTPDHIGAI AKAVGSTPTR RLFYPESA // ID A9CHY2_AGRT5 Unreviewed; 304 AA. AC A9CHY2; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 27-MAY-2015, entry version 36. DE SubName: Full=S-methyltransferase {ECO:0000313|EMBL:AAK88102.2}; GN OrderedLocusNames=Atu2362 {ECO:0000313|EMBL:AAK88102.2}; 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 {ECO:0000313|EMBL:AAK88102.2, ECO:0000313|Proteomes:UP000000813}; RN [1] {ECO:0000313|EMBL:AAK88102.2, ECO:0000313|Proteomes:UP000000813} 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] {ECO:0000313|EMBL:AAK88102.2, ECO:0000313|Proteomes:UP000000813} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C58 / ATCC 33970 {ECO:0000313|Proteomes:UP000000813}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE007869; AAK88102.2; -; Genomic_DNA. DR RefSeq; NP_355317.2; NC_003062.2. DR RefSeq; WP_010972258.1; NC_003062.2. DR ProteinModelPortal; A9CHY2; -. DR STRING; 176299.Atu2362; -. DR DNASU; 1134400; -. DR EnsemblBacteria; AAK88102; AAK88102; Atu2362. DR GeneID; 1134400; -. DR KEGG; atu:Atu2362; -. DR PATRIC; 20814511; VBIAgrTum91616_2374. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; PYVDVWL; -. DR OrthoDB; EOG6Q5NS7; -. DR Proteomes; UP000000813; Chromosome circular. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000813}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:AAK88102.2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000813}; KW Transferase {ECO:0000313|EMBL:AAK88102.2}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 304 AA; 31809 MW; E9612C6A6A72A42E CRC64; MGTIRILDGG MSRELQRLGA ELKQPEWSAL ALINAPDIVR QVHAEFIEAG ADVVTTNSYA LVPFHIGEER FQKDGASLIA LSGQLAREAA DASGRKVQVA GSLPPIFGSY EPQNFDATRV QDYLKVLVDN LAPSVDVWLG ETLSLIAEGE AVRQAVAATD KPFWISFTLN DDAAAVAGGE PALRSGETVK AAAEWAAQSG AAALLFNCSK PEIMKAAVET ASAVFADKGV SLEIGVYANA FEGEQGDSAA NEGLHGTRTD LTDDVYSRFA CSWADAGATM IGGCCGIGAA HIHTVATALR RAAA // ID A9CV91_9GAMM Unreviewed; 1256 AA. AC A9CV91; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 27-MAY-2015, entry version 38. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EDQ02814.1}; GN ORFNames=KT99_06597 {ECO:0000313|EMBL:EDQ02814.1}; OS Shewanella benthica KT99. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=314608 {ECO:0000313|EMBL:EDQ02814.1}; RN [1] {ECO:0000313|EMBL:EDQ02814.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=KT99 {ECO:0000313|EMBL:EDQ02814.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EDQ02814.1}. 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; ABIC01000001; EDQ02814.1; -; Genomic_DNA. DR RefSeq; WP_005495909.1; NZ_ABIC01000001.1. DR ProteinModelPortal; A9CV91; -. DR SMR; A9CV91; 676-914. DR EnsemblBacteria; EDQ02814; EDQ02814; KT99_06597. DR PATRIC; 28555016; VBISheBen91426_0163. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EDQ02814.1}; KW Transferase {ECO:0000313|EMBL:EDQ02814.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 261 261 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 325 325 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 782 782 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1256 AA; 139074 MW; 0507440B10F0E150 CRC64; MASDTLSTQR LTKEKGQQLT LKLTRQLEQG ILILDGAMGT MIQDLKLQEE DFRGEQFKHW HKDVKGNNDM LVLTQPAAIK GIHKQYLLAG ADIIETNTFN STRIAMADYD MQEFSAQINL EGARLARAAA DEVEKETGRS CYVAGVLGPT NRTCSISPDV NDPGYRNVTF DELVEAYVES INALIEGGAD IIMLETIFDT LNAKAALFAV ETVYDDLGAR LPIMISGTIT DASGRTLTGQ TTEAFYNSLR HVKPLSIGLN CALGPKELRP YVEELAKIAE CFVSAHPNAG LPNEFGGYDE TPKQMADIIG EWAQEGFLNI IGGCCGTTPE HIRVIREAVI KYPARPLPDI PVACRLAGLE PLTIDENSLF LNVGERTNVT GSAKFLRLIK GGEFEEALSV ARDQVENGAQ IIDINMDEGM LDGSEIMHKF LNLIASEPDI SRVPIMIDSS KWEVIEAGLK CIQGKGIVNS ISLKEGEEKF IQQATLVKRY GAAAIIMAFD EQGQADTKAR KIEICTRAYR VLVDKVGFPP EDIIFDPNIF AIATGIEEHD NYAVDFIEAT AEIKRTLPHA MISGGVSNVS FSFRGNNPVR EAIHAVFLYH AIQAGMDMGI VNAGQLAIYD DIDPELKQRV EAIVGNLPCT SVDKNGDVTN NTELLLEVAE KFRGDGSQTT KKADLEWRSW EVNKRLSHAL VKGITDYIIQ DTEEARAASS RPLDVIEGAL MDGMNVVGDL FGSGKMFLPQ VVKSARVMKK SVAYLNPYIE EEKTPGQSNG KILMVTVKGD VHDIGKNIVG VVLACNGYDV IDLGVMVPVE KIIDVAIAEN VDIIGMSGLI TPSLDEMVHN VKSFHKAGLT IPIIIGGATC SKIHTAVKIA PHSPTGAIYI ADASRAVPMV SKLINNQTRQ ATIDATYQEY DVMREKRLSQ TKRKIITTIE AARDNRCKYD WDKYTPFIPN QLGRQVFDDY PLEDLVERID WTPFFRSWEL HGRYPQILTD KVVGIEATKL FADGKAMLKQ IIDEKWLTAK GVIGLFPANS VNHDDIELYS CDGTIESREK PIMTLHHLRM QIERVGNDNF CLADFVAPKD SGVADYMGGF AVTTGHGIDE HIARFEADHD DYSAIMLKCL ADRLAEAFAE RMHERVRKEF WGYASDEVLD NEALIREKYK GIRPAPGYPA CPDHTEKGLL WDLLKPDETI GLNLTESYAM YPTAAVSGWY FAHPKSRYFG VTNIGKDQVE DYAQRKGMSI EETERWLSPV LDYDPE // ID A9DBB3_9RHIZ Unreviewed; 311 AA. AC A9DBB3; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 2. DT 04-MAR-2015, entry version 20. DE SubName: Full=Homocysteine/selenocysteine methylase (S-methylmethionine-dependent) {ECO:0000313|EMBL:EDQ32478.2}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EDQ32478.2}; GN ORFNames=HPDFL43_11781 {ECO:0000313|EMBL:EDQ32478.2}; OS Hoeflea phototrophica DFL-43. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Hoeflea. OX NCBI_TaxID=411684 {ECO:0000313|EMBL:EDQ32478.2, ECO:0000313|Proteomes:UP000004291}; RN [1] {ECO:0000313|EMBL:EDQ32478.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DFL-43 {ECO:0000313|EMBL:EDQ32478.2}; 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 (OCT-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EDQ32478.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DFL-43 {ECO:0000313|EMBL:EDQ32478.2}; RA Fiebig A.; 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. {ECO:0000313|EMBL:EDQ32478.2}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABIA03000004; EDQ32478.2; -; Genomic_DNA. DR EnsemblBacteria; EDQ32478; EDQ32478; HPDFL43_11781. DR PATRIC; 27534953; VBIHoePho121037_0165. DR Proteomes; UP000004291; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000004291}; KW Methyltransferase {ECO:0000313|EMBL:EDQ32478.2}; KW Reference proteome {ECO:0000313|Proteomes:UP000004291}; KW Transferase {ECO:0000313|EMBL:EDQ32478.2}. SQ SEQUENCE 311 AA; 32811 MW; BB031B301965D220 CRC64; MPPQAGTNRM PHTVRILDGG MSRELTRLGA RLVQPEWSAL ALIESPEIVR QVHVEFIDAG ADAITTNSYA LVPFHIGEER FASDGAALIE LSGRLAREAA DASKVRNIMV CGSLPPLFGS YEPENFDAAR APEYLSVLVG NLAPNVDVWL GETLSLIAEA EAVKTAVADT GKPLWVAFTL KDDVAALSQA PVLRSGETVA DAVAWAAQSG IEALLFNCSR PEIMEAAIAQ AAAVFEQKGV GIEIGVYANA FEQETASEKA NEGLSGMRAE LEGEGYIGFA RSWVAAGATL VGGCCGIGAS QIRRLAEDLK A // ID A9DBX6_9RHIZ Unreviewed; 336 AA. AC A9DBX6; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=Methionine synthase I (Cobalamin-dependent), methyltransferase domain protein {ECO:0000313|EMBL:EDQ32314.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EDQ32314.1}; GN ORFNames=HPDFL43_12633 {ECO:0000313|EMBL:EDQ32314.1}; OS Hoeflea phototrophica DFL-43. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Hoeflea. OX NCBI_TaxID=411684 {ECO:0000313|EMBL:EDQ32314.1, ECO:0000313|Proteomes:UP000004291}; RN [1] {ECO:0000313|EMBL:EDQ32314.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DFL-43 {ECO:0000313|EMBL:EDQ32314.1}; 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 (OCT-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EDQ32314.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DFL-43 {ECO:0000313|EMBL:EDQ32314.1}; RA Fiebig A.; 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. {ECO:0000313|EMBL:EDQ32314.1}. 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; ABIA03000004; EDQ32314.1; -; Genomic_DNA. DR ProteinModelPortal; A9DBX6; -. DR EnsemblBacteria; EDQ32314; EDQ32314; HPDFL43_12633. DR PATRIC; 27535281; VBIHoePho121037_0328. DR Proteomes; UP000004291; Chromosome. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000004291}; KW Methyltransferase {ECO:0000313|EMBL:EDQ32314.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000004291}; KW Transferase {ECO:0000313|EMBL:EDQ32314.1}. SQ SEQUENCE 336 AA; 35514 MW; 5442AEA8D9014132 CRC64; MSVSNPLADL LAEKGVLLAD GATGTNLFAM GLESGDAPEL WNESAQHKIT KLHQDFVDAG SDIILTNSFG GTRNRLKLHH AQDRVHELNK KAGEIARAVA DKAPRKVIVA GSVGPTGDLL VPLGALTYDE AISSFVEQIE GLKAGGVDVI WIETMSAVDE IRAAAEAATR IGMPYTYTGS FDTAGKTMMG LHPRDIHGVT KDLEQGPFAV GANCGVGASD ILSSLLDMTT ADPEAIVIVK GNCGIPEFRG TEIHYSGTPP LMADYARLAM DSGAKIIGGC CGTSCEHLAA MRQAIDSHSK ASRPTVEEIV ERIGPMRNTV ATDNAAPKRE RRGRRG // ID A9DJE7_9FLAO Unreviewed; 333 AA. AC A9DJE7; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=Methionine synthase I, homocysteine S-methyltransferase {ECO:0000313|EMBL:EDP98086.1}; GN ORFNames=KAOT1_12752 {ECO:0000313|EMBL:EDP98086.1}; OS Kordia algicida OT-1. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Kordia. OX NCBI_TaxID=391587 {ECO:0000313|EMBL:EDP98086.1}; RN [1] {ECO:0000313|EMBL:EDP98086.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=OT-1 {ECO:0000313|EMBL:EDP98086.1}; RA Kim S.-J., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EDP98086.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=OT-1 {ECO:0000313|EMBL:EDP98086.1}; RX PubMed=21622754; DOI=10.1128/JB.05241-11; RA Lee H.S., Kang S.G., Kwon K.K., Lee J.H., Kim S.J.; RT "Genome sequence of the algicidal bacterium Kordia algicida OT-1."; RL J. Bacteriol. 193:4031-4032(2011). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDP98086.1}. 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; ABIB01000001; EDP98086.1; -; Genomic_DNA. DR RefSeq; WP_007095099.1; NZ_DS544873.1. DR ProteinModelPortal; A9DJE7; -. DR EnsemblBacteria; EDP98086; EDP98086; KAOT1_12752. DR PATRIC; 30131039; VBIKorAlg103762_2151. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EDP98086.1}; KW Transferase {ECO:0000313|EMBL:EDP98086.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 243 243 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 333 AA; 36319 MW; F94F9D4E088449BF CRC64; MKNIWNEIEK RILVLDGAMG TMLQAYKFTE ADFRGERFKD FQVPLQGNND LLSITQPHAI KEVHAKYFAA GADIVETNTF SGTTIAMADY EMEDLVYELN YESAKIAKEV ADEFTEKEPH KPRFVAGSIG PTNKTASMSP DVNDPGYRAV TFDELRIAYK QQVEALIDGG VDILLVETVF DTLNAKAALF AIEEVKAERK IEIPTMLSGT ITDASGRTLS GQTAEAFLIS VSHIPLLSVG FNCALGANLL QPHLEAIANK TDFAVSAHPN AGLPNAFGEY DETPEEMAVQ IEEYLKKNLI NIIGGCCGTT PDHISAIAAV AAKYKPRNVV VNA // ID A9E595_9RHOB Unreviewed; 337 AA. AC A9E595; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=Methionine synthase I {ECO:0000313|EMBL:EDQ04716.1}; GN ORFNames=OIHEL45_13485 {ECO:0000313|EMBL:EDQ04716.1}; OS Oceanibulbus indolifex HEL-45. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Oceanibulbus. OX NCBI_TaxID=391624 {ECO:0000313|EMBL:EDQ04716.1}; RN [1] {ECO:0000313|EMBL:EDQ04716.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HEL-45 {ECO:0000313|EMBL:EDQ04716.1}; 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. {ECO:0000313|EMBL:EDQ04716.1}. 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; ABID01000003; EDQ04716.1; -; Genomic_DNA. DR RefSeq; WP_007119712.1; NZ_ABID01000003.1. DR ProteinModelPortal; A9E595; -. DR EnsemblBacteria; EDQ04716; EDQ04716; OIHEL45_13485. DR PATRIC; 25528440; VBIOceInd27211_2267. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 337 AA; 35539 MW; F558D72212F2B6DB CRC64; MSNAFTDLLA EKGTLLADGA TGTNLFNMGL MSGDAPEMWN TDEPKKITKL YRFAVDSGSD LFLTNSFGAN ASRLKLHGAE KRVHELSRVA AELAREVADT AERKVIVAGS VGPTGEIMEP VGTLSHSLAV EMFHETADGL KAGGADIGWL ETISAPEEYR AAAEGFALAD LPWCGTMSFD TAGRTMMGLT SEGMVDMVHG LDNTPLAYGA NCGTGASDLL RTVLGFAAKN GTLPIISKGN AGIPKYVEGH IHYDGTPELM ARYATMARDA GASIIGGCCG TLPEHLVAMR DALDSTEKGP APTLEQIREE IGEFSSESDG TDGQGPVRAP RRGRRRG // ID A9FAG8_SORC5 Unreviewed; 1281 AA. AC A9FAG8; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 27-MAY-2015, entry version 57. DE SubName: Full=MetH2 protein {ECO:0000313|EMBL:CAN97902.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAN97902.1}; GN Name=metH2 {ECO:0000313|EMBL:CAN97902.1}; GN OrderedLocusNames=sce7733 {ECO:0000313|EMBL:CAN97902.1}; 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 {ECO:0000313|EMBL:CAN97902.1, ECO:0000313|Proteomes:UP000002139}; RN [1] {ECO:0000313|EMBL:CAN97902.1, ECO:0000313|Proteomes:UP000002139} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=So ce56 {ECO:0000313|Proteomes:UP000002139}; 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., 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., Ruckert 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., Wilhelm S., Wittmann C., Blocker H., Puhler A., RA Muler R.; RT "Complete genome sequence of the myxobacterium Sorangium cellulosum."; RL Nat. Biotechnol. 25:1281-1289(2007). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AM746676; CAN97902.1; -; Genomic_DNA. DR RefSeq; WP_012240341.1; NC_010162.1. DR RefSeq; YP_001618382.1; NC_010162.1. DR ProteinModelPortal; A9FAG8; -. DR SMR; A9FAG8; 698-1279. DR STRING; 448385.sce7733; -. DR EnsemblBacteria; CAN97902; CAN97902; sce7733. DR KEGG; scl:sce7733; -. DR PATRIC; 23674493; VBISorCel80414_8438. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SCEL448385:GJ75-8015-MONOMER; -. DR Proteomes; UP000002139; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002139}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAN97902.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002139}; KW Transferase {ECO:0000313|EMBL:CAN97902.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 275 275 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 340 340 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 341 341 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 813 813 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1281 AA; 140508 MW; 7ECD49F305C2AFFD CRC64; MPSNNTTPPL HPLQKLLQRR IVIIDGAMGT TIRTYGMKEA DIRGQRFADS KKDLLNNGDL FSLTQPEMIC DIHRRFLEAG ADIIETNTFG ATSITQSEFF VDDPREHGGR KDPAFYQGII DDPFLNDLAW EINEQSARQC REWADRVANA DGRQRFVAGA IGPLTVSLSN SPDADDPGFR VVTFDQVKQA YVHQIRALIA GGSDVLLVET IFDSLNAKAA LVAIREVFDK DGKTLPVMIS AAVGRGGETM ISAQTVEAFW NAVKHVNPLA IGLNCSLGPD LMYPFLSDLS EKSSAAISCY PNAGLPNPLS PTGFDLEPPD MARHIGGFAD AGLLNIAGGC CGNTPEHIAA IAKALAGKPP RALEPRTPAE APPGGAVSSG SGAPIPLRLS GSQPFTQQPG VYMILGERTN VAGSPKFAKL IKEGKFEEAV GVARQQVENG ANVIDICMDE GMIDGVSAMT RFLLLLASEP EVAKVPFMVD SSKWEVIEAG LRCMQGKGIV NSISLKEGEA KFRENARTIL KYGAAVVVMA FDEQGQAATY EDKIRICKRA YGILVDEVGF PPEDIIFDPN ILTVATGMEE HNNYAVDFIE ATRWIKANLP HAKVSGGVSN ISFSFRGNNR VREAMHSAFL YHAIRAGMDM GIVNAGMLEV YEEIEPELRE LVEDVLLNRR PDATERLVDF GEALKARSAG AAEAEKKEEE WRKGTVEERL SHALVKGIDT YIDIDTEEAR AKLGRPLSVI EGPLMDGMSV VGDLFGAGKM FLPQVVKSAR VMKKAVAYLT PFMEAEKAAM AAAGQEVKTQ GKIVLATVKG DVHDIGKNIV GVVLACNNYE VIDMGVMVPC EKILERARQE KADLIGLSGL ITPSLDEMIH VAREMERQNF KLPLLIGGAT TSKAHTAVKV APHYSEPVVH VVDASRAVPV TTSLLSEEGK AAFVAQHRAE YEKLRRLHAA PKHKLVSLEA ARANRTRIAW RAEDLPVPEF TGARVLEDFP LAALREYIDW TPFFHTWELK GVYPRILEHE KYGEQARQLF SEANALLDTI IEKKLLTARG VYGFFPASAV GDDVEVYTDG TRAKVLERFH FLRQQTAKEG GEPNRSLADF IAPRETGLRD HIAGFAVTSG IGLKELCERF RAVHDDYNAI MAEAIADRLA EAFAECLHKR VRDEWGYGRQ EDLTKAELIE EKYRGIRPAA GYPACPDHTE KGTLWRLLDV EKSTGIQITE SFAMWPGSSV SGLYFAHPEA RYFSLGKIDR DQVVDYHARK GMTVAEVERW LGPNLNYDAS N // ID A9FZY9_SORC5 Unreviewed; 624 AA. AC A9FZY9; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 27-MAY-2015, entry version 54. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=sce8634 {ECO:0000313|EMBL:CAN98804.1}; 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 {ECO:0000313|EMBL:CAN98804.1, ECO:0000313|Proteomes:UP000002139}; RN [1] {ECO:0000313|EMBL:CAN98804.1, ECO:0000313|Proteomes:UP000002139} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=So ce56 {ECO:0000313|Proteomes:UP000002139}; 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., 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., Ruckert 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., Wilhelm S., Wittmann C., Blocker H., Puhler A., RA Muler R.; RT "Complete genome sequence of the myxobacterium Sorangium cellulosum."; RL Nat. Biotechnol. 25:1281-1289(2007). CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {ECO:0000256|RuleBase:RU004255}. CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; CAN98804.1; -; Genomic_DNA. DR RefSeq; WP_012241243.1; NC_010162.1. DR RefSeq; YP_001619284.1; NC_010162.1. DR ProteinModelPortal; A9FZY9; -. DR STRING; 448385.sce8634; -. DR EnsemblBacteria; CAN98804; CAN98804; sce8634. DR KEGG; scl:sce8634; -. DR PATRIC; 23676461; VBISorCel80414_9419. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; SCEL448385:GJ75-8947-MONOMER; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000002139; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004255}; KW Complete proteome {ECO:0000313|Proteomes:UP000002139}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:CAN98804.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000002139}; KW Transferase {ECO:0000313|EMBL:CAN98804.1}. SQ SEQUENCE 624 AA; 66617 MW; 464908DB2A673573 CRC64; MRTMSRTRPE APFLDALRRS ILVFDGAMGS LLYERGVFVT QNFEQLNVAR PDLVKKIHAE YVAAGANVIE TNTFGANRFR LERYGLVNEV RNFNLAGARL AREIAGGDAY VAGSIGPTGL VPGVATRDDL AAASATFAEQ AGALAEGGAD LLILETFRHL DEIKLAIDAA RSAAPGLPVL ASMTFDTSGV AADGSEPERV ARTLRDWGVE LLGVNCGDGP QLSLAMAERM ATAGLPLCVQ PNAGLPRTVD GRQLYMATPE YFDVFARRMI QAGAAMIGGC CGTTPEHVRW MAKSARMLRG GAAPEAAARP HVTMDAPTGL EPTPLGERSP LAAKIAAGKF VVSVEVNPAP GLNPESALSA AKMLIDSGVD VVNVADGPRA TARMTNLAFC SLLVQRYGIE PILHVCGRDR NLIGQMAHLL GAHAIGIKNL VIITGDPPKV GDYPEATAVY DLDSIGLLHM ASTMNRGLDP AGKPIPGGKT SFLLATGLEP GAQDLDKEIA RLERKRAAGA DIIMTQPVFH QDLLEKVLRR IEHLGMPVLV GVLPLVSHKN AEFLHNEVPG MQIPEEIRER MRKVPAGPEA RKEGVKIARE MLFSVRDRVQ GAYLMPPLGK YELALEVLDG LKTG // ID A9G8T0_SORC5 Unreviewed; 1259 AA. AC A9G8T0; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 27-MAY-2015, entry version 57. DE SubName: Full=MetH1 protein {ECO:0000313|EMBL:CAN96034.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAN96034.1}; GN Name=metH1 {ECO:0000313|EMBL:CAN96034.1}; GN OrderedLocusNames=sce5871 {ECO:0000313|EMBL:CAN96034.1}; 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 {ECO:0000313|EMBL:CAN96034.1, ECO:0000313|Proteomes:UP000002139}; RN [1] {ECO:0000313|EMBL:CAN96034.1, ECO:0000313|Proteomes:UP000002139} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=So ce56 {ECO:0000313|Proteomes:UP000002139}; 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., 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., Ruckert 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., Wilhelm S., Wittmann C., Blocker H., Puhler A., RA Muler R.; RT "Complete genome sequence of the myxobacterium Sorangium cellulosum."; RL Nat. Biotechnol. 25:1281-1289(2007). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AM746676; CAN96034.1; -; Genomic_DNA. DR RefSeq; WP_012238499.1; NC_010162.1. DR RefSeq; YP_001616514.1; NC_010162.1. DR ProteinModelPortal; A9G8T0; -. DR SMR; A9G8T0; 658-897. DR STRING; 448385.sce5871; -. DR EnsemblBacteria; CAN96034; CAN96034; sce5871. DR KEGG; scl:sce5871; -. DR PATRIC; 23670461; VBISorCel80414_6419. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; TWTFPRQ; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SCEL448385:GJ75-6084-MONOMER; -. DR Proteomes; UP000002139; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002139}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAN96034.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002139}; KW Transferase {ECO:0000313|EMBL:CAN96034.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 253 253 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 316 316 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 765 765 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1259 AA; 138039 MW; 8B474F06ECE378DB CRC64; MSRAMNGSER PARIEELLER RILCLDGAMG TMIQRYRLGE ADYRGERFRD HAIDLKGNSD LLVLTRPDVI SEIHGAYLDA GADIIETNTF TGTSIAQADY RLESLAYEIN LTAAQIARKA ADAWTARTPG KPRFVAGAMG PTPKTLSISP SVSDPSFRAV GFDELRRAFA EQVRGLVDGG VDVILAETFL DTLNMKACLV AMEEVFAERG RRLPILLSVT ITDRSGRTLS GQTIDAFWTS VEHASPLSVG LNCALGASDM RPYLVDLAKL ARARVSCYPN AGLPNAFGEY DELPETTSRL LAEFAESGLV NIVGGCCGTT PDHIRAIVRA TADLRPRPVP VERDGFGRFA GLETLVIRPE TNFLMIGERT NVTGSARFME LIKKGDFTTA LEVALDQVRG GANLLDVNMD EGMLDSEQAM TTFLNLVATE PEIARIPIMV DSSRWSVIEA GLKCIQGKGI VNSISLKEGP EDFLEKARAV RRYGAGVVVM AFDEIGQAES VERKVAICQR AYRLLTEEAG FDPQDIVFDP NILAIATGIE EHCDFAKNFI EATRIIKATC PGARVSGGVS NLSFSFRGNN VVREAMHSAF LFHAIRAGMD MGIVNAGQLA VYEDIPKDLL ERVEDVLFNR RPDATERLVE LAEQVKGKGK KKELDLAWRD GPVEERLSHA LVKGLVDFIE ADVEEARRKY DKPLSIIEGP LMDGMKTVGE LFGAGKMFLP QVVKSARVMK RAVAHLLPFM EAEKAAGGSS SQGKIVMATV KGDVHDIGKN IVGVVLGCNN YEVIDLGVMV HQDRILEAAL REEADMIGLS GLITPSLDEM VSVAREMERR GIRLPLLIGG ATTSRQHTAV KIAPEFSGTV VHVLDASRAV GVVSSLLDRA NRPAFDAQNR EEQARLRELF ARKRAKPLVT LAAADGGRLE IAWRPEDIAR PSFTGRRVVE VPLSEIARYI DWTFFFTAWE LRGPFPQILE HPQYGEAARE LFDHAQKVLQ RIIEGRLLEA RGVYGFWPAS GEQRDIVLYA DEARERELVR FNMLRQQQVK GRGGAEEDGD GGDKAAGGVR PHLSLADFVA PRERGLADHV GAFAVTAGLG LDEIVRAYEK DKDDYSAIIA KALADRLAEA FAELLHERAR KDWGYGAGEA LTSEELIEEK YRGIRPAFGY PACPDHTEKR KLFALLDAPS VGIELTESCA MTPAASVSGI YLAHPKARYF MVGRLGRDQV ADYAKRKGMT VEEVERWLSP NLGYDPKAAV EEESAVVAA // ID A9GBM7_SORC5 Unreviewed; 271 AA. AC A9GBM7; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 27-MAY-2015, entry version 33. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CAN96065.1}; GN OrderedLocusNames=sce5901 {ECO:0000313|EMBL:CAN96065.1}; 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 {ECO:0000313|EMBL:CAN96065.1, ECO:0000313|Proteomes:UP000002139}; RN [1] {ECO:0000313|EMBL:CAN96065.1, ECO:0000313|Proteomes:UP000002139} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=So ce56 {ECO:0000313|Proteomes:UP000002139}; 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., 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., Ruckert 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., Wilhelm S., Wittmann C., Blocker H., Puhler A., RA Muler 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; CAN96065.1; -; Genomic_DNA. DR RefSeq; WP_012238530.1; NC_010162.1. DR RefSeq; YP_001616545.1; NC_010162.1. DR ProteinModelPortal; A9GBM7; -. DR STRING; 448385.sce5901; -. DR EnsemblBacteria; CAN96065; CAN96065; sce5901. DR KEGG; scl:sce5901; -. DR PATRIC; 23670541; VBISorCel80414_6460. DR eggNOG; proNOG00526; -. DR BioCyc; SCEL448385:GJ75-6116-MONOMER; -. DR Proteomes; UP000002139; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002139}; KW Reference proteome {ECO:0000313|Proteomes:UP000002139}. SQ SEQUENCE 271 AA; 27510 MW; AFF206EE1E97C9B5 CRC64; MLRESPRAIA ELHEQEIALG IDVVRALTSA TTTRALAPIG MAFRAAALTG TAVELATEAA GGAARRVAVA GILGHTAAAP MADRIAEDYA VHAARLAAAG CEILVACGFD PAQAACVGPT VARLARRAAV VSASTTQLAT WALVELDGAG RTADGEGFEE VARSALDSGA DALLFEVPSV ELGLNVLRRL EGVAHEVQVG VLLGAESAQA DGADRIAPAE ICDAWAASAA RLIEAGARML GGGTGTTLAH LGALAKMLRT TQRAPLLRRA L // ID A9GUQ7_SORC5 Unreviewed; 309 AA. AC A9GUQ7; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 27-MAY-2015, entry version 39. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CAN90654.1}; GN OrderedLocusNames=sce0497 {ECO:0000313|EMBL:CAN90654.1}; 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 {ECO:0000313|EMBL:CAN90654.1, ECO:0000313|Proteomes:UP000002139}; RN [1] {ECO:0000313|EMBL:CAN90654.1, ECO:0000313|Proteomes:UP000002139} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=So ce56 {ECO:0000313|Proteomes:UP000002139}; 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., 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., Ruckert 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., Wilhelm S., Wittmann C., Blocker H., Puhler A., RA Muler R.; RT "Complete genome sequence of the myxobacterium Sorangium cellulosum."; RL Nat. Biotechnol. 25:1281-1289(2007). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; CAN90654.1; -; Genomic_DNA. DR RefSeq; WP_012233132.1; NC_010162.1. DR RefSeq; YP_001611134.1; NC_010162.1. DR ProteinModelPortal; A9GUQ7; -. DR STRING; 448385.sce0497; -. DR EnsemblBacteria; CAN90654; CAN90654; sce0497. DR KEGG; scl:sce0497; -. DR PATRIC; 23658617; VBISorCel80414_0538. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; QPEVMAA; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; SCEL448385:GJ75-525-MONOMER; -. DR Proteomes; UP000002139; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002139}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000002139}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 213 213 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 280 280 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 281 281 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 309 AA; 31733 MW; 6073FD6698556B4D CRC64; MEDVARSPLG SAAVSAEAAI VVLDGPLGTE LAARGVETPA PLWSAAALLD ARGRDVVRAI HRDYARAGAT VHTANTFRTR RRQAGAAWAE LASRAVSLAR EAVRGEGPRH RVAGSIAPLE DCYRPDLSPA DARQEHRELA RALASAGVDL LLCETFPHVG EALVALEEAV ATGVEAWVSF TAGPGSDLLS PEDVGRAARE AAARGASAVL VNCTPATRTL AHIERLAACG VPFGAYANAG AEAEGLGWGV GVDQRGSAAA RYAELARRWL EAGATIVGGC CGTGPGHIAA LRALVDGARP AREPAGSPR // ID A9H4J4_GLUDA Unreviewed; 1168 AA. AC A9H4J4; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 27-MAY-2015, entry version 65. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CAP57445.1}; DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACI52612.1}; GN Name=metH {ECO:0000313|EMBL:CAP57445.1}; GN OrderedLocusNames=GDI3502 {ECO:0000313|EMBL:CAP57445.1}, GN Gdia_2881 {ECO:0000313|EMBL:ACI52612.1}; OS Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / OS PAl5). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Gluconacetobacter. OX NCBI_TaxID=272568 {ECO:0000313|EMBL:CAP57445.1, ECO:0000313|Proteomes:UP000001176}; RN [1] {ECO:0000313|EMBL:ACI52612.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PAl 5 {ECO:0000313|EMBL:ACI52612.1}; 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., 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] {ECO:0000313|EMBL:CAP57445.1, ECO:0000313|Proteomes:UP000001176} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49037 / DSM 5601 / PAl5 RC {ECO:0000313|Proteomes:UP000001176}, and RC PAl 5 {ECO:0000313|EMBL:CAP57445.1}; RX PubMed=19775431; DOI=10.1186/1471-2164-10-450; RA Bertalan M., Albano R., 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., Filho G., Flores V., Ferreira B., Branco A., Gonzalez P., RA Guillobel H., Lemos M., Seibel L., Macedo J., Alves-Ferreira M., RA Sachetto-Martins G., Coelho A., Santos E., Amaral G., Neves A., RA Pacheco A.B., Carvalho D., Lery L., Bisch P., Rossle S.C., Urmenyi T., RA Kruger W.V., 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] {ECO:0000313|EMBL:ACI52612.1, ECO:0000313|Proteomes:UP000000736} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49037 / DSM 5601 / PAl5 RC {ECO:0000313|Proteomes:UP000000736}, and RC PAl 5 {ECO:0000313|EMBL:ACI52612.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001189; ACI52612.1; -; Genomic_DNA. DR EMBL; AM889285; CAP57445.1; -; Genomic_DNA. DR RefSeq; WP_012228136.1; NC_011365.1. DR RefSeq; YP_001603731.1; NC_010125.1. DR RefSeq; YP_002277227.1; NC_011365.1. DR ProteinModelPortal; A9H4J4; -. DR STRING; 272568.GDI_3502; -. DR EnsemblBacteria; ACI52612; ACI52612; Gdia_2881. DR EnsemblBacteria; CAP57445; CAP57445; GDI3502. DR KEGG; gdi:GDI_3502; -. DR KEGG; gdj:Gdia_2881; -. DR PATRIC; 22054158; VBIGluDia203729_2854. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; GDIA272568:GJPS-3562-MONOMER; -. DR Proteomes; UP000000736; Chromosome. DR Proteomes; UP000001176; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001176}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001176}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 225 225 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 292 292 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 737 737 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1168 AA; 128386 MW; B030033C84FA2341 CRC64; MTARPHLLDA LRDQVLLCDG GMGSRVQVLD LDVERDYWGQ ENCTEILNLS RPELVREIHR GYFEAGADMV ETNSFGGTPI TLGEFGLADR AREINRTAAH LAREAAESFA DGRHRYVIGS VGPGTKLPSL GNIDYDTLEA GLAEQCRGLI DGGVDALLIE TCQDTLQIKA AVNGAKIARA ELGTDTPIFV QVTVETTGTL LVGPDIAAAA TAIHALDVPL MGLNCATGPQ EMAEHVRWLA GNWPGLISIQ PNAGLPELVD GQTHYPLSPA DMATWVDRFI TEDGLNLVGG CCGTSTPHIA ALDAMLRRRA EGTGRHRPAP VPRRPVWIPS VSSLYTQVPL RQENSYFSIG ERCNANGSKK WRTLQEEGDW DGCVSIGREQ VAEGSNALDL CTAFVGRDEM REMNEVVTRF TSSVNAPLVI DSTETPVIEA ALKLYGGKAI INSINFEDGE GHATDRMLLA RKFGAAVVAL TIDEVGMAKT AEDKLRIATR LVEFACDRHG LPQSDLMIDP LTFTIGTGVE DDRKLGLWTL EGIRQIRDRF PDIQIVLGLS NISFGLNPAA RAVLNSVFLD HAVRAGMTAA IVHVSKIRPL HLIPEEEVKV AEDLIFDRRE EGYDPLQRLL ELFADRKASD AVKKTRSDRV DERLKERIVD GDRKGLEADL DEAMRTIPPL DIINTILLDG MKVVGELFGA GKMQLPFVLQ SAETMKAAVA HLEPHMERAE GQTRGTIVLA TVKGDVHDIG KNLVDIILTN NGYRVVNLGI KVPVADMIAA TREHAADAVG MSGLLVKSTV VMRENLEEMA RQGLDVPVLL GGAALTRNYV EEDCTAAYGT DGRVAYARDA FDGLSLMDQV AQGEFDNYLA ATRARRAGKA TRARPRDMEQ ADTRGFAPVD VAAARARRAR LTQDEPAVEP PFWGARVIEA APDAVLPFLN ERSLYQFQWG FRKQGRSLDD FMGWARQELR PVLRRMLALA AEQDILRPQA AYGYWKAAGQ GNDLILFEAD GTTEAARFTL PRQPREDGEC IADFVRDVDD ARRDVIGLQV VTVGQKASDM AREWFEANRY KDYLYLHGLS VEMAEAMAEY THKRIRAELG FAAEDDRDMN KLLQQGYRGS RYSFGYPACP RLEDQDPILK LLDAERIGVS LTDGYQLHPE QSTSALVVLN PKAKYFSV // ID A9I155_BORPD Unreviewed; 1257 AA. AC A9I155; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 29-APR-2015, entry version 55. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CAP40826.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAP40826.1}; GN Name=metH {ECO:0000313|EMBL:CAP40826.1}; GN OrderedLocusNames=Bpet0494 {ECO:0000313|EMBL:CAP40826.1}; OS Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=340100 {ECO:0000313|Proteomes:UP000001225}; RN [1] {ECO:0000313|EMBL:CAP40826.1, ECO:0000313|Proteomes:UP000001225} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448 RC {ECO:0000313|Proteomes:UP000001225}; RX PubMed=18826580; DOI=10.1186/1471-2164-9-449; RA Gross R., Guzman C.A., Sebaihia M., Martins Dos Santos V.A., 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., Vorhoelter 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AM902716; CAP40826.1; -; Genomic_DNA. DR RefSeq; WP_012247517.1; NC_010170.1. DR RefSeq; YP_001629097.1; NC_010170.1. DR ProteinModelPortal; A9I155; -. DR SMR; A9I155; 673-928. DR STRING; 340100.Bpet0494; -. DR EnsemblBacteria; CAP40826; CAP40826; Bpet0494. DR KEGG; bpt:Bpet0494; -. DR PATRIC; 21162437; VBIBorPet31633_0498. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; BPET340100:GJBO-497-MONOMER; -. DR Proteomes; UP000001225; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001225}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAP40826.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001225}; KW Transferase {ECO:0000313|EMBL:CAP40826.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 256 256 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 789 789 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1257 AA; 138080 MW; 699E4C61F52F405F CRC64; MPYPRLPYPP SSYTRGGDFA RLLGQRILIL DGAMGTMIQR YKLSEADFRG ERFADHGKDL KGDNELLSLV RPDIIDEIHR QYLEAGADVI ETNTFGATSV AQGDYDLPGL AYELNLASAR LARAACDAYS TPERPRFAAG ALGPQPKTAS ISPDVNDPGA RNITFDELCE AYTEQLNGLL DGGIDIVLIE TIFDTLNAKA AIFAVESVFE ARGERLPVMI SGTVTDASGR ILSGQTVEAF WNSVRHARPI TIGLNCALGA ALMRPYVAEL SKICDTYVCV YPNAGLPNPM AETGFDEAPA DTSGLLEEFA RAGLVNMSGG CCGTTPDHIR AIADKVASLT PRAVPEIPVK TRLSGLEPLN IDEESLFVNV GERTNVTGSK MFARLIREEK YDEALAVARQ QVENGAQIID INMDEAMLDS VACMRRFLNL IASEPDIARV PIMIDSSKWE VIEAGLKCVQ GKAVVNSISM KEGEEAFRHH ARLCRRYGAA VVVMAFDEQG QADTLERRKE ICARAYKILT EQEQFPPEDI IFDPNVFAVA TGIDEHNHYA MDFIEGVRWI RQNLPHARLS GGISNVSFSF RGNEPMREAI HTVFLYYAIR EGLTMGIVNA GQLGVYADLE PRLRDLVEDV ILDRAEPVGK EGAADERTPT ERLVQFADSV KGSGAKKEED LAWRAGTVEE RLSHALVHGI TTFIVEDTEE VRQKIAARGG RPIEVIEGPL MDGMNIVGDL FGAGKMFLPQ VVKSARVMKQ AVAHLIPFIE EEKRQIAAAG GDVRAKGKMV IATVKGDVHD IGKNIVSVVL QCNNFEVVNM GVMVPCAQIL EKAKEEQADI VGLSGLITPS LEEMAYVASE MQRDPYFRER KIPLMIGGAT TSRVHTAVKI APNYDGPVIY TPDASRAVGV AANLVSEQAQ AYIDEVAQEY ADVRRRHANR KATPLVSLAE ARAARPQIDW SAYVPPRPKF IGRRSFKSYD LAEIARYLDW TPFFQTWSLF GQFPAILEDK VVGEQAQKVY ADGQAMLKRI IEGRWLTANG AVAFYPANTV NDEDIEVYAD ESRSEVLFTY RNLRQQGVKR EGVSNKCLAD FIAPKSSGVA DYIGMFAVTA GLGIEKKEAE FQAALDDYSG IMLKAMADRL AEAFAECLHA RVRQDLWGYA ADEALSNDEM IAEKYVGIRP APGYPACPEH VVKRDLFRVL DGDDIGMLLT DSYAMYPASS VSGFYFSHPQ SQYFNVGTIG ADQLADYIAR SGRSEEDVRR TLASSLG // ID A9KSG0_CLOPH Unreviewed; 841 AA. AC A9KSG0; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 27-MAY-2015, entry version 50. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABX43612.1}; GN OrderedLocusNames=Cphy_3258 {ECO:0000313|EMBL:ABX43612.1}; OS Clostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg) OS (Lachnoclostridium phytofermentans). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=357809 {ECO:0000313|EMBL:ABX43612.1, ECO:0000313|Proteomes:UP000000370}; RN [1] {ECO:0000313|Proteomes:UP000000370} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700394 / DSM 18823 / ISDg RC {ECO:0000313|Proteomes:UP000000370}; RA Leschine S.B., Warnick T.A., Blanchard J.L., Schnell D.J., Petit E.L., RA LaTouf W.G., Copeland A., Lucas S., Lapidus A., Barry K., RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., RA Brettin T., Bruce D., Detter J.C., Han C., Kuske C., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E.A., Richardson P.; RT "Complete genome sequence of Clostridium phytofermentans ISDg."; 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; CP000885; ABX43612.1; -; Genomic_DNA. DR RefSeq; WP_012201262.1; NC_010001.1. DR RefSeq; YP_001560351.1; NC_010001.1. DR ProteinModelPortal; A9KSG0; -. DR STRING; 357809.Cphy_3258; -. DR EnsemblBacteria; ABX43612; ABX43612; Cphy_3258. DR KEGG; cpy:Cphy_3258; -. DR PATRIC; 19506364; VBICloPhy16213_3405. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CPHY357809:GHCL-3315-MONOMER; -. DR Proteomes; UP000000370; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000370}; KW Methyltransferase {ECO:0000313|EMBL:ABX43612.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000370}; KW Transferase {ECO:0000313|EMBL:ABX43612.1}. SQ SEQUENCE 841 AA; 92349 MW; 16013E18FBADCF93 CRC64; MTKNEFKAMI EQKIVILDGA TGSNLQNAGM PSGVCPETWI LDNKEVLITL QKEYLYAGTD ILYAPTFTSN RIKLSEYGLE HRIEEINHSL VELSKEAINR YLEETGETRS IMIAGDLTMT GEQLLPFGKM DFEELITIYK EQIGHLVSSG VDLLVVETML SLQECRAAVI AAKEICELPV MVSLTFGEDN RTLYGTDPKT AMIVLQSLGA DAVGVNCSSG PKKLSEVIEQ MLPVANVPLI AKPNAGLPKL VEDRTVFTMD ADEFAASCKI FLELGVSILG GCCGTTPKHI NLLNELAKTY QAPVIHKKPL RVLTTERRSM EFSLVDRFLV VGERINPTGK KVLQAQLREG VLDLVSEMAI EQEELGADIL DINMGMNGID EKEMMLKVMD EVLQVTNLPL SIDSSHVSVI EAALRRYPGR ALINSISLEK EKFEKLLPVA KKYGAMFILL PLSDAGLPKD LEEKKQIIHT IVSAAKEIGL TAEDIVVDGL VNTVGANKEA AIQTMETIRY CKEELSLATI VGLSNISFGL PERQFVNATF LSFAIQAGLT MAIANPSQDL LMNTAYAADL LRNKEGADLR YIERVTTHPM INAESTPKKV IERGEDKADN KKSVREASNV NANESLNDNS TEKSSSQIYE AVIKGNKRKI LALVIEEVNN KTSAAEILDT ILIPAINQVG QYFDSGKYYL PQLIASAETM KTAIDYLEPM LKKDSKEEKV GTIIIATVAG DIHDIGKNLV ALMLKNYGFN VIDLGKDVSS EKIIETAKEL DADIIALSAL MTTTMLEMKR VVNYRNEASL RAKVIIGGAV ITQDYCDEIG ADGYSKDAQE AVNLVKKLLK I // ID A9KYD4_SHEB9 Unreviewed; 300 AA. AC A9KYD4; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 27-MAY-2015, entry version 41. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABX50405.1}; GN OrderedLocusNames=Sbal195_3243 {ECO:0000313|EMBL:ABX50405.1}; OS Shewanella baltica (strain OS195). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=399599 {ECO:0000313|EMBL:ABX50405.1, ECO:0000313|Proteomes:UP000000770}; RN [1] {ECO:0000313|EMBL:ABX50405.1, ECO:0000313|Proteomes:UP000000770} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OS195 {ECO:0000313|EMBL:ABX50405.1, RC ECO:0000313|Proteomes:UP000000770}; 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; ABX50405.1; -; Genomic_DNA. DR RefSeq; WP_012197425.1; NC_009997.1. DR ProteinModelPortal; A9KYD4; -. DR STRING; 399599.Sbal195_3243; -. DR EnsemblBacteria; ABX50405; ABX50405; Sbal195_3243. DR GeneID; 11773293; -. DR KEGG; sbn:Sbal195_3243; -. DR PATRIC; 23472801; VBISheBal33754_3353. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; PYVDVWL; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; SBAL399599:GH6B-3348-MONOMER; -. DR Proteomes; UP000000770; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000770}; KW Methyltransferase {ECO:0000313|EMBL:ABX50405.1}; KW Transferase {ECO:0000313|EMBL:ABX50405.1}. SQ SEQUENCE 300 AA; 32117 MW; BD9F75F98A38E225 CRC64; MDKQQLWVLD GGMGRELARR GAPFRQPEWS ALALIEAPQT VTEVHQAYVA SGAKVITTNS YALVPFHIGD ERFAAEGEVL AALAGKLARD VVDEHANAVR VAGSLPPLFG SYRADLFDAA RVSELALPLI RALSPSIDLW LAETMSLIAE PLAIKALLPE DGKPFWVSFT LEDETLGSEP TLRSGERVAD AIDALVAVGV DAILFNCCQP EVIEAALQVA SDRLSALGRA DIRLGAYANA FPPQPKEATA NDGLDEIRAD LGPLDYLGWA ERWRAVGASL IGGCCGIGPE HIQALSTRLR // ID A9L3D4_SHEB9 Unreviewed; 1244 AA. AC A9L3D4; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 27-MAY-2015, entry version 57. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABX48183.1}; GN OrderedLocusNames=Sbal195_1007 {ECO:0000313|EMBL:ABX48183.1}; OS Shewanella baltica (strain OS195). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=399599 {ECO:0000313|EMBL:ABX48183.1, ECO:0000313|Proteomes:UP000000770}; RN [1] {ECO:0000313|EMBL:ABX48183.1, ECO:0000313|Proteomes:UP000000770} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OS195 {ECO:0000313|EMBL:ABX48183.1, RC ECO:0000313|Proteomes:UP000000770}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000891; ABX48183.1; -; Genomic_DNA. DR RefSeq; WP_006085885.1; NC_009997.1. DR ProteinModelPortal; A9L3D4; -. DR SMR; A9L3D4; 668-1244. DR STRING; 399599.Sbal195_1007; -. DR EnsemblBacteria; ABX48183; ABX48183; Sbal195_1007. DR GeneID; 11771300; -. DR KEGG; sbn:Sbal195_1007; -. DR PATRIC; 23468046; VBISheBal33754_1047. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SBAL399599:GH6B-1036-MONOMER; -. DR Proteomes; UP000000770; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000770}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 258 258 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 774 774 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1244 AA; 137996 MW; 92B587BE99122EEE CRC64; MTIPSTKAGQ ILADIRKQLA ERILILDGAM GTMIQDHKLE EEDYRGERFK DWHTDVKGNN DLLVLSQPHI IKQIHTDYLN AGADIIETNT FNATTIAMAD YDMQSLSAEI NLAGARLARE ACDEVFAATG IPRYVAGVLG PTNRTCSISP DVNDPGYRNV SFDELVSAYR ESTKALIEGG ADIIMVETIF DTLNAKAALF AIESVFDDLF GQHSKDRLPI MISGTITDAS GRTLTGQTTE AFYNSLRHIK PLSIGLNCAL GPKELRPYVE ELSRISECYV SAHPNAGLPN EFGGYDETPE DMANVIEDWA REGMLNIIGG CCGSTPEHIR VIREAVDRHN PRVLPDIPVA CRLAGLEPLT IDAQSLFVNV GERTNVTGSA KFLKLIKDGK FEQALDVARE QVESGAQIID INMDEGMLDG AEIMHKFLNL IASEPDISRV PIMIDSSKWE VIEAGLKCIQ GKGIVNSISL KEGEAKFIEQ ATLVKRYGAA AIIMAFDEQG QADTKARKIE ICTRAYRVLV DKVGFPPEDI IFDPNIFAIA TGIDEHDNYA VDFIDAIKAI KATLPHAMIS GGVSNVSFSF RGNNPVREAI HAVFLYHAIK VGMDMGIVNA GQLAIYDDID PELKVRVENV VLNLPCPVEG SSNTEQLLEI AEKFRGDGAQ VGKKEDLEWR SWPVSQRLSH ALVKGITEFI DEDTEAARQE AKRPLDVIEG ALMDGMNVVG DLFGSGKMFL PQVVKSARVM KKAVAYLNPY IELEKVEGQS NGKILMVTVK GDVHDIGKNI VGVVLACNGF EVFDLGVMVS VERILDAVKE HNIDIIGMSG LITPSLDEMV HNVKTFHREG LTIPAIIGGA TCSKIHTAVK IAPHYPHGAI YIADASRAVP MVSKLINNET RQATIDETYA EYDDMRTKRL SQAKRKEIVS LEAARDNRCQ HDWANYTPFT PNVLGRQVFD NYPLEDLVER IDWTPFFRSW ELHGHYPEIL TDKVVGVEAQ KLFADGQAML KQIIEEKWLT AKAVIGLFPA NTVNYDDIEL YTDESRTTVE MTTHHLRMQL ERVGNDNFCL SDFVAPKDSG VADYMGGFAV TTGHGIDEHV ARFEANHDDY NAIMLKCLAD RLAEAFAERM HERVRKEFWG YAADEQLSNE ALIREKYKGI RPAPGYPACP DHTEKGLLWD LLKPDETIDL NITESYAMFP TAAVSGWYFA HPKSRYFGVS NIGRDQVEDY AKRKGMSIAE TEKWLAPVLD YDPE // ID A9LYL9_HELTB Unreviewed; 134 AA. AC A9LYL9; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 29-OCT-2014, entry version 16. DE SubName: Full=Putative betaine homocysteine methyltransferase {ECO:0000313|EMBL:ABX45056.1}; DE Flags: Fragment; OS Heliocidaris tuberculata (Sea urchin). OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; OC Echinoidea; Euechinoidea; Echinacea; Echinoida; Echinometridae; OC Heliocidaris. OX NCBI_TaxID=7635 {ECO:0000313|EMBL:ABX45056.1}; RN [1] {ECO:0000313|EMBL:ABX45056.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=18184359; DOI=10.1111/j.1525-142X.2007.00215.x; RA Love A.C., Lee A.E., Andrews M.E., Raff R.A.; RT "Co-option and dissociation in larval origins and evolution: the sea RT urchin larval gut."; RL Evol. Dev. 10:74-88(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; EU282134; ABX45056.1; -; mRNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 2: Evidence at transcript level; KW Methyltransferase {ECO:0000313|EMBL:ABX45056.1}; KW Transferase {ECO:0000313|EMBL:ABX45056.1}. FT NON_TER 1 1 {ECO:0000313|EMBL:ABX45056.1}. SQ SEQUENCE 134 AA; 15610 MW; 1FD1E9A50DC15E81 CRC64; RHEIMTRWEC HRYARESYDM GIRYIGGCCG FEPYHIRAVC EELNKERGFF PAGTEKHALW GDGLRQHTKP WVRARARRDY WENLKPASGR PDCPSMSKPD AWGETRGDAN LVQHVEATDD VELKKLYQQS AVKT // ID A9LYM0_HELER Unreviewed; 128 AA. AC A9LYM0; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 29-OCT-2014, entry version 16. DE SubName: Full=Putative betaine homocysteine methyltransferase {ECO:0000313|EMBL:ABX45057.1}; DE Flags: Fragment; OS Heliocidaris erythrogramma (Sea urchin). OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; OC Echinoidea; Euechinoidea; Echinacea; Echinoida; Echinometridae; OC Heliocidaris. OX NCBI_TaxID=7634 {ECO:0000313|EMBL:ABX45057.1}; RN [1] {ECO:0000313|EMBL:ABX45057.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=18184359; DOI=10.1111/j.1525-142X.2007.00215.x; RA Love A.C., Lee A.E., Andrews M.E., Raff R.A.; RT "Co-option and dissociation in larval origins and evolution: the sea RT urchin larval gut."; RL Evol. Dev. 10:74-88(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; EU282135; ABX45057.1; -; mRNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 2: Evidence at transcript level; KW Methyltransferase {ECO:0000313|EMBL:ABX45057.1}; KW Transferase {ECO:0000313|EMBL:ABX45057.1}. FT NON_TER 1 1 {ECO:0000313|EMBL:ABX45057.1}. FT NON_TER 128 128 {ECO:0000313|EMBL:ABX45057.1}. SQ SEQUENCE 128 AA; 14825 MW; B748D24AAFFA5A33 CRC64; RWECHRYARE AYDMGIRYIG GCCGFEPYHI RAVCEELNKE RGFFPAGTEK HALWGDGLRQ HTKPWVRARA RRDYWENLKP ASGRPECPSM SKPDAWGETR GDANLVQHSE ATDDSELKQL YQHSAVKT // ID A9M7D3_BRUC2 Unreviewed; 1261 AA. AC A9M7D3; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 27-MAY-2015, entry version 54. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABX61292.1}; GN Name=metH {ECO:0000313|EMBL:ABX61292.1}; GN OrderedLocusNames=BCAN_A0193 {ECO:0000313|EMBL:ABX61292.1}; OS Brucella canis (strain ATCC 23365 / NCTC 10854). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=483179 {ECO:0000313|EMBL:ABX61292.1, ECO:0000313|Proteomes:UP000001385}; RN [1] {ECO:0000313|EMBL:ABX61292.1, ECO:0000313|Proteomes:UP000001385} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23365 / NCTC 10854 {ECO:0000313|Proteomes:UP000001385}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000872; ABX61292.1; -; Genomic_DNA. DR RefSeq; WP_004691381.1; NC_010103.1. DR RefSeq; YP_001592063.1; NC_010103.1. DR ProteinModelPortal; A9M7D3; -. DR SMR; A9M7D3; 673-921. DR STRING; 483179.BCAN_A0193; -. DR EnsemblBacteria; ABX61292; ABX61292; BCAN_A0193. DR KEGG; bcs:BCAN_A0193; -. DR PATRIC; 17829040; VBIBruCan25663_0198. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; BCAN483179:GJ7I-192-MONOMER; -. DR PRO; PR:A9M7D3; -. DR Proteomes; UP000001385; Chromosome I. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001385}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 263 263 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 326 326 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 327 327 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 783 783 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1261 AA; 138712 MW; 86A5B2805EE934BF CRC64; MASSLDDLFG ATAAKPDGSE VLAALTQAAR ERILILDGAM GTQIQGLSFH EEHFRGDRFA TCDCQLQGNN DLLTLTQPKA IEEIHYAYAM AGADILETNT FSSTSIAQAD YGMEAMVYDL NRDGARLARR AALRAEQKDG RRRFVAGALG PTNRTASLSP DVNNPGFRAV TFDDLRIAYS EQIRGLIDGG SDIILIETIF DTLNAKAAVF ATEEVFAEKG VRLPVMISGT ITDLSGRTLS GQTPTAFWYS LRHARPFTIG LNCALGANAM RAHLDELSGI ADTFICAYPN AGLPNEFGQY DETPEAMAAQ IEGFARDGLV NVVGGCCGST PDHIRAIAQA VAKYEPRKPA KVPPLMRLSG LEPFTLTKDI PFVNIGERTN VTGSARFRKL VKAGDFAAAL DVARDQVANG AQIIDINMDE GLIDSEKAMV EFLNLIAAEP DIARVPIMLD SSKWEVIEAG LKCVQGKAVV NSISLKEGEE AFLHHARLVR AYGAAVVIMA FDETGQADTQ ARKIEICTRA YKILTEQVGF PPEDIIFDPN IFAVATGIEE HNNYGVDFIE ATREIVRTLP HVHISGGVSN LSFSFRGNEP VREAMHAVFL YHAIQAGMDM GIVNAGQLAV YDTIDAELRE ACEDVVLNRP TKTGESATER LLEIAERFRD SGSREARTQD LSWREWPVEK RLEHALVNGI TEYIEADTEE ARLAAERPLH VIEGPLMAGM NVVGDLFGSG KMFLPQVVKS ARVMKQAVAV LLPFMEEEKR LNGGEGRQSA GKVLMATVKG DVHDIGKNIV GVVLACNNYE IIDLGVMVPS QKILQVARDE KVDIIGLSGL ITPSLDEMAH VAAEMEREGF DIPLLIGGAT TSRVHTAVKI HSRYERGQAV YVVDASRAVG VVSNLLSPEG KQAYIDGLRN EYAKVAAAHA RNEAEKQRLP IARARANPHQ LDWENYEPVK PAFTGTKVFE TYDLAEIARY IDWTPFFQTW ELRGRYPAIL EDEKQGEAAR QLWADAQAML RKIIDEKWFT PRAVVGFWPA NAVGDDIRLF TDESRKEELA TLFTLRQQLT KRDGRPNVAM ADFVAPVESG KQDYVGGFVV TAGIGEIAIT ERFERANDDY SAILVKALAD RFAEAFAELM HERVRKEFWA YAPDEAFTPE ELISEPYKGI RPAPGYPAQP DHTEKTTLFR LLDATANTGV ELTESYAMWP GSSVSGLYIG HPESYYFGVA KVERDQVEDY ARRKDMDVEA VERWLTPILN YVPGASKDEA A // ID A9MHB4_SALAR Unreviewed; 1294 AA. AC A9MHB4; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 01-APR-2015, entry version 54. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ABX23297.1}; GN OrderedLocusNames=SARI_03468 {ECO:0000313|EMBL:ABX23297.1}; OS Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=41514 {ECO:0000313|EMBL:ABX23297.1, ECO:0000313|Proteomes:UP000002084}; RN [1] {ECO:0000313|EMBL:ABX23297.1, ECO:0000313|Proteomes:UP000002084} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980 RC {ECO:0000313|Proteomes:UP000002084}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000880; ABX23297.1; -; Genomic_DNA. DR ProteinModelPortal; A9MHB4; -. DR SMR; A9MHB4; 718-1294. DR STRING; 41514.SARI_03468; -. DR EnsemblBacteria; ABX23297; ABX23297; SARI_03468. DR PATRIC; 18475921; VBISalEnt13497_3300. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SENT882884:GJ8H-3464-MONOMER; -. DR Proteomes; UP000002084; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002084}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 377 377 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 378 378 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 826 826 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1294 AA; 143039 MW; A11DA387FC9FA719 CRC64; MALRLSAYVL GAGRVICRLD KALAPPSGEV TDAGSKLNMS HVARCSLFRQ HALCQYDSLR GALSGASVSS KVEQLRAQLN ERILVLDGGM GTMIQSYRLH EEDFRGERFA DWPCDLKGNN DLLVLSKPEV IAAIHNAYFE AGADIIETNT FNSTTIAMAD YQMESLSAEI NYAAAKLARA CADEWSARTP EKPRYVAGVL GPTNRTASIS PDVNDPAFRN ITFDQLVAAY RESTKALVEG GADLILIETV FDTLNAKAAV FAVKAELEAL GVDLPIMISG TITDASGRTL SGQTTEAFYN SLRHAGALTF GLNCALGPDE LRQYVQELSR IAECYVTAHP NAGLPNAFGE YDLDADTMAK HIREWAQAGF LNIVGGCCGT TPEHIAAMSR AVEDLPPRKL PDIPVACRLS GLEPLNIGDD SLFVNVGERT NVTGSAKFKR LIKEEKYSEA LDVARQQVES GAQIIDINMD EGMLDAEAAM VRFLSLIAGE PDIARVPIMI DSSKWEVIEK GLKCIQGKGI VNSISMKEGV ETFIHHAKLL RRYGAAVVVM AFDEQGQADT RERKIEICRR AYNILTKEVG FPPEDIIFDP NIFAVATGID EHNNYAQDFI GACEDIKREL PHALISGGVS NVSFSFRGND PVREAIHAVF LYYAIRNGMD MGIVNAGQLA IYDDLPAELR DAVEDVILNR REDGTERLLE LAEKYRGSKT DEAANAQQAE WRSWDVKKRL EYSLVKGITE FIEQDTEEAR QQAARPIEVI EGPLMDGMNV VGDLFGEGKM FLPQVVKSAR VMKQAVAYLE PFIEASKEKG SSNGKMVIAT VKGDVHDIGK NIVGVVLQCN NYDIVDLGVM VPAEKILKTA KEVNADLIGL SGLITPSLDE MVNVAKEMER QGFTIPLLIG GATTSKAHTA VKIEQNYSGP TVYVQNASRT VGVVAALLSD TQRDDFVART RKEYETVRIQ HARKKPRTPP VTLEAARDND LAFDWERYTP PVAHRLGVQE VEASIETLRN YIDWTPFFMT WSLAGKYPRI LEDEVVGEEA KRLFKDANDM LDKLSAEKLL NPRGVVGLFP ANRVGDDIEI YRDETRTHVL TVSHHLRQQT EKVGFANYCL ADFVAPKLSG KADYIGAFAV TAGLEEDALA DVYEAQHDDY NKIMVKAIAD RLAEAFAEYL HERVRKVYWG YAPNESLSNE ELIRENYQGI RPAPGYPACP EHTEKGTIWQ LLDVEKHTGM KLTESFAMWP GASVSGWYFS HPDSKYFAVA QIQRDQVTDY AFRKGMSVED VERWLAPNLG YDAD // ID A9N1H8_SALPB Unreviewed; 1301 AA. AC A9N1H8; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 27-MAY-2015, entry version 56. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ABX70459.1}; GN OrderedLocusNames=SPAB_05182 {ECO:0000313|EMBL:ABX70459.1}; OS Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=1016998 {ECO:0000313|EMBL:ABX70459.1, ECO:0000313|Proteomes:UP000008556}; RN [1] {ECO:0000313|EMBL:ABX70459.1, ECO:0000313|Proteomes:UP000008556} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1250 / SPB7 {ECO:0000313|Proteomes:UP000008556}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000886; ABX70459.1; -; Genomic_DNA. DR RefSeq; WP_012219461.1; NC_010102.1. DR ProteinModelPortal; A9N1H8; -. DR SMR; A9N1H8; 725-1301. DR STRING; 272994.SPAB_05182; -. DR EnsemblBacteria; ABX70459; ABX70459; SPAB_05182. DR PATRIC; 18536779; VBISalEnt120821_4190. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SENT28901:GH9O-5171-MONOMER; -. DR Proteomes; UP000008556; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008556}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 384 384 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 385 385 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 833 833 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1301 AA; 143934 MW; 0D1F2AE21FA48B0B CRC64; MTSQDARWRC AYQAYALGAA KVICRLDKAL ASPSGKATEV GGKLNMSHVA RCSLFRQHAL CQYGSLRGAL SGASVSSKVE QLRAQLNERI LVLDGGMGTM IQSYRLHEED FRGERFADWP CDLKGNNDLL VLSKPEVIAA IHNAYFEAGA DIIETNTFNS TTIAMADYRM ESLSAEINYA AAKLARACAD EWTVRTPNKP RYVAGVLGPT NRTASISPDV NDPAFRNITF DQLVAAYRES TKALVEGGAD LILIETVFDT LNAKAAVFAV KEEFEALGVD LPIMISGTIT DASGRTLSGQ TTEAFYNSLR HAEALTFGLN CALGPDELRQ YVQELSRIAE CYVTAHPNAG LPNAFGEYDL DADTMAKQIR EWAEAGFLNI VGGCCGTTPE HIAAMSRAVA GLPPRQLPDI PVACRLSGLE PLNIGDDSLF VNVGERTNVT GSAKFKRLIK EEKYSEALDV ARQQVESGAQ IIDINMDEGM LDAEAAMVRF LSLIAGEPDI ARVPIMIDSS KWEVIEKGLK CIQGKGIVNS ISMKEGVEAF IHHAKLLRRY GAAVVVMAFD EQGQADTRER KIEICRRAYK ILTEEVGFPP EDIIFDPNIF AVATGIEEHN NYAQDFIGAC EDIKRELPHA LISGGVSNVS FSFRGNDPVR EAIHAVFLYY AIRNGMDMGI VNAGQLAIYD DLPAELRDAV EDVILNRRDD GTERLLELAE KYRGSKTDEA ANAQQAEWRS WDVKKRLEYS LVKGITEFIE QDTEEARQQA ARPIEVIEGP LMDGMNVVGD LFGEGKMFLP QVVKSARVMK QAVAYLEPFI EASKEKGSSN GKMVIATVKG DVHDIGKNIV GVVLQCNNYE IVDLGVMVPA EKILRTAREV NADLIGLSGL ITPSLDEMVN VAKEMERQGF TIPLLIGGAT TSKAHTAVKI EQNYSGPTVY VQNASRTVGV VAALLSDNQR DDFVARTRKE YETVRIQHAR KKPRTPPVTL EAARDNDLAF DWERYTPPVA NRLGVQEVEA SIETLRNYID WTPFFMTWSL AGKYPRILED EVVGVEAQRL FKDANDMLDK LSAEKLLNPR GVVGLFPANR VGDDIEIYRD ETRTHVLTVS HHLRQQTEKV GFANYCLADF VAPRLSGKAD YIGAFAVTGG LEEDALADAY EAQHDDYNKI MVKAIADRLA EAFAEYLHER VRKVYWGYAP NESLSNDELI RENYQGIRPA PGYPACPEHT EKGTIWQLLD VEKHTGMKLT ESFAMWPGAS VSGWYFSHPE SKYFAVAQIQ RDQVTDYAFR KGMSVEDVER WLAPNLGYDA D // ID A9QPD6_METI4 Unreviewed; 617 AA. AC A9QPD6; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 27-MAY-2015, entry version 54. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN Name=metF {ECO:0000313|EMBL:ABX56594.1}; GN OrderedLocusNames=Minf_1622 {ECO:0000313|EMBL:ACD83676.1}; OS Methylacidiphilum infernorum (isolate V4) (Methylokorus infernorum OS (strain V4)). OC Bacteria; Verrucomicrobia; unclassified Verrucomicrobia; OC Methylacidiphilales; Methylacidiphilaceae; Methylacidiphilum. OX NCBI_TaxID=481448 {ECO:0000313|EMBL:ABX56594.1, ECO:0000313|Proteomes:UP000009149}; RN [1] {ECO:0000313|EMBL:ABX56594.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=V4 {ECO:0000313|EMBL:ABX56594.1}; RX PubMed=18004300; DOI=10.1038/nature06411; RA Dunfield P.F., Yuryev A., Senin P., Smirnova A.V., Stott M.B., Hou S., RA Ly B., Saw J.H., Zhou Z., Ren Y., Wang J., Mountain B.W., Crowe M.A., RA Weatherby T.M., Bodelier P.L.E., Liesack W., Feng L., Wang L., RA Alam M.; RT "Methane oxidation by an extremely acidophilic bacterium of the phylum RT Verrucomicrobia."; RL Nature 450:879-882(2007). RN [2] {ECO:0000313|EMBL:ACD83676.1, ECO:0000313|Proteomes:UP000009149} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Isolate V4 {ECO:0000313|Proteomes:UP000009149}, and RC V4 {ECO:0000313|EMBL:ACD83676.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EU223852; ABX56594.1; -; Genomic_DNA. DR EMBL; CP000975; ACD83676.1; -; Genomic_DNA. DR RefSeq; WP_012463958.1; NC_010794.1. DR ProteinModelPortal; A9QPD6; -. DR STRING; 481448.Minf_1622; -. DR EnsemblBacteria; ACD83676; ACD83676; Minf_1622. DR KEGG; min:Minf_1622; -. DR PATRIC; 22492413; VBIMetInf111569_1684. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; MINF481448:GJEI-1656-MONOMER; -. DR Proteomes; UP000009149; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009149}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000009149}. SQ SEQUENCE 617 AA; 67934 MW; 54FA072D3B7C9D53 CRC64; MPWEKRMATL IDRLNESLLI GDGALGTYLY SLGVPRNYCI EELSLSQPYL IEKVHKDYIE AGAKIIRANT AEANAYHLSF FKLEKKLKEI VSSSIGLAKK ALGFKEGWIA GTINPIWVRP ADPPIDLSTR RTLYEEQISL LLEEGCDLLF FETFTDLSDL LLGLELARNK GAQFLFAFVA SFEEGKLSSG QSLKEAFSKL REAGALLVGI NGASGVQASL HLLEEIEKKE TDLLGAYPNA GKPEFYEGKL TYSASPSYFG QNVLKFVEEG LNLLGGDYGT EPVHVAAMAQ AAVGVKPIKR KLAKIRLRYE VGEKETLPQV EPSLLDRLNI KPVFMVEYDS PKTLSMGKFL EGVKAIEKAG ADALTLADNS LAILRVSNFA AAIHVRRVSK LIPVLHVACR DRNLLGLQSE LMGLGTLGFR HILALTGDPA KSGDHPGATS VYDLNSVGLI RLLAGLNRGV NAAGKDLKGK TDFIIGCAFN PNTVQFDAQV RKLEAKLAAG ARFVMTQPVF DFELIKKIFN YLKPLGVPVF VGIMPILNYR NAEFLHNEVP GISIPEKIRS RMKDLEGEKA TEAGVEFARE LGEEILSHFR AIYLITPFLR YDISVRLLES LQSKKTA // ID A9RGI7_PHYPA Unreviewed; 341 AA. AC A9RGI7; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 07-JAN-2015, entry version 34. DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EDQ81842.1}; GN ORFNames=PHYPADRAFT_65820 {ECO:0000313|EMBL:EDQ81842.1}; OS Physcomitrella patens subsp. patens (Moss). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta; OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; OC Physcomitrella. OX NCBI_TaxID=3218 {ECO:0000313|Proteomes:UP000006727}; RN [1] {ECO:0000313|EMBL:EDQ81842.1, ECO:0000313|Proteomes:UP000006727} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Gransden 2004 {ECO:0000313|Proteomes:UP000006727}; 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; DS544897; EDQ81842.1; -; Genomic_DNA. DR RefSeq; XP_001753213.1; XM_001753161.1. DR UniGene; Ppa.13157; -. DR STRING; 3218.JGI65820; -. DR GeneID; 5916486; -. DR KEGG; ppp:PHYPADRAFT_65820; -. DR InParanoid; A9RGI7; -. DR KO; K00547; -. DR Proteomes; UP000006727; Partially assembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006727}; KW Reference proteome {ECO:0000313|Proteomes:UP000006727}. SQ SEQUENCE 341 AA; 37468 MW; 709DD2CCCC536A4F CRC64; MGHTLNLHHD TFQEPERSET ITELLKQAGG CVVTDGGFAT QLERHGADIN DPLWSALCLI TMPHLIRTVH KEYLQAGASV ISTASYQATI QGFQSRGLST KEAEDLLQTS VRIAQEERDS FWKEYQNKVR AGTAHAGLYQ RALAAASVGS YGAGDYGPSM TVDKLKDFHR RRLMVLADAG PDLIALETIP CKLETQALVE LLAEENLRVP AWISFNSKDG TNVVSGDSLS DCVALADKCT QVRAVGINCT PPRFILDLIQ AVRKVTNKLI VVYPNSGEYY DPEIKQWVES TGVSDTDFVS YVHEWRNAGA QLIGGCCRTT PNTIEAISKA LREHTHAHVT N // ID A9RI39_PHYPA Unreviewed; 350 AA. AC A9RI39; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EDQ81492.1}; GN ORFNames=PHYPADRAFT_159171 {ECO:0000313|EMBL:EDQ81492.1}; OS Physcomitrella patens subsp. patens (Moss). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta; OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; OC Physcomitrella. OX NCBI_TaxID=3218 {ECO:0000313|Proteomes:UP000006727}; RN [1] {ECO:0000313|EMBL:EDQ81492.1, ECO:0000313|Proteomes:UP000006727} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Gransden 2004 {ECO:0000313|Proteomes:UP000006727}; 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; DS544899; EDQ81492.1; -; Genomic_DNA. DR RefSeq; XP_001753740.1; XM_001753688.1. DR UniGene; Ppa.9423; -. DR ProteinModelPortal; A9RI39; -. DR STRING; 3218.JGI159171; -. DR GeneID; 5917018; -. DR KEGG; ppp:PHYPADRAFT_159171; -. DR InParanoid; A9RI39; -. DR KO; K00547; -. DR OMA; SSVEGFM; -. DR Proteomes; UP000006727; Partially assembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006727}; KW Reference proteome {ECO:0000313|Proteomes:UP000006727}. SQ SEQUENCE 350 AA; 38557 MW; 54D6A7CE756D3896 CRC64; MGRTIDVPED TLQESETSNV VLELLKQAGG CVVTDGGFAT QLERHGANIN DPLWSAVCLI TMPDLIRKVH REYLEAGAAV ISTASYQATI QGFEMRGLST KDSEDLLQLS VRIAREERDR FWKEYQNKVH TGPGQAGSYH HALVAASIGS YGAYLADGSE YSGDYGSFVT VEKLKNFHRR RLLVLADAGP DLLAFETIPC KLEIQALVEL LDEEKIRIPA WVALNSKDGV NVVNGDSLTD CVGLLDNCTK VVAVGINCTP PRFILDLIRV ARKVTSKPIM VYPNSGEHYD AVIKQWVECK GSTDTDFVSH VQEWRKAGAQ LIGGCCRTTP NTIRAISRVL YEHTQVYAAK // ID A9SFD6_PHYPA Unreviewed; 344 AA. AC A9SFD6; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 27-MAY-2015, entry version 39. DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EDQ70079.1}; GN ORFNames=PHYPADRAFT_128971 {ECO:0000313|EMBL:EDQ70079.1}; OS Physcomitrella patens subsp. patens (Moss). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta; OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; OC Physcomitrella. OX NCBI_TaxID=3218 {ECO:0000313|Proteomes:UP000006727}; RN [1] {ECO:0000313|EMBL:EDQ70079.1, ECO:0000313|Proteomes:UP000006727} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Gransden 2004 {ECO:0000313|Proteomes:UP000006727}; 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; DS544962; EDQ70079.1; -; Genomic_DNA. DR RefSeq; XP_001765084.1; XM_001765032.1. DR UniGene; Ppa.18700; -. DR ProteinModelPortal; A9SFD6; -. DR STRING; 3218.JGI128971; -. DR GeneID; 5928275; -. DR KEGG; ppp:PHYPADRAFT_128971; -. DR InParanoid; A9SFD6; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR Proteomes; UP000006727; Partially assembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006727}; KW Reference proteome {ECO:0000313|Proteomes:UP000006727}. SQ SEQUENCE 344 AA; 37600 MW; C415A9C332AD5566 CRC64; MGRAVDIPED KLNALSELLK TAGGCVTTDG GFATQLERHG ADINDPLWSA SCLITIPELV RKVHREYLEA GAGVISTASY QATIQGFQSR GLSTNEAEDL LQRSVRIAQE ERDRVWKESQ NREHARTARA GSNLRALVAA SIGSYGAYLA DGSEYSGDYG PSMTVDKLKD FHRRRLVVLA DAGPDLLAIE TIPCKLETQA LVELLHEEDL RIPAWISFNS KDGVNVVSGD SFSDCVALVD KCPEVAAVGI NCTPPRFILD LIHAARKVTN KPIVVYPNSG EHYDPVIKQW VESTGITDTD FVSYVHEWRK AGAQLIGGCC RTTPNTIGAI YKALHEHPHV HVTN // ID A9U7N9_PHYPA Unreviewed; 401 AA. AC A9U7N9; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 04-FEB-2015, entry version 46. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; DE Flags: Fragment; GN ORFNames=PHYPADRAFT_103986 {ECO:0000313|EMBL:EDQ48314.1}; OS Physcomitrella patens subsp. patens (Moss). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta; OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; OC Physcomitrella. OX NCBI_TaxID=3218 {ECO:0000313|Proteomes:UP000006727}; RN [1] {ECO:0000313|EMBL:EDQ48314.1, ECO:0000313|Proteomes:UP000006727} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Gransden 2004 {ECO:0000313|Proteomes:UP000006727}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {ECO:0000256|RuleBase:RU004254}. CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS546591; EDQ48314.1; -; Genomic_DNA. DR RefSeq; XP_001786872.1; XM_001786820.1. DR ProteinModelPortal; A9U7N9; -. DR STRING; 3218.JGI103986; -. DR GeneID; 5950069; -. DR KEGG; ppp:PHYPADRAFT_103986; -. DR InParanoid; A9U7N9; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000006727; Partially assembled WGS sequence. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006727}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000006727}. FT NON_TER 1 1 {ECO:0000313|EMBL:EDQ48314.1}. FT NON_TER 401 401 {ECO:0000313|EMBL:EDQ48314.1}. SQ SEQUENCE 401 AA; 42852 MW; 726FFFBD526FAE85 CRC64; RIAREVAGSA GYVVGAIGSI RGGKRTNVST AELKKYFEQQ IQALLQEGVD GILLETFYDV EELYLALSIV RKLSPLPVIC QFAVEDVART LDGYTMPEAF RMMQQQGADV IGFNCRTGPN GIMSAMKTLG GHMSVPMSVY PNAGVADYVD GEYQYGAKPD YFGQMAVKFA DLGARIIGGC CGTTPAHIAA ISSALQGYEP QPITYGPIDI APAPIEIHEH LAPDGDGEGE GGSPNLVDLV KERHTVIVEL DPPRDLDIAK FMKGAQVLKD AGADALTLAD NSLAVTRMSN MALGHLVQAE TGLRPLVHIA CRDRNLIGTQ SHLMGFDALG IDHVLAVTGD PARFGDLPGS SSVYDLTSFE IIRMIKQLNE GIAFSGKPLK QKANFVVGAA FNPHGKHLDK A // ID A9V1Z5_MONBE Unreviewed; 1268 AA. AC A9V1Z5; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 01-APR-2015, entry version 45. DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EDQ88652.1}; GN ORFNames=37476 {ECO:0000313|EMBL:EDQ88652.1}; OS Monosiga brevicollis (Choanoflagellate). OC Eukaryota; Choanoflagellida; Codonosigidae; Monosiga. OX NCBI_TaxID=81824 {ECO:0000313|Proteomes:UP000001357}; RN [1] {ECO:0000313|EMBL:EDQ88652.1, ECO:0000313|Proteomes:UP000001357} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MX1 / ATCC 50154 {ECO:0000313|Proteomes:UP000001357}; RX PubMed=18273011; DOI=10.1038/nature06617; RG JGI Sequencing; RA King N., Westbrook M.J., Young S.L., Kuo A., Abedin M., Chapman J., RA Fairclough S., Hellsten U., Isogai Y., Letunic I., Marr M., Pincus D., RA Putnam N., Rokas A., Wright K.J., Zuzow R., Dirks W., Good M., RA Goodstein D., Lemons D., Li W., Lyons J.B., Morris A., Nichols S., RA Richter D.J., Salamov A., Sequencing J.G., Bork P., Lim W.A., RA Manning G., Miller W.T., McGinnis W., Shapiro H., Tjian R., RA Grigoriev I.V., Rokhsar D.; RT "The genome of the choanoflagellate Monosiga brevicollis and the RT origin of metazoans."; RL Nature 451:783-788(2008). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CH991554; EDQ88652.1; -; Genomic_DNA. DR RefSeq; XP_001746756.1; XM_001746704.1. DR ProteinModelPortal; A9V1Z5; -. DR SMR; A9V1Z5; 665-924, 930-1264. DR STRING; 81824.JGI37476; -. DR GeneID; 5891877; -. DR KEGG; mbr:MONBRDRAFT_37476; -. DR eggNOG; COG1410; -. DR InParanoid; A9V1Z5; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR Proteomes; UP000001357; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001357}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001357}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 260 260 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 789 789 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1268 AA; 140241 MW; 2937BF417F1E3E0F CRC64; MAPAASIPAD MAQRGEQIKA ELDAILQQRI MFLDGAMGTL IQTLKLEEEN FRGEEFKSHP KPLQGNNDVL VLTMPDDIVE LHKRYLRAGA DIVETNTFNA NVISQADYAM EHLVERLNIE AARVARRACD EIQAEGLGKK YVAGAVGPTN RTLSISPSVE QPELRNITFP ELVKAYSQQI RALIEGGVDI LLVETIFDTA NAKAALFAID ALVEEGYPRL PLLISGTITD RSGRTLSGQT PDAFTVSVSH ANPLALGLNC ALGAEDMRPH LEEIAKATDA YIICYPNAGL PNAMGGYDET PEITGSHVEA FARDGLLNIV GGCCGTMPEH IASIVQKCSK FSPRPRPPKP HPNEMLLCGL ETFLIGENTN FVNIGERCNV AGSARFCRLI KENKYDDALA VAKSQVENGA QVIDINMDDG MLDGIKAMTT FCNLIASEPD ISRVPLCIDS SNFDVVKAGL ECVQGKCIVN SISLKEGVDD FKNKASIIKR YGAAVVVMAF DEDGQAADLD GKIRICQRSY RILVEEVGFN PNDIIFDPNI LTIGTGIAEH DNYGVNFIKC IRPIRESCPG AHISGGVSNL SFAFRGMNAV RESMHSVFLY HAIKEGMDFG IVNAGVMPIY TEIDPKLVKL CEDLILNRDP DATEKMLAFA QSMTAEVKKD EKVDEWRSLP VEKRLEHSLV KGIDKFVVED TEEARLNTTL YPKPLNVIEG PLMAGMSIVG DLFGAGKMFL PQVIKSARVM KRAVAHLIPF MEAERDAAFR EQGIDPNTAD VSDMYNGTMV IATVKGDVHD IGKNIVAVVL GCNNYKVVDL GVMVPANKIL DACREHKADV LGLSGLITPS LDEMIFVAKE MQRTGLDIPL LIGGATTSKM HTAVKIAPKY QQPVIHVLDA SRSVVTVSSV LDKKNREEYI EDIKDEYDEI REEYLDSLAD RTYVSLADAR ERRCVIDWAA EAPAKPNMTG LKVIEDVDLE RVVKYIDWKP FFEVWQLRGK YPNRNYPKIF DDAHVGEEAQ RVFADGQALL RRIIDEKLIR GKGVFGIFPA NTVNHDDIEI YADDTRTEPT ATLFGLRQQA EKMDKSDAYF CQSDFVAPKE SGIPDYVGLF AVNCGIGADE LANKFLADHD DYNNIMVKAL ADRLAEAFAE MLHEDVRREY WGYAKDESFN SRELHQLKYD GIRPAPGYPT QPDHTEKATY WKLLDAEARA AMSLTESFSM MPAASVSGLF FAHPKSEYFA VGKITREQVV DYAERKGQEV ETVERWLAPI LAYDPDEE // ID A9VH38_BACWK Unreviewed; 1132 AA. AC A9VH38; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 29-APR-2015, entry version 57. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABY45270.1}; GN OrderedLocusNames=BcerKBAB4_4108 {ECO:0000313|EMBL:ABY45270.1}; OS Bacillus weihenstephanensis (strain KBAB4). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=315730 {ECO:0000313|EMBL:ABY45270.1, ECO:0000313|Proteomes:UP000002154}; RN [1] {ECO:0000313|EMBL:ABY45270.1, ECO:0000313|Proteomes:UP000002154} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KBAB4 {ECO:0000313|EMBL:ABY45270.1, RC ECO:0000313|Proteomes:UP000002154}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000903; ABY45270.1; -; Genomic_DNA. DR RefSeq; WP_012261711.1; NC_010184.1. DR RefSeq; YP_001646898.1; NC_010184.1. DR ProteinModelPortal; A9VH38; -. DR STRING; 315730.BcerKBAB4_4108; -. DR EnsemblBacteria; ABY45270; ABY45270; BcerKBAB4_4108. DR KEGG; bwe:BcerKBAB4_4108; -. DR PATRIC; 19012863; VBIBacWei55973_4748. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; BWEI315730:GHRU-4223-MONOMER; -. DR Proteomes; UP000002154; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002154}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 126242 MW; 7720261A41E9E228 CRC64; MKRIEERLQH EILILDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVKTRP DVILNIHKVY IEAGADIIET NTFGATNIVL SDYALSHLDE ELNERAALLA KQAVKESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLRGE VDVLLVETSQ DMRNVKAAYI GIQSAFEELN KIVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR EHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPASLAEKV KRFAEEGWIN IIGGCCGTTP EHIRVMKSAL ASINPREHHE RVGHGISGLE ALQYDDSMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMERF LAEVTKVLKV PIMIDSTDEN VMAKALTYIQ GKGVINSINL EDGEERFERV TPLLRKYGAA IVVGTIDEDG MAVSAERKIE IAKRSYELLT KKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYALIPEE EKRLADALLF ETTKETLEKF TNFYRVAKKK DVVIQETLTL DERLANYIVE GTKQGLQEDL SLALTEGRKP LDIINGPLMT GMDEVGRLFN GNELIVAEVL QSAESMKAAV SYLEPHMESS ESAKKGKVLL ATVKGDVHDI GKNLVEIILS NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAANIDIPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKR DKKERHLHIV KQEEKKIEIP AVIEPLPKAT VMIPDSTKRV VLRDIPALHL APFLNRQMLI GHHLGLKGNV KKLLQEGDKR AHELNDLIDE LLQEGQSWLR PKAVYQFFPA QSDGQNIIIY DPEDHTRIIE RFEFPRQGKA PYRTLGDYIR PIGDEMDYVA FLSVTVGEGV RDIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID A9VH39_BACWK Unreviewed; 610 AA. AC A9VH39; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 27-MAY-2015, entry version 50. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=BcerKBAB4_4109 {ECO:0000313|EMBL:ABY45271.1}; OS Bacillus weihenstephanensis (strain KBAB4). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=315730 {ECO:0000313|EMBL:ABY45271.1, ECO:0000313|Proteomes:UP000002154}; RN [1] {ECO:0000313|EMBL:ABY45271.1, ECO:0000313|Proteomes:UP000002154} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KBAB4 {ECO:0000313|EMBL:ABY45271.1, RC ECO:0000313|Proteomes:UP000002154}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ABY45271.1; -; Genomic_DNA. DR RefSeq; WP_002190677.1; NC_010184.1. DR RefSeq; YP_001646899.1; NC_010184.1. DR ProteinModelPortal; A9VH39; -. DR STRING; 315730.BcerKBAB4_4109; -. DR EnsemblBacteria; ABY45271; ABY45271; BcerKBAB4_4109. DR KEGG; bwe:BcerKBAB4_4109; -. DR PATRIC; 19012865; VBIBacWei55973_4749. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; BWEI315730:GHRU-4224-MONOMER; -. DR Proteomes; UP000002154; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002154}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ABY45271.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:ABY45271.1}. SQ SEQUENCE 610 AA; 67097 MW; 8EF6BA867F436E3B CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNLSDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVVQ INKAAVNIAK ASVTDRNAIL GTIGGMKHIG AVTTTDIERE FMLLEQAGAL LEEQVDGLLL ETFYDEFELL HAVKVLRKQT NIPIVAQLAL HEAGTTQNGN DVNEILKQLL DYGANVVGLN CQLGPLHMTE AFKMISIPQN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEE MTPKFIEQGI RLLGGCCGTT PEHIEGMKRA IANVAPVIAK ETIQRPKVVH THEKRSRAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRVSNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDVA LIEEVYEATK HLEQPIFIGI MPLVSKRNAD FLHFEVPGIT LPEEIRQRMD GHETKEAAIE EGIRISQELI DAAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID A9VV25_BACWK Unreviewed; 325 AA. AC A9VV25; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 27-MAY-2015, entry version 44. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABY46457.1}; GN OrderedLocusNames=BcerKBAB4_5466 {ECO:0000313|EMBL:ABY46457.1}; OS Bacillus weihenstephanensis (strain KBAB4). OG Plasmid pBWB401 {ECO:0000313|EMBL:ABY46457.1, OG ECO:0000313|Proteomes:UP000002154}. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=315730 {ECO:0000313|EMBL:ABY46457.1, ECO:0000313|Proteomes:UP000002154}; RN [1] {ECO:0000313|EMBL:ABY46457.1, ECO:0000313|Proteomes:UP000002154} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KBAB4 {ECO:0000313|EMBL:ABY46457.1, RC ECO:0000313|Proteomes:UP000002154}; 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; CP000904; ABY46457.1; -; Genomic_DNA. DR RefSeq; WP_012259799.1; NC_010180.1. DR RefSeq; YP_001642432.1; NC_010180.1. DR STRING; 315730.BcerKBAB4_5466; -. DR EnsemblBacteria; ABY46457; ABY46457; BcerKBAB4_5466. DR KEGG; bwe:BcerKBAB4_5466; -. DR PATRIC; 19003197; VBIBacWei55973_0037. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; BWEI315730:GHRU-5463-MONOMER; -. DR Proteomes; UP000002154; Plasmid pBWB401. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002154}; KW Methyltransferase {ECO:0000313|EMBL:ABY46457.1}; KW Plasmid {ECO:0000313|EMBL:ABY46457.1}; KW Transferase {ECO:0000313|EMBL:ABY46457.1}. SQ SEQUENCE 325 AA; 36267 MW; 56D9747098383E6C CRC64; MSNKTNPIDA ILSQHSIMLL DGALATELEA HGCNLDDPLW SARVLLENPE LIYQVHSDYF RAGADCAMTA SYQATISGFS ARGIQEQEAL ELIKKTVLLA RRARDDFWKE NTQTNRPKPL VVASVGPYGA YLADGSEYVG NYGVTDKTLA DFHRSRMSAL IEAGADLLAF ETIPSLQEAR VLETLLREFP ATYAWLSFSL KNEKEISEGM KLVECARVFE KSEQIVAIGI NCAPVTVVTG AIQELRANTK KPIIVYPNSG ETYNPETKTW HGHEQCNALD IQSEEWYQAG ARLIGGCCRT TPYHIEEISN KWRSSEFFYS NEAKQ // ID A9W344_METEP Unreviewed; 1250 AA. AC A9W344; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 27-MAY-2015, entry version 54. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABY30000.1}; GN OrderedLocusNames=Mext_1601 {ECO:0000313|EMBL:ABY30000.1}; OS Methylobacterium extorquens (strain PA1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=419610 {ECO:0000313|EMBL:ABY30000.1, ECO:0000313|Proteomes:UP000008546}; RN [1] {ECO:0000313|EMBL:ABY30000.1, ECO:0000313|Proteomes:UP000008546} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PA1 {ECO:0000313|EMBL:ABY30000.1, RC ECO:0000313|Proteomes:UP000008546}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000908; ABY30000.1; -; Genomic_DNA. DR RefSeq; WP_012253198.1; NC_010172.1. DR RefSeq; YP_001639071.1; NC_010172.1. DR ProteinModelPortal; A9W344; -. DR SMR; A9W344; 660-909. DR STRING; 419610.Mext_1601; -. DR EnsemblBacteria; ABY30000; ABY30000; Mext_1601. DR KEGG; mex:Mext_1601; -. DR PATRIC; 22533691; VBIMetExt98426_1606. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; MEXT419610:GI32-1640-MONOMER; -. DR Proteomes; UP000008546; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008546}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 254 254 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 318 318 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 771 771 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1250 AA; 137121 MW; 43D8FB16AD1BCE42 CRC64; MTAFPPVDGT EIERALRQRA SEKILVLDGA MGTVIQRLKY TEEDFRGERF KDHSHDQKGN NDLLILTQPD AIRQIHLDYF LAGADVCETN TFSGTTIAQA DYGMESIIHE LNAEGARLAR EAAKLAEEQD GRRRFVAGAI GPTNRTLSIS PDVNNPGYRA VTFDGVKQAY VEQVRGLIDG GAELILIETI FDTLNAKAAI AAAWQVFDET GIRLPIQISG TITDLSGRTL SGQTPAAFWN SLRHSSPLTF GLNCALGAKE MRGHIAELSR ICDTLVCAYP NAGLPNEFGL YDESPEAMGK LVGEFAASGL VNMVGGCCGT TPDHIRAIAE AVADKKPREI PEIPRLMRLS GLEPFVLTKE IPFVNVGERT NVTGSAKFRK LITNNDYAAA LDVARDQVAA GAQVIDVNMD EGLLDSEKAM VEFLNLVAAE PDIARVPVMV DSSKFEVIEA GLKCIQGKPI VNSISMKEGE AKFIEAAKIC RSYGAAVVVM AFDEQGQADS YERKVEICTK AYKILTEQVG FPPEDIIFDP NIFAVATGIE EHNPYGVAFI EATRTIRETL PHAHISGGVS NLSFAFRGNE PVREAMHAVF LFHCIKAGMD MGIVNAGQLA VYDEIPAELR ELCEDVVLNR REDSTERLLE AAERFKTGAS AQAKTADLTW REAPVAKRIE HALVNGITEY IVADTEEARK EAARPLHVIE GPLMAGMNVV GDLFGSGKMF LPQVVKSARV MKQAVAYLEP FMEEEKRANG GDGKRQAAGK VLMATVKGDV HDIGKNIVGV VLACNNYEII DLGVMVPAAK ILETAKRENV DIVGLSGLIT PSLDEMVHVA AEMEREGMEM PLLIGGATTS RVHTAVKIHP AYAKGQAVYV TDASRAVGVV SSLISKETRG ATVEKVRAEY AKVADAHRRS EADKQRLPLA KARANAFKVD WSAYKPAKPS FTGTRVYGSY EVADLVPYID WTPFLQTYEF KGRYPAILDD PEQGPAARAL FEDAQVMLKQ IVEERWFNPK AVIGFWPANS VGDDIRLFTG ESRQEMLATF HGLRQQLSKR DGRANTCISD FVAPAETGIA DYVGAFVVTA GLEEVRIAER FERANDDYRS ILVKALADRI AEAFAERMHE RVRKEFWGYA PDEAYAPEEL VSEKYDGIRP APGYPAQPDH TEKVQLFDLL KAESRIGVKL TESYAMWPGS SVSGLYLAHP DAHYFGVAKV ERDQVEDYAL RKGMDVSEVE RWLGPILNYD PVRYLKAAAE // ID A9WDH2_CHLAA Unreviewed; 1197 AA. AC A9WDH2; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 27-MAY-2015, entry version 58. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABY37091.1}; GN OrderedLocusNames=Caur_3914 {ECO:0000313|EMBL:ABY37091.1}; OS Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl). OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae; OC Chloroflexaceae; Chloroflexus. OX NCBI_TaxID=324602 {ECO:0000313|EMBL:ABY37091.1, ECO:0000313|Proteomes:UP000002008}; RN [1] {ECO:0000313|Proteomes:UP000002008} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29366 / DSM 635 / J-10-fl RC {ECO:0000313|Proteomes:UP000002008}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000909; ABY37091.1; -; Genomic_DNA. DR RefSeq; WP_012259744.1; NC_010175.1. DR RefSeq; YP_001637480.1; NC_010175.1. DR ProteinModelPortal; A9WDH2; -. DR STRING; 324602.Caur_3914; -. DR EnsemblBacteria; ABY37091; ABY37091; Caur_3914. DR GeneID; 5825724; -. DR KEGG; cau:Caur_3914; -. DR PATRIC; 21419316; VBIChlAur28763_4389. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR InParanoid; A9WDH2; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CAUR324602:GIXU-3970-MONOMER; -. DR Proteomes; UP000002008; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002008}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002008}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 233 233 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 765 765 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1197 AA; 131944 MW; 45A026F38C837D26 CRC64; MSRPTYLQAL AERVLIFDGA MGTSIDTFDL TAADYGGEAT FGCRDYLVIT RPDVIEAIHT SFLEAGCDVL ETCTFQSTRP RLAEWGLGER TVEINRAAAA LARRVADRFA ARDGRPRYVA GSMGPTGKLP SSDDPALSDI TFAELSDIYY EQAIGLIEGG VDLLLVETSV DILEVKAALD GIRRAKIDLQ RPDIAVQAQV FLDLSGRMLL GTDVPAMIAT LEAMPVDVIG LNCSTGPEHM RAAIQYLTTH SRKPISCIPN AGLPLEVDGR TVYPMEPEPF AAILGEFVRE YGVAVVGGCC GTRPAHIARL RQILGDAPRP KQRQVEYIPS VSSGIRAAAL RQDATLTMIG ERLNTLGSRK VKRLLLRDDY DGALEVAREQ VESGAHMLDV CVAMTERNDE KEQMTRLIKK LTLNIELPLV IDTTEADVLE AALSIYPGRA LINSVSLEGG RGAKIDKVLP LAARYGAAVI AMTIDEEGMA HTAERKVAIA ERIARIAQEE YGIPAEALVF DVLTFPITTG QEELRYSAIE TLEGIRLVKQ RIPGCFTTLG VSNLSFGVAP HARAALNSVF LYHAVAAGLD TAIINPAHVT PYAEIDPAQR EVCEDLIFAR REDALARFIA YFEQHAASQD NEREDPTAAM TVDQRLHWKI LHRKKEGIED DIDQAVDQRL QASGLRLSDP AAALRNEHGT SPQGQAAVDV LNTVLLPAMK EVGDLFGAGQ LILPFVLQSA EAMKKAVARL ERYLDRIEGA SKGKVVLATV YGDVHDIGKN LVYTILSNNG YTVYDLGKQV PINTIIEKAL EVQADAIGLS ALLVSTSKQM PLCVQELYRR GIHIPVLVGG AAINRQYGQR ITFVDDEEPY PAGVFYCKDA FEGLETMDRL SDPATREQFI EQTIREAANV LHRRVTGRVA LTELGEAAKA SADGVRSAVR TDVPVPVPPF WGWRATSRIR LSDVVECLDR NSLYRLQWGA KNAKGAEWER LRTEFDQKVR ELIAEAERDG WLQPRVIYGY FPVQSDGLEL IVYDPADRRR ELTRFVFPRQ PARERLCISD YFRSVESGEY DLAAFQIVTM GSAVDELVET LQQRGDYSRS YYIHGLGVSL AEALAEYTNR IIRQGLGLDE RRGKRYSWGY PACPDLAEHA KLWQILPGEE IGVTLTEAFQ LVPEQSTAAI VVHHPEAKYF SIGSALERAE MDQRGDD // ID A9WHG0_CHLAA Unreviewed; 322 AA. AC A9WHG0; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABY36286.1}; GN OrderedLocusNames=Caur_3087 {ECO:0000313|EMBL:ABY36286.1}; OS Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl). OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae; OC Chloroflexaceae; Chloroflexus. OX NCBI_TaxID=324602 {ECO:0000313|EMBL:ABY36286.1, ECO:0000313|Proteomes:UP000002008}; RN [1] {ECO:0000313|Proteomes:UP000002008} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29366 / DSM 635 / J-10-fl RC {ECO:0000313|Proteomes:UP000002008}; 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 ----------------------------------------------------------------------- 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; ABY36286.1; -; Genomic_DNA. DR RefSeq; WP_012258939.1; NC_010175.1. DR RefSeq; YP_001636675.1; NC_010175.1. DR ProteinModelPortal; A9WHG0; -. DR STRING; 324602.Caur_3087; -. DR DNASU; 5827561; -. DR EnsemblBacteria; ABY36286; ABY36286; Caur_3087. DR GeneID; 5827561; -. DR KEGG; cau:Caur_3087; -. DR PATRIC; 21417501; VBIChlAur28763_3490. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR InParanoid; A9WHG0; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; CAUR324602:GIXU-3136-MONOMER; -. DR Proteomes; UP000002008; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002008}; KW Methyltransferase {ECO:0000313|EMBL:ABY36286.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002008}; KW Transferase {ECO:0000313|EMBL:ABY36286.1}. SQ SEQUENCE 322 AA; 34425 MW; 1377ABA42981BFFE CRC64; MLKMSSPNPI TAALAQRPLL ILDGALATEL ERRGCDLADP LWSAKVLIEN PSLIQAVHAD YFAAGADVAI TASYQATIPG FMARGIAPDQ AILLLQRSVA LAQAARDQFW ADPANREGRL RPLVAASVGP YGAFLHDGSE YRGNYGLSVA ELIEFHRPRM AALAAARPDL FACETIPCLD EARALVALLP EFPHLTAWIS FSARDGAHTA QGEPIAECAA EIAAHPQVAA IGVNCTAPRF LPDLIRAVQA VTDKPIVVYP NSGEVYDPVG QCWIGTTEID DFVAQARQWY AMGARLIGGC CRTTPDHIRA LAAWAAAGVN HD // ID B0A6J2_9FIRM Unreviewed; 796 AA. AC B0A6J2; DT 26-FEB-2008, integrated into UniProtKB/TrEMBL. DT 26-FEB-2008, sequence version 1. DT 27-MAY-2015, entry version 32. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EDQ97804.1}; GN ORFNames=CLOBAR_00202 {ECO:0000313|EMBL:EDQ97804.1}; OS Intestinibacter bartlettii DSM 16795. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Intestinibacter. OX NCBI_TaxID=445973 {ECO:0000313|EMBL:EDQ97804.1}; RN [1] {ECO:0000313|EMBL:EDQ97804.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 16795 {ECO:0000313|EMBL:EDQ97804.1}; 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 (OCT-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EDQ97804.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 16795 {ECO:0000313|EMBL:EDQ97804.1}; 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. {ECO:0000313|EMBL:EDQ97804.1}. 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; ABEZ02000006; EDQ97804.1; -; Genomic_DNA. DR RefSeq; WP_007285369.1; NZ_DS499558.1. DR ProteinModelPortal; B0A6J2; -. DR EnsemblBacteria; EDQ97804; EDQ97804; CLOBAR_00202. DR PATRIC; 25247112; VBICloBar105643_0176. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDQ97804.1}; KW Transferase {ECO:0000313|EMBL:EDQ97804.1}. SQ SEQUENCE 796 AA; 87066 MW; B6BF4EA91AEA3E1F CRC64; MVVEVRQYIQ DNILIFDGAM GTMLQGRGLQ AGQNPEAFGF DNPDVLVDIH KEYFKAGANV ATTDTFGCNE LKLPQGYELE KVIDSAIKSA KKAASLVDNG KQKYVALDIG PIGEMLEPMG TLSFDRAYEI FKRQMVQGEK SGADIIVIET MMDLYEIKAA LLAAKENTNL PVFCTMTFDE NGRSFTGCLP ESMVVTLQGL GADAIGVNCS LGPDLLIPIV EKIIKRATIP VMVQANAGLP CIKCGETVYE MTAGQFLEGA SKFAKMGAKI IGGCCGTNPE FIKALAENIK DVEVEPLEKN LECVVCSPSK ILEISGPTIM GERLNPTGRK PLQDALINGD LDYVVSLGLD QIEEGAEILN MNVGLPEIDE KVMMPKVIKT LQEIINVPIQ LDSSNVEALE QGLRYYNGRT IVNSVNGKEE ALNKILPIVK KYGAGLVGLT LDENGIPKTA EGRFEIAKKI VERAESYGIR RQDIFIDCLS LTVSAQQEEA METIKAIRMV KENLGCKTIL GVSNISFGVP NRRALNSTFL NLALGAGLDL AIINTSEEVM MESMYAYRVI NNIDKGCEKY IKKYMDAPKS SNSKTSNNDS KEMSLDILVE RGLKDETKEL TNKLLEEHDG HYILDKILIP ALDKIGVKYD NGEIFLPQMI QAAETIKVSL NIIKDKLSVN TDSNETKGKI IVATVKGDIH DIGKNIVKIM LENYGYEVID LGKDVPIETV VETAKKQNIK LIGLSALMTT TVQNMKDTIK AIRESGIDAK VIVGGAVLTE EYAKKIDADY YAKDAKSSVE IAKLTF // ID B0BQ18_ACTPJ Unreviewed; 297 AA. AC B0BQ18; DT 26-FEB-2008, integrated into UniProtKB/TrEMBL. DT 26-FEB-2008, sequence version 1. DT 27-MAY-2015, entry version 39. DE SubName: Full=Homocysteine/selenocysteine methylase(S-methylmethionine-dependent) {ECO:0000313|EMBL:ABY69653.1}; GN OrderedLocusNames=APJL_1097 {ECO:0000313|EMBL:ABY69653.1}; OS Actinobacillus pleuropneumoniae serotype 3 (strain JL03). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=434271 {ECO:0000313|EMBL:ABY69653.1, ECO:0000313|Proteomes:UP000008547}; RN [1] {ECO:0000313|EMBL:ABY69653.1, ECO:0000313|Proteomes:UP000008547} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JL03 {ECO:0000313|EMBL:ABY69653.1, RC ECO:0000313|Proteomes:UP000008547}; RX PubMed=18197260; DOI=10.1371/journal.pone.0001450; RA Xu Z., Zhou Y., Li L., Zhou R., Xiao S., Wan Y., Zhang S., Wang K., RA Li W., Li L., Jin H., Kang M., Dalai B., Li T., Liu L., Cheng Y., RA Zhang L., Xu T., Zheng H., Pu S., Wang B., Gu W., Zhang X.L., RA Zhu G.-F., Wang S., Zhao G.-P., Chen H.; RT "Genome biology of Actinobacillus pleuropneumoniae JL03, an isolate of RT serotype 3 prevalent in China."; RL PLoS ONE 3:E1450-E1450(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; CP000687; ABY69653.1; -; Genomic_DNA. DR RefSeq; WP_005597940.1; NC_010278.1. DR RefSeq; YP_001652097.1; NC_010278.1. DR ProteinModelPortal; B0BQ18; -. DR STRING; 434271.APJL_1097; -. DR EnsemblBacteria; ABY69653; ABY69653; APJL_1097. DR KEGG; apj:APJL_1097; -. DR PATRIC; 20751436; VBIActPle136345_1094. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; PYVDVWL; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; APLE434271:GIX7-1093-MONOMER; -. DR Proteomes; UP000008547; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008547}; KW Methyltransferase {ECO:0000313|EMBL:ABY69653.1}; KW Transferase {ECO:0000313|EMBL:ABY69653.1}. SQ SEQUENCE 297 AA; 32341 MW; E74F7F51335D3F4A CRC64; MTITILDGGM SRELMRLNAP FKQPEWSALS LYEKPSAVQQ VHEDFIANGA EVITTNSYAV VPFHIGEQRF SADGKMLADL AGRLAKQAVK NSGKSAKIAG SLPPMFGSYR ADLIQADRFA EIAQPIIDGL APYVDIWLCE TQSAIIEPTS IKPLLPKDDR PLWVSFTLTD DEPTPEPQLR SGEPVALAIE KMVELGVDAI LFNCCQPEVI EQALAITQSI LKEKNVTHIQ TGAYANAFAP QPKDATANDG LDEVRKDLDP EAYLAWAQKW TAQGATIIGG CCGIGIEYIN TLAKNLK // ID B0BZL9_ACAM1 Unreviewed; 321 AA. AC B0BZL9; DT 26-FEB-2008, integrated into UniProtKB/TrEMBL. DT 26-FEB-2008, sequence version 1. DT 27-MAY-2015, entry version 38. DE SubName: Full=Homocysteine S-methyltransferase, putative {ECO:0000313|EMBL:ABW25945.1}; GN OrderedLocusNames=AM1_0903 {ECO:0000313|EMBL:ABW25945.1}; OS Acaryochloris marina (strain MBIC 11017). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Acaryochloris. OX NCBI_TaxID=329726 {ECO:0000313|EMBL:ABW25945.1, ECO:0000313|Proteomes:UP000000268}; RN [1] {ECO:0000313|EMBL:ABW25945.1, ECO:0000313|Proteomes:UP000000268} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MBIC 11017 {ECO:0000313|Proteomes:UP000000268}; 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 ----------------------------------------------------------------------- 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; ABW25945.1; -; Genomic_DNA. DR RefSeq; WP_012161514.1; NC_009925.1. DR RefSeq; YP_001515259.1; NC_009925.1. DR STRING; 329726.AM1_0903; -. DR EnsemblBacteria; ABW25945; ABW25945; AM1_0903. DR KEGG; amr:AM1_0903; -. DR PATRIC; 20616298; VBIAcaMar40141_0798. DR eggNOG; COG2040; -. DR HOGENOM; HOG000179103; -. DR OMA; CCGTDHR; -. DR OrthoDB; EOG6R5C46; -. DR BioCyc; AMAR329726:GCZJ-894-MONOMER; -. DR Proteomes; UP000000268; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000268}; KW Methyltransferase {ECO:0000313|EMBL:ABW25945.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000268}; KW Transferase {ECO:0000313|EMBL:ABW25945.1}. SQ SEQUENCE 321 AA; 35036 MW; 4A5DE8DB979F8790 CRC64; MPQYRQNLPQ LSSDVFLTDG GLETTLIFHE GIDLPDFAAF DLLKDNQGYE ALYEYFQTYA QLAQTYEVGL ILESATWRAN PDWGTKLGYD AAELAAVNRN AIALLHTIRQ QYETEASRMV ISGCIGPRGD GYQVDTAMTP AEAQVYHLPQ IEAFKEAEAD MVSAVTMTYT EEAIGITRAA HLVGMPVVIS FTVETDGKLP TGQGLKDAIA QVDAATGNGP IYYMINCAHP SHFEQIFATN EPWLTRIHGL RANASTKSHA ELDEAVDLDD GNPQELGQQY LNLSDALPNL NVLGGCCGTD HRHIEAICKA CLPARSAVHA S // ID B0C433_ACAM1 Unreviewed; 1198 AA. AC B0C433; DT 26-FEB-2008, integrated into UniProtKB/TrEMBL. DT 26-FEB-2008, sequence version 1. DT 27-MAY-2015, entry version 58. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABW26293.1}; GN Name=metH {ECO:0000313|EMBL:ABW26293.1}; GN OrderedLocusNames=AM1_1256 {ECO:0000313|EMBL:ABW26293.1}; OS Acaryochloris marina (strain MBIC 11017). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Acaryochloris. OX NCBI_TaxID=329726 {ECO:0000313|EMBL:ABW26293.1, ECO:0000313|Proteomes:UP000000268}; RN [1] {ECO:0000313|EMBL:ABW26293.1, ECO:0000313|Proteomes:UP000000268} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MBIC 11017 {ECO:0000313|Proteomes:UP000000268}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000828; ABW26293.1; -; Genomic_DNA. DR RefSeq; WP_012161831.1; NC_009925.1. DR RefSeq; YP_001515607.1; NC_009925.1. DR ProteinModelPortal; B0C433; -. DR STRING; 329726.AM1_1256; -. DR EnsemblBacteria; ABW26293; ABW26293; AM1_1256. DR KEGG; amr:AM1_1256; -. DR PATRIC; 20616942; VBIAcaMar40141_1118. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; AMAR329726:GCZJ-1246-MONOMER; -. DR Proteomes; UP000000268; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000268}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000268}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 228 228 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 749 749 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1198 AA; 132512 MW; 47746DA14C2BF88D CRC64; MKSVFLDRLH SPERPVIVFD GAMGTSLQMQ NLTAEDFGGP EYEGCNEYLI QTKPGAVATV HRNFLKAGAD VIETDTFGAT SIVLAEYDLA DQAYELNKAA AELAKQVTAE FSTPEKPRFV AGSMGPGTKL PTLGHIDFDT LKAAYVEQAQ GLYDGGADLL LVETCQDVLQ IKAALNAIEV VFAEKGARLP LMVSVTVENF GTMLVGSEIG AALTVLEPYP IDILGLNCAT GPDLMKEHIK YLSEQSPFIV SCIPNAGLPE NVGGQAHYLL TPMELRMALM HFIEDLGVQV IGGCCGTRPD HIQQLAEMSQ DLKPKAREIG SRQSLPPYAP LPFVPAAASI MTTQSYDQDN SFLIVGERLN ASGSKKCRET LNAEDWDGLV SLARSQVKEG AHVLDVNVDY VGRDGERDMR ELASRLVNTV SLPLMLDSTE WTKMEAGLKV AGGKCILNST NYEDGEERFY KVLELAKTYG AGVVVGTIDE DGMARTAEKK FEIAKRAYDD AINYGIPAYE IFFDPLALPA STGIEEDRNN ANATISAIWQ IRDELPGCHI ILGVSNVSFG LNPAARVTLN SVFLHEAMAV GMDAAIVSAS KILPLAKIEE EHKQVCLDLI YDRRQFDGEV CTYDPLTKLT TLFEGKTTKR DRSVDTSLPV EERLKNHIID GERIGLEEQL DIALKDHAPL AIINTFLLDG MKVVGELFGS GQMQLPFVLQ SAQTMKAAVA YLEPMMDKEE ADDSGKGTVV IATVKGDVHD IGKNLVDIIL SNNGYQVINL GIKQPVDTII AAYREHNADC IAMSGLLVKS TAFMKDNLET FNQEGITVPV ILGGAALTPK FVNQDCQNTY NGQVIYGKDA FADLHFMDKL MPAKTEGQWD NLKGFLNEQD EVPESVSTNG SQPQENAAEA ATAAMPVDTR RSEAVDIDIE RPTPPFWGTT ILQPEDLPFD ELFWHLDLQA LIAGQWQFRK PKDQSREDYD AFLDQKVYPI LNQWKQRIVA EKLLHPQAIY GYFPCLAEEN SLHIYDPKVA ENPGDTLPEP VTTFTFPRQK SMRRLCIADF FLPKEQGIAQ KRFDVFPMQA VTVGDIATEF AQKLFAGDEY TEYLYFHGLA VQTAEAIAEW THARIRRELG YGESEPDNIR DMLAQRYQGS RYSFGYPACP NMQDQYKQLD LLQTDRINLH MDESEQLYPE QSTTAIMVYH PVAKYFSA // ID B0CJ47_BRUSI Unreviewed; 1265 AA. AC B0CJ47; DT 26-FEB-2008, integrated into UniProtKB/TrEMBL. DT 26-FEB-2008, sequence version 1. DT 27-MAY-2015, entry version 54. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABY37291.1}; GN Name=metH {ECO:0000313|EMBL:ABY37291.1}; GN OrderedLocusNames=BSUIS_A0189 {ECO:0000313|EMBL:ABY37291.1}; OS Brucella suis (strain ATCC 23445 / NCTC 10510). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=470137 {ECO:0000313|EMBL:ABY37291.1, ECO:0000313|Proteomes:UP000008545}; RN [1] {ECO:0000313|EMBL:ABY37291.1, ECO:0000313|Proteomes:UP000008545} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23445 / NCTC 10510 {ECO:0000313|Proteomes:UP000008545}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000911; ABY37291.1; -; Genomic_DNA. DR RefSeq; WP_006072011.1; NC_010169.1. DR RefSeq; YP_001626861.1; NC_010169.1. DR ProteinModelPortal; B0CJ47; -. DR SMR; B0CJ47; 677-925. DR STRING; 470137.BSUIS_A0189; -. DR EnsemblBacteria; ABY37291; ABY37291; BSUIS_A0189. DR KEGG; bmt:BSUIS_A0189; -. DR PATRIC; 17867842; VBIBruSui83806_1724. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; BSUI470137:GJIC-188-MONOMER; -. DR PRO; PR:B0CJ47; -. DR Proteomes; UP000008545; Chromosome I. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008545}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 267 267 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 330 330 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 331 331 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 787 787 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1265 AA; 139091 MW; 452550D8E881F220 CRC64; MASSLDDLFG ATAAKPDGSE VPAALTQAAR ERILILDGAM GTQIQGLGFH EEHFRGDRFA TCDCQLQGNN DLLTLTQPKA IEEIHYAYAY AYAMAGADIL ETNTFSSTSI AQADYGMEAM VYDLNRDGAR LARRAALRAE QKDGRRRFVA GALGPTNRTA SLSPDVNNPG FRAVTFDDLR IAYSEQIRGL IDGGSDIILI ETIFDTLNAK AAVFATEEVF AEKGVRLPVM ISGTITDLSG RTLSGQTPTA FWYSLRHARP FTIGLNCALG ANAMRAHLDE LSGIADTFIC AYPNAGLPNE FGQYDETPEA MAAQIEGFAR DGLVNVVGGC CGSTPDHIRA IAQAVAKYEP RKPAKVPPLM RLSGLEPFTL TKDIPFVNIG ERTNVTGSAR FRKLVKAGDF AAALDVARDQ VANGAQIIDI NMDEGLIDSE KAMVEFLNLI AAEPDIARVP IMLDSSKWEV IEAGLKCVQG KAVVNSISLK EGEEAFLHHA RLVRAYGAAV VIMAFDETGQ ADTQARKIEI CTRAYKILTE QVGFPPEDII FDPNIFAVAT GIEEHNNYGV DFIEATREIV RTLPHVHISG GVSNLSFSFR GNEPVREAMH AVFLYHAIQA GMDMGIVNAG QLAVYDTIDA ELREACEDVV LNRPTKTGES ATERLLEIAE RFRDSGSREA RTQDLSWREW PVEKRLEHAL VNGITEYIEA DTEEARLAAE RPLHVIEGPL MAGMNVVGDL FGSGKMFLPQ VVKSARVMKQ AVAVLLPFME EEKRLNGGEG RQSAGKVLMA TVKGDVHDIG KNIVGVVLAC NNYEIIDLGV MVPSQKILQV ARDEKVDIIG LSGLITPSLD EMAHVAAEME REGFDIPLLI GGATTSRVHT AVKIHSRYER GQAVYVVDAS RAVGVVSNLL SPEGKQAYVD GLRNEYAKVA AAHARNEAEK QRLPIARARA NPHQLDWENY EPVKPAFTGT KVFETYDLAE IARYIDWTPF FQTWELRGRY PAILEDEKQG EAARQLWADA QAMLRKIIDE KWFTPRAVVG FWPANAVGDD IRLFTDESRK EELATLFTLR QQLTKRDGRP NVAMADFVAP VESGKQDYVG GFVVTAGIGE IAIAERFERA NDDYSAILVK ALADRFAEAF AELMHERVRK EFWAYAPDEA FTPEELISEP YKGIRPAPGY PAQPDHTEKT TLFRLLDATA NTGVELTESY AMWPGSSVSG LYIGHPESYY FGVAKVERDQ VEDYARRKDM DVEAVERWLT PILNYVPGAS KDEAA // ID B0CN36_STRLA Unreviewed; 1127 AA. AC B0CN36; DT 26-FEB-2008, integrated into UniProtKB/TrEMBL. DT 26-FEB-2008, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=Putative methionine synthase {ECO:0000313|EMBL:ABI22142.1}; GN Name=sfmS3 {ECO:0000313|EMBL:ABI22142.1}; OS Streptomyces lavendulae. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1914 {ECO:0000313|EMBL:ABI22142.1}; RN [1] {ECO:0000313|EMBL:ABI22142.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NRRL 11002 {ECO:0000313|EMBL:ABI22142.1}; RX PubMed=17981978; DOI=10.1128/JB.00826-07; RA Li L., Deng W., Song J., Ding W., Zhao Q.F., Peng C., Song W.W., RA Tang G.L., Liu W.; RT "Characterization of the saframycin A gene cluster from Streptomyces RT lavendulae NRRL 11002 revealing a nonribosomal peptide synthetase RT system for assembling the unusual tetrapeptidyl skeleton in an RT iterative manner."; RL J. Bacteriol. 190:251-263(2008). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; DQ838002; ABI22142.1; -; Genomic_DNA. DR ProteinModelPortal; B0CN36; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 194 194 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 260 260 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 261 261 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 704 704 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1127 AA; 123498 MW; 082B62DF42FCB970 CRC64; MEDFQQLEGC NEVLNVTRPD IVANVHREYF AVGVDCVETN TFGANFAALA EYDIPERNFE LSEAGARIAR QVADEFTAST GRQRWVLGSM GPGTKLPTLG HIDYAQIRDA YQVNAEGLIS GGADALLVET TQDLLQTKAA IIGARRALSN CGEDMPVICS VTVEATGTML LGSEIGAALT ALEPLGIDMI GLNCATGPAE MSEHLRYLAR NARIPLSCMP NAGLPVLTKQ GAHYPLSAAE LADAQETFVR EYGLSLVGGC CGTTPEHLRQ VVERVRGTAV TERSPQPEPG AASLYQTVPF RQDTSYMAIG ERTNANGSKK FREAMLEARW DDCVEMARDQ IREGAHMLDL CVDYVGRDGV ADMQELAGRF ATASTLPIVL DSTEVPVIQA GLEKLGGRAV INSVNYEDGD GPESRFAKVT RLAQEHGAAL IALTIDEEGQ ARSVEHKVAI AERLIEDLTS NWGIRESDIL IDTLTFTICT GQEESRKDGI ATIESIRELK RRHPEVQTTL GLSNISFGLN PAARVLLNSV FLDECVKAGL DSAIVHASKI LPIARFDEEQ VSTALDLIYD RREGDYDPLQ KLMALFEGVN TKSLKAGRAE ELLALPLDER LQRRIIDGEK NGLEADLDEA LASRPALDIV NDTLLEGMKV VGELFGSGQM QLPFVLQSAE VMKTAVAYLE PHMEKTDADG KGTIVLATVR GDVHDIGKNL VDIILTNNGY NVVNIGIKQP VSAILEAAQE HKADVIGMSG LLVKSTVIMK ENLEELNQRK LAADYPVILG GAALTRAYVE QDLHEIYEGE VRYARDAFEG LRLMDALIAV KRGIPGAELP PLKQRRVAKR DTPALQVEEP EETGGRSDVA VDNPVPTPPF WGTRVIKGIP LKDYASWLDE GALFKGQWGL KQARAGGATY EELVESEGRP RLRGLLEKLH TENLLEAAVV YGYFPCVSKG EDLIILDEQG NERTRFTFPR QRRGRRLCLA DFFRPEESGE TDVIGLQVVT VGSRIGEATA KLFEADSYRE YLELHGLSVQ LAEALAEYWH ARVRAELGFG GEDPEKVEDM FDLKYRGARF SLGYGACPDL EDRAKIADLL QPERIGVHLS EEFQLHPEQS TDAIVIHHPD ATYFNAR // ID B0DTQ2_LACBS Unreviewed; 418 AA. AC B0DTQ2; DT 26-FEB-2008, integrated into UniProtKB/TrEMBL. DT 26-FEB-2008, sequence version 1. DT 07-JAN-2015, entry version 28. DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EDR02019.1}; GN ORFNames=LACBIDRAFT_310210 {ECO:0000313|EMBL:EDR02019.1}; 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 {ECO:0000313|Proteomes:UP000001194}; RN [1] {ECO:0000313|EMBL:EDR02019.1, ECO:0000313|Proteomes:UP000001194} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S238N-H82 / ATCC MYA-4686 {ECO:0000313|Proteomes:UP000001194}; 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; DS547134; EDR02019.1; -; Genomic_DNA. DR RefSeq; XP_001887410.1; XM_001887375.1. DR STRING; 29883.JGI310210; -. DR GeneID; 6082975; -. DR KEGG; lbc:LACBIDRAFT_310210; -. DR InParanoid; B0DTQ2; -. DR KO; K00547; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000001194; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 2. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001194}; KW Reference proteome {ECO:0000313|Proteomes:UP000001194}. SQ SEQUENCE 418 AA; 45711 MW; 17B2AB4968A8C90B CRC64; MPAHVRRFSG VSNDAESEYS PQAKRRKVSV RNARFDAMID AMNAVRRIWM QGTTLEDVFH KSIKTPLWSA TLTETDPETV IAAHLAFLEA GSLVIMTSTY QRAFETFERA GYGEADAVTL MNKSVELASE AKSRFLAQNP SITATYIKIA LALGPFGATL TTAQEFSGYY PPPYGPQEFT PDLDGTNTNA FSAEESEAEA VAVDSLASFH LRRLRVFCNH PSWDLVDVIV FETVPLVREI AAIRRAVGML PEFAMKSWWV ATVWLDGVFL QESVPGGERL LAADVVDALL RDASPANPVP TGIGVNCTQI EYYPEIIQAH RIAFNALLLS QVGDSKFARP RLVVYSNGGV KYDPIAHVWL DSGVAHRGGT GKAQWVKELV SLAKEEGKFG SWAGIVVGGC CKTAPDDIHA LAEELKLS // ID B0G1H1_9FIRM Unreviewed; 801 AA. AC B0G1H1; DT 18-MAR-2008, integrated into UniProtKB/TrEMBL. DT 18-MAR-2008, sequence version 1. DT 27-MAY-2015, entry version 31. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EDR48544.1}; GN ORFNames=DORFOR_00090 {ECO:0000313|EMBL:EDR48544.1}; OS Dorea formicigenerans ATCC 27755. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Dorea. OX NCBI_TaxID=411461 {ECO:0000313|EMBL:EDR48544.1}; RN [1] {ECO:0000313|EMBL:EDR48544.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27755 {ECO:0000313|EMBL:EDR48544.1}; 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] {ECO:0000313|EMBL:EDR48544.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27755 {ECO:0000313|EMBL:EDR48544.1}; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., 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. {ECO:0000313|EMBL:EDR48544.1}. 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; AAXA02000003; EDR48544.1; -; Genomic_DNA. DR RefSeq; WP_005330279.1; NZ_AAXA02000003.1. DR ProteinModelPortal; B0G1H1; -. DR EnsemblBacteria; EDR48544; EDR48544; DORFOR_00090. DR PATRIC; 26657193; VBIDorFor18168_0083. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDR48544.1}; KW Transferase {ECO:0000313|EMBL:EDR48544.1}. SQ SEQUENCE 801 AA; 87409 MW; 316C97F9B654846B CRC64; MILDRLGKEL IYFDGGTGTL LQERGLKPGE LPETWSLEHA DDMIDIARQY YEAGSDIVLS NTFGANALKF HDSRHELDEI VKAAIENVRK GAKLGVKDGR ETYVGLDIGP TGKLLKPMGD LDFEDAYQAF AEVARLGEEA GADLIHIETM SDTYEVKAAV LAAKENTSLP VFATMIFDDK GKLLTGGDVP SVVAMLEGLR VDALGINCGM GPEQMMPILD EILQYASVPV IVKPNAGLPK QKDGEVYYDV EPEEFGRFMA EILKRGASLI GGCCGTTPAH IRAMVEATKD QRDITDRPGK EFKNRTIVSS YGRAVELGGK PMIIGERINP TGKKKFKQAL KDHDIDYILR EAISQQDAGA HILDVNVGLP DIDEPALMRE VVQELQSVTS LPLQIDTVDI SALEAAMRIY NGKPMVNSVN GKQSSMDAVF PLIKKYGGVV VGLTLDEDGI PATAEGRVKV AGKIIEEAKK YGIDKKDIVI DVLCMTISSE PTGAITTLEA LRQVREKYGV CAVLGVSNIS FGLPYRPAVN SNFYTMAMQS GLSAGIINPL SEDMMRSYYS FCALMNYDEN CEKYIEQYGS QKVQAVTPAT KAEMTLKTAI EKGLKEEAHH ITAELVKDKA PLDIINEELI PALDQVGKGF EKGTVFLPQL LMSADAAKIA FAVLKDELAK SGESEQAKDK VILATVKGDI HDIGKNIVKV LLENYSFDVI DLGKDVPPEE IVETAIKEDV RLVGLSALMT TTVVSMEETI RQLRKKKPEC KVMVGGAVLN QDYSDMIGAD FYGKDAMQSV YYAQQLFGGE K // ID B0JFV5_MICAN Unreviewed; 1187 AA. AC B0JFV5; DT 18-MAR-2008, integrated into UniProtKB/TrEMBL. DT 18-MAR-2008, sequence version 1. DT 27-MAY-2015, entry version 55. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:BAG01960.1}; GN Name=metH {ECO:0000313|EMBL:BAG01960.1}; GN OrderedLocusNames=MAE_21380 {ECO:0000313|EMBL:BAG01960.1}; OS Microcystis aeruginosa (strain NIES-843). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Microcystis. OX NCBI_TaxID=449447 {ECO:0000313|Proteomes:UP000001510}; RN [1] {ECO:0000313|EMBL:BAG01960.1, ECO:0000313|Proteomes:UP000001510} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NIES-843 {ECO:0000313|Proteomes:UP000001510}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP009552; BAG01960.1; -; Genomic_DNA. DR RefSeq; WP_012265356.1; NC_010296.1. DR RefSeq; YP_001657152.1; NC_010296.1. DR ProteinModelPortal; B0JFV5; -. DR STRING; 449447.MAE_21380; -. DR PaxDb; B0JFV5; -. DR PRIDE; B0JFV5; -. DR EnsemblBacteria; BAG01960; BAG01960; MAE_21380. DR GeneID; 5862947; -. DR KEGG; mar:MAE_21380; -. DR PATRIC; 22629265; VBIMicAer59304_1961. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; MAER449447:GHO8-2151-MONOMER; -. DR Proteomes; UP000001510; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001510}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAG01960.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001510}; KW Transferase {ECO:0000313|EMBL:BAG01960.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 228 228 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 737 737 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1187 AA; 131641 MW; 00B8B69D78B11BC4 CRC64; MNSPFLDYLN GPKHPVLVFD GAMGTSLQSQ NLTAEDFGGA EYEGCNEYLV HTKPSAVAKV HEAFLAVGAD VIETDTFGGT SIVLAEYDLA DQAYYLNKTA AELAKACANK YSTPEKPRFV AGSMGPGTKL PTLGHIDFDT LKNAYVEQVE GLYDGGADLL LVETCQDVLQ IKAALNAIEE VFQQKGQRLP LMVSVTMETM GTMLVGTEIN AVVSILQPYK IDILGLNCAT GPDLMKPHIK YLSENSPFIV SCIPNAGLPE NVGGQAHYRL TPVELKMALM HFIEDLGVQI IGGCCGTRPD HIQALAELCQ GLTPKSRHYH YEPSAASIYS TQPYIQDNSF LIVGEKLNAS GSKKCRELLN AEDWDSLVSM AKAQVKEGAH ILDVNVDYVG RDGVRDMHQL ASRLVNNVTL PLMLDSTEWE KMEAGLKVAG GKCILNSTNY EDGEPRFYQV LDLAKKYGAG VVIGTIDEEG MGRTAEKKFQ IAKRAYYAAI EYGIPPYEIF FDPLALPIST GIEEDRENGK ATIEAMGRIR QELPECHILL GVSNISFGLN PAARQVLNSV FLNEAMQVGM DGAIVSANKI LPLAKIEPEY QQVCRDLIYD NRRFDGDICV YDPLTKLTEL FAGKTTKKDP SSNANLPVEE RLKQHIIDGE RLGLEDALNQ ALQDYPPLDI INIFLLDGMK VVGELFGSGQ MQLPFVLQSA QTMKAAVAFL EPFMEKKEGD NNAKGTFIIA TVKGDVHDIG KNLVDIILTN NGYKVINLGI KQPVENIIEA YKEHKADCIA MSGLLVKSTA FMKENLEVFN EKGITVPVIL GGAALTPKFV HDDCQKTYKG QVIYGKDAFS DLHFMDKLMP AKAGGQWDDS KGFLAECAET EKTPVVAEEL EVNPDTIFTD GSVDKELVID TRRSEAVEVN IPRPTPPFWG TKILTAAEIP IEEVFWYLDL QALFVGQWQF RKPKSQSKPE YDQFLQEKVH PILAAWKEKI VKENLLNPTL IYGYFPCQSS GNSLLIYDPE SIQAGEKPEN LQPIAIFEFP RQKSGRRLCI ADFFAPQESG IIDVFPMQAV TVGEIATEYA KSLFDANQYT EYLYYHGMAV QTAEAMAEWT HTRIRRELGF AEFDPDNIRD ILQQRYQGSR YSFGYPACPN IQDQYKQLDL LGCDRIGMSM DESEQLYPEQ STTAIITYHP TAKYFST // ID B0K6M9_THEPX Unreviewed; 807 AA. AC B0K6M9; DT 18-MAR-2008, integrated into UniProtKB/TrEMBL. DT 18-MAR-2008, sequence version 1. DT 27-MAY-2015, entry version 45. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABY92505.1}; GN OrderedLocusNames=Teth514_1211 {ECO:0000313|EMBL:ABY92505.1}; OS Thermoanaerobacter sp. (strain X514). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Thermoanaerobacter. OX NCBI_TaxID=399726 {ECO:0000313|EMBL:ABY92505.1, ECO:0000313|Proteomes:UP000002155}; RN [1] {ECO:0000313|EMBL:ABY92505.1, ECO:0000313|Proteomes:UP000002155} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=X514 {ECO:0000313|EMBL:ABY92505.1, RC ECO:0000313|Proteomes:UP000002155}; 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 ----------------------------------------------------------------------- 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; ABY92505.1; -; Genomic_DNA. DR RefSeq; WP_009052924.1; NC_010320.1. DR ProteinModelPortal; B0K6M9; -. DR STRING; 399726.Teth514_1211; -. DR EnsemblBacteria; ABY92505; ABY92505; Teth514_1211. DR KEGG; tex:Teth514_1211; -. DR PATRIC; 23892056; VBITheSp86957_1265. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; TSP399726:GHCK-1245-MONOMER; -. DR Proteomes; UP000002155; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002155}; KW Methyltransferase {ECO:0000313|EMBL:ABY92505.1}; KW Transferase {ECO:0000313|EMBL:ABY92505.1}. SQ SEQUENCE 807 AA; 88138 MW; 3FC4DC69FAA2F5EE CRC64; MLDIFKELSN RVIVFDGAMG TQLQERGLKT GECPEYMNIT HPEVVFDIHR SYIEAGADVI ETNTFGANRI KLAKYGLENE VFNIVTQAVK IAKEASKDKP VALSIGPIGE LLTPYGDMTF DEAYDVFKEV VIAAERAGAD IVLIETMSDM LEAKAAILAA KENSNMKVIC TMTFQEDGRT LMGSDPITVV VSLQGLGLDA IGVNCSTGPD KMVSVVEKMS QVSRIPIIAQ PNAGMPVIRD GKTVYDLKPE EFASFFPSLV EKGASIVGGC CGTTPHYIKL VKKAVKDLKP KVKVNKFTAV ASNTKTVFIG HDYSLRVIGE RINPTGKKKL SEAFLAGNVS LAVEEAIKQQ KCGAEILDVN VGVPGVNEEE LLPKVVSEIQ NVVDIPLQID STNIKAVEKA IRILRGRPII NSVSAKEESL KEVLPIVKKY GACVVGLTVG DKGLPKDRHE RIENAKKIIK KAEEYGIPKE DILIDCIVLT VSSEQEAAIE TLEAIKLAKE ELGANTVVGL SNVSFGLPER RLINSTFLAM AASYGLTTAI INPCDEAMMD TLRASMVLLN KDKGSVNYLK IYGNRQKEEG KEKEQQKIQE EDLKSKFYIQ ILEGKKSGVE DIVKNILEKE VQPLSIVDNI IIPALKEVGD RYEKGIYFLP QLLSSAEVVQ NAFRIIKEKL PKGSVSKGKI ILATVEGDVH DIGKNIVKVL LENYGYDVID LGKDVKGEVI LEEVKRTGAP LVGLSALMTT TLFNMEKIIK LLKANTDVKI MVGGAVLTEE YAYKIGADYY GKTAQDAVKI ADKFFLKNAL LCKTCGI // ID B0K7W0_THEP3 Unreviewed; 807 AA. AC B0K7W0; DT 18-MAR-2008, integrated into UniProtKB/TrEMBL. DT 18-MAR-2008, sequence version 1. DT 27-MAY-2015, entry version 46. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABY94359.1}; GN OrderedLocusNames=Teth39_0697 {ECO:0000313|EMBL:ABY94359.1}; OS Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) OS (Clostridium thermohydrosulfuricum). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Thermoanaerobacter. OX NCBI_TaxID=340099 {ECO:0000313|EMBL:ABY94359.1, ECO:0000313|Proteomes:UP000002156}; RN [1] {ECO:0000313|Proteomes:UP000002156} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33223 / 39E {ECO:0000313|Proteomes:UP000002156}; 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 ----------------------------------------------------------------------- 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; ABY94359.1; -; Genomic_DNA. DR RefSeq; WP_012269136.1; NC_010321.1. DR RefSeq; YP_001664695.1; NC_010321.1. DR ProteinModelPortal; B0K7W0; -. DR STRING; 340099.Teth39_0697; -. DR EnsemblBacteria; ABY94359; ABY94359; Teth39_0697. DR KEGG; tpd:Teth39_0697; -. DR PATRIC; 23886014; VBIThePse6203_0731. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; TPSE340099:GH4W-718-MONOMER; -. DR Proteomes; UP000002156; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002156}; KW Methyltransferase {ECO:0000313|EMBL:ABY94359.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002156}; KW Transferase {ECO:0000313|EMBL:ABY94359.1}. SQ SEQUENCE 807 AA; 88155 MW; F1FFC3822A63FBB4 CRC64; MLDIFKELSN RVIVFDGAMG TQLQERGLKT GECPEYMNIT HPEVVFDIHR SYIEAGADVI ETNTFGANRI KLAKYGLENE VFNIVTQAVK IAKEASKDKP VALSIGPIGE LLTPYGDMTF DEAYDVFKEV VIAAERAGAD IVLIETMSDM LEAKAAILAA KENSNMKVIC TMTFQEDGRT LMGSDPITVV VSLQGLGLDA IGVNCSTGPD KMVSVVEKMS QVSRIPIIAQ PNAGMPVIRD GKTVYDLKPE EFASFFPLLV EKGASIVGGC CGTTPHYIKL VKKAVKDLKP KVKVNKFTAV ASNTKTVFIG ENYLLRVIGE RINPTGKKKL SEAFLAGNVS LAVEEAIKQQ KCGAEILDVN VGVPGVNEEE LLPKVVSEIQ NVVDIPLQID STNIKAVEKA IRILRGRPII NSVSAKEESL KEVLPIVKKY GACVVGLTVG DKGLPKDRHE RIENAKKIIK KAEEYGIPKE DILIDCIVLT VSSEQEAAIE TLEAIKLAKE ELGVNTVVGL SNVSFGLPER RLINSTFLAM AASYGLTTAI INPCDEAMMD TLRASMVLLN KDKGSVNYLK IYGNRQKEEG KEKEQQKIQE EDLKSKFYIQ ILEGKKSGVE DIVKNILEEE VQPLSIVDNI IIPALKEVGD RYEKGIYFLP QLLSSAEVVQ SAFKIIKEKL PKGSVSKGKI ILATVEGDVH DIGKNIVKVL LENYGYDVID LGKDVKGEVI LEEVKRTGAP LVGLSALMTT TLFNMEKIIK LLKANTDVKI MVGGAVLTEE YAYKIGADYY GKTAQDAVKI ADKFFLKNAL LCKTCGI // ID B0KKH9_PSEPG Unreviewed; 1235 AA. AC B0KKH9; DT 18-MAR-2008, integrated into UniProtKB/TrEMBL. DT 18-MAR-2008, sequence version 1. DT 29-APR-2015, entry version 52. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABY97885.1}; GN OrderedLocusNames=PputGB1_1982 {ECO:0000313|EMBL:ABY97885.1}; OS Pseudomonas putida (strain GB-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=76869 {ECO:0000313|EMBL:ABY97885.1, ECO:0000313|Proteomes:UP000002157}; RN [1] {ECO:0000313|EMBL:ABY97885.1, ECO:0000313|Proteomes:UP000002157} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GB-1 {ECO:0000313|EMBL:ABY97885.1, RC ECO:0000313|Proteomes:UP000002157}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000926; ABY97885.1; -; Genomic_DNA. DR RefSeq; WP_012271637.1; NC_010322.1. DR RefSeq; YP_001668221.1; NC_010322.1. DR ProteinModelPortal; B0KKH9; -. DR SMR; B0KKH9; 655-1235. DR STRING; 76869.PputGB1_1982; -. DR EnsemblBacteria; ABY97885; ABY97885; PputGB1_1982. DR KEGG; ppg:PputGB1_1982; -. DR PATRIC; 19930999; VBIPsePut76638_1987. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PPUT76869:GIXB-2043-MONOMER; -. DR Proteomes; UP000002157; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002157}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1235 AA; 135454 MW; 31B2D0EFC4ED7E1E CRC64; MSDRSARLQA LQNALKERIL ILDGGMGTMI QSYRLEEHDY RGTRFADWPS DVKGNNDLLL LSRPDVIAAI EKAYLDAGAD ILETNTFNAT QISQADYGME SLVYELNVEG ARIARQVADA KTLETPNKPR FVAGVLGPTS RTCSISPDVN DPGYRNVTFD ELVENYIEAT RGLIEGGADL ILIETIFDTL NAKAAIFAVQ QVFEDDNVEL PIMISGTITD ASGRTLSGQT TEAFWNSVRH AKPISVGLNC ALGAKDLRPY LEELSTKADT HVSAHPNAGL PNAFGEYDET PAEMAEVVEE FAASGFLNII GGCCGTTPGH IQAIAEAVAK YKPREIPEIA KACRLSGLEP FTIDRQSLFV NVGERTNITG SAKFARLIRE ENYTEALEVA LQQVEAGAQV IDINMDEGML DSQAAMVRFL NMIAGEPDIS RVPIMIDSSK WDVIEAGLKC IQGKGIVNSI SMKEGVEQFK HHARLCKRYG AAVVVMAFDE VGQADTAARK KEICKRSYDI LVNEVGFPPE DIIFDPNIFA VATGIEEHNN YAVDFIEACA YIRDHLPHAL SSGGVSNVSF SFRGNNPVRE AIHSVFLFHA IRNGLTMGIV NAGQLEIYDE IPAELREKVE DVVLNRTPEG TDALLAIADD YKGGGATKEV ENEAWRSLPV DKRLEHALVK GITAHIVEDT EECRQQCARP IEVIEGPLMS GMNVVGDLFG AGKMFLPQVV KSARVMKQAV AHLIPFIEAE KGDKPEAKGK ILMATVKGDV HDIGKNIVGV VLGCNGYDIV DLGVMVPAEK ILQTARDEKC DIIGLSGLIT PSLDEMVHVA REMQRQGFEL PLMIGGATTS KAHTAVKIEP KYSNDAVIYV TDASRAVGVA TQLLSKELKP GFVEKTRLEY VDVRERTANR SARTERLSYT QAIAAKPQYD WAGYQPVEPT FTGVKVLENI DLRTLAEYID WTPFFISWDL AGKFPRILTD EVVGEAATAL YQDAREMLDK LIDEKLISAR AVFGFWPANQ VADDDIEVYG EDGQTLATLH HLRQQTIKPD GKPNWSLADF VAPKASGVTD YVGGFITTAG IGAEEVAKAY QDKGDDYSSI MVKALADRLA EACAEWLHEQ VRKEHWGYAR DEHLDNEALI KEQYSGIRPA PGYPACPDHT EKETLFRLLD GTAIGETGPS GVFLTEHFAM FPAAAVSGWY FAHPQAQYFA VGKVDKDQIE RYSARKGQDV SVSERWLAPN LGYDS // ID B0LJ01_STRRH Unreviewed; 1133 AA. AC B0LJ01; DT 18-MAR-2008, integrated into UniProtKB/TrEMBL. DT 18-MAR-2008, sequence version 1. DT 27-MAY-2015, entry version 41. DE SubName: Full=Lct18 {ECO:0000313|EMBL:ABX71101.1}; GN Name=lct18 {ECO:0000313|EMBL:ABX71101.1}; OS Streptomyces rishiriensis. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=68264 {ECO:0000313|EMBL:ABX71101.1}; RN [1] {ECO:0000313|EMBL:ABX71101.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MJ773-88K4 {ECO:0000313|EMBL:ABX71101.1}; RA Zhang X.J., Alemany L.B., Fiedler H.-P., Goodfellow M., Parry R.J.; RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ABX71101.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MJ773-88K4 {ECO:0000313|EMBL:ABX71101.1}; RX PubMed=18070976; DOI=10.1128/AAC.00717-07; RA Zhang X., Alemany L.B., Fiedler H.P., Goodfellow M., Parry R.J.; RT "Biosynthetic investigations of lactonamycin and lactonamycin z: RT cloning of the biosynthetic gene clusters and discovery of an unusual RT starter unit."; RL Antimicrob. Agents Chemother. 52:574-585(2008). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; EU147298; ABX71101.1; -; Genomic_DNA. DR ProteinModelPortal; B0LJ01; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 205 205 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 271 271 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 272 272 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 715 715 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1133 AA; 123333 MW; 98CA7725976449FD CRC64; MGTMLQAQEP TLEDFQELEG CNEILNVTRP DIVRSVHEEY FEAGVDCVET NTFGANHAAL GEYGIADRVH ELSEAGARVA RQVADEFTER TGRQRWVLGS MGPGTKLPTL GHVSFGVLRD AYRRNAEGLL AGGVDALIVE TTQDLLQTKA AVLGARRAGA LAGVDVPLIV SVTVETTGTM LLGSEIGAAL TALEPLGIDM IGLNCATGPA EMTEHLRHLA RTARVPLACM PNAGLPVLGG DGATYPLGAS ELADAQADFV RDYGLSLVGG CCGTTPEHLR RLVERVRGVS PAERDPRPEP GAASLYQSVA FRQDTAYMAI GERTNANGSK KFREAMLEGR WDDCVEMARD QIREGAHMLD LCVDYVGRDG VADMDELAGR FATASTLPIV LDSTEVEVVR AGLERLGGRA VINSVNYEDG DGPESRFAKV TALAREHGAA LIALTIDEEG QARTVESKVA IAERLIEDLT GNWGIRESDI LIDCLTFTIC TGQEESRKDG VATIEAIREL KRRRPEVQTT LGLSNISFGL NPAARILLNS VFLDECVKAG LDSAIVHASK ILPIARFSEE EVATALDLIH DRRAEGYDPL QKLMALFEGA TAKSLKAGKA QELAALPLDE RLKRRIIDGE KNGLEADLAE ALRSRPALDI VNETLLDGMK VVGELFGSGQ MQLPFVLQSA EVMKTAVACL EPHMEKSDAE GKGTIVLATV RGDVHDIGKN LVDIILSNNG YNVVNLGIKQ PVSAILDAAR EHRADVIGMS GLLVKSTVIM KENLEELNQR KMAADYPVIL GGAALTRAYV EQDLHEIYQG EVRYARDAFE GLRLMDALIG VKRGVPGAKL PELKQRRVRA SVAAVEVEER PQEGHVRSDV ATDNPVPKPP FEGTRVVKGI QLKEYASWLD EGALFKGQWG LTKELIETEG RPRARGWLDR LHTENLLEAA VVHGYFPCVS KDDDLIVLDE QGNERTRFTF PRQRRGRRLC LADFFRPEES GETDVVGFQV VTVGSRIGEE TARLFASDSY RDYLELHGLS VQLAEALAEY WHARVRSELG IAGDDPDSLD GMFRSSYQGC RYSLGYPACP DLADRAKIAE LLEPERIGVH LSEEFQLHPE QSTDAIVVHH PDAGYFNAGG GRP // ID B0MEJ4_9FIRM Unreviewed; 784 AA. AC B0MEJ4; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EDR97382.1}; GN ORFNames=ANACAC_01989 {ECO:0000313|EMBL:EDR97382.1}; OS Anaerostipes caccae DSM 14662. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Anaerostipes. OX NCBI_TaxID=411490 {ECO:0000313|EMBL:EDR97382.1}; RN [1] {ECO:0000313|EMBL:EDR97382.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 14662 {ECO:0000313|EMBL:EDR97382.1}; 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] {ECO:0000313|EMBL:EDR97382.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 14662 {ECO:0000313|EMBL:EDR97382.1}; 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. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDR97382.1}. 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; ABAX03000013; EDR97382.1; -; Genomic_DNA. DR RefSeq; WP_006567470.1; NZ_DS499734.1. DR ProteinModelPortal; B0MEJ4; -. DR EnsemblBacteria; EDR97382; EDR97382; ANACAC_01989. DR PATRIC; 24506711; VBIAnaCac18038_1968. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDR97382.1}; KW Transferase {ECO:0000313|EMBL:EDR97382.1}. SQ SEQUENCE 784 AA; 85877 MW; 562DA29B763DB02E CRC64; MLLDRIGKEL LIFDGAMGTQ LQEAGLRAGD IPEELNIDRP ELIVSIHEKY LGAGADFITT NTFGCNELKM QESKYEYRDM LRAAVSNANE ARKNAGREQD AYIVLDIGPI GQLLEPMGTL TFDEAYDIIL SQVETVKHDV DAVLFETMSD LYEVKAGILA VKENTSLPVF VTMTFEQNGR TLSGNDPVTF VNTVQGLGAD MLGVNCSLGP AELGPIIEEI LSVSSVPVMI QPNAGLPCLE HGETHYHVTS DEYAELMQGY LKDGISAAGG CCGTTPEFIR KLKAASPKKA APRKIEKKTR VSSQTKTVTF GDRVIVCGER LNPTGKKKLK LALKEERYDE LVSEAIKQDE AGADVLDVNV GLPGIDEPET MKHVVKLLQE VITLPLQIDS SNARAIELAC RYYNGKPLIN SVNGKDEVME AIFPIVKKYG GVVIGLTLDE GIPLKAEERF EIAQKIIAKA AEYGIGKEDI IIDCLTLTAS AQQKEVKETL KAIEMVKKLG VHTVLGVSNV SFGLPNRPLL NRTFLALAMQ AGLDLPIINP LDKELMGTID AFHVLFYKDI DSESYIRNQS NAAETKAAVQ TEFSLHDIIL HGLKDEVEAK TREELEKKEP LVLINEVIIP ALNVVGKDYE TGKIFLPQLI QSAETTKKAF EVVKQCFTAD AGEEKGPVVM ATVEGDIHDI GKNIVKVVLE SYGYRIIDLG KDVKIEKVVE AWKKYQPKAI GLSALMTTTV ISMEKTIQRL REEDCSCPIW VGGAVLTEDI ANSIGADYYA EDAMASVALL EKLI // ID B0MM61_9FIRM Unreviewed; 414 AA. AC B0MM61; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EDS01244.1}; GN ORFNames=EUBSIR_00915 {ECO:0000313|EMBL:EDS01244.1}; OS [Eubacterium] siraeum DSM 15702. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminiclostridium. OX NCBI_TaxID=428128 {ECO:0000313|EMBL:EDS01244.1}; RN [1] {ECO:0000313|EMBL:EDS01244.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 15702 {ECO:0000313|EMBL:EDS01244.1}; 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 (OCT-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EDS01244.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 15702 {ECO:0000313|EMBL:EDS01244.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDS01244.1}. 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; ABCA03000040; EDS01244.1; -; Genomic_DNA. DR RefSeq; WP_005355299.1; NZ_KB907526.1. DR ProteinModelPortal; B0MM61; -. DR EnsemblBacteria; EDS01244; EDS01244; EUBSIR_00915. DR PATRIC; 30675547; VBIEubSir110241_1164. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDS01244.1}; KW Transferase {ECO:0000313|EMBL:EDS01244.1}. SQ SEQUENCE 414 AA; 44936 MW; 26F17C9A66D62EFE CRC64; MDSNPVSQDI PIRLPILLDG GTGTGLEKYG YDHTVSTAQF VCANPEALIE LQQGFLDAGS QILYTATHGA NCENLKAYGV EDKTEQLNAA AAKITYDSFH EKALIAGCLS STGLYIEPYG DYTFTEIMSV YRQQVKALSP YCDMFVIETV PALWNMRAAV LACKKENKPI IATMKVDEDG ETAIGTNVLC TLLVLQAMGI SAFGLNCTSA DLCPDIISEI APYAKIPLIV KPSAVYEQDG ERQSISPEEF AFAVKKSVLS GAEIAGGCCG TGKEHIAALR EMFASLDASE INPVEKQDTS LALATENQMF FLDPETTEFS PAVECGPYME DDIAQMCGES YDVLTVSINS PDDAIDFGRN MHMATLPVAF LSDDEISLKM ALMLYQGRAI IDRKSLIEPE KLEAMAEKYG AVLY // ID B0MQG9_9FIRM Unreviewed; 790 AA. AC B0MQG9; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 31. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EDS00148.1}; GN ORFNames=EUBSIR_02085 {ECO:0000313|EMBL:EDS00148.1}; OS [Eubacterium] siraeum DSM 15702. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminiclostridium. OX NCBI_TaxID=428128 {ECO:0000313|EMBL:EDS00148.1}; RN [1] {ECO:0000313|EMBL:EDS00148.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 15702 {ECO:0000313|EMBL:EDS00148.1}; 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 (OCT-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EDS00148.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 15702 {ECO:0000313|EMBL:EDS00148.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDS00148.1}. 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; ABCA03000051; EDS00148.1; -; Genomic_DNA. DR RefSeq; WP_005357151.1; NZ_KB907518.1. DR ProteinModelPortal; B0MQG9; -. DR EnsemblBacteria; EDS00148; EDS00148; EUBSIR_02085. DR PATRIC; 30676983; VBIEubSir110241_1867. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDS00148.1}; KW Transferase {ECO:0000313|EMBL:EDS00148.1}. SQ SEQUENCE 790 AA; 84881 MW; 213F389EE44C3743 CRC64; MEIKTLLEQR GLLIFDGAMG TQLQAKGLKT GETPELLNLT AKDLLKEIHR SYIDAGADII SANTFGANSY KLSHSGKSVD EIITAGIINC KEAIKESGKD VFCALDIGPI GQLLEPTGSL KFEEAYDIFR EEIVAGYKAG ADVVLFETMT DLYELKAAIL AAKENCDLPI ICSMTFEENG RTFTGCPAEA EILLCEGLGV SAVGVNCSLG PKELMPIIKT LCEKSKIPVI VMPNAGLPDP ATGEYSIDAE EFSDYAVEIA DLGAGIIGGC CGTTPEFIRR TAEKVKGRKY ESKKIERVCT ICSGTNVVEV SQPRIIGERI NPTGKKLFKQ ALINDDIDYI LGQAIEQVGA GADILDVNVG LPDIDEKAMM IKAVKSIQGV TNVPLQIDST IPEVLEAALR VYNGKPMVNS VNGEEESLKN VLPLVKKYGA AVVGLTLDKD GIPPKAEQRV AIAEKIIKRC EKIGIPKEDI AIDCLTLTAS AEQLAVNETL KAVRAVKERF GVRTVLGVSN ISFGLPNREL LNHIFLTMAL ENGLDLPIIN PNVASMTGAV RAFKLLKAID VNSVEYIAAY GSDTPTAVAK PKSSEVTLEY AIDNGLKADA AKITEQLLID TDPMVIINER LIPALDKTGT LFEQGKIFLP QLILSAGVAQ SCFDVIKAHL AKNNSETVSK GKIVLATVKG DVHDIGKNIV KVLLENYGYT VIDLGKDVEY QAVVDAARKH EVKLVGLSAL MTTTLKSMEE TIKLIRDNGL PCKVVVGGAV LTPEYAEKIG ADFYAKDAKE TVDIAKKVIG // ID B0N048_9BACT Unreviewed; 1211 AA. AC B0N048; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EDS03234.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EDS03234.1}; GN Name=metH {ECO:0000313|EMBL:EDS03234.1}; GN ORFNames=ALIPUT_02775 {ECO:0000313|EMBL:EDS03234.1}; OS Alistipes putredinis DSM 17216. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Rikenellaceae; OC Alistipes. OX NCBI_TaxID=445970 {ECO:0000313|EMBL:EDS03234.1}; RN [1] {ECO:0000313|EMBL:EDS03234.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17216 {ECO:0000313|EMBL:EDS03234.1}; 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 (OCT-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EDS03234.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17216 {ECO:0000313|EMBL:EDS03234.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EDS03234.1}. 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; ABFK02000020; EDS03234.1; -; Genomic_DNA. DR RefSeq; WP_004328825.1; NZ_DS499577.1. DR ProteinModelPortal; B0N048; -. DR SMR; B0N048; 647-891. DR EnsemblBacteria; EDS03234; EDS03234; ALIPUT_02775. DR PATRIC; 24452112; VBIAliPut4767_1076. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EDS03234.1}; KW Transferase {ECO:0000313|EMBL:EDS03234.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 755 755 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1211 AA; 133830 MW; 0FE58D58717214EE CRC64; MTKNRDIRHE LEHRILLLDG GFGTMIQQYG LDEADYRGKE FAASEKLLRG CNDLLNLTRP ETIREIHEKY LQAGSDVITS NTFNANSISL ADYGLAAEAY RINRVGAAIA REAADAFTAR NPQKPRFVGG SMGPTSHTLS MSADVDNPGA RAFTFEQLSQ AYYDQARGLM DGGVDLLMLE TVFDALNAKA AIFAIESLFA ERGMRLPVIV SGTLTSSGRT LAGQTIEAFY TSVAHAEPLA VSLNCSFGAK ALLPYLERLA AVSEFRVAVY PNAGLPNVMG GYDETPAMFA ADVEEYMRRG LVNLVGGCCG TTPLHIFELA KIVNNYAPRP LPQRRHVTCL SGLEQLRIVP EANFVNVGER TNVAGSAKFA RLIREKNYEE ALSVARAQVE AGAQIVDVCM DDGLIDGPEA MRDFLNLMGS EPEIAAVPVM IDSSKWEVLE TGLRVVQGKS VVNSISLKEG KQEFLHRARL IRRYGAAAVV MLFDEQGQAD TYARKIEVAQ RAYKLLTDDG FPAEDIIFDP NILAVATGIE AHDAYARDFI EAVRWIKQNL PHAKISGGVS NLSFAFRGNN AVREAMHSVF LYHAIQAGMD MAIVNPQMLQ IYSDIEPELL ERVEDVILCR RADAAERLTE YASQFTKTAA TQTQHTDAWR SEPLGKRIEY AMLKGVADYI EQDALEGYRT LGSPLAVIDR LLMPAMEVVG NLFGQGKMFL PQVVKTARVM KKAVAVLTPY IEQGSEANAK SAGKVLVATV KGDVHDIGKN IVAVVMACNG YTIRDLGVMV ECPRIIDEAV AWGADAICLS GLITPSLEEM IHVCEELERR GLQIPVLIGG ATTSDVHTAV KIAPTYSGPV IHADNASRNN KILGELLGPG REEYLARVRE EQQTLRDQYR RREEIRTILP FGQVRKLRVP KPASEIAVPA HTGRLVFPDI SIADVEPLID WNFFFPAWGL KGRVPEIFEN PEHGAEARKL YDDAQKMLAR IREEKLLTLQ GVAGIFAAVS RGDDIVVTGP KDKKYILPML RSQAPVREAQ ARCLADFIAD EKAGRTDYIG AFALTGGIGL KELTEKFRAE GDDYNAILSK LLADRLTEAL CEWVHIFIRR QMWGYETGPA LTPEQIIRSK YRGRRMAFGY PACPDHSLKR EVFDLLAADK TTAMRLNDNY MITPEEALCG LFFADAEYFS VGRIDREQLA DYAARRNMDI ETIEKLIPNN I // ID B0N2P4_9FIRM Unreviewed; 784 AA. AC B0N2P4; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 34. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EDS19337.1}; GN ORFNames=CLORAM_01335 {ECO:0000313|EMBL:EDS19337.1}; OS Erysipelatoclostridium ramosum DSM 1402. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae; Erysipelatoclostridium. OX NCBI_TaxID=445974 {ECO:0000313|EMBL:EDS19337.1}; RN [1] {ECO:0000313|EMBL:EDS19337.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 1402 {ECO:0000313|EMBL:EDS19337.1}; 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] {ECO:0000313|EMBL:EDS19337.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 1402 {ECO:0000313|EMBL:EDS19337.1}; 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. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDS19337.1}. 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; ABFX02000004; EDS19337.1; -; Genomic_DNA. DR RefSeq; WP_003536636.1; NZ_DS499655.1. DR ProteinModelPortal; B0N2P4; -. DR EnsemblBacteria; EDS19337; EDS19337; CLORAM_01335. DR PATRIC; 27221585; VBICloRam24443_1286. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDS19337.1}; KW Transferase {ECO:0000313|EMBL:EDS19337.1}. SQ SEQUENCE 784 AA; 85452 MW; E5134BF302724244 CRC64; MLQERLKNDI LVFDGAMGTQ LQDAGLKAGD IPECLNITDP KLIQTIHLNY LNAGADFITT NTFGANPLKM AEAPYSYEEI INAAIDNATI ARKTADRQND SYIVLDIGPI GQLLEPMGTL TFDEAYEIIK KQVIIAKDKV DAVLLETMTD IYEVKAGILA VKENSDLPVF VTMTYENNLR TLSGCDPLTM VNVLEGLNVD VLGVNCSLGP IELTPIIDQI LAAATIPVLL QPNAGLPCLV EGKTCYNMDK ETFVQESLKH VKNGVAIIGG CCGTTPDFIA SLKNNLPVRK KITPKRATRV SSGTKTVEFG HHVVVCGERL NPTGKKKLKL ALKEERYDEL VVEAIKQDQA GAHVLDVNVG LPGINEVATM KHVIKLLQEV ISLPLQIDSS VPGAIEQACR YYNGKPLINS VNGKDETMDA IFPIVKKYGG VVIGLTLDEN GIPPLAKDRY KIAKKIINKA ASYGITKENI IIDCLVLTVS AQQKEVMETV KAVAMVKELG VHTVLGVSNV SFGLPNRPLL NKTFLAMAMS AGLDLPIINP MDQELMATID AFNVLYNYDH DAAVYIERRA NQETITKKDT STFTLNDIVL HGLKDEVTNA TKELLKTTPG LEIINNILIP ALDTVGKQYE KNIIFLPQLI QSAETSKIAF GIIKDTFKDT AATKGPIIMA TVHGDIHDIG KNIVKVVLES YGYKVIDLGK DVPPETVVEA FHKHHPKAIG LSALMTTTVV SMAKTIELLK QIDNICPIFV GGAVLTADYA KEINADYYSK DAMEAVELLN KIIK // ID B0NAH0_CLOSV Unreviewed; 795 AA. AC B0NAH0; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 30. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EDS08128.1}; GN ORFNames=CLOSCI_00439 {ECO:0000313|EMBL:EDS08128.1}; OS [Clostridium] scindens ATCC 35704. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=411468 {ECO:0000313|EMBL:EDS08128.1}; RN [1] {ECO:0000313|EMBL:EDS08128.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35704 {ECO:0000313|EMBL:EDS08128.1}; 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] {ECO:0000313|EMBL:EDS08128.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35704 {ECO:0000313|EMBL:EDS08128.1}; 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. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDS08128.1}. 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; ABFY02000009; EDS08128.1; -; Genomic_DNA. DR RefSeq; WP_004605991.1; NZ_DS499697.1. DR ProteinModelPortal; B0NAH0; -. DR EnsemblBacteria; EDS08128; EDS08128; CLOSCI_00439. DR PATRIC; 27227646; VBICloSci136883_1135. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDS08128.1}; KW Transferase {ECO:0000313|EMBL:EDS08128.1}. SQ SEQUENCE 795 AA; 86486 MW; CC9F1A42FC4414D0 CRC64; MILERLGKEL LYFDGGMGTL LQSKGLKPGE LPEVWNIEHA DEVVDIHRQY FEAGSDIVLA NTFGANALKF HDASYDLKEI VNAAIENVKK GASLGADAGR RTYTALDVGP TGKLLKPMGD LGFEDAYEAF REVMKYGEEA GADLIHIETM SDTYEVKAAV LAAKETTDLP VFATMIFDEK GKLLTGGDVP SVVALLEGLR VDALGINCGM GPEQMLPILE EILAYTSLPV IVKPNAGLPK QKDGQVYYDV DPDQFAQTME KIVHMGACVI GGCCGTTPGH IRAMVERTKG LSVILPSHKD LTIVSSYGKA VMLGEKPVII GERINPTGKK KFKQALKDHD LDYILKEGIT QQDKGAHILD VNVGLPDIDE AAMMQEVVTQ LQSVTSLPLQ IDTVDAKAME TAMRIYNGKP MVNSVNGKKE SMDEVFPLIR KYGGVVIGLT IDEDGIPQTA EGRVKVAGKI IEEAGKYGID KKDIVIDVLA MTISSEPEGA KVTLDALKGV REAYGVRTVL GVSNISFGLP YRPAINSNFY TMAMQNGLSA GIINPSSEDM MRSYYSFLAL MNYDSNCEAY IRQYGSQPVP PAASSGSRMT LKEAIEKGLK EEAHHATRTL LKEQEPLSII NQYLIPALDV VGKGFEKGTI FLPQLLMSAD AAKIAFAVLK DELAKSGGDM EKKDKIILAT VKGDIHDIGK NIVKVLLENY SFDVIDLGKD VPPKTIVETA IKEEVSLVGL SALMTTTVTS MEETIRLLRK HKPDCKVMVG GAVLNQDYAD MIGADFYGKD AMQSVYYAQR FFGHE // ID B0NQS8_BACSE Unreviewed; 918 AA. AC B0NQS8; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 39. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EDS15227.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EDS15227.1}; GN Name=metH {ECO:0000313|EMBL:EDS15227.1}; GN ORFNames=BACSTE_01728 {ECO:0000313|EMBL:EDS15227.1}; OS Bacteroides stercoris ATCC 43183. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=449673 {ECO:0000313|EMBL:EDS15227.1}; RN [1] {ECO:0000313|EMBL:EDS15227.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43183 {ECO:0000313|EMBL:EDS15227.1}; 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] {ECO:0000313|EMBL:EDS15227.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43183 {ECO:0000313|EMBL:EDS15227.1}; 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. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EDS15227.1}. 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; ABFZ02000019; EDS15227.1; -; Genomic_DNA. DR RefSeq; WP_005654757.1; NZ_DS499673.1. DR ProteinModelPortal; B0NQS8; -. DR SMR; B0NQS8; 653-897. DR EnsemblBacteria; EDS15227; EDS15227; BACSTE_01728. DR PATRIC; 27169238; VBIBacSte95829_1501. DR GO; GO:0000786; C:nucleosome; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000558; Histone_H2B. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SMART; SM00427; H2B; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EDS15227.1}; KW Transferase {ECO:0000313|EMBL:EDS15227.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 238 238 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 301 301 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 302 302 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 762 762 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 918 AA; 100816 MW; 90F2190213C1D270 CRC64; MLVRERILIL DGAMGTMIQQ YNLTEDDFRG KRFAQIPGQL KGNNDILCLT RPDVIRDIHR KYLVAGADII ETNTFNSTSV SMADYHVQEY VREINFAAVK LAREVADEFT VLTPDKPRFV AGSIGPTNKT CSMSPDVNNP AFRALTYDEL AAAYREQMEA MLEAGVDALL IETIFDTLNA KAAIYAAEQA MEAIGVRVPL MLSVTVSDIG GRTLSGQTLE AFLASVQHAD IFSVGLNCSF GARQLKPFLE QLAARAPYYI SAYPNAGLPN SLGTYDQTPA EMADEIREYI HEGLVNIIGG CCGTTDEYIA AYSSLIVGAV PRIPASLPDN LWLSGLELLE VKPENNFINV GERCNVAGSR KFLRLINEKK YDEALSIARQ QVEDGAQIID INMDDGLLDA EKEMTTFLNL ITSEPEIARV PVMIDSSKWD VIVAGLKCMQ GKSIVNSISL KEGEEKFLEH ARTIKRYGAA AVVMAFDEQG QADTYERRIE VCERAYRLLV DRGGFNPQDI IFDPNVLAVA TGMDEHNNYA VDFIRATGWI RKNLPGAHVS GGVSNLSFSF RGNNYIREAM HAVFLYHAIR EGMDMGIVNP ATSVLYTDIP ADILERIEDV VLNRRSDAAE RLIETAERLK AEAEAAKSSL SNGNSQLSSF SSQLAWREDT VEERLKYALT KGIGDYLEED LAEALKVYPK AVDIIEGPLM AGMNHVGDLF GAGKMFLPQV VKTARTMKKA VAVLQPVIES EKQEGAASAG KVLLATVKGD VHDIGKNIVS VVMACNGYEI IDLGVMVPAE TIVQRAIEEK VNMIGLSGLI TPSLDEMVHV AIELEKAGLD VPLLIGGATT SPLHTALKIA PVYHAPVIHL KDASQNATVA ARLMNPNQKE EFVKKLSNKY QQLREKNQEK QVETVSLEEA KANRLNLF // ID B0NWZ7_9CLOT Unreviewed; 319 AA. AC B0NWZ7; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EDS23189.1}; GN ORFNames=CLOSS21_00190 {ECO:0000313|EMBL:EDS23189.1}; OS Clostridium sp. SS2/1. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=411484 {ECO:0000313|EMBL:EDS23189.1}; RN [1] {ECO:0000313|EMBL:EDS23189.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SS2/1 {ECO:0000313|EMBL:EDS23189.1}; 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] {ECO:0000313|EMBL:EDS23189.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SS2/1 {ECO:0000313|EMBL:EDS23189.1}; 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. {ECO:0000313|EMBL:EDS23189.1}. 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; ABGC03000011; EDS23189.1; -; Genomic_DNA. DR RefSeq; WP_008391814.1; NZ_DS547006.1. DR ProteinModelPortal; B0NWZ7; -. DR EnsemblBacteria; EDS23189; EDS23189; CLOSS21_00190. DR PATRIC; 27254296; VBICloSp52530_0774. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDS23189.1}; KW Transferase {ECO:0000313|EMBL:EDS23189.1}. SQ SEQUENCE 319 AA; 35800 MW; 7A4FEC6221A43F41 CRC64; MMKNSIENII KENKIMVIDG SMSTPLENRG VSLNSKLWTA KILAEQPELI KQVHKNYFKA GADCGITCSY QASIPGLMEN GYTLEEAENL IRSAVKIFCE ARDEWWEEEG REARRAWPLC LGAAGPYGAY LADGSEYRGN YGITDEQLKE FHKRRVELLH EAGADIILFE TVPSLKEAKV EAEIAEEYGY DYWISFSCLS ENIICEGTPI AECATTFAKG YPHLKMIGVN CTKPEYITGL IHKIKENCDI PIGVYPNSGE EYDAVKKVWF GKQSALSFEQ YAYNYMKSGA SAVGGCCTTV AKHVEEVVRA KKRFSEEQK // ID B0NXP4_9CLOT Unreviewed; 791 AA. AC B0NXP4; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 33. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EDS23031.1}; GN ORFNames=CLOSS21_00445 {ECO:0000313|EMBL:EDS23031.1}; OS Clostridium sp. SS2/1. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=411484 {ECO:0000313|EMBL:EDS23031.1}; RN [1] {ECO:0000313|EMBL:EDS23031.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SS2/1 {ECO:0000313|EMBL:EDS23031.1}; 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] {ECO:0000313|EMBL:EDS23031.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SS2/1 {ECO:0000313|EMBL:EDS23031.1}; 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. {ECO:0000313|EMBL:EDS23031.1}. 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; ABGC03000018; EDS23031.1; -; Genomic_DNA. DR RefSeq; WP_008392153.1; NZ_DS547011.1. DR ProteinModelPortal; B0NXP4; -. DR EnsemblBacteria; EDS23031; EDS23031; CLOSS21_00445. DR PATRIC; 27254775; VBICloSp52530_1009. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDS23031.1}; KW Transferase {ECO:0000313|EMBL:EDS23031.1}. SQ SEQUENCE 791 AA; 86556 MW; CF2CEBDABBF04460 CRC64; MLQNRLGKEL LIFDGAMGTQ LQNAGLSAGD IPEELNIDRP DLLRSIHKNY LKAGADFITT NTFGCNRLKM EEAKYEAKDM LLAAVENARV ARTEAGREDD SYIVLDIGPI GQLLEPMGTL TFDEAYDIIL EQVETVKDQV DLVLFETMSD LYEVKAGVLA VKEHTDLPVF VTMTFEQNGR TLSGNDPETF INVAEGLGVD ALGVNCSLGP DELKPIIDEI LEKASIPVML QPNAGLPCLE HGETHYHVTP EEYVESMKDY MARGAAIVGG CCGTTPEFIG KLAEAAPKAV AERTVEKKTR VSSQTQTVTF GDHVIVCGER LNPTGKKKMK KALLEERYDE LVVEAVKQVE AGAEVLDVNV GLPGIDEPET MKRVVRLLQE VVTLPLQIDS SEADAIENAC RYYNGKPLIN SVNGKDEVME KIFPIAKKYG GVVIGLTLED GIPLKAEERF EIAKKIVNKA AEYGIGKENI IIDCLTLTAS AQQKEVKETL RAIKMVKKEL GVNTVLGVSN VSFGLPNRPL LNRTFLALAM EAGLDLPIIN PLDAELMGTI DAFHVLFYKD VDSQTYIKNQ SKDKETKPAA AAATTNFTLK DVIIHGLKDE VEKVTKEELK DKEALTVINE VIIPALNIVG KDYETGKIFL PQLIQSAETT KKAFEVVKET FSANDGEEKG PIIIATVEGD IHDIGKNIVK VVLESYGYKI IDLGKDVKVE KVVEAYKKYK PKAIGLSALM TTTVASMERT IKALHEAGCS EPIWVGGAVV TEDIAHNIGA DYYTEDAMAA VNLLENEILI L // ID B0PF81_9FIRM Unreviewed; 582 AA. AC B0PF81; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 34. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=ANACOL_03460 {ECO:0000313|EMBL:EDS10014.1}; OS Anaerotruncus colihominis DSM 17241. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Anaerotruncus. OX NCBI_TaxID=445972 {ECO:0000313|EMBL:EDS10014.1}; RN [1] {ECO:0000313|EMBL:EDS10014.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17241 {ECO:0000313|EMBL:EDS10014.1}; 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] {ECO:0000313|EMBL:EDS10014.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17241 {ECO:0000313|EMBL:EDS10014.1}; 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. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDS10014.1}. 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; ABGD02000025; EDS10014.1; -; Genomic_DNA. DR RefSeq; WP_006876322.1; NZ_DS544186.1. DR ProteinModelPortal; B0PF81; -. DR EnsemblBacteria; EDS10014; EDS10014; ANACOL_03460. DR PATRIC; 24516029; VBIAnaCol135235_2990. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EDS10014.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EDS10014.1}. SQ SEQUENCE 582 AA; 62207 MW; F07F666CC847A606 CRC64; MHFDRPFLFD GAFGTYYFSK TGDEAPCELA NLTAPQTVLD IHREYAASGC AALKTNTFAA NPVSIPDSVR LNEVIAAGWS LAQRAAQENG ARVFADIGGI CADTAEADYL TVVRHFLELG AQNFLFETLA CYQDVQRAVG LIRQSVPDAT VIVSFAVSQD GYSRRGLYCR ALFDQAESDP QVDAVGLNCS CGPSHMRSLL RALGQRVKPV AAMPNAGYPS SLNGRVFFED NAGYFAQQLS ALYMDGADIL GGCCGTTPQH IRCAAAALAA AAARPKGTGQ PKPQAASATG AGAPGGGRLG LPRKEIAVEL DPPFDHDCSF VLAAASELRA CGVDLITVTD SPLSRTRADS LMTAAKIRRE AGIEVMPHIS CRDKNHIALR AGLLGAAFEG IGRVLIVTGD PPMQAGTRGS DGVYHLSSYD LIAWIHSMNS EVFADAPFLI GGALNVNAAN FDAELARAKK KLSLGASMLF TQPIFSDKAV DHFLRARQEL KDCRLFAGIL PVAGYKNALF LINEVSGIEI PDNVVRSLEG KTPDEAAAIS VAYSAGIMRR VYDAADGFYI MTPLKKVNIV RGLIEEIRRY EQ // ID B0PG09_9FIRM Unreviewed; 406 AA. AC B0PG09; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EDS09597.1}; GN ORFNames=ANACOL_03741 {ECO:0000313|EMBL:EDS09597.1}; OS Anaerotruncus colihominis DSM 17241. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Anaerotruncus. OX NCBI_TaxID=445972 {ECO:0000313|EMBL:EDS09597.1}; RN [1] {ECO:0000313|EMBL:EDS09597.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17241 {ECO:0000313|EMBL:EDS09597.1}; 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] {ECO:0000313|EMBL:EDS09597.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17241 {ECO:0000313|EMBL:EDS09597.1}; 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. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDS09597.1}. 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; ABGD02000027; EDS09597.1; -; Genomic_DNA. DR RefSeq; WP_006876598.1; NZ_DS544188.1. DR ProteinModelPortal; B0PG09; -. DR EnsemblBacteria; EDS09597; EDS09597; ANACOL_03741. DR PATRIC; 24516555; VBIAnaCol135235_3249. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDS09597.1}; KW Transferase {ECO:0000313|EMBL:EDS09597.1}. SQ SEQUENCE 406 AA; 43516 MW; 0AF27A6D70508DDF CRC64; MTTDQNGRLR LPLLLDGATG TEYMKAGLPS GVCVEQWAAE HPDVVARVAR GYADAGSDIV YAPTFLANAG NLKNYGLSEQ VIPLNRKIVS TVKQALAGRD VLVAGDMSTT GLMCEPFGET EFVHLIGIYA EQASALADAG AELLVIETMS ALSECRAAVI AARQTGLPVF LTMTVDAEGR TMWGDDVLAS MIVLQDMGIS AFGLNCSQGP DDMVPLFERI APYAKLPLIA KPNAGEPPLS PVQFCDKCAR LMRRGVKIIG GCCGTTPEYV SALRHMIDSF DIGRVNIAPA GYDILAAGRN VYYLDNDLEY SKPIACEIDM ADALLEASHE SCDAVLIHLD TPDDGYRFSL NAHMVDMPVA FESESLEALD AALLHYNGKA LVVSTSCELE REVLEEVAAR YGAVVL // ID B0RCV4_CLAMS Unreviewed; 301 AA. AC B0RCV4; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 41. DE SubName: Full=Homocysteine s-methyltransferase {ECO:0000313|EMBL:CAQ03045.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:CAQ03045.1}; GN Name=mmuM {ECO:0000313|EMBL:CAQ03045.1}; GN OrderedLocusNames=CMS2974 {ECO:0000313|EMBL:CAQ03045.1}; 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 {ECO:0000313|EMBL:CAQ03045.1, ECO:0000313|Proteomes:UP000001318}; RN [1] {ECO:0000313|EMBL:CAQ03045.1, ECO:0000313|Proteomes:UP000001318} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / C-1 RC {ECO:0000313|Proteomes:UP000001318}; RX PubMed=18192393; DOI=10.1128/JB.01598-07; RA Bentley S.D., Corton C., Barron A., Clark L., Doggett J., Harris B., RA Ormond D., Quail M.A., Brown S.E., Knudson D., Francis D., RA Parkhill P., Ishimaru C.; 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; CAQ03045.1; -; Genomic_DNA. DR RefSeq; WP_012300194.1; NC_010407.1. DR RefSeq; YP_001711603.1; NC_010407.1. DR ProteinModelPortal; B0RCV4; -. DR STRING; 31964.CMS_2974; -. DR EnsemblBacteria; CAQ03045; CAQ03045; CMS2974. DR KEGG; cms:CMS_2974; -. DR PATRIC; 21462985; VBIClaMic4666_3027. DR eggNOG; COG2040; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; CMIC31964:GJBN-2968-MONOMER; -. DR Proteomes; UP000001318; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001318}; KW Methyltransferase {ECO:0000313|EMBL:CAQ03045.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001318}; KW Transferase {ECO:0000313|EMBL:CAQ03045.1}. SQ SEQUENCE 301 AA; 31372 MW; 218F83E3262D0F70 CRC64; MTRPRPLPNR PLVLDGGLGT LLEARGHDLS DPLWSARVLA DEPDAVRAAH AEYFRAGADV AITASYQVGF EAFAARGLSA AETEELLRAS VRLAAEARDE VAQDDAPGAG RDRWIAASVG PYGATLGDGS EYAASSGLTR AELRRWHAPR FAVLADSGAD LLACETVPSL DEGRALVDLA RGSGASAWLA FTVQGGRLRS GEPMAEGFRL ANGADEIVAV GINCAHPEEV PAAIAAARGV TDRPVAVYPN SGERWDAVAR AWGGDPALPS VDAWIAAGAS IVGGCCRVGP DEIRRMRDAL G // ID B0RVQ3_XANCB Unreviewed; 379 AA. AC B0RVQ3; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 46. DE SubName: Full=MetH1 protein {ECO:0000313|EMBL:CAP52121.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAP52121.1}; GN Name=metH1 {ECO:0000313|EMBL:CAP52121.1}; GN OrderedLocusNames=xcc-b100_2760 {ECO:0000313|EMBL:CAP52121.1}; OS Xanthomonas campestris pv. campestris (strain B100). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=509169 {ECO:0000313|Proteomes:UP000001188}; RN [1] {ECO:0000313|EMBL:CAP52121.1, ECO:0000313|Proteomes:UP000001188} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B100 {ECO:0000313|EMBL:CAP52121.1, RC ECO:0000313|Proteomes:UP000001188}; RX PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013; RA Vorholter F.J., Schneiker S., Goesmann A., Krause L., Bekel T., RA Kaiser O., Linke B., Patschkowski T., Ruckert C., Schmid J., RA Sidhu V.K., Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., RA Niehaus K., Puhler 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 ----------------------------------------------------------------------- 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; CAP52121.1; -; Genomic_DNA. DR RefSeq; WP_012438707.1; NC_010688.1. DR RefSeq; YP_001904165.1; NC_010688.1. DR ProteinModelPortal; B0RVQ3; -. DR STRING; 509169.xccb100_2760; -. DR EnsemblBacteria; CAP52121; CAP52121; xcc-b100_2760. DR KEGG; xca:xccb100_2760; -. DR PATRIC; 24085445; VBIXanCam108527_2802. DR eggNOG; COG0646; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; XCAM509169:GHW4-2821-MONOMER; -. DR Proteomes; UP000001188; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001188}; KW Methyltransferase {ECO:0000313|EMBL:CAP52121.1}; KW Transferase {ECO:0000313|EMBL:CAP52121.1}. SQ SEQUENCE 379 AA; 40389 MW; CBE3983C597915BB CRC64; MTHLPIPSAE SSIPFSLPWL HPERAAKLTA ALRERILIID GAMGTMIQRH DLQESDYRGT RFAEGYDSAQ GHVHGAGCDH APQGHDLKGN NDLLLLSSPE IIAGIHRAYL DAGADLLETN TFNATSVSQA DYHLEHLVYE LNKAGAQVAR ACCDAVEALT PQKPRFVIGV LGPTSRTASI SPDVNDPGYR NTSFDALRET YREAIDGLID GGADTLMVET IFDTLNAKAA LYAIEEVFEA RGGRLPVMIS GTITDASGRT LSGQTAEAFY ASVAHGKPLS VGLNCALGAK ELRPHVETLS QIADAYVSAH PNAGLPNAFG EYDETPAEMA ETLREFAKSG LLNLVGGCCG TTPDHIRAIA EAVADLPPRQ LPNALEQAA // ID B0RW95_XANCB Unreviewed; 320 AA. AC B0RW95; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 38. DE SubName: Full=MmuM protein {ECO:0000313|EMBL:CAP52313.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:CAP52313.1}; GN Name=mmuM {ECO:0000313|EMBL:CAP52313.1}; GN OrderedLocusNames=xcc-b100_2952 {ECO:0000313|EMBL:CAP52313.1}; OS Xanthomonas campestris pv. campestris (strain B100). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=509169 {ECO:0000313|Proteomes:UP000001188}; RN [1] {ECO:0000313|EMBL:CAP52313.1, ECO:0000313|Proteomes:UP000001188} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B100 {ECO:0000313|EMBL:CAP52313.1, RC ECO:0000313|Proteomes:UP000001188}; RX PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013; RA Vorholter F.J., Schneiker S., Goesmann A., Krause L., Bekel T., RA Kaiser O., Linke B., Patschkowski T., Ruckert C., Schmid J., RA Sidhu V.K., Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., RA Niehaus K., Puhler 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 ----------------------------------------------------------------------- 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; CAP52313.1; -; Genomic_DNA. DR RefSeq; WP_012438832.1; NC_010688.1. DR RefSeq; YP_001904357.1; NC_010688.1. DR ProteinModelPortal; B0RW95; -. DR STRING; 509169.xccb100_2952; -. DR EnsemblBacteria; CAP52313; CAP52313; xcc-b100_2952. DR KEGG; xca:xccb100_2952; -. DR PATRIC; 24085818; VBIXanCam108527_2987. DR eggNOG; COG2040; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; XCAM509169:GHW4-3014-MONOMER; -. DR Proteomes; UP000001188; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001188}; KW Methyltransferase {ECO:0000313|EMBL:CAP52313.1}; KW Transferase {ECO:0000313|EMBL:CAP52313.1}. SQ SEQUENCE 320 AA; 33726 MW; CADDA0965F7EF924 CRC64; MTVVPRQPRA GAPFSDVLQR DGEVVLDGAL ATELEQRGCD LNDALWSARV LMEQPELIYQ VHRDYFAAGA QCAITASYQA TPQGFAARGL GLAQSQALIA RSVALAAQAR ADHLAAHPQA APLWVAGSVG PYGAYLADGS EYRGDYALPV AQMLDFHRPR IAALVDAGVD LLACETLPSA SEITALRLLL EEFPQVHAWF SFTLRDAAHL SDGTPLAQVI PALDACPQVV AVGINCIAIE QVTAALQSLA ALTSLPLVVY PNSGEHYDAS DKRWHAGTTV ACSLATQRAQ WHAAGARLIG GCCRTTPADI AALVAARTAG // ID B0SU32_LEPBP Unreviewed; 1250 AA. AC B0SU32; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 01-APR-2015, entry version 55. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABZ99716.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABZ99716.1}; GN Name=metH {ECO:0000313|EMBL:ABZ99716.1}; GN OrderedLocusNames=LEPBI_II0183 {ECO:0000313|EMBL:ABZ99716.1}; OS Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / OS Paris). OC Bacteria; Spirochaetes; Spirochaetales; Leptospiraceae; Leptospira. OX NCBI_TaxID=456481 {ECO:0000313|EMBL:ABZ99716.1, ECO:0000313|Proteomes:UP000001847}; RN [1] {ECO:0000313|EMBL:ABZ99716.1, ECO:0000313|Proteomes:UP000001847} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Patoc 1 / ATCC 23582 / Paris RC {ECO:0000313|Proteomes:UP000001847}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000787; ABZ99716.1; -; Genomic_DNA. DR RefSeq; WP_012476654.1; NC_010843.1. DR RefSeq; YP_001964580.1; NC_010843.1. DR ProteinModelPortal; B0SU32; -. DR SMR; B0SU32; 668-908. DR STRING; 456481.LEPBI_II0183; -. DR EnsemblBacteria; ABZ99716; ABZ99716; LEPBI_II0183. DR KEGG; lbi:LEPBI_II0183; -. DR PATRIC; 22354206; VBILepBif123590_3715. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; LBIF456481:GCM0-3618-MONOMER; -. DR Proteomes; UP000001847; Chromosome II. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001847}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABZ99716.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001847}; KW Transferase {ECO:0000313|EMBL:ABZ99716.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 264 264 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 327 327 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 328 328 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 776 776 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1250 AA; 139093 MW; 50E788C6D3AFD50E CRC64; MNLPNSIIHR NIMKFEYTNP SSKTLLKLLT ERILVLDGAM GTMIQRHSLE EDDFRGDRFK DWPCSIKGNN DVLAITRPDI IESVHLEYLE AGADIIETNT FSSNIVSQAD YKMESAVRDL NLAAVQCAKN AVAKYKEKTG KTEVFIAGSI GPTVKTASLS PDVNNPAFRA VTFDELVDCF YEQVSALLDG GVDLLLPETN IDTLNLKACI FAIEKVFEER KIRIPVVLSV TITDASGRTL SGQTGEAFYI SIKHAKPLAV GINCALGAGE MRPYIEEISR VADCYVSCYP NAGLPNAFGG YDQTPDEFGG WMKNFAEAGF LNIVGGCCGT TPAHIQAAKE AVTSIKPRPL REQPKLSAFA GLEPLKLTKD QGFINVGERN NVTGSPKFKK LILDGNFEEA VQVALQQVQA GANIIDINFD EALLDGEASM TKFLNLISGE PDIARVPFMI DSSKWSVLLA GLKCIQGKPI VNSISLKEGE EVFLNHARTI QRFGASAIVM AFDEQGQAAT RDEKVRICKR AYDLLVSKLD FDPTDIIFDP NILTVATGIE EHNNYAVDFI EATREIKKVC PGAKVSGGLS NISFSFRGNN PVREAMHSAF LYHAIQAGMD MAIVNAGMLE VYEQIPKDLL ELVEDVLLNR RPDATERLID AAGSFHGEAK VQKKDDVWRS GTVEERLTHA LVKGIDEFVT QDTEEARQSL AKPLDVIEGP LMNGMKVVGE LFGAGKMFLP QVVKSARVMK KAVAYLMPYM EEEKRNQKDE SKQAKFLIAT VKGDVHDIGK NIVGVVLACN NYEVIDLGVM VPCEKILETA KKENVAAIGL SGLITPSLDE MVYVAKEMER LEFKVPLLIG GATTSPAHTA VKIAEKYSQP VLHVMDASRV VNVMNSVLNP QTTKEYAKTV KEEQSRIREE FYSRENERNI LPIADAIQNK FKADWDSYTP PKPSFTGIKV FDDVTLKDLI PFIDWSPFFL AWELKGRYPQ ILKDPIIGKE ATSLYNDAQV ILNQMLENPN LKPRAVVGMF PAVSHGETVE IFSDENKSKS LGFYPMLRQQ TTKMSNQPNY SLADFVAPKE KNKNDYIGFF AVTAGHGIEE LAKTYEVKHD DYNSILVKAL ADRFAEAFAE YMHHKMREDW GFGKDEQLTT EDLIREKYRG IRPAPGYPAC PDHTEKRKIW KLLDVEKNAG IQLTESCAMW PASSVSGYYF SHPEARYFAI GKINEDQVDT YTKLKEMEKS EVERWLSPIL NYDPSRKSKG // ID B0T507_CAUSK Unreviewed; 358 AA. AC B0T507; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 44. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABZ72534.1}; GN OrderedLocusNames=Caul_3407 {ECO:0000313|EMBL:ABZ72534.1}; OS Caulobacter sp. (strain K31). OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Caulobacter. OX NCBI_TaxID=366602 {ECO:0000313|EMBL:ABZ72534.1, ECO:0000313|Proteomes:UP000001316}; RN [1] {ECO:0000313|EMBL:ABZ72534.1, ECO:0000313|Proteomes:UP000001316} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K31 {ECO:0000313|EMBL:ABZ72534.1, RC ECO:0000313|Proteomes:UP000001316}; 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; ABZ72534.1; -; Genomic_DNA. DR RefSeq; WP_012287431.1; NC_010338.1. DR RefSeq; YP_001685032.1; NC_010338.1. DR ProteinModelPortal; B0T507; -. DR STRING; 366602.Caul_3407; -. DR EnsemblBacteria; ABZ72534; ABZ72534; Caul_3407. DR KEGG; cak:Caul_3407; -. DR PATRIC; 21319950; VBICauSp18104_3818. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; CSP366602:GH0Y-3438-MONOMER; -. DR Proteomes; UP000001316; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001316}; KW Methyltransferase {ECO:0000313|EMBL:ABZ72534.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001316}; KW Transferase {ECO:0000313|EMBL:ABZ72534.1}. SQ SEQUENCE 358 AA; 39349 MW; 2F512816FD2D0D43 CRC64; MTDLTTRAGR IKALKAAAKE RILILDGSWG VMFQKRKLSE ADYRAERFAD YDGQMKGNND ILCLTRPDIV ADLHHQYFAA GADISETNTF SGTTIAQADY RLGADVVRDI NYEGARIARS VADEWLAKEP EKPRFVAGSI GPLNVMLSMS SDVNDPGARK VTFDQVYQAY REQVMALHDG GVDLFLIETI TDTLNCKAAI KAIMDLVDEG YEELPIWISG TITDRSGRTL SGQTAEAFWN SIKHCKPFAV GFNCALGADL MRPHIAEMAR IADTLVAAYP NAGLPNAMGE YDEEPHQTGH QLHEWAKDGI VNILGGCCGT TPDHIKHVAD EVRGVKPRAI PERPKAMRLA GLEPFELA // ID B0TAJ7_HELMI Unreviewed; 807 AA. AC B0TAJ7; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 47. DE SubName: Full=Methionine synthase, putative {ECO:0000313|EMBL:ABZ85047.1}; GN Name=metH {ECO:0000313|EMBL:ABZ85047.1}; GN ORFNames=HM1_2499 {ECO:0000313|EMBL:ABZ85047.1}; OS Heliobacterium modesticaldum (strain ATCC 51547 / Ice1). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Heliobacteriaceae; OC Heliobacterium. OX NCBI_TaxID=498761 {ECO:0000313|EMBL:ABZ85047.1, ECO:0000313|Proteomes:UP000008550}; RN [1] {ECO:0000313|EMBL:ABZ85047.1, ECO:0000313|Proteomes:UP000008550} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51547 / Ice1 {ECO:0000313|Proteomes:UP000008550}; 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 ----------------------------------------------------------------------- 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; ABZ85047.1; -; Genomic_DNA. DR RefSeq; WP_012283543.1; NC_010337.2. DR RefSeq; YP_001681058.1; NC_010337.2. DR ProteinModelPortal; B0TAJ7; -. DR STRING; 498761.HM1_2499; -. DR EnsemblBacteria; ABZ85047; ABZ85047; HM1_2499. DR KEGG; hmo:HM1_2499; -. DR PATRIC; 22109069; VBIHelMod36755_2255. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; HMOD498761:GI46-2515-MONOMER; -. DR Proteomes; UP000008550; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008550}; KW Reference proteome {ECO:0000313|Proteomes:UP000008550}. SQ SEQUENCE 807 AA; 84130 MW; 4B67CCFDB82C7246 CRC64; MIKLFDGAMG TMLQAAGLLP GACPERFNLE HPERVTAIHR RYVEMGAEII ETNTFGATRL KLAHYRMADQ VEAVCHAAVR AARAACGPAT KIAGSVGPTG KLIAPLGELS FEEAVDVYSE QISALAAVGV DYILIETIID IQEMRAALLA AKAVAKVPVI CQLSFGADGR TVTGTDPATA AYLLEAMGAD VIGVNCSLGP AQLLPVIEAI AGATNLPISA QPNAGMPELI DGRTVFPMSP EEFASWAPKL AAAGATYLGG CCGTTPEHIA AAKAALEAAY PGGAAPARLI KDPVTALTSR SRTVFLGPAF SPVIIGERIN PTGRKALAAE IKGGSWLTVK RDAIEQVRAG AQILDVNMGV PGINQAKAME TAITELSLLV DVPLAIDTTD AAALEAGLRV YPGRALINSV SAEPDRLREF LPLAKKYGAA VLCLPIAPGG VPQTAQERVA IAQQIVDAAL AAGLRRQDLL LDPLVMTVAT DANAARETLE TLRSYRKTFG FPTVMGLSNV SFGLPRRNLV NAAFCALALD AGLDAPIMNP FDETLSDCWN AAQVLLGHDK QGQRFCIRYA QSAGAPSSAK VAGNAATEGD VLTCIRKAVI AGEKESVIPL VRKALAEGLT AIAITEGGLT TAMTEIGEAY GSGRCFLPQV MLAAETMRVA FQTLKAELPS QDMASKGRVL LATVRGDIHD LGKNIVAALL ENNGFTVIDL GKDVPAERIV AEARAQRADV VGLCALMTTT LPEIDHTIAA LKAAGVECLT MAGGAVVTAE YAAAAGVDGY APDAVSAVKL TEELLKRRKR GKTRGLT // ID B0TT67_SHEHH Unreviewed; 1260 AA. AC B0TT67; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 55. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABZ78008.1}; GN OrderedLocusNames=Shal_3462 {ECO:0000313|EMBL:ABZ78008.1}; OS Shewanella halifaxensis (strain HAW-EB4). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=458817 {ECO:0000313|EMBL:ABZ78008.1, ECO:0000313|Proteomes:UP000001317}; RN [1] {ECO:0000313|EMBL:ABZ78008.1, ECO:0000313|Proteomes:UP000001317} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HAW-EB4 {ECO:0000313|EMBL:ABZ78008.1, RC ECO:0000313|Proteomes:UP000001317}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000931; ABZ78008.1; -; Genomic_DNA. DR RefSeq; WP_012278528.1; NC_010334.1. DR RefSeq; YP_001675667.1; NC_010334.1. DR ProteinModelPortal; B0TT67; -. DR SMR; B0TT67; 680-918. DR STRING; 458817.Shal_3462; -. DR EnsemblBacteria; ABZ78008; ABZ78008; Shal_3462. DR KEGG; shl:Shal_3462; -. DR PATRIC; 23509880; VBISheHal24697_3627. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SHAL458817:GH1X-3582-MONOMER; -. DR Proteomes; UP000001317; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001317}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 265 265 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 328 328 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 329 329 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 786 786 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1260 AA; 139306 MW; 5F28D719C91B3DC0 CRC64; MATCTPTHAL SAVAHTQDTA DKVLAVLTQK LLDGILILDG AMGTMIQDRK FDEADFRGEQ FKEWHCDVKG NNDMLVLTQA GAIKQIHKEY LLAGSDIIET NTFNATRIAM ADYDMQAHSA EINLAGARLA REAANEVEAE TGRQCYVAGV LGPTNRTCSI SPDVNDPGYR NVSFDELVEA YIESINALIA GGCDIIMVET IFDTLNAKAA LFAIETVYDT QGFRLPIMIS GTITDASGRT LTGQTTEAFY NSLRHVKPLS IGLNCALGPK ELRPYVEELS KISECFVSAH PNAGLPNEFG GYDESPEQMA DVIEEWAEEG FLNIIGGCCG TTPDHIRVIR NAVIKHNARK LPDIPVACRL SGLEPLTIDD NSLFLNVGER TNVTGSAKFL RLIKTGEYEE ALSVAREQVE SGAQIIDINM DEGMLDGVEV MQKFLNLIAS EPDISRVPIM IDSSKWEVIE AGLKCIQGKG IVNSISLKEG EEKFIEQAKL VKRYGAAAII MAFDEVGQAD TKARKIEICT RAYRVLVDKV GFPPEDIIFD PNIFAIATGI DEHDNYAVDF IEATREIKRT LPHAMVSGGV SNVSFSFRGN NPVREAIHAV FLYHAIQAGM DMGIVNAGQL AIYDDIDPEL KERVEAVVQN LLCTAVDNNG DPSNNTEQLL DVAEKYRGDG SQTIKKEDLE WRGWDVNKRL AHALVKGITD FIDQDTEEAR AAATRPLDVI EGPLMDGMNI VGDLFGSGKM FLPQVVKSAR VMKKAVAYLN PYIELEKVPG QSNGKILMVT VKGDVHDIGK NIVGVVLACN GYEVIDLGVM VPVEKIIEVA KAENVDVIGM SGLITPSLDE MVHNVKAFHK AGLTIPSIIG GATCSKIHTA VKIAPHSPTG AIYIADASRA VPMVSKLINN DTRQATIDEA YAEYDVMREK RLSQTKRKVI TSIEAARENR CQHDWQNYTP FVPNQLGRQV FDDYPLEDLV ERIDWTPFFR SWELHGHFPR ILDDELVGTE ARELYSNAQK MLDKIISEKW LTAKAVMGLF PANSVNHDDI ELYSADGTDG SREKPIMTLH HLRMQIERVG NHNFCLSDFV APKDSDVADY MGGFAVTAGH GIDEHIARFE AEHDDYSAIM LKSLADRLAE AFAEHMHERV RKEFWGYAAD EALDNEALIK EKYKGIRPAP GYPACPDHTE KGLLWDLLKP DETIGLRLTE SYAMYPTAAV SGWYFSHPQS RYFGVTNIGR DQVEDYAARK GMSIEETERW LAPVLDYDPE // ID B0TW11_FRAP2 Unreviewed; 356 AA. AC B0TW11; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 45. DE SubName: Full=Betaine-homocysteine methyltransferase {ECO:0000313|EMBL:ABZ86919.1}; GN OrderedLocusNames=Fphi_0698 {ECO:0000313|EMBL:ABZ86919.1}; OS Francisella philomiragia subsp. philomiragia (strain ATCC 25017). OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Francisellaceae; Francisella. OX NCBI_TaxID=484022 {ECO:0000313|EMBL:ABZ86919.1, ECO:0000313|Proteomes:UP000001320}; RN [1] {ECO:0000313|Proteomes:UP000001320} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25017 {ECO:0000313|Proteomes:UP000001320}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; ABZ86919.1; -; Genomic_DNA. DR RefSeq; WP_012280134.1; NC_010336.1. DR RefSeq; YP_001677420.1; NC_010336.1. DR STRING; 484022.Fphi_0698; -. DR PRIDE; B0TW11; -. DR EnsemblBacteria; ABZ86919; ABZ86919; Fphi_0698. DR KEGG; fph:Fphi_0698; -. DR PATRIC; 17938249; VBIFraPhi43880_0723. DR eggNOG; COG0646; -. DR HOGENOM; HOG000231636; -. DR OMA; KAHYMSQ; -. DR OrthoDB; EOG6NSGDJ; -. DR BioCyc; FPHI484022:GHVB-712-MONOMER; -. DR Proteomes; UP000001320; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001320}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ABZ86919.1}; KW Transferase {ECO:0000313|EMBL:ABZ86919.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 216 216 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 356 AA; 39595 MW; 0382ACD5404BFECF CRC64; MSIKKKEGLI ERLNKGPVIC AEGFIFELER RGFLASGEFV PTVVLDHPEI VEGLHREFQH AGSDVVEALT YYAHREKLKV AGQEHIIEDL NRQALRIAKK VADSAPKGVQ PNLMAGNICN SNIWKQGDRK AQLEVERMFD EMVTWAVEEG ADMIIGETFS YAEEAFKAVE VIKKSGLPAV LTIAPMGQNV MLDGWSIVDT CKELEQLGAD VVGLNCFRGP QTMLPYLKDI RKAVKCHVAA LPVPYRTTDD HPTFFNLPDN NGCSCPSPHG RPFPTALDPL FCNRYEIREF AKEAYDFGVN YLGVCCGASP ALIREVAEAV GLTVPASKYR EKMQNHSMYG THQRIAKHIQ AYGDKA // ID B0UK72_METS4 Unreviewed; 1247 AA. AC B0UK72; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 29-APR-2015, entry version 55. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACA18709.1}; GN OrderedLocusNames=M446_4366 {ECO:0000313|EMBL:ACA18709.1}; OS Methylobacterium sp. (strain 4-46). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=426117 {ECO:0000313|EMBL:ACA18709.1, ECO:0000313|Proteomes:UP000001185}; RN [1] {ECO:0000313|EMBL:ACA18709.1, ECO:0000313|Proteomes:UP000001185} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4-46 {ECO:0000313|EMBL:ACA18709.1, RC ECO:0000313|Proteomes:UP000001185}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000943; ACA18709.1; -; Genomic_DNA. DR RefSeq; WP_012334098.1; NC_010511.1. DR RefSeq; YP_001771143.1; NC_010511.1. DR ProteinModelPortal; B0UK72; -. DR SMR; B0UK72; 659-907. DR STRING; 426117.M446_4366; -. DR EnsemblBacteria; ACA18709; ACA18709; M446_4366. DR KEGG; met:M446_4366; -. DR PATRIC; 22589882; VBIMetSp32184_4274. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; MSP426117:GI2I-4408-MONOMER; -. DR Proteomes; UP000001185; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001185}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001185}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 254 254 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 318 318 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 769 769 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1247 AA; 136394 MW; 2120944B5AEF0BDF CRC64; MTDLRPADGA NVLATLRKRA AERILVLDGA MGTMIQRLKL GEADFRGKRF LDHAHDQRGN NDLLILTQPE AIRQIHLDYF LAGADVVETN TFSGTAIAQA DYGMEAIVRE LNREGARLAR EAAVEAERRD GRRRFVAGAI GPTNRTLSIS PDVNNPGYRS VTFDQVRDAY AEQVRGLIEG GSDLVLIETI FDTLNAKAAI AATWQVFGEM GVRLPIMISG TITDLSGRTL SGQTPSAFWH SLRHAEPLTF GLNCALGARE MRAHISELSR VCDTLVCAYP NAGLPNEFGL YDESPEAMGA LVGEFAGSGL VNMVGGCCGT TPDHIRAIAE AVAGKAPRRV PEVPRLMRLS GLEPFTLTKE IPFVNVGERT NVTGSAKFRK LVTSGDYAAA LDVARDQVAA GAQVIDVNMD EGLLDSRAAM VEFLNLVAAE PDIARVPVMV DSSKFEVIEA GLKCIQGKPI VNSISLKEGK EKFLTEARIC RAYGAAVVVM AFDEQGQADT LERKVAICTR AYRILTEEVG FPPEDIIFDP NIFAVATGIE EHDGYGVAFI EAARQIRETL PHAHISGGVS NLSFAFRGNE PVREAMHAVF LYHAIRAGMD MGIVNAGQLA VYDELDPELR DLCEDVVLNR RPDATERLLE QAAKFKGGGA QLRTADLAWR EAPVEKRLEH ALVNGITEYI EADTEEARRT ATRPLDVIEG PLMAGMNVVG DLFGSGKMFL PQVVKSARVM KQAVAYLMPF MEEEKRANGG TGRQAAGKVL MATVKGDVHD IGKNIVGVVL ACNNYEIIDL GVMVPAAKIL DTARKEKVDI VGLSGLITPS LDEMVHVASE MEREGFEVPL LIGGATTSRV HTAVKIHPAY AKGQAVYVTD ASRAVGVVSS LLSPETKAAT IEGVRAEYKR VAEAHARSEA DKQRLPLAKA RANPFRAEFS TYRPAKPSFT GTRVFRSYDV AELVPYIDWT PFLQTYEFKG RFPALLDDPV QGPAARALFD DAQAMLARIV EERWFNPKAV IGFWPANAVG DDIRLFTGES RTDRLATFHG LRQQLSKRDG RPNTCLSDFV APLDSGVPDY VGGFVVTAGL EEVRIAERFE RQNDDYRSIL VKALADRIAE AFAERMHERV RKEFWGYAAD ETFAPADLVL EEYQGIRPAP GYPAQPDHTE KATLFDLLQA EPRIGVKLTE SYAMWPGSSV SGLYLAHPGA HYFGVAKVER DQVEDYAARK GMDVAEVERW LGPILNYDPR RHLAAAE // ID B0V948_ACIBY Unreviewed; 292 AA. AC B0V948; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 39. DE SubName: Full=Acinetobacter baumannii str. AYE, complete genome {ECO:0000313|EMBL:CAM87698.1}; DE EC=2.1.1.- {ECO:0000313|EMBL:CAM87698.1}; GN OrderedLocusNames=ABAYE2871 {ECO:0000313|EMBL:CAM87698.1}; OS Acinetobacter baumannii (strain AYE). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=509173 {ECO:0000313|Proteomes:UP000002446}; RN [1] {ECO:0000313|EMBL:CAM87698.1, ECO:0000313|Proteomes:UP000002446} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AYE {ECO:0000313|EMBL:CAM87698.1, RC ECO:0000313|Proteomes:UP000002446}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; CAM87698.1; -; Genomic_DNA. DR RefSeq; WP_000696108.1; NC_010410.1. DR RefSeq; YP_001714673.1; NC_010410.1. DR ProteinModelPortal; B0V948; -. DR STRING; 509173.ABAYE2871; -. DR EnsemblBacteria; CAM87698; CAM87698; ABAYE2871. DR KEGG; aby:ABAYE2871; -. DR PATRIC; 20728911; VBIAciBau69881_2768. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; PYVDVWL; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; ABAU509173:GJXF-2766-MONOMER; -. DR Proteomes; UP000002446; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002446}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:CAM87698.1}; KW Transferase {ECO:0000313|EMBL:CAM87698.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 202 202 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 275 275 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 276 276 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 292 AA; 32064 MW; EB1B58B1EF96D60A CRC64; MKILDGGLGR ELARRGAPFR QPEWSALALI EAPETVKEVH LDFINAGAEV ITTNNYAVVP FHIGQERFET DGVRLIKVAI EQAKNAVKES GKNVKIAGCL PPLFGSYRAD LFQPEQAKNL AEPIINTLAP EVDFWLAETQ SCLKEVETVH ALLPQDGKDY WVSFTLQDEI KQEQALLRSG ENMQQVADFI KQSNAKAVLF NCCQPEVILQ AINEIKGLIP ESVQIGAYAN AFPPQDESAT ANDGLDEIRK DLDAPAYLGF AKQWQQAGAS LVGGCCGIGP EHIAELSQFF KE // ID B0V9J6_ACIBY Unreviewed; 1228 AA. AC B0V9J6; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 54. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CAM87650.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAM87650.1}; GN Name=metH {ECO:0000313|EMBL:CAM87650.1}; GN OrderedLocusNames=ABAYE2822 {ECO:0000313|EMBL:CAM87650.1}; OS Acinetobacter baumannii (strain AYE). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=509173 {ECO:0000313|Proteomes:UP000002446}; RN [1] {ECO:0000313|EMBL:CAM87650.1, ECO:0000313|Proteomes:UP000002446} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AYE {ECO:0000313|EMBL:CAM87650.1, RC ECO:0000313|Proteomes:UP000002446}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CU459141; CAM87650.1; -; Genomic_DNA. DR RefSeq; WP_000105326.1; NC_010410.1. DR RefSeq; YP_001714625.1; NC_010410.1. DR ProteinModelPortal; B0V9J6; -. DR SMR; B0V9J6; 654-893. DR STRING; 509173.ABAYE2822; -. DR EnsemblBacteria; CAM87650; CAM87650; ABAYE2822. DR KEGG; aby:ABAYE2822; -. DR PATRIC; 20728811; VBIAciBau69881_2718. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; ABAU509173:GJXF-2718-MONOMER; -. DR Proteomes; UP000002446; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002446}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAM87650.1}; KW Transferase {ECO:0000313|EMBL:CAM87650.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1228 AA; 135817 MW; DDD77AD11982DA91 CRC64; MSTLATLKAL LAKRILIIDG AMGTMIQRHK LEEADYRGER FADWAHDLKG NNDLLVLTQP QIIQGIHEAY LDAGADIIET NSFNGTRVSM SDYHMEDLVP EINREAARLA KAACEKYSTP DKPRFVAGVL GPTSRTCSIS PDVNNPAFRN ISFDELKENY IEATHALIEG GADIILIETV FDTLNCKAAI FAVKEVFKQI GRELPIMISG TITDASGRTL TGQTAEAFWN SVRHGDLLSI GFNCALGADA MRPHVKTISD VADTFVSAHP NAGLPNAFGE YDETPEQTAA FLKEFAESGL INITGGCCGT TPDHIRAIAN AVKDIAPRQV PETVPACRLS GLEPFNIYDD SLFVNVGERT NVTGSKKFLR LIREENFAEA LEVAQQQVEA GAQIIDINMD EGMLDSQNAM VHFLNLVASE PDISRVPIMI DSSKWEIIEA GLKCVQGKPV VNSISLKEGY DEFVEKARLC RQYGAAIIVM AFDEVGQADT AERKREICKR SYDILVNEVG FPAEDIIFDP NVFAVATGIE EHNNYAVDFI EATGWIKQNL PHAMISGGVS NVSFSFRGNE PVREAIHSVF LYHAIKQGMT MGIVNAGQMA IYDDIPTELK EAVEDVILNQ NQGESGQAAT EKLLEVAEKY RGQGGATKEA ENLEWRNESV EKRLEYALVK GITTYIDQDT EEARLKSKRP LDVIEGPLMD GMNVVGDLFG SGKMFLPQVV KSARVMKQAV AWLNPYIEAE KTEGQSKGKV LMATVKGDVH DIGKNIVGVV LGCNGYDIVD LGVMVPCEKI LQTAIDEKCD IIGLSGLITP SLDEMVFVAK EMQRKGFNIP LLIGGATTSK AHTAVKIDPQ YQNDAVIYVA DASRAVGVAT TLLSKEMRGA FIEEHRAEYA KIRERLANKQ PKAAKLTYKE SVENGFKIDE SYVPPKPNLL GTQVLKNYPL ATLVDYFDWT PFFISWSLTG KFPKILEDEV VGEAATDLYN QAQAMLKDII DNNRFDARAV FGMFPAQRTD ADTVSVFDEA GQNVTHTFEH LRQQSDKVTG KPNLSLADYI RADREQQDYL GGFTVSIFGA EELANEYKAK GDDYSAILVQ SLADRFAEAF AEHLHERIRK EFWGYKADEQ LSNEELIKEK YVGIRPAPGY PACPEHSEKA VLFDWLGSTD KIGTKLTEHF AMMPPSSVSG FYYSHPQSEY FNVGKISQDQ LEDYAKRKGW TLDEAKRWLA PNLDDSIV // ID B0WAH1_CULQU Unreviewed; 996 AA. AC B0WAH1; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=Numb-associated kinase {ECO:0000313|EMBL:EDS41394.1}; GN ORFNames=CpipJ_CPIJ004075 {ECO:0000313|EMBL:EDS41394.1}; OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; OC Culicidae; Culicinae; Culicini; Culex; Culex. OX NCBI_TaxID=7176 {ECO:0000313|Proteomes:UP000002320}; RN [1] {ECO:0000313|Proteomes:UP000002320} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JHB {ECO:0000313|Proteomes:UP000002320}; RG The Broad Institute Genome Sequencing Platform; RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.D., RA Hannick L.I., Megy K., O'Leary S.B., Pearson M., Haas B.J., RA Mauceli E., Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., RA Amedeo P., Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., RA Camaro F., Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., RA Lawson D., Montgomery P., Nene V., Nusbaum C., Puiu D., RA Romero-Severson J., Severson D.W., Shumway M., Sisk P., Stolte C., RA Zeng Q., Eisenstadt E., Fraser-Liggett C.M., Strausberg R., RA Galagan J., Birren B., Collins F.H.; RT "Annotation of Culex pipiens quinquefasciatus."; 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; DS231872; EDS41394.1; -; Genomic_DNA. DR RefSeq; XP_001845705.1; XM_001845653.1. DR ProteinModelPortal; B0WAH1; -. DR STRING; 7176.CPIJ004075-PA; -. DR EnsemblMetazoa; CPIJ004075-RA; CPIJ004075-PA; CPIJ004075. DR GeneID; 6035547; -. DR KEGG; cqu:CpipJ_CPIJ004075; -. DR VectorBase; CPIJ004075; Culex quinquefasciatus. DR eggNOG; COG0515; -. DR HOGENOM; HOG000044963; -. DR InParanoid; B0WAH1; -. DR KO; K08853; -. DR OMA; HQLIRYM; -. DR OrthoDB; EOG7PP566; -. DR PhylomeDB; B0WAH1; -. DR Proteomes; UP000002320; Partially assembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002320}; KW Kinase {ECO:0000313|EMBL:EDS41394.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002320}; KW Transferase {ECO:0000313|EMBL:EDS41394.1}. SQ SEQUENCE 996 AA; 108921 MW; 2FC456A78CB7D17A CRC64; MKKFISKFET KNEATPSKET NSFVGKTFKL SRDNVVTVEE VLAEGGFAVV FLVKGSNGQR FALKRLYVNN EHDLGVCNRE IKIASNLSGH KNIIGYIDHS VNPKGNGVHE ILLLMPYCKT NLLTLMNARI PNGFSEQDVL QIFCDVAEAV ARLHQCQTPI IHRDLKVENI LQNDIGNFVL CDFGSATARV LNPVTHGRTV VEEEIQKYTT LSYRAPEMID LFSGQDITVK ADIWALGCLL YKLCFFTLPF GESALAIQSG HFSIPDNSKY SREMHQLIRY MLEPDIERRP NIYQVCEVAF KIAGKTNPVR NLTKSTVPAL ETLPVPPLES ETKRVPSSSV GGGAKTPAKT VTPIIEGTSV APRQRPKASQ ANVSNSFTLG LPPNPSPKNI LSSPTPGATP TTILQEQQPQ PAPAAAPAQV EPFVAKFTAN FPPLSGQEAQ SGNLFQTTYP DPFREVEVAT EVVGDTAATR ESSTSSILQS PSHGSGSGTP HGSGSSMAGS LLPPPKQPSV AAAVVGHRRN MSDTSAFNKA YTTETSQFLA PYDVSSNNYQ PAISGSGNGS EQNLHSIPAS FESRSSNPQL NPPVSAQQQP WNPFGDPTPF SQMTEDHIFG EEFDKIRKQG SQGSLKTPPE STSRHPSLPL FSPENIPDTL EDDPFSSAPF SLPVKSRSLK MTSKRIIVID GGFSTQLATH VGQTTLDKDP LWSSRYNATN PNAVIETHLD FLKAGADCIL TNTYQASIEG YMDFLNLSEE DSIKLIKTAV ELAKLARTRY LAEKIENKTH KIPWVVGSIG PYGAHLHDGS EYTGAYADTV PYARIQKWHR QRINAVLEAG VDALAIETIP CRKEAEALLE LLTTEHPTVR FWVSFQCKDG VNTARGENFA ETAAAIWSQA RALKNPNLLA IGVNCLHPVH AVQLLKTANE RRPDDDKIPL IVYPNSGEIW DNGVWKGEED CVPLETYVPQ FVEYGVKFVG GCCRTTAQDI KRIKKTVINL CGGRST // ID B0WQ03_CULQU Unreviewed; 324 AA. AC B0WQ03; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 36. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EDS32593.1}; GN ORFNames=CpipJ_CPIJ008869 {ECO:0000313|EMBL:EDS32593.1}; OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; OC Culicidae; Culicinae; Culicini; Culex; Culex. OX NCBI_TaxID=7176 {ECO:0000313|Proteomes:UP000002320}; RN [1] {ECO:0000313|Proteomes:UP000002320} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JHB {ECO:0000313|Proteomes:UP000002320}; RG The Broad Institute Genome Sequencing Platform; RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.D., RA Hannick L.I., Megy K., O'Leary S.B., Pearson M., Haas B.J., RA Mauceli E., Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., RA Amedeo P., Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., RA Camaro F., Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., RA Lawson D., Montgomery P., Nene V., Nusbaum C., Puiu D., RA Romero-Severson J., Severson D.W., Shumway M., Sisk P., Stolte C., RA Zeng Q., Eisenstadt E., Fraser-Liggett C.M., Strausberg R., RA Galagan J., Birren B., Collins F.H.; RT "Annotation of Culex pipiens quinquefasciatus."; 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; DS232031; EDS32593.1; -; Genomic_DNA. DR RefSeq; XP_001850787.1; XM_001850735.1. DR UniGene; Cpi.5594; -. DR ProteinModelPortal; B0WQ03; -. DR STRING; 7176.CPIJ008869-PA; -. DR EnsemblMetazoa; CPIJ008869-RA; CPIJ008869-PA; CPIJ008869. DR GeneID; 6041540; -. DR KEGG; cqu:CpipJ_CPIJ008869; -. DR VectorBase; CPIJ008869; Culex quinquefasciatus. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR InParanoid; B0WQ03; -. DR KO; K00547; -. DR OMA; QCKDENT; -. DR OrthoDB; EOG7GQXW0; -. DR PhylomeDB; B0WQ03; -. DR Proteomes; UP000002320; Partially assembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002320}; KW Methyltransferase {ECO:0000313|EMBL:EDS32593.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002320}; KW Transferase {ECO:0000313|EMBL:EDS32593.1}. SQ SEQUENCE 324 AA; 35958 MW; 46094DE5C956C703 CRC64; MTSSRLPVTV LDGGFATQLS VHVGKHVDGD PLWSARFNAT NPNAVYKTHL DFLEAGAQCI MTNTYQASIE GYGEYLDLSE AASIQLIKST VKLAHMARTK HLAESDIREI PLVVASIGPY GAHLHDGSEY TGEYADYVSA NTIQKWHRSR IDACLEAGVD VLGIETIPCK MEADAMLEMM TEDYPHVKFW ISFQCKDSAH LARGENFAET VSYIWNKAKL LGNDNLIALG VNCVHPQFVT PLFRAVNEKR SPVERIPLIV YPNSGEVYSV ETGWQGKEDC VPLEQYVPQW IDLGARFIGG CCRTYARDIK RIKQAVTALQ TGTL // ID B0XWR6_ASPFC Unreviewed; 313 AA. AC B0XWR6; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 07-JAN-2015, entry version 25. DE SubName: Full=Homocysteine S-methyltransferase, putative {ECO:0000313|EMBL:EDP53525.1}; GN ORFNames=AFUB_047060 {ECO:0000313|EMBL:EDP53525.1}; 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 {ECO:0000313|Proteomes:UP000001699}; RN [1] {ECO:0000313|Proteomes:UP000001699} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163 RC {ECO:0000313|Proteomes:UP000001699}; 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; DS499596; EDP53525.1; -; Genomic_DNA. DR EnsemblFungi; CADAFUBT00004696; CADAFUBP00004613; CADAFUBG00004696. DR HOGENOM; HOG000179103; -. DR OrthoDB; EOG7XH70V; -. DR PhylomeDB; B0XWR6; -. DR Proteomes; UP000001699; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001699}; KW Methyltransferase {ECO:0000313|EMBL:EDP53525.1}; KW Transferase {ECO:0000313|EMBL:EDP53525.1}. SQ SEQUENCE 313 AA; 33680 MW; 0421F3EE3ECE8B66 CRC64; MALPQLLSPK PFLTECGMET SLVYKDKVHL PCFSSLPLVD SDSSRKLISH YYDSYISIAA ANGTGIVLDT RTWRGATPWA QPMGLSADKL LELNRAAVRL AKEARNRAVG GENNIPVVIS GTMGPLRDAY VDTSELITLE DAREGYREQV EVLADAGVDM LAIMTVTNLN EAIAVVELAK EVRLPVVVSF SIESDGRLLG GRSLGSAIRT VDEKTGGSVV YYGVNCAHPV RISAALRDVP EDVRGRIGLI KGNASLKSHD ELDNSETLDR GDISVFTDGF EGVLPLVPNV KVIGGCCGTD EEHLEAVAKR CIK // ID B0Y1P6_ASPFC Unreviewed; 343 AA. AC B0Y1P6; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 07-JAN-2015, entry version 25. DE SubName: Full=Homocysteine S-methyltransferase, putative {ECO:0000313|EMBL:EDP51002.1}; GN ORFNames=AFUB_050040 {ECO:0000313|EMBL:EDP51002.1}; 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 {ECO:0000313|Proteomes:UP000001699}; RN [1] {ECO:0000313|Proteomes:UP000001699} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163 RC {ECO:0000313|Proteomes:UP000001699}; 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; DS499597; EDP51002.1; -; Genomic_DNA. DR EnsemblFungi; CADAFUBT00004984; CADAFUBP00004895; CADAFUBG00004984. DR HOGENOM; HOG000265278; -. DR OrthoDB; EOG79SF86; -. DR PhylomeDB; B0Y1P6; -. DR Proteomes; UP000001699; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001699}; KW Methyltransferase {ECO:0000313|EMBL:EDP51002.1}; KW Transferase {ECO:0000313|EMBL:EDP51002.1}. SQ SEQUENCE 343 AA; 37199 MW; F71777164F236702 CRC64; MTSIQILDGG LGTSLQDQHG VTFDSSTPLW SSHLLVSDPT TLLACQRNFI TAGCDVLLTA TYQVSIEGFA RTKTPEFPDG IPRPAIGKYL RTALAVAEQA RVSPSAAKIA LSLGPYGACM IPGQEYSGKY DAEHDSEETL FQWHLERLRL FLEADEKLAE RVQYVAFETL PRLDEIRAVR RAIRTAGLNV PFWVACVFPG EEATLPDGSS IGQIVQAALA EMDGAAVPWG VGINCTKIYK LDGLVREFGE EVASAVGQGQ VGAVPSLVLY PDGTNGEVYN TTTQTWEKQE GYTSDARGPW EVQLAQIVTN ARATGPFTSF LVGGCCKASH RDIRKLAEQL KNE // ID B1A1E6_9BACT Unreviewed; 242 AA. AC B1A1E6; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 29-OCT-2014, entry version 15. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:ACA05081.1}; DE Flags: Fragment; OS Flammeovirga yaeyamensis. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Flammeovirgaceae; OC Flammeovirga. OX NCBI_TaxID=367791 {ECO:0000313|EMBL:ACA05081.1}; RN [1] {ECO:0000313|EMBL:ACA05081.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MY04 {ECO:0000313|EMBL:ACA05081.1}; RA Han W.J., Gu J.Y., Zhu B.L., Liu S.Y., Gao C.J., Shi Y.L.; RT "Cloning and sequence analysis of functional genes of Flammeovirga RT yaeyamensis strain MY04 (CGMCC 2777)."; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACA05081.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MY04 {ECO:0000313|EMBL:ACA05081.1}; RA Zhu B.L., Shi Y.L.; 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; EU414954; ACA05081.1; -; Genomic_DNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:ACA05081.1}; KW Transferase {ECO:0000313|EMBL:ACA05081.1}. FT NON_TER 1 1 {ECO:0000313|EMBL:ACA05081.1}. SQ SEQUENCE 242 AA; 27201 MW; 89C0CFD66FD74D41 CRC64; HQEEVIKNAH LNYLKSGAEI IISSSYQASI KGFMEKGFSH EVAIDLLKKT TEIAQSAKEE YREISKREVF IAGSIGPYAA YLADGSEYKG YDEAVDENTL RSFHNERLRI IDATDIDVLA VETIPSLEEA KVLNDLIEKC GHKAWFSFSC KNEKQLNDGT DIIDIVSLLK HNNNVMALGI NCTHPKYILG LISEILNAGW KKKIVIYPNA GMVYNPDTKT LAGNLISRRF PHFSFTMERG RS // ID B1B9Q9_CLOBO Unreviewed; 805 AA. AC B1B9Q9; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EDS77986.1}; GN ORFNames=CBC_A0640 {ECO:0000313|EMBL:EDS77986.1}; OS Clostridium botulinum C str. Eklund. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=445337 {ECO:0000313|EMBL:EDS77986.1}; RN [1] {ECO:0000313|EMBL:EDS77986.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Eklund {ECO:0000313|EMBL:EDS77986.1}; RA Paulsen I.; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EDS77986.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Eklund {ECO:0000313|EMBL:EDS77986.1}; 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. {ECO:0000313|EMBL:EDS77986.1}. 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; ABDQ01000003; EDS77986.1; -; Genomic_DNA. DR RefSeq; WP_003365127.1; NZ_ABDQ01000003.1. DR ProteinModelPortal; B1B9Q9; -. DR EnsemblBacteria; EDS77986; EDS77986; CBC_A0640. DR PATRIC; 26421407; VBICloBot5690_0990. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDS77986.1}; KW Transferase {ECO:0000313|EMBL:EDS77986.1}. SQ SEQUENCE 805 AA; 88969 MW; CE949CDC9916E299 CRC64; MDIRNYIKNN ILIFDGAMGT MLQKSGLKLG ETPEKLNFSH EELIIDIHKK YINAGCNIIT TNTFGANEIK LKNVPFSVEN TITKAVSIAK KASENSNCFI ALDIGPIGKL LEPMGTVKFE EAINIFKKQI KVGVECGVDL ILIETMTDLY ELKAAIIAAK EISDLPIFAT MSFEENGRTF TGCLPESMSI TLEALGVDAL GVNCSLGPKE LKPIVKKIIE HTNLPVIVQP NAGIPSIVKG KTLYTISPKE FCNYVEALID IGVSIIGGCC GTTPEFIKHL KYICNHKKIL KRSPIKKSFV TTPSKIVELN EVRIIGEKIN PTGKKRLKEA LINNDIDYIL KQAIDEVDRG ADILDINVGL PEINEADTLE YTLKKIQCIV DTPLQIDSSN VEAIERALRI YNGKPIVNSV NGEDKSLENI LPLVKKYGAS VIGLTLDNKG IPKTASERFK IAERILNTAL DYGIKKEDIY IDCLTLTVSA QQNEVMETLK ALKMVKERLG VKTVLGISNI SFGLPNRDII NETFLSLALG SGLDLPIMNP TKQGMINIIN AYKVLNNNDK NAKNYIETYR NKQILTTILT NNSTSNTQIK DNKNSKLEEH TNLEEFILQG LKNNTKNLTC DLLKTNTELE IVNKFLIPAL DNIGTKYENG EIFLPQLIQS AETVKVAFEL IKENLLKSRN KAVSKGKIIL ATVKGDIHDI GKNIVKVILE NYGYEILDLG KDVSSKKIVK EAIDKNIKLV GLSALMTTTI KSMEDTIIAL KNANFEGKIM VAGAVLTKEY AIKMGADFYA KDAKDSIEIA KKIFN // ID B1BN91_CLOPF Unreviewed; 790 AA. AC B1BN91; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EDS78753.1}; GN ORFNames=CPC_1653 {ECO:0000313|EMBL:EDS78753.1}; OS Clostridium perfringens C str. JGS1495. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=445334 {ECO:0000313|EMBL:EDS78753.1}; RN [1] {ECO:0000313|EMBL:EDS78753.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=JGS1495 {ECO:0000313|EMBL:EDS78753.1}; 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. {ECO:0000313|EMBL:EDS78753.1}. 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; ABDU01000083; EDS78753.1; -; Genomic_DNA. DR RefSeq; WP_003454626.1; NZ_ABDU01000083.2. DR ProteinModelPortal; B1BN91; -. DR EnsemblBacteria; EDS78753; EDS78753; CPC_1653. DR PATRIC; 30623906; VBICloPer103972_3232. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDS78753.1}; KW Transferase {ECO:0000313|EMBL:EDS78753.1}. SQ SEQUENCE 790 AA; 87589 MW; C35133CB554B8818 CRC64; MIKIFDGAMG TILQKLGLKL GENPEVLNIY NEEVICDIHR RYIDVGANFI TTNTFGANRK KLVNTDFKVE EIISKALKIA KRARGEKEVK IALDIGPIGE LLEPMGTLSF DEAYDIFKEQ VIVGVENGAD IILIETMSDL YEAKAAILAA KENSSLPVFC TMSFEKNERT FTGCIPESMA MTLEGLGVDA LGVNCSLGPR EMESVIKRIA KSTNKEIIVQ ANAGMPSIDR NSTSYEVNKY EFAEYGKKFV DLGANYIGGC CGTTPEYIEE LSKKLKNKES IKRGKVSLTG VCTPSLTIKE KGVYVIGERI NPTGKKRFKE ALKNNDIDYI VKQGIEQVEA GASILDVNVG IPEVDEKNLM VKIVKNLQSV LDTPLQIDSS NPEVIEKALR YYNGKCILNS VNGEEGTLDK ILPIVKKYGT MVIGLTLNNK GIPKSCKEKL EIGKKIIEKA SEYGISKDNI ILDPLILTAA TNQTEVKETL RTIRKIKEEL GVKTTLGVSN VSFGLPEREN INEVFLGMAL NEGLDFPIVN PNKEGIMKVI RGFELLYGYD KGANNYVKYY SNKNNIHKEN LKENVENILT LKEIVIKGLK GEAKEKTKEL LKSIKGMEIV NKELIPALDI VGEKFEKEEI FLPQLIASAE TVKESFEVIK SSIDFSKENK NNGCIVLATV KGDIHDIGKN IVKVILENYG YDIIDLGKNV EPEEILKVCT EKDVKLLGLS ALMTTTLGSM EATIKKVKEK GLKTKIFVGG AVLTKGYAEK IGADFYAKDA NRAVEIAKVV FRNYFDWRMH // ID B1BN92_CLOPF Unreviewed; 279 AA. AC B1BN92; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EDS78747.1}; GN ORFNames=CPC_1652 {ECO:0000313|EMBL:EDS78747.1}; OS Clostridium perfringens C str. JGS1495. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=445334 {ECO:0000313|EMBL:EDS78747.1}; RN [1] {ECO:0000313|EMBL:EDS78747.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=JGS1495 {ECO:0000313|EMBL:EDS78747.1}; 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. {ECO:0000313|EMBL:EDS78747.1}. 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; ABDU01000083; EDS78747.1; -; Genomic_DNA. DR RefSeq; WP_003454613.1; NZ_ABDU01000083.2. DR ProteinModelPortal; B1BN92; -. DR EnsemblBacteria; EDS78747; EDS78747; CPC_1652. DR PATRIC; 30623908; VBICloPer103972_3233. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDS78747.1}; KW Transferase {ECO:0000313|EMBL:EDS78747.1}. SQ SEQUENCE 279 AA; 31050 MW; 5770FDC508562AF3 CRC64; MKKLYLKNGV IIADGAMGTR IIELGVNLKE TPSELLNIKK PELIEKIHRE YVESGSNLIL SNTFICNIIN AKRNNYNLEE VIEAGISIAK KVCGDHGLVA LDIGPLSYYI EENDSSFKEF VYENTERIIN ASKDKFDLVI FETLGSLKEG EFAVKKAKTL TDKKVICSFT LAYKKDIPNF IKNMVSTLEP LGVDALGINC TGYEEILMAL DILKENTNLP IMIKANSGIP KKVGEELVYD KTLEEFKNLS KRAIEKGVNI IGGCCGTTPE YIRAICNLK // ID B1BTS9_CLOPF Unreviewed; 279 AA. AC B1BTS9; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EDT14898.1}; GN ORFNames=AC3_1878 {ECO:0000313|EMBL:EDT14898.1}; OS Clostridium perfringens E str. JGS1987. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=451755 {ECO:0000313|EMBL:EDT14898.1, ECO:0000313|Proteomes:UP000005337}; RN [1] {ECO:0000313|EMBL:EDT14898.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=JGS1987 {ECO:0000313|EMBL:EDT14898.1}; 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. {ECO:0000313|EMBL:EDT14898.1}. 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; ABDW01000016; EDT14898.1; -; Genomic_DNA. DR RefSeq; WP_003463818.1; NZ_ABDW01000016.1. DR ProteinModelPortal; B1BTS9; -. DR EnsemblBacteria; EDT14898; EDT14898; AC3_1878. DR PATRIC; 30642513; VBICloPer82820_1983. DR Proteomes; UP000005337; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005337}; KW Methyltransferase {ECO:0000313|EMBL:EDT14898.1}; KW Transferase {ECO:0000313|EMBL:EDT14898.1}. SQ SEQUENCE 279 AA; 31188 MW; 7E1C1C69E04095FF CRC64; MKNLDLKNGV IIADGAMGTR IMELGVNLKE TPSELLNIKK PELIEKIHRE YIESGANLIL SNTFMCNIIN AKRNNYNLEE VIESGLHIAK RAWGDEGLVA LDIGPLSYYI EENDSSFKEI VYENTERIIN ASKDKFDLVI FETLGSLKEG EFAVKKAKTL TNKKVICSFT LAYKKDIPNF IKNMVSTLEP LGVDALGINC TGYEEILMAL DILKENTNLP IMIKANLGIP KKVGEEFVYD KTLEEFKNLS KRALEKGVNI IGGCCGTTPE YIRAICNLK // ID B1C150_9FIRM Unreviewed; 785 AA. AC B1C150; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 32. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EDS75105.1}; GN ORFNames=CLOSPI_00933 {ECO:0000313|EMBL:EDS75105.1}; OS [Clostridium] spiroforme DSM 1552. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae; Erysipelatoclostridium. OX NCBI_TaxID=428126 {ECO:0000313|EMBL:EDS75105.1}; RN [1] {ECO:0000313|EMBL:EDS75105.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 1552 {ECO:0000313|EMBL:EDS75105.1}; 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] {ECO:0000313|EMBL:EDS75105.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 1552 {ECO:0000313|EMBL:EDS75105.1}; 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 (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. {ECO:0000313|EMBL:EDS75105.1}. 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; ABIK02000007; EDS75105.1; -; Genomic_DNA. DR RefSeq; WP_004608683.1; NZ_DS562844.1. DR ProteinModelPortal; B1C150; -. DR EnsemblBacteria; EDS75105; EDS75105; CLOSPI_00933. DR PATRIC; 27258898; VBICloSpi85079_0052. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDS75105.1}; KW Transferase {ECO:0000313|EMBL:EDS75105.1}. SQ SEQUENCE 785 AA; 86253 MW; 8DA4AFBBF8814276 CRC64; MLQERLKKEI LVFDGAMGTQ LQAAKLKAGE IPEYLNITDP YLIQKIHLDY LNAGANFITT NTFGANPLKL KDAPYQYNEI IETAINNAII ARKKANREND SYIVLDIGPI GQLLEPMGTL TFDEAYEIIK KQVLIAKDKV DAILLETFTD IYEAKAGILA VKENSNLPVF VTMTFESNLR TLSGCDPITM VNVLEGLNVD VLGVNCSLGP IELTPIINDI LKVATVPVMI QPNAGLPCLV EGKTCYNMDI DTFVSKSIEH VKNGVRIIGG CCGTTPEFIA RLKDALPEKI TLTKPVIATR VSSGNQTVEF GHHIVVCGER LNPTGKKKLK LALKEERYDE LIVEAIKQDQ AGAHVLDVNV GLPGIDEVST MKKVIKLLQE VISLPLQIDS SNPEAIEQAC RYYNGKPLIN SVNGKMETME AIFPIVKKYG GVVIGLTLDE NGIPSMAKDR YEIAKKIIAT AKKFGISKEN IIIDCLVLTV SAQQKDVIET IKAVKMVKEL GVHTVLGVSN VSFGLPNRPL LNKTFLTMAM TNGLDLPIIN PLDQELMAAI DAFNVLFNYD HDATNYIQKQ SNQTITSQSK PSDFSLNDII IHGLKEEVIN ATKKQLEKQP GLQIINQILI PALDTVGKQY ENNIIFLPQL IQAAETSKIA FGVIKETFKE TSATKGPIIM ATVHGDIHDI GKNIVKVVLE SYGYKIIDLG KDVPPETIVE AYHRHQPKAI GLSALMTTTV VSMEKTIALL KEIDNMCPIF VGGAVLTADF AKEINADFYV KDAMDTVELM NKIVK // ID B1C621_9FIRM Unreviewed; 795 AA. AC B1C621; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 30. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EDS73590.1}; GN ORFNames=ANASTE_00159 {ECO:0000313|EMBL:EDS73590.1}; OS Anaerofustis stercorihominis DSM 17244. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Anaerofustis. OX NCBI_TaxID=445971 {ECO:0000313|EMBL:EDS73590.1}; RN [1] {ECO:0000313|EMBL:EDS73590.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17244 {ECO:0000313|EMBL:EDS73590.1}; 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] {ECO:0000313|EMBL:EDS73590.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17244 {ECO:0000313|EMBL:EDS73590.1}; 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 (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. {ECO:0000313|EMBL:EDS73590.1}. 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; ABIL02000003; EDS73590.1; -; Genomic_DNA. DR RefSeq; WP_007049615.1; NZ_DS560017.1. DR ProteinModelPortal; B1C621; -. DR EnsemblBacteria; EDS73590; EDS73590; ANASTE_00159. DR PATRIC; 24499607; VBIAnaSte97905_0778. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDS73590.1}; KW Transferase {ECO:0000313|EMBL:EDS73590.1}. SQ SEQUENCE 795 AA; 87181 MW; 31563AD815705795 CRC64; MDILKLIKKR KVFFDGGMGS LLQEKGLKAG EFPEMWNVDK SDVVKDIHKE YLLSGADIIS ANTFGCNSLK FDKEGTYSVE NIIRSGVRNA KEAVKESGKD AYVALDIGPT GKLLKPLGDL DFNDAYEIYK EIILFGVKEN PDIILIETMS DGYEAKAAIL AAKENCDLPV FVSMTLGEDG KLLTGGNAES IIAMMEGLRV DIIGLNCGLG PLQLKPFIGK MLEVSSTPLM LNPNAGLPRS EGGKTVYDIN SGEFAFTMKE IADMGVSVLG GCCGTTPEHI KKTVELCKYV EIKEITKKDL TMISSFSKCV YIDKDPIIIG ERINPTGKKR FKQALIEDDI EYVLNEANTQ VEAGAHVLDV NVGLPEINEA EMMEKVIKEL QFSVDVPLQV DTSNTEAMER ALRLYNGKAL INSVNGKKEV MDEVFPLVKK YGGVVVALCL DEDGIPSTAK GRIKIANKII KEAEKYGIER KDIIIDALAM TVSADTSSAL VTLDTLSIVK NELKMNSVLG VSNISFGLPN RMIINSVFFA MALDRGLNAA IINPNNEDMM RSYISFRTLS DMDEKCMDYI DKYASEKRET GIKKEGLMSL EDSIVKGMKE RAKTATLEEL EKSEPLEIIN KKLIPSLDIV GKGFEEGTIF LPQLLMSAEA AKAAFNEVKN HLVKSGQKEE KIGKIVIATV KGDIHDIGKN IVKVLLENYG YDVIDLGKDV DPDLIVNTVI KEDVKLVGLS ALMTTTVPSM EETIKKLNKK VPDCKVFVGG AVLTKDYAKT INADYYAKDA MASVAYAENL FKVSP // ID B1ERK5_ESCAT Unreviewed; 1227 AA. AC B1ERK5; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 38. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EDS90151.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EDS90151.1}; GN Name=metH {ECO:0000313|EMBL:EDS90151.1}; GN ORFNames=ESCAB7627_4832 {ECO:0000313|EMBL:EDS90151.1}; OS Escherichia albertii (strain TW07627). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=502347 {ECO:0000313|EMBL:EDS90151.1, ECO:0000313|Proteomes:UP000003042}; RN [1] {ECO:0000313|EMBL:EDS90151.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TW07627 {ECO:0000313|EMBL:EDS90151.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EDS90151.1}. 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; ABKX01000015; EDS90151.1; -; Genomic_DNA. DR RefSeq; WP_000096072.1; NZ_CH991859.1. DR ProteinModelPortal; B1ERK5; -. DR SMR; B1ERK5; 651-1227. DR EnsemblBacteria; EDS90151; EDS90151; ESCAB7627_4832. DR PATRIC; 30328842; VBIEscAlb18499_0249. DR Proteomes; UP000003042; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000003042}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EDS90151.1}; KW Transferase {ECO:0000313|EMBL:EDS90151.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136129 MW; 00A86C21BAB22723 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLSEADFRGE RFADWPCDLK GNNDLLVLSK PDVISAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV TAYRESTKAL VEGGVDLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHADA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPQHIAV MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY NEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELREAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAKRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVLNVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID B1FCD0_9BURK Unreviewed; 355 AA. AC B1FCD0; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EDT04820.1}; GN ORFNames=BamIOP4010DRAFT_1689 {ECO:0000313|EMBL:EDT04820.1}; OS Burkholderia ambifaria IOP40-10. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=396596 {ECO:0000313|EMBL:EDT04820.1}; RN [1] {ECO:0000313|EMBL:EDT04820.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=IOP40-10 {ECO:0000313|EMBL:EDT04820.1}; 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. {ECO:0000313|EMBL:EDT04820.1}. 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; ABLC01000027; EDT04820.1; -; Genomic_DNA. DR RefSeq; WP_006750892.1; NZ_ABLC01000027.1. DR EnsemblBacteria; EDT04820; EDT04820; BamIOP4010DRAFT_1689. DR PATRIC; 38368044; VBIBurAmb78662_1698. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDT04820.1}; KW Transferase {ECO:0000313|EMBL:EDT04820.1}. SQ SEQUENCE 355 AA; 38203 MW; 5AB7345843794DC9 CRC64; MSATPLAASV PLDAPYTRGA ELPALLKSRI LILDGAMGTM IQRYKLDEAA YRGERFKDFP RDIKGNNELL SLTQPQIIRE IHDQYFAAGA DIVETNTFGA TTVAQADYGM EDLVVEMNVE SARLARESAA KYATPDKPRF VAGAIGPTPK TASISPDVND PGARNVTFDE LRGAYYQQAK ALLDGGVDLF LVETIFDTLN AKAALFALDE LFEDTGERLP IMISGTVTDA SGRILSGQTV EAFWNSLRHA KPLTFGLNCA LGAALMRPYI AELAKLCDTY VSCYPNAGLP NPMSDTGFDE TPDVTSGLLK EFAQAGLVNL AGGCCGTTPE HIAEIAKALA DVKPRRWPSH YSDAA // ID B1FVV3_9BURK Unreviewed; 356 AA. AC B1FVV3; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EDT11972.1}; GN ORFNames=BgramDRAFT_1578 {ECO:0000313|EMBL:EDT11972.1}; OS Burkholderia graminis C4D1M. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=396598 {ECO:0000313|EMBL:EDT11972.1}; RN [1] {ECO:0000313|EMBL:EDT11972.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C4D1M {ECO:0000313|EMBL:EDT11972.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDT11972.1}. 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; ABLD01000003; EDT11972.1; -; Genomic_DNA. DR RefSeq; WP_006048138.1; NZ_ABLD01000003.1. DR EnsemblBacteria; EDT11972; EDT11972; BgramDRAFT_1578. DR PATRIC; 26875671; VBIBurGra66597_1591. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDT11972.1}; KW Transferase {ECO:0000313|EMBL:EDT11972.1}. SQ SEQUENCE 356 AA; 38458 MW; F509A1B58C340211 CRC64; MNQPAQTVKP IRPERDYTRG ATLPALLKSR ILILDGAMGT MIQRYKLDEA RYRGERFADY GRDIKGNNEL LSITQPQIIS EIHEQYLAAG ADIIETNTFG ATTVAQADYG MEALAVEMNL ESAKLARAAC DKYSTPDKPR FVAGAIGPTP KTASISPDVN DPGARNVTFD ELHAAYYQQA KALLDGGADL FLVETIFDTL NAKAALFALD ELFEDTGERL PIMISGTVTD ASGRILSGQT VEAFWNSLRH AKPLTFGLNC ALGAALMRPY IAELAKLCDT YVSCYPNAGL PNPMSDTGFD ELPADTSGLL KEFAEAGLVN IAGGCCGTTP EHIAAIARAL AEVKPRKWPT QYRDAA // ID B1H0N5_UNCTG Unreviewed; 801 AA. AC B1H0N5; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 48. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:BAG14067.1}; GN OrderedLocusNames=TGRD_584 {ECO:0000313|EMBL:BAG14067.1}; OS Uncultured termite group 1 bacterium phylotype Rs-D17. OC Bacteria; Elusimicrobia; environmental samples. OX NCBI_TaxID=471821 {ECO:0000313|EMBL:BAG14067.1, ECO:0000313|Proteomes:UP000001691}; RN [1] {ECO:0000313|EMBL:BAG14067.1, ECO:0000313|Proteomes:UP000001691} 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 ----------------------------------------------------------------------- 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; BAG14067.1; -; Genomic_DNA. DR RefSeq; WP_015423591.1; NC_020419.1. DR RefSeq; YP_001956528.1; NC_020419.1. DR ProteinModelPortal; B1H0N5; -. DR STRING; 471821.TGRD_584; -. DR EnsemblBacteria; BAG14067; BAG14067; TGRD_584. DR GeneID; 6373242; -. DR KEGG; rsd:TGRD_584; -. DR PATRIC; 38571568; VBIUncTer52152_0963. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; UTER471821:GJAD-626-MONOMER; -. DR Proteomes; UP000001691; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001691}; KW Methyltransferase {ECO:0000313|EMBL:BAG14067.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001691}; KW Transferase {ECO:0000313|EMBL:BAG14067.1}. SQ SEQUENCE 801 AA; 87050 MW; AAF3CD456FC963B1 CRC64; MNKQKFLDIL KSRILIMDGA TGTELQKKKY LDGVEIPEEI NIKFPERIAD IYSSYINAGS DIILANTFGA NLIRLKQHGL LDKADDIIKS GIDLIREISS DTIVAGDISS IGEYIEPLGS LTFDEAYNSF AFQVSLLQKH GADVIVIETM TEIKETKAAI LAAKENFDGA IIVQMTFSKD GVTVTGTDLK SFIAMAESLG VDALGLNCSI GSRDLAELAK VLCVNTNLPI SFKPNAGIPV LINRETCFPE TKEEFIEASL KAYSYGVNMF GGCCGTNPEF IKILSGELMN KAPKIRSVKS KYFLSTRTKT IDINEAEKPV IIGERINPTN RKKFQEELLK GNLSTVKDEA RSQVWSGANL LDVNMGVPGT DEIKLLINAV NQIQETVSVP LCIDSSNSGA LEQAVKNCAG RPLINSVNGE QAKLDVILPI AKRYGAALIA LTTDDNGIPA TAEKRLKIAA KILNFADRCG LERKNIVFDY LVLSASSSPD QIGETLKAMR ESKRMYPECK LVLGVSNVSF GLPSRQTINS TFLKMAVAVG LDFAIANPHE NWDIDDPFAK NLLENKDKGA VKYMEVFTSF RKQIPETETE KLTTDKQLYF AILNGNRDSV DDILSQIIAS GDSNPFRTVN NNVLKALNVV GEKFASKEYF LPQIIMSAQA AQSAFAIVKA TLKKDEASSA GKIIIATVKG DMHDIGKNIV GAVLESYGFD VIDMGVNVDS QSIIDEAHKI NPIAIGLSAL MTTTMPEMGM VVKLKNAARV PTKIIVGGAA VTEKFAKEIG ADAYARDAME AAGYVKTLQK N // ID B1HTR8_LYSSC Unreviewed; 647 AA. AC B1HTR8; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 50. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=Bsph_0175 {ECO:0000313|EMBL:ACA37809.1}; OS Lysinibacillus sphaericus (strain C3-41). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; OC Lysinibacillus. OX NCBI_TaxID=444177 {ECO:0000313|EMBL:ACA37809.1, ECO:0000313|Proteomes:UP000002164}; RN [1] {ECO:0000313|EMBL:ACA37809.1, ECO:0000313|Proteomes:UP000002164} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C3-41 {ECO:0000313|EMBL:ACA37809.1, RC ECO:0000313|Proteomes:UP000002164}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ACA37809.1; -; Genomic_DNA. DR RefSeq; WP_012291978.1; NC_010382.1. DR RefSeq; YP_001695939.1; NC_010382.1. DR ProteinModelPortal; B1HTR8; -. DR STRING; 444177.Bsph_0175; -. DR EnsemblBacteria; ACA37809; ACA37809; Bsph_0175. DR KEGG; lsp:Bsph_0175; -. DR PATRIC; 22412811; VBILysSph89750_0328. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; LSPH444177:GJEL-189-MONOMER; -. DR Proteomes; UP000002164; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002164}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ACA37809.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000002164}; KW Transferase {ECO:0000313|EMBL:ACA37809.1}. SQ SEQUENCE 647 AA; 71533 MW; 62F99D8AB52B6181 CRC64; MRRNNNDESL KPSFYIKEGF LLYRDRGREA RFMGLLERLK THVLTADGAI GTVLYGYGLE YCHEEMNVQR PELIEKIHRE YIAAGADIIQ TNTYGANAIK LARYGLESSV QRFNEAAITI AKRAAADGGQ FVLGTIGGIR GIRKSDATLN DILKTVEEQA SVLLAGNPDG LLLETYYDFE ELTATLKMLR AKTNIPIIAQ VSMHEPGVLQ NGMSLNIALH ELEILGADIV GVNCRLGPYH TIQAFEGVEL PEKAFMSAYP NASLLDLEDG RVVYESEADY FGRAAVELRD QGVRLIGGCC GTTPKHIAAA KKYLEELSPV SEKYAKPAKI EIVRDAEPAK YEPLHEKVKR ERSVIVELDT PRHLEIEGFL EGAKQLYEAG ADVVMMADNS LASPRISNIA MGALLKSTNG VRPLTHITCR DRNLIGLQSH LMGLNALGIH DVLAVTGDPT KVGDFPGATS VYDVSSMELI QLIKQLNEGV SFSGKPLRKK ANFSVAAAFN PNVRVLDRAV ARLEKKIEHG ADYFISQPVY TKEKMIEIYE ATKHLQAPIY IGIMPVTSYK SAEFLHHEVP GIKLSEDALA RMKACGEDKE RATLEGIAIA KELVEVAAQY FNGIYLITPF LRYDVTLELM KYIEQLDEQK KGVSING // ID B1HTR9_LYSSC Unreviewed; 1143 AA. AC B1HTR9; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 55. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACA37810.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ACA37810.1}; GN OrderedLocusNames=Bsph_0176 {ECO:0000313|EMBL:ACA37810.1}; OS Lysinibacillus sphaericus (strain C3-41). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; OC Lysinibacillus. OX NCBI_TaxID=444177 {ECO:0000313|EMBL:ACA37810.1, ECO:0000313|Proteomes:UP000002164}; RN [1] {ECO:0000313|EMBL:ACA37810.1, ECO:0000313|Proteomes:UP000002164} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C3-41 {ECO:0000313|EMBL:ACA37810.1, RC ECO:0000313|Proteomes:UP000002164}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000817; ACA37810.1; -; Genomic_DNA. DR RefSeq; WP_012291979.1; NC_010382.1. DR RefSeq; YP_001695940.1; NC_010382.1. DR ProteinModelPortal; B1HTR9; -. DR STRING; 444177.Bsph_0176; -. DR EnsemblBacteria; ACA37810; ACA37810; Bsph_0176. DR GeneID; 6023274; -. DR KEGG; lsp:Bsph_0176; -. DR PATRIC; 22412813; VBILysSph89750_0329. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; LSPH444177:GJEL-190-MONOMER; -. DR Proteomes; UP000002164; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002164}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACA37810.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002164}; KW Transferase {ECO:0000313|EMBL:ACA37810.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 725 725 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1143 AA; 126271 MW; 963FEC8CBD9AAA13 CRC64; MAKHLIEEQL DKRILILDGA MGTMLQNENL TADDFGGEEL DGCNENLVLT RPDVIEKIHH KYLEAGADII CTNTFGGTPL VLNEYSLGAK AEEINKRAVE IARQAVDNYS TSDWPRFVAG AMGPTTKTLS VTGGITFDEL EENFYVQAKA LIEAGADVLL LETSQDMLNV KAGTLGVTRA FEKTGKELPV MISGTIEPMG TTLAGQTIDA FYISIEHIQP LSVGLNCATG PEFMTDHIRS LAELSTGYIS CYPNAGLPDE EGCYHESPES LSQKLKGFAE KGWLNIVGGC CGTTPAHIAA IREALKDEKP RQLPEKTHGH VVSGIEPLLY DDSMRPLFIG ERTNVIGSRK FKNLIIDGKF EEAAEIARAQ VKNGAHVIDI CLANPDRDEL ADIRGFMQEV VKKVKVPLVI DSTDEKVIEE ALKFSQGKAI INSINLEDGE ERFDAVLPLV KKYGASLVVG TIDETGMAVD RHRKLEIAER SYQLLTEKWG IEPEDIIFDP LMFPVGTGDE QYIGSALETI EGIRLIKEKM PRTLTVLGVS NISFGLPPVG REVLNAVYLY HCTQAGLDYA IVNTEKLERY ASIPEAEIKL ANDLLFNTND ETLAVFTDFY RDKKKEKTEA DIPKTVEGRL AYYILEGTKE GLIADLEAAR EIFETPLDII NGPLMNGMAE VGRLFNDNQL IVAEVLQSAG VMKAAVAHLE QYMEKNEESA GKGKMVLATV KGDVHDIGKN LVDIILSNNG YKVVDLGIKV TPAQLIEAIR KEKPDFIGLS GLLVKSAQQM VTTAQDFKEA GIDVPILVGG AALSRRFTET KIADEYGGPV IYSKDAMQGL EQANLLMGEG TRENFLAEIA ESRQKRLEAD EKRAARPAKE VTIKPARTVK EAPVFLPADL RRHVKKEYAV SHLYPYVNMR TLLGHHLGLK GQVQPLLDAG DPRATELKDL VDDYLKSDLL KPSGLYQFFP AQADGDDVII YDPADSKTEI ERFTFPRQQI DPFLCLADFL RTVESGEMDY IALMVVTAGQ GVMAKARQLK EDGKFLESHA LQSTALELAE GFAERMHQEI RDQWGFPDVT DFTMRDRFAA KYQGQRFSFG YPACPNLEDQ EKLFGLLKPE DIGVHLTEGF MMEPEASVSA IVFAHPDARY FNV // ID B1ILP3_CLOBK Unreviewed; 792 AA. AC B1ILP3; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 29-APR-2015, entry version 47. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:ACA43594.1}; GN OrderedLocusNames=CLD_2933 {ECO:0000313|EMBL:ACA43594.1}; OS Clostridium botulinum (strain Okra / Type B1). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=498213 {ECO:0000313|EMBL:ACA43594.1, ECO:0000313|Proteomes:UP000008541}; RN [1] {ECO:0000313|EMBL:ACA43594.1, ECO:0000313|Proteomes:UP000008541} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Okra / Type B1 {ECO:0000313|Proteomes:UP000008541}; 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 ----------------------------------------------------------------------- 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; ACA43594.1; -; Genomic_DNA. DR RefSeq; WP_015957447.1; NC_010516.1. DR RefSeq; YP_001781255.1; NC_010516.1. DR ProteinModelPortal; B1ILP3; -. DR STRING; 498213.CLD_2933; -. DR EnsemblBacteria; ACA43594; ACA43594; CLD_2933. DR KEGG; cbb:CLD_2933; -. DR PATRIC; 19403726; VBICloBot127283_1767. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CBOT498213:GCNI-1680-MONOMER; -. DR Proteomes; UP000008541; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008541}; KW Methyltransferase {ECO:0000313|EMBL:ACA43594.1}; KW Transferase {ECO:0000313|EMBL:ACA43594.1}. SQ SEQUENCE 792 AA; 87452 MW; A648C013553D4EDD CRC64; MNIKDYIKEN VLIFDGAMGT MLQKLGLKIS DLPEELNILE PEKIINIHKK YIEAGAKVVT TNTFGANEIK LKQSKFSLES IIDKAIDNVK KAGKNEEILI ALDIGPIGQL LEPMGTLKFE EAYEIFKRQI VQGQKSGADI ILIETMTDLY EAKAAILAAK ENTNLPVFCT MTFEKNKRTF TGCTPLSMVL TLEGLGVDAL GVNCSLGPNE LGDIVDEIIK YSSIPIMVQP NAGLPTIKEG RTIYNIKPKE FADFQRSIVE KGVRIVGGCC GTTDEFIREI VYSLKDVEIK NSKENNICGV CSPTKTVLID GVKIIGERIN PTGKKLFKEA LRNNDIDYIL KEAISQVESG ADILDVNVGL PEIDEEDTMK KVIKEIQSII DTPLQIDSNN PKVIEKALRV YNGKSIVNSV NGEDKVLDNV LPLIKKYGAA VVGLTLDDKG IPKKAEERLK IAEKIANKAL DYGIRREDIF IDCLVLTASA QQEDVGETLK AVNLVKEKLN VKTILGISNI SFGLPNRELI NKTFLAMSLQ SGLDLPILNP NNKEMINIIN AFKVLNNQDI GAANYIDMYG NETSNSNGLK IQSGNLTLKE IVMKGIKEEA YSKTKELLKD RGELSIINEE LIPALDEVGE KYEKGIIFLP QLIQSAETVK NAFTAIKEKL REDNSPKINK GKILMATVKG DIHDIGKNIV KVILENYGFD IIDLGKDVET ERIVEEVKKN NIKLVGLSAL MTTTVNSMKD TIKALKESGM DCKVFVGGAV LNKEYAEMIN ADYYAKDAKE AVDIAKRFFG GF // ID B1J6P9_PSEPW Unreviewed; 1235 AA. AC B1J6P9; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 29-APR-2015, entry version 53. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACA72391.1}; GN OrderedLocusNames=PputW619_1888 {ECO:0000313|EMBL:ACA72391.1}; OS Pseudomonas putida (strain W619). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=390235 {ECO:0000313|EMBL:ACA72391.1, ECO:0000313|Proteomes:UP000000720}; RN [1] {ECO:0000313|Proteomes:UP000000720} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=W619 {ECO:0000313|Proteomes:UP000000720}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000949; ACA72391.1; -; Genomic_DNA. DR RefSeq; WP_012313784.1; NC_010501.1. DR RefSeq; YP_001748760.1; NC_010501.1. DR ProteinModelPortal; B1J6P9; -. DR SMR; B1J6P9; 655-1235. DR STRING; 390235.PputW619_1888; -. DR EnsemblBacteria; ACA72391; ACA72391; PputW619_1888. DR KEGG; ppw:PputW619_1888; -. DR PATRIC; 19953608; VBIPsePut93764_1904. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PPUT390235:GHHJ-1932-MONOMER; -. DR Proteomes; UP000000720; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000720}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1235 AA; 135124 MW; 8D5C733F86E7F557 CRC64; MSDRSARLQA LQHALNERIL ILDGGMGTMI QSYRLEEHDY RGTRFADWPS DVKGNNDLLL LSRPDVIAAI EKAYLDAGAD ILETNTFNAT QISQADYGME SLVYELNVQG ARIARQVADA KTLETPDKPR FVAGVLGPTS RTCSISPDVN DPGYRNVTFD ELVENYIEAT RGLIEGGADL ILIETIFDTL NAKAAIFAVQ QVFEDDGIEL PIMISGTITD ASGRTLSGQT TEAFWNSVRH AKPISVGLNC ALGAKDLRPY LEELSTKADT HVSAHPNAGL PNAFGEYDET PAEMAAVVEE FAASGFLNII GGCCGTTPGH IQAIAEAVAK YKPRQIPTIA KACRLSGLEP FTIDRQSLFV NVGERTNITG SAKFARLIRE ENYTEALEVA LQQVEAGAQV IDINMDEGML DSQAAMVRFL NMIAGEPDIS RVPIMIDSSK WEVIEAGLKC IQGKGIVNSI SMKEGVEQFK HHARLCKRYG AAVVVMAFDE VGQADTAARK KEICQRSYDI LVNEVGFPPE DIIFDPNIFA VATGIEEHNN YAVDFIEACA YIRDHLPHAL SSGGVSNVSF SFRGNNPVRE AIHSVFLFHA IRNGLTMGIV NAGQLEIYDE IPAELRERVE DVVLNRTPEG TDALLAIADD YKGGGATKEV ENEAWRSLPV GKRLEHALVK GITAHIVEDT EECRQQCARP IEVIEGPLMS GMNVVGDLFG AGKMFLPQVV KSARVMKQAV AHLIPFIEAE KGDKPEAKGK ILMATVKGDV HDIGKNIVGV VLGCNGYDIV DLGVMVPAEK ILQTARDEKC DIIGLSGLIT PSLDEMVHVA REMQRQGFEL PLMIGGATTS KAHTAVKIEP KYSNDAVIYV TDASRAVGVA TQLLSKELKP GFVEKTRLDY IEVRERTANR SARTERLSYA QAVAAKPKYD WAAYQPAVPA FTGVKVLDNI DLRTLAEYID WTPFFISWDL AGKFPRILTD EVVGEAATSL YKDAREMLDK LIDEKLISAR AVFGFWPANQ VADDDIQVYG DNGQPLATLH HLRQQTIKPD GKPNLSLADF VAPKDSGVTD YVGGFITTAG IGAEEVAKAY QDKGDDYNSI MVKALADRLA EACAEWLHEQ VRKEHWGYAR DEHLDNEALI KEQYSGIRPA PGYPACPDHT EKETLFRLLD GTAIGETGPS GVFLTEHFAM FPAAAVSGWY FAHPQAQYFA VGKIDKDQID SYSARKGQDV SVSERWLAPN LGYDS // ID B1JFL3_PSEPW Unreviewed; 299 AA. AC B1JFL3; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 34. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACA75597.1}; GN OrderedLocusNames=PputW619_5121 {ECO:0000313|EMBL:ACA75597.1}; OS Pseudomonas putida (strain W619). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=390235 {ECO:0000313|EMBL:ACA75597.1, ECO:0000313|Proteomes:UP000000720}; RN [1] {ECO:0000313|Proteomes:UP000000720} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=W619 {ECO:0000313|Proteomes:UP000000720}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; ACA75597.1; -; Genomic_DNA. DR RefSeq; WP_012316873.1; NC_010501.1. DR RefSeq; YP_001751966.1; NC_010501.1. DR ProteinModelPortal; B1JFL3; -. DR STRING; 390235.PputW619_5121; -. DR EnsemblBacteria; ACA75597; ACA75597; PputW619_5121. DR KEGG; ppw:PputW619_5121; -. DR PATRIC; 19960222; VBIPsePut93764_5155. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; PYVDVWL; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; PPUT390235:GHHJ-5216-MONOMER; -. DR Proteomes; UP000000720; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000720}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ACA75597.1}; KW Transferase {ECO:0000313|EMBL:ACA75597.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 207 207 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 299 AA; 31654 MW; 4EC711F6396AAD7A CRC64; MGERTLEILD GGMGRELQRR GAPFRQPEWS ALALSEAPEA VVAVHAAYIE AGAAVITSNS YAVVPFHIGE DRFADEGFAL AATAGQLART AADASPRPVR VAGSLPPLFG SYRPDLFEPQ RVSEVLLPLV VGLAPYVDLW LAETQSAIAE VQAVAGQLPA DGKPLWVSFT LQDEEVGDVP QLRSGESVTA AAEAVATLGV KAMLFNCSQP EVIGAAIDAA REVFERLGVD IAIGAYANAF PPQPKDATAN DGLDELREDL DPPGYLSWAQ DWRQRGASLL GGCCGIGPEH IAELKRNLS // ID B1JZC3_BURCC Unreviewed; 355 AA. AC B1JZC3; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 41. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACA92089.1}; GN OrderedLocusNames=Bcenmc03_2931 {ECO:0000313|EMBL:ACA92089.1}; OS Burkholderia cenocepacia (strain MC0-3). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=406425 {ECO:0000313|EMBL:ACA92089.1, ECO:0000313|Proteomes:UP000002169}; RN [1] {ECO:0000313|Proteomes:UP000002169} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC0-3 {ECO:0000313|Proteomes:UP000002169}; 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 ----------------------------------------------------------------------- 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; ACA92089.1; -; Genomic_DNA. DR RefSeq; WP_006477666.1; NC_010508.1. DR RefSeq; YP_001766211.1; NC_010508.1. DR STRING; 406425.Bcenmc03_2931; -. DR EnsemblBacteria; ACA92089; ACA92089; Bcenmc03_2931. DR KEGG; bcm:Bcenmc03_2931; -. DR PATRIC; 19093120; VBIBurCen61509_3041. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; BCEN406425:GHD9-3005-MONOMER; -. DR Proteomes; UP000002169; Chromosome 1. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002169}; KW Methyltransferase {ECO:0000313|EMBL:ACA92089.1}; KW Transferase {ECO:0000313|EMBL:ACA92089.1}. SQ SEQUENCE 355 AA; 38239 MW; 6857B74674E6F938 CRC64; MSATPLAASV PLDARYTRGA ALPALLKSRI LILDGAMGTM IQRYKLDEAA YRGERFKDFP RDIKGNNELL SLTQPQIIRE IHDQYFAAGA DIVETNTFGA TTVAQADYGM EDLVVEMNVA SAKLARESAA KYATPDKPRF VAGAIGPTPK TASISPDVND PGARNVTFDE LRTSYYQQAK ALLDGGVDLF LVETIFDTLN AKAALFALDE LFEDTGERLP IMISGTVTDA SGRILSGQTV EAFWNSLRHA KPLTFGLNCA LGAALMRPYI AELAKLCDTY VSCYPNAGLP NPMSDTGFDE TPDVTSGLLK EFAQAGLVNL AGGCCGTTPE HIAEIAKALA DVKPRRWPNQ YSDNA // ID B1KCG4_BURCC Unreviewed; 313 AA. AC B1KCG4; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 35. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACA95911.1}; GN OrderedLocusNames=Bcenmc03_6804 {ECO:0000313|EMBL:ACA95911.1}; OS Burkholderia cenocepacia (strain MC0-3). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=406425 {ECO:0000313|EMBL:ACA95911.1, ECO:0000313|Proteomes:UP000002169}; RN [1] {ECO:0000313|Proteomes:UP000002169} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC0-3 {ECO:0000313|Proteomes:UP000002169}; 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 3 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; CP000960; ACA95911.1; -; Genomic_DNA. DR RefSeq; WP_012337273.1; NC_010512.1. DR RefSeq; YP_001774406.1; NC_010512.1. DR ProteinModelPortal; B1KCG4; -. DR STRING; 406425.Bcenmc03_6804; -. DR EnsemblBacteria; ACA95911; ACA95911; Bcenmc03_6804. DR KEGG; bcm:Bcenmc03_6804; -. DR PATRIC; 19095342; VBIBurCen61509_4142. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; DVITANS; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; BCEN406425:GHD9-6891-MONOMER; -. DR Proteomes; UP000002169; Chromosome 3. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002169}; KW Methyltransferase {ECO:0000313|EMBL:ACA95911.1}; KW Transferase {ECO:0000313|EMBL:ACA95911.1}. SQ SEQUENCE 313 AA; 32608 MW; 096BF7FBB0E2379E CRC64; MHGITVLDGG MGRELARMGA PFRQPEWSAL ALMEAPHYVG LAHDAFIAAG ADVITANSYA VVPFHIGEQR FRRDGVALAA LAGQLARQAA DRAVRPVRVA GSLPPTGGSY RPDLFDAARA DAILATLVDG LDPYVDLWLA ETQSLTGEID AVRRALGANR KPLWVSFTLR DDVGADTGAG PVLRSGQALD EAIDAAVSAR ARALLFNCSQ PEAMGAAIET VQRTLAGMGA GAALMIGAYA NAFPPQRADA RANEELDVLR GDIDPPGYAK WAEQWLALGA QIVGGCCGIG PGHIAALRDA VDARNAGHTG SGQ // ID B1KH32_SHEWM Unreviewed; 1251 AA. AC B1KH32; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 01-APR-2015, entry version 52. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACA88344.1}; GN OrderedLocusNames=Swoo_4088 {ECO:0000313|EMBL:ACA88344.1}; OS Shewanella woodyi (strain ATCC 51908 / MS32). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=392500 {ECO:0000313|EMBL:ACA88344.1, ECO:0000313|Proteomes:UP000002168}; RN [1] {ECO:0000313|EMBL:ACA88344.1, ECO:0000313|Proteomes:UP000002168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51908 / MS32 {ECO:0000313|Proteomes:UP000002168}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000961; ACA88344.1; -; Genomic_DNA. DR RefSeq; WP_012326673.1; NC_010506.1. DR RefSeq; YP_001762439.1; NC_010506.1. DR ProteinModelPortal; B1KH32; -. DR SMR; B1KH32; 675-1251. DR STRING; 392500.Swoo_4088; -. DR EnsemblBacteria; ACA88344; ACA88344; Swoo_4088. DR KEGG; swd:Swoo_4088; -. DR PATRIC; 23610841; VBISheWoo126588_4206. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SWOO392500:GI2C-4222-MONOMER; -. DR Proteomes; UP000002168; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002168}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002168}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 260 260 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 781 781 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1251 AA; 138504 MW; E71CC0595CD4D0DE CRC64; MTTGTLRTKN IKAKGQQLEQ QLKQQLSDGI LILDGAMGTM IQDCKFEEDA FRGEQFKEWH CDVKGNNDML VLTQPDAIKQ IHKDYLLAGA DIIETNTFNA TRIAMADYDM QEHSASINLE GARLARAAAD EVEQETGRSC YVAGVLGPTN RTCSISPDVN DPGYRNVSFD ELVEAYIESI NALVQGGADI LMVETIFDTL NAKAALFAIE TVFDEQDFRL PIMISGTITD ASGRTLTGQT TEAFYNSLRH VKPLSIGLNC ALGPKELRPY VEELSKISEC FVSAHPNAGL PNEFGGYDET PKQMADIIGE WAEEGFLNII GGCCGTTPDH IRVIREAVIK HPARKLPDIP VACRLSGLEP LTIDENSLFL NVGERTNVTG SAKFLRLIKT GEYEEALSVA RDQVENGAQI IDINMDEGML DGVEVMHKFL NLIASEPDIS RVPIMIDSSK WEVIEAGLKC IQGKGIVNSI SLKEGEEKFI EQAKLVKRYG AAAIIMAFDE TGQADTEARK VEICTRAYNV LVDKVGFPPE DIIFDPNIFA IATGIEEHDN YAVDFIEATR EIKRTLPHAM ISGGVSNVSF SFRGNNPVRE AIHAVFLYHA IQAGMDMGIV NAGQLAIYDD IDPELKEKVE AIVQNLPCSA VDKNGEATNN TEQLLEVAEK FRGDGAQAGK KEDLEWRTKP VNERLAHALV KGITDYIDED TEEARTAATR PLDVIEGPLM DGMNIVGDLF GSGKMFLPQV VKSARVMKKA VAYLNPYIEL EKVAGQSNGK ILMVTVKGDV HDIGKNIVGV VLACNGYEVI DLGVMVPVEK IIEVAKAENV DIIGMSGLIT PSLDEMVHNV KSFHKAGLTI PSIIGGATCS KIHTAVKIAP HAPTGAIYIA DASRAVPMVS KLINDDTRQA TIDEAYNEYD VMREKRLSQA KRKMITSIEA ARENRCQHDW ESYTPFVPNQ LGRQVFDDYP LEDLVDRIDW TPFFRSWELH GHFPKILDDE VVGEEARKLF SDGKAMLKKI IDEKWLTAKG VIGLFPANTV GHDDIELYTD ESRSELEMTT HHLRMQIERV GNDNFCLADF VAPKDSGVAD YMGGFAVTAG HGIDEHVERF EADHDDYSAI MLKCLADRLA EAFAERMHER VRKEFWGYAA DEVLDNEALI REKYKGIRPA PGYPACPDHT EKGLLWDLLK PDETIGLNIT ESFAMFPTAA VSGWYFAHPK SRYFGVTNIG RDQVEDYAAR KGMSVEEVER WLAPVLDYDP E // ID B1L1X1_CLOBM Unreviewed; 792 AA. AC B1L1X1; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 48. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:ACA56589.1}; GN OrderedLocusNames=CLK_1087 {ECO:0000313|EMBL:ACA56589.1}; OS Clostridium botulinum (strain Loch Maree / Type A3). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=498214 {ECO:0000313|EMBL:ACA56589.1, ECO:0000313|Proteomes:UP000000722}; RN [1] {ECO:0000313|EMBL:ACA56589.1, ECO:0000313|Proteomes:UP000000722} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Loch Maree / Type A3 {ECO:0000313|Proteomes:UP000000722}; 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 ----------------------------------------------------------------------- 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; ACA56589.1; -; Genomic_DNA. DR RefSeq; WP_012344441.1; NC_010520.1. DR RefSeq; YP_001787027.1; NC_010520.1. DR ProteinModelPortal; B1L1X1; -. DR STRING; 498214.CLK_1087; -. DR EnsemblBacteria; ACA56589; ACA56589; CLK_1087. DR KEGG; cbl:CLK_1087; -. DR PATRIC; 19388788; VBICloBot822_2007. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CBOT498214:GH05-1744-MONOMER; -. DR Proteomes; UP000000722; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000722}; KW Methyltransferase {ECO:0000313|EMBL:ACA56589.1}; KW Transferase {ECO:0000313|EMBL:ACA56589.1}. SQ SEQUENCE 792 AA; 87660 MW; 062436C5DF1E6B97 CRC64; MNIKDYIKEN ILIFDGAMGT MLQKLGLNIS DLPEELNILE PKKIINIHKK YIEAGAKVIT TNTFGANEIK LKQSKFSLES IIDKAIDNVK KARENKEILI ALDIGPIGQL LEPMGTLKFE EAYEIFKRQI VQGQKSGADI ILIETMTDLY EAKAAILAAK ENTNLPVFCT MTFEKNKRTF TGCTPLSMVL TLEGLGVDAL GVNCSLGPNE LGDIVDEIIK YSSIPIMVQP NAGLPTIKEG RTIYNIKPKE FADFQRSIVE KGVRIVGGCC GTTDEFIREI VYSLKDVKAK KLKENNICGV CSSTKAVLID GVKIIGERIN PTGKKLFKEA LRNNDTDYIL KEAISQVECG ADILDVNVGL PEINEEETMK KVIKEIQSII DTPLQIDSNN PKVIEKALRV YNGKAIVNSV NGEEEVLDSV LPLIKKYGAA VVGLTLDDKG IPKKAEERLK IAEKIVNKAL EYGIRREDIF IDCLVLTASA QQEDVGETLK AVALVKEKLK VKTILGVSNI SFGLPNRELI NKTFLAMSLQ SGLDLPILNP NNKEMINIIN AFKVLNNEDI GATNYIDMYG NETSNSKDVK IQRDNLTLKE IVIKGIKEGA YSKTKKLLKD RDELSIINEE LIPALDEVGE KYEKGIIFLP QLIQSAETVK KAFKAIKEKL REDNSPKINK GKILMATVKG DIHDIGKNIV KVILENYGFD IIDLGKDVEA DKIVEEVKKN NIKLVGLSAL MTTTVNSMKD TIKDLKESGI DCKVFVGGAV LNKEYAEMIN ADYYAKDAKE AVDIAKEFFG GF // ID B1LPH5_ECOSM Unreviewed; 1227 AA. AC B1LPH5; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 54. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACB17132.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ACB17132.1}; GN Name=metH {ECO:0000313|EMBL:ACB17132.1}; GN OrderedLocusNames=EcSMS35_4472 {ECO:0000313|EMBL:ACB17132.1}; OS Escherichia coli (strain SMS-3-5 / SECEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=439855 {ECO:0000313|EMBL:ACB17132.1, ECO:0000313|Proteomes:UP000007011}; RN [1] {ECO:0000313|EMBL:ACB17132.1, ECO:0000313|Proteomes:UP000007011} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SMS-3-5 / SECEC {ECO:0000313|Proteomes:UP000007011}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000970; ACB17132.1; -; Genomic_DNA. DR RefSeq; WP_000096003.1; NC_010498.1. DR RefSeq; YP_001746400.1; NC_010498.1. DR ProteinModelPortal; B1LPH5; -. DR SMR; B1LPH5; 651-1227. DR STRING; 439855.EcSMS35_4472; -. DR EnsemblBacteria; ACB17132; ACB17132; EcSMS35_4472. DR KEGG; ecm:EcSMS35_4472; -. DR PATRIC; 18437862; VBIEscCol6161_4586. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; ECOL439855:GHHB-4463-MONOMER; -. DR Proteomes; UP000007011; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007011}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACB17132.1}; KW Transferase {ECO:0000313|EMBL:ACB17132.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136019 MW; E7304A8527FA411B CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPAEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANTQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEACK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KMLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID B1LVN7_METRJ Unreviewed; 1250 AA. AC B1LVN7; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 54. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACB24118.1}; GN OrderedLocusNames=Mrad2831_2123 {ECO:0000313|EMBL:ACB24118.1}; OS Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM OS 2831). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=426355 {ECO:0000313|EMBL:ACB24118.1, ECO:0000313|Proteomes:UP000006589}; RN [1] {ECO:0000313|EMBL:ACB24118.1, ECO:0000313|Proteomes:UP000006589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27329 / DSM 1819 / JCM 2831 RC {ECO:0000313|Proteomes:UP000006589}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001001; ACB24118.1; -; Genomic_DNA. DR RefSeq; WP_012319098.1; NC_010505.1. DR RefSeq; YP_001754801.1; NC_010505.1. DR ProteinModelPortal; B1LVN7; -. DR SMR; B1LVN7; 660-909. DR STRING; 426355.Mrad2831_2123; -. DR EnsemblBacteria; ACB24118; ACB24118; Mrad2831_2123. DR GeneID; 23622262; -. DR KEGG; mrd:Mrad2831_2123; -. DR PATRIC; 22572576; VBIMetRad70578_2183. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; MRAD426355:GJB5-2145-MONOMER; -. DR Proteomes; UP000006589; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006589}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006589}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 254 254 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 318 318 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 771 771 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1250 AA; 136890 MW; 2F6355E1489FEFDF CRC64; MTDFAPVDGT EIAKALRQRA AEKILVLDGA MGTVIQRLKF SEEDFRGDRF KDHGHDQKGN NDLLILTQPD AIRQIHLDYF LAGADVCETN TFSGTTIAQA DYGMESIIHE LNAEGARLAR EAAKLAEQKD GRRRFVAGAI GPTNRTLSIS PDVNNPGFRA VTFDQVKQAY VEQVRGLIDG GAELILIETI FDTLNAKAAV AAAWQVFDET GIRLPIQISG TITDLSGRTL SGQTPAAFWH SLRHSEPLTF GLNCALGARE MRGHIAELSR ICDTLVCAYP NAGLPNEFGL YDESPEAMGK LVGEFAESGL VNMVGGCCGT TPDHIRAIAE AVAGKAPRPI PEVPRLMRLS GLEPFVLTPE IPFVNVGERT NVTGSAKFRK LITNGDYAAA LDVARDQVAA GAQVIDVNMD EGLLDSQKAM VEFLNLVAAE PDIARVPVMV DSSKFEVIEA GLKCIQGKPI VNSISMKEGE EKFIEAAKVC RSYGAAVVVM AFDEQGQADS YERKVEICTK AYRILTEQVG FPPEDIIFDP NIFAVATGIE EHNPYGVAFI EATRTIRETL PHAHISGGVS NLSFAFRGNE PVREAMHAVF LFHCIKAGMD MGIVNAGQLA VYDEIPAELR ELCEDVVLNR RDDSTERLLE AAERFKTGAS AQAKTADLTW REAPVEKRIE HALVNGITEY IVADTEEARQ KAERPLHVIE GPLMAGMNVV GDLFGSGKMF LPQVVKSARV MKQAVAYLEP FMEEEKRANG GDGKRQAAGK VLMATVKGDV HDIGKNIVGV VLACNNYEII DLGVMVPAAK ILETAKTEKV DIVGLSGLIT PSLDEMVHVA GEMEREGLDV PLLIGGATTS RVHTAVKIHP AYAKGQAVYV TDASRAVGVV SSLISKETRG ATIEKVRAEY AKVADAHKRS EADKQRLPLA KARTNAFKID WSAYKPAKPS FTGTRVYGSY EVADLVPYID WTPFLQTYEF KGRFPAILDD PEQGPAARAL YEDAQGMLKQ IVEERWFNPK AVIGFWPANS VGDDIALYTG ESRSERLATF HGLRQQLSKR DGRSNTCLSD FVAPAETGIA DYVGGFVVTA GLEEVRIAER FERANDDYRA ILVKALADRI AEAFAERMHE RVRKEFWGYA ADEAYGPDEL VLEKYDGIRP APGYPAQPDH TEKTTLFDLL KAERRIGVKL TESYAMWPGS SVSGIYIAHP EAHYFGVAKV ERDQVEDYAA RKGMDIREVE RWLGPILNYD PARYLAQAAE // ID B1MPF9_MYCA9 Unreviewed; 1253 AA. AC B1MPF9; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 29-APR-2015, entry version 51. DE SubName: Full=Chromosome, complete sequence {ECO:0000313|EMBL:CAM62210.1}; GN OrderedLocusNames=MAB_2129 {ECO:0000313|EMBL:CAM62210.1}; OS Mycobacterium abscessus (strain ATCC 19977 / DSM 44196). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium abscessus. OX NCBI_TaxID=561007 {ECO:0000313|EMBL:CAM62210.1, ECO:0000313|Proteomes:UP000007137}; RN [1] {ECO:0000313|Proteomes:UP000007137} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19977 / DSM 44196 {ECO:0000313|Proteomes:UP000007137}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CU458896; CAM62210.1; -; Genomic_DNA. DR ProteinModelPortal; B1MPF9; -. DR SMR; B1MPF9; 660-916. DR STRING; 561007.MAB_2129; -. DR EnsemblBacteria; CAM62210; CAM62210; MAB_2129. DR PATRIC; 17975978; VBIMycAbs55940_2168. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR OMA; QPFFNAW; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; MABS36809-WGS:GSQO-2141-MONOMER; -. DR BioCyc; MABS561007:GJTG-2141-MONOMER; -. DR Proteomes; UP000007137; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007137}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007137}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 253 253 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 316 316 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 779 779 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1253 AA; 137146 MW; CED3FCC5309130C6 CRC64; MTNLQPNVRP DCTEALTAAL EQRILVIDGA MGTAIQRDRP DEAGYRGERF ADWPSDLVGN NDLLTLTQPH IIEGIHREYL EAGADILETN TFNANAVSLS DYGMEELSYE LNYAGAALAR VAADEYSTPA KPRYVAGALG PTTRTASISP DVNDPGARNV SYDQLVAAYL EAANGLVDGG ADIILVETIF DSLNAKAAVF AIETLFEQRG RRWPIIISGT ITDASGRTLS GQVTEAFWNA IRHARPIAVG LNCALGAPEM RPYIAEMSRI ADTFVSCYPN AGLPNAFGEY DESPEHQAGY LAEFAEAGLV NLVGGCCGTA PAHIAEIAKV VEGVKPRDVP SIDVATRLSG LEPLNITDDS LFVNIGERTN ITGSARFRNL IKAEDYDTAL SVALQQVEVG AQVIDINMDE GMIDGVAAMD RFTKLIAAEP DISRVPVMID SSKWEVIEAG LKNVQGKPIV NSISMKEGEE KFIREARLCR KYGAAVVVMA FDEKGQADNL ERRKEICGRA YRILTEEVGF PAEDIIFDPN CFALATGIEE HATYGIDFIE ACAWIKENLP GVHISGGISN VSFSFRGNNP VREAIHAVFL FHAIKAGLDM GIVNAGALVP YDSIDSELRD RIEDVVLNRR ADAAERLLEI AERFNSTENS GGGDDRAAQE WRSLPVRERI THALVKGIDA HVDDDTEELR AEIAAAGGRP IEVIEGPLMD GMNVVGDLFG SGKMFLPQVV KSARVMKKAV AYLLPFIEAE KEDNGTAGDS KSKDTNGTIV MATVKGDVHD IGKNIVGVVL QCNNFEVIDL GVMVPAQKIL DAAKEHDADI IGLSGLITPS LDEMANFAVE MEREGLEIPL LIGGATTSRA HTAVKISPRR KGPVVWVKDA SRSVPVAAAL LDDKQRPGLL EATEKDYASL RERHAQKNER PTLTLEKARA NRTPVEWDGY TPPVPAQGLG VREFLDYDLA EVREYIDWQP FFNAWEMKGR FPDILNNPAT GEAARKLHDD AQQILDTLIK EKWLTANGVI GFFPANAVGP GFEDIEVYTD DTRTEVLTTL HNLRQQGEHR DGIPNRSLGD YIAPKETGLR DYIGAFAVTA GLGSQDKIME FKADLDDYSA ILLESIADRL AEAFAERMHQ RVRTEFWGFQ PDEQLDNEAL IGEKYRGIRP APGYPACPEH TEKVTLFDLL DVTKRTGIEL TESMAMWPGA AVSGWYFAHP QSQYFVVGRL AQDQVADYAK RKGWTLQEAE RWLGPNLGYN PED // ID B1MXY2_LEUCK Unreviewed; 303 AA. AC B1MXY2; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 27-MAY-2015, entry version 39. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACA82384.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ACA82384.1}; GN OrderedLocusNames=LCK_00551 {ECO:0000313|EMBL:ACA82384.1}; OS Leuconostoc citreum (strain KM20). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostocaceae; OC Leuconostoc. OX NCBI_TaxID=349519 {ECO:0000313|EMBL:ACA82384.1, ECO:0000313|Proteomes:UP000002166}; RN [1] {ECO:0000313|EMBL:ACA82384.1, ECO:0000313|Proteomes:UP000002166} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KM20 {ECO:0000313|EMBL:ACA82384.1, RC ECO:0000313|Proteomes:UP000002166}; 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 ----------------------------------------------------------------------- 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; ACA82384.1; -; Genomic_DNA. DR RefSeq; WP_012305090.1; NC_010471.1. DR RefSeq; YP_001727828.1; NC_010471.1. DR ProteinModelPortal; B1MXY2; -. DR STRING; 349519.LCK_00551; -. DR EnsemblBacteria; ACA82384; ACA82384; LCK_00551. DR KEGG; lci:LCK_00551; -. DR PATRIC; 32614381; VBILeuCit37309_0673. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; LCIT349519:GHNF-574-MONOMER; -. DR Proteomes; UP000002166; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002166}; KW Methyltransferase {ECO:0000313|EMBL:ACA82384.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002166}; KW Transferase {ECO:0000313|EMBL:ACA82384.1}. SQ SEQUENCE 303 AA; 33636 MW; 8312D70C0F018D67 CRC64; MTKFSELLLQ GPVILDGGLG SEIDKQHIAV ANNLWSASAL IQAPNLVRDI HQSYFNAGAQ IAIVDTYQAH PQTFVDSGLS ENEAYELIDL AVALARDGLK KSEKSLGIIA GSVGPYGAYL ANGAEYTGDY DLSIQAYQAF HRQRIKRLVH NNVDILALET MPNFKEAQAI ALLLQNEFPE VEAYLSFATE VGDHLWDGTR LAHAVAYFNQ FEQIKAIGIN CTAPDNILPA IMRIKPNTDK KVILYPNAGE VYNPETKRWV TNNEPINWRR LVPLWQHAGA DIIGGCCRTS PEDIREIHDI LQK // ID B1R6R5_CLOPF Unreviewed; 279 AA. AC B1R6R5; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EDT24010.1}; GN ORFNames=AC1_1817 {ECO:0000313|EMBL:EDT24010.1}; OS Clostridium perfringens B str. ATCC 3626. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=451754 {ECO:0000313|EMBL:EDT24010.1, ECO:0000313|Proteomes:UP000004342}; RN [1] {ECO:0000313|EMBL:EDT24010.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 3626 {ECO:0000313|EMBL:EDT24010.1}; 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. {ECO:0000313|EMBL:EDT24010.1}. 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; ABDV01000009; EDT24010.1; -; Genomic_DNA. DR RefSeq; WP_003457158.1; NZ_ABDV01000009.1. DR ProteinModelPortal; B1R6R5; -. DR EnsemblBacteria; EDT24010; EDT24010; AC1_1817. DR PATRIC; 30612587; VBICloPer46771_1389. DR Proteomes; UP000004342; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000004342}; KW Methyltransferase {ECO:0000313|EMBL:EDT24010.1}; KW Transferase {ECO:0000313|EMBL:EDT24010.1}. SQ SEQUENCE 279 AA; 30749 MW; 0FEE944B04642E5D CRC64; MKKLDLKNGV IIADGAMGTR IMELGVNLKE TPSELLNIKK PELIEKIHRE YIESGANLIL SNTFMCNIIN AKRNNYNLEE VVGAGIHIAK KACGDGGLVA LDIGPLSYYI EENDSSFKEI VYENTERIIN ASKDKFDLVI FETLGSLKEG EFAVKKAKTL TDKPVICSFT LAGKKDIPNF IKNIVSTLET LGVDSLGINC TGYEEILMAL DILKENTNLP IMIKANLGIP KKVGEELVYD KTLEEFKNLS KRALEKGVNI IGGCCGTTPE YIRAICNLK // ID B1RID4_CLOPF Unreviewed; 279 AA. AC B1RID4; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EDT26250.1}; GN ORFNames=AC5_1790 {ECO:0000313|EMBL:EDT26250.1}; OS Clostridium perfringens CPE str. F4969. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=451756 {ECO:0000313|EMBL:EDT26250.1, ECO:0000313|Proteomes:UP000003224}; RN [1] {ECO:0000313|EMBL:EDT26250.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F4969 {ECO:0000313|EMBL:EDT26250.1}; 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. {ECO:0000313|EMBL:EDT26250.1}. 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; ABDX01000020; EDT26250.1; -; Genomic_DNA. DR RefSeq; WP_003469072.1; NZ_ABDX01000020.1. DR ProteinModelPortal; B1RID4; -. DR EnsemblBacteria; EDT26250; EDT26250; AC5_1790. DR PATRIC; 30628536; VBICloPer69736_2213. DR Proteomes; UP000003224; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000003224}; KW Methyltransferase {ECO:0000313|EMBL:EDT26250.1}; KW Transferase {ECO:0000313|EMBL:EDT26250.1}. SQ SEQUENCE 279 AA; 30951 MW; 2D834FC62EE58EAD CRC64; MKNLNLKNGV IIADGAMGTR IMELGVNLKE TPSELLNIKK PELIEKIHRE YIESGANLIL SNTFMCNIIN AKRNNYNLEE IIEAGISIAK KACGYHGLVA LDIGPLSYYI EENDSSFKEI VYENTERIIN ASKDKFDLVI FETLGSLKEG EFAVKKAKTL TDKPVICSFT LAGKRDIPNF IKNIVSTLET LGVDSLGINC TGYEEILMAL DILKKNTNLP IMIKANLGIP KKVGEELIYE QTPEEFKNLS KRALEKGVNI IGGCCGTTPE YIRAICNLK // ID B1SCD2_9STRE Unreviewed; 618 AA. AC B1SCD2; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 27-MAY-2015, entry version 31. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=STRINF_00308 {ECO:0000313|EMBL:EDT48384.1}; OS Streptococcus infantarius subsp. infantarius ATCC BAA-102. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=471872 {ECO:0000313|EMBL:EDT48384.1}; RN [1] {ECO:0000313|EMBL:EDT48384.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-102 {ECO:0000313|EMBL:EDT48384.1}; 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] {ECO:0000313|EMBL:EDT48384.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-102 {ECO:0000313|EMBL:EDT48384.1}; 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 (MAR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDT48384.1}. 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; ABJK02000012; EDT48384.1; -; Genomic_DNA. DR RefSeq; WP_006531232.1; NZ_DS572684.1. DR ProteinModelPortal; B1SCD2; -. DR EnsemblBacteria; EDT48384; EDT48384; STRINF_00308. DR PATRIC; 25725170; VBIStrInf64650_0269. DR OrthoDB; EOG6SNDP1; -. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EDT48384.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EDT48384.1}. SQ SEQUENCE 618 AA; 68003 MW; D80CB4C693291011 CRC64; MSGLLERLKT DILVADGAMG TLLYANGLDN CYEAYNLTHP EKVLAIHKAY INAGADVIQT NTYAAKRHRL GGYGYGDKIK EINQAGVKIA RQAAGEDTFV LGTVGALRGL KQCELSLDEI IKETLEQVGY LLETKEIDGL LFETYYDEEE IIEILKAVRP LTKLPIITNI SIHEAGITEN GRPLVEIFGK LVMLGADVVG LNCHLGPYHM IQSLKQVPLF AQSYLSVYPN ASLLSFVDDN GSGQYGFSQN ADYFGKSAEL LVAEGARLIG GCCGTTPDHI RAVKRAIKGL KPVSRKFVTP MVEEAELIKA VKQSETIVDK VNRKVTIIAE LDPPKTLDIR KFTKGVKALD EAGVSAITLA DNSLAKTRIC NVSIASLLKN EISTPFLLHL SCRDHNMIGL QSRLLGMDVL GFHQVLAITG DPSKIGDFPG ATSVYDATSF KLLELIKQLN KGIGYSGASI KKETTFTAAA AFNPNVKNLS RCGRLIERKI AAGADCFITQ PIFNSEIIEN LAKLTRDYET PFFVGIMPIT SYNNAIFLHN EVPGIQLSDN FLAKLEAVKD DKEKCQQLAL EESKQLIDHA LKFFNGIYLI TPFMRYDLTV ELVEYIHQKV EQSHQIIP // ID B1SCH2_9STRE Unreviewed; 314 AA. AC B1SCH2; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EDT48432.1}; GN ORFNames=STRINF_00356 {ECO:0000313|EMBL:EDT48432.1}; OS Streptococcus infantarius subsp. infantarius ATCC BAA-102. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=471872 {ECO:0000313|EMBL:EDT48432.1}; RN [1] {ECO:0000313|EMBL:EDT48432.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-102 {ECO:0000313|EMBL:EDT48432.1}; 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] {ECO:0000313|EMBL:EDT48432.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-102 {ECO:0000313|EMBL:EDT48432.1}; 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 (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. {ECO:0000313|EMBL:EDT48432.1}. 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; ABJK02000012; EDT48432.1; -; Genomic_DNA. DR RefSeq; WP_006531280.1; NZ_DS572684.1. DR ProteinModelPortal; B1SCH2; -. DR EnsemblBacteria; EDT48432; EDT48432; STRINF_00356. DR PATRIC; 25725262; VBIStrInf64650_0315. DR OrthoDB; EOG6C019S; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDT48432.1}; KW Transferase {ECO:0000313|EMBL:EDT48432.1}. SQ SEQUENCE 314 AA; 34709 MW; 71724B2C48F401E6 CRC64; MGKLKELLES TDYLILDGAL GTELENRGHD VSGKLWSAKY LLENPQIIQE LHEDYLRSGA DIVTTSSYQA TVQGLEDYGL SEKEALDTIV LTVELAKNAR QNFWQSLSDD EKKKRVYPLI AGDVGPYAAY LADGSEYTGD YQLSKESFKD FHRSRIQTLL AAGSDFLAIE TIPNMTEATA LVELLADEFP DTEAYMSFTA QDSQSISDGT LMTEVAKLCD SSKQILAFGI NCSRPAIISD LLKASRTISQ KPLVTYPNSG EIYDGATQTW KSLPDNSHTL CENSQVWHKL GAKIVGGCCR TRPEDIKLLA DKLK // ID B1T8D2_9BURK Unreviewed; 355 AA. AC B1T8D2; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EDT40171.1}; GN ORFNames=BamMEX5DRAFT_4048 {ECO:0000313|EMBL:EDT40171.1}; OS Burkholderia ambifaria MEX-5. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=396597 {ECO:0000313|EMBL:EDT40171.1}; RN [1] {ECO:0000313|EMBL:EDT40171.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MEX-5 {ECO:0000313|EMBL:EDT40171.1}; 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. {ECO:0000313|EMBL:EDT40171.1}. 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; ABLK01000142; EDT40171.1; -; Genomic_DNA. DR RefSeq; WP_006759889.1; NZ_ABLK01000142.1. DR EnsemblBacteria; EDT40171; EDT40171; BamMEX5DRAFT_4048. DR PATRIC; 38387746; VBIBurAmb126694_4072. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDT40171.1}; KW Transferase {ECO:0000313|EMBL:EDT40171.1}. SQ SEQUENCE 355 AA; 38259 MW; 1909D41478CC556F CRC64; MSATPLAASV PLDAPYTRGA ELPALLKSRI LILDGAMGTM IQRYKLDEAA YRGERFKDFP RDIKGNNELL SLTQPQIIRE IHDQYFAAGA DIVETNTFGA TTVAQADYGM EDLVVEMNVE SARLARESAV RYATPDKPRF VAGAIGPTPK TASISPDVND PGARNVTFDE LRSAYYQQAK ALLDGGVDLF LVETIFDTLN AKAALFALDE LFEDTGERLP IMISGTVTDA SGRILSGQTV EAFWNSLRHA KPLTFGLNCA LGAALMRPYI AELAKLCDTY VSCYPNAGLP NPMSDTGFDE TPDVTSGLLK EFAQAGLVNL AGGCCGTTPE HIAEIAKALA DVKPRRWPGH YSDAA // ID B1V5W3_CLOPF Unreviewed; 279 AA. AC B1V5W3; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Transcriptional regulator, TetR family {ECO:0000313|EMBL:EDT70794.1}; GN ORFNames=CJD_0040 {ECO:0000313|EMBL:EDT70794.1}; OS Clostridium perfringens D str. JGS1721. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=488537 {ECO:0000313|EMBL:EDT70794.1}; RN [1] {ECO:0000313|EMBL:EDT70794.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=JGS1721 {ECO:0000313|EMBL:EDT70794.1}; 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. {ECO:0000313|EMBL:EDT70794.1}. 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; ABOO01000037; EDT70794.1; -; Genomic_DNA. DR RefSeq; WP_003475766.1; NZ_ABOO01000037.1. DR ProteinModelPortal; B1V5W3; -. DR EnsemblBacteria; EDT70794; EDT70794; CJD_0040. DR PATRIC; 30636090; VBICloPer13534_2650. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 279 AA; 31012 MW; 79BCFD8921E0DC71 CRC64; MKNLDLKNGV IIADGAMGTR IMELGVNLKE TPSELLNIKK PELIEKIHRE YIESGANLIL SNTFMCNIIN AKRNNYNLEE VIEAGISIAK KACGDHGLVA LDIGPLSYYI EENDSSFKEI VYENTERIIN ASKDKFDLVI FETLGSLKEG EFAVKKAKTL TDKKVICSFT LAYKKDIPNF IKNMVLTLEP LGVDALGINC TGYEEILMAL DILKENTNLP IMIKANLGIP KKVGEELVYD KTLEEFKNLS KRALEKGVNI IGGCCGTTPE YIRAICNLK // ID B1VCK1_ECOLX Unreviewed; 310 AA. AC B1VCK1; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:CEE10427.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:CEE10427.1}; DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:CDY55060.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:CDY55060.1}; DE SubName: Full=MmuM protein {ECO:0000313|EMBL:CAP07823.1}; GN Name=MmuM {ECO:0000313|EMBL:CAP07823.1}; GN Synonyms=mmuM {ECO:0000313|EMBL:CDY55060.1}; GN ORFNames=BN1008_4142 {ECO:0000313|EMBL:CEE10427.1}, GN ECHMS174_00266 {ECO:0000313|EMBL:CDY55060.1}, GN ECRV308_00266 {ECO:0000313|EMBL:CDZ19154.1}, GN EL78_3267 {ECO:0000313|EMBL:KGM72745.1}, GN IPF_81 {ECO:0000313|EMBL:CAP07823.1}, GN LS90_24240 {ECO:0000313|EMBL:KGP47200.1}, GN UO92_25330 {ECO:0000313|EMBL:KJH99407.1}, GN UO94_24600 {ECO:0000313|EMBL:KJH98393.1}, GN UO95_25890 {ECO:0000313|EMBL:KJI09844.1}; OS Escherichia coli. OG Plasmid pIP1206 {ECO:0000313|EMBL:CAP07823.1}, and OG Plasmid pMR0713 {ECO:0000313|EMBL:KGP47200.1}. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562 {ECO:0000313|EMBL:CAP07823.1}; RN [1] {ECO:0000313|EMBL:CAP07823.1} RP NUCLEOTIDE SEQUENCE. RC PLASMID=pIP1206 {ECO:0000313|EMBL:CAP07823.1}; RA Perichon B., Bogaerts P., Lambert T., Frangeul L., Courvalin P., RA Galimand M.; RT "Sequence of conjugative plasmid pIP1206 mediating resistance to RT aminoglycosides by 16S rRNA methylation and to hydrophilic RT fluoroquinolones."; RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CEE10427.1} RP NUCLEOTIDE SEQUENCE. RA Montero Manuel; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:KGM72745.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=G5 {ECO:0000313|EMBL:KGM72745.1}; RA Zschuettig A., Auerbach C., Meltke S., Eichhorn C., Brandt M., RA Blom J., Goesmann A., Jarek M., Scharfe M., Zimmermann K., RA Wassenaar T.M., Gunzer F.; RT "Complete sequence of probiotic Symbioflor2 E. coli strain G3/10 and RT draft sequences of Symbioflor2 strains G1/2, G4/9, G5, G6/7 and G8."; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:CDY55060.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=K-12 substr. HMS174 {ECO:0000313|EMBL:CDY55060.1}, and RC K-12 substr. RV308 {ECO:0000313|EMBL:CDZ19154.1}; RA Krempl M.Peter.; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|EMBL:KGP47200.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MRSN22624 {ECO:0000313|EMBL:KGP47200.1}; RC PLASMID=pMR0713 {ECO:0000313|EMBL:KGP47200.1}; RA McGann P., Snesrud E., Ong A.C., Appalla L., Koren M., Kwak Y.I., RA Waterman P.E., Lesho E.; RT "War Wound Treatment Complications due to in vivo Transfer of an IncN RT Plasmid Harboring blaOXA-181 from Morganella morgannii to CTX-M-27- RT producing Escherichia coli."; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000313|EMBL:KJH98393.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MNCRE46 {ECO:0000313|EMBL:KJH98393.1}; RA Johnson T.J., Danzeisen J., Hargreaves M., Shaw K., Snippes P., RA Silverstein K., Youmans B.; RT "Epidemic clone of carbapenem resistant Enterobacter cloacae in RT Minnesota."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000313|EMBL:KJH99407.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MNCRE45 {ECO:0000313|EMBL:KJI09844.1}, and RC MNCRE47 {ECO:0000313|EMBL:KJH99407.1}; RA Johnson T., Danzeisen J., Hargreaves M., Shaw K., Snippes P., RA Silverstein K., Youmans B.; RT "Epidemic clone of carbapenem resistant Enterobacter cloacae in RT Minnesota."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM886293; CAP07823.1; -; Genomic_DNA. DR EMBL; LM993812; CDY55060.1; -; Genomic_DNA. DR EMBL; LM995446; CDZ19154.1; -; Genomic_DNA. DR EMBL; CCNI01000231; CEE10427.1; -; Genomic_DNA. DR EMBL; JPKK01000054; KGM72745.1; -; Genomic_DNA. DR EMBL; JRKV01000044; KGP47200.1; -; Genomic_DNA. DR EMBL; JYLS01000139; KJH98393.1; -; Genomic_DNA. DR EMBL; JYLT01000146; KJH99407.1; -; Genomic_DNA. DR EMBL; JYLV01000185; KJI09844.1; -; Genomic_DNA. DR RefSeq; WP_000081352.1; NZ_JSSJ01000043.1. DR RefSeq; YP_001816637.1; NC_010558.1. DR ProteinModelPortal; B1VCK1; -. DR SMR; B1VCK1; 11-307. DR EnsemblBacteria; CEE10427; CEE10427; BN1008_4142. DR EnsemblBacteria; KCW93807; KCW93807; DP79_24605. DR EnsemblBacteria; KGM72745; KGM72745; EL78_3267. DR EnsemblBacteria; KGP43950; KGP43950; LS89_23620. DR EnsemblBacteria; KGP47200; KGP47200; LS90_24240. DR EnsemblBacteria; KHD44034; KHD44034; LS41_24410. DR EnsemblBacteria; KHD47684; KHD47684; LS42_24765. DR EnsemblBacteria; KHH41010; KHH41010; PU58_20820. DR EnsemblBacteria; KHH86487; KHH86487; PU51_02310. DR GeneID; 6275998; -. DR KEGG; pg:6275998; -. DR KO; K00547; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:CDY55060.1}; KW Plasmid {ECO:0000313|EMBL:CAP07823.1}; KW Transferase {ECO:0000313|EMBL:CDY55060.1}. SQ SEQUENCE 310 AA; 33423 MW; 8381CFF475E5FB7A CRC64; MSQNNPLRAL LDKQDILLLD GAMATELEAR GCNLADSLWS AKVLVENPEL IREVHLDYYR AGAQCAITAS YQATPAGFAA RGLDEAQSKA LIGKSVELAR KAREAYLAEN PQAGTLLVAG SVGPYGAYLA DGSEYRGDYH CSVEAFQAFH RPRVEALLDA GADLLACETL PNFSEIEALA ELLTAYPRAR AWFSFTLRDS EHLSDGTPLR DVVALLAGYP QVVALGINCI ALENTTAALQ HLHGLTVLPL VVYPNSGEHY DAVSKTWHHH GEHCAQLADY LPQWQAAGAR LIGGCCRTTP ADIAALKARS // ID B1VWS9_STRGG Unreviewed; 307 AA. AC B1VWS9; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 27-MAY-2015, entry version 36. DE SubName: Full=Putative homocysteine S-methyltransferase {ECO:0000313|EMBL:BAG18405.1}; GN OrderedLocusNames=SGR_1576 {ECO:0000313|EMBL:BAG18405.1}; OS Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=455632 {ECO:0000313|EMBL:BAG18405.1, ECO:0000313|Proteomes:UP000001685}; RN [1] {ECO:0000313|EMBL:BAG18405.1, ECO:0000313|Proteomes:UP000001685} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 4626 / NBRC 13350 {ECO:0000313|Proteomes:UP000001685}; 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 ----------------------------------------------------------------------- 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; BAG18405.1; -; Genomic_DNA. DR RefSeq; WP_012378631.1; NC_010572.1. DR RefSeq; YP_001823088.1; NC_010572.1. DR ProteinModelPortal; B1VWS9; -. DR STRING; 455632.SGR_1576; -. DR EnsemblBacteria; BAG18405; BAG18405; SGR_1576. DR KEGG; sgr:SGR_1576; -. DR PATRIC; 23749569; VBIStrGri32265_1593. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; SGRI455632:GD3A-1580-MONOMER; -. DR Proteomes; UP000001685; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001685}; KW Methyltransferase {ECO:0000313|EMBL:BAG18405.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001685}; KW Transferase {ECO:0000313|EMBL:BAG18405.1}. SQ SEQUENCE 307 AA; 32256 MW; A35E5D33EF42B5CB CRC64; MAVRTVRTLA EALDAGPVLL DGGLSNQLEA QGCDLSDALW SARLLADAPE QIEAAHLAYL RAGARVLITA SYQATFEGFG RYGLDRAATG ALLARSVELA RRAAEAARRA DPGRETWVAA SVGPYGAMLA DGSEYRGRYG LSVRELERFH RPRVAALAAA GPDALALETV PDLDEAEALV RVAEETGLPY WLSYSVADGR TRAGQPLQEA FAVAAGRDSV LAVGVNCCDP QEARGAVEQA VAVTGRPAVV YPNSGEGWDA GARGWTGHGT FDPGQVRAWT RAGARLVGGC CRVGPDLITE LDGRLEG // ID B1W2Z4_STRGG Unreviewed; 1170 AA. AC B1W2Z4; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 27-MAY-2015, entry version 52. DE SubName: Full=Putative 5-methyltetrahydrofolate:homocysteine S-methyltransferase {ECO:0000313|EMBL:BAG22676.1}; GN OrderedLocusNames=SGR_5847 {ECO:0000313|EMBL:BAG22676.1}; OS Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=455632 {ECO:0000313|EMBL:BAG22676.1, ECO:0000313|Proteomes:UP000001685}; RN [1] {ECO:0000313|EMBL:BAG22676.1, ECO:0000313|Proteomes:UP000001685} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 4626 / NBRC 13350 {ECO:0000313|Proteomes:UP000001685}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP009493; BAG22676.1; -; Genomic_DNA. DR RefSeq; WP_003970155.1; NC_010572.1. DR RefSeq; YP_001827359.1; NC_010572.1. DR ProteinModelPortal; B1W2Z4; -. DR STRING; 455632.SGR_5847; -. DR EnsemblBacteria; BAG22676; BAG22676; SGR_5847. DR GeneID; 6215386; -. DR KEGG; sgr:SGR_5847; -. DR PATRIC; 23758507; VBIStrGri32265_5992. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SGRI455632:GD3A-5923-MONOMER; -. DR Proteomes; UP000001685; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001685}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAG22676.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001685}; KW Transferase {ECO:0000313|EMBL:BAG22676.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 237 237 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 747 747 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1170 AA; 127832 MW; 1BA539CB913C0C3A CRC64; MASLPTSAAD SRTRADALRE ALATRVVVAD GAMGTMLQAQ DPTLEDFENL EGCNEILNIT RPDIVRSVHE EYFAVGVDCV ETNTFGANHS AANEYEIADR IFELSESGAR IAREVADEFG AKDGRQRWVL GSIGPGTKLP SLGHIAYDVL RDGYQKNAEG LLTGGSDALI VETTQDLLQT KSSIIGARRA MDALGVHVPL ICSLAFETTG VMLLGSEIGA ALTALEPLGI DLIGLNCSTG PDEMSEHLRY LARHSRTPLM CMPNAGLPVL TKDGAHFPLG PDGLADSQEN FVRDYGLSLI GGCCGTTPEH LRAVVDRARE LTPTERDPRP EPGAASLYQT IPFRQDTAYL AIGERTNANG SKKFREAMLE ARWDDCVEMA RDQIREGAHM LDLCVDYVGR DGVADMAELA GRFATASTLP IVLDSTELPV LRAGLEKLGG RAVLNSVNYE DGDGPESRFA QVSALAAEHG AALIALTIDE EGQARTVENK VAIAERLIED LTANWSIRES DILIDTLTFT ICTGQEESRG DGIATIGAIR ELKKRHPDVQ TTLGLSNISF GLNPAARVVL NSVFLDECVK AGLDSAIVHA SKILPIARLE EEQVKVALDL IYDRRAEGYD PLQKLMELFE GVNMKSMKAG KAEELMALPL DERLQRRIID GEKNGLEADL DEALQDTPAL DIVNNTLLEG MKVVGELFGS GQMQLPFVLQ SAEVMKSAVA HLEPHMEKSD DEGKGTIVLA TVRGDVHDIG KNLVDIILSN NGYNVVNLGI KQPVSAILEA AEEHRADVIG MSGLLVKSTV IMKENLQELN QRKMAADFPV ILGGAALTRA YVEQDLHEIY EGEVRYARDA FEGLRLMDAL IGVKRGVPGA ALPELKQRRV PKKDVAVLEV EEPEGSVRSD VSTTNPIPEP PFRGTRVIKG IPLKDYASWL DEGALFKGQW GLKQARTGDG PTYEELVETE GRPHLRGWLD HLQSNNLLEA AVVYGYFPCV SKGDDLVLLH EDGSERTRFT FPRQRRGRRL CLADFFRPEE SGETDVIGLQ IVTVGSRIGE ATAELFAANS YRDYLELHGL SVQLAEALAE YWHARVRSEL GFAGEDPEDV EDMFALKYRG ARFSLGYGAC PDLEDRAKIA DLLQPERIGV HLSEEFQLHP EQSTDAIVIH HPEAKYFNAR // ID B1WZ63_CYAA5 Unreviewed; 1193 AA. AC B1WZ63; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 27-MAY-2015, entry version 56. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:ACB49429.1}; GN Name=metH {ECO:0000313|EMBL:ACB49429.1}; GN OrderedLocusNames=cce_0077 {ECO:0000313|EMBL:ACB49429.1}; OS Cyanothece sp. (strain ATCC 51142). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Cyanothece. OX NCBI_TaxID=43989 {ECO:0000313|EMBL:ACB49429.1, ECO:0000313|Proteomes:UP000001203}; RN [1] {ECO:0000313|EMBL:ACB49429.1, ECO:0000313|Proteomes:UP000001203} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51142 {ECO:0000313|EMBL:ACB49429.1, RC ECO:0000313|Proteomes:UP000001203}; RX PubMed=18812508; DOI=10.1073/pnas.0805418105; RA Welsh E.A., Liberton M., Stoeckel 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000806; ACB49429.1; -; Genomic_DNA. DR RefSeq; WP_009543124.1; NC_010546.1. DR RefSeq; YP_001801495.1; NC_010546.1. DR ProteinModelPortal; B1WZ63; -. DR STRING; 43989.cce_0077; -. DR EnsemblBacteria; ACB49429; ACB49429; cce_0077. DR KEGG; cyt:cce_0077; -. DR PATRIC; 21538622; VBICyaSp130209_0162. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CSP43989:GKC8-80-MONOMER; -. DR Proteomes; UP000001203; Chromosome circular. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001203}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACB49429.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001203}; KW Transferase {ECO:0000313|EMBL:ACB49429.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 228 228 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 739 739 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1193 AA; 133169 MW; 97F5FBE651A345B6 CRC64; MNSTFLNHLN SPKRPVLVFD GATGTSLQSQ NLTADDFGGP EYEGCNEYLV HTKPEAVEKV HRGFLEVGAD VIETDTFGGT SIVLAEYDLA DKAYYLNKKA AEIAKKMAAE YSTPEKPRFV AGSMGPGTKL PTLGHIDFDT LRDAYIEQAE GLYDGGADLL IIETCQDVLQ IKAALNAVEA VFEKKRNRLP IMVSITMETM GTMLVGTEIS AALAILEPYK IDILGLNCAT GPEQMKEHIK YLSEHSPFIV SCIPNAGLPE NVGGQAHYRL TPIELKMALM HFIEDLGVQI IGGCCGTRPD HIKALSELSQ DLTPKERHPD YEPSAASIYS TQPYIQDNSF LIVGERLNAS GSKKCRQLLD AEDWDSLVSL AKSQVKEGAH VLDVNVDYVG RDGVRDMHEL ASRLVNNITL PLMLDSTEWQ KMESGLKVAG GKCILNSTNY EDGEERFLKV LELAKKYGAG VVVGTIDEEG MGRTADKKFE IAKRAYNAAI DYGIPAHEIF FDPLALPIST GIEEDRENGK ATVEAIKRIR EELPGCHIIL GISNISFGLN PAARQVLNSV FLYESMQVGL DGAIVSASKI LPLVKIEEDH QKVCRDLIYD RREFDGDICT YDPLTKLTEL FAGKTTKKDP SKTASLPIEE RLKQHIIDGE RLGLEDALSE ALKQYPPLDI INVFLLDGMK TVGELFGSGQ MQLPFVLQSA QTMKAAVAYL EPFMDKEEGE ENDSGKGKFL IATVKGDVHD IGKNLVDIIL SNNGYKVINL GIKQPVENII QAYEEHQPDC IAMSGLLVKS TAFMKDNLEV FNERGIDVPV ILGGAALTPK FVYEDCQNTY KGKVVYGKDA FSDLHFMDKL MPAKSAENWD NLQGFLGEFT DNNSLFQEER GEKAAEKATE KNGKSSTQET PTVIDTKRSE AVEILEPATP PFWGTKILKS NEFDLNEIFW YLDLQALIAG QWQFRKPKDQ SREEYEAFLA EKVYPILEEW KQKVVTENLL HPTVIYGYFP CQSQDNSLLV YDPETIRNAN NKIPEDLDPI WKIDFPRQKS GRRLCIADFF SPKESGKIDV FPMQAVTVGD IATEYAQKLF AANDYTNYLY YHGMAVQTAE ALAEWTHAKI RRELGFADKE PDNIREMLQQ HYQGSRYSFG YPACPNIQDQ YKQLEVMGCD RINMYMDESE QIYPEQSTTA IIAYHPVAKY FSA // ID B1XKG9_SYNP2 Unreviewed; 1180 AA. AC B1XKG9; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 27-MAY-2015, entry version 54. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase (Methionine synthase) {ECO:0000313|EMBL:ACB00444.1}; GN Name=metH {ECO:0000313|EMBL:ACB00444.1}; GN OrderedLocusNames=SYNPCC7002_A2466 {ECO:0000313|EMBL:ACB00444.1}; OS Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum OS quadruplicatum). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechococcus. OX NCBI_TaxID=32049 {ECO:0000313|EMBL:ACB00444.1, ECO:0000313|Proteomes:UP000001688}; RN [1] {ECO:0000313|Proteomes:UP000001688} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27264 / PCC 7002 / PR-6 RC {ECO:0000313|Proteomes:UP000001688}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000951; ACB00444.1; -; Genomic_DNA. DR RefSeq; WP_012308062.1; NC_010475.1. DR RefSeq; YP_001735699.1; NC_010475.1. DR ProteinModelPortal; B1XKG9; -. DR STRING; 32049.SYNPCC7002_A2466; -. DR EnsemblBacteria; ACB00444; ACB00444; SYNPCC7002_A2466. DR KEGG; syp:SYNPCC7002_A2466; -. DR PATRIC; 23819584; VBISynSp37135_2722. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SSP32049:GKF7-2467-MONOMER; -. DR Proteomes; UP000001688; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001688}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACB00444.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001688}; KW Transferase {ECO:0000313|EMBL:ACB00444.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 228 228 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 737 737 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1180 AA; 130902 MW; 1221BE2C15B6C058 CRC64; MKSAFLDRLN SPERPVLVFD GAMGTNLQVQ NLTAADFGGA EYEGCNEYLV QTKPEAVATV HRAFLAAGAD VIETDTFGGT SIVLAEYDLG DRAYELNKKA AELAKSVTAE FSTSEKPRFV AGSIGPGTKL PSLGHIDYDT LENAFAEQAE GLYDGGADLM LVETCQDVLQ IKAALNGIER TFTKKGDRLP IMVSVTMETM GTMLVGTEIA AAVAILEPYR IDILGLNCAT GPDLMKEHVK YLSEHSPFIV SCIPNAGLPE NVGGQAHYKL TPLEMKMAMM HFVEDLGVQV IGGCCGTRPE HIQALAEIAA ELTPKERHPD YEPAAASIYS PQPYIQDNSF LIVGERLNAS GSKKCRTLLN EEDWDSLVSL AKSQVKEGAH VLDVNVDYVG RDGVRDMHEL ASRLVNNVTL PLMLDSTEWE KMEAGLKVAG GKCILNSTNY EDGEERFYQV LSLAKKYGAG VVIGTIDEEG MARTAEKKFE IAKRAYDAAI AYGLPAHEVF FDPLALPIST GIEEDRNNGQ ATLDAIERIH KELPGCHIIL GVSNISFGLN PAARQVLNSV FLHDAMQLGM DSAIVSASKI LPMAKIDPEH IKICRDLIGD RREFEGEVCT YDPLTKLTEL FAGKKAKKSE AIDKNLPVNE RLKQHIIDGE RLGLEEALTE ALEQYPPLDI INIFLLDGMK VVGELFGSGQ MQLPFVLQSA QTMKAAVAFL EPYMDKEEGD DSGKGTFIIA TVKGDVHDIG KNLVDIILSN NGYKVINLGI KQPVENIIQA YEENGADCIA MSGLLVKSTA FMKDNLEAFN EKGITVPVIL GGAALTPKFV YQDCQNTYKG QVIYGKDAFA DLHFMDKLMP AKAEQQWDDF DGFLGDYAEA NQRTYSGDGE EIAVEETKSQ EPEVVDTRRS EFVEDNIARP RPPFWGTKIL RAEDIDLEEI FWHLDLQALF VGQWQFRKTK EQSKEEYDQF IQDTVHPLLE QWKQKAIAEK ILDPTVIYGY FPCQSEGNTL IIYDPDEYVS EQTLSEVARF EFPRQKSGKR LCIADFFAST ESGVLDVFPM QAVTVGEVAT EYARKLFAAD EYTDYLYYHG IAVQTAEALA EWCHARIRRE LGFGDAEPDN IKDMLKQRYQ GSRYSFGYPA CPNILDQYTQ LDLLKTDRIG MYMDESEQIY PEQSTSAIIT YHPVAKYFNV // ID B1XSF7_POLNS Unreviewed; 354 AA. AC B1XSF7; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 27-MAY-2015, entry version 41. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACB44756.1}; GN OrderedLocusNames=Pnec_1689 {ECO:0000313|EMBL:ACB44756.1}; OS Polynucleobacter necessarius subsp. necessarius (strain STIR1). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Polynucleobacter. OX NCBI_TaxID=452638 {ECO:0000313|EMBL:ACB44756.1, ECO:0000313|Proteomes:UP000006582}; RN [1] {ECO:0000313|EMBL:ACB44756.1, ECO:0000313|Proteomes:UP000006582} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=STIR1 {ECO:0000313|EMBL:ACB44756.1, RC ECO:0000313|Proteomes:UP000006582}; 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; ACB44756.1; -; Genomic_DNA. DR RefSeq; WP_012358514.1; NC_010531.1. DR RefSeq; YP_001798370.1; NC_010531.1. DR ProteinModelPortal; B1XSF7; -. DR STRING; 452638.Pnec_1689; -. DR EnsemblBacteria; ACB44756; ACB44756; Pnec_1689. DR KEGG; pne:Pnec_1689; -. DR PATRIC; 22972699; VBIPolNec8289_1944. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; PNEC452638:GI4T-1688-MONOMER; -. DR Proteomes; UP000006582; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006582}; KW Methyltransferase {ECO:0000313|EMBL:ACB44756.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006582}; KW Transferase {ECO:0000313|EMBL:ACB44756.1}. SQ SEQUENCE 354 AA; 38161 MW; B6DE01FB7563770E CRC64; MQSNGFSQPY TRGQKIPELL KQRILILDGA MGTMIQQYKL TEADYRGLPG GTRFADHPGD IKGNNELLVL TQPQIISKIH EQYLEAGADI IETNTFGATS IAQEDYKMAN LAREMNEVSA RLARAACEKY STSDKPRFAA GAIGPTPKTA SISPDVNDPG ARNVTFDALR ASYHEQIEGL FAGGVDLFLV ETIFDTLNAK AALFALDEFF EETGERLPVM ISGTVTDASG RILSGQTVEA FWNSLRHIKP LTFGLNCALG AALMRPYIAE LARICDAAVS CYPNAGLPNP MSDTGFDETP EITSSLVDGF AKDGLVNLVG GCCGTTPDHI RAIANAVAQR KPRAFYRENA GVSA // ID B1Y1R4_LEPCP Unreviewed; 357 AA. AC B1Y1R4; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 27-MAY-2015, entry version 42. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACB35526.1}; GN OrderedLocusNames=Lcho_3268 {ECO:0000313|EMBL:ACB35526.1}; 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 {ECO:0000313|EMBL:ACB35526.1, ECO:0000313|Proteomes:UP000001693}; RN [1] {ECO:0000313|EMBL:ACB35526.1, ECO:0000313|Proteomes:UP000001693} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51168 / LMG 8142 / SP-6 RC {ECO:0000313|Proteomes:UP000001693}; 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; ACB35526.1; -; Genomic_DNA. DR RefSeq; WP_012348273.1; NC_010524.1. DR RefSeq; YP_001792291.1; NC_010524.1. DR STRING; 395495.Lcho_3268; -. DR EnsemblBacteria; ACB35526; ACB35526; Lcho_3268. DR KEGG; lch:Lcho_3268; -. DR PATRIC; 22396945; VBILepCho83238_3296. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; LCHO395495:GHYL-3314-MONOMER; -. DR Proteomes; UP000001693; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001693}; KW Methyltransferase {ECO:0000313|EMBL:ACB35526.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001693}; KW Transferase {ECO:0000313|EMBL:ACB35526.1}. SQ SEQUENCE 357 AA; 38395 MW; C3C7408606223212 CRC64; MNTPSPQSNP SPAYTRGAQL PALLQQRILV LDGAMGTMVQ RYKLDEAAFR GERFADHPSD LKGNNDLLVL TRPDVIAEIH DQYLAAGADI IETNTFGATF VAQDDYQLGE LAYEMNLVAA RLARQCCDRY STPDKPRFVA GALGPTPRTA SISPDVNDAG ARNTDFDQLH AAYKEQARGL MDGGCDLFLV ETIFDTLNAK AAIFALDELM EETGERLPVI ISGTVTDASG RILSGQTVGA FWHSVRHAKP IAIGLNCALG ATLMRPYIEE LAKIAGETFV SCYPNAGLPN PMSDTGFDET PEVTGALIEE FAKAGFLNIA GGCCGTTPAH IAEIAQRVGR YQPRCRHTAP FSDLLAA // ID B1YG53_EXIS2 Unreviewed; 310 AA. AC B1YG53; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 27-MAY-2015, entry version 37. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACB62437.1}; GN OrderedLocusNames=Exig_2991 {ECO:0000313|EMBL:ACB62437.1}; 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 {ECO:0000313|EMBL:ACB62437.1, ECO:0000313|Proteomes:UP000001681}; RN [1] {ECO:0000313|Proteomes:UP000001681} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17290 / JCM 13490 / 255-15 RC {ECO:0000313|Proteomes:UP000001681}; 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; ACB62437.1; -; Genomic_DNA. DR RefSeq; WP_012371852.1; NC_010556.1. DR RefSeq; YP_001815454.1; NC_010556.1. DR ProteinModelPortal; B1YG53; -. DR STRING; 262543.Exig_2991; -. DR EnsemblBacteria; ACB62437; ACB62437; Exig_2991. DR KEGG; esi:Exig_2991; -. DR PATRIC; 32139658; VBIExiSib53410_3034. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; ESIB262543:GHBP-3089-MONOMER; -. DR Proteomes; UP000001681; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001681}; KW Methyltransferase {ECO:0000313|EMBL:ACB62437.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001681}; KW Transferase {ECO:0000313|EMBL:ACB62437.1}. SQ SEQUENCE 310 AA; 33927 MW; AA0F2161D9CFC1B0 CRC64; MSKNNNPVEQ LLKEKPYILL DGALATELER HGRNLDDPLW SARVLLEEPE QIHRVHANYF KIGADCAITS SYQASVAGFS SRGIKEEEAI ELMKQTVYLA QQARAETGPA ADHALIAGSI GPYGAYLSDG SEYIGHYGVD DAQLEAFHRP RLEALIAAGA DVLAFETIPS LQEAKMLFRL LEEFPEQSAW LAFSLRDATH ISEGTPLSEC IEALGDHPQL AAIGANCFPA SIATEFITTL KQLTDVPIIV YPNSGEQYDP VSKTWSGETV RTAFEDIAPE WYAAGARLIG GCCRTTPEQI GEIRKIVHAQ // ID B1YNQ4_BURA4 Unreviewed; 355 AA. AC B1YNQ4; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 27-MAY-2015, entry version 43. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACB65304.1}; GN OrderedLocusNames=BamMC406_2828 {ECO:0000313|EMBL:ACB65304.1}; OS Burkholderia ambifaria (strain MC40-6). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=398577 {ECO:0000313|EMBL:ACB65304.1, ECO:0000313|Proteomes:UP000001680}; RN [1] {ECO:0000313|Proteomes:UP000001680} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC40-6 {ECO:0000313|Proteomes:UP000001680}; 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; ACB65304.1; -; Genomic_DNA. DR RefSeq; WP_012364814.1; NC_010551.1. DR RefSeq; YP_001809520.1; NC_010551.1. DR STRING; 398577.BamMC406_2828; -. DR EnsemblBacteria; ACB65304; ACB65304; BamMC406_2828. DR KEGG; bac:BamMC406_2828; -. DR PATRIC; 19035246; VBIBurAmb82852_2919. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; BAMB398577:GH38-2900-MONOMER; -. DR Proteomes; UP000001680; Chromosome 1. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001680}; KW Methyltransferase {ECO:0000313|EMBL:ACB65304.1}; KW Transferase {ECO:0000313|EMBL:ACB65304.1}. SQ SEQUENCE 355 AA; 38289 MW; 1909D41478CC48AF CRC64; MSATPLAASV PLDAPYTRGA ELPALLKSRI LILDGAMGTM IQRYKLDEAA YRGERFKDFP RDIKGNNELL SLTQPQIIRE IHDQYFAAGA DIVETNTFGA TTVAQADYGM EDLVVEMNVE SARLARESAV RYATPDKPRF VAGAIGPTPK TASISPDVND PGARNVTFDE LRSAYYQQAK ALLDGGVDLF LVETIFDTLN AKAALFALDE LFEDTGERLP IMISGTVTDA SGRILSGQTV EAFWNSLRHA KPLTFGLNCA LGAALMRPYI AELAKLCDTY VSCYPNAGLP NPMSDTGFDE TPDVTSGLLK EFAQAGLVNL AGGCCGTTPE HIAEIAKALA DVKPRRWPSH YSDAA // ID B1YYZ0_BURA4 Unreviewed; 309 AA. AC B1YYZ0; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 27-MAY-2015, entry version 36. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACB67287.1}; GN OrderedLocusNames=BamMC406_4837 {ECO:0000313|EMBL:ACB67287.1}; OS Burkholderia ambifaria (strain MC40-6). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=398577 {ECO:0000313|EMBL:ACB67287.1, ECO:0000313|Proteomes:UP000001680}; RN [1] {ECO:0000313|Proteomes:UP000001680} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC40-6 {ECO:0000313|Proteomes:UP000001680}; 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; ACB67287.1; -; Genomic_DNA. DR RefSeq; WP_012366573.1; NC_010552.1. DR RefSeq; YP_001811503.1; NC_010552.1. DR ProteinModelPortal; B1YYZ0; -. DR STRING; 398577.BamMC406_4837; -. DR EnsemblBacteria; ACB67287; ACB67287; BamMC406_4837. DR KEGG; bac:BamMC406_4837; -. DR PATRIC; 19039461; VBIBurAmb82852_5019. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; DVITANS; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; BAMB398577:GH38-4914-MONOMER; -. DR Proteomes; UP000001680; Chromosome 2. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001680}; KW Methyltransferase {ECO:0000313|EMBL:ACB67287.1}; KW Transferase {ECO:0000313|EMBL:ACB67287.1}. SQ SEQUENCE 309 AA; 32376 MW; E5CEA65836AAF10F CRC64; MHDITVLDGG MGRELARMGA PFRQPEWSAL ALMEAPDYVG LAHDAFIAAG ADVITANSYA VVPFHIGEER FRRDGVALAA LAGQLARQAA DRAGRPVRVA GSLPPTGGSY RPDLFDAARA DAILATLVDG LDPYVDLWLA ETQSLTDEIG AVRRALDANP KPLWVSFTLR DDVDAGATPV LRSGQTLDEA IDAAVSARAT ALLFNCSQPE VMGAAIETAQ RTLARAGTSL AIGAYANAFP PQRADARANE ELDGLRGDID PPGYARWAEQ WLALGARIVG GCCGIGPGHI AALRDAVDAR GAGHTGFGQ // ID B1ZGE4_METPB Unreviewed; 1250 AA. AC B1ZGE4; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 27-MAY-2015, entry version 56. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACB79802.1}; GN OrderedLocusNames=Mpop_1638 {ECO:0000313|EMBL:ACB79802.1}; OS Methylobacterium populi (strain ATCC BAA-705 / NCIMB 13946 / BJ001). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=441620 {ECO:0000313|EMBL:ACB79802.1, ECO:0000313|Proteomes:UP000007136}; RN [1] {ECO:0000313|EMBL:ACB79802.1, ECO:0000313|Proteomes:UP000007136} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-705 / NCIMB 13946 / BJ001 RC {ECO:0000313|Proteomes:UP000007136}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001029; ACB79802.1; -; Genomic_DNA. DR RefSeq; WP_012453549.1; NC_010725.1. DR RefSeq; YP_001924337.1; NC_010725.1. DR ProteinModelPortal; B1ZGE4; -. DR SMR; B1ZGE4; 660-909. DR STRING; 441620.Mpop_1638; -. DR EnsemblBacteria; ACB79802; ACB79802; Mpop_1638. DR KEGG; mpo:Mpop_1638; -. DR PATRIC; 22560509; VBIMetPop124700_1673. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; MPOP441620:GHMI-1680-MONOMER; -. DR Proteomes; UP000007136; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007136}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 254 254 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 318 318 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 771 771 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1250 AA; 137291 MW; D9CAAAA25F79F1E2 CRC64; MTAFPPVDGT EIERALRQRA SEKILVLDGA MGTVIQRLKF TEEDFRGERF KDHGHDQKGN NDLLILTQPD AIRQIHLDYF LAGADVCETN TFSGTTIAQA DYGMESIIHE LNAEGARLAR EAAKLAEEQD GRRRFVAGAI GPTNRTLSIS PDVNNPGYRA VTFDQVKQAY VEQVRGLIDG GAELILIETI FDTLNAKAAI AAAWQVFSEV GIKLPIQISG TITDLSGRTL SGQTPAAFWN SLRHSDPLTF GLNCALGARE MRGHIAELSR ICDTLVCAYP NAGLPNEFGL YDESPEAMGK LVGEFAESGL VNMVGGCCGT TPDHIRAIAE AVAGKTPRKI PEIPRLMRLS GLEPFVLTKE IPFVNVGERT NVTGSAKFRK LITNGDYAAA LDVARDQVAA GAQVIDVNMD EGLLDSQKAM VEFLNLVAAE PDIARVPVMV DSSKFEVIEA GLKCIQGKPI VNSISMKEGE EKFIETAKVC RSYGAAVVVM AFDEQGQADS YERKVEICTK AYKILTEQVG FPPEDIIFDP NIFAVATGIE EHNPYGVAFI EATRTIRETL PHAHISGGVS NLSFAFRGNE PVREAMHAVF LFHCIKAGMD MGIVNAGQLA VYDEIPAELR ELCEDVVLNR REDSTERLLD AAERFKTGAS AQAKTADLSW REAPVAKRIE HALVNGITEY IVADTEEARK EAERPLHVIE GPLMAGMNVV GDLFGSGKMF LPQVVKSARV MKQAVAYLEP FMEEEKRANG GTGQRQAAGK VLMATVKGDV HDIGKNIVGV VLACNNYEII DLGVMVPAAK ILETAKKENV DIIGLSGLIT PSLDEMVHVA AEMEREGMEM PLLIGGATTS RVHTAVKIHP AYERGQAVYV TDASRAVGVV SSLISKETRG STIERVRAEY AKVADAHRRS EADKQRLPLA KARSNAFKID WSGYAPKKPS FTGTRVYGSY EVADLVPYID WTPFLQTYEF KGRYPAILDD PEQGPAARAL FEDAQVMLKQ IVEERWFNPK AVIGFWPANS VGDDIRLFTG ESRQETLATF HGLRQQLSKR DGRANTCISD FVAPAETGIA DYVGAFVVTA GLEEVRIAER FERANDDYRS ILVKALADRI AEAFAERMHE RVRKEFWGYA PDESFTADEL VHEKYDGIRP APGYPAQPDH TEKVTLFDLL KAESRIGVKL TESYAMWPGS SVSGLYLAHP EAHYFGVAKV ERDQVEDYAL RKGMDITEVE RWLGPILNYD PARYLKAAAE // ID B1ZPB5_OPITP Unreviewed; 302 AA. AC B1ZPB5; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 27-MAY-2015, entry version 37. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACB77604.1}; GN OrderedLocusNames=Oter_4332 {ECO:0000313|EMBL:ACB77604.1}; OS Opitutus terrae (strain DSM 11246 / PB90-1). OC Bacteria; Verrucomicrobia; Opitutae; Opitutales; Opitutaceae; OC Opitutus. OX NCBI_TaxID=452637 {ECO:0000313|EMBL:ACB77604.1, ECO:0000313|Proteomes:UP000007013}; RN [1] {ECO:0000313|EMBL:ACB77604.1, ECO:0000313|Proteomes:UP000007013} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11246 / PB90-1 {ECO:0000313|Proteomes:UP000007013}; RX PubMed=21398538; DOI=10.1128/JB.00228-11; RA van Passel M.W., Kant R., Palva A., Copeland A., Lucas S., Lapidus A., RA Glavina del Rio T., Pitluck S., Goltsman E., Clum A., Sun H., RA Schmutz J., Larimer F.W., Land M.L., Hauser L., Kyrpides N., RA Mikhailova N., Richardson P.P., Janssen P.H., de Vos W.M., Smidt H.; RT "Genome sequence of the verrucomicrobium Opitutus terrae PB90-1, an RT abundant inhabitant of rice paddy soil ecosystems."; RL J. Bacteriol. 193:2367-2368(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; CP001032; ACB77604.1; -; Genomic_DNA. DR RefSeq; WP_012377130.1; NC_010571.1. DR RefSeq; YP_001821204.1; NC_010571.1. DR ProteinModelPortal; B1ZPB5; -. DR STRING; 452637.Oter_4332; -. DR EnsemblBacteria; ACB77604; ACB77604; Oter_4332. DR KEGG; ote:Oter_4332; -. DR PATRIC; 22820499; VBIOpiTer17422_4507. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265278; -. DR KO; K00548; -. DR OMA; GTNLFAM; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; OTER452637:GHBR-4400-MONOMER; -. DR Proteomes; UP000007013; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007013}; KW Methyltransferase {ECO:0000313|EMBL:ACB77604.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007013}; KW Transferase {ECO:0000313|EMBL:ACB77604.1}. SQ SEQUENCE 302 AA; 31637 MW; 67D69B2B5F6F3D72 CRC64; MKKPLLETVL ERRLVCDGAM GTQLMLAGLE QGGCGEAWNL THADRVLAIQ QRYANAGADC LITNTFGGSR LMLRRHGHEG DVAEINRAAA RIARGAFGAK PGFVLGDVGP LGGLLEPYGE ISLADAQSAL EEQCVALVAA GVDAIIIETQ TSIEELSVAI DAAKAANAPC IIASLAYDLS MDGTFYKTMM GVAPEDAAEF AEARGAHVIA LNCGTGMDMT GAAKVARLYR ERTKLPIMVQ PNAGLPVLEN MKAVYKQTPA DMAKGVPDVL AADVAIIGSC CGSTPEHTRA IREVVDRGES AV // ID B2A781_NATTJ Unreviewed; 793 AA. AC B2A781; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 27-MAY-2015, entry version 53. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACB84275.1}; GN OrderedLocusNames=Nther_0682 {ECO:0000313|EMBL:ACB84275.1}; 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 {ECO:0000313|EMBL:ACB84275.1, ECO:0000313|Proteomes:UP000001683}; RN [1] {ECO:0000313|EMBL:ACB84275.1, ECO:0000313|Proteomes:UP000001683} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF RC {ECO:0000313|Proteomes:UP000001683}; 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 ----------------------------------------------------------------------- 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; ACB84275.1; -; Genomic_DNA. DR RefSeq; WP_012447159.1; NC_010718.1. DR RefSeq; YP_001916863.1; NC_010718.1. DR ProteinModelPortal; B2A781; -. DR STRING; 457570.Nther_0682; -. DR EnsemblBacteria; ACB84275; ACB84275; Nther_0682. DR KEGG; nth:Nther_0682; -. DR PATRIC; 22669988; VBINatThe92436_0704. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; NTHE457570:GHRL-708-MONOMER; -. DR Proteomes; UP000001683; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001683}; KW Methyltransferase {ECO:0000313|EMBL:ACB84275.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001683}; KW Transferase {ECO:0000313|EMBL:ACB84275.1}. SQ SEQUENCE 793 AA; 87409 MW; 4B92A97A2CF0FA3A CRC64; MKLKDQLVNK TLEKLLFLDG SYGTELQRRG FEGNAEILNL QDQDLVKNVH YDYASAGADL ILTNTFGGNR LKLKDAGYED KVAEINSRGV ELAKESAENI DRDVLVVGDI SSTGRFIEPV GDLSFTKAQQ VFQEQGRYLI ESGVDLIKIE TMTDIKELKA AILGIRSIDE DLPLIVSMSF EQDGKTITGT SVPSYVTLMN DLPVDIIGLN CGVKSKDMLD LVKQASYYSL KPLSISPNAG DPDLDLSYSE DPQEFSFYLD AISDLDMVAI VGGCCGTTPE YVDNYCSKLK GKEKSRKLLQ QSQIHKDIPT LISSRTYQLD LDNNFVKIGE RINPASKKNF QEEINNKDFS RIYDEAFSQM NEGSDVIDLN LGVEEDVELE DVETIVNGLD SLGCKPLSLD IQSSVLLEKA LQVYPGRPII NSSSCDKEDL DNAIDLMKKY GGVLVLLAMS GTPKKTIQKR LDELKYGLEY LESKGIDESR IMVDPLVLPV GTEHDPKTTL ELIKIISQEM ECKTTLGLSN LSHGLPDRPQ LNSAFVSMAI YNGLDSAIMD TSDQLVTQTV EKSLMLMGKE TIWEDVAIDT EDQMVKDILT GNSDKVLTQV KSYLKDMTPL EVSQQLLGKA MKEIGDLYND KSIYLPQLLL SAETVQPSFD YLNKLVGEHQ EDSKGKIMLA TVEGDVHDIG KKIVGTILKS GGFEIYDLGV DLPANEIVAE VKDIKPDILG LSAMMTSTIK KIAEVTEQLQ AEGIDVKVIG GGASLNPELA QKFGCHAYAK DAHEALTKCE QLMTGEKALS NER // ID B2AAZ0_PODAN Unreviewed; 371 AA. AC B2AAZ0; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 07-JAN-2015, entry version 33. DE SubName: Full=Podospora anserina S mat+ genomic DNA chromosome 1, supercontig 1 {ECO:0000313|EMBL:CAP60252.1}; DE SubName: Full=Putative homocysteine S-methyltransferase {ECO:0000313|EMBL:CDP22892.1}; GN ORFNames=PODANS_1_5620 {ECO:0000313|EMBL:CAP60252.1}; 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 {ECO:0000313|EMBL:CAP60252.1, ECO:0000313|Proteomes:UP000001197}; RN [1] {ECO:0000313|EMBL:CAP60252.1, ECO:0000313|Proteomes:UP000001197} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383 RC {ECO:0000313|Proteomes:UP000001197}, and RC S mat+ {ECO:0000313|EMBL:CAP60252.1}; 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., Henrissat B., Khoury R.E., 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). RN [2] {ECO:0000313|EMBL:CAP60252.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP60252.1}; RA Genoscope - CEA; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:CDP22892.1} RP NUCLEOTIDE SEQUENCE. RA Genoscope - CEA; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:CDP22892.1} RP NUCLEOTIDE SEQUENCE. RA Grognet P., Bidard F., Kuchly C., Chan Ho Tong L., Coppin E., RA Ait Benkhali J., Couloux A., Wincker P., Debuchy R., Silar P.; RT "Maintaining two mating types: Structure of the mating type locus and RT its role in heterokaryosis in Podospora anserina."; RL Submitted (SEP-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; CU633438; CAP60252.1; -; Genomic_DNA. DR EMBL; FO904936; CDP22892.1; -; Genomic_DNA. DR RefSeq; XP_001912770.1; XM_001912735.1. DR GeneID; 6196799; -. DR KEGG; pan:PODANSg09819; -. DR KO; K00547; -. DR Proteomes; UP000001197; Chromosome 1. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001197}; KW Methyltransferase {ECO:0000313|EMBL:CDP22892.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001197}; KW Transferase {ECO:0000313|EMBL:CDP22892.1}. SQ SEQUENCE 371 AA; 41118 MW; 4D6D3F1E0293DA26 CRC64; MSIRFQTPIM EGRKPRTIKF LDGGLGTTLE TIHGVKFSES TPLWSSHLLL TDLQTLADCQ MSFAKAGADV ITTATYQASI NGFKNTKTEN WPNGVPLPNI GHFLKDAVSI ARRAAGKVGG RVALSLGPYG ATMIPSTEYT GHYDIEPSQD IVDKLFHWHS ERYNLYVQVP NLLFDVSYIA FETIPRLDEI LAIRRFLNAD ISGGVKLGPR EFYHDIPVWI SVLFPSDDDK MPDGTSVEDA VAAMISKEFG SKTPQFVGIN CTQVSKLEGL VRQFTKAVEK LVATGAVEKW PGLVLYPDGT KVGERYNTAT KEWEISGEGS KKTPEDVSWE RQLAMVVKEA YDTGGWSSFL IGGCCRTTPE NIQRLTWAIR E // ID B2AG67_CUPTR Unreviewed; 353 AA. AC B2AG67; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 27-MAY-2015, entry version 45. DE SubName: Full=MetHa protein {ECO:0000313|EMBL:CAP62766.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAP62766.1}; GN Name=metHa {ECO:0000313|EMBL:CAP62766.1}; GN OrderedLocusNames=RALTA_A0093 {ECO:0000313|EMBL:CAP62766.1}; 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 {ECO:0000313|EMBL:CAP62766.1, ECO:0000313|Proteomes:UP000001692}; RN [1] {ECO:0000313|EMBL:CAP62766.1, ECO:0000313|Proteomes:UP000001692} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R1 / LMG 19424 {ECO:0000313|Proteomes:UP000001692}; 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; CAP62766.1; -; Genomic_DNA. DR STRING; 164546.RALTA_A0093; -. DR EnsemblBacteria; CAP62766; CAP62766; RALTA_A0093. DR KEGG; cti:RALTA_A0093; -. DR PATRIC; 21526814; VBICupTai42494_0093. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; CTAI164546:GJNE-93-MONOMER; -. DR BioCyc; CTAI977880:GLC7-93-MONOMER; -. DR Proteomes; UP000001692; Chromosome 1. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001692}; KW Methyltransferase {ECO:0000313|EMBL:CAP62766.1}; KW Transferase {ECO:0000313|EMBL:CAP62766.1}. SQ SEQUENCE 353 AA; 38260 MW; 1E172C42B86513FE CRC64; MSAPESRAAA PRPYTRAAEL PRLLQERILI LDGAMGTMIQ RYKLSEADYR GTRFAEHKVD VKGNNELLLL TRPQVISEIH EQYLAAGADL IETNTFGATR VAQEDYKMAD LAYEMNVEAA RLARAACDKY STPDKPRFVA GAFGPTPKTA SISPDVNDPG ARNVTFEELR QSYYEQGKAL LEGGADVFLV ETIFDTLNAK AALFAIDQLF EDTGERVPVM ISGTVTDASG RILSGQTVEA FWNSLRHARP VTFGLNCALG ATLMRPYIAE LAKVCDAAVS CYPNAGLPNP MSDTGFDETP EVTSALVEEF AASGLVNLVG GCCGTTPEHI AAIAQRVADK KPRTWPGQYR DAA // ID B2FLB2_STRMK Unreviewed; 363 AA. AC B2FLB2; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 27-MAY-2015, entry version 43. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:CAQ46619.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAQ46619.1}; GN Name=metH2 {ECO:0000313|EMBL:CAQ46619.1}; GN OrderedLocusNames=Smlt3176 {ECO:0000313|EMBL:CAQ46619.1}; OS Stenotrophomonas maltophilia (strain K279a). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Stenotrophomonas; OC Stenotrophomonas maltophilia group. OX NCBI_TaxID=522373 {ECO:0000313|EMBL:CAQ46619.1, ECO:0000313|Proteomes:UP000008840}; RN [1] {ECO:0000313|EMBL:CAQ46619.1, ECO:0000313|Proteomes:UP000008840} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K279a {ECO:0000313|EMBL:CAQ46619.1, RC ECO:0000313|Proteomes:UP000008840}; 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 ----------------------------------------------------------------------- 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; CAQ46619.1; -; Genomic_DNA. DR RefSeq; WP_012480774.1; NC_010943.1. DR RefSeq; YP_001972910.1; NC_010943.1. DR STRING; 522373.Smlt3176; -. DR EnsemblBacteria; CAQ46619; CAQ46619; Smlt3176. DR GeneID; 6395025; -. DR KEGG; sml:Smlt3176; -. DR PATRIC; 23701821; VBISteMal45202_2973. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; SMAL522373:GJE8-3072-MONOMER; -. DR Proteomes; UP000008840; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008840}; KW Methyltransferase {ECO:0000313|EMBL:CAQ46619.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008840}; KW Transferase {ECO:0000313|EMBL:CAQ46619.1}. SQ SEQUENCE 363 AA; 38433 MW; EA069B4C6E5BE2B5 CRC64; MPALPWLHPE RANALLDALR ERILIIDGAM GTMIQRHGLQ EDDYRGERFA GGYDHSHGPG CDHGTPEGHD LKGNNDLLLL TRPQIVADIH TAYLEAGADL VETNTFNATS VSQADYHLEH LVYELNKAGA AVARTCCDAV AATTPGKPRF VIGVVGPTSR TASISPDVND PGFRNTSFDE LRDTYREAIE GLIDGGADTI MVETIFDTLN AKAALYALEE AFDARGARLP VMISGTITDA SGRTLSGQTA EAFHASLAHA RPLSIGLNCA LGADAMRPHV ETLAQVADCY VSAHPNAGLP NAFGEYDETP EDMASTLRGF AEDGLLNLVG GCCGSTPDHI RAIAAAVTGL PPRALPGTRE QAA // ID B2GBY2_LACF3 Unreviewed; 310 AA. AC B2GBY2; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 27-MAY-2015, entry version 33. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:BAG27164.1}; GN OrderedLocusNames=LAF_0828 {ECO:0000313|EMBL:BAG27164.1}; OS Lactobacillus fermentum (strain NBRC 3956 / LMG 18251). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=334390 {ECO:0000313|EMBL:BAG27164.1, ECO:0000313|Proteomes:UP000001697}; RN [1] {ECO:0000313|EMBL:BAG27164.1, ECO:0000313|Proteomes:UP000001697} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 3956 / LMG 18251 {ECO:0000313|Proteomes:UP000001697}; 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 ----------------------------------------------------------------------- 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; BAG27164.1; -; Genomic_DNA. DR RefSeq; WP_003681749.1; NC_010610.1. DR RefSeq; YP_001843644.1; NC_010610.1. DR STRING; 334390.LAF_0828; -. DR EnsemblBacteria; BAG27164; BAG27164; LAF_0828. DR GeneID; 6232276; -. DR KEGG; lfe:LAF_0828; -. DR PATRIC; 22225850; VBILacFer15497_0911. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; LFER334390:GJ2S-873-MONOMER; -. DR Proteomes; UP000001697; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001697}; KW Methyltransferase {ECO:0000313|EMBL:BAG27164.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001697}; KW Transferase {ECO:0000313|EMBL:BAG27164.1}. SQ SEQUENCE 310 AA; 33675 MW; 7DA01ED5B30D73D5 CRC64; MKLLERLAQG PLVLDGSMST PLEVAGAKTN SDLWTSQTLI DNPDLVYQVH LDYFKAGADL TITDTYQTNV DALVRHGLSE EEARNLIKRA VQLANQARDD YEKETGKHNY VAGSIGPYGA YLADGSEYRG DYDLTAIQLQ NFHLPRLAAI LATGVDCLAL ETQPKLTEVV AILALLKTLE PTMPVYVSFS LRDAEHLSDG TSLKEAVQVV TKDPQVFAVG VNCVGLDLVT PAIKAIKEVT DKPVIVYPNS GATYDPTVKQ WRFEEGTPRF VNAIDDWITA GAAIIGGCCT TLPQDIAVVA EKLRGVGNNR // ID B2HGB8_MYCMM Unreviewed; 1244 AA. AC B2HGB8; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 29-APR-2015, entry version 49. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase, MetH {ECO:0000313|EMBL:ACC43230.1}; GN Name=metH {ECO:0000313|EMBL:ACC43230.1}; GN OrderedLocusNames=MMAR_4825 {ECO:0000313|EMBL:ACC43230.1}; OS Mycobacterium marinum (strain ATCC BAA-535 / M). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=216594 {ECO:0000313|EMBL:ACC43230.1, ECO:0000313|Proteomes:UP000001190}; RN [1] {ECO:0000313|EMBL:ACC43230.1, ECO:0000313|Proteomes:UP000001190} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-535 / M {ECO:0000313|Proteomes:UP000001190}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000854; ACC43230.1; -; Genomic_DNA. DR RefSeq; WP_012396362.1; NC_010612.1. DR RefSeq; YP_001853085.1; NC_010612.1. DR STRING; 216594.MMAR_4825; -. DR EnsemblBacteria; ACC43230; ACC43230; MMAR_4825. DR KEGG; mmi:MMAR_4825; -. DR PATRIC; 18071039; VBIMycMar75906_5181. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; QPFFNAW; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; MMAR216594:GJOB-4862-MONOMER; -. DR Proteomes; UP000001190; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001190}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACC43230.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001190}; KW Transferase {ECO:0000313|EMBL:ACC43230.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 253 253 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 316 316 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 773 773 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1244 AA; 135964 MW; 4F209878C748C412 CRC64; MSAFEPNIRP DCTDALTAAL GQRIMVIDGA MGTAIQRDRP DEAGYRGERF KDWPSDLVGN NDLLSLTQPQ IIEGIHREYL QAGADILETN TFNANAVSLS DYDMAELAYE LNYAGAALAR AAADEFSTPE KPRYVAGALG PTTRTASISP DVNDPGARNV SYDQLVAAYL EAANGLVDGG ADIIIIETIF DSLNAKAAVF AVETLFEDRG RRWPVIISGT ITDASGRTLS GQVTEAFWNA IRHAKPIAVG LNCALGAPEM RPYIAEMARI ADTFVSCYPN AGLPNAFGEY DETPEHQAGY IAEFADAGLV NLVGGCCGTA PPHIAEIAKV VEGKAPRELP EIPVATRLSG LEPLNISDDS LFVNIGERTN ITGSARFRNL IKAEDYDTAL SVALQQVEVG AQVIDINMDE GMIDGVAAMD RFTKLIAAEP DISRVPVMID SSKWEVIEAG LKNVQGKPIV NSISMKEGEE KFVREARLCR KYGAAVVVMA FDEKGQADNL ERRKEICGRA YRILTEEVGF PAEDIIFDPN CFALATGIEE HATYGIDFIE ACAWIKENLP GVHISGGISN VSFSFRGNNP VREAIHAVFL FHAIKAGLDM GIVNAGALVP YDSIDPELRE RIEDVVLNRR EDAAERLLEI AERFNTKGKS EDPAAAEWRS LPVRERITHA LVKGIDAHVD ADTEELRAEI AAAGGRPIEV IEGPLMDGMN VVGDLFGAGK MFLPQVVKSA RVMKKAVAYL LPFIEAEKAQ SGSTEQDKTN GIIIMATVKG DVHDIGKNIV GVVLQCNNYT VVDLGVMVPA EKILAAAREY DADIIGLSGL ITPSLDEMVN FAAAMEREGM QIPLLIGGAT TSRAHTAVKV APRRSGPVVW VKDASRSVPV AAALLDDKQR PGLLEATAAD YAALRERHSQ KNERPMLTLE KARANRTPID WDGYTPPLPA QGLGVREFHD YDLAELREYI DWQPFFNAWE MKGRFPDILN NPATGEAARK LYNDAQEMLD TLIREKWLTA NGVIGFFPAN AVGDDIEVYT DETRAEVLTT LHNLRQQGEH RAGIPNRSLG DFIAPKDTGL ADYVGAFAVT AGLGSQTKIV EFKEALDDYS AILLESIADR LAEAFAERMH QRVREEFWGY QPDEQLDNEA LIGERYVGIR PAPGYPACPE HTEKTTLFEL MDVTKRTGIE LTESMAMWPG AAVSGWYFSH PQSQYFVVGR MAQDQVADYA KRKGWTLPEA ERWLGPNLGY NPED // ID B2IJ02_BEII9 Unreviewed; 1246 AA. AC B2IJ02; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 27-MAY-2015, entry version 51. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACB94765.1}; GN OrderedLocusNames=Bind_1123 {ECO:0000313|EMBL:ACB94765.1}; 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 {ECO:0000313|EMBL:ACB94765.1, ECO:0000313|Proteomes:UP000001695}; RN [1] {ECO:0000313|Proteomes:UP000001695} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 9039 / DSM 1715 / NCIB 8712 RC {ECO:0000313|Proteomes:UP000001695}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001016; ACB94765.1; -; Genomic_DNA. DR RefSeq; WP_012384122.1; NC_010581.1. DR RefSeq; YP_001832254.1; NC_010581.1. DR STRING; 395963.Bind_1123; -. DR EnsemblBacteria; ACB94765; ACB94765; Bind_1123. DR KEGG; bid:Bind_1123; -. DR PATRIC; 21084977; VBIBeiInd21058_1435. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; BIND395963:GJA7-1137-MONOMER; -. DR Proteomes; UP000001695; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001695}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001695}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 253 253 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 316 316 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 768 768 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1246 AA; 136754 MW; FDEB58734617CC3D CRC64; MSQSPLNGPA TTKALLEAAA ERVLVLDGAM GTMIQQRKFT EADFRGERFK DWPSDLRGNN DLLTLTQPDA IVAIHRAYFE AGADIIGTNT FNSTRISQAD YGMEELVAEL NRESARLARQ AADEAEAKDG RRRFVAGALG PTNRTASISP DVNNPGFRAV TFDDLRAAYA EAASALIEGG ADILIVETIF DTLNAKAALA AIDDVYESLN VRLPVMISGT ITDLSGRTLS GQTPTAFWYS LRHVKPITIG LNCALGAREM RAHIAELSRV ADTLICAYPN AGLPNEFGLY DESPEYMASL VGEFAEAGLV NIVGGCCGTT PAHIHAIAKR VAGIAPRKIP AIEPLLRLSG LEPFTLTKDI RFVNVGERTN VTGSAKFRKL IKEGQFSAAL DVARDQVVMG AQVIDVNMDE GLLDSEAVMR DFLNLVAAEP DIARVPVMID SSKFVVIEAG LKCIQGKGIV NSISLKEGEE NFIQAAKAVH RYGAAVVVMA FDEQGQADTR ARKVEICSRA YDILVNRCGF PPEDIIFDPN IFAVATGIEE HNNYGVDFIE ATREIRQKFP LVHISGGVSN LSFSFRGNEP VRQAMHSVFL YHAIAAGMDM GIVNAGQLSV YEELDPELRE ACEDVVLNRR PEATERLLAL AENYKGQGTE KQEKSLAWRE EPVEKRLEHA LVNGITEFID QDVEEARLAS TRTLDVIEGP LMAGMNVVGD LFGSGKMFLP QVVKSARVMK AAVAYLMPFM EAEKAANGGA VRSSAGKILM ATVKGDVHDI GKNIVGVVLA CNNYEIIDLG VMVPAAKILE TARAEQVDCI GLSGLITPSL DEMCFVAAEL EREGFDVPLL IGGATTSRVH TAVKIHPNYT RGQTVYVTDA SRAVGTVQSL LSETSRGAYI ETIRAEYQKV SDAHRRAEAE KQRLPLQRAR QNAFRPDWAA YQPPRPTFTG ARIFGSYDVG ELVPYIDWTP FFQTWELRGR YPALLDDPKQ GASARQLFDD AQAMLKRIVE EHWFDPKAVI GFWPANAVDD DIKLYTGESR SEELATFFTL RQQLSKQGDK PNLALADFVA PRDSGKADYI GGFVVTAGAR EEKIAERFAK ANDDYGSIMV KALADRIAEA FAERMHERVR REFWAYAPDE NLTNEERISE SYRGIRPAPG YPAQPDHSEK ATLFRLLEAE RRISVSLTES FAMWPGSSVS GLYIAQPEAY YFGVAKVERD QVEDYARRKG MSIAEVERWL TPILNYNPAA VAEAAE // ID B2J2H4_NOSP7 Unreviewed; 1177 AA. AC B2J2H4; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 27-MAY-2015, entry version 51. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACC78866.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ACC78866.1}; GN OrderedLocusNames=Npun_F0065 {ECO:0000313|EMBL:ACC78866.1}; OS Nostoc punctiforme (strain ATCC 29133 / PCC 73102). OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc. OX NCBI_TaxID=63737 {ECO:0000313|EMBL:ACC78866.1, ECO:0000313|Proteomes:UP000001191}; RN [1] {ECO:0000313|Proteomes:UP000001191} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29133 / PCC 73102 {ECO:0000313|Proteomes:UP000001191}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001037; ACC78866.1; -; Genomic_DNA. DR RefSeq; WP_012406895.1; NC_010628.1. DR RefSeq; YP_001863809.1; NC_010628.1. DR ProteinModelPortal; B2J2H4; -. DR STRING; 63737.Npun_F0065; -. DR EnsemblBacteria; ACC78866; ACC78866; Npun_F0065. DR KEGG; npu:Npun_F0065; -. DR PATRIC; 22751708; VBINosPun48114_0073. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR PhylomeDB; B2J2H4; -. DR BioCyc; NPUN63737:GJNP-65-MONOMER; -. DR Proteomes; UP000001191; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001191}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACC78866.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001191}; KW Transferase {ECO:0000313|EMBL:ACC78866.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 230 230 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 296 296 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 297 297 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 739 739 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1177 AA; 130945 MW; ACAD7EF99011BC2D CRC64; MTHSFLERLR SPDSPVLVFD GAMGTNLQTQ NLTAEDFGGP QYEGCNEYLV HTKPEAEAVA KVHRDFLAAG ADVIETDTFG STSLVLAEYD LADQAYYLSK TAAELAKRVA AEFSTPEKPR FVAGSIGPTT KLPTLGHIDF DTMKATFAEQ AEALWDGGVD LFLVETCQDV LQIKAALNGI EEVFAKKGDR RPLMVSVTME SMGTMLVGSE ISAVLAILEP YPIDILGLNC ATGPDLMKPH IKYLSEHSPF IVSCIPNAGL PENVGGQAHY RLTPLELRMS LMHFVEDLGV QVIGGCCGTR PEHIQQLAEV AKDLKPKVRQ PSLEPAAASI YTTQPYDQDN SFLIVGERLN ASGSKKCRDL LNAEDWDGLV SMARAQVKEG AHILDINVDY VGRDGVRDMH ELVSRIVNNV TLPLMLDSTE WEKMEAGLKV AGGKCLLNST NYEDGEPRFL KVLELAKKYG AGVIIGTIDE DGMARTADKK FAIAGRAYRQ AVEYGIPPTE IFFDTLALPI STGIEEDREN GKATIESIRR IRQELPGSHV ILGVSNISFG LTPASRMVLN SVFLHEATTA GMDAAIVSAN KILPLSKIDA RHQEICRQLI YDERKFEGDV CVYDPLGELT TVFAGVTTKR DRSLDESLPI PERLKRHIID GERIGLEEHL KKALEEHPPL EIINTFLLDG MKVVGELFGS GQMQLPFVLQ SAETMKAAVA FLEPFMEKSE SGNNAKGTFI IATVKGDVHD IGKNLVDIIL SNNGYKVINL GIKQPVENII KAYEQHKADC IAMSGLLVKS TAFMKENLEV FNEKGISVPV ILGGAALTPK FVYEDCQNTY KGKVVYGKDA FSDLHFMDKL MPAKATGNWE DLQGFLNEVE TAEVSTNGHK EPKTKTAEET SAEPKVVDTR RSEAVAVDIE RPTPPFWGTK LLQPSDIPIE EIFWHLDLQA LVAGQWQFRK PKEQSKEEYQ AFLAEKVYPI LETWKQRIIE ENLLHPQVIY GYFPCQSEGN SLHIYDSENQ SQQITTFEFP RQKSLRRLCI ADFFAPKESG IIDVFPMQAV TVGEIATEFA QKLFADNQYT DYLYFHGMAV QVAEAVAEWT HARIRRELGF TAEEPDNIRD ILAQRYRGSR YSFGYPACPN IQDQYKQLEL LQTDRIKLYM DESEQLYPEQ STTAIITYHP VAKYFSA // ID B2JKJ5_BURP8 Unreviewed; 356 AA. AC B2JKJ5; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 27-MAY-2015, entry version 41. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACC69384.1}; GN OrderedLocusNames=Bphy_0191 {ECO:0000313|EMBL:ACC69384.1}; OS Burkholderia phymatum (strain DSM 17167 / STM815). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=391038 {ECO:0000313|EMBL:ACC69384.1, ECO:0000313|Proteomes:UP000001192}; RN [1] {ECO:0000313|Proteomes:UP000001192} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17167 / STM815 {ECO:0000313|Proteomes:UP000001192}; 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; ACC69384.1; -; Genomic_DNA. DR RefSeq; WP_012399613.1; NC_010622.1. DR RefSeq; YP_001856430.1; NC_010622.1. DR STRING; 391038.Bphy_0191; -. DR EnsemblBacteria; ACC69384; ACC69384; Bphy_0191. DR KEGG; bph:Bphy_0191; -. DR PATRIC; 19186499; VBIBurPhy25146_0208. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; BPHY391038:GI4Z-194-MONOMER; -. DR Proteomes; UP000001192; Chromosome 1. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001192}; KW Methyltransferase {ECO:0000313|EMBL:ACC69384.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001192}; KW Transferase {ECO:0000313|EMBL:ACC69384.1}. SQ SEQUENCE 356 AA; 38106 MW; A389A647BC4C4CDB CRC64; MNQPAPSAVP ARAGAAYTRG AALPALLESR ILILDGAMGT MIQRYKLDEA AYRGERFKDY ARDIKGNNEL LSITQPHVIS EIHEQYLAAG ADIIETNTFG ATTVAQADYG MEDLAVEMNR ESAKLARAAC DKYSTPDKPR FVAGAIGPTP KTASISPDVN DPGARNVTFD ELRAAYYEQA KALMEGGADL FLVETIFDTL NAKAALFALD ELFEDTGERL PIMISGTVTD ASGRILSGQT VEAFWNSLRH AKPLTFGLNC ALGAALMRPY IAELAKLCDT YVSCYPNAGL PNPMSDTGFD ELPADTSGLL KEFAQAGLVN IAGGCCGTTP DHIAAIAKAL SEVKPRKWPG QYRDAA // ID B2Q553_PROST Unreviewed; 1221 AA. AC B2Q553; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 27-MAY-2015, entry version 37. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EDU57972.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EDU57972.1}; GN Name=metH {ECO:0000313|EMBL:EDU57972.1}; GN ORFNames=PROSTU_04024 {ECO:0000313|EMBL:EDU57972.1}; OS Providencia stuartii ATCC 25827. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Providencia. OX NCBI_TaxID=471874 {ECO:0000313|EMBL:EDU57972.1, ECO:0000313|Proteomes:UP000004506}; RN [1] {ECO:0000313|EMBL:EDU57972.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 25827 {ECO:0000313|EMBL:EDU57972.1}; 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] {ECO:0000313|EMBL:EDU57972.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 25827 {ECO:0000313|EMBL:EDU57972.1}; 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] {ECO:0000313|EMBL:EDU57972.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 25827 {ECO:0000313|EMBL:EDU57972.1}; 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 (MAY-2008) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EDU57972.1}. 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; ABJD02000103; EDU57972.1; -; Genomic_DNA. DR RefSeq; WP_004926096.1; NZ_DS607679.1. DR EnsemblBacteria; EDU57972; EDU57972; PROSTU_04024. DR PATRIC; 25545990; VBIProStu71739_3739. DR Proteomes; UP000004506; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000004506}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EDU57972.1}; KW Transferase {ECO:0000313|EMBL:EDU57972.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 241 241 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 752 752 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1221 AA; 135851 MW; 9541E4130447B647 CRC64; MLEQELQKRI LVLDGAMGTM IQRHKLTEEQ FRGERFADWP CDLKGNNDLL VLTQPEIIRD IHDQYFAAGA DIVETNTFNS TTIAMADYKM ESLSAEINEA AARIARECAD EWTRKTPEQP RYVAGVLGPT NRTASISPDV NDPAFRNINF DQLVEAYRES THALIKGGVD LIMIETIFDT LNAKAAIFAV ETEFEALGVT LPVMISGTIT DASGRTLSGQ TTEAFYNSLR HARPLSFGLN CALGPNELRQ YVSELSRIAE CYVSAHPNAG LPNAFGEYDL DAQNMAEQIR EWAQAGFLNI VGGCCGTTPL HIKKIVEAVK GIAPRALPKL PVECRLSGLE PLNIGKDSLF VNVGERTNVT GSAKFKRLIK EGNYQEALDI ARQQVENGAQ IIDINMDEGM LDSEAAMVRF LNLIAGEPDI ARVPIMIDSS KWDVIEKGLK CIQGKGIVNS ISMKEGESAF IEHAKLVRKY GAAVIVMAFD EVGQADTRER KIEICRRAYH VLTDTVGFPP EDIIFDPNIF AVATGIEEHN NYAVDFIEVC QDIKQQLPHA MISGGVSNVS FSFRGNDPVR EAIHAVFLYY AIRNGMDMGI VNAGQLAIYD DLPKELKDAV EDVILNRRED STERLLELAE KYRASGSEEQ QVQQAEWRSW AVEKRLEYAL VKGITEFIIP DTEEARQLAA SPIEVIEGPL MNGMNVVGDL FGEGKMFLPQ VVKSARVMKQ AVAYLEPYIQ ALKQSGSSAG KILLATVKGD VHDIGKNIVG VVLQCNNYEI VDLGVMVPCE TILKTAREQN VDVIGLSGLI TPSLDEMVHV AKEMERQGFT IPLMIGGATT SKAHTAVKIE PNYSHSVTYV QNASRTVGVV SALLSATQKA EFVARTRREY EIVREQHGRK KPKTPPVSLE IARANSVKID WQNYQPPVPR FLGVKEVKAS IETLRHYIDW TPFFMTWSLA GKYPRILEDE VVGEEARKLL KDANNMLDQL AKDNALTPRG IFGLFPANSV GDDIEIYRSS ARDSADVIAL NLRQQTEKKE FPNYCLSDFV APKASGKADY IGAFAVTGGL EEDALADGYE QQHDDYNKIM LKALADRLAE AFAEYLHQQV RKEYWGYAPD EDLPNDELIR EKYQGIRPAP GYPACPEHTE KAKIWQLLDV ENRVGMQLTS SYAMWPGASV SGWYFSHPES KYFAVAQVQR DQVEDYAKRK GMSVSELERW LAPNLGYDPE D // ID B2RCQ6_HUMAN Unreviewed; 406 AA. AC B2RCQ6; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 04-MAR-2015, entry version 34. DE SubName: Full=cDNA, FLJ96222, highly similar to Homo sapiens betaine-homocysteine methyltransferase (BHMT), mRNA {ECO:0000313|EMBL:BAG37653.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG37653.1}; RN [1] {ECO:0000313|EMBL:BAG37653.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Kidney {ECO:0000313|EMBL:BAG37653.1}; RA Wakamatsu A., Yamamoto J., Kimura K., Kaida T., Tsuchiya K., Iida Y., RA Takayama Y., Murakawa K., Kanehori K., Andoh T., Kagawa N., Sato R., RA Kawamura Y., Tanaka S., Kisu Y., Sugano S., Goshima N., Nomura N., RA Isogai T.; RT "NEDO functional analysis of protein and research application RT project."; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK315224; BAG37653.1; -; mRNA. DR UniGene; Hs.80756; -. DR ProteinModelPortal; B2RCQ6; -. DR SMR; B2RCQ6; 10-398. DR PRIDE; B2RCQ6; -. DR HOVERGEN; HBG080367; -. DR UniPathway; UPA00051; UER00083. DR NextBio; 35468195; -. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000313|EMBL:BAG37653.1}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000313|EMBL:BAG37653.1}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 217 217 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 406 AA; 44968 MW; 147F25B8CEDA7D56 CRC64; MPPVGGKKAK KGILERLNAG EIVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAVRQLH REFLRAGSNV MQTFTFYASE DKLENRGNYV LEKISGQEVN EAACDIARQV ADEGDALVAG GVSQTPSYLS CKSETEVKKV FLQQLEVFMK KNVDFLIAEY FEHVEEAVWA VETLIASGKP VAATMCIGPE GDLHGVPPGE CAVRLVKAGA SIIGVNCHFD PTISLKTVKL MKEGLEAARL KAHLMSQPLA YHTPDCNKQG FIDLPEFPFG LEPRVATRRD IQKYAREAYN LGVRYIGGCC GFEPYHIRAI AEELAPERGF LPPASEKHGS WGSGLDMHTK PWVRARARKE YWENLRIASG RPYNPSMSKP DGWGVTKGTA ELMQQKEATT EQQLKELFEK QKFKSQ // ID B2RDF4_HUMAN Unreviewed; 363 AA. AC B2RDF4; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 04-MAR-2015, entry version 31. DE SubName: Full=cDNA, FLJ96586, highly similar to Homo sapiens betaine-homocysteine methyltransferase 2 (BHMT2), mRNA {ECO:0000313|EMBL:BAG37901.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG37901.1}; RN [1] {ECO:0000313|EMBL:BAG37901.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Tongue {ECO:0000313|EMBL:BAG37901.1}; RA Wakamatsu A., Yamamoto J., Kimura K., Kaida T., Tsuchiya K., Iida Y., RA Takayama Y., Murakawa K., Kanehori K., Andoh T., Kagawa N., Sato R., RA Kawamura Y., Tanaka S., Kisu Y., Sugano S., Goshima N., Nomura N., RA Isogai T.; RT "NEDO functional analysis of protein and research application RT project."; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK315520; BAG37901.1; -; mRNA. DR UniGene; Hs.114172; -. DR ProteinModelPortal; B2RDF4; -. DR SMR; B2RDF4; 10-362. DR HOVERGEN; HBG080367; -. DR UniPathway; UPA00051; UER00083. DR NextBio; 35468260; -. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000313|EMBL:BAG37901.1}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000313|EMBL:BAG37901.1}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 208 208 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 363 AA; 40324 MW; 92CEE2CFA2D56003 CRC64; MAPAGRPGAK KGILERLESG EVVIGDGSFL ITLEKRGYVK AGLWTPEAVI EHPDAVRQLH MEFLRAGSNV MQTFTFSASE DNMESKWEDV NAAACDLARE VAGKGDALVA GGICQTSIYK YQKDEARIKK LFRQQLEVFA WKNVDFLIAE YFEHVEEAVW AVEVLKESDR PVAVTMCIGP EGDMHDITPG ECAVRLVKAG ASIVGVNCRF GPDTSLKTME LMKEGLEWAG LKAHLMVQPL GFHAPDCGKE GFVDLPEYPF GLESRVATRW DIQKYAREAY NLGVRYIGGC CGFEPYHIRA IAEELAPERG FLPPASEKHG SWGSGLDMHA KPWIRARARR EYWENLLPAS GRPFCPSLSK PDF // ID B2SWV8_BURPP Unreviewed; 356 AA. AC B2SWV8; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 27-MAY-2015, entry version 44. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACD14902.1}; GN OrderedLocusNames=Bphyt_0477 {ECO:0000313|EMBL:ACD14902.1}; OS Burkholderia phytofirmans (strain DSM 17436 / PsJN). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=398527 {ECO:0000313|EMBL:ACD14902.1, ECO:0000313|Proteomes:UP000001739}; RN [1] {ECO:0000313|Proteomes:UP000001739} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17436 / PsJN {ECO:0000313|Proteomes:UP000001739}; 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 ----------------------------------------------------------------------- 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; ACD14902.1; -; Genomic_DNA. DR RefSeq; WP_012431545.1; NC_010681.1. DR RefSeq; YP_001894126.1; NC_010681.1. DR STRING; 398527.Bphyt_0477; -. DR EnsemblBacteria; ACD14902; ACD14902; Bphyt_0477. DR KEGG; bpy:Bphyt_0477; -. DR PATRIC; 19210839; VBIBurPhy117947_4210. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; BPHY398527:GJEX-479-MONOMER; -. DR Proteomes; UP000001739; Chromosome 1. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001739}; KW Methyltransferase {ECO:0000313|EMBL:ACD14902.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001739}; KW Transferase {ECO:0000313|EMBL:ACD14902.1}. SQ SEQUENCE 356 AA; 38335 MW; 860ACE5C8C5F896F CRC64; MNQPAQTATP ARPDAAYTRG TALPALLKSR ILILDGAMGT MIQRYKLDEA RYRGERFKDY GRDIKGNNEL LSITQPQIIR EIHEQYLAAG ADIIETNTFG ATTVAQADYG MEGLAIEMNL ESAKLARAAC DKYSTPDKPR FVAGAIGPTP KTASISPDVN DPGARNVTFD ELRAAYYEQA KALLDGGADL FLVETIFDTL NAKAALFALD ELFEDTGERL PIMISGTVTD ASGRILSGQT VEAFWNSLRH AKPLTFGLNC ALGAALMRPY IAELAKLCDT YVSCYPNAGL PNPMSDTGFD ELPADTSGLL KEFAQAGLVN IAGGCCGTTP EHIAAIAQAL AEVKPRQWPT QYRDAA // ID B2TP83_CLOBB Unreviewed; 799 AA. AC B2TP83; U4P8N5; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 27-MAY-2015, entry version 47. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:ACD24053.1}; DE SubName: Full=MetH protein {ECO:0000313|EMBL:CDH91759.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CDH91759.1}; GN Name=metH {ECO:0000313|EMBL:CDH91759.1}; GN OrderedLocusNames=CLL_A2853 {ECO:0000313|EMBL:ACD24053.1}; GN ORFNames=CB17B2770 {ECO:0000313|EMBL:CDH91759.1}; OS Clostridium botulinum (strain Eklund 17B / Type B). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=935198 {ECO:0000313|EMBL:ACD24053.1, ECO:0000313|Proteomes:UP000001195}; RN [1] {ECO:0000313|Proteomes:UP000001195} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Eklund 17B / Type B {ECO:0000313|Proteomes:UP000001195}; 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. RN [2] {ECO:0000313|EMBL:ACD24053.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Eklund 17B {ECO:0000313|EMBL:ACD24053.1}; 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., 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., Gronow S., Klenk H.-P., Eisen J.A.; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:ACD24053.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Eklund 17B {ECO:0000313|EMBL:ACD24053.1}; RA Shrivastava S., Brinkac L.M., Dodson R.J., Harkins D.M., Durkin A.S., RA Sutton G.; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:CDH91759.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=B str. Eklund 17B {ECO:0000313|EMBL:CDH91759.1}; RX PubMed=23679073; DOI=10.1186/1471-2164-14-333; RA Stringer S.C., Carter A.T., Webb M.D., Wachnicka E., Crossman L.C., RA Sebaihia M., Peck M.W.; RT "Genomic and physiological variability within Group II (non- RT proteolytic) Clostridium botulinum."; RL BMC Genomics 14:333-333(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; CP001056; ACD24053.1; -; Genomic_DNA. DR EMBL; FR745875; CDH91759.1; -; Genomic_DNA. DR RefSeq; WP_012424836.1; NC_010674.1. DR RefSeq; YP_001887040.1; NC_010674.1. DR ProteinModelPortal; B2TP83; -. DR STRING; 508765.CLL_A2853; -. DR EnsemblBacteria; ACD24053; ACD24053; CLL_A2853. DR GeneID; 19965956; -. DR PATRIC; 19398518; VBICloBot123574_2762. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CBOT508765:GJ4H-2842-MONOMER; -. DR Proteomes; UP000001195; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001195}; KW Methyltransferase {ECO:0000313|EMBL:ACD24053.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001195}; KW Transferase {ECO:0000313|EMBL:ACD24053.1}. SQ SEQUENCE 799 AA; 87942 MW; D29D68354A09016D CRC64; MGLKEFIKDN ILVFDGAMGT MLQKEGLKLG ENPEIFNIEE SEKVKKIHEE YIKNGAMIIT SNTFGANELK LENTGYTVEE IINAAISLAK EATGNEKVYI ALDIGPIGEL LEPMGTLSFD RAYEIFKRQI VQGEKSGADL ILIETMTDLY EAKAALLAAK ENTSLPVFCT MSFDENGRTF TGCTPESMAI TLEGIGADAV GINCSLGPKE LLPIVKRIKK ATNLPIMTQP NAGLPKLSFG EAIYDITSDE FEYWVNEFVK EGVSIIGGCC GTTPKFIKRL RVLADNNKRI IRDKIEFSAV CTPSNVVKIE GVKVIGERIN PTGKKLFKEA LKNNDIDYIL KQAIEQIEAG AEILDVNVGL PEINEKEMMK KVVKEIQGII DAPLQIDSSN IAAIETGLRA YNGKPIVNSV NGEDEVLEKI LPLVKKYGAS VVGLTLDKRG IPATADERFK IAEKIVKKAK EYGIEKHNVF IDCLVLTASA QQAEVKETLK ALRRVKEELG VKTLLGVSNI SFGLPCRELI NETFLAMAIA NGLDLPIMNP NSTGMMAVIN SYNVLANIDK RSEKYISIYG NVKVERGLRD TSKKNIEVIK SENIDLKYIV IKGLKDEAEE ATKHILKTMN ELSVVNEILI PALDEVGLKY EKGEIFLPQL IQCAETVKKA FEVIKKRLVI NKSNSISKGK IVLATVKEDI HDIGKNIVKV ILENYGYQII DLGKDVSVET VVDVSLKNDI KLVGLSALMT TTLKSMEETI KGLRENGYKG KVFVGGAVLT SEYAKQIGAD YYAKDARESV EIAKIVLNN // ID B2UDX2_RALPJ Unreviewed; 346 AA. AC B2UDX2; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 27-MAY-2015, entry version 43. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACD25312.1}; GN OrderedLocusNames=Rpic_0149 {ECO:0000313|EMBL:ACD25312.1}; OS Ralstonia pickettii (strain 12J). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=402626 {ECO:0000313|EMBL:ACD25312.1, ECO:0000313|Proteomes:UP000002566}; RN [1] {ECO:0000313|Proteomes:UP000002566} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=12J {ECO:0000313|Proteomes:UP000002566}; 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; ACD25312.1; -; Genomic_DNA. DR RefSeq; WP_009239243.1; NC_010682.1. DR RefSeq; YP_001897744.1; NC_010682.1. DR STRING; 402626.Rpic_0149; -. DR EnsemblBacteria; ACD25312; ACD25312; Rpic_0149. DR GeneID; 6288831; -. DR KEGG; rpi:Rpic_0149; -. DR PATRIC; 20251164; VBIRalPic63053_1351. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; RPIC402626:GH94-148-MONOMER; -. DR Proteomes; UP000002566; Chromosome 1. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002566}; KW Methyltransferase {ECO:0000313|EMBL:ACD25312.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002566}; KW Transferase {ECO:0000313|EMBL:ACD25312.1}. SQ SEQUENCE 346 AA; 37540 MW; 7D5FFC461E5C1ADE CRC64; MTAPLPYTRA ANLPALLRER ILILDGAMGT MIQRYKLNEA QYRGERFANH PIDVKGNNEL LLLTRPDVIR EIHEQYLAAG ADLIETNTFG ATTIAQEDYK MAELAYEMNV VAARLAREAC DKYSTPDKPR FVAGAFGPTP KTASISPDVN DPGARNVSFD QLRDAYYEQG KALLEGGADV FLVETIFDTL NAKAALFAID QLFEDTGERV PVMISGTVTD ASGRILSGQT VEAFWNSLRH AKPITFGLNC ALGAALMRPY IAELAKICDT AVSCYPNAGL PNPMSETGFD ETPEVTSSLV DEFASAGLVN LVGGCCGTTP EHIKAIADRV ANRKPRAWPG QYLEAA // ID B2UNQ8_AKKM8 Unreviewed; 1253 AA. AC B2UNQ8; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 29-APR-2015, entry version 52. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACD05774.1}; GN OrderedLocusNames=Amuc_1961 {ECO:0000313|EMBL:ACD05774.1}; OS Akkermansia muciniphila (strain ATCC BAA-835 / Muc). OC Bacteria; Verrucomicrobia; Verrucomicrobiae; Verrucomicrobiales; OC Verrucomicrobiaceae; Akkermansia. OX NCBI_TaxID=349741 {ECO:0000313|EMBL:ACD05774.1, ECO:0000313|Proteomes:UP000001031}; RN [1] {ECO:0000313|Proteomes:UP000001031} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-835 / Muc {ECO:0000313|Proteomes:UP000001031}; RX PubMed=21390229; DOI=10.1371/journal.pone.0016876; RA van Passel M.W., Kant R., Zoetendal E.G., Plugge C.M., Derrien M., RA Malfatti S.A., Chain P.S., Woyke T., Palva A., de Vos W.M., Smidt H.; RT "The genome of Akkermansia muciniphila, a dedicated intestinal mucin RT degrader, and its use in exploring intestinal metagenomes."; RL PLoS ONE 6:E16876-E16876(2011). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001071; ACD05774.1; -; Genomic_DNA. DR RefSeq; WP_012420988.1; NC_010655.1. DR RefSeq; YP_001878555.1; NC_010655.1. DR ProteinModelPortal; B2UNQ8; -. DR SMR; B2UNQ8; 689-928. DR STRING; 349741.Amuc_1961; -. DR EnsemblBacteria; ACD05774; ACD05774; Amuc_1961. DR KEGG; amu:Amuc_1961; -. DR PATRIC; 20837036; VBIAkkMuc16855_2240. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; AMUC349741:GHZ7-2017-MONOMER; -. DR Proteomes; UP000001031; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001031}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001031}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 279 279 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 344 344 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 345 345 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 794 794 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1253 AA; 138234 MW; D361B91C1AB2327E CRC64; MSRASRTERL DYLKDQLRKR VVILDGAMGT NIQKFRLGEG DYRGERFADA ECYPNDLKNN NDLLVLTRPD IILDIHRRFL DTGRTDILET CTFGATSIGQ HDYFWHRPEE GSHKDQQYFQ EVVDAPELKA LVRELNLAAA ALARQACDEA EAADGKPRLV AGSIGPMPVT CSLSPDVNDP GFRAVNFRQL RQAYRDQVLA LLEGGVDMLL VETIFDTLNA KAALFAIEEI FEEQPESSVP VMVSVTLTDK AGRTLSGQTI EAFWNSIRHV RPFSVGINCA LGPDLMRPFA EELSGLADCH MSIYANAGLP NPLSPTGYDL LPADMARFMK EYAEQGLLNI VGGCCGTTPE HIGAIAAAVE GMPPRVPAPQ TPALRLSGYE AYNHTREKNT LFVGERCNVA GSPKFARLIR EGNYEEAVSI ARQQVENGAL VLDFCFDDGL IDGPQAMVRF LNLVSAEPDI ARVPFMVDSS KWEVLEAGLQ CMQGKGIVNS ISLKEGEEEF LKKAALIKKY GAAVVVMAFD EQGQAANYED RVRISRRAYD LLVNRVQFPP EDIIFDPNVL TVGTGIAEHA DYALDFFKAA GWISRNLPHA HISGGISNVS FAFRGNNPVR EAMHSAFLYH ATQQGLDMCI VNAGMLEVYD NIPKDRLELI EDVLLNRRTD ATERLTDYAE KLAAEKTGDG KEKKTVQAWR EQDVAKRLEY SLIKGITEFV DADTEEAFQE LGSPLNVIEG PLMAGMKVVG QLFGDGKMFL PQVVKSARVM KQAVAWLTPY IEADSKGAAK AGKAVIATVK GDVHDIGKNI VGVVLSCNGF EMIDLGVMVH CDTILDRAEA EQADLVMLSG LITPSLEEMS HVAAEMERRG MTIPLMVGGA TTSALHTALK IAPHYQGAVV HTEDASQVVP AAASLVGEKK DSYIAAVKAR QEELRNNHEN KPVRDLLPLE KARELRWKGA EGGYLPPVPA RLGPVSIGSL HSSVSCGCCS DDPRYYVTVQ ELIERMDWTP FFHAWELHGT WDRARREFRT KDPSKAEAAA ALYQDALRLL EQAVKENRYQ ARGVIGIFPA NSTASHDDIT VWADESRTIP LATLLTQRQQ LDKQGKPRLA LADFIAPEGV RDYVGAMAVS IHGSRRWAKE WEARNDSYRA LLVSSLADRL VEAFAAIAHD KLRLLWNIPE GSGVRPACGY PSQPDHQEKE TVFTLLHARE EAGMSLTETW MMQPVSSVCA LVFSHPESTY FSVGVTGEDQ QEDYASRKRA SRP // ID B2VBG5_ERWT9 Unreviewed; 300 AA. AC B2VBG5; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 27-MAY-2015, entry version 36. DE SubName: Full=Strain ET1/99 complete chromosome {ECO:0000313|EMBL:CAO97438.1}; GN OrderedLocusNames=ETA_23920 {ECO:0000313|EMBL:CAO97438.1}; OS Erwinia tasmaniensis (strain DSM 17950 / Et1/99). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Erwinia. OX NCBI_TaxID=338565 {ECO:0000313|EMBL:CAO97438.1, ECO:0000313|Proteomes:UP000001726}; RN [1] {ECO:0000313|EMBL:CAO97438.1, ECO:0000313|Proteomes:UP000001726} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17950 / Et1/99 {ECO:0000313|Proteomes:UP000001726}; RX PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x; RA Kube M., Migdoll A.M., Muller 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; CAO97438.1; -; Genomic_DNA. DR RefSeq; YP_001908316.1; NC_010694.1. DR STRING; 465817.ETA_23920; -. DR EnsemblBacteria; CAO97438; CAO97438; ETA_23920. DR KEGG; eta:ETA_23920; -. DR PATRIC; 20430655; VBIErwTas9546_2479. DR HOGENOM; HOG000265278; -. DR OMA; PYVDVWL; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; ETAS465817:GI36-2472-MONOMER; -. DR Proteomes; UP000001726; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001726}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000001726}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 208 208 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 300 AA; 31748 MW; E8FD25718E58D3C0 CRC64; MTQQIKILDG GMGRELARVG APFRQPEWSA LALYEAPQRV REVHDSFISA GADIITTNSY AIVPFHIGEA RFKADAERLS TLAGQLARQA AEAAAHPVQV AGSLPPALGS YRPDLFDARE ALKIYQIQVA ALAPYVDIWL GETISSLAEV QAIHQAVVNQ PHPLWLSFSL HDDPDQTRQN STLRSGESVS DAVALAVEKG AATILFNCSS PEVMLSAVQQ AAATLGRLGS SAGIGVYANA FEQGSNEGGA NEGLSGIRQD THPEGYLGWA QEWVAAGATL IGGCCGIGPE HIQRLASALK // ID B2VXK3_PYRTR Unreviewed; 319 AA. AC B2VXK3; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 07-JAN-2015, entry version 26. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EDU45772.1}; GN ORFNames=PTRG_03249 {ECO:0000313|EMBL:EDU45772.1}; 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 {ECO:0000313|Proteomes:UP000001471}; RN [1] {ECO:0000313|Proteomes:UP000001471} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471}; 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; DS231616; EDU45772.1; -; Genomic_DNA. DR RefSeq; XP_001933582.1; XM_001933547.1. DR EnsemblFungi; EDU45772; EDU45772; PTRG_03249. DR GeneID; 6341476; -. DR InParanoid; B2VXK3; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000001471; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001471}; KW Methyltransferase {ECO:0000313|EMBL:EDU45772.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001471}; KW Transferase {ECO:0000313|EMBL:EDU45772.1}. SQ SEQUENCE 319 AA; 34534 MW; 507B2632F241EF25 CRC64; MTFTAPPNRL SAHIVKGSPL ILDGALATYL ETLGADISGA LWSASILLDQ PSLIKQTHLD YYRANANVAI TASYQASIPG LVKHLQLNEK EAKDVVKKSV ELAQEARDQY ITESTAKVGN QLFIAGSVGP YGAFLADGSE YRGDYSIPKE EMKDFHRGRI QALVEAGVDI LACETIPSKA ETEAIIDLLT TEFASTEAWF GFTLRDSEHI SDGTSLAEIA ALFDNVQQVV ALGFNCVPDD LSVAALKTLK PLVKRGTLVV YPNSGEQWNA QAREWEGKRT EGSSLAEKTR EWRDAGAGLI GGCCRTTPKD IGVMKQALE // ID B2ZZ99_METME Unreviewed; 1265 AA. AC B2ZZ99; DT 22-JUL-2008, integrated into UniProtKB/TrEMBL. DT 22-JUL-2008, sequence version 1. DT 01-APR-2015, entry version 34. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:BAG48547.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:BAG48547.1}; GN Name=metH {ECO:0000313|EMBL:BAG48547.1}; OS Methylophilus methylotrophus (Bacterium W3A1). OC Bacteria; Proteobacteria; Betaproteobacteria; Methylophilales; OC Methylophilaceae; Methylophilus. OX NCBI_TaxID=17 {ECO:0000313|EMBL:BAG48547.1}; RN [1] {ECO:0000313|EMBL:BAG48547.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AS1 {ECO:0000313|EMBL:BAG48547.1}; RA Nishio Y., Usuda Y., Koseki C., Gunji Y., Yasueda H., Sugimoto S.; RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:BAG48547.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AS1 {ECO:0000313|EMBL:BAG48547.1}; RX PubMed=18460806; DOI=10.1271/bbb.70818; RA Ishikawa K., Asahara T., Gunji Y., Yasueda H., Asano K.; RT "Disruption of metF increased L-lysine production by Methylophilus RT methylotrophus from methanol."; RL Biosci. Biotechnol. Biochem. 72:1317-1324(2008). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AB371705; BAG48547.1; -; Genomic_DNA. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAG48547.1}; KW Transferase {ECO:0000313|EMBL:BAG48547.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 260 260 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 325 325 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 326 326 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 793 793 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1265 AA; 139345 MW; 2B78F92CD4DBF87A CRC64; MKRMTQLPVS ATEQWLREAL SQRILILDGA MGTMIQRYKL TEADYRGERF KDFQGPAGER ELFVKGNNEL LTLTQPHVIQ EIHEQYLAAG ADIIETNTFG ATSVAQDDYH MAHLVYEMNV EAAKLAKAAC VKYSTPDKPR FVAGALGPTP KTASISPDVN DPAARNVSFD QLVTSYLEQI RGLVEGGADI LMVETIFDTL NCKAALFAID SFFEEQGKTW PIMISGTVTD ASGRILSGQT VTAFWHSVRH AKPLTVGLNC ALGATLMRPY AEELSKVADT FVCIYPNAGL PNPMSDTGFD ETPDITASLV KEFAQSGFIN IAGGCCGTTP PHINAIYNAI KDLPPRQVPT LPVTTKLSGL EPFVIDEQSL FVNVGERTNV TGSKAFARMI INEQYEEALS VARQQVENGA QVIDINMDEG MLDAVKAMTH FLNLVASEPD IARVPIMIDS SKWSVIEAGL KCVQGKAIVN SISMKEGEAE FLRQAKLCRR YGASVIVMAF DEKGQADTFE RKIEICKRAY DLLVSTGFPP EDIIFDPNIF AIATGIEEHN NYAVDFIEAT RWIKQNLPYA RISGGVSNVS FSFRGNEPAR EAIHTVFLYH AIKAGMTMGI VNAGMVGVYD DIDPELRERV EDVVLNRVVD PANPLAATER MIEIAGTLVA GGKKAEATLA WRGTPENPVP ATKRLEYALV HGITDFIVAD TEEVRQDIMS KGGRPIHVIE GPLMDGMNVV GDLFGQGKMF LPQVVKSARV MKSAVAHLIP FIEEEKAAEE RRTGMVAKPK GKVVIATVKG DVHDIGKNIV SVVLQCNNFE VVNMGVMVPA AEILEMAKRE NADIIGLSGL ITPSLEEMAY IAKEMQRDPH FVENQTPLLI GGATTSRAHT AVKIAPNYEG PVIYVPDASR SVSVMQNLLT PETRGAYLAE IQADYEKARS QHANKKGVPM LSLAEARANA AKFEFTGENT PVKPKFIGRR VFKNIDLALI AQYIDWGPFF QTWDLAGFYP AILKDEVVGE AATKVFAEAQ VMLKRIIDGR WLSANGVIAL LPANRVNEDD IEIYTDDSRS QVALTWYGMR QQTQKPVIDG VARPNQCMAD FIAPKGTDDY IGLFAVTAGL GMEKRLAEFE KNHDDYNAIM FKSLADRLAE AFAEYMHERV RKDLWGYAAD ESLSNEALIK EQYKGIRPAP GYPACPDHTV KSEMFKVLQA SEIEMQLTDS YAMIPAAAVS GFYLAHPESR YFSVDKIGND QLEDMAKRRN VDKAWLERWL APNLG // ID B3CBB4_9BACE Unreviewed; 297 AA. AC B3CBB4; DT 22-JUL-2008, integrated into UniProtKB/TrEMBL. DT 22-JUL-2008, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Homocysteine S-methyltransferase domain protein {ECO:0000313|EMBL:EDV04366.1}; GN ORFNames=BACINT_03501 {ECO:0000313|EMBL:EDV04366.1}; OS Bacteroides intestinalis DSM 17393. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=471870 {ECO:0000313|EMBL:EDV04366.1}; RN [1] {ECO:0000313|EMBL:EDV04366.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17393 {ECO:0000313|EMBL:EDV04366.1}; 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] {ECO:0000313|EMBL:EDV04366.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17393 {ECO:0000313|EMBL:EDV04366.1}; 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 (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. {ECO:0000313|EMBL:EDV04366.1}. 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; ABJL02000008; EDV04366.1; -; Genomic_DNA. DR RefSeq; WP_007665047.1; NZ_ABJL02000008.1. DR EnsemblBacteria; EDV04366; EDV04366; BACINT_03501. DR PATRIC; 27034844; VBIBacInt56937_3318. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDV04366.1}; KW Transferase {ECO:0000313|EMBL:EDV04366.1}. SQ SEQUENCE 297 AA; 32796 MW; 59C944516207AB0B CRC64; MEGALGERLK REYGLTINGS VAMADLIYSQ QGRVALETLW RGYMGIAGKY NLPFLATTPT RRANKQQVIQ AGYDEAIIED NVRFLRKIKE TSNIEMYIGG LMGCKGDAYT GVGALNIEEA YDFHHWQSQL FKLAKADFLY TGIMPVLTEA AGMARAMSDT GIPYIISFTI QKDGKLIDGH TIDYAIRFID DNVSRKPACY MTNCVHPCIV YEALAHNFNQ TDTVRTRFIG IQANTSALSY SELDGSADLQ SSSPADLAEG MMKLKSEYDF RIFGGCCGTD DTHMEEIAKS ISCGALS // ID B3CH02_9BACE Unreviewed; 916 AA. AC B3CH02; DT 22-JUL-2008, integrated into UniProtKB/TrEMBL. DT 22-JUL-2008, sequence version 1. DT 27-MAY-2015, entry version 35. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDV03824.1}; GN ORFNames=BACINT_02950 {ECO:0000313|EMBL:EDV03824.1}; OS Bacteroides intestinalis DSM 17393. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=471870 {ECO:0000313|EMBL:EDV03824.1}; RN [1] {ECO:0000313|EMBL:EDV03824.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17393 {ECO:0000313|EMBL:EDV03824.1}; 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] {ECO:0000313|EMBL:EDV03824.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17393 {ECO:0000313|EMBL:EDV03824.1}; 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 (APR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EDV03824.1}. 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; ABJL02000008; EDV03824.1; -; Genomic_DNA. DR RefSeq; WP_007664140.1; NZ_ABJL02000008.1. DR EnsemblBacteria; EDV03824; EDV03824; BACINT_02950. DR PATRIC; 27033792; VBIBacInt56937_2800. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 241 241 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 916 AA; 100095 MW; 246114BB4EC56B3D CRC64; MVSIEKLVRE RILILDGAMG TMIQRYNLTE EDFRGERFAG IPGQMKGNND LLCLTRPDVI QDIHRKYLMA GADIIETNTF SSTSVSMADY HVQEYVREMN LAAVRLAREV ADEFSTPDKP RFVAGSIGPT NKTCSMSPDV NNPAMRALTY DELADAYREQ MEALLEGGVD ALLIETIFDT LNAKAAIFAA EKAMEATGIQ VPVMLSVTVS DTGGRTLSGQ TLEAFLASVQ HANIFSVGLN CSFGARQLKP FLEQLAARAP YYISAYPNAG LPNSLGQYDQ TPADMAHEVK EYIQEGLINI IGGCCGTTDA YIAEYPALIA GAAPHVPAPK PESLWLSGLE LLEVTPEKNF INVGERCNVA GSRKFLRLVN EKKYDEALSI ARQQVEDGAQ IIDVNMDDGL LDAQAEMTTF LNLIASEPEI ARVPVMIDSS KWDVIVAGLK CLQGKSIVNS ISLKEGEEKF LEHARTIRQY GAATVVMAFD EKGQADTYER KIEVCARAYQ LLVEKVGFNP HDIIFDPNVL AVATGMDEHN NYAVDFIRAT GWIRKNLPGA HVSGGVSNLS FSFRGNNYIR EAMHAVFLYH AIREGMDMGI VNPATAVLYT DIPADILERI EDVVLNRRLD AAERLIETAE QLKAAAEQQK GNATDKQVAP LSWRNGTSVE ERLKHALTKG IGDYLEEDLA EALKLYPKAV DIIEGPLMAG MNYVGELFGA GKMFLPQVVK TARTMKKAVA ILQPVIEAEK QEGSASAGKV LLATVKGDVH DIGKNIVSVV MACNGYEIID LGVMVPAETI VQRALEEKVD MIGLSGLITP SLEEMVHVAM ELEKAGADIP LLIGGATTSR LHTALKIAPV YHAPVVHLKD ASQNATVAAR LMNPKAKEEL KEKLSSEYQQ LREKNAAQAP KTVPLEEAQK NKLNLF // ID B3E428_GEOLS Unreviewed; 1169 AA. AC B3E428; DT 22-JUL-2008, integrated into UniProtKB/TrEMBL. DT 22-JUL-2008, sequence version 1. DT 27-MAY-2015, entry version 56. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACD95849.1}; GN OrderedLocusNames=Glov_2133 {ECO:0000313|EMBL:ACD95849.1}; OS Geobacter lovleyi (strain ATCC BAA-1151 / DSM 17278 / SZ). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=398767 {ECO:0000313|EMBL:ACD95849.1, ECO:0000313|Proteomes:UP000002420}; RN [1] {ECO:0000313|EMBL:ACD95849.1, ECO:0000313|Proteomes:UP000002420} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1151 / DSM 17278 / SZ RC {ECO:0000313|Proteomes:UP000002420}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001089; ACD95849.1; -; Genomic_DNA. DR RefSeq; WP_012470188.1; NC_010814.1. DR RefSeq; YP_001952369.1; NC_010814.1. DR ProteinModelPortal; B3E428; -. DR STRING; 398767.Glov_2133; -. DR EnsemblBacteria; ACD95849; ACD95849; Glov_2133. DR KEGG; glo:Glov_2133; -. DR PATRIC; 21995951; VBIGeoLov31523_2073. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; GLOV398767:GH32-2167-MONOMER; -. DR Proteomes; UP000002420; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002420}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002420}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 231 231 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 730 730 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1169 AA; 126042 MW; 482AB7F84F7010D1 CRC64; MTNNPVLQAL SQCILILDGA MGTQLQARNL TAADFGGEAY EGCNEMLVLT RPDVIEDVHK AYLEAGADIV ETCSFGSTDI VLAEYGLADK VFELNKAAAL VARKACDAYS TPDKPRFVAG SMGPTTRTIS VTGGVTFEQL VTAFRDQTIG LLAGGVDLLL LETAQDTLNL KAGAEGIRLA FEQTGQRVPL MVSGTIEPTG TMLAGQNVEA LYASLTHLEE NLGLISIGLN CATGPEFMTD HLRALSELAT CHISVYPNAG LPDENGNYAE SPDSLAQKLS RFVDEGWLNI IGGCCGTSPA HIAAIANMAA GRQPRKPVTI RRRLVSGIEP LFIEEDNRPI LVGERTNVIG SRKFKNMIVA GQFEEAAEIA RAQVKTGAQV IDICVANPDR DELADMEQML VYLPKKVRAP IMIDSTDAKV TELALQRLQG KCVINSINLE DGEERFAKVA PLLRHYGGAV VVGCIDEDPA NGMAVTRQRK LEVAQRSYDL LVNKYGLRPE DLIFDPLVFP VGSGDDNYIG SAVETIEGVR LITETFPQCS TILGISNVSF GLPAAGREVL NAVFLYHCVK AGLGYAIVNT EKLERYASIP EAERRLAEDL IFWRGADPVA AFAAAFRDKK PVSHAPAAEL PLDERLPLYI IEGSKDGLTA DLDAALTRGD KPLEIINGPL MAGMAEVGRL FNDNQLIVAE VLQSAEAMKA AVSHLEPHLS KDETSSKGKM LLATVKGDVH DIGKNLVEII LSNNGFEVIN LGIKVGPEEL IAAAKKENPD FIGLSGLLVK SALQMIVTAA DLKAAGIDAP LLVGGAALSR AFADTRITPE YNGPVLYAKD AMAGLELANQ LVDPALRQQL MLDLARQQEA SAKIAAAKAA GQSTVATGST HSAISSNAPI LVAPDLEQHI LRDIPVGQII PYLNRQMLYT KHLGLTGSVD KLLAGQDEKA TKLHLTVEAM LERVLQEGLI KPQAIYRFYQ ANGDGNDLIL FNQDGSEATR FTLPRQKSGE QLCVADFVRP LSGTEKDTMA LFAVTCGQGV RELSEQWKAE GDYLNSHLLQ ALALEMAEAT AEYLHKRIRT SWGIVDDQTL TMKQLFNAEY QGIRVSFGYP ACPNLDDQKK LFSLLKPEQI GINLTEGDMM DPEASVSALV FHHPEGKYFD LISANLPLGE VLLPAASLF // ID B3EG82_CHLL2 Unreviewed; 1228 AA. AC B3EG82; DT 22-JUL-2008, integrated into UniProtKB/TrEMBL. DT 22-JUL-2008, sequence version 1. DT 29-APR-2015, entry version 52. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACD91091.1}; GN OrderedLocusNames=Clim_2062 {ECO:0000313|EMBL:ACD91091.1}; OS Chlorobium limicola (strain DSM 245 / NBRC 103803). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Chlorobium. OX NCBI_TaxID=290315 {ECO:0000313|EMBL:ACD91091.1, ECO:0000313|Proteomes:UP000008841}; RN [1] {ECO:0000313|EMBL:ACD91091.1, ECO:0000313|Proteomes:UP000008841} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 245 / NBRC 103803 {ECO:0000313|Proteomes:UP000008841}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001097; ACD91091.1; -; Genomic_DNA. DR RefSeq; WP_012466960.1; NC_010803.1. DR RefSeq; YP_001944070.1; NC_010803.1. DR ProteinModelPortal; B3EG82; -. DR SMR; B3EG82; 648-893. DR STRING; 290315.Clim_2062; -. DR EnsemblBacteria; ACD91091; ACD91091; Clim_2062. DR KEGG; cli:Clim_2062; -. DR PATRIC; 21376393; VBIChlLim118737_2216. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CLIM290315:GHUH-2111-MONOMER; -. DR Proteomes; UP000008841; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008841}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1228 AA; 136097 MW; 13A8B42FFA3DF016 CRC64; MKNTLLQLLE QRILVLDGAM GTMIQRHKLQ EADYRGERFA SHDHPLIGNN DMLVLTQPDI IYAIHCDFLE AGSDIIETNT FNANPISQGD YNAVELVREL NLEAARLARK AADAYSAKTP DKPRFVAGSI GPTNKTLSLS PDVNNPGYRA VTFREVVDNY IVQLEGLMEG GVDLLLIETV FDTLNCKAAL FAVEEYFNAI GRRVPVMVSG TVVDASGRTL SGQTTEAFWI SIAHMPDLIS VGLNCALGSK QMRPFIEALS GIAESYVSVY PNAGLPNEFG EYDDSPAYMA AQIAGFAESG FVNIVGGCCG TTPQHIKAIA DAVSSLKPRR KPEPKHELQL SGLEPLMVNQ TTGFINVGER TNVTGSRKFA RLIKEGNYDE ALSIARQQVE SGAQVIDVNV DEGMLDSEKV MKEFLNLIAS EPEISRVPVM IDSSRWSVIE EGLQCVQGKS IVNSISLKEG EDPFRERALK ILQYGAAAVV MAFDEQGQAD SLERRKEICG RAYDILTREV GFPPEDIIFD PNVLTVATGI DEHNNYALDF IESVRWIREN LPYAKVSGGI SNVSFSFRGN EPVREAMHAA FLYHAIRAGL DMGIVNAGQL AIYEDIEPTL LELVEDVLFN RRPDATERLV SHAETIREGG EKIEAKAAEW RNAPVEERLR HALVKGIVEY IDVDTEEARQ LYPSPLQVIE GPLMDGMNTI GDLFAEGKMF LPQVVKSARV MKRSVAWLIP YIEEEKAQQK NSKPAARVLL ATVKGDVHDI GKNIVSVVLS CNNYEVIDIG VMMPCDRILD AVEREKADIL GLSGLITPSL DEMVHVAREM ERLGMKIPLL IGGATTSKMH TAVKIAPVYS GPVVQVLDAS RSVPVVSSLL NPMLCDDYLA RLKADQATMR QSHESRSREK KYLSIEDARK NRPDLQWDET TVRTPLKTGI TLFEDVTVSA LRPYIDWTPF FLTWELHGRY PEIFGNAKFG SEARQLFDDA NELLDTIDRE KLLGLKGVAG IFPANSSGDD VVIYTDDNRS SALMQVHTLR QQQEKQEGEP NLALADFIAP EESGIRDYIG AFAVTAGLGI EKTLNRFSLE QDDYRRILTQ ALADRLAEAF AEMLHEKVRR ELWGYAPAEI LGSEELLSEK YRGIRPAPGY PACPDHTEKA ELFTLLNAET NTGITLTETY AMNPAASVSG FYFAHPEARY FVLGKIGRDQ VEDYALRKGM SVQETEKWLA PALNYDPE // ID B3EN13_CHLPB Unreviewed; 1227 AA. AC B3EN13; DT 22-JUL-2008, integrated into UniProtKB/TrEMBL. DT 22-JUL-2008, sequence version 1. DT 27-MAY-2015, entry version 54. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACE05002.1}; GN OrderedLocusNames=Cphamn1_2093 {ECO:0000313|EMBL:ACE05002.1}; OS Chlorobium phaeobacteroides (strain BS1). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Chlorobium. OX NCBI_TaxID=331678 {ECO:0000313|EMBL:ACE05002.1, ECO:0000313|Proteomes:UP000001228}; RN [1] {ECO:0000313|EMBL:ACE05002.1, ECO:0000313|Proteomes:UP000001228} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BS1 {ECO:0000313|EMBL:ACE05002.1, RC ECO:0000313|Proteomes:UP000001228}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001101; ACE05002.1; -; Genomic_DNA. DR RefSeq; WP_012475469.1; NC_010831.1. DR RefSeq; YP_001960483.1; NC_010831.1. DR ProteinModelPortal; B3EN13; -. DR SMR; B3EN13; 647-894. DR STRING; 331678.Cphamn1_2093; -. DR EnsemblBacteria; ACE05002; ACE05002; Cphamn1_2093. DR KEGG; cpb:Cphamn1_2093; -. DR PATRIC; 21386596; VBIChlPha121022_2280. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CPHA331678:GHME-2145-MONOMER; -. DR Proteomes; UP000001228; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001228}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001228}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135481 MW; FF7F2F1E351C444E CRC64; MKESLASLLE KRILVLDGAM GTLIQTYKLE ENDYRGERFA SHGHSLKGNN DILVLTQPDI IHAIHCEFLE AGSDIIETNT FNANPVSQSD YGTENLVKHI NLEAARLARK AADAYSLKDP SKPRFVAGSI GPTNKTLSLS PDVNNPGYRA VSFKEMADNY REQLEGLIEG GVDLLLVETV FDTLNCKAAI LAIEEISREK GVRLPIMISG TIVDASGRTL SGQTTEAFWI SVAHTPGLLS VGLNCALGAK QMRPFLEALS HVAGSLVSVY PNAGLPNEFG EYDDSPEYMA SQIADFAQSG FVNIVGGCCG TKPEHIRAIA ETVATIEPRK KPSMPTELRL AGLEPLIVNK TTGFINIGER TNVTGSRKFA RLIREEKYDE ALSIARQQVE NGAQVIDINV DEGMLDSEKV MRDFVNMIGS EPEIARVPLM IDSSKWSVIE SGLCCVQGKS IVNSISLKEG EDLFRERAKK VMIYGAAAVV MAFDEKGQAD SLERRIEICE RAYRILVDEV GFHPENIIFD PNVLTVATGI EEHDNYAVDF IESVRWIKEN LPHARVSGGI SNVSFSFRGN NPVREAMHAA FLFHAIHAGL DMGIVNAGQL AVYDDIEPEL LERVEDVLLN RRKDATERLV EFAETIKDDG QKAEAKQAEW RNGTVEERLQ HALVKGIVDY IDSDTEEARQ AYASPLDIIE GPLMGGMNVI GDLFAEGKMF LPQVVKSARV MKKAVAWLIP YIEEEKAKNK DTRPVAKVLL ATVKGDVHDI GKNIVSVVLA CNNFEVVDIG VMMPCENILE AAEKEKADII GLSGLITPSL DEMVHVAKEM ERKGMRIPLL IGGATTSRVH TAVKIAPNYS GPVVQVLDAS RSVPAVNSLL TSSMKGAFVK KLTEEQHSLR ESHAARQTSR QHRSIGESRE NRAKLSWSPE TVTIPNHPGI TEQANVSLSE LREYIDWTPF FNVWELHGKY PDIFENKHCG SEARKLFEDA NSLLDRICEE KSLVAKGVAG IFPANSVGDD IEIYTDESRA TVLTTLHTLR QQHEKNTGSA NLALADFIAP KSSGRDDYIG AFTLTAGHGV KELMKRFEAE HDDYHRIMVQ ALADRLAEAF AEMLHQRVRK ELWGYAIDEN LTKKQLLNEK YRGIRPAPGY PACPDHTEKP LIFNLLNSEA ITGVTLTETY AMNPPASVCG LYFAHPEAKY FVLGSIGKDQ VEEYALRKGM SMAEAEKWLA PNLNYTP // ID B3H1W4_ACTP7 Unreviewed; 297 AA. AC B3H1W4; DT 22-JUL-2008, integrated into UniProtKB/TrEMBL. DT 22-JUL-2008, sequence version 1. DT 27-MAY-2015, entry version 37. DE SubName: Full=Homocysteine/selenocysteine methylase {ECO:0000313|EMBL:ACE61791.1}; GN OrderedLocusNames=APP7_1139 {ECO:0000313|EMBL:ACE61791.1}; OS Actinobacillus pleuropneumoniae serotype 7 (strain AP76). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=537457 {ECO:0000313|EMBL:ACE61791.1, ECO:0000313|Proteomes:UP000001226}; RN [1] {ECO:0000313|Proteomes:UP000001226} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AP76 {ECO:0000313|Proteomes:UP000001226}; 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 ----------------------------------------------------------------------- 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; ACE61791.1; -; Genomic_DNA. DR RefSeq; WP_005597940.1; NC_010939.1. DR RefSeq; YP_001968933.1; NC_010939.1. DR ProteinModelPortal; B3H1W4; -. DR STRING; 537457.APP7_1139; -. DR EnsemblBacteria; ACE61791; ACE61791; APP7_1139. DR KEGG; apa:APP7_1139; -. DR PATRIC; 20755923; VBIActPle116979_1163. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; PYVDVWL; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; APLE537457:GJI0-1161-MONOMER; -. DR Proteomes; UP000001226; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001226}; KW Methyltransferase {ECO:0000313|EMBL:ACE61791.1}; KW Transferase {ECO:0000313|EMBL:ACE61791.1}. SQ SEQUENCE 297 AA; 32341 MW; E74F7F51335D3F4A CRC64; MTITILDGGM SRELMRLNAP FKQPEWSALS LYEKPSAVQQ VHEDFIANGA EVITTNSYAV VPFHIGEQRF SADGKMLADL AGRLAKQAVK NSGKSAKIAG SLPPMFGSYR ADLIQADRFA EIAQPIIDGL APYVDIWLCE TQSAIIEPTS IKPLLPKDDR PLWVSFTLTD DEPTPEPQLR SGEPVALAIE KMVELGVDAI LFNCCQPEVI EQALAITQSI LKEKNVTHIQ TGAYANAFAP QPKDATANDG LDEVRKDLDP EAYLAWAQKW TAQGATIIGG CCGIGIEYIN TLAKNLK // ID B3JGL1_9BACE Unreviewed; 914 AA. AC B3JGL1; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 27-MAY-2015, entry version 33. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EDV01913.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EDV01913.1}; GN Name=metH {ECO:0000313|EMBL:EDV01913.1}; GN ORFNames=BACCOP_01013 {ECO:0000313|EMBL:EDV01913.1}; OS Bacteroides coprocola DSM 17136. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=470145 {ECO:0000313|EMBL:EDV01913.1}; RN [1] {ECO:0000313|EMBL:EDV01913.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17136 {ECO:0000313|EMBL:EDV01913.1}; 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] {ECO:0000313|EMBL:EDV01913.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17136 {ECO:0000313|EMBL:EDV01913.1}; 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 (APR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EDV01913.1}. 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; ABIY02000067; EDV01913.1; -; Genomic_DNA. DR RefSeq; WP_007568733.1; NZ_DS981479.1. DR EnsemblBacteria; EDV01913; EDV01913; BACCOP_01013. DR PATRIC; 26983133; VBIBacCop77500_1957. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EDV01913.1}; KW Transferase {ECO:0000313|EMBL:EDV01913.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 240 240 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 757 757 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 914 AA; 100891 MW; 79641598553251DD CRC64; MQQLINERIL VLDGAMGTMI QQYNLSEADF RGERFKDLPG LLKGNNDMLC LTRPDVIEEI HRKYLEAGAD IIETNTFNAT AVSMADYHMQ AYCREINLAA ARLARKIADE YTARTPEKPR FVAGSVGPTN KTCSMSPDVN NPAFRALTFD ELSEAYREQM EALLEGGVDA ILIETIFDTL NAKAAVLAAE TAMQNLGRKV PLMLSVTVSD VAGRTLSGQT LDAFLASVQH ADIFSIGLNC SFGARQLKPF LEQLARRAPY YISAYPNAGL PNSLGQYDQT PEEMAAEVKE YIDEGLVNII GGCCGTTEAY IAKYQELIKD AKPHAPAPKP DYLWLSGLEL LEVTPEINFV NVGERCNVAG SRKFLRLINE KKYDEALSIA RKQVEDGALV IDVNMDDGLL DAAEEMTTFL NLVASEPDIA RVPVMIDSSK WEVILAGLKC VQGKCIVNSI SLKEGEEAFV EHARTVKQYG AAVIVMAFDE KGQADTFERK IEVCERAYRI LTEKVGFRPQ DIIFDPNVLA VATGIEEHNN YAVDFIKATG WIRRHLPGAH VSGGVSNLSF SFRGNNYIRE AMHAVFLYHA IQQGMDMGIV NPGTSVLYTD IPSDILERIE DVVLNRRPDA AERLIETAEK LKAEKENSGE QQTASSHLAW REGTTVEERL QYALVKGLGD YLDEDLHEAL AKYPDAVSII EGPLMSGMNH VGDLFGSGKM FLPQVVKTAR TMKKAVAILQ PYIETEKKEG ARSAGKVLLA TVKGDVHDIG KNIVSVVMAC NNYEIIDLGV MVPAEKIVET AIREKVDIIG LSGLITPSLE EMVHVVSELE RAGLDIPVMI GGATTSKLHT ALKIAPVYHA PVVYMKDASL NAPVAARLMN LDFRSTFAEE LESEYRELRE KNKTKQVKTV SLEEAQKNKL NLWE // ID B3LCY0_PLAKH Unreviewed; 512 AA. AC B3LCY0; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 27-MAY-2015, entry version 32. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CAQ42289.1}; GN ORFNames=PKH_145080 {ECO:0000313|EMBL:CAQ42289.1}; OS Plasmodium knowlesi (strain H). OC Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium). OX NCBI_TaxID=5851 {ECO:0000313|EMBL:CAQ42289.1, ECO:0000313|Proteomes:UP000000622}; RN [1] {ECO:0000313|Proteomes:UP000000622} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H {ECO:0000313|Proteomes:UP000000622}; 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; AM910996; CAQ42289.1; -; Genomic_DNA. DR RefSeq; XP_002262411.1; XM_002262375.1. DR EnsemblProtists; PKH_145080; PKH_145080; PKH_145080. DR GeneID; 7323198; -. DR KEGG; pkn:PKH_145080; -. DR EuPathDB; PlasmoDB:PKH_145080; -. DR HOGENOM; HOG000283439; -. DR InParanoid; B3LCY0; -. DR Proteomes; UP000031513; Chromosome 14. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 4. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 4. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000031513}; KW Reference proteome {ECO:0000313|Proteomes:UP000031513}. SQ SEQUENCE 512 AA; 58825 MW; 821796DB56127E07 CRC64; MAKEVFTLDG GKISEFERLG LGNFDFLSYP QECNKEEMVS TLESIHLSYL LAGCNVISTN TFQVNLHSLQ EKGISIEEGQ GIIDTYIDIA HNALLKYERI KRTTDFPLHL GMTQVEEKES SPYDHLEKFQ KMRIHWGILH PNDSVDTREY VDRFDLNDDV WTGNPIRRCQ DYYVAFSTGG YSSAFRDFSE YSGVLRKERK ATNWGDGGGV VQPDKAVVGC RSQNQSYDII IKTPPEVEGS LMHRQNQLPD IEMVPLSSTQ RSATSTEDFP NKHFFNYGLE YYIDVRDEEI ISNSKFRIDS YKRNEHKLQL FSVITSSNVR EVFTLYHHLK TCGGGFEKNV VVSFYCNSNK NIGCTDYSFL DMVLTLLYLD SRNHFIKAIG VNCVNIDYVR ELILPLTRCI KPDGNIDVNA YPCPNGELGR LIKTVLKDLK KNTYLGDIHF FASPNKSLNR VTYDHSRNDI QFDISQKRHK HLYNYVGDWI DVGLTGFGGC CYYNPYDISL LDYKLGRMAQ MQ // ID B3LKG0_YEAS1 Unreviewed; 325 AA. AC B3LKG0; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 07-JAN-2015, entry version 26. DE SubName: Full=AdoMet-homocysteine methyltransferase {ECO:0000313|EMBL:EDV10958.1}; DE SubName: Full=Homocysteine S-methyltransferase 2 {ECO:0000313|EMBL:EDV11812.1}; GN ORFNames=SCRG_02218 {ECO:0000313|EMBL:EDV11812.1}, GN SCRG_02228 {ECO:0000313|EMBL:EDV10958.1}; OS Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=285006 {ECO:0000313|EMBL:EDV10958.1, ECO:0000313|Proteomes:UP000008335}; RN [1] {ECO:0000313|Proteomes:UP000008335} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RM11-1a {ECO:0000313|Proteomes:UP000008335}; 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; EDV10958.1; -; Genomic_DNA. DR EMBL; CH408047; EDV11812.1; -; Genomic_DNA. DR ProteinModelPortal; B3LKG0; -. DR SMR; B3LKG0; 15-315. DR OrthoDB; EOG7X9GHR; -. DR Proteomes; UP000008335; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008335}; KW Methyltransferase {ECO:0000313|EMBL:EDV10958.1}; KW Transferase {ECO:0000313|EMBL:EDV10958.1}. SQ SEQUENCE 325 AA; 36669 MW; 54658C7B92A610F0 CRC64; MARLPLKQFL ADNPKKVLVL DGGQGTELEN RGIKVANPVW STIPFISESF WSDESSANRK IVKEMFNDFL NAGAEILMTT TYQTSYKSVS ENTPIRTLSE YNNLLNRIVD FSRNCIGEDK YLIGCIGPWG AHICREFTGD YGAEPENIDF YQYFKPQLEN FNKNDKLDLI GFETIPNIHE LKAILSWDES ILSRPFYIGL SVHEHGVLRD GTTMEEIAQV IKDLGDKINP NFSFLGINCV SFNQSPDILE SLHQALPNMA LLAYPNSGEV YDTEKKIWLP NSDKLNSWDT VVKQYISSGA RIIGGCCRTS PKDIQEISAA VKKYT // ID B3LTB7_YEAS1 Unreviewed; 324 AA. AC B3LTB7; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 07-JAN-2015, entry version 24. DE SubName: Full=S-Methylmethionine Homocysteine methylTransferase {ECO:0000313|EMBL:EDV09260.1}; GN ORFNames=SCRG_04932 {ECO:0000313|EMBL:EDV09260.1}; OS Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=285006 {ECO:0000313|EMBL:EDV09260.1, ECO:0000313|Proteomes:UP000008335}; RN [1] {ECO:0000313|Proteomes:UP000008335} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RM11-1a {ECO:0000313|Proteomes:UP000008335}; 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; CH408054; EDV09260.1; -; Genomic_DNA. DR ProteinModelPortal; B3LTB7; -. DR SMR; B3LTB7; 3-313. DR OrthoDB; EOG7X9GHR; -. DR Proteomes; UP000008335; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008335}; KW Methyltransferase {ECO:0000313|EMBL:EDV09260.1}; KW Transferase {ECO:0000313|EMBL:EDV09260.1}. SQ SEQUENCE 324 AA; 36715 MW; A77194694B6E5C14 CRC64; MKRIPIKELI VEHPGKVLIL DGGQGTELEN RGININSPVW SAAPFTSESF WEPSSQERKV VEEMYRDFMI AGANILMTIT YQANFQSISE NTSIKTLAAY KRFLDKIVSF TREFIGEERY LIGSIGPWAA HVSCEYTGDY GPHPENIDYY GFFKPQLENF NQNRDIDLIG FETIPNFHEL KAILSWDEDI ISKPFYIGLS VDDNSLLRDG TTLEEISVHI KGLGNKINKN LLLMGVNCVS FNQSALILKM LHEHLPGMPL LVYPNSGEIY NPKEKTWHRP TNKLDDWETT VKKFVDNGAR IIGGCCRTSP KDIAEIASAV DKYS // ID B3MPE3_DROAN Unreviewed; 331 AA. AC B3MPE3; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 07-JAN-2015, entry version 36. DE SubName: Full=GF14647 {ECO:0000313|EMBL:EDV31239.1}; GN Name=Dana\GF14647 {ECO:0000313|EMBL:EDV31239.1}; GN ORFNames=Dana_GF14647 {ECO:0000313|EMBL:EDV31239.1}, GN GF14647 {ECO:0000313|FlyBase:FBgn0091674}; OS Drosophila ananassae (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7217 {ECO:0000313|Proteomes:UP000007801}; RN [1] {ECO:0000313|EMBL:EDV31239.1, ECO:0000313|Proteomes:UP000007801} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tucson 14024-0371.13 {ECO:0000313|Proteomes:UP000007801}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 genomes consortium; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(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; CH902620; EDV31239.1; -; Genomic_DNA. DR RefSeq; XP_001962018.1; XM_001961982.1. DR STRING; 7217.FBpp0117839; -. DR EnsemblMetazoa; FBtr0119347; FBpp0117839; FBgn0091674. DR GeneID; 6497469; -. DR KEGG; dan:Dana_GF14647; -. DR FlyBase; FBgn0091674; Dana\GF14647. DR eggNOG; COG2040; -. DR InParanoid; B3MPE3; -. DR KO; K00547; -. DR OrthoDB; EOG7GQXW0; -. DR PhylomeDB; B3MPE3; -. DR Proteomes; UP000007801; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007801}; KW Reference proteome {ECO:0000313|Proteomes:UP000007801}. SQ SEQUENCE 331 AA; 36736 MW; 6168EB5E363C6B8C CRC64; MGLTRVLVKD GGFGTQMTVH VGNSVDGDPL WSSRFNATNP SAIISTHLDF LQNGADIILT NTYQSSVEGY MEYLELDEEQ SIELIRNTVR LAHIAKERYL SECYQAQLSV PEGYPLIIAS IGPFGAHLHD GSEYTGSYAD YVPAKEITDW HRVRIEACLE AGVDALAIET IPCQMEAEAL VEMLCDDYPD VKFWVAFQCK DESTLAHGET FADAATAIWD LLAERNAQDK CLAVGVNCVH PKFVTPLFKS LNGERGADEQ IPLVVYPNSG ETYDVDNGWQ GREHCVPLAN YVPEWAQLGA KVIGGCCRTY ARDIRHIGEA IRDWNKLKKL S // ID B3MPE4_DROAN Unreviewed; 329 AA. AC B3MPE4; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 07-JAN-2015, entry version 36. DE SubName: Full=GF14646 {ECO:0000313|EMBL:EDV31240.1}; GN Name=Dana\GF14646 {ECO:0000313|EMBL:EDV31240.1}; GN ORFNames=Dana_GF14646 {ECO:0000313|EMBL:EDV31240.1}, GN GF14646 {ECO:0000313|FlyBase:FBgn0091673}; OS Drosophila ananassae (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7217 {ECO:0000313|Proteomes:UP000007801}; RN [1] {ECO:0000313|EMBL:EDV31240.1, ECO:0000313|Proteomes:UP000007801} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tucson 14024-0371.13 {ECO:0000313|Proteomes:UP000007801}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 genomes consortium; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(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; CH902620; EDV31240.1; -; Genomic_DNA. DR RefSeq; XP_001962019.1; XM_001961983.1. DR STRING; 7217.FBpp0117838; -. DR EnsemblMetazoa; FBtr0119346; FBpp0117838; FBgn0091673. DR GeneID; 6497468; -. DR KEGG; dan:Dana_GF14646; -. DR FlyBase; FBgn0091673; Dana\GF14646. DR eggNOG; COG2040; -. DR InParanoid; B3MPE4; -. DR KO; K00547; -. DR OrthoDB; EOG7GQXW0; -. DR PhylomeDB; B3MPE4; -. DR Proteomes; UP000007801; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007801}; KW Reference proteome {ECO:0000313|Proteomes:UP000007801}. SQ SEQUENCE 329 AA; 36168 MW; 8757FC98B70C0067 CRC64; MEVSNRFRSP KPILVKCGGF SSQLAKNVTE KVDGDPLWGS RFDATNPEAV IKTHLDFLHS GADIILTNTY QSSVDGFVKY LGVSKERGKE LIRKSVQLAQ EAKAQYLKET ASDSTLPLIL ASIGPYGACL HDGSEYSGSY ADKITKKQLQ EWHRTRIEIC LAEGVNGLAL ETLPCQLEAE AVTELVLDSY EGVNFWVSFQ CQDNARLASG ESYAQAALSI WRLVQQRQAQ HRLLGIGVNC VNPQFVTPLL TSFLKAAGSN EKIPLVVYSN RGEIYDAEQG EWTGTGEQVV KFVPEWIQLG AGIVGGCCRV YPSDVLEIRQ YVDGLSIDA // ID B3NL77_DROER Unreviewed; 331 AA. AC B3NL77; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 07-JAN-2015, entry version 34. DE SubName: Full=GG21670 {ECO:0000313|EMBL:EDV54727.1}; GN Name=Dere\GG21670 {ECO:0000313|EMBL:EDV54727.1}; GN ORFNames=Dere_GG21670 {ECO:0000313|EMBL:EDV54727.1}, GN GG21670 {ECO:0000313|FlyBase:FBgn0113848}; OS Drosophila erecta (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7220 {ECO:0000313|Proteomes:UP000008711}; RN [1] {ECO:0000313|EMBL:EDV54727.1, ECO:0000313|Proteomes:UP000008711} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tucson 14021-0224.01 {ECO:0000313|Proteomes:UP000008711}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 genomes consortium; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(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; CH954179; EDV54727.1; -; Genomic_DNA. DR RefSeq; XP_001974327.1; XM_001974291.1. DR EnsemblMetazoa; FBtr0141724; FBpp0140216; FBgn0113848. DR GeneID; 6549347; -. DR KEGG; der:Dere_GG21670; -. DR FlyBase; FBgn0113848; Dere\GG21670. DR KO; K00547; -. DR OrthoDB; EOG7GQXW0; -. DR PhylomeDB; B3NL77; -. DR Proteomes; UP000008711; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008711}. SQ SEQUENCE 331 AA; 36793 MW; E53AFB53AA39FC32 CRC64; MNDSEKWNWD TKRILVKCGG FSSQLARNVS EKVDGDPLWG SRFDATNPEA VIQTHLDFLR NGADIILTNT YQSSVEGFMK YLGVTRERGV ELIQKSVQLA RQAKEQYLSE IGSELESALP LILGSIGPYG AYLHDGSEYS GNYVENISKE QLKAWHRTRI EICLAAGVDG LALETLPCQL EAEAVTELVL DNFPDAKFWV SMQCRDEKHL ASGETFAEAA LSVWRLVQSR KAENRLLGIG LNCVNPLFVT PLLSSLTKVA GSDRIPLVVY SNRGEIYDTE QGEWTGTGEE VVKFVPEWLQ LGVRIVGGCC RVYPTDVLAI RTYVDGLNIK P // ID B3NL78_DROER Unreviewed; 331 AA. AC B3NL78; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 07-JAN-2015, entry version 34. DE SubName: Full=GG21671 {ECO:0000313|EMBL:EDV54728.1}; GN Name=Dere\GG21671 {ECO:0000313|EMBL:EDV54728.1}; GN ORFNames=Dere_GG21671 {ECO:0000313|EMBL:EDV54728.1}, GN GG21671 {ECO:0000313|FlyBase:FBgn0113849}; OS Drosophila erecta (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7220 {ECO:0000313|Proteomes:UP000008711}; RN [1] {ECO:0000313|EMBL:EDV54728.1, ECO:0000313|Proteomes:UP000008711} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tucson 14021-0224.01 {ECO:0000313|Proteomes:UP000008711}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 genomes consortium; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(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; CH954179; EDV54728.1; -; Genomic_DNA. DR RefSeq; XP_001974328.1; XM_001974292.1. DR EnsemblMetazoa; FBtr0141725; FBpp0140217; FBgn0113849. DR GeneID; 6549323; -. DR KEGG; der:Dere_GG21671; -. DR FlyBase; FBgn0113849; Dere\GG21671. DR KO; K00547; -. DR OrthoDB; EOG7GQXW0; -. DR PhylomeDB; B3NL78; -. DR Proteomes; UP000008711; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008711}. SQ SEQUENCE 331 AA; 36750 MW; B2E90D0DD3AE3D57 CRC64; MGLTRVLLKD GGFGTQMTVH VGNSVDGDPL WSSRFNATNP AAIISTHLDF LQNGADIILT NTYQSSLEGY MEYLELDEEQ SIELIKNTVR LAHIAKERYL TECYQAQLTV PEGYPLIIAS IGPYGAHLHD GSEYTGSYAD YVPAKEITDW HRVRIEACLE AGVDALAIET IPCQMEAEAL VEMLCDDYPD VKFWVAFQCN GENTLAHGET FADATNAIWD LLAERNAQDK CLAIGVNCVN PKFVTPLFKS LNGDREVAEQ IPLVVYPNSG EVYDVVNGWQ GKEHCVPLAN YVPEWAQLGA KVIGGCCRTY ARDIRHIGEA IRDWNKLKKL S // ID B3PL28_CELJU Unreviewed; 1247 AA. AC B3PL28; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 27-MAY-2015, entry version 52. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACE84914.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ACE84914.1}; GN Name=metH {ECO:0000313|EMBL:ACE84914.1}; GN OrderedLocusNames=CJA_2542 {ECO:0000313|EMBL:ACE84914.1}; OS Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. OS cellulosa). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Cellvibrio. OX NCBI_TaxID=498211 {ECO:0000313|EMBL:ACE84914.1, ECO:0000313|Proteomes:UP000001036}; RN [1] {ECO:0000313|EMBL:ACE84914.1, ECO:0000313|Proteomes:UP000001036} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ueda107 {ECO:0000313|EMBL:ACE84914.1, RC ECO:0000313|Proteomes:UP000001036}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000934; ACE84914.1; -; Genomic_DNA. DR RefSeq; WP_012488138.1; NC_010995.1. DR RefSeq; YP_001983002.1; NC_010995.1. DR STRING; 498211.CJA_2542; -. DR EnsemblBacteria; ACE84914; ACE84914; CJA_2542. DR KEGG; cja:CJA_2542; -. DR PATRIC; 21328462; VBICelJap122165_2499. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CJAP498211:GHIT-2533-MONOMER; -. DR Proteomes; UP000001036; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001036}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACE84914.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001036}; KW Transferase {ECO:0000313|EMBL:ACE84914.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 260 260 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 772 772 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1247 AA; 137679 MW; 10D21E68A2EA6D48 CRC64; MTVPAALHAR PAALETRISA LYQAIRERIL ILDGGMGTMI QSYKLKEADY RGARFADYHM DIAGNNDLLS ITKPEVIRDI QRAYLDAGAD ILETNTFNAT RISMADYDME DLVPELNYAA ARLARELCDE FTAANPAKPR FVAGVLGPTS RTCSISPDVN DPGARNVTFD QLVENYVEAT DSLVKGGADI ILIETVFDTL NAKAAVFAVQ QYFDQAGFEL PIMISGTITD ASGRTLSGQT TEAFYNSLAH ARPLSMGLNC ALGAKELRQY VQELSRVANC FVSAHPNAGL PNEFGEYDQT AQEMVEIVEE FAASGFLNII GGCCGTTPAH IKAIADAMAK YPPRPLPAIE PACRLSGLEP FNITRDSLFV NVGERCNVTG SARFKRLIVE EDYTTALEVA LEQVENGAQV IDINMDEGML DAEKAMVRFL NLIAGEPDIA RVPIMVDSSK WEVIEAGLKC IQGKPIVNSI SLKEGEEEFL HKAKLCMRYG AAVVVMAFDE TGQADTMARK MEICARSYRT LVDKLDFPPE DIIFDPNIFA VATGIEEHNN YAVDFIEATR WIRTHLPHAG VSGGVSNVSF SFRGNNPVRE AIHSVFLYHA IKAGMNMGIV NAGQLALYDD LPQELKDKVE DVILNRHSGA TEALLDIAEK YRGDGNTGDK KEDLEWRSLP IAKRIEHALV KGISTYIEAD TEEARQHYPR PLDVIEGPLM DGMNVVGDLF GAGKMFLPQV VKSARVMKQS VAYLQPYIEA EKTEASKPNG KILMATVKGD VHDIGKNIVG VVLQCNNFEV VDLGVMVPCD KILDTAISQN CDIIGLSGLI TPSLDEMVFV AREMERRGIN KPLLIGGATT SKAHTAVKID PVFHLNQVVY VPDASRAVGI ASTLLSDELR PKFVDDVKQE YVQVRERNAN RKPRGTVRTY PEAIAKGLKL DWENYIPPTP AFTGVKVFED YDLNILVDFI DWTPFFISWD LAGKFPRILN DEIVGEAARA LWADAQAMLR KLIDEKLIKA NGVIGFWPAN TVNTDDIAVF DSAGKQLSIL HHIRQQHLKQ GNESKPHMSL ADFVAPKESG KQDYIGGFAV TTGIGAEELA KEYQNKGDDY NSIMVKALAD RLAEAFAEHM HQRVRREFWG YDRDENLDNE ALIKEQYRGI RPAPGYPACP DHTEKASLFK LLDAEQNTGI TLTEHFAMLP TAAVSGWYFS HPESVYFNTD KIEKDQVESL AQRKGVSVAE VERWLSPVLA YEPGTAE // ID B3PUC4_RHIE6 Unreviewed; 1264 AA. AC B3PUC4; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 01-APR-2015, entry version 51. DE SubName: Full=5-methyltetrahydrofolate--homocysteine S-methyltransferase protein {ECO:0000313|EMBL:ACE92005.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ACE92005.1}; GN Name=metH {ECO:0000313|EMBL:ACE92005.1}; GN OrderedLocusNames=RHECIAT_CH0003056 {ECO:0000313|EMBL:ACE92005.1}; OS Rhizobium etli (strain CIAT 652). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=491916 {ECO:0000313|EMBL:ACE92005.1, ECO:0000313|Proteomes:UP000008817}; RN [1] {ECO:0000313|EMBL:ACE92005.1, ECO:0000313|Proteomes:UP000008817} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIAT 652 {ECO:0000313|EMBL:ACE92005.1, RC ECO:0000313|Proteomes:UP000008817}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001074; ACE92005.1; -; Genomic_DNA. DR RefSeq; WP_012484550.1; NC_010994.1. DR RefSeq; YP_001979183.1; NC_010994.1. DR STRING; 491916.RHECIAT_CH0003056; -. DR EnsemblBacteria; ACE92005; ACE92005; RHECIAT_CH0003056. DR KEGG; rec:RHECIAT_CH0003056; -. DR PATRIC; 23099605; VBIRhiEtl120572_3035. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; RETL491916:GH4T-3055-MONOMER; -. DR Proteomes; UP000008817; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008817}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACE92005.1}; KW Transferase {ECO:0000313|EMBL:ACE92005.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 267 267 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 330 330 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 331 331 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 783 783 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1264 AA; 139500 MW; 2F5FAC586BA9C795 CRC64; MTSRSPPVFD TLFGPETGKR DGSEVFAALR KAASERILVL DGAMGTQIQG LGYDEDQFRG TRFIGCACHQ KGNNDLLILT QPDAIEEIHY KYAKAGADIL ETNTFSSTRI AQADYQMEGE VYALNKEGAE IVRRAAIRAE REDGRRRFVA GAIGPTNRTA SISPDVNNPG FRAVTFDDLR SAYGEQIDGL IDGGADIILI ETIFDTLNAK AAIFACEERF EAKGVRLPVM ISGTITDLSG RTLSGQTPSA FWNSVRHANP FTIGLNCALG ANAMRPHLQE LSGAADTFIC AYPNAGLPNE FGQYDETPEL MAAQIDSFAR EGLVNIVGGC CGSTPEHIRA IAETVAKYKP RSIPEHRPFM SLSGLEPFEL TKDIPFVNVG ERTNVTGSAK FRKLITNADY TAALDVARDQ VENGAQVIDI NMDEGLIDSE KAMVEFLNLI AAEPDIARVP VMIDSSKFSI IESGLKRVQG KPIVNSISLK EGEENFLAQA RLLRNYGAAV VVMAFDETGQ ADNYDRKVEI CTRAYKLLTE KIGFPPEDII FDPNIFAVAT GIEEHNNYGV DFIEATRTIR ERMPLVHISG GVSNLSFSFR GNEPVREAMH AVFLYHAIQA GMDMGIVNAG QLAVYDNIDP ELREACEDVV LNRRPDSTER LLEVAERFRG AGAKEGRIQD LSWREWSVEK RLEHALVNGI TEYIEADTEE ARQQAARPLH VIEGPLMAGM NVVGDLFGSG KMFLPQVVKS ARVMKQAVAV LLPYMEEEKR LTGGDDRQSA GKILMATVKG DVHDIGKNIV GVVLACNNYE IVDLGVMVPA TKILETAIAE KVDVIGLSGL ITPSLDEMVH VAAEMERQGF EIPLLIGGAT TSRVHTAVKI HPGYNKGQAI YVTDASRAVG VVSALLSPET RQGYVDDVRA EYAKVAAAHA RSEAEKVRLP LPRARENAHK VDWSAYQPTK PQFFGTRVFE DYDLAELARY IDWTPFFQTW ELRGRYPAIL EDEKQGEAAR ALWADAQAML KKIIDEKWFR PRAVIGFWPA GAVGDDIRLF TDESRSHELA TFYTLRQQLS KRDGRANVAL SDFVAPVASG VQDYVGGFVV TAGIEEVAIA ERFERANDDY SSILVKALAD RFAEAFAERM HEQVRREYWG YARDEHLSNE DLIGEAYAGI RPAPGYPAQP DHTEKKTLFK LLDAEHTAGV KLTESYAMWP GSSVSGLYIG HPDSYYFGVA KVERDQVEDY AKRKGMEISE VERWLGPVLN YVPRKADDEI EDAA // ID B3QGP3_RHOPT Unreviewed; 1293 AA. AC B3QGP3; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 01-APR-2015, entry version 49. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACF02720.1}; GN OrderedLocusNames=Rpal_4224 {ECO:0000313|EMBL:ACF02720.1}; OS Rhodopseudomonas palustris (strain TIE-1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Rhodopseudomonas. OX NCBI_TaxID=395960 {ECO:0000313|EMBL:ACF02720.1, ECO:0000313|Proteomes:UP000001725}; RN [1] {ECO:0000313|EMBL:ACF02720.1, ECO:0000313|Proteomes:UP000001725} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TIE-1 {ECO:0000313|EMBL:ACF02720.1, RC ECO:0000313|Proteomes:UP000001725}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001096; ACF02720.1; -; Genomic_DNA. DR RefSeq; WP_012497105.1; NC_011004.1. DR RefSeq; YP_001993195.1; NC_011004.1. DR ProteinModelPortal; B3QGP3; -. DR SMR; B3QGP3; 655-1238. DR STRING; 395960.Rpal_4224; -. DR EnsemblBacteria; ACF02720; ACF02720; Rpal_4224. DR KEGG; rpt:Rpal_4224; -. DR PATRIC; 23312955; VBIRhoPal88240_4268. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; RPAL395960:GHPC-4267-MONOMER; -. DR Proteomes; UP000001725; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001725}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 770 770 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1293 AA; 140172 MW; B9FD41752215D72E CRC64; MTKPISAKRT QLLALAAQRI LVLDGAMGTM IQQLQLDEAA FRGERFKDFH RDLRGNNDLL ILTQPQAIED IHAQYLRAGA DIVATNTFSS TSIAQADYDM SELAYEMSRD GARLARNAAA KVEAEDGKPR FVAGAIGPTN RTASISPDVA NPGYRAVTFD DLRIAYSEQI NGLLDGGADI LLLETIFDTL NAKAALYAIA EITEARGIDV PVMISGTITD KSGRLLSGQM PEAFWNSVRH ARPITIGFNC ALGAKDLRAH IADISRVADT LVCAYPNAGL PNEFGQYDES PEYMASLVGE FAEAGLVNIV GGCCGTTPAH IKAIAEAVAP HKPRVIPTIE PRLRLSGLEP FELTKDIPFV NVGERTNVTG SAKFRKLITA GDYAAALQVA RDQVDNGAQI IDVNMDEGLL DSEAAMVTFL NLVAAEPDIA KVPVMVDSSK FNVIEAGLKC LQGKPVVNSI SLKEGEDKFL HEARIARRHG AAVVVMAFDE TGQADTYARK TEICARAYDI LVNRVGFPPE DIIFDPNIFA IATGLEEHNN YGVDFIEATR WIRSSLPHAH ISGGVSNLSF SFRGNEPVRE AMHSVFLYHA IKAGMDMGIV NAGQMIVYDD IDPELRQVCE DVILNRDPGA SERLLALADK YRGQGKQQKE QDLAWRSWPV EQRLSHALVH GITEFIELDT EEARAKAERP LHVIEGPLMA GMNVVGDLFG DGKMFLPQVV KSARVMKQAV AYLMPFMEEE KARNLAAGTD TGERATAGKI VLATVKGDVH DIGKNIVGIV LQCNNFEVID LGVMVPAAKI IETAKAENAD IIGLSGLITP SLDEMSFLAG ELQRSGFNIP LLIGGATTSR VHTAVKIDPA YPSGSVVYVN DASRAVGVAS SLLSKDRGAA YATEVRADYA KISAAHHRAQ ADKKRLTLSA ARANSTKIDW TATRPVKPSF IGTRSFSGYS LAELAEYIDW TPFFQAWELA GRFPAILDDS VVGEAARSLY ADARKMLDRI VTENWFTAKA TIGFWPANAD GDDILVYADE TRTTPIATLH TLRQQLDKRE GRANAALSDF IAPVASGVAD YIGGFVVTAG IGEDVIADKF KAERDDYSSI MVKALADRLA EAFAERMHAR VRREFWGYAA DENLSAEDLI LEKYQGIRPA PGYPAQPDHT EKATLFELLD AEASASVTLT ESFAMWPGSS VSGLYFSHPQ SAYFGVGKIE RDQVEDYAAR KGWDVATAER WLAPVLNYIP SRSTGATDET GMPPLAPQAA APLSAEDAAL ASHPQGCTCA LHLAWRKQKV AAK // ID B3QKY2_CHLP8 Unreviewed; 1227 AA. AC B3QKY2; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 27-MAY-2015, entry version 50. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACF10770.1}; GN OrderedLocusNames=Cpar_0346 {ECO:0000313|EMBL:ACF10770.1}; 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 {ECO:0000313|EMBL:ACF10770.1, ECO:0000313|Proteomes:UP000008811}; RN [1] {ECO:0000313|EMBL:ACF10770.1, ECO:0000313|Proteomes:UP000008811} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCIB 8327 {ECO:0000313|EMBL:ACF10770.1, RC ECO:0000313|Proteomes:UP000008811}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001099; ACF10770.1; -; Genomic_DNA. DR RefSeq; WP_012501603.1; NC_011027.1. DR RefSeq; YP_001997970.1; NC_011027.1. DR STRING; 517417.Cpar_0346; -. DR EnsemblBacteria; ACF10770; ACF10770; Cpar_0346. DR KEGG; cpc:Cpar_0346; -. DR PATRIC; 21363912; VBIChlPar72705_0340. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CPAR517417:GH95-360-MONOMER; -. DR Proteomes; UP000008811; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008811}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 134312 MW; 4E0F3C2F8C9C3800 CRC64; MNDNLYGLIE QRILVLDGAM GTMIQRHGLD EQDYRGERFA SHSHPLKGNN DLLVITQPDI IRSIHCDFLD AGADIVETCT FNANPISQSD YQLQHLTKEL NVAAAKVARS AADEFTAKTP DKPRFVAGSI GPTNKTLSLS PDVNNPGFRA VTFQEVVDNY TAQLEGLHEG GVDLLLVETV FDTLNCKAAL YAIEQYAAKT GWQVPVMVSG TVVDASGRTL SGQTTEAFWI SISHMPSLLS VGLNCALGSK QMRPFIEALS NIAGSYVSVY PNAGLPNEFG EYDDSPEYMA AQIAGFAESG FVNIVGGCCG TTPTHIRAIA EAVKTLTPRK RPANEHVLKL SGLEPLVVDE TTGFINVGER TNVTGSRKFA RLIKEANYDE ALSIARQQVE NGAQVIDVNL DEGMLDSEKV IVEFLNLIAS EPEIAKVPVM IDSSKWAVIE NGLRCTQGKS IVNSISLKEG EEPFKEHARK IMQYGAATVV MAFDEQGQAD SLHRRIEICS RAYKILTEEV GFPPEDIIFD PNVLTVATGI DEHNNYALDF IESVRWIKQN LPHAKVSGGI SNVSFSFRGN EPVREAMHTA FLYHAIHAGL DMGIVNAAQL GIYEDIDPEL LVYVEDVLLN RRDDATERLV AFAETIRDGG EKAEAKTAEW RNAPVEERLK HALVKGIVDY IDEDTEEARQ LYPSPLEVIE GPLMNGMNHI GDLFAEGKMF LPQVVKSARV MKRSVAVLVP YIEEEKAKSC DTSAKAKVLL ATVKGDVHDI GKNIVSVVLA CNNFDVVDIG VMMPCDKILD AVVKEKPDVL GLSGLITPSL EEMAHVAKEM ERLGMNIPLI IGGATTSKVH TAVKLAPNYS GAVVHVLDAS RSVPVVSNLC NPAQREGYIA ALNSEQEAMR KSHAERTAAK KYISLDAARD NRLAIDWEAE TIDKPAQTGV TVLEDVTVGA LRSYIDWTPF FRSWELHGVY PQILEDEKVG EEATKLFNDA TALLDRIDSE KLLGIKGVAG IFPANSIGDD IFVYSDDERS MIRTVLHTLR QQSEKHGEAN LALADFVAPR ESGVNDWIGC FTVTAGLGIQ SLLQEFAAEN DDYHRIMTQA LADRLAEAFA EMLHEKVRRE LWGYAPGEIL GSEELIAEQY RGIRPAPGYP ACPDHTEKAT IFDLLNAEAA TGVTLTETFA MNPAASVCGL YFANPASKYF VLGKIGKDQV EDYANRKGLE VSEAEKWLAP ALNYDPA // ID B3QTZ4_CHLT3 Unreviewed; 1233 AA. AC B3QTZ4; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 27-MAY-2015, entry version 51. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACF12792.1}; GN OrderedLocusNames=Ctha_0321 {ECO:0000313|EMBL:ACF12792.1}; OS Chloroherpeton thalassium (strain ATCC 35110 / GB-78). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chloroherpeton. OX NCBI_TaxID=517418 {ECO:0000313|EMBL:ACF12792.1, ECO:0000313|Proteomes:UP000001208}; RN [1] {ECO:0000313|EMBL:ACF12792.1, ECO:0000313|Proteomes:UP000001208} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35110 / GB-78 {ECO:0000313|Proteomes:UP000001208}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001100; ACF12792.1; -; Genomic_DNA. DR RefSeq; WP_012498876.1; NC_011026.1. DR RefSeq; YP_001995239.1; NC_011026.1. DR STRING; 517418.Ctha_0321; -. DR EnsemblBacteria; ACF12792; ACF12792; Ctha_0321. DR KEGG; cts:Ctha_0321; -. DR PATRIC; 21429091; VBIChlTha99257_0375. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CTHA517418:GHTO-323-MONOMER; -. DR Proteomes; UP000001208; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001208}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001208}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1233 AA; 136430 MW; 50B97CE40EB8AD1B CRC64; MQRDIIKLLQ ERILVLDGAM GTLIQRHKLT EEDFRGERFK DHSHSLKGNN DILVITQPEI IKDIHRQFLE AGSDIIETNT FSSTPISLAD YEVQDLTYEL NLTATKLARE VADEMTAKTP DKPRFVAGSI GPTNKTLSLS PDVNNPGYRA ITFQNVVDAY TEQLKGLLDG GVDILLVETV FDTLNCKAAL FAIHEFFNKT QRRVPVMVSG TVVDASGRTL SGQTTEAFWI SISHMPDLMS VGLNCALGAK QMRPFVEAMS NVAQTYTSVY PNAGLPNEFG EYDDSPEYMA AQIEDFAKSG FVNIVGGCCG TTPAHIKAIA ETVKTLPPRK RPEPHHILQL SGLEPLAVDK TTGFINIGER TNVTGSRKFA RLIKEGNYDA ALSIARQQVE SGAQVIDVNV DEGMLDSEKV MAEFLNLIAS EPEIARVPIM IDSSKWSVIE AGLRCTQGKC IVNSISLKEG EAIFKERAEK ILEYGAAAVV MAFDEKGQAD SYERRVEICS RAYKILTEEV GFPPEDIIFD PNVLTVATGI EEHNNYAVDF INSVRWIKQN LPHAKISGGI SNISFSFRGN EPVREAMHAA FLYHAIREGL DMGIVNAGQL AIYEDIDKDL LERVEDVLLN RREDATERLV DFAETIKSDG SKSEAKKAEW RNLPVEERLK HALIKGIVEH IDEDTEEARQ KYPRPLHVIE GPLMDGMNTI GDLFAEGKMF LPQVVKSARV MKKSVAYLIP FIEEEKAQCE DSKPAAKVLL ATVKGDVHDI GKNIVGVVLA CNNFQVVDIG VMMPCEKIME AIEKEKPDVV GLSGLITPSL DEMAHVAKEM QRAGMNIPLL IGGATTSKVH TAVKLAPHYS APVLHVLDAS RSVPVVNNLV SDEQKSDYIA KHFAEQAQMR EDHEKRNAKR KFVSLEAARE NALKIDWSES EVFAPKQAGI TKFENVSLAE LRKYIDWTPF FLTWELHGKY PNIFEHEKFG EEAKKVFDDA NALLDKIITE NAIQAKGVVG IFPANSVGDD IEVYADENRS ETCTVLHTLR QQNEKSSGQS NIALADFVAP KESGLKDYVG GFAVTAGLGI EKLMKEFAAA HDDYHRIMTQ ALADRLAEAF AEMLHEKVRR ELWGYATSES LSSDELIHEK YQGIRPAPGY PASPDHSEKP ILFKLLGAEE ATGISLTETC AMSPAASVSG LYFAHPKASY FSVGKIGKDQ AEDYAARKGM KMEEVEKWLS TALNYEPNVE TVG // ID B3RR62_TRIAD Unreviewed; 441 AA. AC B3RR62; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 04-MAR-2015, entry version 33. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EDV26288.1}; GN ORFNames=TRIADDRAFT_63716 {ECO:0000313|EMBL:EDV26288.1}; OS Trichoplax adhaerens (Trichoplax reptans). OC Eukaryota; Metazoa; Placozoa; Trichoplax. OX NCBI_TaxID=10228 {ECO:0000313|Proteomes:UP000009022}; RN [1] {ECO:0000313|EMBL:EDV26288.1, ECO:0000313|Proteomes:UP000009022} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV26288.1, RC ECO:0000313|Proteomes:UP000009022}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS985243; EDV26288.1; -; Genomic_DNA. DR RefSeq; XP_002110284.1; XM_002110248.1. DR STRING; 10228.JGI63716; -. DR EnsemblMetazoa; TriadT63716; TriadP63716; TriadG63716. DR GeneID; 6752031; -. DR KEGG; tad:TRIADDRAFT_63716; -. DR eggNOG; COG0646; -. DR HOGENOM; HOG000231636; -. DR InParanoid; B3RR62; -. DR KO; K00544; -. DR OMA; WGVTKGT; -. DR OrthoDB; EOG79GT7C; -. DR Proteomes; UP000009022; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009022}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000009022}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 257 257 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 339 339 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 340 340 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 441 AA; 48183 MW; 7F424F45D45D4E64 CRC64; MTTGNDQICF LSSKDFASAS TTAVIASWKI CPSSVTTDSL HIDSNFSSFF PNQGILERLN EGVVIGDGGF VFALEKRGYV KAGPWTPEAV IEYPEAVKQL HREFLRAGSD VMQCFTFYAS EDKLENRGNK AAQHGVGAVN EAACKIAREV ANEGDALIAG GMCQTPTYLS GGNKETVQIE FQKQADAFVK CGVDFLICEY FEHVEEATWA VEVCKKTGMA VAATLCINDE GDMHGVSTAD CAVKLANAGA DIIGINCHFD PDATLAGIRE MKRGLDEAGL KRHLMSQPLA FKTPDVNKQG FIDLPEFPFA LEPRILTRWD CHRYAREAYD LGVRYIGACC GFEPYHVRAI AEELSKERGC LPAASEKHDM WGGGLQLHTK PWVRARARRD YWENLSPASG RAESSAFSKP NAWGVTAGDD LLKQQKEATT LAEISNLAGR S // ID B3RR63_TRIAD Unreviewed; 368 AA. AC B3RR63; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 04-MAR-2015, entry version 32. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EDV26822.1}; GN ORFNames=TRIADDRAFT_63717 {ECO:0000313|EMBL:EDV26822.1}; OS Trichoplax adhaerens (Trichoplax reptans). OC Eukaryota; Metazoa; Placozoa; Trichoplax. OX NCBI_TaxID=10228 {ECO:0000313|Proteomes:UP000009022}; RN [1] {ECO:0000313|EMBL:EDV26822.1, ECO:0000313|Proteomes:UP000009022} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV26822.1, RC ECO:0000313|Proteomes:UP000009022}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS985243; EDV26822.1; -; Genomic_DNA. DR RefSeq; XP_002110818.1; XM_002110782.1. DR STRING; 10228.JGI63717; -. DR EnsemblMetazoa; TriadT63717; TriadP63717; TriadG63717. DR GeneID; 6751500; -. DR KEGG; tad:TRIADDRAFT_63717; -. DR eggNOG; COG0646; -. DR HOGENOM; HOG000231636; -. DR InParanoid; B3RR63; -. DR OMA; NINEAAC; -. DR OrthoDB; EOG79GT7C; -. DR Proteomes; UP000009022; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009022}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000009022}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 207 207 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 368 AA; 40471 MW; 5BAF952249E60468 CRC64; MGKGILERLD EGVIIGDGGF VVALEKRGYV QAGPWTPEAV IEHPEAVLEL HREFLRAGSD VMQCFTFYAS EDKLTVRGNK AGRHGSTNIN EAACLLAREV ANEGDALIAG GMSQTPTYAE GGSKEAVQEH FQKQADAFTK CGVDFLICEY FEHAEEACWA VEICKKTGLA VAATLCINKE GDVDGVPTSE CAVRLANAGA DIIGINCNFD PDTVLAGVRE MKRGLEEAGL KRHLITQPLG YRTPDANKHG FVDIPEFPFA MEPRTLTRWD CHRYAREAYD LGVRYIGACC GFEPYHVRAI AEELVTERGG KLPLASEKHE MWGGGLKLHT KPWVRARASR EYWENLRPAT GRPECPAYSK PSSHDITD // ID B3S7K9_TRIAD Unreviewed; 321 AA. AC B3S7K9; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 07-JAN-2015, entry version 30. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EDV21215.1}; GN ORFNames=TRIADDRAFT_60203 {ECO:0000313|EMBL:EDV21215.1}; OS Trichoplax adhaerens (Trichoplax reptans). OC Eukaryota; Metazoa; Placozoa; Trichoplax. OX NCBI_TaxID=10228 {ECO:0000313|Proteomes:UP000009022}; RN [1] {ECO:0000313|EMBL:EDV21215.1, ECO:0000313|Proteomes:UP000009022} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV21215.1, RC ECO:0000313|Proteomes:UP000009022}; 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; DS985254; EDV21215.1; -; Genomic_DNA. DR RefSeq; XP_002116182.1; XM_002116146.1. DR STRING; 10228.JGI60203; -. DR EnsemblMetazoa; TriadT60203; TriadP60203; TriadG60203. DR GeneID; 6757489; -. DR KEGG; tad:TRIADDRAFT_60203; -. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR InParanoid; B3S7K9; -. DR KO; K00547; -. DR OMA; AINDPLW; -. DR OrthoDB; EOG7GQXW0; -. DR Proteomes; UP000009022; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009022}; KW Reference proteome {ECO:0000313|Proteomes:UP000009022}. SQ SEQUENCE 321 AA; 35964 MW; EB949F8520BBCC52 CRC64; MDKEILVIDG ACGTELQRLG YDVDADPLWS ASLLLTNPQV IKDLHTSYLN AGADIILTAT YQASIPGLVQ YADLTEASAS AVIAMAVRLA IEARDEFWAE QKACNKNVRR PKPLVVGSVG PFGACQHDGS EFHGRYTDEM TIEELKQWHK PRIMELIQNG VDLIAFETIP AEKEAIALIQ VLETFRGVKA WLSFVCKDDL HLNHGELFAD VMERFRNHNQ IVAIGTNCTN PQNVDNLIQS CKRLDAYDKP FIAYPNSGES WSVDRWDPTI PPVELSDYVQ RWIKNGIRWI GGCCRTTPSD ILKIRNKVDG IPKLKESKSL I // ID B3T148_9ZZZZ Unreviewed; 348 AA. AC B3T148; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 29-APR-2015, entry version 14. DE SubName: Full=Putative Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABZ06307.1}; GN ORFNames=ALOHA_HF4000008G09ctg1g8 {ECO:0000313|EMBL:ABZ06307.1}; OS uncultured marine microorganism HF4000_008G09. OC unclassified sequences; environmental samples. OX NCBI_TaxID=455513 {ECO:0000313|EMBL:ABZ06307.1}; RN [1] {ECO:0000313|EMBL:ABZ06307.1} 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; EU016572; ABZ06307.1; -; Genomic_DNA. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:ABZ06307.1}; KW Transferase {ECO:0000313|EMBL:ABZ06307.1}. SQ SEQUENCE 348 AA; 39008 MW; 146FF6BA1CF450A8 CRC64; MSKNLISRLN EGPVLCAEGY LFAMERRGYL QAGAFVPEVV LEHPEVVSQL HREFIRAGSD IVQAFTYYGH REKLRIIGKE NLLESLQKNA LKIAKDARNE FKDLDLLVCG DVANTNVYDP NDKKSNIECQ KMFEEQVAWA KEAGVDFIVA ETITWLEEAK IALKTIKSVG LIAVSNLSIK KGDKTRDGYT PEDACKILED NGAEVVGLNC FRGPKMTMKL LNKIREKVSC HVAGLPVPYR TTEKDPGFLN QTDPGCDCIP GGNAFPVALD NLYCNRFEMA EFAKECATKK INFIGICCGA SPHHVREMAV ALGRKPISYK YYPDMSKHYV HGTDKTLKKI YTDHAKEY // ID B3T2H6_9ZZZZ Unreviewed; 305 AA. AC B3T2H6; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 29-APR-2015, entry version 14. DE SubName: Full=Putative homocysteine S-methyltransferase {ECO:0000313|EMBL:ABZ06785.1}; GN ORFNames=ALOHA_HF4000141I21ctg1g7 {ECO:0000313|EMBL:ABZ06785.1}; OS uncultured marine microorganism HF4000_141I21. OC unclassified sequences; environmental samples. OX NCBI_TaxID=455526 {ECO:0000313|EMBL:ABZ06785.1}; RN [1] {ECO:0000313|EMBL:ABZ06785.1} 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; EU016585; ABZ06785.1; -; Genomic_DNA. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:ABZ06785.1}; KW Transferase {ECO:0000313|EMBL:ABZ06785.1}. SQ SEQUENCE 305 AA; 34070 MW; 7140354ADBD7562E CRC64; MNTNYFSKTR ILDGGMGQEL LKRGLKPQGS LWSASALIEE KYHQLVVDTH LDFINAGADV IVTTTFTTRR NRLIQNKCEE HFEYVNTKAV ELALKARDIS KKNILIAGGL PNQNQTYSAN LGDDLNLIEK NFYDQAKLLK SNIDFFYLDV MGSGKECEIA LKTIKSFNLP VLVGVHIKKD GKLPSGENIS NIVKKYKEEN WLGIIAACVH PESYEIIIKE LKNSDISYGF KLNAFKNIPD DLRVSSTAAW GKGGNPTTIL GQREDITESK FYEFVKKFKD AGATILGGCC EIRPSHISKI ASLKN // ID B3XL43_LACRE Unreviewed; 310 AA. AC B3XL43; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EDX42250.1}; GN ORFNames=Lreu23DRAFT_3763 {ECO:0000313|EMBL:EDX42250.1}; OS Lactobacillus reuteri 100-23. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=349123 {ECO:0000313|EMBL:EDX42250.1}; RN [1] {ECO:0000313|EMBL:EDX42250.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=100-23 {ECO:0000313|EMBL:EDX42250.1}; 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.; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EDX42250.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=100-23 {ECO:0000313|EMBL:EDX42250.1}; 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., 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDX42250.1}. 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; AAPZ02000001; EDX42250.1; -; Genomic_DNA. DR RefSeq; WP_003663553.1; NZ_AAPZ02000001.1. DR ProteinModelPortal; B3XL43; -. DR EnsemblBacteria; EDX42250; EDX42250; Lreu23DRAFT_3763. DR PATRIC; 26514568; VBILacReu112121_0041. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDX42250.1}; KW Transferase {ECO:0000313|EMBL:EDX42250.1}. SQ SEQUENCE 310 AA; 33752 MW; E5A0E3934DEB7CD7 CRC64; MTKITAELTK PLLIDGAMST ALEQLGADTN NSLWTASVLA NQPALVKKVH QEYFKAGARL AITDTYQANV PAFIRNGYSK QEAHSLIQRA VALAKEARDE YQQETGIYNY VAGALGPYGA YLANGSEYTG DYHLSAIEYQ QFHRPRLTDI LTVGVDVIAI ETQPRLDEVL AELDLVKELA PYILCYVSFS LKDSTHLPDG TPLAVAARTV AKYPNVFAVG VNCIPLEEVT AAIETVHQVT DKPVIAYPNS SATYDPTTKT WSYPHGRRGL VDYLPQWLAA GLTIIGGCCT TTPQGIAALH EYLKGGAHHD // ID B3YH48_SALET Unreviewed; 1227 AA. AC B3YH48; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 27-MAY-2015, entry version 39. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EDX47285.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EDX47285.1}; GN Name=metH {ECO:0000313|EMBL:EDX47285.1}; GN ORFNames=SeKA_A3832 {ECO:0000313|EMBL:EDX47285.1}; OS Salmonella enterica subsp. enterica serovar Kentucky str. CVM29188. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=439842 {ECO:0000313|EMBL:EDX47285.1, ECO:0000313|Proteomes:UP000005051}; RN [1] {ECO:0000313|EMBL:EDX47285.1, ECO:0000313|Proteomes:UP000005051} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CVM29188 {ECO:0000313|EMBL:EDX47285.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EDX47285.1}. 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; ABAK02000001; EDX47285.1; -; Genomic_DNA. DR RefSeq; WP_000095985.1; NZ_ABAK02000001.1. DR EnsemblBacteria; EDX47285; EDX47285; SeKA_A3832. DR PATRIC; 27976750; VBISalEnt954_3960. DR Proteomes; UP000005051; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000005051}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EDX47285.1}; KW Transferase {ECO:0000313|EMBL:EDX47285.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135972 MW; 6DB9E5BF8E3E8009 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLHEEDFRGE RFADWPCDLK GNNDPLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYRMESLS AEINYAAAKL ARACADEWTA RTPEKPRFVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKEEF EALGVDLPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPEHIAA MSRAVAGLPP RQLPDIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VESGAQIIDI NMDEGMLDAE AAMVRFLSLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVEAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLDLAEKYRG SKTDEAANAQ QAEWRSWDVK KRLEYSLVKG ITEFIEQDTE EARQQAARPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EKGSSNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAREVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHARKKPR TPPVTLEAAR DNDLAFDWER YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KLLNPRGVVG LFPANRVGDD IEIYRDETRT HVLTVSHHLR QQTEKVGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA IADRLAEAFA EYLHERVRKV YWGYAPNESL SNDELIRENY QGIRPAPGYP ACPEHTEKGT IWQLLDVEKH TGMKLTESFA MWPGASVSGW YFSHPESKYF AVAQIQRDQV TDYAFRKGMS VEDVERWLAP NLGYDAD // ID B3ZET1_BACCE Unreviewed; 1132 AA. AC B3ZET1; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 27-MAY-2015, entry version 36. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EDX66178.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EDX66178.1}; GN Name=metH {ECO:0000313|EMBL:EDX66178.1}; GN ORFNames=BC059799_4329 {ECO:0000313|EMBL:EDX66178.1}; OS Bacillus cereus NVH0597-99. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=451707 {ECO:0000313|EMBL:EDX66178.1}; RN [1] {ECO:0000313|EMBL:EDX66178.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NVH0597-99 {ECO:0000313|EMBL:EDX66178.1}; 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] {ECO:0000313|EMBL:EDX66178.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NVH0597-99 {ECO:0000313|EMBL:EDX66178.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EDX66178.1}. 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; ABDK02000020; EDX66178.1; -; Genomic_DNA. DR RefSeq; WP_000649731.1; NZ_ABDK02000020.1. DR EnsemblBacteria; EDX66178; EDX66178; BC059799_4329. DR PATRIC; 24998081; VBIBacCer85191_4650. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EDX66178.1}; KW Transferase {ECO:0000313|EMBL:EDX66178.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 125973 MW; CE416BF47A9053A3 CRC64; MKCIEEKLQN SILLLDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYELSHLDE ELNEKAARLA KQAVKESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGE VDVLLVETSQ DMRNVKAAYI GIQAAFDELK KIVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWVN IIGGCCGTTP EHIKAMKEAL ASLKPREHHE REGHGVSGLE ALQYDDSMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMENF LAEVTKVLKV PIMIDSTDEH VMERALTYIQ GKAVINSINL EDGEERFIKV TPLLQKYGAA IVVGTIDEDG MAVSAERKLE IAKRSYELLT TKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPDE EKRLADALLF ETTQETLEEF TNFYRVAKKK DVVVQETLTL DERLANYIVE GTKQGLHEDL SLALTEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILA NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAADIDIPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV TKEEKKVEIP AVIEPLPKSE VMVPDSTKRV VLRDVPALHL APFLNRQMLL GHHLGLKGSV KKLLKEGDKR AHELNDLIDE LLREGQSWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRVIE RFTFPRQGRA PYRTLGDYLR PIGDEMDYVA FLSVTVGEGV RDIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID B3ZET2_BACCE Unreviewed; 610 AA. AC B3ZET2; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 27-MAY-2015, entry version 31. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=BC059799_4330 {ECO:0000313|EMBL:EDX66162.1}; OS Bacillus cereus NVH0597-99. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=451707 {ECO:0000313|EMBL:EDX66162.1}; RN [1] {ECO:0000313|EMBL:EDX66162.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NVH0597-99 {ECO:0000313|EMBL:EDX66162.1}; 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] {ECO:0000313|EMBL:EDX66162.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NVH0597-99 {ECO:0000313|EMBL:EDX66162.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDX66162.1}. 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; ABDK02000020; EDX66162.1; -; Genomic_DNA. DR RefSeq; WP_000770331.1; NZ_ABDK02000020.1. DR ProteinModelPortal; B3ZET2; -. DR EnsemblBacteria; EDX66162; EDX66162; BC059799_4330. DR PATRIC; 24998083; VBIBacCer85191_4651. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EDX66162.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EDX66162.1}. SQ SEQUENCE 610 AA; 67298 MW; 3F0A2353CD3128EB CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNISDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTE INRAAVKLAK ASVTDRNAIL GTIGGMKHIG AVTTTDMERE FMLLEQASAL LEEQVDGLLL ETFYDEFELL HAVQVLRKET NIPIVAQLAL HEAGTTQNGN DVNEILKQLL DYGANVVGLN CQLGPLHMTE AFKMISIPKN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPKFIEQGI RLLGGCCGTT PEHIESMKRA TLNVTPVIEK DTIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRISNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIA LIEEVYEATK HLEQPIFIGI MPLISKRNAD FLHFEVPGIT LPEAVRERMD GHETKEAAIE EGIRISQELI DETMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID B3ZT21_BACCE Unreviewed; 610 AA. AC B3ZT21; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 27-MAY-2015, entry version 30. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=AK40_2844 {ECO:0000313|EMBL:AJI11933.1}; OS Bacillus cereus 03BB108. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=451709 {ECO:0000313|EMBL:AJI11933.1, ECO:0000313|Proteomes:UP000031861}; RN [1] {ECO:0000313|EMBL:AJI11933.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=03BB108 {ECO:0000313|EMBL:AJI11933.1}; RA Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O., Coyne S.R., RA Daligault H.E., Davenport K.W., Erkkila T., Frey K.G., Gibbons H.S., RA Gu W., Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C., RA Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N., RA Scholz M.B., Teshima H., Xu Y.; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009641; AJI11933.1; -; Genomic_DNA. DR RefSeq; WP_001995221.1; NZ_ABDM02000014.1. DR ProteinModelPortal; B3ZT21; -. DR EnsemblBacteria; EDX61514; EDX61514; BC03BB108_4180. DR Proteomes; UP000031861; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031861}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:AJI11933.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:AJI11933.1}. SQ SEQUENCE 610 AA; 67188 MW; 9FD948A1F0722DFD CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNISDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTE INRAAVKLAK ASVTDRNAIL GTIGGMKHIG AVTTTDMERE FMLLEQASAL LEEQVDGLLL ETFYDEFELL HAVQVLRKET NIPIVAQLAL HEAGTTQNGN DVNEILKQLL DYGANVVGLN CQLGPLHMTE ALKMISIPKN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPKFIEQGI RLLGGCCGTT PEHIESMKRA TLNVTPVIEK DTIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRISNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIA LIEEVYEAIK HLEQPIFIGI MPLISKRNAD FLHFEVPGIT LPEAVRERMD GHETKEAAIE EGIRISQELI DAAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID B3ZT22_BACCE Unreviewed; 1132 AA. AC B3ZT22; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 27-MAY-2015, entry version 37. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AJI13061.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AJI13061.1}; GN Name=metH {ECO:0000313|EMBL:AJI13061.1}; GN ORFNames=AK40_2843 {ECO:0000313|EMBL:AJI13061.1}; OS Bacillus cereus 03BB108. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=451709 {ECO:0000313|EMBL:AJI13061.1, ECO:0000313|Proteomes:UP000031861}; RN [1] {ECO:0000313|EMBL:AJI13061.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=03BB108 {ECO:0000313|EMBL:AJI13061.1}; RA Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O., Coyne S.R., RA Daligault H.E., Davenport K.W., Erkkila T., Frey K.G., Gibbons H.S., RA Gu W., Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C., RA Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N., RA Scholz M.B., Teshima H., Xu Y.; RL Submitted (OCT-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; CP009641; AJI13061.1; -; Genomic_DNA. DR RefSeq; WP_001995203.1; NZ_ABDM02000014.1. DR EnsemblBacteria; EDX61467; EDX61467; BC03BB108_4179. DR Proteomes; UP000031861; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000031861}; KW Methyltransferase {ECO:0000313|EMBL:AJI13061.1}; KW Transferase {ECO:0000313|EMBL:AJI13061.1}. SQ SEQUENCE 1132 AA; 126001 MW; 9FABE85EE3A7CECB CRC64; MKCIEEKLRN NILLLDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYELSHLDE ELNEKAARLA KQAVEESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGE VDVLLVETSQ DMRNVKAAYI GIQAAFDELN KIVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWVN IIGGCCGTTP EHIKAMKEAL ASLKPREHHE REGHGVSGLE ALQYDDSMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMENF LAEVTKVLKV PIMIDSTDEH VMERALTYIQ GKAVINSINL EDGEERFIKV TPLLQKYGAA IVVGTIDEDG MAVSAERKLE IAKRSYELLT TKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPDE EKRLADALLF ETTQETLEEF TNFYRVAKKK DVVVQETLTL DERLANYIVE GTKQGLHEDL SLALTEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILA NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAADIDIPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV TKEEKKVEIP AVIEPLPKSE VMVPDSTKRI VLRDVPALHL APFLNRQMLL GHHLGLKGSV KKLLKEGDKR AHELNDLIDE LLQEGQSWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRVIE RFTFPRQGRA PYRTLGDYLR PIGDEMDYVA FLSVTVGEGV RDIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID B4AFE8_BACPU Unreviewed; 613 AA. AC B4AFE8; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 27-MAY-2015, entry version 28. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=BAT_3037 {ECO:0000313|EMBL:EDW23370.1}; OS Bacillus pumilus ATCC 7061. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=536229 {ECO:0000313|EMBL:EDW23370.1}; RN [1] {ECO:0000313|EMBL:EDW23370.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 7061 {ECO:0000313|EMBL:EDW23370.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDW23370.1}. 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; ABRX01000001; EDW23370.1; -; Genomic_DNA. DR RefSeq; WP_003211896.1; NZ_ABRX01000001.1. DR ProteinModelPortal; B4AFE8; -. DR EnsemblBacteria; EDW23370; EDW23370; BAT_3037. DR PATRIC; 25203486; VBIBacPum54595_0800. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EDW23370.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EDW23370.1}. SQ SEQUENCE 613 AA; 68227 MW; F2E2C7C152BA1F4B CRC64; MGLLQDLQNR VLIADGAMGT LLYSYGIDRC FEELNLSKED EVRRVHEAYV QAGADIIQTN TYGANYIKLS RYGLEEETKR INTKAVQIAK TAAGSAYVLG TIGGIRTFNK NAYTIEEIKR SFREQLYILL NEQPDGLLLE TYYDMEEAKA VLQIARKETT LPIVMNVSMH EQGVLQDGTP LKDGLSELSS LGADVVGINC RLGPYHMIQA LEGVPILENS HLSVYPNSSL PSLEEGRLVY DTDNDYFRKS ALEFRNQGAR IIGGCCGTTP QHIHAMAEAV KDLAPITEKE VKVLKEEIIS IQDQRTEPGL DELATKKRTI IVELDPPKKL NFEKFLVAAN ELKNAGIDAL TLADNSLATP RISNVACGAL LKQQLDMRSL VHITCRDRNL IGLQSHLMGL DTLGLTDILA ITGDPSKIGD FPGATSVYDL TSFDLIRLIK QFNEGLSFSG KPLGKKTNFS VAGAFNPNVR HIDKAVKRLE KKIEYGADYF ISQPVYSEEQ LVKIHEESRH LDKPIYIGVM PLTSSRNAEF IHHEIPGIKL SDSIRDIMAK AGEDKEKQRA EGLAIARSLL DTACELFNGI YLITPFLRSD LTAELTTYIH QKEKESNTHV NYH // ID B4AFE9_BACPU Unreviewed; 1142 AA. AC B4AFE9; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 27-MAY-2015, entry version 37. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EDW23056.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EDW23056.1}; GN Name=metH {ECO:0000313|EMBL:EDW23056.1}; GN ORFNames=BAT_3038 {ECO:0000313|EMBL:EDW23056.1}; OS Bacillus pumilus ATCC 7061. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=536229 {ECO:0000313|EMBL:EDW23056.1}; RN [1] {ECO:0000313|EMBL:EDW23056.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 7061 {ECO:0000313|EMBL:EDW23056.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EDW23056.1}. 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; ABRX01000001; EDW23056.1; -; Genomic_DNA. DR RefSeq; WP_003211310.1; NZ_ABRX01000001.1. DR EnsemblBacteria; EDW23056; EDW23056; BAT_3038. DR PATRIC; 25203488; VBIBacPum54595_0801. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EDW23056.1}; KW Transferase {ECO:0000313|EMBL:EDW23056.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 225 225 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 722 722 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1142 AA; 126825 MW; EC1BE11BC25B615E CRC64; MSTITEQLKK RILVLDGAMG TMIQNANLTA EDFGGEEYEG CNEYLNVTAP HIIRAIHREY LEASADLIET NTFGATKLVL DEYGLGHLAY ELNIRAAQLA KDEADRFSTP EQPRFVVGAM GPTTKTLSVT GGTTFDELVR NYEEQARALI DGKCDALLLE TSQDMLNVKA GFKGIQEAFQ QTGIELPLMV SGTIEPMGTT LAGQDIEAFY ISLEHMKPMS VGLNCATGPE FMTDHIRTLS SIAKSAVSCY PNAGLPDEEG QYHESPASLA KKISAFAKEG WLNIVGGCCG TTPAHIQALS DEVRTIQPRH IAHESSQHTV SGIEPLIYEE SMRPLFVGER TNVIGSRKFK RLIAEQKFEE ASEIARAQVK NGAHVIDVCL ADPDREEAAD MEGFLQEAMK KVKAPFVIDS TDKHVIEKAL TYSQGKAIIN SINLEDGEER FEEILPLVKL YGGALVVGTI DETGMAVTAE RKLEIAVRSH DLLTKKYGIP ASDIIFDPLV FPVGTGDEQY IGAAEETIKG IKMIKENLPE CLTILGISNV SFGLPPLGRE ILNAVYLYHC VQAGLDYAIV NTEKLERFAS IPKEEIKLAE TLLYETNDQT LAEFTQFYRG KKKTEKKPKV SLSLDERLAL YVVEGTKEGL IDDLSLALEQ FESPLHIING PLMQGMAEVG RLFNQNELIV AEVLQSAEVM KASVSYLEQY MEKQHANGKG KILLATVKGD VHDIGKNLVD IILSNNGFQV VDLGIKVTPQ TLIEAVQKEK PDMIGLSGLL VKSAQQMVLT AQDLQKANIS VPILVGGAAL SRKFTKMKIS PHYDGPVLYA KDAMDGLSLA NELKANPLQF QIKPDEEPVA PFKKKETKQP QAVIELLEKR AALPDAPIFT PENTARHYVR DIDLHHIMPY VNEQMLIGHH LGLKGKVKTL LAQQHPKALE LKQLVTDLLN EGREKNWFAP AFVYQFYPAS SNGNDLHIYD PEAPDRIIET FQFPRQEKLP YRSISDYVRG SGEREKDYIA LFAVTAGARI REVAQHFKQE GDYLKMHAVQ ALALELAEGL AERTHQVIRD KWGFPDPVDF TMEKRFQAKY QGQRYSFGYP ACPNLEDQEK LFKLLQPEKI GIHLTEGFMM EPEASVSAIV VSHPEARYFN VH // ID B4AMQ3_BACPU Unreviewed; 312 AA. AC B4AMQ3; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=Homocysteine S-methyltransferase 2 (S-methylmethionine:homocysteine methyltransferase 2) (SMM:Hcy S-methyltransferase 2) (ZmHMT-2) {ECO:0000313|EMBL:EDW20349.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EDW20349.1}; GN ORFNames=BAT_3890 {ECO:0000313|EMBL:EDW20349.1}; OS Bacillus pumilus ATCC 7061. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=536229 {ECO:0000313|EMBL:EDW20349.1}; RN [1] {ECO:0000313|EMBL:EDW20349.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 7061 {ECO:0000313|EMBL:EDW20349.1}; 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. {ECO:0000313|EMBL:EDW20349.1}. 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; ABRX01000007; EDW20349.1; -; Genomic_DNA. DR RefSeq; WP_003217053.1; NZ_ABRX01000007.1. DR EnsemblBacteria; EDW20349; EDW20349; BAT_3890. DR PATRIC; 25208791; VBIBacPum54595_3405. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDW20349.1}; KW Transferase {ECO:0000313|EMBL:EDW20349.1}. SQ SEQUENCE 312 AA; 34418 MW; 02803D82B4552050 CRC64; MNPIQSRLQA HAPLILDGAL ATELERKGCN LNDSLWSAKI LIEQPELIQQ VHLDYFKAGA DCATTASYQT TIDGFAEKGY SKEEAIELMK RSVTLAKEAR DLFWQDEARR KGRTKPFVAG SVGPFGAYLS DGSEYKGNYG LTEQTLIDFH RPRIQALVEA GADILACETI PCLIEATAIA KLLQDEFNGV SAWITFSAKD DLHISEGDLL RECVQALEPY EQIAAVGVNC TPPQFISSLI QEMKKGTSKP IVVYPNSGEL YDPEEKVWSG DTLQHTFGEC AHQWYQDGAH IIGGCCRTTP EDITDILKLT TA // ID B4D950_9BACT Unreviewed; 1287 AA. AC B4D950; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 27-MAY-2015, entry version 37. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EDY17095.1}; GN ORFNames=CfE428DRAFT_5440 {ECO:0000313|EMBL:EDY17095.1}; OS Chthoniobacter flavus Ellin428. OC Bacteria; Verrucomicrobia; Spartobacteria; Chthoniobacter. OX NCBI_TaxID=497964 {ECO:0000313|EMBL:EDY17095.1}; RN [1] {ECO:0000313|EMBL:EDY17095.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Ellin428 {ECO:0000313|EMBL:EDY17095.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EDY17095.1}. 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; ABVL01000024; EDY17095.1; -; Genomic_DNA. DR RefSeq; WP_006982761.1; NZ_ABVL01000024.1. DR EnsemblBacteria; EDY17095; EDY17095; CfE428DRAFT_5440. DR PATRIC; 27081926; VBIChtFla82190_5539. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 272 272 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 337 337 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 338 338 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 801 801 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1287 AA; 140517 MW; 37F7CB942CE478D2 CRC64; MSAEKSLHPL AALLQKRIAI IDGAMGTTIR TYGMKEADIR GTRFVDAKKD LLNNGDLFSL TQAAMIGDIH RRFLEAGADI IETNTFSATS IGQSEFFVDD PREHGGRKDP AFYQKIIDDP FLNELAWDIN FQSASQCREW ADRVGSKDGK QRFVAGAVGP LTVSLSNSPD ADDPGFRTVT FDQVKAAYIQ QVRALIAGGS DILLVETIFD SLNAKAALVA IQEVFEKDKV SLPISISAAV GRGGETMISA QTVEAFWNAV KHVNPLSVGL NCSLGPDLMR PFLEELSTKS DSAISCYPNA GLPNPLSPTG FDLEPEDMGR YLGDFAQSGL LNIAGGCCGN TPEHIAAIAR TLADLPPREP KEETKYSTGG PLPLRLSGSQ PFTQQIGSYL MIGERTNVAG SPKFAKLIKE GKYEEAVAIA RQQVENGANV IDICMDEGMI DGVAAMTRFL LLLGSEPEVA KVPFMVDSSK WEVIEAGLKC LQGKGIVNSI SLKEGEDIFR EHARTVLRYG AAVVVMAFDE QGQAATLADK IRICERAYRI LVDEVGFPPE DIIFDPNVLT VATGIEEHNN YAIDFIEATR WIKANLPHAK VSGGVSNISF SFRGNNVVRE AMHSAFLFHA IGAGMDMGIV NAGMLEVYEE IQPELKMLVE DVLLNRRPDA TERLVDFGEK LKAAGAGKDA AAEKKEEEWR KGTVEARLSH ALVKGIDTYI DTDTEEARAK FGRPLAVIEG PLMDGMGVVG DLFGAGKMFL PQVVKSARVM KKAVAYLTPF MEEEKAAMAA AGKAVRSQGK IVLATVKGDV HDIGKNIVGV VLACNNYDVI DMGVMVPCEK ILERARQEGA DVIGLSGLIT PSLDEMTHVA REMERTGLKL PLLIGGATTS KAHTAVKIAP GYGGPVVHVL DASRAVPVVT SLISEEARPA FIAKNLDEQA RARATHFGQK QELISLKAAR ANRTPIEWRA EDVPQPEFIG ARVLEDFPLA TLREFIDWSP FFHTWELRGV YPAIFEHEKY GEQARKLFAE AQELLDRMIG EKLVVAKAVY GFFPANAVGD DVEVYTDETR QTVRTTFHFL RQQVVKKEGE PSQSLSDFIA PKSTGLPDHI AAFAVTSGHG LKELVERFKA EHDDYNAIMA EALADRLAEA FAECLHKRVR DEWGYGRAEN LTSEQLIHEQ YRGIRPAAGY PACPDHTEKG ILWELLDVER KAGIQITESF AMWPGSSVSG LYFAHPRSRY FGLGKIDRDQ VLDYHLRKGM TVPEVERWLS PNLNYDPDAP APAGGAASPS GAAQLVS // ID B4DBI1_9BACT Unreviewed; 283 AA. AC B4DBI1; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EDY16168.1}; GN ORFNames=CfE428DRAFT_6272 {ECO:0000313|EMBL:EDY16168.1}; OS Chthoniobacter flavus Ellin428. OC Bacteria; Verrucomicrobia; Spartobacteria; Chthoniobacter. OX NCBI_TaxID=497964 {ECO:0000313|EMBL:EDY16168.1}; RN [1] {ECO:0000313|EMBL:EDY16168.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Ellin428 {ECO:0000313|EMBL:EDY16168.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDY16168.1}. 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; ABVL01000038; EDY16168.1; -; Genomic_DNA. DR RefSeq; WP_006983590.1; NZ_ABVL01000038.1. DR EnsemblBacteria; EDY16168; EDY16168; CfE428DRAFT_6272. DR PATRIC; 27083576; VBIChtFla82190_6346. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EDY16168.1}; KW Transferase {ECO:0000313|EMBL:EDY16168.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 199 199 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 261 261 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 262 262 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 283 AA; 29920 MW; 002DE094F548A362 CRC64; MDFLDELQHR VLIGDGAMGT ELLAHGVPPG RCLEELCVSD PDLVRGVHER YIAAGARLIE TNTFGANAVR LAQYGCEHRV GELNWTAAQL AKDVARGKDV YVAGCVGPLG ITAEEAAARG IDRHEVFTDQ IGALLDGGCR IIFLETFLDA DELLVALEAK QALHHCPVVA MLTSNDRQAF QAAIAKVRAA EAEVVGANCV DGTHALHLLD GMDPDATLAA FPSAGLPKTH DQQLAYPTTP EVFAANARTL AERGVRLLGG CCGVGPQHIA ALAAAFRETT TPT // ID B4DFV0_HUMAN Unreviewed; 229 AA. AC B4DFV0; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 01-APR-2015, entry version 46. DE SubName: Full=cDNA FLJ53729, moderately similar to Methionine synthase (EC 2.1.1.13) {ECO:0000313|EMBL:BAG57561.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG57561.1}; RN [1] {ECO:0000313|EMBL:BAG57561.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Amygdala {ECO:0000313|EMBL:BAG57561.1}; RA Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., RA Sugiyama A., Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., RA Kumagai A., Oishi Y., Yamamoto S., Ono Y., Komori Y., Yamazaki M., RA Kisu Y., Nishikawa T., Sugano S., Nomura N., Isogai T.; RT "NEDO human cDNA sequencing project focused on splicing variants."; 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; AK294270; BAG57561.1; -; mRNA. DR UniGene; Hs.498187; -. DR ProteinModelPortal; B4DFV0; -. DR SMR; B4DFV0; 140-225. DR PRIDE; B4DFV0; -. DR ChiTaRS; MTR; human. DR NextBio; 35471590; -. DR Bgee; B4DFV0; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; SQ SEQUENCE 229 AA; 24271 MW; 5E5C8D39B98DC2EA CRC64; MSAGLRAGCH VVLLCRFSLG SFSVPSRDSA SGRACLAARP TPRTGRVPGK KARAPAVAAP SPERGPRALR AFGVRSPPAT RANGRRQKTR ALCGRLAWRW LAWPLAVVTC GEHVFSAAPS AQGGDSTTCH PRSKTCRNPE YLLAGADIIE TNTFSSTSIA QADYGLEHLA YRMNMCSAGV ARKAAEEVTL QTGIKRFVAG ALGPTNKTLS VSPSVERPDY RNINLPVGS // ID B4DPF0_HUMAN Unreviewed; 365 AA. AC B4DPF0; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 04-MAR-2015, entry version 33. DE SubName: Full=cDNA FLJ54604, highly similar to Betaine--homocysteine S-methyltransferase (EC 2.1.1.5) {ECO:0000313|EMBL:BAG60562.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG60562.1}; RN [1] {ECO:0000313|EMBL:BAG60562.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Kidney {ECO:0000313|EMBL:BAG60562.1}; RA Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., RA Sugiyama A., Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., RA Kumagai A., Oishi Y., Yamamoto S., Ono Y., Komori Y., Yamazaki M., RA Kisu Y., Nishikawa T., Sugano S., Nomura N., Isogai T.; RT "NEDO human cDNA sequencing project focused on splicing variants."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK298308; BAG60562.1; -; mRNA. DR UniGene; Hs.80756; -. DR PRIDE; B4DPF0; -. DR HOGENOM; HOG000231636; -. DR HOVERGEN; HBG080367; -. DR UniPathway; UPA00051; UER00083. DR NextBio; 35473856; -. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000313|EMBL:BAG60562.1}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000313|EMBL:BAG60562.1}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 176 176 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 258 258 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 259 259 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 365 AA; 40485 MW; 787CE1E97A0816B0 CRC64; MPPVGGKKAK KGILERLNAG EFLRAGSNVM QTFTFYASED KLENRGNYVL EKISGQEVNE AVCDIARQVA DEGDALVAGG VSQTPSYLSC KSETEVKKVF LQQLEVFMKK NVDFLIAEYF EHVEEAVWAV ETLIASGKPV AATMCIGPEG DLHGVPPGEC AVRLVKAGAS IIGVNCHFDP TISLKTVKLM KEGLEAAQLK AHLMSQPLAY HTPDCNKQGF IDLPEFPFGL EPRVATRWDI QKYAREAYNL GVRYIGGCCG FEPYHIRAIA EELAPERGFL PPASEKHGSW GSGLDMHTKP WVRARARKEY WENLRIASGR PYNPSMSKPD GWGVTKGTAE LMQQKEATTE QQLKELFEKQ KFKSQ // ID B4DST3_HUMAN Unreviewed; 1118 AA. AC B4DST3; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 27-MAY-2015, entry version 50. DE SubName: Full=cDNA FLJ56487, highly similar to Methionine synthase (EC 2.1.1.13) {ECO:0000313|EMBL:BAG61745.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG61745.1}; RN [1] {ECO:0000313|EMBL:BAG61745.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Brain {ECO:0000313|EMBL:BAG61745.1}; RA Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., RA Sugiyama A., Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., RA Kumagai A., Oishi Y., Yamamoto S., Ono Y., Komori Y., Yamazaki M., RA Kisu Y., Nishikawa T., Sugano S., Nomura N., Isogai T.; RT "NEDO human cDNA sequencing project focused on splicing variants."; 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; AK299904; BAG61745.1; -; mRNA. DR UniGene; Hs.498187; -. DR ProteinModelPortal; B4DST3; -. DR SMR; B4DST3; 370-514, 518-1117. DR UCSC; uc010pxy.2; human. DR HOGENOM; HOG000251409; -. DR HOVERGEN; HBG006347; -. DR NextBio; 35474754; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 2: Evidence at transcript level; SQ SEQUENCE 1118 AA; 124077 MW; 6CEE61312C4FB444 CRC64; MSPALQDLSQ PEGLKKTLRD EINAILQKRI MVLDGGMGTM IQREKLNEEH FRGQEFKDHA RPLKGNNDIL SITQPDVIYQ IHKEYLLAGA DIIETNTFSS TSIAQADYGL EHLAYRMNMC SAGVARKAAE EVTLQTGIKR FVAGALGPTN KTLSVSPSVE RPDYRNITFD ELVEAYQEQA KGLLDGGVDI LLIETIFDTA NAKAALFALQ NLFEEKYAPR PIFISGTIVD KSGRTLSGQT GEGFVISVSH GEPLCIGLNC ALGAAEMRPF IEIIGKCTTA YVLCYPNAGL PNTFGDYDET PSMMAKHLKD FAMDGLVNIV GGCCGSTPDH IREIAEAVKN CKPRVPPATA FEGHMLLSGL EPFRIGPYTN FVNIGERCNV AGSRKFAKLI MAGNYEEALC VAKVQVEMGA QVLDVNMDDG MLDGPSAMTR FCNLIASEPD IAKVPLCIDS SNFAVIEAGL KCCQGKCIVN SISLKEGEDD FLEKARKIKK YGAAMVVMAF DEEGQTQGTG GKKVIQTDEW RNGPVEERLE YALVKGIEKH IIEDTEEARL NQKKYPRPLN IIEGPLMNGM KIVGDLFGAG KMFLPQVIKS ARVMKKAVGH LIPFMEKERE ETRVLNGTVE EEDPYQGTIV LATVKGDVHD IGKNIVGVVL GCNNFRVIDL GVMTPCDKIL KAALDHKADI IGLSGLITPS LDEMIFVAKE MERLAIRIPL LIGGATTSKT HTAVKIAPRY SAPVIHVLDA SKSVVVCSQL LDENLKDEYF EEIMEEYEDI RQDHYESLKE RRYLPLSQAR KSGFQMDWLS EPHPVKPTFI GTQVFEDYDL QKLVDYIDWK PFFDVWQLRG KYPNRGFPKI FNDKTVGGEA RKVYDDAHNM LNTLISQKKL RARGVVGFWP AQSIQDDIHL YAEAAVPQAA EPIATFYGLR QQAEKDSAST EPYYCLSDFI APLHSGIRDY LGLFAVACFG VEELSKAYED DGDDYSSIMV KALGDRLAEA FAEELHERVR RELWAYCGSE QLDVADLRRL RYKGIRPAPG YPSQPDHTEK LTMWRLADIE QSTGIRLTES LAMAPASAVS GLYFSNLKSK YFAVGKISKD QVEDYALRKN ISVAEVEKCM SVYRKIGE // ID B4E1C7_HUMAN Unreviewed; 203 AA. AC B4E1C7; E7EQJ7; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 27-MAY-2015, entry version 39. DE SubName: Full=cDNA FLJ50349, moderately similar to Betaine--homocysteine S-methyltransferase (EC 2.1.1.5) {ECO:0000313|EMBL:BAG64739.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG64739.1}; RN [1] {ECO:0000313|EMBL:BAG64739.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Liver {ECO:0000313|EMBL:BAG64739.1}; RA Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., RA Sugiyama A., Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., RA Kumagai A., Oishi Y., Yamamoto S., Ono Y., Komori Y., Yamazaki M., RA Kisu Y., Nishikawa T., Sugano S., Nomura N., Isogai T.; RT "NEDO human cDNA sequencing project focused on splicing variants."; 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; AK303780; BAG64739.1; -; mRNA. DR UniGene; Hs.80756; -. DR ProteinModelPortal; B4E1C7; -. DR SMR; B4E1C7; 10-122. DR PRIDE; B4E1C7; -. DR NextBio; 35476993; -. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. PE 2: Evidence at transcript level; KW Methyltransferase {ECO:0000313|EMBL:BAG64739.1}; KW Transferase {ECO:0000313|EMBL:BAG64739.1}. SQ SEQUENCE 203 AA; 21738 MW; 19D78198C4D31C70 CRC64; MPPVGGKKAK KGILERLNAG EIVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAGASII GVNCHFDPTI SLKTVKLMKE GLEAARLKAH LMSQPLAYHT PDCNKQGFID LPEFPFGLEP ELPPDGIFKN TPERPTTWGS GTLAGAVDLS PTTSGQLQRS WPQKGAFCHQ LQKNMAAGEV VWTCTPNPGL EQGPGRNTGR IFG // ID B4E9N2_BURCJ Unreviewed; 355 AA. AC B4E9N2; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:CAR50991.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAR50991.1}; GN Name=metH2 {ECO:0000313|EMBL:CAR50991.1}; GN ORFNames=BCAL0682 {ECO:0000313|EMBL:CAR50991.1}; 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 {ECO:0000313|EMBL:CAR50991.1, ECO:0000313|Proteomes:UP000001035}; RN [1] {ECO:0000313|EMBL:CAR50991.1, ECO:0000313|Proteomes:UP000001035} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / RC CF5610 {ECO:0000313|Proteomes:UP000001035}; 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; AM747720; CAR50991.1; -; Genomic_DNA. DR RefSeq; WP_006489099.1; NC_011000.1. DR RefSeq; YP_002229840.1; NC_011000.1. DR STRING; 216591.BCAL0682; -. DR EnsemblBacteria; CAR50991; CAR50991; BCAL0682. DR GeneID; 6933813; -. DR KEGG; bcj:BCAL0682; -. DR PATRIC; 19073077; VBIBurCen118154_0715. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; BCEN216591:GJI4-710-MONOMER; -. DR Proteomes; UP000001035; Chromosome 1. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001035}; KW Methyltransferase {ECO:0000313|EMBL:CAR50991.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001035}; KW Transferase {ECO:0000313|EMBL:CAR50991.1}. SQ SEQUENCE 355 AA; 38195 MW; FC5D19655A945C6C CRC64; MSETPLAASA PLDARYTRGA ALPALLKSRI LILDGAMGTM IQRYKLDEAA YRGERFKDFP RDIKGNNELL SLTQPQIIRE IHDQYFAAGA DIVETNTFGA TTVAQADYGM EDLVVEMNVA SAKLARESAA KYATPDKPRF VAGAIGPTPK TASISPDVND PGARNVTFDE LRTAYYQQAK ALLDGGVDLF LVETIFDTLN AKAALFALDE LFEDTGERLP IMISGTVTDA SGRILSGQTV EAFWNSLRHA KPLTFGLNCA LGAALMRPYI AELAKLCDTY VSCYPNAGLP NPMSDTGFDE TPDVTSGLLK EFAQAGLVNL AGGCCGTTPE HIAEIAKALA GVKPRRWPNQ YSDNA // ID B4EYS2_PROMH Unreviewed; 1223 AA. AC B4EYS2; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 27-MAY-2015, entry version 50. DE SubName: Full=Methionine synthase (5-methyltetrahydrofolate--homocysteine methyltransferase) {ECO:0000313|EMBL:CAR45437.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAR45437.1}; GN Name=metH {ECO:0000313|EMBL:CAR45437.1}; GN OrderedLocusNames=PMI2758 {ECO:0000313|EMBL:CAR45437.1}; OS Proteus mirabilis (strain HI4320). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Proteus. OX NCBI_TaxID=529507 {ECO:0000313|Proteomes:UP000008319}; RN [1] {ECO:0000313|EMBL:CAR45437.1, ECO:0000313|Proteomes:UP000008319} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HI4320 {ECO:0000313|EMBL:CAR45437.1, RC ECO:0000313|Proteomes:UP000008319}; 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.; RT "Complete genome sequence of uropathogenic Proteus mirabilis, a master RT of both adherence and motility."; RL J. Bacteriol. 190:4027-4037(2008). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AM942759; CAR45437.1; -; Genomic_DNA. DR RefSeq; WP_012368495.1; NC_010554.1. DR RefSeq; YP_002152459.1; NC_010554.1. DR STRING; 529507.PMI2758; -. DR EnsemblBacteria; CAR45437; CAR45437; PMI2758. DR GeneID; 6800225; -. DR KEGG; pmr:PMI2758; -. DR PATRIC; 20520176; VBIProMir120933_2687. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PMIR529507:GJIW-2807-MONOMER; -. DR Proteomes; UP000008319; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008319}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAR45437.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008319}; KW Transferase {ECO:0000313|EMBL:CAR45437.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 756 756 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1223 AA; 135456 MW; 1643D5C2C2A19D24 CRC64; MITQQLTQAL AKRILVLDGA MGTMIQQYQL AEEDYRGERF AHWQCDVKGN NDLLVLTQPQ IITEIHNAYF EAGADIVETN TFNATSIAMA DYQMEGLCAE LNEEAAKLAR ACADKWSALT PDKPRYVAGV LGPTNRTASI SPDVNDPAFR NISFDTLVMA YREAICGLIK GGVDLIMVET IFDTLNAKAA IFAIKCEFDN LNIELPVMIS GTITDASGRT LTGQTTEAFY HSLRHADALS FGLNCALGPK ELRQYIQTLS QISETYVSAH PNAGLPNAFG GYDLDANEMA EQIKEWAQAG FLNIVGGCCG TTPAHIQAIA QAVDGIAPRT LPVIKKACRL SGLEPLVIDD NSLFVNVGER TNVTGSAKFK RLIKEGNYQE ALDVARQQVE NGAQIIDINM DEGMLDAIEA MTRFLNLIAG EPDIAKVPIM IDSSKWQVIE EGLKCIQGKG IVNSISMKEG EALFIEHAKL VRKYGAAVVV MAFDEIGQAD TRERKIKICR RAYYLLTEKA GFPPEDIIFD PNIFAVATGI AEHNNYAVDF IEVCADIKSQ LPYALISGGV SNVSFSFRGN DPVREAIHSV FLYYAVKNGM DMGIVNAGQL AIYDSLPDEL RNAVEDVILN RHAESTDNLL ALAERYRGTK SEEQHSTLAQ WRQWEVEKRL EYALVKGITE FIIEDTEACR QQASSPIEVI EGPLMNGMNT VGDLFGEGKM FLPQVVKSAR VMKQAVAYLE PYIQATKKAG SSAGKVLLAT VKGDVHDIGK NIVGVVLQCN NYEIIDLGVM VPCDKILQTA IDENVDIIGL SGLITPSLDE MVNVAKEMER RGFSLPLMIG GATTSKAHTA VKIEPNYSHP TVYVQNASRT VGVVAALLSA TQKADFVAKT RHEYEVVRQQ YARKKPRTPP VSLATARANA LQLDWQHYTP PKPNQLGVQQ VTANIETLRK YIDWTPFFMT WSLAGKYPRI LEDEVVGEEA RRVFADANAM LDKLSREKLL TPKGIVGLFP ANRLGDDIII YQDETRQHEL LRCCHLRQQT EKKEYPNYCL ADFIAPVDSG LADYFGAFAV TGGLEEDALA NGYDNAHDDY NKIMVKALSD RLAEAFAEYL HQQVRTKIWG YSPDEALSND ELIREKYQGT RPAPGYPACP EHTEKAKIWQ LLNVENRIGM KLTDAYAMWP GASVSGWYFS HPESKYFAVA QIQKDQVEDY AKRRGMSISE VERWLAPNLG YEP // ID B4FK22_MAIZE Unreviewed; 323 AA. AC B4FK22; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 27-MAY-2015, entry version 32. DE SubName: Full=Homocysteine S-methyltransferase 1 {ECO:0000313|EMBL:ACG43181.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ACF82465.1}; 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 {ECO:0000313|EMBL:ACF82465.1}; RN [1] {ECO:0000313|EMBL:ACG43181.1} 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). RN [2] {ECO:0000313|EMBL:ACF82465.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=B73 {ECO:0000313|EMBL:ACF82465.1}; 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; BT037460; ACF82465.1; -; mRNA. DR EMBL; BT037580; ACF82585.1; -; mRNA. DR EMBL; EU971063; ACG43181.1; -; mRNA. DR RefSeq; NP_001105011.1; NM_001111541.1. DR UniGene; Zm.13424; -. DR ProteinModelPortal; B4FK22; -. DR GeneID; 541873; -. DR KEGG; zma:541873; -. DR Gramene; B4FK22; -. DR KO; K00547; -. DR ExpressionAtlas; B4FK22; baseline and differential. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Methyltransferase {ECO:0000313|EMBL:ACG43181.1}; KW Transferase {ECO:0000313|EMBL:ACG43181.1}. SQ SEQUENCE 323 AA; 34927 MW; 1B1B8F19DA0B743D CRC64; MGVLEDLVAR AGGCAVIDGG FATQLEALGA DINDPLWSAA CLITRPHLVK EVHMQYLEAG ADVIISSSYQ ATIPGFIARG MSVAEAEDLL RTSVKLANEA RDEFWKSTLR KSKPIYNRAL VAASIGSYGA YLADGSEYSG SYGADITAEK LKDFHRRRLQ VLASAGPDLI AFEAIPNQME AQALVELLEE EKVQIPSWIC FSSVDGKNLC SGESFADCLK ILNASEKVAV VGVNCTPPQF IEGIICEFRK QTKKAIAVYP NSGEVWDGRA KRWLPVECLG HKSFDALAKR WQEAGASLIG GCCRTTPSTI RAVSKILKGR TGH // ID B4G7F5_DROPE Unreviewed; 349 AA. AC B4G7F5; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 07-JAN-2015, entry version 35. DE SubName: Full=GL19625 {ECO:0000313|EMBL:EDW29288.1}; GN Name=Dper\GL19625 {ECO:0000313|EMBL:EDW29288.1}; GN ORFNames=Dper_GL19625 {ECO:0000313|EMBL:EDW29288.1}, GN GL19625 {ECO:0000313|FlyBase:FBgn0157223}; OS Drosophila persimilis (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7234 {ECO:0000313|Proteomes:UP000008744}; RN [1] {ECO:0000313|EMBL:EDW29288.1, ECO:0000313|Proteomes:UP000008744} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MSH-3 / Tucson 14011-0111.49 RC {ECO:0000313|Proteomes:UP000008744}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 genomes consortium; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(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; CH479180; EDW29288.1; -; Genomic_DNA. DR RefSeq; XP_002015292.1; XM_002015256.1. DR EnsemblMetazoa; FBtr0185240; FBpp0183732; FBgn0157223. DR GeneID; 6589403; -. DR KEGG; dpe:Dper_GL19625; -. DR FlyBase; FBgn0157223; Dper\GL19625. DR KO; K00547; -. DR OrthoDB; EOG7GQXW0; -. DR PhylomeDB; B4G7F5; -. DR Proteomes; UP000008744; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008744}; KW Reference proteome {ECO:0000313|Proteomes:UP000008744}. SQ SEQUENCE 349 AA; 38684 MW; C1E1804946433AFD CRC64; MYAFEEENEN QNRPEQPRVL VKCGGFSSQL AHNVDEKVDG DPLWGSRFDA TNPQAVIKTH LDFLRSGADI ILTNTYQSSV EGFMKYLALT REQSVALIEK SVHLTQQAKA QYLKEILQSG EIIKPFFPLI LASIGPYGAH LHDGSEYSGS YADKISKEKL QDWHRTRIET CLLAGVDGLA AETLPCQLEA LAITESILEN YTNVKFWVSF QCKDDTSLAD GESFAEAALA VWRMVQAYKA QTRLLGIGVN CVNPTFVTPL LRSLNAAAGL DRIPLVVYSN RGEIYDSVRG EWTGTGEDVA KFVPEWVRLG ARVVGGCCRV YPDDVLKIRK CVDSLNIGYS AESPQSHIV // ID B4G7F6_DROPE Unreviewed; 331 AA. AC B4G7F6; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 27-MAY-2015, entry version 38. DE SubName: Full=GL19626 {ECO:0000313|EMBL:EDW29289.1}; GN Name=Dper\GL19626 {ECO:0000313|EMBL:EDW29289.1}; GN ORFNames=Dper_GL19626 {ECO:0000313|EMBL:EDW29289.1}, GN GL19626 {ECO:0000313|FlyBase:FBgn0157224}; OS Drosophila persimilis (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7234 {ECO:0000313|Proteomes:UP000008744}; RN [1] {ECO:0000313|EMBL:EDW29289.1, ECO:0000313|Proteomes:UP000008744} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MSH-3 / Tucson 14011-0111.49 RC {ECO:0000313|Proteomes:UP000008744}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 genomes consortium; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(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; CH479180; EDW29289.1; -; Genomic_DNA. DR RefSeq; XP_002015293.1; XM_002015257.1. DR ProteinModelPortal; B4G7F6; -. DR EnsemblMetazoa; FBtr0185241; FBpp0183733; FBgn0157224. DR GeneID; 6589404; -. DR KEGG; dpe:Dper_GL19626; -. DR FlyBase; FBgn0157224; Dper\GL19626. DR KO; K00547; -. DR OrthoDB; EOG7GQXW0; -. DR PhylomeDB; B4G7F6; -. DR Proteomes; UP000008744; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008744}; KW Reference proteome {ECO:0000313|Proteomes:UP000008744}. SQ SEQUENCE 331 AA; 36719 MW; 72BFDE1E984E8CA6 CRC64; MGLTRVLVKD GGFGTQMTVH VGNSVDGDPL WSARFNATNP AAIINTHLDF LQNGADIILT NTYQASVEGY MEYLELDEDQ SIELIRNTVR LAHIAKEKYL TECYQAQLAV PEGYPLIIAS IGPFGAHLHD GSEYTGSYAD YVPAKTITDW HRIRIEACLE AGVDALAIET IPCQMEAEAL VEMLCDDYPD VKFWVAFQCK DESTLAHGET FADAANAIWD MLAERNAQDK CLAVGVNCVH PKFVTSLFKS LNGDRSVEDQ IPLVVYPNSG EVYDVVKGWE GREHCVPLAN YVPEWSQLGA KIIGGCCRTY ARDIRHIGEA IRNWNKLKKV A // ID B4I5M7_DROSE Unreviewed; 331 AA. AC B4I5M7; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 07-JAN-2015, entry version 34. DE SubName: Full=GM17050 {ECO:0000313|EMBL:EDW55683.1}; GN Name=Dsec\GM17050 {ECO:0000313|EMBL:EDW55683.1}; GN ORFNames=Dsec_GM17050 {ECO:0000313|EMBL:EDW55683.1}, GN GM17050 {ECO:0000313|FlyBase:FBgn0171962}; OS Drosophila sechellia (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7238 {ECO:0000313|Proteomes:UP000001292}; RN [1] {ECO:0000313|EMBL:EDW55683.1, ECO:0000313|Proteomes:UP000001292} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Rob3c / Tucson 14021-0248.25 RC {ECO:0000313|Proteomes:UP000001292}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 genomes consortium; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(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; CH480822; EDW55683.1; -; Genomic_DNA. DR RefSeq; XP_002039037.1; XM_002039001.1. DR EnsemblMetazoa; FBtr0200035; FBpp0198527; FBgn0171962. DR GeneID; 6614609; -. DR KEGG; dse:Dsec_GM17050; -. DR FlyBase; FBgn0171962; Dsec\GM17050. DR KO; K00547; -. DR OrthoDB; EOG7GQXW0; -. DR PhylomeDB; B4I5M7; -. DR Proteomes; UP000001292; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001292}; KW Reference proteome {ECO:0000313|Proteomes:UP000001292}. SQ SEQUENCE 331 AA; 36779 MW; D573A8D48FC03D19 CRC64; MGLTRVLVKD GGFGTQMTVH VGDSVDGDPL WSARFNATNP AAIISTHLDF LQNGADIILT NTYQSSVDGY MEYMELDEEQ SIELIKNTVR LAHIAKERYL SECYQEQLSV QEGYPLIIAS IGPFGAHLHD GSEYTGSYAD FVPAKEITDW HRGRIEACLE AGVDALAIET IPCQMEAEAL VEMLCDDYPD VKFWVAFQCK DEKTLAHGET FSDAANAIWD LLAERNAQDK CLAIGVNCVH PKFVTPLFKS LNGDREVGEQ IPLVVYPNSG EVYDVVNGWQ GREHCVPLAN YVPEWAQLGA KVIGGCCRTY ARDVRHIGEA IRDWNKLKKV S // ID B4I5M8_DROSE Unreviewed; 331 AA. AC B4I5M8; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 07-JAN-2015, entry version 34. DE SubName: Full=GM17049 {ECO:0000313|EMBL:EDW55684.1}; GN Name=Dsec\GM17049 {ECO:0000313|EMBL:EDW55684.1}; GN ORFNames=Dsec_GM17049 {ECO:0000313|EMBL:EDW55684.1}, GN GM17049 {ECO:0000313|FlyBase:FBgn0171961}; OS Drosophila sechellia (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7238 {ECO:0000313|Proteomes:UP000001292}; RN [1] {ECO:0000313|EMBL:EDW55684.1, ECO:0000313|Proteomes:UP000001292} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Rob3c / Tucson 14021-0248.25 RC {ECO:0000313|Proteomes:UP000001292}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 genomes consortium; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(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; CH480822; EDW55684.1; -; Genomic_DNA. DR RefSeq; XP_002039038.1; XM_002039002.1. DR EnsemblMetazoa; FBtr0200034; FBpp0198526; FBgn0171961. DR GeneID; 6614610; -. DR KEGG; dse:Dsec_GM17049; -. DR FlyBase; FBgn0171961; Dsec\GM17049. DR KO; K00547; -. DR OrthoDB; EOG7GQXW0; -. DR PhylomeDB; B4I5M8; -. DR Proteomes; UP000001292; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001292}; KW Reference proteome {ECO:0000313|Proteomes:UP000001292}. SQ SEQUENCE 331 AA; 36541 MW; F00B466F50D19BA6 CRC64; MEVNQKWNWD SKPILVKCGG FSSQLAKNVT EKVDGDPLWG SRFDATNPEA VIQTHLDFLR NGADIILTNT YQSSVEGFVK YLGVTRERGV ELIQKSVQLA KQAKEQYLSE IGSEADSALP LIMGSIGPYG AYLHDGSEYT GNYADKMSKE QLKAWHTARI EICLAAGVDG LALETLPCLM EAEAVTELVL DNFPDAKFWV SLQCMDEKHM ASGESFAEAA LSLWRLVQSR KAENRLLGIG LNCVNPLFVT PLLSSLTKVA GSDRIPLVVY SNRGEIYDVE QGDWTGTGEE VVKFVPEWIQ LGVRIVGGCC RVYPTDVLAI RKYVDGLNIK P // ID B4JBY1_DROGR Unreviewed; 349 AA. AC B4JBY1; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 07-JAN-2015, entry version 38. DE SubName: Full=GH11601 {ECO:0000313|EMBL:EDW04084.1}; GN Name=Dgri\GH11601 {ECO:0000313|EMBL:EDW04084.1}; GN ORFNames=Dgri_GH11601 {ECO:0000313|EMBL:EDW04084.1}, GN GH11601 {ECO:0000313|FlyBase:FBgn0119081}; OS Drosophila grimshawi (Fruit fly) (Idiomyia grimshawi). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Hawaiian Drosophila. OX NCBI_TaxID=7222 {ECO:0000313|Proteomes:UP000001070}; RN [1] {ECO:0000313|EMBL:EDW04084.1, ECO:0000313|Proteomes:UP000001070} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tucson 15287-2541.00 {ECO:0000313|Proteomes:UP000001070}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 genomes consortium; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(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; CH916368; EDW04084.1; -; Genomic_DNA. DR RefSeq; XP_001989217.1; XM_001989181.1. DR STRING; 7222.FBpp0145507; -. DR EnsemblMetazoa; FBtr0147015; FBpp0145507; FBgn0119081. DR GeneID; 6561867; -. DR KEGG; dgr:Dgri_GH11601; -. DR FlyBase; FBgn0119081; Dgri\GH11601. DR eggNOG; COG2040; -. DR InParanoid; B4JBY1; -. DR KO; K00547; -. DR OMA; SSVEGFM; -. DR OrthoDB; EOG7GQXW0; -. DR PhylomeDB; B4JBY1; -. DR Proteomes; UP000001070; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001070}; KW Reference proteome {ECO:0000313|Proteomes:UP000001070}. SQ SEQUENCE 349 AA; 38466 MW; 06F170C4600FCAD4 CRC64; MLPATIGKWN VEKAERILVK CGGFSSQLAR NVNEKVDGDP LWGSRFDCTQ PTAVVKTHLD FLRNGADIIL TNTYQSSVEG FMKHLGKTRE ESIALIAKSV QLAHDAKSEY LAELAAANNG NIDADMPWIL ASIGPYGAHL HDGSEYQGSY ANRVNYEQLQ QWHTTRIDTC LLAGVDGLAV ETLPCQLEAL AVTELILKRS TTAKFWVSFQ CKDELHLAHG ESFAGAALAV WRLVQQHEAQ SRLLAIGVNC VNPSYVTPLI ESLRATMAQE QLPPLVIYSN RGEVYDAERG EWTGTGLNAI SFVPQWLQLG ARIIGGCCRV YPDDILEIRK YIDSIAQQPQ AQIQTSSVP // ID B4JBY2_DROGR Unreviewed; 328 AA. AC B4JBY2; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 07-JAN-2015, entry version 37. DE SubName: Full=GH11602 {ECO:0000313|EMBL:EDW04085.1}; GN Name=Dgri\GH11602 {ECO:0000313|EMBL:EDW04085.1}; GN ORFNames=Dgri_GH11602 {ECO:0000313|EMBL:EDW04085.1}, GN GH11602 {ECO:0000313|FlyBase:FBgn0119082}; OS Drosophila grimshawi (Fruit fly) (Idiomyia grimshawi). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Hawaiian Drosophila. OX NCBI_TaxID=7222 {ECO:0000313|Proteomes:UP000001070}; RN [1] {ECO:0000313|EMBL:EDW04085.1, ECO:0000313|Proteomes:UP000001070} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tucson 15287-2541.00 {ECO:0000313|Proteomes:UP000001070}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 genomes consortium; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(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; CH916368; EDW04085.1; -; Genomic_DNA. DR RefSeq; XP_001989218.1; XM_001989182.1. DR STRING; 7222.FBpp0145508; -. DR EnsemblMetazoa; FBtr0147016; FBpp0145508; FBgn0119082. DR GeneID; 6561868; -. DR KEGG; dgr:Dgri_GH11602; -. DR FlyBase; FBgn0119082; Dgri\GH11602. DR eggNOG; COG2040; -. DR InParanoid; B4JBY2; -. DR KO; K00547; -. DR OMA; SEWCKDG; -. DR OrthoDB; EOG7GQXW0; -. DR PhylomeDB; B4JBY2; -. DR Proteomes; UP000001070; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001070}; KW Reference proteome {ECO:0000313|Proteomes:UP000001070}. SQ SEQUENCE 328 AA; 36682 MW; D0C6B7ADCF672833 CRC64; MVLTRLLVKD GGFGTQMTVH VGNSVDGDPL WSARFNATNP TAVINTHLDF LQNGADMILT NTYQTSVEGY MEYLELDEQE SIELIKNTVQ LAHVAKEKYL TECYEAQLEV NEGYPLIIAS IGPFGAHLHD GSEYTGEYAD YVAPKTITDW HRVRIEACLE AGVDALAIET IPCQMEAEAL VEMLCDDYPD VKFWVAFQCK DESRLAHGEE FADAANAIWD ILRERKALDN CLAVGVNCVH PKFVTPLFKS LNGERSVEEQ IPLVVYPNSG EVYDVTTGWQ GREHCVPLEK YVPEWAQLGA KIIGGCCRTY ARDIRHISEA VHAINNHK // ID B4KJP8_DROMO Unreviewed; 349 AA. AC B4KJP8; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 07-JAN-2015, entry version 33. DE SubName: Full=GI17170 {ECO:0000313|EMBL:EDW11493.1}; GN Name=Dmoj\GI17170 {ECO:0000313|EMBL:EDW11493.1}; GN ORFNames=Dmoj_GI17170 {ECO:0000313|EMBL:EDW11493.1}, GN GI17170 {ECO:0000313|FlyBase:FBgn0139914}; OS Drosophila mojavensis (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7230 {ECO:0000313|Proteomes:UP000009192}; RN [1] {ECO:0000313|EMBL:EDW11493.1, ECO:0000313|Proteomes:UP000009192} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tucson 15081-1352.22 {ECO:0000313|Proteomes:UP000009192}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 genomes consortium; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(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; CH933807; EDW11493.1; -; Genomic_DNA. DR RefSeq; XP_002002051.1; XM_002002015.1. DR EnsemblMetazoa; FBtr0167895; FBpp0166387; FBgn0139914. DR GeneID; 6576048; -. DR KEGG; dmo:Dmoj_GI17170; -. DR FlyBase; FBgn0139914; Dmoj\GI17170. DR InParanoid; B4KJP8; -. DR KO; K00547; -. DR OMA; SSVEGFM; -. DR OrthoDB; EOG7GQXW0; -. DR PhylomeDB; B4KJP8; -. DR Proteomes; UP000009192; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009192}; KW Reference proteome {ECO:0000313|Proteomes:UP000009192}. SQ SEQUENCE 349 AA; 38531 MW; 90A64847E39BD447 CRC64; MMPEFTGNWH QHKEKPRILV KCGGFSSQLA RNVNEKVDGD PLWGSRFDAT QPDAVIQTHL DFLRKGADII LTNTYQSSVE GFMKHLGKTR EESIALIAKS VELARQARTK YLSEVAANNG DIGPDMPWIL ASIGPYGAHL HDGSEYTGSY ANLVNFSQLQ AWHKPRIDTC LSAGIDGLAV ETLPCQLEAL AVTDLLLTCY CTPRFWVSFQ CKDSSSLAHG ESFAEAALAV WNMVVKHKAQ SRLLGIGVNC VNPNYVTPLL KSLLAKLPHG VTVPLVVYSN RGEIYDSDRG EWTGNGLNVA SFVPEWLRLG ARIIGGCCRV YPDDIYEIRQ TIEDIAQQPQ SPIQTSLVM // ID B4KJP9_DROMO Unreviewed; 331 AA. AC B4KJP9; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 07-JAN-2015, entry version 33. DE SubName: Full=GI17171 {ECO:0000313|EMBL:EDW11494.1}; GN Name=Dmoj\GI17171 {ECO:0000313|EMBL:EDW11494.1}; GN ORFNames=Dmoj_GI17171 {ECO:0000313|EMBL:EDW11494.1}, GN GI17171 {ECO:0000313|FlyBase:FBgn0139915}; OS Drosophila mojavensis (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7230 {ECO:0000313|Proteomes:UP000009192}; RN [1] {ECO:0000313|EMBL:EDW11494.1, ECO:0000313|Proteomes:UP000009192} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tucson 15081-1352.22 {ECO:0000313|Proteomes:UP000009192}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 genomes consortium; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(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; CH933807; EDW11494.1; -; Genomic_DNA. DR RefSeq; XP_002002052.1; XM_002002016.1. DR EnsemblMetazoa; FBtr0167896; FBpp0166388; FBgn0139915. DR GeneID; 6576049; -. DR KEGG; dmo:Dmoj_GI17171; -. DR FlyBase; FBgn0139915; Dmoj\GI17171. DR InParanoid; B4KJP9; -. DR KO; K00547; -. DR OMA; SEWCKDG; -. DR OrthoDB; EOG7GQXW0; -. DR PhylomeDB; B4KJP9; -. DR Proteomes; UP000009192; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009192}; KW Reference proteome {ECO:0000313|Proteomes:UP000009192}. SQ SEQUENCE 331 AA; 36899 MW; DA69CA8114DC861A CRC64; MGLTRVLVKD GGFGTQMTVH VGNSVDGDPL WSARFNATNP TAVINTHLDF LQNGADLVLT NTYQTSVEGY MEYLELDEQE SVELIKNTVR LAHIAKEKYL TECYEAQLEI HEGYPLIIAS IGPFGAHLHD GSEYTGSYAD YVPAKTITDW HRVRIEACLE AGVDALAIET IPCQMEAEAL VEMLCDDYPD VKFWVAFQCK DESTLAHGED FADAVNAIWD LLAERKALDK CLAVGVNCVH PKFVTPLFKS LNGERSPDEQ IPLVVYPNSG EVYDVTTGWQ GREHCVPLEN YVPEWTQLGA KIIGGCCRTY ARDIRRISEA VHDINKLKKL V // ID B4LSJ6_DROVI Unreviewed; 350 AA. AC B4LSJ6; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 07-JAN-2015, entry version 39. DE SubName: Full=GJ17676 {ECO:0000313|EMBL:EDW64818.1}; GN Name=Dvir\GJ17676 {ECO:0000313|EMBL:EDW64818.1}; GN ORFNames=Dvir_GJ17676 {ECO:0000313|EMBL:EDW64818.1}, GN GJ17676 {ECO:0000313|FlyBase:FBgn0204845}; OS Drosophila virilis (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7244 {ECO:0000313|Proteomes:UP000008792}; RN [1] {ECO:0000313|EMBL:EDW64818.1, ECO:0000313|Proteomes:UP000008792} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tucson 15010-1051.87 {ECO:0000313|Proteomes:UP000008792}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 genomes consortium; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(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; CH940649; EDW64818.1; -; Genomic_DNA. DR RefSeq; XP_002052663.1; XM_002052627.1. DR STRING; 7244.FBpp0232093; -. DR EnsemblMetazoa; FBtr0233601; FBpp0232093; FBgn0204845. DR GeneID; 6627938; -. DR KEGG; dvi:Dvir_GJ17676; -. DR FlyBase; FBgn0204845; Dvir\GJ17676. DR eggNOG; COG2040; -. DR InParanoid; B4LSJ6; -. DR KO; K00547; -. DR OMA; SSVEGFM; -. DR OrthoDB; EOG7GQXW0; -. DR PhylomeDB; B4LSJ6; -. DR Proteomes; UP000008792; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008792}; KW Reference proteome {ECO:0000313|Proteomes:UP000008792}. SQ SEQUENCE 350 AA; 38436 MW; EE0F0B1575E74AB1 CRC64; MLPAFTGNWN QVKEKPRVLV KCGGFSSQLA RNVQEKVDGD PLWGSRFDAT QPAAVVKTHL DFLRNGADII LTNTYQSSVE GFMKHLGKSR EESIELIAKS VHLARQAKSQ HLGELATSNG NIAPDMPWIM ASIGPYGAHL HDGSEYAGSY ANLVNFTQLQ QWHTVRIDTC LSAGVDGLAV ETLPCQLEAM AVTELILSRY ATARFWVSFQ CKDASSLAHG ESFAQAAMAV WRLVQEFKAQ SRLLGIGVNC VNPSYVTPLL KSLLAITPPD EKIPLVVYSN RGEIYDSERG EWTGNGLNVT SFVPEWLQLG ARIIGGCCRV YPDDILEIRN TIDKIAQQPD SPIQTSLVSC // ID B4LSJ7_DROVI Unreviewed; 331 AA. AC B4LSJ7; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 07-JAN-2015, entry version 38. DE SubName: Full=GJ17677 {ECO:0000313|EMBL:EDW64819.1}; GN Name=Dvir\GJ17677 {ECO:0000313|EMBL:EDW64819.1}; GN ORFNames=Dvir_GJ17677 {ECO:0000313|EMBL:EDW64819.1}, GN GJ17677 {ECO:0000313|FlyBase:FBgn0204846}; OS Drosophila virilis (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7244 {ECO:0000313|Proteomes:UP000008792}; RN [1] {ECO:0000313|EMBL:EDW64819.1, ECO:0000313|Proteomes:UP000008792} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tucson 15010-1051.87 {ECO:0000313|Proteomes:UP000008792}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 genomes consortium; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(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; CH940649; EDW64819.1; -; Genomic_DNA. DR RefSeq; XP_002052664.1; XM_002052628.1. DR STRING; 7244.FBpp0232094; -. DR EnsemblMetazoa; FBtr0233602; FBpp0232094; FBgn0204846. DR GeneID; 6627939; -. DR KEGG; dvi:Dvir_GJ17677; -. DR FlyBase; FBgn0204846; Dvir\GJ17677. DR eggNOG; COG2040; -. DR InParanoid; B4LSJ7; -. DR KO; K00547; -. DR OMA; SEWCKDG; -. DR OrthoDB; EOG7GQXW0; -. DR PhylomeDB; B4LSJ7; -. DR Proteomes; UP000008792; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008792}; KW Reference proteome {ECO:0000313|Proteomes:UP000008792}. SQ SEQUENCE 331 AA; 36822 MW; 93AA7F19A1A49268 CRC64; MGSTRLLVKD GGFGTQMTVH VGNSVDGDPL WSARFNATNP TAVINTHLDF LQNGADMILT NTYQTSVEGY MEYLELDEQE SIELIKNTVR LAHIAKEKYL TECYEAQLAV PEGFPLIIAS IGPFGAHLHD GSEYTGSYAD YVEPKTITDW HRVRIEACLE AGVDALAIET IPCQMEAEAL VEMLCDDYPE VKFWVAFQCK DESTLAHGED FAEAANAIWD ILRERKALDK CLALGVNCVH PKFVTPLFKS LNGERTADEQ IPLVVYPNSG EVYDVTTGWQ GREHCVPLEN YVPEWTQLGA KIIGGCCRTY ARDIRRISEA VHAVNKLKKA A // ID B4MZM6_DROWI Unreviewed; 350 AA. AC B4MZM6; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 07-JAN-2015, entry version 38. DE SubName: Full=GK24683 {ECO:0000313|EMBL:EDW77811.1}; GN Name=Dwil\GK24683 {ECO:0000313|EMBL:EDW77811.1}; GN ORFNames=Dwil_GK24683 {ECO:0000313|EMBL:EDW77811.1}, GN GK24683 {ECO:0000313|FlyBase:FBgn0226643}; OS Drosophila willistoni (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7260 {ECO:0000313|Proteomes:UP000007798}; RN [1] {ECO:0000313|EMBL:EDW77811.1, ECO:0000313|Proteomes:UP000007798} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tucson 14030-0811.24 {ECO:0000313|Proteomes:UP000007798}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 genomes consortium; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(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; CH963920; EDW77811.1; -; Genomic_DNA. DR RefSeq; XP_002066825.1; XM_002066789.1. DR STRING; 7260.FBpp0253826; -. DR EnsemblMetazoa; FBtr0255334; FBpp0253826; FBgn0226643. DR GeneID; 6644153; -. DR KEGG; dwi:Dwil_GK24683; -. DR FlyBase; FBgn0226643; Dwil\GK24683. DR eggNOG; COG2040; -. DR InParanoid; B4MZM6; -. DR KO; K00547; -. DR OMA; SSVEGFM; -. DR OrthoDB; EOG7GQXW0; -. DR PhylomeDB; B4MZM6; -. DR Proteomes; UP000007798; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007798}; KW Reference proteome {ECO:0000313|Proteomes:UP000007798}. SQ SEQUENCE 350 AA; 38517 MW; 6B276C8C7661651A CRC64; MDADSSSSRI STDSNKNPCG HGIWESRGIL VKCGGFASQL SRNLGQKVDG HPLWSSRFDA SNPEAVIQTH LDFLHSGADI ILTNTYQSSV EGFMKHLQVT REQSIELIAQ SVKLALQAKD TYLKDLEEAE DTPCKNSRRD PIVLASIGPY GAHLHDGSEY TGDYSDQVQT ELLQKWHKVR IDTCLLNGVD GLAVETMPCL LEAKAVTELI LTSYSNVKFW VSFQCRDETS LANGESFAHA AHTIWRMVQD AGQESRLLAI GVNCVNPNFV SSLFKSLNSL AGPDRIPLIV YSNRGEIYDS ASGEWIGSGQ NVVEFVPEWI KLGARIVGGC CRVYPADIAR IRQCADSNHI // ID B4MZM7_DROWI Unreviewed; 331 AA. AC B4MZM7; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 07-JAN-2015, entry version 37. DE SubName: Full=GK24684 {ECO:0000313|EMBL:EDW77812.1}; GN Name=Dwil\GK24684 {ECO:0000313|EMBL:EDW77812.1}; GN ORFNames=Dwil_GK24684 {ECO:0000313|EMBL:EDW77812.1}, GN GK24684 {ECO:0000313|FlyBase:FBgn0226644}; OS Drosophila willistoni (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7260 {ECO:0000313|Proteomes:UP000007798}; RN [1] {ECO:0000313|EMBL:EDW77812.1, ECO:0000313|Proteomes:UP000007798} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tucson 14030-0811.24 {ECO:0000313|Proteomes:UP000007798}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 genomes consortium; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(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; CH963920; EDW77812.1; -; Genomic_DNA. DR RefSeq; XP_002066826.1; XM_002066790.1. DR STRING; 7260.FBpp0253827; -. DR EnsemblMetazoa; FBtr0255335; FBpp0253827; FBgn0226644. DR GeneID; 6644154; -. DR KEGG; dwi:Dwil_GK24684; -. DR FlyBase; FBgn0226644; Dwil\GK24684. DR eggNOG; COG2040; -. DR InParanoid; B4MZM7; -. DR KO; K00547; -. DR OMA; GEAIRNW; -. DR OrthoDB; EOG7GQXW0; -. DR PhylomeDB; B4MZM7; -. DR Proteomes; UP000007798; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007798}; KW Reference proteome {ECO:0000313|Proteomes:UP000007798}. SQ SEQUENCE 331 AA; 36708 MW; 9AA8DC4C4843A1C0 CRC64; MALSRVLVKD GGFGTQMTVH VGNSVDGDPL WSARFNSTNM SAVINTHLDF LQNGADIILT NTYQASVEGY MEYLELDEEQ SIELIKNTVR LAHIAKEKYL TECYEAKLAV PEGFPLIIAS IGPFGAHLHD GSEYTGSYAD FVPAKTITDW HRQRIEACVE AGVDALAIET IPCQMEAEAL VEMLCDDYPD VKFWVAFQCK DETSLAHGES FADAANSIWD ILSERNALDK CLAVGVNCVH PKFVTALFKS LNGERSVDEQ IPLVVYPNSG EVYDVLNGWQ GREHCVPLAN YVPEWAQLGA KIIGGCCRTY ARDIRHIGEA IRNWNKLKKN A // ID B4PAD4_DROYA Unreviewed; 331 AA. AC B4PAD4; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 07-JAN-2015, entry version 33. DE SubName: Full=GE12692 {ECO:0000313|EMBL:EDW90342.1}; GN Name=Dyak\GE12692 {ECO:0000313|EMBL:EDW90342.1}; GN ORFNames=Dyak_GE12692 {ECO:0000313|EMBL:EDW90342.1}, GN GE12692 {ECO:0000313|FlyBase:FBgn0230417}; OS Drosophila yakuba (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7245 {ECO:0000313|Proteomes:UP000002282}; RN [1] {ECO:0000313|EMBL:EDW90342.1, ECO:0000313|Proteomes:UP000002282} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 genomes consortium; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(2007). RN [2] {ECO:0000313|EMBL:EDW90342.1, ECO:0000313|Proteomes:UP000002282} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tai18E2 / Tucson 14021-0261.01 RC {ECO:0000313|Proteomes:UP000002282}; RX PubMed=17550304; DOI=10.1371/journal.pbio.0050152; RA Ranz J.M., Maurin D., Chan Y.S., von Grotthuss M., Hillier L.W., RA Roote J., Ashburner M., Bergman C.M.; RT "Principles of genome evolution in the Drosophila melanogaster species RT group."; RL PLoS Biol. 5:E152-E152(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; CM000158; EDW90342.1; -; Genomic_DNA. DR RefSeq; XP_002090630.1; XM_002090594.1. DR STRING; 7245.FBpp0257702; -. DR EnsemblMetazoa; FBtr0259210; FBpp0257702; FBgn0230417. DR GeneID; 6529636; -. DR KEGG; dya:Dyak_GE12692; -. DR FlyBase; FBgn0230417; Dyak\GE12692. DR eggNOG; COG2040; -. DR KO; K00547; -. DR OMA; QCKDENT; -. DR OrthoDB; EOG7GQXW0; -. DR PhylomeDB; B4PAD4; -. DR Proteomes; UP000002282; Chromosome 2R. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002282}. SQ SEQUENCE 331 AA; 36804 MW; 2553DB652FB007E2 CRC64; MGLTRVLLKD GGFGTQMTVH VGDSVDGDPL WSSRFNATNP AAIISTHLDF LQNGADIILT NTYQSSVDGY MEYLELDEEQ SIELIRNTVR LAHIAKERYL TECYQAQLAM PEGYPLIIAS IGPFGAHLHD GSEYTGSYAD YVPAKEITDW HRVRIEACLE AGVDALAIET IPCQMEAEAL VEMLCDDYPD VKFWVAFQCK DENTLAHGET FADATNAIWD LLAERNAQDK CLAIGVNCVH PKFVTPLFKS LNGDREVGEQ IPLVVYPNSG EVYDVVNGWQ GKEHCVPLAN YVPEWAQLGA KVIGGCCRTY ARDVRHIGEA IRDWNKLKKL S // ID B4PAD5_DROYA Unreviewed; 331 AA. AC B4PAD5; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 07-JAN-2015, entry version 33. DE SubName: Full=GE12691 {ECO:0000313|EMBL:EDW90343.1}; GN Name=Dyak\GE12691 {ECO:0000313|EMBL:EDW90343.1}; GN ORFNames=Dyak_GE12691 {ECO:0000313|EMBL:EDW90343.1}, GN GE12691 {ECO:0000313|FlyBase:FBgn0230416}; OS Drosophila yakuba (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7245 {ECO:0000313|Proteomes:UP000002282}; RN [1] {ECO:0000313|EMBL:EDW90343.1, ECO:0000313|Proteomes:UP000002282} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 genomes consortium; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(2007). RN [2] {ECO:0000313|EMBL:EDW90343.1, ECO:0000313|Proteomes:UP000002282} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tai18E2 / Tucson 14021-0261.01 RC {ECO:0000313|Proteomes:UP000002282}; RX PubMed=17550304; DOI=10.1371/journal.pbio.0050152; RA Ranz J.M., Maurin D., Chan Y.S., von Grotthuss M., Hillier L.W., RA Roote J., Ashburner M., Bergman C.M.; RT "Principles of genome evolution in the Drosophila melanogaster species RT group."; RL PLoS Biol. 5:E152-E152(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; CM000158; EDW90343.1; -; Genomic_DNA. DR RefSeq; XP_002090631.1; XM_002090595.1. DR STRING; 7245.FBpp0257701; -. DR EnsemblMetazoa; FBtr0259209; FBpp0257701; FBgn0230416. DR GeneID; 6529637; -. DR KEGG; dya:Dyak_GE12691; -. DR FlyBase; FBgn0230416; Dyak\GE12691. DR eggNOG; COG2040; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG7GQXW0; -. DR PhylomeDB; B4PAD5; -. DR Proteomes; UP000002282; Chromosome 2R. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002282}. SQ SEQUENCE 331 AA; 36622 MW; A3B979F8BE046AA2 CRC64; MKENQNWNWD TKPILVKCGG FSSQLARNVN EKVDGDPLWG SRFDATNPEA VVQTHLDFLR NGADIILTNT YQSSVEGFVK YLGVTRERGV ELIQKSVQLA RQAKEQYLTE IGSDLESALP LILGSIGPYG ACLHDGSEYS GNYAHKISKE QLKSWHRTRI EILLAAGVDG LALETLPCQL EVEAVAELVL DNFSDAKFWV SLQCKDEKHL ASGEPFAEAA LSVWRLVQSR KAENRLLGIG LNCVNPLFVT PLLSSLTKVA GSDRIPLVVY SNRGEIYDAE QGEWTGTGEE VVKFVPEWIQ LGARIVGGCC RVYPTDVLAI RKYVDGLNIK P // ID B4Q902_DROSI Unreviewed; 331 AA. AC B4Q902; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 07-JAN-2015, entry version 35. DE SubName: Full=GD21797 {ECO:0000313|EMBL:EDX05434.1}; GN Name=Dsim\GD21797 {ECO:0000313|EMBL:EDX05434.1}; GN ORFNames=Dsim_GD21797 {ECO:0000313|EMBL:EDX05434.1}, GN GD21797 {ECO:0000313|FlyBase:FBgn0193217}; OS Drosophila simulans (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7240 {ECO:0000313|EMBL:EDX05434.1, ECO:0000313|Proteomes:UP000000304}; RN [1] {ECO:0000313|EMBL:EDX05434.1, ECO:0000313|Proteomes:UP000000304} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Mixed {ECO:0000313|EMBL:EDX05434.1}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 genomes consortium; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(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; CM000361; EDX05434.1; -; Genomic_DNA. DR RefSeq; XP_002079849.1; XM_002079813.1. DR UniGene; Dsi.9929; -. DR EnsemblMetazoa; FBtr0221707; FBpp0220199; FBgn0193217. DR GeneID; 6732735; -. DR KEGG; dsi:Dsim_GD21797; -. DR FlyBase; FBgn0193217; Dsim\GD21797. DR KO; K00547; -. DR OrthoDB; EOG7GQXW0; -. DR PhylomeDB; B4Q902; -. DR Proteomes; UP000000304; Chromosome 2L. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000304}; KW Reference proteome {ECO:0000313|Proteomes:UP000000304}. SQ SEQUENCE 331 AA; 36716 MW; 702CF62D2DCC7234 CRC64; MGLTRVLVKD GGFGTQMTVH VGDSVDGDPL WSARFNATNP AAIISTHLDF LQNGADIILT NTYQSSVDGY MEYLELDEEQ SIELIKNTVR LAHIAKERYL TECYQAQLSV QEGYPLIIAS IGPFGAHLHD GSEYTGSYAD FVPAKEITDW HRVRIEACLE AGVDALAIET IPCQMEAEAL VEMLCDDYPD VKFWVAFQCK DENTLAHGET FADAANAIWD LLADRNAQDK CLAIGVNCVH PKFVTPLFKS LNGDREVGEQ IPLVVYPNSG EVYDVVNGWQ GREHCVPLAS YVPEWAQLGA KVIGGCCRTY ARDVRHIGEA IRDWNKLKKL T // ID B4Q903_DROSI Unreviewed; 331 AA. AC B4Q903; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 07-JAN-2015, entry version 35. DE SubName: Full=GD21796 {ECO:0000313|EMBL:EDX05435.1}; GN Name=Dsim\GD21796 {ECO:0000313|EMBL:EDX05435.1}; GN ORFNames=Dsim_GD21796 {ECO:0000313|EMBL:EDX05435.1}, GN GD21796 {ECO:0000313|FlyBase:FBgn0193216}; OS Drosophila simulans (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7240 {ECO:0000313|EMBL:EDX05435.1, ECO:0000313|Proteomes:UP000000304}; RN [1] {ECO:0000313|EMBL:EDX05435.1, ECO:0000313|Proteomes:UP000000304} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Mixed {ECO:0000313|EMBL:EDX05435.1}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 genomes consortium; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(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; CM000361; EDX05435.1; -; Genomic_DNA. DR RefSeq; XP_002079850.1; XM_002079814.1. DR UniGene; Dsi.3568; -. DR PRIDE; B4Q903; -. DR EnsemblMetazoa; FBtr0221706; FBpp0220198; FBgn0193216. DR GeneID; 6732736; -. DR KEGG; dsi:Dsim_GD21796; -. DR FlyBase; FBgn0193216; Dsim\GD21796. DR KO; K00547; -. DR OrthoDB; EOG7GQXW0; -. DR PhylomeDB; B4Q903; -. DR Proteomes; UP000000304; Chromosome 2L. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000304}; KW Reference proteome {ECO:0000313|Proteomes:UP000000304}. SQ SEQUENCE 331 AA; 36607 MW; 91AEDCD55CC630FA CRC64; MEVNQKWNWD SKPILVKCGG FSSQLAKNVT EKVDGDPLWG SRFDATNPEA VIQTHLDFLR NGADIILTNT YQSSVEGFMK YLGVSRERGV ELIQKSVQLA KQAKEQYLSE IGSEADSALP LIMGSIGPYG AYLHDGSEYT GNYADKMSKE QLKAWHTARI EICLAAGVDG LALETLPCLM EAEAVTELVL DNFPDAKFWV SLQCMDEKHM ASGESFAEAA LSLWRLVQSR KAENRLLGIG FNCVNPLFVT PLLSSLTKVA GSDRIPLVVY SNRGEIYDVE QGDWTGTGEE VIKFVPEWIQ LGVRIVGGCC RVYPTDVLAI RKYVDGLNIK P // ID B4R914_PHEZH Unreviewed; 313 AA. AC B4R914; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 27-MAY-2015, entry version 35. DE SubName: Full=Putative homocysteine/selenocysteine methylase {ECO:0000313|EMBL:ACG77684.1}; GN OrderedLocusNames=PHZ_c1270 {ECO:0000313|EMBL:ACG77684.1}; OS Phenylobacterium zucineum (strain HLK1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Phenylobacterium. OX NCBI_TaxID=450851 {ECO:0000313|EMBL:ACG77684.1, ECO:0000313|Proteomes:UP000001868}; RN [1] {ECO:0000313|EMBL:ACG77684.1, ECO:0000313|Proteomes:UP000001868} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HLK1 {ECO:0000313|EMBL:ACG77684.1, RC ECO:0000313|Proteomes:UP000001868}; 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; ACG77684.1; -; Genomic_DNA. DR RefSeq; WP_012521828.1; NC_011144.1. DR RefSeq; YP_002130113.1; NC_011144.1. DR STRING; 450851.PHZ_c1270; -. DR EnsemblBacteria; ACG77684; ACG77684; PHZ_c1270. DR KEGG; pzu:PHZ_c1270; -. DR PATRIC; 22925380; VBIPheZuc44517_1772. DR eggNOG; COG2040; -. DR HOGENOM; HOG000179103; -. DR OMA; CCGTDHR; -. DR OrthoDB; EOG6R5C46; -. DR BioCyc; PZUC450851:GHUG-1287-MONOMER; -. DR Proteomes; UP000001868; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001868}; KW Methyltransferase {ECO:0000313|EMBL:ACG77684.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001868}; KW Transferase {ECO:0000313|EMBL:ACG77684.1}. SQ SEQUENCE 313 AA; 33163 MW; DFF7F614DFCFF2E2 CRC64; MSPRLPQLSN GLFLTDGGLE TTLIFHEGLE LPHFAAFTLL RDPAGRDVLR RYYRTYLDIA AAEGVGFVLE SPTWRASPDW AERLGISADD LGELNRQAIA MMEALRTAYA GQVSPIVVSG CVGPRGDGYD PGEAMTAEAA EAYHAGQVAA FAEAGADMVC AITMTNTPEA VGVVRAAQTF GLPVAISFTV ETDGRLPTGE ALGRAVQAVD EATGGAPAYY MVNCAHPSHF AEALAADAPW AKRIQGLRAN ASRRSHQELN DSPDLDDGDP AELAAEHAEI LRRRPWIRVI GGCCGTDHRH VAALGRACVA VAA // ID B4RHL8_PHEZH Unreviewed; 353 AA. AC B4RHL8; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 27-MAY-2015, entry version 42. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:ACG79059.1}; GN OrderedLocusNames=PHZ_c2650 {ECO:0000313|EMBL:ACG79059.1}; OS Phenylobacterium zucineum (strain HLK1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Phenylobacterium. OX NCBI_TaxID=450851 {ECO:0000313|EMBL:ACG79059.1, ECO:0000313|Proteomes:UP000001868}; RN [1] {ECO:0000313|EMBL:ACG79059.1, ECO:0000313|Proteomes:UP000001868} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HLK1 {ECO:0000313|EMBL:ACG79059.1, RC ECO:0000313|Proteomes:UP000001868}; 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; ACG79059.1; -; Genomic_DNA. DR RefSeq; WP_012523197.1; NC_011144.1. DR RefSeq; YP_002131488.1; NC_011144.1. DR STRING; 450851.PHZ_c2650; -. DR EnsemblBacteria; ACG79059; ACG79059; PHZ_c2650. DR KEGG; pzu:PHZ_c2650; -. DR PATRIC; 22928482; VBIPheZuc44517_3304. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; PZUC450851:GHUG-2686-MONOMER; -. DR Proteomes; UP000001868; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001868}; KW Methyltransferase {ECO:0000313|EMBL:ACG79059.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001868}; KW Transferase {ECO:0000313|EMBL:ACG79059.1}. SQ SEQUENCE 353 AA; 38385 MW; E3BE997A0464438A CRC64; MTRAERIAAL KAAARARILI LDGSWGVMIQ KRGLAEADYR GERFKDAPGE LRGNNDLLCL TRPDIIAELH DAYYAAGADI SETNTFSATS IAQAEYGLQA AVRDINLEGA RIARACADRW TEKEPGKPRF VAGSIGPLPV MLSMSSDVND PGARKVTFEQ VYEAYAEQVR ALHDGGVDMF LIETITDTLN CKAAIKAILD LEDEGYEPLP IWISGTITDR SGRTLSGQTV EAFWNSVRHA KPFAVGLNCA LGAELMRPHI AELARIADTL VSAYPNAGLP NAMGEYDEQP HETGHMLHDW AKDGLVNILG GCCGTTPEHI KHVADEVRGV KPRPVPERPT AMRLAGLEPF ELA // ID B4S4L0_PROA2 Unreviewed; 1229 AA. AC B4S4L0; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 27-MAY-2015, entry version 53. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACF46906.1}; GN OrderedLocusNames=Paes_1894 {ECO:0000313|EMBL:ACF46906.1}; OS Prosthecochloris aestuarii (strain DSM 271 / SK 413). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Prosthecochloris. OX NCBI_TaxID=290512 {ECO:0000313|EMBL:ACF46906.1, ECO:0000313|Proteomes:UP000002725}; RN [1] {ECO:0000313|EMBL:ACF46906.1, ECO:0000313|Proteomes:UP000002725} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 271 / SK 413 {ECO:0000313|Proteomes:UP000002725}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001108; ACF46906.1; -; Genomic_DNA. DR RefSeq; WP_012506439.1; NC_011059.1. DR RefSeq; YP_002016553.1; NC_011059.1. DR STRING; 290512.Paes_1894; -. DR EnsemblBacteria; ACF46906; ACF46906; Paes_1894. DR KEGG; paa:Paes_1894; -. DR PATRIC; 23043704; VBIProAes37017_2017. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PAES290512:GHUT-1942-MONOMER; -. DR Proteomes; UP000002725; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002725}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002725}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1229 AA; 136082 MW; 6CFBDE8618A15258 CRC64; MRETPQSLLE KKILVLDGAM GTMIQRHKLE EKDFRSERFA SHSHPLKGNN DILVLTQPEI IYDIHCDFLE AGADIIETNT FNANPVSQAD YGTEDLIKEL NLSAASIARR AADAYTAKNP SKPRYVAGSM GPTNKTLSLS PDVNNPGYRA VTFQDVVDNY ILQLDGLVEG GVDLLLVETV FDTLNCKAAL YAIEEHSRKT GKNLPIMISG TVVDASGRTL SGQTTEAFWI SVAHTPNLLS VGLNCALGSK QMRPFVEALS GIAESYVSVY PNAGLPNEFG EYDDSPEYMA SQIADFARSG FVNIVGGCCG TTPDHIRAIA RDVAAIEPRR KPKASHELQL SGLEPLLVNK TTGFINIGER TNVTGSRKFA RLIKEENYDE ALSVAREQVE NGAQVIDINV DEGMLDSEKV MHEFINLIAS EPEISKVPLM IDSSKWSVIE SGLRCSQGKC IVNSISLKEG EELFKQRAKK ILQYGAATVV MAFDEKGQAD SLERRIEICS RAYSILCEEV GFPPEDIIFD PNVLTVATGI EEHDNYAVDF IESVRWIKQN LPFAKISGGI SNVSFSFRGN NPVREAMHAA FLYHAIHAGL DMGIVNAGQL AIYQDIEPEL LERVEDVLLN RRKDATERLV DYAGSMISED TTKNSPKKAE WRNESVEKRL EHALIKGIVD FINEDIEEAR LKYASPLKVI EGPLMHGMDV IGDLFAAGKM FLPQVVKSAR VMKKGVAYLI PFIEEEKRKG NDSSAAAKVL LATVKGDVHD IGKNIVSVVL ACNNYDVVDI GVMMPCEKIL DAAEKEHADI IGLSGLITPS LDEMVHIAKE MERRGMTIPL LIGGATTSKV HTAVKIAEHY SGPIVHVLDA SRSVPAVNNL VTPSLKTNYV EKLLAGQEEL RRKHKEKNAA KTYLSIAEAR KNHAELSWND APPAPPLKPG ITTFDRVSLD ELREYIDWTP FFRVWEIHGL WPAIKSDPHY GEEATKLYDD ANRLLDTMCA DTSSLQARGV AGIFPANSNG DDIEVYTDEE RTTLRCTLHT LRQQAEQKQA SPNLALADFI APKSSGIKDY IGCFTLTTGH GLQEIMDRFA EDHDDYHRIM AQALADRLAE AFAEMLHRKV RMELWGYAPD ESLDHDQLIG EKYRGIRPAP GYPACPDHTE KPKIFDLLNS EAATGVTLTE TFAMNPQASV CGLYFAHPEA KYFILGQIGK DQVEEYAERK KMTRSEVEKW LAPNLNYTP // ID B4SEX1_PELPB Unreviewed; 1240 AA. AC B4SEX1; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 01-APR-2015, entry version 49. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACF44647.1}; GN OrderedLocusNames=Ppha_2463 {ECO:0000313|EMBL:ACF44647.1}; OS Pelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Pelodictyon. OX NCBI_TaxID=324925 {ECO:0000313|EMBL:ACF44647.1, ECO:0000313|Proteomes:UP000002724}; RN [1] {ECO:0000313|EMBL:ACF44647.1, ECO:0000313|Proteomes:UP000002724} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 5477 / BU-1 {ECO:0000313|Proteomes:UP000002724}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001110; ACF44647.1; -; Genomic_DNA. DR RefSeq; WP_012509121.1; NC_011060.1. DR RefSeq; YP_002019264.1; NC_011060.1. DR ProteinModelPortal; B4SEX1; -. DR SMR; B4SEX1; 648-894. DR STRING; 324925.Ppha_2463; -. DR EnsemblBacteria; ACF44647; ACF44647; Ppha_2463. DR KEGG; pph:Ppha_2463; -. DR PATRIC; 22905741; VBIPelPha134556_2634. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PPHA324925:GHBF-2509-MONOMER; -. DR Proteomes; UP000002724; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002724}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002724}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1240 AA; 136453 MW; 2356DE3AF9A486E5 CRC64; MKDTLLNSLE ERILVLDGAM GTMIQRHKLK EADYRGTRFA NHSHPLIGNN DILVLTRPDI IYALHCDFLE AGSDIIETNT FNANPISQAD YSASDLVKEL NVEAARLARR AADEYTARNP DKPRFVAGSI GPTNKTLSLS PDVNNPGFRA VTFQEVVDNY TLQLEGLMEG GVDLLLVETV FDTLNCKAAL FSIEEFFNRT GVRIPVMVSG TVVDASGRTL SGQTTEAFWI SIAHMPDLLS IGLNCALGSK QMRPFIEALA GIAESYVSVY PNAGLPNEFG EYDDSPEYMA GQIAGFATSG FVNIVGGCCG TTPQHIKAIA EAVEKLQPRR RPVKKHELQL SGLEPLFVNR TTGFINVGER TNVTGSKKFS RLIKESKYDE ALSIARQQVE SGAQVIDVNV DEGMLDSEVV MREFLNLIGS EPEISRVPVM IDSSKWSVIE SGLRCVQGKS IVNSISLKEG EALFIERARK VLQYGAATVV MAFDEEGQAD SYQRRIEICK RAYDILTQQV GFPPEDIIFD PNVLTVATGI DEHNNYAVDF IETVRWIKEN LPHAKVSGGI SNVSFSFRGN ETVREAMHAA FLYHAIQAGL DMGIVNAGQL AIYEDIEPEL LLRVEDVLLN RRADATERLV SFAETIQSGG EKIEAKAAEW RSLPVEERLR HALIKGIVEH IEEDTEEARQ LYPSPLQVIE GPLMNGMNAI GDLFAEGKMF LPQVVKSARV MKRSVAVLLP YIAAEKALNK DTRAAAKVLL ATVKGDVHDI GKNIVAVVLA CNNYDVVDIG VMMPCDKILE AVEREKADLL GLSGLITPSL DEMVHVASEM ERLGMTIPLL IGGATTSRMH TAVKIAPVYS GAVVQVLDAS RSVPVVNSLL NPALSPDYIA GLKAEQAGLR ESHASRAAGK KYLTLQEARN NRLALQGSIC KPLQPGITLF EHVTAGELRP YIDWTPFFMT WELHGRYPQI LDDPKYGSEA KKLFDDANSL LDRIEQEQLL GLKGVAGLFP ANSSGDDIEV YSDESRTSLL AILHTLRQQQ EKGEPNLALA DFIAPVGSGL EDYIGAFAVT AGLGIEKGLR EFSDQQDDYH RIMMQALADR LAEAFAEMLH ERVRRELWGY ECAEKRDGDK GCACHPAPQC QPHPIHELLA EKYQGIRPAP GYPACPDHTE KAELFTLLNA ETNTGITLTE TFAMKPAASV CGLYFAHPQA KYFMLGKIGR DQVEEYAERK GMSIKETEKW LAPALNYDPE // ID B4SPB6_STRM5 Unreviewed; 363 AA. AC B4SPB6; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 27-MAY-2015, entry version 42. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACF52311.1}; GN OrderedLocusNames=Smal_2611 {ECO:0000313|EMBL:ACF52311.1}; OS Stenotrophomonas maltophilia (strain R551-3). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Stenotrophomonas; OC Stenotrophomonas maltophilia group. OX NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF52311.1, ECO:0000313|Proteomes:UP000001867}; RN [1] {ECO:0000313|EMBL:ACF52311.1, ECO:0000313|Proteomes:UP000001867} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R551-3 {ECO:0000313|EMBL:ACF52311.1, RC ECO:0000313|Proteomes:UP000001867}; 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 ----------------------------------------------------------------------- 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; ACF52311.1; -; Genomic_DNA. DR RefSeq; WP_012511567.1; NC_011071.1. DR RefSeq; YP_002028994.1; NC_011071.1. DR ProteinModelPortal; B4SPB6; -. DR STRING; 391008.Smal_2611; -. DR EnsemblBacteria; ACF52311; ACF52311; Smal_2611. DR KEGG; smt:Smal_2611; -. DR PATRIC; 23710154; VBISteMal40512_2621. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; SMAL391008:GH1H-2672-MONOMER; -. DR Proteomes; UP000001867; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001867}; KW Methyltransferase {ECO:0000313|EMBL:ACF52311.1}; KW Transferase {ECO:0000313|EMBL:ACF52311.1}. SQ SEQUENCE 363 AA; 38257 MW; 9EC9AB44C4777752 CRC64; MPALPWLHPD RANALLDALR ERILIIDGAM GTMIQRHGLQ EDDYRGERFA GGFDHAHGPG CDHVAQEGHD LKGNNDLLLL TRPQIIADIH TAYLDAGADL VETNTFNATS VSQADYHLEH LVYELNKAGA AVARACCDAV AATTPGKPRF VIGVLGPTSR TASISPDVND PGFRNTSFDE LRGTYREAID GLIDGGADTI MVETIFDTLN AKAALYAVEE AFDARGARLP VMISGTITDA SGRTLSGQTA EAFHASLAHA RPLSIGLNCA LGADAMRPHV ETLSQVSDCH VSAHPNAGLP NAFGEYDETP EEMAATLRGF AEAGLLNLVG GCCGSTPDHI RAIAQAVAGL PPRALPGAQE QAA // ID B4TDG5_SALHS Unreviewed; 1227 AA. AC B4TDG5; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 27-MAY-2015, entry version 50. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACF67944.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ACF67944.1}; GN Name=metH {ECO:0000313|EMBL:ACF67944.1}; GN OrderedLocusNames=SeHA_C4523 {ECO:0000313|EMBL:ACF67944.1}; OS Salmonella heidelberg (strain SL476). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=454169 {ECO:0000313|EMBL:ACF67944.1, ECO:0000313|Proteomes:UP000001866}; RN [1] {ECO:0000313|EMBL:ACF67944.1, ECO:0000313|Proteomes:UP000001866} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SL476 {ECO:0000313|EMBL:ACF67944.1, RC ECO:0000313|Proteomes:UP000001866}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001120; ACF67944.1; -; Genomic_DNA. DR RefSeq; WP_000095956.1; NC_011083.1. DR RefSeq; YP_002048173.1; NC_011083.1. DR STRING; 454169.SeHA_C4523; -. DR EnsemblBacteria; ACF67944; ACF67944; SeHA_C4523. DR PATRIC; 18516477; VBISalEnt43179_4279. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SENT454169:GHYG-4492-MONOMER; -. DR Proteomes; UP000001866; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001866}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACF67944.1}; KW Transferase {ECO:0000313|EMBL:ACF67944.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136017 MW; 59FF2C6882064063 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLHEEDFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYRMESLS AEINYAAAKL ARACADEWTA RTPEKPRFVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKEEF EALGVDLPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPEHIAA MSRAVAGLLP RQLPDIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VESGAQIIDI NMDEGMLDAE AAMVRFLSLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVEAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLDLAEKYRG SKTDEAANAQ QAEWRSWDVK KRLEYSLVKG ITEFIEQDTE EARQQAARPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EKGSSNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAREVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDNQRDDFV ARTRKEYETV RIQHARKKPR TPPVTLEAAR DNDLAFDWER YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KLLNPRGVVG LFPANRVGDD IEIYRDETRT HVLTVSHHLR QQTEKVGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA IADRLAEAFA EYLHERVRKV YWGYAPNESL SNDELIRENY QGIRPAPGYP ACPEHTEKGT IWQLLDVEKH TGMKLTESFA MWPGASVSGW YFSHPESKYF AVAQIQRDQV TDYAFRKGMS VEDVERWLAP NLGYDAD // ID B4TQM7_SALSV Unreviewed; 1227 AA. AC B4TQM7; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 27-MAY-2015, entry version 49. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACF91885.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ACF91885.1}; GN Name=metH {ECO:0000313|EMBL:ACF91885.1}; GN OrderedLocusNames=SeSA_A4401 {ECO:0000313|EMBL:ACF91885.1}; OS Salmonella schwarzengrund (strain CVM19633). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=439843 {ECO:0000313|EMBL:ACF91885.1, ECO:0000313|Proteomes:UP000001865}; RN [1] {ECO:0000313|EMBL:ACF91885.1, ECO:0000313|Proteomes:UP000001865} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CVM19633 {ECO:0000313|EMBL:ACF91885.1, RC ECO:0000313|Proteomes:UP000001865}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001127; ACF91885.1; -; Genomic_DNA. DR RefSeq; WP_000095976.1; NC_011094.1. DR RefSeq; YP_002117088.1; NC_011094.1. DR STRING; 439843.SeSA_A4401; -. DR EnsemblBacteria; ACF91885; ACF91885; SeSA_A4401. DR PATRIC; 32377361; VBISalEnt87589_4360. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SENT439843:GHHR-3370-MONOMER; -. DR Proteomes; UP000001865; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001865}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACF91885.1}; KW Transferase {ECO:0000313|EMBL:ACF91885.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136105 MW; AC05830C284EC2C0 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLHEEDFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYRMESLS AEINYAAAKL ARACADEWTA RTPEKPRFVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGVDLILI ETVFDTLNAK AAVFAVKEEF EALGVDLPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPEHIAA MSRAVAGLPP RQLPDIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VESGAQIIDI NMDEGMLDAE AAMVRFLSLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVEAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRERKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLDLAEKYRG SKTDEAANAQ QAEWRSWDVK KRLEYSLVKG ITEFIEQDTE EARQQASRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EKGSSNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAREVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHARKKPR TPPVTLEAAR DNDLAFDWER YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KLLNPRGVVG LFPANRVGDD IEIYRDETRT HVLTVSHHLR QQTEKVGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAYEAQH DDYNKIMVKA IADRLAEAFA EYLHERVRKV YWGYAPNESL SNDELIRENY QGIRPAPGYP ACPEHTEKGT IWQLLDVEKH TGMKLTESFA MWPGASVSGW YFSHPESKYF AVAQIQRDQV TDYAFRKGMS VENVERWLAP NLGYDAD // ID B4UC59_ANASK Unreviewed; 286 AA. AC B4UC59; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 27-MAY-2015, entry version 35. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACG73290.1}; GN OrderedLocusNames=AnaeK_2062 {ECO:0000313|EMBL:ACG73290.1}; OS Anaeromyxobacter sp. (strain K). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter. OX NCBI_TaxID=447217 {ECO:0000313|EMBL:ACG73290.1, ECO:0000313|Proteomes:UP000001871}; RN [1] {ECO:0000313|EMBL:ACG73290.1, ECO:0000313|Proteomes:UP000001871} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K {ECO:0000313|EMBL:ACG73290.1, RC ECO:0000313|Proteomes:UP000001871}; 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 ----------------------------------------------------------------------- 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; ACG73290.1; -; Genomic_DNA. DR RefSeq; WP_012526091.1; NC_011145.1. DR RefSeq; YP_002134419.1; NC_011145.1. DR ProteinModelPortal; B4UC59; -. DR STRING; 447217.AnaeK_2062; -. DR EnsemblBacteria; ACG73290; ACG73290; AnaeK_2062. DR KEGG; ank:AnaeK_2062; -. DR PATRIC; 20938771; VBIAnaSp90767_2084. DR eggNOG; NOG129730; -. DR HOGENOM; HOG000265278; -. DR KO; K00548; -. DR OMA; VLTCTFN; -. DR BioCyc; ASP447217:GHB0-2085-MONOMER; -. DR Proteomes; UP000001871; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001871}; KW Methyltransferase {ECO:0000313|EMBL:ACG73290.1}; KW Transferase {ECO:0000313|EMBL:ACG73290.1}. SQ SEQUENCE 286 AA; 27915 MW; BE2BA351C3722088 CRC64; MTPASPRPFD GPTLLDGAMG TALLAGGLPA GALPEAWVLE RPEAIAAVHA AHAAAGAQVV LTCTFNAAGP RLDPLVPPDR VGALCAAAVR LARRAAPGAR VAGDLGPTAL YGPGRPPPDG AAVRARYARA AGALAAAGAD LLWAESQWDL AEARLALDAA RAAGLPVVVT FALRAEAGRL AAPDGTPAEA LLEAVADAGA AAAGVNCVPP GPALAALAAW AARRLAVRFV AKPSPGLPGE VLGPDAFAEA LRPAVQAGLG VAGGCCGAGP GHLAALRRLL AAARAG // ID B4UKP4_ANASK Unreviewed; 1150 AA. AC B4UKP4; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 01-APR-2015, entry version 51. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACG71335.1}; GN OrderedLocusNames=AnaeK_0092 {ECO:0000313|EMBL:ACG71335.1}; OS Anaeromyxobacter sp. (strain K). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter. OX NCBI_TaxID=447217 {ECO:0000313|EMBL:ACG71335.1, ECO:0000313|Proteomes:UP000001871}; RN [1] {ECO:0000313|EMBL:ACG71335.1, ECO:0000313|Proteomes:UP000001871} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K {ECO:0000313|EMBL:ACG71335.1, RC ECO:0000313|Proteomes:UP000001871}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001131; ACG71335.1; -; Genomic_DNA. DR RefSeq; WP_012524171.1; NC_011145.1. DR RefSeq; YP_002132464.1; NC_011145.1. DR ProteinModelPortal; B4UKP4; -. DR STRING; 447217.AnaeK_0092; -. DR EnsemblBacteria; ACG71335; ACG71335; AnaeK_0092. DR KEGG; ank:AnaeK_0092; -. DR PATRIC; 20934748; VBIAnaSp90767_0094. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; ASP447217:GHB0-94-MONOMER; -. DR Proteomes; UP000001871; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001871}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 733 733 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1150 AA; 124744 MW; 206D9DFF3ABBDC6F CRC64; MNFREALERR PLVFDGAMGT QIQRHQLTAA EFGGKEGAND LLTLTRPDLI EEIHARYFAV GCDVVETNTF GSSRLKLDEY GLGHRTYEVN CRAAILARRA ADRYSTPDQP RFVAGSIGPT GMLPSSSDPA LGNITSDALE RIFFEQAKGL VEGGVDALII ETQQDMLELR AAVLACDAVR REALRDVFVI AQPTLIDANG RMLLGTDIGS AVATLERLPV DAIGLNCSTG PDEMRASVKA LAEKCSHFVS VLPNAGMPEN VDGRAVYKLS PDDLARALVG FVAEYGVDIV GGCCGTTPEH LRKVVEALRA RPAPRRRRPA PAAELSSAMK AVPLAMEPRP LVVGERLNSQ GSRKVKELLL ADDYAGLVQI ARGQVEAGAH VLDVCVALNE RDDEAAQMRT LAKLLAQSVD APLMIDSTEP DVIEGALKVY PGRCIVNSVN LEKSGERVRR VLPLVRRYGA AVVAMTIDEK GMAQTAERKA EVARRIVAVA KDHGIPPDSL VFDALTFTLA TGGEEYRRSA VETLEGIRRI KAENPGVLTT LGVSNVSFGL AKSAREVVNS VFLYHAVQAG LDLAIVNPKD ILPYPAIDAA ERALAEDLVF DRRPDALARL IAHFGAKGAP EKAAVDPLAG AGGKSAEERI HLQILHRRPE GIEALIDEAL TRRSAVDVLN QVLLPAMKDV GDRFGAGELI LPFVLQSAEV MKKAVAHLEQ FLEKKAGATK GNVVLATVYG DVHDIGKNLV KTILSNNGFT VHDLGKQVPV ATVLDKALQV NADAIGLSAL LVSTSKQMPF CVEELHRRNL SFPVIIGGAA INRRFGYRTH FAQDGNPYAG GVFYAKDAFE GLEVVEALVD PARREALRRE VLQKAVAEKS RPAAEPVAQA PARRTGSVAP AARVPAPPFW GPRVVPSGSI ALADVWPHLD LAELFKLQWG VKAKGAEYER LIREEFGPKL EELKAEAQAQ GWLVPKVVYG YFPCHAEGND LVVLDPTHRK AEVARLQFPR QPDDRNLCLA DYFREERGAD VCALQVVTVG DQATHLAEQA QERGDYTRAL FLHGLAVETA EALAEYWHRQ VRGELGLADG QGKRYSPGYP SWPELSDQRQ VWKLLDPVRT IGVSLTDACQ MVPEQSTSAI VLHHPDAIYF LVRGLERAAG // ID B4UMU5_ANASK Unreviewed; 319 AA. AC B4UMU5; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 01-APR-2015, entry version 31. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACG74541.1}; GN OrderedLocusNames=AnaeK_3324 {ECO:0000313|EMBL:ACG74541.1}; OS Anaeromyxobacter sp. (strain K). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter. OX NCBI_TaxID=447217 {ECO:0000313|EMBL:ACG74541.1, ECO:0000313|Proteomes:UP000001871}; RN [1] {ECO:0000313|EMBL:ACG74541.1, ECO:0000313|Proteomes:UP000001871} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K {ECO:0000313|EMBL:ACG74541.1, RC ECO:0000313|Proteomes:UP000001871}; 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 ----------------------------------------------------------------------- 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; ACG74541.1; -; Genomic_DNA. DR RefSeq; WP_012527315.1; NC_011145.1. DR RefSeq; YP_002135670.1; NC_011145.1. DR STRING; 447217.AnaeK_3324; -. DR EnsemblBacteria; ACG74541; ACG74541; AnaeK_3324. DR KEGG; ank:AnaeK_3324; -. DR PATRIC; 20941385; VBIAnaSp90767_3373. DR eggNOG; COG2040; -. DR HOGENOM; HOG000179103; -. DR OMA; CCGTDHR; -. DR OrthoDB; EOG6R5C46; -. DR BioCyc; ASP447217:GHB0-3367-MONOMER; -. DR Proteomes; UP000001871; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001871}; KW Methyltransferase {ECO:0000313|EMBL:ACG74541.1}; KW Transferase {ECO:0000313|EMBL:ACG74541.1}. SQ SEQUENCE 319 AA; 33705 MW; 70CC92B1D3F1F32F CRC64; MTVVARHAAF LRALAEAPLL LAEGSVVERV RRHPGGLLDP HVANAGLLFR PDGREVLAGI YRDYRHIGLR HGMPTLLLTP TWRANAERLE RAGLAGRDVF GEAVGLLSAL RDEAGAPGAS VFIGGLVGCR GDAYLPAQAL PREEAAAFHA PHVEALAQAG VDFLVAQTLP AVSEAEGLAL AMGRTGAPFL LSFVLRSTGT LLDGTPLREA VARIDALPGA RPAAYMVNCV HASVFRTAFA LELSSAPWLA TRVVGLQANT SRLSPEELEG RAELDTESPA AFAREMARVH AELGMRLLGG CCGTDERHIA ALADLLTSR // ID B4V6E7_9ACTO Unreviewed; 1163 AA. AC B4V6E7; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 01-APR-2015, entry version 34. DE SubName: Full=5-methyltetrahydrofolate:homocysteine S-methyltransferase {ECO:0000313|EMBL:EDX23534.1}; GN ORFNames=SSAG_03325 {ECO:0000313|EMBL:EDX23534.1}; OS Streptomyces sp. Mg1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=465541 {ECO:0000313|EMBL:EDX23534.1}; RN [1] {ECO:0000313|EMBL:EDX23534.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Mg1 {ECO:0000313|EMBL:EDX23534.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; DS570401; EDX23534.1; -; Genomic_DNA. DR RefSeq; WP_008740562.1; NZ_DS570401.1. DR EnsemblBacteria; EDX23534; EDX23534; SSAG_03325. DR PATRIC; 25456651; VBIStrSp106026_3102. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EDX23534.1}; KW Transferase {ECO:0000313|EMBL:EDX23534.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 237 237 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 747 747 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1163 AA; 127158 MW; AC9E0131E7F2D109 CRC64; MASLPTLSGD SRNRSNALRE ALATRVVVAD GAMGTMLQAQ DPTLDDFQNL EGCNEILNVT RPDIVRTVHE AYFSVGVDCV ETNTFGANFA ALAEYDIAER NFELSEAGAR IAREAADEFT AATGQQRWVL GSMGPGTKLP TLGHIDYATI RDAYQANAEG LLTGGADALL VETTQDLLQT KSSVIGARRA MEALGLSVPL ICSVTVETTG TMLLGSEIGA ALTALEPLGI DMIGLNCATG PAEMSEHLRY LARNSRIPLS CMPNAGLPVL TKDGAHYPLS ASELADAQES FVREYGLSLV GGCCGTTPEH LRQVVERVRG LAPAVREPSP EPGAASLYQT VPFRQDTSYM AIGERTNANG SKQFREAMLE ARWDDCVEMV RDQISEGAHM LDLCVDYVGR DGVADMAELA GRFATASTLP IVLDSTEVPV IQAGLEKLGG RAVINSVNYE DGDGPDSRFA KVTRLAREHG AALIALTIDE EGQARTVEHK VEIAERLIQD LTENWGILES DILIDTLTFT ICTGQEESRG DGIATIGAIR ELKRRHPDVQ TTLGLSNISF GLNPAARILL NSVFLDECVK AGLDSAIVHA SKILPIARFD EEQVGTALDL IYDRRAEGYD PLQKLMALFE GVNTKSLKAG RAEELMALPL EERLRRRIID GEKNGLEADL DEALQTRPAL DIVNDTLLEG MKVVGELFGS GQMQLPFVLQ SAEVMKTAVA HLEPHMEKTD ADGKGTIVLA TVRGDVHDIG KNLVDIILSN NGYNVANIGI KQPVSAILEA AEQHKADVIG MSGLLVKSTV IMKENLEELN TRGLAERYPV ILGGAALTRA YVEQDLHEIY QGEVRYARDA FEGLRLMDTL MAVKRGVPGA ELPPLKQRRV ARRSVPLPDL PEQDVPARSD VCVDNPVPTP PFWGTRVVKG IPLKDYASWL DEAALFKGQW GLGRETIETE GRPRLRMWLD RMRTENLLEA AVVHGYFRCV SKGEDLIVLD ENGSERTRFT FPRQERTRRL CLADYFRSAD SGESDVIGFQ IVTVGNRIGE ATAKLFEADS YRDYLELHGL SVQLAEALAE YWHARVRAEL GIGSDDPADL GGMLRTEYQG RRYSFGYPAC PDLEDRAKIA DLLRPERIGV QLSEEFQLHP EQSTDAMVVH HPEATYFNTG VRR // ID B4VAC2_9ACTO Unreviewed; 1170 AA. AC B4VAC2; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 01-APR-2015, entry version 36. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EDX24909.1}; GN ORFNames=SSAG_04700 {ECO:0000313|EMBL:EDX24909.1}; OS Streptomyces sp. Mg1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=465541 {ECO:0000313|EMBL:EDX24909.1}; RN [1] {ECO:0000313|EMBL:EDX24909.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Mg1 {ECO:0000313|EMBL:EDX24909.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; DS570416; EDX24909.1; -; Genomic_DNA. DR RefSeq; WP_008741929.1; NZ_DS570416.1. DR EnsemblBacteria; EDX24909; EDX24909; SSAG_04700. DR PATRIC; 25459418; VBIStrSp106026_4462. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 237 237 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 747 747 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1170 AA; 127882 MW; 96D5A4A4B515A4A9 CRC64; MASLPNLPTD PQNRADALRE ALATRVVVAD GAMGTMLQAQ DPTLEDFQNL EGCNEVLNVT RPDIVRSVHE EYFSVGVDCV ETNTFGANFA ALAEYDIPER NFELSESGAR IAREVADEFT AATGQQRWVL GSMGPGTKLP TLGHIEYATI RDAYQTNAEG LISGGADALL VETTQDLLQT KSSIIGARRA MEALGVRVPL ICSVTVETTG TMLLGSEIGA ALTSLEPLGI DMIGLNCATG PAEMSEHLRY LARNSRIPLS CMPNAGLPVL GKNGAHYPLS ASELADAQET FVREYGLSLV GGCCGTTPEH LRQVVERVRD LSPVTRVPQP EPGASSLYQT VPFRQDTSYM AIGERTNANG SKKFREAMLE ARWDDCVEMA RDQIREGAHM LDLCVDYVGR DGVADMRELA GRFATASTLP IVLDSTEVPV IQAGLEKLGG RAVINSVNYE DGDGPESRFA KVTRLAQEHG AALIALTIDE EGQARSAEHK VAIAERLIDD LTGNWGIHES DILIDTLTFT ICTGQEESRG DGIATIEAIR ELKRRHPDVQ TTLGLSNISF GLNPAARVLL NSVFLDECVK AGLDSAIVHA SKILPIARFD EEQVGTALDL IYDRRAEGYD PLQKLMALFE GVNTKSLKAG RAEELLALPL DERLQRRIID GEKNGLEADL DEALQTRPAL DIVNDTLLEG MKVVGELFGS GQMQLPFVLQ SAEVMKTAVA YLEPHMEKTD DEGKGTIVLA TVRGDVHDIG KNLVDIILTN NGYNVVNIGI KQPVSAILEA AEEHKADVIG MSGLLVKSTV IMKENLEELN QRKLAADYPV ILGGAALTRA YVEQDLHEIY EGEVRYARDA FEGLRLMDAL IAVKRGVPGA TLPELKQRRV AKRDTSALQV EEEQEPGGRS DVSVDNPVPT PPFWGTRVVK GIPLKDYASW LDEGALFKGQ WGLKQARAGG ATYEELVENE GRPRLRGLLD KLHTENLLEA AVVYGYFPCV SKGEDLIILD DSGNERTRFT FPRQRRGRRL CLADFFRPEE SGETDVVGLQ VVTVGSKIGE ATAKLFESDS YRDYLELHGL SVQLAEAMAE YWHARVRAEL GFGGEDPAAV EDMFDLKYRG ARFSLGYGAC PDLEDRAKIA DLLQPERIGV HLSEEFQLHP EQSTDAIVIH HPEAKYFNAR // ID B4VDN5_9ACTO Unreviewed; 291 AA. AC B4VDN5; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 01-OCT-2014, entry version 14. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:EDX26072.1}; GN ORFNames=SSAG_05883 {ECO:0000313|EMBL:EDX26072.1}; OS Streptomyces sp. Mg1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=465541 {ECO:0000313|EMBL:EDX26072.1}; RN [1] {ECO:0000313|EMBL:EDX26072.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Mg1 {ECO:0000313|EMBL:EDX26072.1}; 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS570440; EDX26072.1; -; Genomic_DNA. DR RefSeq; WP_008743088.1; NZ_DS570440.1. DR EnsemblBacteria; EDX26072; EDX26072; SSAG_05883. DR PATRIC; 25461726; VBIStrSp106026_5607. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDX26072.1}; KW Transferase {ECO:0000313|EMBL:EDX26072.1}. SQ SEQUENCE 291 AA; 29647 MW; 0B6B978E2E673C53 CRC64; MPRASGPLAE ALARRTVLLD GGLSNQLADQ GCDLSGDLWT GRVLAERPGQ VARAHAAYAG AGAEVLITAS YQLGSAAPAE LFARSVRLAA GAAETAGHEV WVAASVGPYG AVLADGSEYR GRYGLGVREL AAFHRPRALA LLAAGPDVLA LETIPDTVEA EALLGILAET GAPAWLSYTV AGGRTRAGQP LAEAFALAAA SPQVIAVGVN CCDPEDVLPA LEAAAGVTGM PLLAYPNDGS VWEAATRTWH APGHPAPWPA EAWQEAGARL IGGCCRIGPA GIAALAARVR W // ID B4W084_9CYAN Unreviewed; 1194 AA. AC B4W084; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 27-MAY-2015, entry version 37. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EDX72491.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EDX72491.1}; GN ORFNames=MC7420_3563 {ECO:0000313|EMBL:EDX72491.1}; OS Coleofasciculus chthonoplastes PCC 7420. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Coleofasciculus. OX NCBI_TaxID=118168 {ECO:0000313|EMBL:EDX72491.1}; RN [1] {ECO:0000313|EMBL:EDX72491.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PCC 7420 {ECO:0000313|EMBL:EDX72491.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; DS989864; EDX72491.1; -; Genomic_DNA. DR RefSeq; WP_006104477.1; NZ_DS989864.1. DR ProteinModelPortal; B4W084; -. DR EnsemblBacteria; EDX72491; EDX72491; MC7420_3563. DR PATRIC; 26254246; VBIMicCht100541_5935. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EDX72491.1}; KW Transferase {ECO:0000313|EMBL:EDX72491.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 228 228 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 737 737 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1194 AA; 133313 MW; 67058B0424124460 CRC64; MNSAFLTRLH SPQRPVLVFD GAMGTNLQTQ NLTAEDFGGA KYEGCNEYLV HTKPEAVATV HRRFLEAGAD VIETDTFGGA SIVLAEYDLA DQAYSLNKAA AELAKKVAAE FSTPEKPRFV AGSIGPTTKL PTLGHIDFDT IQATFAEQAE GLYDGGVDLM IIETCQDVLQ IKAALNGVEE VFRKKGERRP IMVSVTVEVQ GTMLVGTEIG AALAILERYP IDILGLNCAT GPDRMKDHIK YLSQHSPFVV SCIPNAGLPE NVGGQAHYKL TPMELRMALM HFIEDLGVQV IGGCCGTRPE HIQQLAEIAQ TLTPKERHPE YEPAAASIYS TQPYEQDNSF LIVGERLNAS GSKKCRTLLN NEDWDGLVAL ARAQVREGAH VLDVNVDYVG RDGEHDMHEL VSRLVTNVTL PLVLDSTEWQ KMEAGLKVAG GKCILNSTNY EDGEERFLKV LDLAKMYGAG VIVGTIDEEG MARTADRKFA IAQRAYHQAI DYGIPAHEIF FDPLALPIST GIEEDRSNGK ATIESIRRMR EELPGCHIIL GVSNISFGLN PAARVVLNSM FLHEAMAVGL DAAIVSASKI LPVAKIEPEH QEICRKLIYD QREFDGDICT YDPLGEITQL FEGKTTKRDR TVDENLPIEE RLKRHIIDGE RIGLDNSLAK ALETYQPLEI INTFLLDGMK VVGELFGSGQ MQLPFVLQSA ETMKAAVAYL EPYMEKEDGE NNAKGIMVIA TVKGDVHDIG KNLVDIILTN NGYKVINLGI KQPVDNIIEA YKEHNADCIA MSGLLVKSTA FMKDNLETFN EKGITVPVIL GGAALTPKFV YQDCQNTYQG KVVYGKDAFS DLHFMDKLMP AKAAEEWDDL KGFLDEVTTD EIPDGTDEPS ENGKSDKQKK TKKSSAKQSV PEVENTRRSE HITLEINRPT PPFWGTRILQ PEDIPIDEAL WYLDLQALIA GQWQFRKPKD QSREEYNQFL EETVYPILDD WKQRVVAENL LHPQIIYGYF PCQSEGNSLH LFDPEMMNQE GEKHPEKWQP IATFKFPRQK SGRRLCIADF FAPKDSGIID VFPMQAVTVG EVATRYAKQL FESDQYTDYL YYHGLAVQMA EALAEWIHAR IRRELGFGGE EPDTIRDVLA QRYQGSRYSF GYPACPNIQD QYKQLELLKC DRINLYMDES EQLYPEQSTT AIVTYHPVAK YFSA // ID B4W9T0_9CAUL Unreviewed; 364 AA. AC B4W9T0; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Homocysteine S-methyltransferase, putative {ECO:0000313|EMBL:EDX81092.1}; GN ORFNames=BBAL3_2249 {ECO:0000313|EMBL:EDX81092.1}; OS Brevundimonas sp. BAL3. OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Brevundimonas. OX NCBI_TaxID=391600 {ECO:0000313|EMBL:EDX81092.1}; RN [1] {ECO:0000313|EMBL:EDX81092.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BAL3 {ECO:0000313|EMBL:EDX81092.1}; 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; EDX81092.1; -; Genomic_DNA. DR RefSeq; WP_008262470.1; NZ_DS989898.1. DR EnsemblBacteria; EDX81092; EDX81092; BBAL3_2249. DR PATRIC; 29028845; VBIBreSp110930_1943. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDX81092.1}; KW Transferase {ECO:0000313|EMBL:EDX81092.1}. SQ SEQUENCE 364 AA; 39601 MW; 1EE62BF0930B407E CRC64; MTSPLTRAER IAALHAAAKE RILVLDGSWG VMIQRRGLSE ADFRADRFVA ANGYDEAQQM KGNNDILCIT RPDIISDLHD QYYAAGADIS ETNTFSGTTI AQEDYALDAQ AVWDINLEGA KLARAAADRW TEKEPHKPRF AAGSIGPLNK MLSMSSDVND PGARSVTFDQ VHEAYRHQVK ALNEGGVDLY LIETITDTLN CKAAIKAIKD LEDEGMDALP IWISGTITDR SGRTLSGQTA EAFWNSVRHA KPFAIGFNCA LGADLMRPFI AELSRVADTL VAAYPNAGLP NAMGQYDEEP HETAHFIEEW AASGLVNIVG GCCGTTPDHI KHVAEEVAPL KPRAIPERPV ALRLSGLEPF EMVA // ID B4WMI4_9SYNE Unreviewed; 358 AA. AC B4WMI4; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 04-MAR-2015, entry version 17. DE SubName: Full=Homocysteine S-methyltransferase, putative {ECO:0000313|EMBL:EDX86981.1}; GN ORFNames=S7335_4688 {ECO:0000313|EMBL:EDX86981.1}; OS Synechococcus sp. PCC 7335. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechococcus. OX NCBI_TaxID=91464 {ECO:0000313|EMBL:EDX86981.1}; RN [1] {ECO:0000313|EMBL:EDX86981.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PCC 7335 {ECO:0000313|EMBL:EDX86981.1}; 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; DS989904; EDX86981.1; -; Genomic_DNA. DR EnsemblBacteria; EDX86981; EDX86981; S7335_4688. DR PATRIC; 29877061; VBISynSp82123_1064. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDX86981.1}; KW Transferase {ECO:0000313|EMBL:EDX86981.1}. SQ SEQUENCE 358 AA; 39526 MW; 1E662CE564D67A9C CRC64; MTTNTYHLPQ LNFLDKTQQS ENRLFITDGG LETDLIFQQG IHLPDFAAFV LLNDVMGVAA LRRYFEKYVA IAHRYGVGLI LESPTWRANS DWGDRLGYDA EALARVNQQA ITLLHTIRLE AQNPTSVVIS GCIGPRGDGY SPSSQMDIQS AQEYHTAQVE TFALSCAANR ADMVSALTMT YVEEAIGIAF AARKARIPVT ISFTVETDGR LPSGQSLRSA IEQVDQATDC APAYYMINCA HPTHFQQTVA VDEPWTERIY GIRSNASRKS HAELDDSDTL DQGSPVELGW QSVELAKSLP NLAVLGGCCG TDYRHIEAIC QAYCSSMDHS ITPSQKSPIE DSSAIDYHKE ITLFDRSF // ID B4WML6_9SYNE Unreviewed; 1195 AA. AC B4WML6; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 01-APR-2015, entry version 39. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EDX86922.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EDX86922.1}; GN ORFNames=S7335_4629 {ECO:0000313|EMBL:EDX86922.1}; OS Synechococcus sp. PCC 7335. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechococcus. OX NCBI_TaxID=91464 {ECO:0000313|EMBL:EDX86922.1}; RN [1] {ECO:0000313|EMBL:EDX86922.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PCC 7335 {ECO:0000313|EMBL:EDX86922.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; DS989904; EDX86922.1; -; Genomic_DNA. DR RefSeq; WP_006456704.1; NZ_DS989904.1. DR EnsemblBacteria; EDX86922; EDX86922; S7335_4629. DR PATRIC; 29873679; VBISynSp82123_3596. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EDX86922.1}; KW Transferase {ECO:0000313|EMBL:EDX86922.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 228 228 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 750 750 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1195 AA; 132307 MW; A21E21AB10C2BABB CRC64; MKSLFLDRLK SPERPVLVFD GAMGTSLQMQ GLTAADFGGP EYEGCNEYLV ETKPEAVDKV HRGFLAVGAD VIETDTFGGT ALVLAEYDLA DKAYELNKKA AEIARKAADE YSTPGKPRFV AGSIGPGTKL PTLGHVDFDT LKDAYLEQVE GLYDGGVDLM LVETCQDVLQ VKAALIAIEE IFEKKGDRLP LMVSVTVEQQ GTMLVGSEIG AALTILEPFG IDILGLNCAT GPAEMKEHIK YLSENSPFII SCVPNAGLPE NVGGQAHYRL TPMELRMALM HFVEDLGVQI IGGCCGTRPD HIEQLADLSK DLTPKPRPIG ERGELPPYGE LPYMPAAASI YSPQPYEQDN SFLIVGERLN ASGSKKCREM LNAEDWDGLV ALAKSQIKEG AHVLDVNVDY VGRDGERDMR ELVSRLVTNA TLPLMLDSTE WEKMEAGLKV AGGKCILNST NYEDGNERFF KVLELAKRYG AGVVIGCIDE DGMARTAQKK FAIAQRAYRD AVEYGFPPYE LFFDTLVLPI STGIEEDRVN AKETIAAIEM IRDNLPGCHI MLGVSNASFG LNPAARVVLN SMFLSEAMKV GMDGAIVSAS KILPLSKIEP EHQKICLDLI YDRREFDGDV CTYDPLGELT TAFTGKSSKQ LRTTLSEDLP LEEKLKRHII DGERIGLEDQ LAKALEQYPP LEIVNTFLLD GMKVVGELFG SGQMQLPFVL QSAQTMKAAV AYLEPFMDKE DSDTSGKGTV VIATVKGDVH DIGKNLVDII LSNNGYRVVN IGIKQPVDNI ISAYKEHQAD CIAMSGLLVK STAFMKENLK TFNEHGIEVP VILGGAALTP KFVNEDCQNT YNGQVIYGKD AFADLHFMDA LMPAKKANQW DNLKGFASDH PMSQVAKKVA INHATEPEEV SNLPIVIDTR RSDDVAVDID RPQPPFWGPK QLGPEDIPLE DLFDYLDMQA LVAGQWQFRK PKGQSREEYD AFLAEKVDPI LAEWKQRIVE EKLLEPKLMY GYFPCLAEGN TLYVYDWQAA QKGEPSEPVT SFEFPRQRSM RRLCIADFFL PKDKAKPGEY DVFPMQAVTM GDIATEYAAK LFAADDYTNY LYYHGLAVQM AEALAEWAHQ RIRIELGYGD QEPEGIRNIL AQRYQGSRYS FGYPACPNMQ DQPKQLNLLE VEKIGMHMDE SEQLYPEQST TAIVAYHEAA KYFSA // ID B4X1C1_9GAMM Unreviewed; 1277 AA. AC B4X1C1; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 01-APR-2015, entry version 37. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EDX90992.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EDX90992.1}; GN ORFNames=ADG881_3094 {ECO:0000313|EMBL:EDX90992.1}; OS Alcanivorax sp. DG881. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Alcanivoracaceae; Alcanivorax. OX NCBI_TaxID=236097 {ECO:0000313|EMBL:EDX90992.1}; RN [1] {ECO:0000313|EMBL:EDX90992.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DG881 {ECO:0000313|EMBL:EDX90992.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; DS989915; EDX90992.1; -; Genomic_DNA. DR RefSeq; WP_007151397.1; NZ_DS989915.1. DR EnsemblBacteria; EDX90992; EDX90992; ADG881_3094. DR PATRIC; 24416236; VBIAlcSp134196_3071. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EDX90992.1}; KW Transferase {ECO:0000313|EMBL:EDX90992.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 353 353 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 354 354 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 805 805 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1277 AA; 142397 MW; FA1A780BCBECF39C CRC64; MASLQPPTMP FYRYFPRKKH HILGICALPR YNARPNFPPL PEPSMSQNPR AKLTAQLQER ILILDGGMGT MIQRCQFSEE EFRGTQFADW PSDLKGNNDL LSMTQPERIK ALHKGYLDAG ADIIETNSFN STSIAMADYD MQDLARDINV AAARVAREAA DEASTPDKPR YVAGVLGPTN RTASISPDVN DPGYRNTNFD ALVNAYLEAL DGLVEGGIDM VLIETIFDTL NAKAAVFAVD QYCYENNLDL PVMVSGTITD ASGRTLTGQT TEAFYNSLRH ARPISFGLNC ALGPMELRPY IEELSRISET YVSAHPNAGL PNEMGEYDLD PFTMAKEVRA WAEKGFLNII GGCCGTTPEH IAAMADAVEG LAPRQLPDIE VACRLSGLEP CTITKDSLFV NVGERTNVTG SKRFLRLIKE EDYDTALEVA RDQVENGAQI IDINMDEGML ESAECMVKFL NLVASEPEIS KVPIMIDSSK WEVIEAGLKC IQGKGVVNSI SMKEGEEAFL HQARLLRRYG AAVIVMAFDE EGQADTRERK VEICTRAYKL LTEEVGFPPE DIIFDPNIFA IATGIEEHNN YAVDFIEAVG DIKRTLPHAM ISGGVSNVSF SFRGNDTVRE AIHAVFLYYA IKNGMDMGIV NPTMLAIYAD IPEELRNAVE DVVLNRHEDG TEVLLDLAEK YRGSGGEKAK KEDLAWREWA VEKRLEHALV KGVADYVEED TELARQNAAR PLHVIEGPLM DGMNVVGDLF GEGKMFLPQV VKSARVMKKA VAYLMPFMEK EKEELGTQDE ANGKILMATV KGDVHDIGKN IVGVVLQCNG YDVVDLGVMV PCETILEVAK EEKVDIIGLS GLITPSLEEM VHVASEMQRL EMNLPLMIGG ATTSRIHTAV KIDPAYNEAV VHVADASRAV GVASKLLSKT AKDDYVSELK ETYEALRVRR KQQQVDRSLI SIDQAREHRF QPDWHDYTPP EPKVKGLKVL DDYPLDDLVQ RIDWTPFFRA WELAGKFPKI LDDEVVGTEA TKLYRDARDM LEKIVEEKWL TARGVIGFWP ANSDMDDIKL YREPGDKEAF MTLHHLRQQL DRSKNDKPDF CLSDFIAPKE TGLTDWLGGF AVTAGIGIDE HVARFEADHD DYSAIMLKAL ADRLAEAFAE RLHEKVRKDY WGYASDEALS NQDMISEKYR GIRPAPGYPA CPDHTEKALL WQLLDPETHA GMTLTESYAM LPTAAVSGWY FSHPQAKYFG TGKLAKDQMN DYAARKGMTR KEIERMVPHL LGYMDED // ID B5BJT2_SALPK Unreviewed; 1227 AA. AC B5BJT2; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 27-MAY-2015, entry version 50. DE SubName: Full=B12-dependent homocysteine-N5-methyltetrahydrofolate transmethylase {ECO:0000313|EMBL:CAR62019.1}; GN OrderedLocusNames=SSPA3735 {ECO:0000313|EMBL:CAR62019.1}; OS Salmonella paratyphi A (strain AKU_12601). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=554290 {ECO:0000313|EMBL:CAR62019.1, ECO:0000313|Proteomes:UP000001869}; RN [1] {ECO:0000313|EMBL:CAR62019.1, ECO:0000313|Proteomes:UP000001869} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AKU_12601 {ECO:0000313|Proteomes:UP000001869}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; FM200053; CAR62019.1; -; Genomic_DNA. DR RefSeq; WP_000095971.1; NC_011147.1. DR RefSeq; YP_002144573.1; NC_011147.1. DR ProteinModelPortal; B5BJT2; -. DR SMR; B5BJT2; 651-1227. DR STRING; 554290.SSPA3735; -. DR EnsemblBacteria; CAR62019; CAR62019; SSPA3735. DR PATRIC; 32348227; VBISalEnt134303_4273. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SENT554290:GJDA-4030-MONOMER; -. DR Proteomes; UP000001869; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001869}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAR62019.1}; KW Transferase {ECO:0000313|EMBL:CAR62019.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135991 MW; D55A7944EDBE91C0 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLHEEDFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYRMESLS AEINYAAAKL ARACADEWTA RTPEKPRFVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGVDLILI ETVFDTLNAK AAVFAVKEEF EALGVDLPIM ISGTITDASG HTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPEHIAA MSRAVAGLPP RQLPDIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VESGAQIIDI NMDEGMLDAE AAMVRFLSLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVEAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRERKIKI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDEAANAQ QAEWRSWDVK KRLEYSLVKG ITEFIEQDTE EARQQAARPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EKGSSNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL KTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGLTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDNQRDDFV ARTRKEYETV RIQHARKKPR TPPVTLEAAR DNDLAFDWER YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KLLNPRGVVG LFPANRVGDD IEIYRDETRT HVLTVSHHLR QQTEKVGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA IADRLAEAFA EYLHERVRKV YWGYAPNESL SNDELIRENY QGIRPAPGYP ACPEHTEKGT IWQLLDVEKH TGMKLTESFA MWPGASVSGW YFSHPESKYF AVAQIQRDQV TDYAFRKGMS VEDVERWLAP NLGYDAD // ID B5CM24_9FIRM Unreviewed; 795 AA. AC B5CM24; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EDY33742.1}; GN ORFNames=RUMLAC_00498 {ECO:0000313|EMBL:EDY33742.1}; OS Ruminococcus lactaris ATCC 29176. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus. OX NCBI_TaxID=471875 {ECO:0000313|EMBL:EDY33742.1}; RN [1] {ECO:0000313|EMBL:EDY33742.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29176 {ECO:0000313|EMBL:EDY33742.1}; 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] {ECO:0000313|EMBL:EDY33742.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29176 {ECO:0000313|EMBL:EDY33742.1}; 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. {ECO:0000313|EMBL:EDY33742.1}. 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; ABOU02000017; EDY33742.1; -; Genomic_DNA. DR RefSeq; WP_005610123.1; NZ_DS990181.1. DR EnsemblBacteria; EDY33742; EDY33742; RUMLAC_00498. DR PATRIC; 29791428; VBIRumLac66300_0995. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDY33742.1}; KW Transferase {ECO:0000313|EMBL:EDY33742.1}. SQ SEQUENCE 795 AA; 86515 MW; C14D14973D2448B6 CRC64; MLRERLGKEL LYFDGGMGTL LQERGLQPGE LPETWNLLHA EEIREIHRKY IEAGSDIVLT NTFGANALKF HDDAYSLEEI VNAAVGHVKA AAEQAGNGRR IYTALDIGPT GKLLKPMGDL DFETAYEAYK EVMIYGEKAG ADLIHIETMS DTYELKAAVL AAKENTSLPV FATTIFDERG KLLTGADVPS VVALLEGLRV DAFGINCGMG PEQMIPILEQ ITKYSSLPVI VKPNAGLPKQ KNGQTYYDVS PEEFAEVMKK IVEMGAVVIG GCCGTTPDHI KAMADACRMI PIKPVEKKNF TMVSSYGQSV FLGTGSKIIG ERINPTGKKR FKQALKEHDL DYILREGITQ QDNGAHILDV NVGLPDIDEP ALMKEVVQEL QSVTSLPLQI DTVDVEAMEG ALRIYNGKAM VNSVSGKQES MDKVFPLIQK YGGVVIGLAL DENGIPADAE GRVQVAKKII AEAAKYGIEK KDIVIDALAM TISSEPEGAK ITLETLRRLR DEVGVCTVLG VSNISFGLPS RPIVNSIFYT MAMQNGLSVG IINPGSEDMM KAWYAFHALM ALDSNCEKYI ARYAQQPGTT PVQAAGGKHT MTLQSAIERG LKEEASSITA ELAEQKDALD IINEELIPAL NNVGEGFEKG TVFLPQLLMS AESAKSAFAV LKERMDQSGE VQEKKGKVIL ATVKGDIHDI GKNIVKVLLE NYSFDVIDLG KDVPPEKVVE TVLEQDVHLV GLSALMTTTV VSMEETIRQL REKAPDCLVM VGGAVLNQEY ADMIGADFYG KDAMQSVHYA QKVFS // ID B5CYG0_BACPM Unreviewed; 920 AA. AC B5CYG0; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 27-MAY-2015, entry version 36. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EDY95491.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EDY95491.1}; GN Name=metH {ECO:0000313|EMBL:EDY95491.1}; GN ORFNames=BACPLE_01757 {ECO:0000313|EMBL:EDY95491.1}; OS Bacteroides plebeius (strain DSM 17135 / JCM 12973 / M2). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=484018 {ECO:0000313|EMBL:EDY95491.1}; RN [1] {ECO:0000313|EMBL:EDY95491.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17135 {ECO:0000313|EMBL:EDY95491.1}; 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] {ECO:0000313|EMBL:EDY95491.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17135 {ECO:0000313|EMBL:EDY95491.1}; 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 (AUG-2008) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EDY95491.1}. 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; ABQC02000019; EDY95491.1; -; Genomic_DNA. DR RefSeq; WP_007561063.1; NZ_DS990130.1. DR EnsemblBacteria; EDY95491; EDY95491; BACPLE_01757. DR PATRIC; 30481164; VBIBacPle58056_1711. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EDY95491.1}; KW Transferase {ECO:0000313|EMBL:EDY95491.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 763 763 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 920 AA; 101421 MW; 1EBA00DB09EC9739 CRC64; MQTKTIQQLI RERILVLDGA MGTMIQQYNL SEADFRGERF KDIPGQLKGN NDLLCLTRPE VIEDIHRKYL VAGADIIETN SFNATSVSMA DYHVQAYCRE INLAAARLAR RMADEFTVLN PEKPRFVAGS VGPTNKTCSM SPDVNNPAFR ALTFDELQAA YCEQMEALLE GGVDALLIET IFDTLNAKAA IRAAELSMGK IGRRVPLMLS VTVSDIAGRT LSGQTLDAFL ASVEHADLFS VGLNCSFGAR QLKPFLEQLA SRAPYYISAY PNAGLPNSLG QYDQTPEDMA AEVKEYIEEG LVNIIGGCCG TTEQYIAKYQ ELIQGVQPRV PVKKHAHLWL SGLELLEVSP EINFVNVGER CNVAGSRKFL RLINEKKYDE ALSIARKQVE DGALVIDVNM DDGLLDAAQE MTTFLNLVAS EPEIARVPIM IDSSKWEVIR AGLKCVQGKC IVNSISLKEG EEVFIAHARE VKQLGAAVIV MAFDEKGQAD TYSRKIEVCE RAYRILVDKV GFAPEDIIFD PNVLAVATGI EEHNNYAVDF IQATGWIRKN LPGAHVSGGV SNLSFSFRGN NYIREAMHAV FLYHAIQQGM DMGIVNPATS VLYTDIPQDI LERIEDVVLN RRPDAAERLI ETAERLKQEK EGTASQEGSA SAQLLWRNNT TVEERLQYAL VKGLSDYLEE DLQEALSRYP NAVSIIEGPL MAGMNHVGDL FGSGKMFLPQ VVKTARTMKK AVAILQPYIE AEKEEGTRSA GKVLVATVKG DVHDIGKNIV SVVMACNNYE IIDLGVMVPA EQIVETAIRE KVDIVGLSGL ITPSLEEMVH VVTELQRAGL DIPVMIGGAT TSKLHTALKI APVYHAPVVY MKDASQNALV AAKLLNREQR PAFVEALNEE YQALREKNRQ KTVQTVSLAE AQKNKLNLWD // ID B5DGE7_SALSA Unreviewed; 400 AA. AC B5DGE7; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 04-MAR-2015, entry version 22. DE SubName: Full=Betaine-homocysteine methyltransferase {ECO:0000313|EMBL:ACH70821.1}; GN Name=bhmt {ECO:0000313|EMBL:ACH70821.1}; OS Salmo salar (Atlantic salmon). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; OC Salmoniformes; Salmonidae; Salmoninae; Salmo. OX NCBI_TaxID=8030 {ECO:0000313|EMBL:ACH70821.1}; RN [1] {ECO:0000313|EMBL:ACH70821.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=White muscle {ECO:0000313|EMBL:ACH70821.1}; RX PubMed=19878547; DOI=10.1186/1471-2164-10-502; RA Andreassen R., Lunner S., Hoyheim B.; RT "Characterization of full-length sequenced cDNA inserts (FLIcs) from RT Atlantic salmon (Salmo salar)."; RL BMC Genomics 10:502-502(2009). CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BT043706; ACH70821.1; -; mRNA. DR RefSeq; NP_001133157.1; NM_001139685.1. DR UniGene; Ssa.1740; -. DR GeneID; 100194600; -. DR CTD; 635; -. DR HOVERGEN; HBG080367; -. DR UniPathway; UPA00051; UER00083. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000313|EMBL:ACH70821.1}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000313|EMBL:ACH70821.1}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 212 212 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 400 AA; 44268 MW; D61EB7444A82EE85 CRC64; MAPAGAKRNI LERLDAGEIV IGDGGFVFAL EKRGYVKAGP WTPEAAAEHP EAVRQLHREF LRAGSNVMQT FTFYASDDKL ENRGNAQRFT GTQINEAACD LAREVANEGD AMVAGGVSQT PSYLSCKCED EVKSIFKRQL DVFVKKNVDF MIAEYFEHVE EAEWAVQVLK TSGKPVCASL CIGPDGDLNG VSPGDCAVRL VKAGANIVGI NCHFDPMTCV KTVKMMKEGV ERAGLKAHYM VQPLAFHTPD CNCQGFIDLP EFPFGLEPRI LTRWDMHKYA REAFNVGIRF IGGCCGFEPY HIRAVAEELA TERGYLPAAS EKHGNWGAGL EMHTKPWVRA RARRDYWEKL KPASGRPKCP SMSTPDSWGV TKGHADLMQH KEATSQEELK PLFEKAKASH // ID B5EA10_GEOBB Unreviewed; 811 AA. AC B5EA10; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=5-methyltetrahydrofolate--homocysteine S-methyltransferase, cobalamin-dependent {ECO:0000313|EMBL:ACH37308.1}; GN Name=metH {ECO:0000313|EMBL:ACH37308.1}; GN OrderedLocusNames=Gbem_0277 {ECO:0000313|EMBL:ACH37308.1}; OS Geobacter bemidjiensis (strain Bem / ATCC BAA-1014 / DSM 16622). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=404380 {ECO:0000313|EMBL:ACH37308.1, ECO:0000313|Proteomes:UP000008825}; RN [1] {ECO:0000313|EMBL:ACH37308.1, ECO:0000313|Proteomes:UP000008825} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bem / ATCC BAA-1014 / DSM 16622 RC {ECO:0000313|Proteomes:UP000008825}; 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; ACH37308.1; -; Genomic_DNA. DR RefSeq; WP_012528716.1; NC_011146.1. DR RefSeq; YP_002137104.1; NC_011146.1. DR ProteinModelPortal; B5EA10; -. DR STRING; 404380.Gbem_0277; -. DR EnsemblBacteria; ACH37308; ACH37308; Gbem_0277. DR KEGG; gbm:Gbem_0277; -. DR PATRIC; 21984225; VBIGeoBem56306_0278. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; GBEM404380:GHFR-280-MONOMER; -. DR Proteomes; UP000008825; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008825}; KW Methyltransferase {ECO:0000313|EMBL:ACH37308.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008825}; KW Transferase {ECO:0000313|EMBL:ACH37308.1}. SQ SEQUENCE 811 AA; 84563 MW; BFC50796E9CA8ABA CRC64; MPFMQAVKER VLVLDGAMGT MLQERGLKPG QSPEEMNLTA ADVVAGVHQA YLDAGADIIV TNTFGGTKAK LEHYGLGDQV ARINAEAVRI AREVAGEKAY VAGSIGPTGR FLEPVGDMSF DEAVSLFREQ AQALVDAGCD LISFETFLDI KEIRAGVIAV REISKEIPVI AMLTFEEKGR SVLGTPPEAA AITLEAVGAT IVGSNCGLGP EGIYQILSGM REVTALPLIS QANAGLPILK DGVTIFPATP DEMTSYHDRL IELGVRIIGG CCGTTPAHIA AIKKALAAKQ TPFVPKKEDG TTWLSSRGSF AAVGSAHPVA LIGERINPTG KKLYSQELRE GKVSYIRREA LEQTGLGATL LDVNVGTPGI DEPAAMERAV FCITGAVQTP LVLDSSSPAA LEAGLKAADG KVLINSVNGE EKSLAAVLPL AKKYGAALVC LTLDEAGIPA EAAGRVAVAE KIAAAAKAAG VKRSDLVVDC LTLTVSAEPK GALVALEAVR QVSALGLNTT LGVSNISFGL PCRPLISSTF FSLAMAAGLT SAIVNVKEAP MMAAWRSSMV LLEKDVNAAC YIEAYKGQAV GATVEPAAAA GATGTRVAAV EPEGVRGRLA KAVINGEADN VVALVEEALA EGLTPMQISS EALLVGLDEV GKRFGSGEFF LPQVMVSADT MKTAFARLKM ELSTGGLQSI GKILMATVEG DIHDIGKNIL VTLLENNGFE VIDLGKNVPA DRILYEARAH QVDAVGLSAL MTTTMAQMDK VVKLLKAEGV KSFTMVGGAV VTQEYADEIG ADLYAKDAME AVARIKKLLA K // ID B5ED55_GEOBB Unreviewed; 610 AA. AC B5ED55; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 29-APR-2015, entry version 48. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN Name=metF-2 {ECO:0000313|EMBL:ACH37641.1}; GN OrderedLocusNames=Gbem_0613 {ECO:0000313|EMBL:ACH37641.1}; OS Geobacter bemidjiensis (strain Bem / ATCC BAA-1014 / DSM 16622). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=404380 {ECO:0000313|EMBL:ACH37641.1, ECO:0000313|Proteomes:UP000008825}; RN [1] {ECO:0000313|EMBL:ACH37641.1, ECO:0000313|Proteomes:UP000008825} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bem / ATCC BAA-1014 / DSM 16622 RC {ECO:0000313|Proteomes:UP000008825}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {ECO:0000256|RuleBase:RU004255}. CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ACH37641.1; -; Genomic_DNA. DR RefSeq; WP_012529048.1; NC_011146.1. DR RefSeq; YP_002137437.1; NC_011146.1. DR ProteinModelPortal; B5ED55; -. DR STRING; 404380.Gbem_0613; -. DR EnsemblBacteria; ACH37641; ACH37641; Gbem_0613. DR KEGG; gbm:Gbem_0613; -. DR PATRIC; 21984889; VBIGeoBem56306_0603. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; GBEM404380:GHFR-620-MONOMER; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000008825; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004255}; KW Complete proteome {ECO:0000313|Proteomes:UP000008825}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ACH37641.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000008825}; KW Transferase {ECO:0000313|EMBL:ACH37641.1}. SQ SEQUENCE 610 AA; 64000 MW; FE1132255530954E CRC64; MGGSFLERVA HEVLIGDGAI GTMLYAKGVA LDANFEHLNL VRPQLVLDLH AEYLAAGAQV IETNTFGANY AKLSAIGIGG KVADINRQGA ILARRAAKVR DVFVAGSMGP MGRGKQEMSA DQVRDSFRLQ AAALAEGGVD LLILETFSEL DELETALSAA RETGLPVVAN LAFGEGSRLA GGIEAEDAAL RLAAAGASLV GANCGAGPLE LLATLKRIAA VTDLPLAAYP NSGFPEYVDG RYIYRTTPDY FAARAEEMVA AGAVLVGGCC GTTPEHIRVM AQRLKGARPA ARVAVGAVSR TPASEKAKTA ASGFLDLWGK EMVVTVELDP PKGLDCSRIL AGSRALKEAG ADAINLAENP LARVRMGNLA LASLIRRDVG IEVIAHITCR DRNLIGLQSD LMGASLLGVS SILAVTGDPA SLGEEAGASS VFDLNSFTLI KLLSDLNRGV NALGNPIGAG TGFTIGAAFN PNTQKMEVQV ARLAKKVANG ACFAQTQPIY DLERFEQMME QTAHLGIPIL PGVLPLVSGR NAEFLHNEVP GITIPDGIRA RMAGKTGEEG VREGLAIARE FIEATMGRVG GFYLIPPFGK YEIAVELVKF IKSRAEHRGH // ID B5F1J7_SALA4 Unreviewed; 1227 AA. AC B5F1J7; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 27-MAY-2015, entry version 50. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACH49064.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ACH49064.1}; GN Name=metH {ECO:0000313|EMBL:ACH49064.1}; GN OrderedLocusNames=SeAg_B4435 {ECO:0000313|EMBL:ACH49064.1}; OS Salmonella agona (strain SL483). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=454166 {ECO:0000313|EMBL:ACH49064.1, ECO:0000313|Proteomes:UP000008819}; RN [1] {ECO:0000313|EMBL:ACH49064.1, ECO:0000313|Proteomes:UP000008819} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SL483 {ECO:0000313|EMBL:ACH49064.1, RC ECO:0000313|Proteomes:UP000008819}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001138; ACH49064.1; -; Genomic_DNA. DR RefSeq; WP_000095952.1; NC_011149.1. DR RefSeq; YP_002149092.1; NC_011149.1. DR STRING; 454166.SeAg_B4435; -. DR EnsemblBacteria; ACH49064; ACH49064; SeAg_B4435. DR PATRIC; 18487080; VBISalEnt65316_4286. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SENT454166:GHBA-4399-MONOMER; -. DR Proteomes; UP000008819; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008819}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACH49064.1}; KW Transferase {ECO:0000313|EMBL:ACH49064.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136165 MW; 1295E406A118F85F CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLHEEDFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYRMESLS AEINYAAAKL ARACADEWTA RTPEKPRFVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKEEF EALGVDLPIM ISGTITDASG RTLSGQTTEA FYNSLRHADA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MATQIHEWAE AGFLNVVGGC CGTTPEHIAA MSRAVDGLPP RKLPEIPVSC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VESGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVETFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRERKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLDLAEKYRG SKTDEAANAQ QAEWRSWDVK KRLEYSLVKG ITEFIEQDTE EARQQAARPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPYIEASK EKGSSNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIIDL GVMVPADKIL KTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHARKKPR TPPVTLEAAR DNDLAFDWER YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KLLNPRGVVG LFPANRIGDD IEIYRDETRT HVLTVSHHLR QQTEKVGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED DLADAYEAQH DDYNKIMVKA IADRLAEAFA EYLHERVRKV YWGYAPNESL SNDELIRENY QGIRPAPGYP ACPEHTEKGT IWQLLDVEKH TGMKLTESFA MWPGASVSGW YFSHPESKYF AVAQIQRDQV TDYAFRKGMS VEDVERWLAP NLGYDVD // ID B5FGL4_VIBFM Unreviewed; 1226 AA. AC B5FGL4; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 29-APR-2015, entry version 50. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACH65684.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ACH65684.1}; GN Name=metH {ECO:0000313|EMBL:ACH65684.1}; GN OrderedLocusNames=VFMJ11_0328 {ECO:0000313|EMBL:ACH65684.1}; OS Vibrio fischeri (strain MJ11). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Aliivibrio. OX NCBI_TaxID=388396 {ECO:0000313|EMBL:ACH65684.1, ECO:0000313|Proteomes:UP000001857}; RN [1] {ECO:0000313|Proteomes:UP000001857} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MJ11 {ECO:0000313|Proteomes:UP000001857}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001139; ACH65684.1; -; Genomic_DNA. DR RefSeq; WP_012533217.1; NC_011184.1. DR RefSeq; YP_002155094.1; NC_011184.1. DR ProteinModelPortal; B5FGL4; -. DR SMR; B5FGL4; 655-1225. DR STRING; 388396.VFMJ11_0328; -. DR EnsemblBacteria; ACH65684; ACH65684; VFMJ11_0328. DR KEGG; vfm:VFMJ11_0328; -. DR PATRIC; 20119117; VBIVibFis37164_0323. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR Proteomes; UP000001857; Chromosome I. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001857}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACH65684.1}; KW Transferase {ECO:0000313|EMBL:ACH65684.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 249 249 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1226 AA; 136284 MW; B18086F86C4F776A CRC64; MAGSNIKVQI EKQLSERILL IDGGMGTMIQ GYKFEEKDYR GERFNQWHCD LKGNNDLLVL SQPQIIRDIH EAYLEAGADI LETNTFNATT IAMADYDMES LSEEINFEAA KLAREVADKW TEKTPNKPRY VAGVLGPTNR TCSISPDVND PGFRNVSFDE LVEAYSESTR ALIRGGSDLI LIETIFDTLN AKACSFAVES VFEELGITLP VMISGTITDA SGRTLSGQTT EAFYNALRHV KPISFGLNCA LGPDELREYV SELSRISECY VSAHPNAGLP NAFGEYDLSP EDMAEHVAEW ASNGFLNLIG GCCGTTPEHI RQMALVVEGV KPRQLPELPV ACRLSGLEPL TIEKDSLFIN VGERTNVTGS ARFKRLIKEE LYDEALSVAQ EQVENGAQII DINMDEGMLD AEACMVRFLN LCASEPEISK VPVMVDSSKW EVIEAGLKCI QGKGIVNSIS LKEGKEKFVH QAKLIRRYGA AVIVMAFDEV GQADTRERKI EICTNAYNIL VDEVGFPPED IIFDPNIFAV ATGIDEHNNY AVDFIEAVGD IKRTLPHAMI SGGVSNVSFS FRGNNYVREA IHAVFLYHCF KNGMDMGIVN AGQLEIYDNV PEDLREAVED VVLNCRDDST ERLLDIATEY LERAVGKVED KSALEWRDWP VEKRLEHSLV KGITEFIVED TEEARINAEK PIEVIEGPLM DGMNVVGDLF GEGKMFLPQV VKSARVMKQA VAHLEPFINA SKEVGATNGK ILLATVKGDV HDIGKNIVGV VLQCNNYEII DLGVMVSCET ILKVAKEENV DIIGLSGLIT PSLDEMVHVA KEMERQGFDL PLLIGGATTS KAHTAVKIEQ NYSQPVVYVN NASRAVGVCT SLLSNELKPS FVEKLDIDYE RVREQHSRKQ PRTKPVTLEV ARANKVAIDW ASYTPPVPLN PGVHIFDNFD VSTLRNYIDW TPFFMTWSLV GKYPKILEHE EVGEEAKRLF KDANDLLDRI EKEGLLKARG MCALFPASSV GDDIEVYTDE SRTTVAKVLH NLRQQTEKPK GFNYCLSDYI APKESGKNDW IGGFAVTGGI GERELADEYK ANGDDYNAIM IQAVADRLAE AFAEYLHEKV RKEIWGYSPN ETLSNDDLIR EKYQGIRPAP GYPACPEHTE KGALWELMNV EESIGMSLTS SYAMWPGASV SGMYFSHPDS RYFAIAQIQQ DQAESYADRK GWNMLEAEKW LGPNLN // ID B5GEB4_STRSH Unreviewed; 1171 AA. AC B5GEB4; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 01-APR-2015, entry version 37. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EDY44660.2}; GN ORFNames=SSBG_02622 {ECO:0000313|EMBL:EDY44660.2}; OS Streptomyces sp. (strain SPB74). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=465543 {ECO:0000313|EMBL:EDY44660.2}; RN [1] {ECO:0000313|EMBL:EDY44660.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SPB74 {ECO:0000313|EMBL:EDY44660.2}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG770539; EDY44660.2; -; Genomic_DNA. DR RefSeq; WP_008748817.1; NZ_GG770539.1. DR EnsemblBacteria; EDY44660; EDY44660; SSBG_02622. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 237 237 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 747 747 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1171 AA; 127381 MW; 3C159A38F8AE922F CRC64; MAHPSPAAAD ATARVTALRE ALVSRVVVAD GAMGTMLQAQ NPTLEDFQDL EGCNEVLNAT RPDIVRSVHE AYFDVGVDCV ETNTFGANHS AFGEYEIADR IHELSEAGAR LARETADSYT ARDGRTRWVL GSIGPGTKLP TLGHLPYGVL RDGFQQNAEG LLAGGADALI VETTQDLLQT KASVLGARRA LDALGADVPL IVSLAFETTG TMLLGSEIGA ALTALEPLGI DLIGLNCSTG PAEMSEHLRY LAKHSRIPLT CMPNAGLPVL TKDGAHFPLT APEMADWQES FVNDYHLSLV GGCCGSTPEH LRQVVERVRG MAPGTREPRP EPGAASLYQT VPFRQETSYL AIGERTNANG SKKFREAMLE GRWDDCVEMA REQIREGAHM LDLCVDYVGR DGVADMRELA GRFATASTLP LVLDSTEVDV LEAGLEMLGG RAVINSVNYE DGDGPESRFA KVTALAREHG AALIALTIDE EGQARTVENK VAVAERLIAD LTGNWGIHES DILVDCLTFT ICTGQEESRK DGIATIEAIR ELKRRHPDVQ TTLGLSNISF GLNPAARILL NSVFLDECVK AGLDSAIVHA SKILPIARFS EEEVATALDL VYDRRAEGYD PLQKLMRLFE GATAKSLKAG KAEELAALPL DERLKRRIID GERNGLEADL DEALQTRPAL DIVNATLLDG MKVVGELFGS GQMQLPFVLQ SAEVMKTAVA HLEPHMEKSD AEGKGTIVLA TVRGDVHDIG KNLVDIILSN NGYNVVNLGI KQPVSAILEA AEEHRADVIG MSGLLVKSTV IMKENLQELN QRGMATDYPV ILGGAALTRA YVEQDLHEIY EGEVRYARDA FEGLRLMDAL IGVKRGVPGV TLPELKQRRV RPTASAVVTE LAEEEGQVRS DVATDNPVPA PPFWGSRVVK GIPLKDYASW LDEGALFKGQ WGLKQNRKGE GPGYEELAET EGRPRLRGWL DHLQTENLLE AAVVYGYFPC VSKGDDLILL GEDGSERTRF TFPRQRRGRR LCLADFFRPE ESGETDVIGL QVVTVGSRVG EATGKLFAAD AYRDYLELHG LSVQLAEALA EYWHARVRAE LGFAGEDPAD VEDMFALKYR GARFSLGYGA CPNLEDRAKI AALLEPERIG VQLSEEFQLH PEQSTDALVI HHPEAKYFNA R // ID B5GES9_STRSH Unreviewed; 304 AA. AC B5GES9; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 01-OCT-2014, entry version 17. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EDY44825.2}; GN ORFNames=SSBG_02917 {ECO:0000313|EMBL:EDY44825.2}; OS Streptomyces sp. (strain SPB74). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=465543 {ECO:0000313|EMBL:EDY44825.2}; RN [1] {ECO:0000313|EMBL:EDY44825.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SPB74 {ECO:0000313|EMBL:EDY44825.2}; 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 ----------------------------------------------------------------------- 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; EDY44825.2; -; Genomic_DNA. DR RefSeq; WP_008744328.1; NZ_GG770539.1. DR EnsemblBacteria; EDY44825; EDY44825; SSBG_02917. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDY44825.2}; KW Transferase {ECO:0000313|EMBL:EDY44825.2}. SQ SEQUENCE 304 AA; 31133 MW; 39B74DBCDAA9B025 CRC64; MDGTEARGTG SEEFVRALGA RAVVLDGGLS NELEAAGHGL ADALWSARLL RDGPAALTAA HRAYASAGAE VATTASYQAS FEGFARHRID AARTRELLAL SVAAARASGS RWVAASVGPY GAMLADGSEY RGRYGVGRAE LERFHGPRVE ALLAAGPDVL ALETVPDTEE ARALLAVVRG CGVPVWLSYS VADGATRAGQ PLDAAFGLAA EAEEIVAVGV NCCAPGEVAD AVRRAVAAGG KPGVAYPNSG ERWDAHARGW RSDPSFVPGL AARWYAAGAR LIGGCCRVGP GEIRGVADVL RAGA // ID B5GUS6_STRC2 Unreviewed; 306 AA. AC B5GUS6; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:EDY50072.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EFG09882.1}; GN Name=mmuM {ECO:0000313|EMBL:EFG09882.1}; GN ORFNames=SCLAV_4809 {ECO:0000313|EMBL:EFG09882.1}, GN SSCG_03061 {ECO:0000313|EMBL:EDY50072.1}; 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 {ECO:0000313|EMBL:EDY50072.1, ECO:0000313|Proteomes:UP000002357}; RN [1] {ECO:0000313|EMBL:EDY50072.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27064 {ECO:0000313|EMBL:EDY50072.1}; 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., Godfrey P., 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 clavuligerus ATCC 27064."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EFG09882.1, ECO:0000313|Proteomes:UP000002357} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27064 {ECO:0000313|EMBL:EFG09882.1}, and RC ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL 3585 RC / VKM Ac-602 {ECO:0000313|Proteomes:UP000002357}; 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS570648; EDY50072.1; -; Genomic_DNA. DR EMBL; CM000913; EFG09882.1; -; Genomic_DNA. DR RefSeq; WP_003955587.1; NZ_DS570648.1. DR EnsemblBacteria; EDY50072; EDY50072; SSCG_03061. DR EnsemblBacteria; EFG09882; EFG09882; SCLAV_4809. DR PATRIC; 29746756; VBIStrCla15562_2689. DR Proteomes; UP000002357; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002357}; KW Methyltransferase {ECO:0000313|EMBL:EDY50072.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002357}; KW Transferase {ECO:0000313|EMBL:EDY50072.1}. SQ SEQUENCE 306 AA; 31522 MW; 18DA16C7D5E2C691 CRC64; MRPRRTLAEA LGAGPLVLDG GLSNQLAAQG CDLSDPLWTA RLLKDGPEQL AAAHTAYADA GAQVLISASY QASHEGFRRA GLGGAESSAL LARSVELARA AADAAPAEVW VAASVGPYGA VLADGSEYRG RYGLTVRELE RFHRPRIEAL AAAGPDVLAL ETVPDTDEAK ALLAAAADCG VPVWLSYTAD GDRTRAGQPL ADAFALAAEH EQVIATGVNC CAPRDAAPAV ARAASVTGRP VVVYPNSGED WDPAAHTWRG PVRYDPAQAP AWVTAGARLI GGCCRVGPAT IAELASFLWL GSPPGC // ID B5H2F7_STRC2 Unreviewed; 1174 AA. AC B5H2F7; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 27-MAY-2015, entry version 43. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EDY52753.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFG05952.1}; GN ORFNames=SCLAV_0875 {ECO:0000313|EMBL:EFG05952.1}, GN SSCG_05781 {ECO:0000313|EMBL:EDY52753.1}; 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 {ECO:0000313|EMBL:EDY52753.1, ECO:0000313|Proteomes:UP000002357}; RN [1] {ECO:0000313|EMBL:EDY52753.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27064 {ECO:0000313|EMBL:EDY52753.1}; 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., Godfrey P., 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 clavuligerus ATCC 27064."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EFG05952.1, ECO:0000313|Proteomes:UP000002357} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27064 {ECO:0000313|EMBL:EFG05952.1}, and RC ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL 3585 RC / VKM Ac-602 {ECO:0000313|Proteomes:UP000002357}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; DS570714; EDY52753.1; -; Genomic_DNA. DR EMBL; CM000913; EFG05952.1; -; Genomic_DNA. DR RefSeq; WP_003958472.1; NZ_DS570714.1. DR EnsemblBacteria; EDY52753; EDY52753; SSCG_05781. DR EnsemblBacteria; EFG05952; EFG05952; SCLAV_0875. DR PATRIC; 29751708; VBIStrCla15562_5110. DR Proteomes; UP000002357; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002357}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFG05952.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002357}; KW Transferase {ECO:0000313|EMBL:EFG05952.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 240 240 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 750 750 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1174 AA; 127640 MW; FC494FE0FFF7EA5A CRC64; MATLPTPSAP SADARSRIDA LREALATRVV VADGAMGTML QAQDPSLEDF QDLEGCNEIL NVTRPDIVRS VHAEYFDAGV DCVETNTFGA NLAALGEYDI PERVYELSEA GARIARETAD AYTASTGAQR WVLGSMGPGT KLPTLGHAPY TALRDAYQSN AEGMIAGGAD ALLIETTQDL LQTKASVLGA RRALEATGTT LPLIVSVTVE TTGTMLLGSE IGAALTALEP LGIDMIGLNC ATGPAEMSEH LRYLARHSRI PLSCMPNAGL PVLGKNGAHY PLSAAELADA QETFVREYGL SLVGGCCGTT PEHLRQVVER VRGLVPAVRE PRPEPGAASL YQTVPFRQDT AYMAIGERTN ANGSKKFREA MLAARWDDCV EMARDQIREG AHMLDLCVDY VGRDGVADMA ELAGRFATAS TLPIVLDSTE VPVIRAGLEK LGGRAVINSV NYEDGDGPDS RFAQVTRLAQ EHGAALIALT IDEEGQARTV EHKVAIAQRL IADLTGNWGI RESDILIDTL TFTICTGQEE SRKDGIHTIE AIRELKRRHP DVQTTLGLSN ISFGLNPAAR ILLNSVFLEE CVKAGLDSAI VHASKILPIA RFQEEEVATA LDLIYDRRAE GYDPLQKLMA LFEGATAKSL KAGKAEELAA LPLEERLRRR IIDGEKNGLE ADLDEALLTR PALDIVNETL LEGMKVVGEL FGSGQMQLPF VLQSAEVMKT AVAHLEPHME KSDAEGKGTI VLATVRGDVH DIGKNLVDII LSNNGYNVIN LGIKQPVSAI LEAAEEHRAD VIGMSGLLVK STVIMKENLE ELNQRKLAAD YPVILGGAAL TRAYVEQDLH EIYEGEVRYA RDAFEGLRLM DALIAVKRGV PGATLPELKQ RRVRPAATAV VVEEPAEEGT VRSDVAIDNP VPTPPFWGTR VIKGIQLKEY ASWLDEGALF KGQWGLKQNR TGDGPDYAEL AETEGRPRLR GWLDQLHTRG LLEAAVVYGY FPCVSKGDDL ILLNEDGSER TRFSFPRQRR GRRLCLADFF RPEESGETDV VGLQVVTVGS RIGEATAELF AADSYRDYLE LHGLSVQLAE ALAEYWHARV RAELGFGGED PADVEDMFAL KYRGARFSLG YGACPDLEDR AKIADLLRPE RIGVQLSEEF QLHPEQSTDA IVIHHPEAKY FNAR // ID B5H8L9_STRPR Unreviewed; 1169 AA. AC B5H8L9; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 27-MAY-2015, entry version 37. DE SubName: Full=5-methyltetrahydrofolate:homocysteine S-methyltransferase {ECO:0000313|EMBL:EDY63180.1}; GN ORFNames=SSDG_01499 {ECO:0000313|EMBL:EDY63180.1}; OS Streptomyces pristinaespiralis ATCC 25486. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=457429 {ECO:0000313|EMBL:EDY63180.1, ECO:0000313|Proteomes:UP000002805}; RN [1] {ECO:0000313|EMBL:EDY63180.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 25486 {ECO:0000313|EMBL:EDY63180.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CM000950; EDY63180.1; -; Genomic_DNA. DR RefSeq; WP_005319508.1; NZ_CM000950.1. DR EnsemblBacteria; EDY63180; EDY63180; SSDG_01499. DR Proteomes; UP000002805; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002805}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EDY63180.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002805}; KW Transferase {ECO:0000313|EMBL:EDY63180.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 237 237 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 747 747 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1169 AA; 127479 MW; B962D36EB0EDAAEA CRC64; MASLPTPSAD SRTRVHALRE ALATRVVVAD GAMGTMLQAQ DPTLEDFENL EGCNEVLNVT RPDIVRSVHE AYFEVGVDCV ETNTFGANHS AMGEYDIPER VYELSESGAR IAREVADEFT ASTGQQRWVL GSIGPGTKLP TLGHAPYTVL RDGFQQNAEG LIAGGADALI VETTQDLLQT KAAILGARRA MEATGADLPL LCSLAFETTG TMLLGSEIGA ALTALEPLGV DMIGLNCSTG PEEMSEHLRY LTRHSRIPLL CMPNAGLPVL TKDGAHFPLG PEGLAEAQEQ FVADYGLSLV GGCCGTTPEH LRQLVERVRG AELTPRDPRP EPGAASLYQT VPFRQDTAYM AIGERTNANG SKKFREAMLE GRWDDCVEMA RDQIREGAHM LDLCVDYVGR DGVADMEELA GRFATASTLP IVLDSTEVDV IEAGLEKLGG RAVINSVNYE DGDGPESRFA KVTALAKEHG AALIALTIDE EGQARSVEHK VAVAERLIED LTGNWGIHES DILIDTLTFT ICTGQEESRK DGLNTIEAIR ELKRRHPDVQ TTLGLSNISF GLNPAARILL NSVFLDECVK AGLDSAIVHA SKILPIARFD EEQVTTALDL IYDRRREGYD PLQKLMALFE GATTKSLKAG KAEELAALPL EERLKRRIID GEKNGLEADL DEALRERAAL DIVNDTLLDG MKVVGELFGS GQMQLPFVLQ SAEVMKNAVA HLEPHMEKTD ADGKGTIVLA TVRGDVHDIG KNLVDIILSN NGYNVVNLGI KQPVSAILDA AKEHKADVIG MSGLLVKSTV IMKENLQELN QRGMAADYPV ILGGAALTRA YVEQDLHEIY EGEVRYARDA FEGLRLMDAL IGIKRGVPGA ALPELKQRRV KATTAVVEER PEEGAVRSDV ATDNPVPTPP FWGTRVVKGI PLKDYASWLD EGALFKGQWG LKQSRAGDGP SYEELVESEG RPRLRGLLDR LQTDNLLEAA VVHGYFPCVS KGDDLIILGD DGSERTRFSF PRQRRGRRLC LADFFRPEES GETDVVGLQV VTVGSRIGEE TAKLFEANSY RDYLELHGLS VQLAEALAEY WHARVRAELG FGGEDPADVE DMFALKYRGA RFSLGYGACP DLEDRAKIAE LLEPERIGVQ LSEEFQLHPE QSTDAIVIHH PEAKYFNAR // ID B5HHC9_STRPR Unreviewed; 300 AA. AC B5HHC9; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:EDY66240.1}; GN ORFNames=SSDG_04574 {ECO:0000313|EMBL:EDY66240.1}; OS Streptomyces pristinaespiralis ATCC 25486. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=457429 {ECO:0000313|EMBL:EDY66240.1, ECO:0000313|Proteomes:UP000002805}; RN [1] {ECO:0000313|EMBL:EDY66240.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 25486 {ECO:0000313|EMBL:EDY66240.1}; 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 ----------------------------------------------------------------------- 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; EDY66240.1; -; Genomic_DNA. DR RefSeq; WP_005310618.1; NZ_CM000950.1. DR EnsemblBacteria; EDY66240; EDY66240; SSDG_04574. DR Proteomes; UP000002805; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002805}; KW Methyltransferase {ECO:0000313|EMBL:EDY66240.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002805}; KW Transferase {ECO:0000313|EMBL:EDY66240.1}. SQ SEQUENCE 300 AA; 31235 MW; 6DCF33FB49980A91 CRC64; MKPARTLAAA LEEGIVVLDG GLSNQLQAQG CDLSGGLWSA RLLADDPEQI RAAHTAYVRA GAQVLITSSY QATFEGFARR GTGRAQAAGL LGRSVGLARS AADAAGHEVW VAASVGPYGA MLADGSEYRG RYGLGVRELE RFHRPRIEAL AAAGPDVLAL ETVPDTDEAQ ALLEAAEGCG VPLWLSYTVA EGRTRAGQPL AEAFALAAGR DEVIAVGVNC CDPREATAAV ALATEITGKP AVVYPNSGER WDAASSSWQG GSGYDPVRVR EWRAAGARLA GGCCRVGPRE IAELARLLHS // ID B5HIQ3_STRPR Unreviewed; 1162 AA. AC B5HIQ3; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 27-MAY-2015, entry version 39. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EDY66714.1}; GN ORFNames=SSDG_05039 {ECO:0000313|EMBL:EDY66714.1}; OS Streptomyces pristinaespiralis ATCC 25486. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=457429 {ECO:0000313|EMBL:EDY66714.1, ECO:0000313|Proteomes:UP000002805}; RN [1] {ECO:0000313|EMBL:EDY66714.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 25486 {ECO:0000313|EMBL:EDY66714.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CM000950; EDY66714.1; -; Genomic_DNA. DR RefSeq; WP_005321881.1; NZ_CM000950.1. DR EnsemblBacteria; EDY66714; EDY66714; SSDG_05039. DR Proteomes; UP000002805; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002805}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002805}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 228 228 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 738 738 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1162 AA; 125948 MW; BB504534083F2D8F CRC64; MTGTRIDALR EALATRVVVA DGAMGTMLQA QDPTLEDFEN LEGCNEVLNV TRPDIVRSVH EAYFDVGVDC VETNTFGANH AALGEYDIPE RVHELSQAGA RIAREVADAY TASTGQQRWV LGSMGPGTKL PTLGHAPYTL LRDAYQANAE GLIAGGADAL LVETTQDLLQ TKAAIIGARR AMDATGSRPP LICSVTVETT GTMLLGSEIG AALTALEPLG IDMIGLNCAT GPAEMSEHLR HLARHSRIPL SCMPNAGLPV LGKDGAHYPL TPAELADAQE QFVADYGLSL VGGCCGTTPE HLRRIVERVR DLTPPAREPR PDPGAASLYQ AVPFRQDTAY MAIGERTNAN GSKKFREAML EGRWDDCVEM ARDQIREGAH MLDLCVDYVG RDGVADMAEL AGRFATASTL PIVLDSTELP VLQAGLEKLG GRAVINSVNY EDGDGPESRF AKVTALAKEH GAALIALTID EEGQARSVEH KVAVAERLIE DLTGNWGIHE SDILIDTLTF TICTGQEESR KDGLNTIEAI RELKRRHPDV QTTLGLSNIS FGLNPAARVL LNSVFLDECV NAGLDSAIVH ASKILPIARF DEEQVTVARD LIHDRRAEGY DPLQKLMELF EGVSTTSLKA GKAEELAALP LEERLQRRII DGEKNGLEAD LDEALKDTPA LAIVNDTLLA GMKVVGELFG SGQMQLPFVL QSAEVMKIAV AHLEPHMEKT DADGKGTIVL ATVRGDVHDI GKNLVDIILS NNGYNVVNLG IKQPVSAILD AAKEHKADVI GMSGLLVKST VIMKENLQEL NQRGMAADYP VILGGAALTR AYVEQDLHEI YDGEVRYARD AFEGLRLMDA LIGIKRGVPG AALPELKQRR VKATPAVVDE RPPEQPTRSD VADDNPVPTP PFWGSRVVKG IPLKDYASWL DESALFKGQW GLKAARGTGP TYEELVESEG RPRLRGLLDR LQTDNLLEAA VVHGYFPCVS KGDDLIILGD DGSERTRFTF PRQSRGRHLC LADFFRPEES GETDVVALQV VTVGSRIGEE TAKLFEANSY RDYLELHGLS VQLAEALAEY WHARVRAELS IAAADPTGLD GMLRTEYQGC RYSLGYPACP DLEDRAKIAA LLEPERIGVQ LSEEFQLHPE QSTDAIVVHH PEASYFNAGG RA // ID B5HRB2_9ACTO Unreviewed; 313 AA. AC B5HRB2; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:EDY55367.1}; GN ORFNames=SSEG_01947 {ECO:0000313|EMBL:EDY55367.1}; OS Streptomyces sviceus ATCC 29083. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=463191 {ECO:0000313|EMBL:EDY55367.1, ECO:0000313|Proteomes:UP000002785}; RN [1] {ECO:0000313|EMBL:EDY55367.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29083 {ECO:0000313|EMBL:EDY55367.1}; 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 ----------------------------------------------------------------------- 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; EDY55367.1; -; Genomic_DNA. DR RefSeq; WP_007385562.1; NZ_CM000951.1. DR EnsemblBacteria; EDY55367; EDY55367; SSEG_01947. DR Proteomes; UP000002785; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002785}; KW Methyltransferase {ECO:0000313|EMBL:EDY55367.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002785}; KW Transferase {ECO:0000313|EMBL:EDY55367.1}. SQ SEQUENCE 313 AA; 32841 MW; FBD49A801A749B8E CRC64; MTSDTPEVPD ALARPFAEAL AAGPVVLDGG MSNQLESAGH DLSDELWSAR LLAERPEAIT EAHLAYYEAG ADVAITSSYQ ATFEGFAKRG IGRERAAELL ALSVGLAQEA TRQAQAKGVR RPLYVAASVG PYGAMLADGS EYRGRYGLSV AELEAFHRPR LEVLAAAGPD VLALETIPDS DEAQALLRAV RGLGVPAWLS YSVAGDRTRA GQPLEEAFAL AADVDEVIAV GVNCCVPEDV DNAIETAARV TGKPVVVYPN SGETWNAGAR RWEGRSSFTS DEVMGWRASG ARLIGGCCRV GPEAISGIAG AVR // ID B5I559_9ACTO Unreviewed; 1173 AA. AC B5I559; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 27-MAY-2015, entry version 39. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EDY60214.1}; GN ORFNames=SSEG_06906 {ECO:0000313|EMBL:EDY60214.1}; OS Streptomyces sviceus ATCC 29083. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=463191 {ECO:0000313|EMBL:EDY60214.1, ECO:0000313|Proteomes:UP000002785}; RN [1] {ECO:0000313|EMBL:EDY60214.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29083 {ECO:0000313|EMBL:EDY60214.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CM000951; EDY60214.1; -; Genomic_DNA. DR RefSeq; WP_007380875.1; NZ_CM000951.1. DR EnsemblBacteria; EDY60214; EDY60214; SSEG_06906. DR Proteomes; UP000002785; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002785}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002785}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 238 238 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 750 750 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1173 AA; 128267 MW; 97464D6D11BBB256 CRC64; MASSPPTPSA DSRTRVSALR EALATRVVVA DGAMGTMLQA QDPTLEDFEN LEGCNEILNV TRPDIVRSVH DAYFAVGVDC VETNTFGSNH TAASEYDIAD RVHELSEAGA RIAREAADDH TARDGRPRWV LGSVGPGTKL PTLGHIDYAT IRDGYQANVE GLLAGGADAL IVETTQDLLQ TKASVLGARR ALEATGADVP LVVSMAFETT GTMLLGSEIG AALTALEPLG IDMIGLNCST GPAEMSEHLR YLARHSRIPL LCMPNAGLPI LTKDGAHFPL DPEGLADAQE NFVRDYGLSL IGGCCGTTPE HLRQVVERVR ELTPAERNPQ PEPGAASLYQ TVPFRQDTSY LAIGERTNAN GSKKFREAML EARWDDCVEM AREQIREGAH MLDLCVDYVG RDGVADMKEL AGRFATASTL PIVLDSTEVP VIQAGLEKLG GRAVINSVNY EDGDGPESRF AKVTKLAQEH GAALIALTID EEGQARTPEK KVEIAERLID DLTGNWGIHE SDILIDTLTF TICTGQEESR KDGVATIEAI RELKRRHPDV QTTLGLSNIS FGLNPAARVL LNSVFLDECT KAGLDSAIVH ASKILPIARF TEEEVQTALD LIYDRRAEGY DPLQKLMALF EGATTKSLKA GRAEELAALP LDERLKRRII DGEKNGLEAD LDEALTDRPA LDIVNDTLLD GMKVVGELFG SGQMQLPFVL QSAEVMKTAV AYLEPHMEKV EGDEAGKGTI VLATVRGDVH DIGKNLVDII LSNNGYNVVN LGIKQPVSAI LDAAAEHRAD VIGMSGLLVK STVIMKENLE ELNQRGLAAD FPVILGGAAL TRAYVEQDLH EIYEGEVRYA RDAFEGLRLM DALIGVKRGV PGAKLPELKQ RRVRASAVQV EEERPEEGHV RSDVATDNPV PTPPFWDTRV IKGIQLKEYA SWLDEGALFK GQWGLKQART GEGPTYEELV ETEGRPRLRG LLDRLQTENL LEAAVVYGYF PCVSKDDDLI ILDEQGNERT RFTFPRQRRG RRLCLADFFR PEESGETDVV GLQVVTVGSR IGEQTAKLFE ANAYRDYLEL HGLSVQLAEA LAEYWHARVR SELGFAGEDP ADVEDMFALK YRGARFSLGY GACPNLEDRA KIADLLRPER IGVQLSEEFQ LHPEQSTDAI VIHHPEAKYF NAR // ID B5IJ26_9CHRO Unreviewed; 345 AA. AC B5IJ26; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 01-OCT-2014, entry version 16. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EDY39717.1}; GN ORFNames=CPCC7001_2598 {ECO:0000313|EMBL:EDY39717.1}; OS Cyanobium sp. PCC 7001. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Cyanobium. OX NCBI_TaxID=180281 {ECO:0000313|EMBL:EDY39717.1}; RN [1] {ECO:0000313|EMBL:EDY39717.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PCC 7001 {ECO:0000313|EMBL:EDY39717.1}; 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; DS990556; EDY39717.1; -; Genomic_DNA. DR RefSeq; WP_006911642.1; NZ_DS990556.1. DR EnsemblBacteria; EDY39717; EDY39717; CPCC7001_2598. DR PATRIC; 27717124; VBICyaSp52852_0338. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDY39717.1}; KW Transferase {ECO:0000313|EMBL:EDY39717.1}. SQ SEQUENCE 345 AA; 37327 MW; 9D7D7259512583BA CRC64; MAVTLTAEGP NVERRSLIQL NGVPLLSDGG LETTLVFHQG IELPGFAAFD LLRRERGAQL LTDYFRSYLA LGREAGTGFV METPTWRANP AWGPELGYSS EELEAANRQA VALLMELREE EERTARSDDR PDPVIQISGC IGPRGDGYVP DQKLSAEEAE VFHSWQIGVL SRSGVDLVTA FTLSAVPEAV GIVRAARAEA VPVVISFTVE TDGRLPSGQP LSEAIERVDA ETDGAAAYFM VNCAHPSHVA AVLEQGGPWR ERIVGLRANA SRRSHAELDA AESLDEGDPD DLARLYRELS PLLPNLAVLG GCCGTDLRHV QAIARATLPL LWEGLNPSLD TRISR // ID B5IJV3_9CHRO Unreviewed; 1194 AA. AC B5IJV3; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 01-APR-2015, entry version 39. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EDY38775.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EDY38775.1}; GN Name=metH {ECO:0000313|EMBL:EDY38775.1}; GN ORFNames=CPCC7001_1654 {ECO:0000313|EMBL:EDY38775.1}; OS Cyanobium sp. PCC 7001. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Cyanobium. OX NCBI_TaxID=180281 {ECO:0000313|EMBL:EDY38775.1}; RN [1] {ECO:0000313|EMBL:EDY38775.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PCC 7001 {ECO:0000313|EMBL:EDY38775.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; DS990556; EDY38775.1; -; Genomic_DNA. DR RefSeq; WP_006910679.1; NZ_DS990556.1. DR EnsemblBacteria; EDY38775; EDY38775; CPCC7001_1654. DR PATRIC; 27717494; VBICyaSp52852_1868. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EDY38775.1}; KW Transferase {ECO:0000313|EMBL:EDY38775.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 213 213 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 279 279 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 280 280 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 741 741 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1194 AA; 130035 MW; 932FD8E87CA346EC CRC64; MLVFDGATGT SLQQMNLTAE DFGGAALEGC NEYLVVSRPD AVQAVHRQFL EVGADVIETD TFGATSLVLA EYDIADQAFA LNQRAAELAR QMADAFSTPE KPRFVAGSMG PTTKLPTLGH VDFDTMKASF QEQAEGLLAG DVDLFIVETC QDVLQIKAAL QGIEAAFTAT GQRRPLMVSV TMETTGTMLV GSDIAAVVAI LEPFPIDVLG LNCATGPEQM KEHIRYLSEH SPFVVSCIPN AGLPENIGGV AHYRLTPLEM KMQLLHFVED LGVQVIGGCC GTTPAHIGAL AELAAELTPA PRAVRTPATR HDRPLLQVEP SAASIYGTTP YHQDNSFLII GERLNASGSK KVRELLAEED WDGLVAVARG QVKENAHVLD VNVDYVGRDG ERDMHELVSR LVTNVNLPLM LDSTEWQKME AGLKVAGGKC ILNSTNYEDG DERFFKVLEL ARAYGSGVVV GTIDEEGMAR TAERKFAIAQ RAYRDALEFG IPAHELFYDP LALPISTGIE EDRENGLATV EAIRLIRENL PGVHVVLGVS NVSFGLSPAA RIVLNSVFLH DCCEAGMDAA IVSPAKILPL IKISDEHQQI CRDLIYDRRR FESEQPGAIC TYDPLTALTT LFEGVSAKEA RASGPSLADL PVEERLKQHI IDGERIGLET ALDEALQTYP ALHIINTFLL DGMKVVGELF GSGQMQLPFV LQSAETMKAA VARLEPHMER VEGESSSKGK FLIATVKGDV HDIGKNLVDI ILTNNGYEVI NLGIKQSCEA IIEAQQQHQA DCIAMSGLLV KSTAFMKDNL EAFNEAGITV PVILGGAALT PRFVHGDCRA AYRGQVVYGR DAFADLRFMD ALMDAKAAEG WDDLQGFLHG APEGVELGTS RPAAEGDATA PADPADANDS SSATVHPPAG DHRSEAVPEE PALEPPFWGS RVLSEAAIPL QEVFAYLDRN ALFAGQWQLR KSQQQSREAY EAMLTEKAEP VLQGWMQRCL AEHLLTPRVA YGYFPCGRDG NAVVVFDPEQ RSRPLGRFHL PRQRAGNRYC IADFYRDLAV GPAGEPLPTD VMPMQAVTMG EQATRFAQQL FAADQYTDYL YFHGLAVQMA EALAEWTHAR IRHELGFGDQ EPEALRDVLA QRYRGSRYSF GYPACPNVAD SRQQLDWLGA ERIGLSMDAS DQLEPEQSTT ALVALHSKAR YFSA // ID B5JEM8_9BACT Unreviewed; 318 AA. AC B5JEM8; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 01-OCT-2014, entry version 17. DE SubName: Full=Homocysteine S-methyltransferase, putative {ECO:0000313|EMBL:EDY82469.1}; GN ORFNames=VDG1235_2091 {ECO:0000313|EMBL:EDY82469.1}; OS Verrucomicrobiae bacterium DG1235. OC Bacteria; Verrucomicrobia; Verrucomicrobiae; Verrucomicrobiales. OX NCBI_TaxID=382464 {ECO:0000313|EMBL:EDY82469.1}; RN [1] {ECO:0000313|EMBL:EDY82469.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DG1235 {ECO:0000313|EMBL:EDY82469.1}; RA Hart 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; DS990592; EDY82469.1; -; Genomic_DNA. DR RefSeq; WP_008100286.1; NZ_DS990592.1. DR EnsemblBacteria; EDY82469; EDY82469; VDG1235_2091. DR PATRIC; 29658134; VBIVerBac104321_1931. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDY82469.1}; KW Transferase {ECO:0000313|EMBL:EDY82469.1}. SQ SEQUENCE 318 AA; 34016 MW; 8CE52B4CEDF72F00 CRC64; MDKVRFAGEF FGVNLQIMSK TLIETLREKV LVSDGAMGTQ LMAAGLEAGG SGEMWNLTHP DRVLAIQKRY VDSGSNCIIT NTFGGNGLML RRHGHFDQLA EINQAAVKIA RDAFGGGEGF VFGDVGPVGG VMEPYGDLKP ADVAEGVRIQ IQALVEAGAD AIIIETQTDL NEIALGIEAA KKYGAPCIIA SLAYDKSHDG SFFRTMMGIS PEKAAEELTD LGVDILALNC GTGIDMTVAR EIIEEYKDNS DAFTMAQPNA GLPVLENMKA VYKQTPTEMV STLDALLEEG VNIVGGCCGS NPDHIRAIRE KVDAWNAR // ID B5JNF3_9BACT Unreviewed; 333 AA. AC B5JNF3; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 01-OCT-2014, entry version 17. DE SubName: Full=Homocysteine S-methyltransferase, putative {ECO:0000313|EMBL:EDY84139.1}; GN ORFNames=VDG1235_3769 {ECO:0000313|EMBL:EDY84139.1}; OS Verrucomicrobiae bacterium DG1235. OC Bacteria; Verrucomicrobia; Verrucomicrobiae; Verrucomicrobiales. OX NCBI_TaxID=382464 {ECO:0000313|EMBL:EDY84139.1}; RN [1] {ECO:0000313|EMBL:EDY84139.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DG1235 {ECO:0000313|EMBL:EDY84139.1}; RA Hart 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; DS990592; EDY84139.1; -; Genomic_DNA. DR RefSeq; WP_008103011.1; NZ_DS990592.1. DR EnsemblBacteria; EDY84139; EDY84139; VDG1235_3769. DR PATRIC; 29665124; VBIVerBac104321_1286. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDY84139.1}; KW Transferase {ECO:0000313|EMBL:EDY84139.1}. SQ SEQUENCE 333 AA; 36418 MW; 26A97AD549094874 CRC64; MTNTQSHITH LLNSGQRFVT FAGSETFLLF QRDYPLRDFC AFEILDNEDV WNDFEKTLLV PILDAAAKAG LGIITDSFCW RAAPDHIANL GYAPAELDRF NQLGIDRVSR MVSKWRTENS YDTTQCPVIL ASEIGPRGDG YSVPESEISI EDAKSYHLTQ IKSIAATGAE MVVALTITNL NEAIGIALAA QEAGLPVIIS PTVETNGRLP DGSSLGDFIK QVDDATSSAP SFYLVNCAHP EHLETTLAEA KETNADWLPR FRGLRANASC KSHEELDNST EIDRGDPSDL GEQMAKLTID FDLSVFGGCC GTDSHHIQEM IEAFNKRSAP SLS // ID B5JQJ5_9BACT Unreviewed; 1242 AA. AC B5JQJ5; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 01-APR-2015, entry version 37. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EDY83365.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EDY83365.1}; GN ORFNames=VDG1235_2991 {ECO:0000313|EMBL:EDY83365.1}; OS Verrucomicrobiae bacterium DG1235. OC Bacteria; Verrucomicrobia; Verrucomicrobiae; Verrucomicrobiales. OX NCBI_TaxID=382464 {ECO:0000313|EMBL:EDY83365.1}; RN [1] {ECO:0000313|EMBL:EDY83365.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DG1235 {ECO:0000313|EMBL:EDY83365.1}; RA Hart 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; DS990592; EDY83365.1; -; Genomic_DNA. DR RefSeq; WP_008101658.1; NZ_DS990592.1. DR EnsemblBacteria; EDY83365; EDY83365; VDG1235_2991. DR PATRIC; 29663006; VBIVerBac104321_4341. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EDY83365.1}; KW Transferase {ECO:0000313|EMBL:EDY83365.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 257 257 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 774 774 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1242 AA; 136922 MW; 9BB99271E9F1EA51 CRC64; MSVLDSQSLP LSETFLRLRH LLGERILFLD GAMGTMIQRH KLEEADFRRG HFEGHAKDLK GNNELLSLTR PEIIAEIHKA FLEAGSDIIE TNTFSATTIA QADYGLEHKV KELNVASARV AKQAVADFVA TNPGRECFVA GAIGPTNRTA SLSPDVNRPE YRAVTFDDLR EAYLEQIRAL GEAGVDLFLP ETTFDTLNLK ACIFALEEYF EERGERMPVM LSVTITDASG RTLSGQTIEA FWNSVSHARP LSVGINCALG AQDMRPYIES LSKIADCYIS CYPNAGLPNP LSETGYDELP ADTARFLEDF AQNSFVNLIG GCCGTTPEHI KAIADKAREY PSRPIPVIEP ALRLSGLEPF EVIGEKAPFV MVGERTNVTG SPRFRKLIKE EKFDDALAVA RQQVENGANI IDINFDEGML DSEACMTKFL NLVASEPDIS RVPIMIDSSK WSVIEAGLKC AQGKCVVNSI SLKEGEEKFL QSASLVRRYG AAVIVMAFDE VGQAATRQDK VRICKRAYDL LVEKLNFPPE DIIFDPNILT VGTGMEEHSN YAVDFIEATR EIKERCPHAR VSGGVSNVSF SFRGNNPVRE AIHAAFLYHA IHAGLDMGIV NAGMLAVYDE IDPKLRDLVE DVLLNRSEDA TELLIELAEE VKANSSGKKV EEKIDEWRSG TVEERLSHSL VKGISTFVDE DAEEARLKLA RPLDVIEGPL MDGMKIVGKL FGEGKMFLPQ VVKSARVMKK AVAHLTPFME AEKQDNTSSS RGKIVLATVK GDVHDIGKNI VGVVLSCNNY EIVDLGVMVA CDKILNTARE IGADAIGLSG LITPSLDEMI HAAKEMERQG FKVPLLIGGA TTSKAHTAIK ISEHYSGPVV HVTDASLVVG VCNDLMNPET KDTFIQELDT AQAGLRERHA AGGTNQARLL SLAQAREKAF VPDWVKADLA KPEAYGLKVW EDVDLATVAE YIDWSPFFWT WELKGVYPAI LKSPKYGKQA TELFEDAQVL LKRVIEERRF RLRGVTAFWP ANSEGEDVVL WADESAQQEL ARFHFLRQQK EKVGDDTYYS LADFIAPKAS GRLDALGGFA VTAGEEVEAF AHTFKDAGDD YSAILVQSLG DRFAEALAEY LHKLVREQWG FGKGENLAIV DLIKEKYRGV RPAAGYPACP DHTEKATLWD LLSAEENTGV SLTSSFAMNP GSSVSGLYFG NEEARYFNVG KIERDQVEDY ARRKGIALEV AEKWLMPNLA YS // ID B5JXV6_9GAMM Unreviewed; 1233 AA. AC B5JXV6; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 01-APR-2015, entry version 37. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EDY85561.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EDY85561.1}; GN Name=metH {ECO:0000313|EMBL:EDY85561.1}; GN ORFNames=GP5015_1696 {ECO:0000313|EMBL:EDY85561.1}; OS gamma proteobacterium HTCC5015. OC Bacteria; Proteobacteria; Gammaproteobacteria. OX NCBI_TaxID=391615 {ECO:0000313|EMBL:EDY85561.1}; RN [1] {ECO:0000313|EMBL:EDY85561.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC5015 {ECO:0000313|EMBL:EDY85561.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; DS990614; EDY85561.1; -; Genomic_DNA. DR RefSeq; WP_008285528.1; NZ_DS990614.1. DR EnsemblBacteria; EDY85561; EDY85561; GP5015_1696. DR PATRIC; 25912155; VBIGamPro11258_2172. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EDY85561.1}; KW Transferase {ECO:0000313|EMBL:EDY85561.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 763 763 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1233 AA; 136096 MW; 4A57A9333403CA38 CRC64; MTLQERIDLL QQSLQERIVV LDGGMGTMIQ GLKFSEEQYR GSRFADWHCD VKGNNDLLVL SQPEAIISLH EDYLRAGADI VETNSFNATP IAMADYDMQE LSAEINLEAA RLARRAADNV AKETGRPRFV AGVLGPTNRT ASISPDVNDP GYRNISFDQL VEAYIESTTA LVEGGCDLIL IETIFDTLNA KAAVFAVKSV FETIGTELPI MISGTITDAS GRTLTGQTTE AFYNSLAHAE PYSIGLNCAL GPDELRQYIA ELSRISDFAV SAHPNAGLPN EMGEYDLHPE PMAEQIREWA ESGFLNIVGG CCGTTPEHIE AIAKAVEGVA PRTIKPRPVA CRLSGLEPLT IDKDSLFINV GERTNVTGSK RFLRLIKEGD FDTALEVAQQ QVEAGAQVID INMDEGMLES KEAMVRFLNL IAGEPEISKV PIMIDSSKWE VIEAGLKCIQ GKGIVNSISM KEGVEPFLEQ ARLIRKYGAA VIVMAFDETG QADTRERKTE ICTRAYQLLT EELGFPPQDI IFDPNIFAIA TGIEEHNNYA VDFIEAVRDI KQTLPHAMIS GGVSNVSFSF RGNEPVREAI HAVFLYHAIN EGMDMGIVNA GQLAVLDDVD AKLREAVEDV VLNRRDDATE RLLDMAEEYR DGGSSGGKKV DLAWREWPIN KRLEHSLVKG ITEFVEADTE EARQAAERPL HVIEGPLMDG MNVVGDLFGA GKMFLPQVVK SARVMKKAVA YLLPYMEKEK EEMGTQDESN GTVIMATVKG DVHDIGKNIV GVVLQCNGYD VIDLGVMVPA EDILKAAREH KADVIGLSGL ITPSLDEMVN VAAEMQRQGF ELPLMIGGAT TSKIHTAVKI EPAYEHGVIY VADASRAVGV VSRLLGENKT EYLQDIREDY ASARAKRLAQ SGAKSLMRYQ DACENALKID FKAEDIVTPR DMGVQVFDDY PLDDLRERID WTPFFNAWEL AGKYPRILED DVVGEEAQKL FRDGQAMLDR IISEKWLTAR AVIGLFPASA IGDDIEVYSD ETREHVTTTL HHLRQQTERR GDRPNLCLSD FIAPKDSGLD DYIGAFAVTA GIGIDEHIAR YEADHDDYNA IMLKALADRL AEALAEHMHE RVRKEFWGYA SDENLDNEAL IAEKYRGIRP APGYPACPDH TEKALLWELL KPDETIGLTI TEHFAMLPTA AVSGWYFAHP ESKYLGTGVI GEDQVSDYAA RKGLKKAEAE RWLAPVLGYE PKS // ID B5Q4R7_SALVI Unreviewed; 1227 AA. AC B5Q4R7; DT 04-NOV-2008, integrated into UniProtKB/TrEMBL. DT 04-NOV-2008, sequence version 1. DT 27-MAY-2015, entry version 41. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EDZ02282.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EDZ02282.1}; GN Name=metH {ECO:0000313|EMBL:EDZ02282.1}; GN ORFNames=SeV_B0737 {ECO:0000313|EMBL:EDZ02282.1}; OS Salmonella enterica subsp. enterica serovar Virchow str. SL491. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=465517 {ECO:0000313|EMBL:EDZ02282.1, ECO:0000313|Proteomes:UP000003614}; RN [1] {ECO:0000313|EMBL:EDZ02282.1, ECO:0000313|Proteomes:UP000003614} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SL491 {ECO:0000313|EMBL:EDZ02282.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EDZ02282.1}. 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; ABFH02000001; EDZ02282.1; -; Genomic_DNA. DR RefSeq; WP_000095960.1; NZ_ABFH02000001.1. DR EnsemblBacteria; EDZ02282; EDZ02282; SeV_B0737. DR PATRIC; 25780550; VBISalEnt69786_0726. DR Proteomes; UP000003614; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000003614}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EDZ02282.1}; KW Transferase {ECO:0000313|EMBL:EDZ02282.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136133 MW; 42679538380F7093 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLHEEDFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYRMESLS AEINYAAAKL ARACADEWTA RTPEKPRFVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKEEF EALGVDLPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPEHIAA MSRAVAGLPP RQLPDIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VESGAQIIDI NMDEGMLDAE AAMVRFLSLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVEAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRERKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDEAANAQ QAEWRSWDVK KRLEYSLVKG ITEFIEQDTE EARQQAARPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EKGSSNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAREVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDNQRDDFV ARTRKEYETV RIQHARKKPR TPPVTLEAAR DNDLAFDWER YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KLLNPRGVVG LFPANRVGDD IEIYRDETRT HVLTVSHHLR QQTEKVGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED DLADAYEAQH DDYNKIMVKA IADRLAEAFA EYLHERVRKV YWGYAPNESL SNDELIRENY QGIRPAPGYP ACPEHTEKGT IWQLLDVEKH TGMKLTESFA MWPGASVSGW YFSHPESKYF AVAQIQRDQV TDYAFRKGMS VEDVERWLAP NLGYDAD // ID B5QYG9_SALEP Unreviewed; 1227 AA. AC B5QYG9; DT 04-NOV-2008, integrated into UniProtKB/TrEMBL. DT 04-NOV-2008, sequence version 1. DT 27-MAY-2015, entry version 53. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CAR35539.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAR35539.1}; GN Name=metH {ECO:0000313|EMBL:CAR35539.1}; GN OrderedLocusNames=SEN3970 {ECO:0000313|EMBL:CAR35539.1}; OS Salmonella enteritidis PT4 (strain P125109). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=550537 {ECO:0000313|EMBL:CAR35539.1, ECO:0000313|Proteomes:UP000000613}; RN [1] {ECO:0000313|EMBL:CAR35539.1, ECO:0000313|Proteomes:UP000000613} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P125109 {ECO:0000313|EMBL:CAR35539.1, RC ECO:0000313|Proteomes:UP000000613}; 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., Sanders M., Whitehead S., Chabalgoity J.A., RA Maskell D., Humphrey 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AM933172; CAR35539.1; -; Genomic_DNA. DR RefSeq; WP_000095957.1; NC_011294.1. DR RefSeq; YP_002246013.1; NC_011294.1. DR STRING; 550537.SEN3970; -. DR EnsemblBacteria; CAR35539; CAR35539; SEN3970. DR PATRIC; 32338675; VBISalEnt14964_4053. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SENT550537:GJFI-4042-MONOMER; -. DR Proteomes; UP000000613; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000613}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAR35539.1}; KW Transferase {ECO:0000313|EMBL:CAR35539.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135887 MW; 0D576C29541D67D6 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLHEEDFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYRMESLS AEINYAAAKL ARACADEWTA RTPEKPRFVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKEEF EALGVDLPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPEHIAA MSRAVAGLLP RQLPDIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VESGAQIIDI NMDEGMLDAE AAMVRFLSLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVEAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLDLAEKYRG SKTDEAANAQ QAEWRSWDVK KRLEYSLVKG ITEFIEQDTE EARQQAARPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EKGSSNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAREVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDNQRDDFV ARTRKEYETV RIQHARKKPR TPPVTLEAAR DNDLAFDWER YTPPVAHRLG VQGVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KLLNPRGVVG LFPANRVGDD IEIYRDATRT HVLTVSHHLR QQTEKVGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA IADRLAEAFA EYLHERVRKV YWGYAPNESL SNDELIRENY QGIRPAPGYP ACPEHTEKGT IWQLLDVEKH TGMKLTESFA MWPGASVSGW YFSHPESKYF AVAQIQRDQV TDYAFRKGMS VEDVERWLAP NLGYDAD // ID B5R7Q7_SALG2 Unreviewed; 1227 AA. AC B5R7Q7; DT 04-NOV-2008, integrated into UniProtKB/TrEMBL. DT 04-NOV-2008, sequence version 1. DT 27-MAY-2015, entry version 53. DE SubName: Full=B12-dependent homocysteine-N5-methyltetrahydrofolate transmethylase {ECO:0000313|EMBL:CAR39818.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAR39818.1}; GN Name=metH {ECO:0000313|EMBL:CAR39818.1}; GN OrderedLocusNames=SG4048 {ECO:0000313|EMBL:CAR39818.1}; OS Salmonella gallinarum (strain 287/91 / NCTC 13346). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=550538 {ECO:0000313|EMBL:CAR39818.1, ECO:0000313|Proteomes:UP000008321}; RN [1] {ECO:0000313|EMBL:CAR39818.1, ECO:0000313|Proteomes:UP000008321} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=287/91 / NCTC 13346 {ECO:0000313|Proteomes:UP000008321}; 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., Sanders M., Whitehead S., Chabalgoity J.A., RA Maskell D., Humphrey 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AM933173; CAR39818.1; -; Genomic_DNA. DR RefSeq; WP_000095957.1; NC_011274.1. DR RefSeq; YP_002228781.1; NC_011274.1. DR STRING; 550538.SG4048; -. DR EnsemblBacteria; CAR39818; CAR39818; EBG00000233843. DR PATRIC; 18506897; VBISalEnt1629_4302. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SENT550538:GJ93-3999-MONOMER; -. DR Proteomes; UP000008321; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008321}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAR39818.1}; KW Transferase {ECO:0000313|EMBL:CAR39818.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135887 MW; 0D576C29541D67D6 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLHEEDFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYRMESLS AEINYAAAKL ARACADEWTA RTPEKPRFVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKEEF EALGVDLPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPEHIAA MSRAVAGLLP RQLPDIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VESGAQIIDI NMDEGMLDAE AAMVRFLSLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVEAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLDLAEKYRG SKTDEAANAQ QAEWRSWDVK KRLEYSLVKG ITEFIEQDTE EARQQAARPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EKGSSNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAREVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDNQRDDFV ARTRKEYETV RIQHARKKPR TPPVTLEAAR DNDLAFDWER YTPPVAHRLG VQGVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KLLNPRGVVG LFPANRVGDD IEIYRDATRT HVLTVSHHLR QQTEKVGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA IADRLAEAFA EYLHERVRKV YWGYAPNESL SNDELIRENY QGIRPAPGYP ACPEHTEKGT IWQLLDVEKH TGMKLTESFA MWPGASVSGW YFSHPESKYF AVAQIQRDQV TDYAFRKGMS VEDVERWLAP NLGYDAD // ID B5U888_STRCL Unreviewed; 133 AA. AC B5U888; DT 04-NOV-2008, integrated into UniProtKB/TrEMBL. DT 04-NOV-2008, sequence version 1. DT 29-OCT-2014, entry version 19. DE SubName: Full=Putative 5-methyltetrahydrofolate:homocysteine S-methyltransferase {ECO:0000313|EMBL:CAR66238.1}; DE Flags: Fragment; GN Name=metH {ECO:0000313|EMBL:CAR66238.1}; OS Streptomyces clavuligerus. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1901 {ECO:0000313|EMBL:CAR66238.1}; RN [1] {ECO:0000313|EMBL:CAR66238.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27064 {ECO:0000313|EMBL:CAR66238.1}; RA Heijne W.H.M.; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CAR66238.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27064 {ECO:0000313|EMBL:CAR66238.1}; RA Banos S., Perez-Redondo R., Koekman B., Liras P.; RT "Glycerol utilization gene cluster in Streptomyces clavuligerus."; RL Appl. Environ. Microbiol. 75:2991-2995(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; FM210760; CAR66238.1; -; Genomic_DNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:CAR66238.1}; KW Transferase {ECO:0000313|EMBL:CAR66238.1}. FT NON_TER 133 133 {ECO:0000313|EMBL:CAR66238.1}. SQ SEQUENCE 133 AA; 14278 MW; 444918232DDD5A33 CRC64; MATLPTPSAP SADARSRIDA LREALATRVV VADGAMGTML QAQDPSLEDF QDLEGCNEIL NVTRPDIVRS VHAEYFDAGV DCVETNTFGA NLAALGEYDI PERVYELSEA GARIARETAD AYTASTGAQR WVL // ID B5UT51_BACCE Unreviewed; 1132 AA. AC B5UT51; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 27-MAY-2015, entry version 36. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EDZ51172.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EDZ51172.1}; GN Name=metH {ECO:0000313|EMBL:EDZ51172.1}; GN ORFNames=BCAH1134_4344 {ECO:0000313|EMBL:EDZ51172.1}; OS Bacillus cereus AH1134. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=405533 {ECO:0000313|EMBL:EDZ51172.1}; RN [1] {ECO:0000313|EMBL:EDZ51172.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AH1134 {ECO:0000313|EMBL:EDZ51172.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EDZ51172.1}. 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; ABDA02000006; EDZ51172.1; -; Genomic_DNA. DR RefSeq; WP_000649670.1; NZ_ABDA02000006.1. DR EnsemblBacteria; EDZ51172; EDZ51172; BCAH1134_4344. DR PATRIC; 24780783; VBIBacCer51833_3953. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EDZ51172.1}; KW Transferase {ECO:0000313|EMBL:EDZ51172.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 125883 MW; 495F70BD8782014C CRC64; MKCIEEKLKN SILILDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVDTRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYKLSHLDE ELNEKAALLA KQAVKESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGA VDVLLVETSQ DMRNVKAAYI GIQAAFEELK KTVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWVN IIGGCCGTTP EHIKAMKSAL ASLKPRDHHE REGHGISGLE ALQYDESMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMENF LAEVTKVLKV PIMIDSTDEN VMERALTYIQ GKAVINSINL EDGEERFKKV TPLLQKYGAA IVVGTIDEDG MAVSAERKIE IAKRSYELLT KKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPEE EKRLADALLF ETTKETLEEF TNFYRVAKKK DIVVQETLTL DERLANYIVE GTKQGLHEDL SLALEEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILA NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAANIDVPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV KKEEKKVEIP AVIEPLPKAE VIVPDSTKRI VLRDIPALHL APFLNRQMLL GHHLGLKGNV KKLLKEGDKR AHELNDLIDE LLQEGQSWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRVIE RFTFPRQGKA PYRTLGDYLR PIGDEMDYVA FLSVTVGEGV RDIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID B5UT52_BACCE Unreviewed; 610 AA. AC B5UT52; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 27-MAY-2015, entry version 28. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=BCAH1134_4345 {ECO:0000313|EMBL:EDZ51070.1}; OS Bacillus cereus AH1134. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=405533 {ECO:0000313|EMBL:EDZ51070.1}; RN [1] {ECO:0000313|EMBL:EDZ51070.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AH1134 {ECO:0000313|EMBL:EDZ51070.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDZ51070.1}. 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; ABDA02000006; EDZ51070.1; -; Genomic_DNA. DR RefSeq; WP_000770360.1; NZ_ABDA02000006.1. DR ProteinModelPortal; B5UT52; -. DR EnsemblBacteria; EDZ51070; EDZ51070; BCAH1134_4345. DR PATRIC; 24780785; VBIBacCer51833_3954. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EDZ51070.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EDZ51070.1}. SQ SEQUENCE 610 AA; 67241 MW; 2994E829027824F4 CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNVSDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTK INRAAVKLAK ASVTDKNAIL GTIGGMKHIG AVTTTDMERE FMLLEQAGAL LEEQVDGLLL ETFYDEFELL HAVKVLRKQT NIPIVAQLAL HEAGTTQNGN DVNEILKQFI DYGANVVGLN CQLGPLHMTE AFKMISIPQN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPKFIEQGI RLLGGCCGTT PEHIQSMKRA VANITPVIEK ETIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRVSNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIK LIEEVYEATK HLEQPIFIGI MPLVSKRNAD FLHFEVPGIT LPEEIRERMD GHETKEAAIE EGIRISQELV DAAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID B5VMP4_YEAS6 Unreviewed; 324 AA. AC B5VMP4; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 07-JAN-2015, entry version 26. DE SubName: Full=YLL062Cp-like protein {ECO:0000313|EMBL:EDZ70799.1}; GN ORFNames=AWRI1631_120020 {ECO:0000313|EMBL:EDZ70799.1}; OS Saccharomyces cerevisiae (strain AWRI1631) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=545124 {ECO:0000313|EMBL:EDZ70799.1, ECO:0000313|Proteomes:UP000008988}; RN [1] {ECO:0000313|EMBL:EDZ70799.1, ECO:0000313|Proteomes:UP000008988} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AWRI1631 {ECO:0000313|EMBL:EDZ70799.1, RC ECO:0000313|Proteomes:UP000008988}; RX PubMed=18778279; DOI=10.1111/j.1567-1364.2008.00434.x; RA Borneman A.R., Forgan A.H., Pretorius I.S., Chambers P.J.; RT "Comparative genome analysis of a Saccharomyces cerevisiae wine RT strain."; RL FEMS Yeast Res. 8:1185-1195(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. {ECO:0000313|EMBL:EDZ70799.1}. 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; ABSV01001530; EDZ70799.1; -; Genomic_DNA. DR ProteinModelPortal; B5VMP4; -. DR SMR; B5VMP4; 3-313. DR OrthoDB; EOG7X9GHR; -. DR Proteomes; UP000008988; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008988}. SQ SEQUENCE 324 AA; 36715 MW; A77194694B6E5C14 CRC64; MKRIPIKELI VEHPGKVLIL DGGQGTELEN RGININSPVW SAAPFTSESF WEPSSQERKV VEEMYRDFMI AGANILMTIT YQANFQSISE NTSIKTLAAY KRFLDKIVSF TREFIGEERY LIGSIGPWAA HVSCEYTGDY GPHPENIDYY GFFKPQLENF NQNRDIDLIG FETIPNFHEL KAILSWDEDI ISKPFYIGLS VDDNSLLRDG TTLEEISVHI KGLGNKINKN LLLMGVNCVS FNQSALILKM LHEHLPGMPL LVYPNSGEIY NPKEKTWHRP TNKLDDWETT VKKFVDNGAR IIGGCCRTSP KDIAEIASAV DKYS // ID B5VSR6_YEAS6 Unreviewed; 261 AA. AC B5VSR6; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=YPL273Wp-like protein {ECO:0000313|EMBL:EDZ69030.1}; GN ORFNames=AWRI1631_160040 {ECO:0000313|EMBL:EDZ69030.1}; OS Saccharomyces cerevisiae (strain AWRI1631) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=545124 {ECO:0000313|EMBL:EDZ69030.1, ECO:0000313|Proteomes:UP000008988}; RN [1] {ECO:0000313|EMBL:EDZ69030.1, ECO:0000313|Proteomes:UP000008988} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AWRI1631 {ECO:0000313|EMBL:EDZ69030.1, RC ECO:0000313|Proteomes:UP000008988}; RX PubMed=18778279; DOI=10.1111/j.1567-1364.2008.00434.x; RA Borneman A.R., Forgan A.H., Pretorius I.S., Chambers P.J.; RT "Comparative genome analysis of a Saccharomyces cerevisiae wine RT strain."; RL FEMS Yeast Res. 8:1185-1195(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. {ECO:0000313|EMBL:EDZ69030.1}. 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; ABSV01002270; EDZ69030.1; -; Genomic_DNA. DR ProteinModelPortal; B5VSR6; -. DR OrthoDB; EOG7X9GHR; -. DR Proteomes; UP000008988; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008988}. SQ SEQUENCE 261 AA; 29529 MW; 033A9E74EBAE569C CRC64; MFNDFLNAGA EILMTTTYQT SYKSVSENTP IRTLSEYNNL LNRIVDFSRN CIGEDKYLIG CIGPWGAHIC REFTGDYGAE PENIDFYQYF KPQLENFNKN DKLDLIGFET IPNIHELKAI LSWDESILSR PFYIGLSVHE HGVLRDGTTM EEIAQVIKDL GDKINPNFSF LGINCVSFNQ SPDILESLHQ ALPNMALLAY PNSGEVYDTE KKIWLPNSDK LNSWDTVVKQ YISSGARIIG GCCRTSPKDI QEISAAVKKY T // ID B5VXJ7_ARTMA Unreviewed; 1181 AA. AC B5VXJ7; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 27-MAY-2015, entry version 41. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EDZ96202.1}; GN ORFNames=AmaxDRAFT_1239 {ECO:0000313|EMBL:EDZ96202.1}; OS Arthrospira maxima CS-328. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Arthrospira. OX NCBI_TaxID=513049 {ECO:0000313|EMBL:EDZ96202.1}; RN [1] {ECO:0000313|EMBL:EDZ96202.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CS-328 {ECO:0000313|EMBL:EDZ96202.1}; 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] {ECO:0000313|EMBL:EDZ96202.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CS-328 {ECO:0000313|EMBL:EDZ96202.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EDZ96202.1}. 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; ABYK01000006; EDZ96202.1; -; Genomic_DNA. DR RefSeq; WP_006668594.1; NZ_ABYK01000006.1. DR EnsemblBacteria; EDZ96202; EDZ96202; AmaxDRAFT_1239. DR PATRIC; 24528500; VBIArtMax3094_1353. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 228 228 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 737 737 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1181 AA; 130848 MW; A63A3D6BA48BEFC1 CRC64; MESLFLQRLH SPQRPVIIFD GAMGTNLQVQ NLTAEDFGGK EYEGCNEYLV HTKPEAVATV HRQFLQAGAD VIETDTFGGT SIVLAEYDLA DQAYQLNKTA ATLAKSVTAE FSSPEKPRFV AGSMGPGTKL PTLGHIDFDT LERAFCQQAE GLFDGGVDLF IVETCQDVLQ IKAALNGIEE VFKMKGERRP IMVSVTMEAF GTMLVGSEIN AALTILEPYK IDILGLNCAT GPDLMKEHIA YLSEHSPFVV SCIPNAGLPE NVGGQAHYKL TPLELKMALM HFIEDLGVQV IGGCCGTRPD HIKALAEIAQ TLTPKPRHPQ ITPSAASIYS TVSYEQENSF LIVGERLNAS GSKKCRDLLN AEDWDGLVAL AKAQVKEGAQ ILDVNVDYVG RNGVRDMHEL VSRLVTNVNL PLMLDSTEWE KMEAGLKVAG GKCLLNSTNY EDGEPRFYKV LELAKKYGAG VVVGTIDEEG MARTATKKFA IAKRAYNDAI AFGIAATEIF FDPLALPIST GIEEDRENGK ATIEAINQMR QELPGCHILL GISNISFGLN PAARQVLNSV FLHETMAVGL DSAIVTANKI LPLAKIEPEH QEVCRHLIYD QRQFDGDVCT YDPLTKLTTL FEGKTTKRDR SGDANLPIEE RLKQHIIDGE RIGLEDALAE ALKKYPPLDI INIFLLDGMK VVGELFGSGQ MQLPFVLQSA QTMKAAVAYL EPFMEKSESG NNAKGTFVIA TVKGDVHDIG KNLVDIILSN NGYKVVNLGI KQPVDNIIAA YREHNADCIA MSGLLVKSTA FMKDNLEVFN QEGITVPVIL GGAALTSKFV YEDCQNTYKG RVIYGKDAFS DLTFMDKLMP AKKSGKWEDF KGFLDEFVED ETITANGDNQ QSAQPDQPEP DTPKVVDTRR SEAVAVDIDR PTPPFWGVKV LEPADMPFDE LFWYLDLQAL TAGQWQFRKP QGQPRSEYNQ FLEAKVYPIL AEWKQRIISE NLLHPRAVYG YFPCQSEGNT LLIYDPEKIK AGEISEPITS FEFPRQRSGR RLCIADFFAP KDSGQMDVFP MHAVTVGQIA TDYAQKLFAA DDYTNYLYFH GMAVQTAEAM AEWLHARIRR ELGFGGEDAD NIRDILKQRY RGSRYSFGYP ACPNMQDQYK QLDLLKAEVI GLYMDESEQL YPEQSTTAII TYHPAAKYFS A // ID B5WJQ9_9BURK Unreviewed; 356 AA. AC B5WJQ9; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEA01350.1}; GN ORFNames=BH160DRAFT_3312 {ECO:0000313|EMBL:EEA01350.1}; OS Burkholderia sp. H160. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=516466 {ECO:0000313|EMBL:EEA01350.1}; RN [1] {ECO:0000313|EMBL:EEA01350.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=H160 {ECO:0000313|EMBL:EEA01350.1}; 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] {ECO:0000313|EMBL:EEA01350.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=H160 {ECO:0000313|EMBL:EEA01350.1}; 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. {ECO:0000313|EMBL:EEA01350.1}. 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; ABYL01000043; EEA01350.1; -; Genomic_DNA. DR RefSeq; WP_008920302.1; NZ_ABYL01000043.1. DR EnsemblBacteria; EEA01350; EEA01350; BH160DRAFT_3312. DR PATRIC; 30431830; VBIBurSp89998_3206. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEA01350.1}; KW Transferase {ECO:0000313|EMBL:EEA01350.1}. SQ SEQUENCE 356 AA; 38376 MW; 99DC34A795A627A4 CRC64; MTQPAQTATP VRSETAYTRG AALPALMNSR ILILDGAMGT MIQRYKLDEA RYRGERFKDY PRDIKGNNEL LSITQPQIIS EIHEQYLAAG ADIIETNTFG ATTVAQADYG MESLAVEMNL ESAKLARAAC DKYSTPDKPR FVAGAIGPTP KTASISPDVN DPGARNVTFD ELRTAYYEQA KALLDGGADL FLVETIFDTL NAKAALFALD ELFEDTGERL PIMISGTVTD ASGRILSGQT VEAFWNSLRH AKPLTFGLNC ALGAALMRPY IAELAKLCDT YVSCYPNAGL PNPMSDTGFD ELPADTSGLL KEFAEAGLVN VAGGCCGTTP EHIAAIAKAL AELKPRKWPT QYRDAA // ID B5X0U2_SALSA Unreviewed; 335 AA. AC B5X0U2; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 01-OCT-2014, entry version 16. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACI32923.1}; GN Name=MMUM {ECO:0000313|EMBL:ACI32923.1}; OS Salmo salar (Atlantic salmon). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; OC Salmoniformes; Salmonidae; Salmoninae; Salmo. OX NCBI_TaxID=8030 {ECO:0000313|EMBL:ACI32923.1}; RN [1] {ECO:0000313|EMBL:ACI32923.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Brain {ECO:0000313|EMBL:ACI32923.1}; RG cGRASP (B.F. Koop & W.S. Davidson); RA Leong J., von Schalburg K., Cooper G., Moore R., Holt R., RA Davidson W.S., Koop B.F.; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACI32923.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Brain {ECO:0000313|EMBL:ACI32923.1}; RX PubMed=20433749; DOI=10.1186/1471-2164-11-279; RA Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., RA Messmer A.M., Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., RA Davidson W.S., Koop B.F.; RT "Salmo salar and Esox lucius full-length cDNA sequences reveal changes RT in evolutionary pressures on a post-tetraploidization genome."; RL BMC Genomics 11:279-279(2010). RN [3] {ECO:0000313|EMBL:ACI32923.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Brain {ECO:0000313|EMBL:ACI32923.1}; RG cGRASP (B.F. Koop & W.S. Davidson); 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; BT044661; ACI32923.1; -; mRNA. DR RefSeq; NP_001133262.1; NM_001139790.1. DR UniGene; Ssa.7383; -. DR GeneID; 100194761; -. DR CTD; 100194761; -. DR HOVERGEN; HBG062720; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Methyltransferase {ECO:0000313|EMBL:ACI32923.1}; KW Transferase {ECO:0000313|EMBL:ACI32923.1}. SQ SEQUENCE 335 AA; 36489 MW; E474209690465949 CRC64; MDKTDILKPF MDVGRGPLII DGGLATELES TGCKLQGDPL WSARLLHTNP QTIKDAHYRF LCAGADVITT ATYQASVEGF TRHLDVTPEQ ANQLIMSGVT LARETVKHFM ADQPPSDRRV PLVAGSVGPY GAFLHNGSEY TGAYAAEMSV EELKAWHRPQ VHCLVTAGVD LIAMETIPSV KEAEALVELL REFPDSKAWL AFSCKDGQCI SDSSRFSEAV LLASRSSQLV AVGVNCCPPA LVKPLLDSAR TQRRPGLGWV VYPNSGEEWD TYSGWRKPEN RLSSIAELSL EWMKQGSALI GGCCRISPAH IAELRRQIHG NMSGSDASQR GQGRP // ID B5XY19_KLEP3 Unreviewed; 1227 AA. AC B5XY19; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 27-MAY-2015, entry version 51. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACI07164.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ACI07164.1}; GN Name=metH {ECO:0000313|EMBL:ACI07164.1}; GN OrderedLocusNames=KPK_5275 {ECO:0000313|EMBL:ACI07164.1}; OS Klebsiella pneumoniae (strain 342). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=507522 {ECO:0000313|EMBL:ACI07164.1, ECO:0000313|Proteomes:UP000001734}; RN [1] {ECO:0000313|EMBL:ACI07164.1, ECO:0000313|Proteomes:UP000001734} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=342 {ECO:0000313|EMBL:ACI07164.1, RC ECO:0000313|Proteomes:UP000001734}; 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.W., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000964; ACI07164.1; -; Genomic_DNA. DR RefSeq; WP_008807326.1; NC_011283.1. DR RefSeq; YP_002241046.1; NC_011283.1. DR STRING; 507522.KPK_5275; -. DR EnsemblBacteria; ACI07164; ACI07164; KPK_5275. DR KEGG; kpe:KPK_5275; -. DR PATRIC; 20443648; VBIKlePne121904_5152. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; KPNE507522:GI0B-5276-MONOMER; -. DR Proteomes; UP000001734; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001734}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACI07164.1}; KW Transferase {ECO:0000313|EMBL:ACI07164.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135805 MW; A1C2039B885B17F2 CRC64; MSSKVEQLHQ QLKERILVLD GGMGTMIQGY RLSEQDFRGE RFADWPCDLK GNNDLLVLSK PEVIREIHDA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARASADAWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTRAL VEGGVDLILI ETVFDTLNAK AAIYAVKEEL EALGVDLPLM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LSFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MATQIREWAE AGFLNIVGGC CGTTPEHIAA MSRAVAGLPP RQLPELPVAC RLAGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VESGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVEPFIHHA KLVRRYGAAV VVMAFDEVGQ ADTRERKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPG ELRDAVEDVI LNRRDDSTER LLELAEKYRG SKADDGANAQ QAEWRSWDVK KRLEYSLVKG ITEFIEQDTE EARQQAARPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPYIEASK EQGSSNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIIDL GVMVPADKIL KTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLAAAR ENDLAFDWES YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG EEAQRLFKDA NDLLDKLSAE KTLNPRGVVG LFPANRIGDD IEIYRDETRT HVLTVSHHLR QQTEKVGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAYEAQH DDYNKIMIKA IADRLAEAFA EYLHEKVRKV YWGYAANENL SNEELIRENY QGIRPAPGYP ACPEHTEKGT IWQLLDVEAH TGMKLTESFA MWPGASVSGW YFSHPDSKYF AVAQIQRDQV EDYALRKGMT PAEVERWLAP NLGYDAD // ID B5Y137_KLEP3 Unreviewed; 310 AA. AC B5Y137; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 27-MAY-2015, entry version 36. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACI10937.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ACI10937.1}; GN Name=mmuM {ECO:0000313|EMBL:ACI10937.1}; GN OrderedLocusNames=KPK_4378 {ECO:0000313|EMBL:ACI10937.1}; OS Klebsiella pneumoniae (strain 342). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=507522 {ECO:0000313|EMBL:ACI10937.1, ECO:0000313|Proteomes:UP000001734}; RN [1] {ECO:0000313|EMBL:ACI10937.1, ECO:0000313|Proteomes:UP000001734} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=342 {ECO:0000313|EMBL:ACI10937.1, RC ECO:0000313|Proteomes:UP000001734}; 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.W., 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 ----------------------------------------------------------------------- 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; ACI10937.1; -; Genomic_DNA. DR RefSeq; WP_008805330.1; NC_011283.1. DR RefSeq; YP_002240178.1; NC_011283.1. DR STRING; 507522.KPK_4378; -. DR EnsemblBacteria; ACI10937; ACI10937; KPK_4378. DR KEGG; kpe:KPK_4378; -. DR PATRIC; 20441960; VBIKlePne121904_4330. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; KPNE507522:GI0B-4379-MONOMER; -. DR Proteomes; UP000001734; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001734}; KW Methyltransferase {ECO:0000313|EMBL:ACI10937.1}; KW Transferase {ECO:0000313|EMBL:ACI10937.1}. SQ SEQUENCE 310 AA; 33231 MW; 7FDF9C6765003029 CRC64; MSQTNPFTAL LAAQPYVLLD GAMATELEAR GCDLADSLWS AKVLLENPQL IRDVHLDYFR AGAQVAITAS YQATPAGFAA RGLDDAQSRA LIGKSVELAR KAREAYLAEN PQAGTLLVAG SVGPYGAFLA DGSEYRGDYQ RSAAEFQDFH RPRVEALLDA GADLLACETL PSFAEIQALT ALLQDYPRAR AWYSFTLRDA EHLSDGTPLR EVMAALADNP QVVAVGINCI ALENTPAALA HLHSLTALPL VVYPNSGEHY DAVSKTWHHH GEACATLADY LPQWLAAGAK LIGGCCRTTP KDIAALNAKR // ID B5Y6I8_COPPD Unreviewed; 775 AA. AC B5Y6I8; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 01-APR-2015, entry version 40. DE SubName: Full=5-methyltetrahydrofolate S-homocysteine methyltransferase {ECO:0000313|EMBL:ACI17204.1}; GN OrderedLocusNames=COPRO5265_0013 {ECO:0000313|EMBL:ACI17204.1}; OS Coprothermobacter proteolyticus (strain ATCC 35245 / DSM 5265 / BT). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermodesulfobiaceae; Coprothermobacter. OX NCBI_TaxID=309798 {ECO:0000313|EMBL:ACI17204.1, ECO:0000313|Proteomes:UP000001732}; RN [1] {ECO:0000313|Proteomes:UP000001732} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35245 / DSM 5265 / BT {ECO:0000313|Proteomes:UP000001732}; 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 ----------------------------------------------------------------------- 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; ACI17204.1; -; Genomic_DNA. DR RefSeq; WP_012543856.1; NC_011295.1. DR RefSeq; YP_002246385.1; NC_011295.1. DR STRING; 309798.COPRO5265_0013; -. DR EnsemblBacteria; ACI17204; ACI17204; COPRO5265_0013. DR KEGG; cpo:COPRO5265_0013; -. DR PATRIC; 21472914; VBICopPro72829_0013. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CPRO309798:GH7M-13-MONOMER; -. DR Proteomes; UP000001732; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001732}; KW Methyltransferase {ECO:0000313|EMBL:ACI17204.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001732}; KW Transferase {ECO:0000313|EMBL:ACI17204.1}. SQ SEQUENCE 775 AA; 84962 MW; 72E769368CAB01E6 CRC64; MNRKTFLELL SERVLFLDGA YGTEFFKQGY KGAVELLNID TPKVVEDLQK AYAEAGADVV LTNTFSANRL KLRSMGLEEY IRKINENAVK IARHAAPGKL VLGDMSSTGM FVRPLGDLDF EEAYNVFREQ AALLIDAGVD GIIVETMSDL KELKAAILAI RNVSTDIPLI AHMTFEADGI SVTGTSVEIF ATLMNDLDVD VVGINCTLEP KDMLPVFMRL AEYCHKPLSV EPNAGKPLYN KGVLTYKSTP EEFAVYMADF VELGANLVGG CCGTGPDHIA LMSKYVGKQK PRQRTVRNDQ FLSSRTVIKT VEPFLVIGER INASGRKKLQ KSFQDMDYTE ILNLARKQEE EGSAVIDVNL GIEKLLTHEH FKQAVLELDR VSSLPLSLDI QDAAFLETAM REYVGRPLIN SALAREEHLN SRLALLKKYG GMLIVLTMEK DIPQTAQERL SVAKKAVEII KANGVDLKRV FFDPLVLPLG AGSDYHVTLN TIKLLTESGL QTSIGLSNLS FGLPNRESIN AAFLGLSVEN GLSAAILNSK EATTMNVLQG CLALKGKQLG TTQNAIDDEL VNLIVKGQKD ALLEFTKQQL KEHDPLYVSQ HILAEAMQKV GELYAKGVIY LPHLILAAET VQPCFDYLNS LLGEAQVKLG KVLLATVHGD IHDIGKNIVA TVLRSGGFDV YDVGKDVPAH TILEACQEYK PDIVGLSAMM TTTVSRVKEV VDMLKANNIQ AFVIAGGASM NRQLADEFGV EYAKDAMEAL QICKAFMERK GGNEP // ID B5YB64_DICT6 Unreviewed; 289 AA. AC B5YB64; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 27-MAY-2015, entry version 33. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|EMBL:ACI18984.1}; GN OrderedLocusNames=DICTH_1778 {ECO:0000313|EMBL:ACI18984.1}; OS Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12). OC Bacteria; Dictyoglomi; Dictyoglomales; Dictyoglomaceae; Dictyoglomus. OX NCBI_TaxID=309799 {ECO:0000313|EMBL:ACI18984.1, ECO:0000313|Proteomes:UP000001733}; RN [1] {ECO:0000313|Proteomes:UP000001733} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35947 / DSM 3960 / H-6-12 RC {ECO:0000313|Proteomes:UP000001733}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; ACI18984.1; -; Genomic_DNA. DR RefSeq; WP_012547616.1; NC_011297.1. DR RefSeq; YP_002251589.1; NC_011297.1. DR STRING; 309799.DICTH_1778; -. DR EnsemblBacteria; ACI18984; ACI18984; DICTH_1778. DR KEGG; dth:DICTH_1778; -. DR PATRIC; 21808178; VBIDicThe33784_1716. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265278; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; DTHE309799:GHF9-1762-MONOMER; -. DR Proteomes; UP000001733; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001733}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ACI18984.1}; KW Transferase {ECO:0000313|EMBL:ACI18984.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 206 206 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 271 271 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 272 272 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 289 AA; 32075 MW; 7B7BA2DB14FF7402 CRC64; MNRKIKLPEF LFFDGAMGTE LQRRGLPPGT PPEVLNLENP TLVEEVHRDY IKAGSMVIET NTFGGNRIRL KRAGLDGKIK EINEKGVEIA KKASEGKVLI AGSVGPLGEL IEPYGDISEE EAEEVFTEQI EILVKSGVDL ILIETMISLN EALIALKSAK KFDIPVGVTM SFEWTERGGR TPFGDEVEYS IKTLEENGAD FVGANCGRGF EDMIKIAPII RKATTLPVLI QPNAGIPQWE NGKLTYPETP DKFKIFVEEM LKLNINFIGG CCGTTPNHIE VFKEFYLKR // ID B5ZX98_RHILW Unreviewed; 1257 AA. AC B5ZX98; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 27-MAY-2015, entry version 49. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACI55922.1}; GN OrderedLocusNames=Rleg2_2651 {ECO:0000313|EMBL:ACI55922.1}; OS Rhizobium leguminosarum bv. trifolii (strain WSM2304). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=395492 {ECO:0000313|EMBL:ACI55922.1, ECO:0000313|Proteomes:UP000008330}; RN [1] {ECO:0000313|Proteomes:UP000008330} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WSM2304 {ECO:0000313|Proteomes:UP000008330}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001191; ACI55922.1; -; Genomic_DNA. DR RefSeq; WP_012558413.1; NC_011369.1. DR RefSeq; YP_002282148.1; NC_011369.1. DR ProteinModelPortal; B5ZX98; -. DR SMR; B5ZX98; 666-1244. DR STRING; 395492.Rleg2_2651; -. DR EnsemblBacteria; ACI55922; ACI55922; Rleg2_2651. DR KEGG; rlt:Rleg2_2651; -. DR PATRIC; 23129408; VBIRhiLeg95088_4523. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; RLEG395492:GJB3-2686-MONOMER; -. DR Proteomes; UP000008330; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008330}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 260 260 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 776 776 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1257 AA; 138849 MW; D5F39D7F179C62DF CRC64; MFDTLFGPET GKRDGNEVFA ALRKAASERI LVLDGAMGTQ IQGLGYDEDQ FRGTRFIGCA CHQKGNNDLL ILTQPDAIEE IHYKYAKAGA DILETNTFSS TRIAQADYEM EGAVYDLNKE GAEIVRRAAL RAEREDGRRR FVAGAIGPTN RTASISPDVN NPGFRAVTFD DLRSAYGEQI DGLIDGGADI ILIETIFDTL NAKAAIFACE ERFEAKGVRL PVMISGTITD LSGRTLSGQT PSAFWNSVRH ANPFTIGLNC ALGANAMRPH LQELSGVADT FICAYPNAGL PNEFGQYDET PELMAAQIDS FAREGLVNIV GGCCGSTPEH IRAIAETVAK YKPRPLPEHR PFMSLSGLEP FELTKDIPFV NVGERTNVTG SAKFRKLITN HDYTAALDVA RDQVENGAQV IDINMDEGLI DSEKAMVEFL NLIAAEPDIA RVPVMIDSSK FSIIESGLKR VQGKPIVNSI SLKEGEENFL AQARLLHNYG AAVVVMAFDE TGQADSYERK VEICTRAYKL LTEKIGFPPE DIIFDPNIFA VATGIEEHNN YGVDFIEATR TIRERMPLVH ISGGVSNLSF SFRGNEPVRE AMHAVFLYHA IQAGMDMGIV NAGQLAVYDN IDPELREACE DVVLNRRPDG TERLLEVAER FRGAGAREGR VQDLSWREWS VEKRLEHALV NGITEYIEAD TEEARQQAAR PLHVIEGPLM AGMNVVGDLF GSGKMFLPQV VKSARVMKQA VAVLLPYMEE EKRLNGGEER RSAGKILMAT VKGDVHDIGK NIVGVVLACN NYEIVDLGVM VPATKILDTA IAEKVDIIGL SGLITPSLDE MVHVAAEMER QGFDIPLLIG GATTSRVHTA VKIHPGYNKG QAIYVTDASR AVGVVSALLS PETRQGYVDD TRAEYAKVAA AHARSEAEKV RLPLPRAREN AHKVDWSAYQ PTKPEFFGTR VFEDYDLAEL ARYIDWTPFF QTWELRGRYP AILEDEKQGE AARALWADAQ SMLKKIIDEK WFRPRAVIGF WPAGAVGDDI RLFTDESRSH ELATFYTLRQ QLSKRDGRAN VALSDFVAPV TSGVQDYVGG FVVTAGIEEI AIAERFERAN DDYSSILVKA LADRFAEAFA ERMHEQVRRE YWGYAKDETL SNEDLITEAY AGIRPAPGYP AQPDHTEKAT LFKLLDAEKA AGVKLTESYA MWPGSSVSGL YIGHPDSYYF GVAKVERDQV EDYAKRKGME VSEVERWLGP VLNYVPRKTS EEIEDAA // ID B6A2W7_RHILW Unreviewed; 302 AA. AC B6A2W7; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 27-MAY-2015, entry version 31. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACI57790.1}; GN OrderedLocusNames=Rleg2_4534 {ECO:0000313|EMBL:ACI57790.1}; OS Rhizobium leguminosarum bv. trifolii (strain WSM2304). OG Plasmid pRLG201 {ECO:0000313|EMBL:ACI57790.1, OG ECO:0000313|Proteomes:UP000008330}. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=395492 {ECO:0000313|EMBL:ACI57790.1, ECO:0000313|Proteomes:UP000008330}; RN [1] {ECO:0000313|Proteomes:UP000008330} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WSM2304 {ECO:0000313|Proteomes:UP000008330}; 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 1 of Rhizobium leguminosarum bv. RT trifolii WSM2304."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001192; ACI57790.1; -; Genomic_DNA. DR RefSeq; WP_003591853.1; NC_011368.1. DR RefSeq; YP_002278530.1; NC_011368.1. DR ProteinModelPortal; B6A2W7; -. DR STRING; 395492.Rleg2_4534; -. DR EnsemblBacteria; ACI57790; ACI57790; Rleg2_4534. DR KEGG; rlt:Rleg2_4534; -. DR PATRIC; 23121617; VBIRhiLeg95088_0660. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; QPEVMAA; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; RLEG395492:GJB3-4600-MONOMER; -. DR Proteomes; UP000008330; Plasmid pRLG201. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008330}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ACI57790.1}; KW Plasmid {ECO:0000313|EMBL:ACI57790.1}; KW Transferase {ECO:0000313|EMBL:ACI57790.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 209 209 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 302 AA; 32390 MW; 32268F5E83858E87 CRC64; MSTTRILDGG MSRELLRLGA ELKQPEWSAL ALINSPDIVR EVHKEFIAAG SEVITTNSYA LVPFHIGEDR FQNEGAALIR LAGRLAREAA DAATDRKVLV AGSLPPIFGS YEPQNFQPSR VQDYLKVLVE NLAPFVDIWL GETLSLIAEG EAVREAVAAT GKPFWISFTL ADDEADIDSG EATLRSGESV EDAASWAVSS GAEAFLFNCS KPEVMRGAVE TAARVFRQAD ARIEIGVYAN AFEGEQGASA ANEGLHDTRD DLNDDAYSRF ACSWAEAGAT IIGGCCGIGA AHIHRLGKTL SR // ID B6AR37_9BACT Unreviewed; 815 AA. AC B6AR37; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 01-OCT-2014, entry version 24. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EDZ38708.1}; GN ORFNames=CGL2_11238056 {ECO:0000313|EMBL:EDZ38708.1}; OS Leptospirillum sp. Group II '5-way CG'. OC Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; Leptospirillum. OX NCBI_TaxID=419541 {ECO:0000313|EMBL:EDZ38708.1}; RN [1] {ECO:0000313|EMBL:EDZ38708.1} 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] {ECO:0000313|EMBL:EDZ38708.1} 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] {ECO:0000313|EMBL:EDZ38708.1} 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS995261; EDZ38708.1; -; Genomic_DNA. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDZ38708.1}; KW Transferase {ECO:0000313|EMBL:EDZ38708.1}. SQ SEQUENCE 815 AA; 87737 MW; E7009937050E7CB9 CRC64; MRPLLERLKN EILLLDGSMG ALLQSRGLPP GYAPDLWNLE RPQDIQQVHS EYVEAGSDII LTNTFGSSRL RLREYDAEGQ IREINEAGVE MARRAAKGKA YVAGDIGPSG TTIAPFGDLP FDDAIGIFYE QARILLGAGV DLIAIETMFD IQEMRAALIG VREAVGNRVP VMALMTFNND GITDSGSDPE TAASVLEGFG VDILGLNCSV GPEAMVPVVR RLGQTTSTFI AVEPNAGLPV HRDGHTVYPA NAEEVARFAP QFVEAGANII GGCCGTTPEY VRLLSRMLKG ISPISRPAPT LMKISSRTHM TLVGPGVPFL IVGEKINPTG KKKFSEAIAA GQTDLIVAEA RKEMEAGAGA LDVNVGVPLV NEAEMMAKAL TAIQNVVQLP IVIDSSYASA LEAGLKVYPG RALVNSVNAE EERLEEVLPI IKKYGAAVIG LVSGDDIPEK ATDRLKNAEK ILRRAHDLGL SPRDLIFDTL ALTVSAVQEA SRQTLETIRL IRQELGLPTI LGLSNVSFGL PARKLVHDNF LAMAIGAGLD AAICDPYDTV LHQTVAAASV FAGRDPDCRI YIDKSAQWAS PDAKDANTPQ KNQPQKPLTT VEAIRKAIEE GERESISGLV QKALAEGESP FAIFLDHMTP AIRHLGDLFG QRIKFIPHLI AGADTMKKGV EVLQPYLESE GPVEKKGTIV FATVKGDIHD IGKNICILML RNFGFNVIDL GRNVPLETIL DAAREHKAQI VALSALMTTT MMQMKLAIDT IQERDLPYKV MIGGAVVTPR FAEEIRSDGY GKDVGAIVPL AEQLIQACLE TRPPV // ID B6AUV9_9RHOB Unreviewed; 338 AA. AC B6AUV9; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 01-OCT-2014, entry version 23. DE SubName: Full=Methionine synthase I {ECO:0000313|EMBL:EDZ43156.1}; GN ORFNames=RB2083_2671 {ECO:0000313|EMBL:EDZ43156.1}; OS Rhodobacteraceae bacterium HTCC2083. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae. OX NCBI_TaxID=314270 {ECO:0000313|EMBL:EDZ43156.1}; RN [1] {ECO:0000313|EMBL:EDZ43156.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2083 {ECO:0000313|EMBL:EDZ43156.1}; 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; EDZ43156.1; -; Genomic_DNA. DR RefSeq; WP_009829993.1; NZ_DS995276.1. DR EnsemblBacteria; EDZ43156; EDZ43156; RB2083_2671. DR PATRIC; 28458835; VBIRhoBac88862_0469. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 338 AA; 35688 MW; 9A58409681ADA45F CRC64; MTNALSKMLS EREWILADGA TGTNLFNMGL MSGDAPELWN EQHPEKIKAL YKSAVDAGSD MFLTNSFGGN ASRLKLHSAQ DRAHDLSRMA AEIGRDVADA AGRPIVVAGS VGPTGDIMEP VGTLSHSDAV EIFHEQAEGL KAGGADVLWL ETISAPEEYL AAAEAFKRAQ MPWVGTMSFD TAGRTMMGLT SAAMVEMVDN IENSPIGFGA NCGTGASDLL RTVLGFAAQG TSVPIVAKGN AGIPKYVDGH IHYDGTPELM GEYAMLARNC GARIIGGCCG TMPEHLSAMR RALENNEQAQ APTLDVISAA LGPFSSSGDG TEENAPVARQ TRRRRRSS // ID B6AUX0_9RHOB Unreviewed; 298 AA. AC B6AUX0; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 01-OCT-2014, entry version 16. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EDZ43252.1}; GN ORFNames=RB2083_2767 {ECO:0000313|EMBL:EDZ43252.1}; OS Rhodobacteraceae bacterium HTCC2083. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae. OX NCBI_TaxID=314270 {ECO:0000313|EMBL:EDZ43252.1}; RN [1] {ECO:0000313|EMBL:EDZ43252.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2083 {ECO:0000313|EMBL:EDZ43252.1}; 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; EDZ43252.1; -; Genomic_DNA. DR RefSeq; WP_009830087.1; NZ_DS995276.1. DR EnsemblBacteria; EDZ43252; EDZ43252; RB2083_2767. DR PATRIC; 28455508; VBIRhoBac88862_2781. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDZ43252.1}; KW Transferase {ECO:0000313|EMBL:EDZ43252.1}. SQ SEQUENCE 298 AA; 31602 MW; 05E199E7CA167D14 CRC64; MTDVMLFDGG MGQELVHRAG DKPTPLWSTQ VMMDKPGLVA DVSRDFFAAG STVATLNSYA IQRDRLVPVG IEDQFDTLHS MALKEGQDAV AAHGSGRLAG SMGPLAASYR PDIHPSADIA VPLYTEVAQK FVGNVDLIVC ETVVSLEHTR CILAGAKTAN LPIYCAFSVS DEDGSKLRSG EPVLEAAQIA KDMGVVAVMA NCSAPEVIPT ALNELAKTSL PFGAYANGFT KISDGFLKDR PTVDALTLRK DFSPDLYADH VMAWVDQGAT LIGGCCEVSP AHIAEIAKRL RAAGHTII // ID B6B707_9RHOB Unreviewed; 298 AA. AC B6B707; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 01-OCT-2014, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EDZ47655.1}; GN ORFNames=RBY4I_2873 {ECO:0000313|EMBL:EDZ47655.1}; OS Rhodobacterales bacterium Y4I. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales. OX NCBI_TaxID=439496 {ECO:0000313|EMBL:EDZ47655.1}; RN [1] {ECO:0000313|EMBL:EDZ47655.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Y4I {ECO:0000313|EMBL:EDZ47655.1}; 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; EDZ47655.1; -; Genomic_DNA. DR RefSeq; WP_008556659.1; NZ_DS995281.1. DR EnsemblBacteria; EDZ47655; EDZ47655; RBY4I_2873. DR PATRIC; 28488682; VBIRhoBac125813_3299. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDZ47655.1}; KW Transferase {ECO:0000313|EMBL:EDZ47655.1}. SQ SEQUENCE 298 AA; 31282 MW; CCAEF8EA2487C076 CRC64; MAEITLLDGS IGQEVVKRSG DRATPLWSTS VMIERPDVVG GVHASYFAAG ATIATMNTYA VLRDRLRRAG IENHFEELLE KAAAQATAAR DAHGSGRIAA ALGPLIASYR PDICPPHGEA APVYAEIVQL LEPQADLFLI ETLSSVEQAN GALLGCAGTG KPVWLAASVQ DGDGTLLRSG EPLAALAPLV GEFQPDAVLL NCSRPEVIGS GLDIIKGFGK PFGAYANGFT RISEDFLKDA PTVDALEQRR DLGPESYAAF AMGWVAQGAT IVGGCCEIGP DHIAELARQL RAAGHRIV // ID B6B937_9RHOB Unreviewed; 325 AA. AC B6B937; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 01-OCT-2014, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EDZ45909.1}; GN ORFNames=RBY4I_1120 {ECO:0000313|EMBL:EDZ45909.1}; OS Rhodobacterales bacterium Y4I. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales. OX NCBI_TaxID=439496 {ECO:0000313|EMBL:EDZ45909.1}; RN [1] {ECO:0000313|EMBL:EDZ45909.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Y4I {ECO:0000313|EMBL:EDZ45909.1}; 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; EDZ45909.1; -; Genomic_DNA. DR RefSeq; WP_008554360.1; NZ_DS995281.1. DR EnsemblBacteria; EDZ45909; EDZ45909; RBY4I_1120. DR PATRIC; 28485857; VBIRhoBac125813_1678. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDZ45909.1}; KW Transferase {ECO:0000313|EMBL:EDZ45909.1}. SQ SEQUENCE 325 AA; 34890 MW; 1A323F74D2B68121 CRC64; MSIQNQSLAF QSEVIRSYLA DPRIYLTDGG FETSMLFLEG FDLPAFAACV LLEEDIARAA MNRYFDCFLQ MAATAGTGFV LDTNTWRSGT HWAKVVGRSP PQMQDLTREA VRFAMAIRAR WQDQVSPILL NGVIGPAGDA YDGSVTLDAA AAEAIHAPQI ALLATCGVDL VSALTFGSLS EAIGFTRAGV KAGVPVVISY TVETDGRLPD GTPLERAILE ADAATEQAPL YYMINCAHPE HFRDVLNNQA WCRRIRGVRA NASRLSHAEL DAAETLDDGD PEEFGTLHAA LSQKLPALKV VGGCCGTDHR HVGCMANAML PSTAA // ID B6BCY0_9RHOB Unreviewed; 340 AA. AC B6BCY0; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 01-OCT-2014, entry version 17. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EDZ46118.1}; GN ORFNames=RBY4I_1330 {ECO:0000313|EMBL:EDZ46118.1}; OS Rhodobacterales bacterium Y4I. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales. OX NCBI_TaxID=439496 {ECO:0000313|EMBL:EDZ46118.1}; RN [1] {ECO:0000313|EMBL:EDZ46118.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Y4I {ECO:0000313|EMBL:EDZ46118.1}; 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; EDZ46118.1; -; Genomic_DNA. DR RefSeq; WP_008554631.1; NZ_DS995281.1. DR EnsemblBacteria; EDZ46118; EDZ46118; RBY4I_1330. DR PATRIC; 28483859; VBIRhoBac125813_0512. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EDZ46118.1}; KW Transferase {ECO:0000313|EMBL:EDZ46118.1}. SQ SEQUENCE 340 AA; 36072 MW; 169556C37794F9F0 CRC64; MTNTFKQLLD TRDVLLADGA TGTNLFAMGL QSGDAPELWN VDEPKKIMAL YQGSVDAGSD LFLTNSFGGT AARLKLHNAQ GRVRELNRIA AELGREVADK AERKIAVAGS VGPTGEIFEP VGAMSHALAV EMFHEQADAL KEGGADVLWL ETISAPEEFR AAAEAFKLAD MPWCGTMSFD TAGRTMMGVT SADFAQLVEE FDNAPLAFGA NCGTGASDIL RTVLGFAAQG TERPIISKGN AGIPKYVDGH IHYDGTPELM GEYAVMARDA GAKIIGGCCG TMPDHLRHMR AALDSRPRGG RPALEQIVEV LGPFTSDSDG TGEDAAAGAE RRGRRGRRRA // ID B6BGS7_SULGG Unreviewed; 1163 AA. AC B6BGS7; H1FZ95; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=Methionine synthase (5-methyltetrahydrofolate--homocysteine methyltransferase) {ECO:0000313|EMBL:EHP29709.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHP29709.1}; GN Name=metH {ECO:0000313|EMBL:EHP29709.1}; GN ORFNames=SMGD1_1185 {ECO:0000313|EMBL:EHP29709.1}; OS Sulfurimonas gotlandica (strain DSM 19862 / JCM 16533 / GD1). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Sulfurimonas. OX NCBI_TaxID=929558 {ECO:0000313|EMBL:EHP29709.1, ECO:0000313|Proteomes:UP000006431}; RN [1] {ECO:0000313|EMBL:EHP29709.1, ECO:0000313|Proteomes:UP000006431} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GD1 {ECO:0000313|EMBL:EHP29709.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHP29709.1}. 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; AFRZ01000001; EHP29709.1; -; Genomic_DNA. DR RefSeq; WP_008334954.1; NZ_DS995286.1. DR EnsemblBacteria; EDZ62781; EDZ62781; CBGD1_399. DR EnsemblBacteria; EHP29709; EHP29709; SMGD1_1185. DR PATRIC; 27778667; VBICamBac111121_0191. DR Proteomes; UP000006431; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006431}; KW Methyltransferase {ECO:0000313|EMBL:EHP29709.1}; KW Transferase {ECO:0000313|EMBL:EHP29709.1}. SQ SEQUENCE 1163 AA; 129518 MW; 3862023D151CDC7E CRC64; MTTKQYILDT IKKRPLIIDG AMGTQLQQRD DKISKEAWEG NEGCNELLNV TAPEVLSEIF HAYLTAGADL ITTNTFGSFS WVLDEYQIGD RAYELTKAGA ELVKQECEKF STPEHPRFCL GSVGPGTKLP SLGHITYDEM HEGYTEFCLA LIDGGVDIFL LETCQDPLQI KAALHACQEA CRQREVEIPM MVSVTIELSG TMLIGTDAAT IATILEPFDI LSLGFNCGTG PEQVLKHVKT LSEVWHKPIS VHANAGLPQN RGGYTYYPMG PDEFTEQQEK FLAFDGVSFL GGCCGTTPQH IRALVDKVNS IRPKAPSGSH ENSIASLFNT TTLMQEPAPL LMGERSNATG SKAFRELLLA EDYEGTLSVA QQQVRAGAHV IDVNVGFAGR DETKDMNAVM GMYNQKIALP LMPDSTQTTG LETALKNIGG KPILNSVNLE DGEPKFDEVC RLAKKFGTSL VCLTIDEVGM AKTVENKLAV ADRIIDLATN RHGIKKEDLI FDVLTFTLGS GDAEYWDAGI NTIEAIRALR KKHPEVSATL GLSNISFGLD KDARPYLNSM FLHHCIEAGL TSVIINVKHI IPINKISKED QEICDDLIFN RKPNGEALFN FIEHFSTKEA IDNDVEDAAY LAMSDEEKIA KLLMDGDKER MIPLVEEARK TIAPEKIVNE ILIDAMKVVG ELFGSGQMQL PFVLQSAETM KKTVDHLNPY LPKVEKTVDT TLALGTVKGD VHDVGKNLVD IILSNNGFKV QNLGIKVELE DFVQATKDGH ISAFGMSGLL VKSTQVMQEN LKALKAEGID IPVLLGGAAL TRTFIDDFCR PFYDGPIFYC KDAFDGVTAM SRIEAGNLDT DLHGKDAEEK VVKEKKEIII PPFKELKMPP RDVKVPTPPF WGRREMKLTT TQIEMAFEWI NHKILFKSRW GYSSKGMTKE QYQKQVDEVI MPAYEKLKAQ FLDEKLFEPT IIYGYWPCRS DDNTLLIFDE SEGYNSSDEV NTEHLEHVMP RAIKQFTFPR QSKAPHRALS DFFHHDRHDV IALTCVSAGG KLSDAERLIY DEGNYTEYYQ FHGLGVELAE ALAEIVHKQI RLDLNISEGE GSKLSDVQMN KYQGSRYSFG YAACPDLELN RPLFDLLKPE EFGIELSETF QIHPEQSTSA LVVYHPNATY YNV // ID B6BQ90_9PROT Unreviewed; 346 AA. AC B6BQ90; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EDZ60973.1}; GN ORFNames=PB7211_1296 {ECO:0000313|EMBL:EDZ60973.1}; OS Candidatus Pelagibacter sp. HTCC7211. OC Bacteria; Proteobacteria; Alphaproteobacteria; SAR11 cluster; OC Candidatus Pelagibacter. OX NCBI_TaxID=439493 {ECO:0000313|EMBL:EDZ60973.1}; RN [1] {ECO:0000313|EMBL:EDZ60973.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC7211 {ECO:0000313|EMBL:EDZ60973.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; EDZ60973.1; -; Genomic_DNA. DR RefSeq; WP_008545912.1; NZ_DS995298.1. DR EnsemblBacteria; EDZ60973; EDZ60973; PB7211_1296. DR PATRIC; 30359003; VBICanPel29514_1261. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EDZ60973.1}; KW Transferase {ECO:0000313|EMBL:EDZ60973.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 210 210 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 297 297 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 298 298 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 346 AA; 38761 MW; 420547816DBDB728 CRC64; MKKDLITRLN EGPIMCAEGY LFAMERRGYL SAGPFVPEVV LEHPEVVTQL HREFIRAGSD VVQAFTYYGH REKLRIIGKE HLLEPMQKNA LKIAKDAAAE FKDLDLMVCG DVANTNVFDP NDANTHKQCQ QMYEEQVAWA KEAGVDFVIA ETINWSDEMK IALKAIKDAG LIAVCNFAIP RGDKTREGHS AEDACKMMED LGADLVGLNC YRGPEMTMKL LKKVRDKVSC HVAGLPVPYR TTEEEPGFLN ISDHGCDLIP GGNAFPVALD NLFCNRYEMA EFAKDCVESK INFIGICCGA EAHHVREMSV AIGKKPISMK YMPDMSKHFH HGTDKSLKKV NKEIKY // ID B6BST6_9PROT Unreviewed; 305 AA. AC B6BST6; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EDZ60322.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EDZ60322.1}; GN Name=mmuM {ECO:0000313|EMBL:EDZ60322.1}; GN ORFNames=PB7211_645 {ECO:0000313|EMBL:EDZ60322.1}; OS Candidatus Pelagibacter sp. HTCC7211. OC Bacteria; Proteobacteria; Alphaproteobacteria; SAR11 cluster; OC Candidatus Pelagibacter. OX NCBI_TaxID=439493 {ECO:0000313|EMBL:EDZ60322.1}; RN [1] {ECO:0000313|EMBL:EDZ60322.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC7211 {ECO:0000313|EMBL:EDZ60322.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; EDZ60322.1; -; Genomic_DNA. DR RefSeq; WP_008544884.1; NZ_DS995298.1. DR EnsemblBacteria; EDZ60322; EDZ60322; PB7211_645. DR PATRIC; 30357803; VBICanPel29514_0678. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 2. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EDZ60322.1}; KW Transferase {ECO:0000313|EMBL:EDZ60322.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 305 AA; 34207 MW; 41BEF9941B8D9D0F CRC64; MNKDFFKQVR ILDGGMGQEL HAKGLISMGT LWSASANLEK KFHNLVVDLH LSYIHSGADV IITNTFSARR IRLIQNKVNE HFKYINEQAC LLAIKAKDLS KKNVLIAGSL PSQSDTYVED QRNSNEIEKD FLDQATIINP YIDFFYLDVL SSGKELDIAS NVAAKLKKPI LAGVHLKKNC LLPSGEAITE VVQKYKNENW LGLIGACVSP EIVEKSIEEL KEINLPFGFK ANLWEIEEPG PQRTFNTAKY DEIGTNPNIA FGKRDKYDPK LFYEFSEKIK EKGATILGGC CETTPSHIEA IAKLK // ID B6BT42_9PROT Unreviewed; 305 AA. AC B6BT42; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Homocysteine S-methyltransferase 4, putative {ECO:0000313|EMBL:EDZ60210.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EDZ60210.1}; GN ORFNames=PB7211_533 {ECO:0000313|EMBL:EDZ60210.1}; OS Candidatus Pelagibacter sp. HTCC7211. OC Bacteria; Proteobacteria; Alphaproteobacteria; SAR11 cluster; OC Candidatus Pelagibacter. OX NCBI_TaxID=439493 {ECO:0000313|EMBL:EDZ60210.1}; RN [1] {ECO:0000313|EMBL:EDZ60210.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC7211 {ECO:0000313|EMBL:EDZ60210.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; EDZ60210.1; -; Genomic_DNA. DR RefSeq; WP_008544733.1; NZ_DS995298.1. DR EnsemblBacteria; EDZ60210; EDZ60210; PB7211_533. DR PATRIC; 30358027; VBICanPel29514_0789. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EDZ60210.1}; KW Transferase {ECO:0000313|EMBL:EDZ60210.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 305 AA; 33485 MW; 1B0E7C337BBCB566 CRC64; MSYQFIKKKL DKNSVVILDG GNGGELEQIG AKMDKDLWAG KSAIDDPDKL FQVHENYIKS GADVITSNTY AITPISMKEY GYEKFTQEWN KKTVDIALKA AASTEREIAV AGSVSTSGSW DKLTKNEITP GFSEQLTILS DAGVDLIILE AMTSKDETVE SIIECSSKIN LPVWLSISCA MNNEEGKLMH GYQESVTNSK AQFYDYLENS LLKFTQLHKG PILVAHSDIK VTSEAVKILK KIHKGSIGAY PNNGYFEKPN WKLVDDISPS SYLEEAKSWV LNGAQIIGGC CGVGPDKIKA ISVLK // ID B6BW08_9PROT Unreviewed; 1249 AA. AC B6BW08; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 29-APR-2015, entry version 38. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EDZ64674.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EDZ64674.1}; GN Name=metH {ECO:0000313|EMBL:EDZ64674.1}; GN ORFNames=KB13_806 {ECO:0000313|EMBL:EDZ64674.1}; OS beta proteobacterium KB13. OC Bacteria; Proteobacteria; Betaproteobacteria; Methylophilales; OC unclassified Methylophilales; OM43 clade. OX NCBI_TaxID=314607 {ECO:0000313|EMBL:EDZ64674.1}; RN [1] {ECO:0000313|EMBL:EDZ64674.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=KB13 {ECO:0000313|EMBL:EDZ64674.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; DS995299; EDZ64674.1; -; Genomic_DNA. DR RefSeq; WP_009852665.1; NZ_DS995299.1. DR EnsemblBacteria; EDZ64674; EDZ64674; KB13_806. DR PATRIC; 30884182; VBIBetPro60814_0040. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EDZ64674.1}; KW Transferase {ECO:0000313|EMBL:EDZ64674.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 255 255 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 320 320 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 782 782 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1249 AA; 138316 MW; 03CBC2D3A50042BE CRC64; MDPYKNTEDF LKAELKKRIL FMDGAMGTMI QQHQFVEADY RGERFKSFAA PEGERELFLK GNNELLSITQ PAVIQKIHED YLAAGADIIE TNTFGANSVA QEDYFMASLV KEMNIESVKL AKAAAEKYST EDKPRFVAGA IGPTPKTASI SPDVNDPGAR NITFDQLFDS YAEQAETLIS NGADIILIET VFDTLNCKAA IAAVQSTFDQ LGKTLPIMIS GTVTDASGRI LSGQTVTAFW NSIRHAKPLT IGLNCALGAA LMRPYAEELS NIADTFVCIY PNAGLPNPMS DTGFDEKPDD TSTLLKEFAE SGFVNVAGGC CGTTPEHIAA ITQSLKNIPP RTLPTIVKKM RLSGLEPMII GDDDLFVNVG ERTNVTGSRV FAKLIIDENY EEAVSVARQQ VENGAQVIDI NMDEGMLDAE KAMTTFLNLI ASEPDISRVP IMIDSSKWSV IEAGLKCIQG KPIVNSISLK EGEESFIHQA KLCMQYGAAV IVMAFDEEGQ ADTYERKIEI CERAYNILKD TVGFPVEDII FDPNIFAIAT GIAEHNNYAV DFINATKWIK DNLPHAKISG GVSNVSFSFR GNEAAREAIH TVFLNHAIKN GMTMGIVNAG MIGVIDDLTE ELKEVVEDVV LNHREDATDR MIEIAGSLQG KKKEKDTNEW RGSDAQPVSV EKKIEYALIH GITNYIEEDT ETARLQIMES GGRPINVIEG PLMDGMNVVG DLFAEGKMFL PQVVKSARVM KQAVAHLIPF IEKEKEEEEA RTGKKSKPKG KMLIATVKGD VHDIGKNIVS VVLQCNNFEV VNMGVMVPCA EILNKAKEEN VDIIGLSGLI TPSLEEMAHV ASEMQRDPYF RSVKMPLLIG GATTSRAHTA VKISPNYEGP VVHVADASRS VSVMQSLLSP DSKVDYIEKL KADYEKVRQL HGQKKGVKYI SLKAARENKL SLNFNPIKPK FIGRRVFKNI NLNELTDFID WTPFFKTWDL AGRYPQILQD EVVGDTASQL FDDAQTMLKK VINDRKLKAH AVVGFCKAHA IEDDIAISDE QDKLQFTFHT LRQQSEKPII SGRPKPNLSL SDFIAPQESH IDDYIGMFAV TAGDGGEFYL NQYEKNKDDY SGIMFKALMD RLAEACAEYM HLRVRQDLWG YAQKEKLSNE ELIQEKYLGI RPAPGYPACP EHSVKEDLFK FLKTDEIGMS LTENYAMIPA SSVSGFYFAH PESTYFSIDK IDADQLNDFA NRSSMDVDNA RRLLSSNIK // ID B6ELR4_ALISL Unreviewed; 1226 AA. AC B6ELR4; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 29-APR-2015, entry version 48. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:CAQ78127.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAQ78127.1}; GN Name=metH {ECO:0000313|EMBL:CAQ78127.1}; GN OrderedLocusNames=VSAL_I0442 {ECO:0000313|EMBL:CAQ78127.1}; OS Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain OS LFI1238)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Aliivibrio. OX NCBI_TaxID=316275 {ECO:0000313|EMBL:CAQ78127.1, ECO:0000313|Proteomes:UP000001730}; RN [1] {ECO:0000313|EMBL:CAQ78127.1, ECO:0000313|Proteomes:UP000001730} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LFI1238 {ECO:0000313|EMBL:CAQ78127.1, RC ECO:0000313|Proteomes:UP000001730}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; FM178379; CAQ78127.1; -; Genomic_DNA. DR RefSeq; WP_012549263.1; NC_011312.1. DR RefSeq; YP_002261970.1; NC_011312.1. DR STRING; 316275.VSAL_I0442; -. DR EnsemblBacteria; CAQ78127; CAQ78127; VSAL_I0442. DR KEGG; vsa:VSAL_I0442; -. DR PATRIC; 20850961; VBIAliSal95923_0544. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR Proteomes; UP000001730; Chromosome 1. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001730}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAQ78127.1}; KW Transferase {ECO:0000313|EMBL:CAQ78127.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 249 249 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1226 AA; 135985 MW; 385CEB8C6A8B7587 CRC64; MAGSMIKNQI EKQLLERILL IDGGMGTMIQ EYKFEENDYR GERFIDWHCD LKGNNDLLVL SNPSVIRDIH LAYLEAGADI LETNTFNATT IAMADYDMES LSAEINFEAA KLARKAADEW TLKTPHKPRY VAGVLGPTNR TCTLSPDVND PGFRNVTFDG LVKAYSESTR ALIKGGSDLI LIETIFDTLN AKACSFAVES VFEEMGITLP VMISGTITDA SGRTLSGQTT EAFYNALRHV KPISFGLNCA LGPDELREYV GELSRISECS VSAHPNAGLP NAFGEYDLSP EEMAEHVAEW ARSGFLNLIG GCCGTTPEHI RQMAAAVEGV KPRVLPDIPV ACRLSGLEPL TISKESLFVN VGERTNVTGS ARFKRLIKEE LYDEALSVAR EQVENGAQII DINMDEGMLE SEACMVRFLN LCASEPEISK VPVMVDSSKW EVIEAGLKCI QGKGIVNSIS LKEGKEKFVE QAKLVRRYGA AVIVMAFDEK GQADTRERKI EICTNAYNIL VNEVGFPPED IIFDPNIFAI ATGIDEHNNY AVDFIEAVAD IKRTLPHAMI SGGVSNVSFS FRGNNYVREA IQAVFLYHCF KHGMDMGIVN AGQLEIYDNV PEELREAVED VVLNRRDDST ERLLDIATAY LEKAVGKVED KSALEWRTWT VEKRLEHSLV KGITDFIVDD TEEARVNSER PIHVIEGPLM DGMNVVGDLF GEGKMFLPQV VKSARVMKQA VAHLEPFINA TKDVGSTNGK ILLATVKGDV HDIGKNIVGV VLQCNNYEII DLGVMVSCEK ILKVAKEENV DIIGLSGLIT PSLDEMVHVA KEMERQGFTV PLLIGGATTS KAHTAVKIEQ NYSQPVVYVN NASRAVGVCT SLLSNELKPA FIEKLDLDYD RVRDQHNRKI PRTKPITLER ARANKVDIDW VSYTPPTPMK PGVHIIDDVD IATLRKYIDW TPFFMTWSLM GKYPAILEHD EVGEEAKRLY KDANDLLDRV DTEGLLKARG MCALFPAAGI GDDIEVYSDE SRTTVVKVLH NLRQQTAKPK GFNYCLSDYI APKESGKKDW IGGFAVTGGI GERDLADAYK ANGDDYNAIM IQAIADRLAE GFAEYLHEKV RKEIWGYATD ENLANDELIR EKYQGIRPAP GYPACPEHTE KGALWELMKI EESIGMSLTS SYAMWPGASV SGMYFSHPDS RYFAIAQIQK DQAESYAERK GWDMLEAEKW LGPNLN // ID B6FS50_9FIRM Unreviewed; 797 AA. AC B6FS50; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEA81120.1}; GN ORFNames=CLONEX_02974 {ECO:0000313|EMBL:EEA81120.1}; OS Tyzzerella nexilis DSM 1787. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Tyzzerella. OX NCBI_TaxID=500632 {ECO:0000313|EMBL:EEA81120.1}; RN [1] {ECO:0000313|EMBL:EEA81120.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 1787 {ECO:0000313|EMBL:EEA81120.1}; 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 (SEP-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EEA81120.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 1787 {ECO:0000313|EMBL:EEA81120.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEA81120.1}. 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; ABWO01000175; EEA81120.1; -; Genomic_DNA. DR RefSeq; WP_004613840.1; NZ_DS995348.1. DR EnsemblBacteria; EEA81120; EEA81120; CLONEX_02974. DR PATRIC; 30598230; VBICloNex32710_2788. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEA81120.1}; KW Transferase {ECO:0000313|EMBL:EEA81120.1}. SQ SEQUENCE 797 AA; 87173 MW; 23BB6EA2C09A0D69 CRC64; MLLERLGKEL LFFDGGMGTL LQAEGLQPGE LPETWNIERK ETIRKIHQSY FEAGSDIVLT NTFGANALKF HDENCSLKAI IDAAVENVRF GAKAGIRDGR DYYVALDIGP TGKLLKPLGD LSFEDAYEAF KEVVQYGEKA GADLIHIETM SDTYEVKAAV LAAKENTNLP VFATMIFDDK GKLLTGGDVP SVVALLEGLR VDALGINCGM GPKQMLPILQ QIAQYTSLPI IVKPNAGLPK QRDGQTYYDV TPDVFAKQLQ EIVKAGACVI GGCCGTTPKH IRAMISACKD LEMTKPTFKN HTIVSSYGKA VELGDMPVII GERINPTGKS KFKQALKEHN LDYILKEGIT QQDKGAHILD VNVGLPDIDE VVMMKEVVRE LQSVTSLPLQ IDTVDTEAME QAMRIYNGKP MVNSVSGKQE SMNAVFPLIQ KYGGVVIGLT LDENGIPKTA KGRLEVAGKI IEEAKKYGID KKDIVIDVLT MTISSEPNGA KTTLEALKMV RDTYGVRTAL GVSNISFGLP SRPVINANFY TMAMQNGLTA GIINPSSEDM MRSYHSYCAL MNYDTNCENY IAHYGNQEPA KTTVPAGQQI DLKTAIEKGL KEDAYQTTVA LVKTKEPLEI INTYLIPALD TVGKGFEKGT VFLPQLLMSA DAAKSSFAVL KEELEKNGGE EKEKEKVILA TVKGDIHDIG KNIVKVLLEN YSFEVIDLGK DVAPECIVET VLEKEVKLVG LSALMTTTVV SMEETIRQLR EKAPDCKVMV GGAVLNQEYA DMIGADFYGK DAMQSVYYAQ KILTNHR // ID B6G243_9FIRM Unreviewed; 796 AA. AC B6G243; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEA84187.1}; GN ORFNames=CLOHIR_02205 {ECO:0000313|EMBL:EEA84187.1}; OS [Clostridium] hiranonis DSM 13275. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Peptoclostridium. OX NCBI_TaxID=500633 {ECO:0000313|EMBL:EEA84187.1}; RN [1] {ECO:0000313|EMBL:EEA84187.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 13275 {ECO:0000313|EMBL:EEA84187.1}; 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 (SEP-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EEA84187.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 13275 {ECO:0000313|EMBL:EEA84187.1}; 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. {ECO:0000313|EMBL:EEA84187.1}. 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; ABWP01000086; EEA84187.1; -; Genomic_DNA. DR RefSeq; WP_006441045.1; NZ_DS995361.1. DR EnsemblBacteria; EEA84187; EEA84187; CLOHIR_02205. DR PATRIC; 31119235; VBICloHir23630_2008. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEA84187.1}; KW Transferase {ECO:0000313|EMBL:EEA84187.1}. SQ SEQUENCE 796 AA; 87041 MW; C6807AD0C67385CA CRC64; MEIRDYLKTG KVLMFDGAMG TMLQRNGLKM GENPEIFAYK NPDILRDIHR QYLDAGTNTV LTCTFGCNEL KLPEGYTVEM IIDNAVKTAR EAIEESSSDK EKFVALDIGP IGEMLEPMGT LSFDRAYEIF KREVVRGVKA GVDVIVIETM MDLLEIKAAV LAAKENSDLP VFATMTFDED GRSFTGCLPE SMVYTIGGLG VDAIGVNCSL GPVQLLPIVE KICSVAQIPV MVQANAGLPS MHDGQATYDI GPDEYWEGVK KFIEAGASII GGCCGTDPSY IKKISDNLSN VEIGDKNNEY VSAVCSPSKV VRIDEPRVVG ERINPTGRKA FKEALKSGNT DYAVRLAIEQ VNGGADILEI NTGLPGIDER KAMVDILKEV QSVTDTPVQI DSSVVESLEA GLRYCNGRTI VNSVNGKDES LEAILPLVKK YGACVVGLTL DERGIPEKAE ERVEIAKNII KRAEEFGIRR EDIYIDCLSL TVSAQQEAAY ETLKAMKEVK KLGVHTTLGV SNISFGLPNR QAVNSAFLTL ALDAGLDLAI INPNNERMME AITSYKVIRN IDKGCTKFVE RYSDVDNKKD VKSSTSSSEM SLFDLVEKGI KDEAKSKTIE MLKDTDENYI LDEILIPALD VVGKKFEKGE IFLPQMIQSA EAVKASLTVI KENLISKNGD KKEDVSKGKI ILATVEGDIH DIGKNIVKIM LENYGYEIID LGRDVPVDKV VEKAVEENIK LVGLSALMTT TVKSMEETIK ALKEKMPEVK IFVGGAVLTE DYASEIGADF YAKDAKSAVE IAKIIL // ID B6GAW1_9ACTN Unreviewed; 848 AA. AC B6GAW1; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEA90637.1}; GN ORFNames=COLSTE_01211 {ECO:0000313|EMBL:EEA90637.1}; OS Collinsella stercoris DSM 13279. OC Bacteria; Actinobacteria; Coriobacteridae; Coriobacteriales; OC Coriobacterineae; Coriobacteriaceae; Collinsella. OX NCBI_TaxID=445975 {ECO:0000313|EMBL:EEA90637.1}; RN [1] {ECO:0000313|EMBL:EEA90637.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 13279 {ECO:0000313|EMBL:EEA90637.1}; 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] {ECO:0000313|EMBL:EEA90637.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 13279 {ECO:0000313|EMBL:EEA90637.1}; 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 (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. {ECO:0000313|EMBL:EEA90637.1}. 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; ABXJ01000068; EEA90637.1; -; Genomic_DNA. DR RefSeq; WP_006720864.1; NZ_DS995475.1. DR EnsemblBacteria; EEA90637; EEA90637; COLSTE_01211. DR PATRIC; 29049448; VBIColSte7090_0756. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEA90637.1}; KW Transferase {ECO:0000313|EMBL:EEA90637.1}. SQ SEQUENCE 848 AA; 88988 MW; D8E7EFC1BCA3CF9A CRC64; MDTTLQRALA GTGHLLFDGG MGTMLQARGL AAGELPELLC LTHPEQITAI HQAYVQAGSD VITTNTFGAN RLKLAGRAQV RDVFRAAVAC ARQSGARLVA ADIGPIGALL RPLGTLSFDE AYDLFAEQAH AAQDAGADLF IIETMTDLLE IKAAVLACRE QTDLPIFATM TFEADGRTFL GTPPEVAAVT LDALGVDALG INCSQGPAEL RPLARRMLAV TEKPVIVQAN AGLPHVEDGC TVFDIEPEAY AQAVAGMVED GVGILGGCCG TDPRHVERMA ELLRDHAPAP RTIEAAFTVT SAQRLVSLPC DASRIAVIGE RINPTGKRLL KEALRSGDYD YVVSQGIAQQ EEGADILDVN VGLPDIDEVT AIQIAGERLS GAVTLPLQFD STVPTALEAA VRRYAGKPII NSVNGKREVL DEILPIAARY GANVIGLTLD EEGIPTTAEG RFAIAERIVH AAAEHGIPAT RILIDCLAMT ASTDQRQAGE TLRAIQMVKR QLGVKCTLGV SNISFGLPQR PLLNSTYLAA ALGAGLDAPI LNPGSERYMD VVRSYRVLNG EDSGAAGYIE RYATWRDPYT TGAPGAVPVP AAPDAGSTGT SRSAAAGAPV ADGARAAGSG QATCGPSTGG TGQTGAAGPS HPGDDHGIEH FVLTGRKGEA ARATRELLST IDPLELIDGH IIPALDEVGA RFDRGTLFLP QLMASAEAAR ASFDVIKEHM PASDGLSKGT ICVATVKGDI HDIGKNIVKM LLDNYGYHVI DLGRDVDPHV ILKTVQERHI RLVGLSALMT TTVANMAQTI ELLHREAPGT LVMVGGAVLT PEYAQQIGAD FYAKDAAESA RIAARVFG // ID B6H6V4_PENCW Unreviewed; 244 AA. AC B6H6V4; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 29-APR-2015, entry version 34. DE SubName: Full=Pc16g00430 protein {ECO:0000313|EMBL:CAP92713.1}; GN ORFNames=Pc16g00430 {ECO:0000313|EMBL:CAP92713.1}, GN PCH_Pc16g00430 {ECO:0000313|EMBL:CAP92713.1}; 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 {ECO:0000313|EMBL:CAP92713.1, ECO:0000313|Proteomes:UP000000724}; RN [1] {ECO:0000313|EMBL:CAP92713.1, ECO:0000313|Proteomes:UP000000724} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 28089 / DSM 1075 / Wisconsin 54-1255 RC {ECO:0000313|Proteomes:UP000000724}; 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., Garcia-Estrada C., Fedorova N.D., Harris D.M., RA Heijne W.H., Joardar V., Kiel J.A., 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., Veenhuis M., von Dohren H., RA Wagner C., Wortman J., Bovenberg R.A.; 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; AM920431; CAP92713.1; -; Genomic_DNA. DR RefSeq; XP_002560465.1; XM_002560419.1. DR GeneID; 8317621; -. DR KEGG; pcs:Pc16g00430; -. DR eggNOG; COG2040; -. DR HOGENOM; HOG000179103; -. DR OMA; NTEDGRQ; -. DR OrthoDB; EOG7XH70V; -. DR BioCyc; PCHR:PC16G00430-MONOMER; -. DR Proteomes; UP000000724; Contig Pc00c16. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000724}; KW Reference proteome {ECO:0000313|Proteomes:UP000000724}. SQ SEQUENCE 244 AA; 26789 MW; 67CD40F67259FA13 CRC64; MASQSKLPQL TSSNLFVTEG GIETTLIYRN NLDLPSFSTL PLLNTEDGRQ TISSIYQEYV NIALAHSTGV VLETRTWRGS PLWSPEIGLS IPQILDLNRT AVKILHDIRN KTPSTSVVIS GALGPLQDAY QDSTGTVSFV DRLTENYTTY FGVNCAHPRY IIKAVRGMHT DVRSRIGSIR GNSSLKSHDE LDNSLVLDRG DISVWVREFN ELLNMLPGLK VVGGCCGTDE EHIDAIASRI NSVG // ID B6HVM8_PENCW Unreviewed; 345 AA. AC B6HVM8; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 29-APR-2015, entry version 35. DE SubName: Full=Pc22g15090 protein {ECO:0000313|EMBL:CAP98797.1}; GN ORFNames=Pc22g15090 {ECO:0000313|EMBL:CAP98797.1}, GN PCH_Pc22g15090 {ECO:0000313|EMBL:CAP98797.1}; 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 {ECO:0000313|EMBL:CAP98797.1, ECO:0000313|Proteomes:UP000000724}; RN [1] {ECO:0000313|EMBL:CAP98797.1, ECO:0000313|Proteomes:UP000000724} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 28089 / DSM 1075 / Wisconsin 54-1255 RC {ECO:0000313|Proteomes:UP000000724}; 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., Garcia-Estrada C., Fedorova N.D., Harris D.M., RA Heijne W.H., Joardar V., Kiel J.A., 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., Veenhuis M., von Dohren H., RA Wagner C., Wortman J., Bovenberg R.A.; 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; AM920437; CAP98797.1; -; Genomic_DNA. DR RefSeq; XP_002565427.1; XM_002565381.1. DR STRING; 500485.B6HVM8; -. DR GeneID; 8304660; -. DR KEGG; pcs:Pc22g15090; -. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG79SF86; -. DR BioCyc; PCHR:PC22G15090-MONOMER; -. DR Proteomes; UP000000724; Contig Pc00c22. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000724}; KW Reference proteome {ECO:0000313|Proteomes:UP000000724}. SQ SEQUENCE 345 AA; 37587 MW; 2354FB4860B21762 CRC64; MATIQILDGG LGTSLGDLYN IKFDSKTTPL WASHLLVSDP ATLQACQRDF GVAGVDILLT ATYQVSAEGF ARTKTAQFPD GILRSAVGPF LQKAVDIAEQ AKVRESASVA LSLGPYGACM IPGQEYSGAY DAEHDSEESL YLWHLDRLRM FAEADGELVS RVRYVAFETL PRLDEVRAVR RAIRASAFRV PFWIACVFPR DDDLLPDGSS VEEVVRAAVA SMEGGDVPWG VGINCTKMHK LAGLVDLFGR AVAEVVAEGQ VSAPPSLVLY PDGTNGEVYN TTTQVWEKRD GLGDNLSANR PWEEQLAQVV NEAYRKGHFT SFLVGGCCKA SHHDIKKLGQ QFKTQ // ID B6I5M7_ECOSE Unreviewed; 1227 AA. AC B6I5M7; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 27-MAY-2015, entry version 46. DE SubName: Full=B12-dependent homocysteine-N5-methyltetrahydrofolate transmethylase {ECO:0000313|EMBL:BAG79828.1}; GN OrderedLocusNames=ECSE_4304 {ECO:0000313|EMBL:BAG79828.1}; OS Escherichia coli (strain SE11). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=409438 {ECO:0000313|EMBL:BAG79828.1, ECO:0000313|Proteomes:UP000008199}; RN [1] {ECO:0000313|EMBL:BAG79828.1, ECO:0000313|Proteomes:UP000008199} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SE11 {ECO:0000313|EMBL:BAG79828.1, RC ECO:0000313|Proteomes:UP000008199}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP009240; BAG79828.1; -; Genomic_DNA. DR RefSeq; WP_000096055.1; NC_011415.1. DR RefSeq; YP_002295579.1; NC_011415.1. DR STRING; 409438.ECSE_4304; -. DR EnsemblBacteria; BAG79828; BAG79828; ECSE_4304. DR KEGG; ecy:ECSE_4304; -. DR PATRIC; 18427326; VBIEscCol83070_4485. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; ECOL409438:GHUU-4399-MONOMER; -. DR Proteomes; UP000008199; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008199}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAG79828.1}; KW Transferase {ECO:0000313|EMBL:BAG79828.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136068 MW; 71F76336C7330F7E CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAD // ID B6JJE8_OLICO Unreviewed; 1286 AA. AC B6JJE8; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 27-MAY-2015, entry version 55. DE SubName: Full=Methionine synthase MetH {ECO:0000313|EMBL:AEI05416.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEI05416.1}; GN Name=metH {ECO:0000313|EMBL:AEI05416.1}; GN OrderedLocusNames=OCA5_c06930 {ECO:0000313|EMBL:AEI05416.1}; OS Oligotropha carboxidovorans (strain ATCC 49405 / DSM 1227 / OM5). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Oligotropha. OX NCBI_TaxID=504832 {ECO:0000313|EMBL:AEI05416.1, ECO:0000313|Proteomes:UP000007730}; RN [1] {ECO:0000313|EMBL:AEI05416.1, ECO:0000313|Proteomes:UP000007730} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49405 / DSM 1227 / OM5 RC {ECO:0000313|Proteomes:UP000007730}; 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; CP002826; AEI05416.1; -; Genomic_DNA. DR RefSeq; WP_012564567.1; NC_015684.1. DR RefSeq; YP_002290407.1; NC_011386.1. DR RefSeq; YP_004631657.1; NC_015684.1. DR ProteinModelPortal; B6JJE8; -. DR SMR; B6JJE8; 655-908. DR STRING; 504832.OCAR_7439; -. DR EnsemblBacteria; ACI94542; ACI94542; OCAR_7439. DR EnsemblBacteria; AEI05416; AEI05416; OCA5_c06930. DR KEGG; oca:OCAR_7439; -. DR KEGG; ocg:OCA5_c06930; -. DR PATRIC; 22808665; VBIOliCar134280_3276. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; OCAR504832:GJPZ-693-MONOMER; -. DR Proteomes; UP000007730; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007730}; KW Methyltransferase {ECO:0000313|EMBL:AEI05416.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007730}; KW Transferase {ECO:0000313|EMBL:AEI05416.1}. SQ SEQUENCE 1286 AA; 141096 MW; 5422BB9D36C5D511 CRC64; MTESSSSTAQ KFRALARERI LVLDGAMGTM IQRLELDEAA FRGERFKDFH RDVRGNNDLL ILTQPQAIED IHYEYLKAGA DIVETNTFSS TSIAQADYDM SDLAYELNRE GARLARNAAN RAEAEDGKPR FVAGALGPTN RTASISPDVA NPGYRAVTFN NLRAAYGEQI NGLLDGGADI LLVETIFDTL NAKAALYAIS EICEERGIDV PVMISGTITD KSGRLLSGQL PEAFWYSVQH AQPLTIGFNC ALGAEDLRAH IADLGRIADT LVCAYPNAGL PNEFGQYDET PEFMAKLVGE FARDGLVNVV GGCCGTTPDH IRAIAQAVAP HKRRVVPTIE PRLRLSGLEP FVLTSDIPFV NVGERTNVTG SARFRKLIKE GDYTAALQVA RDQVANGAQV IDVNMDEGLL DSKQAMIDFL NLVASEPDIA RVPVMVDSSK FEVIEAGLQC IQGKPIVNSI SMKEGEEKFL AEAAIARRHG AAVVVMAFDE VGQADTFARK TEICKRAYEL LTTKLNFPPQ DIIFDPNIFA IATGLEEHNN YGVDFIEATR WIRKNLPHVH ISGGVSNLSF SFRGNEPVRE AMHSVFLYHA IKAGMDMGIV NAGQMVIYDD IDPELRQVCE DVILNRDPGA SERLLQLAEK FRGQGKQAKE QDLSWREWSV EKRLSHALVN GITEYIEVDT EEARQTVDRP LAVIEGPLMA GMNVVGDLFG SGKMFLPQVV KSARVMKQAV AYLMPFMEEE KERNKAAGLS AGARASAGKI VMATVKGDVH DIGKNIVGIV LQCNNFEVVD LGVMVPAAKI LETAKAENAD MVGLSGLITP SLDEMVFVAS EMERQGFDLP LLIGGATTSR VHTAVKIDPR YRRGPVVHVN DASRAVGVAS TLLSAEKREE YISEVRADYA RIADAHFRAQ QNKKRLTLEA ARTNRLKVDW KTIKPVKPSF LGLKTFTDYP LAELAECIDW TPFFQAWELA GRFPGILKDP NVGEVAQSLY NDARKMLDTI IKEKWFTANA TIGFWPANAE GDDVTLYSDE ARTKPLATLH TLRQQLERRA GVPNLALADF IAPKDSGVAD YIGAFVVTAG IGEEAITMRF KKANDDYSSI IVKALADRLA EAFAERMHQR VRMEFWGYAP DEALSNDDLI LEKYRGIRPA PGYPAQPDHN EKTTLFRLLD AERNAGVTLT ESLAMWPGSS VSGVYYSHPD SAYFGVGKIE RDQVEDYAER TGMSIAETER SLASVLNYIP ASEPQPPAAA EDDDVTSLPP AQHPPGCGCA IHMRMRMKSG GGVQPN // ID B6K6T6_SCHJY Unreviewed; 314 AA. AC B6K6T6; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 29-APR-2015, entry version 21. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:EEB09240.1}; GN ORFNames=SJAG_04425 {ECO:0000313|EMBL:EEB09240.1}; 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 {ECO:0000313|EMBL:EEB09240.1, ECO:0000313|Proteomes:UP000001744}; RN [1] {ECO:0000313|EMBL:EEB09240.1, ECO:0000313|Proteomes:UP000001744} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=yFS275 / FY16936 {ECO:0000313|Proteomes:UP000001744}; 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; KE651167; EEB09240.1; -; Genomic_DNA. DR RefSeq; XP_002175533.1; XM_002175497.2. DR EnsemblFungi; EEB09240; EEB09240; SJAG_04425. DR GeneID; 7050242; -. DR EuPathDB; FungiDB:SJAG_04425; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000001744; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001744}; KW Methyltransferase {ECO:0000313|EMBL:EEB09240.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001744}; KW Transferase {ECO:0000313|EMBL:EEB09240.1}. SQ SEQUENCE 314 AA; 35128 MW; 1AF05C4D13412089 CRC64; MLVLDGGSTS ILPKLPNDIL KSKLWTSEAL VRFPDQVREQ HTEFLGPCNV ISTYTYQLDE SIYDEAEENA PLDVVYSRGM ELPLQAKQQS AQANRFVAIS LGSYAATVPG AMEYNMVYDE EDFDKLYNFH KRRLERMQRS NPKAFASIDF LAFESLPHVV EASAVLKLID DMKGYGKRCW ITFTCPSVEA IDRVDGILES VMKGPLTYLW GTGVNCCHIS LLPQIANVLE KHISPHPTLH AVLYPDGRGL WNAHPYSPNG IAPTPREWAQ AVAPYVRLND GKLLLGGCCE TTVEHLQILR DLITSETAKS SQKL // ID B6KB25_TOXGO Unreviewed; 434 AA. AC B6KB25; B9QBQ1; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 27-MAY-2015, entry version 37. DE SubName: Full=Homocysteine s-methyltransferase domain-containing protein {ECO:0000313|EMBL:ESS28567.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ESS28567.1}; GN ORFNames=TGVEG_257750 {ECO:0000313|EMBL:ESS28567.1}; OS Toxoplasma gondii. OC Eukaryota; Alveolata; Apicomplexa; Conoidasida; Coccidia; OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma. OX NCBI_TaxID=5811 {ECO:0000313|Proteomes:UP000002226}; RN [1] {ECO:0000313|Proteomes:UP000002226} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 50861 / VEG {ECO:0000313|Proteomes:UP000002226}; RA Lorenzi H., Inman J., Amedeo P., Brunk B., Roos D., Caler E.; RT "Annotation of Toxoplasma gondii VEG."; 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. {ECO:0000313|EMBL:ESS28567.1}. 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; AAYL02000337; ESS28567.1; -; Genomic_DNA. DR ProteinModelPortal; B6KB25; -. DR EuPathDB; ToxoDB:TGME49_257750; -. DR InParanoid; B6KB25; -. DR OMA; ERENEGP; -. DR Proteomes; UP000002226; Partially assembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 3. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 3. DR SUPFAM; SSF82282; SSF82282; 3. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002226}; KW Methyltransferase {ECO:0000313|EMBL:ESS28567.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002226}; KW Transferase {ECO:0000313|EMBL:ESS28567.1}. SQ SEQUENCE 434 AA; 46593 MW; 6E7B55CC257D4EFA CRC64; MPHAGFTDDI LLLDGGLGTH LRALGAEFHG DPLWASKAVL SAPDLVRRAH FDFFDAGADV AITATYQASL TGFAQIGLSP STAHDAVALA INLAAEARRL AEEGDVSARS FGEERENEGP EVDALRNAAT SDTDSVQQGN ARDADRRYRR RNRKILVSNG SYGASLGGGA EYRGNYGVSE KTFHDYHRWR LQAALEQEHL VDGVVFETLP EHAEAKAIVS LLREFPSLRG KTWLAFTCKS PTELAGGEDF RSVVADVLKQ DGADQYISGI GVNCAPISTT VPLLCSPPLR DSLAASLEKT RDPWSLQVVC YPNNEAARNT KDCSSKDFES QEESCHGHVS RAETCMCSIG VDQSTTVKPQ TSLVSGSAAG GLRCQPKLRA NRMPHGFTKT IKHPLASRVP AWLNGGVTAV GGCCGTGPED LKEIRAVLEN LGVY // ID B6QZT0_9RHOB Unreviewed; 1248 AA. AC B6QZT0; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 01-APR-2015, entry version 36. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEA95877.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEA95877.1}; GN Name=metH {ECO:0000313|EMBL:EEA95877.1}; GN ORFNames=PJE062_4916 {ECO:0000313|EMBL:EEA95877.1}; OS Pseudovibrio sp. JE062. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Pseudovibrio. OX NCBI_TaxID=439495 {ECO:0000313|EMBL:EEA95877.1}; RN [1] {ECO:0000313|EMBL:EEA95877.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=JE062 {ECO:0000313|EMBL:EEA95877.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; DS996806; EEA95877.1; -; Genomic_DNA. DR RefSeq; WP_008547873.1; NZ_DS996806.1. DR EnsemblBacteria; EEA95877; EEA95877; PJE062_4916. DR PATRIC; 25633969; VBIPseSp14949_1072. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEA95877.1}; KW Transferase {ECO:0000313|EMBL:EEA95877.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 255 255 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 318 318 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 319 319 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 770 770 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1248 AA; 137171 MW; 6AC646184A2DC46B CRC64; MSLQVKKTGS DIFAALEAAA KERILVLDGA MGTMIQNLQF SEEQFRGERF KSWNQDLKGN NDLLILTQPD AIRDIHLQYL KAGADIIETN TFSSTSIAQA DYAMESIVYE LNKEGARLCC EAVEQMKEID PSRRRFVAGG LGPTNRTASI SPDVNNPGFR AVSFDDLKDS YAEATRGLID GGCDLILVET IFDTLNAKAA LFAIDEVFEE KGVKLPVMIS GTITDLSGRT LSGQTPEAFW NSVRHAAPFT VGLNCALGAK EMRAHVDEIS RVADTLVCAY PNAGLPNEFG EYDESPEYMA GLLKEFAEAG LVNVVGGCCG TTPEHIKAVA DAVEGLPPRA LPEVPRLMRL SGLEPFTFTK DVNFVNVGER TNVTGSARFR KLIKNDDYTT ALDVARSQVE NGAQIIDINM DEGLLDSEEA MVTFLNLIAA EPDIAKVPVM IDSSKWTVIE AGLKCVQGKA VVNSISLKEG EENFIAQAKL IRRYGAAVVV MAFDETGQAD TLQRKIEICK RSYDVLVNKV GFGPEDIIFD PNIFAVATGI EEHDNYGVDF IEATRWISEN LPYAHISGGV SNLSFSFRGN EPVREAMHSV FLYHAIQAGM DMGIVNAGQL AVYDDLPAEL RELCEDVVLN RRSDSTDRLL DAAEKFKGAG GKKREVDLTW REGTVEKRLE HSLVHGITDF IVEDTEEARQ KADRPLHVIE GPLMDGMNVV GDLFGAGKMF LPQVVKSARV MKAAVAYLMP YLEQEKKELG LDESSSNGKI LMATVKGDVH DIGKNIVGVV LQCNNFEVID LGVMVPTAKI IDEAKKHNVD IIGLSGLITP SLDEMCHVAS EMEREGLDIP LLIGGATTSR VHTAVKIHPN YSKGQAIYVT DAGRAVGVAS RLMAEGGREE IYENTRLEYV DVAEKHAAAR NKKVRASIEK ARANRFKPDF ETHKPTKPKF LGTKTFTDFS LEELVDYIDW TPFFATWEIK GAYPAVLTDD RYGPAAQALY NDAREMLKEI VDGKLLQANA VVGFWPCAQD GDDLVLYTDE SRTKELKRLY TLRQQMDRSS SDRGNVALAD FVAPVESGIP DYVGGFAVTA GIGEDVLAKR YADAGDDYNK ILSQAIADRL AEALAERMHQ LVRTELWAYA PDETLSNADL IAEGYDGIRP APGYPAQPDH TEKGTLWELL DAEAQTGISL TESYAMWPGS AVSGLYFSHP DSHYFGVGKI ERDQVQDYAV RKGWDLETAE RWLAPILNYN PMAREAAE // ID B6TK96_MAIZE Unreviewed; 355 AA. AC B6TK96; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Homocysteine S-methyltransferase 3 {ECO:0000313|EMBL:ACG37529.1}; 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 {ECO:0000313|EMBL:ACG37529.1}; RN [1] {ECO:0000313|EMBL:ACG37529.1} 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; EU965411; ACG37529.1; -; mRNA. DR Gramene; B6TK96; -. DR HOGENOM; HOG000265278; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Methyltransferase {ECO:0000313|EMBL:ACG37529.1}; KW Transferase {ECO:0000313|EMBL:ACG37529.1}. SQ SEQUENCE 355 AA; 38439 MW; C7C2AF934F389247 CRC64; MVGTAEGGAE RAVRRWVDAA GGRLVLDGGL ATELEANGAD LNDPLWSAKC LLSSPHLIRK VHMDYLEAGA NIIITASYQA TIQGFESKGF SKEQSENLLT KSVQIALEAR EMFLKEHLEK STPIQHPILV AAALGSYGAY LADGSEYSGD YGEAGTKEFL KDFHRRRLQV LAEAGPDLIA FETIPNKLEA QAYVELLEEC NINIPSWLSF NSKDGVHVVS GDSLIECATI ADKCAKVGAV GINCTPPRFI HGLILSIRKV TDKPILIYPN SGERYDGEKK EWVESTGVSD GDFVSYVNEW CKDGAALIGG CCRTTPNTIR AIHRTLNQGC HKHQLPVGCS IDLCSTPNAL LPAVP // ID B6TYG7_MAIZE Unreviewed; 339 AA. AC B6TYG7; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 01-APR-2015, entry version 32. DE SubName: Full=Homocysteine S-methyltransferase 3 {ECO:0000313|EMBL:ACG42150.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ACN28428.1}; 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 {ECO:0000313|EMBL:ACG42150.1}; RN [1] {ECO:0000313|EMBL:ACG42150.1} 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). RN [2] {ECO:0000313|EMBL:ACN28428.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=B73 {ECO:0000313|EMBL:ACN28428.1}; 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; EU970032; ACG42150.1; -; mRNA. DR EMBL; BT063731; ACN28428.1; -; mRNA. DR RefSeq; NP_001105012.1; NM_001111542.1. DR UniGene; Zm.529; -. DR ProteinModelPortal; B6TYG7; -. DR GeneID; 541874; -. DR KEGG; zma:541874; -. DR Gramene; B6TYG7; -. DR KO; K00547; -. DR OMA; SSVEGFM; -. DR ExpressionAtlas; B6TYG7; baseline and differential. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Methyltransferase {ECO:0000313|EMBL:ACG42150.1}; KW Transferase {ECO:0000313|EMBL:ACG42150.1}. SQ SEQUENCE 339 AA; 36959 MW; 12B2144B5501F51D CRC64; MVVTAAGSAE EAVRRWVDAA GGRLVLDGGL ATELEANGAD LNDPLWSAKC LLSSPHLIRK VHMDYLEAGA NIIITASYQA TIQGFESKGF SKEQSENLLT KSVEIALEAR EMFLKEHLEK STPIQHPVLV AASLGSYGAY LADGSEYSGD YGEAGTKEFL KDFHRRRLQV LAEAGPDLIA FETIPNKLEA EAYVELLEEC NINIPAWFSF NSKDGVHIVS GDSLIECTTI ADKCAKVGAV GINCTPPRFI HGLILSIRKV TDKPILIYPN SGERYDGEKK EWVESTGVSD GDFVSYVNEW CKDGAVLIGG CCRTTPNTIR AIHRTLNKSP NKQQLPAVE // ID B6W3N6_9BACE Unreviewed; 917 AA. AC B6W3N6; DT 20-JAN-2009, integrated into UniProtKB/TrEMBL. DT 20-JAN-2009, sequence version 1. DT 27-MAY-2015, entry version 35. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EEB23528.1}; GN ORFNames=BACDOR_03981 {ECO:0000313|EMBL:EEB23528.1}; OS Bacteroides dorei DSM 17855. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=483217 {ECO:0000313|EMBL:EEB23528.1}; RN [1] {ECO:0000313|EMBL:EEB23528.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17855 {ECO:0000313|EMBL:EEB23528.1}; 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] {ECO:0000313|EMBL:EEB23528.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17855 {ECO:0000313|EMBL:EEB23528.1}; 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 (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; ABWZ01000075; EEB23528.1; -; Genomic_DNA. DR RefSeq; WP_007837694.1; NZ_DS995537.1. DR EnsemblBacteria; EEB23528; EEB23528; BACDOR_03981. DR PATRIC; 27000893; VBIBacDor28639_3753. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 243 243 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 917 AA; 100924 MW; 505D6BDEA9B137EE CRC64; MATLKQIINE RVLILDGAMG TMIQRYNLSE QDFRGERFAG IPGQMKGNND LLCLTRPDVI KDIHRKYLEA GADIIETNTF NAQRISMADY HMQDLCREIN LAAARLAREL ADEYTAKTPR KPRFVAGSVG PTNKTCSMSP DVNNPALRAL TYDELATAYQ EQMEALLEGG VDALLIETIF DSLNAKAAIY AAETAMKKTG REVPLMLSVT VSDIAGRTLS GQTLDAFLAS VQYAPIFSIG LNCSFGAKQL KPFLEGLAAR APYYISAYPN AGLPNSLGQY DQTPEEMASE VKEYIDEGLV NIIGGCCGTT EEYIAKYQEL IVSGSAWVPP HIPATTPERL WLSGLELLEQ TPEMNFINVG ERCNVAGSRK FLRLINEKKY EEALSIARKQ VEDGALVIDV NMDDGLLDAR EEMTTFLNLV MSEPDIARVP IMIDSSKWEV IEAGLKCLQG KSIVNSISLK EGEEKFIEHA RLIKKLGAAT VVMAFDEKGQ ADTFERKIEV CARAYKILTE QVGFNPHDII FDPNVLAVAT GIEEHNNYAV DFINATGWIK KNLPGAHISG GVSNLSFSFR GNNYIREAMH AVFLYHAIRQ GMDMGIVNPA TSVLYTDIPA DVLERIEDVV LNRRPDAAER LIETAEALKN TATGTEAVKQ DVWREEPMVE KRLQYALIKG VGDHLEEDLA EAVKLYPKAV DIIEGPLMEG MNRVGELFGA GKMFLPQVVK TARTMKKAVA ILQPLIEADK QEGARSAGKV LMATVKGDVH DIGKNIVSVV MACNNYEIID LGVMVPAEMI VRKAIEEKVD IIGLSGLITP SLEEMAHVAV ELKRAGLDIP IMIGGATTSK LHTALKIAPV YGGPVIHMKD ASQNALVAAR LLNPESSSEF VERLNKEYEE LRLKNSTKQV KTVSLEEAQK NKLNLWS // ID B6WQU0_9DELT Unreviewed; 333 AA. AC B6WQU0; DT 20-JAN-2009, integrated into UniProtKB/TrEMBL. DT 20-JAN-2009, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEB34547.1}; GN ORFNames=DESPIG_00419 {ECO:0000313|EMBL:EEB34547.1}; OS Desulfovibrio piger ATCC 29098. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=411464 {ECO:0000313|EMBL:EEB34547.1}; RN [1] {ECO:0000313|EMBL:EEB34547.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29098 {ECO:0000313|EMBL:EEB34547.1}; 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] {ECO:0000313|EMBL:EEB34547.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29098 {ECO:0000313|EMBL:EEB34547.1}; 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. {ECO:0000313|EMBL:EEB34547.1}. 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; ABXU01000021; EEB34547.1; -; Genomic_DNA. DR RefSeq; WP_006004272.1; NZ_DS996353.1. DR EnsemblBacteria; EEB34547; EEB34547; DESPIG_00419. DR PATRIC; 27359238; VBIDesPig88804_0321. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEB34547.1}; KW Transferase {ECO:0000313|EMBL:EEB34547.1}. SQ SEQUENCE 333 AA; 36464 MW; 33637F10D4E3F272 CRC64; MEPTTTPPST KRPLSLVRCF ERHDALLLEG ALGERLKREY ALTPDPHVAL AAFVRSEAGR HALCELWQGY WQTAVRYGLP FLATTPTRRA NRERTRQAGE DEGLLRDCMT LLAGLKAGWE RTPTYTGGLM GCKGDAYTGE GALDEEDARR FHAWQADILA DAGADFLYAG IMPTLPEALG MARALAATCL PYIISFSLLD KGTLVDGTPL HTAIQHIDSR TERPPLCYMT NCVHPDIVRK ALLQPVNRTE LVRRRFQGIQ ANAAPLEYAV MDNATSLLTS APDDLAHGML GLRELTAMKI FGGCCGTDGR HLEAIARRFS LRRSATPDSG TGA // ID B6WT17_9DELT Unreviewed; 800 AA. AC B6WT17; DT 20-JAN-2009, integrated into UniProtKB/TrEMBL. DT 20-JAN-2009, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEB33929.1}; GN ORFNames=DESPIG_01222 {ECO:0000313|EMBL:EEB33929.1}; OS Desulfovibrio piger ATCC 29098. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=411464 {ECO:0000313|EMBL:EEB33929.1}; RN [1] {ECO:0000313|EMBL:EEB33929.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29098 {ECO:0000313|EMBL:EEB33929.1}; 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] {ECO:0000313|EMBL:EEB33929.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29098 {ECO:0000313|EMBL:EEB33929.1}; 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. {ECO:0000313|EMBL:EEB33929.1}. 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; ABXU01000029; EEB33929.1; -; Genomic_DNA. DR RefSeq; WP_006005764.1; NZ_DS996355.1. DR EnsemblBacteria; EEB33929; EEB33929; DESPIG_01222. DR PATRIC; 27360590; VBIDesPig88804_0971. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEB33929.1}; KW Transferase {ECO:0000313|EMBL:EEB33929.1}. SQ SEQUENCE 800 AA; 84471 MW; 48725EA2A45DBD0D CRC64; MKFVQRLAER RPLLLDGAMG TMLQASGLPA GVSPEEFCME RPDILQGIHK AYLDAGVDII TSCTFGGNPC KLPASLDVFT FNKRMVETAR AAAAQAGRPV FVAGNVGPSG HFARPLGDME PEELIKAFSE QIRGLVAGGA DLIFIETQFD LAEARAAVTA ARQVCDLPVM VSMTFEQGAS LTGSSPTIFA ETMQNMGVAA LGTNCSLGPD QMLPVVEELL SVCACPVVAE PNAGLPELRG SETVFPLGPE AFAQKTAAFA ARGARVLGGC CGTTPRHLAA LRQALESVSC DERPVVSPAG ICLTSRSQLL RLGEGQPFSV IGERINPTGK KELTRQLQAG QFDEAFRLAD EQLQAGARIL DVNVGASLVD ETVLLPDLVQ RLVSRVDVPL SLDSSNAQAI ARALPYCPGS FLVNSISGEA GRMELLGPVC RDFGAPFILL PLQGTKLPVR ASERIAIVEK LLEQADALGI PRRLVMVDIL ALSVSSKPEG ALQCLEMVRW CRSQGLATTL GLSNVSFGLP ARDLLNATFM AMCAGAGLSS CIANPSAPRL HEACDAVAVL QGSDSNAGSF IASYADWKAS GGVVRAGTGP GAAAETLGDA VLFGDLENVL PLLEKELAAG AEPFALVQDV LIPAITEVGT RYERREYFLP QLIRAAETMQ KAFAHLKPLL EKSRGPEERP VIVMATVEGD IHDIGKNIVC LLLGNHGFDV IDAGKDVPAE QIVACALEHK ARIIGLSALM TTTMVRMEDT IRLVRERDLP IKVLVGGAAV TQAFADAIGA DAYCEDAVSA VRAAKQFVTG // ID B6XE62_9ENTR Unreviewed; 1227 AA. AC B6XE62; DT 20-JAN-2009, integrated into UniProtKB/TrEMBL. DT 20-JAN-2009, sequence version 1. DT 27-MAY-2015, entry version 35. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEB46340.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEB46340.1}; GN Name=metH {ECO:0000313|EMBL:EEB46340.1}; GN ORFNames=PROVALCAL_01638 {ECO:0000313|EMBL:EEB46340.1}; OS Providencia alcalifaciens DSM 30120. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Providencia. OX NCBI_TaxID=520999 {ECO:0000313|EMBL:EEB46340.1}; RN [1] {ECO:0000313|EMBL:EEB46340.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 30120 {ECO:0000313|EMBL:EEB46340.1}; 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] {ECO:0000313|EMBL:EEB46340.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 30120 {ECO:0000313|EMBL:EEB46340.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEB46340.1}. 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; ABXW01000044; EEB46340.1; -; Genomic_DNA. DR RefSeq; WP_006658587.1; NZ_ABXW01000044.1. DR EnsemblBacteria; EEB46340; EEB46340; PROVALCAL_01638. DR PATRIC; 26406321; VBIProAlc107602_1475. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEB46340.1}; KW Transferase {ECO:0000313|EMBL:EEB46340.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136770 MW; D224230D81BAB23B CRC64; MSSKKNQLEQ QLKNRILVLD GAMGTMIQRH KLSEEQFRGE RFADWSSDLK GNNDLLVLTQ PDIIRDIHNQ YFAAGADIIE TNTFNSTIIA MADYKMEALS AEINETAARL ARECADEWTR KTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNVTFDQLV EAYRESTRSL IKGGADLIMI ETIFDTLNAK AAIFAVETEF EALGIHLPVM ISGTITDASG RTLSGQTTEA FYNSLRHSQP ISFGLNCALG PDELRQYIAE LSRISECYVS AHPNAGLPNA FGEYDLDAQN MAQQIREWAE AGFLNIVGGC CGTTPLHIQK MAQAVEGVKP RQLPTLPVEC RLSGLEPLNI GAQSLFVNVG ERTNVTGSAK FKRLIKEENY QEALDIARQQ VENGAQIIDI NMDEGMLDSH AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGIDAFIDHA KLVRKYGAAM VVMAFDEVGQ ADTRARKIEI CRRAYQILTE TVGFPPEDII FDPNIFAVAT GIEEHNNYAV DFIEVCKDIK DQLPHALISG GVSNVSFSFR GNDPVREAIH AVFLYHAIRN GMDMGIVNAG QLAIYDDLPI ELKDAVEDVI LNRRDDGTER LLELAEKYRG SGGQEQQIQQ AEWRSWEVEK RLEYSLVKGI TEFIIQDTEE TRQRAASPIE VIEGPLMNGM NVVGDLFSEG KMFLPQVVKS ARVMKQAVAY LEPYIQELKQ SGSSAGKILL ATVKGDVHDI GKNIVGVVLQ CNNYEIIDLG VMVSCETILK TAREKNVDVI GLSGLITPSL DEMVHVAKEM ERQGFTLPLL IGGATTSKAH TAVKIEQNYS GPTVYVQNAS RTVGVVAALL SDIQKNDFVA RTRREYDTVR QQHGRKKPRT PPVPLEVARA NAVKIDWQHY QPPVPKFLGV QEVTASIKIL RDYIDWTPFF MTWSLAGKYP RILEDEVVGE EARKLLADAN AMLDKLDSQN LLTPKGIFGI FPANRVVDDV EIYRSSERDQ VQAVSLNLRQ QTLKTDFPNY CLSDFVAPKE SGKADYIGAF AVTGGLEEDT LAEQYENAHD DYNKIMVKAL ADRLAEAFAE YLHQQVRTQY WGYAPDESLS NEELIRENYQ GIRPAPGYAA CPEHTEKEKI WQLLNVEDKI GMQLTSSYAM WPGASVSGWY FSHPDSKYFA VAQVQKDQIE DYAKRKGMTV AELERWLAPN LGYDPED // ID B6YR37_AZOPC Unreviewed; 1224 AA. AC B6YR37; DT 20-JAN-2009, integrated into UniProtKB/TrEMBL. DT 20-JAN-2009, sequence version 1. DT 27-MAY-2015, entry version 50. DE SubName: Full=Cobalamin-dependent methionine synthase {ECO:0000313|EMBL:BAG83659.1}; GN OrderedLocusNames=CFPG_396 {ECO:0000313|EMBL:BAG83659.1}; OS Azobacteroides pseudotrichonymphae genomovar. CFP2. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Candidatus Azobacteroides. OX NCBI_TaxID=511995 {ECO:0000313|EMBL:BAG83659.1, ECO:0000313|Proteomes:UP000000723}; RN [1] {ECO:0000313|EMBL:BAG83659.1, ECO:0000313|Proteomes:UP000000723} 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP010656; BAG83659.1; -; Genomic_DNA. DR RefSeq; WP_012573420.1; NC_011565.1. DR RefSeq; YP_002309070.1; NC_011565.1. DR STRING; 511995.CFPG_396; -. DR EnsemblBacteria; BAG83659; BAG83659; CFPG_396. DR KEGG; aps:CFPG_396; -. DR PATRIC; 31962536; VBICanAzo57536_0635. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CAZO511995:GKF1-420-MONOMER; -. DR Proteomes; UP000000723; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000723}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000723}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 243 243 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 768 768 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1224 AA; 136953 MW; 5C71455B276501FC CRC64; MNSISQLLQE RILLLDGGMG SMIQNYRLKE TDYRGLQFAH LSGEMYGNSD ILCITRPDII QSIHEAYLEA GADIIETNSM NMTAISMADY GIESHVESLN KAAATIAKEV AQKYTKLTPD KPRFVAGSIG PTNKTSSLSP DVNNPGYRNI TFTELYKAYC EQIAALIFGG VDILLVETAF DTLNVKAALM AAEDEMKIAK KELPLMLSYT LSGNSGRILS GQTLEAVLES ISHINLLSIG LNCSFGARTM KPFLKKLGQI APCYVSAYPN AGLPNAFGKY NETPEMMAEQ IREYIDESLV NIVGGCCGTT PQHIAAIARL VNECKRSIRV PVIKSTELIL SGLEILRISS TNSNCKEIKK GSNFVIIGER CNVAGSRKFL QLIREKNYEE ALKVAQKQIE NGAQVLDVNV DDGLLNGIQE ITTFLNLITS DPDIASIPIM IDSSDWNVIE AGLQCLQGKS IVNSISLKDG EDDFLDKAQK VKSYGAAVIA MAFDEKGQAS DFNRKITVCA RMYELLTSKI DFQPSNIIFD PNILAIATGI EEHNNYAVDF IQAIKWIKKH LPFAKVSGGI SNLSFSFRGN NYLRQAIHSV FLSHAINAGM DMGIINPMEN FMQENISLDL RKLIEDILFN RSSHALENLT EYIRKQTVLS NEEKSSKKKN EWRILPVTER LKYAVIKGID DFLKTDLQEA IKIYPQVMDI IDQPLMEGMN TVSNLFGKGQ MFLPQVVKTA RIMKKAIDIL QPYLEANKKE QIVKSGKILF ATVKGDVHDI GKNITSTILS CNNYEVIDMG VMVPSEEIVR KAKEYHVDII ALSGLITPSL QEMSIVASEM EKAGLSLPLL IGGATTSKLH TALKIDPLYR GAVIHVSDAS KAVPTANHLV NSSTKEDYIK KIKDTYHTLR KYVTNRKELV SLDYARNHSL KIKYTEYNIP KPILNGTKVL DFIHIKDIVP YINWAAFLAA WKFPVQYASF FREKKQVLGD EQEKFNKAIH LINEAQRQLS IWSKDDLQTV RAVIGLYPVK VENESLIVEK RNIPLLRQQE RRADDIYKSL IDFINPEGDY MGFFVVTAGA NIHLSKDDYQ NMLEQILYDR LVEAATEYLH EKVRKEYWGY APNESFTPKE LLLKAPYQGI RPASGYPVHP DISLNFIIND LLKMERIGVK LTSNGAIYPS ASIAGMYIAH PKAEYFHIGK IDDVQLSDYA IRKGISVNEA KKWLGEVVTE QIEI // ID B7A7K0_THEAQ Unreviewed; 1185 AA. AC B7A7K0; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 27-MAY-2015, entry version 37. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EED10692.1}; GN ORFNames=TaqDRAFT_5403 {ECO:0000313|EMBL:EED10692.1}; OS Thermus aquaticus Y51MC23. OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; OC Thermus. OX NCBI_TaxID=498848 {ECO:0000313|EMBL:EED10692.1}; RN [1] {ECO:0000313|EMBL:EED10692.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Y51MC23 {ECO:0000313|EMBL:EED10692.1}; 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., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EED10692.1}. 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; ABVK02000003; EED10692.1; -; Genomic_DNA. DR RefSeq; WP_003045757.1; NZ_ABVK02000003.1. DR EnsemblBacteria; EED10692; EED10692; TaqDRAFT_5403. DR PATRIC; 25940962; VBITheAqu66851_0890. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 256 256 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1185 AA; 131036 MW; 6F40396F305360AD CRC64; MVEVHTCSPG CRHHLGGAGW GEAPLVRLGY NKEARARKFP YLKALLERPV IFDGAMGTEL QKRDLTPEDY GGEAYYGCPE VLNATRPEVI REIHLAYLEA GAEVIETNTF GALRHVLAEY GLGHRAEELA YLGARLAKEA AEPYGAFVAG ALGPGTKLIS LGQITWDELF AAYKEAVRGL LRGGVDLVLL ETAQDILQVR CAVLAAREAM AEVGREVPLQ VQVTIEATGT MLVGTDEQAA LAALESLPID VVGMNCATGP DLMDNKIRYF AQNSTRFVSC LPNAGLPRNE GGKVVYDLTP EELARWHRKF VAEYGVNAVG GCCGTGPEHI RRVAEAVRGL PAPGRPKAFP PQVASLYLAV PLKQEASVFL VGERLNATGS KRFREMLFGR DLEGILALAR EQVEEGAHAL DLSVAWTGRD ELEDLQWLLP HLATAVTVPF MVDSTSPEAM ELALKHLPGR VLLNSVNLED GLEKFDRVAS LAKAHGAALV ALTIDEKGMA KTRAEKVRVA LRMYERLTLH HGFRPEDLLL DLLTFPITQG DEESRPLARE TLLAMEELKE RLPGVGFILG ISNVSFGLKP RARRVLNSVF LDEARKRGLT AAIVDAGKIL PIAQIPEEAY ALALDLIHDR RREGYDPLFA FMAYFEAHRE DVGAKEDAFS ALPLLERLKR RVVEGRKGGL EADLEEALKA GHRPLDLING PLLEGMKEVG ELFGAGKMQL PFVLQAAEVM KRAVAFLEPH MEKRGEGKGK MVLATVKGDV HDIGKNLVDI ILTNNGYQVI NLGIKVPIEE MLKAVEEHRP HALGMSGLLV KSTVVMKENL EYMAERGYTL PVILGGAALT RAYVEELKAI YPNVYYAEDA FEGLRLMEEL TGHAPPELTR REVKGREAPL PRVEVKAKPV GEPAFIPRPP FFGVRKEEGL DLYTIAHYVN KLALYRGQWG YSRKGLSREA WQALVEREAE PVFRRLLKEA REEGWLRPRV LYGFFPVARE GEELLVFSPE TGEVLERFPF PRQKGGGLSL VDYFRPRFAP PLGDEAAWMP EAAFQAGARD VLGVQLVTMG EEPSLKAKAL FESGAYQDYL FVHGFSVEMT EALAEYWHKR MRQMWGIAGK DATDVRKLFQ QGYQGARYSF GYPACPDLSD QAKLDRLMGF SQIGVGLTEN YQLVPEHSTS ALVVHHPEAR YFSAD // ID B7AHY1_9BACE Unreviewed; 923 AA. AC B7AHY1; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 27-MAY-2015, entry version 34. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EEC53757.1}; GN ORFNames=BACEGG_02015 {ECO:0000313|EMBL:EEC53757.1}; OS Bacteroides eggerthii DSM 20697. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=483216 {ECO:0000313|EMBL:EEC53757.1}; RN [1] {ECO:0000313|EMBL:EEC53757.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 20697 {ECO:0000313|EMBL:EEC53757.1}; 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] {ECO:0000313|EMBL:EEC53757.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 20697 {ECO:0000313|EMBL:EEC53757.1}; 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 (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; ABVO01000035; EEC53757.1; -; Genomic_DNA. DR RefSeq; WP_004290322.1; NZ_DS995510.1. DR EnsemblBacteria; EEC53757; EEC53757; BACEGG_02015. DR PATRIC; 27006490; VBIBacEgg69811_2555. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 243 243 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 767 767 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 923 AA; 101022 MW; F14FEA0F9D67FF2C CRC64; MSRLEGLVRE RILILDGAMG TMIQQYNLTE EDFRGERFAQ IPGQLKGNND ILCLTRPDVI RDIHRKYLAV GADIIETNTF SSTSVSMADY HVQDYVREIN LAAVKLAREV ADEFTALTPD KPRFVAGSVG PTNKTCSMSP DVNNPAFRAL TYDELVIAYR EQMEAMLEAG VDALLIETIF DTLNAKAAIY AAKQAMNVAG IRVPLMLSVT VSDIAGRTLS GQTLDAFLAS VQHADIFSIG LNCSFGARQL KPFLEQLAAR APYYVSAYPN AGLPNSLGTY DQTPAEMAAE IKEYIHEGLV NIVGGCCGTT DEYIAAYSSL IDGVVPRIPV GKPDCLWLSG LELLEVRPEN NFVNVGERCN VAGSRKFLRL INEKKYDEAL SIARQQVEDG AQVIDINMDD GLLDAEQEMT TFLHLIASEP EIARVPVMID SSKWDVIVAG LKCVQGKSIV NSISLKEGEE TFLEHARTVK EYGAAAIVMA FDERGQADTY ERRIEVCERA YRLLVDKVGF NPHDIIFDPN VLAVATGMDE HNNYAVDFIR ATGWIRKNLP GAHVSGGVSN LSFSFRGNNY IREAMHAVFL YHAIREGMDM GIVNPATSVL YTDIPADILE RIEDVVLNRR ADAAERLIET AERLKAEADA AKVSAPNGDS QLSASGSRFQ WREGAVEERL KYALTKGVGD YLEEDLAEAL NAYPKAVDII EGPLMAGMNH VGDLFGAGKM FLPQVVKTAR TMKKAVAILQ PVIESEKQAG AASAGKVLLA TVKGDVHDIG KNIVAVVMAC NGYEIIDLGV MVPAETIVQR AIEEKADMIG LSGLITPSLD EMVHVAMELE KAGLDIPLLI GGATTSPLHT ALKIAPVYHA PVVHLKDASQ NASIAARLMN PNQKEELAKN LFTEYQRLRE KNQERQVETV SLEEAKANRL KLF // ID B7AQD9_9FIRM Unreviewed; 603 AA. AC B7AQD9; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 27-MAY-2015, entry version 31. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=BACPEC_00896 {ECO:0000313|EMBL:EEC57911.1}; OS [Bacteroides] pectinophilus ATCC 43243. OC Bacteria; Firmicutes; Clostridia; Clostridiales. OX NCBI_TaxID=483218 {ECO:0000313|EMBL:EEC57911.1}; RN [1] {ECO:0000313|EMBL:EEC57911.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43243 {ECO:0000313|EMBL:EEC57911.1}; 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] {ECO:0000313|EMBL:EEC57911.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43243 {ECO:0000313|EMBL:EEC57911.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; EEC57911.1; -; Genomic_DNA. DR RefSeq; WP_008119891.1; NZ_DS996921.1. DR ProteinModelPortal; B7AQD9; -. DR EnsemblBacteria; EEC57911; EEC57911; BACPEC_00896. DR PATRIC; 27051896; VBIBacPec49690_2166. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 603 AA; 67628 MW; B6C2D32F3693FDB8 CRC64; MMESLREYLK GHRLITDGAM GTYYSEITNN PEAFAEFANI ERPDIIERIH NEYIDAGAKL IRTNTFAANT QMLGIGRDEL KKLIEDACRI AQRCADGRAY VAGDIGPIKE NAESEGSAVE EYKMICDIFL DMKVDAIRFE TFADFDDIKE VAEYVRSKSD MFIMADFCLN KNGFTAGGIS AARIMQQAGQ MDCIDSCGFN CGIGSGHMNN IMQKLTFAKD KYMSCLPNAG YPEQMNNRMV FMNNASYFCD NMQKISAYGM NIIGGCCGTK PAYIRELCRR IGDAVPAGRT ETSDGNEPVN GNNPAEAADI RVNEKRPNEF MQLFKSGHKV VAVELDPPYD AKYDRLIEQA QYLKSIGVDI LTFADSPMGR SRVDSVLMSL KVTQETGMMV MPHVCCRDKN VIAMRSTLLG AYINGIRQLL LVTGDPVPSV SRVSTTGVFD YNSIRLMNFV KEMNQEHFAD EPLYYGGALN VTLGRIDRIM ERMQKKIDNG ASYFMTQPVF SKEGIERLAI IKEKMDTKIL CGIMPLVSYR NANFIKNEFI GIDVPDEIVA RYSPDMSKEE GEAVGAQIAN ELIGQMYDYV DGFYFMLPFN RVSLMDKINI NNR // ID B7AQQ5_9FIRM Unreviewed; 810 AA. AC B7AQQ5; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EEC58027.1}; GN ORFNames=BACPEC_01012 {ECO:0000313|EMBL:EEC58027.1}; OS [Bacteroides] pectinophilus ATCC 43243. OC Bacteria; Firmicutes; Clostridia; Clostridiales. OX NCBI_TaxID=483218 {ECO:0000313|EMBL:EEC58027.1}; RN [1] {ECO:0000313|EMBL:EEC58027.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43243 {ECO:0000313|EMBL:EEC58027.1}; 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] {ECO:0000313|EMBL:EEC58027.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43243 {ECO:0000313|EMBL:EEC58027.1}; 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. {ECO:0000313|EMBL:EEC58027.1}. 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; ABVQ01000035; EEC58027.1; -; Genomic_DNA. DR RefSeq; WP_008120102.1; NZ_DS996921.1. DR EnsemblBacteria; EEC58027; EEC58027; BACPEC_01012. DR PATRIC; 27052118; VBIBacPec49690_2277. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; SQ SEQUENCE 810 AA; 87031 MW; 99848DE8C71C60D5 CRC64; MNNSFRDLLK NEYVILDGAM GTMLQAAGMK MGETPEVLSI TQPELLENIH SQYIKAGSQI VYANTFGANP YKLEGCGYSL EEIVKAAIAN ARRASDANPA EDGSKALVAL DIGPIGQLME PTGTMSFEEA YDMYAQLIKA GSDADLIVFE TMTDLLEVKA GVLAAKENSD LPVMVTMTFE MNHRTFTGVS VQSMALTLEG LGVDAIGVNC SLGPKELEPV VKELADWTNL PIVLKPNAGL PDPKTNKYNL SAADFAESMK ILLPYGIKVF GGCCGTTPDF IRELKNMLKT EGNPATHSKK TGAAVCSPTQ AVAISQPRII GERINPTGKK LFKEALLNND IDYILNQALE QVKGGADILD VNVGLPGIDE KEMMVKVVKA LQGIVDVPLQ IDSTIPEVLE AALRVYNGKP IVNSVNGEEK SLATVLPLVK KYGAAVVGLT LDEGGIPKKA EDRFRIAQKI LDRAQAIGIP KEDVFIDCLT LTASAEQENV METINALHRV KTELGLKTVL GVSNISFGLP NRELVNHIFL AMALNNGLDL PIINPNNEAM TGTVRAYKLL ANYDVNSVEY IKAYANMPKV KKIVIDDNAS GAAAKADGNA PLGGGDTLMH AVLNGLKTEG AQCTEELLKT MDSMEIVNDI LIPALDRIGA DFEKGKIFLP QLIQSAGVAQ AAFEVIKKQM AGKDSKPVSK GKIVIATVKG DIHDIGKNIV KVLLENYGYD VIDLGKDVEY QAVVDAVRES GAKLVGLSAL MTTTLVSMEE TIKLIHENNL DCKIMVGGAV LTPEYAEQIH ADFYAKDAKE SVDIAKRVIG // ID B7BD90_9PORP Unreviewed; 1231 AA. AC B7BD90; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 27-MAY-2015, entry version 35. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEC95600.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEC95600.1}; GN Name=metH {ECO:0000313|EMBL:EEC95600.1}; GN ORFNames=PRABACTJOHN_03010 {ECO:0000313|EMBL:EEC95600.1}; OS Parabacteroides johnsonii DSM 18315. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Parabacteroides. OX NCBI_TaxID=537006 {ECO:0000313|EMBL:EEC95600.1}; RN [1] {ECO:0000313|EMBL:EEC95600.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 18315 {ECO:0000313|EMBL:EEC95600.1}; 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] {ECO:0000313|EMBL:EEC95600.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 18315 {ECO:0000313|EMBL:EEC95600.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEC95600.1}. 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; ABYH01000328; EEC95600.1; -; Genomic_DNA. DR RefSeq; WP_008150888.1; NZ_DS996453.1. DR EnsemblBacteria; EEC95600; EEC95600; PRABACTJOHN_03010. DR PATRIC; 25867296; VBIParJoh38674_2563. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEC95600.1}; KW Transferase {ECO:0000313|EMBL:EEC95600.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1231 AA; 136480 MW; ED43370C1A82B27B CRC64; MDKEMFLNAL KERILILDGG MGTMVQGFKL TEKDYRGEQF ADWPGDLKGN NDLLCITRPD VIKSIHRQYL DAGADIFATN TFNANAISME DYGMQEQVRN INLAAGKLAR EVADGFMAEH PDRTIFVAGS IGPTNKTASM SPDVSDPAYR AVTYMDLYDA YKEQVDALVD GGVDIVLFET TFDTLNVKAG LEAAETVLKE KGKDLPIMLS LTLSAQGGRT FSGQTLLAFL ASVGHANIVS VGLNCSFGAA DMKPYLAELA KHAPYYISAY PNAGLPNSFG SYDETPEKMA VHVKPFIEEG LVNILGGCCG TTPAHIAKYP ELVKGARPHV PAPKPDCLWL SGLELLEVKP ENNFVNVGER CNVAGSRKFL RLIKEENYEE ALTIARKQVE DGAQVIDINM DDGMLDAVKE MTTFLNLIAA EPDISRVPVM IDSSKWEVIE KGLMCVQGKS IVNSISLKEG EELFLQHAAR IKQLGAATVV MAFDEKGQAD TFERKIEVCG RAYRLLREKV DFDPNGIIFD PNVLAIATGM EEHNGYGLDF IRAVEWIKKN LPGAKVSGGI SNLSFSFRGN NYVREAMHSV FLYHAINKGM DMGIVNPSSS VLYEDIEPVF RTLLEDVILA RRPEAAEELI EYAQNLHVKA QEREEEKLEA WREYPLKERL ENALIKGVGD HLEEDLKEAL KEYPRAVDII DGPLMGGMNK VGELFGAGKM FLPQVVKTAR TMKKAVAILQ PAIEAEKVSS DSAKAGKVLF ATVKGDVHDI GKNIVSIVLA CNNYEVIDLG VMVPADVIVK KAIEEKPDLV CLSGLITPSL EEMVHVTDEM QKAGLSIPIM VGGATTSKLH TAIKIAPHYD YPVIHVLDAS QNPLIAAKLL NPDTRDAYIA QLNSEYEALR ASMNKKKEIL VPLAEARTNR PEIDWASYSP VVPARGGVQV IPYIPLEEII PYIHWTFFFS AWKLNGRFSE ITRIHDCDAC RAAWLAEFPE ADRAKASEAM QLYKDTVKLL DRLVEMKAEY CKAIYGFFPA NGDGDNIRMG EVLLPVLRQQ AKREEGIYKS LADYVMPVSE GRTDYVGAFV VTAGVGAESL KERFEREGDT YNSMLLQTLT DRLAEATAEY LHEKVRKEYW GYAPDESLSI SDLYKVKYQG IRPAVGYPSL PDQLLNYTLD KLLDMSQIGV RLTENGAMYP TATVSGIYIA HPDSQYFMIG TIDEEQMKDY ARRRNLSETE TKKLLNKNIS N // ID B7DPN2_9BACL Unreviewed; 641 AA. AC B7DPN2; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 07-JAN-2015, entry version 26. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=AaLAA1DRAFT_0948 {ECO:0000313|EMBL:EED07888.1}; OS Alicyclobacillus acidocaldarius LAA1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Alicyclobacillaceae; OC Alicyclobacillus. OX NCBI_TaxID=543302 {ECO:0000313|EMBL:EED07888.1}; RN [1] {ECO:0000313|EMBL:EED07888.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=LAA1 {ECO:0000313|EMBL:EED07888.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EED07888.1}. 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; ACCS01000007; EED07888.1; -; Genomic_DNA. DR ProteinModelPortal; B7DPN2; -. DR EnsemblBacteria; EED07888; EED07888; AaLAA1DRAFT_0948. DR PATRIC; 24432917; VBIAliAci16525_0972. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EED07888.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EED07888.1}. SQ SEQUENCE 641 AA; 69391 MW; DFF91525E83B5BA1 CRC64; MSDAVWRQWR RPPRDVEGPL GAYVLFDGAM STYLHQLGVP IGTPVEQLNL TSPDLVARVH RRYVESGCTV LQTNTFMGNR VALERHGLTV DVQSLNRRGV EIARSAARGE ASVYGTMGPA MGGYRYGALL QDEERDLLAR VYAEQAEALV SAGIDGLILE TFPDLEEALV AIAAVRPILG DLPLVVNLSP EEIGVTRDGV PLAEAFRRIK AAGADVVGLN CRLGPYGILR SYEQAGVAAD GPYAAVPNAG ILQRSEGDEI AYTGDTQDFS RLMLRIAQLG VRWLGGCCGT TPEYIRTLRD ALMRADHEPH GASIQAETHA TSRPSAVTTG AGAYHDGVSV VDIAKKKKAI VVELDPPKHL SIARFLEGAE ALAGAGADLI TMADNSLGSV RVSNMALASL LKQRGIEPLV HVTCRDRNLI GQQSHLMGLA VLGIRNVLLV TGDPSRYGEL PGATSVYDVS SMDLTKMVRR LNEGIGFSGQ PLKQPSRFVI GTAFNPHVHN FQKAVERLRR KVEAGADFVM TQPVFDPDLM AAIAEATRDL GVPVFVGIMP LTSARNAEFL HHQVPGIRLS EQALRRMQEA APEEAPAVGE AIARELVEIA IRLFPGIYLV TPFLRYEMTV RLTEYARSLE TRLVSQSHGP N // ID B7G6P4_PHATC Unreviewed; 346 AA. AC B7G6P4; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 04-MAR-2015, entry version 25. DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EEC45628.1}; GN ORFNames=PHATRDRAFT_48307 {ECO:0000313|EMBL:EEC45628.1}; OS Phaeodactylum tricornutum (strain CCAP 1055/1). OC Eukaryota; Stramenopiles; Bacillariophyta; Bacillariophyceae; OC Bacillariophycidae; Naviculales; Phaeodactylaceae; Phaeodactylum. OX NCBI_TaxID=556484 {ECO:0000313|Proteomes:UP000000759}; RN [1] {ECO:0000313|EMBL:EEC45628.1, ECO:0000313|Proteomes:UP000000759} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCAP 1055/1 {ECO:0000313|EMBL:EEC45628.1, RC ECO:0000313|Proteomes:UP000000759}; 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] {ECO:0000313|EMBL:EEC45628.1, ECO:0000313|Proteomes:UP000000759} RP GENOME REANNOTATION. RC STRAIN=CCAP 1055/1 {ECO:0000313|EMBL:EEC45628.1, RC ECO:0000313|Proteomes:UP000000759}; 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; CM000619; EEC45628.1; -; Genomic_DNA. DR RefSeq; XP_002182892.1; XM_002182856.1. DR UniGene; Ptc.18924; -. DR STRING; 2850.JGI48307; -. DR EnsemblProtists; Phatr3_J48307.t1; Phatr3_J48307.p1; Phatr3_J48307. DR GeneID; 7203734; -. DR KEGG; pti:PHATRDRAFT_48307; -. DR HOGENOM; HOG000265278; -. DR InParanoid; B7G6P4; -. DR Proteomes; UP000000759; Chromosome 17. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 2. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000759}; KW Reference proteome {ECO:0000313|Proteomes:UP000000759}. SQ SEQUENCE 346 AA; 37107 MW; 217AC163E891F913 CRC64; MTPSAANTND ANRPFILLDG GTGREIQQRG GPFRQPEWSA LALYEDPDIV RAVHESFLNA GSTAITTNTY ALVPYHIGSD RFRKDAPRLF SLAISLAAEA KGDRQHVQIL GSIPPVCGSY EPQSFDEATA KSILDWFMPV LGDSPLVDAY LLETVGSTRE ARFYLQYMQS FVKAVAESLD SLSNGTLARE KPVWLSFCIA SHPGATQTPH LLTGETLTQA VHALIEEGLL TAATVPVVLV NCCDVKLVLN AVQELHAVLS PLGIRVGAYP NAFSIPPPNA ANHTLRQVDY NVTPGRWAAT AKSWINAGAS VVGGCCGVGP KYITALASVV AQSKESTDVD IFETLD // ID B7G9Z1_PHATC Unreviewed; 418 AA. AC B7G9Z1; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 04-MAR-2015, entry version 25. DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EEC44528.1}; GN ORFNames=PHATRDRAFT_39914 {ECO:0000313|EMBL:EEC44528.1}; OS Phaeodactylum tricornutum (strain CCAP 1055/1). OC Eukaryota; Stramenopiles; Bacillariophyta; Bacillariophyceae; OC Bacillariophycidae; Naviculales; Phaeodactylaceae; Phaeodactylum. OX NCBI_TaxID=556484 {ECO:0000313|Proteomes:UP000000759}; RN [1] {ECO:0000313|EMBL:EEC44528.1, ECO:0000313|Proteomes:UP000000759} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCAP 1055/1 {ECO:0000313|EMBL:EEC44528.1, RC ECO:0000313|Proteomes:UP000000759}; 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] {ECO:0000313|EMBL:EEC44528.1, ECO:0000313|Proteomes:UP000000759} RP GENOME REANNOTATION. RC STRAIN=CCAP 1055/1 {ECO:0000313|EMBL:EEC44528.1, RC ECO:0000313|Proteomes:UP000000759}; 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; CM000623; EEC44528.1; -; Genomic_DNA. DR RefSeq; XP_002183859.1; XM_002183823.1. DR STRING; 2850.JGI39914; -. DR EnsemblProtists; Phatr3_J39914.t1; Phatr3_J39914.p1; Phatr3_J39914. DR GeneID; 7195541; -. DR KEGG; pti:PHATRDRAFT_39914; -. DR InParanoid; B7G9Z1; -. DR Proteomes; UP000000759; Chromosome 21. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000759}; KW Reference proteome {ECO:0000313|Proteomes:UP000000759}. SQ SEQUENCE 418 AA; 46045 MW; 6C2382B976736FAF CRC64; MVRPSIDYYL PQMPSLLQDW FTSPDSASHT DRILVLDGGV STHLESNLSS TNADSASSDK LSCRTCAFPH RELWSSSLLL SESGRRLVRQ GHDDWLRAGA NVLSTVTYQC HYQAAYWPKG KMATNDKDSR VMDDAVVNTL WNDGVEIAQQ AVKDYCHNQQ RPHTLRQPEL ETSSVPRYVV ASSGCYGAIL ANGAEYTGNY GPVTVDDLVH FHRRKVRRAV QLHPDGIAIE TVPSLLECHA LVQLFQPTNG AAPMLLNKTA CWISLSCRNE RELNDGTPLV AALNVLSQIP CTAVSAWGLN CCSVTHLPAL VRILTQHVAQ EASGKHRRGL VLYPNSGELW DAVTGTWHTG TGCTAPAAMA SEIVAVLRTV EDEWRRHRPT DPTPSILIGG CCRTSPATIA ALRVLVDDHL QQEYKGWF // ID B7GBG7_PHATC Unreviewed; 1245 AA. AC B7GBG7; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 01-APR-2015, entry version 45. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEC44210.1}; GN Name=METH {ECO:0000313|EMBL:EEC44210.1}; GN ORFNames=PHATRDRAFT_23399 {ECO:0000313|EMBL:EEC44210.1}; OS Phaeodactylum tricornutum (strain CCAP 1055/1). OC Eukaryota; Stramenopiles; Bacillariophyta; Bacillariophyceae; OC Bacillariophycidae; Naviculales; Phaeodactylaceae; Phaeodactylum. OX NCBI_TaxID=556484 {ECO:0000313|Proteomes:UP000000759}; RN [1] {ECO:0000313|EMBL:EEC44210.1, ECO:0000313|Proteomes:UP000000759} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCAP 1055/1 {ECO:0000313|EMBL:EEC44210.1, RC ECO:0000313|Proteomes:UP000000759}; 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] {ECO:0000313|EMBL:EEC44210.1, ECO:0000313|Proteomes:UP000000759} RP GENOME REANNOTATION. RC STRAIN=CCAP 1055/1 {ECO:0000313|EMBL:EEC44210.1, RC ECO:0000313|Proteomes:UP000000759}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CM000625; EEC44210.1; -; Genomic_DNA. DR RefSeq; XP_002184461.1; XM_002184425.1. DR UniGene; Ptc.1599; -. DR ProteinModelPortal; B7GBG7; -. DR STRING; 2850.JGI23399; -. DR GeneID; 7198319; -. DR KEGG; pti:PHATRDRAFT_23399; -. DR HOGENOM; HOG000251409; -. DR InParanoid; B7GBG7; -. DR KO; K00548; -. DR Proteomes; UP000000759; Chromosome 23. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000759}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000759}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 230 230 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 765 765 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1245 AA; 137880 MW; 36A6AF159FD29367 CRC64; MGTMIQNYAK KNRLDEEEYR GERFRDWNCA VKGNNDMLSI SQPHIIKGIY MQYLEEGGSN MIGTNTFSST TIAMADYQME AYAYELNYVG ARLAREACDE VTAKDPSKPR FVVGAIGPTN RTCSISPSVE DPAARNVTFD ELVETYLEQV VGLVDGGADV LMVETIFDTL NAKAALYAIG EFLEFSGLDI PVFVSGTLVD QSGRTLSGQT GEAFYVSIRH AKPMCVGLNC ALGAKHMVPF VERLSKAAEC FVHVYSNAGL PNAMGGYDDT PEDMARENEV FFENGWLNMV GGCCGSTPPH IKAIRETAER YQPRKLPDVG RPKMWLSGLE DLKVEDVHNQ LGLPFLNVGE RCNIAGSIKF KKLMMKGDYG AAMDIAKQQV EDGAHVIDIN VDDGMLDGLA AMQKFVKIAV TEPEIAKVPF MLDASKFDIV MAGLKWCQGK CIVNSISLKV GEELFMEQAT LLKKHGAAVV VMAFDEQGQA ATEDEKIRIC KRSYDVLVNK VGFPPEDIVF DPNVLTIGTG MEEHANYGVD FINSVKRIKE ECPYVKISGG ISNLSFGFRG VTKIRESIHA VFLHHAITES GMDVGIVNSH ELLSVDDLEP DMKLLCENLV FNKTPDATDD MLERTNFERS KGGVVDEVKK SSWRDLEPSK RLEHSLVNGI SEFVDSDVEE ARVLATKPLD VIEGPLMDGM NVVGDLFGAG KMFLPQVIKS ARVMKKAVAY LLPFMDAEKR ENMIAAGLDP DDVDPDDDSN YAGKVLMATV KGDVHDIGKN IVAVVLGCNN YKVYDIGVMC SCEKILAKAK EYNVDVIGLS GLITPSLDEM VDVAKEMSKQ GFKQPLLIGG ATTSKMHTSV KIAPSYTTPE HPTIHVLDAS RSVTVVNSLL GENKGEFVED IMEEYEEMRE DYYAGLEDRN FLTFEKAKEQ KITINFDQSP VADTPNKIGI TVIDTVKISA VVPYIDWNPF FQTWELRGRY PNRGYPKIFN DEAVGGEAKK LFHDAQTMLN QICEDGSMTL KGVVGIFPAN RSEDGEDVHV YETEADRESG NVSTTFCMLR QQAEKESDDP YLSQADFVAP AGYKDHLGMF AVSCFGCDAL VKKFESENDD YSKIMAQALA DRFVEAFAEY VHREMRLDLW GYAAGEQLNE SDLLKVKYDG IRPAPGYPSQ PDHTEKRTMW NLLQAQELAG IELSESLSMM PASSVSALVF AHPESEYFAV GQVGKDQVTN YASRKQMDLA LCERWLSPIL NYERD // ID B7GLS4_ANOFW Unreviewed; 617 AA. AC B7GLS4; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 27-MAY-2015, entry version 40. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=Aflv_2165 {ECO:0000313|EMBL:ACJ34524.1}; OS Anoxybacillus flavithermus (strain DSM 21510 / WK1). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Anoxybacillus. OX NCBI_TaxID=491915 {ECO:0000313|EMBL:ACJ34524.1, ECO:0000313|Proteomes:UP000000742}; RN [1] {ECO:0000313|EMBL:ACJ34524.1, ECO:0000313|Proteomes:UP000000742} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 21510 / WK1 {ECO:0000313|Proteomes:UP000000742}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ACJ34524.1; -; Genomic_DNA. DR RefSeq; WP_012575702.1; NC_011567.1. DR RefSeq; YP_002316509.1; NC_011567.1. DR ProteinModelPortal; B7GLS4; -. DR STRING; 491915.Aflv_2165; -. DR EnsemblBacteria; ACJ34524; ACJ34524; Aflv_2165. DR KEGG; afl:Aflv_2165; -. DR PATRIC; 20956233; VBIAnoFla45531_2224. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; AFLA491915:GHEO-2235-MONOMER; -. DR Proteomes; UP000000742; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000742}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ACJ34524.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000000742}; KW Transferase {ECO:0000313|EMBL:ACJ34524.1}. SQ SEQUENCE 617 AA; 68746 MW; 31B025FB9FD77F02 CRC64; MDVGLLDDLK ERIVIADGAM GTLLYAHGID RCFEELNVTK PEEIVHIHEA YIDAGAEIIQ TNTYGANYVK LARYGLQDDV KKINEAAVSL AKQAAKGRAY VLGTIGGLRS TNKSTISLEE VKRTFREQLY VLLNENVDGL LLETYYDFEE LQTVLSIARQ ETTLPIIAHV TLHDIGVLQH GMPLAEALRQ LEQLGADVVG LNCHLGPYHM LRSLEEVPIP SRAFLSVYPN ASLPQYRDGR FVYETSEQYF EETARAFRDQ GVRLIGGCCG TTPKHIAAIA RALSDRTPVY KKEVKQRHTI IIQEEKQTTA PSLADIARMR RSIIVELDPP KKLGLTKFLE GAKALKEAHI DALTLADNSL ATPRISNVAV GTIVKQQLNM RPLIHITCRD RNLIGLQSHL MGLHTLGMTD VLALTGDPSK VGDFPGATSV YDLSSFDLIS LIRQFNEGLS YSGKPLGQKT NFSIAAAFNP NVRHLDKAVK RLEKKIECGA HYFLTQPLYS EKQMEDVYEA TKHLSTPIYI GIMPLTSARN ADFLHHEVPG ITLSDDIRAR MAACANDPIQ ATKEGLAIAK SLIDAAFDLF QGIYLITPFL RYDMTVELVR YIHEKERLAK ERTVYYG // ID B7GLS5_ANOFW Unreviewed; 1142 AA. AC B7GLS5; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 29-APR-2015, entry version 49. DE SubName: Full=Methionine synthase I containing methyltransferase and cobalamin-binding domains {ECO:0000313|EMBL:ACJ34525.1}; GN OrderedLocusNames=Aflv_2166 {ECO:0000313|EMBL:ACJ34525.1}; OS Anoxybacillus flavithermus (strain DSM 21510 / WK1). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Anoxybacillus. OX NCBI_TaxID=491915 {ECO:0000313|EMBL:ACJ34525.1, ECO:0000313|Proteomes:UP000000742}; RN [1] {ECO:0000313|EMBL:ACJ34525.1, ECO:0000313|Proteomes:UP000000742} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 21510 / WK1 {ECO:0000313|Proteomes:UP000000742}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000922; ACJ34525.1; -; Genomic_DNA. DR RefSeq; WP_012575703.1; NC_011567.1. DR RefSeq; YP_002316510.1; NC_011567.1. DR ProteinModelPortal; B7GLS5; -. DR STRING; 491915.Aflv_2166; -. DR EnsemblBacteria; ACJ34525; ACJ34525; Aflv_2166. DR KEGG; afl:Aflv_2166; -. DR PATRIC; 20956235; VBIAnoFla45531_2225. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; AFLA491915:GHEO-2236-MONOMER; -. DR Proteomes; UP000000742; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000742}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACJ34525.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000742}; KW Transferase {ECO:0000313|EMBL:ACJ34525.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 238 238 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 301 301 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 302 302 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 734 734 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1142 AA; 126026 MW; F6D0BDA484610D3A CRC64; MKKNGSQKKG RFTMASLFAQ LEKKILIIDG AMGTMIQAAN LTADDFGGEA YEGCNEYLTL TAPHVISHIH EAYFAAGADI VETNTFGATR IVLDEYNLGH LALELNMEAA KLAKRAAEKY TTSDHPRFVA GSMGPTTKTL SVTGGATFAE LISSYEEQAR GLLLGGVDLL LLETCQDTLN VKAAFLGITK AFQAVGKQVP LMISGTIEPM GTTLAGQTIE SFFISVQHMK PFAIGLNCAT GPEFMTDHLR SLASLANTAV SCYPNAGLPD EEGHYHETPE MLAKKIRQFA EKGWLNIVGG CCGTTPQHIQ AIAEAVRDIP PRAIPKQFAM HAVSGIDALI YDETMRPLFV GERTNVIGSR KFKRLIAEGK YEEAAEIARA QVKNGAHVID ICLADPDRDE KEDMEQFIQQ VVKKVKVPLV IDSTDEDVIA CALSYSQGKA IINSINLEDG EERFEKIVPL LHQYGAAVVV GTIDEQGMAI EAKRKLDIAL RSYDLLVNKY GVSPHDIIFD PLVFPIGTGD EQYIGAAKET IEGIRLIKQH LPNCLTMLGI SNVSFGLPPV GREVLNSVFL YHCTQAGLDY AIVNTEKLER FASIPEEEVR LAEALLFDTN DETLNAFIQF YRDKTKQPKQ TNVHMTLEER LAAYVVEGTK DGLIEDLTLA LQTYSPLDII NGPLMNGMDE VGRLFNDNQL IVAEVLQSAE VMKAAVAFLE PYMEKNETSV KGKVLLATVK GDVHDIGKNL VDIILSNNGF HVVDLGIKVT PQQLIEAVRH EQPDMIGLSG LLVKSAQQMV LTAQDLKQAG ISLPILVGGA ALSRKFTDTK IAPEYDGIVL YAKDAMEGLT LANRIVQQDI VYEKKEQVEH VTKQQSAVAV MTKSNVKQAP IYVPVDTERH ILQHIPLSHI EPYVNWQMLL GHHLGLKGNV KQLLAEGNEK AMMLKELIDE LLAEAKRTNS LAPKAVYQFF PATSDGDTVI IYDPRDQQTV IETFTFPRQT KAPYLCLADY LSSEQIDYVG LFAVTAGAGV RDLAQRFKEE GQFLKSHAIQ ALALELAEGL AERVHQIMRD RWGFPDSPDF TMEQRFAAKY QGQRFSFGYP ACPNLEDQEK LFRLLRPEEI GIQLTEGYMM EPEASVSAIV FAHPEARYFN VL // ID B7HCM6_BACC4 Unreviewed; 1132 AA. AC B7HCM6; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 01-APR-2015, entry version 46. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACK61099.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ACK61099.1}; GN Name=metH {ECO:0000313|EMBL:ACK61099.1}; GN OrderedLocusNames=BCB4264_A4366 {ECO:0000313|EMBL:ACK61099.1}; OS Bacillus cereus (strain B4264). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=405532 {ECO:0000313|EMBL:ACK61099.1, ECO:0000313|Proteomes:UP000007096}; RN [1] {ECO:0000313|EMBL:ACK61099.1, ECO:0000313|Proteomes:UP000007096} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B4264 {ECO:0000313|EMBL:ACK61099.1, RC ECO:0000313|Proteomes:UP000007096}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001176; ACK61099.1; -; Genomic_DNA. DR RefSeq; WP_000649673.1; NC_011725.1. DR RefSeq; YP_002369059.1; NC_011725.1. DR STRING; 405532.BCB4264_A4366; -. DR EnsemblBacteria; ACK61099; ACK61099; BCB4264_A4366. DR KEGG; bcb:BCB4264_A4366; -. DR PATRIC; 18880627; VBIBacCer117876_4220. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; BCER405532:GI1K-4326-MONOMER; -. DR Proteomes; UP000007096; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007096}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACK61099.1}; KW Transferase {ECO:0000313|EMBL:ACK61099.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 125831 MW; 9EB3147EB5408A18 CRC64; MKCIEEKLKN SILILDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYDLSHLDE ELNEKAALLA KQAVKESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGA VDVLLVETSQ DMRNVKAAYI GIQAAFEELK KTVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWVN IIGGCCGTTP EHIKAMKSAL ASLRPRDHHE REGHGISGLE ALQYDESMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMENF LAEVTKVLKV PIMIDSTDEN VMERALTYIQ GKAVINSINL EDGEERFKKV TPLLQKYGAA IVVGTIDEDG MAVSAERKIE IAKRSYELLT KKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIDGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPEE EKRLADALLF ETTKETLEEF TNFYRVAKKK DVVVQETLTL DERLANYIVE GTKQGLHEDL SLALEEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILA NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAANIDVPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV KKEEKKVEIP AVIEPLPKSE VMVPDSTKRI VLRDVPALHL APFLNRQMLL GHHLGLKGNV KKLLKEGDKR AHELNDLIDE LLQEGQSWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRVIE RFTFPRQGKA PYRTLGDYLR PIGDEMDYVA FLSVTVGEGV RDIAEELKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID B7HCM7_BACC4 Unreviewed; 610 AA. AC B7HCM7; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 27-MAY-2015, entry version 41. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=BCB4264_A4367 {ECO:0000313|EMBL:ACK63920.1}; OS Bacillus cereus (strain B4264). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=405532 {ECO:0000313|EMBL:ACK63920.1, ECO:0000313|Proteomes:UP000007096}; RN [1] {ECO:0000313|EMBL:ACK63920.1, ECO:0000313|Proteomes:UP000007096} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B4264 {ECO:0000313|EMBL:ACK63920.1, RC ECO:0000313|Proteomes:UP000007096}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ACK63920.1; -; Genomic_DNA. DR RefSeq; WP_000770352.1; NC_011725.1. DR RefSeq; YP_002369060.1; NC_011725.1. DR ProteinModelPortal; B7HCM7; -. DR STRING; 405532.BCB4264_A4367; -. DR EnsemblBacteria; ACK63920; ACK63920; BCB4264_A4367. DR KEGG; bcb:BCB4264_A4367; -. DR PATRIC; 18880629; VBIBacCer117876_4221. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; BCER405532:GI1K-4327-MONOMER; -. DR Proteomes; UP000007096; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007096}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ACK63920.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:ACK63920.1}. SQ SEQUENCE 610 AA; 67207 MW; 6AAA70A0BB40008A CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNVSDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTE INRAAVKLAK ASVTDKNAIL GTIGGMKHIG AVTTTDMERE FMLLEQAGAL LEEQVDGLLL ETFYDEFELL HAVKVLRKQT NIPIVAQLAL HEAGTTQNGN DVNEILKQLI DYGANVVGLN CQLGPLHMTE AFKMISIPQN GYLSAYPNAG LPNYVDGRYV YEGSPAYFEA MTPRFIEQGI RLLGGCCGTT PEHIQSMKRA VANITPVIEK DTIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRVSNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIK LIEEVYEATK HLEQPIFIGI MPLVSKRNAD FLHFEVPGIT LPEEIRERMD GHETKEAAIE EGIRISQELV DAAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID B7HPF4_BACC7 Unreviewed; 1132 AA. AC B7HPF4; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 27-MAY-2015, entry version 46. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:ACJ77985.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ACJ77985.1}; GN Name=metH {ECO:0000313|EMBL:ACJ77985.1}; GN OrderedLocusNames=BCAH187_A4385 {ECO:0000313|EMBL:ACJ77985.1}; OS Bacillus cereus (strain AH187). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=405534 {ECO:0000313|EMBL:ACJ77985.1, ECO:0000313|Proteomes:UP000002214}; RN [1] {ECO:0000313|EMBL:ACJ77985.1, ECO:0000313|Proteomes:UP000002214} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AH187 {ECO:0000313|EMBL:ACJ77985.1, RC ECO:0000313|Proteomes:UP000002214}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001177; ACJ77985.1; -; Genomic_DNA. DR RefSeq; WP_000649709.1; NC_011658.1. DR RefSeq; YP_002340315.1; NC_011658.1. DR ProteinModelPortal; B7HPF4; -. DR STRING; 405534.BCAH187_A4385; -. DR EnsemblBacteria; ACJ77985; ACJ77985; BCAH187_A4385. DR KEGG; bcr:BCAH187_A4385; -. DR PATRIC; 18834203; VBIBacCer120511_4572. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; BCER405534:GHXM-4320-MONOMER; -. DR Proteomes; UP000002214; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002214}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACJ77985.1}; KW Transferase {ECO:0000313|EMBL:ACJ77985.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 125917 MW; CAF651DF42EF4C1F CRC64; MKCIEEKLQN NILLLDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYELSHLDE ELNEKAARLA KQAVEESGKE IYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGE VDVLLVETSQ DMRNVKAAYI GIQAAFDELN TVVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWVN IIGGCCGTTP EHIKAMKSAL TSLKPREQQE RAGHGVSGLE ALQYDDSMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEI ARAQVKKNAH IIDICMADPD RDEIEDMENF LAEVTKVLKV PIMIDSTDEH VMERALTYIQ GKAVINSINL EDGEERFEKV TPLLRKYGAA IVVGTIDEDG MAVSAERKLE IAKRSYELLT TKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPDE EKRLADALLF ETTQETLEKF TNFYRVAKKK DVVVQETLTL DERLANYIVE GTKQGLHEDL SLALTEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILA NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAADIDIPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV TKEEKKVEIP AVIEPLPKSE VMVPDSTKRI VLRDVPVSHL APFLNRQMLL GHHLGLKGSV KKLLREGDKR AHELNDLIDE LLQEGQSWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRIIE RFTFPRQGKA PYRTLGDYLR PVGDEMDYVA FLSVTVGEGV RDIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID B7HPF5_BACC7 Unreviewed; 610 AA. AC B7HPF5; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 27-MAY-2015, entry version 39. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=BCAH187_A4386 {ECO:0000313|EMBL:ACJ77366.1}; OS Bacillus cereus (strain AH187). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=405534 {ECO:0000313|EMBL:ACJ77366.1, ECO:0000313|Proteomes:UP000002214}; RN [1] {ECO:0000313|EMBL:ACJ77366.1, ECO:0000313|Proteomes:UP000002214} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AH187 {ECO:0000313|EMBL:ACJ77366.1, RC ECO:0000313|Proteomes:UP000002214}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ACJ77366.1; -; Genomic_DNA. DR RefSeq; WP_000770335.1; NC_011658.1. DR RefSeq; YP_002340316.1; NC_011658.1. DR ProteinModelPortal; B7HPF5; -. DR STRING; 405534.BCAH187_A4386; -. DR EnsemblBacteria; ACJ77366; ACJ77366; BCAH187_A4386. DR KEGG; bcr:BCAH187_A4386; -. DR PATRIC; 18834205; VBIBacCer120511_4573. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; BCER405534:GHXM-4321-MONOMER; -. DR Proteomes; UP000002214; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002214}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ACJ77366.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:ACJ77366.1}. SQ SEQUENCE 610 AA; 67212 MW; C311353A7C332F2C CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNISDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTE INRAAVKLAK ASVTDRNAIL GTIGGMKHIG AVTTTDMERE FMLLEQASAL LEEQVDGLLL ETFYDEFELL HAVQVLRKET NIPIVAQLAL HEAGTTQNGN DVNEILKQLL DYGANVVGLN CQLGPLHMTE AFKMISIPKN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPKFIEQGI RLLGGCCGTT PEHIESMKRA TLNVTPVIEK DTVQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRISNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSVL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIA LIEEVYEATK HLEQPIFIGI MPLISKRNAD FLHFEVPGIT LPEAVRERMD GHETKETAIE EGIRISQELI DAAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID B7IHI6_THEAB Unreviewed; 773 AA. AC B7IHI6; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 29-APR-2015, entry version 40. DE SubName: Full=5-methyltetrahydrofolate S-homocysteine methyltransferase {ECO:0000313|EMBL:ACJ75550.1}; GN OrderedLocusNames=THA_1094 {ECO:0000313|EMBL:ACJ75550.1}; OS Thermosipho africanus (strain TCF52B). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermosipho. OX NCBI_TaxID=484019 {ECO:0000313|EMBL:ACJ75550.1, ECO:0000313|Proteomes:UP000002453}; RN [1] {ECO:0000313|EMBL:ACJ75550.1, ECO:0000313|Proteomes:UP000002453} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TCF52B {ECO:0000313|EMBL:ACJ75550.1, RC ECO:0000313|Proteomes:UP000002453}; RX PubMed=19124572; DOI=10.1128/JB.01448-08; RA Nesboe C.L., Bapteste E., Curtis B., Dahle H., Lopez P., Macleod D., RA Dlutek M., Bowman S., Zhaxybayeva O., Birkeland N.-K., Doolittle W.F.; RT "The genome of Thermosipho africanus TCF52B: lateral genetic RT connections to the Firmicutes and Archaea."; RL J. Bacteriol. 191:1974-1978(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; CP001185; ACJ75550.1; -; Genomic_DNA. DR RefSeq; WP_012579997.1; NC_011653.1. DR RefSeq; YP_002334891.1; NC_011653.1. DR STRING; 484019.THA_1094; -. DR EnsemblBacteria; ACJ75550; ACJ75550; THA_1094. DR KEGG; taf:THA_1094; -. DR PATRIC; 23919194; VBITheAfr129358_1109. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; TAFR484019:GJOH-1126-MONOMER; -. DR Proteomes; UP000002453; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002453}; KW Methyltransferase {ECO:0000313|EMBL:ACJ75550.1}; KW Transferase {ECO:0000313|EMBL:ACJ75550.1}. SQ SEQUENCE 773 AA; 86231 MW; E4E80EFC359E04F3 CRC64; MNRKEFLQML NERIYFLDGA YGTEFFKKGF KGVIETLNIT DKEMVFDLQK AYVDAGVDFL LTNTFSANRL KLKSLKVSYN IKDINYNAVK IAKQAAGQKN VYVLGDISST GFLIEPLGEI SFDEAYDVFR EQGEILLNAG VDGFIIETMS DLKELKAAIL ALRDLSQDIP IIAQMTFEEN SKAVTGTSVE IFATLLNDLD VDVIGINCTL EPEKLLSVFK KLAQYSKKPI SVEPNAGKPK LQRDGSIVYK TSPEKFAIYM EDFVEVGANI VGGCCGTSPE HIRLMIKFLK NRKPKKRKII AEEFVSSRTK LQKISPFLII GERINAAGKK KFQEKIKNKD FSKIVELSSM QEQEGAHVLD VNLGIEKLLD KSHFSLVVNT LDKIGSLPLS LDIQEFEFME EALKEYVGRP IINSSTAKKE KLDNAIYLLK RYGGVLVLLT MKDKIPETAK ERFEIAKEAV EYLEKNGIER NRILVDPLVL PVGAKKDPKV TVETIELLSK EGLMTSVGLS NLSFGMPNRE ALNASFLTLC LDKGLNAAIL NTSEKCTMNA IFGTLVLKGK ELAKQEFLKE DPLVEMILKK KEKEIKQEIE KLLEEYSPLQ ISQNILSKAM EHIGELYSKG VIYLPHLILA AETVTPVFEY LNSLLEKNDK QKIGTIIVAT VEGDVHDIGK KIVATLFKSS GFNVIDLGKD VPASKILEEV KKHKPDILGL SAMMTTTIGR IKEVKDLLEK EGVKIPIIAG GASLNKEIAE NFGVYYAKNA SEGLKLSKKI LKR // ID B7IXP7_BACC2 Unreviewed; 1132 AA. AC B7IXP7; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 29-APR-2015, entry version 47. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACK98397.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ACK98397.1}; GN Name=metH {ECO:0000313|EMBL:ACK98397.1}; GN OrderedLocusNames=BCG9842_B0868 {ECO:0000313|EMBL:ACK98397.1}; OS Bacillus cereus (strain G9842). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=405531 {ECO:0000313|EMBL:ACK98397.1, ECO:0000313|Proteomes:UP000006744}; RN [1] {ECO:0000313|EMBL:ACK98397.1, ECO:0000313|Proteomes:UP000006744} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G9842 {ECO:0000313|EMBL:ACK98397.1, RC ECO:0000313|Proteomes:UP000006744}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001186; ACK98397.1; -; Genomic_DNA. DR RefSeq; WP_000649724.1; NC_011772.1. DR RefSeq; YP_002447831.1; NC_011772.1. DR STRING; 405531.BCG9842_B0868; -. DR EnsemblBacteria; ACK98397; ACK98397; BCG9842_B0868. DR KEGG; bcg:BCG9842_B0868; -. DR PATRIC; 18904269; VBIBacCer50903_4286. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; BCER405531:GI5L-4387-MONOMER; -. DR Proteomes; UP000006744; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006744}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACK98397.1}; KW Transferase {ECO:0000313|EMBL:ACK98397.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 125940 MW; 03312D522E03B9C4 CRC64; MKCIEEKLQN SILILDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYELSHLDE ELNEKAALLA KQAVKESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGE VDVLLVETSQ DMRNVKAAYI GIQAAFEEMK KTVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWVN IIGGCCGTTP EHIKAMKSAL ASLKPRDHHE REGHGISGLE ALQYDESMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMEKF LTEVTKVLKV PIMIDSTDEN VMARALTYIQ GKAVINSINL EDGEERFEKV TPLLRKYGAA IVVGTIDEDG MAVSAERKLE IAKRSYELLT TKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPEE EKHLADALLF ETTKETLEEF TNFYRVAKKK DVVVQETLTL NERLANYIVE GTKQGLHEDL SLALEEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPYMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILA NNGYEIINLG INVRSDRIVQ EVQEKNPDII GLSGLLVKSA QQMVTTAEDL KAANIDVPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV KKEEKKVEIP AVIEPLPKAE VIVPDSTKRI VLRDIPALHL APFLNRQMLL GHHLGLKGNV KKLLKEGDKR AHELNDLIDE LLQEGQSWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRVIE RFTFPRQGKA PYRTLGDYLR PIGDEMDYVA FLSVTVGEGV RDIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID B7IXP8_BACC2 Unreviewed; 610 AA. AC B7IXP8; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 01-APR-2015, entry version 42. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=BCG9842_B0867 {ECO:0000313|EMBL:ACK94865.1}; OS Bacillus cereus (strain G9842). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=405531 {ECO:0000313|EMBL:ACK94865.1, ECO:0000313|Proteomes:UP000006744}; RN [1] {ECO:0000313|EMBL:ACK94865.1, ECO:0000313|Proteomes:UP000006744} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G9842 {ECO:0000313|EMBL:ACK94865.1, RC ECO:0000313|Proteomes:UP000006744}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ACK94865.1; -; Genomic_DNA. DR RefSeq; WP_000770366.1; NC_011772.1. DR RefSeq; YP_002447832.1; NC_011772.1. DR ProteinModelPortal; B7IXP8; -. DR STRING; 405531.BCG9842_B0867; -. DR EnsemblBacteria; ACK94865; ACK94865; BCG9842_B0867. DR KEGG; bcg:BCG9842_B0867; -. DR PATRIC; 18904271; VBIBacCer50903_4287. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; BCER405531:GI5L-4388-MONOMER; -. DR Proteomes; UP000006744; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006744}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ACK94865.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:ACK94865.1}. SQ SEQUENCE 610 AA; 67213 MW; 44842EA915BA1A49 CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNVSDPD LIISIHKQYV AAGADVIQTN TYGANETKLR MYGLENQVTE INRAAVKLAK ASVTDRNAIL GTIGGMKHIG AVTTTDMERE FMLLEQAGAL LEEQVDGLLL ETFYDEFELL HAVKVLRKQT NIPIVAQLAL HEAGTTQNGN DVNEILKQLI DCGANVVGLN CQLGPLHMTE AFKMISIPQN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPRFIEQGI RLLGGCCGTT PEHIQSMKHA VANITPVIEK DTIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRISNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIA LIEEVYEATK HLEQPIFIGI MPLVSKRNAD FLHFEVPGIT LPEEIRERMD GHETKEAAIE EGIRISQELI DIAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID B7JMX8_BACC0 Unreviewed; 1132 AA. AC B7JMX8; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 27-MAY-2015, entry version 47. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:ACK87173.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ACK87173.1}; GN Name=metH {ECO:0000313|EMBL:ACK87173.1}; GN OrderedLocusNames=BCAH820_4274 {ECO:0000313|EMBL:ACK87173.1}; OS Bacillus cereus (strain AH820). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=405535 {ECO:0000313|EMBL:ACK87173.1, ECO:0000313|Proteomes:UP000001363}; RN [1] {ECO:0000313|EMBL:ACK87173.1, ECO:0000313|Proteomes:UP000001363} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AH820 {ECO:0000313|EMBL:ACK87173.1, RC ECO:0000313|Proteomes:UP000001363}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001283; ACK87173.1; -; Genomic_DNA. DR RefSeq; WP_000649714.1; NC_011773.1. DR RefSeq; YP_002453224.1; NC_011773.1. DR STRING; 405535.BCAH820_4274; -. DR EnsemblBacteria; ACK87173; ACK87173; BCAH820_4274. DR KEGG; bcu:BCAH820_4274; -. DR PATRIC; 18845522; VBIBacCer122868_4269. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; BCER405535:GHSL-4287-MONOMER; -. DR Proteomes; UP000001363; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001363}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACK87173.1}; KW Transferase {ECO:0000313|EMBL:ACK87173.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 125942 MW; CFD6E26EBD6CBE3C CRC64; MKCIEEKLQN NILLLDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYELSHLDE ELNEKAARLA KQAVKESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGE VDVLLVETSQ DMRNVKAAYI GIQAAFDELK KIVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWVN IIGGCCGTTP EHIKAMKEAL ASLKPREHHE REGHGVSGLE ALQYDDSMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMENF LAEVTKVLKV PIMIDSTDEH VMERALTYIQ GKAVINSINL EDGEERFIKV TPLLQKYGAA IVVGTIDEDG MAVSAERKLE IAKRSYELLT TKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPDE EKRLADALLF ETTQETLEEF TNFYRVAKKK DVVVQETLTL DERLANYIVE GTKQGLHEDL SLALTEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILA NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAADIDIPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV TKEEKKIEIP AVIEPLPKSE VMVPDSTKRI VLRDVPALHL APFLNRQMLL GHHLGLKGSV KKLLKEGDKR AHELNDLIDE LLQEGQSWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRVIE RFTFPRQGRA PYRTLGDYLR PIGDEMDYVA FLSVTVGEGV RGIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID B7JMX9_BACC0 Unreviewed; 610 AA. AC B7JMX9; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 27-MAY-2015, entry version 45. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=BCAH820_4275 {ECO:0000313|EMBL:ACK88483.1}; OS Bacillus cereus (strain AH820). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=405535 {ECO:0000313|EMBL:ACK88483.1, ECO:0000313|Proteomes:UP000001363}; RN [1] {ECO:0000313|EMBL:ACK88483.1, ECO:0000313|Proteomes:UP000001363} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AH820 {ECO:0000313|EMBL:ACK88483.1, RC ECO:0000313|Proteomes:UP000001363}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ACK88483.1; -; Genomic_DNA. DR RefSeq; WP_000770329.1; NC_011773.1. DR RefSeq; YP_002453225.1; NC_011773.1. DR ProteinModelPortal; B7JMX9; -. DR STRING; 405535.BCAH820_4275; -. DR EnsemblBacteria; ACK88483; ACK88483; BCAH820_4275. DR KEGG; bcu:BCAH820_4275; -. DR PATRIC; 18845524; VBIBacCer122868_4270. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; BCER405535:GHSL-4288-MONOMER; -. DR Proteomes; UP000001363; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001363}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ACK88483.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:ACK88483.1}. SQ SEQUENCE 610 AA; 67289 MW; 3E0571E319652DAE CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNISDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTE INRAAVKLAK ASVTDRNAIL GTIGGMKHIG AVTTTDMERE FMLLEQASAL LEEQVDGLLL ETFYDEFELL HAVQVLRKET NIPIVAQLAL HEAGTTQNGN DVNEILKQLL DYGANVVGLN CQLGPLHMTE AFKMISIPKN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPKFIEQGI RLLGGCCGTT PEHIESMKRA TLNVTPVIEK DTIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRISNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KAMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIA LIEEVYEATK HLEQPIFIGI MPLISKRNAD FLHFEVPGIT LPEAVRERMD GHETKEAAIE EGIRISQELI DETMKYFYGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID B7K3W4_CYAP8 Unreviewed; 1191 AA. AC B7K3W4; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 27-MAY-2015, entry version 53. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACK66504.1}; GN OrderedLocusNames=PCC8801_2495 {ECO:0000313|EMBL:ACK66504.1}; 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 {ECO:0000313|EMBL:ACK66504.1, ECO:0000313|Proteomes:UP000008204}; RN [1] {ECO:0000313|Proteomes:UP000008204} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 8801 {ECO:0000313|Proteomes:UP000008204}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001287; ACK66504.1; -; Genomic_DNA. DR RefSeq; WP_012595771.1; NC_011726.1. DR RefSeq; YP_002372660.1; NC_011726.1. DR ProteinModelPortal; B7K3W4; -. DR STRING; 41431.PCC8801_2495; -. DR EnsemblBacteria; ACK66504; ACK66504; PCC8801_2495. DR KEGG; cyp:PCC8801_2495; -. DR PATRIC; 21577291; VBICyaSp125535_2665. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CSP41431:GHLK-2520-MONOMER; -. DR Proteomes; UP000008204; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008204}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008204}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 228 228 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 737 737 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1191 AA; 132642 MW; 73CE08DA00A3F6B6 CRC64; MNSTFLNYLN SPKRPVLVFD GATGTSLQTQ NLTAEDFGGP EYEGCNEYLV HTKPEAVEKV HRGFLEVGAD VIETDTFGGT SIVLAEYDLA DKAYYLNKKA TEIAKRLAQD YSTPEKPRFV AGSMGPGTKL PTLGHIDFDT LKNAYVEQAE GLYDGGADLF IIETCQDVLQ IKAALNAVEE VFEKKGNRIP IMVSITMETM GTMLVGTEIS AALAILEPYN IDILGLNCAT GPEQMKEHIK YLSEHSPFIV SCIPNAGLPE NIGGKAHYRL TPVELKMALM HFIEDLGVQI IGGCCGTRPD HIKALAELSQ GLTPKERHPI YEPSAASIYS TQPYIQDNSF LIVGERLNAS GSKKCRDLLN VEDWDSLVSL AKSQVKEGAH ILDVNVDYVG RDGVQDMHEL ASRLVNNVTL PLMLDSTEWQ KMEAGLKVAG GKCILNSTNY EDGEERFLKV LDLAKKYGAG VVVGTIDEEG MGRTADKKFE IAKRAYNAAI DYGIPPHEIF FDPLALPIST GIEEDRENGK ATIESIRRIR EELPGCHILL GISNISFGLN AAARQVLNSV FLYEAMQVGL DGAIVSASKI LPLAKIEPEY QEICRDLIYD NRRFEGDICV YDPLTKLTEV FAGKTTKKDA SQTANLSLEE RLKQHIIDGE RLGLEDTLAE ALKQHPPLDI INIFLLDGMK VVGELFGSGQ MQLPFVLQSA QTMKAAVAYL EPFMDKADSD GSGKGTFIIA TVKGDVHDIG KNLVDIILSN NGYKVINLGI KQPVENIIQA YQEHKADCIA MSGLLVKSTA FMKDNLEVFN ERGITVPVIL GGAALTPKFV YEDCQNTYKG KVVYGKDAFS DLHFMDKLMP AKSTNSWDDL QGFLGDFNDN NSVFQEERAE KAAAKISEKN GKSATSETPK VVDTKRSEAV ELIEPATPPF WGTKLLKPQE FDLTEIFWYL DLQALIAGQW QFRKPQEQSR EEYEQFLAEK VYPILEEWKQ KVITDNLLHP TVIYGYFPCQ SQGNSLLVYD PEIVQNNNNK IPETIDPIWV IDFPRQKSGR RLCIADFFAP KESGLTDVFP MQAVTVGEIA TEYAQKLFAS NDYTNYLYYH GMAVQTAEAL AEWTHAKIRR ELGFGDKEPD NIREMLQQHY QGSRYSFGYP ACPNIQDQYK QLEILGCDRI NMYMDESEQI YPEQSTTAII TYHPVAKYFN A // ID B7KCS9_CYAP7 Unreviewed; 1183 AA. AC B7KCS9; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 01-APR-2015, entry version 50. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACK71630.1}; GN OrderedLocusNames=PCC7424_3230 {ECO:0000313|EMBL:ACK71630.1}; OS Cyanothece sp. (strain PCC 7424) (Synechococcus sp. (strain ATCC OS 29155)). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Cyanothece. OX NCBI_TaxID=65393 {ECO:0000313|EMBL:ACK71630.1, ECO:0000313|Proteomes:UP000002384}; RN [1] {ECO:0000313|Proteomes:UP000002384} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7424 {ECO:0000313|Proteomes:UP000002384}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001291; ACK71630.1; -; Genomic_DNA. DR RefSeq; WP_015955227.1; NC_011729.1. DR RefSeq; YP_002378498.1; NC_011729.1. DR STRING; 65393.PCC7424_3230; -. DR EnsemblBacteria; ACK71630; ACK71630; PCC7424_3230. DR KEGG; cyc:PCC7424_3230; -. DR PATRIC; 21555424; VBICyaSp136448_3318. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CSP65393:GJP7-3269-MONOMER; -. DR Proteomes; UP000002384; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002384}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002384}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 228 228 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 737 737 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1183 AA; 132334 MW; 95E77E6BFDFEE58A CRC64; MNSPFLNRLH SPERPVLVFD GAMGTSLQTQ NLTAEDFGGL QYEGCNEYLV HTKPEAVEKV HRGYLEAGAD VIETDTFGGT SIVLAEYDLA DKAYYLNKTA AQLAKRVAQE YSTPQKPRFV AGSMGPGTKL PTLGHIDFDT LKNAYIEQAE GLYDGGADLF IVETCQDVLQ IKAALNAIEE VFQKKGNRIP IMVSITMEVM GTMLIGTEIG AALTILEPYN IDILGLNCAT GPDQMKEHIK YLSENSPFII SCIPNAGLPE NVGGQAHYRL TPLELRMALM HFVEDLGVQI IGGCCGTRAD HIKALAEITK DLKPKERHPH YEPSAASIYS PQPYIQDNSF LIVGERLNAS GSKKCRELLN KEDWDSLVSM AKSQVKEGAH ILDVNVDYVG RDGVKDMKEL ASRLVNNVTL PLMLDSTEWE KMEAGLKVVG GKCILNSTNY EDGEPRFYQV LDLAKKYGAG VVVGTIDEEG MARTAEKKFA IAKRAYEAAV NYGLPPEEIF FDPLALPIST GIEEDRNNGK ATIEAIKRIR DELPKCHILL GVSNISFGLN PAARQVLNSV FLHECMGVGL DSAIVSASKI LPLAKIDPEH QEICRDLIYD RRRFEGDVCV YDPLTKLTEV FAGKTTKKTA SDKASLPIEE RLKQHIIDGE RIGLDDALAE ALKQYPPLEI INTFLLDGMK VVGELFGSGQ MQLPFVLQSA QTMKAAVAYL EPFMEKEEGN GNTKGKFIIA TVKGDVHDIG KNLVDIILSN NGYTVINLGI KQPVENIIQA YQEHQADCIA MSGLLVKSTA FMKENLEVFN ERGITVPVIL GGAALTPKFV HEDCQNTYKG QVIYGKDAFS DLHFMDKLMP AKVEGKWDDL KGFLDESADE RRLTRMVESV RVIDKDDEDG KISEPVIIDT RRSDEVSIDI DRPIPPFWGT KILTPDEIVL DEVFKYLDLQ ALFVGQWQFR KPKDQSREEY DQFLTDTVHP ILQGWKQRIL EEKLLHPTVI YGYFPCQSEG NSLLVYDPEI WQQSEKLDLI WTLDFPRQKS NRRLCIADFF APKESGMIDV FPMQAVTVGE IATEFAKTLF DGNQYTDYLY YHGMAVQTAE ALAEWTHVKI RQELGFGDKE PDTIRDILQQ RYQGSRYSFG YPACPNIQDQ YKQLELLGCD RISMYMDDSE QIYPEQSTTA IIAYHPVAKY FST // ID B7KV74_METC4 Unreviewed; 1250 AA. AC B7KV74; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 29-APR-2015, entry version 49. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACK82745.1}; GN OrderedLocusNames=Mchl_1882 {ECO:0000313|EMBL:ACK82745.1}; OS Methylobacterium extorquens (strain CM4 / NCIMB 13688) OS (Methylobacterium chloromethanicum). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=440085 {ECO:0000313|EMBL:ACK82745.1, ECO:0000313|Proteomes:UP000002385}; RN [1] {ECO:0000313|Proteomes:UP000002385} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CM4 / NCIMB 13688 {ECO:0000313|Proteomes:UP000002385}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001298; ACK82745.1; -; Genomic_DNA. DR RefSeq; WP_015950502.1; NC_011757.1. DR RefSeq; YP_002420673.1; NC_011757.1. DR ProteinModelPortal; B7KV74; -. DR SMR; B7KV74; 660-909. DR STRING; 440085.Mchl_1882; -. DR EnsemblBacteria; ACK82745; ACK82745; Mchl_1882. DR KEGG; mch:Mchl_1882; -. DR PATRIC; 22497954; VBIMetChl132133_1816. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; MCHL440085:GCXT-1928-MONOMER; -. DR Proteomes; UP000002385; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002385}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 254 254 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 318 318 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 771 771 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1250 AA; 137107 MW; C6368FCE736855FA CRC64; MTAFPPVDGT EIERALRQRA SEKILVLDGA MGTVIQRLKY TEEDFRGERF KDHSHDQKGN NDLLILTQPD AIRQIHLDYF LAGADVCETN TFSGTTIAQA DYGMESIIHE LNAEGARLAR EAAKLAEEQD GRRRFVAGAI GPTNRTLSIS PDVNNPGYRA VTFDGVKQAY VEQVRGLIDG GAELILIETI FDTLNAKAAI AAAWQVFDET GIRLPIQISG TITDLSGRTL SGQTPAAFWN SLRHSSPLTF GLNCALGAKE MRGHIAELSR ICDTLVCAYP NAGLPNEFGL YDESPEAMGK LVGEFAASGL VNMVGGCCGT TPDHIRAIAE AVADKKPREI PEIPRLMRLS GLEPFVLTKE IPFVNVGERT NVTGSAKFRK LITNNDYAAA LDVARDQVAA GAQVIDVNMD EGLLDSEKAM VEFLNLVAAE PDIARVPVMV DSSKFEVIEA GLKCIQGKPI VNSISMKEGE AKFIEAAKIC RSYGAAVVVM AFDEQGQADS YERKVEICTK AYKILTEQVG FPPEDIIFDP NIFAVATGIE EHNPYGVAFI EATRTIRETL PHAHISGGVS NLSFAFRGNE PVREAMHAVF LFHCIKAGMD MGIVNAGQLA VYDEIPAELR ELCEDVVLNR REDSTERLLE AAERFKTGAS AQAKTADLTW REAPVAKRIE HALVNGITEY IVSDTEEARK EAARPLHVIE GPLMAGMNVV GDLFGSGKMF LPQVVKSARV MKQAVAYLEP FMEEEKRANG GDGKRQAAGK VLMATVKGDV HDIGKNIVGV VLACNNYEII DLGVMVPAAK ILETAKRENV DIVGLSGLIT PSLDEMVHVA AEMEREGMEM PLLIGGATTS RVHTAVKIHP AYAKGQAVYV TDASRAVGVV SSLISKETRG ATVEKVRAEY AKVADAHRRS EADKQRLPLA KARANAFKVD WSAYKPAKPS FTGTRVYGSY EVADLVPYID WTPFLQTYEF KGRYPAILDD PEQGPAARAL FEDAQVMLKQ IVEERWFNPK AVIGFWPANS VGDDIRLFTG ESRQETLATF HGLRQQLSKR DGRANTCISD FVAPAETGIA DYVGAFVVTA GLEEVRIAER FERANDDYRS ILVKALADRI AEAFAERMHE RVRKEFWGYA PDEAYAPEEL VSEKYDGIRP APGYPAQPDH TEKVQLFDLL KAESRIGVKL TESYAMWPGS SVSGLYLAHP DAHYFGVAKV ERDQVEDYAL RKGMDVSEVE RWLGPILNYD PVRYLKAAAE // ID B7L1F1_METC4 Unreviewed; 312 AA. AC B7L1F1; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 27-MAY-2015, entry version 34. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACK81045.1}; GN OrderedLocusNames=Mchl_0089 {ECO:0000313|EMBL:ACK81045.1}; OS Methylobacterium extorquens (strain CM4 / NCIMB 13688) OS (Methylobacterium chloromethanicum). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=440085 {ECO:0000313|EMBL:ACK81045.1, ECO:0000313|Proteomes:UP000002385}; RN [1] {ECO:0000313|Proteomes:UP000002385} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CM4 / NCIMB 13688 {ECO:0000313|Proteomes:UP000002385}; 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; ACK81045.1; -; Genomic_DNA. DR RefSeq; WP_012605259.1; NC_011757.1. DR RefSeq; YP_002418973.1; NC_011757.1. DR ProteinModelPortal; B7L1F1; -. DR STRING; 440085.Mchl_0089; -. DR EnsemblBacteria; ACK81045; ACK81045; Mchl_0089. DR KEGG; mch:Mchl_0089; -. DR eggNOG; COG2040; -. DR HOGENOM; HOG000179103; -. DR OMA; CCGTDHR; -. DR OrthoDB; EOG6R5C46; -. DR BioCyc; MCHL440085:GCXT-91-MONOMER; -. DR Proteomes; UP000002385; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002385}; KW Methyltransferase {ECO:0000313|EMBL:ACK81045.1}; KW Transferase {ECO:0000313|EMBL:ACK81045.1}. SQ SEQUENCE 312 AA; 33669 MW; 92B7FA37248E421B CRC64; MPRYRTALPQ LDGHVFLTDG GLETTLVFHE GLELTCFAAF PLVCTEEGRD KLTHYFQPYL DLAEERQLGF ILDTPTWRAN PDWGAQLGFT GQALTDVSRA AVTYLEGLRR RHAHSGLPIV LNGVIGPRGD GYKIETSLTA AEAATYHGPQ IQAFRDTEAD MVSAITMTSV EEAIGIAWAA QTAGMPVVIS FTVETNGRLP SGQALGSAIE EADGTTGAYP AYYMINCAHP THFKAVLVGN APWLNRIRGL RANASAKSHA ELDVASELDI GDPQELGLHY ADLCARLRSL KILGGCCGTD RRHVAAICDA CL // ID B7LAW1_ECO55 Unreviewed; 1227 AA. AC B7LAW1; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 27-MAY-2015, entry version 51. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CAV01276.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAV01276.1}; GN Name=metH {ECO:0000313|EMBL:CAV01276.1}; GN OrderedLocusNames=EC55989_4504 {ECO:0000313|EMBL:CAV01276.1}; OS Escherichia coli (strain 55989 / EAEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=585055 {ECO:0000313|EMBL:CAV01276.1, ECO:0000313|Proteomes:UP000000746}; RN [1] {ECO:0000313|Proteomes:UP000000746} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=55989 / EAEC {ECO:0000313|Proteomes:UP000000746}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CU928145; CAV01276.1; -; Genomic_DNA. DR RefSeq; WP_000096011.1; NC_011748.1. DR ProteinModelPortal; B7LAW1; -. DR SMR; B7LAW1; 6-639, 651-1227. DR STRING; 585055.EC55989_4504; -. DR PRIDE; B7LAW1; -. DR EnsemblBacteria; CAV01276; CAV01276; EC55989_4504. DR KEGG; eck:EC55989_4504; -. DR PATRIC; 38482600; VBIEscCol113220_4531. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; ECOL585055:GJOM-4577-MONOMER; -. DR Proteomes; UP000000746; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000746}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAV01276.1}; KW Transferase {ECO:0000313|EMBL:CAV01276.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135997 MW; 91F0CAA1E9127D9A CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAD // ID B7LKA7_ESCF3 Unreviewed; 1227 AA. AC B7LKA7; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 27-MAY-2015, entry version 46. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CAQ91495.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAQ91495.1}; GN Name=metH {ECO:0000313|EMBL:CAQ91495.1}; GN OrderedLocusNames=EFER_4072 {ECO:0000313|EMBL:CAQ91495.1}; OS Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CDC 0568-73). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=585054 {ECO:0000313|EMBL:CAQ91495.1, ECO:0000313|Proteomes:UP000000745}; RN [1] {ECO:0000313|Proteomes:UP000000745} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35469 / DSM 13698 / CDC 0568-73 RC {ECO:0000313|Proteomes:UP000000745}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CU928158; CAQ91495.1; -; Genomic_DNA. DR RefSeq; WP_000096028.1; NC_011740.1. DR STRING; 585054.EFER_4072; -. DR EnsemblBacteria; CAQ91495; CAQ91495; EFER_4072. DR KEGG; efe:EFER_4072; -. DR PATRIC; 32132446; VBIEscFer122920_3908. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; EFER585054:GJJM-4063-MONOMER; -. DR Proteomes; UP000000745; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000745}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAQ91495.1}; KW Transferase {ECO:0000313|EMBL:CAQ91495.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136071 MW; DC5BFD60C9C8A4B5 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG EEAKRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAE // ID B7MJ00_ECO45 Unreviewed; 1227 AA. AC B7MJ00; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 27-MAY-2015, entry version 46. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CAR05644.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAR05644.1}; GN Name=metH {ECO:0000313|EMBL:CAR05644.1}; GN OrderedLocusNames=ECS88_4483 {ECO:0000313|EMBL:CAR05644.1}; OS Escherichia coli O45:K1 (strain S88 / ExPEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=585035 {ECO:0000313|EMBL:CAR05644.1, ECO:0000313|Proteomes:UP000000747}; RN [1] {ECO:0000313|Proteomes:UP000000747} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S88 / ExPEC {ECO:0000313|Proteomes:UP000000747}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CU928161; CAR05644.1; -; Genomic_DNA. DR RefSeq; WP_000096024.1; NC_011742.1. DR STRING; 585035.ECS88_4483; -. DR EnsemblBacteria; CAR05644; CAR05644; ECS88_4483. DR KEGG; ecz:ECS88_4483; -. DR PATRIC; 18416645; VBIEscCol91599_4384. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; ECOL585035:GJWP-4456-MONOMER; -. DR Proteomes; UP000000747; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000747}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAR05644.1}; KW Transferase {ECO:0000313|EMBL:CAR05644.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136133 MW; 7EFEC4A33E7961FE CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTSEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPAEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPT ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANTQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KMLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAE // ID B7N2L7_ECO81 Unreviewed; 1227 AA. AC B7N2L7; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 27-MAY-2015, entry version 49. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CAR10686.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAR10686.1}; GN Name=metH {ECO:0000313|EMBL:CAR10686.1}; GN OrderedLocusNames=ECED1_4725 {ECO:0000313|EMBL:CAR10686.1}; OS Escherichia coli O81 (strain ED1a). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=585397 {ECO:0000313|EMBL:CAR10686.1, ECO:0000313|Proteomes:UP000000748}; RN [1] {ECO:0000313|Proteomes:UP000000748} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ED1a {ECO:0000313|Proteomes:UP000000748}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CU928162; CAR10686.1; -; Genomic_DNA. DR RefSeq; WP_000096035.1; NC_011745.1. DR ProteinModelPortal; B7N2L7; -. DR SMR; B7N2L7; 651-1227. DR STRING; 585397.ECED1_4725; -. DR EnsemblBacteria; CAR10686; CAR10686; ECED1_4725. DR KEGG; ecq:ECED1_4725; -. DR PATRIC; 38493550; VBIEscCol8292_4709. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; ECOL585397:GJCU-4772-MONOMER; -. DR Proteomes; UP000000748; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000748}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAR10686.1}; KW Transferase {ECO:0000313|EMBL:CAR10686.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136133 MW; D6BA2CF6A156F516 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPAEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPT ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANTQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KMLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK VSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAE // ID B7NFV5_ECOLU Unreviewed; 1227 AA. AC B7NFV5; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 27-MAY-2015, entry version 46. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CAR15662.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAR15662.1}; GN Name=metH {ECO:0000313|EMBL:CAR15662.1}; GN OrderedLocusNames=ECUMN_4545 {ECO:0000313|EMBL:CAR15662.1}; OS Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=585056 {ECO:0000313|EMBL:CAR15662.1, ECO:0000313|Proteomes:UP000007097}; RN [1] {ECO:0000313|Proteomes:UP000007097} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UMN026 / ExPEC {ECO:0000313|Proteomes:UP000007097}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CU928163; CAR15662.1; -; Genomic_DNA. DR RefSeq; WP_000096036.1; NC_011751.1. DR RefSeq; YP_002415152.1; NC_011751.1. DR STRING; 585056.ECUMN_4545; -. DR EnsemblBacteria; CAR15662; CAR15662; ECUMN_4545. DR GeneID; 7156786; -. DR KEGG; eum:ECUMN_4545; -. DR PATRIC; 18448439; VBIEscCol32010_4709. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR Proteomes; UP000007097; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007097}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAR15662.1}; KW Transferase {ECO:0000313|EMBL:CAR15662.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136053 MW; 84615BFEF095AB25 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARLQAERPI QVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID B7P2U0_IXOSC Unreviewed; 381 AA. AC B7P2U0; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 27-MAY-2015, entry version 39. DE SubName: Full=Homocysteine S-methyltransferase, putative {ECO:0000313|EMBL:EEC00912.1}; DE EC=2.1.1.5 {ECO:0000313|EMBL:EEC00912.1}; GN ORFNames=IscW_ISCW001818 {ECO:0000313|EMBL:EEC00912.1}; OS Ixodes scapularis (Black-legged tick) (Deer tick). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; OC Acari; Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes. OX NCBI_TaxID=6945 {ECO:0000313|Proteomes:UP000001555}; RN [1] {ECO:0000313|EMBL:EEC00912.1, ECO:0000313|Proteomes:UP000001555} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Wikel {ECO:0000313|Proteomes:UP000001555}; RG Ixodes scapularis Genome Project Consortium; RA Caler E., Hannick L.I., Bidwell S., Joardar V., Thiagarajan M., RA Amedeo P., Galinsky K.J., Schobel S., Inman J., Hostetler J., RA Miller J., Hammond M., Megy K., Lawson D., Kodira C., Sutton G., RA Meyer J., Hill C.A., Birren B., Nene V., Collins F., RA Alarcon-Chaidez F., Wikel S., Strausberg R.; RT "Annotation of Ixodes scapularis."; 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; DS624571; EEC00912.1; -; Genomic_DNA. DR RefSeq; XP_002403007.1; XM_002402963.1. DR UniGene; Isc.4340; -. DR STRING; 6945.ISCW001818-PA; -. DR EnsemblMetazoa; ISCW001818-RA; ISCW001818-PA; ISCW001818. DR GeneID; 8023777; -. DR KEGG; isc:IscW_ISCW001818; -. DR VectorBase; ISCW001818; Ixodes scapularis. DR CTD; 8023777; -. DR eggNOG; COG0646; -. DR InParanoid; B7P2U0; -. DR KO; K00544; -. DR OMA; WGVTKGT; -. DR OrthoDB; EOG79GT7C; -. DR PhylomeDB; B7P2U0; -. DR Proteomes; UP000001555; Unassembled WGS sequence. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 2. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001555}; KW Methyltransferase {ECO:0000313|EMBL:EEC00912.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001555}; KW Transferase {ECO:0000313|EMBL:EEC00912.1}. SQ SEQUENCE 381 AA; 42470 MW; 1763A3C0C2B95593 CRC64; MPGKGLLERL DSGVVLGDGG FVFALEKRGY VKAGPWTPEA CVEHPEAVRQ LHREFLRAGA DVMQAFTFYA SDDKLINRGN EAGRSFSGAE INTAACKLAR EVALEQDALV AGGISQTPSY LSGCTKEEIQ AEFKKQIDVF VANKMDFLIC EYFEHVEEME MAIEVCKKTG LPTVASLCIG PEGDMHGVSA GQCAVRMVKA GGCPRHTASI HRCRERIPLG VRFKKEQFFL QQKINHGLSR CHLLSAALEP RVCSRWDIQR YAREAYEMGV RYIGGCCGFE PYHVRAMAEE LSPERGGALP KGSEKHDLWG EGLRMHTKPW VRARAYRNYW ENLKPSTGRP FSSSFSQPDN WGVTAGANEL KQQAEATTKE EISKLKEFKK E // ID B7Q2S9_IXOSC Unreviewed; 185 AA. AC B7Q2S9; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 07-JAN-2015, entry version 32. DE SubName: Full=5-methyltetrahydrofolate:homocysteine methyltransferase, putative {ECO:0000313|EMBL:EEC13151.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EEC13151.1}; GN ORFNames=IscW_ISCW020738 {ECO:0000313|EMBL:EEC13151.1}; OS Ixodes scapularis (Black-legged tick) (Deer tick). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; OC Acari; Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes. OX NCBI_TaxID=6945 {ECO:0000313|Proteomes:UP000001555}; RN [1] {ECO:0000313|EMBL:EEC13151.1, ECO:0000313|Proteomes:UP000001555} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Wikel {ECO:0000313|Proteomes:UP000001555}; RG Ixodes scapularis Genome Project Consortium; RA Caler E., Hannick L.I., Bidwell S., Joardar V., Thiagarajan M., RA Amedeo P., Galinsky K.J., Schobel S., Inman J., Hostetler J., RA Miller J., Hammond M., Megy K., Lawson D., Kodira C., Sutton G., RA Meyer J., Hill C.A., Birren B., Nene V., Collins F., RA Alarcon-Chaidez F., Wikel S., Strausberg R.; RT "Annotation of Ixodes scapularis."; 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; DS845271; EEC13151.1; -; Genomic_DNA. DR RefSeq; XP_002410979.1; XM_002410934.1. DR STRING; 6945.ISCW020738-PA; -. DR EnsemblMetazoa; ISCW020738-RA; ISCW020738-PA; ISCW020738. DR GeneID; 8035042; -. DR KEGG; isc:IscW_ISCW020738; -. DR VectorBase; ISCW020738; Ixodes scapularis. DR CTD; 8035042; -. DR eggNOG; COG2040; -. DR InParanoid; B7Q2S9; -. DR KO; K00547; -. DR OrthoDB; EOG7GQXW0; -. DR PhylomeDB; B7Q2S9; -. DR Proteomes; UP000001555; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001555}; KW Methyltransferase {ECO:0000313|EMBL:EEC13151.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001555}; KW Transferase {ECO:0000313|EMBL:EEC13151.1}. SQ SEQUENCE 185 AA; 20276 MW; 4D71E7A626149342 CRC64; MQPTSAFAGS VGSYGAYPYD GSEYTGSYAD TMSVKELCDW HRFRVQHLVR LGCDLLAFET IPALQEALAL LQLLREHPGT KGWLSFGCQD EKLTAKGECL QKAIQAVLGK DSGSQICAIR VNCCRPDMVG LLLKDARKEG QPPLVAYADA EVASWTLVPK DSDQLGNYVA EWYRAGVRPS QAMNI // ID B7QTR8_9RHOB Unreviewed; 340 AA. AC B7QTR8; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 01-OCT-2014, entry version 18. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEB71393.1}; GN ORFNames=RR11_2153 {ECO:0000313|EMBL:EEB71393.1}; OS Ruegeria sp. R11. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Ruegeria. OX NCBI_TaxID=439497 {ECO:0000313|EMBL:EEB71393.1}; RN [1] {ECO:0000313|EMBL:EEB71393.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=R11 {ECO:0000313|EMBL:EEB71393.1}; 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; EEB71393.1; -; Genomic_DNA. DR RefSeq; WP_008561333.1; NZ_DS999054.1. DR ProteinModelPortal; B7QTR8; -. DR EnsemblBacteria; EEB71393; EEB71393; RR11_2153. DR PATRIC; 29768907; VBIRueSp9964_2865. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEB71393.1}; KW Transferase {ECO:0000313|EMBL:EEB71393.1}. SQ SEQUENCE 340 AA; 36003 MW; 23D6920F5D801762 CRC64; MTNTFITLLE SKDALLADGA TGTNLFNMGL QSGDAPELWN VDEPKKIEAL YQGSVDAGSD LFLTNTFGGT AARLKLHDAQ RRVRELNMAG AELGRNVADR AERKIAVAGS VGPTGEIMEP VGELSHALAV EMFHEQAEAL KEGGVDVLWL ETISAPEEFR AAAEAFKLAD MPWCGTMSFD TAGRTMMGVT SADMAKLVED FDPAPLAYGA NCGTGASDIL RTVLGFAAQG TTRPIISKGN AGIPKYVDGH IHYDGTPELM GEYAAMARDC GAKIIGGCCG TMPEHLRAMR EALDTRSRGD APTLDQIVSV LGPFSSDSDG TGDDASAGGE RRRGRGRRRA // ID B7RA13_9THEO Unreviewed; 803 AA. AC B7RA13; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Homocysteine S-methyltransferase domain protein {ECO:0000313|EMBL:EEB75245.1}; GN ORFNames=CDSM653_520 {ECO:0000313|EMBL:EEB75245.1}; OS Caldanaerobacter subterraneus subsp. pacificus DSM 12653. OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Caldanaerobacter. OX NCBI_TaxID=391606 {ECO:0000313|EMBL:EEB75245.1}; RN [1] {ECO:0000313|EMBL:EEB75245.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 12653 {ECO:0000313|EMBL:EEB75245.1}; 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999137; EEB75245.1; -; Genomic_DNA. DR RefSeq; WP_009611154.1; NZ_DS999137.1. DR EnsemblBacteria; EEB75245; EEB75245; CDSM653_520. DR PATRIC; 30386819; VBICarPac114674_2115. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEB75245.1}; KW Transferase {ECO:0000313|EMBL:EEB75245.1}. SQ SEQUENCE 803 AA; 87513 MW; E9CEADF93CE6D845 CRC64; MVDIFKECEN RVVVFDGAMG TQLQERGLKA GECPEYINLK MPEVVFDIHK AYIEAGAEVI ETNTFGANRI KLAKYGLEDK VEEIVTKGVE IARKAAGDRP VALSVGPTGE LLAPFGDMTF DEAYEVFKEV VVAAEKAGAD IVIIETMSDM LEAKAAILAA KENTNMKVIC TMTFQEDGRT LMGSDPVTVV VSLQGLGLDA IGVNCSTGPD KMVKVVEKMA QVARIPIIAQ PNAGMPVIRD GKTVYDLKPE EFASFFPQLV EKGACIVGGC CGTTPYYIKL VKKAVENLKP KKLENKFTAL SSNTRTVFIG KEYPLRVIGE RINPTGKKKL SGALLSGDVN LAVEEALKQQ KCGAEILDVN VGVPGIEEEE MLPKVAFEVE KAVDLPLQLD STNVKAIEKA IRILRGRPII NSVNAKEESL KEVLPIVKKY GACVVGLTVG DKGLPKDRHE RVENARKILK KAEEYGIPKE DVIIDPVVLT VSSEQGAAIE TLEAMKIISE ELGVNTVVGL SNISFGLPER KLINSTFLAM AASHGLTAAI VNPCDESLMD TLRASMVLLN KDKGSENYLK VYGQRVKPKE EVIKRHEEDF SKKLYDQILE GKKSGVEEIV MALLEDNPPL SLVDEIIIPA LKEVGDRYEK GIYFLPQLLS SAEVVQSAFK LIKEKLPKGT ASKGKIILAT VEGDVHDIGK NIVKVLLENY GYEVIDLGKD VKGEVIVEEV KKTGAPLVGL SALMTTTLFN MEKIIKMLTE NTEAKVMVGG AVLTEEYAFK IGVDYYGKTA QDAVKIADKF FLKNALVCKT CSF // ID B7RLM6_9RHOB Unreviewed; 296 AA. AC B7RLM6; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 01-APR-2015, entry version 17. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEB86535.1}; GN ORFNames=RGAI101_3692 {ECO:0000313|EMBL:EEB86535.1}; OS Roseobacter sp. GAI101. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseobacter. OX NCBI_TaxID=391589 {ECO:0000313|EMBL:EEB86535.1}; RN [1] {ECO:0000313|EMBL:EEB86535.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=GAI101 {ECO:0000313|EMBL:EEB86535.1}; 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; EEB86535.1; -; Genomic_DNA. DR RefSeq; WP_008229450.1; NZ_DS999213.1. DR EnsemblBacteria; EEB86535; EEB86535; RGAI101_3692. DR PATRIC; 28104408; VBIRosSp12209_2107. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEB86535.1}; KW Transferase {ECO:0000313|EMBL:EEB86535.1}. SQ SEQUENCE 296 AA; 31322 MW; 377AD5861D45F91A CRC64; MAEITLLDGG MGQELVHRAG DKATPLWGTQ VMIDHPGMVE AVHRDYFAAG ATIATSNTYA IFRDRLDGTP YESQFAELND AAMAEAKAAA ADFEGARVAG AIGPIKASYR PDLHPDFDTA VKIYREKAQM TAPFSDLILC ETVASILHAR SVLDASLETG LPVWLALTVD DQDGTRLRSG EPLADLLPHV DKAAALLVNC SSPEAIAPAL GILKTAGLPF GAYANGFEKI TQEFLGDKPT VDSLNARQDL TPAAYADHVM GWIGQGATIV GGCCEVGPAH IEEIATRLRA AGHTIV // ID B7RQC2_9RHOB Unreviewed; 164 AA. AC B7RQC2; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 04-MAR-2015, entry version 19. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEB85189.1}; GN ORFNames=RGAI101_2340 {ECO:0000313|EMBL:EEB85189.1}; OS Roseobacter sp. GAI101. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseobacter. OX NCBI_TaxID=391589 {ECO:0000313|EMBL:EEB85189.1}; RN [1] {ECO:0000313|EMBL:EEB85189.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=GAI101 {ECO:0000313|EMBL:EEB85189.1}; 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; EEB85189.1; -; Genomic_DNA. DR EnsemblBacteria; EEB85189; EEB85189; RGAI101_2340. DR PATRIC; 28100883; VBIRosSp12209_0260. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEB85189.1}; KW Transferase {ECO:0000313|EMBL:EEB85189.1}. SQ SEQUENCE 164 AA; 17102 MW; 055D6A0543919E10 CRC64; MSFDTAGRTM MGMTSEAMVD MVHALDNMPL AYGANCGTGA SDVLRTVLGF ASKGKSTPIV SKGNAGIPKY VEGHIHYDGT PELMADYAEM ARNCGASIIG GCCGTMPEHL VHMREALDSR PKGDAPTLEQ IVEALGAFSS ASDGTDGEGP VRGPRRGRRG AKPV // ID B7RQC3_9RHOB Unreviewed; 171 AA. AC B7RQC3; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 04-MAR-2015, entry version 18. DE SubName: Full=Methionine synthase I {ECO:0000313|EMBL:EEB84662.1}; GN ORFNames=RGAI101_1812 {ECO:0000313|EMBL:EEB84662.1}; OS Roseobacter sp. GAI101. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseobacter. OX NCBI_TaxID=391589 {ECO:0000313|EMBL:EEB84662.1}; RN [1] {ECO:0000313|EMBL:EEB84662.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=GAI101 {ECO:0000313|EMBL:EEB84662.1}; 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; EEB84662.1; -; Genomic_DNA. DR EnsemblBacteria; EEB84662; EEB84662; RGAI101_1812. DR PATRIC; 28100885; VBIRosSp12209_0261. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 171 AA; 18088 MW; F65D0158CB81BF14 CRC64; MSNPLIDLLA EKGTLLADGA TGTNLFNMGL MSGDAPEMWN TDEPQNIIKL YKGAVESGSD IFLTNSFGAN ASRLKLHGAE KRAHELSRVS AELAREVADQ AGRKVIVAGS VGPTGEIMEP VGPLTHALAV EMFHETADGL KAGGADVGWL ETISAPEEYR AAAERVQTCR P // ID B7RVB9_9GAMM Unreviewed; 1234 AA. AC B7RVB9; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 01-APR-2015, entry version 36. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEB79802.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEB79802.1}; GN Name=metH {ECO:0000313|EMBL:EEB79802.1}; GN ORFNames=GPB2148_3647 {ECO:0000313|EMBL:EEB79802.1}; OS marine gamma proteobacterium HTCC2148. OC Bacteria; Proteobacteria; Gammaproteobacteria; OMG group; OM60 clade. OX NCBI_TaxID=247634 {ECO:0000313|EMBL:EEB79802.1}; RN [1] {ECO:0000313|EMBL:EEB79802.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2148 {ECO:0000313|EMBL:EEB79802.1}; RA Amann R., Fuchs B., Giovannoni S.J., Ferriera S., Johnson J., RA Kravitz S., Beeson K., Sutton G., Rogers Y.-H., Friedman R., RA Frazier M., Venter J.C.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; DS999223; EEB79802.1; -; Genomic_DNA. DR RefSeq; WP_007227838.1; NZ_DS999223.1. DR EnsemblBacteria; EEB79802; EEB79802; GPB2148_3647. DR PATRIC; 30952923; VBIMarGam120175_0986. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEB79802.1}; KW Transferase {ECO:0000313|EMBL:EEB79802.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 254 254 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 318 318 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 766 766 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1234 AA; 136081 MW; CBDCC72547C01C05 CRC64; MSKRRPMSKT SEQHLIQSLQ QRILVIDGAM GTMIQEEGLE EADYRGERLA SHSLDVKGNN DLLCLTRPDI IEKIHLEYLE AGADLIETNS FNATSIGQDD YQLGHLAYEL NLASAKVARK AADAVTARTP DKPRFVAGVL GPTPKTASIS PDVNDPGARS ITFDQLSEVY LEATLALIEG NVDLLLIETV FDALNAKAAI FAVKEAFDKT GIELPIMISV TFPDISGRVL SGQNPEAFYN AIAHANPLIV GSNCGRRYSE IRPFLEELSN VSDCYFSAHL NAGLPNAFGE FDETPEIMHD DFREFAQRGF LNLAGGCCGT TPAHIRAIAD AVADVEPRKL PDIAPACRLS GLEPFNISAD SLFVNIGERC NVTGSAKFKR LILDDDYEAA LEVARIQVED GAQIIDVNMD EGMLDAEKAM VTFLNLIASE PDISRVPIMV DSSKWSAIEA GLKCIPGKPV VNSISLKAGE EEFIEQARLC LRYGAAVVVM AFDEDGQADN LERRKQICKR SYDLLVDKIG FNPRDIIFDP NIFAVATGIE EHNNYAVDFI EGTRYVKQAL PGALVSGGVS NVSFSFRGNN AVREAIHSVF LYHAIKAGMD MGIVNAGQLA VYDDLPDDLR DAVEDVVLNR REDGTERLLD VAEQYRETGG AEGRKEDLSW REQDVSKRIE HALVKGINTY VVEDAEEARL QFDRPIQVIE GPLMDGMNVV GDLFGEGKMF LPQVVKSARV MKQAVAHLQP FIEEEKSGGS SSNGKILMAT VKGDVHDIGK NIVGVVLQCN NFEVIDLGVM VACEEILRVA KEEQVDIIGL SGLITPSLDE MVHVASEMQR LDFHVPLLIG GATTSNAHTA VKIEPQYTND IVAYVPDASR SVSVATQLMN ETKNRFITER REQYKTVRER IANREPKAKR LSYAEAVSRA PQLEWDNYQP PRPSFVGTRV FDEFPLQGLI DTIDWTPFFI TWELAGKFPA ILEDSIVGEQ ATELFLDAQA MLKRIVDEDL LTAKGVIGFW PAARKGSDDV ELFSDESRGE TLATLHHLRQ QTDKPGGKPN LSLADYVAPE GSGIEDYVGG FCVTTGHGVD ELAAQFEADH DDYSSIMLKA LADRLAESFA EHMHRMVRKE LWGYAPQESL DNAELIRERY QGIRPAPGYP ACPDHTEKAT LFKLLDATKN ADVTLSDSYA MSPASSVSGF YYAHPEAKYF AVGKIGKDQV EDIATRKNES FATMERWLRP NLNY // ID B7RXA7_9GAMM Unreviewed; 302 AA. AC B7RXA7; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Homocysteine S-methyltransferase, putative {ECO:0000313|EMBL:EEB78971.1}; GN ORFNames=GPB2148_2179 {ECO:0000313|EMBL:EEB78971.1}; OS marine gamma proteobacterium HTCC2148. OC Bacteria; Proteobacteria; Gammaproteobacteria; OMG group; OM60 clade. OX NCBI_TaxID=247634 {ECO:0000313|EMBL:EEB78971.1}; RN [1] {ECO:0000313|EMBL:EEB78971.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2148 {ECO:0000313|EMBL:EEB78971.1}; RA Amann R., Fuchs B., Giovannoni S.J., Ferriera S., Johnson J., RA Kravitz S., Beeson K., Sutton G., Rogers Y.-H., Friedman R., RA Frazier M., Venter J.C.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999226; EEB78971.1; -; Genomic_DNA. DR RefSeq; WP_007228956.1; NZ_DS999226.1. DR EnsemblBacteria; EEB78971; EEB78971; GPB2148_2179. DR PATRIC; 30954364; VBIMarGam120175_1691. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EEB78971.1}; KW Transferase {ECO:0000313|EMBL:EEB78971.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 214 214 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 302 AA; 32261 MW; 8159794795D215FD CRC64; MLLLGAMENK KMVDITLLDG GMGQELLKRS ANPAHPMWSA KVLLDEPGIV QSAHEDYIKA GADVITLNTY SVTPERLQRD GKPEWFKPLQ AKAIELANAA RASAGKNVRV AGCLPPLRAS YRPDLSPDFE DNLRRYREIV AEQKDHVDLI QCETMASIAE ATAACTAAVE SSLPVWICLT VADDGSHTLR SGENLKDALD ALAGRGAEAV LLNCSIPEAI TANLPILADH GLRFGAYANG FTSIKALEPG GTVDALEART DLTPEKYANH VDAWIDIGAT IVGGCCEVGP AHIAELAARL KS // ID B7T9J4_PIMPR Unreviewed; 78 AA. AC B7T9J4; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 29-OCT-2014, entry version 12. DE SubName: Full=Betaine-homocysteine methyltransferase {ECO:0000313|EMBL:ACJ67890.1}; DE Flags: Fragment; OS Pimephales promelas (Fathead minnow). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Pimephales. OX NCBI_TaxID=90988 {ECO:0000313|EMBL:ACJ67890.1}; RN [1] {ECO:0000313|EMBL:ACJ67890.1} RP NUCLEOTIDE SEQUENCE. RA Martyniuk C.J., Denslow N.D.; RT "Fathead minnow sequencing project."; 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; FJ030935; ACJ67890.1; -; mRNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 2: Evidence at transcript level; KW Methyltransferase {ECO:0000313|EMBL:ACJ67890.1}; KW Transferase {ECO:0000313|EMBL:ACJ67890.1}. FT NON_TER 1 1 {ECO:0000313|EMBL:ACJ67890.1}. FT NON_TER 78 78 {ECO:0000313|EMBL:ACJ67890.1}. SQ SEQUENCE 78 AA; 8688 MW; BE14F8175E920CEF CRC64; LENRGNKLTY TGQQINEAAC DLAREVANQG DALVAGGVSQ TPSYLSCKSQ EEVTKIFKKQ LDVFIKKNVD FLIAEYFE // ID B7UPG9_ECO27 Unreviewed; 1227 AA. AC B7UPG9; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 27-MAY-2015, entry version 47. DE SubName: Full=Homocysteine-N5-methyltetrahydrofolate transmethylase, B12-dependent {ECO:0000313|EMBL:CAS11869.1}; GN Name=metH {ECO:0000313|EMBL:CAS11869.1}; GN OrderedLocusNames=E2348C_4321 {ECO:0000313|EMBL:CAS11869.1}; OS Escherichia coli O127:H6 (strain E2348/69 / EPEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS11869.1, ECO:0000313|Proteomes:UP000008205}; RN [1] {ECO:0000313|EMBL:CAS11869.1, ECO:0000313|Proteomes:UP000008205} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; FM180568; CAS11869.1; -; Genomic_DNA. DR RefSeq; WP_000095940.1; NC_011601.1. DR STRING; 574521.E2348C_4321; -. DR EnsemblBacteria; CAS11869; CAS11869; E2348C_4321. DR KEGG; ecg:E2348C_4321; -. DR PATRIC; 18347932; VBIEscCol90278_4422. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; ECOL574521:GJAO-4499-MONOMER; -. DR Proteomes; UP000008205; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008205}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAS11869.1}; KW Transferase {ECO:0000313|EMBL:CAS11869.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136052 MW; 0CD8269975292F72 CRC64; MSSKVEQLCA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVISAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPAEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPT ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANTQ QAEWRSWVVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KMLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK VSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAE // ID B7VI88_VIBTL Unreviewed; 1225 AA. AC B7VI88; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 27-MAY-2015, entry version 50. DE SubName: Full=Vibrio splendidus LGP32 chromosome 1 {ECO:0000313|EMBL:CAV17325.1}; GN OrderedLocusNames=VS_0315 {ECO:0000313|EMBL:CAV17325.1}; OS Vibrio tasmaniensis (strain LGP32) (Vibrio splendidus (strain Mel32)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=575788 {ECO:0000313|EMBL:CAV17325.1, ECO:0000313|Proteomes:UP000009100}; RN [1] {ECO:0000313|EMBL:CAV17325.1, ECO:0000313|Proteomes:UP000009100} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LGP32 {ECO:0000313|EMBL:CAV17325.1, RC ECO:0000313|Proteomes:UP000009100}; RA Mazel D., Le Roux F.; RT "Vibrio splendidus str. LGP32 complete genome."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; FM954972; CAV17325.1; -; Genomic_DNA. DR RefSeq; WP_012603124.1; NC_011753.2. DR RefSeq; YP_002415977.1; NC_011753.2. DR STRING; 575788.VS_0315; -. DR EnsemblBacteria; CAV17325; CAV17325; VS_0315. DR GeneID; 7159954; -. DR KEGG; vsp:VS_0315; -. DR PATRIC; 20151334; VBIVibSpl48387_1682. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; VSPL575788:GH64-297-MONOMER; -. DR Proteomes; UP000009100; Chromosome 1. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000009100}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000009100}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1225 AA; 136184 MW; DE59E5F2D719812D CRC64; MGSNVRQKID ALLKQRILLI DGGMGTTIQD YKLEEQDYRG ERFADWHSDL KGNNDLLVLT QPKLIKDIHM EYLEAGADIL ETNTFNATTI AMADYDMESL SEEINYAAAK LAREAADEWT VKTPDKPRFV AGVLGPTNRT CSLSPDVNDP GYRNVSFDEL VEAYSESTRA LIKGGSDLIL IETIFDTLNA KACAFAVESV FEEVGIILPV MISGTITDAS GRTLSGQTTE AFYNALRHVK PISFGLNCAL GPDELREYVG EMSRISECHV SAHPNAGLPN AFGEYDLSPE DMAEHVKEWA ESGFLNLIGG CCGTTPEHIR QMAEAVEGVT PRQLPDLPVS CRLSGLEPLT ISKESLFVNV GERTNVTGSA RFKRLIKEEL YDEALSVARE QVENGAQIID INMDEGMLDA EACMVKFLNL CASEPEISKV PVMVDSSKWE VIEAGLKCIQ GKGIVNSISL KEGKEKFVEQ AKLVRRYGAA VIVMAFDEVG QADTRERKVE ICTNAYNILV DEVGFPPEDI IFDPNIFAVA TGIDEHNNYA VDFIEAVGDI KRDLPHAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK NGMDMGIVNA GQLEIYDNVP EDLREAVEDV VLNRRDDSTE RLLDIATEYL ERAVGKVEDK SALEWRTWPV EKRLEHSLVK GITDFIVEDT EEARVNASRP IEVIEGPLMD GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AHLEPFINAT KDVGATNGKI LLATVKGDVH DIGKNIVGVV LQCNNYEIID LGVMVSCEKI LKVAKEENVD IIGLSGLITP SLDEMVHVAK EMERQGFKLP LLIGGATTSK AHTAVKIEQN YSEPVVYVNN ASRAVGVCTS LLSNELKPAF VEKLDIDYDR VRDQHNRKKP RTKPVTLERA RANKVAIDWD AYTPPAPAKP GVHIFNDFDV ATLRQYIDWT PFFMTWSLVG KYPAILNHEE VGEEAKRLFK DANDLLDRVQ KEKLLEARGM CAMFPANSVG DDIEVYTDES RTEVLKVLHN LRQQTEKPKG FNYCLSDYIA PKDSGKADWI GGFAVTGGIG ERELADEYKA NGDDYNAIMI QAVADRLAEA FAEYLHKEVR KDIWGYSPDE ELSNDDLIRE KYQGIRPAPG YPACPEHTEK GTLWELMDVE KAIDMSLTTS YAMWPGASVS GMYFSHPDAR YFAIAQIQQD QVDSYADRKG WNMLEAERWL GPNIN // ID B7VQ49_VIBTL Unreviewed; 301 AA. AC B7VQ49; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 27-MAY-2015, entry version 33. DE SubName: Full=Vibrio splendidus LGP32 chromosome 2 {ECO:0000313|EMBL:CAV25315.1}; GN OrderedLocusNames=VS_II0079 {ECO:0000313|EMBL:CAV25315.1}; OS Vibrio tasmaniensis (strain LGP32) (Vibrio splendidus (strain Mel32)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=575788 {ECO:0000313|EMBL:CAV25315.1, ECO:0000313|Proteomes:UP000009100}; RN [1] {ECO:0000313|EMBL:CAV25315.1, ECO:0000313|Proteomes:UP000009100} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LGP32 {ECO:0000313|EMBL:CAV25315.1, RC ECO:0000313|Proteomes:UP000009100}; RA Mazel D., Le Roux F.; RT "Vibrio splendidus str. LGP32 complete genome."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; CAV25315.1; -; Genomic_DNA. DR RefSeq; WP_012600087.1; NC_011744.2. DR RefSeq; YP_002394681.1; NC_011744.2. DR STRING; 575788.VS_II0079; -. DR EnsemblBacteria; CAV25315; CAV25315; VS_II0079. DR KEGG; vsp:VS_II0079; -. DR PATRIC; 20148030; VBIVibSpl48387_0076. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; PYVDVWL; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; VSPL575788:GH64-3164-MONOMER; -. DR Proteomes; UP000009100; Chromosome 2. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009100}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000009100}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 206 206 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 281 281 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 282 282 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 301 AA; 32746 MW; 2DCA30E4DAE3C8B6 CRC64; MNMKTLTILD GGMGRELKEI GAPFSQPLWS AQALIEAPDF VSQAHQNFVD AGAEILITNS YACVPFHLGE ELFEQRGFEL AALSGELAKA VADNASHTIK VAGAIPPPFG SYRPDLFKVE EAAPIIQTLY DAQDPNIDLW IAETICSLQE FESIHAVLKQ SNKPCYYAFS LEDTKGDSAN IRSGESVTDS IKLACQSNAK GIMFNCSVPE VMDQAIIDAK KVIGELGSDL EIGVYANNFA PISSEHEAND MLQEIRELDG QGYLVYAKRW HALGANIIGG CCGIGPKHIQ ALADWKRHTQ S // ID B7X069_COMTE Unreviewed; 358 AA. AC B7X069; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EED69977.1}; GN ORFNames=CtesDRAFT_PD4925 {ECO:0000313|EMBL:EED69977.1}; OS Comamonas testosteroni KF-1. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Comamonas. OX NCBI_TaxID=399795 {ECO:0000313|EMBL:EED69977.1}; RN [1] {ECO:0000313|EMBL:EED69977.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=KF-1 {ECO:0000313|EMBL:EED69977.1}; 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] {ECO:0000313|EMBL:EED69977.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=KF-1 {ECO:0000313|EMBL:EED69977.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EED69977.1}. 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; AAUJ02000001; EED69977.1; -; Genomic_DNA. DR RefSeq; WP_003059671.1; NZ_AAUJ02000001.1. DR ProteinModelPortal; B7X069; -. DR EnsemblBacteria; EED69977; EED69977; CtesDRAFT_PD4925. DR PATRIC; 29061453; VBIComTes39478_4901. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EED69977.1}; KW Transferase {ECO:0000313|EMBL:EED69977.1}. SQ SEQUENCE 358 AA; 38566 MW; 95850237FC5976FD CRC64; MSQSHPTPAY TRAQELPATL AKRLVILDGA MGTMIQRFKL GEAQYRGEGY AGADAVDERF KDFAYDVKGN NELLSLTRPD VIRDIHEKYL AAGADLIETN TFGATTIAQE DYHMADLAYE MNLKSAQLAR AACDKYSTPD HKRYVAGALG PTPKTASISP DVNDPAARNI TFEQLRQAYL EQTLALIEGG ADVILVETIF DTLNAKAALF AVDEAFEQTG ERLPIMISGT VTDASGRILS GQTVTAFWHS VRHSNPLSVG LNCALGATLM RPYVQELAKA APDTFISCYP NAGLPNPMSD TGFDETPEIT SRLVHEFAAE GLVNIVGGCC GTTPDHIGAI AKAVQATATR KLFYPAEA // ID B7ZLW8_HUMAN Unreviewed; 1265 AA. AC B7ZLW8; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 01-APR-2015, entry version 41. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|EMBL:AAI44098.1}; GN Name=MTR {ECO:0000313|EMBL:AAI44098.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:AAI44098.1}; RN [1] {ECO:0000313|EMBL:AAI44098.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., RA Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., RA Feolo M., Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., RA Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J., RA Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N., RA Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B., RA Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B., RA Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S., RA Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R., RA Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L., RA Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E., RA Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., RA Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., RA Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., RA Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., RA Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D., RA Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A., RA Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S., RA Makowski K.A., Bosak S., Malek J.; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; BC144097; AAI44098.1; -; mRNA. DR UniGene; Hs.498187; -. DR PRIDE; B7ZLW8; -. DR HOVERGEN; HBG006347; -. DR ChiTaRS; MTR; human. DR NextBio; 35481344; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 2: Evidence at transcript level; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AAI44098.1}; KW Transferase {ECO:0000313|EMBL:AAI44098.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 260 260 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 785 785 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1265 AA; 140599 MW; EA4C26BC86AC8C41 CRC64; MSPALQDLSQ PEGLKKTLRD EINAILQKRI MVLDGGMGTM IQREKLNEEH FRGQEFKDHA RPLKGNNDIL SITQPDVIYQ IHKEYLLAGA DIIETNTFSS TSIAQADYGL EHLAYRMNMC SAGVARKAAE EVTLQTGIKR FVAGALGPTN KTLSVSPSVE RPDYRNITFD ELVEAYQEQA KGLLDGGVDI LLIETIFDTA NAKAALFALQ NLFEEKYAPR PIFISGTIVD KSGRTLSEQT GEGFVISVSH GEPLCIGLNC ALGAAEMRPF IEIIGKCTTA YVLCYPNAGL PNTFGDYDET PSMMAKHLKD FAMDGLVNIV GGCCGSTPDH IREIAEAVKN CKPRVPPATA FEGHMLLSGL EPFRIGPYTN FVNIGERCNV AGSRKFAKLI MAGNYEEALC VAKVQVEMGA QVLDVNMDDG MLDGPSAMTR FCNLIASEPD IAKVPLCIDS SNFAVIEAGL KCCQGKCIVN SISLKEGEDD FLEKARKIKK YGAAMVVMAF DEEGQATETD TKIRVCTRAY HLLVKKLGFN PNDIIFDPNI LTIGTGMEEH NLYAINFIHA TKVIKETLPG ARISGGLSNL SFSFRGMEAI REAMHGVFLY HAIKSGMDMG IVNAGNLPVY DDIHKELLQL CEDLIWNKDP EATEKLLRYA QTQGTGGKKV IQTDEWRNGP VEERLEYALV KGIEKHIIED TEEARLNQKK YPRPLNIIEG PLMNGMKIVG DLFGAGKMFL PQVIKSARVM KKAVGHLIPF MEKEREETRV LNGTVEEEDP YQGTIVLATV KGDVHDIGKN IVGVVLGCNN FRVIDLGVMT PCDKILKAAL DHKADIIGLS GLITPSLDEM IFVAKEMERL AIRIPLLIGG ATTSKTHTAV KIAPRYSAPV IHVLDASKSV VVCSQLLDEN LKDEYFEEIM EEYEDIRQDH YESLKERRYL PLSQARKSGF QMDWLSEPHP VKPTFIGTQV FEDYDLQKLV DYIDWKPFFD VWQLRGKYPN RGFPKIFNDK TVGGEARKVY DDAHNMLNTL ISQKKLRARG VVGFWPAQSI QDDIHLYAEA AVPQAAEPIA TFYGLRQQAE KDSASTEPYY CLSDFIAPLH SGIRDYLGLF AVACFGVEEL SKAYEDDGDD YSSIMVKALG DRLAEAFAEE LHERVRRELW AYCGSEQLDV ADLRRLRYKG IRPAPGYPSQ PDHTEKLTMW RLADIEQSTG IRLTESLAMA PASAVSGLYF SNLKSKYFAV GKISKDQVED YALRKNISVA EVEKWLGPIL GYDTD // ID B8A042_MAIZE Unreviewed; 338 AA. AC B8A042; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 01-APR-2015, entry version 33. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ACL53541.1}; 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 {ECO:0000313|EMBL:ACL53541.1}; RN [1] {ECO:0000313|EMBL:ACL53541.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=B73 {ECO:0000313|EMBL:ACL53541.1}; 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; BT054934; ACL53541.1; -; mRNA. DR EMBL; BT069278; ACN36175.1; -; mRNA. DR RefSeq; NP_001105013.1; NM_001111543.1. DR UniGene; Zm.530; -. DR ProteinModelPortal; B8A042; -. DR GeneID; 541875; -. DR KEGG; zma:541875; -. DR Gramene; B8A042; -. DR KO; K00547; -. DR OMA; SEWCKDG; -. DR ExpressionAtlas; B8A042; baseline. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; SQ SEQUENCE 338 AA; 36757 MW; 9C787F9F10D794E2 CRC64; MVGTAEGGAE RAVRRWVDAA GGRLVLDGGL ATELEANGAD LNDPLWSAKC LLSSPHLIRK VHMDYLEAGA NIIITASYQA TIQGFESKGF SKEQSENLLT KSVQIALEAR EMFLKEHLEK STPIQHPILV AAALGSYGAY LADGSEYSGD YGEAGTKEFL KDFHRRRLQV LAEAGPDLIA FETIPNKLEA QAYVELLEEC NINIPSWLSF NSKDGVHVVS GDSLIECATI ADKCAKVGAV GINCTPPRFI HGLILSIRKV TDKPILIYPN SGERYDGEKK EWVESTGVSD GDFVSYVNEW CKDGAALIGG CCRTTPNTIR AIHRTLNQGC HKHQLPVA // ID B8AA61_ORYSI Unreviewed; 328 AA. AC B8AA61; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 04-MAR-2015, entry version 27. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EEC71560.1}; GN ORFNames=OsI_03916 {ECO:0000313|EMBL:EEC71560.1}; 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 {ECO:0000313|EMBL:EEC71560.1, ECO:0000313|Proteomes:UP000007015}; RN [1] {ECO:0000313|EMBL:EEC71560.1, ECO:0000313|Proteomes:UP000007015} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. 93-11 {ECO:0000313|Proteomes:UP000007015}; 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). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000126; EEC71560.1; -; Genomic_DNA. DR ProteinModelPortal; B8AA61; -. DR STRING; 39946.BGIOSIBCE003793; -. DR PRIDE; B8AA61; -. DR EnsemblPlants; BGIOSGA000732-TA; BGIOSGA000732-PA; BGIOSGA000732. DR Gramene; B8AA61; -. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; SYIGKWR; -. DR Proteomes; UP000007015; Chromosome 1. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 2. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007015}; KW Reference proteome {ECO:0000313|Proteomes:UP000007015}. SQ SEQUENCE 328 AA; 34554 MW; 35E87556DA984EA1 CRC64; MGRGGDVDGA AGALRRFVRE AGGCAVVDGG LATELEAHGA DLHDELWSAS CLVSAPHLIR KVHLDYLDAG ANIITSASYQ ATIQGFQARG LSRERSEALL RRSVHIAQEA RAIFAEGWSK GPYANHRSSP RRPVLVAASI GSYGAYLADG SEYTGDYGIS VTKETLKSFH RRRLQVLADA GPDLIAFETI PNKLEAQASG DPITECAAVA DACARVGAVG VNCTAPRLVH GLILSIRKVT SKPVVVYPNS GETYVAETKE WVESEGGASE TDFVSCVGKW RQAGAALVGG CCRTSPATVR AISWALRESD DAVGGDGDRD DFPAVAVL // ID B8AQV5_ORYSI Unreviewed; 329 AA. AC B8AQV5; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 30. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EEC74781.1}; GN ORFNames=OsI_10560 {ECO:0000313|EMBL:EEC74781.1}; 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 {ECO:0000313|EMBL:EEC74781.1, ECO:0000313|Proteomes:UP000007015}; RN [1] {ECO:0000313|EMBL:EEC74781.1, ECO:0000313|Proteomes:UP000007015} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. 93-11 {ECO:0000313|Proteomes:UP000007015}; 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). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000128; EEC74781.1; -; Genomic_DNA. DR ProteinModelPortal; B8AQV5; -. DR STRING; 39947.LOC_Os03g12110.1; -. DR EnsemblPlants; BGIOSGA012137-TA; BGIOSGA012137-PA; BGIOSGA012137. DR Gramene; B8AQV5; -. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; AINDPLW; -. DR Proteomes; UP000007015; Chromosome 3. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007015}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000007015}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 236 236 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 329 AA; 35811 MW; 0F5D87D224C7CB1B CRC64; MAVAVEEIVR RAGGCAVIDG GFATQLEALG ADINDPLWSA ACLITKPHLI KEVHMQYLEA GADVIISSSY QATIPGFLAR GMLLEEAEGL LRRSIELALE ARDEFWKSTL RKSKPVYNRA LVAASIGSYG AYLADGSEYS GSYGEDITAE KLKDFHRRRL QVLASAGPDL IAFEAIPNKM EAQALVELLE EENIQVPSWI CFSSVDGKNL CSGESFAECL QFLNASDKVT IVGVNCTPPQ FIEGIIRELK KQTKKAIAVY PNSGEIWDGR AKRWLPAQCF GHKSFDALAK RWQEAGASLV GGCCRTTPST IRAVSKVLKG KTSYSATQI // ID B8C9X1_THAPS Unreviewed; 1251 AA. AC B8C9X1; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 01-APR-2015, entry version 43. DE SubName: Full=5-methyltretrahydrofolate-homocysteine s-methyltransferase {ECO:0000313|EMBL:EED89581.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EED89581.1}; GN Name=MHMT1 {ECO:0000313|EMBL:EED89581.1}; GN ORFNames=THAPSDRAFT_693 {ECO:0000313|EMBL:EED89581.1}; OS Thalassiosira pseudonana (Marine diatom) (Cyclotella nana). OC Eukaryota; Stramenopiles; Bacillariophyta; Coscinodiscophyceae; OC Thalassiosirophycidae; Thalassiosirales; Thalassiosiraceae; OC Thalassiosira. OX NCBI_TaxID=35128 {ECO:0000313|Proteomes:UP000001449}; RN [1] {ECO:0000313|EMBL:EED89581.1, ECO:0000313|Proteomes:UP000001449} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCMP1335 {ECO:0000313|EMBL:EED89581.1, RC ECO:0000313|Proteomes:UP000001449}; 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] {ECO:0000313|EMBL:EED89581.1, ECO:0000313|Proteomes:UP000001449} RP GENOME REANNOTATION. RC STRAIN=CCMP1335 {ECO:0000313|EMBL:EED89581.1, RC ECO:0000313|Proteomes:UP000001449}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CM000647; EED89581.1; -; Genomic_DNA. DR RefSeq; XP_002293120.1; XM_002293084.1. DR STRING; 35128.JGI693; -. DR EnsemblProtists; Thaps693; Thaps693; Thaps693. DR GeneID; 7443225; -. DR KEGG; tps:THAPSDRAFT_693; -. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR InParanoid; B8C9X1; -. DR KO; K00548; -. DR Proteomes; UP000001449; Chromosome 12. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001449}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EED89581.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001449}; KW Transferase {ECO:0000313|EMBL:EED89581.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 230 230 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 771 771 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1251 AA; 139257 MW; 9F974AB131E99149 CRC64; MGTMIQNYAK RNRLEEEEYR GDRFANWKCN MKGNNDQLSI TQPHIISGIY KEYLEVGGSD LIGTNTFSST TIAMADYEME DYVYELNYEG ARLAREACDE VTAKDPTRPR FVVGAIGPTN RTGSISPSVE DPSARNVTFD ELVEAYFEQI VALMDGGSDI LMVETIFDTL NAKAALYAVG EYLEFSGLDI PVFVSGTLVD QSGRTLSGQT GEAFYASIRH AKPMCVGLNC ALGANHMVPF VEKLANCVEC FLHVYSNAGL PNAMGGYDET PDMMAIQNKV FFENGWLNMV GGCCGSTPPH IKAIREMSEG YKPRKLPDVG RPKMWLSGLE DLVVDDVHNH LGLPFLNVGE RCNISGSIRF KKLMMAGDYG TAMDIAKKQV EDGAHVIDIN VDDGMLDGLA AMQKFVKIAV TEPEVAKVPF MLDASKFEIV LAGLKWCQGK CIVNSISLKV GEELFKEQAT LLKKHGCAVV VMAFDEEGQA ATEDEKVRIC KRSYDILVNE VHFPPEDIIF DPNVLTIGTG MEEHANYGVD FINATKTIKE ICPYVKISGG ISNLSFGFRG VMKIRESIHS VFLQHAILES GMDVGIVNAH EMLALSELED DIKAACENLV FNKTPDATDV MLELTKRERA RIEASKNGPA AAEVKQTSWR DLDVIKRLEH ALINGISQYI DGDVEEARQQ VEKPLHIIEG PLMDGMNIIG DLFGAGKMFL PQVIKSARVM KKAVAYLIPF MEKEKRDKLI AEGKDPEDFD ENDDSNFAGK VLMATVKGDV HDIGKNIVAV VLGCNNYKVY DIGVMCSCEK ILEKAKEYNV DVIGLSGLIT PSLDEMVVVA KEMSKAGFKQ PLLIGGATTS KMHTAVKVSP NYFTLEHPVI HVLDASRSVT VVSSLLGENK EEYVTDIMEE YDEMREDYYA GLEDRYFLTF DQAKQQKLTI DFDTFPPAPA PKKMGVTLID SVTLEDVVPY IDWNPFFQTW ELRGRYPNRG YPKIFNDEAV GSEAKKLFDD AQNLMTEIIA NKSMNLKGVV GLFPANRTDE GEDVRIYASE EDRDAGKSLD TFCMLRQQAE KESDDPYLSQ ADFIAPAGYK DHLGMFAVSC FGCDDLVKKY ESEHDDYNKI MSQALADRFV EAFAEYLHRV IRTDMWGYAQ NESLNEEDLL KIKYVGVRPA PGYPSQPDHT EKTTMWNVIK AEELAGIELS ESLSMMPAAS VSALVFAHPQ SCYFAVGQVG KDQVESYAER KKMDLPVTER WLSPILNYER D // ID B8CJ33_SHEPW Unreviewed; 1247 AA. AC B8CJ33; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 49. DE SubName: Full=Dihydropteroate synthase, DHPS:Homocysteine S-methyltransferase:Cobalamin-dependent methionine synthase, B12-binding:Vitamin B12 dependent methionine synthase, activation region:Coenzyme B12-binding {ECO:0000313|EMBL:ACJ27795.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ACJ27795.1}; GN OrderedLocusNames=swp_0992 {ECO:0000313|EMBL:ACJ27795.1}; OS Shewanella piezotolerans (strain WP3 / JCM 13877). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=225849 {ECO:0000313|EMBL:ACJ27795.1, ECO:0000313|Proteomes:UP000000753}; RN [1] {ECO:0000313|EMBL:ACJ27795.1, ECO:0000313|Proteomes:UP000000753} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WP3 / JCM 13877 {ECO:0000313|Proteomes:UP000000753}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000472; ACJ27795.1; -; Genomic_DNA. DR RefSeq; WP_020911173.1; NC_011566.1. DR RefSeq; YP_002310382.1; NC_011566.1. DR STRING; 225849.swp_0992; -. DR EnsemblBacteria; ACJ27795; ACJ27795; swp_0992. DR KEGG; swp:swp_0992; -. DR PATRIC; 23540620; VBIShePie65056_0896. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SPIE225849:GH6V-956-MONOMER; -. DR Proteomes; UP000000753; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000753}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACJ27795.1}; KW Transferase {ECO:0000313|EMBL:ACJ27795.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 261 261 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 325 325 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 777 777 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1247 AA; 138255 MW; E858A5F48AC62693 CRC64; MATHTLSPVP HTQETADKVL AVLTKKLEEG ILLLDGAMGT MIQDRKFEEQ QFRGEQFKDW HCDVKGNNDM LVLTQPEAIK QIHKDYFLAG SDIIETNTFN ATRIAMADYD MQAHSAEINL QGARLAREAA NEVEAETGRQ CYVAGVLGPT NRTCSISPDV NDPGYRNVSF DELVEAYIES INALIAGGAD IIMVETIFDT LNAKAALFAI ETVYDAQGFR LPIMISGTIT DASGRTLTGQ TTEAFYNSLR HVKPLTIGLN CALGPKELRP YVEELSKISE CFVSAHPNAG LPNEFGGYDE TPEQMSEVIE EWALEGFLNV IGGCCGTTPA HIRAIREAVI KHPARVLPDI PVACRLSGLE PLTIDENSLF LNVGERTNVT GSAKFLRLIK TGEYEEALSV ARDQVENGAQ IIDINMDEGM LDGSDTMHKF LNLIASEPDI SRVPIMIDSS KWEVIEAGLK CIQGKGIVNS ISLKEGEEKF IEQATLVKRY GAAAIVMAFD EVGQADTKAR KVEICTRAYN VLVDKVGFPP EDIIFDPNIF AIATGIEEHD NYAVDFIEAT AEIKRTLPHA MISGGVSNVS FSFRGNNPVR EAIHAVFLYH AIQAGMDMGI VNAGQLAIYD DIDPELKERV EAIVQNLPCT VSDSSNTEQL LEVAEKFRGD GNQVAKKEDL EWRTKPVNER LAHALVKGIT DFIDEDTEEA RIQASRPLDV IEGPLMDGMN IVGDLFGSGK MFLPQVVKSA RVMKKAVAYL NPYIELEKVA GQSNGKILMV TVKGDVHDIG KNIVGVVLAC NGYEVIDLGV MVPVEKIIEV AKAENVDIIG MSGLITPSLD EMVHNVKSFH KAGLTIPSII GGATCSKIHT AVKIAPHSPE GAIYIADASR AVPMVSKLIN NDTRQATIDE AYQEYDVMRE KRLSQTKRKV ITSLEAAREN RCQHDWENYT PFVPNQLGRQ VFDDYPLEDL VERIDWTPFF RSWELHGHFP QILDDEVVGE EARKLFSDGK AMLQKIISEK WLTAKGVIGL FPANTVNHDD IELYTDESRT ELEMTTHHLR MQIERVGNDN FCLADFVAPK DSGVADYMGG FAVTAGHGID EHVARFEAEH DDYSAIMLKC LADRLAEAFA ERMHERVRKE FWGYASDETL DNEALIREKY KGIRPAPGYP ACPDHTEKGL LWDLLKPDET IGLNITESYA MFPTAAVSGW YFAHPKSRYF GVTNIGRDQV EDYATRKGMS IEETERWLMP VLDYDPE // ID B8CZI7_HALOH Unreviewed; 819 AA. AC B8CZI7; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 44. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACL70706.1}; GN OrderedLocusNames=Hore_19590 {ECO:0000313|EMBL:ACL70706.1}; OS Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562). OC Bacteria; Firmicutes; Clostridia; Halanaerobiales; Halanaerobiaceae; OC Halothermothrix. OX NCBI_TaxID=373903 {ECO:0000313|EMBL:ACL70706.1, ECO:0000313|Proteomes:UP000000719}; RN [1] {ECO:0000313|EMBL:ACL70706.1, ECO:0000313|Proteomes:UP000000719} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H 168 / OCM 544 / DSM 9562 {ECO:0000313|Proteomes:UP000000719}; RX PubMed=19145256; DOI=10.1371/journal.pone.0004192; RA Mavromatis K., Ivanova N., Anderson I., Lykidis A., Hooper S.D., RA Sun H., Kunin V., Lapidus A., Hugenholtz P., Patel B., Kyrpides N.C.; RT "Genome analysis of the anaerobic thermohalophilic bacterium RT Halothermothrix orenii."; RL PLoS ONE 4:E4192-E4192(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; CP001098; ACL70706.1; -; Genomic_DNA. DR RefSeq; WP_015923675.1; NC_011899.1. DR RefSeq; YP_002509701.1; NC_011899.1. DR ProteinModelPortal; B8CZI7; -. DR STRING; 373903.Hore_19590; -. DR EnsemblBacteria; ACL70706; ACL70706; Hore_19590. DR KEGG; hor:Hore_19590; -. DR PATRIC; 22103476; VBIHalOre56292_2088. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; HORE373903:GHB1-2025-MONOMER; -. DR Proteomes; UP000000719; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000719}; KW Methyltransferase {ECO:0000313|EMBL:ACL70706.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000719}; KW Transferase {ECO:0000313|EMBL:ACL70706.1}. SQ SEQUENCE 819 AA; 89712 MW; 88164F7BB78FB322 CRC64; MANDFTSTLQ EKIIIGDGAM GTMLQACGLS SGHAPESWVI KKPDTIYKIH KEYVAAGAGL IETNTFGANR LKLKSLGLED KIEEINVKAT GLARKAAGKV FVAGSVGPTG KLMEPHGDLS FDRARDVFKE QISYLVHAGV DVVIIETMSD LKELRAAVVA AKEFNVPVIA QMTFTERGIT LTGSPPEVVA IVLDKMGVDV IGVNCVAGIE EALIVIKKMS RVTSKPLSVF PNAGLPESKG GETVYPQTPD AFTDKIPELL KYNVKLIGGC CGTNPRFIKG IKQVVYEAKV SNNTNTDAKD ENKNRTYLTS NHTYLQASED KPVFLIGERI NPTGRNDLKE ALKGEKWSVL RKEAREQVIA GAHLLDVNIG MAGIDREKCM KKVIQELQLE VDVPLVIDTP RTGVLETALK EYTGRALINS VNGNPDVMDK VFPLACRYGA AVIGLTLDDR GIPSEVEGRL EIARQIIARA REYGLGEEDI IIDPIVLTAG SNQSEVMKGI ETLKRIKEEL GVKTTMGISN VSHGLPNRKL INRTFLAMAL GAGLDFPIVD PVDEDLMATV RAANLLTARD RNGQNFLKWY GNFQGNKSLE EDRLDNNKET KSSRDKENDR LLSSIADIVV SGDTDIIEEQ VARALELYQP REIINRAMVK GLKRVGDLYD RGEYFLPQLM QSSRVVKKAF DLLKERMNSK GREINKAGRI LLATVEGDIH DIGKNIVKVV FNNYGFEVVD LGVNVKSDDI VEAAFDHKVD IVGLSALMTV TMEKMRETVN ILKQKGFKGG IIIGGAVTSE DFAREIGADL YAGDALDGVR KVKKYLNLN // ID B8DKK4_DESVM Unreviewed; 818 AA. AC B8DKK4; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 01-APR-2015, entry version 38. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACL07433.1}; GN OrderedLocusNames=DvMF_0476 {ECO:0000313|EMBL:ACL07433.1}; OS Desulfovibrio vulgaris (strain Miyazaki F / DSM 19637). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=883 {ECO:0000313|EMBL:ACL07433.1, ECO:0000313|Proteomes:UP000001361}; RN [1] {ECO:0000313|Proteomes:UP000001361} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Miyazaki F / DSM 19637 {ECO:0000313|Proteomes:UP000001361}; 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 ----------------------------------------------------------------------- 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; ACL07433.1; -; Genomic_DNA. DR RefSeq; WP_012611625.1; NC_011769.1. DR RefSeq; YP_002434901.1; NC_011769.1. DR STRING; 883.DvMF_0476; -. DR EnsemblBacteria; ACL07433; ACL07433; DvMF_0476. DR KEGG; dvm:DvMF_0476; -. DR PATRIC; 21770895; VBIDesVul86729_0499. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; DVUL883:GCJ5-495-MONOMER; -. DR Proteomes; UP000001361; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001361}; KW Methyltransferase {ECO:0000313|EMBL:ACL07433.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001361}; KW Transferase {ECO:0000313|EMBL:ACL07433.1}. SQ SEQUENCE 818 AA; 85656 MW; 8E8A526461271D94 CRC64; MPDFRQALRS GRRLVFDGGM GTMLQSRGLP PGVSPELFCL ARPDVLVGIH ADYLRAGADV LTTNTFGGCI HKLGTGPGAP DVVEFNRAMA RAAREAVLAS GREAFVAGSV GPSGHFMRPL GDLDPAELVA AFRAQIRGLV QGGVDLILAE TQFDLAEARA IVLAARAECD LPVGVSMTFE NGVSLTGTRP EVFVQSMLNM GVDLVGTNCS AGPEQMAEVA DELLAISEVP VLVEPNAGLP ELVDGKTVFR LGPDDFARHT ARFAASGVRM LGGCCGTTPD HIAALRGALD NLSGGLVPDP ARRDGIVLTT RAQAVHIGAG SPIRIIGERI NPTGKKLLTA ELQAGEFAQA LRFADEQVEA GAPLLDVNVG APMVDEAVLL PALVERLVAR HSLPLSLDSS NADAIAAALP FHPGSPLVNS ISGEPGRMEH LGPLCRDHGA PFILLPLKGR KLPVTAAERI AIIEELLQQA DSLRIPRRLV MVDVLALAVS SKAEAARHCL DTIRWCAAQG LPTTIGLSNI SFGLPARELL NSTFLAMAAG AGLSSCIAHP GNARIREAVA ASSVLLGLDA NAESFIEGYS GWTPGGDATG ATPAGVAGGT GGGTGGVKAK AATLEEAVIR GDREGALALV ERALSEGADP FSLVQEKLIP GITEVGRRYE RREYFLPQLI RSAETMQHAF RKLQPLLEAQ RGHEARPVII MATVEGDIHD IGKNIVTLML GNHGFDVVDL GKDVKAADIV EAAERHGARV IGLSALMTTT MVRMEDTVRL VRERGLPVKV MVGGAVVTPA YAEAIGADGY SADAVEAVRV AKELLTVQ // ID B8DYM9_DICTD Unreviewed; 290 AA. AC B8DYM9; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 04-FEB-2015, entry version 31. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACK41411.1}; GN OrderedLocusNames=Dtur_0073 {ECO:0000313|EMBL:ACK41411.1}; OS Dictyoglomus turgidum (strain Z-1310 / DSM 6724). OC Bacteria; Dictyoglomi; Dictyoglomales; Dictyoglomaceae; Dictyoglomus. OX NCBI_TaxID=515635 {ECO:0000313|EMBL:ACK41411.1, ECO:0000313|Proteomes:UP000007719}; RN [1] {ECO:0000313|EMBL:ACK41411.1, ECO:0000313|Proteomes:UP000007719} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Z-1310 / DSM 6724 {ECO:0000313|Proteomes:UP000007719}; 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 ----------------------------------------------------------------------- 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; ACK41411.1; -; Genomic_DNA. DR RefSeq; WP_012582497.1; NC_011661.1. DR RefSeq; YP_002352025.1; NC_011661.1. DR STRING; 515635.Dtur_0073; -. DR EnsemblBacteria; ACK41411; ACK41411; Dtur_0073. DR GeneID; 7082340; -. DR KEGG; dtu:Dtur_0073; -. DR PATRIC; 21808756; VBIDicTur93964_0074. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265278; -. DR InParanoid; B8DYM9; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; DTUR515635:GH4F-73-MONOMER; -. DR Proteomes; UP000007719; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007719}; KW Methyltransferase {ECO:0000313|EMBL:ACK41411.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007719}; KW Transferase {ECO:0000313|EMBL:ACK41411.1}. SQ SEQUENCE 290 AA; 32312 MW; D54FDE5A1DF5E644 CRC64; MSNKKIKLPE FLFFDGAMGT ELQRRGLPPG TPPEILNLEN PSLVEEVHKD YIKAGSMVIE TNTFGGNRVR LQRAGLEEKI KEINEKGVEI AQKASEGKVL IAGSVGPLGE LIEPYGDISE EEAEEFFTEQ IEILVNSGVD LILIETMISL NEALIALKSA KKFDIPVGVT MSFEWTEKGG RTPFGDEVEY SIKKLEENGA DFVGSNCGKG FEDMLKIAPI IRRSTRLPVL IQPNAGIPRW ENGKLLYPES PEKFKTFVDE MIKLKINFIG GCCGTTPKHI EVFKEFYLKK // ID B8E4M5_SHEB2 Unreviewed; 1244 AA. AC B8E4M5; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 29-APR-2015, entry version 47. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACK45511.1}; GN OrderedLocusNames=Sbal223_0995 {ECO:0000313|EMBL:ACK45511.1}; OS Shewanella baltica (strain OS223). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=407976 {ECO:0000313|EMBL:ACK45511.1, ECO:0000313|Proteomes:UP000002507}; RN [1] {ECO:0000313|Proteomes:UP000002507} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OS223 {ECO:0000313|Proteomes:UP000002507}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001252; ACK45511.1; -; Genomic_DNA. DR RefSeq; WP_012586948.1; NC_011663.1. DR RefSeq; YP_002356934.1; NC_011663.1. DR STRING; 407976.Sbal223_0995; -. DR EnsemblBacteria; ACK45511; ACK45511; Sbal223_0995. DR KEGG; sbp:Sbal223_0995; -. DR PATRIC; 23478036; VBISheBal125792_1033. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SBAL407976:GJ6Y-1017-MONOMER; -. DR Proteomes; UP000002507; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002507}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 258 258 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 774 774 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1244 AA; 137939 MW; 538AD7549712F2A9 CRC64; MTIPSTKAGQ ILADIRKQLA ARILILDGAM GTMIQDHKLE EEDYRGERFK DWHTDVKGNN DLLVLSQPQI IKQIHTDYLN AGADIIETNT FNATTIAMAD YDMQSLSAEI NLAGARLARE ACDEVFAATG IPRYVAGVLG PTNRTCSISP DVNDPGYRNV SFDELVSAYR ESTKALIEGG ADIIMVETIF DTLNAKAALF AIESVFDDLF GQHSKDRLPI MISGTITDAS GRTLTGQTTE AFYNSLRHIK PLSIGLNCAL GPKELRPYVE ELSRIAECYV SAHPNAGLPN EFGGYDETPE DMANVIEDWA REGMLNIIGG CCGSTPEHIR VIREAVDRHN PRVLPDIPVA CRLAGLEPLT IDAQSLFVNV GERTNVTGSA KFLKLIKDGK FEQALDVARE QVESGAQIID INMDEGMLDG AEIMHKFLNL IASEPDISRV PIMIDSSKWE VIEAGLKCIQ GKGIVNSISL KEGEAKFIEQ ATLVKRYGAA AIIMAFDEQG QADTKARKIE ICTRAYRVLV DKVGFPPEDI IFDPNIFAIA TGIDEHDNYA VDFIDAIKAI KATLPHAMIS GGVSNVSFSF RGNNPVREAI HAVFLYHAIK VGMDMGIVNA GQLAIYDDID PELKVRVENV VLNLPCPVEG SSNTEQLLEI AEKFRGDGAQ VGKKEDLEWR SWPVSQRLSH ALVKGITEFI DEDTEAARQE AKRPLDVIEG ALMDGMNVVG DLFGSGKMFL PQVVKSARVM KKAVAYLNPY IELEKVEGQS NGKILMVTVK GDVHDIGKNI VGVVLACNGF EVFDLGVMVS VERILDAVKE HNIDIIGMSG LITPSLDEMV HNVKTFHREG LTIPAIIGGA TCSKIHTAVK IAPHYPHGAI YIADASRAVP MVSKLINNET RQATIDEAYA EYDDMRTKRL SQAKRKEIVS LEAARENRCQ HDWANYTPFT PNVLGRQVFD NYPLEDLVER IDWTPFFRSW ELHGHYPEIL TDKVVGEEAQ KLFADGQAML KQIIEEKWLT AKAVIGLFPA NTVNYDDIEL YTDESRITVE MTTHHLRMQL ERVGNDNFCL SDFVAPKDSG VADYMGGFAV TTGHGIDEHV ARFEANHDDY NAIMLKCLAD RLAEAFAERM HERVRKEFWG YAADEQLSNE ALIREKYKGI RPAPGYPACP DHTEKGLLWD LLKPDETIDL NITESYAMFP TAAVSGWYFA HPKSRYFGVS NIGRDQVEDY AKRKGMTVAE TEKWLAPVLD YDPE // ID B8E8X0_SHEB2 Unreviewed; 300 AA. AC B8E8X0; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 31. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACK45786.1}; GN OrderedLocusNames=Sbal223_1277 {ECO:0000313|EMBL:ACK45786.1}; OS Shewanella baltica (strain OS223). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=407976 {ECO:0000313|EMBL:ACK45786.1, ECO:0000313|Proteomes:UP000002507}; RN [1] {ECO:0000313|Proteomes:UP000002507} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OS223 {ECO:0000313|Proteomes:UP000002507}; 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; ACK45786.1; -; Genomic_DNA. DR RefSeq; WP_012587123.1; NC_011663.1. DR RefSeq; YP_002357209.1; NC_011663.1. DR ProteinModelPortal; B8E8X0; -. DR STRING; 407976.Sbal223_1277; -. DR EnsemblBacteria; ACK45786; ACK45786; Sbal223_1277. DR KEGG; sbp:Sbal223_1277; -. DR PATRIC; 23478644; VBISheBal125792_1319. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; PYVDVWL; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; SBAL407976:GJ6Y-1315-MONOMER; -. DR Proteomes; UP000002507; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002507}; KW Methyltransferase {ECO:0000313|EMBL:ACK45786.1}; KW Transferase {ECO:0000313|EMBL:ACK45786.1}. SQ SEQUENCE 300 AA; 32073 MW; 218E6360D96AD990 CRC64; MDKQQLWVLD GGMGRELARR GAPFRQPEWS ALALIEAPQT VTEVHQAYVA SGAKVITTNS YALVPFHIGD ERFAAEGEVL AALAGKLARD VADEHANAVR VAGSLPPLFG SYRADLFEAA RVSELALPLI RALSPSVDLW LAETMSLIAE PLAIKALLPE DGKPFWVSFT LEDETLGSEP TLRSGERVAD AIDALVAVGV DAILFNCCQP EVIEAALQVA SDRLSALGRA DIRLGAYANA FPPQPKEATA NDGLDEIRAD LGPLDYLGWA ERWRAVGASL IGGCCGIGPE HIQALATRLR // ID B8ETT2_METSB Unreviewed; 1245 AA. AC B8ETT2; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 01-APR-2015, entry version 47. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACK52434.1}; GN OrderedLocusNames=Msil_3545 {ECO:0000313|EMBL:ACK52434.1}; OS Methylocella silvestris (strain BL2 / DSM 15510 / NCIMB 13906). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Beijerinckiaceae; Methylocella. OX NCBI_TaxID=395965 {ECO:0000313|EMBL:ACK52434.1, ECO:0000313|Proteomes:UP000002257}; RN [1] {ECO:0000313|EMBL:ACK52434.1, ECO:0000313|Proteomes:UP000002257} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BL2 / DSM 15510 / NCIMB 13906 RC {ECO:0000313|Proteomes:UP000002257}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001280; ACK52434.1; -; Genomic_DNA. DR RefSeq; WP_012592503.1; NC_011666.1. DR RefSeq; YP_002363796.1; NC_011666.1. DR STRING; 395965.Msil_3545; -. DR EnsemblBacteria; ACK52434; ACK52434; Msil_3545. DR KEGG; msl:Msil_3545; -. DR PATRIC; 22602902; VBIMetSil55537_3799. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; MSIL395965:GCND-3598-MONOMER; -. DR Proteomes; UP000002257; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002257}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002257}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 252 252 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 315 315 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 316 316 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 767 767 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1245 AA; 136112 MW; 697889C05E03F99B CRC64; MTHRFDGAET RAAFLDAARK RILVLDGAMG TMIQQHKFTE EQFRGERFAD WPSDLRGNND LLSLTQPKAI EQIHRAYIDA GADIIATNTF NSTSISQADY GMQELVFELN RESARLCRVA ADAAEKHDGK RRFVAGALGP TSRTASISPD VNNPGFRAVS FDELRDAYDE AARALIEGGA DLLIIETIFD TLNAKAALAG VRDAFAKLGV EAPVMISGTI TDLSGRTLSG QTPTAFWHSL RHADPLTIGL NCALGAREMR AHLAELSRIA DTLVCAYPNA GLPNEFGLYD ESPEYMASLV GEFADSGLVN VVGGCCGTTP AHIHAIAKRI EGVAPREIPE IAPLLRLSGL EPFVLAPEIP FVNVGERTNV TGSAKFRKLI KQGDFAAALD VARDQVAAGA QIIDVNMDEG LLDSEKAMVE FLNLIAAEPD IARVPVMIDS SKFSVIEAGL KCVQGKSVVN SISMKEGVEK FIADARTVRA YGAAVVVMAF DEKGQADTFE RKVEICAKAY QILTQEAGFP PEDIIFDPNI FAIATGIEEH NNYGVDFIEA TREIRKRFPL VHISGGVSNL SFSFRGNEPV REAMHAVFLY HAIQAGMDMG IVNAGQLAVY AEIEPGLREA CEDVVLNRRP DATERLLAIA EGFRGHGVEK AERDLVWREQ PVIKRLEHAL VNGITEFVEL DVEEARAASK RPLDVIEGPL MAGMNVVGDL FGAGKMFLPQ VVKSARVMKQ AVAYLLPYMD EEKRKNGGSE RSTAGKILMA TVKGDVHDIG KNIVGVVLAC NNYEIIDLGV MVPAAKILSV ARAEKVDAIG LSGLITPSLD EMCYVAAEME REGFDLPLLI GGATTSRVHT AVKIHPNYTR GQTVYVNDAS RAVGVVQSLL GESARDAAET FRAEYEKVAA AHRRGEAEKL RLPIGKARAN ALKIDWDDYA PPRPTFTGSR VFRSYDVAEL IPYIDWTPFF QTWELRGRYP AILDDPKQGE AARSLFDDAQ AMLKRMVEEH WLDPKAVIGF WPANSVGDDI ALYTGESRSE KLAAFHTLRQ QLTRRDGKPN IALSDFIAPA GGKPDYIGAF VVTAGAQEGK IADRFAKAND DYGSILVKAL ADRIAEALAE RMHERVRREF WAYAPDEAIS EDDRLREEYR GIRPAPGYPA QPDHTEKATL FELLAAEKRI GVSLTESFAM WPGASVSGLY FAHPQAHYFG VAKIERDQVE DYALRKGMSV AEMERWLAPI LNYDPASVAE AAAAE // ID B8FX16_DESHD Unreviewed; 285 AA. AC B8FX16; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 37. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACL18902.1}; GN OrderedLocusNames=Dhaf_0839 {ECO:0000313|EMBL:ACL18902.1}; OS Desulfitobacterium hafniense (strain DCB-2 / DSM 10664). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfitobacterium. OX NCBI_TaxID=272564 {ECO:0000313|EMBL:ACL18902.1, ECO:0000313|Proteomes:UP000007726}; RN [1] {ECO:0000313|EMBL:ACL18902.1, ECO:0000313|Proteomes:UP000007726} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DCB-2 / DSM 10664 {ECO:0000313|Proteomes:UP000007726}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; ACL18902.1; -; Genomic_DNA. DR RefSeq; WP_015943058.1; NC_011830.1. DR RefSeq; YP_002457338.1; NC_011830.1. DR ProteinModelPortal; B8FX16; -. DR STRING; 272564.Dhaf_0839; -. DR EnsemblBacteria; ACL18902; ACL18902; Dhaf_0839. DR KEGG; dhd:Dhaf_0839; -. DR PATRIC; 21659359; VBIDesHaf15223_0881. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265278; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; DHAF272564:GCV8-864-MONOMER; -. DR Proteomes; UP000007726; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007726}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ACL18902.1}; KW Transferase {ECO:0000313|EMBL:ACL18902.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 200 200 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 265 265 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 266 266 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 285 AA; 30805 MW; D7D6CDD05C72781C CRC64; MILDKDSYVI FDGAMGTMLQ KYDLAPGQPP EVLNITRPEV IEEVHRKYIK AGSNIITTNT FGAIETKLNG TGYSVEEVVQ SAIAIARRAA GKNLVALDVG PTGELIEPLG DLSFEEVYDL YACQIKAAAL TGNVDLVLIE TFFDLTEAHA AIRAAKDHSS LPVICTFTFQ QKGRTLMGKD IKTVVTSLEE YGVDAVGVNC SLGPGEMLSI VETMVSSTQL PILVQPNAGL PKLIGDRTVY DVEPEEFARY IQVMANLGVK WFGGCCGTTP EFISAIKESL GLKHN // ID B8G5S4_CHLAD Unreviewed; 316 AA. AC B8G5S4; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 34. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACL23785.1}; GN OrderedLocusNames=Cagg_0866 {ECO:0000313|EMBL:ACL23785.1}; OS Chloroflexus aggregans (strain MD-66 / DSM 9485). OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae; OC Chloroflexaceae; Chloroflexus. OX NCBI_TaxID=326427 {ECO:0000313|EMBL:ACL23785.1, ECO:0000313|Proteomes:UP000002508}; RN [1] {ECO:0000313|Proteomes:UP000002508} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MD-66 / DSM 9485 {ECO:0000313|Proteomes:UP000002508}; 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 ----------------------------------------------------------------------- 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; ACL23785.1; -; Genomic_DNA. DR RefSeq; WP_012616151.1; NC_011831.1. DR RefSeq; YP_002462221.1; NC_011831.1. DR ProteinModelPortal; B8G5S4; -. DR STRING; 326427.Cagg_0866; -. DR EnsemblBacteria; ACL23785; ACL23785; Cagg_0866. DR KEGG; cag:Cagg_0866; -. DR PATRIC; 21404202; VBIChlAgg85409_0904. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; CAGG326427:GHS8-872-MONOMER; -. DR Proteomes; UP000002508; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002508}; KW Methyltransferase {ECO:0000313|EMBL:ACL23785.1}; KW Transferase {ECO:0000313|EMBL:ACL23785.1}. SQ SEQUENCE 316 AA; 33992 MW; 829B8494BD06A2FA CRC64; MNPIAQALTQ RPLLVLDGAL ATELERRGCD LADPLWSAKV LIENPTLIQA VHADYFAAGA DVAITASYQA TIPGFMARGL SEAEAIALLQ RSVALARAAR DAFWADPANR VGRIRPLVAA SIGPYGAYLH DGSEYRGEYG LSVADLIDFH RPRMAALAAA EPDLFACETI PCWDEARALV ALLPEFPQLT AWISFSARDG AHTSRGEPIT EVVAEIAAHP QVAAIGINCT APRFIPDLIR AIRSVTTKPI VVYPNSGEVY DPVGQCWIGT TEIDDFAAQA RQWYAVGARL IGGCCRTTPD HIRAVAAWAA REVQHG // ID B8GC11_CHLAD Unreviewed; 1196 AA. AC B8GC11; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 53. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACL22985.1}; GN OrderedLocusNames=Cagg_0032 {ECO:0000313|EMBL:ACL22985.1}; OS Chloroflexus aggregans (strain MD-66 / DSM 9485). OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae; OC Chloroflexaceae; Chloroflexus. OX NCBI_TaxID=326427 {ECO:0000313|EMBL:ACL22985.1, ECO:0000313|Proteomes:UP000002508}; RN [1] {ECO:0000313|Proteomes:UP000002508} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MD-66 / DSM 9485 {ECO:0000313|Proteomes:UP000002508}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001337; ACL22985.1; -; Genomic_DNA. DR RefSeq; WP_012615351.1; NC_011831.1. DR RefSeq; YP_002461421.1; NC_011831.1. DR ProteinModelPortal; B8GC11; -. DR STRING; 326427.Cagg_0032; -. DR EnsemblBacteria; ACL22985; ACL22985; Cagg_0032. DR KEGG; cag:Cagg_0032; -. DR PATRIC; 21402448; VBIChlAgg85409_0034. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CAGG326427:GHS8-33-MONOMER; -. DR Proteomes; UP000002508; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002508}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 233 233 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 765 765 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1196 AA; 131832 MW; 138B3DBDD483B631 CRC64; MTRPTYLQAL AERVLVYDGA MGTSIDTFDL TAEDYGGEAT FGCRDYLVIT RPDVIESIHT SFLEAGCDVI ETCTFQSTRL RLAEWGLGDR TIEINRAAAA LARRVADRFA ARDGRPRYVA GSIGPTGKLP SSDDPELSNI TFAELSDIFR EQAIGLIEGG VDLLLVETSV DILEVKAALD GIRRAKIDLN RPDIAVQAQV FLDLSGRMLL GTDVPAMIAT LEAMPVDVIG LNCGTGPEHM RAAIQYLTAH SRKPISCIPN AGLPLEVEGR TVYPMEPEPF AEVLAEFVRD YGVAVVGGCC GTRPAHIARL RQLLGNDPTP KVRQVEYIPS VSSGIRATAL RQDATLTMIG ERLNTLGSRK VKRLLLRDDY DGALEVAREQ VESGAHMLDV CVAMTERSDE REQMTRLIKK LTLNIELPLV IDTTEAEVLE AALSIYPGRA LINSVSLEGG RGAKIDKVLP LAARYGAAVI AMTIDEEGMA HTAERKVAIA ERIAQIARDE YGLPAEALVF DVLTFPITTG QEELRYSAIE TLEGIRLVKQ RIPGCFTTLG VSNLSFGVAP HARAALNSVF LYHAVAAGLD TAIINPAHIT PYAEIDPVQR ELCEDLIFAR RDDALARFIA YFEQHTASSD NEREDPTASM TVDQRLHWKI LHRKKEGIED DIDQAVDERL QAIGLRLSDP AAAVRDDQGA SPQGRAAVEV LNNVLLPAMK EVGDLFGAGQ LILPFVLQSA EAMKKAVARL ERYLDRVEGT SKAKVVLATV YGDVHDIGKN LVNTILSNNG YTVYDLGKQV PINTIVEKAL EVQADAIGLS ALLVSTSKQM PLCVQELHRR GLRIPVLVGG AAINRQYGQR ITFVDDEEPY PAGVFYCKDA FEGLETMDRL SNPATRDQFI EQTIREAANV LHRRMTGRVA LADLGEAASA TAAGVRSAVR TDVPVPVPPF WGWRATSRIR LRDVVECLDR NSLYRLQWGA KNAKGEEWER LRAEFDQKVR ELIAEAERDG WLQPKVIYGY FPVQSDGLEL IVYDPVNRSR ELTRFVFPRQ PARERLCISD YFRSVDSGEY DVAAFQIVTI GSTVDELVDT LQQRGDYSRS YYIHGLGVSL AEALAEYTNR IIRQGLGLDE RRGKRYSWGY PACPDLSEHA KLWQILPGEE IGVTLTEAFQ LVPEQSTAAI VVHHPEAKYF SIGSAVERAE TDVQNQ // ID B8GLZ0_THISH Unreviewed; 1250 AA. AC B8GLZ0; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 47. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACL71743.1}; GN OrderedLocusNames=Tgr7_0650 {ECO:0000313|EMBL:ACL71743.1}; OS Thioalkalivibrio sulfidiphilus (strain HL-EbGR7). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Thioalkalivibrio. OX NCBI_TaxID=396588 {ECO:0000313|EMBL:ACL71743.1, ECO:0000313|Proteomes:UP000002383}; RN [1] {ECO:0000313|EMBL:ACL71743.1, ECO:0000313|Proteomes:UP000002383} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HL-EbGR7 {ECO:0000313|EMBL:ACL71743.1, RC ECO:0000313|Proteomes:UP000002383}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001339; ACL71743.1; -; Genomic_DNA. DR RefSeq; WP_012637231.1; NC_011901.1. DR RefSeq; YP_002512730.1; NC_011901.1. DR STRING; 396588.Tgr7_0650; -. DR EnsemblBacteria; ACL71743; ACL71743; Tgr7_0650. DR KEGG; tgr:Tgr7_0650; -. DR PATRIC; 23960770; VBIThiSp19295_0643. DR eggNOG; COG1410; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; TSUL396588:GH5B-652-MONOMER; -. DR Proteomes; UP000002383; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002383}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002383}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1250 AA; 139095 MW; FBFAE5B4F8CF60D9 CRC64; MTDDRTRLLE THIKERILIL DGAMGTMIQG YGLGEADYRG ERFADWQIDL KGNNDLLALT RPEIIAEIHG QYLEAGADIL ETNTFNATTI AMADYAMEEL VPEINREAAR LARRVADEWT AKTPDRPRFV AGVLGPTNRT ASISPDVNDP GFRNVDFDQL VAAYRQAAEA LIEGGADLLL IETVFDTLNA KAAVFAVESL FDETGRRLPV MISGTITDAS GRTLSGQTAE AFWNSLRHAR PFSFGLNCAL GPRELRAHVE EISRIANTHV SAHPNAGLPN EFGGYDLSPA DMAVHIREWA ESGFLNIVGG CCGTTPAHIR AIAEAVADLP PRSIPKREPA CRLSGLEPCN ITEDSLFVNV GERTNVTGSA RFKRLIKDGD YETALEVAAS QVENGAQIID VNMDEGMLDS KAAMVRFLNL MAAEPDISRV PVMIDSSKWE VIEAGLKCIQ GKGVVNSISL KEGEATFIEH AKLVRRYGAA VIVMAFDEQG QADTQARKVE ICERAYRILT EQVCFPAEDI IFDPNIFAIA TGIEEHNNYG VDFIEATREI KKRLPHALVS GGVSNVSFSF RGNEPVREAI HAVFLYHAIH AGMDMGIVNA GQLAVYDEID RELRELVEDV VLNRRPDATE RLLEAAERYR GEGGEAKKED LEWRKLPVAK RLEHALVKGI DAFVVEDTEE ARQGVDHPIH VIEGPLMDGM NVVGDLFGDG KMFLPQVVKS ARVMKKAVAH LIPFIEALKQ EGDRPNGKVL MATVKGDVHD IGKNIVGVVL QCNNFEVIDL GVMVPAQKIL DTAVEQDVDV IGLSGLITPS LEEMAHMAKE MQRLGMKLPL LIGGATTSRA HTAVKIEPHY EGPTVWVKDA SRAVGVVQSL ISQNTREEYV AKIRAEYEEV RRHHAERQKE QKWLTLAQAR DNRTPIDWQG YQPPRPRALE AEPAGPGITV LHPFGPDSVV IRFDDYPLED LLDYIDWTPF FHAWQLHAAY PRIFDDEVVG EEAKKLFADA RVMLETIIRE GWLKARGVIG FFPANSVDAD DIELYRDEDR TAPLMRLHHL RQQTERRGKG PNQCLADFIA PRETGLPDYL GGFAVTAGIG IDEHVRRFEQ AHDDYHAIML KALADRLAEA LAERMHERVR REFWGYASDE RLDNEALIKE QYRGIRPAPG YPACPEHTEK GLLWELLKPE ENAGMSITES YAMLPTAAVS GWYFAHPEAR YFNVGKINRD QVADYARRKG MKPAEAERWL APNLGYEPED // ID B8GT09_THISH Unreviewed; 319 AA. AC B8GT09; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=Putative homocysteine/selenocysteine methylase {ECO:0000313|EMBL:ACL73024.1}; GN OrderedLocusNames=Tgr7_1943 {ECO:0000313|EMBL:ACL73024.1}; OS Thioalkalivibrio sulfidiphilus (strain HL-EbGR7). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Thioalkalivibrio. OX NCBI_TaxID=396588 {ECO:0000313|EMBL:ACL73024.1, ECO:0000313|Proteomes:UP000002383}; RN [1] {ECO:0000313|EMBL:ACL73024.1, ECO:0000313|Proteomes:UP000002383} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HL-EbGR7 {ECO:0000313|EMBL:ACL73024.1, RC ECO:0000313|Proteomes:UP000002383}; 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 ----------------------------------------------------------------------- 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; ACL73024.1; -; Genomic_DNA. DR RefSeq; WP_012638503.1; NC_011901.1. DR RefSeq; YP_002514011.1; NC_011901.1. DR STRING; 396588.Tgr7_1943; -. DR EnsemblBacteria; ACL73024; ACL73024; Tgr7_1943. DR KEGG; tgr:Tgr7_1943; -. DR PATRIC; 23963404; VBIThiSp19295_1937. DR eggNOG; COG2040; -. DR OMA; CCGTDHR; -. DR OrthoDB; EOG6R5C46; -. DR BioCyc; TSUL396588:GH5B-1973-MONOMER; -. DR Proteomes; UP000002383; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002383}; KW Methyltransferase {ECO:0000313|EMBL:ACL73024.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002383}; KW Transferase {ECO:0000313|EMBL:ACL73024.1}. SQ SEQUENCE 319 AA; 34449 MW; A51ACDADA103F11D CRC64; MNTDTGFPSE PGSETFLTEG GIETELMYKW GFELPHFAAF PLLEVPKAVD VMRDIYRRCL DVAAAQGLSA MLTGLDYRAS PDWGALLGYS PQGLADANHQ AIEFLRDVAA EYEGDIETTL VGGIVGPRGD AYQLNRDITA AEAEDYHSVQ LSTLRQAGVD YACAMTFNNI EEAVGVARAA AGAGVPLVMS LTVDGTSRLK SGPSLAEAVA AIDEQTDAAP VCYLLNCSHP VEFEPGLETG DWIRRMRGFR PNASKMEKIA LCQLGHLEEG DPEELGRLMG GLAQRYPHMD IWGGCCGTGH VHLEEIARNV RQARESAQA // ID B8HEA2_ARTCA Unreviewed; 319 AA. AC B8HEA2; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 34. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACL39137.1}; GN OrderedLocusNames=Achl_1146 {ECO:0000313|EMBL:ACL39137.1}; OS Arthrobacter chlorophenolicus (strain ATCC 700700 / DSM 12829 / JCM OS 12360 / NCIMB 13794 / A6). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Micrococcaceae; Arthrobacter. OX NCBI_TaxID=452863 {ECO:0000313|EMBL:ACL39137.1, ECO:0000313|Proteomes:UP000002505}; RN [1] {ECO:0000313|EMBL:ACL39137.1, ECO:0000313|Proteomes:UP000002505} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700700 / DSM 12829 / JCM 12360 / NCIMB 13794 / A6 RC {ECO:0000313|Proteomes:UP000002505}; 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 ----------------------------------------------------------------------- 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; ACL39137.1; -; Genomic_DNA. DR RefSeq; WP_015936360.1; NC_011886.1. DR RefSeq; YP_002487226.1; NC_011886.1. DR STRING; 452863.Achl_1146; -. DR EnsemblBacteria; ACL39137; ACL39137; Achl_1146. DR KEGG; ach:Achl_1146; -. DR PATRIC; 20988805; VBIArtChl38304_1801. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; ACHL452863:GH1A-1168-MONOMER; -. DR Proteomes; UP000002505; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002505}; KW Methyltransferase {ECO:0000313|EMBL:ACL39137.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002505}; KW Transferase {ECO:0000313|EMBL:ACL39137.1}. SQ SEQUENCE 319 AA; 33306 MW; 48138AC36232DE6D CRC64; MRIVTIMPAN PTLSALLETG ETLVTDGALA TELEDRGCNL DDPLWSAKVL LEHPGLIRDV HRDYFAAGAR IATTASYQAT PQGFAARGMT EQEALDLVAL SVRLADEARR DHLANQSEAR PLFIAGSVGP YGAYLADGSE YRGDYALTPA EFRDFHRPRL EALVESGADA LACETLPSFA EARALAELTR DLGVESWFSF SLRDAGHISD GTPLAAVAEL LDGESHVAAV GVNCVPLALV APALTALRGG TGKPLVAYPN SGETYDAGTK TWDAAPAATA PAALADGVPA WQALGARIIG GCCRTTPADI SAVAGHVNS // ID B8HGP1_ARTCA Unreviewed; 1214 AA. AC B8HGP1; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 52. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACL41307.1}; GN OrderedLocusNames=Achl_3349 {ECO:0000313|EMBL:ACL41307.1}; OS Arthrobacter chlorophenolicus (strain ATCC 700700 / DSM 12829 / JCM OS 12360 / NCIMB 13794 / A6). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Micrococcaceae; Arthrobacter. OX NCBI_TaxID=452863 {ECO:0000313|EMBL:ACL41307.1, ECO:0000313|Proteomes:UP000002505}; RN [1] {ECO:0000313|EMBL:ACL41307.1, ECO:0000313|Proteomes:UP000002505} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700700 / DSM 12829 / JCM 12360 / NCIMB 13794 / A6 RC {ECO:0000313|Proteomes:UP000002505}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001341; ACL41307.1; -; Genomic_DNA. DR RefSeq; WP_015938501.1; NC_011886.1. DR RefSeq; YP_002489396.1; NC_011886.1. DR STRING; 452863.Achl_3349; -. DR EnsemblBacteria; ACL41307; ACL41307; Achl_3349. DR KEGG; ach:Achl_3349; -. DR PATRIC; 20993335; VBIArtChl38304_4030. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; ACHL452863:GH1A-3407-MONOMER; -. DR Proteomes; UP000002505; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002505}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002505}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 240 240 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 768 768 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1214 AA; 131872 MW; 97AB4004240111B6 CRC64; MPRFALDIES VARPVRAQAL LDAVNHRVVI ADGAMGTMLQ GRDLSLETDF QNLEGCNEIL NDTRPDVIAD IHDAYFATGI DAVETNTFGA NWSNLSDYGI DDRIEELANK GARIARQRAE AAEETDGRMR WVLGSMGPGT KLPSLGHTTY DHLKQTFALQ AEGLIDGGAD AFLIETSQDL LQTKAAVNGC RQAIVSKGIR LPIFVEVTVE TTGTMLMGSE IGAALTALEP LGVDAIGLNC ATGPDEMSEH LRHLSKQSTV AIACMPNAGL PVLGPNGAHY PLSPAELATA HEQFVREFGL GLVGGCCGTT PEHLAAVVER LAPFRAKAVE TEDKTAPARI PTEREAGIAS LYHHVNFDQE SAYLAIGERT NANGSKAFRQ AMLEERWDDC VDIAREQVRV GAHLLDVCID YVGRDGVADI KEIVSRFASA STLPLVIDST EPPVLQAGLE LIGGRPVVNS VNYEDGDGPT SRFARIMPLV KEHGTAVIAL TIDEQGQART TDGKVAIASR LVDSLVNDWG MRVEDIIVDA LTFPVATGQE ETRRDGIETI EAIRQITTKY PGINTTLGVS NVSFGLNPAA RMVLNSVFLH EAVQAGLTSG IIDAAKIVPL ASLPEEQRKV ALDLVYDRRE YDADGNVTYD PLAIMLDLFA GVDTAALKDQ RAAELAALPT GERLQRRIID GEGKGLEADL DLARSEGMSP LSIINDQLLE GMKVVGERFG AGEMQLPFVL QSAEVMKNAV ALLEPHMEKS DSSGKGTMVI ATVRGDVHDI GKNLVDIILT NNGYNVINIG IKQGIAEIIA AAEEHDADVI GMSGLLVKST VVMKDNLAEL QSRGLAKKWP VILGGAALTR AYVEQDLAEQ FEGTVRYAKD AFEGLALMEP LVRVARGEDP NSVGLPPLKK RIHRSGPTFT VTEPEAMPGR SDVVADNAVP APPFWGTRIV RGVALNDYAS FLDERATFMG QWGLKPGRGE DGASYEELVE REGRPRLRYW LDRILGEGML DASVAYGYFP VVTEGEDVVV LHHGEDRDGV LGAAGLLAPD GGSGGSIGTE RLRFSFPRQR RDRHLCLADF VRSRESGQID VLPVQLVTAG SKIEEFTSKM FAANQYRDYY ELNGLVMQLT ESLAEFWHSR IRKELGFAAE EPKDKAGLFK LDYRGARFSL GYPACPDMED RRKVVELLKP ERMGVILSDE LMLHPEQSTD AFVFHHPEAK YFKV // ID B8HJU0_CYAP4 Unreviewed; 328 AA. AC B8HJU0; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 01-APR-2015, entry version 29. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACL45043.1}; GN OrderedLocusNames=Cyan7425_2696 {ECO:0000313|EMBL:ACL45043.1}; OS Cyanothece sp. (strain PCC 7425 / ATCC 29141). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Cyanothece. OX NCBI_TaxID=395961 {ECO:0000313|EMBL:ACL45043.1, ECO:0000313|Proteomes:UP000002511}; RN [1] {ECO:0000313|Proteomes:UP000002511} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7425 / ATCC 29141 {ECO:0000313|Proteomes:UP000002511}; 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 ----------------------------------------------------------------------- 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; ACL45043.1; -; Genomic_DNA. DR RefSeq; WP_012628115.1; NC_011884.1. DR RefSeq; YP_002483404.1; NC_011884.1. DR STRING; 395961.Cyan7425_2696; -. DR EnsemblBacteria; ACL45043; ACL45043; Cyan7425_2696. DR KEGG; cyn:Cyan7425_2696; -. DR PATRIC; 21566347; VBICyaSp30657_2683. DR eggNOG; COG2040; -. DR HOGENOM; HOG000179103; -. DR OMA; CCGTDHR; -. DR OrthoDB; EOG6R5C46; -. DR BioCyc; CSP395961:GJDE-2525-MONOMER; -. DR Proteomes; UP000002511; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002511}; KW Methyltransferase {ECO:0000313|EMBL:ACL45043.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002511}; KW Transferase {ECO:0000313|EMBL:ACL45043.1}. SQ SEQUENCE 328 AA; 36293 MW; 2C1321E721042B3E CRC64; MAQYRNNLPQ LSSDLFITDG GIETTLIFRE GLELPEFAAF DLFKSASGYQ ALQKYFRTYA RMASTYAVGC ILESATWRAN PDWGTKLGYD RDALTAVNGQ AIALLHEIRH EFETEQSRMV ISGCLGPRGD GYIPADAMSE TEAEFYHRPQ IETFRQAGAD LVTAITMNYV EEAIGIARGA KTVGIPVVIS FTVETDGKLP TGQPLKEAIA QVDKATDAAP AYYMLNCAHP THFMDELRTG ETWVERIRGI RANASTKSHA ELNESETLDE GNPAELGSLY QQLREHLPHL NVLGGCCGTD DRHIEAICKA CLPVLWAHRS PQTLMQFV // ID B8HR05_CYAP4 Unreviewed; 1212 AA. AC B8HR05; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 01-APR-2015, entry version 50. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACL45826.1}; GN OrderedLocusNames=Cyan7425_3503 {ECO:0000313|EMBL:ACL45826.1}; OS Cyanothece sp. (strain PCC 7425 / ATCC 29141). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Cyanothece. OX NCBI_TaxID=395961 {ECO:0000313|EMBL:ACL45826.1, ECO:0000313|Proteomes:UP000002511}; RN [1] {ECO:0000313|Proteomes:UP000002511} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7425 / ATCC 29141 {ECO:0000313|Proteomes:UP000002511}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001344; ACL45826.1; -; Genomic_DNA. DR RefSeq; WP_012628886.1; NC_011884.1. DR RefSeq; YP_002484187.1; NC_011884.1. DR STRING; 395961.Cyan7425_3503; -. DR EnsemblBacteria; ACL45826; ACL45826; Cyan7425_3503. DR KEGG; cyn:Cyan7425_3503; -. DR PATRIC; 21567959; VBICyaSp30657_3483. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; TWTFPRQ; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CSP395961:GJDE-3334-MONOMER; -. DR Proteomes; UP000002511; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002511}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002511}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 228 228 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 762 762 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1212 AA; 134307 MW; D5D76A19B86758D4 CRC64; MVNSFLARLH HPDRPVLVFD GAMGTNIQTQ NLTAEDFGGP QYEGCNEYLV HTKPEAIAKV HRDFLAAGAD VIETDTFGSS PLVLAEYDLA DQSYYLSKTA AELAKQCAAE FSTPEKPRFV AGSIGPGTKL PTLGHINYDQ LKAAFTVQAE GLFDGGVDLF IIETCQDVLQ IKAALNAVEA VFEQKGERRP LMVSVTMEVQ GTMLVGTDIS GVLAILEPYP IDILGLNCAT GPDRMADHIK YLTENAPFVV SCIPNAGLPE NIGGHAHYKL TPMELRLALH RFVEDWGVQV IGGCCGTRPA HIQALAEIAQ SLQPKARNVR VGEQTWLNGS LHPIDTPRPT LNYTPAAASI YTAQPYEQDN SFLIVGERLN ASGSKKVREL LNADDWDGLI AIAKAQVKEG AHVLDVNVDY VGRNGERDMH ELVSRLVTNI TLPLMLDSTE WQKMEAGLKV AGGKCILNST NYEDGPERFF KVLELAKTYG AGVVIGTIDE EGMARTAERK FQIAQRAYRD AVEFGLPPHE LFFDTLALPI STGIEEDREN GKATIEAIRR IRAELPGVHF MLGVSNISFG LSPAARITLN SMFLHEAMQV GMDGAIVSAA KILPLSKISE DHQQVCQDLI YDRRRFEGDI CIYDPLTQLT TLFEGVSAKE ARSSSSLADL PIEERLKQHI IDGERIGLEA ALKIALETYK PLEIINTFLL DGMKVVGELF GSGQMQLPFV LQSAETMKAA VAFLEPLMDK VEGQGDSGKG KFLIATVKGD VHDIGKNLVD IILTNNGYKV INLGIKQPVD AIIDAYTQHQ PDCIAMSGLL VKSTAFMKEN LEVFNQRGIT VPVILGGAAL TPKFVYEDCQ QTYNGQVIYG RDAFADLTFM DRLMPAKTQG KWSDREGFQA DLAHYNQKGR QAIDAAEREL NPTKPEKATT TDVVDTVRSE AVELNIPRPT PPFWGSQILN PADIDLEEVF RYLDLQALVS GQWQFRKPQG QSREEYDTFL AEKVYPILDS WQQRIIDEKL LHPQLVYGYF PCVAEGNSVH LYDPAVIAQG LTPQTATAIV TWTFPRQKSM RRLCIADFFR PITENQFDVF PMQAVTVGQI ATEFAQQLFA ENLYTDYLYF HGLAVQTAEA LAEWCHVRIR RELGYGDLEP EHIRDILAQR YQGSRYSFGY PACPNVADQF KQLELLATDR IGMSIDDSEQ LYPEQSTTAI ITYHPIAKYF SA // ID B8HZC5_CYAP4 Unreviewed; 328 AA. AC B8HZC5; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 01-APR-2015, entry version 28. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACL47773.1}; GN OrderedLocusNames=Cyan7425_0064 {ECO:0000313|EMBL:ACL47773.1}; OS Cyanothece sp. (strain PCC 7425 / ATCC 29141). OG Plasmid pP742502 {ECO:0000313|EMBL:ACL47773.1, OG ECO:0000313|Proteomes:UP000002511}. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Cyanothece. OX NCBI_TaxID=395961 {ECO:0000313|EMBL:ACL47773.1, ECO:0000313|Proteomes:UP000002511}; RN [1] {ECO:0000313|Proteomes:UP000002511} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7425 / ATCC 29141 {ECO:0000313|Proteomes:UP000002511}; 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001346; ACL47773.1; -; Genomic_DNA. DR RefSeq; WP_012630633.1; NC_011885.1. DR RefSeq; YP_002485974.1; NC_011885.1. DR STRING; 395961.Cyan7425_0064; -. DR EnsemblBacteria; ACL47773; ACL47773; Cyan7425_0064. DR KEGG; cyn:Cyan7425_0064; -. DR PATRIC; 21571678; VBICyaSp30657_5325. DR eggNOG; COG2040; -. DR HOGENOM; HOG000179103; -. DR OMA; NTEDGRQ; -. DR OrthoDB; EOG6R5C46; -. DR BioCyc; CSP395961:GJDE-5347-MONOMER; -. DR Proteomes; UP000002511; Plasmid pP742502. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002511}; KW Methyltransferase {ECO:0000313|EMBL:ACL47773.1}; KW Plasmid {ECO:0000313|EMBL:ACL47773.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002511}; KW Transferase {ECO:0000313|EMBL:ACL47773.1}. SQ SEQUENCE 328 AA; 36238 MW; 5EE2CD5D6F8D9247 CRC64; MAQYRNNLPQ LSSDLFITDG GIETTLIFRE GLELPEFAAF DLFKSASGYQ ALQKYFRTYA RMASTYAVGC ILESATWRAN PDWGTKLGYD RDALTAVNGQ AIALLHEIRH EFETEQSRLV ISGCLGPRGD GYIPADAMSE TEAEFYHRPQ IETFRQAGAD LVTAITMNYV EEAIGIARGA KTVGIPVVIS FTVETDGKLP TGQPLKEAIA QVDKATDAAP AYYMLNCAHP THFMDELRTG ETWVERIRGI RANASTKSHA ELNESETLDE GNPAELGSLY QQLREHLPHL NVLGGCCGTD DRHIEAICKA CSPVLWSYLS NRFFSVAI // ID B8I366_CLOCE Unreviewed; 434 AA. AC B8I366; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 01-APR-2015, entry version 31. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACL76209.1}; GN OrderedLocusNames=Ccel_1861 {ECO:0000313|EMBL:ACL76209.1}; OS Clostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / OS H10). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=394503 {ECO:0000313|EMBL:ACL76209.1, ECO:0000313|Proteomes:UP000001349}; RN [1] {ECO:0000313|EMBL:ACL76209.1, ECO:0000313|Proteomes:UP000001349} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35319 / DSM 5812 / JCM 6584 / H10 RC {ECO:0000313|Proteomes:UP000001349}; 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 ----------------------------------------------------------------------- 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; ACL76209.1; -; Genomic_DNA. DR RefSeq; WP_015925314.1; NC_011898.1. DR RefSeq; YP_002506189.1; NC_011898.1. DR STRING; 394503.Ccel_1861; -. DR EnsemblBacteria; ACL76209; ACL76209; Ccel_1861. DR KEGG; cce:Ccel_1861; -. DR PATRIC; 19434623; VBICloCel57783_1917. DR eggNOG; COG0646; -. DR HOGENOM; HOG000269747; -. DR KO; K00548; -. DR OMA; GTNLFAM; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CCEL394503:GJET-1903-MONOMER; -. DR Proteomes; UP000001349; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001349}; KW Methyltransferase {ECO:0000313|EMBL:ACL76209.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001349}; KW Transferase {ECO:0000313|EMBL:ACL76209.1}. SQ SEQUENCE 434 AA; 46865 MW; C25B6833BEC458F8 CRC64; MSFLNDIEKK VLVFDGSMGI MLQSKGLEVG TCPEEWNITH PEMVKEIYTA YRDAGANVIQ SNTFQSNLMK LSEYGLQDKH YDINFAGVSL AKEVMGDKGY VAASIGPLGK LLEPFGELTF EQAYNTFKEQ VVAVTAGGAD IISFETFTDV SEMRIALLAS KENCNLPVIC SISYEQNGRT LMGSDPAVCA CILHSLGADM IGTNCSFGPE YMIKVAESYG KTGLKFSIKP NAGIPKTVDG NLVYDETPEK FAEYAQEFIK YGARLVGGCC GTRPEFIAEI SKAVSGCDAV SFPLNVDFIT SSSKAVAFSD IMGAGIGWID INKEETLKKE LLAGSISTIT DAAMDLMEED CELIAIDVDV PGENELLLSY VVKEAQTYLK QPFILKSNNP SALEAALRIY KGKAGVLTNN SSDVAGIMNK YGAVNVGGFI SNEK // ID B8I637_CLOCE Unreviewed; 615 AA. AC B8I637; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 41. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=Ccel_2474 {ECO:0000313|EMBL:ACL76802.1}; OS Clostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / OS H10). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=394503 {ECO:0000313|EMBL:ACL76802.1, ECO:0000313|Proteomes:UP000001349}; RN [1] {ECO:0000313|EMBL:ACL76802.1, ECO:0000313|Proteomes:UP000001349} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35319 / DSM 5812 / JCM 6584 / H10 RC {ECO:0000313|Proteomes:UP000001349}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ACL76802.1; -; Genomic_DNA. DR RefSeq; WP_015925891.1; NC_011898.1. DR RefSeq; YP_002506782.1; NC_011898.1. DR ProteinModelPortal; B8I637; -. DR STRING; 394503.Ccel_2474; -. DR EnsemblBacteria; ACL76802; ACL76802; Ccel_2474. DR KEGG; cce:Ccel_2474; -. DR PATRIC; 19435925; VBICloCel57783_2551. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; CCEL394503:GJET-2530-MONOMER; -. DR Proteomes; UP000001349; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001349}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000001349}. SQ SEQUENCE 615 AA; 68091 MW; 78ADB4DA652E6DCF CRC64; MTALSTKSII IAMKGGLSTR LIKRKRKGKE DMNIFSNRDY FLFDGAIGTY YSLKYRSNTP CELANINERE NIFNIHSEYI QAGVNAIKTN TFSANRFSLG CNQSEVEKII KSGYDIAVQA CSGQEVVVFA DIGPIPDEKG INPKEEYIKI VDIFLECGAK NFLFETFANT DILIGVAAYI RLRLPEAVVV TSFAVYPDGY SKEGLFYVDL MDKMYASGLV DAVGLNCISG PAHMYRLIKK ADIRGKSIII MPNSGYPGSE RGRTVYSDNS EYYAEKLLDL KNLGVKIFGG CCGTTPKHIA AAAQLLSRNP TKTDAQSKTH IETCNLANEN ILDKLVKTKK PILVEVDPPF DTNWEYMLRD TLLLKQAGAD IITIADSPLA KARAESTIMA AKIQREAVIP VMPHITCRDK NLLGIKASLL GVHIEGIRNV LVITGDPIAN IERSRIKGVF SFNSSNLANY IKSLNSNVFC GQEIKIAGAL NVNAVNFSAE LKKAFTKIEN GISCLLTQAI YTKSAVDNLL KAVETLKVPI FAGFMPIVGY KNALFIDNEV PGIDIDNETI EKFRDKSREE SEKLGMEITM DILKEIYPHV SGIYLMTPLK RTNVICELIK KIKEI // ID B8IH83_METNO Unreviewed; 1248 AA. AC B8IH83; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 52. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACL59775.1}; GN OrderedLocusNames=Mnod_4918 {ECO:0000313|EMBL:ACL59775.1}; OS Methylobacterium nodulans (strain ORS2060 / LMG 21967). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=460265 {ECO:0000313|EMBL:ACL59775.1, ECO:0000313|Proteomes:UP000008207}; RN [1] {ECO:0000313|EMBL:ACL59775.1, ECO:0000313|Proteomes:UP000008207} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ORS2060 / LMG 21967 {ECO:0000313|Proteomes:UP000008207}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001349; ACL59775.1; -; Genomic_DNA. DR RefSeq; WP_015931404.1; NC_011894.1. DR RefSeq; YP_002500078.1; NC_011894.1. DR ProteinModelPortal; B8IH83; -. DR SMR; B8IH83; 660-908. DR STRING; 460265.Mnod_4918; -. DR EnsemblBacteria; ACL59775; ACL59775; Mnod_4918. DR KEGG; mno:Mnod_4918; -. DR PATRIC; 22551672; VBIMetNod76414_5534. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; MNOD460265:GCZK-4970-MONOMER; -. DR Proteomes; UP000008207; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008207}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008207}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 254 254 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 318 318 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 770 770 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1248 AA; 136250 MW; CB58DC6676B2BF81 CRC64; MTDFRPADGA DVLATLRKRA AERILVLDGA MGTMIQRLKL GEADFRGKRF MDHPHDQKGN NDLLILTQPD AIRQIHLDYF LAGADVAETN TFSGTVIAQA DYGMEAIVRE LNREGARLAR EAAAEAERRD GRRRFVAGAV GPTNRTLSIS PDVNNPGYRA VTFDQVRDAY AEQVRGLIEG GSDLVLIETI FDTLNAKAAI AATWQVFGEM GVRLPIMISG TITDLSGRTL SGQTPTAFWH SLRHAEPLTF GLNCALGARE MRAHISELSR VCDTLVCAYP NAGLPNEFGL YDESPEAMAA LVGEFAGSGL VNMVGGCCGT TPDHIRAIAE AVAGKAPRRV PEVPRLMRLS GLEPFTLTKE IPFVNVGERT NVTGSAKFRK LITNGDYAAA LDVARDQVAA GAQVIDVNMD EGLLDSAAAM VEFLNLVAAE PDIARVPVMV DSSKFAVIEA GLKCIQGKPI VNSISLKEGE EKFIHEAKVC RSYGAAVVVM AFDEKGQADT LARKVEICTR AYRILTDEVG FPPEDIVFDP NIFAVATGIE EHDGYGVAFI EAARQIRQTL PHAHISGGVS NLSFAFRGNE PVREAMHAVF LYHAIHAGMD MGIVNAGQLA VYDELDPELR DLCEDVVLNR RSDATERLLE QAARFKEGGG AQVRTADLAW REAPVEKRLE HALVNGITEY IEADTEEARA KAARPLDVIE GPLMAGMNVV GDLFGSGKMF LPQVVKSARV MKQAVAYLMP FMEAEKQANG GVGRQAAGKV LMATVKGDVH DIGKNIVGVV LACNNYEIID LGVMVPAAKI LDTARKEKVD IVGLSGLITP SLDEMVHVAS EMEREGFDVP LLIGGATTSR VHTAVKIHPA YARGQAVYVT DASRAVGVVS SLLSPETRVT TIESVRAEYK RVAEAHTRAE ADKQRLPLSR ARANAFKADF ASYRPAKPTF TGTRVFRTYD VAELVPYIDW TPFLQTYEFK GRFPAILEDP VQGPAARALF DDAQAMLARI VEERWFNPKA VIGFWPANAV GDDIRLFTGE SRSERLATFH GLRQQLSKRD GRPNTCLSDF VAPLESGVAD YVGGFVVTAG LEEVRIAERF ERQNDDYRSI LVKALADRIA EAFAERMHER VRREFWAYAP DEACTPDDLV AEAYQGIRPA PGYPAQPDHT EKATLFDLLQ AEPRIGVKLT ESYAMWPGSS VSGLYLAHPE AHYFGVAKVE RDQVEDYAAR KGMAVAEVER WLGPILNYDP ARHLAAAE // ID B8IIJ1_METNO Unreviewed; 312 AA. AC B8IIJ1; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 29-APR-2015, entry version 34. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACL59868.1}; GN OrderedLocusNames=Mnod_5017 {ECO:0000313|EMBL:ACL59868.1}; OS Methylobacterium nodulans (strain ORS2060 / LMG 21967). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=460265 {ECO:0000313|EMBL:ACL59868.1, ECO:0000313|Proteomes:UP000008207}; RN [1] {ECO:0000313|EMBL:ACL59868.1, ECO:0000313|Proteomes:UP000008207} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ORS2060 / LMG 21967 {ECO:0000313|Proteomes:UP000008207}; 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; ACL59868.1; -; Genomic_DNA. DR RefSeq; WP_015931496.1; NC_011894.1. DR RefSeq; YP_002500171.1; NC_011894.1. DR STRING; 460265.Mnod_5017; -. DR EnsemblBacteria; ACL59868; ACL59868; Mnod_5017. DR KEGG; mno:Mnod_5017; -. DR PATRIC; 22551852; VBIMetNod76414_5623. DR eggNOG; COG2040; -. DR HOGENOM; HOG000179103; -. DR OMA; CCGTDHR; -. DR OrthoDB; EOG6R5C46; -. DR BioCyc; MNOD460265:GCZK-5070-MONOMER; -. DR Proteomes; UP000008207; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008207}; KW Methyltransferase {ECO:0000313|EMBL:ACL59868.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008207}; KW Transferase {ECO:0000313|EMBL:ACL59868.1}. SQ SEQUENCE 312 AA; 33688 MW; 4018A2CA4EE4027A CRC64; MPQFRNSLPQ LTGRPFLTEG GVATTLKFRE NIDLPDGARF PLLNSAEGRG ALTRCFEPYL ELARRYRVGL ILDTPTWRAN ADWGAKLGYD ADALAEVNRA AVGFVDALRR QHAEPDLPLV LNGVIGPRGD GYTAEATMSA EDAAAYHRPQ IEVFQNSEAD MVSAHTLTFV DEAIGIAMAA RDAKMPLAIS FTLETDGHLP SGQTLGSAIE ETDAATGAYP AYYMIGCTHP LHFEPALTRD ASWLARIRGV RANASTKSHA DLDGASDLDS GDPQDLGHRY ATLRGRLPNL NVLGGCCGTD HRHIEAICEA CL // ID B8J0R7_DESDA Unreviewed; 802 AA. AC B8J0R7; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 01-APR-2015, entry version 36. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACL49344.1}; GN OrderedLocusNames=Ddes_1442 {ECO:0000313|EMBL:ACL49344.1}; OS Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=525146 {ECO:0000313|EMBL:ACL49344.1, ECO:0000313|Proteomes:UP000002598}; RN [1] {ECO:0000313|EMBL:ACL49344.1, ECO:0000313|Proteomes:UP000002598} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27774 / DSM 6949 {ECO:0000313|Proteomes:UP000002598}; 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 ----------------------------------------------------------------------- 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; ACL49344.1; -; Genomic_DNA. DR RefSeq; WP_012625068.1; NC_011883.1. DR RefSeq; YP_002480022.1; NC_011883.1. DR STRING; 525146.Ddes_1442; -. DR EnsemblBacteria; ACL49344; ACL49344; Ddes_1442. DR KEGG; dds:Ddes_1442; -. DR PATRIC; 21736642; VBIDesDes50650_1671. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; DDES525146:GIWF-1487-MONOMER; -. DR Proteomes; UP000002598; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002598}; KW Methyltransferase {ECO:0000313|EMBL:ACL49344.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002598}; KW Transferase {ECO:0000313|EMBL:ACL49344.1}. SQ SEQUENCE 802 AA; 84334 MW; C9C97851794BF777 CRC64; MTFRQALGSG RPLLLDGAMG TMLQASGLPA GTSPEEFCME NPDILRGIHA SYLKAGVDLL TSCTFGGNAY KLSKNLDVFS FNKRMASVAR AAAADVSRPD GRPIFVAGNV GPTGHFAKPL GPVEPAELIE VFAQQIRGLV AGGADLVFIE TQFDLAEARA AVVAARQVCD LPVMVSMTFE QGVSLTGSTP AIFAETMQNM GVDVVGTNCS LGPEQMEPVV AELLGVCACP VMAEPNAGLP ELRGTQTVFP LGPEDFARKT ASFAHMGAQV LGGCCGTTPE HLAALAHSLR GLGEVRPTGV KRSGICLTSR SQMVRIGAGR PLAIIGERIN PTGKKQLTLE LQEGRFDTAL QFADAQIEAG ATVLDVNVGA PLVDETALLP DLVQRLVGRL TVPLSLDSSN AQAIAAALPY CPGSFLVNSI SGEEGRMELL GPLCRDYGAP FILLPLEGAT LPEKAVERIR TVESLLLRAE RLGIPRRLMM VDILALAVSS SPDGARQCLE MTRWCAEQGL PTTLGLSNLS FGLPARDLLN ATFLAYAAGA GLSSCIANPS AQRLREAADA LKVLGEHDPH ASSFISSYAN WKPGEGSVLQ RQGGGGASKS LGEAVLNGDR ENVLSLLEAE LAAGAEPFSL VQEVLIPAIT EVGARYERRE YFLPQLIRAA ETMQTAFGHL KPRLEAGRGA EERPVVIMAT VEGDIHDIGK NIVSLLLGNH GFDVIDAGKD VPAEDIVACA LEHNARIIGL SALMTTTMVR MEDTIKLVKE KGLAIKVMVG GAAVTQAFAD AIGADAYCAD AVGAVRAAKN FM // ID B8J7W9_ANAD2 Unreviewed; 1150 AA. AC B8J7W9; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 48. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACL63461.1}; GN OrderedLocusNames=A2cp1_0102 {ECO:0000313|EMBL:ACL63461.1}; OS Anaeromyxobacter dehalogenans (strain 2CP-1 / ATCC BAA-258). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter. OX NCBI_TaxID=455488 {ECO:0000313|EMBL:ACL63461.1, ECO:0000313|Proteomes:UP000007089}; RN [1] {ECO:0000313|Proteomes:UP000007089} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2CP-1 / ATCC BAA-258 {ECO:0000313|Proteomes:UP000007089}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001359; ACL63461.1; -; Genomic_DNA. DR RefSeq; WP_012631549.1; NC_011891.1. DR RefSeq; YP_002490527.1; NC_011891.1. DR ProteinModelPortal; B8J7W9; -. DR STRING; 455488.A2cp1_0102; -. DR EnsemblBacteria; ACL63461; ACL63461; A2cp1_0102. DR KEGG; acp:A2cp1_0102; -. DR PATRIC; 20906987; VBIAnaDeh28364_0097. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; ADEH455488:GH35-104-MONOMER; -. DR Proteomes; UP000007089; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007089}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 733 733 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1150 AA; 124696 MW; 283F4E15196A443C CRC64; MNFREALERR PLVFDGAMGT QIQRHQLTAA EFGGKEGAND LLTLTRPDLI EEIHARYFAV GCDVVETNTF GSSRLKLDEY GLGHRTYEVN CRAAILARRA ADRYSTPDHP RFVAGSIGPT GMLPSSSDPA LGNITSDALE RIFFEQAKGL VEGGVDALII ETQQDMLELR AAVLACDAVR REALRDVFVI AQPTLIDANG RMLLGTDIGS AVATLERLPV DAVGLNCSTG PDEMRASVKA LAEKCSHFVS VLPNAGMPEN VDGRAVYKLS PDDLARALVG FVAEYGVDIV GGCCGTTPEH LRKVVEALRA RPAPRRRRPA PAAELSSAMK AVPLAMEPRP LVVGERLNSQ GSRKVKELLL ADDYAGLVQI ARGQVEAGAH VLDVCVALNE RDDEAAQMRT LAKLLAQSVD APLMIDSTEP DVIEGALKVY PGRCIVNSVN LEKSGERVRR VLPLVRRYGA AVVAMTIDEK GMAQTAERKA EVARRIVAVA KDHGIPPDSL VFDALTFTLA TGGEEYRRSA VETLEGIRRI KAENPGVLTT LGVSNVSFGL AKSAREVVNS VFLYHAVQAG LDLAIVNPKD ILPYPAIDAA ERALAEDLVF DRRPDALARL IAHFGAKGAP EKAAVDPLAG AGGKSAEERI HLQILHRRPE GIEALIDEAL TRRSAVDVLN QVLLPAMKDV GDRFGAGELI LPFVLQSAEV MKKAVAHLEQ FLEKKAGATK GNVVLATVYG DVHDIGKNLV KTILSNNGFT VHDLGKQVPV ATVLDKALQV NADAIGLSAL LVSTSKQMPF CVEELHRRNL SFPVIIGGAA INRRFGYRTH FAQDGTPYAG GVFYAKDAFE GLEVVEALVD PARREALRRE VLQKAVAEKS RPAAEPVAQA PARRTGSVAP AARVPAPPFW GPRVVPSGSI ALADVWPHLD LAELFKLQWG VKAKGAEYER LIREEFGPKL EELKAEAQAQ GWLVPKVVYG YFPCHAEGND LVVLDPAHRK AEVARLQFPR QPDDRNLCLA DYFREERGAD VCALQVVTVG DQATHLAEQA QERGDYTRAL FLHGLAVETA EALAEYWHRQ VRGELGLADG QGKRYSPGYP SWPELSDQRQ VWKLLDPVRT IGVSLTDACQ MVPEQSTSAI VLHHPDAIYF LVRGLERAAG // ID B8J988_ANAD2 Unreviewed; 286 AA. AC B8J988; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 31. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACL65494.1}; GN OrderedLocusNames=A2cp1_2154 {ECO:0000313|EMBL:ACL65494.1}; OS Anaeromyxobacter dehalogenans (strain 2CP-1 / ATCC BAA-258). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter. OX NCBI_TaxID=455488 {ECO:0000313|EMBL:ACL65494.1, ECO:0000313|Proteomes:UP000007089}; RN [1] {ECO:0000313|Proteomes:UP000007089} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2CP-1 / ATCC BAA-258 {ECO:0000313|Proteomes:UP000007089}; 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 ----------------------------------------------------------------------- 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; ACL65494.1; -; Genomic_DNA. DR RefSeq; WP_012633344.1; NC_011891.1. DR RefSeq; YP_002492560.1; NC_011891.1. DR ProteinModelPortal; B8J988; -. DR STRING; 455488.A2cp1_2154; -. DR EnsemblBacteria; ACL65494; ACL65494; A2cp1_2154. DR KEGG; acp:A2cp1_2154; -. DR PATRIC; 20911204; VBIAnaDeh28364_2191. DR HOGENOM; HOG000265278; -. DR KO; K00548; -. DR OMA; VLTCTFN; -. DR BioCyc; ADEH455488:GH35-2176-MONOMER; -. DR Proteomes; UP000007089; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007089}; KW Methyltransferase {ECO:0000313|EMBL:ACL65494.1}; KW Transferase {ECO:0000313|EMBL:ACL65494.1}. SQ SEQUENCE 286 AA; 28029 MW; C19B5AC8ED0DDFB2 CRC64; MTPASPRPFD GPTLLDGAMG TALLAGGLPA GTLPEAWVLE RPEAVAAVHA AHAAAGAEVV LTCTFNAAGP RLDPLVPPDR VGALCAAAVR LARRAAPGAR VAGDLGPTAL YGPGRPPPDG AAVRARYARA AGALAAAGAD LLWAESQWDL AEARLALDAA RATGLPVVVT FALREAAGRL AAPDGTPAEE LLEAVADAGA AAAGVNCVPP GPALAALAAW AARRLAVRFV AKPSPGLPGE VLGPDAFAEA LRPAVHAGLG VAGGCCGAGP GHLAALRRLL AAARAG // ID B8K630_9VIBR Unreviewed; 297 AA. AC B8K630; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EED27761.1}; GN ORFNames=VPMS16_1168 {ECO:0000313|EMBL:EED27761.1}; OS Vibrio sp. 16. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=391586 {ECO:0000313|EMBL:EED27761.1}; RN [1] {ECO:0000313|EMBL:EED27761.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=16 {ECO:0000313|EMBL:EED27761.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999329; EED27761.1; -; Genomic_DNA. DR RefSeq; WP_005470733.1; NZ_DS999329.1. DR EnsemblBacteria; EED27761; EED27761; VPMS16_1168. DR PATRIC; 28333492; VBIVibPar22686_0999. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EED27761.1}; KW Transferase {ECO:0000313|EMBL:EED27761.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 202 202 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 277 277 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 278 278 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 297 AA; 32010 MW; 21BAF32F5EA197E5 CRC64; MLTILDGGMG RELKRVDAPF SQPLWSAQAL LESPQHVTQV HQSFVQAGAE IIITNAYACV PFHLGDERFQ QQGAALARSA ATIARKVADN HKGVLVAGCL PPALGSYRPD LFDVAKATPI LETLIQAQVP YIDLWMVETL ASIKEFETNH GLLSNCDKPC HYAFTLMDEP QGKNAQLRSG ETVTDAALKV AESGASGMLF NCSIPEVLEQ AVIDAKAIFD QNGAKITIGA YANNFDIITP DHQANGSLQS IRALTPEDYL EFAKAWQQAG AEIIGGCCGI GPEYIQVLAE WKTKGAI // ID B8KDU5_9VIBR Unreviewed; 1226 AA. AC B8KDU5; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 01-APR-2015, entry version 38. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EED24993.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EED24993.1}; GN Name=metH {ECO:0000313|EMBL:EED24993.1}; GN ORFNames=VPMS16_794 {ECO:0000313|EMBL:EED24993.1}; OS Vibrio sp. 16. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=391586 {ECO:0000313|EMBL:EED24993.1}; RN [1] {ECO:0000313|EMBL:EED24993.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=16 {ECO:0000313|EMBL:EED24993.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; DS999370; EED24993.1; -; Genomic_DNA. DR RefSeq; WP_005476230.1; NZ_DS999370.1. DR EnsemblBacteria; EED24993; EED24993; VPMS16_794. DR PATRIC; 28339243; VBIVibPar22686_3773. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EED24993.1}; KW Transferase {ECO:0000313|EMBL:EED24993.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1226 AA; 136633 MW; 2FD1CE3DAE8B3E8D CRC64; MGSNVRQQIE AQLKQRILLI DGGMGTMIQG YKLEEQDYRG ERFADWHCDL KGNNDLLVLT QPQLIKEIHC AYLEAGADIL ETNTFNATTI AMADYEMESL SEEINFAAAK LAREAADEWT AKTPERPRYV AGVLGPTNRT CSISPDVNDP GYRNVSFDEL VEAYSESTRA LIKGGSDLIL IETIFDTLNA KACAFAVDSV FEELGIELPV MISGTITDAS GRTLSGQTTE AFYNSLRHVN PISFGLNCAL GPDELRPYVE ELSRISESFV STHPNAGLPN AFGEYDLSPE DMAEHVKEWA ESGFLNLIGG CCGTTPEHIR HMAMAVEGVK PRDLPELTVA CRLSGLEPLT IEKETLFINV GERTNVTGSA RFKRLIKEEL YDEALEVARQ QVENGAQIID INMDEGMLDA EACMVRFLNL CASEPEISKV PIMVDSSKWE VIEAGLKCIQ GKGIVNSISL KEGKEKFVEQ AKLIRRYGAA VIVMAFDEVG QAETRERKLE ICTNAYRILV DEVGFPPEDI IFDPNIFAVA TGIEEHNNYA VDFIEAVADI KRDLPHAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK NGMDMGIVNA GQLEIYDNVP DKLREAVEDV VLNRRDDSTE RLLDIAAEYA GKGVGKEEDA SALEWRTWTV EKRLEHALVK GITEFIVEDT EEARLNASKP LEVIEGPLMD GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AHLEPFINKE KQVGSSNGKI LLATVKGDVH DIGKNIVGVV LQCNNYEIID LGVMVPCEKI LKVAKEENVD IIGLSGLITP SLDEMVHVAK EMERLDFDLP LLIGGATTSK AHTAVKIEQN YKHPVVYVNN ASRAVGVCTS LLSDELRPSF VEKLDVDYER VRDQHNRKKP RTKPVTLEEA RANKAAIDWD KYTPPAPVKP GIHIFDDFEV STLRKYIDWT PFFMTWSLVG KYPTIFDHEE VGEEAQRLYK DANELLDRVE REGLLKARGM CGLFPAASVG DDIEVYTDES RTEVAKVLHN LRQQTEKPKG FNYCLSDYVA PKESGKRDWV GAFAVTGGIG ERELADEYKA QGDDYNAIMI QAVADRLAEA FAEYLHERVR KEIWGYAADE ALSNEDLIRE KYQGIRPAPG YPACPEHTEK GPLWELMNVE ENIGMSLTSS YAMYPGASVS GWYFSHPDSR YFAIAQIQED QVESYAARKG WDMLEAEKWL GPNINS // ID B8KGM0_9GAMM Unreviewed; 1221 AA. AC B8KGM0; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 01-APR-2015, entry version 36. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EED32986.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EED32986.1}; GN Name=metH {ECO:0000313|EMBL:EED32986.1}; GN ORFNames=NOR53_1222 {ECO:0000313|EMBL:EED32986.1}; OS gamma proteobacterium NOR5-3. OC Bacteria; Proteobacteria; Gammaproteobacteria. OX NCBI_TaxID=566466 {ECO:0000313|EMBL:EED32986.1}; RN [1] {ECO:0000313|EMBL:EED32986.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOR5-3 {ECO:0000313|EMBL:EED32986.1}; RA Amann R., Fuchs B., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; DS999405; EED32986.1; -; Genomic_DNA. DR RefSeq; WP_009022363.1; NZ_DS999405.1. DR EnsemblBacteria; EED32986; EED32986; NOR53_1222. DR PATRIC; 36991608; VBIGamPro33483_0643. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EED32986.1}; KW Transferase {ECO:0000313|EMBL:EED32986.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1221 AA; 134547 MW; BE7D94FC9436BF93 CRC64; MDAFIPESGP LADALRKRIL VIDGAMGTMI QAEGLQEADY RGERFADHAG DLKGNNDLLS ITRPDVIKGI HLAYLEAGAD IIETNTFNAT AVALEDYGLQ AIARELNETS AHIARSAAQA MSEETPQKPR FVAGVLGPTP RTASISPDVN DPGARNVDFA RLSDDYSEAV RGLLDGGVDL LMIETIFDTL NAKAAIFAIE SVFEERGLRV PVMISVTFPD VSGRNLSGQS PTAFWYSVAH ARPLVVGSNC GRRFLEVRPF LEELSKATQG YFSAHLNAGL PNAFGEYDEA PEVMAAEFKD FAERGFVNLV GGCCGTTPAH IRAIAHAVEG IAPRALPESS GACQLSGLEP FTFDAQSLFV NVGERCNVTG SARFKKLILS GDYEAALDVA RTQVEDGAQI IDVNMDEGML DAKEAMVTFL NLIASEPDIS RVPVMIDSSR WEVIEAGLRC VQGKAVVNSI SLKAGEEEFL EQARLCQRYG AAVVVMAFDE DGQADTVARR REICQRSWDL LRERLDFNPE DIIFDPNIFA VATGIEIHNS YAVDFIEATR WIKENLPGAK VSGGVSNVSF SFRGNNPVRE AIHSVFLYHA IRAGMDMGIV NAGQLAVYDE LPGELREAVE DVVLNRRDDS TERLLDIASK YHADGPATVR VEDLAWRDEP VTKRLEYALV KGINNYIEED AEEARQQAAR PIEVIEGPLM DGMNVVGDLF GQGKMFLPQV VKSARVMKQA VAYLQPYIEE EKAEGSTNGR ILMATVKGDV HDIGKNIVGV VLQCNNYEVI DLGVMVHCEE ILRVAKEQNV DIIGLSGLIT PSLDEMMHVA SEMQRTGLSV PLMIGGATTS KAHTAVKIEP NYQNDLVVYV PDASRSVSVA SQLLGEQKSG FVKERREEYV QVRERIANRK PKAKRLSYQD ALANRAIFDW ENYQAPTPSF TGVRVFENIP LQDLVDTIDW TPFFITWELA GKYPKILQDE VVGEQARDLF ADAQAMLKKI VDENWLEARA VIGFWPAHSD GEDILVDTGD DADELRLHHL RQQTEKANEQ PNLSLSDYVA PSNDYIGGFC VTTGHGVSER AAAFEANHDD YNSIMLKALA DRLAESLAEH MHLRVRQEFW GYASDEQLSN EDLIREKYRG IRPAPGYPAC PDHTEKRALF DLLDAEERCG VTLSDNYAME PASSVSGWYF SHPEARYFAV GKIGEDQLEA LAARKNVKTA ALARWLAPNL D // ID B8KQY4_9GAMM Unreviewed; 1214 AA. AC B8KQY4; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 38. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EED36420.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EED36420.1}; GN Name=metH {ECO:0000313|EMBL:EED36420.1}; GN ORFNames=NOR51B_2371 {ECO:0000313|EMBL:EED36420.1}; OS Luminiphilus syltensis NOR5-1B. OC Bacteria; Proteobacteria; Gammaproteobacteria; OMG group; OM60 clade; OC Luminiphilus. OX NCBI_TaxID=565045 {ECO:0000313|EMBL:EED36420.1}; RN [1] {ECO:0000313|EMBL:EED36420.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOR5-1B {ECO:0000313|EMBL:EED36420.1}; RA Amann R., Fuchs B., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; DS999411; EED36420.1; -; Genomic_DNA. DR RefSeq; WP_009021163.1; NZ_DS999411.1. DR EnsemblBacteria; EED36420; EED36420; NOR51B_2371. DR PATRIC; 25917518; VBIGamPro119993_1239. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EED36420.1}; KW Transferase {ECO:0000313|EMBL:EED36420.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 239 239 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 302 302 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 750 750 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1214 AA; 133926 MW; B6D9C86E5FF1F795 CRC64; MKSLEERIVI LDGATGTALQ KYALDEADYR GSRLAERAGE FKGNNDLLNL TQPDIVSEVH RSYLDAGADI IETNTFNGTR IAQSDYGLED LVDEINLAGA QLARSAADVA SKKTPDKPRY VAGVLGPTPR TASISPDVND PGARNITFEQ LVDDYQSAAE TLIDGGVDLL MVETIFDTLN AKAAIFAIEA AMENRGVVLP LMLSVTFPDT SGRLLSGQTG EAFWHSIAHA KPLVVGSNCG RRFTEVQPFL ESLANVAPCY FSAHLNAGLP NAFGEYDETP EDMHSDFKGF AERGFLNLAG GCCGTTPEHI RAIADAVEGV APRSIPEPLP DTRLSGLEPF EFAGKNFVNV GERCNVTGSA KFKRLILDND FDTALDVART QVEDGAQIID VNMDEGMLDS KAAMIQFLRM AAAEPEIAKV PFMIDSSKWE VIEAGLKCVQ GKAVVNSISL KSGEAEFLEQ ARLCQRYGAA VVVMAFDEEG QADTLERRQH ICRRSYDLLI ERLDFNPCDI IFDPNIFAVG TGIEAHNDYA LDFIEATRFI KQDLPGARVS GGVSNVSFSF RGNNAVREAI HSVFLYHSIK AGLDMGIVNA GQLAVYDDLP DELREAVLDL VLNRRDDATE RLLDIAESYR SAGGEARRNE DLTWREQEVE KRLEYALLKG ITNWIEEDTE EARQRANKPI EVIEGPLMDG MNTVGDLFGE GKMFLPQVVK SARVMKQAVA YLQPYIEEEK AGGSGNNGKI LLATVKGDVH DIGKNIVGIV LQCNNFEIID LGVMVHCDEI LRVAEEENVD IIGLSGLITP SLEEMSHVAR EMQRRNLQTP LMIGGATTSK AHTAVKIQPE YQNNTVVYVP DASRSVAVAS KLVGTQNAAF GEAIKEEYDQ IRTRVANRKG RSERIDYATA CERRLAIDWE AYQPPKPAFT GTRIFSDYPI AQLLDTIDWT PFFITWDLHG KFPAILEDPV VGEQARQLFD DAQTMLQQII DQHWLTAKGA IGFWSACQVD NDDISVRDSD NTEIARLHQM RQQLQKREGE PNLSLADFIA PEDGPDDYIG AFCVTVGHGV DERVAAYEAQ HDDYNAILLK SLADRLAESF AETLHREVRK QHWGYAPDES LSNDALIRER YRGIRPAPGY PACPDHLEKG TIFDLLDVSE KMGVELTESF AMTPTASVSG LYFSHPSSRY FSVGKIGTDQ LEALAVRKAM EQDELARWLA PNLD // ID B8L4T1_9GAMM Unreviewed; 364 AA. AC B8L4T1; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EED38692.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EED38692.1}; GN Name=metH_2 {ECO:0000313|EMBL:EED38692.1}; GN ORFNames=SSKA14_1705 {ECO:0000313|EMBL:EED38692.1}; OS Stenotrophomonas sp. SKA14. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Stenotrophomonas. OX NCBI_TaxID=391601 {ECO:0000313|EMBL:EED38692.1}; RN [1] {ECO:0000313|EMBL:EED38692.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SKA14 {ECO:0000313|EMBL:EED38692.1}; 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 ----------------------------------------------------------------------- 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; EED38692.1; -; Genomic_DNA. DR RefSeq; WP_008266056.1; NZ_DS999412.1. DR EnsemblBacteria; EED38692; EED38692; SSKA14_1705. DR PATRIC; 30945942; VBISteSp70125_1407. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EED38692.1}; KW Transferase {ECO:0000313|EMBL:EED38692.1}. SQ SEQUENCE 364 AA; 38582 MW; A51BEF4BDB09615D CRC64; MSALPWLHPD RADALLDALR ERILIIDGAM GTMIQRHGLQ EDDYRGERFA GGYDHAHGPG CDHGMPEGHD LKGNNDLLLL TRPQVIADIH TAYLEAGADL VETNTFNATS VSQADYHLQH LVYELNKAGA AVARACCDAV EATTPDKPRF VIGVIGPTSR TASISPDVND PGYRNTSFDE LRDTYREAIE GLIDGGADTL MVETIFDTLN AKAALYALEE AFDARGARLP VMISGTITDA SGRTLSGQTA EAFHASLAHA RPLSIGLNCA LGAAAMRPHV ETLSQVAGCH VSAHPNAGLP NAFGEYDETP EEMSATLRGF AEDGLLNLVG GCCGSTPDHI RAIAEAVAGL PPRALPGNQE QQAA // ID B8M2P0_TALSN Unreviewed; 369 AA. AC B8M2P0; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 29-APR-2015, entry version 23. DE SubName: Full=Homocysteine S-methyltransferase, putative {ECO:0000313|EMBL:EED21951.1}; GN ORFNames=TSTA_091920 {ECO:0000313|EMBL:EED21951.1}; 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 {ECO:0000313|Proteomes:UP000001745}; RN [1] {ECO:0000313|Proteomes:UP000001745} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006 RC {ECO:0000313|Proteomes:UP000001745}; 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; EED21951.1; -; Genomic_DNA. DR RefSeq; XP_002478914.1; XM_002478869.1. DR GeneID; 8098578; -. DR EuPathDB; FungiDB:TSTA_091920; -. DR InParanoid; B8M2P0; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000001745; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001745}; KW Methyltransferase {ECO:0000313|EMBL:EED21951.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001745}; KW Transferase {ECO:0000313|EMBL:EED21951.1}. SQ SEQUENCE 369 AA; 41037 MW; 9BDE1184614BAED0 CRC64; MNLLQGPGSA LKIHISKLVN TMQILLLDGG LGTTLEASPF NVQFTPEKPL WSSHLLIDSP STLQAAHHAF CDAGADIILT ATYQTSTEGF TRTNSSYTAR DAAQYMRSAI PLVRSAVSST ADDKKRSVAL SLGPYGATMS PVSAEYTGIY PPEMDGENAL REWHTQRLKI FTESEDESWD QVDYIAFETL RRADEVCAVR GAVCDVVGRD STSKKPWWIC GVFPGEQVDE EEIRQWVRAA VGNHPGLPRP WGIGLNCTRI DRVEAIVSIM RDEVRRLLDQ AQIDEWASSK PWLVLYPDGT KGEKYDPVTK TWVQSVTDTV KRPWDEIFWD IIQHQSKAEW GGIVVGGCCR AGPADIAALR RRIDSDRVD // ID B8NVJ1_ASPFN Unreviewed; 376 AA. AC B8NVJ1; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 29-APR-2015, entry version 29. DE SubName: Full=Scf_1106286419448 genomic scaffold, whole genome shotgun sequence {ECO:0000313|EMBL:EED45449.1}; GN ORFNames=AFLA_116780 {ECO:0000313|EMBL:EED45449.1}; 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 {ECO:0000313|EMBL:EED45449.1, ECO:0000313|Proteomes:UP000001875}; RN [1] {ECO:0000313|Proteomes:UP000001875} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167 RC {ECO:0000313|Proteomes:UP000001875}; 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; EQ963485; EED45449.1; -; Genomic_DNA. DR RefSeq; XP_002384385.1; XM_002384344.1. DR STRING; 5059.CADAFLAP00012250; -. DR EnsemblFungi; CADAFLAT00012250; CADAFLAP00012250; CADAFLAG00012250. DR GeneID; 7909291; -. DR KEGG; afv:AFLA_116780; -. DR EuPathDB; FungiDB:AFLA_116780; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000001875; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 2. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001875}; KW Reference proteome {ECO:0000313|Proteomes:UP000001875}. SQ SEQUENCE 376 AA; 41753 MW; B02B0F0E6FAB8E2E CRC64; MMTRQLPILL LDGGLGTTLG DPPHNITFTA ETPLWSAHLL ISSPSTLEEV HKAFATVGAD IILTATYQTS FEGFTLTDPR YTADDAAHFM RSAIPLARRA GSSSGRTVKV ALSLGPYGAT MSPVGAEYTG LYPEEMNSEA KLREWHARRL CVFVDETGSW DNFEYIAFET VRRADEVKAI RGAMSDVLAD MYQGQGPDSE KNQLAMGKKP WWICGVFPDE EVDEEDVRAW VRAAVGTQEE ETGVYLPRPW GIGVNCTRIG NVGRIVSIMQ DELRNLEDLR TKGYVDEWNS VTGKPWLVLY PDGTNGEKYD PVTKTWVATE TGKETRPWHE IYWDVVQGLP EGAWEGVVMG GCCRAGPEQI ATLRRRIDER SNAQGV // ID B8PAR1_POSPM Unreviewed; 380 AA. AC B8PAR1; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 07-JAN-2015, entry version 27. DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EED82075.1}; DE Flags: Fragment; GN ORFNames=POSPLDRAFT_33838 {ECO:0000313|EMBL:EED82075.1}; 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 {ECO:0000313|Proteomes:UP000001743}; RN [1] {ECO:0000313|EMBL:EED82075.1, ECO:0000313|Proteomes:UP000001743} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 44394 / Madison 698-R {ECO:0000313|Proteomes:UP000001743}; 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; EQ966295; EED82075.1; -; Genomic_DNA. DR RefSeq; XP_002472772.1; XM_002472727.1. DR STRING; 104341.JGI33838; -. DR GeneID; 8148040; -. DR KEGG; ppl:POSPLDRAFT_33838; -. DR InParanoid; B8PAR1; -. DR KO; K00547; -. DR OMA; GEAIRNW; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000001743; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 2. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001743}; KW Reference proteome {ECO:0000313|Proteomes:UP000001743}. FT NON_TER 1 1 {ECO:0000313|EMBL:EED82075.1}. FT NON_TER 380 380 {ECO:0000313|EMBL:EED82075.1}. SQ SEQUENCE 380 AA; 41297 MW; 98419FF272218C13 CRC64; VLILDGGFGT TLEDVFHQDI STPLWSARPI EDNPELIIAA HLAFLRAGAD VILTSTYQCA FQTFERSGYT REDGVRILRK AVLLATEARR QYKEEGAPDD TSTGLSGTAH VRDIKIALSL GPFGATLSPA QEFDGFYPPP YGPKGLSQEG GNYNAFPDSD DGKAQEEKAV AALTAFHLER LRALVEDVET WAAIDFVAFE TVPLVREIRA IRHAMELLVQ ENGASAAKPW WISTVYPGGR FPQERSPGEG RLTVRIVVEA IMGEGRLGAP QSPAPWGLGV NCTEPQFIGG LLKEMTNIME GLGNTAGRSQ SPWLVVYPNR GDVYDAASQT WSKGAESIRQ NWAVHVWADV QRVAGSKAWS GCLIGGCCKT GPQEIAELLR // ID B9B381_9BURK Unreviewed; 356 AA. AC B9B381; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEE00896.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEE00896.1}; GN ORFNames=BURMUCGD1_0291 {ECO:0000313|EMBL:EEE00896.1}; OS Burkholderia multivorans CGD1. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=513051 {ECO:0000313|EMBL:EEE00896.1}; RN [1] {ECO:0000313|EMBL:EEE00896.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CGD1 {ECO:0000313|EMBL:EEE00896.1}; 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. {ECO:0000313|EMBL:EEE00896.1}. 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; ACFB01000003; EEE00896.1; -; Genomic_DNA. DR RefSeq; WP_006398117.1; NZ_ACFB01000003.1. DR EnsemblBacteria; EEE00896; EEE00896; BURMUCGD1_0291. DR PATRIC; 26959701; VBIBurMul43326_1659. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEE00896.1}; KW Transferase {ECO:0000313|EMBL:EEE00896.1}. SQ SEQUENCE 356 AA; 38185 MW; 6C019CE7F3894FE2 CRC64; MSATPTAASA APLDASYTRG AELPALLKSR ILILDGAMGT MIQRYKLDEA AYRGERFKDF PRDVKGNNEL LSITQPQVIR EIHDQYFAAG ADIVETNTFG ATTVAQADYG MEDLVVEMNV ESAKLARASA AQYATPDKPR FVAGAIGPTP KTASISPDVN DPGARNVTFD ELRDAYYMQA KALLDGGVDL FLVETIFDTL NAKAALFALD QLFEDTGERL PIMISGTVTD ASGRILSGQT VEAFWNSLRH AKPLTFGLNC ALGAALMRPY IAELAKLCDT FVSCYPNAGL PNPMAETGFD ETPDVTSGLL REFAQAGLVN LAGGCCGTTP EHIAEIAKAL ADVKPRRWPS QYSEAA // ID B9BVT9_9BURK Unreviewed; 356 AA. AC B9BVT9; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEE05111.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEE05111.1}; GN ORFNames=BURMUCGD2_0511 {ECO:0000313|EMBL:EEE05111.1}; OS Burkholderia multivorans CGD2. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=513052 {ECO:0000313|EMBL:EEE05111.1, ECO:0000313|Proteomes:UP000004535}; RN [1] {ECO:0000313|EMBL:EEE05111.1, ECO:0000313|Proteomes:UP000004535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CGD2 {ECO:0000313|EMBL:EEE05111.1}; 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. {ECO:0000313|EMBL:EEE05111.1}. 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; ACFC01000011; EEE05111.1; -; Genomic_DNA. DR RefSeq; WP_006398117.1; NZ_ACFC01000011.1. DR EnsemblBacteria; EEE05111; EEE05111; BURMUCGD2_0511. DR PATRIC; 27793183; VBIBurMul91169_4510. DR Proteomes; UP000004535; Unassembled WGS sequence. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000004535}; KW Methyltransferase {ECO:0000313|EMBL:EEE05111.1}; KW Transferase {ECO:0000313|EMBL:EEE05111.1}. SQ SEQUENCE 356 AA; 38185 MW; 6C019CE7F3894FE2 CRC64; MSATPTAASA APLDASYTRG AELPALLKSR ILILDGAMGT MIQRYKLDEA AYRGERFKDF PRDVKGNNEL LSITQPQVIR EIHDQYFAAG ADIVETNTFG ATTVAQADYG MEDLVVEMNV ESAKLARASA AQYATPDKPR FVAGAIGPTP KTASISPDVN DPGARNVTFD ELRDAYYMQA KALLDGGVDL FLVETIFDTL NAKAALFALD QLFEDTGERL PIMISGTVTD ASGRILSGQT VEAFWNSLRH AKPLTFGLNC ALGAALMRPY IAELAKLCDT FVSCYPNAGL PNPMAETGFD ETPDVTSGLL REFAQAGLVN LAGGCCGTTP EHIAEIAKAL ADVKPRRWPS QYSEAA // ID B9DIA5_STACT Unreviewed; 613 AA. AC B9DIA5; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 29-APR-2015, entry version 44. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN Name=metH {ECO:0000313|EMBL:CAL26928.1}; GN OrderedLocusNames=Sca_0013 {ECO:0000313|EMBL:CAL26928.1}; OS Staphylococcus carnosus (strain TM300). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=396513 {ECO:0000313|EMBL:CAL26928.1, ECO:0000313|Proteomes:UP000000444}; RN [1] {ECO:0000313|EMBL:CAL26928.1, ECO:0000313|Proteomes:UP000000444} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TM300 {ECO:0000313|EMBL:CAL26928.1, RC ECO:0000313|Proteomes:UP000000444}; RX PubMed=19060169; DOI=10.1128/AEM.01982-08; RA Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., RA Schuster S.C., Gotz F.; RT "Genome analysis of the meat starter culture bacterium Staphylococcus RT carnosus TM300."; RL Appl. Environ. Microbiol. 75:811-822(2009). CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; CAL26928.1; -; Genomic_DNA. DR RefSeq; WP_012664043.1; NC_012121.1. DR RefSeq; YP_002633113.1; NC_012121.1. DR ProteinModelPortal; B9DIA5; -. DR STRING; 396513.Sca_0013; -. DR KEGG; sca:Sca_0013; -. DR PATRIC; 19600756; VBIStaCar105558_0013. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; SCAR396513:GJ9G-13-MONOMER; -. DR Proteomes; UP000000444; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000444}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:CAL26928.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000000444}; KW Transferase {ECO:0000313|EMBL:CAL26928.1}. SQ SEQUENCE 613 AA; 68079 MW; 27B45095504AEC23 CRC64; MSRFLQTLKE NVLVADGAIG TILYSEGIDT CPEAYNITHP KKIEQIHRSY IQAGADVIQT NTYGANFEKL QTFGLEHQVK DITRAAVRIA KKAANEDTFI LGTVGGFKGV KQNELSLSTI LYHTDIQIDT LIDEGVDALL FETYYDLNEL LQVIRATKKK YDIPVIAQLT ASNTNYLQDG TEINEALKQV EAEGADVIGL NCHHGPHHMQ QSFTHIELPQ HALLSCYPNA SLLDFENSSI KYSDNASYFG KIAKSLVKEG VHLIGGCCGT TPEHIHYIKE AVEGLEPINE KKVIPIRRKS NHPSIPVQKD NLTTKVKSGP TVIVELDTPK HLDTTKFFVN VTKLDKANVD AITLADNSLA TVRVSNIAAA SIIKQNYNIE PLVHITCRDR NLIGLQSHLL GLSLLGINEI LAITGDPSKV GHLPGANNVY DVNSKGLTEL AVRFNQGLNI DGGALKTTTN FNIAGAFNPN VRKMEAAVRR LDKKLDSGMN YFITQPVYTV EKIQEIAEKT AHLDSPFFIG IMPITSYRNA QFLHNEVPGI TLPEDVLEQF EAVKDDKQKT KELSLRICRK LVDEVTKHFN GLYLITPFEQ VDYSLELATY FKTKTENNQE AII // ID B9E0A6_CLOK1 Unreviewed; 801 AA. AC B9E0A6; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:BAH05931.1}; GN OrderedLocusNames=CKR_0880 {ECO:0000313|EMBL:BAH05931.1}; OS Clostridium kluyveri (strain NBRC 12016). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=583346 {ECO:0000313|EMBL:BAH05931.1, ECO:0000313|Proteomes:UP000007969}; RN [1] {ECO:0000313|Proteomes:UP000007969} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 12016 {ECO:0000313|Proteomes:UP000007969}; 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; BAH05931.1; -; Genomic_DNA. DR RefSeq; WP_012101348.1; NC_011837.1. DR RefSeq; YP_002471345.1; NC_011837.1. DR ProteinModelPortal; B9E0A6; -. DR STRING; 583346.CKR_0880; -. DR EnsemblBacteria; BAH05931; BAH05931; CKR_0880. DR KEGG; ckr:CKR_0880; -. DR PATRIC; 19471568; VBICloKlu118830_1031. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CKLU583346:GJNQ-925-MONOMER; -. DR Proteomes; UP000007969; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007969}. SQ SEQUENCE 801 AA; 87798 MW; C9F79F51DFEF6D92 CRC64; MNFKNLVDKF NNRFIFFDGA MGTMLQKAGL KLGELPEVLN ITNPEIISGI HRKYLDAGAD IITTNTFGAN ELKYDSSDYT IEDVISAGVK LAKQEAGDKL VALDIGPIGK IMEPTGNLSF ESAYKLFKNQ IVIGEKSGAD VVLIETMTDL YEAKAAVLAA KENSNIPIFC TMTFQEDGRT LMGTDAKTMV FVLEALGVDV LGVNCSLGPK ELQGIVEEIL KYSSIPVMVQ PNAGLPRYDG ENTIYDISPE DFAENVLTMA QKGIRVLGGC CGTTPEFIRM CRKDLEGLTP LNIEEKHYTA VCSATDTVIV GEKIKIIGER INPTGRSIYK KELKEGSINY IQKEAIMQKE EGANILGVNV GLPEINEVEI MKKAIRAVQK VVQLPLSIDS PDPQVLETGI RMYNGKPVIN SVNGSKKSME EVFPIVKKYG GCVIALTIDE KGIPHTAEGR VKIAEKIIKT ASIYGINKKN IIIDCLTLTV SAQQKEVLET IKAIKMVTEK FGVKTVLGVS NISFGLPNRS ILNRTFLAMA LQAGLNLPIM NPADESMKEV IAAFQVLTNI DKEGKEYVIK YGNKSKDEKP KGEGNSPLKN ADNNLKDLKQ LIIDGIEDEA EAMTTELLKN KKALEIVNSY IIPALDEVGK QYELQDIFLP QLIQSAETVK KSFEIIKDNM LSSGQKSLEK GTIVLATVKG DIHDIGKNIV KVLLENYGFE VIDLGRDVDI DNIVNTIRDN NIKLVGLSAL MTTTVASMKK TIEAIRENNL NCKIVVGGAV LNQNYADMIG ADYYAKDARE AVKIAEEVFL I // ID B9E2G1_CLOK1 Unreviewed; 590 AA. AC B9E2G1; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 29-APR-2015, entry version 44. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=CKR_1635 {ECO:0000313|EMBL:BAH06686.1}; OS Clostridium kluyveri (strain NBRC 12016). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=583346 {ECO:0000313|EMBL:BAH06686.1, ECO:0000313|Proteomes:UP000007969}; RN [1] {ECO:0000313|Proteomes:UP000007969} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 12016 {ECO:0000313|Proteomes:UP000007969}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; BAH06686.1; -; Genomic_DNA. DR RefSeq; WP_012102157.1; NC_011837.1. DR RefSeq; YP_002472100.1; NC_011837.1. DR ProteinModelPortal; B9E2G1; -. DR STRING; 583346.CKR_1635; -. DR EnsemblBacteria; BAH06686; BAH06686; CKR_1635. DR KEGG; ckr:CKR_1635; -. DR PATRIC; 19473164; VBICloKlu118830_1829. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; CKLU583346:GJNQ-1680-MONOMER; -. DR Proteomes; UP000007969; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007969}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 590 AA; 66365 MW; D248E82F8DC700B5 CRC64; MNIKEKPLIF DGAMGTYYPR ISKDPLPKCE LANIYDRNTI LKIHREYIEA GCMAIKTNTF GANKVSLESD FNKVKEVIIN GYEIAKEAAK DTEVLVFADI GPIPFLESMD LYEGYKEIVD LFLELGAKYF IFETFSSDEY LREISEYIKG KDPEAYILME FAVSPEGYTR VGKSGKKLIE NILKIPTIDA CGFNCFSGPY HLLQYIKTFN IGNETISVMP NSGYPTVIDN RTFFDNTKEY FAQRMLEIAK QGVSILGGCC GTTPEFIRET VIKLKKLSKS EIVLKKQAEK IHTEKPVVKN VLLEKINKGK KIIAVELDPP IDTEVDFFLN SARTLKEQEI DAITIADCPI ARARVDSSLL ACKLKRELDI TTIPHMTCRD RNINATKALL LGLNIEGVNN VLVVTGDPIP SAERDEVKAM FSFNSAILAN YITNLNDTIF SSPFNICGAL NVNSRNFNTE LKRAKTKIEN GIAVFLTQPI LTEEALENLK LARRELTARI LGGIIPVVSY RNACFMNNEI SGIRVSEEII KQYKDVSKEE AVKLAVKIST DIAEQIYPYV DGYYLITPFK RIDIISEIIN NIKAKNTITI // ID B9E3G4_CLOK1 Unreviewed; 313 AA. AC B9E3G4; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 37. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:BAH07039.1}; GN OrderedLocusNames=CKR_1988 {ECO:0000313|EMBL:BAH07039.1}; OS Clostridium kluyveri (strain NBRC 12016). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=583346 {ECO:0000313|EMBL:BAH07039.1, ECO:0000313|Proteomes:UP000007969}; RN [1] {ECO:0000313|Proteomes:UP000007969} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 12016 {ECO:0000313|Proteomes:UP000007969}; 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; BAH07039.1; -; Genomic_DNA. DR RefSeq; WP_012102601.1; NC_011837.1. DR RefSeq; YP_002472453.1; NC_011837.1. DR ProteinModelPortal; B9E3G4; -. DR STRING; 583346.CKR_1988; -. DR EnsemblBacteria; BAH07039; BAH07039; CKR_1988. DR KEGG; ckr:CKR_1988; -. DR PATRIC; 19473990; VBICloKlu118830_2242. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; CKLU583346:GJNQ-2033-MONOMER; -. DR Proteomes; UP000007969; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007969}. SQ SEQUENCE 313 AA; 34832 MW; 58D558CB1DDCB0B2 CRC64; MNPLKHILKD FKVIILDGAL ATELEKIGCN IDDSLWSAKI LYEDPKIIEG VHYDYFVSGA DCAITSSYQA TIRGFMEKGF KEDEAIELIR LSVQVAKKAR DRFWKNPLNR INRPKPLIAG SIGPYGAYLA DGSEYIGHYN ISEEELMEFH RPRMKILIEE GVDILACETI PSLVEAQAIL KLLEEFPSVC SWISFSAKDE LNISEGTSLA KCAKYLDSNR QVAAIGVNCT PPKYINSLIE QISKNSSKPI IVYPNSGEEY DGITKTWHGD SSSKAFSCSA KEWFDGGARL IGGCCRTTPE DIKSTCKVLK NNL // ID B9E9X6_MACCJ Unreviewed; 295 AA. AC B9E9X6; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 38. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:BAH17037.1}; GN OrderedLocusNames=MCCL_0330 {ECO:0000313|EMBL:BAH17037.1}; OS Macrococcus caseolyticus (strain JCSC5402). OC Bacteria; Firmicutes; Bacilli; Bacillales; Macrococcus. OX NCBI_TaxID=458233 {ECO:0000313|EMBL:BAH17037.1, ECO:0000313|Proteomes:UP000001383}; RN [1] {ECO:0000313|EMBL:BAH17037.1, ECO:0000313|Proteomes:UP000001383} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCSC5402 {ECO:0000313|EMBL:BAH17037.1, RC ECO:0000313|Proteomes:UP000001383}; 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; BAH17037.1; -; Genomic_DNA. DR RefSeq; WP_012656238.1; NC_011999.1. DR RefSeq; YP_002559733.1; NC_011999.1. DR STRING; 458233.MCCL_0330; -. DR EnsemblBacteria; BAH17037; BAH17037; MCCL_0330. DR KEGG; mcl:MCCL_0330; -. DR PATRIC; 22422942; VBIMacCas48391_0414. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; MCAS458233:GI03-343-MONOMER; -. DR Proteomes; UP000001383; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001383}; KW Reference proteome {ECO:0000313|Proteomes:UP000001383}. SQ SEQUENCE 295 AA; 32332 MW; EB1F0EAFD1AF8BFF CRC64; MQLRDKLQQD IVILDGGFGT TVEQFGYDVK HELWSSNLIQ SNPEAVYKVH KAFVDSGAEI ILTNTYQASV QSFLNIGIDK ATACTYLATA VELATRAASN RTIIAGSLGP YGAMLGNGSE YTGDYEETEA DYIQYHKERL DILIEAGVSV FAFETIPNIE EIKAVRTLLL DYPHIEAWIS VTLKDHDHLS DGTPLEAVIE VVNEIENVLA FGVNCTSVNV IDAAVDKLIT LSDKPLILYP NSGRQYDAVH KVWIDQEDAS LVEAAPRWKE KGVKIIGGCC QVGPGEIKEL GTALK // ID B9GSK5_POPTR Unreviewed; 332 AA. AC B9GSK5; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 11-DEC-2013, sequence version 2. DT 04-MAR-2015, entry version 38. DE SubName: Full=Selenocysteine methyltransferase family protein {ECO:0000313|EMBL:EEE80097.2}; GN ORFNames=POPTR_0002s05070g {ECO:0000313|EMBL:EEE80097.2}; 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 {ECO:0000313|EMBL:EEE80097.2, ECO:0000313|Proteomes:UP000006729}; RN [1] {ECO:0000313|EMBL:EEE80097.2, ECO:0000313|Proteomes:UP000006729} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nisqually {ECO:0000313|Proteomes:UP000006729}; 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). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000338; EEE80097.2; -; Genomic_DNA. DR RefSeq; XP_002300824.2; XM_002300788.2. DR STRING; 3694.fgenesh4_pg.C_LG_II000468; -. DR EnsemblPlants; POPTR_0002s05070.1; POPTR_0002s05070.1; POPTR_0002s05070. DR GeneID; 7480020; -. DR KEGG; pop:POPTR_0002s05070g; -. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR InParanoid; B9GSK5; -. DR KO; K00547; -. DR OMA; SSVEGFM; -. DR Proteomes; UP000006729; Linkage group LGII. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006729}; KW Methyltransferase {ECO:0000313|EMBL:EEE80097.2}; KW Reference proteome {ECO:0000313|Proteomes:UP000006729}; KW Transferase {ECO:0000313|EMBL:EEE80097.2}. SQ SEQUENCE 332 AA; 36167 MW; D1A297511D395264 CRC64; MTDFLRQSGG VAIIDGGLAT ELERHGADLN DPLWSAKCLL TSPHLVRAVH LDYLEAGADI IITASYQATI QGFEAKGFSR EDSEALLRKS VEIACEARDI YYGRCREGSP DGSDDGRVLK HRPILVAASV GSYGAYLADG SEYSGNYGDA ITLETLKDFH RRRVQILAES GADLIAFETV PNKVEAQAYA KLLEEEDIKI PAWFSFNSKD GINVVSGDSL LECASIAESC KNAVAVGINC TPPRFIHELI LSIKKVTTKP ILIYPNSGES YDGDRKEWVQ NTGISDQDFV SYVNKWCEIG AALVGGCCRT TPHTIRAIYK TLPNRSAALS SH // ID B9H8B8_POPTR Unreviewed; 342 AA. AC B9H8B8; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 11-DEC-2013, sequence version 2. DT 04-MAR-2015, entry version 37. DE SubName: Full=Selenocysteine methyltransferase family protein {ECO:0000313|EMBL:EEE94598.2}; DE Flags: Fragment; GN ORFNames=POPTR_0005s23480g {ECO:0000313|EMBL:EEE94598.2}; 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 {ECO:0000313|EMBL:EEE94598.2, ECO:0000313|Proteomes:UP000006729}; RN [1] {ECO:0000313|EMBL:EEE94598.2, ECO:0000313|Proteomes:UP000006729} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nisqually {ECO:0000313|Proteomes:UP000006729}; 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). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000341; EEE94598.2; -; Genomic_DNA. DR RefSeq; XP_002307602.2; XM_002307566.2. DR STRING; 3694.eugene3.00051204; -. DR EnsemblPlants; POPTR_0005s23480.1; POPTR_0005s23480.1; POPTR_0005s23480. DR GeneID; 7464849; -. DR KEGG; pop:POPTR_0005s23480g; -. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR InParanoid; B9H8B8; -. DR KO; K00547; -. DR OMA; KIACEAR; -. DR Proteomes; UP000006729; Linkage group LGV. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006729}; KW Methyltransferase {ECO:0000313|EMBL:EEE94598.2}; KW Reference proteome {ECO:0000313|Proteomes:UP000006729}; KW Transferase {ECO:0000313|EMBL:EEE94598.2}. FT NON_TER 1 1 {ECO:0000313|EMBL:EEE94598.2}. SQ SEQUENCE 342 AA; 37401 MW; 4C90D8AFC6A22B9B CRC64; ATDINWEGKT NFSNTKTLCW GGKDTSFKMG HPAAETSSFM TDFLRQSGGV AIIDGGLATE LERHGADLND PLWSAKCLLT SPHLVREVHL DYLEAGADII ITASYQATIQ GFEAKGFSGE ESESLLRKSV KIACEARDIY YDRCQKGSPD SNNGRVLKQR PILVAASIGS YGAYLADGSE YSGNYGDAIT LETLKDFHRR RVQILAESGA DLIAFETVPN KVEAQAYVEL LKEEDIKIPA WFSFNSKDGV NVVSGDSLLD CASIAESCQN VVAVGINCTP PRFIHGLILS IKKVTTKPIL IYPNSGESYD GKRKEWVQNT GISDQDFVSY VNKWCEIGAA LF // ID B9HK01_POPTR Unreviewed; 339 AA. AC B9HK01; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 07-JAN-2015, entry version 34. DE SubName: Full=Homocysteine S-methyltransferase 3 family protein {ECO:0000313|EMBL:EEE89909.1}; GN ORFNames=POPTR_0008s15570g {ECO:0000313|EMBL:EEE89909.1}; 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 {ECO:0000313|EMBL:EEE89909.1, ECO:0000313|Proteomes:UP000006729}; RN [1] {ECO:0000313|EMBL:EEE89909.1, ECO:0000313|Proteomes:UP000006729} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nisqually {ECO:0000313|Proteomes:UP000006729}; 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). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000344; EEE89909.1; -; Genomic_DNA. DR RefSeq; XP_002312542.1; XM_002312506.2. DR STRING; 3694.fgenesh4_pg.C_LG_VIII001390; -. DR EnsemblPlants; POPTR_0008s15570.1; POPTR_0008s15570.1; POPTR_0008s15570. DR GeneID; 7467500; -. DR KEGG; pop:POPTR_0008s15570g; -. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR InParanoid; B9HK01; -. DR KO; K00547; -. DR OMA; SYIGKWR; -. DR Proteomes; UP000006729; Linkage group LGVIII. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006729}; KW Methyltransferase {ECO:0000313|EMBL:EEE89909.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006729}; KW Transferase {ECO:0000313|EMBL:EEE89909.1}. SQ SEQUENCE 339 AA; 37071 MW; 2BF24AE91E033A5C CRC64; MEMGIVETSS RLMTDFLQKC GGYAVVDGGF ATELERHGAD LNDPLWSAKC LISSPHLVRK VHLDYLHAGA NIITTASYQA TIQGFVAKGL SEEEAELLLR RSVEIACEAR EIYYDKCTTK GSLDYIESGN ISRRPVLVAA SIGSYGAYLA DGSEYSGKYG DAVSLRTLKD FHRRRLQILA KSGADLIAFE TIPNKLEAKA YAELLEEEEI NIPAWFSFNS KDGINVVSGD SILECASIAD SCKRVVAVGI NCTPPRFIHG LVLSIQKATS KPIVIYPNSG ETYNAELKQW VKSSGVVVDE DFVSYIGKWR EAGASLFGGC CRTTPNTIRA ISRVLSKYP // ID B9HUS6_POPTR Unreviewed; 338 AA. AC B9HUS6; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 07-JAN-2015, entry version 38. DE SubName: Full=Homocysteine S-methyltransferase 3 family protein {ECO:0000313|EMBL:EEF00845.1}; GN ORFNames=POPTR_0010s09370g {ECO:0000313|EMBL:EEF00845.1}; 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 {ECO:0000313|EMBL:EEF00845.1, ECO:0000313|Proteomes:UP000006729}; RN [1] {ECO:0000313|EMBL:EEF00845.1, ECO:0000313|Proteomes:UP000006729} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nisqually {ECO:0000313|Proteomes:UP000006729}; 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). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000346; EEF00845.1; -; Genomic_DNA. DR RefSeq; XP_002314674.1; XM_002314638.2. DR STRING; 3694.grail3.0175003501; -. DR EnsemblPlants; POPTR_0010s09370.1; POPTR_0010s09370.1; POPTR_0010s09370. DR GeneID; 7474182; -. DR KEGG; pop:POPTR_0010s09370g; -. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR InParanoid; B9HUS6; -. DR KO; K00547; -. DR OMA; WHHERIS; -. DR Proteomes; UP000006729; Linkage group LGX. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006729}; KW Methyltransferase {ECO:0000313|EMBL:EEF00845.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006729}; KW Transferase {ECO:0000313|EMBL:EEF00845.1}. SQ SEQUENCE 338 AA; 36735 MW; 1568CA5165A2EEE3 CRC64; MELGNVENSS TTLMTDFLKK CGGYAVVDGG LATELERHGA DLNDPLWSAK CLISSPHLVR RVHLDYLDAG ANIILSASYQ ATIQGFVAKG LSVEEAESLL RRSVEIACEA REIYYDKSTK GSWDYIESGN ISRRPVLVAA SIGSYGAYLA DGSEYSGKYG DAVSLETLKD FHRRRLQVLL KSGADLIACE TIPNRLEAKA YAELLEEEGI NIPAWFSFNS KDGINVVSGD SILECASIAD SCKQVVAVGI NCTPPRFIHG LVLSIRKATS KPIVIYPNSG ETYNAELKQW TKSSGVVDED FVSYINKWRE AGASLFGGCC RTTPNTIRAI GNVLSKNP // ID B9HWH8_POPTR Unreviewed; 329 AA. AC B9HWH8; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 39. DE SubName: Full=Homocysteine S-methyltransferase 1 family protein {ECO:0000313|EMBL:EEF02112.1}; GN ORFNames=POPTR_0010s13500g {ECO:0000313|EMBL:EEF02112.1}; 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 {ECO:0000313|EMBL:EEF02112.1, ECO:0000313|Proteomes:UP000006729}; RN [1] {ECO:0000313|EMBL:EEF02112.1, ECO:0000313|Proteomes:UP000006729} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nisqually {ECO:0000313|Proteomes:UP000006729}; 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). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000346; EEF02112.1; -; Genomic_DNA. DR RefSeq; XP_002315941.1; XM_002315905.2. DR STRING; 3694.estExt_fgenesh4_pg.C_LG_X1132; -. DR EnsemblPlants; POPTR_0010s13500.1; POPTR_0010s13500.1; POPTR_0010s13500. DR GeneID; 7466898; -. DR KEGG; pop:POPTR_0010s13500g; -. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR InParanoid; B9HWH8; -. DR KO; K00547; -. DR OMA; AINDPLW; -. DR Proteomes; UP000006729; Linkage group LGX. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006729}; KW Methyltransferase {ECO:0000313|EMBL:EEF02112.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006729}; KW Transferase {ECO:0000313|EMBL:EEF02112.1}. SQ SEQUENCE 329 AA; 36174 MW; 668C54CF1EB0788E CRC64; MGFQKAKTSL EDLIKKAGGC AVIDGGFATQ LERHGATIND PLWSALCLIK DPDLIKRVHL EYLEAGADIL VTSSYQATLP GFLSRGLSAE EGELLLKKSV TLAVEARNKF WDAVERNPGH SYNRALVAAS IGSYGAYLAD GSEYSGCYGP DVNLEKLKDF HRRRLQVLVK ASPDLLAFET IPNKLEAQAC VELLEEENIN IPSWICFSCV DGENAPSGES FQQCLEAINK SDRVKAVGIN CAPPHFIESL ICKFKELTEK LIVVYPNSGE VWDGRAKRWL PSTCFDDDKF EVFATRWHDL GASLIGGCCR TTPSTIQAIS KVLKDPKQS // ID B9IXP5_BACCQ Unreviewed; 1132 AA. AC B9IXP5; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 01-APR-2015, entry version 46. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:ACM14466.1}; GN Name=metH {ECO:0000313|EMBL:ACM14466.1}; GN OrderedLocusNames=BCQ_4038 {ECO:0000313|EMBL:ACM14466.1}; OS Bacillus cereus (strain Q1). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=361100 {ECO:0000313|EMBL:ACM14466.1, ECO:0000313|Proteomes:UP000000441}; RN [1] {ECO:0000313|EMBL:ACM14466.1, ECO:0000313|Proteomes:UP000000441} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Q1 {ECO:0000313|EMBL:ACM14466.1, RC ECO:0000313|Proteomes:UP000000441}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000227; ACM14466.1; -; Genomic_DNA. DR RefSeq; WP_000649712.1; NC_011969.1. DR RefSeq; YP_002531755.1; NC_011969.1. DR STRING; 361100.BCQ_4038; -. DR EnsemblBacteria; ACM14466; ACM14466; BCQ_4038. DR KEGG; bcq:BCQ_4038; -. DR PATRIC; 18915826; VBIBacCer120424_4081. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; BCER361100:GJ7M-4026-MONOMER; -. DR Proteomes; UP000000441; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000441}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACM14466.1}; KW Transferase {ECO:0000313|EMBL:ACM14466.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 125812 MW; 0D397EA351A77770 CRC64; MKCIEEKLQN NILLLDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYELSHLDE ELNEKAARLA KQAVEESGKE VYVAGAMGPT TKAISVTGGV TFEELIGAYT RQARGLLKGE VDVLLVETSQ DMRNVKAAYI GIQAAFDELN TVVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWVN IIGGCCGTTP EHIKAMKSAL TSLKPREQQE RAGHGVSGLE ALQYDDSMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEI ARAQVKKNAH IIDICMADPD RDEIEDMENF LAEVTKVLKV PIMIDSTDEH VMERALTYIQ GKAVINSINL EDGEERFKKV TPLLRKYGAA IVVGTIDEDG MAVSAERKLE IAKRSYELLT TKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPDE EKRLADALLF ETTQETLEKF TNFYRVAKKK DVVVQETLTL DERLANYIVE GTKQGLHEDL SLALTEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILA NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAADIDIPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV TKEEKKVEIP AVIEPLPKAE VIVPDSTKRI VLRDVPVSHL TPFLNRQMLL GHHLGLKGSV KKLLREGDKR AHELNDLIDE LLQEGQSWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRVIE RFTFPRQGKA PYRTLGDYLR PVGDEMDYVA FLSVTVGEGV RDIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID B9IXP6_BACCQ Unreviewed; 610 AA. AC B9IXP6; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 39. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN Name=metE {ECO:0000313|EMBL:ACM14467.1}; GN OrderedLocusNames=BCQ_4039 {ECO:0000313|EMBL:ACM14467.1}; OS Bacillus cereus (strain Q1). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=361100 {ECO:0000313|EMBL:ACM14467.1, ECO:0000313|Proteomes:UP000000441}; RN [1] {ECO:0000313|EMBL:ACM14467.1, ECO:0000313|Proteomes:UP000000441} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Q1 {ECO:0000313|EMBL:ACM14467.1, RC ECO:0000313|Proteomes:UP000000441}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ACM14467.1; -; Genomic_DNA. DR RefSeq; WP_000770334.1; NC_011969.1. DR RefSeq; YP_002531756.1; NC_011969.1. DR STRING; 361100.BCQ_4039; -. DR EnsemblBacteria; ACM14467; ACM14467; BCQ_4039. DR KEGG; bcq:BCQ_4039; -. DR PATRIC; 18915828; VBIBacCer120424_4082. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; BCER361100:GJ7M-4027-MONOMER; -. DR Proteomes; UP000000441; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000441}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ACM14467.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:ACM14467.1}. SQ SEQUENCE 610 AA; 67182 MW; D604353A7C299F2C CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNISDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTE INRAAVKLAK ASVTDRNAIL GTIGGMKHIG AVTTTDMERE FMLLEQASAL LEEQVDGLLL ETFYDEFELL HAVQVLRKET NIPIVAQLAL HEAGTTQNGN DVNEILKQLL DYGANVVGLN CQLGPLHMTE AFKMISIPKN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPKFIEQGI RLLGGCCGTT PEHIESMKRA TLNVTPVIEK DTVQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRISNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSVL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIA LIEEVYEATK HLEQPIFIGI MPLISKRNAD FLHFEVPGIT LPEAVRERMD GHETKEAAIE EGIRISQELI DAAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID B9JGD8_AGRRK Unreviewed; 337 AA. AC B9JGD8; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 39. DE SubName: Full=5-methyltetrahydrofolate--homocysteine S-methyltransferase protein {ECO:0000313|EMBL:ACM26913.1}; GN Name=metH {ECO:0000313|EMBL:ACM26913.1}; GN OrderedLocusNames=Arad_2810 {ECO:0000313|EMBL:ACM26913.1}; 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 {ECO:0000313|EMBL:ACM26913.1, ECO:0000313|Proteomes:UP000001600}; RN [1] {ECO:0000313|EMBL:ACM26913.1, ECO:0000313|Proteomes:UP000001600} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K84 / ATCC BAA-868 {ECO:0000313|Proteomes:UP000001600}; 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; ACM26913.1; -; Genomic_DNA. DR RefSeq; WP_012651711.1; NC_011985.1. DR RefSeq; YP_002544842.1; NC_011985.1. DR STRING; 311403.Arad_2810; -. DR EnsemblBacteria; ACM26913; ACM26913; Arad_2810. DR KEGG; ara:Arad_2810; -. DR PATRIC; 20805174; VBIAgrRad129173_4670. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265278; -. DR KO; K00548; -. DR OMA; GTNLFAM; -. DR OrthoDB; EOG693GKH; -. DR BioCyc; ARAD311403:GHU8-2177-MONOMER; -. DR Proteomes; UP000001600; Chromosome 1. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001600}; KW Methyltransferase {ECO:0000313|EMBL:ACM26913.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001600}; KW Transferase {ECO:0000313|EMBL:ACM26913.1}. SQ SEQUENCE 337 AA; 35376 MW; 6472DDDFB065BFC2 CRC64; MTVTANPLTD LLAEKGVLLA DGATGTNLFA MGLEAGEAPE IWNEQHPERI TKLHQDFVDA GADIILTNTF GGTRHRLKLH HAQDRVHNLN KTAAEIARAV ADKAGRKVIV AGSVGPTGEL LVPLGALTYE DAVAAFAEQI EGLKAGGVDV AWIETMSSAE EIRAAAEAAV KVGLPYTYTG SFDTAGKTMM GLHPKDLHDV AKDVGEGPLA TGANCGVGAS DILSSLLDMT EADPTATIIV KGNCGIPEYR GAEIYYSGTP PLMADYARLA RDAGAKIIGG CCGTSCNHLA AMREALDNYT PGPRPTLETI IERIGPLRNK TANEGGAAPA RERRRRG // ID B9JHA8_AGRRK Unreviewed; 1292 AA. AC B9JHA8; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 52. DE SubName: Full=5-methyltetrahydrofolate--homocysteine S-methyltransferase protein {ECO:0000313|EMBL:ACM27105.1}; GN Name=metH {ECO:0000313|EMBL:ACM27105.1}; GN OrderedLocusNames=Arad_3069 {ECO:0000313|EMBL:ACM27105.1}; 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 {ECO:0000313|EMBL:ACM27105.1, ECO:0000313|Proteomes:UP000001600}; RN [1] {ECO:0000313|EMBL:ACM27105.1, ECO:0000313|Proteomes:UP000001600} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K84 / ATCC BAA-868 {ECO:0000313|Proteomes:UP000001600}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000628; ACM27105.1; -; Genomic_DNA. DR RefSeq; WP_012651865.1; NC_011985.1. DR RefSeq; YP_002545035.1; NC_011985.1. DR STRING; 311403.Arad_3069; -. DR EnsemblBacteria; ACM27105; ACM27105; Arad_3069. DR KEGG; ara:Arad_3069; -. DR PATRIC; 20805593; VBIAgrRad129173_4878. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; ARAD311403:GHU8-2376-MONOMER; -. DR Proteomes; UP000001600; Chromosome 1. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001600}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACM27105.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001600}; KW Transferase {ECO:0000313|EMBL:ACM27105.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 357 357 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 358 358 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 811 811 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1292 AA; 141581 MW; F279BF9D122511AA CRC64; MFLRQGTIAH RYVDIKISLC DLDAQSQSGQ GNSLMFDNLF GSETAKRDGS EVFAALRQAA SERILVLDGA MGTQIQGLGF DEDHFRGDRF IGCACHQQGN NDLLILTQPD AIEEIHYRYA KAGADILETN TFSSTRIAQA DYQMEGAVYD LNKEGAAVVR RAALRAERED GKRRFVAGAI GPTNRTASIS PDVNNPGYRA VSFDDLRLAY GEQIDGLIDG GADIILIETI FDTLNAKAAI FACEERFEAK GIRLPVMISG TITDLSGRTL SGQTPSAFWN SVRHASPFTI GLNCALGANA MRPHLQELSG AADTFICAYP NAGLPNEFGQ YDESPEMMAE QVEGFARDGL VNIVGGCCGS TPEHIAAIAE AVSKYPPRQL PAHRPFMSLS GLEPFELTKD IPFVNVGERT NVTGSAKFRK LITNADYTAA LAVARDQVEN GAQVIDINMD EGLIDSEKAM VEFLNLIAAE PDIARVPVMI DSSKFSIIEA GLKCVQGKPI VNSISLKEGE ENFLKQARLL RNYGAAVVVM AFDEQGQADS YQRKVEICAR AYKILTEEAG LPPEDIIFDP NIFAVATGIE EHNNYGVDFI EATRTIRKTM PLVHISGGVS NLSFSFRGNE PVREAMHAVF LYHAIQAGMD MGIVNAGQLA VYDNIDPELR EACEDVVLNR RSDGTERLLD VAERFRGAGT REAKVQDLAW REWPVEKRLE HALVNGITEY IEADTEEARQ TVARPLHVIE GPLMAGMNVV GDLFGSGKMF LPQVVKSARV MKQAVAVLLP FMEAEKLANG GSGERQASGK VLMATVKGDV HDIGKNIVGV VLACNNYEII DLGVMVPATK ILETAIAEKV DIIGLSGLIT PSLDEMVHVA SEMERQGFDI PLLIGGATTS RVHTAVKINP RYEKGQTVYV TDASRAVGVV SALLSPEAKQ GYVDTIKAEY AKVAAAHARS EAEKVRLPIA RARANAEKLD WANYKTVKPQ FFGTKVFENY DLAELAKYID WTPFFQTWEL KGRFPAILED EKQGEAARQL YADAQAMLEK IIAETWFRPR AVIGFWPAGA VGDDIKLFTD ETRTNGLATF YTLRQQLSKR DGRPNVALSD FVAPVASGIE EYVGGFVVTA GIEEIAIAER FERANDDYSS ILVKALADRF AEAFAERMHE RVRREFWGYA TDENLSSDEL LSETYAGIRP APGYPAQPDH TEKETLFRLL DAEAATGVKL TESYAMWPGS SVSGIYIGHP ASYYFGVAKV EHDQVEDYAA RKGMPIVEVE RWLGPVLNYV PEKRDAVVDD AA // ID B9JL78_AGRRK Unreviewed; 304 AA. AC B9JL78; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 35. DE SubName: Full=Homocysteine S-methyltransferase protein {ECO:0000313|EMBL:ACM30670.1}; GN OrderedLocusNames=Arad_9677 {ECO:0000313|EMBL:ACM30670.1}; 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 {ECO:0000313|EMBL:ACM30670.1, ECO:0000313|Proteomes:UP000001600}; RN [1] {ECO:0000313|EMBL:ACM30670.1, ECO:0000313|Proteomes:UP000001600} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K84 / ATCC BAA-868 {ECO:0000313|Proteomes:UP000001600}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; ACM30670.1; -; Genomic_DNA. DR RefSeq; WP_015917935.1; NC_011983.1. DR RefSeq; YP_002542267.1; NC_011983.1. DR STRING; 311403.Arad_9677; -. DR EnsemblBacteria; ACM30670; ACM30670; Arad_9677. DR KEGG; ara:Arad_9677; -. DR PATRIC; 20800054; VBIAgrRad129173_2154. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; DVITANS; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; ARAD311403:GHU8-5946-MONOMER; -. DR Proteomes; UP000001600; Chromosome 2. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001600}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ACM30670.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001600}; KW Transferase {ECO:0000313|EMBL:ACM30670.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 210 210 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 287 287 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 304 AA; 32529 MW; CE9328F6CD45D4E2 CRC64; MTKRGLILDG GTGRELERIG APFRQPEWSA LALMEAPEFV RKVHDNYIEA GADVITTNSY AVVPFHIGDE SFEADGAMLA ARAGRIAREA ADASTARKIL VAGSLPPVFG SYQPDLFDAK RAGHYLDTLV GGMAPYVDLW LAETQSSLAE ARAAREATLS TGKPLWISFT LRDDLVPSDM PEPLLRSNET VKAAAELVAS FGGEAMLFNC SMPEVMEAAI ETARATFAAL GADIQVGVYA NAFPSQQDDE EANATLTEIR NDLDPDSYGR WAGRWAASGA SIIGGCCGIG VDHIHALSGR YRCV // ID B9JYB0_AGRVS Unreviewed; 1257 AA. AC B9JYB0; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 29-APR-2015, entry version 52. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACM37140.1}; GN Name=metH {ECO:0000313|EMBL:ACM37140.1}; GN OrderedLocusNames=Avi_2966 {ECO:0000313|EMBL:ACM37140.1}; 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 {ECO:0000313|EMBL:ACM37140.1, ECO:0000313|Proteomes:UP000001596}; RN [1] {ECO:0000313|EMBL:ACM37140.1, ECO:0000313|Proteomes:UP000001596} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S4 / ATCC BAA-846 {ECO:0000313|Proteomes:UP000001596}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000633; ACM37140.1; -; Genomic_DNA. DR RefSeq; WP_015916561.1; NC_011989.1. DR RefSeq; YP_002550149.1; NC_011989.1. DR STRING; 311402.Avi_2966; -. DR EnsemblBacteria; ACM37140; ACM37140; Avi_2966. DR KEGG; avi:Avi_2966; -. DR PATRIC; 20829908; VBIAgrVit37146_4605. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; AVIT311402:GH2Y-2232-MONOMER; -. DR Proteomes; UP000001596; Chromosome 1. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001596}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001596}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 260 260 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 777 777 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1257 AA; 138064 MW; DF8D1EDC233A4074 CRC64; MLDQLFGREG ANRDGAEILK ALQQAARERI LILDGAMGTE IQGLGLDEDD FRGERFIGCA CHQKGNNDLL ILTQPEAIED IHFRYAMAGA DIVETNTFSS TRIAQADYEM EGAVYDLNKH GAQVVRRALL RAEREDGKRR FVAGAIGPTN RTASISPDVN NPGYRAVSFD DLRLAYGEQI DGLIDGGADL ILIETIFDTL NAKAAIFACE ERFLAKGIRL PVMISGTITD LSGRTLSGQT PSAFWNSVRH AKPFTIGLNC ALGADAMRPH LQELSGLADT FVSAYPNAGL PNEFGQYDQS PEYMAKLVEG FAEEGIVNVV GGCCGSTPAH IQAIAEAVKG KTPRQPVEHR PFMSLSGLEP FVLTKDIPFV NVGERTNVTG SAKFRKLITA GDYNAALVVA RDQVENGAQI IDINMDEGLI DSEKAMVEFL NLIAAEPDIA RVPVMIDSSK FQIIESGLKC VQGKPIVNSI SLKEGEENFV AQAKLIRNYG AAVVVMAFDE TGQADTYERK VAICERAYKI LTEDAGFSPE DIIFDPNVFA VATGIEEHNN YGVDFIEATR TIRQRMPLVH ISGGVSNLSF SFRGNEPVRE AMHAVFLYHA IQAGMDMGIV NAGQLAVYES IDAELREACE DVVLNRREDG TERLLEIAER YRGTGEAKAR VQDMSWRELP VEKRLEHALV NGITEFIDAD TEEARQNAAR PLHVIEGPLM AGMNVVGDLF GAGKMFLPQV VKSARVMKQA VAVLLPYMEE EKRANGGTGE REAAGKILMA TVKGDVHDIG KNIVGVVLAC NNYEIIDLGV MVPAAKILEV AIKENVDIIG LSGLITPSLD EMVHVAAEMQ RQGFNVPLLI GGATTSRVHT AVKIHPQYQK GQAVYVLDAS RAVGVVSSLL SPDTRDTTIE TLRTEYAKVA DAHARAELEK QRLPISRARA NAAKVDWASY KPKKPSFTGI KVFENYDLKE LAKYIDWTPF FQTWELKGRY PAILEDEKQG EAARALYADA QAMLAKIIDE TWFRPRAVIG FWPANTVGDD IRLFADEERS QELATFFTLR QQLSKRDGRP NVALSDFVAP VDSGVEDYVG GFVVTAGIEE VAISERFERA NDDYSSIMVK ALADRFAEAF AERMHERVRK EFWGYGADET YTPEELISES YAGIRPAPGY PAQPDHTEKV TLFNLLDATA TTGVTLTESY AMWPGSSVSG IYIGHPDSYY FGVAKVERDQ VEDYAARKGM EVREIERWLG PVLNYVPKAA VEEDAAA // ID B9K019_AGRVS Unreviewed; 301 AA. AC B9K019; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 35. DE SubName: Full=S-methyltransferase {ECO:0000313|EMBL:ACM38217.1}; GN OrderedLocusNames=Avi_5017 {ECO:0000313|EMBL:ACM38217.1}; 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 {ECO:0000313|EMBL:ACM38217.1, ECO:0000313|Proteomes:UP000001596}; RN [1] {ECO:0000313|EMBL:ACM38217.1, ECO:0000313|Proteomes:UP000001596} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S4 / ATCC BAA-846 {ECO:0000313|Proteomes:UP000001596}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; ACM38217.1; -; Genomic_DNA. DR RefSeq; WP_012653459.1; NC_011988.1. DR RefSeq; YP_002546933.1; NC_011988.1. DR STRING; 311402.Avi_5017; -. DR EnsemblBacteria; ACM38217; ACM38217; Avi_5017. DR KEGG; avi:Avi_5017; -. DR PATRIC; 20822841; VBIAgrVit37146_1124. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; PYVDVWL; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; AVIT311402:GH2Y-3328-MONOMER; -. DR Proteomes; UP000001596; Chromosome 2. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001596}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ACM38217.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001596}; KW Transferase {ECO:0000313|EMBL:ACM38217.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 208 208 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 301 AA; 31479 MW; B484EF7A9E292CC1 CRC64; MTKVRILDGG MSRELLRLGA ELKQPEWSAL ALINAPDIVR QVHAEFIAAG ADVVTTNSYA LVPFHIGEER FQSEGPSLIA LSGELARQAA DASGRKVLVA GSLPPIFGSY EPQNFDPSTV DAYLDVLVAN LAPFVDVWLG ETLSLIAEGE AVQKAVAATG KPFWISFTLA DEAGQDIGGS PKLRSGELVQ DAALWAAGSG ASALLFNCSK PEVMKAAVDV AAATFRQKGV SLDIGVYANA FEGEQGEAAA NEGLHETRAD LTDDAYCRFA CDWADAGATM IGGCCGIGAA HIHQLSKALS A // ID B9KC48_THENN Unreviewed; 768 AA. AC B9KC48; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 38. DE SubName: Full=5-methyltetrahydrofolate S-homocysteine methyltransferase {ECO:0000313|EMBL:ACM22594.1}; GN OrderedLocusNames=CTN_0418 {ECO:0000313|EMBL:ACM22594.1}; OS Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NS-E). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=309803 {ECO:0000313|EMBL:ACM22594.1, ECO:0000313|Proteomes:UP000000445}; RN [1] {ECO:0000313|Proteomes:UP000000445} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49049 / DSM 4359 / NS-E RC {ECO:0000313|Proteomes:UP000000445}; RA Lim S.K., Kim J.S., Cha S.H., Park B.C., Lee D.S., Tae H.S., RA Kim S.-J., Kim J.J., Park K.J., Lee S.Y.; RT "The genome sequence of the hyperthermophilic bacterium Thermotoga RT neapolitana."; 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; CP000916; ACM22594.1; -; Genomic_DNA. DR RefSeq; WP_015918913.1; NC_011978.1. DR RefSeq; YP_002533960.1; NC_011978.1. DR ProteinModelPortal; B9KC48; -. DR STRING; 309803.CTN_0418; -. DR EnsemblBacteria; ACM22594; ACM22594; CTN_0418. DR KEGG; tna:CTN_0418; -. DR PATRIC; 23939591; VBITheNea118396_0410. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; TNEA309803:GJFG-430-MONOMER; -. DR Proteomes; UP000000445; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000445}; KW Methyltransferase {ECO:0000313|EMBL:ACM22594.1}; KW Transferase {ECO:0000313|EMBL:ACM22594.1}. SQ SEQUENCE 768 AA; 85266 MW; 159705BB0D339F8E CRC64; MRNRREVAKM LSEKVLLLDG AYGTEFMKLG HEELPEELNI KAPEVVFKVH RTYIESGSDA VLTNTFGATK MKLRKHGLEN ELDSIVRNAV RIARKAAGER LVFGDIGPTG ELPFPLGNTL FEEFYENFKE TARIMVEEGV DGIILETFSD ILELKAAVLA VRDVSKDVFL IAHMTFDENG RSLTGTDPVN FALTFDELDV DALGINCSLG PEEILPIFQE LSQYTDKFLV VEPNAGKPIL ENGKTVYPLK PEDFAVHIDS YYEAGVNIFG GCCGTTPEHI KLFRKVLGSR KPLPRKKKKI IAVSSPSKLV TFDHFVVIGE RINPAGRKKL WKKMQEGNLD VVANEAKDQV EKGAEVLDVN FGIESQVDPS YVEKVVQSLP YTASVPLSLD VQSLNLAERS LRVYPGRPLF NSSKVTEKDL EEKINMLKKY GGVLIVLLME NDVPKTFEER KKNFEKALKI LEEHRFLDRV LFDPGVLPLG AEGKPTEVLK TIEYISKMDF KTTVGLSNLS FGLPDRSFYN TAFLVLGISK GLSSAIMNPL DENLMKTLDS TLVILEKKDL PKAEVREDKL VEAILSGRRE DVEKEVENLL KEKDPLSIIE EHLRPAMEKI GLLYDKGKIF LPQLILAAQT VKPVFDKLAS MLSSENQGET FVIATVKGDV HDIGKNIVAS VIRSSGYRVV DLGKDVDTER IVEAVEKEKP VALGLSAMMT TTVGRIKEVV ESLKKKGLKV PVIAGGASLN EKLAKELGAD YYAKNASEAV KILKSLGR // ID B9KNL7_RHOSK Unreviewed; 335 AA. AC B9KNL7; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 41. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACM00295.1}; GN OrderedLocusNames=RSKD131_0435 {ECO:0000313|EMBL:ACM00295.1}; OS Rhodobacter sphaeroides (strain KD131 / KCTC 12085). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=557760 {ECO:0000313|EMBL:ACM00295.1, ECO:0000313|Proteomes:UP000001597}; RN [1] {ECO:0000313|EMBL:ACM00295.1, ECO:0000313|Proteomes:UP000001597} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KD131 / KCTC 12085 {ECO:0000313|Proteomes:UP000001597}; 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., RA Lee J.K.; RT "Complete genome sequence of Rhodobacter sphaeroides KD131."; RL J. Bacteriol. 191:1118-1119(2009). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; ACM00295.1; -; Genomic_DNA. DR RefSeq; WP_012643716.1; NC_011963.1. DR RefSeq; YP_002524796.1; NC_011963.1. DR STRING; 557760.RSKD131_0435; -. DR EnsemblBacteria; ACM00295; ACM00295; RSKD131_0435. DR KEGG; rsk:RSKD131_0435; -. DR PATRIC; 23179958; VBIRhoSph125910_1849. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265278; -. DR KO; K00548; -. DR OMA; GTNLFAM; -. DR OrthoDB; EOG693GKH; -. DR BioCyc; RSPH557760:GH1P-440-MONOMER; -. DR Proteomes; UP000001597; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001597}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ACM00295.1}; KW Transferase {ECO:0000313|EMBL:ACM00295.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 212 212 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 278 278 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 279 279 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 335 AA; 35357 MW; ACEE492799BDFC72 CRC64; MTDALSRLLQ TRDWLMADGA TGTNLFNMGL SSGEPPELWT VERPDNIRSL YRAAVEAGSD IFLTNSFGGN AARLKLHEAQ GRVGELNRIA AELGREVADA AGRPVVVAGS MGPTGEIFEP MGTLTHRMAV EIFHEQAEAL KAGGADVLWV ETISAAEEFK AAAEAARLAG MPWCGTMSFD TAGRTMMGIT AATLVDLVTK LPNPPLAFGA NCGVGASDLL RTVLGFAAQG IEVPIIAKGN AGIPKYHDGH IHYDGTPELM AEYAVLARDA GARIIGGCCG TMPEHLKAMR AALEGRPRGP RPSLETISET LGGFSSASDG SDDAGPTRER RRRRS // ID B9KTK1_RHOSK Unreviewed; 341 AA. AC B9KTK1; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 44. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACM03379.1}; GN OrderedLocusNames=RSKD131_3519 {ECO:0000313|EMBL:ACM03379.1}; OS Rhodobacter sphaeroides (strain KD131 / KCTC 12085). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=557760 {ECO:0000313|EMBL:ACM03379.1, ECO:0000313|Proteomes:UP000001597}; RN [1] {ECO:0000313|EMBL:ACM03379.1, ECO:0000313|Proteomes:UP000001597} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KD131 / KCTC 12085 {ECO:0000313|Proteomes:UP000001597}; 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., RA 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; ACM03379.1; -; Genomic_DNA. DR RefSeq; WP_012641082.1; NC_011958.1. DR RefSeq; YP_002520452.1; NC_011958.1. DR STRING; 557760.RSKD131_3519; -. DR EnsemblBacteria; ACM03379; ACM03379; RSKD131_3519. DR KEGG; rsk:RSKD131_3519; -. DR PATRIC; 23177039; VBIRhoSph125910_0412. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; RSPH557760:GH1P-3572-MONOMER; -. DR Proteomes; UP000001597; Chromosome 2. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001597}. SQ SEQUENCE 341 AA; 36018 MW; 0BC9DE29B311E4D8 CRC64; MLTFSLPPSC AVQALEALVR QRILILDGAM GTQIQALGLS EEDYAGCGCR HHAERPQKGN NDLLILTQPQ AIEEIHFRYA VAGADIVETN TFSATTIAQA DYGMESAVED LNREGARLVR RALDRATALD GRPRFVAGAV GPTNRTASIS PDVNDPGYRA VSFDDLRVAY ATQVRALIAG GADLILIETI FDTLNAKAAI FACFEAFAEA GRRLPLMISG TITDASGRTL SGQTPTAFWH SVRHARPFTL GLNCALGAAA MRPHLAELAG VADAAICAYP NAGLPNAFGQ YDEGPDETAA QVARFAREGL VNVVGGCCGT TPDHVRAIAC AVADLPPRTL A // ID B9L045_THERP Unreviewed; 624 AA. AC B9L045; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 39. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=trd_1049 {ECO:0000313|EMBL:ACM05450.1}; OS Thermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2). OC Bacteria; Chloroflexi; Thermomicrobiales; Thermomicrobiaceae; OC Thermomicrobium. OX NCBI_TaxID=309801 {ECO:0000313|EMBL:ACM05450.1, ECO:0000313|Proteomes:UP000000447}; RN [1] {ECO:0000313|EMBL:ACM05450.1, ECO:0000313|Proteomes:UP000000447} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27502 / DSM 5159 / P-2 RC {ECO:0000313|Proteomes:UP000000447}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ACM05450.1; -; Genomic_DNA. DR RefSeq; WP_015922003.1; NC_011959.1. DR RefSeq; YP_002522259.1; NC_011959.1. DR ProteinModelPortal; B9L045; -. DR STRING; 309801.trd_1049; -. DR EnsemblBacteria; ACM05450; ACM05450; trd_1049. DR KEGG; tro:trd_1049; -. DR PATRIC; 23913270; VBITheRos91376_0986. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; TROS309801:GI0S-1037-MONOMER; -. DR Proteomes; UP000000447; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000447}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ACM05450.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000000447}; KW Transferase {ECO:0000313|EMBL:ACM05450.1}. SQ SEQUENCE 624 AA; 67965 MW; 19A335283D80191E CRC64; MKHPFRDRIE QGVLLADGAM GTQLYERGIR LDRCFESANL THPQLVVEIH RAYILAGAEL IETNTFGANR FKLEAYGMAE RVREINRRAV RHAREAREIC GVPVFIAGAI GPSGRLLAPV GTVAPESLRP VFREQIEALL EGGVDLLIFE TMSQLAEIRE AIMAAREVCD LPIVAQMTFA ADGRTIAGHG PEEVVAALAE LGVDVIGVNC SVGPRPTLEV LRAMIAANRW GTALSAMPNA GWPTVVGHRV IYGASPEYFA DFAREAASLG VRLIGGCCGT TPEHIAAMRR ALDDIKGQVR PAVEVRARVS TPVMDAVAPE EPTRLRQKLG REFVVSVEID PPKGLNPSKA IEGARLLRQV GVEFINVADS PMARVRMSAL ALCVILQQET GVETILHLTT RDRNLMGLQA DLLGAHALGV RNILALTGDP PTLGDYPHAT PVYDLDSIGL VRLLQNFRQG FDAGGASIGR PAMFTIGVAC DPTRPDLQQE IERLHAKLAA GADFVMTQPV FDFSTWRNFV AQYEIRYGPI EVPVLLGVLP LQSFRHASFL HNEVPGITLT EEALERMRRA GPNGRAEGVA MARELIAEAC EFVQGIYLMP SFGRYEVVAE VLSALPERLR VSTR // ID B9M1X9_GEODF Unreviewed; 607 AA. AC B9M1X9; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 44. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN Name=metF-2 {ECO:0000313|EMBL:ACM19275.1}; GN OrderedLocusNames=Geob_0913 {ECO:0000313|EMBL:ACM19275.1}; OS Geobacter daltonii (strain DSM 22248 / JCM 15807 / FRC-32). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=316067 {ECO:0000313|EMBL:ACM19275.1, ECO:0000313|Proteomes:UP000007721}; RN [1] {ECO:0000313|EMBL:ACM19275.1, ECO:0000313|Proteomes:UP000007721} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22248 / JCM 15807 / FRC-32 RC {ECO:0000313|Proteomes:UP000007721}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {ECO:0000256|RuleBase:RU004255}. CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ACM19275.1; -; Genomic_DNA. DR RefSeq; WP_012646004.1; NC_011979.1. DR RefSeq; YP_002536376.1; NC_011979.1. DR ProteinModelPortal; B9M1X9; -. DR STRING; 316067.Geob_0913; -. DR EnsemblBacteria; ACM19275; ACM19275; Geob_0913. DR KEGG; geo:Geob_0913; -. DR PATRIC; 22008323; VBIGeoSp137169_0939. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; GSP316067:GHSV-923-MONOMER; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000007721; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004255}; KW Complete proteome {ECO:0000313|Proteomes:UP000007721}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ACM19275.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000007721}; KW Transferase {ECO:0000313|EMBL:ACM19275.1}. SQ SEQUENCE 607 AA; 64278 MW; B68064BF7264ED04 CRC64; MNFLQALQHE VLIGDGAIGT MLYAKGVSPD ANFEHLNLVR PSLVLDLHRE YVTAGARVIE TNTFGANFAK LDAIGIGAKL HDINVKGAQL ARQAASGRDV YVAGSIGPLV GAKGEEKDLV EDQIRRMFDA QVDALVEGGV DLFLLETFSD LRQLEIGVAV AKKTGLPVVA SMAFGENSRI AGGIPVESVA ERLAAAGADV IGANCGAGPL EILRTVKRLG KVTALPIAVY PNSGFPEYVN GRYLYRATPE YFAGMAEEMA AAGAVLIGGC CGTTPDHIRE IAAKVKGRKP AQRQISTSVP LAESGETRAV AAPGFLSSWG KGPVVTVELD PPRGLDCSNV LTGSRILKEA GADAINLAEN PLARVRMGNI ALANLIQREI GIEVIVHITC RDRNLLGLQS DLMGASLLGI RSILAVTGDP ASLGEQAGAS SVFDLNSFTL IKLLDDLNRG VNALGNPLGG GTGFTIGAAF NPNTARMDVQ TGRLLKKVTN GASFAQTQPI YDLKRLDDML EQTAHLNIPI LPGVLPLVSE RNAEFLHNEV PGIVIPEEIR GRMKGKEKEE GAREGLAIAR EFIDAARDRV GGFYLIPPFG RHGIAAELVR YIKGIGE // ID B9M4J9_GEODF Unreviewed; 807 AA. AC B9M4J9; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=5-methyltetrahydrofolate--homocysteine S-methyltransferase, cobamide-dependent {ECO:0000313|EMBL:ACM19725.1}; GN Name=metH {ECO:0000313|EMBL:ACM19725.1}; GN OrderedLocusNames=Geob_1365 {ECO:0000313|EMBL:ACM19725.1}; OS Geobacter daltonii (strain DSM 22248 / JCM 15807 / FRC-32). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=316067 {ECO:0000313|EMBL:ACM19725.1, ECO:0000313|Proteomes:UP000007721}; RN [1] {ECO:0000313|EMBL:ACM19725.1, ECO:0000313|Proteomes:UP000007721} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22248 / JCM 15807 / FRC-32 RC {ECO:0000313|Proteomes:UP000007721}; 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; ACM19725.1; -; Genomic_DNA. DR RefSeq; WP_012646454.1; NC_011979.1. DR RefSeq; YP_002536826.1; NC_011979.1. DR ProteinModelPortal; B9M4J9; -. DR STRING; 316067.Geob_1365; -. DR EnsemblBacteria; ACM19725; ACM19725; Geob_1365. DR KEGG; geo:Geob_1365; -. DR PATRIC; 22009263; VBIGeoSp137169_1403. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; GSP316067:GHSV-1380-MONOMER; -. DR Proteomes; UP000007721; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007721}; KW Methyltransferase {ECO:0000313|EMBL:ACM19725.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007721}; KW Transferase {ECO:0000313|EMBL:ACM19725.1}. SQ SEQUENCE 807 AA; 85067 MW; FF25074E3C4791CE CRC64; MKQPFLQSIK DRVLVLDGAM GTMLQQRGLK AGQSPEELNL TLPEVVAGVH QEYLDAGADI IVTNTFGGSR EKLSHYGLEG KLAEINARGV EIARQVAGAR AYVAASMGPT GKFVEPVGDM TFDRMAAQFR EQAEALVGAG ADLITLETFL DIKEIRAAII AIREVSAEIP IIAMLTFDDK GRTVLGTPPE AAAITLEAVG ADIIGSNCGL GVEGIYEILS AMRRVTSLPL ISQANAGLPV LKEGKTIFPA TPDEMTAYHD RMLQLGVRII GGCCGTTPAH IGAMKDALAG KNQSLPDIAS SGGTTWLSSR GGHAALGNGR PVAIIGERIN PTGKKAFAAE LREGKVSYIR REAMEQVVAG ATLLDVNVGA PGIDEPAAME QAVFCAAGAA SVPLVLDSSN PEALERGLKS ADGKVLINSV NGEEKSLGRI LPLAKKYGAA VIGLTLDENG IPETAEARTA IAAKIANRAV SLGIRRNDVI IDCLTLAVSA EQKRALETLE AIRRVKGQLG LSTVLGVSNI SFGLPCRPLI SSAFFAMAME AGLDAAIINP KEQAMMDVWR SVMVLLNRDA NAATYIDAYK GAVAASAGQV EAAPQDIRGI LARAVIDGDV ENIVVHVEAA LAQGLSPLEI SNNGLLPGLE EVGRRFEKNI VFLPQVMLSA ETMKTAFSRL KQEMQGMKLE SSGRILMATV EGDIHDIGKN IVCTLLENHG FEVIDLGKNV PAARIVAEAK AHDVDAVGLS ALMTTTMSEM ETVVQQLRTA GVKTFTMVGG AVLTQDYAIE IGADIYAKDA MEAVSKIKAI IGKIKRS // ID B9MAE2_ACIET Unreviewed; 344 AA. AC B9MAE2; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 35. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACM31589.1}; GN OrderedLocusNames=Dtpsy_0102 {ECO:0000313|EMBL:ACM31589.1}; OS Acidovorax ebreus (strain TPSY) (Diaphorobacter sp. (strain TPSY)). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Acidovorax. OX NCBI_TaxID=535289 {ECO:0000313|EMBL:ACM31589.1, ECO:0000313|Proteomes:UP000000450}; RN [1] {ECO:0000313|EMBL:ACM31589.1, ECO:0000313|Proteomes:UP000000450} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TPSY {ECO:0000313|EMBL:ACM31589.1, RC ECO:0000313|Proteomes:UP000000450}; 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; ACM31589.1; -; Genomic_DNA. DR RefSeq; WP_012655210.1; NC_011992.1. DR RefSeq; YP_002551589.1; NC_011992.1. DR STRING; 535289.Dtpsy_0102; -. DR EnsemblBacteria; ACM31589; ACM31589; Dtpsy_0102. DR KEGG; dia:Dtpsy_0102; -. DR PATRIC; 21777184; VBIDiaSp55748_0109. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; AEBR535289:GHOO-102-MONOMER; -. DR Proteomes; UP000000450; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000450}; KW Methyltransferase {ECO:0000313|EMBL:ACM31589.1}; KW Transferase {ECO:0000313|EMBL:ACM31589.1}. SQ SEQUENCE 344 AA; 37027 MW; 8F84D23DF4D17F7C CRC64; MTLPHYTRAQ ALPAILEQRI AILDGAMGTM IQRFKLTEAQ YRGERFKDFA RDVKGNNELL SLTRPDVIRD IHEGYLAAGA DLIETNTFGA TSIAQDDYGL AELAYEMNLE SAKLARAACD KFSTPDKPRF VAGALGPTPK TASISPDVND PGARNITFEQ LRAAYHEQAR GLIEGGADVL LVETIFDTLN AKAALFAIDE VFEETGECLP IMISGTVTDA SGRILSGQTV TAFWHSVRHA RPLSIGLNCA LGAALMRPYI QELNRAAPDT FISCYPNAGL PNPMSDTGFD ETPEVTSRLV HEFAAEGLVN IVGGCCGTTP DHIGAIARAV APVGTRRLFQ TEAA // ID B9MN08_CALBD Unreviewed; 413 AA. AC B9MN08; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 01-APR-2015, entry version 37. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACM59464.1}; GN OrderedLocusNames=Athe_0324 {ECO:0000313|EMBL:ACM59464.1}; 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 {ECO:0000313|EMBL:ACM59464.1, ECO:0000313|Proteomes:UP000007723}; RN [1] {ECO:0000313|Proteomes:UP000007723} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1888 / DSM 6725 / Z-1320 RC {ECO:0000313|Proteomes:UP000007723}; 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 ----------------------------------------------------------------------- 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; ACM59464.1; -; Genomic_DNA. DR RefSeq; WP_015906929.1; NC_012034.1. DR RefSeq; YP_002572237.1; NC_012034.1. DR STRING; 521460.Athe_0324; -. DR EnsemblBacteria; ACM59464; ACM59464; Athe_0324. DR KEGG; ate:Athe_0324; -. DR PATRIC; 20897630; VBIAnaThe135187_0345. DR eggNOG; COG0646; -. DR HOGENOM; HOG000269747; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CBES521460:GH8H-326-MONOMER; -. DR Proteomes; UP000007723; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007723}; KW Methyltransferase {ECO:0000313|EMBL:ACM59464.1}; KW Transferase {ECO:0000313|EMBL:ACM59464.1}. SQ SEQUENCE 413 AA; 46001 MW; B5279DAD5D0D039D CRC64; MALLQDELYR RVLIFDGAMG TQLIQNGLTE DECPDLWSVT RQDVVSSIHR QYFEAGSDCV ETNTFGANRE KLKKYGLENE VENINKCAVK LAKEVAKEYS GYVGLSVGPT GRLFIPSGDL SFDEAESIFY EQILSGIEAG ADFVSIETMS DIKEAKAAFF AYKKAKEELK KDIPCLISLT FEQNKRLLMG TPPEVAAYYF SSIGCDIVGA NCSGGAIQLL EIIKQMQFFS FVPLSVKPNA GLPKVVDGKT IYESCIPEFV NLADEFVENG VRLYGGCCGT NPEYIKSISK VLKGKEVSFE SSTQKKFITS IYSLLDISQK FSVYEFKLTN DFSPEAVFEL AGLEEDVIFV DIDENVEPEV LKEFLIESQD FSKKPYIFNI ETKSHVDVIE RYYFGAYGAV SSIHGKSAVN VQI // ID B9MN09_CALBD Unreviewed; 605 AA. AC B9MN09; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 42. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=Athe_0325 {ECO:0000313|EMBL:ACM59465.1}; 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 {ECO:0000313|EMBL:ACM59465.1, ECO:0000313|Proteomes:UP000007723}; RN [1] {ECO:0000313|Proteomes:UP000007723} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1888 / DSM 6725 / Z-1320 RC {ECO:0000313|Proteomes:UP000007723}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ACM59465.1; -; Genomic_DNA. DR RefSeq; WP_015906930.1; NC_012034.1. DR RefSeq; YP_002572238.1; NC_012034.1. DR ProteinModelPortal; B9MN09; -. DR STRING; 521460.Athe_0325; -. DR EnsemblBacteria; ACM59465; ACM59465; Athe_0325. DR KEGG; ate:Athe_0325; -. DR PATRIC; 20897632; VBIAnaThe135187_0346. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; CBES521460:GH8H-327-MONOMER; -. DR Proteomes; UP000007723; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007723}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ACM59465.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:ACM59465.1}. SQ SEQUENCE 605 AA; 67102 MW; A132D445920F1686 CRC64; MKKSFREFLK EQAIVIFDGA MGTQLLLRGF SVDFPLEWAN VANPELVKQI HTDYILAGAT CVETNTFGAN ECKLKVFGFE NEVERINRSA VRIAKEVAEN KVYVIGSVGP LGKPVGNGFE IDDKKAKDVY KRQLYFLLDE GVDAIIFETA ASTHEVQIAI EALKELNDKI PYIIQFSFTK ELSTVYGEDI YRVIEFLKST NADVVGLNCG NGPQKTLEAL KIFSQHLKGP FSVQPNAGYP QLIQGRPVFS TSANYFASFV PEYIKLGAKI IGGCCGTGPE HIKAVKEKIK EVSPSIEIEV VERKEEQKAV LKDTPSELSQ KLGKKFIFTV EISPPKGIEL EKTKEGVKLL KEAGADTVNI ADSPMARVRI SPIALAHILK EELGMESILH FTCRDRNLIS LQSELLGAAA LGVKNVLALT GDPPSIGDHP QAKPVFDVNS EGLVLILSRL NNGTDYMGNP IGKATNFTIG VALNLNADDL GKEIEKLKHK IENGAHFIET QPIYEPETLE RFFEKVDFKL PPILGGILPL RSPRHAEFLH NEVPGITIPD KIRERMRTSK EPAKEGVEIA CEIVEKIKHM VSGIYIMPPF EKYEMAVEII RNFKI // ID B9NLU8_9RHOB Unreviewed; 309 AA. AC B9NLU8; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EEE36908.1}; GN ORFNames=RKLH11_743 {ECO:0000313|EMBL:EEE36908.1}; OS Rhodobacteraceae bacterium KLH11. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae. OX NCBI_TaxID=467661 {ECO:0000313|EMBL:EEE36908.1}; RN [1] {ECO:0000313|EMBL:EEE36908.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=KLH11 {ECO:0000313|EMBL:EEE36908.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; EEE36908.1; -; Genomic_DNA. DR RefSeq; WP_008756089.1; NZ_DS999531.1. DR EnsemblBacteria; EEE36908; EEE36908; RKLH11_743. DR PATRIC; 28447040; VBIRhoBac95025_1048. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EEE36908.1}; KW Transferase {ECO:0000313|EMBL:EEE36908.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 201 201 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 274 274 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 275 275 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 309 AA; 32946 MW; 21D67C594BFE6D7D CRC64; MADITLLDGS IGQELVKRSG DQPTPLWSTQ VMMDRPDLVG DVHADYFRRG ATVATTNTYA LHRSRLRRIG MEDKLASLVD AALSQAERAC VGSEGQIAGA LGPVLASYRP DLKPDPDEAA ARFSELVQLM ADRVDLFLIE TVSSVLEGEG ALRGTANCGK PVWLAVSVND EDGTRLRSGE RLADIQPLIA RFDVAAVLIN CSKPEAIPAA LDVIALMGRP FGAYANGFSH IADAFLTEAP TVDVLEQRHD LGPAAYAAHA MQWVAQGATI VGGCCEVGPD HIETLARALR DAGHRIVPGA RDGCDLKAR // ID B9NSA5_9RHOB Unreviewed; 337 AA. AC B9NSA5; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Methionine synthase I {ECO:0000313|EMBL:EEE37615.1}; GN ORFNames=RKLH11_1451 {ECO:0000313|EMBL:EEE37615.1}; OS Rhodobacteraceae bacterium KLH11. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae. OX NCBI_TaxID=467661 {ECO:0000313|EMBL:EEE37615.1}; RN [1] {ECO:0000313|EMBL:EEE37615.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=KLH11 {ECO:0000313|EMBL:EEE37615.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; EEE37615.1; -; Genomic_DNA. DR RefSeq; WP_008756791.1; NZ_DS999531.1. DR EnsemblBacteria; EEE37615; EEE37615; RKLH11_1451. DR PATRIC; 28449392; VBIRhoBac95025_2369. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 212 212 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 278 278 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 279 279 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 337 AA; 35602 MW; 4D28902CDFF1D198 CRC64; MTNALSTLLE TVDVVLADGA TGTNLFAMGL QSGDAPELWN VDAPDKIRAL YEGSVNAGSD LFLTNTFGGT AARLKLHEAQ NRVSELNRIG AELGREVADK ADRPVIVAGS VGPTGEIMEP VGTLSHAEAV EMFHEQAEAL KAGGADVLWL ETISAPEEFR AAAEAFSMAD MPWCGTMSFD TAGRTMMGVT SSDLANIVET LPNPPLAFGA NCGTGASDIL RTILGFAAQG TERPLISKGN AGIPKYVDGH IHYDGTPELM GQYAAMARDA GATIIGGCCG TMPEHLRKMR EALDTQPGRE RPTLDQITDA LGPFTSPSDG TGDQAAPERR TRRRRRA // ID B9P1X2_PROMR Unreviewed; 1189 AA. AC B9P1X2; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 01-APR-2015, entry version 35. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEE39376.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEE39376.1}; GN Name=metH {ECO:0000313|EMBL:EEE39376.1}; GN ORFNames=P9202_147 {ECO:0000313|EMBL:EEE39376.1}; OS Prochlorococcus marinus str. MIT 9202. OC Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae; OC Prochlorococcus. OX NCBI_TaxID=93058 {ECO:0000313|EMBL:EEE39376.1}; RN [1] {ECO:0000313|EMBL:EEE39376.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MIT 9202 {ECO:0000313|EMBL:EEE39376.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; DS999537; EEE39376.1; -; Genomic_DNA. DR EnsemblBacteria; EEE39376; EEE39376; P9202_147. DR PATRIC; 26394485; VBIProMar1821_1884. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEE39376.1}; KW Transferase {ECO:0000313|EMBL:EEE39376.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 228 228 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 747 747 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1189 AA; 132597 MW; 7BE039232597F05B CRC64; MMESFRTYLN RNEKPLIIFD GGTGTSFQNL NLTADDFGGK ELEGCNENLV LSSPKVVERV HNSFLEAGCH VIETNTFGAS SIVLDEYDIA DKAYEINKNA ALLAKKAAAK YTSVDKPRFV AGSIGPTTKL PTLGHIDFDE LKQSYKEQIY GLIDGGVDLL LIETCQDVLQ IKSALLASKE VLDSRNIDIP IMVSITMETT GTMLVGSDIA SALTILEPFN IDILGLNCAT GPEQMKEHIK YLSENSPFAI SCIPNAGLPE NIGGVAHYRL KPIELKMQLM NFIYDFNVQL IGGCCGTTPE HIKYLSSIID EIIYKERSNK NGNNNLSGYI PSASSIYNSV PYKQDNSILI VGERLNASGS KKVRELLNND DWDGLVSIAK QQQKENAHVL DVNVDYVGRD GVKDMKEITS RLVTNINLPL MIDSTDADKM ESGLKSAGGK CIINSTNYED GNERFDQVLN LALGYGSGLV VGTIDEDGMA RNADKKYNIV KRAINRTREC GLSDYELFFD PLALPISTGI EEDRLNAKET INAISKIREN FPDIHIILGI SNISFGLSPL SRINLNSIFL DECIKAGLDS AIIAPNKILP LSKISEKTKK LCLDLIYDKR EFENDICIYD PLVELTKTFQ DLSIQDFKKA SSENKNLTLE ESLKNHIIDG EKIGLEDQLN KALKKYKPLE IINTFLLDGM KVVGDLFGSG QMQLPFVLQS AETMKFAVSI LEPYMETVDE NISNGKLLIA TVKGDVHDIG KNLVDIILTN NGYDVINLGI KQDVSAIINA QKKHNADCIA MSGLLVKSTA FMKDNLEAFN NENISVPVIL GGAALTPKFV NEDCSKIYKG KILYGKDAFT DLKFMNEYMD NKRKGNWSNT EGFINNEGIN INLASSKSNS QSVKKSISIN TQTSKLYLKE NFIRSKFINE EEPIQAPFLG TKVLNDFDID LNKLIFYLDT KALFSGQWQI KKGKNQSVDE YNNYLDSYAK PLLNRWIETI IEKKLISPKA VYGYFRCGRK DNSIFLFDDK SLNKISQFNF PRQKSGNNLC IADFYCDLKN DKPIDIFPMQ AVTMGNIASE YSQKLFKEDK YSDYLLFHGL TVQLAEALAE YVHALIRVEC GFSTEEPAKN REILAQKYRG ARYSFGYPAC PKVSDSNIQL SLLDAKRINL TMDESEQLHP EQSTTAIISL HSKAKYFSA // ID B9QVB9_LABAD Unreviewed; 392 AA. AC B9QVB9; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=Homocysteine S-methyltransferase, putative {ECO:0000313|EMBL:EEE45710.1}; GN ORFNames=SADFL11_2999 {ECO:0000313|EMBL:EEE45710.1}; OS Labrenzia alexandrii (strain DSM 17067 / NCIMB 14079 / DFL-11) OS (Stappia alexandrii). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Labrenzia. OX NCBI_TaxID=244592 {ECO:0000313|EMBL:EEE45710.1}; RN [1] {ECO:0000313|EMBL:EEE45710.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DFL-11 {ECO:0000313|EMBL:EEE45710.1}; 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; EEE45710.1; -; Genomic_DNA. DR RefSeq; WP_008193848.1; NZ_EQ973121.1. DR EnsemblBacteria; EEE45710; EEE45710; SADFL11_2999. DR PATRIC; 30173912; VBILabAle118631_4815. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEE45710.1}; KW Transferase {ECO:0000313|EMBL:EEE45710.1}. SQ SEQUENCE 392 AA; 41327 MW; FB7200FAF2F09FA4 CRC64; MFYGFGPGAG SGQPKNRKTK PRVDIRAGSA IAGLRFAFGL ETTRKDQKDM SKFEDFLAQK GALLADGATG TNLFDMGLVS GDAPELWNVD EPEKIKALYK SFVDAGSDII LTNTFGCNRH RLKLHSAQDR VKELNIAAVE LAKDVIAESG RDVLIGGSIG PTGELFQPLG ALSYEEGVEA FREQIEGLVD GGVDVLWVET MSAIEEMKAA AEAAQDFDLP LVITASFDTA GKTMMGLSPK GLGDLQNQFA CSPVAIGSNC GVGASDLLAA ILEITEAYPD AVVVAKANCG IPQIKGDEVV YTGTPELMAD YARMALDAGA RIIGGCCGTS PSHLKAMRLA LDDYKKGVRP TLDQVISDIG PLVSPPNKEA DAARAAEGEG AGSGRRRGRR RG // ID B9R5I6_LABAD Unreviewed; 294 AA. AC B9R5I6; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Homocysteine S-methyltransferase, putative {ECO:0000313|EMBL:EEE45207.1}; GN ORFNames=SADFL11_2496 {ECO:0000313|EMBL:EEE45207.1}; OS Labrenzia alexandrii (strain DSM 17067 / NCIMB 14079 / DFL-11) OS (Stappia alexandrii). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Labrenzia. OX NCBI_TaxID=244592 {ECO:0000313|EMBL:EEE45207.1}; RN [1] {ECO:0000313|EMBL:EEE45207.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DFL-11 {ECO:0000313|EMBL:EEE45207.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; EEE45207.1; -; Genomic_DNA. DR RefSeq; WP_008192974.1; NZ_EQ973121.1. DR EnsemblBacteria; EEE45207; EEE45207; SADFL11_2496. DR PATRIC; 30181228; VBILabAle118631_3526. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EEE45207.1}; KW Transferase {ECO:0000313|EMBL:EEE45207.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 202 202 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 275 275 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 276 276 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 294 AA; 31435 MW; E1FE84B15BDEEB88 CRC64; MSNITILDGG MGQELVHRSG RVPSGLWSCE LMMERPDLVR AIHDDFFAAG AHVATVNSYT LHRDRLRPNG LDDQFERLHH LACDLACQSR DAHGSGLVAG CLGPLGWSYS HDGAPSEDQS IDLYDEICRV QKDHVDLFVI ETIASVAQAR ASLTAALRHD KPVWIALTVD DGDGGALRSG EPLQEVVEVV NDLGPEAVLI NCSVPEAVTR GMAVLGPSGL KTGAYANGFT AIKPEFLKKG SSVSKLTART DMTPEVYAGH GADWIDLGAT IVGGCCEVSP SHIAELSRRF NPAV // ID B9R5L4_LABAD Unreviewed; 1242 AA. AC B9R5L4; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 36. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEE48043.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEE48043.1}; GN Name=metH {ECO:0000313|EMBL:EEE48043.1}; GN ORFNames=SADFL11_5333 {ECO:0000313|EMBL:EEE48043.1}; OS Labrenzia alexandrii (strain DSM 17067 / NCIMB 14079 / DFL-11) OS (Stappia alexandrii). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Labrenzia. OX NCBI_TaxID=244592 {ECO:0000313|EMBL:EEE48043.1}; RN [1] {ECO:0000313|EMBL:EEE48043.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DFL-11 {ECO:0000313|EMBL:EEE48043.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; EQ973121; EEE48043.1; -; Genomic_DNA. DR RefSeq; WP_008197402.1; NZ_EQ973121.1. DR EnsemblBacteria; EEE48043; EEE48043; SADFL11_5333. DR PATRIC; 30181284; VBILabAle118631_3554. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEE48043.1}; KW Transferase {ECO:0000313|EMBL:EEE48043.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 249 249 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 764 764 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1242 AA; 136148 MW; 4687DBA3B6C2B1C3 CRC64; MTKSDAFARL QEIAKSRILV LDGAMGTEIQ LLKLDEAAYR GERFKDWPSD VKGNNDLLSL TMPDAIRQIH VDYLEAGADI VETNTFSSTT IAQADYGMEE LAYELNVESA RLAREACEQV TAQDTSRPRY VAGALGPTNR TASISPDVNN PGYRAVSFDD LRIAYAEAVR GLIEGGADIL LVETIFDTLN AKAALFAIEE VFEEIGRELP VMISGTITDL SGRTLSGQTP EAFWNSVRHT NPLTIGLNCA LGAKEMRAHV DELGRVADTL VCAYPNAGLP NEFGEYDESP EHMAGLIEEF ASAGLVNMVG GCCGTTPAHI KAIAEAVEGK KPREIPTVDR YMRLSGLEPF SLTPEVNFVN VGERTNVTGS ARFRKLIKEG DYATALDVAR SQVENGAQII DINMDEGLLD SEDAMVTFLN LVAAEPDIAK VPVMIDSSKW TVIEAGLKCI QGKGVVNSIS MKEGEEAFLE QAKLIRRYGA AVVVMAFDEQ GQADTFERKT EICARSYKIL TEKAGFAPED IVFDPNIFAV ATGIEEHDNY GVDFIEATGW IRENLPHAHV SGGVSNLSFS FRGNEAVREA MHSVFLYHCI KRGMDMGIVN AGQLAVYNDL DTELRELCED VVLNRRSDAT DRMLDAAERW KGEGGKKKEA DLTWRTWDVA KRLEHALVHG IDDYVVEDTE EARQSFDRPL HVIEGPLMDG MNVVGDLFGS GQMFLPQVVK SARVMKKAVA YLMPFMEKEK EEQGLTGYSS QGKILMATVK GDVHDIGKNI VGVVLQCNNF EVIDLGVMVP AAKILETAKQ EKVDIIGLSG LITPSLDEMC HVAAEMEREG LDIPLLIGGA TTSKIHTAVK IHPNYAKGQA IYVTDAGRAV GVASKLMSEG GRAPYYGEVR TEYADIAEKH AAGRGAARRV QLLDARANAF KVDFEGKAPV RPNQLGTTVF DDFPLEELVP VIDWTPFFAT WEIKGRYPQV LTDDRYGVAA TALFDDARRM LDEIVEKKLL TARGVAKLWP ANAVGDDILV YSGENRGEVA ATFHTLRQQM ARTSGGRANV AMSDFVAPLD SGINDWIGGF AVTAGHGEDE LAGRYAKQGD DYNKILSQAL ADRLAEAFAE KLHQIVRKDL WGYAAGETLS SEELIAEKYQ GIRPAPGYPA QPDHTEKDTL FRLLDAEKLT GIQLTESRAM LPGSSVSGLY FAHPDSHYFG VGKIEKDQIV DYAKRKGWDV EYAERWLAPI LNYDPARMVA AE // ID B9RTM3_RICCO Unreviewed; 348 AA. AC B9RTM3; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 07-JAN-2015, entry version 25. DE SubName: Full=5-methyltetrahydrofolate:homocysteine methyltransferase, putative {ECO:0000313|EMBL:EEF45255.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EEF45255.1}; GN ORFNames=RCOM_0911480 {ECO:0000313|EMBL:EEF45255.1}; 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 {ECO:0000313|Proteomes:UP000008311}; RN [1] {ECO:0000313|Proteomes:UP000008311} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311}; 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; EQ973814; EEF45255.1; -; Genomic_DNA. DR RefSeq; XP_002517092.1; XM_002517046.1. DR GeneID; 8280877; -. DR KEGG; rcu:RCOM_0911480; -. DR InParanoid; B9RTM3; -. DR KO; K00547; -. DR Proteomes; UP000008311; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008311}; KW Methyltransferase {ECO:0000313|EMBL:EEF45255.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008311}; KW Transferase {ECO:0000313|EMBL:EEF45255.1}. SQ SEQUENCE 348 AA; 38038 MW; 1502E80D0B9CA2E6 CRC64; MGLENQDMTR SFMSDFLQKC GGYAVIDGGF ATELERHGAD LNDPLWSAKC LISSPHLVRR VHLDYIDAGA NIILTASYQA TIQGFEAKGL STEEAEQLLR RSVEIACEAR EIYYDNCTKG SWDLMEDGKM SRHPVLVAAS IGSYGAYLAD GSEYSGDYGD AVSIQTLKDF HRRRLQILAK SGADLIAFET IPNKLEAKAY AELLEEEGIN IPAWFSFNSK DGINVVSGDS ILECASIADS SKQVVAVGIN CTPPRFIHGL ILSMREATSK PIVIYPNSGE TYDAALKQWV KSCGASDEDF VSYIGKWREA GASLFGGCCR TTPNTIRAIC RNISNKSSPP LISNRDVN // ID B9SFH3_RICCO Unreviewed; 343 AA. AC B9SFH3; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 07-JAN-2015, entry version 25. DE SubName: Full=5-methyltetrahydrofolate:homocysteine methyltransferase, putative {ECO:0000313|EMBL:EEF37585.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EEF37585.1}; GN ORFNames=RCOM_0646290 {ECO:0000313|EMBL:EEF37585.1}; 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 {ECO:0000313|Proteomes:UP000008311}; RN [1] {ECO:0000313|Proteomes:UP000008311} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311}; 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; EQ973945; EEF37585.1; -; Genomic_DNA. DR RefSeq; XP_002524742.1; XM_002524696.1. DR GeneID; 8275420; -. DR KEGG; rcu:RCOM_0646290; -. DR InParanoid; B9SFH3; -. DR KO; K00547; -. DR Proteomes; UP000008311; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008311}; KW Methyltransferase {ECO:0000313|EMBL:EEF37585.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008311}; KW Transferase {ECO:0000313|EMBL:EEF37585.1}. SQ SEQUENCE 343 AA; 37093 MW; 171260532EB99A0A CRC64; MRHSSGANPS SLMTDFLKQS GGVAVIDGGL ATELERHGAD LNDPLWSAKC LLTSPHLIRM VHLDYLEAGA DIIITASYQA TIQGFEAKGF SSAESEALLK KSVEIACEAR EVYHDKCLAG ACDDNNDGRV LKKRPILVAA SVGSYGAYLA DGSEYSGDYG EAVTLGTLKD FHRRRVQVLA EAGADLIAFE TVPNRVEAQA YAELLEEEDI KVPAWFSFNS KDGINVVSGD SLLECASIAE SCRKVIAVGI NCTPPSFIHG LILSIKKVTS KPILIYPNSG ESYDADRKEW VQNTGVTDED FVSYVNKWCE VGASLVGGCC RTTPNTIRAI YRTLSNRSPD MPL // ID B9T060_RICCO Unreviewed; 327 AA. AC B9T060; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 07-JAN-2015, entry version 25. DE SubName: Full=5-methyltetrahydrofolate:homocysteine methyltransferase, putative {ECO:0000313|EMBL:EEF30757.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EEF30757.1}; GN ORFNames=RCOM_0030180 {ECO:0000313|EMBL:EEF30757.1}; 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 {ECO:0000313|Proteomes:UP000008311}; RN [1] {ECO:0000313|Proteomes:UP000008311} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311}; 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; EQ974296; EEF30757.1; -; Genomic_DNA. DR RefSeq; XP_002531629.1; XM_002531583.1. DR GeneID; 8285786; -. DR KEGG; rcu:RCOM_0030180; -. DR InParanoid; B9T060; -. DR KO; K00547; -. DR Proteomes; UP000008311; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008311}; KW Methyltransferase {ECO:0000313|EMBL:EEF30757.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008311}; KW Transferase {ECO:0000313|EMBL:EEF30757.1}. SQ SEQUENCE 327 AA; 36256 MW; 1AF97649EEB57750 CRC64; MGVEKRRSLL EDLIEKAGGC AVIDGGFATQ LETHGAAIND PLWSALCLIK DPELIKRVHL EYLEAGADIL VTSSYQATLP GFMSKGLTIE EGELLLKKSV KLAIEARDKF WDAVKRNPLH RYNRALVAAS IGSYGAYLAD GSEYSGYYGP DVNLEKLKDF HRHRLQVLAE AGPDLLAFET IPNKLEAEAC VELLEEENIK IPSWICFSSV DGENAPSGES FQECLDVINK SNKVVAAGIN CAPPHFIESL ICKFKKLTQK FVVVYPNSGE IWDGRAKRWL PSACFNDDKF EFFATRWHDL GANLIGGCCR TTPSTIRAIS KVLKERD // ID B9V3V7_EPICO Unreviewed; 205 AA. AC B9V3V7; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Betaine-homocysteine methyltransferase {ECO:0000313|EMBL:ACL98132.1}; DE Flags: Fragment; OS Epinephelus coioides (Orange-spotted grouper) (Epinephelus nebulosus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Serranoidei; Serranidae; Epinephelinae; OC Epinephelini; Epinephelus. OX NCBI_TaxID=94232 {ECO:0000313|EMBL:ACL98132.1}; RN [1] {ECO:0000313|EMBL:ACL98132.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Brain {ECO:0000313|EMBL:ACL98132.1}; RA Chang C.-Y., Lee Y.-C.; RT "Gene expression profiling of nodavirus infected-orange spotted RT grouper Epinephelus coioides."; RL Submitted (NOV-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; FJ438508; ACL98132.1; -; mRNA. DR HOVERGEN; HBG080367; -. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Methyltransferase {ECO:0000313|EMBL:ACL98132.1}; KW Transferase {ECO:0000313|EMBL:ACL98132.1}. FT NON_TER 1 1 {ECO:0000313|EMBL:ACL98132.1}. SQ SEQUENCE 205 AA; 23065 MW; 1F8744F2A9AAF99A CRC64; ECAVRLVKAG AQIVGVNCHF DPMTCVNAVK LMKEGVEKAG LKAHYMVQPL AYHTPDCNCQ GFIDLPEFPF GLEPRILSRW DMHKYAREAY NAGIHFIGGC CGFEPYHIRA VAEELAPERG FLPVASEKHG NWGAGLEMHT KPWVRARARR DYWENLKPAS GRPLCPSMST PDSWGVTKGH TDLMQQKEAT SQDQLKQLFD RTKSH // ID B9W8L8_CANDC Unreviewed; 311 AA. AC B9W8L8; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 29-APR-2015, entry version 29. DE SubName: Full=Candida dubliniensis CD36 chromosome 1, complete sequence {ECO:0000313|EMBL:CAX45091.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:CAX45091.1}; GN ORFNames=CD36_07920 {ECO:0000313|EMBL:CAX45091.1}; 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; Debaryomycetaceae; OC Candida/Lodderomyces clade; Candida. OX NCBI_TaxID=573826 {ECO:0000313|EMBL:CAX45091.1, ECO:0000313|Proteomes:UP000002605}; RN [1] {ECO:0000313|EMBL:CAX45091.1, ECO:0000313|Proteomes:UP000002605} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841 RC {ECO:0000313|Proteomes:UP000002605}; 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., 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., 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; FM992688; CAX45091.1; -; Genomic_DNA. DR RefSeq; XP_002417438.1; XM_002417393.1. DR STRING; 573826.CD36_07920; -. DR GeneID; 8044983; -. DR KEGG; cdu:CD36_07920; -. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000002605; Chromosome 1. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002605}; KW Methyltransferase {ECO:0000313|EMBL:CAX45091.1}; KW Transferase {ECO:0000313|EMBL:CAX45091.1}. SQ SEQUENCE 311 AA; 34357 MW; 5F9E7E01215855D5 CRC64; MGRVKDLLEK KKLVIDGALG TELERLLPTT STYLPSSSPL WSGQVLIKNP ELVEQVHLDY INAGADMIIT STYQTSYASL HKYIGYDMDQ AVTLWNSALD VAKSAVKKSG RDDVIIAGSI GPYATLLANG SEYNGDYQGV SDQELIEYHT PLFEFYNNSD VDIICIETIP SFQELKVIIG LTKKYTSKEF FISINPQTGS ALSDGTSLTE VAQLFAEIND PRFVAVGINC TSYENVDQIS TYLTNFPIFI YPNLGFVYDT TVHKFVSKML QESAWANSIA KWLNLPNVKA IGGCCSTTPA EIQQVAQLIK Q // ID B9X9Q1_PEDPL Unreviewed; 109 AA. AC B9X9Q1; DT 14-APR-2009, integrated into UniProtKB/TrEMBL. DT 14-APR-2009, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Methionine synthase I (Cobalamin-dependent) methyltransferase domain-like protein {ECO:0000313|EMBL:EEF63199.1}; DE Flags: Fragment; GN ORFNames=Cflav_PD5834 {ECO:0000313|EMBL:EEF63199.1}; OS Pedosphaera parvula (strain Ellin514). OC Bacteria; Verrucomicrobia; Verrucomicrobiae; Verrucomicrobiales; OC Verrucomicrobia subdivision 3; Pedosphaera. OX NCBI_TaxID=320771 {ECO:0000313|EMBL:EEF63199.1}; RN [1] {ECO:0000313|EMBL:EEF63199.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Ellin514 {ECO:0000313|EMBL:EEF63199.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEF63199.1}. 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; ABOX02000001; EEF63199.1; -; Genomic_DNA. DR RefSeq; WP_007412506.1; NZ_ABOX02000001.1. DR EnsemblBacteria; EEF63199; EEF63199; Cflav_PD5834. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEF63199.1}; KW Transferase {ECO:0000313|EMBL:EEF63199.1}. FT NON_TER 109 109 {ECO:0000313|EMBL:EEF63199.1}. SQ SEQUENCE 109 AA; 12765 MW; 81A0231B3F2CF312 CRC64; MNISTYQDRL ILCFSSQCKE VTLLSVNQNI KTKRWEQLEA LLRERIVIID GAMGTMIQQY KLDEAAFRGD RFQNWHKDLK GNNDLLNVTR PQVIQEIHRK YLEAGADII // ID B9XKW8_PEDPL Unreviewed; 624 AA. AC B9XKW8; DT 14-APR-2009, integrated into UniProtKB/TrEMBL. DT 14-APR-2009, sequence version 1. DT 27-MAY-2015, entry version 27. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=Cflav_PD2306 {ECO:0000313|EMBL:EEF59462.1}; OS Pedosphaera parvula (strain Ellin514). OC Bacteria; Verrucomicrobia; Verrucomicrobiae; Verrucomicrobiales; OC Verrucomicrobia subdivision 3; Pedosphaera. OX NCBI_TaxID=320771 {ECO:0000313|EMBL:EEF59462.1}; RN [1] {ECO:0000313|EMBL:EEF59462.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Ellin514 {ECO:0000313|EMBL:EEF59462.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEF59462.1}. 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; ABOX02000027; EEF59462.1; -; Genomic_DNA. DR RefSeq; WP_007416461.1; NZ_ABOX02000027.1. DR ProteinModelPortal; B9XKW8; -. DR EnsemblBacteria; EEF59462; EEF59462; Cflav_PD2306. DR PATRIC; 31328771; VBIBacEll73607_4291. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EEF59462.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EEF59462.1}. SQ SEQUENCE 624 AA; 67767 MW; 6AE0930B1E055E5D CRC64; MSNFLNRLNQ GVLLGDGAIG TLLYQRGQPL NASYDALNLQ HPEIVSQLHR DYLDAGAHLI ETNTFGANRI KLEKFGLAQK TVDINKHGAQ LALEVACGRG AFVAGSVGPL SADPSSLSTQ TKDSAYREQL EALVSEGVDA LFLETFNRLD ELAFVLRIAR SLGNTPIIAS LSFGDDGHTA DGLRINEAFS RLKEAGADVV GLNCHFGPTI AEKLLEELIV RPGDLISIYP NAGRPYFYEG RYIYHSTPSY FADFAPKLIA QGARLIGGCC GTTPETIAAM ARVLPGLKPV ESKQGLIVPP SRISPSLKPA APRTKSLLEL SREKPIIVTE LDPPKSLSLD KLLEGAQALK QAGTDFVTLA DNSLAILRVS NMAAGFLVKE KTGAEPLIHL ACRDKNLIGL QSELMGLHAL GIDHVLALTG DPAKVGDHQE ATSVYDVNSV GLIRMIKRLN EGFAANGRDL KTKTQFVIGC AFNPNARNLD SQVRKLEDKL EAGAQFVMTQ PIFDPVLAKV THEKTKGLGV PVLVGVMPLL NSRNAEFLHN EVPGIIIPEM TRDRLRGKEG AQANAEGLAI SRELCDAVLD CFNGIYLITP LMRYDLTVEL SRYVREHVRR PKVPLRHFDN ISVD // ID B9XS35_PEDPL Unreviewed; 1170 AA. AC B9XS35; DT 14-APR-2009, integrated into UniProtKB/TrEMBL. DT 14-APR-2009, sequence version 1. DT 27-MAY-2015, entry version 37. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEF57331.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEF57331.1}; DE Flags: Fragment; GN ORFNames=Cflav_PD0446 {ECO:0000313|EMBL:EEF57331.1}; OS Pedosphaera parvula (strain Ellin514). OC Bacteria; Verrucomicrobia; Verrucomicrobiae; Verrucomicrobiales; OC Verrucomicrobia subdivision 3; Pedosphaera. OX NCBI_TaxID=320771 {ECO:0000313|EMBL:EEF57331.1}; RN [1] {ECO:0000313|EMBL:EEF57331.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Ellin514 {ECO:0000313|EMBL:EEF57331.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEF57331.1}. 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; ABOX02000073; EEF57331.1; -; Genomic_DNA. DR RefSeq; WP_007418618.1; NZ_ABOX02000073.1. DR EnsemblBacteria; EEF57331; EEF57331; Cflav_PD0446. DR PATRIC; 31333527; VBIBacEll73607_6628. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEF57331.1}; KW Transferase {ECO:0000313|EMBL:EEF57331.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 163 163 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 228 228 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 229 229 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 677 677 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. FT NON_TER 1 1 {ECO:0000313|EMBL:EEF57331.1}. SQ SEQUENCE 1170 AA; 128694 MW; 71ABDE6A0692E2E4 CRC64; SQAISLADYK MEDLAYELSK AGAACARRAA EEVMAAQPGR VCFVAGAMGP TTRTSSISTD VNNPAARGTT YDELVQAYYD QAKGLIDGGA DILLVETIFD TLNSKAAFFA IERLYDDLGY RLPIMASVTF IQAGSNRGVT GQTVEAFWNS ISHVPLVSVG MNCALGPKEM RALIEELSNI APIYMSAYPN AGLPNPLLPT GFPETPESLA PQLKEWASNG WLNVVGGCCG TTPPHIKMIA EAVRGLKPRV VPTVEPYLRL SGLEALTVRP ETNFVNVGER TNVTGSPKFS KLILEGKYEE ALSVAKQQVV NGAQVIDVNM DEGMLDGAKA MTHFLNLIAS EPDIARVPIM VDSSKWSVIE AGLKCIQGKG VVNSISLKEG EEKFKEHAKL VRRYGAAVVV MAFDEKGQAD NFARKIEVCK RSYDILTKEV GFPPQDIIFD PNILTVATGM DEHNNYAVDF IEATRWIKQN LPHAKVSGGI SNISFSFRGN NTVREAMHSA FLYHAIKAGL DMGIVNAGML EVYEEIPKDL LELVEDVLLN RKPDATERLI KFAESVKQKG KTEVVADEWR KGTVEERLSH ALVKGIVDFI DQDTEEARQK YGKPLLIIEG PLMSGMNVVG DLFGSGKMFL PQVVKSARVM KKAVAYLLPY MEEEKKKTGI TRANGKILMA TVKGDVHDIG KNIVGVVLGC NSYEVIDLGV MVSSEKILAA AKEHNVDVIG LSGLITPSLD EMAHVAKEMK RQGFTLPLLI GGATTSRAHT SVKIAPGYNE AVVHVLDASR AVGVVGQLLN PELKTAFVQK NREEQERLRQ QHAAQKDAKP LLKIEEARKR KTPIDWKESD IAKPSFTGPK VLENAPLDEL IPFIDWSPFF HTWELRGRYP AILDEPKAKE LFDDAQALLK RIVDEKLFTA RAVYGFFPAN SVGDDIELYT DDSRTKVLTT FHTLRQQMDK PADQFNHALA DYVAPKASGL KDYLGAFAVT SGHGVDELAK HFEKDHDDYN SIMAKALADR LAEAFAEYLH KKAREEWGFG KTENLSNEDL IREKYRGIRP AAGYPASPDH TEKQILWKLL DAERKAGIKL TESCAMWPAS SVSGLYFAHP ESKYFGVGKI GRDQVLDYHL RKQMDLGSVE RWLGPYLDYD PDNVKPEANG APSTNNIAIV CGCGVPHPVN // ID B9Z380_9NEIS Unreviewed; 321 AA. AC B9Z380; DT 14-APR-2009, integrated into UniProtKB/TrEMBL. DT 14-APR-2009, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEG09033.1}; GN ORFNames=FuraDRAFT_1793 {ECO:0000313|EMBL:EEG09033.1}; OS Pseudogulbenkiania ferrooxidans 2002. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Chromobacteriaceae; Pseudogulbenkiania. OX NCBI_TaxID=279714 {ECO:0000313|EMBL:EEG09033.1}; RN [1] {ECO:0000313|EMBL:EEG09033.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=2002 {ECO:0000313|EMBL:EEG09033.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEG09033.1}. 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; ACIS01000004; EEG09033.1; -; Genomic_DNA. DR RefSeq; WP_008953813.1; NZ_ACIS01000004.1. DR EnsemblBacteria; EEG09033; EEG09033; FuraDRAFT_1793. DR PATRIC; 30253247; VBILutNit9412_1802. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEG09033.1}; KW Transferase {ECO:0000313|EMBL:EEG09033.1}. SQ SEQUENCE 321 AA; 34597 MW; 407EB8F0AACC8F25 CRC64; MTSPTTDPVA AILADYPVLI LDGALATELQ QRGCDLNDPL WSARVLIEEP ELIRQVHEDY FAAGADVATT ASYQATFEGF ARRGYDAEAA AALMRRAVTL AVEARDAFWS DPAHRQGRPK PLVAASVGPY GAMLADGSEY RGDYGLGEQQ LMDFHRPRLK VLLEAGADLL ACETIPCQVE ARALARLLAE EFPSARAWIS FSCKDGEHTC QGEKLADAVA ELNEVEQAVA VGVNCTAPEF IPALVAAAHG ATTKPLLVYP NSGEHYDPEH KCWHGHADAN RFAEAARGWH QAGARLIGGC CRTTPQDIRA VAEWARPAAG H // ID B9Z5C5_9NEIS Unreviewed; 1115 AA. AC B9Z5C5; DT 14-APR-2009, integrated into UniProtKB/TrEMBL. DT 14-APR-2009, sequence version 1. DT 27-MAY-2015, entry version 39. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEG07772.1}; GN ORFNames=FuraDRAFT_2560 {ECO:0000313|EMBL:EEG07772.1}; OS Pseudogulbenkiania ferrooxidans 2002. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Chromobacteriaceae; Pseudogulbenkiania. OX NCBI_TaxID=279714 {ECO:0000313|EMBL:EEG07772.1}; RN [1] {ECO:0000313|EMBL:EEG07772.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=2002 {ECO:0000313|EMBL:EEG07772.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEG07772.1}. 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; ACIS01000007; EEG07772.1; -; Genomic_DNA. DR RefSeq; WP_008954580.1; NZ_ACIS01000007.1. DR EnsemblBacteria; EEG07772; EEG07772; FuraDRAFT_2560. DR PATRIC; 30254784; VBILutNit9412_2564. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 768 768 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1115 AA; 122075 MW; D6D3603019172FA8 CRC64; MTIATNPTLY DHLSRRILIL DGGMGTMIQR HQLTEQDYRG ERFADWRCDV KGNNDLLVLT QPGIIGGIHQ AYLDAGADIV ETNTFNATSI AMADYEMEAL VWEINHAAAR LVKELCVAET AKNPAKPRYC AGVLGPTNRT CSISPDVNDP GYRNVTFDAL VESYTEAIDG LVKGGADLLL VETIFDTLNA KAAVFAIHKY FDERPEAIRL PIMVSGTITD QSGRTLTGQT TEAFYNSLSH ADAISFGLNC ALGPDLLRPY VEEMARISST FVSVHANAGL PNAFGGYDLS PADMAVNVRE WAESGLINIV GGCCGTTPEH IGAIYQAVQD LPPRALPALE PKCRLSGLEP FNIGDNDLFV NVGERTNVTG SKAFARLILN GDYATALDVA RQQVENGAQI IDINMDEGML DAHAAMVRFL NLIAAEPDIA RVPIMIDSSK WEVIEAGLKC IQGKGIVNSI SMKEGVDKFV EQARLIRRYG AAVIVMAFDE AGQADTYARK VEICEKSYRI LVDEVGFPPE DIIFDPNIFA VATGIEEHAR YGLDFIEATG WIKQNLPHAK ISGGVSNVSF SFRGNNKVRE AIHAVFLYHA IKRGMTMGIV NAGALEVYDE VDPVLRERIE DVVLMQGDDS MAATEALITL AESFRGDAKE AKGEDLAWRS LPVEKRLEHA LIKGITTYIV EDTEEVRLKC ERPIHVIEGP LMDGMNVVGD LFGAGKMFLP QVVKSARVMK AAVAHLEPFI EEEKIAMGLQ DAPAKGVIIM ATVKGDVHDI GKNIVGVVLR CNNYKVIDLG VMVPCQKILD AAIEHKADII GLSGLITPSL EEMSHVAKEM QRQGFTIPLL IGGATTSRVH TAVKIAPNYH GPVIYVPDAS RAVGVCSNLL SDTLRDVFVE EVAADYAKAR AIFEGRGEAK LLPIAEAREQ RHQIDWANYT PPKPSWLGVR RFEHYDLAEI ARCIDWTPFF QSWELAGRYP AILSDEVVGE SARALWADAQ AMLKQIIDEK WLTANAVIGL FPAASVGHDD IEIYHPDSGE RLMTWVGLRQ QIVKTDKDGN RNPDWCLADF IAPKDSGVED YIGAFAVTGG LGIDPHVARF EAANDDIRRS CSRRWPTVSP RPSPS // ID BHMT1_BOVIN Reviewed; 407 AA. AC Q5I597; Q2KIL0; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 27-MAY-2015, entry version 76. DE RecName: Full=Betaine--homocysteine S-methyltransferase 1; DE EC=2.1.1.5; GN Name=BHMT; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RA Charest R., Beaudry D., Girard C., Palin M.-F.; RT "Interactions folic acid-vitamin B12-methionine: effects on liver RT metabolism and production of dairy cows."; RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Testis; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC Converts betaine and homocysteine to dimethylglycine and CC methionine, respectively. This reaction is also required for the CC irreversible oxidation of choline (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Trimethylammonioacetate + L-homocysteine = CC dimethylglycine + L-methionine. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Amine and polyamine degradation; betaine degradation; CC sarcosine from betaine: step 1/2. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY854632; AAW39034.1; -; mRNA. DR EMBL; BC112599; AAI12600.1; -; mRNA. DR RefSeq; NP_001011679.1; NM_001011679.1. DR UniGene; Bt.16399; -. DR ProteinModelPortal; Q5I597; -. DR SMR; Q5I597; 10-398. DR PaxDb; Q5I597; -. DR PRIDE; Q5I597; -. DR Ensembl; ENSBTAT00000002916; ENSBTAP00000002916; ENSBTAG00000002255. DR GeneID; 497025; -. DR KEGG; bta:497025; -. DR CTD; 635; -. DR eggNOG; COG0646; -. DR GeneTree; ENSGT00390000003122; -. DR HOGENOM; HOG000231636; -. DR HOVERGEN; HBG080367; -. DR InParanoid; Q5I597; -. DR KO; K00544; -. DR OMA; WGVTKGT; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR BioCyc; CATTLE:497025-MONOMER; -. DR Reactome; REACT_351398; Sulfur amino acid metabolism. DR UniPathway; UPA00051; UER00083. DR UniPathway; UPA00291; UER00432. DR NextBio; 20865838; -. DR Proteomes; UP000009136; Chromosome 10. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IBA:GO_Central. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006579; P:amino-acid betaine catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl. DR GO; GO:0033528; P:S-methylmethionine cycle; IBA:GO_Central. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Complete proteome; Cytoplasm; Metal-binding; Methyltransferase; KW Reference proteome; Transferase; Zinc. FT INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q95332}. FT CHAIN 2 407 Betaine--homocysteine S-methyltransferase FT 1. FT /FTId=PRO_0000236274. FT DOMAIN 11 314 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 217 217 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 299 299 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 300 300 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT MOD_RES 40 40 N6-succinyllysine. FT {ECO:0000250|UniProtKB:O35490}. FT MOD_RES 93 93 N6-succinyllysine. FT {ECO:0000250|UniProtKB:O35490}. FT MOD_RES 98 98 N6-succinyllysine. FT {ECO:0000250|UniProtKB:O35490}. FT MOD_RES 232 232 N6-succinyllysine. FT {ECO:0000250|UniProtKB:O35490}. FT MOD_RES 241 241 N6-succinyllysine. FT {ECO:0000250|UniProtKB:O35490}. FT MOD_RES 340 340 N6-succinyllysine. FT {ECO:0000250|UniProtKB:O35490}. FT MOD_RES 377 377 N6-succinyllysine. FT {ECO:0000250|UniProtKB:O35490}. FT CONFLICT 216 216 N -> K (in Ref. 2; AAI12600). FT {ECO:0000305}. SQ SEQUENCE 407 AA; 44878 MW; 101C4070BAA30096 CRC64; MAPAGGKNVK KGILERLNSG EVIIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAVRQLH REFLRAGSNV MQTFTFYASE DKLENRGNYV AEKISGQKVN EAACDIARQV ADEGDALVAG GVSQTPSYLS CKSETEVKKV FQQQLEVFVK KNVDFLIAEY FEHVEEAVWA VEALKASGKP VAATMCIGPE GDLHSVTPGE CAVRLVKAGA SIVGVNCHFD PTISLQTVKL MKEGLEAAGL KAHLMSQPLA YHTPDCGKQG FIDLPEFPFG LEPRVATRWD IQKYAREAYN LGVRYIGGCC GFEPYHIRAI AEELAPERGF LPLASEKHGS WGSGLDMHTK PWIRARARKE YWENLQIASG RPYNPSMSKP DAWGVTKGTA ELMQQKEATT EQQLRELFEK QKFKSAQ // ID BHMT1_DANRE Reviewed; 400 AA. AC Q32LQ4; Q5PSM1; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2005, sequence version 1. DT 04-FEB-2015, entry version 71. DE RecName: Full=Betaine--homocysteine S-methyltransferase 1; DE EC=2.1.1.5; GN Name=bhmt; ORFNames=wu:fb53h01, zgc:123027; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Lapek J.D. Jr., Warren J.T. Jr.; RT "Molecular genetic analysis of folate metabolism in the zebrafish."; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC Converts betaine and homocysteine to dimethylglycine and CC methionine, respectively. This reaction is also required for the CC irreversible oxidation of choline (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Trimethylammonioacetate + L-homocysteine = CC dimethylglycine + L-methionine. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Amine and polyamine degradation; betaine degradation; CC sarcosine from betaine: step 1/2. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY830415; AAV74219.1; -; mRNA. DR EMBL; BC109472; AAI09473.1; -; mRNA. DR RefSeq; NP_001012498.1; NM_001012480.1. DR UniGene; Dr.75610; -. DR ProteinModelPortal; Q32LQ4; -. DR SMR; Q32LQ4; 7-393. DR STRING; 7955.ENSDARP00000040421; -. DR GeneID; 322228; -. DR KEGG; dre:322228; -. DR CTD; 635; -. DR ZFIN; ZDB-GENE-030131-947; bhmt. DR eggNOG; COG0646; -. DR HOGENOM; HOG000231636; -. DR HOVERGEN; HBG080367; -. DR InParanoid; Q32LQ4; -. DR KO; K00544; -. DR PhylomeDB; Q32LQ4; -. DR UniPathway; UPA00051; UER00083. DR UniPathway; UPA00291; UER00432. DR NextBio; 20807724; -. DR PRO; PR:Q32LQ4; -. DR Proteomes; UP000000437; Unplaced. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IBA:GO_Central. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006579; P:amino-acid betaine catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0055123; P:digestive system development; IMP:ZFIN. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR GO; GO:0033528; P:S-methylmethionine cycle; IBA:GO_Central. DR GO; GO:0003323; P:type B pancreatic cell development; IMP:ZFIN. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Complete proteome; Cytoplasm; Metal-binding; Methyltransferase; KW Reference proteome; Transferase; Zinc. FT CHAIN 1 400 Betaine--homocysteine S-methyltransferase FT 1. FT /FTId=PRO_0000273221. FT DOMAIN 8 309 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 212 212 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 294 294 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 295 295 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT CONFLICT 189 189 H -> P (in Ref. 1; AAV74219). FT {ECO:0000305}. FT CONFLICT 192 192 I -> T (in Ref. 1; AAV74219). FT {ECO:0000305}. FT CONFLICT 224 224 A -> V (in Ref. 1; AAV74219). FT {ECO:0000305}. SQ SEQUENCE 400 AA; 44066 MW; A6A3A9A824D5D26A CRC64; MAPVGSKRGV LERLNAGEVV IGDGGFVFAL EKRGYVKAGP WTPEAAAEHP EAVRQLHREF LRAGSNVMQT FTFYASDDKL ENRGNKLSFT GQQINEAACD LAREVANEGD ALVAGGVSQT PSYLSCKSEE EVKKTFKKQL DVFIKKNVDL LIAEYFEHVE EAEWAVQVLK ATGKPVAATL CIGPDGDMHG VIPGECAVRL VKAGADIVGV NCHFDPLTCV KTVAMMKAAV EKAGLKAHYM TQPLAYHTPD CSCQGFIDLP EFPFALEPRI LTRWEMQQYA REAYKAGIRY IGGCCGFEPY HIRAVAEELS AERGFLPEAS QKHGLWGSGL EMHTKPWVRA RARRDYWEKL KPASGRPLCP SMSTPDGWGV TRGHAALMQQ KEATTAEQLR PLFQQADAKH // ID BHMT1_HUMAN Reviewed; 406 AA. AC Q93088; Q9UNI9; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 17-APR-2007, sequence version 2. DT 27-MAY-2015, entry version 144. DE RecName: Full=Betaine--homocysteine S-methyltransferase 1; DE EC=2.1.1.5; GN Name=BHMT; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLN-239. RC TISSUE=Liver; RX PubMed=8798461; RA Garrow T.A.; RT "Purification, kinetic properties, and cDNA cloning of mammalian RT betaine-homocysteine methyltransferase."; RL J. Biol. Chem. 271:22831-22838(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Lung; RX PubMed=10075673; DOI=10.1074/jbc.274.12.7816; RA Park E.I., Garrow T.A.; RT "Interaction between dietary methionine and methyl donor intake on rat RT liver betaine-homocysteine methyltransferase gene expression and RT organization of the human gene."; RL J. Biol. Chem. 274:7816-7824(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP TISSUE SPECIFICITY. RX PubMed=9281325; DOI=10.1006/abbi.1997.0246; RA Sunden S.L.F., Renduchintala M.S., Park E.I., Miklasz S.D., RA Garrow T.A.; RT "Betaine-homocysteine methyltransferase expression in porcine and RT human tissues and chromosomal localization of the human gene."; RL Arch. Biochem. Biophys. 345:171-174(1997). RN [5] RP CHARACTERIZATION, AND ZINC-BINDING. RC TISSUE=Liver; RX PubMed=9681996; DOI=10.1006/abbi.1998.0757; RA Millian N.S., Garrow T.A.; RT "Human betaine-homocysteine methyltransferase is a zinc RT metalloenzyme."; RL Arch. Biochem. Biophys. 356:93-98(1998). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS), AND SUBUNIT. RX PubMed=12220488; DOI=10.1016/S0969-2126(02)00796-7; RA Evans J.C., Huddler D.P., Jiracek J., Castro C., Millian N.S., RA Garrow T.A., Ludwig M.L.; RT "Betaine-homocysteine methyltransferase: zinc in a distorted barrel."; RL Structure 10:1159-1171(2002). RN [8] RP VARIANT GLN-239. RX PubMed=12818402; DOI=10.1016/S0021-9150(03)00010-8; RA Weisberg I.S., Park E., Ballman K.V., Berger P., Nunn M., Suh D.S., RA Breksa A.P., Garrow T.A., Rozen R.; RT "Investigations of a common genetic variant in betaine-homocysteine RT methyltransferase (BHMT) in coronary artery disease."; RL Atherosclerosis 167:205-214(2003). CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC Converts betaine and homocysteine to dimethylglycine and CC methionine, respectively. This reaction is also required for the CC irreversible oxidation of choline. CC -!- CATALYTIC ACTIVITY: Trimethylammonioacetate + L-homocysteine = CC dimethylglycine + L-methionine. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 1 zinc ion per subunit.; CC -!- PATHWAY: Amine and polyamine degradation; betaine degradation; CC sarcosine from betaine: step 1/2. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12220488}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Found exclusively in liver and kidney. CC {ECO:0000269|PubMed:9281325}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U50929; AAC50668.1; -; mRNA. DR EMBL; AF118378; AAD22043.1; -; Genomic_DNA. DR EMBL; AF118371; AAD22043.1; JOINED; Genomic_DNA. DR EMBL; AF118372; AAD22043.1; JOINED; Genomic_DNA. DR EMBL; AF118373; AAD22043.1; JOINED; Genomic_DNA. DR EMBL; AF118374; AAD22043.1; JOINED; Genomic_DNA. DR EMBL; AF118375; AAD22043.1; JOINED; Genomic_DNA. DR EMBL; AF118376; AAD22043.1; JOINED; Genomic_DNA. DR EMBL; AF118377; AAD22043.1; JOINED; Genomic_DNA. DR EMBL; BC012616; AAH12616.1; -; mRNA. DR CCDS; CCDS4046.1; -. DR RefSeq; NP_001704.2; NM_001713.2. DR UniGene; Hs.80756; -. DR PDB; 1LT7; X-ray; 2.15 A; A/B=1-406. DR PDB; 1LT8; X-ray; 2.05 A; A/B=1-406. DR PDB; 4M3P; X-ray; 1.90 A; A/B/C/D=1-406. DR PDBsum; 1LT7; -. DR PDBsum; 1LT8; -. DR PDBsum; 4M3P; -. DR ProteinModelPortal; Q93088; -. DR SMR; Q93088; 8-403. DR BioGrid; 107104; 12. DR IntAct; Q93088; 5. DR MINT; MINT-246738; -. DR STRING; 9606.ENSP00000274353; -. DR BindingDB; Q93088; -. DR ChEMBL; CHEMBL4328; -. DR DrugBank; DB00134; L-Methionine. DR PhosphoSite; Q93088; -. DR BioMuta; BHMT; -. DR DMDM; 145559446; -. DR PaxDb; Q93088; -. DR PRIDE; Q93088; -. DR Ensembl; ENST00000274353; ENSP00000274353; ENSG00000145692. DR GeneID; 635; -. DR KEGG; hsa:635; -. DR UCSC; uc003kfu.4; human. DR CTD; 635; -. DR GeneCards; GC05P078443; -. DR HGNC; HGNC:1047; BHMT. DR HPA; HPA038285; -. DR HPA; HPA058310; -. DR MIM; 602888; gene. DR neXtProt; NX_Q93088; -. DR PharmGKB; PA25350; -. DR eggNOG; COG0646; -. DR HOGENOM; HOG000231636; -. DR HOVERGEN; HBG080367; -. DR InParanoid; Q93088; -. DR KO; K00544; -. DR OMA; WGVTKGT; -. DR OrthoDB; EOG79GT7C; -. DR PhylomeDB; Q93088; -. DR TreeFam; TF329202; -. DR BioCyc; MetaCyc:HS07273-MONOMER; -. DR BRENDA; 2.1.1.5; 2681. DR Reactome; REACT_115639; Sulfur amino acid metabolism. DR SABIO-RK; Q93088; -. DR UniPathway; UPA00051; UER00083. DR UniPathway; UPA00291; UER00432. DR ChiTaRS; BHMT; human. DR EvolutionaryTrace; Q93088; -. DR GenomeRNAi; 635; -. DR NextBio; 2568; -. DR PRO; PR:Q93088; -. DR Proteomes; UP000005640; Chromosome 5. DR Bgee; Q93088; -. DR CleanEx; HS_BHMT; -. DR ExpressionAtlas; Q93088; baseline and differential. DR Genevestigator; Q93088; -. DR GO; GO:0005737; C:cytoplasm; IDA:HPA. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0043234; C:protein complex; IEA:Ensembl. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; NAS:UniProtKB. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IDA:BHF-UCL. DR GO; GO:0006579; P:amino-acid betaine catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006577; P:amino-acid betaine metabolic process; IDA:BHF-UCL. DR GO; GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome. DR GO; GO:0071267; P:L-methionine salvage; IDA:BHF-UCL. DR GO; GO:0006479; P:protein methylation; NAS:UniProtKB. DR GO; GO:0050666; P:regulation of homocysteine metabolic process; NAS:UniProtKB. DR GO; GO:0010243; P:response to organonitrogen compound; IEA:Ensembl. DR GO; GO:0033528; P:S-methylmethionine cycle; IBA:GO_Central. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR GO; GO:0000096; P:sulfur amino acid metabolic process; TAS:Reactome. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Metal-binding; KW Methyltransferase; Polymorphism; Reference proteome; Transferase; KW Zinc. FT INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q95332}. FT CHAIN 2 406 Betaine--homocysteine S-methyltransferase FT 1. FT /FTId=PRO_0000114621. FT DOMAIN 11 314 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 217 217 Zinc. FT METAL 299 299 Zinc. FT METAL 300 300 Zinc. FT MOD_RES 40 40 N6-succinyllysine. FT {ECO:0000250|UniProtKB:O35490}. FT MOD_RES 93 93 N6-succinyllysine. FT {ECO:0000250|UniProtKB:O35490}. FT MOD_RES 232 232 N6-succinyllysine. FT {ECO:0000250|UniProtKB:O35490}. FT MOD_RES 241 241 N6-succinyllysine. FT {ECO:0000250|UniProtKB:O35490}. FT MOD_RES 340 340 N6-succinyllysine. FT {ECO:0000250|UniProtKB:O35490}. FT MOD_RES 377 377 N6-succinyllysine. FT {ECO:0000250|UniProtKB:O35490}. FT VARIANT 199 199 G -> S (in dbSNP:rs59866108). FT /FTId=VAR_061345. FT VARIANT 239 239 R -> Q (may decrease risk for coronary FT artery disease; dbSNP:rs3733890). FT {ECO:0000269|PubMed:12818402, FT ECO:0000269|PubMed:8798461}. FT /FTId=VAR_015886. FT HELIX 13 18 {ECO:0000244|PDB:4M3P}. FT HELIX 29 35 {ECO:0000244|PDB:4M3P}. FT TURN 41 43 {ECO:0000244|PDB:4M3P}. FT HELIX 48 51 {ECO:0000244|PDB:4M3P}. FT HELIX 53 66 {ECO:0000244|PDB:4M3P}. FT STRAND 69 72 {ECO:0000244|PDB:4M3P}. FT HELIX 97 111 {ECO:0000244|PDB:4M3P}. FT TURN 112 115 {ECO:0000244|PDB:4M3P}. FT STRAND 117 123 {ECO:0000244|PDB:4M3P}. FT HELIX 126 129 {ECO:0000244|PDB:1LT8}. FT HELIX 134 151 {ECO:0000244|PDB:4M3P}. FT STRAND 154 162 {ECO:0000244|PDB:4M3P}. FT HELIX 164 175 {ECO:0000244|PDB:4M3P}. FT STRAND 181 185 {ECO:0000244|PDB:4M3P}. FT HELIX 198 207 {ECO:0000244|PDB:4M3P}. FT STRAND 211 219 {ECO:0000244|PDB:4M3P}. FT HELIX 221 237 {ECO:0000244|PDB:4M3P}. FT STRAND 243 247 {ECO:0000244|PDB:4M3P}. FT HELIX 261 263 {ECO:0000244|PDB:4M3P}. FT TURN 265 269 {ECO:0000244|PDB:4M3P}. FT HELIX 272 274 {ECO:0000244|PDB:4M3P}. FT HELIX 278 290 {ECO:0000244|PDB:4M3P}. FT STRAND 293 296 {ECO:0000244|PDB:4M3P}. FT HELIX 304 313 {ECO:0000244|PDB:4M3P}. FT HELIX 315 318 {ECO:0000244|PDB:4M3P}. FT HELIX 323 327 {ECO:0000244|PDB:4M3P}. FT HELIX 330 335 {ECO:0000244|PDB:4M3P}. FT HELIX 341 344 {ECO:0000244|PDB:4M3P}. FT HELIX 349 354 {ECO:0000244|PDB:4M3P}. FT HELIX 377 400 {ECO:0000244|PDB:4M3P}. SQ SEQUENCE 406 AA; 44998 MW; 557855B8CEDD0D54 CRC64; MPPVGGKKAK KGILERLNAG EIVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAVRQLH REFLRAGSNV MQTFTFYASE DKLENRGNYV LEKISGQEVN EAACDIARQV ADEGDALVAG GVSQTPSYLS CKSETEVKKV FLQQLEVFMK KNVDFLIAEY FEHVEEAVWA VETLIASGKP VAATMCIGPE GDLHGVPPGE CAVRLVKAGA SIIGVNCHFD PTISLKTVKL MKEGLEAARL KAHLMSQPLA YHTPDCNKQG FIDLPEFPFG LEPRVATRWD IQKYAREAYN LGVRYIGGCC GFEPYHIRAI AEELAPERGF LPPASEKHGS WGSGLDMHTK PWVRARARKE YWENLRIASG RPYNPSMSKP DGWGVTKGTA ELMQQKEATT EQQLKELFEK QKFKSQ // ID BHMT1_MOUSE Reviewed; 407 AA. AC O35490; Q3UEM1; Q3UL72; Q561N0; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 01-APR-2015, entry version 119. DE RecName: Full=Betaine--homocysteine S-methyltransferase 1; DE EC=2.1.1.5; GN Name=Bhmt; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129/SvEv; RX PubMed=10854776; DOI=10.1016/S0378-1119(00)00191-8; RA Neece D.J., Griffiths M.A., Garrow T.A.; RT "Isolation and characterization of a mouse betaine-homocysteine S- RT methyltransferase gene and pseudogene."; RL Gene 250:31-40(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=129; TISSUE=Liver; RA Sowden M.P., Smith H.C.; RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [5] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-40; LYS-93; LYS-98; RP LYS-232; LYS-241; LYS-340 AND LYS-377, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC Converts betaine and homocysteine to dimethylglycine and CC methionine, respectively. This reaction is also required for the CC irreversible oxidation of choline. CC -!- CATALYTIC ACTIVITY: Trimethylammonioacetate + L-homocysteine = CC dimethylglycine + L-methionine. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Amine and polyamine degradation; betaine degradation; CC sarcosine from betaine: step 1/2. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AH009623; AAF85944.1; -; Genomic_DNA. DR EMBL; AF033381; AAB87501.1; -; mRNA. DR EMBL; AK145668; BAE26578.1; -; mRNA. DR EMBL; AK149457; BAE28890.1; -; mRNA. DR EMBL; AK166754; BAE38995.1; -; mRNA. DR EMBL; AK166818; BAE39044.1; -; mRNA. DR EMBL; BC037004; AAH37004.1; -; mRNA. DR EMBL; BC093510; AAH93510.1; -; mRNA. DR EMBL; BC110307; AAI10308.1; -; mRNA. DR CCDS; CCDS36748.1; -. DR RefSeq; NP_057877.1; NM_016668.3. DR UniGene; Mm.329582; -. DR UniGene; Mm.423099; -. DR ProteinModelPortal; O35490; -. DR SMR; O35490; 10-398. DR IntAct; O35490; 3. DR MINT; MINT-1870182; -. DR PhosphoSite; O35490; -. DR REPRODUCTION-2DPAGE; O35490; -. DR MaxQB; O35490; -. DR PaxDb; O35490; -. DR PRIDE; O35490; -. DR Ensembl; ENSMUST00000091776; ENSMUSP00000135956; ENSMUSG00000069324. DR Ensembl; ENSMUST00000099309; ENSMUSP00000096912; ENSMUSG00000074768. DR GeneID; 12116; -. DR KEGG; mmu:12116; -. DR UCSC; uc007rli.1; mouse. DR CTD; 635; -. DR MGI; MGI:1339972; Bhmt. DR eggNOG; COG0646; -. DR GeneTree; ENSGT00390000003122; -. DR HOGENOM; HOG000231636; -. DR HOVERGEN; HBG080367; -. DR InParanoid; O35490; -. DR KO; K00544; -. DR OMA; WGVTKGT; -. DR OrthoDB; EOG79GT7C; -. DR PhylomeDB; O35490; -. DR TreeFam; TF329202; -. DR BRENDA; 2.1.1.5; 3474. DR Reactome; REACT_277860; Sulfur amino acid metabolism. DR UniPathway; UPA00051; UER00083. DR UniPathway; UPA00291; UER00432. DR NextBio; 280431; -. DR PRO; PR:O35490; -. DR Proteomes; UP000000589; Chromosome 13. DR Proteomes; UP000000589; Chromosome 18. DR Bgee; O35490; -. DR CleanEx; MM_BHMT; -. DR Genevestigator; O35490; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006579; P:amino-acid betaine catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Metal-binding; Methyltransferase; KW Reference proteome; Transferase; Zinc. FT INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q95332}. FT CHAIN 2 407 Betaine--homocysteine S-methyltransferase FT 1. FT /FTId=PRO_0000114622. FT DOMAIN 11 314 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 217 217 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 299 299 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 300 300 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT MOD_RES 40 40 N6-succinyllysine. FT {ECO:0000269|PubMed:23806337}. FT MOD_RES 93 93 N6-succinyllysine. FT {ECO:0000269|PubMed:23806337}. FT MOD_RES 98 98 N6-succinyllysine. FT {ECO:0000269|PubMed:23806337}. FT MOD_RES 232 232 N6-succinyllysine. FT {ECO:0000269|PubMed:23806337}. FT MOD_RES 241 241 N6-succinyllysine. FT {ECO:0000269|PubMed:23806337}. FT MOD_RES 340 340 N6-succinyllysine. FT {ECO:0000269|PubMed:23806337}. FT MOD_RES 377 377 N6-succinyllysine. FT {ECO:0000269|PubMed:23806337}. FT CONFLICT 7 7 K -> E (in Ref. 3; BAE26578). FT {ECO:0000305}. SQ SEQUENCE 407 AA; 45021 MW; 1C600BE9CC44EE32 CRC64; MAPVAGKKAK KGILERLNAG EVVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAVRQLH REFLRAGSNV MQTFTFYASE DKLENRGNYV AEKISGQKVN EAACDIARQV ADEGDALVAG GVSQTPSYLS CKSEVEVKKI FRQQLEVFMK KNVDFLIAEY FEHVEEAVWA VEALKASGKP VAATMCIGPE GDLHGVPPGE CAVRLVKAGA SIVGVNCHFD PSVSLQTVKL MKEGLEAARL KAYLMSQPLA YHTPDCGKQG FIDLPEFPFG LEPRVATRWD IQKYAREAYN LGVRYIGGCC GFEPYHIRAI AEELAPERGF LPPASEKHGS WGSGLDMHTK PWIRARARKE YWQNLRIASG RPYNPSMSRP DAWGVTKGAA ELMQQKEATT EQQLRELFEK QKFKSAQ // ID BHMT1_PIG Reviewed; 278 AA. AC Q95332; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 01-APR-2015, entry version 87. DE RecName: Full=Betaine--homocysteine S-methyltransferase 1; DE EC=2.1.1.5; DE Flags: Fragment; GN Name=BHMT; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; OC Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-273, AND PROTEIN SEQUENCE OF 2-22 AND RP 257-278. RC TISSUE=Liver; RX PubMed=8798461; RA Garrow T.A.; RT "Purification, kinetic properties, and cDNA cloning of mammalian RT betaine-homocysteine methyltransferase."; RL J. Biol. Chem. 271:22831-22838(1996). RN [2] RP TISSUE SPECIFICITY. RX PubMed=9281325; DOI=10.1006/abbi.1997.0246; RA Sunden S.L.F., Renduchintala M.S., Park E.I., Miklasz S.D., RA Garrow T.A.; RT "Betaine-homocysteine methyltransferase expression in porcine and RT human tissues and chromosomal localization of the human gene."; RL Arch. Biochem. Biophys. 345:171-174(1997). CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC Converts betaine and homocysteine to dimethylglycine and CC methionine, respectively. This reaction is also required for the CC irreversible oxidation of choline. CC -!- CATALYTIC ACTIVITY: Trimethylammonioacetate + L-homocysteine = CC dimethylglycine + L-methionine. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Amine and polyamine degradation; betaine degradation; CC sarcosine from betaine: step 1/2. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Found exclusively in liver and kidney. CC {ECO:0000269|PubMed:9281325}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U53421; AAC48632.1; -; mRNA. DR UniGene; Ssc.16105; -. DR UniGene; Ssc.82464; -. DR ProteinModelPortal; Q95332; -. DR SMR; Q95332; 10-278. DR MINT; MINT-246731; -. DR STRING; 9823.ENSSSCP00000015001; -. DR PaxDb; Q95332; -. DR eggNOG; COG0646; -. DR HOGENOM; HOG000231636; -. DR HOVERGEN; HBG080367; -. DR InParanoid; Q95332; -. DR BRENDA; 2.1.1.5; 6170. DR Reactome; REACT_307543; Sulfur amino acid metabolism. DR UniPathway; UPA00051; UER00083. DR UniPathway; UPA00291; UER00432. DR Proteomes; UP000008227; Unplaced. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006579; P:amino-acid betaine catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Direct protein sequencing; KW Metal-binding; Methyltransferase; Reference proteome; Transferase; KW Zinc. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:8798461}. FT CHAIN 2 >278 Betaine--homocysteine S-methyltransferase FT 1. FT /FTId=PRO_0000114623. FT DOMAIN 11 >278 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 217 217 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT MOD_RES 40 40 N6-succinyllysine. FT {ECO:0000250|UniProtKB:O35490}. FT MOD_RES 93 93 N6-succinyllysine. FT {ECO:0000250|UniProtKB:O35490}. FT MOD_RES 98 98 N6-succinyllysine. FT {ECO:0000250|UniProtKB:O35490}. FT MOD_RES 232 232 N6-succinyllysine. FT {ECO:0000250|UniProtKB:O35490}. FT MOD_RES 241 241 N6-succinyllysine. FT {ECO:0000250|UniProtKB:O35490}. FT NON_TER 278 278 SQ SEQUENCE 278 AA; 30134 MW; 58D3CAFEE7294CA3 CRC64; MAPVGDKKAK KGILERLNSG EVVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAVRQLH REFLRAGSNV MQTFTFYASE DKLENRGNYV AEKISGQKVN EAACDIARQV ADEGDALVAG GVSQTPSYLS CKSETEVKKV FRQQLEVFMK KNVDFLIAEY FEHVEEAVWA VEALKASGKP VAATMCIGPE GDLHGVTPGQ CAVRLVKAGA SIVGVNCHFD PTISLQTVKL MKEGLQAAGL KAHLMSQPLA YHTPDCGKQG FIDLPEFPFG LEPRVATR // ID BHMT1_PONAB Reviewed; 406 AA. AC Q5RFG2; DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 04-MAR-2015, entry version 57. DE RecName: Full=Betaine--homocysteine S-methyltransferase 1; DE EC=2.1.1.5; GN Name=BHMT; OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pongo. OX NCBI_TaxID=9601; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RG The German cDNA consortium; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC Converts betaine and homocysteine to dimethylglycine and CC methionine, respectively. This reaction is also required for the CC irreversible oxidation of choline (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Trimethylammonioacetate + L-homocysteine = CC dimethylglycine + L-methionine. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Amine and polyamine degradation; betaine degradation; CC sarcosine from betaine: step 1/2. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR857196; CAH89495.1; -; mRNA. DR RefSeq; NP_001127156.1; NM_001133684.1. DR ProteinModelPortal; Q5RFG2; -. DR SMR; Q5RFG2; 10-398. DR GeneID; 100174207; -. DR KEGG; pon:100174207; -. DR CTD; 635; -. DR HOVERGEN; HBG080367; -. DR InParanoid; Q5RFG2; -. DR KO; K00544; -. DR UniPathway; UPA00051; UER00083. DR UniPathway; UPA00291; UER00432. DR Proteomes; UP000001595; Unplaced. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006579; P:amino-acid betaine catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Complete proteome; Cytoplasm; Metal-binding; Methyltransferase; KW Reference proteome; Transferase; Zinc. FT INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q95332}. FT CHAIN 2 406 Betaine--homocysteine S-methyltransferase FT 1. FT /FTId=PRO_0000234128. FT DOMAIN 11 314 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 217 217 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 299 299 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 300 300 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT MOD_RES 40 40 N6-succinyllysine. FT {ECO:0000250|UniProtKB:O35490}. FT MOD_RES 93 93 N6-succinyllysine. FT {ECO:0000250|UniProtKB:O35490}. FT MOD_RES 98 98 N6-succinyllysine. FT {ECO:0000250|UniProtKB:O35490}. FT MOD_RES 232 232 N6-succinyllysine. FT {ECO:0000250|UniProtKB:O35490}. FT MOD_RES 241 241 N6-succinyllysine. FT {ECO:0000250|UniProtKB:O35490}. FT MOD_RES 340 340 N6-succinyllysine. FT {ECO:0000250|UniProtKB:O35490}. FT MOD_RES 377 377 N6-succinyllysine. FT {ECO:0000250|UniProtKB:O35490}. SQ SEQUENCE 406 AA; 45112 MW; 6BCCB007E7ED5B8B CRC64; MPPVVGKKAK KGILERLNAG EIVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAVRQLH REFLRAGSNV MQTFTFYASE DKLENRGNYV LEKISGQKVN EAACDIARQV ADEGDALVAG GVSQTPSYLS CKSETEVKKV FLQQLEVFMK KNVDFLIAEY FEHVEEAVWA VETLIASGKP VAATMCIGPE GDLHGVPPGE CAVRLVKAGA SIIGVNCHFD PTISLKTVKL MKEGLEAARL KAHLMSQPLA YHTPDCNKQG FIDLPEFPFG LEPRVATRWD IQKYAREAYN MGIRYIGGCC GFEPYHIRAI AEELAPERGF LPPASEKHGS WGSALDMHTK PWVRARARKE YWENLRIASG RPYNPSMSKP DGWGVTKGTA ELMQQKEATT EQQLKELFEK QKFKLQ // ID BHMT1_RAT Reviewed; 407 AA. AC O09171; Q6AZ06; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 27-MAY-2015, entry version 118. DE RecName: Full=Betaine--homocysteine S-methyltransferase 1; DE EC=2.1.1.5; GN Name=Bhmt; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Sprague-Dawley; TISSUE=Liver; RX PubMed=8753772; DOI=10.1006/bbrc.1996.1183; RA Forestier M., Reichen J., Solioz M.; RT "Application of mRNA differential display to liver cirrhosis: reduced RT fetuin expression in biliary cirrhosis in the rat."; RL Biochem. Biophys. Res. Commun. 225:377-383(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=10417327; DOI=10.1042/0264-6021:3410639; RA Sowden M.P., Collins H.L., Smith H.C., Garrow T.A., Sparks J.D., RA Sparks C.E.; RT "Apolipoprotein B mRNA and lipoprotein secretion are increased in RT McArdle RH-7777 cells by expression of betaine-homocysteine S- RT methyltransferase."; RL Biochem. J. 341:639-645(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND SUBUNIT. RX PubMed=15099744; DOI=10.1016/j.jmb.2004.03.005; RA Gonzalez B., Pajares M.A., Martinez-Ripoll M., Blundell T.L., RA Sanz-Aparicio J.; RT "Crystal structure of rat liver betaine homocysteine S- RT methyltransferase reveals new oligomerization features and RT conformational changes upon substrate binding."; RL J. Mol. Biol. 338:771-782(2004). CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC Converts betaine and homocysteine to dimethylglycine and CC methionine, respectively. This reaction is also required for the CC irreversible oxidation of choline. CC -!- CATALYTIC ACTIVITY: Trimethylammonioacetate + L-homocysteine = CC dimethylglycine + L-methionine. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 1 zinc ion per subunit.; CC -!- PATHWAY: Amine and polyamine degradation; betaine degradation; CC sarcosine from betaine: step 1/2. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15099744}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U96133; AAB53763.1; -; mRNA. DR EMBL; AF038870; AAB95481.1; -; mRNA. DR EMBL; BC078811; AAH78811.1; -; mRNA. DR RefSeq; NP_110477.1; NM_030850.1. DR UniGene; Rn.11406; -. DR PDB; 1UMY; X-ray; 2.50 A; A/B/C/D=1-407. DR PDBsum; 1UMY; -. DR ProteinModelPortal; O09171; -. DR SMR; O09171; 10-398. DR IntAct; O09171; 2. DR STRING; 10116.ENSRNOP00000015336; -. DR PhosphoSite; O09171; -. DR PaxDb; O09171; -. DR PRIDE; O09171; -. DR GeneID; 81508; -. DR KEGG; rno:81508; -. DR UCSC; RGD:621496; rat. DR CTD; 635; -. DR RGD; 621496; Bhmt. DR eggNOG; COG0646; -. DR HOGENOM; HOG000231636; -. DR HOVERGEN; HBG080367; -. DR InParanoid; O09171; -. DR KO; K00544; -. DR OrthoDB; EOG79GT7C; -. DR PhylomeDB; O09171; -. DR TreeFam; TF329202; -. DR BioCyc; MetaCyc:MONOMER-9241; -. DR BRENDA; 2.1.1.5; 5301. DR Reactome; REACT_289986; Sulfur amino acid metabolism. DR UniPathway; UPA00051; UER00083. DR UniPathway; UPA00291; UER00432. DR EvolutionaryTrace; O09171; -. DR NextBio; 614975; -. DR PRO; PR:O09171; -. DR Proteomes; UP000002494; Unplaced. DR Genevestigator; O09171; -. DR GO; GO:0005829; C:cytosol; IDA:RGD. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0043234; C:protein complex; IDA:RGD. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IDA:RGD. DR GO; GO:0008168; F:methyltransferase activity; IDA:RGD. DR GO; GO:0032403; F:protein complex binding; IDA:RGD. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006579; P:amino-acid betaine catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl. DR GO; GO:0009086; P:methionine biosynthetic process; IDA:RGD. DR GO; GO:0006479; P:protein methylation; IDA:RGD. DR GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD. DR GO; GO:0033528; P:S-methylmethionine cycle; IBA:GO_Central. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Metal-binding; KW Methyltransferase; Reference proteome; Transferase; Zinc. FT INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q95332}. FT CHAIN 2 407 Betaine--homocysteine S-methyltransferase FT 1. FT /FTId=PRO_0000114624. FT DOMAIN 11 314 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 217 217 Zinc. FT METAL 299 299 Zinc. FT METAL 300 300 Zinc. FT MOD_RES 40 40 N6-succinyllysine. FT {ECO:0000250|UniProtKB:O35490}. FT MOD_RES 93 93 N6-succinyllysine. FT {ECO:0000250|UniProtKB:O35490}. FT MOD_RES 98 98 N6-succinyllysine. FT {ECO:0000250|UniProtKB:O35490}. FT MOD_RES 232 232 N6-succinyllysine. FT {ECO:0000250|UniProtKB:O35490}. FT MOD_RES 241 241 N6-succinyllysine. FT {ECO:0000250|UniProtKB:O35490}. FT MOD_RES 340 340 N6-succinyllysine. FT {ECO:0000250|UniProtKB:O35490}. FT MOD_RES 377 377 N6-succinyllysine. FT {ECO:0000250|UniProtKB:O35490}. FT CONFLICT 247 248 HA -> QP (in Ref. 3; AAH78811). FT {ECO:0000305}. FT HELIX 13 18 {ECO:0000244|PDB:1UMY}. FT HELIX 29 35 {ECO:0000244|PDB:1UMY}. FT TURN 41 43 {ECO:0000244|PDB:1UMY}. FT HELIX 48 51 {ECO:0000244|PDB:1UMY}. FT HELIX 53 66 {ECO:0000244|PDB:1UMY}. FT STRAND 70 72 {ECO:0000244|PDB:1UMY}. FT HELIX 96 112 {ECO:0000244|PDB:1UMY}. FT TURN 113 115 {ECO:0000244|PDB:1UMY}. FT STRAND 117 122 {ECO:0000244|PDB:1UMY}. FT HELIX 126 129 {ECO:0000244|PDB:1UMY}. FT HELIX 134 150 {ECO:0000244|PDB:1UMY}. FT STRAND 154 158 {ECO:0000244|PDB:1UMY}. FT HELIX 164 175 {ECO:0000244|PDB:1UMY}. FT STRAND 181 185 {ECO:0000244|PDB:1UMY}. FT HELIX 198 207 {ECO:0000244|PDB:1UMY}. FT STRAND 211 219 {ECO:0000244|PDB:1UMY}. FT HELIX 221 236 {ECO:0000244|PDB:1UMY}. FT TURN 237 239 {ECO:0000244|PDB:1UMY}. FT STRAND 243 247 {ECO:0000244|PDB:1UMY}. FT HELIX 261 263 {ECO:0000244|PDB:1UMY}. FT TURN 265 269 {ECO:0000244|PDB:1UMY}. FT HELIX 272 274 {ECO:0000244|PDB:1UMY}. FT HELIX 278 291 {ECO:0000244|PDB:1UMY}. FT HELIX 304 313 {ECO:0000244|PDB:1UMY}. FT HELIX 315 318 {ECO:0000244|PDB:1UMY}. FT HELIX 323 327 {ECO:0000244|PDB:1UMY}. FT STRAND 330 332 {ECO:0000244|PDB:1UMY}. FT HELIX 333 335 {ECO:0000244|PDB:1UMY}. FT HELIX 341 344 {ECO:0000244|PDB:1UMY}. FT HELIX 349 354 {ECO:0000244|PDB:1UMY}. FT HELIX 378 397 {ECO:0000244|PDB:1UMY}. SQ SEQUENCE 407 AA; 44976 MW; 36E1D04A8E425887 CRC64; MAPIAGKKAK RGILERLNAG EVVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAVRQLH REFLRAGSNV MQTFTFYASE DKLENRGNYV AEKISGQKVN EAACDIARQV ADEGDALVAG GVSQTPSYLS CKSETEVKKI FHQQLEVFMK KNVDFLIAEY FEHVEEAVWA VEALKTSGKP IAATMCIGPE GDLHGVSPGE CAVRLVKAGA AIVGVNCHFD PSTSLQTIKL MKEGLEAARL KAYLMSHALA YHTPDCGKQG FIDLPEFPFG LEPRVATRWD IQKYAREAYN LGVRYIGGCC GFEPYHIRAI AEELAPERGF LPPASEKHGS WGSGLDMHTK PWIRARARKE YWQNLRIASG RPYNPSMSKP DAWGVTKGAA ELMQQKEATT EQQLRALFEK QKFKSAQ // ID BHMT1_XENLA Reviewed; 403 AA. AC Q5XGM3; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 07-JAN-2015, entry version 59. DE RecName: Full=Betaine--homocysteine S-methyltransferase 1; DE EC=2.1.1.5; GN Name=bhmt; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; OC Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC Converts betaine and homocysteine to dimethylglycine and CC methionine, respectively. This reaction is also required for the CC irreversible oxidation of choline (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Trimethylammonioacetate + L-homocysteine = CC dimethylglycine + L-methionine. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Amine and polyamine degradation; betaine degradation; CC sarcosine from betaine: step 1/2. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC084414; AAH84414.1; -; mRNA. DR RefSeq; NP_001088416.1; NM_001094947.1. DR UniGene; Xl.21139; -. DR ProteinModelPortal; Q5XGM3; -. DR SMR; Q5XGM3; 7-394. DR GeneID; 495275; -. DR KEGG; xla:495275; -. DR CTD; 635; -. DR Xenbase; XB-GENE-1008388; bhmt. DR HOVERGEN; HBG080367; -. DR KO; K00544; -. DR UniPathway; UPA00051; UER00083. DR UniPathway; UPA00291; UER00432. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006579; P:amino-acid betaine catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Cytoplasm; Metal-binding; Methyltransferase; Transferase; Zinc. FT CHAIN 1 403 Betaine--homocysteine S-methyltransferase FT 1. FT /FTId=PRO_0000273222. FT DOMAIN 8 311 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 214 214 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 296 296 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 297 297 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. SQ SEQUENCE 403 AA; 44181 MW; D7FAFA7DD70F3782 CRC64; MAPVGAKKGL LERLDAGEVV IGDGGFVFAL EKRGYVKAGP WTPEAAVEHP EAVRQLHREF LRAGANVMQT FTFYASDDKL ENRGNYVAEK ISGQKVNEVA CDIAREVANE GDALVAGGVS QTPSYLSCKS EVEVKGIFRK QLDVFIKKNV DFLIAEYFEH VEEAVWAVEV LKESGKPVAA TLCIGPEGDL NGVSPGECAV RLAKAGASVV GVNCHFDPMT CVATVKLMKE GLVAAKVKAH LMTQPLAYHT PDCGKQGFID LPEFPFALEP RIVTRWDIHK YARAAYDLGV RYIGGCCGFE PYHTRAIAEE LAPERGFLPK GSEKHGSWGS GLEMHTKPWV RARARRDYWE KLPPASGRPY CPSMSKPDEW GVTKGDADLM QQKEATTEQQ LKDLIAKQGI KSN // ID BHMT1_XENTR Reviewed; 403 AA. AC Q5M8Z0; Q5FWR7; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-2005, sequence version 1. DT 27-MAY-2015, entry version 70. DE RecName: Full=Betaine--homocysteine S-methyltransferase 1; DE EC=2.1.1.5; GN Name=bhmt; OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; OC Silurana. OX NCBI_TaxID=8364; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC Converts betaine and homocysteine to dimethylglycine and CC methionine, respectively. This reaction is also required for the CC irreversible oxidation of choline (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Trimethylammonioacetate + L-homocysteine = CC dimethylglycine + L-methionine. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Amine and polyamine degradation; betaine degradation; CC sarcosine from betaine: step 1/2. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC087774; AAH87774.1; -; mRNA. DR EMBL; BC089235; AAH89235.1; -; mRNA. DR RefSeq; NP_001011217.1; NM_001011217.1. DR UniGene; Str.8632; -. DR ProteinModelPortal; Q5M8Z0; -. DR SMR; Q5M8Z0; 7-395. DR STRING; 8364.ENSXETP00000001133; -. DR PaxDb; Q5M8Z0; -. DR Ensembl; ENSXETT00000001133; ENSXETP00000001133; ENSXETG00000000523. DR GeneID; 496651; -. DR KEGG; xtr:496651; -. DR CTD; 635; -. DR Xenbase; XB-GENE-1008382; bhmt. DR eggNOG; COG0646; -. DR GeneTree; ENSGT00390000003122; -. DR HOGENOM; HOG000231636; -. DR HOVERGEN; HBG080367; -. DR InParanoid; Q5M8Z0; -. DR KO; K00544; -. DR Reactome; REACT_313856; Sulfur amino acid metabolism. DR UniPathway; UPA00051; UER00083. DR UniPathway; UPA00291; UER00432. DR Proteomes; UP000008143; Unassembled WGS sequence. DR Bgee; Q5M8Z0; -. DR ExpressionAtlas; Q5M8Z0; baseline. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006579; P:amino-acid betaine catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Complete proteome; Cytoplasm; Metal-binding; Methyltransferase; KW Reference proteome; Transferase; Zinc. FT CHAIN 1 403 Betaine--homocysteine S-methyltransferase FT 1. FT /FTId=PRO_0000273223. FT DOMAIN 8 311 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 214 214 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 296 296 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 297 297 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. SQ SEQUENCE 403 AA; 44154 MW; 079A8C12A4A73CDB CRC64; MAPTGAKKGL LERLDAGEVV IGDGGFVFAL EKRGYVKAGP WTPEAAVEHP EAVRQLHREF LRAGANVMQT FTFYASDDKL ENRGNYVAKK ISGQKVNEAA CDIAREVANE GDALVAGGVS QTPSYLSCKS EVEVKGIFRK QLDVFIKKNV DFLIAEYFEH VEEAVWAVEV LKESGKPVAA TLCIGPQGDL NGVTPGECAV RLAKAGASVV GVNCHFDPMT CIATVKLMKE GLVAAKVKAH LMTQPLAYHT PDCGKQGFID LPEFPFALEP RIVTRWDIHK YAREAYNLGV RYIGGCCGFE PYHTRAIAEE LAPERGFLPP GSEKHGSWGS GLEMHTKPWV RARARRDYWE KLPPASGRPC CPSMSKPDAW GVTKGDADLM QQKEATTEQQ LIDLFAKQCI KSN // ID BHMT2_HUMAN Reviewed; 363 AA. AC Q9H2M3; B7Z516; Q9NXX7; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAY-2015, entry version 110. DE RecName: Full=S-methylmethionine--homocysteine S-methyltransferase BHMT2; DE Short=SMM-hcy methyltransferase; DE EC=2.1.1.10; DE AltName: Full=Betaine--homocysteine S-methyltransferase 2; GN Name=BHMT2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND RP POSSIBLE INTERACTION WITH PRNP. RX PubMed=11087663; DOI=10.1006/geno.2000.6319; RA Chadwick L.H., McCandless S.E., Silverman G.L., Schwartz S., RA Westaway D., Nadeau J.H.; RT "Betaine-homocysteine methyltransferase-2: cDNA cloning, gene RT sequence, physical mapping, and expression of the human and mouse RT genes."; RL Genomics 70:66-73(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 11-363 (ISOFORM 1). RC TISSUE=Adipose tissue, and Kidney; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., RA Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND ZINC-BINDING. RX PubMed=18230605; DOI=10.1074/jbc.M710449200; RA Szegedi S.S., Castro C.C., Koutmos M., Garrow T.A.; RT "Betaine-homocysteine S-methyltransferase-2 is an S-methylmethionine- RT homocysteine methyltransferase."; RL J. Biol. Chem. 283:8939-8945(2008). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC Converts homocysteine to methionine using S-methylmethionine (SMM) CC as a methyl donor. {ECO:0000269|PubMed:18230605}. CC -!- CATALYTIC ACTIVITY: S-methyl-L-methionine + L-homocysteine = 2 L- CC methionine. {ECO:0000269|PubMed:18230605}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:18230605}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:18230605}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. CC -!- SUBUNIT: Homotetramer (By similarity). May interact with PRNP. CC {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9H2M3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9H2M3-2; Sequence=VSP_042938; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Expressed in liver and kidney and at reduced CC levels in the brain, heart, and skeletal muscle. CC {ECO:0000269|PubMed:11087663}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA90880.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF257473; AAG41356.1; -; mRNA. DR EMBL; AK000008; BAA90880.1; ALT_INIT; mRNA. DR EMBL; AK298298; BAH12752.1; -; mRNA. DR EMBL; AC008502; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC020665; AAH20665.1; -; mRNA. DR CCDS; CCDS4045.1; -. [Q9H2M3-1] DR CCDS; CCDS54871.1; -. [Q9H2M3-2] DR RefSeq; NP_001171476.1; NM_001178005.1. [Q9H2M3-2] DR RefSeq; NP_060084.2; NM_017614.4. [Q9H2M3-1] DR UniGene; Hs.114172; -. DR ProteinModelPortal; Q9H2M3; -. DR SMR; Q9H2M3; 10-362. DR BioGrid; 117245; 4. DR STRING; 9606.ENSP00000255192; -. DR BindingDB; Q9H2M3; -. DR ChEMBL; CHEMBL2163167; -. DR DrugBank; DB00134; L-Methionine. DR PhosphoSite; Q9H2M3; -. DR BioMuta; BHMT2; -. DR DMDM; 74733563; -. DR PaxDb; Q9H2M3; -. DR PRIDE; Q9H2M3; -. DR DNASU; 23743; -. DR Ensembl; ENST00000255192; ENSP00000255192; ENSG00000132840. [Q9H2M3-1] DR Ensembl; ENST00000521567; ENSP00000430278; ENSG00000132840. [Q9H2M3-2] DR GeneID; 23743; -. DR KEGG; hsa:23743; -. DR UCSC; uc003kft.3; human. [Q9H2M3-1] DR UCSC; uc011cth.2; human. [Q9H2M3-2] DR CTD; 23743; -. DR GeneCards; GC05P078366; -. DR HGNC; HGNC:1048; BHMT2. DR HPA; HPA044573; -. DR MIM; 605932; gene. DR neXtProt; NX_Q9H2M3; -. DR PharmGKB; PA25351; -. DR eggNOG; COG0646; -. DR GeneTree; ENSGT00390000003122; -. DR HOGENOM; HOG000231636; -. DR HOVERGEN; HBG080367; -. DR InParanoid; Q9H2M3; -. DR OMA; PEGDMHD; -. DR OrthoDB; EOG79GT7C; -. DR PhylomeDB; Q9H2M3; -. DR TreeFam; TF329202; -. DR BioCyc; MetaCyc:HS05696-MONOMER; -. DR UniPathway; UPA00051; UER00083. DR ChiTaRS; BHMT2; human. DR GenomeRNAi; 23743; -. DR NextBio; 46663; -. DR PRO; PR:Q9H2M3; -. DR Proteomes; UP000005640; Chromosome 5. DR Bgee; Q9H2M3; -. DR CleanEx; HS_BHMT2; -. DR ExpressionAtlas; Q9H2M3; baseline and differential. DR Genevestigator; Q9H2M3; -. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IDA:BHF-UCL. DR GO; GO:0061627; F:S-methylmethionine-homocysteine S-methyltransferase activity; IDA:BHF-UCL. DR GO; GO:0008270; F:zinc ion binding; IDA:BHF-UCL. DR GO; GO:0071267; P:L-methionine salvage; IDA:BHF-UCL. DR GO; GO:0046500; P:S-adenosylmethionine metabolic process; IDA:BHF-UCL. DR GO; GO:0033528; P:S-methylmethionine cycle; IBA:GO_Central. DR GO; GO:0033477; P:S-methylmethionine metabolic process; IDA:BHF-UCL. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; Metal-binding; KW Methyltransferase; Phosphoprotein; Reference proteome; Transferase; KW Zinc. FT CHAIN 1 363 S-methylmethionine--homocysteine S- FT methyltransferase BHMT2. FT /FTId=PRO_0000273224. FT DOMAIN 11 305 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 208 208 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 290 290 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 291 291 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT MOD_RES 321 321 Phosphoserine. FT {ECO:0000269|PubMed:24275569}. FT VAR_SEQ 87 150 Missing (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_042938. SQ SEQUENCE 363 AA; 40354 MW; 92D35414D2D56003 CRC64; MAPAGRPGAK KGILERLESG EVVIGDGSFL ITLEKRGYVK AGLWTPEAVI EHPDAVRQLH MEFLRAGSNV MQTFTFSASE DNMESKWEDV NAAACDLARE VAGKGDALVA GGICQTSIYK YQKDEARIKK LFRQQLEVFA WKNVDFLIAE YFEHVEEAVW AVEVLKESDR PVAVTMCIGP EGDMHDITPG ECAVRLVKAG ASIVGVNCRF GPDTSLKTME LMKEGLEWAG LKAHLMVQPL GFHAPDCGKE GFVDLPEYPF GLESRVATRW DIQKYAREAY NLGVRYIGGC CGFEPYHIRA IAEELAPERG FLPPASEKHG SWGSGLDMHT KPWIRARARR EYWENLLPAS GRPFCPSLSK PDF // ID BHMT2_MOUSE Reviewed; 363 AA. AC Q91WS4; B1B1C9; Q8C1U2; Q9EQE8; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAY-2015, entry version 87. DE RecName: Full=S-methylmethionine--homocysteine S-methyltransferase BHMT2; DE Short=SMM-hcy methyltransferase; DE EC=2.1.1.10; DE AltName: Full=Betaine--homocysteine S-methyltransferase 2; GN Name=Bhmt2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RX PubMed=11087663; DOI=10.1006/geno.2000.6319; RA Chadwick L.H., McCandless S.E., Silverman G.L., Schwartz S., RA Westaway D., Nadeau J.H.; RT "Betaine-homocysteine methyltransferase-2: cDNA cloning, gene RT sequence, physical mapping, and expression of the human and mouse RT genes."; RL Genomics 70:66-73(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Gall bladder, and Liver; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [6] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=18230605; DOI=10.1074/jbc.M710449200; RA Szegedi S.S., Castro C.C., Koutmos M., Garrow T.A.; RT "Betaine-homocysteine S-methyltransferase-2 is an S-methylmethionine- RT homocysteine methyltransferase."; RL J. Biol. Chem. 283:8939-8945(2008). CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC Converts homocysteine to methionine using S-methylmethionine (SMM) CC as a methyl donor. {ECO:0000269|PubMed:18230605}. CC -!- CATALYTIC ACTIVITY: S-methyl-L-methionine + L-homocysteine = 2 L- CC methionine. {ECO:0000269|PubMed:18230605}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Expressed in fetal heart, lung, liver, kidney CC and eye. {ECO:0000269|PubMed:11087663}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF257474; AAG41357.1; -; mRNA. DR EMBL; AK090308; BAC41163.1; -; mRNA. DR EMBL; AK145901; BAE26737.1; -; mRNA. DR EMBL; CT030023; CAO77969.1; -; Genomic_DNA. DR EMBL; AC158524; CAO77969.1; JOINED; Genomic_DNA. DR EMBL; BC013515; AAH13515.1; -; mRNA. DR CCDS; CCDS26689.1; -. DR RefSeq; NP_075022.2; NM_022884.2. DR UniGene; Mm.29981; -. DR ProteinModelPortal; Q91WS4; -. DR SMR; Q91WS4; 10-363. DR PhosphoSite; Q91WS4; -. DR PaxDb; Q91WS4; -. DR PRIDE; Q91WS4; -. DR Ensembl; ENSMUST00000015941; ENSMUSP00000015941; ENSMUSG00000042118. DR GeneID; 64918; -. DR KEGG; mmu:64918; -. DR UCSC; uc007rlk.1; mouse. DR CTD; 23743; -. DR MGI; MGI:1891379; Bhmt2. DR eggNOG; COG0646; -. DR GeneTree; ENSGT00390000003122; -. DR HOGENOM; HOG000231636; -. DR HOVERGEN; HBG080367; -. DR InParanoid; Q91WS4; -. DR OMA; PEGDMHD; -. DR OrthoDB; EOG79GT7C; -. DR PhylomeDB; Q91WS4; -. DR TreeFam; TF329202; -. DR UniPathway; UPA00051; UER00083. DR NextBio; 320219; -. DR PRO; PR:Q91WS4; -. DR Proteomes; UP000000589; Chromosome 13. DR Bgee; Q91WS4; -. DR CleanEx; MM_BHMT2; -. DR Genevestigator; Q91WS4; -. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0070062; C:extracellular exosome; ISO:MGI. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IBA:GO_Central. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; ISO:MGI. DR GO; GO:0061627; F:S-methylmethionine-homocysteine S-methyltransferase activity; ISO:MGI. DR GO; GO:0008270; F:zinc ion binding; ISO:MGI. DR GO; GO:0071267; P:L-methionine salvage; ISO:MGI. DR GO; GO:0009086; P:methionine biosynthetic process; ISO:MGI. DR GO; GO:0046500; P:S-adenosylmethionine metabolic process; ISO:MGI. DR GO; GO:0033528; P:S-methylmethionine cycle; IBA:GO_Central. DR GO; GO:0033477; P:S-methylmethionine metabolic process; ISO:MGI. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 1: Evidence at protein level; KW Complete proteome; Metal-binding; Methyltransferase; Phosphoprotein; KW Reference proteome; Transferase; Zinc. FT CHAIN 1 363 S-methylmethionine--homocysteine S- FT methyltransferase BHMT2. FT /FTId=PRO_0000273225. FT DOMAIN 11 305 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 208 208 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 290 290 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 291 291 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT MOD_RES 321 321 Phosphoserine. FT {ECO:0000269|PubMed:17242355}. FT CONFLICT 13 13 I -> V (in Ref. 1; AAG41357). FT {ECO:0000305}. FT CONFLICT 27 27 S -> G (in Ref. 4; AAH13515). FT {ECO:0000305}. FT CONFLICT 36 36 R -> G (in Ref. 1; AAG41357). FT {ECO:0000305}. FT CONFLICT 327 327 N -> S (in Ref. 1; AAG41357). FT {ECO:0000305}. SQ SEQUENCE 363 AA; 39872 MW; C7367F1B10B07EEF CRC64; MAPAGSTRAK KGILERLDSG EVVVGDSGFL FTLEKRGFVK AGLWTPEAVV EHPSAVRQLH TEFLRAGADV LQTFTFSATE DNMASKWEAV NAAACDLAQE VAGGGGALVA GGICQTSLYK YHKDETRIKN IFRLQLEVFA RKNVDFLIAE YFEHVEEAVW AVEVLREVGA PVAVTMCIGP EGDMHDVTPG ECAVKLARAG ADIIGVNCRF GPWTSLQTMK LMKEGLRDAS LQAHLMVQCL GFHTPDCGKG GFVDLPEYPF GLEPRVATRW DIQKYAREAY NLGIRYIGGC CGFEPYHIRA IAEELAPERG FLPPASEKHG SWGSGLNMHT KPWIRARARR EYWENLLPAS GRPFCPSLSK PDA // ID BHMT2_PONAB Reviewed; 363 AA. AC Q5RF32; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 04-MAR-2015, entry version 56. DE RecName: Full=S-methylmethionine--homocysteine S-methyltransferase BHMT2; DE Short=SMM-hcy methyltransferase; DE EC=2.1.1.10; DE AltName: Full=Betaine--homocysteine S-methyltransferase 2; GN Name=BHMT2; OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pongo. OX NCBI_TaxID=9601; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RG The German cDNA consortium; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC Converts betaine and homocysteine to dimethylglycine and CC methionine, respectively. This reaction is also required for the CC irreversible oxidation of choline (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: S-methyl-L-methionine + L-homocysteine = 2 L- CC methionine. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR857329; CAH89625.1; -; mRNA. DR RefSeq; NP_001127177.1; NM_001133705.2. DR ProteinModelPortal; Q5RF32; -. DR SMR; Q5RF32; 10-362. DR Ensembl; ENSPPYT00000018128; ENSPPYP00000017422; ENSPPYG00000015585. DR GeneID; 100174229; -. DR KEGG; pon:100174229; -. DR CTD; 23743; -. DR GeneTree; ENSGT00390000003122; -. DR HOVERGEN; HBG080367; -. DR InParanoid; Q5RF32; -. DR OrthoDB; EOG79GT7C; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000001595; Chromosome 5. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Complete proteome; Metal-binding; Methyltransferase; Phosphoprotein; KW Reference proteome; Transferase; Zinc. FT CHAIN 1 363 S-methylmethionine--homocysteine S- FT methyltransferase BHMT2. FT /FTId=PRO_0000273226. FT DOMAIN 11 305 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 208 208 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 290 290 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 291 291 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT MOD_RES 321 321 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9H2M3}. SQ SEQUENCE 363 AA; 40336 MW; D2B34B3F8EF4A103 CRC64; MAPAGHPGAK RGILERLESG EVVIGDGSFL ITLEKRGYVK AGLWTPEAVI EHPDAVRQLH MEFLRAGSNV MQTFTFSASE DNMESKWEDV NAAACDLARE VAGKGDALVA GGICQTSIYK YHKDEARIKK LFRQQLEVFA WKNVDFLIAE YFEHVEEAVW AVEVLKESDR PVAVTMCISP EGDMHDITPG ECAVRLVKAG ASIVGVNCRF GPETSLKTIE LMKEGLQRAG LKAHLMVQPL GFHTPDCGKE GFVDLPEYPF GLESRAATRW DIQKYAREAY NQGVRYIGGC CGFEPYHIRA IAEELAPERG FLPPASEKHG SWGSALDMHT KPWVRARARR EYWENLLPAS GRPFCPSLSK PDV // ID BHMT2_RAT Reviewed; 363 AA. AC Q68FT5; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 04-FEB-2015, entry version 75. DE RecName: Full=S-methylmethionine--homocysteine S-methyltransferase BHMT2; DE Short=SMM-hcy methyltransferase; DE EC=2.1.1.10; DE AltName: Full=Betaine--homocysteine S-methyltransferase 2; GN Name=Bhmt2; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC Converts betaine and homocysteine to dimethylglycine and CC methionine, respectively. This reaction is also required for the CC irreversible oxidation of choline (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: S-methyl-L-methionine + L-homocysteine = 2 L- CC methionine. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC079366; AAH79366.1; -; mRNA. DR RefSeq; NP_001014278.2; NM_001014256.2. DR UniGene; Rn.8494; -. DR ProteinModelPortal; Q68FT5; -. DR SMR; Q68FT5; 10-363. DR STRING; 10116.ENSRNOP00000058419; -. DR PaxDb; Q68FT5; -. DR PRIDE; Q68FT5; -. DR GeneID; 365972; -. DR KEGG; rno:365972; -. DR UCSC; RGD:1359418; rat. DR CTD; 23743; -. DR RGD; 1359418; Bhmt2. DR eggNOG; COG0646; -. DR HOGENOM; HOG000231636; -. DR HOVERGEN; HBG080367; -. DR InParanoid; Q68FT5; -. DR PhylomeDB; Q68FT5; -. DR UniPathway; UPA00051; UER00083. DR NextBio; 688443; -. DR PRO; PR:Q68FT5; -. DR Proteomes; UP000002494; Unplaced. DR Genevestigator; Q68FT5; -. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IBA:GO_Central. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IBA:GO_Central. DR GO; GO:0061627; F:S-methylmethionine-homocysteine S-methyltransferase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR GO; GO:0033528; P:S-methylmethionine cycle; IBA:GO_Central. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Complete proteome; Metal-binding; Methyltransferase; KW Reference proteome; Transferase; Zinc. FT CHAIN 1 363 S-methylmethionine--homocysteine S- FT methyltransferase BHMT2. FT /FTId=PRO_0000273227. FT DOMAIN 11 305 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 208 208 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 290 290 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 291 291 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. SQ SEQUENCE 363 AA; 39929 MW; 403AAC188B979BFE CRC64; MAPAGGPRVK KVILERLDSG EVVVGDGGFL FTLEKRGFVK AGLWTPEAVV EYPSAVRQLH TEFLRAGADV LQTFTFSAAE DRMESKWEAV NAAACDLAQE VADGGAALVA GGICQTSLYK YHKDETRIKN IFRLQLGVFA RKNVDFLIAE YFEHVEEAVW AVEVLREVGA PVAVTMCIGP EGDMHGVTPG ECAVRLSRAG ANIIGVNCRF GPWTSLQTMK LMKEGLRDAG LQAHLMVQCL GFHTPDCGKG GFVDLPEYPF GLEPRVATRW DIQKYAREAY NLGVRYIGGC CGFEPYHIRA IAEELAPERG FLPPASEKHG IWGSGLDMHT KPWIRARARR EYWETLLPAS GRPFCPSLSK PDA // ID C0ARP3_9ENTR Unreviewed; 1081 AA. AC C0ARP3; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 27-MAY-2015, entry version 36. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEG87393.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEG87393.1}; GN Name=metH {ECO:0000313|EMBL:EEG87393.1}; GN ORFNames=PROPEN_00464 {ECO:0000313|EMBL:EEG87393.1}; OS Proteus penneri ATCC 35198. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Proteus. OX NCBI_TaxID=471881 {ECO:0000313|EMBL:EEG87393.1}; RN [1] {ECO:0000313|EMBL:EEG87393.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35198 {ECO:0000313|EMBL:EEG87393.1}; 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] {ECO:0000313|EMBL:EEG87393.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35198 {ECO:0000313|EMBL:EEG87393.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEG87393.1}. 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; ABVP01000018; EEG87393.1; -; Genomic_DNA. DR RefSeq; WP_006536383.1; NZ_GG661997.1. DR EnsemblBacteria; EEG87393; EEG87393; PROPEN_00464. DR PATRIC; 36113646; VBIProPen132194_3338. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEG87393.1}; KW Transferase {ECO:0000313|EMBL:EEG87393.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 103 103 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 166 166 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 167 167 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 614 614 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1081 AA; 119999 MW; 301EED2FD214AC90 CRC64; MLMIQPFRNV SFDKLVEAYR EATRGLIKGG VDLIMVETIF DTLNAKAAIF AIKCEFESLN IELPVMISGT ITDASGRTLT GQTTEAFYHS LRHADALSFG LNCALGPKEL RQYIQTLSQI SETYVSAHPN AGLPNAFGGY DLDAQEMAEQ IKEWAQAGFL NIVGGCCGTT PAHILAISQA VEGIAPRVLP TLKKACRLSG LEPLVIDDNS LFVNVGERTN VTGSAKFKRL IKEGNYQEAL DVARQQVENG AQIIDINMDE GMLDAVEAMT RFLNLIAGEP DIAKVPVMID SSKWEVIEEG LKCIQGKGIV NSISMKEGEI PFLEHAKLVR KYGAAVVVMA FDEVGQADTR ERKIEICRRA YQLLTEQAGF PPEDIIFDPN IFAVATGIAE HNNYAVDFIE VCADIKSQLP YALISGGVSN VSFSFRGNDP VREAIHSVFL YYAVKNGMDM GIVNAGQLAI YDSLPDELRN AVEDVILNRH EESTDNLLAL AERYRGSKSD EQNHQLAEWR QWDVEKRLEY ALVKGITEFI VEDTEACRQQ ASSPIEVIEG PLMNGMNTVG DLFGEGKMFL PQVVKSARVM KQAVAYLEPY IQATKQAGTS AGKILLATVK GDVHDIGKNI VGVVLQCNNY EIIDLGVMVP CDKILQTAID EKVDIIGLSG LITPSLDEMV NVAKEMERRG FSLPLMIGGA TTSKAHTAVK IEPNYSHPTV YVQNASRTVG VVAALLSETQ KADFVAKTRR EYEVVRQQYA RKKPRTPPVS LEAARQNALQ IDWQNYIPPK PNQLGVQEIA ASIETLREYI DWTPFFMTWS LAGKYPRILE DDVVGEEAKR VFADANAMLD KLSHEKLLTP KGIVGLFPAN RVGDDIVIYR DETRQQPLLY SCHLRQQTEK KEFPNYCLAD FIAPVESGVP DYFGAFAVTG GLEEDTLANA YDNAHDDYNK IMVKALSDRL AEAFAEYLHQ QVRTKILGYN PDEALSNDEL IREKYQGTRP APGYPACPEH TEKAKIWQLL DVENRIGMKL TDAYAMWPGA SVSGWYFSHP ESKYFAVAQI QKDQVDDYAK RRGMSVSEVE RWLAPNLGYE S // ID C0ARP4_9ENTR Unreviewed; 152 AA. AC C0ARP4; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEG87394.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEG87394.1}; GN Name=metH {ECO:0000313|EMBL:EEG87394.1}; GN ORFNames=PROPEN_00465 {ECO:0000313|EMBL:EEG87394.1}; OS Proteus penneri ATCC 35198. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Proteus. OX NCBI_TaxID=471881 {ECO:0000313|EMBL:EEG87394.1}; RN [1] {ECO:0000313|EMBL:EEG87394.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35198 {ECO:0000313|EMBL:EEG87394.1}; 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] {ECO:0000313|EMBL:EEG87394.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35198 {ECO:0000313|EMBL:EEG87394.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEG87394.1}. 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; ABVP01000018; EEG87394.1; -; Genomic_DNA. DR RefSeq; WP_006536384.1; NZ_GG661997.1. DR EnsemblBacteria; EEG87394; EEG87394; PROPEN_00465. DR PATRIC; 36113648; VBIProPen132194_3339. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEG87394.1}; KW Transferase {ECO:0000313|EMBL:EEG87394.1}. SQ SEQUENCE 152 AA; 16776 MW; 3AC72F5C94B3501E CRC64; MANIKQQLVE ALEKRILVLD GAMGTMIQQY QLTEADYRGE RFADWNCDVK GNNDLLVLTQ PQIIADIHDA YFQAGADIVE TNTFNSTSIA MADYHMESLC FELNEEAAKL AKACADKWSA LTPDKPRYVA GVLGPTNRTA SISPDVNDPA FS // ID C0B742_9FIRM Unreviewed; 808 AA. AC C0B742; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEG90735.1}; GN ORFNames=COPCOM_00963 {ECO:0000313|EMBL:EEG90735.1}; OS Coprococcus comes ATCC 27758. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Coprococcus. OX NCBI_TaxID=470146 {ECO:0000313|EMBL:EEG90735.1}; RN [1] {ECO:0000313|EMBL:EEG90735.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27758 {ECO:0000313|EMBL:EEG90735.1}; 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] {ECO:0000313|EMBL:EEG90735.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27758 {ECO:0000313|EMBL:EEG90735.1}; 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. {ECO:0000313|EMBL:EEG90735.1}. 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; ABVR01000037; EEG90735.1; -; Genomic_DNA. DR RefSeq; WP_008369245.1; NZ_GG662007.1. DR EnsemblBacteria; EEG90735; EEG90735; COPCOM_00963. DR PATRIC; 29071134; VBICopCom38835_0345. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEG90735.1}; KW Transferase {ECO:0000313|EMBL:EEG90735.1}. SQ SEQUENCE 808 AA; 88525 MW; 8652F99247F3123A CRC64; MNIRERLGKE LLFLDGGMGT LLQAEGLAPG ELPETWNIEH PEKVEAIHRR YYEAGSDVVL ANTFGANICK FHDDRYTVEE VIRAGIANAK RAGEQIGKET YVALDMGPTG KLLKPMGDLD FDDAYEAFAE AVRYGEKYGA DLIHIETMSD TYEVKAAILA AKENSSLPVF VTMIFDERGK LLTGGDVPSV VAMLEGLRVD ALGLNCGLGP KQMLPILNDL RRYTSLPIIV KPNAGLPKQK NGETYYDVEP DEFARIMQEV VKGGACVIGG CCGTTPEHIK KLVEECKDLP LREIEKKHDT IVSSYGQAVI LDDMPRIIGE RINPTGKKKF KEALKNEDMD YILKEAITQQ DKGAHILDVN VGLPDIDEVA MMEKVVKELQ SVTSLPLQID TVDGKAMERA MRIYNGKPMI NSVNGKQVSM DEVFPLVRKY GGVVVGLTID EEGIPKDAEG RVRVAGKIIN EAAKYGIDKK DIVIDVLTMT ISSEKDGAKV TLEALKRVRE EFGVRTVLGV SNISFGLPRR PIVNSYFYAM AMQNGLTAGI INPSSEDMMK AYRSYNALMG FDENCTNYIS TYAGTTETVT VQASQAAAVA GNAPKAAGVE MTLKYAIERG LKEEAHHITR DLIGTREPLD IIQEELIPAL NVVGEGFEKG TVFLPQLLMS ADAAKIAFAV IKDVLASSGQ EEEKKEKIIL ATVKGDIHDI GKNIVKVLLE NYGFDVIDLG KDVPPEAIVE KAVEENVTLV GLSALMTTTV VSMEETIKLL REKKPDCKVM VGGAVLNQDY ADMIGADFYG KDAMQSVHYA QKFFGMVE // ID C0BFV6_FLABM Unreviewed; 334 AA. AC C0BFV6; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEG41959.1}; GN ORFNames=Flav2ADRAFT_1267 {ECO:0000313|EMBL:EEG41959.1}; OS Flavobacteria bacterium (strain MS024-2A). OC Bacteria; Bacteroidetes; Flavobacteriia. OX NCBI_TaxID=487796 {ECO:0000313|EMBL:EEG41959.1}; RN [1] {ECO:0000313|EMBL:EEG41959.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS024-2A {ECO:0000313|EMBL:EEG41959.1}; RG US DOE Joint Genome Institute (JGI-PGF); RA Woyke T., Xie G., Copeland A., Gonzalez J., Han C., Kiss H., Saw J., RA Senin P., Chatterji S., Cheng J.-F., Eisen J.A., Sieracki M.E., RA Stepanauskas R.; RT "Assembling the metagenome, one cell at a time."; 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. {ECO:0000313|EMBL:EEG41959.1}. 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; ABVV01000001; EEG41959.1; -; Genomic_DNA. DR RefSeq; WP_008865289.1; NZ_ABVV01000001.1. DR EnsemblBacteria; EEG41959; EEG41959; Flav2ADRAFT_1267. DR PATRIC; 27390906; VBIFlaBac39156_0123. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEG41959.1}; KW Transferase {ECO:0000313|EMBL:EEG41959.1}. SQ SEQUENCE 334 AA; 36783 MW; 0782A347CD486065 CRC64; MSIVKELEQR ILVLDGAMGT MIQNHNLEEE HFRGERFLNH PAILKGNNDL LSITQPEIIK DIHRKYFEAG ADIVETNTFS STSIGMADYQ MEILAYELNY ESAKIAKEVS KEYLEKTPNQ PRYVAGSIGP TNKTASMSPD VNDPGYRAIT FDELVTAYKE QVNGLVDGGS DLLLVETIFD TLNAKAALYA INEIKEERGI DIPVMVSGTI TDASGRTLSG QTVEAFRISM SHIPILSIGF NCALGADQLL PYVKRLANQS DLFVSAHPNA GLPNAFGAYD QSPTEMQTLI EDYLKQNAVN IIGGCCGTTP DHIRLIAEVV KKYTPRNPKL HSDV // ID C0BM50_9BACT Unreviewed; 1237 AA. AC C0BM50; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 01-APR-2015, entry version 37. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEG43251.1}; GN ORFNames=Flav3CDRAFT_0725 {ECO:0000313|EMBL:EEG43251.1}; OS Flavobacteria bacterium MS024-3C. OC Bacteria; Bacteroidetes; Flavobacteriia. OX NCBI_TaxID=487797 {ECO:0000313|EMBL:EEG43251.1}; RN [1] {ECO:0000313|EMBL:EEG43251.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS024-3C {ECO:0000313|EMBL:EEG43251.1}; RG US DOE Joint Genome Institute (JGI-PGF); RA Woyke T., Xie G., Copeland A., Gonzalez J., Han C., Kiss H., Saw J., RA Senin P., Chatterji S., Cheng J.-F., Eisen J.A., Sieracki M.E., RA Stepanauskas R.; RT "Assembling the metagenome, one cell at a time."; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEG43251.1}. 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; ABVW01000002; EEG43251.1; -; Genomic_DNA. DR RefSeq; WP_008867459.1; NZ_ABVW01000002.1. DR EnsemblBacteria; EEG43251; EEG43251; Flav3CDRAFT_0725. DR PATRIC; 27395408; VBIFlaBac105578_0521. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 253 253 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 316 316 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 771 771 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1237 AA; 135653 MW; 62922EF780E27DE6 CRC64; MSNTPQSTLE KPLVKDLIRE KVLVLDGAMG TMIQEYKFTE EDYRGSRFAT YEHPLQGNND LLTLTQPEAI QTIHEKYLAA GADIIETNTF SCTTIAMADY YMEDLVYELN YEATRIALKA AEKYTLLDPS KPRYVAGSIG PTNRTASLSP DVNNPGYRAV SFEDLRIAYR QQVEALLDAG VDILLVETVF DTLNAKAALY AIDEVKAERN IATPVMVSGT ITDASGRTLS GQTAEAFLIS IAHSDLLSVG FNCALGAKAL LPHLEVLAKK APFGVSAHPN AGLPNAFGGY DESAAEMAAQ IQEYVDLGLV NIVGGCCGTR PSHIEAIAAI AAKASPRKII QKQLGPMQLS GLEPLILTPD LNFVNVGERT NVAGSKMFLR LIKEELYDQA LAVAREQVEN GAQIIDINMD DGLIDGEEAM VNFLNLVVAE PDISRVPIMI DSSKWPIIEA GLRVVQGKCV VNSISLKEGE AAFLAQALKI KNYGAAVIIM AFDEVGQADN YHRRIEIAKR SYDLLVSQID FPAQDIIFDL NIFPVATGMD EHKLNAIDFI KATKWVRENL PGVSVSGGVS NVSFSFRGNN PVREAMHSVF LYHAVKAGMN MGIVNPAMLE VYSDIPKDLL AHVEDVILNR REDATERLLD FAEGFVGAKK ESKVDLSWRE EPLQNRITRA LVKGLDAYII EDVEAARNSV SAPIQVIEGH LMTGMNVVGD LFGSGKMFLP QVVKSARVMK KAVAYLLPYI EEAKKLQVDY DATASQSAGK ILMATVKGDV HDIGKNIVSV VLACNNYEII DLGVMVPPDK IIAAAKEHQV DAIGLSGLIT PSLDEMVFLA EAMQREGFTM PLLIGGATTS KAHTAVKIAP QYGQTVVHVN DASRAVTVVG DLLQPDTSAA YKTKLKEDYD QFRTQFLNRS KTKEYVSLAV ARENALQLDF KNTLPKAPNT MGIQVIEKQD LRALVPFIDW TPFFRSWELH GRFPDILTDA VVGEQASTLF EEAQAMLEKI ISEERFTAKA VFGLFPAERS GSDDISIQKD ANTSYVFRTL RQQIKKKEGV AHRALSDYIA PPSEGVHDHM GAFCVTAGFG SEEMALTYQA ALDDYNSIMV KALADRLAEA FAEYLHLEVR KEHWGYAAQE SLDPNALIAE EYKGIRPAPG YPACPDHLEK TTLWELLEVE EKIGVSLTES LAMWPAASVS GYYFAHPEAK YFGVGKITQD QLEDFASRKD ISLATAKKWL APNLADL // ID C0C3T5_9FIRM Unreviewed; 794 AA. AC C0C3T5; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEG73184.1}; GN ORFNames=CLOHYLEM_06747 {ECO:0000313|EMBL:EEG73184.1}; OS [Clostridium] hylemonae DSM 15053. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=553973 {ECO:0000313|EMBL:EEG73184.1}; RN [1] {ECO:0000313|EMBL:EEG73184.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 15053 {ECO:0000313|EMBL:EEG73184.1}; 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] {ECO:0000313|EMBL:EEG73184.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 15053 {ECO:0000313|EMBL:EEG73184.1}; 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. {ECO:0000313|EMBL:EEG73184.1}. 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; ABYI02000030; EEG73184.1; -; Genomic_DNA. DR RefSeq; WP_006444106.1; NZ_GG657759.1. DR EnsemblBacteria; EEG73184; EEG73184; CLOHYLEM_06747. DR PATRIC; 30579146; VBICloHyl57588_2296. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEG73184.1}; KW Transferase {ECO:0000313|EMBL:EEG73184.1}. SQ SEQUENCE 794 AA; 86740 MW; 782A11AC77ED928A CRC64; MISQRLGREL LFFDGGMGTL LQSKGLKPGE LPETWNLTHR EEIIDIHRQY VEAGSDIVLT NTFGANALKF HDTEYDLEEI VTSAVGNVRE AARTGVNDGR RVYTALDIGP TGKLLKPMGD LGFEEAYEAF KEVVRYGEAA GADLVHIETM SDTYEVKAAV LAVKENTDLP VFATMIFDER GKLLTGADVL SVVALLEGLR VDALGINCGM GPEQMMSILD EIMRYTSIPV VVKPNAGLPK QREGEVYYDV DPEHFAEAMC RIVKKGACVI GGCCGTTPAH IKAMTERCAG LVPAVPTSKK ETVVSSYGQG VVLGDRPVII GERINPTGKS KFKQALKEHD LDYILREGIT QQEKGAHILD VNVGLPDIDE VSMMREVVCE LQSVTSLPLQ IDTVDIEAME AAMRIYNGKP MVNSVNGKKE SMDAVFPLIQ KYGGVVIGLT IDENGIPDSA DGRVKVAGNI IEEAAKYGID RKDIVIDVLA MTISSEPEGA KVTLEALRKV RECYGVRTVL GVSNISFGLP FRPAVNANFY TMAMQSGLSA GIINPSSEDM MRSYYSFCAL MNFDHNCEQY IAQYGSQTSA PVQMSEMTLK SAIEKGLKEE SYQAALRLVK EKAPLEIINE YLIPALDVVG KGFEKGTVFL PQLLMSADAA KLAFAVLKEE LARSGESAQK KEKVILATVK GDIHDIGKNI VKVLLENYSF DVIDLGKDVP PEEIVLRAVS EDVRLVGLSA LMTTTVVSME RTIKLLRRDK PDCKVMVGGA VLNEEYAEMI GADFYGKDAM QSVYYAQKIL QTAE // ID C0CIQ1_9FIRM Unreviewed; 288 AA. AC C0CIQ1; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EEG50370.1}; GN ORFNames=RUMHYD_00715 {ECO:0000313|EMBL:EEG50370.1}; OS Blautia hydrogenotrophica DSM 10507. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Blautia. OX NCBI_TaxID=476272 {ECO:0000313|EMBL:EEG50370.1}; RN [1] {ECO:0000313|EMBL:EEG50370.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 10507 {ECO:0000313|EMBL:EEG50370.1}; 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] {ECO:0000313|EMBL:EEG50370.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 10507 {ECO:0000313|EMBL:EEG50370.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEG50370.1}. 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; ACBZ01000026; EEG50370.1; -; Genomic_DNA. DR RefSeq; WP_005946139.1; NZ_GG657679.1. DR EnsemblBacteria; EEG50370; EEG50370; RUMHYD_00715. DR PATRIC; 38359069; VBIBlaHyd72091_0482. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 207 207 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 273 273 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 274 274 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 288 AA; 30870 MW; B401BB3E98DDED32 CRC64; MKREEFQTQI KFPLLLDGAT GSNLMAAGMP RGVCTEIWVR DHKDVFLRLQ KAYIEAGSQV IYAPTFGGNR ISLSMHGLEN EIEALNKTLV SYSLEAADDK VLVAGDLTTT GKMMAPAGEL SYEQAFEVYQ EQIHYLAEAG VDLLAVETMI SIEETLAALD AALSVCDLPV MCSMTIESDG SLFTGGNIFE AALALESAGA SAVGINCSVG PEQLVAIIRT LYETVSIPVI AKPNAGMPVI DDLGQAVYNM TPQDFALHMK TLVDMGASIV GGCCGTTPEF IRRMTEIL // ID C0D4W7_9FIRM Unreviewed; 836 AA. AC C0D4W7; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEG53646.1}; GN ORFNames=CLOSTASPAR_04313 {ECO:0000313|EMBL:EEG53646.1}; OS [Clostridium asparagiforme] DSM 15981. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=518636 {ECO:0000313|EMBL:EEG53646.1}; RN [1] {ECO:0000313|EMBL:EEG53646.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 15981 {ECO:0000313|EMBL:EEG53646.1}; 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] {ECO:0000313|EMBL:EEG53646.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 15981 {ECO:0000313|EMBL:EEG53646.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEG53646.1}. 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; ACCJ01000351; EEG53646.1; -; Genomic_DNA. DR RefSeq; WP_007714689.1; NZ_GG657592.1. DR EnsemblBacteria; EEG53646; EEG53646; CLOSTASPAR_04313. DR PATRIC; 25242288; VBICloAsp20370_3000. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEG53646.1}; KW Transferase {ECO:0000313|EMBL:EEG53646.1}. SQ SEQUENCE 836 AA; 89626 MW; BD10EE6E2F9FAF33 CRC64; MDLLREMRQR RLFFDGGTGS LLQAQGLKAG ELPEVWSITR PEVCVKLHRD YLEAGADIIK TNTFGANGLK FKGRENASGA QGPEAGLPAA DRPADSYSVD EIVTAAMKNA RRAVAEAGHG YIALDLGPTG KLLKPLGDLD FEAAVELYKE VVRIGRREGA DLVLIETMSD SYELKAAVLA AKEAGEGLPV FATVVFDGKG KLLTGGNVES TVALLEGLRV DALGINCGLG PVQMKGIVEE LLKVSSLPVI VNPNAGLPRS ENGVTLYDID GDRFAQVMEE IARMGACFLG GCCGTTPEHI QKTVGRCKDV PLVLPQARKR TVISSYSQAV CIEGKTVIIG ERINPTGKSK FKQALRDHNL EYILKEGVTQ QDNGAQVLDV NVGLPEIDEP SVMEEVVKEL QAIIDLPLQI DTSNPRAMER ALRVYNGKAL INSVNGKAEV MDEIFPLVAR YGGAVVALCL DESGIPETAE GRIQVAKKII REAARYGIGT EDLIFDGLCM TVSSDSKGAL TTLETLRRIR DELGCKSVLG VSNISFGLPQ REIINASFFT MAMECGLSAA IVNPNSEAMM RAYYSFNALM DMDPQCGEYI RIYGGQAGSL GKTLPRNPGA GSAGAAGAGP ESAAAFEIAS RLSAAIERGL REEAHRAVGE LLETREPLDV INTEMIPALD RVGKGFEAGT IFLPQLLMSA EAAKAAFEVI KDRMASSGQV QEKKGTIILA TVKGDIHDIG KNIVKVLLEN YSYEVIDLGR DVPPKTIVQT AMERKVRLVG LSALMTTTVP SMEETIRLLR EQLPGTLVMV GGAVLTPEYA RTIGADAYCR DAMASVNYAE EVFAGT // ID C0E3A2_9CORY Unreviewed; 1189 AA. AC C0E3A2; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 27-MAY-2015, entry version 35. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEG27036.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEG27036.1}; GN Name=metH {ECO:0000313|EMBL:EEG27036.1}; GN ORFNames=CORMATOL_01465 {ECO:0000313|EMBL:EEG27036.1}; OS Corynebacterium matruchotii ATCC 33806. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=566549 {ECO:0000313|EMBL:EEG27036.1}; RN [1] {ECO:0000313|EMBL:EEG27036.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33806 {ECO:0000313|EMBL:EEG27036.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEG27036.1}. 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; ACEB01000021; EEG27036.1; -; Genomic_DNA. DR RefSeq; WP_005521156.1; NZ_EQ973329.1. DR EnsemblBacteria; EEG27036; EEG27036; CORMATOL_01465. DR PATRIC; 25305453; VBICorMat118582_1329. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEG27036.1}; KW Transferase {ECO:0000313|EMBL:EEG27036.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 233 233 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 745 745 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1189 AA; 129719 MW; DC05F2ABC9169772 CRC64; MSTVLPVKTP DFLDALHSRV LIGDGAMGTQ LQGFDLDVET DFLGLEGCNE ILNDTRPDVV AQIHRAYFTA GADLVETNTF GCNLPNLADY NIADRCQELA YKGTRIARTV ADELGPGRDG MRRFVLGSMG PGTKLPSLGH APYLDLKTYY REAALGMVDG GADGILIETA QDLLQVKAAI HGCQEAFAEV GYRLPIVCHV TVETTGTMLL GSEIGAALTA LEPLGIDMIG LNCATGPDEM SEHLRYLSHN AQIPVSVMPN AGLPILGKNG AEYPLKPAEL AASLKTFIEE YGLAMVGGCC GTTPEHITAV HTMVTGGITP AERATPDSDA VSSLYTSVNL TQDAGVTIIG ERTNANGSKA FREAMLAGDL ETCVDIAKQQ TRDGAHMLDL CVDYVGRDGR GDMAALASLL ATSSTLPIMI DSTEPDVIQT GLEHLGGRCA VNSVNFEDGD GPGSRYQRIM QLVKTHGAAV VALTIDEEGQ ARTAEKKLAI AERLITDITE NWGLDESDII VDTLTFPIST GQEETRRDGI ETINAIRELK ARHPRVHTTL GLSNISFGLN PAARQVLNSV FLNECVAAGL DSAIAHSSKL VPMNRIEDRQ REVALDMIYD RRRDGYDPLQ TFMDLFEGVS AAEAKDARAE ALAALPLFER LSQRIIDGEK TGIETDLDAA MAEKSPIDII NQDLLGGMKT VGELFGSGQM QLPFVLQSAE TMKHAVAYLE NYMEATDDSG NKGTMVIATV KGDVHDIGKN LVDIILSNNG YNVINIGIKQ PIATIISAAR EHNADVVGMS GLLVKSTVVM KENLEEMNAQ NASDIPVILG GAALTRSYVE HDLDNIYAGD VHYARDAFEG LSLMDEIMAR KRGETITEDV TKQRKKAERK ARRERSQKIA AERKAKAKPV QLPERSEVAA DFPVATPPFW GTRIIKGLSV SDYLPMLDER ALFMGQWGLK STRGDGPDYE ALVESEGRPR LRAWIDQLKS RGVLDHAAVV YGYFPAVSVK DTVLILAEPR PDAEVIRELK FPRQQRGKFL CIADYVRSRT LAEETGQVDV LPLQLVTMGD PIARYANELF AMNNYRDYLE VHGIGVQLTE ALAEYWHSRI RAELRLPDGT HVGDSDAHDT RRFFDLDYSG ARYSFGYGSC PNLTDRQAIV DLLHSERIGV TLSEEYQLHP EQSTDAFVLY HPEAKYFNV // ID C0ECI7_9FIRM Unreviewed; 784 AA. AC C0ECI7; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEG30803.1}; GN ORFNames=CLOSTMETH_01558 {ECO:0000313|EMBL:EEG30803.1}; OS [Clostridium] methylpentosum DSM 5476. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminiclostridium. OX NCBI_TaxID=537013 {ECO:0000313|EMBL:EEG30803.1}; RN [1] {ECO:0000313|EMBL:EEG30803.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 5476 {ECO:0000313|EMBL:EEG30803.1}; 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] {ECO:0000313|EMBL:EEG30803.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 5476 {ECO:0000313|EMBL:EEG30803.1}; 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. {ECO:0000313|EMBL:EEG30803.1}. 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; ACEC01000052; EEG30803.1; -; Genomic_DNA. DR RefSeq; WP_006354362.1; NZ_EQ973339.1. DR EnsemblBacteria; EEG30803; EEG30803; CLOSTMETH_01558. DR PATRIC; 30589757; VBICloMet71124_0853. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEG30803.1}; KW Transferase {ECO:0000313|EMBL:EEG30803.1}. SQ SEQUENCE 784 AA; 84481 MW; EB89251E7F59D8D1 CRC64; MDVREYLKDH ILVFDGAMGT MLQNKGMQVG DLPETLNFTH PELVTEIHRE YVEAGSDVVS ANTFQANEFK LHGCGYTVEQ VITQAVKLGK QSGAKFVALD VGPLGQLVEP MGTVKFETAY ELFRQQVVTG ERAGADLIII ETMSDLYETK AALLAAKENT SLPVIVSLTY QGDGRTFTGT DPITGTITLQ SLGADAVGVN CSIGPDDLIP IVEQILTYAQ VPVIMQANAG LPKIEDGKTV YDVHAEEFAE AVSRMMDRGV RIVGGCCGTD PDYIRLLRKK ADGMKPVATN PKRVTAVTSG TRTVVLDRCV TVIGERINPT GKKRLKEALR ENRMDYIVGE AINQANAGAD VLDVNVGLPE IDEPAMIARA VKEVQGVTNL PVQVDSSDPA AIESGVRACN GRPIINSVNG KAENLAAVLP IVKKYGAVVV GLTLDEDGIP ATAEGRFAVA KRIVETAAEY GIPKEDILID CLTLTASAQQ EQVLATLDAI KLVKERLGVK TVLGVSNVSF GLPSRPLLNS VFLAAAFGAG LDAPILNPLS KEMMDAVNTF RVINYQDRDA VRYIDRYANA QPAQQAAVGE ISLKEMIVQG RKEEAPAKVR ELLQTTPALE VIDSHFVPAL DIVGQRYEKG EIFLPQLMQS AETVKASFEV IKASMDAGEK TQSKGRVIVA TVLGDIHDIG KNIAKMLLEN YGYDVIDLGK DVPIETVVQT AKEQDIQLIG LSALMTTTVK NMKDTISAIR GAGLNCKIMV GGAVLNEEYA EFVGADFYVK DGRESVELAQ SIFR // ID C0ELV7_NEIFL Unreviewed; 295 AA. AC C0ELV7; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEG33961.1}; GN ORFNames=NEIFLAOT_00919 {ECO:0000313|EMBL:EEG33961.1}; OS Neisseria flavescens NRL30031/H210. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=546264 {ECO:0000313|EMBL:EEG33961.1}; RN [1] {ECO:0000313|EMBL:EEG33961.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NRL30031/H210 {ECO:0000313|EMBL:EEG33961.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEG33961.1}. 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; ACEN01000024; EEG33961.1; -; Genomic_DNA. DR RefSeq; WP_003679992.1; NZ_ACEN01000024.1. DR EnsemblBacteria; EEG33961; EEG33961; NEIFLAOT_00919. DR PATRIC; 29954312; VBINeiFla114371_0802. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EEG33961.1}; KW Transferase {ECO:0000313|EMBL:EEG33961.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 204 204 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 277 277 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 278 278 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 295 AA; 32206 MW; 398D75FDA8ACCD6A CRC64; MTVTILDGGM GRELHRRGAP FRQPEWSALA LMETPEIVRE THLDFLRAGA QVVTTNSYAL VPFHIGQERF DARAAEWARQ AGRLAREAVE QSGTAAKVAA SLPPLFGSYR PDLFDKQVAP ALARPLISGL MPFADIWLAE TVSSLEEARF WRSSLPDDGK PFWVSFTLED TMPHDVPVLR SGENVHEAAD FAVEIGAAAM LFNCSQPEVM AEALKVAHEA QGRLKLGVYA NAFEPVQGQM NEANDGLDPI RADATPENYL AWARKWADLG AEIIGGCCGI APEHIRALAQ GFKAV // ID C0EVI7_9FIRM Unreviewed; 638 AA. AC C0EVI7; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 27-MAY-2015, entry version 28. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=EUBHAL_01425 {ECO:0000313|EMBL:EEG36842.1}; OS [Eubacterium] hallii DSM 3353. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium. OX NCBI_TaxID=411469 {ECO:0000313|EMBL:EEG36842.1}; RN [1] {ECO:0000313|EMBL:EEG36842.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 3353 {ECO:0000313|EMBL:EEG36842.1}; 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] {ECO:0000313|EMBL:EEG36842.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 3353 {ECO:0000313|EMBL:EEG36842.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEG36842.1}. 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; ACEP01000064; EEG36842.1; -; Genomic_DNA. DR RefSeq; WP_005346646.1; NZ_ACEP01000064.1. DR ProteinModelPortal; C0EVI7; -. DR EnsemblBacteria; EEG36842; EEG36842; EUBHAL_01425. DR PATRIC; 30667696; VBIEubHal63356_1253. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EEG36842.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EEG36842.1}. SQ SEQUENCE 638 AA; 71183 MW; D0B235F4F184D13C CRC64; MRMNIREYLE NHKLLTDGAM GTYFDSIEKE NYICSEEANI TNPALVREIH RSYVKNGAQL LRSNTFLANE GTFLSLTQAK AEAFENITLK QLIIAGYQLA KETAQEVYQE EYPIFAAADI GPILEERDSE EADILQQYYE ICDSFLEAGA DIFVLETFPD TQYVLKMAEY IRKSCPEAFI IGQFSLTPTG YSRTGFHYKT ILQEATQSGL LDGAGLNCGV GAAHMKKFLK SYIEEFGVPE DMVLTSLPNC GYPQIVRGHA VYSDSVPYFG EKLGEISELG VQVLGGCCGT TPEYIGEIYK TVFQAKKTEG AVKIPTKIVW GDVTKRVQKR KEAAVHITQA GEQKEAIKEK QVTNTFRQKL EMGELVCAVE LDPPFDTDDT KLLNGAKALL STKADIITIA DSPLARSRAD ASLMAAKIKM TTGMDVMPHL SCRDKNRIAI RSGLLGSYAS GIRNYLFVTG DPVAREDREF TKSVFDFNSI RLMKFAQSMN QEVFKDDTIF YGGALNQNGA SPENIAGRML KKMEAGCRYF LTQPVYDKEG IERLTFLKER TGAKILIGIM PLVSRRNALF IKNEMPGIHV PDEVVAKYKE GASREEFEEA AIEISKQIIE MGKGIGAGFY FMTPFNRVSL VKSILEYV // ID C0EVI8_9FIRM Unreviewed; 823 AA. AC C0EVI8; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEG36843.1}; GN ORFNames=EUBHAL_01426 {ECO:0000313|EMBL:EEG36843.1}; OS [Eubacterium] hallii DSM 3353. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium. OX NCBI_TaxID=411469 {ECO:0000313|EMBL:EEG36843.1}; RN [1] {ECO:0000313|EMBL:EEG36843.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 3353 {ECO:0000313|EMBL:EEG36843.1}; 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] {ECO:0000313|EMBL:EEG36843.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 3353 {ECO:0000313|EMBL:EEG36843.1}; 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. {ECO:0000313|EMBL:EEG36843.1}. 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; ACEP01000064; EEG36843.1; -; Genomic_DNA. DR RefSeq; WP_005346648.1; NZ_ACEP01000064.1. DR EnsemblBacteria; EEG36843; EEG36843; EUBHAL_01426. DR PATRIC; 30667698; VBIEubHal63356_1254. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEG36843.1}; KW Transferase {ECO:0000313|EMBL:EEG36843.1}. SQ SEQUENCE 823 AA; 88768 MW; E2152748AD3D0F0C CRC64; MKTEELYTMI QQKPVILDGA TGSNLQKVGM KPGVCPEEWI LENEDKLIDL QKSFVEAGTN ILYAPTFSGN RVKLEEYGLA DRAEEINKRL VGLSKRAAGD KALVAGDMTM TGVALEPVGP MKLEALINIY KEQAKYLLEA GVDLFVVETM MSLAETRAAV IAIKEVCNLP VIASLTFQED GRTLYGTDPV TAVVVLQSIG ADIIGVNCST GPGEMIPVIK KMKEYAEVPI LAKPNAGLPV LEDGVTVYPM TPEEFASWGP AFIEAGAGLI GGCCGSTPEH IRMLTEKVSG LTTKAPCNIH PIMLASERKS QEIALDGKFL VIGERINPTG KKKLQEELRA GKLDLVEEMA EQQEEMGAHI LDINMGTNGI DEKEMMLKAI SKVTMVSSLP LCIDTSYVEV MEAALRAYPG RALINSISLE TEKIEKLLPL AKKYGAMFIL LPLSDEGLPK SLAEKKEIIN TILEKAKKLG VSKNQIIVDG LVTTVGANKN AALETLETIR YCKEDLKLCT TMGLSNISFG LPERPYVNGA FASMAIASGL TMAIANPSNQ LLMGISFASD LLRNKEGSDI AYIEQIQRME PLKEAAIAKA AKTAGNGEKQ PNEKNAAVGE ADGNIKKNPV FEAVLKGNKD GIVDVVKKEL SKGTKPGEIL DGLLIPAINE VGVLFDKQKY FLPQLISSAN TMEQAVEYLE PLLKEGGIQE KMPTIIIATV EGDIHDIGKN LVALMLRNYG YDVIDLGKDV PADEIIAAAK EHNASIIVLS ALMTTTMMRM KDTIALKEKE HLDVKVMIGG AVTTQSFADE IGADGYSADA ADAVRLAKKL LAE // ID C0FPZ7_9FIRM Unreviewed; 617 AA. AC C0FPZ7; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEG95340.1}; GN ORFNames=ROSEINA2194_00800 {ECO:0000313|EMBL:EEG95340.1}; OS Roseburia inulinivorans DSM 16841. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Roseburia. OX NCBI_TaxID=622312 {ECO:0000313|EMBL:EEG95340.1}; RN [1] {ECO:0000313|EMBL:EEG95340.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 16841 {ECO:0000313|EMBL:EEG95340.1}; 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] {ECO:0000313|EMBL:EEG95340.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 16841 {ECO:0000313|EMBL:EEG95340.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEG95340.1}. 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; ACFY01000036; EEG95340.1; -; Genomic_DNA. DR RefSeq; WP_007883463.1; NZ_ACFY01000036.1. DR EnsemblBacteria; EEG95340; EEG95340; ROSEINA2194_00800. DR PATRIC; 30047011; VBIRosInu13871_0725. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEG95340.1}; KW Transferase {ECO:0000313|EMBL:EEG95340.1}. SQ SEQUENCE 617 AA; 67768 MW; 05375A8D81253FF4 CRC64; MTKAEFKKLV ENGPVILDGA TGTNLQKAGM PVGVCPEQWI LENPDIMIKL QEDYVAAGTD ILYAPTFTAN RIKLEEYGLA DRLEEMNREL IALSQKAAQG KALVAADMTM TGQQLYPIGD LMFEDLVDVY KEQAEVVADA GADLFVVETM MSLQECRAAV IAIREVCDLP IMVSLTYNPD GRTLYGTDPA TATVVLQSLG ADAIGINCST GPEDMIEPVE KMAEYATIPI LAKPNAGLPE LENGVTVYKT GPEEFASCGK KLVEAGASII GGCCGTTPEH IRALKEAVKD MPVHKPLTQK RRILTSERKL VEITLDGNFM VIGERINPTG KKKLQAELRE GSLNMVRQMA LDQEENGAAI LDVNMGMNGI DEKEMMINTI YEVTSTVDCP LCIDSSHVDI IEAALRIYPG RALINSISME KEKMDKLLPI AEKYGAMFIL LPLSDAGLPN DSEEKHAIIR TVMEQAIKIG MSKEDIIVDG LVATIGANPR AAIECYETFS YCKNELGLPT ACGLSNISFG LPERTYVNTA FLTMAIAHGL TMAIANPSQE LLMNAAFASD LLLAREESDI RYIERMNMLA EKYAGQERVL VPVKKRRRMI RQNLDHRKEE VLFLKLF // ID C0G3W0_9RHIZ Unreviewed; 1261 AA. AC C0G3W0; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 27-MAY-2015, entry version 37. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEH15425.1}; DE EC=1.1.1.133 {ECO:0000313|EMBL:EEH15425.1}; GN Name=metH {ECO:0000313|EMBL:EEH15425.1}; GN ORFNames=BCETI_1000362 {ECO:0000313|EMBL:EEH15425.1}; OS Brucella ceti str. Cudo. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=595497 {ECO:0000313|EMBL:EEH15425.1, ECO:0000313|Proteomes:UP000003678}; RN [1] {ECO:0000313|EMBL:EEH15425.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Cudo {ECO:0000313|EMBL:EEH15425.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEH15425.1}. 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; ACJD01000001; EEH15425.1; -; Genomic_DNA. DR RefSeq; WP_002965438.1; NZ_ACJD01000001.1. DR ProteinModelPortal; C0G3W0; -. DR SMR; C0G3W0; 673-921. DR EnsemblBacteria; EEH15425; EEH15425; BCETI_1000362. DR GeneID; 3786978; -. DR PATRIC; 35209127; VBIBruCet28239_0383. DR Proteomes; UP000003678; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008831; F:dTDP-4-dehydrorhamnose reductase activity; IEA:UniProtKB-EC. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000003678}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Oxidoreductase {ECO:0000313|EMBL:EEH15425.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 263 263 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 326 326 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 327 327 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 783 783 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1261 AA; 138652 MW; B65506A5F8F0B796 CRC64; MASSLDDLFG ATAAKPDGSE VLAALTQAAR ERILILDGAM GTQIQGLGFH EEHFRGDRFA TCDCQLQGNN DLLTLTQPKA IEEIHYAYAM AGADILETNT FSSTSIAQAD YGMEAMVYDL NRDGARLARR AALRAEQKDG RRRFVAGALG PTNRTASLSP DVNNPGFRAV TFDDLRIAYS EQIRGLIDGG SDIILIETIF DTLNAKAAVF ATEEVFAEKG VRLPVMISGT ITDLSGRTLS GQTPTAFWYS LRHARPFTIG LNCALGANAM RAHLDELSGI ADTFICAYPN AGLPNEFGQY DETPEAMAAQ IEGFARDGLV NVVGGCCGST PDHIRAIAQA VAKYEPRKPA KVPPLMRLSG LEPFTLTKDI PFVNIGERTN VTGSARFRKL VKAGDFAAAL DVARDQVANG AQIIDINMDE GLIDSEKAMV EFLNLIAAEP DIARVPIMLD SSKWEVIEAG LKCVQGKAVV NSISLKEGEE AFLHHARLVR AYGAAVVIMA FDETGQADTQ ARKIEICTRA YKILTEQVGF PPEDIIFDPN IFAVATGIEE HNNYGVDFIE ATREIVRTLP HVHISGGVSN LSFSFRGNEP VREAMHAVFL YHAIQAGMDM GIVNAGQLAV YDTIDAELRE ACEDVVLNRP TKTGESATER LLEIAERFRD SGSREARTQD LSWREWPVEK RLEHALVNGI TEYIEADTEE ARLAAERPLH VIEGPLMAGM NVVGDLFGSG KMFLPQVVKS ARVMKQAVAV LLPFMEEEKR LNGGEGRQSA GKVLMATVKG DVHDIGKNIV GVVLACNNYE IIDLGVMVPS QKILQVARDE KVDIIGLSGL ITPSLDEMAH VAAEMEREGF DIPLLIGGAT TSRVHTAVKI HSRYERGQAV YVVDASRAVG VVSNLLSPEG KQAYIDGLRN EYAKVAAAHA RNEAEKQRLP IARARANPHQ LDWENYEPVK PAFTGTKVFE TYDLAEIARY IDWTPFFQTW ELRGRYPAIL EDEKQGEAAR QLWADAQAML RKIIDEKWFT PRAVVGFWPA NAVGDDIRLF TDESRKEELA TLFTLRQQLT KRDGRPNVAM ADFVAPVESG KQDYVGGFVV TAGIGEIAIA ERFERANDDY SAILVKALAD RFAEAFAELM HERVRKEFWA YAPDEAFTPE ELISEPYKGI RPAPGYPAQP DHTEKTTLFR LLDATANTGV ELTESYAMWP GSSVSGLYIG HPESYYFGVA KVERDQVEDY ARRKDMDVEA VERWLTPILN YVPGASKDEA A // ID C0MKB3_DROME Unreviewed; 331 AA. AC C0MKB3; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 29-OCT-2014, entry version 18. DE SubName: Full=CG10623-PA {ECO:0000313|EMBL:CAR93711.1}; GN Name=CG10623 {ECO:0000313|EMBL:CAR93711.1}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000313|EMBL:CAR93711.1}; RN [1] {ECO:0000313|EMBL:CAR93711.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MEL02 {ECO:0000313|EMBL:CAR93711.1}; RX PubMed=19126864; DOI=10.1093/molbev/msn297; RA Parsch J., Zhang Z., Baines J.F.; RT "The influence of demography and weak selection on the McDonald- RT Kreitman test: an empirical study in Drosophila."; RL Mol. Biol. Evol. 26:691-698(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; FM245785; CAR93711.1; -; Genomic_DNA. DR Bgee; C0MKB3; -. DR ExpressionAtlas; C0MKB3; differential. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 331 AA; 36716 MW; CAE7E21C9E531DFD CRC64; MEVNQKWNWD TKPILVKCGG FSSQLAKNVT EKVDGDPLWG SRFDATNPEA VIQTHLDFLR NGADIILTNT YQSSVEGFVK YLGVTRERGV ELIQKSVQLA KQAKEQYLSE IGSEAESALP LIMGSIGPYG AYLHDGSEYT GNYADKMSKE ELRAWHKTRI EICLAAGVDG LALETLPCLM EAEAVTELVL DNFPDAKFWV SLQCMDEKHM ASGENFAEAA LSLWRLVQSR KAENRLLGIG LNCVNPLFVT PLLSSLTKVA GSDRIPLVVY SNRGEIYDVE QGDWTGTGEE VVKFVPEWIQ LGVRIVGGCC RVYPTDVFAI RKYVDGLNIK P // ID C0MKB4_DROME Unreviewed; 331 AA. AC C0MKB4; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 29-OCT-2014, entry version 18. DE SubName: Full=CG10623-PA {ECO:0000313|EMBL:CAR93712.1}; GN Name=CG10623 {ECO:0000313|EMBL:CAR93712.1}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000313|EMBL:CAR93712.1}; RN [1] {ECO:0000313|EMBL:CAR93712.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MEL11 {ECO:0000313|EMBL:CAR93712.1}, and RC MEL16 {ECO:0000313|EMBL:CAR93716.1}; RX PubMed=19126864; DOI=10.1093/molbev/msn297; RA Parsch J., Zhang Z., Baines J.F.; RT "The influence of demography and weak selection on the McDonald- RT Kreitman test: an empirical study in Drosophila."; RL Mol. Biol. Evol. 26:691-698(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; FM245786; CAR93712.1; -; Genomic_DNA. DR EMBL; FM245790; CAR93716.1; -; Genomic_DNA. DR Bgee; C0MKB4; -. DR ExpressionAtlas; C0MKB4; differential. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 331 AA; 36695 MW; 30EB54AE79E25590 CRC64; MEVNQKWNWD TKPILVKCGG FSSQLAKNVT EKVDGDPLWG SRFDATNPEA VIQTHLDFLR NGADIILTNT YQSSVEGFVK YLGVTRERGV ELIQKSVQLA KQAKEQYLSE IGSEAESALP LIMGSIGPYG AYLHDGSEYT GNYADKMSKE ELRAWHKTRI EICLAAGVDG LALETLPCLM EAEAVTELVL DKFPDAKFWV SLQCMDEKHM ASGENFAEAA LSLWRLVQSR KAENRLLGIG LNCVNPLFVT PLLSSLTKVA GSDRIPLVVY SNRGEIYNVE QGDWTGTGEE VVKFVPEWIQ LGVRIVGGCC RVYPTDVLAI RKYVDGLNIK P // ID C0MKB5_DROME Unreviewed; 331 AA. AC C0MKB5; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 29-OCT-2014, entry version 18. DE SubName: Full=CG10623-PA {ECO:0000313|EMBL:CAR93713.1}; GN Name=CG10623 {ECO:0000313|EMBL:CAR93713.1}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000313|EMBL:CAR93713.1}; RN [1] {ECO:0000313|EMBL:CAR93713.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MEL12 {ECO:0000313|EMBL:CAR93713.1}; RX PubMed=19126864; DOI=10.1093/molbev/msn297; RA Parsch J., Zhang Z., Baines J.F.; RT "The influence of demography and weak selection on the McDonald- RT Kreitman test: an empirical study in Drosophila."; RL Mol. Biol. Evol. 26:691-698(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; FM245787; CAR93713.1; -; Genomic_DNA. DR Bgee; C0MKB5; -. DR ExpressionAtlas; C0MKB5; differential. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 331 AA; 36668 MW; 3107F9A685FA05E6 CRC64; MEVNQKWNWD TKPILVKCGG FSSQLAKNVT EKVDGDPLWG SRFDATNPEA VIQTHLDFLR NGADIILTNT YQSSVEGFVK YLGVTRERGV ELIQKSVQLA KQAKEQYLSE IGSEAESALP LIMGSIGPYG AYLHDGSEYT GNYADKMSKE ELRAWHKTRI EICLAAGVDG LALETLPCLM EAEAVTELVL DNFPDAKFWV SLQCMDEKHM ASGENFAEAA LSLWRLVQSR KAENRLLGIG VNCVNPLFVT PLLSSLTKVA GSDRIPLVVY SNRGEIYDVE QGDWTGTGEE VVKFVPEWIQ LGVRIVGGCC RVYPTDVLAI RKYVDGLNIK P // ID C0MKB6_DROME Unreviewed; 331 AA. AC C0MKB6; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 29-OCT-2014, entry version 18. DE SubName: Full=CG10623-PA {ECO:0000313|EMBL:CAR93714.1}; GN Name=CG10623 {ECO:0000313|EMBL:CAR93714.1}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000313|EMBL:CAR93714.1}; RN [1] {ECO:0000313|EMBL:CAR93714.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MEL13 {ECO:0000313|EMBL:CAR93714.1}; RX PubMed=19126864; DOI=10.1093/molbev/msn297; RA Parsch J., Zhang Z., Baines J.F.; RT "The influence of demography and weak selection on the McDonald- RT Kreitman test: an empirical study in Drosophila."; RL Mol. Biol. Evol. 26:691-698(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; FM245788; CAR93714.1; -; Genomic_DNA. DR Bgee; C0MKB6; -. DR ExpressionAtlas; C0MKB6; differential. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 331 AA; 36686 MW; 310622D4624E54E6 CRC64; MEVNQKWNWD TKPILVKCGG FSSQLAKNVT EKVDGDPLWG SRFDATNPEA VIQTHLDFLR NGADIILTNT YQSSVEGFVK YLGVTRERGV ELIQKSVQLA KQAKEQYLSE IGSEAESALP LIMGSIGPYG AYLHDGSEYT GNYADKMSKE ELRAWHKTRI EICLAAGVDG LALETLPCLM EAEAVTELVL DKFPDAKFWV SLQCMDEKHM ASGENFAEAA LSLWRLVQSR KAENRLLGIG VNCVNPLFVT PLLSSLTKVA GSDRIPLVVY SNRGEIYDVE QGDWTGTGEE VVKFVPEWIQ LGVRIVGGCC RVYTTDVLAI RKYVDGLNIK P // ID C0MKC0_DROME Unreviewed; 331 AA. AC C0MKC0; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 29-OCT-2014, entry version 18. DE SubName: Full=CG10623-PA {ECO:0000313|EMBL:CAR93718.1}; GN Name=CG10623 {ECO:0000313|EMBL:CAR93718.1}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000313|EMBL:CAR93718.1}; RN [1] {ECO:0000313|EMBL:CAR93718.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MEL18 {ECO:0000313|EMBL:CAR93718.1}; RX PubMed=19126864; DOI=10.1093/molbev/msn297; RA Parsch J., Zhang Z., Baines J.F.; RT "The influence of demography and weak selection on the McDonald- RT Kreitman test: an empirical study in Drosophila."; RL Mol. Biol. Evol. 26:691-698(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; FM245792; CAR93718.1; -; Genomic_DNA. DR Bgee; C0MKC0; -. DR ExpressionAtlas; C0MKC0; differential. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 331 AA; 36642 MW; 30EB41BB79E25590 CRC64; MEVNQKWNWD TKPILVKCGG FSSQLAKNVT EKVDGDPLWG SRFDATNPEA VIQTHLDFLR NGADIILTNT YQSSVEGFVK YLGVTRERGV ELIQKSVQLA KQAKEQYLSE IGSEAESALP LIMGSIGPYG AYLHDGSEYT GNYADKMSKE ELRAWHKTRI EICLAAGVDG LALETLPCLM EAEAVTELVL DKFPDAKFWV SLQCMDEKHM ASGENFAEAA LSLWRLVQSR KAENRLLGIG LNCVNPLFVT PLLSSLTKVA GSDRIPLVVY SNRGEIYNVE QGDWTGTGEE VVKFVPEWIQ LGVRIVGGCC RVYPTDVLAI CKYVDGLNIK P // ID C0N6S9_9GAMM Unreviewed; 1232 AA. AC C0N6S9; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 27-MAY-2015, entry version 38. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEF79560.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEF79560.1}; GN Name=metH {ECO:0000313|EMBL:EEF79560.1}; GN ORFNames=MDMS009_2147 {ECO:0000313|EMBL:EEF79560.1}; OS Methylophaga thiooxydans DMS010. OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Piscirickettsiaceae; Methylophaga. OX NCBI_TaxID=637616 {ECO:0000313|EMBL:EEF79560.1}; RN [1] {ECO:0000313|EMBL:EEF79560.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DMS010 {ECO:0000313|EMBL:EEF79560.1}; 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] {ECO:0000313|EMBL:EEF79560.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DMS010 {ECO:0000313|EMBL:EEF79560.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG657899; EEF79560.1; -; Genomic_DNA. DR RefSeq; WP_008291651.1; NZ_GG657899.1. DR EnsemblBacteria; EEF79560; EEF79560; MDMS009_2147. DR PATRIC; 26227538; VBIMetThi34374_1963. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEF79560.1}; KW Transferase {ECO:0000313|EMBL:EEF79560.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 246 246 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1232 AA; 137027 MW; 05363D4CC51EDC62 CRC64; MTAFHQLRTQ LEQRILILDG GMGTLIQSYQ LEEKDFRGER FAEHPCDVKG NNDLLSLTQP QIIRDIHRAY FEAGADIVET NTFNGTSIAM ADYQMEDLVY ELNKVSAELA KEVADEFTAK NPEKPRFVTG VLGPTNRTAS ISPDVNNPGF RNTNFDELVV AYTEAIRGLV DGGADLLLVE TVFDTLNAKA ALFAIDKFCE DHDIHLPVMI SGTITDASGR TLSGQTAEAF WNSLSHIQPI SIGLNCALGA EQLRQYVEEL SNVVTTYVSA HPNAGLPNEF GEYDESPEVM AAQIKEWAEA GFLNIVGGCC GTAPAHIKAI AEAVEGITPR KPKENLHHCR LSGLEPLNIT EDSLFVNVGE RTNVTGSLRF ARLIKEGDYD TALEVARQQV ENGAQIIDIN MDEGMLDSKE AMVTFLNLLA AEPDISRVPV MIDSSKWEVI EAGLKCIQGK GIVNSISLKE GEENFIEQAK LVRRYGAAVI VMAFDETGQA DTRERKREIC TRSYEVLTEK VHFPPEDIIF DPNIFAVATG IEEHNNYAVD FIEATHDIKQ SLPHAMISGG VSNVSFSFRG NNVVREAIHA VFLYHAIKAG MDMGIVNAGQ LAIYDDLPDE LREVVEDVIL NRRDDSTDRL LELAEKYKGE GGTAAKQEDL SWRELPVSKR LEHALVKGIA DYVEDDTEEA RQQFPKPLEV IEGPLMDGMN VVGDLFGEGK MFLPQVVKSA RVMKKAVAYL MPYIEAAKEE GDTSKNNGKI LMATVKGDVH DIGKNIVGVV LQCNNFEVID LGVMVPAQKI LDVAREENVD IIGLSGLITP SLDEMVHVAK EMERLGFETP MMIGGATTSL IHTAVKIEPN YHGCSIYVKD ASRAVGVAQK LVSKEASVPF IAELKKDYEE KRARHKGRKS TRRQLPIAEA RANKTKIDWQ AYQPTKPAKL GLEVFDDYPL DELVERIDWT PFFQSWELAG KFPRILKDEI VGEHATHLFE DAKKMLKQIV DEKWLKARAV IGLFAANSIN DDDIEVYTDD SRNEVLMTLH SLRQQTERPP GRPNAALADF IAPKDSGVDD YIGAFAVTAG IGIDEHVERF DEDHDDYHSI MLKALADRLA EAFAERMHER VRKEFWGYVQ DEQLDNDALI DEKYQGIRPA PGYPACPDHT EKGLLWDLID PINNAGMTIT ESYAMLPTAA VSGFYFAHPE SRYFGLGKID QDQVEDYAQR KGWDKPTAER WLGPALSYDG DI // ID C0PRQ1_PICSI Unreviewed; 348 AA. AC C0PRQ1; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 01-OCT-2014, entry version 15. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:ACN40491.1}; OS Picea sitchensis (Sitka spruce) (Pinus sitchensis). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Pinidae; Pinales; Pinaceae; Picea. OX NCBI_TaxID=3332 {ECO:0000313|EMBL:ACN40491.1}; RN [1] {ECO:0000313|EMBL:ACN40491.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Green portion of the leader tissue RC {ECO:0000313|EMBL:ACN40491.1}; RA Reid K.E., Liao N., Ralph S., Kolosova N., Oddy C., Moore R., Mayo M., RA Wagner S., King J., Yanchuk A., Holt R., Jones S., Marra M., RA Ritland C.E., Ritland K., Bohlmann J.; RT "Full length sequence-verified cDNA sequences from Sitka spruce (Picea RT sitchensis)."; 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; BT071006; ACN40491.1; -; mRNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; SQ SEQUENCE 348 AA; 37720 MW; DD12E4C6CA7C5459 CRC64; MKFGSGERMK VLEEFLQQVG GFGVIDGGLA TQLESHGADL NDPLWSGRCL IESPHLIQKV HQEYLEAGAE IIITASYQAT IQGFESRGLS ITEGEALLRR SVEIACEARD QFWKKCAESL NGSVDDAQIP KVRPILVAAS VGSYGAYLAD GSEYSGDYGP GMTVHTLKDF HRGRVQVLAD SGADLLAFET IPNKLEAQAY IELLEENDIQ IPAWFSFNSK DGVNVVSGDS FTECAALADS CTNVVAVGIN CTPPRFIHGL ILSIQKVTAK PILVYPNSGE TYDADRKQWV ASTGVSDVDF VSYVQKWQEI GASLIGGCCR TTPNTIKAIS RAMNRTPQIL PPQLLDGQ // ID C0Q492_SALPC Unreviewed; 1227 AA. AC C0Q492; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 27-MAY-2015, entry version 52. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:ACN48311.1}; GN Name=metH {ECO:0000313|EMBL:ACN48311.1}; GN OrderedLocusNames=SPC_4248 {ECO:0000313|EMBL:ACN48311.1}; OS Salmonella paratyphi C (strain RKS4594). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=476213 {ECO:0000313|EMBL:ACN48311.1, ECO:0000313|Proteomes:UP000001599}; RN [1] {ECO:0000313|EMBL:ACN48311.1, ECO:0000313|Proteomes:UP000001599} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RKS4594 {ECO:0000313|EMBL:ACN48311.1, RC ECO:0000313|Proteomes:UP000001599}; 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., RA Peng Y.-H., Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R., RA 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000857; ACN48311.1; -; Genomic_DNA. DR RefSeq; WP_000095981.1; NC_012125.1. DR RefSeq; YP_002639752.1; NC_012125.1. DR STRING; 476213.SPC_4248; -. DR EnsemblBacteria; ACN48311; ACN48311; SPC_4248. DR PATRIC; 32367512; VBISalEnt12305_4309. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SENT476213:GH8J-4337-MONOMER; -. DR Proteomes; UP000001599; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001599}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136089 MW; 51EA1847A85B2F8D CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLHEEDFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYRMESLS AEINYAAAKL ARACADEWTV RTPNKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKEEF EALGVDLPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPEHIAA MSRAVAGLPP RQLPDIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VESGAQIIDI NMDEGMLDAE AAMVRFLSLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVEAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRERKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDEAANAQ QAEWRSWDVK KRLEYSLVKG ITEFIEQDTE EARQQAARPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EKGSSNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAREVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPV LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHARKKPR TPPVTLEAAR DNDLAFDWER YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KLLNPRGVVG LFPANRIGDD IEIYRDETRT HVLTVSHHLR QQTEKVGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA IADRLAEAFA EYLHERVRKV YWGYAPNESL SNDELIRENY QGIRPAPGYP ACPEHTEKGT IWQLLDVEKH TGMKLTESFA MWPGASVSGW YFSHPESKYF AVAQIQRDQV TDYAFRKGMS VEDVERWLAP NLGYDAD // ID C0QE23_DESAH Unreviewed; 303 AA. AC C0QE23; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 27-MAY-2015, entry version 33. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACN17444.1}; GN OrderedLocusNames=HRM2_43880 {ECO:0000313|EMBL:ACN17444.1}; OS Desulfobacterium autotrophicum (strain ATCC 43914 / DSM 3382 / HRM2). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales; OC Desulfobacteraceae; Desulfobacterium. OX NCBI_TaxID=177437 {ECO:0000313|EMBL:ACN17444.1, ECO:0000313|Proteomes:UP000000442}; RN [1] {ECO:0000313|EMBL:ACN17444.1, ECO:0000313|Proteomes:UP000000442} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43914 / DSM 3382 / HRM2 RC {ECO:0000313|Proteomes:UP000000442}; 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., Puehler A., Klenk H.P., Richter M., RA Schuler M., Gloeckner 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; ACN17444.1; -; Genomic_DNA. DR RefSeq; WP_015906172.1; NC_012108.1. DR RefSeq; YP_002605608.1; NC_012108.1. DR STRING; 177437.HRM2_43880; -. DR EnsemblBacteria; ACN17444; ACN17444; HRM2_43880. DR KEGG; dat:HRM2_43880; -. DR PATRIC; 21688633; VBIDesAut25181_4543. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; PYVDVWL; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; DAUT177437:GHLR-4385-MONOMER; -. DR Proteomes; UP000000442; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000442}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ACN17444.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000442}; KW Transferase {ECO:0000313|EMBL:ACN17444.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 210 210 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 287 287 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 303 AA; 33005 MW; 2F7B0CEBA099D430 CRC64; MGTRKITILD GGMGRELKKW GAPFKQPEWS ALAMMVAPEI VKEVHKAFIA SGASVITTNS YALVPFHIGE KRFKDQGKAL ATCAGKMARS AVTETQTGVR VAGSIPPLFG SYRADLYRSE RVVEIASPLI EGLSPYVDLW LCETQSLIDE PIRIKSLIDR LDIQQKPFWV SFTLEDSQLN NEPLLRSGES VVDAVKAMVN AKVDAILFNC CQPEVINQSV KVTQHQLASI GAKNIEIGAY ANAFPPQPKD ATANKGLNEL RADLTPSAYL DWARQWIQDG ATLIGGCCGI GPEHIAVLAE NLV // ID C0QE32_DESAH Unreviewed; 294 AA. AC C0QE32; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 27-MAY-2015, entry version 34. DE SubName: Full=Methionine synthase I, cobalamin-binding domain protein {ECO:0000313|EMBL:ACN17453.1}; GN OrderedLocusNames=HRM2_43970 {ECO:0000313|EMBL:ACN17453.1}; OS Desulfobacterium autotrophicum (strain ATCC 43914 / DSM 3382 / HRM2). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales; OC Desulfobacteraceae; Desulfobacterium. OX NCBI_TaxID=177437 {ECO:0000313|EMBL:ACN17453.1, ECO:0000313|Proteomes:UP000000442}; RN [1] {ECO:0000313|EMBL:ACN17453.1, ECO:0000313|Proteomes:UP000000442} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43914 / DSM 3382 / HRM2 RC {ECO:0000313|Proteomes:UP000000442}; 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., Puehler A., Klenk H.P., Richter M., RA Schuler M., Gloeckner 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; ACN17453.1; -; Genomic_DNA. DR RefSeq; WP_015906181.1; NC_012108.1. DR RefSeq; YP_002605617.1; NC_012108.1. DR STRING; 177437.HRM2_43970; -. DR EnsemblBacteria; ACN17453; ACN17453; HRM2_43970. DR KEGG; dat:HRM2_43970; -. DR PATRIC; 21688651; VBIDesAut25181_4552. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265278; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; DAUT177437:GHLR-4394-MONOMER; -. DR Proteomes; UP000000442; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000442}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000442}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 211 211 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 277 277 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 278 278 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 294 AA; 31304 MW; B87A8DFED8E8E947 CRC64; MNIIETIKTR GLLFDGGMGS MLIARGLQGG DAPERWNLTR PEAIQEVHQA YYKAGADMAT TNTFGASAIK LAKMAVTEGM EEINRAGVKV AKDAKEVWGP GKFIAGDIGE AGDMLAPMGP LSQEDAQACF KEQAEVLAHA GVDIFIIETQ FDLNMALAAI RGIRSVTDIP IACTMTFKQT PKGFFTIMGN PPAESMKTLA GEGAFVVGAN CSMGSDTMVE LAGVIRDAVD TPVMIQPNAG MPQAGPDQTV TYPETADFFA DNIMKMKSLG IEVVGGCCGT TPDYIRTIHD RLNR // ID C0QRY9_PERMH Unreviewed; 1182 AA. AC C0QRY9; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 27-MAY-2015, entry version 50. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACO03041.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ACO03041.1}; GN Name=metH {ECO:0000313|EMBL:ACO03041.1}; GN OrderedLocusNames=PERMA_1670 {ECO:0000313|EMBL:ACO03041.1}; OS Persephonella marina (strain DSM 14350 / EX-H1). OC Bacteria; Aquificae; Aquificales; Hydrogenothermaceae; Persephonella. OX NCBI_TaxID=123214 {ECO:0000313|EMBL:ACO03041.1, ECO:0000313|Proteomes:UP000001366}; RN [1] {ECO:0000313|EMBL:ACO03041.1, ECO:0000313|Proteomes:UP000001366} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14350 / EX-H1 {ECO:0000313|Proteomes:UP000001366}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001230; ACO03041.1; -; Genomic_DNA. DR RefSeq; WP_012675280.1; NC_012440.1. DR RefSeq; YP_002731435.1; NC_012440.1. DR STRING; 123214.PERMA_1670; -. DR EnsemblBacteria; ACO03041; ACO03041; PERMA_1670. DR KEGG; pmx:PERMA_1670; -. DR PATRIC; 22916789; VBIPerMar119911_1681. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PMAR123214:GIZP-1668-MONOMER; -. DR Proteomes; UP000001366; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 2. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001366}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACO03041.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001366}; KW Transferase {ECO:0000313|EMBL:ACO03041.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 728 728 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1182 AA; 132880 MW; 6BCDE59D7ACFE722 CRC64; MKSIRDLIGK KVLVIDGAMG TMIQSMIIPM EAWEGKTGCN EILNVTAPDV IRSIHEKYAL AGADLIKTNT FGALPWVLEE YGISDRAYEL SKAGAELVRQ VCDKYSTPEK PRFVAGSLGP GTKLPSLGHI DYDEMYEGYR ISAKGLIDGG VDIFLLETFQ DPLQIKAALH AVQDTAEEYG KDIPVMVSAT IELTGTMLIG TDVQTLAVIM EPFDILTLGF NCGTGPDQIE SHLKKLSQVW DGYISIHSNA GLPENRGGHT YYPMGAEEFA DKESRFLDFD GVAVVGGCCG TTPAHIKALA EKVKDKKPKP PKGNQPRALA SLYGIQPLKQ EPPPFLVGER TNATGSKKFR ELLLSEDYDG ILSVAQDQVK AGAHALDVSV NFAGRDEIKD MKAVISRFNE KIPIPLMPDS TQPSALETAL KCIGGRPILN SANLEDGEER FNRICQLAKR YGAALVLLTI DEKGMAKTKE RKVEIAERMY RIATEKHGIN PGDLVFDVLT FTVGSGDEEY RDAAVHTIEA IKEIKEKHPE VGFVLGISNV SFGLDKTARK YLNSVFLHHC VEAGLTMAII NPKHLIPYYR ISEEDRKICE NLLFNIWEDG EDPLFRFIQH FSKTERKDTG EDQDDFSDLP VEERIKKLLI DGEKEKLIKT VEEARHSIPP EKIINEVLID AMKVVGDLFG EGKMQLPFVL QSAEAMKAAV DYLNQYLPKK KKEKETTLIL GTVKGDVHDV GKNLVDIILT NNGFKVVNIG IKAELEDFIK AYKEHNADAI GMSGLLVKST LEMKNNLEEM RKRGINVPVL LGGAALNKSF VDQYCRPVYD GPVFYCRDAF DGIEAMSRIE RWDGISPLDT DLGHKGEEEV KPEIKEEVEI PPLSQIKMPD RSVPVPVPPF WGRKVWVYPD MEDKNFYRYI QELAFRWINK GSLFKRAWGY TRGGKSKEEY ERIKKEEVIP AFERLKELLI NEDIFQPKII YGYWPCRSDL PLEEGENREC SLLIFPETEG WFKDNDANRD PLKDVIGTAQ IVMNFPRSKK PPYRCVADYF HSNRHDLVAF TVVSAGNRLS EYENELFRSG KYKEYHLVHG LGVELAEALA EIVHKKIRIE LNIAENEGKT LDDVNYQMRR YQGARYSPGY PACPDLSLNE KIFQLLKPEE LGITLTENYL IVPEQSTDAI VVYHPEATYF SV // ID C0QY88_BRAHW Unreviewed; 873 AA. AC C0QY88; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 29-APR-2015, entry version 47. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:ACN82960.1}; GN Name=metH {ECO:0000313|EMBL:ACN82960.1}; GN OrderedLocusNames=BHWA1_00464 {ECO:0000313|EMBL:ACN82960.1}; OS Brachyspira hyodysenteriae (strain ATCC 49526 / WA1). OC Bacteria; Spirochaetes; Spirochaetales; Brachyspiraceae; Brachyspira. OX NCBI_TaxID=565034 {ECO:0000313|EMBL:ACN82960.1, ECO:0000313|Proteomes:UP000001803}; RN [1] {ECO:0000313|EMBL:ACN82960.1, ECO:0000313|Proteomes:UP000001803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49526 / WA1 {ECO:0000313|Proteomes:UP000001803}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001357; ACN82960.1; -; Genomic_DNA. DR RefSeq; WP_012670012.1; NC_012225.1. DR RefSeq; YP_002720633.1; NC_012225.1. DR STRING; 565034.BHWA1_00464; -. DR EnsemblBacteria; ACN82960; ACN82960; BHWA1_00464. DR KEGG; bhy:BHWA1_00464; -. DR PATRIC; 21179015; VBIBraHyo62857_0454. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; BHYO565034:GJI7-463-MONOMER; -. DR Proteomes; UP000001803; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001803}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACN82960.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001803}; KW Transferase {ECO:0000313|EMBL:ACN82960.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 237 237 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 750 750 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 873 AA; 96434 MW; 5A971AEAFD4ABD69 CRC64; MNNTKEKLKD LIKKQYLIID GATGTELQKK EIKKESWIIN GNNIEGCNEI LNITAPNIMK EIHIDYLNAN ANITKTNSFG AIPWVLSEYD IADKTYELAK SAALIANEAR EEYLKNPNSK GDLNRDIFIA GSLGPGVKLP SLGQISFDEM YNGYTEAVRG LIDGGVDIIL LETAQDVLQL KSAILAVNDT AKKLNKEIPI MVSVTIEKEG TMLLGTDIET AYTILSNLDI FSIGMNCGTG PDMAMRHIKK LSEISYLPIS IHSNAGLPEN RGGKAYYSMT PEEFADINSK FFELDGLAFI GGCCGTTPLH INALANKVKG IKPKKTALEK PRPYIASLFN VVSIKQNPSP LMIGERSNAT GSKIFRELMI AGDMDGMLDI GIKQVKAGSH AIDVNAAWAG RDEVEDITKI ISAYVKQISL PLVIDAIKPN VIEAALKVYG GKPIINSANM EQGEEKFDAI CSLAKRYGAS IMLLTIDEKS MALTCEDKLR MAERMYDRAV NIHKILPHDI IFDPLTFTLA SGDENSFMAG VETLNAIKEL SNKYPEASIS LGVSNISFGL KEEARKIMNS VFLYEAINNG LTTAIVNVAQ ILPLSKIDEK EIELARELIY NKSNSKEPLI NYINHFSDKK EKKELNNEEN IKKPIREAIR DAMLDGEWKD MQNLLNEVKE DSEEFGGEKK FAQAIIDEIL LPTMADIGVK FGEGTIQLPF VLGSAEVMKK SVDFLSEFLE KKKQEKTAKI ILGTVAGDVH DVGKNLVEII IKNNGFETVN IGTKVPIEKF LEAYHEHNAD CIGMSGLLVK STEVMKDNLA YIREKGLKIP IILGGAALTK EFVENDCKKV YGDTAKIFYC KDGFDDILAI KEIIADRDKE NNN // ID C0RGP1_BRUMB Unreviewed; 1261 AA. AC C0RGP1; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 27-MAY-2015, entry version 50. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACN99998.1}; DE EC=1.1.1.133 {ECO:0000313|EMBL:ACN99998.1}; GN Name=metH {ECO:0000313|EMBL:ACN99998.1}; GN OrderedLocusNames=BMEA_A0196 {ECO:0000313|EMBL:ACN99998.1}; OS Brucella melitensis biotype 2 (strain ATCC 23457). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=546272 {ECO:0000313|EMBL:ACN99998.1, ECO:0000313|Proteomes:UP000001748}; RN [1] {ECO:0000313|Proteomes:UP000001748} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23457 {ECO:0000313|Proteomes:UP000001748}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001488; ACN99998.1; -; Genomic_DNA. DR RefSeq; WP_004686643.1; NC_012441.1. DR RefSeq; YP_002731953.1; NC_012441.1. DR STRING; 546272.BMEA_A0196; -. DR EnsemblBacteria; ACN99998; ACN99998; BMEA_A0196. DR KEGG; bmi:BMEA_A0196; -. DR PATRIC; 17836086; VBIBruMel14466_0207. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; BMEL546272:GJOX-187-MONOMER; -. DR PRO; PR:C0RGP1; -. DR Proteomes; UP000001748; Chromosome I. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008831; F:dTDP-4-dehydrorhamnose reductase activity; IEA:UniProtKB-EC. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001748}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Oxidoreductase {ECO:0000313|EMBL:ACN99998.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 263 263 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 326 326 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 327 327 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 783 783 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1261 AA; 138728 MW; BF7DDF052C8F6A2C CRC64; MASSLDDLFG ATAAKPDGSE VLAALTQAAR ERILILDGAM GTQIQGLGFH EEHFRGDRFA TCDCQLQGNN DLLTLTQPKA IEEIHYAYAM AGADILETNT FSSTSIAQAD YGMEAMVYDL NRDGARLARR AALRAEQKDG RRRFVAGALG PTNRTASLSP DVNNPGFRAV TFDDLRIAYS EQIRGLIDGG SDIILIETIF DTLNAKAAVF ATEEVFAEKG VRLPVMISGT ITDLSGRTLS GQTPTAFWYS LRHARPFTIG LNCALGANAM RAHLDELSGI ADTFICAYPN AGLPNEFGQY DETPEAMAAQ IEGFARDGLV NVVGGCCGST PDHIRAIAQA VAKYEPRKPA KVPPLMRLSG LEPFTLTKDI PFVNIGERTN VTGSARFRKL VKAGDFAAAL DVARDQVANG AQIIDINMDE GLIDSEKAMV EFLNLIAAEP DIARVPIMLD SSKWEVIEAG LKCVQGKAVV NSISLKEGEE AFLHHARLVR AYGAAVVIMA FDETGQADTQ ARKIEICTRA YKILTEQVGF PPEDIIFDPN IFAVATGIEE HNNYGVDFIE ATREIVRTLP HVHISGGVSN LSFSFRGNEP VREAMHAVFL YHAIQAGMDM GIVNAGQLAV YDTIDAELRE ACEDVVLNRP TKTGESATER LLEIAERFRD SSSREARTQD LSWREWPVEK RLEHALVNGI TEYIEADTEE ARLAAERPLH VIEGPLMAGM NVVGDLFGSG KMFLPQVVKS ARVMKQAVAV LLPFMEEEKR LNGGEGRQSA GKVLMATVKG DVHDIGKNIV GVVLACNNYE IIDLGVMVPS QKILQVARDE KVDIIGLSGL ITPSLDEMAH VAAEMEREGF DIPLLIGGAT TSRVHTAVKI HSRYERGQAV YVVDASRAVG VVSNLLSPEG KQAYIDGLRN EYAKVAAAHA RNEAEKQRLP IARARANPHQ LDWENYEPVK PTFTGTKVFE TYDLAEIARY IDWTLFFQTW ELRGRYPAIL EDEKQGEAAR QLWADAQAML RKIIDEKWFT PRAVVGFWPA NAVGDDIRLF TDESRKEELA TLFTLRQQLT KRDGRPNVAM ADFVAPVESG KQDYVGGFVV TAGIGEIAIA ERFERANDDY SAILVKALAD RFAEAFAELM HERVRKEFWA YAPDEAFTPE ELISEPYKGI RPAPGYPAQP DHTEKTTLFR LLDATANTGV ELTESYAMWP GSSVSGLYIG HPESYYFGVA KVERDQVEDY ARRKDMDVEA VERWLTPILN YVPGASKDEA A // ID C0VIC7_9GAMM Unreviewed; 1228 AA. AC C0VIC7; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 27-MAY-2015, entry version 35. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEH69567.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEH69567.1}; GN Name=metH {ECO:0000313|EMBL:EEH69567.1}; GN ORFNames=HMPREF0023_0896 {ECO:0000313|EMBL:EEH69567.1}; OS Acinetobacter sp. ATCC 27244. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=525244 {ECO:0000313|EMBL:EEH69567.1}; RN [1] {ECO:0000313|EMBL:EEH69567.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27244 {ECO:0000313|EMBL:EEH69567.1}; 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 (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEH69567.1}. 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; ABYN01000056; EEH69567.1; -; Genomic_DNA. DR RefSeq; WP_008941728.1; NZ_GG665954.1. DR EnsemblBacteria; EEH69567; EEH69567; HMPREF0023_0896. DR PATRIC; 24346074; VBIAciSp60119_1367. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEH69567.1}; KW Transferase {ECO:0000313|EMBL:EEH69567.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1228 AA; 135672 MW; F1B4052EDC2A7A07 CRC64; MSTLATLKSL LAQRILIIDG AMGTMIQRHK LEEEDYRGER FADWASDLKG NNDLLVLTQP QIIQGIHEAY LDAGADIIET NSFNGTRVSM SDYHMEDLVP EINREAARLA RAACDKYSTP EKPRFVAGVL GPTSRTCSIS PNVNDPAFRN ITFDELKENY IEATHALIEG GADILLIETV FDTLNCKAAI FAVKEVFKQI GYELPLMISG TITDASGRTL TGQTAEAFWN SVRHGDLLSI GFNCALGADA MRPHVKTIAD VADTFVSAHP NAGLPNAFGE YDETPEQTAA LIKEFAESGL INITGGCCGT TPDHIRAIYQ AVKDIPPRKI PETVHACRLS GLEPFNIYDD SLFVNVGERT NVTGSKKFLR LIREENFAEA LEVAQQQVEA GAQIIDINMD EGMLDSQGAM VHFLNLVASE PDISRVPIMI DSSKWEIIEA GLKCVQGKPV VNSISLKEGY DEFVEKARLC RQYGAAVIVM AFDEVGQADT AERKREICKR SYDILVNEVG YPAEDIIFDP NVFAVATGIE EHNNYAVDFI EATGWITQNL PHAMISGGVS NVSFSFRGNE PVREAIHSVF LYHAIKQGMT MGIVNAGQMA IYDDINKELK DAVEDVVLNQ NQGETGQAAT EKLLEVAEKY RGQAGATKEA ENLEWRNESV EKRLEYALVK GITTYIDQDT EEARLKSKRP LDVIEGPLMD GMNVVGDLFG SGKMFLPQVV KSARVMKQAV AWLNPYIEAE KSEGQSKGKV LMATVKGDVH DIGKNIVGVV LGCNGYDIVD LGVMVPAEKI LQTAIDEKCD IIGLSGLITP SLDEMVFVAK EMQRKGFNIP LLIGGATTSK AHTAVKIDPQ YSNDAVIYVA DASRAVGVAT TLLSPEMRGN FIAEHRAEYA KIRERLANKQ PKAAKLSYAE SVENGFKIDN HYVPPKPNAL GTQVIKNYPL ETLVEYFDWT PFFISWSLAG KFPKILEDEV VGEAATDLYN QAQAMLKDII ENNRFDARAV FGLYPAQRTA ADTVSVFDEA GQKVTHTFEH VRQQSDKVTG KPNLSLADYI KPSEQPEDYL GGFTVSIFGA EELANEYKAK GDDYSAILVQ SLADRFAEAF AEHLHERIRK EFWGYKADET LSNEELIKEK YVGIRPAPGY PACPEHSEKA VLFDWLGSEE KIGTKLTEHF AMMPPSSVSG FYYSHPQSEY FNVGKISQDQ LEDYAKRKGW TLDEAKRWLA PNLDDSIG // ID C0WB71_9FIRM Unreviewed; 803 AA. AC C0WB71; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEH90353.1}; GN ORFNames=ACDG_00712 {ECO:0000313|EMBL:EEH90353.1}; OS Acidaminococcus sp. D21. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; OC Acidaminococcaceae; Acidaminococcus. OX NCBI_TaxID=563191 {ECO:0000313|EMBL:EEH90353.1}; RN [1] {ECO:0000313|EMBL:EEH90353.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=D21 {ECO:0000313|EMBL:EEH90353.1}; 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., 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. {ECO:0000313|EMBL:EEH90353.1}. 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; ACGB01000009; EEH90353.1; -; Genomic_DNA. DR RefSeq; WP_009015182.1; NZ_ACGB01000009.1. DR EnsemblBacteria; EEH90353; EEH90353; ACDG_00712. DR PATRIC; 24311953; VBIAciSp85863_0725. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEH90353.1}; KW Transferase {ECO:0000313|EMBL:EEH90353.1}. SQ SEQUENCE 803 AA; 84973 MW; 6C52B4725D3AC03C CRC64; MEIRERLEKE RLFFDGGMGT MLQSAGLMPG ELPELWNLSH ADVIQGVHEA YIRAGAQIIK TNTFGCNGLK FGKAHGTPAV STLVTAAVKL AQKAFQACGE KGCVALDLGP TGKLLQPYGD LPFEEAVSLY AEAVEAGKKA GADLVLIETM SDTYEAKAAI LAVKEHSNLP FVVTFTFDEE GKLLSGADVE TAMIVASSLG ASAVGFNCGL GPKEISRLVP RALAATDLPL VVNPNAGLPV THDGVTQFEV GSEEFAATML EFAPQTALLG GCCGTTPQHI KALVESCAEL PPPEKRNGAP ECITGYGAPV CFDRMPVIIG ERINPTGKKR LKEALKAGDM DYVCQLALEQ IDKGAQVLDV NVGVPGIDEP ALLEKAMRTL QSITPLPLQI DTSDLKAMER ALRLYNGRPL LNSVNGKTSS LSSVLPLAKK YGAMLVGLCL DDDGIAESLE GRLKSARRVI DGAKKAGLSE KALLLDPLAM TISTGGQNAQ IALSIIAALK KAGLKTVMGV SNISFGLPHR DAVNSAFFAS AMQLGLSAGI INPNSAPMME TYLAYGALSG YDTSCKAYVS YFADLPTEKR EPHVPAAKDS GEQGRYGLDE AIEKGLISPA ETAVAALLDE GRDALSIINE YMIPALNRVG DAFEKKTLFL PQLLMSADAA KAGFEIIKKA MFQKGADRGK GDPVIVATVK GDIHDIGKNI VKVLLENYGY DVIDLGKDVP PEAIVEKTLE RDVKLVGLSA LMTTTLGSMA ETIRQLREKA PGCRVIVGGA VMTKEYAEEL GADAYAGNAV AAVSYANALF RKK // ID C0WBZ5_9FIRM Unreviewed; 320 AA. AC C0WBZ5; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEH90627.1}; GN ORFNames=ACDG_00986 {ECO:0000313|EMBL:EEH90627.1}; OS Acidaminococcus sp. D21. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; OC Acidaminococcaceae; Acidaminococcus. OX NCBI_TaxID=563191 {ECO:0000313|EMBL:EEH90627.1}; RN [1] {ECO:0000313|EMBL:EEH90627.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=D21 {ECO:0000313|EMBL:EEH90627.1}; 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., 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. {ECO:0000313|EMBL:EEH90627.1}. 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; ACGB01000015; EEH90627.1; -; Genomic_DNA. DR RefSeq; WP_009015456.1; NZ_ACGB01000015.1. DR EnsemblBacteria; EEH90627; EEH90627; ACDG_00986. DR PATRIC; 24312569; VBIAciSp85863_1020. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEH90627.1}; KW Transferase {ECO:0000313|EMBL:EEH90627.1}. SQ SEQUENCE 320 AA; 35221 MW; F0F65017E0682BA8 CRC64; MRQTLAKILE KKQICVIDGS MGTALEHLGA NLNNSLWTAR VLLDQPELVK KVHLDYFHAG ADAGITCSYQ ATIPGLMANG LSEKEAEDLI VRSVKVFQEA RNEWWEKEGK AADRAYPMCL AGIGPYGAYL ADGSEYKGHY GIPDAALHDF HQRRAELLWE AGADVLLFET QPSLGEAKIE AAIAERLGAD YWISFSCKDG LHINEGDLIR DCAAAFRSGY PRLRALGVNC TKPEYLESLI KELGKETDLP IVVYPNSGET YDPVTKTWNG KGDGHSFKDY ARTYMEAGAR AVGGCCTTVS EHIVAVAKAR EEFLDRQSKA // ID C0WM67_LACBU Unreviewed; 315 AA. AC C0WM67; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEI20892.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EEI20892.1}; GN Name=mmuM {ECO:0000313|EMBL:EEI20892.1}; GN ORFNames=HMPREF0497_0220 {ECO:0000313|EMBL:EEI20892.1}; OS Lactobacillus buchneri ATCC 11577. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=525318 {ECO:0000313|EMBL:EEI20892.1}; RN [1] {ECO:0000313|EMBL:EEI20892.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 11577 {ECO:0000313|EMBL:EEI20892.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEI20892.1}. 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; ACGH01000012; EEI20892.1; -; Genomic_DNA. DR RefSeq; WP_003556568.1; NZ_GG669710.1. DR EnsemblBacteria; EEI20892; EEI20892; HMPREF0497_0220. DR PATRIC; 30696116; VBILacBuc113131_0851. DR OrthoDB; EOG6C019S; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEI20892.1}; KW Transferase {ECO:0000313|EMBL:EEI20892.1}. SQ SEQUENCE 315 AA; 34848 MW; A87F8C727117DC7E CRC64; MMDLIKENLD SKRALVLDGA MATELEKHGV DTSNDLWSAT ALINDPDAVK AVHTSYFEAG ADITITDTYQ ANVEAFKKVG FTEDQSEKLI TEAVRLALES RDDFYATLPT AERAKRAFYP LVAGSVGPYG AYLADGSEYT GHYQLTNEAY QTFHQRRMRL MDEAGVDVFA FETQPNFEET KALADLLREK FSDRFAWLTF SIKDPEHLCD GTSLAKAVSY FEDNPQISAV GVNCTSMNLI EDSIKTIASN TNKPIIVYPN NGDIYDPKTK TWTPNPNATT FAELTPKWLA AGAKIVGGCC RTTPVDIEQV AESVF // ID C0WX66_LACFE Unreviewed; 310 AA. AC C0WX66; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEI22320.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EEI22320.1}; GN Name=mmuM {ECO:0000313|EMBL:EEI22320.1}; GN ORFNames=HMPREF0511_0717 {ECO:0000313|EMBL:EEI22320.1}; OS Lactobacillus fermentum ATCC 14931. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=525325 {ECO:0000313|EMBL:EEI22320.1}; RN [1] {ECO:0000313|EMBL:EEI22320.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 14931 {ECO:0000313|EMBL:EEI22320.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEI22320.1}. 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; ACGI01000069; EEI22320.1; -; Genomic_DNA. DR RefSeq; WP_003681749.1; NZ_GG669901.1. DR EnsemblBacteria; EEI22320; EEI22320; HMPREF0511_0717. DR GeneID; 6232276; -. DR PATRIC; 30722737; VBILacFer68609_0437. DR OrthoDB; EOG6C019S; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEI22320.1}; KW Transferase {ECO:0000313|EMBL:EEI22320.1}. SQ SEQUENCE 310 AA; 33675 MW; 7DA01ED5B30D73D5 CRC64; MKLLERLAQG PLVLDGSMST PLEVAGAKTN SDLWTSQTLI DNPDLVYQVH LDYFKAGADL TITDTYQTNV DALVRHGLSE EEARNLIKRA VQLANQARDD YEKETGKHNY VAGSIGPYGA YLADGSEYRG DYDLTAIQLQ NFHLPRLAAI LATGVDCLAL ETQPKLTEVV AILALLKTLE PTMPVYVSFS LRDAEHLSDG TSLKEAVQVV TKDPQVFAVG VNCVGLDLVT PAIKAIKEVT DKPVIVYPNS GATYDPTVKQ WRFEEGTPRF VNAIDDWITA GAAIIGGCCT TLPQDIAVVA EKLRGVGNNR // ID C0XID0_LACHI Unreviewed; 315 AA. AC C0XID0; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEI24874.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EEI24874.1}; GN Name=mmuM {ECO:0000313|EMBL:EEI24874.1}; GN ORFNames=HMPREF0519_0991 {ECO:0000313|EMBL:EEI24874.1}; OS Lactobacillus hilgardii DSM 20176 = ATCC 8290. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423757 {ECO:0000313|EMBL:EEI24874.1}; RN [1] {ECO:0000313|EMBL:EEI24874.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 8290 {ECO:0000313|EMBL:EEI24874.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEI24874.1}. 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; ACGP01000111; EEI24874.1; -; Genomic_DNA. DR RefSeq; WP_003556568.1; NZ_GG669992.1. DR EnsemblBacteria; EEI24874; EEI24874; HMPREF0519_0991. DR PATRIC; 27426694; VBILacHil40002_0764. DR OrthoDB; EOG6C019S; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEI24874.1}; KW Transferase {ECO:0000313|EMBL:EEI24874.1}. SQ SEQUENCE 315 AA; 34848 MW; A87F8C727117DC7E CRC64; MMDLIKENLD SKRALVLDGA MATELEKHGV DTSNDLWSAT ALINDPDAVK AVHTSYFEAG ADITITDTYQ ANVEAFKKVG FTEDQSEKLI TEAVRLALES RDDFYATLPT AERAKRAFYP LVAGSVGPYG AYLADGSEYT GHYQLTNEAY QTFHQRRMRL MDEAGVDVFA FETQPNFEET KALADLLREK FSDRFAWLTF SIKDPEHLCD GTSLAKAVSY FEDNPQISAV GVNCTSMNLI EDSIKTIASN TNKPIIVYPN NGDIYDPKTK TWTPNPNATT FAELTPKWLA AGAKIVGGCC RTTPVDIEQV AESVF // ID C0Z1E9_LACRE Unreviewed; 310 AA. AC C0Z1E9; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEI08378.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EEI08378.1}; GN Name=mmuM {ECO:0000313|EMBL:EEI08378.1}; GN ORFNames=HMPREF0535_1864 {ECO:0000313|EMBL:EEI08378.1}; OS Lactobacillus reuteri MM2-3. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=585517 {ECO:0000313|EMBL:EEI08378.1, ECO:0000313|Proteomes:UP000004961}; RN [1] {ECO:0000313|EMBL:EEI08378.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MM2-3 {ECO:0000313|EMBL:EEI08378.1}; 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 (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. {ECO:0000313|EMBL:EEI08378.1}. 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; ACLB01000098; EEI08378.1; -; Genomic_DNA. DR RefSeq; WP_003667059.1; NZ_GG693760.1. DR ProteinModelPortal; C0Z1E9; -. DR EnsemblBacteria; EEI08378; EEI08378; HMPREF0535_1864. DR GeneID; 5189060; -. DR PATRIC; 37025167; VBILacReu127513_1470. DR OrthoDB; EOG6C019S; -. DR Proteomes; UP000004961; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000004961}; KW Methyltransferase {ECO:0000313|EMBL:EEI08378.1}; KW Transferase {ECO:0000313|EMBL:EEI08378.1}. SQ SEQUENCE 310 AA; 33808 MW; DE82383D6DDE118D CRC64; MTKITAELTK PLLIDGAMST ALEQLGADTN NSLWTASVLA NQPALVKKVH QEYFKAGDRL AITDTYQANV PAFIKNGYSK QEAHSLIQRA VVLAKEARDE YQQETGIYNY VAGALGPYGA YLANGSEYSG AYHLSTIEYQ QFHRPRLTDI LTVGVDVIAI ETQPRLDEVL AELDLVKELA PDTLCYVSFS LKDSTHLPDG TPLAVAARTV AKYTNVFAVG VNCIPLEEVT AAIETVHQVT EKPVIAYPNS SATYDPTTKT WSYPHGRRGL VDYLPQWIAA GLIIVGGCCT TTPQDIAALH EYLKGGAYHD // ID C0ZBM1_BREBN Unreviewed; 1148 AA. AC C0ZBM1; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 01-APR-2015, entry version 51. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:BAH43180.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:BAH43180.1}; GN Name=metH {ECO:0000313|EMBL:BAH43180.1}; GN OrderedLocusNames=BBR47_22030 {ECO:0000313|EMBL:BAH43180.1}; OS Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Brevibacillus. OX NCBI_TaxID=358681 {ECO:0000313|Proteomes:UP000001877}; RN [1] {ECO:0000313|EMBL:BAH43180.1, ECO:0000313|Proteomes:UP000001877} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=47 / JCM 6285 / NBRC 100599 RC {ECO:0000313|Proteomes:UP000001877}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP008955; BAH43180.1; -; Genomic_DNA. DR RefSeq; WP_012685907.1; NC_012491.1. DR RefSeq; YP_002771684.1; NC_012491.1. DR STRING; 358681.BBR47_22030; -. DR EnsemblBacteria; BAH43180; BAH43180; BBR47_22030. DR KEGG; bbe:BBR47_22030; -. DR PATRIC; 21234734; VBIBreBre96763_2191. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; BBRE358681:GHYS-2327-MONOMER; -. DR Proteomes; UP000001877; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR023467; MeTrfase_MtrH/MtxH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR ProDom; PD009948; MtrH_MeTrfase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001877}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAH43180.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001877}; KW Transferase {ECO:0000313|EMBL:BAH43180.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 226 226 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 721 721 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1148 AA; 126672 MW; C13166BABA70BF40 CRC64; MKPTFREQLS RKILILDGAM GTMLQQANLT ADDFGGEAYD GCNELLNLTR PDVIRSIHEK YLEAGADIVE TNTFGAASIV LAEYDVAEKD LEINIAAARL AREAVDAYST EEWPRFVAGA MGPTTKTLSL TGGVTFEELV EAYYRQAKGL ILGGSDVLLL ETSQDTLNVK AGGIGIRKAF EELGQEIPVM LSGTIEPMGT TLAGQNIEAF YISLEHIKPV SIGLNCATGP EFMRDHLRTL SGIAQCAVSC YPNAGLPDEN GHYHETPQGL ASKMRAFAEQ GWINVAGGCC GTTPDHIQAM AETLKDCKPR STAVEPLSAV SGIEVVYVED DNRPLLVGER TNVIGSKKFR EMIAAGHYEE ASDIARAQVK RGAHVIDICL ADPDRDEYED MEKFLQFIVK KVKAPLMIDS TDAKVMELGL RYSQGKAILN SINLEDGLER FEEVVPLIHK FGASVVVGTI EEAGMAITRE KKLEVAQRSY DILVNQYGIK PQDIIFDPLV FPVGTGDEQY IGSAKETVEG IRLIKQAMPA CKTILGVSNV SFGLPPAGRE VLNAVFLYHT TLAGLDYAIV NTEKLERYAS IPEDERKLAE ALLFETNDET LAAFTEFYRQ KKKEVSVEVS SLTLEERLAR YVVEGSKDGL VEDLKLALDK YAPLEIINGP LMTGMEEVGR LFNGNQLIVA EVLQSAEVMK ASVSFLEPFM EKSDAAAKGK ILLATVKGDV HDIGKNLVEI ILSNNGYNVV NLGIKVPPEQ LIAACREEKP DAIGLSGLLV KSAQQMVITA QDLRDAGIDI PMMVGGAALT RKFTSNRIAP EYRGIVLYAK DAMDGLDLVN RLQNPEERDR LVEEQQHLLE AVATAQPVVE EKKAPLPARS AISRTVPIHL PPDCERHVLR QYPLSHLQPY LNLRMLLGKH LGVRGNVDRL IEEGDEKVLE LYGIVEELLK EAKQKGTITT HGVYQFFPAQ SDGNDILVYD PKDHSKLLER FSFPRQLEEP HLCLSDFLRP VESKEMDYVG FLTVTAGGGI REKSTELKDR GDYLRSHVLQ SLALELAEAF AERIHHVMRD VWGIPDPVEM TMLERFGARY QGIRVSFGYP ACPNLEDQAQ LFRLLRPEDI GVQLTEGFMM EPEASVSAMV FAHPEARYFN AGPSIFEV // ID C0ZBM2_BREBN Unreviewed; 621 AA. AC C0ZBM2; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 27-MAY-2015, entry version 38. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=BBR47_22040 {ECO:0000313|EMBL:BAH43181.1}; OS Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Brevibacillus. OX NCBI_TaxID=358681 {ECO:0000313|Proteomes:UP000001877}; RN [1] {ECO:0000313|EMBL:BAH43181.1, ECO:0000313|Proteomes:UP000001877} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=47 / JCM 6285 / NBRC 100599 RC {ECO:0000313|Proteomes:UP000001877}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; BAH43181.1; -; Genomic_DNA. DR RefSeq; WP_012685908.1; NC_012491.1. DR RefSeq; YP_002771685.1; NC_012491.1. DR ProteinModelPortal; C0ZBM2; -. DR STRING; 358681.BBR47_22040; -. DR EnsemblBacteria; BAH43181; BAH43181; BBR47_22040. DR KEGG; bbe:BBR47_22040; -. DR PATRIC; 21234736; VBIBreBre96763_2192. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; BBRE358681:GHYS-2328-MONOMER; -. DR Proteomes; UP000001877; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001877}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862, KW ECO:0000313|EMBL:BAH43181.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001877}. SQ SEQUENCE 621 AA; 67919 MW; 88F7D436EC2DD411 CRC64; MTTRKKDLRA YLKDHLLVGD GAMATQLHGL GVPVGVSFEE LCLSNPRLVH EVHTSYYQAG ARFLETNTYS ANRDALSRYG LEHKVARINR LAVAIAREAA QDDAYVAGSI GSILAGRVKK KVLDEYRDQY EEQAIALLHA GVDGLILETF LDLEELLLAI EVIRPLTDVP VIAQLATLEV GRTRDGYALT DAFSELKAAG ADVVGLNCRL GPAELLRSFE NTVIPEDALL SVFPNAGRLG MTDGEYAFKS SPEYFGQSAL RLREQGVRLI GGCCGTTPAH VKAIADALES LEPQARVNPT IVAGDRPTIS VQNTREREKP SIVERVKTAT TIIVEFDPPR DLDADQFLHG CCELHKAGAD AITLADNSLA TVRMSNMALG ALMKSRHGID PLLHLACRDR NLIGQQSHLM GLNALGIDQI LVITGDPSRF GDLPGASSVF DVTSFDLIRM VKQLNEGVSF SGRPLKQKAQ FIVGAAFNPN VRNMDAAVAR LEKKVEAGAD YIMTQPVYDA ESIRNVYEAT KHIGIPVFIG IMPLTSSRNA EFLHNEVPGI KLSTEALERM KKVQGEAARQ EGIAIAKELV DTAVRYFNGI YLITPFNYYE MAAELIQYTR QQSSLVRMAQ T // ID C0ZDZ0_BREBN Unreviewed; 311 AA. AC C0ZDZ0; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 01-APR-2015, entry version 31. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:BAH43999.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:BAH43999.1}; GN Name=ybgG {ECO:0000313|EMBL:BAH43999.1}; GN OrderedLocusNames=BBR47_30220 {ECO:0000313|EMBL:BAH43999.1}; OS Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Brevibacillus. OX NCBI_TaxID=358681 {ECO:0000313|Proteomes:UP000001877}; RN [1] {ECO:0000313|EMBL:BAH43999.1, ECO:0000313|Proteomes:UP000001877} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=47 / JCM 6285 / NBRC 100599 RC {ECO:0000313|Proteomes:UP000001877}; 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; BAH43999.1; -; Genomic_DNA. DR RefSeq; WP_015891317.1; NC_012491.1. DR RefSeq; YP_002772503.1; NC_012491.1. DR STRING; 358681.BBR47_30220; -. DR EnsemblBacteria; BAH43999; BAH43999; BBR47_30220. DR KEGG; bbe:BBR47_30220; -. DR PATRIC; 21236374; VBIBreBre96763_3007. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; BBRE358681:GHYS-3150-MONOMER; -. DR Proteomes; UP000001877; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001877}; KW Methyltransferase {ECO:0000313|EMBL:BAH43999.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001877}; KW Transferase {ECO:0000313|EMBL:BAH43999.1}. SQ SEQUENCE 311 AA; 34548 MW; D574AD8FFC8D5E93 CRC64; MNPIATILEK FPMMILDGAM ATELERHGCN LNDSLWSAKV LMENPELIKR VHTEYFLAGA DCAITASYQA SVEGFVRLGM SQRDALLLIQ ASVQIAVQAR DEFWKNSDGR LDRPKPIVAA SVGPYGAYLA DGSEYRGAYE LSEEELIDFH RPRMKALIDA GADILACETI PCLSEARALV RLLEEFPGVY AWISFSAKDE LHISDGTSIT ECAIWLDKKE QIAALGINCT SPRNIPRLVQ EIRSCTMKPI VVYPNAGERY DPTTKTWYGA SSREGYGNNA LEWYESGARL IGGCCRTKPE DIKAIADWAR K // ID C0ZZW2_RHOE4 Unreviewed; 1189 AA. AC C0ZZW2; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 27-MAY-2015, entry version 52. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:BAH33897.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:BAH33897.1}; GN Name=metH {ECO:0000313|EMBL:BAH33897.1}; GN OrderedLocusNames=RER_31890 {ECO:0000313|EMBL:BAH33897.1}; OS Rhodococcus erythropolis (strain PR4 / NBRC 100887). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Nocardiaceae; Rhodococcus. OX NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH33897.1, ECO:0000313|Proteomes:UP000002204}; RN [1] {ECO:0000313|Proteomes:UP000002204} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204}; 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. RN [2] {ECO:0000313|EMBL:BAH33897.1, ECO:0000313|Proteomes:UP000002204} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204}; RA Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N., RA Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K., RA Ito M., Narita H., Tago S., Fujita N., Harayama S.; RT "Sequence analysis of three plasmids harboured in Rhodococcus RT erythropolis strain PR4."; RL Environ. Microbiol. 8:334-346(2006). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP008957; BAH33897.1; -; Genomic_DNA. DR RefSeq; WP_020907816.1; NC_012490.1. DR RefSeq; YP_002766636.1; NC_012490.1. DR STRING; 234621.RER_31890; -. DR EnsemblBacteria; BAH33897; BAH33897; RER_31890. DR GeneID; 7709379; -. DR KEGG; rer:RER_31890; -. DR PATRIC; 23192820; VBIRhoEry66701_3695. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; RERY234621:GHDE-3223-MONOMER; -. DR Proteomes; UP000002204; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002204}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAH33897.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002204}; KW Transferase {ECO:0000313|EMBL:BAH33897.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 229 229 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 296 296 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 739 739 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1189 AA; 129153 MW; 9F75C10A541B183D CRC64; MSAPFNSALL DALKQRVVIG DGAMGTMLQA ADLTLDDFLG LEGCNEILND TRPDVLKDIH RAYFAAGADA VETNTFGCNL PNLADYDISH RIRELAEKGT ALAREVADEM GPGRDGMARF VLGSMGPGTK LPSLGHAPYA VLRDAYTEAA LGMIDGGADA ILVETCQDLL QVKAAILGSQ RAMEQLGLRL PIITHVTVET TGTMLLGSEI GAALTALEPL GIDMIGLNCA TGPAEMSEHL RHLSKYSTLP VSVMPNAGLP QLGPKGAEYP LTADELAEAL SGFVSEFGLG LVGGCCGTTP EHISAVADAV RQVEKAQRTP IHEPSTSSLY SAVPFEQDAS ILMIGERTNS NGSKAFREAM LSADYQKCLD IAKDQTRDGA HMLDLNVDYV GRDGAADMSE LASRLATSST LPIMLDSTEP AVLQAGLEHL GGRCAVNSVN YEDGAGPESR FHKIMTLVKE HGAAVVALTI DEEGQARTAE TKVAIAKRLI EDIKGNWGLA ESDIIVDALT FPISTGQEEV RRDGIETIEA IRQLKAAYPE LHFTLGISNI SFGLNPAARQ VLNSVFLHEC TEAGLDTAIV HASKILPMAR IPDEQRETAL DLVYDRRSEG YDPLQKLMAL FEGVSAASAR ESRAQELAGL PLFDRLERRI VDGERNGLDD DLTEAMTVKS PIEIINETLL SGMKTVGELF GSGQMQLPFV LQSAEVMKAA VAFLEPHMEA TDDDGKGRLV IATVKGDVHD IGKNLVDIIL SNNGYDVVNL GIKQPIATIL DAAIEHKADV IGMSGLLVKS TVVMKDNLKE LNSRGVSEQF PVLLGGAALT RSYVENDLQE VYEGDVSYAR DAFEGLNLMD QIMTTKRGGG PAPDSPEAIA AREKAAERKA RHERSKRIAE KRKAAAVPVV LPERSDVATD IAVPTPPFWG SRIVKGISLS EYSGLLDERA LFLGQWGLRG QRKGDGPTYE ELVESEGRPR LRYWLDRLTS EGILAHAAVV YGYFPAISEG DDVIVLTEPK PDAPERFRFT YPRQHRDRFL CIADFVRSRK EAEATGQVDV LPFQLVTMGQ PIADFANELF ASNSYRDYLE VHGIGVQLTE SLAEYWHRRV REELVLPEGH TVAEQDPTEV AGYFDLEYRG ARYSFGYGAC PDLEDRAKLV ALLEPERIGV ELSEELQLHP EQSTDAFVLH HPEAKYFNV // ID C1A5U0_GEMAT Unreviewed; 629 AA. AC C1A5U0; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 27-MAY-2015, entry version 40. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=GAU_0558 {ECO:0000313|EMBL:BAH37600.1}; OS Gemmatimonas aurantiaca (strain T-27 / DSM 14586 / JCM 11422 / NBRC OS 100505). OC Bacteria; Gemmatimonadetes; Gemmatimonadales; Gemmatimonadaceae; OC Gemmatimonas. OX NCBI_TaxID=379066 {ECO:0000313|EMBL:BAH37600.1, ECO:0000313|Proteomes:UP000002209}; RN [1] {ECO:0000313|Proteomes:UP000002209} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T-27 / DSM 14586 / JCM 11422 / NBRC 100505 RC {ECO:0000313|Proteomes:UP000002209}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; BAH37600.1; -; Genomic_DNA. DR RefSeq; WP_012682047.1; NC_012489.1. DR RefSeq; YP_002760070.1; NC_012489.1. DR ProteinModelPortal; C1A5U0; -. DR STRING; 379066.GAU_0558; -. DR EnsemblBacteria; BAH37600; BAH37600; GAU_0558. DR KEGG; gau:GAU_0558; -. DR PATRIC; 21953906; VBIGemAur55831_0577. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; GAUR379066:GI3W-560-MONOMER; -. DR Proteomes; UP000002209; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002209}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000002209}. SQ SEQUENCE 629 AA; 67426 MW; 6A36DFAAB626BE49 CRC64; MTTAAQHPTP RHALLARLLD PEQVVMFDGA MGTMLYARGV FINLCYDELA LRSPELVRDI HAAYVKAGAE VVETNTFGAN RPKLSQYGLE SQVALINRRA AELAREAAGE HRLVAGAVGP LGVRLEPYGP TSREEAGRHF AEQMQALLEG GADCFVLETF GDLDELQQAV LAARAVDARV PVIAQATIGQ DLRTAFGATP EDVAVALDRW GVDIIGLNCS IGPQTILEAI ERMAAVTDRK LSAQPNAGMP RDVAGRRMYM ASPEYMASYA RHLVNAGAKV IGGCCGTTPE HIKAMVEGVR PLAPRTRVQV GNTREFAVEN AAPVGREPVP LGERSRFGAK LAAGQFVTSV EIVPPRGIDT SKLELDAQAL AKAGVDAINV PDGPRAQSRM GAIATSLIIE RHGIESVTHY ACRDRNLLGM LSDLLGASAL GLRNLLLVTG DPPKMGPYPD ATAVFDIDAI GLTNLVSKLN RGLDPGANPI GEPTRFVVGV GVNPAAIDPE QELRRFHWKV EAGAEYAITQ PVFDPAQLER FLESIHDVRI PVVAGIWPLV SARNAEFLAN EVPGVTVPES VLVRMRKANE RSKEHALAEG IAIAREALER VQSSVQGVQI SAPFGRVEYA LDVLTARTV // ID C1A5U1_GEMAT Unreviewed; 1245 AA. AC C1A5U1; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 27-MAY-2015, entry version 45. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:BAH37601.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:BAH37601.1}; GN Name=metH {ECO:0000313|EMBL:BAH37601.1}; GN OrderedLocusNames=GAU_0559 {ECO:0000313|EMBL:BAH37601.1}; OS Gemmatimonas aurantiaca (strain T-27 / DSM 14586 / JCM 11422 / NBRC OS 100505). OC Bacteria; Gemmatimonadetes; Gemmatimonadales; Gemmatimonadaceae; OC Gemmatimonas. OX NCBI_TaxID=379066 {ECO:0000313|EMBL:BAH37601.1, ECO:0000313|Proteomes:UP000002209}; RN [1] {ECO:0000313|Proteomes:UP000002209} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T-27 / DSM 14586 / JCM 11422 / NBRC 100505 RC {ECO:0000313|Proteomes:UP000002209}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP009153; BAH37601.1; -; Genomic_DNA. DR RefSeq; WP_012682048.1; NC_012489.1. DR RefSeq; YP_002760071.1; NC_012489.1. DR STRING; 379066.GAU_0559; -. DR EnsemblBacteria; BAH37601; BAH37601; GAU_0559. DR KEGG; gau:GAU_0559; -. DR PATRIC; 21953908; VBIGemAur55831_0578. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; GAUR379066:GI3W-561-MONOMER; -. DR Proteomes; UP000002209; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002209}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAH37601.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002209}; KW Transferase {ECO:0000313|EMBL:BAH37601.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 266 266 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 329 329 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 330 330 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 776 776 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1245 AA; 135239 MW; EBC15D7D62AD62B7 CRC64; MSNPVQPKPI ASNDARTARL AQLDEALARR LLIIDGAMGT MLQRHRLTEA DYRGGMDHPR FGAWPHDVKG NNDLLVLTQP DIVADVHRQY LAAGADILET NTFNATAISM ADYGMEALAY ELNVAGTALA RRVADEFEAQ DPTRPRWVAG VLGPTNRTAS ISPDVENPGS RNVSYDDLAA AYGEAVRGLV DGGADILLVE TIFDSLNAKA ALFAIERYFE ETGTRFPVMI SGTITDASGR TLSGQTAEAF WNSMAHVQPV SIGLNCALGA EQLRQYVQEL GRVADCHVSA HPNAGLPNAF GGYDETPERM AEQIGEWARS GLVNIVGGCC GTTPEHIAAI AAAVHQVPPR KRPVLDHQLH LSGLEPFTVG PTTNFVNVGE RTNVTGSARF AKLILEGSYA EALVVARQQV LSGAQVIDVN MDEGLLDAER AMTTFLNLVA SEPDIARVPV MVDSSKWTVL EAGLKCLQGK GIVNSISLKE GEAEFLRQAR LVRRYGAAVI VMAFDEDGQA DTVARRVAIC TRAYRLLTET IGFPPEDIIF DPNIFAIGTG IEEHANYAVD FFAATREIKR TLPHVKVSGG VSNVSFSFRG NNPLREAIHA VFLYHAIRAG MDMGIVNAGQ LVPYEDIPVD LRERVEDLVL NRRPDATERL MDVAEQVKGR AARAVEDEVW RALPVEDRLS HALVHGIDSH VVADAEEARQ LVAHPIEVIE GPLMRGMNIV GDLFGAGKLF LPQVVKSARV MKKAVAHLIP FIEALKTSET KSAGRVLMAT VKGDVHDIGK NIVGVVLQCN GYEVIDIGVM QSCAKILDKA REIEADVIGL SGLITPSLEE MSFVASEMER QGFTIPLLIG GATTSKAHTA LKIEPVYSGP VVHVLDASRA VGVTSSLLSP ERRSAYVAAL RQEYAGIREA RAARGGADRL ISIEAARENR VNIDLTVPVP TPAFTGVRTI APYPLEDLVP FIDWTPFFQT WELAGRFPAI LDDEIVGEAA RSLYADAQAL LERLVREKRL EARAVFGFWP AQAVGDDILL YDPEGGSETP TVAATLHMLR QQLDKKGDGR PNYCLADFVA KRDSGVLDYV GAFAVTAGHG LESILEEFHA QHDDYGSIMA KALADRLAEA LAERLHQRVR TEFWGYANAE SLDNDGLIRE QYQGIRPAPG YPACPDHREK GTLFALTGAA ERAGMELTET YSMIPGASVS GWYFWRPEST YFGVGKILPD QLAEYEARAG RTAPDPQFTS VLMAS // ID C1ASR2_RHOOB Unreviewed; 1189 AA. AC C1ASR2; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 29-APR-2015, entry version 50. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:BAH48844.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:BAH48844.1}; GN Name=metH {ECO:0000313|EMBL:BAH48844.1}; GN OrderedLocusNames=ROP_05970 {ECO:0000313|EMBL:BAH48844.1}; OS Rhodococcus opacus (strain B4). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Nocardiaceae; Rhodococcus. OX NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH48844.1, ECO:0000313|Proteomes:UP000002212}; RN [1] {ECO:0000313|EMBL:BAH48844.1, ECO:0000313|Proteomes:UP000002212} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B4 {ECO:0000313|EMBL:BAH48844.1, RC ECO:0000313|Proteomes:UP000002212}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP011115; BAH48844.1; -; Genomic_DNA. DR RefSeq; WP_012687849.1; NC_012522.1. DR RefSeq; YP_002777789.1; NC_012522.1. DR STRING; 632772.ROP_05970; -. DR EnsemblBacteria; BAH48844; BAH48844; ROP_05970. DR KEGG; rop:ROP_05970; -. DR PATRIC; 23218343; VBIRhoOpa21106_0590. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; ROPA632772:GH0Q-596-MONOMER; -. DR Proteomes; UP000002212; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002212}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAH48844.1}; KW Transferase {ECO:0000313|EMBL:BAH48844.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 229 229 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 296 296 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 739 739 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1189 AA; 129561 MW; EFEBD199B456CE68 CRC64; MSAPFHSALL DALNQRVVIG DGAMGTMLQA ADLTLDDFLG LEGCNEILND TRPDVLKEIH RAYFEAGADA VETNTFGCNL PNLADYDISD RIRELAEKGT RLAREVADEM GPGRDGMGRF VLGSMGPGTK LPTLGHAPFA ILRDAYAEAA MGMIDGGADA ILVETCQDLL QVKAAILGSQ RAMETLGSRL PIITHVTVET TGTMLLGSEI GAALTALEPL GIDMIGLNCA TGPAEMSEHL RHLSKYSSLP VSVMPNAGLP QLGPNGAEYP LTAEELAEAL SGFVTEFGLG LVGGCCGTTP EHIRQVADAV RLVEKAARNP VHESGTSSLY TAVPFEQDAS ILMIGERTNS NGSKAFREAM IAEDYQKCLD IAKDQTRDGA HMLDLNVDYV GRDGAADMAA LASRFATSST LPIMLDSTEP AVLQAGLEHL GGRCAVNSVN YEDGDGPDSR FQKIMRLVKE HGAAVVALTI DEEGQARTAE HKVRIAERLL EDITVNWGLD ESDIIIDALT FPISTGQEEV RRDGIETIEA IRELKKRHPR VHFTLGVSNI SFGLNPAARQ VLNSVFLHEC TEAGLDTAIV HASKILPMAR IPDEQRETAL DLVYDRRREG YDPLQKLMEL FEGVSAASAR ESRAQELAAL PLFERLERRI VDGERNGLDD DLTAAMEEKP PLAIINETLL SGMKTVGELF GSGQMQLPFV LQSAEVMKAA VAYLEPHMEA TDEDGKGRIV IATVKGDVHD IGKNLVDIIL SNNGYDVVNL GIKQPIATIL DAAIEQKADV IGMSGLLVKS TVVMKDNLQE LNAKGVAEKF PVLLGGAALT RSYVENDLAE VYEGDVSYAR DAFEGLHKMD EIMAVKRGGA PDPDSPEAIA AREKAAERKA RHERSKRIAE KRKAAEVPVE LPERSDVATD IAVPSPPFWG NRIVKGVSLS DYSGLLDERA LFLGQWGLRG QRSGDGPTYE ELVETEGRPR LRYWLDRLST EGILAHAAVV YGYFPAVSEG DDVVVLTDPT PDAEERFRFT FPRQHRDRFL CVADFVRSRT EAKETGQVDV FPMQLVTMGQ PIADFANELF AANAYRDYLE VHGIGVQLTE SLAEYWHQRV REELVLPGGH NVGEQDPSEV SGFFDLAYRG ARYSFGYGAC PNLEDRAKMV ALLEPERIGV KLSEELQLHP EQSTDAFVLH HPEAKYFNV // ID C1C2Y0_CALCM Unreviewed; 391 AA. AC C1C2Y0; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 01-OCT-2014, entry version 11. DE SubName: Full=Homocysteine S-methyltransferase 1 {ECO:0000313|EMBL:ACO15633.1}; GN Name=HMT1 {ECO:0000313|EMBL:ACO15633.1}; OS Caligus clemensi (Sea louse). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Maxillopoda; OC Copepoda; Siphonostomatoida; Caligidae; Caligus. OX NCBI_TaxID=344056 {ECO:0000313|EMBL:ACO15633.1}; RN [1] {ECO:0000313|EMBL:ACO15633.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Whole {ECO:0000313|EMBL:ACO15633.1}; RA Yasuike M., von Schalburg K., Cooper G., Leong J., Jones S.R.M., RA Koop B.F.; RT "Caligus clemensi ESTs and full-length cDNAs."; 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; BT081209; ACO15633.1; -; mRNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Methyltransferase {ECO:0000313|EMBL:ACO15633.1}; KW Transferase {ECO:0000313|EMBL:ACO15633.1}. SQ SEQUENCE 391 AA; 44504 MW; CED9DF790471EE79 CRC64; MTDIFYPVYP RVLGSRNEIF ILDGGFSTQI QQHAGKDSFE GRPQWTSELN TENPEAVKRS HMDYLSNCSG DLISSNTYQA ASSSIEKAVE LCDEAILEAS HVPRKAGIVG SLGPYAAFQP SGSEYNSSDG MSYPPLADEE LKEWYKDRIR HLMIAGVDVI AFETMPCIKE ALVALDIIDN VINAKCWISF QCRDGKHLAY GESFKDAVER LLNHPAFVKR KLLYIGINCT SPKYISSLLK LAERVNKKMN FPDKYGYWRI PYVVYPNRGV YCKEKCCYVL DKDDPLGGGD EGILKRCHEW MLLGTRVIGG CCGVDANLIK EIRNQVSEHL FDVLDKENDI DYFIDHEVIE SRLLKPVEKD KIERRTKTND FTDSLWNMCE MPYKNPGWVN E // ID C1CUZ4_DEIDV Unreviewed; 1229 AA. AC C1CUZ4; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 27-MAY-2015, entry version 47. DE SubName: Full=Putative methionine synthase (5-methyltetrahydrofolate--homocysteine methyltransferase) (Vitamin B12 methyltransferase) {ECO:0000313|EMBL:ACO46011.1}; GN OrderedLocusNames=Deide_11120 {ECO:0000313|EMBL:ACO46011.1}; OS Deinococcus deserti (strain VCD115 / DSM 17065 / LMG 22923). OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; OC Deinococcaceae; Deinococcus. OX NCBI_TaxID=546414 {ECO:0000313|EMBL:ACO46011.1, ECO:0000313|Proteomes:UP000002208}; RN [1] {ECO:0000313|EMBL:ACO46011.1, ECO:0000313|Proteomes:UP000002208} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VCD115 / DSM 17065 / LMG 22923 RC {ECO:0000313|Proteomes:UP000002208}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001114; ACO46011.1; -; Genomic_DNA. DR RefSeq; WP_012693134.1; NC_012526.1. DR RefSeq; YP_002785765.1; NC_012526.1. DR STRING; 546414.Deide_11120; -. DR PaxDb; C1CUZ4; -. DR EnsemblBacteria; ACO46011; ACO46011; Deide_11120. DR KEGG; ddr:Deide_11120; -. DR PATRIC; 21615962; VBIDeiDes121019_1263. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; DDES546414:GHOM-1261-MONOMER; -. DR Proteomes; UP000002208; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002208}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACO46011.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002208}; KW Transferase {ECO:0000313|EMBL:ACO46011.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 241 241 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 750 750 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1229 AA; 133747 MW; 7C334DAB0125EFE0 CRC64; MASLHSEAQR RILVLDGAWG TMLQRAGLTE GDFRWDGADP LRMYRGNFDL LQLTRPDVIR EVHRAYFEAG ADIASTNTFN STVISQADYG TEHLARAMSE AGARLAREVA DEFTARDGRP RWVAGAVGPT NRTATLSPDV ERPEFRNVTF DDLVAAYVEQ VDGLIAGGAD LILIETVFDT LNAKAALFAC EEAFAQAGRT LPIMLSGTIT DASGRTLSGQ TPEAFVISTE HAQLFSVGLN CALGADLLRP HLRAVAASSG TLVSVHPNAG LPNAFGEYDE TPEHTAAVLR SFAEDGLVNI VGGCCGTTPD HIRAIAEAVA GLPPRTPPTL PPYLRLSGLE AFTVTPETNF VNVGERTNVT GSPKFSKAIL ADDYDSGLKI ARQQVVNGAQ LVDVNFDEGM LDGEAAMVKF LNLLAGEPDI SRVPLMLDSS KWEILESGLK RVQGKAVVNS ISLKDGEEKF LERARLLRRY GAAAVVMAFD EQGQADNLER RKEITSRAYR LLTQEAGFPP QDIIFDPNVL TVATGMEEHD RYAIDFIEAT RWIKENLPGA LVSGGISNVS FSFRGNNHVR EAMHSVFLYH AIRAGLDMGI VNAGMLAVYE DIEPELREAV EDVILARRPD ATERLITLAE SYKGVKREAS AQSAWRELPV TERLKHALVS GITDHVTEDA EEAYQLLGSP LAVIEGPLMD GMNVVGDLFG AGKMFLPQVV KSARVMKRAV AHLTPYLEAE QTSQSGKGKV LLATVKGDVH DIGKNIVGVV LACNGYQVTD LGVMVSTEKI LDTASEMGAD VIGLSGLITP SLDEMVTVAR EMTRRGLKTP LLIGGATTSR AHTAVKIDPA YDGTVVHVMD ASRAVGVVND LLTQPEAVQE RTRDEYASLR ERHGERTVRL IPLAQARARA PQLSPAVPPA PAQPGRQLIE QPIAELLDYI DWTPFFIAWE MKGIYPNILT DPLRGPEARK LFEDAQALLQ RVIAEGTLTA RGVIGLWPAH REGDDIVVTA GAQSDTLDHH THELAAGRAD FDTEFRLHTL RQQRDQTTPN TALADFVAQQ GDHVGAFAVA IHGAEELARA FEAAHDDYNS ILVKAVADRL AEAFAEKLHR DVRVRHWGYA PDEALANDDL IRERYAGIRP APGYPAQPDH TEKRTLFQLL RAEEAGLALT ESCAMTPAAA VSGLYFAHPD AQYFAVGRIG RDQVEDYAHR KGWTLEEAER WLGPLLAYDP ARRAEAVAL // ID C1D3E7_DEIDV Unreviewed; 314 AA. AC C1D3E7; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=Putative homocysteine S-methyltransferase {ECO:0000313|EMBL:ACO48026.1}; GN OrderedLocusNames=Deide_3p00853 {ECO:0000313|EMBL:ACO48026.1}; OS Deinococcus deserti (strain VCD115 / DSM 17065 / LMG 22923). OG Plasmid pDeide3 {ECO:0000313|Proteomes:UP000002208}. OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; OC Deinococcaceae; Deinococcus. OX NCBI_TaxID=546414 {ECO:0000313|EMBL:ACO48026.1, ECO:0000313|Proteomes:UP000002208}; RN [1] {ECO:0000313|EMBL:ACO48026.1, ECO:0000313|Proteomes:UP000002208} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Plasmid pDeide3 {ECO:0000313|Proteomes:UP000002208}, and RC VCD115 / DSM 17065 / LMG 22923 {ECO:0000313|Proteomes:UP000002208}; 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001117; ACO48026.1; -; Genomic_DNA. DR RefSeq; WP_012694899.1; NC_012528.1. DR RefSeq; YP_002787530.1; NC_012528.1. DR EnsemblBacteria; ACO48026; ACO48026; Deide_3p00853. DR KEGG; ddr:Deide_3p00853; -. DR eggNOG; COG2040; -. DR HOGENOM; HOG000179103; -. DR OMA; CCGTDHR; -. DR OrthoDB; EOG6R5C46; -. DR BioCyc; DDES546414:GHOM-2779-MONOMER; -. DR Proteomes; UP000002208; Plasmid pDeide3. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002208}; KW Methyltransferase {ECO:0000313|EMBL:ACO48026.1}; KW Plasmid {ECO:0000313|EMBL:ACO48026.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002208}; KW Transferase {ECO:0000313|EMBL:ACO48026.1}. SQ SEQUENCE 314 AA; 33791 MW; 99E571FFCA56F5D7 CRC64; MKGPLPQLTR RVLTDGGLET DLLFNRGIDL PLFSSVVLLA TLEGREALET YYRPYLELAH RHSAGFILES ATWRASPDWA APLGLHQCGL DQLNVAAVEL LHRLRSKSAT DPLEIVVSGC VGPRGDGYDP GQIMNVAEAA NYHGHQVRVL ASAGVDMLSA LTMTNINEAT GITLAAAEVG LPVSVSFTVE TDGRLPTGDS LMDAVTAVDE ATNDYAAYFM VNCAHPDHFA AVLDEPAAWT RRIRGVRANA SRCSHKELDA MTELDAGDPL ELGQLYRKLL HEHPQITVLG GCCGTDLRHV TAIAEACARL PMSS // ID C1D9Z0_LARHH Unreviewed; 1239 AA. AC C1D9Z0; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 29-APR-2015, entry version 47. DE SubName: Full=MetH {ECO:0000313|EMBL:ACO73103.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ACO73103.1}; GN Name=metH {ECO:0000313|EMBL:ACO73103.1}; GN OrderedLocusNames=LHK_00107 {ECO:0000313|EMBL:ACO73103.1}; OS Laribacter hongkongensis (strain HLHK9). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Chromobacteriaceae; Laribacter. OX NCBI_TaxID=557598 {ECO:0000313|EMBL:ACO73103.1, ECO:0000313|Proteomes:UP000002010}; RN [1] {ECO:0000313|EMBL:ACO73103.1, ECO:0000313|Proteomes:UP000002010} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HLHK9 {ECO:0000313|EMBL:ACO73103.1, RC ECO:0000313|Proteomes:UP000002010}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001154; ACO73103.1; -; Genomic_DNA. DR RefSeq; WP_012695598.1; NC_012559.1. DR RefSeq; YP_002794112.1; NC_012559.1. DR STRING; 557598.LHK_00107; -. DR EnsemblBacteria; ACO73103; ACO73103; LHK_00107. DR KEGG; lhk:LHK_00107; -. DR PATRIC; 22297347; VBILarHon49832_0109. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; LHON557598:GHO5-107-MONOMER; -. DR Proteomes; UP000002010; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002010}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACO73103.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002010}; KW Transferase {ECO:0000313|EMBL:ACO73103.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 249 249 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 769 769 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1239 AA; 135059 MW; 4BCB83088E779AC8 CRC64; MTTRHALLTN LLQSRILILD GGMGTMIQRH QLQEADYRGS RFADWPHDVK GNNDLLVLTR PDVIGGIHQA YLDAGADIIE TNTFNATSIA MADYGMEGLV HEMNVAAARL VKDLCEAETA RNPAKPRFCA GVLGPTNRTC SISPDVNDPG YRNISFDELV SSYTEAIDGL VAGGADLLLV ETIFDTLNAK AAVFAIQRYF DLRPELERLP IMISGTITDQ SGRTLTGQTT EAFYNSLSHA DALSFGLNCA LGPDLLRPYV EEMSRVSAGF VSVHANAGLP NAFGGYDLAP ADMGRAVREW AEAGLINIVG GCCGTTPEHI AAIAEAVAGV APRPRPVITP KCRLAGLEPF NIGDKDLFVN VGERTNVTGS RAFAKLILNG DYATALDVAR QQVENGAQII DINMDEGMLD AHAAMVRFLN LIAAEPDIAR VPVMIDSSKW EVIEAGLKCI QGKGIVNSIS MKEGVDKFIE QARLVRRYGA AVIVMAFDEQ GQADTFARKV EICEKSYRIL VDEVGFPPED IIFDPNVFAV ATGIEEHARY GLDFIEATGW IKQNLPHAKI SGGVSNVSFS FRGNNKVREA IHAVFLYHAI QRGMTMGIVN AGALEVYNEV DPELRDRIED VVLMRTPKDG GDATEHLIAL AEKFKGEAVA GKQGEDLAWR DWPVEKRLEH ALVKGITTYI EQDTEEVRAK SERPIHVIEG PLMDGMNVVG DLFGAGKMFL PQVVKSARVM KAAVAYLEPF IDEEKIRLGL QDAPAKGVII MATVKGDVHD IGKNIVGVVL RCNNYKVIDL GVMVPCQTIL DAAREHKADI IGLSGLITPS LEEMAYVAKE MQRQGFDIPL LIGGATTSRV HTAVKIAPHY RGPVIYVPDA SRAVGVCSNL LSDTLRDGFV QEVADDYAKA RAIFEGRGEA RLLPLAEARA HRFAGEWALY TPPVPRWLGV RRFEVELADI VPFIDWTPFF QSWELAGRFP AILDDAVVGE SARQLFADAQ AMLGQVVEGR WLEARAVIGL FPANSVNDDD IELYDPETGE RRLSWTGLRQ QIVKTDKQGG GQPDWALADF VAPKGSGVRD YLGAFAVTAG LGIEPHVARF EAANDDYSAI LLKALADRLA EGLAELMHAR VRREFWGYAD SEALDNEALI DERYVGIRPA PGYPACPDHT VKRGLFDLLD APAIGMTLTE GYAMLPTAAV SGFYFSHPDS RYFGVGKIGR DQVQSYAARR GVSVEQAERD LAPNLGYSA // ID C1DM06_AZOVD Unreviewed; 1278 AA. AC C1DM06; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 27-MAY-2015, entry version 47. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase, MetH {ECO:0000313|EMBL:ACO79093.1}; GN Name=metH {ECO:0000313|EMBL:ACO79093.1}; GN OrderedLocusNames=Avin_29240 {ECO:0000313|EMBL:ACO79093.1}; OS Azotobacter vinelandii (strain DJ / ATCC BAA-1303). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Azotobacter. OX NCBI_TaxID=322710 {ECO:0000313|EMBL:ACO79093.1, ECO:0000313|Proteomes:UP000002424}; RN [1] {ECO:0000313|EMBL:ACO79093.1, ECO:0000313|Proteomes:UP000002424} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DJ / ATCC BAA-1303 {ECO:0000313|Proteomes:UP000002424}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001157; ACO79093.1; -; Genomic_DNA. DR RefSeq; WP_012701480.1; NC_012560.1. DR RefSeq; YP_002800068.1; NC_012560.1. DR ProteinModelPortal; C1DM06; -. DR SMR; C1DM06; 699-1275. DR STRING; 322710.Avin_29240; -. DR EnsemblBacteria; ACO79093; ACO79093; Avin_29240. DR KEGG; avn:Avin_29240; -. DR PATRIC; 21032001; VBIAzoVin72790_2758. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; AVIN322710:GJ0M-2926-MONOMER; -. DR Proteomes; UP000002424; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002424}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACO79093.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002424}; KW Transferase {ECO:0000313|EMBL:ACO79093.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 358 358 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 359 359 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 806 806 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1278 AA; 139982 MW; DAF47ED46DDDAC04 CRC64; MPGGDSEAAA VQHERASCKS GPTSKAVQLC YYLHPFPRLY PGISFMSDRA ARLQALQQAL KERILILDGG MGTMIQSYKL EESDYRGTRF ADWPQDVKGN NDLLLLTRPD VIQAIEQAYL DAGADILETN TFNATRVSQA DYGMEELVYE LNVEGARLAR QVADAKSAEN PARPRFVAGV IGPTSRTCSI SPDVNNPGYR NVTFDELVDN YTEATRGLIE GGADLILIET IFDTLNAKAA IYAVQQVFEE DGVSLPIMIS GTITDASGRT LSGQTTEAFW NSVRHAEPIS VGLNCALGAK DLRPYLEELA TKADTHVSAH PNAGLPNAFG EYDETPAQMA EVIEEFAAAG FLNIVGGCCG TTPAHIRAIA EAVAKYPPRA IPEIPRACRL SGLEPFTIDR DSLFVNVGER TNITGSARFA RLIREENYAE ALDVARQQVE AGAQVIDINM DEGMLDSKAA MVTFLNLIAS EPDISRVPIM IDSSKWEVIE AGLKCIQGKG IVNSISMKEG VEPFKHHAHL CKRYGAAVVV MAFDEAGQAD TAARKREICQ RSYDILVDEV GFPPEDIIFD PNIFAVATGI EEHNNYAVDF IEACAYIRDN LPYALSSGGV SNVSFSFRGN NPVREAIHSV FLYHAIRNGL TMGIVNAGQL EIYDEIPEEL RDKVEDVVLN RHPGATEALL AIADRYKGDG TVKEAETEEW RGYPVGKRLE HALVKGITTW IVEDTEECRR QCARPIEVIE GPLMSGMNVV GDLFGAGKMF LPQVVKSARV MKQAVAHLIP FIEAEKGDKP EAKGKILMAT VKGDVHDIGK NIVGVVLGCN GYDVVDLGVM VPAEKILQTA REEKCDIIGL SGLITPSLDE MVHVAREMQR QGFALPLMIG GATTSKAHTA VKIEPQYAND AVVYVTDASR AVGVATSLLS KELKPDYVAK IRTDYAEVRE RTANRGARAE RLSYAQAVAN KPQLDWTGYR PPQPAFTGVK VLEDIDLAVL AGYIDWTPFF MSWDLAGKYP RILEDAVVGE AASALFKDAQ GMLKKLIDEK LIRAKAVFGF WPANQVRDDD LEVYGDDGRP LATLHHLRQQ AAKPDGKPNQ SLADFVAPKD SGVTDYVGGF IVTAGIGAEE LAKAYQDQGD DYSSIMVKAL ADRLAEACAE WLHERVRKEY WGYAPNERLS NEELIKEQYK GIRPAPGYPA CPDHTEKGTL FRLLDPQGTS GVTLTEHYAM FPAAAVSGWY FAHPEAKYFA VGKIDRDQVE SYSQRKGQSV EESERWLMPN LGYEATTP // ID C1DU66_SULAA Unreviewed; 1176 AA. AC C1DU66; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 27-MAY-2015, entry version 50. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACN98994.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ACN98994.1}; GN Name=metH {ECO:0000313|EMBL:ACN98994.1}; GN OrderedLocusNames=SULAZ_0668 {ECO:0000313|EMBL:ACN98994.1}; OS Sulfurihydrogenibium azorense (strain Az-Fu1 / DSM 15241 / OCM 825). OC Bacteria; Aquificae; Aquificales; Hydrogenothermaceae; OC Sulfurihydrogenibium. OX NCBI_TaxID=204536 {ECO:0000313|EMBL:ACN98994.1, ECO:0000313|Proteomes:UP000001369}; RN [1] {ECO:0000313|EMBL:ACN98994.1, ECO:0000313|Proteomes:UP000001369} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Az-Fu1 / DSM 15241 / OCM 825 RC {ECO:0000313|Proteomes:UP000001369}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001229; ACN98994.1; -; Genomic_DNA. DR RefSeq; WP_012674314.1; NC_012438.1. DR RefSeq; YP_002728653.1; NC_012438.1. DR STRING; 204536.SULAZ_0668; -. DR EnsemblBacteria; ACN98994; ACN98994; SULAZ_0668. DR KEGG; saf:SULAZ_0668; -. DR PATRIC; 23762468; VBISulAzo123226_0650. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SAZO204536:GHRE-666-MONOMER; -. DR Proteomes; UP000001369; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001369}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACN98994.1}; KW Transferase {ECO:0000313|EMBL:ACN98994.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 221 221 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 287 287 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 727 727 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1176 AA; 132606 MW; 12D865582FBB13A6 CRC64; MDLRSLIKER VLVIDGAMGT MIQSTIIPMS AWDGKVGCNE ILNITAPQII QNIHEKYLQA GADIIKTNTF GALPWVLEEY GIPDKAYELA KAGALLVKQL CDKYSTAEKP RFVAGSLGPG TKLPSLGHID YDTMYEGYKV AAYGLIDGGV DVFLVETCQD PLQIKVALHA LNDASKERRK DIPIMVSATI ELTGTMLIGT DAQTLAAIME PFDILTLGFN CGTGPDQVEQ HLRKLSQVWK GYISVHANAG LPENRGGQTY YPMNAEEFAE KESKFLDIDG VAIVGGCCGT TPSHIKALYE KVKGKKPKKP VGKQPKSLAS LFMTQPLKQD PPPFLVGERT NATGSKQFRE LLLKEDYDGI LAIAQDQVKS GSHALDVSVN YAGRDEIKDM KEVIRRFNEK IPIPLMVDST QPKAIEAGLK HIGGKPIINS ANLEDSEEKF DKICQLAKRF GTSLVLLAID EQGMAKTKER KLEVAERMYE RATKVHGLDP EDLVFDLLTF TVGSGDQEYR DAAVQTIEAI RELRKRHPEV GAVLGISNVS FGLDMHARKY LNSVFLHHCV EAGLTMAIVN PKHLIPFHKI SEEDRKVCEN LLFNVWENGK DPLFEFIHYF SKKKESILSE ESKDFKNLPI EEKIKKLLID GEKEKLIKAV EEARHKIPPE KIINEILIDA MKIVGDLFGE GKMQLPFVLQ SAESMKAAVD YLNQFLPKTT KKKKTTLVLG TVKGDVHDVG KNLVDIILTN NGFNVVNLGI KVELEQFLKA AEEHKADAIG MSGLLVKSTL EMKNNLEEMQ KRGIKIPVLL GGAALNKKFV DEYCRPVYDG PIFYCRDAFD GIEAMTRIEK GIFDTDLGYK EEEETQVKIE EKLEIPPLKD IKMPSMDVVV PTPPFWGRKV WIHPDSPEYE EIRELAFRWI NKGALFKRAW GYTRGDKSRE EYEKLKKEEI LPNFERLKKL LIENDLFNPI IIYGYYPCRS DFPIRLKNND NRESSLLIFP PSEGWKSEED VNREPLENIL DRVYKKIDFP RSSKPPYRSL SDYFHHDRHD VVAFTVVSAG KKLSEYENEL FKQGKYKDYH LIHGLGVELA EALAEIVHKK IRIELGIAKA EGESLYDVNW QIRNYQGARY SPGYPACPDL AINDIIFDIL KPQEYGITLT ENHLIVPEQS TDAIVVYHPE ATYFSV // ID C1EAX2_MICSR Unreviewed; 1378 AA. AC C1EAX2; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 01-APR-2015, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ACO64932.1}; GN ORFNames=MICPUN_105867 {ECO:0000313|EMBL:ACO64932.1}; OS Micromonas sp. (strain RCC299 / NOUM17) (Picoplanktonic green alga). OC Eukaryota; Viridiplantae; Chlorophyta; prasinophytes; Mamiellophyceae; OC Mamiellales; Mamiellaceae; Micromonas. OX NCBI_TaxID=296587 {ECO:0000313|EMBL:ACO64932.1, ECO:0000313|Proteomes:UP000002009}; RN [1] {ECO:0000313|EMBL:ACO64932.1, ECO:0000313|Proteomes:UP000002009} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RCC299 / NOUM17 {ECO:0000313|Proteomes:UP000002009}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001328; ACO64932.1; -; Genomic_DNA. DR RefSeq; XP_002503674.1; XM_002503628.1. DR ProteinModelPortal; C1EAX2; -. DR GeneID; 8244965; -. DR KEGG; mis:MICPUN_105867; -. DR HOGENOM; HOG000251409; -. DR InParanoid; C1EAX2; -. DR KO; K00548; -. DR Proteomes; UP000002009; Chromosome 7. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002009}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002009}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 360 360 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 423 423 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 424 424 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 900 900 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1378 AA; 151850 MW; A1CEC53A213426DE CRC64; MAPSIAGYTW HDAYNFAIVN PGQASGAILL AWPLFIAFAA VCVVLSPLVF PGAMLVAYVL NKRGAQPVEK PRPKAVAAGQ GASYAEMYPE VQPKANLPPV PKYAKWVDPV KPTAAFDQIN KIMKERIMVI DGAMGTAVQK YKLSEDDFRG ERYKNHTHDL KGNNDVLVIT RPDVIEEIHT AYLAAGADII ETNTFNSTMI SQADYELDKK EEVYLLNKTA AQLAKKCCVE FTKKNPAKPR FAAGAVGPTN KTLSVSPSVE NPAFRGCTYD EIVEAYYEQV EALIDGGVDV LLVETIFDTL NAKAAMFAID MYFEKWGQKI PVFVSGTIVD NSGRTLSGQT NEAFWNSMSH SKPIAIGLNC ALGAKDMVPY IENLSRVADC WVFCYPNAGL PNAMGGYDQK GAEMAEDCRV FPEKGLINAI GGCCGTTDEH IKCLADMVAT YKPRERHDVP DIMRLSGLEP FNYAPNEKDY RKTFINLGER CNVAGSTIFK KAIVDGNYEK ALAIALKQVE NGAHVIDVNM DDGLIDGESA MTKFVNLMVS EPDVAKVPFM IDSSKFHVVE AGLKCSQGKC IMNSISLKGG EEEFLNQAKI VKRHGAAVVV MAFDEEGQAA TEAEKVRICC RAYKLLVEKV GFNPQDIIFD PNILTIGTGM EEHNNYGVDF INATREIKRL CPGCKISGGV SNLAFSFRGN EPVRRAFHSA FLYHACKAGM DMGIVNAAQV EEDVYEKIDK ELLEYVEDVL LNRCTNATER MLEFAATLDP KSKPTALRKK GAEGGAGAAK KDDAKAWRNQ TVGKRLEHAL VKGIDEFCIA DTEECRTNGD YKTPLEIIEG PLMDGMNVVG DLFGAGKMFL PQVIKSARVM KKSVGHLIPF MEEEKRLNGG SGEASNAGVF LIATVKGDVH DIGKNIVAVV LGCNNFKVID IGVMCPKDKI IDALKEHNAD ICGLSGLITP SLDEMVDMAK AMEAEGMKIP LLIGGATTSK MHTAVKLAPN YSGGVVHVLD ASRAVPVAQT LMDQNKRGEY LDDINETYAE MREEFYAGLE DRKYLTLGQA RDTAAKCAVD FKSKEHTPVT PQFTGVKALV DVPIADVIDY IDWNPFFQVW QLRGRYPNRG YPKIFNDETV GAEAKKLYEE AQRMLKSIMD NKRLKLNGII GFYPANSVGD DIEVYADESR TTKTHTFHTL RQQAEKDVDE PYMALSDFIA PKDSGVKDYL GMFVATAGIG LHELTAEFKA ANDDYSYIMA EALADRLAEA FAELMHEKVR KEHWGYAKDE KFNCEDLLKV KYQGIRPAPG YPSQPDHTEK ATMWDLMKVQ EEIGVELTES FAMLPSASVS GLYFAGKCSQ YFNVGKITAD QVKEYADRKG QDFKTAEKWL SPILSYEP // ID C1F3L2_ACIC5 Unreviewed; 636 AA. AC C1F3L2; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 27-MAY-2015, entry version 40. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=ACP_1004 {ECO:0000313|EMBL:ACO33263.1}; OS Acidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / JCM 7670 / OS NBRC 15755 / NCIMB 13165 / 161). OC Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae; OC Acidobacterium. OX NCBI_TaxID=240015 {ECO:0000313|EMBL:ACO33263.1, ECO:0000313|Proteomes:UP000002207}; RN [1] {ECO:0000313|EMBL:ACO33263.1, ECO:0000313|Proteomes:UP000002207} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51196 / DSM 11244 / JCM 7670 / NBRC 15755 / NCIMB 13165 / RC 161 {ECO:0000313|Proteomes:UP000002207}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ACO33263.1; -; Genomic_DNA. DR RefSeq; WP_015896163.1; NC_012483.1. DR RefSeq; YP_002754110.1; NC_012483.1. DR ProteinModelPortal; C1F3L2; -. DR STRING; 240015.ACP_1004; -. DR EnsemblBacteria; ACO33263; ACO33263; ACP_1004. DR KEGG; aca:ACP_1004; -. DR PATRIC; 20665359; VBIAciCap40988_0971. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; ACAP240015:GKF4-982-MONOMER; -. DR Proteomes; UP000002207; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002207}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ACO33263.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000002207}; KW Transferase {ECO:0000313|EMBL:ACO33263.1}. SQ SEQUENCE 636 AA; 67859 MW; 027A87CDE87B9586 CRC64; MNNRLKEIFG DRPVLCDGAM GTSLYARGIF INRCFDELNL SQPELVRSVH EDYLQAGAEI IETNTFGANA IRLRRYGLQD KVAEINQAGA RIARAAVAQL ADKQAGNAWV AGSVGPLGVR LEPLGKVGLD EAQAIFAEQI EGLVAGGVDL LVIETMPALN EAQQAIRAAR AVAPELPVIA MVTVDEESRC LDGTAPEVAA ARLAGWGADA VGVNCSTGPA AVLTAIECMA EATDLPLAAM PNAGMPRAVD GRNIYLCSPE YMASFARKFH KSGVQFLGGC CGTTPNHIRA MKSFLRASEA QKAAVQHSRS APIVTETPPA PIEQRSRLGQ MIHDRTFVTM VEIVPPRGID CQKEIDGATM LAGLGVHVIN VPDSPRASAR MSAQSLCIQL QQKSGIETLL HYTCRDRNVL SIQSDLLGAS SIGLRNILCL TGDPPKLGNY PDATAVFDVD AIGLVNIVRR LNHGLDIGGN PIGASTGFTI GCAANPGVPD IDNEVRRFAY KVEAGAEYAI TQPVFDLRIL ESFLKRIEGF RIPVIAGIWP LTSLRNAEFM RNDLRVSVPD SILLRMQQAA TPELARAEGI RIAQEMLETA RPMVEGVQVS APFGRYTAAA EVLAGILPGT SKSDKAQPAS EGMQIG // ID C1F5Y3_ACIC5 Unreviewed; 310 AA. AC C1F5Y3; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 29-APR-2015, entry version 29. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACO33099.1}; GN OrderedLocusNames=ACP_1392 {ECO:0000313|EMBL:ACO33099.1}; OS Acidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / JCM 7670 / OS NBRC 15755 / NCIMB 13165 / 161). OC Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae; OC Acidobacterium. OX NCBI_TaxID=240015 {ECO:0000313|EMBL:ACO33099.1, ECO:0000313|Proteomes:UP000002207}; RN [1] {ECO:0000313|EMBL:ACO33099.1, ECO:0000313|Proteomes:UP000002207} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51196 / DSM 11244 / JCM 7670 / NBRC 15755 / NCIMB 13165 / RC 161 {ECO:0000313|Proteomes:UP000002207}; 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; ACO33099.1; -; Genomic_DNA. DR RefSeq; WP_015896525.1; NC_012483.1. DR RefSeq; YP_002754478.1; NC_012483.1. DR STRING; 240015.ACP_1392; -. DR EnsemblBacteria; ACO33099; ACO33099; ACP_1392. DR KEGG; aca:ACP_1392; -. DR PATRIC; 20666095; VBIAciCap40988_1337. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; YGRSVTK; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; ACAP240015:GKF4-1361-MONOMER; -. DR Proteomes; UP000002207; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002207}; KW Methyltransferase {ECO:0000313|EMBL:ACO33099.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002207}; KW Transferase {ECO:0000313|EMBL:ACO33099.1}. SQ SEQUENCE 310 AA; 33426 MW; F10BECBD65BEF0B3 CRC64; MQPLYHDEFL RIRVLDGGMA TELERRGFNI SGPLWSAHVL DESPEAIQAV HLDYLRAGSD CISTVSYQIS AQGYAELSRP DPAFATALRR SVALAEEARA RYAQENSRPI WIAASLGPYG AALHNGAEFH GNYSITFDDL VEFHRARLAV LAETGADLVA FETIPSLDEA RAILTALTHT PNVSAWLSFT CRDEAHIAHG EPLAACAQLL DSAVQVLALG INCTAPRHVA PLLAAAQSQT RKPVIAYPNS GESWNAATRA WQGRTDLAAE VKDYQTLAGQ WFAAGAQAIG GCCRTTPEHI RAVAAAAVRQ // ID C1F6A7_ACIC5 Unreviewed; 1157 AA. AC C1F6A7; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 29-APR-2015, entry version 50. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACO33904.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ACO33904.1}; GN Name=metH {ECO:0000313|EMBL:ACO33904.1}; GN OrderedLocusNames=ACP_3337 {ECO:0000313|EMBL:ACO33904.1}; OS Acidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / JCM 7670 / OS NBRC 15755 / NCIMB 13165 / 161). OC Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae; OC Acidobacterium. OX NCBI_TaxID=240015 {ECO:0000313|EMBL:ACO33904.1, ECO:0000313|Proteomes:UP000002207}; RN [1] {ECO:0000313|EMBL:ACO33904.1, ECO:0000313|Proteomes:UP000002207} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51196 / DSM 11244 / JCM 7670 / NBRC 15755 / NCIMB 13165 / RC 161 {ECO:0000313|Proteomes:UP000002207}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001472; ACO33904.1; -; Genomic_DNA. DR RefSeq; WP_015898370.1; NC_012483.1. DR RefSeq; YP_002756336.1; NC_012483.1. DR STRING; 240015.ACP_3337; -. DR EnsemblBacteria; ACO33904; ACO33904; ACP_3337. DR KEGG; aca:ACP_3337; -. DR PATRIC; 20669871; VBIAciCap40988_3193. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; ACAP240015:GKF4-3284-MONOMER; -. DR Proteomes; UP000002207; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002207}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACO33904.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002207}; KW Transferase {ECO:0000313|EMBL:ACO33904.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 735 735 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1157 AA; 127610 MW; BBDC603924E4856B CRC64; MSDFLEALKQ RVLVYDGAMG TNIQKHALTL DDYWGKEGCN ELLVLSRPDI IRDIHASFFA VGCDVVETDS FGSSRIVLAE YDLQDQTREL NIAAAKLARE VADSFSTPDR PRFVAGSIGP TTKLPSLGHI SYDDMALTYR EQIEALIEGG VDVLLIETAQ DLLQAKIALA ACHDAMRATG RHLPIQMQVT IEATGTMLLG TEIGAALATL ECFDPDIIGL NCATGPAEMN DAVRFLCQNA TRPVSVLPNA GLPQNVGGHA VYALTPEELA KYHRSFVTEY GVQVVGGCCG TTPEHLKAVV EAVKDAKPAP RHVQPQSVAA SAFSALPLEV DGQPVIVAEE MNTTTRVEHF RNMVRAGDYD GILALAKKLV AEGSQMLDLC CAIVGEDEKA YMCSVLEKIA TRVTAPILVD STEADVIEEG LKRIPGKPVI NSINLEDGEK RTSQVLPMAK RYGAAVIALT IDEDGMALTA EKKVAVARRI HDLAVNKYGL RPQDLIFDPL TLPISTGQED YRTAGIETLE AVRRIKQEIP YVKTILGVSN ISFGLNAYAR RVLNSVFLKE AVDRGLDSAI VNYSKIYPLY KIPEREVELA RRLVFYDTVE GDPLQAYMAH FAGTKGKVQD DSEELASLPV DETLKQLIIR GERSVGSGSN KRSLEEVLES ALTDWKPLDL INDVLLDGMK TVGELFGARK MQLPSVLDSA AVMKAAVAYL EPKMERVEGS QRGTIVLATV KGDVHDIGKN LVDIILSNNG FKVVNLGIKQ PADTIIQAAR EHKADAIGLS GLLVKSTLEM KYVVQDMQRL AMEIPVICGG AALTRKYVEE DLRQEYSQGV FYAEDAFAGL HVMTDITSEE ALREARMSEG RTVKVFPKKP VVEVSAVDAA APVVRSSWVT ENPEVPVPPF FGVRVKKDYD LDTVFEYINE IALFKNQWQL KTASATDYAR LVEEKYRPVL EELKTEVKRE GWFHPQMVYG FFPAQSEGND LIVYDAEDPA KERLRITFPR QAEGRKLSIA DFFRPKSEGV YDVVGFSVVT IGHEASEVTK RLFDAGDFTR YLYLHGLSVE TAEALAELAH REIRQDLGIA GEDAPRINDL FHQKYRGSRY SFGYPACPNL EDQTKIFELL EPEKNIGVRL TEGFHLEPEQ STNALIVHHP QAKYFVV // ID C1FN90_CLOBJ Unreviewed; 792 AA. AC C1FN90; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 29-APR-2015, entry version 40. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:ACO84091.1}; GN OrderedLocusNames=CLM_1865 {ECO:0000313|EMBL:ACO84091.1}; OS Clostridium botulinum (strain Kyoto / Type A2). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=536232 {ECO:0000313|EMBL:ACO84091.1, ECO:0000313|Proteomes:UP000001374}; RN [1] {ECO:0000313|EMBL:ACO84091.1, ECO:0000313|Proteomes:UP000001374} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Kyoto / Type A2 {ECO:0000313|Proteomes:UP000001374}; 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 ----------------------------------------------------------------------- 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; ACO84091.1; -; Genomic_DNA. DR RefSeq; WP_012704039.1; NC_012563.1. DR RefSeq; YP_002804042.1; NC_012563.1. DR ProteinModelPortal; C1FN90; -. DR STRING; 536232.CLM_1865; -. DR EnsemblBacteria; ACO84091; ACO84091; CLM_1865. DR KEGG; cby:CLM_1865; -. DR PATRIC; 19380233; VBICloBot91161_1742. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CBOT536232:GCO3-1799-MONOMER; -. DR Proteomes; UP000001374; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001374}; KW Methyltransferase {ECO:0000313|EMBL:ACO84091.1}; KW Transferase {ECO:0000313|EMBL:ACO84091.1}. SQ SEQUENCE 792 AA; 87751 MW; EBD5CB48243C063C CRC64; MNIKDYIKEN VLIFDGAMGT MLQKLGLKIS DLPEELNILE PEKIINIHRK YIETGAKVIT TNTFGANEIK LKQSKFSLES IIDKAIDNVK KAGKNKEILI ALDIGPIGQL LEPMGTLKFE EAYEIFKRQI VQGQKSGADI VLIETMTDLY EAKAAILAAK ENTNLPVFCT MTFEKNKRTF TGCTPLSMVL TLEGLGVDAL GVNCSLGPNE LGDIVDEIIK YSSIPIMVQP NAGLPTIKAG RTIYNIEPKE FADFQRSIVE KGVRIVGGCC GTTDEFIREI VYSLKDVKIK KLKEKNICGV CSSTKSVLIE GVKIIGERIN PTGKRLFKEA LRNNDTDYIL KEAISQVECG TDILDVNVGL PEINEEETMK KVVKEIQSII DAPLQIDSNN PKVIEKALRV YNGKAIVNSV NGEEEVLDSV LPLIKKYGAA VVGLTLDDKG IPKKAEERLK VAEKIVNKAL EYGIRREDIF IDCLVLTASA QQGDVGETLK AVNLVKEKLN VKTILGVSNI SFGLPNRELI NKTFLAMSLQ SGLDLPILNP NNKEMINIIN AYKVLNNEDK RAANYIERYT NEISNSREVK IPKNDLTLKE IVMKGIKEES YSKTKDLLKD RGELSIINEE LIPALDEVGD KYEKGIIFLP QLIQSAETVK KAFTAIKEKL REDNSPKINK GKILMATVKG DIHDIGKNIV KVILENYGFD IIDLGKDVEA EKIVEEVKKN NIKLVGLSAL MTTTVNSMKD TIKALKESEM DCKVFVGGAV LNKEYAEMIN ADYYAKDAKE AVDIAKGFFG GF // ID C1MHB3_MICPC Unreviewed; 1222 AA. AC C1MHB3; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 01-APR-2015, entry version 42. DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EEH60712.1}; GN ORFNames=MICPUCDRAFT_45154 {ECO:0000313|EMBL:EEH60712.1}; OS Micromonas pusilla (strain CCMP1545) (Picoplanktonic green alga). OC Eukaryota; Viridiplantae; Chlorophyta; prasinophytes; Mamiellophyceae; OC Mamiellales; Mamiellaceae; Micromonas. OX NCBI_TaxID=564608 {ECO:0000313|Proteomes:UP000001876}; RN [1] {ECO:0000313|EMBL:EEH60712.1, ECO:0000313|Proteomes:UP000001876} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCMP1545 {ECO:0000313|EMBL:EEH60712.1, RC ECO:0000313|Proteomes:UP000001876}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG663735; EEH60712.1; -; Genomic_DNA. DR RefSeq; XP_003055460.1; XM_003055414.1. DR GeneID; 9680882; -. DR KEGG; mpp:MICPUCDRAFT_45154; -. DR KO; K00548; -. DR Proteomes; UP000001876; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001876}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001876}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 238 238 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 301 301 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 302 302 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 744 744 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1222 AA; 135043 MW; D2EFC2FC3449C4B4 CRC64; MKERIMVIDG AMGTAVQKYK LQEEDFRGER YKNHTHDLKG NNDILVITRP DVVEEIHSKY LAAGADIIET NTFNATMISQ ADYELDKKEE VYLINKTAAQ LAKKCCVAFT KKNPKKPRFA AGAVGPTNKT LSVSPSVENP AFRGCTYDEI VEAYMEQVEA LVEGGVDMLL VETIFDTLNA KAAMFAIDLF FEKWGKKIPV FVSGTIVDNS GRTLSGQTNE AFWNSMSHSK PIAIGLNCAL GAKDMVPYIE NLSKAADCWV FCYPNAGLPN AMGGYDQKGP EMAEDCRVFP EMNLINAIGG CCGTTDEHIG CLAEMVSKFK PREKHGVKDI MRLSGLQPFN YDPDDEKNCR KTFINLGERC NVAGSSIFKK AIVDGNYEKA LAIALKQVEN GAHVIDVNMD DGLIDGESAM IRFVNLMVSE PDVSKVPFMI DSSKFHVVEA GLKCSQGKCI MNSISLKGGQ EEFLKHARTV KRHGAAVVVM AFDEEGQAAT ESEKVRICMR AYKLLVEEVG FNPQDIIFDP NILTIGTGME EHNNYGVDFI NATREIKRLC PGSKISGGVS NLAFSFRGNE PVRRAFHSAF LYHACKAGMD MGIVNAAQVE EDVYEKIDKE LLEYVEDVLL NKCSNATERM LENQPVGKRL EHALVKGIDE FCIADTEECR VGGDYPGPLQ IIEGPLMDGM NVVGDLFGAG KMFLPQVIKS ARVMKKSVGH LIPFMEEERL ANGGTGEAAN AGVFLIATVK GDVHDIGKNI VAVVLGCNNF KVIDIGVMCP KDKIIAALKD NNADICGLSG LITPSLDEMV DMAKAMEAEG MKIPLLIGGA TTSKMHTAVK LAPNYSGGVV HVLDASRAVP VAQTLMDMNK RGEFLEDILD TYAEMREEFY AGLEDRRYLT ISQARATAEK AAVDFSSPEH LPVTPKFCGV KALVDVPIAD VIDYVDWNPF FQVWQLRGRY PNRGYPKIFN DETVGAEAKK LFEEANAMLK MIMEKKRLKL NGIIGFYPAN SVGDDIELYA DENRGEKTHT FHTLRQQAEK DVDEPYMALS DFIAPKESGV KDYLGMFVAT AGIGLDELTA EYKAANDDYS YIMAEALADR LAEAFAELMH EQVRKDHWGY AKDEKFDASD LLKVKYQGIR PAPGYPSQPD HTEKATMWDL MNVKEEISVE LTESFAMLPS ASVSGLYFAG KSSQYFNVGK ITADQVQEYA DRKKQDYKVA EKWLSPILSY EP // ID C2CQL6_CORST Unreviewed; 295 AA. AC C2CQL6; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 01-OCT-2014, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEI78016.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EEI78016.1}; GN Name=mmuM {ECO:0000313|EMBL:EEI78016.1}; GN ORFNames=HMPREF0308_1695 {ECO:0000313|EMBL:EEI78016.1}; OS Corynebacterium striatum ATCC 6940. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=525268 {ECO:0000313|EMBL:EEI78016.1}; RN [1] {ECO:0000313|EMBL:EEI78016.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 6940 {ECO:0000313|EMBL:EEI78016.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEI78016.1}. 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; ACGE01000080; EEI78016.1; -; Genomic_DNA. DR EnsemblBacteria; EEI78016; EEI78016; HMPREF0308_1695. DR PATRIC; 27672351; VBICorStr83233_0239. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEI78016.1}; KW Transferase {ECO:0000313|EMBL:EEI78016.1}. SQ SEQUENCE 295 AA; 31830 MW; 11C67DB1152B5DB1 CRC64; MRRLLVRLQR MKCFETPLIF DGGLGTHLES RGNDISGQLW SAQILRENPA EIQAAHEDFY RAGAQVATTA SYQVTFDALG DEAEELLRRS VEVARVAANN ARPDGLVAAS VGPYGAGPGE GTDYDGAYGL GCEELKHWHQ RRIEVLAATD ADFLLAETIP NVDEAAALLE LLDATGKPYA LSVTGVLAAD PAKVAQVIEF AKQARNLGAL GVNCCDAETA KGVVKRMREG IDLPVLAYPN SGETWDHAAR QWRRDEEHSL GLVEAAPQLR ALGVTLLGGC CRTTPEQIRL ISQQA // ID C2CY68_LACBR Unreviewed; 315 AA. AC C2CY68; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEI72373.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EEI72373.1}; GN Name=mmuM {ECO:0000313|EMBL:EEI72373.1}; GN ORFNames=HMPREF0496_0240 {ECO:0000313|EMBL:EEI72373.1}; OS Lactobacillus brevis subsp. gravesensis ATCC 27305. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=525310 {ECO:0000313|EMBL:EEI72373.1}; RN [1] {ECO:0000313|EMBL:EEI72373.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27305 {ECO:0000313|EMBL:EEI72373.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEI72373.1}. 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; ACGG01000010; EEI72373.1; -; Genomic_DNA. DR RefSeq; WP_003550872.1; NZ_GG669604.1. DR EnsemblBacteria; EEI72373; EEI72373; HMPREF0496_0240. DR PATRIC; 30188286; VBILacBre13134_1121. DR OrthoDB; EOG6C019S; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEI72373.1}; KW Transferase {ECO:0000313|EMBL:EEI72373.1}. SQ SEQUENCE 315 AA; 34770 MW; C261EF067F8693A8 CRC64; MTDLIKENLD SKRALVLDGA MATELEKHGV DTSNDLWSAT ALINDPDAVK AVHTSYFEAG ADITITDTYQ ANVEAFKKVG FTEDQSEKLI TEAVRLALES RDDFYATLPT AERAKRALYP LVAGSVGPYG AYLADGSEYT GHYQLTNEAY QTFHQRRMRL MDEAGVDVFA FETQPNFEET KALADLLREK FSDRFAWLTF SIKDPEHLCD GTSLAKAVSY FEDNPQISAV GVNCTSMNLI EDSIKTIASN TNKPIIVYPN NGDIYDPKTK TWTPNPNATT FAELTPKWLA AGAKIVGGCC RTTPADIEQV AESLF // ID C2EGM1_9LACO Unreviewed; 307 AA. AC C2EGM1; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEJ74293.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EEJ74293.1}; GN Name=mmuM {ECO:0000313|EMBL:EEJ74293.1}; GN ORFNames=HMPREF0545_0793 {ECO:0000313|EMBL:EEJ74293.1}; OS Lactobacillus salivarius DSM 20555 = ATCC 11741. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423799 {ECO:0000313|EMBL:EEJ74293.1}; RN [1] {ECO:0000313|EMBL:EEJ74293.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 11741 {ECO:0000313|EMBL:EEJ74293.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEJ74293.1}. 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; ACGT01000005; EEJ74293.1; -; Genomic_DNA. DR RefSeq; WP_003700965.1; NZ_GG693225.1. DR EnsemblBacteria; EEJ74293; EEJ74293; HMPREF0545_0793. DR PATRIC; 29215430; VBILacSal82003_1366. DR OrthoDB; EOG6C019S; -. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EEJ74293.1}; KW Transferase {ECO:0000313|EMBL:EEJ74293.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 223 223 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 307 AA; 34497 MW; 4ECCFECCD25BA185 CRC64; MDFTEFLTNN PVVLDGAMST PLERLGADTN NDLWTAKALI DNEELVYEVH KMYFEAGADL IITDTYQANV QAFEKVGYSE KEARNLIKKA VKIAQKARDD YENRTGKHNY IAGTIGPYGA YLANGSEYRG DYELSVEEYQ QFHLPRIEEL VNAGVDILAI ETQPKLDEVL AILELLKKKY PQQKVYVSYT LSDDDTISDG TPLPRAIHAL EDYSQVIAVG INCVKLELVE PALKNMKEIT DKHLIVYPNS SAVYDPKSKT WSQPKTSATF EELIPNWYEA GARIIGGCCT TGPKEIKAVA DFIKRNR // ID C2EMY5_9LACO Unreviewed; 328 AA. AC C2EMY5; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEJ72113.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EEJ72113.1}; GN Name=mmuM1 {ECO:0000313|EMBL:EEJ72113.1}; GN ORFNames=HMPREF0548_1045 {ECO:0000313|EMBL:EEJ72113.1}; OS Lactobacillus ultunensis DSM 16047. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=525365 {ECO:0000313|EMBL:EEJ72113.1}; RN [1] {ECO:0000313|EMBL:EEJ72113.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 16047 {ECO:0000313|EMBL:EEJ72113.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEJ72113.1}. 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; ACGU01000047; EEJ72113.1; -; Genomic_DNA. DR RefSeq; WP_007125573.1; NZ_GG693253.1. DR EnsemblBacteria; EEJ72113; EEJ72113; HMPREF0548_1045. DR PATRIC; 29217708; VBILacUlt69912_0307. DR OrthoDB; EOG6C019S; -. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EEJ72113.1}; KW Transferase {ECO:0000313|EMBL:EEJ72113.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 220 220 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 328 AA; 37099 MW; B413844642D11BFB CRC64; MNLINQISNK GLILDGAMST ALEKQGIDTN NDLWTAIALE KDLDKVHMDY FKAGAQMTIT DTYQANVQAF KKHGYTEEQA EDMIAKAVEI AKQARDDYEK KTGIHNFVAA SVGSYGAYLA RGDEFRGDYK LTSKQYLNFH LPRLKVLLKN KPDCLAIETQ PKLEEVVAIL DWLKANSPQI PVYVSFTLHD TTKISDGTPL KQAMQKLNEY NQVFAVGANC FKPFLATAAI DKMKEFTKKA IIIYPNLGGV YDEFQRNWIP FNAKFDFRKL SQEWYEHGAR IIGGCCSTGI KEVGQIATFY KTISSQKSKQ KENLNLNNDL MKFRSSNI // ID C2EN27_9LACO Unreviewed; 322 AA. AC C2EN27; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEJ72069.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EEJ72069.1}; GN Name=mmuM2 {ECO:0000313|EMBL:EEJ72069.1}; GN ORFNames=HMPREF0548_1073 {ECO:0000313|EMBL:EEJ72069.1}; OS Lactobacillus ultunensis DSM 16047. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=525365 {ECO:0000313|EMBL:EEJ72069.1}; RN [1] {ECO:0000313|EMBL:EEJ72069.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 16047 {ECO:0000313|EMBL:EEJ72069.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEJ72069.1}. 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; ACGU01000049; EEJ72069.1; -; Genomic_DNA. DR RefSeq; WP_007125601.1; NZ_GG693253.1. DR EnsemblBacteria; EEJ72069; EEJ72069; HMPREF0548_1073. DR PATRIC; 29217758; VBILacUlt69912_0332. DR OrthoDB; EOG6C019S; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEJ72069.1}; KW Transferase {ECO:0000313|EMBL:EEJ72069.1}. SQ SEQUENCE 322 AA; 36476 MW; 99A0EC287FDB023B CRC64; MSAFLFLLKN EKEVGRMSLI DDAKSGIVLD GAMSDELEKQ GVETDNKLWT ATALVDQLNK VYNAHQDYFR AGAELVITDT YQANVQAFEE AGYSEKEAEK FIKNAVKIAK KARDDYQKET GKHNYVAGTI GSYGAFLADG NEYRGEYNLS EKEYLDFHLP RLKLVLEEKP DLIALETQPK ITEPVAVLNW LQKNHSNIPV YVSFTLKDTK HISDGTSIEQ ATQEVSKYKQ VFAIGINCVS PKLVDQALKE FAKYTAKPLV VYPNLGATYD PKIKKWRSFK EKFDFAELTQ KWYEDGARLI GGCCTTGPKE IKEIRQSIDK LR // ID C2ET26_9LACO Unreviewed; 75 AA. AC C2ET26; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EEJ40941.1}; DE Flags: Fragment; GN ORFNames=HMPREF0549_0612 {ECO:0000313|EMBL:EEJ40941.1}; OS Lactobacillus vaginalis DSM 5837 = ATCC 49540. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423814 {ECO:0000313|EMBL:EEJ40941.1}; RN [1] {ECO:0000313|EMBL:EEJ40941.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 49540 {ECO:0000313|EMBL:EEJ40941.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEJ40941.1}. 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; ACGV01000099; EEJ40941.1; -; Genomic_DNA. DR RefSeq; WP_003718027.1; NZ_GG693497.1. DR EnsemblBacteria; EEJ40941; EEJ40941; HMPREF0549_0612. DR OrthoDB; EOG6091CH; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; FT NON_TER 75 75 {ECO:0000313|EMBL:EEJ40941.1}. SQ SEQUENCE 75 AA; 8240 MW; 368A1957686D56A6 CRC64; MRHAEALTFG LNCALGPDEL RQYVQELSRI AECYVTAHPN AGLPNAFGEY DLDADTMAKQ IREWAQAGFL NIVGG // ID C2HTK7_VIBAB Unreviewed; 1226 AA. AC C2HTK7; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 38. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEO03681.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEO03681.1}; GN ORFNames=VCA_002692 {ECO:0000313|EMBL:EEO03681.1}; OS Vibrio albensis VL426. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=593585 {ECO:0000313|EMBL:EEO03681.1}; RN [1] {ECO:0000313|EMBL:EEO03681.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=VL426 {ECO:0000313|EMBL:EEO03681.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEO03681.1}. 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; ACHV01000001; EEO03681.1; -; Genomic_DNA. DR RefSeq; WP_000514265.1; NZ_ACHV01000001.1. DR EnsemblBacteria; EEO03681; EEO03681; VCA_002692. DR PATRIC; 30089589; VBIVibCho6562_1671. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEO03681.1}; KW Transferase {ECO:0000313|EMBL:EEO03681.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1226 AA; 135782 MW; 8A185A38CA0D8F0F CRC64; MGKEVRQQLE QQLKQRILLI DGGMGTMIQS YKLQEEDYRG ARFVDWHCDL KGNNDLLVLT QPQIIKEIHS AYLEAGADIL ETNTFNSTTI AMADYDMQSL SAEINFAAAK LAREVADEWT AKDPSRPRYV AGVLGPTNRT CSISPDVNDP GFRNVTFDGL VEAYSESTRA LIKGGSDLIL IETIFDTLNA KACAFAVDSV FEELGISLPV MISGTITDAS GRTLSGQTTE AFYNALRHVR PISFGLNCAL GPDELRQYVE ELSRISECYV SAHPNAGLPN AFGEYDLSAE EMAEHIAEWA QAGFLNLVGG CCGTTPEHIA AIAKAVEGVK PRALPDLKVE CRLSGLEPLN IGPETLFVNV GERTNVTGSA RFKRLIKEEQ YDEALDVARE QVENGAQIID INMDEGMLDA EACMVRFLNL CASEPEISKV PVMVDSSKWE VIEAGLKCIQ GKGIVNSISL KEGKEKFIAQ AKLVRRYGAA VIVMAFDEVG QADTRERKLE ICRRAYHILV DEVGFPPEDI IFDPNIFAVA TGIDEHNNYA LDFINAVADI KRELPHAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK HGMDMGIVNA GQLEIYDNVP LKLREAVEDV ILNRRSDGTE RLLEIAEAYR ENSVGKEEDA SALEWRAWPV AKRLEHALVK GITEFIVQDT EEARQQATKP LEVIEGPLMD GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AYLEPFINAQ KSGSTSNGKI LLATVKGDVH DIGKNIVGVV LQCNNFEIID LGVMVPCEQI LKVAREQNVD IIGLSGLITP SLDEMVHVAK EMERQGFELP LLIGGATTSK AHTAVKIEQN YHAPVVYVNN ASRAVGVCTS LLSDELRPGF IERLDLDYER TRDQHARKTP KSRPVTLEQA RANKAALDWA NYTPPAPAKP GVHVFENIAL ATLRPYIDWT PFFMTWSLMG KYPAILEHEE VGEEAKRLFH DANALLDKVE REGLLKASGM CALFPAASLG DDIEVYSDES RTQVAHVLYN LRQQTEKPKG ANYCLSDYVA PKESGKRDWI GAFAVTGGIG ERALADAYKA QGDDYNAIMI QAVADRLAEA FAEYLHEKVR KEIWGYASDE NLSNDELIRE RYQGIRPAPG YPACPEHTEK ATLWQMLNVE ETIGMSLTTS YAMWPGASVS GWYFSHPDSR YFAVAQIQQD QLHSYAERKG WSLEEAEKWL APNLDA // ID C2KF75_9LACO Unreviewed; 329 AA. AC C2KF75; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEJ69425.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EEJ69425.1}; GN Name=mmuM {ECO:0000313|EMBL:EEJ69425.1}; GN ORFNames=HMPREF0506_1500 {ECO:0000313|EMBL:EEJ69425.1}; OS Lactobacillus crispatus JV-V01. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=491076 {ECO:0000313|EMBL:EEJ69425.1, ECO:0000313|Proteomes:UP000005415}; RN [1] {ECO:0000313|EMBL:EEJ69425.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=JV-V01 {ECO:0000313|EMBL:EEJ69425.1}; 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 (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. {ECO:0000313|EMBL:EEJ69425.1}. 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; ACKR01000173; EEJ69425.1; -; Genomic_DNA. DR RefSeq; WP_005719570.1; NZ_GG669818.1. DR EnsemblBacteria; EEJ69425; EEJ69425; HMPREF0506_1500. DR GeneID; 9107864; -. DR PATRIC; 30711243; VBILacCri16252_0955. DR OrthoDB; EOG6C019S; -. DR Proteomes; UP000005415; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005415}; KW Methyltransferase {ECO:0000313|EMBL:EEJ69425.1}; KW Transferase {ECO:0000313|EMBL:EEJ69425.1}. SQ SEQUENCE 329 AA; 37079 MW; AC5A97247149A998 CRC64; MNLLKQIRDR GLILDGAMST ALEKLGIDTN NELWTAIALE HNLAQIYQVH MNYFKAGAQM AITDTYQANI PAFEKHGFTQ DQATKLITNA VQIAKKARDD FAKTTGIHNY VAASVGPYGA YLAQGDEFRG DYSLTTEEYL NFHLPRLKIL LANKPDCLAL ETQPKLDEVV AILDWLKENA PEIPVYVSFT LHDTTKISDG TPLKRVVQKL NEYDQVFAIG ANCFKPFLAT AVIDKIHDFT DKQIVIYPNL GGVYNEFERN WIPFNAKFDF KKLSQEWYEH GARIIGGCCS TTEKEIGQIS AFFKTINNAK SKSVKSELKK VKNDSNIQI // ID C2LM17_PROMI Unreviewed; 1225 AA. AC C2LM17; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 34. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEI47151.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEI47151.1}; GN Name=metH {ECO:0000313|EMBL:EEI47151.1}; GN ORFNames=HMPREF0693_2907 {ECO:0000313|EMBL:EEI47151.1}; OS Proteus mirabilis ATCC 29906. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Proteus. OX NCBI_TaxID=525369 {ECO:0000313|EMBL:EEI47151.1, ECO:0000313|Proteomes:UP000006419}; RN [1] {ECO:0000313|EMBL:EEI47151.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29906 {ECO:0000313|EMBL:EEI47151.1}; 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 (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEI47151.1}. 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; ACLE01000069; EEI47151.1; -; Genomic_DNA. DR EnsemblBacteria; EEI47151; EEI47151; HMPREF0693_2907. DR PATRIC; 36136907; VBIProMir92659_2598. DR Proteomes; UP000006419; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006419}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEI47151.1}; KW Transferase {ECO:0000313|EMBL:EEI47151.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1225 AA; 135697 MW; 7796B79330A80F37 CRC64; MTMITQQLTQ ALAKRILVLD GAMGTMIQQY QLAEEDYRGE RFAHWQCDVK GNNDLLVLTQ PQIITEIHNA YFEAGADIVE TNTFNATSIA MADYQMEGLC AELNEEAAKL ARACADKWSA LTPDKPRYVA GVLGPTNRTA SISPDVNDPA FRNISFDTLV MAYREAICGL IKGGVDLIMV ETIFDTLNAK AAIFAIKCEF DNLNIELPVM ISGTITDASG RTLTGQTTEA FYHSLRHADA LSFGLNCALG PKELRQYIQT LSQISETYVS AHPNAGLPNA FGGYDLDANE MAEQIKEWAQ AGFLNIVGGC CGTTPAHIQA IAQAVDGIAP RTLPVIKKAC RLSGLEPLVI DDNSLFVNVG ERTNVTGSAK FKRLIKEGNY QEALDVARQQ VENGAQIIDI NMDEGMLDAI EAMTRFLNLI AGEPDIAKVP IMIDSSKWQV IEEGLKCIQG KGIVNSISMK EGEALFIEHA KLVRKYGAAV VVMAFDEIGQ ADTRERKIEI CQRAYHLLTE KAGFPPEDII FDPNIFAVAT GIAEHNNYAV DFIEVCADIK SQLPYALISG GVSNVSFSFR GNDPVREAIH SVFLYYAVKN GMDMGIVNAG QLAIYDSLPD ELRNAVEDVI LNRHAESTDN LLALAERYRG TKSEEQHSTL AQWRQWEVEK RLEYALVKGI TEFIIEDTEA CRQQASSPIE VIEGPLMNGM NTVGDLFGEG KMFLPQVVKS ARVMKQAVAY LEPYIQATKK AGSSAGKVLL ATVKGDVHDI GKNIVGVVLQ CNNYEIIDLG VMVPCDKILQ TAIDEHVDII GLSGLITPSL DEMVNVAKEM ERRGFSLPLM IGGATTSKAH TAVKIEPNYS HPTVYVQNAS RTVGVVAALL SATQKADFVA KTRREYEVVR QQYARKKPRT PPVSLATARA NALQLDWQHY TPPKPNQLGV QQVTANIETL REYIDWTPFF MTWSLAGKYP RILEDEVVGE EARRVFADAN AMLDKLSREK LLTPKGIVGL FPANRLGDDI IIYQDETRQH ELLRCCHLRQ QTEKKEYPNY CLADFIAPVD SGLADYFGAF AVTGGLEEDA LANGYDNAHD DYNKIMVKAL SDRLAEAFAE YLHQQVRTKI WGYSPDEALS NDELIREKYQ GTRPAPGYPA CPEHTEKAKI WQLLNVENRI GMKLTDAYAM WPGASVSGWY FSHPESKYFA VAQIQKDQVE DYAKRRGMSM SEVERWLAPN LGYEP // ID C2LUX8_STRSL Unreviewed; 316 AA. AC C2LUX8; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEK09093.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EEK09093.1}; GN ORFNames=STRSA0001_0856 {ECO:0000313|EMBL:EEK09093.1}; OS Streptococcus salivarius SK126. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=596322 {ECO:0000313|EMBL:EEK09093.1}; RN [1] {ECO:0000313|EMBL:EEK09093.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK126 {ECO:0000313|EMBL:EEK09093.1}; RA Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Strausberg R.L., Nelson K.E.; 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. {ECO:0000313|EMBL:EEK09093.1}. 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; ACLO01000092; EEK09093.1; -; Genomic_DNA. DR RefSeq; WP_002885890.1; NZ_ACLO01000092.1. DR EnsemblBacteria; EEK09093; EEK09093; STRSA0001_0856. DR GeneID; 10972247; -. DR PATRIC; 29725058; VBIStrSal51046_1777. DR OrthoDB; EOG6C019S; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEK09093.1}; KW Transferase {ECO:0000313|EMBL:EEK09093.1}. SQ SEQUENCE 316 AA; 34854 MW; AEE493FE5A69C341 CRC64; MAIFKDYLEN KSPLILHGAL GTEMESLGYD ISGKLWSAKY LLDKPEVIQK IHETYVAAGS DLITTSSYQA TLPGLIDAGL TEKEAEQIIA LTVQLAKNAR DKVWATLDDS EKAKRPYPLI SGDVGPYAAY LANGSEYTGD YGRITIKELK EFHRPRIQIL LDQGVDLLAL ETIPNHLEAQ ALIELLAEEF PEAEAYISFT VQEPGTISDG TSLDEITQLV SQSDQILALG INCSSPLLYN QALTILKNAG KALITYPNSG EVYDGSTQTW KPKDKDALTL VEHSKDWHDQ FGVKILGGCC RTRPNDIKAL YAEFRT // ID C2MQP2_BACCE Unreviewed; 1132 AA. AC C2MQP2; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEK43194.1}; GN ORFNames=bcere0001_39120 {ECO:0000313|EMBL:EEK43194.1}; OS Bacillus cereus m1293. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526973 {ECO:0000313|EMBL:EEK43194.1, ECO:0000313|Proteomes:UP000002290}; RN [1] {ECO:0000313|EMBL:EEK43194.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M1293 {ECO:0000313|EMBL:EEK43194.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEK43194.1}. 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; ACLS01000100; EEK43194.1; -; Genomic_DNA. DR RefSeq; WP_000649711.1; NZ_CM000714.1. DR EnsemblBacteria; EEK43194; EEK43194; bcere0001_39120. DR PATRIC; 25124703; VBIBacCer121715_0069. DR Proteomes; UP000002290; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002290}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 125858 MW; 19B5E60B4746DC8E CRC64; MKCIEEKLQN NILLLDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYELSHLDE ELNEKAARLA KQAVEESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGE VDVLLVETSQ DMRNVKAAYI GIQAAFDELN TVVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWVN IIGGCCGTTP EHIKAMKSAL TSLKPREQQE RAGHGVSGLE ALQYDDSMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEI ARAQVKKNAH IIDICMADPD RDEIEDMENF LAEVTKVLKV PIMIDSTDEH VMERALTYIQ GKAVINSINL EDGEERFKKV TPLLRKYGAA IVVGTIDEDG MAVSAERKLE IAKRSYELLT TKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASISDE EKRLADALLF ETTQETLEKF TNFYRVAKKK DVVVQETLTL DERLANYIVE GTKQGLHEDL SLALTEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILA NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAADIDIPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV TKEEKKVEIP AVIEPLPKAE VIVPDSTKRI VLRDVPVSHL APFLNRQMLL GHHLGLKGSV KKLLREGDKR AHELNDLIDE LLQEGQSWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRVIE RFTFPRQGKA PYRTLGDYLR PVGDEMDYVA FLSVTVGEGV REIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID C2MQP3_BACCE Unreviewed; 610 AA. AC C2MQP3; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 31. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=bcere0001_39130 {ECO:0000313|EMBL:EEK43195.1}; OS Bacillus cereus m1293. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526973 {ECO:0000313|EMBL:EEK43195.1, ECO:0000313|Proteomes:UP000002290}; RN [1] {ECO:0000313|EMBL:EEK43195.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M1293 {ECO:0000313|EMBL:EEK43195.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEK43195.1}. 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; ACLS01000100; EEK43195.1; -; Genomic_DNA. DR RefSeq; WP_000770334.1; NZ_CM000714.1. DR EnsemblBacteria; EEK43195; EEK43195; bcere0001_39130. DR PATRIC; 25124705; VBIBacCer121715_0070. DR Proteomes; UP000002290; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002290}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 610 AA; 67182 MW; D604353A7C299F2C CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNISDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTE INRAAVKLAK ASVTDRNAIL GTIGGMKHIG AVTTTDMERE FMLLEQASAL LEEQVDGLLL ETFYDEFELL HAVQVLRKET NIPIVAQLAL HEAGTTQNGN DVNEILKQLL DYGANVVGLN CQLGPLHMTE AFKMISIPKN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPKFIEQGI RLLGGCCGTT PEHIESMKRA TLNVTPVIEK DTVQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRISNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSVL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIA LIEEVYEATK HLEQPIFIGI MPLISKRNAD FLHFEVPGIT LPEAVRERMD GHETKEAAIE EGIRISQELI DAAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID C2N6C4_BACCE Unreviewed; 1132 AA. AC C2N6C4; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 39. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEK48897.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:KFL77790.1}; GN Name=metH {ECO:0000313|EMBL:KFL77790.1}; GN ORFNames=bcere0002_41170 {ECO:0000313|EMBL:EEK48897.1}, GN DJ50_3586 {ECO:0000313|EMBL:KFL77790.1}; OS Bacillus cereus ATCC 10876. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526980 {ECO:0000313|EMBL:EEK48897.1, ECO:0000313|Proteomes:UP000001484}; RN [1] {ECO:0000313|EMBL:EEK48897.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 10876 {ECO:0000313|EMBL:EEK48897.1}; 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] {ECO:0000313|EMBL:KFL77790.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 10876 {ECO:0000313|EMBL:KFL77790.1}; RA Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O., Coyne S.R., RA Daligault H.E., Davenport K.W., Erkkila T., Frey K.G., Gibbons H.S., RA Gu W., Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C., RA Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N., RA Scholz M.B., Teshima H., Xu Y.; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEK48897.1}. 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; ACLT01000089; EEK48897.1; -; Genomic_DNA. DR EMBL; JMPW01000022; KFL77790.1; -; Genomic_DNA. DR RefSeq; WP_000649680.1; NZ_KN050654.1. DR ProteinModelPortal; C2N6C4; -. DR EnsemblBacteria; EEK48897; EEK48897; bcere0002_41170. DR EnsemblBacteria; KFL77790; KFL77790; DJ50_3586. DR PATRIC; 24865739; VBIBacCer12024_5301. DR Proteomes; UP000001484; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001484}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:KFL77790.1}; KW Transferase {ECO:0000313|EMBL:KFL77790.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 126077 MW; B43BAF17DBF75588 CRC64; MKCIEEKLKN SILILDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYELSHLDE ELNEKAALLA KQAVKESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGE VDVLLVETSQ DMRNVKAAYI GIQAAFEELK KTVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWVN IIGGCCGTTP EHIKAMKSAL ASLKPRDHHE REGHGISGLE ALQYDESMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMENF LAEVTKVLKV PIMIDSTDEN VMERALTYIQ GKAVINSINL EDGEERFKKV TPLLQKYGAT IVVGTIDEDG MAVSAERKIE IAKRSYELLT KKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPQE EKRLADALLF ETTKETLEEF TNFYRVAKKK DIVVQETLTL DERLANYIVE GTKQGLHEDL SLALEEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKSDVHDI GKNLVEIILA NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAANIDVPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV KKEEKKVEIP AVIEPLPKAE VIVPDSTKRI VLRDIPAFHL APFLNRQMLL GHHLGLKGNV KKLLKEGDKR AHELNDLIDE LLQEGQSWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRVIE RFTFPRQGKA PYRTLGDYLR PIGDEMDYVA FLSVTVGEGV RDIAEEWKVK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID C2N6C5_BACCE Unreviewed; 610 AA. AC C2N6C5; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 34. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=bcere0002_41180 {ECO:0000313|EMBL:EEK48898.1}, GN DJ50_3585 {ECO:0000313|EMBL:KFL78105.1}; OS Bacillus cereus ATCC 10876. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526980 {ECO:0000313|EMBL:EEK48898.1, ECO:0000313|Proteomes:UP000001484}; RN [1] {ECO:0000313|EMBL:EEK48898.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 10876 {ECO:0000313|EMBL:EEK48898.1}; 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] {ECO:0000313|EMBL:KFL78105.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 10876 {ECO:0000313|EMBL:KFL78105.1}; RA Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O., Coyne S.R., RA Daligault H.E., Davenport K.W., Erkkila T., Frey K.G., Gibbons H.S., RA Gu W., Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C., RA Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N., RA Scholz M.B., Teshima H., Xu Y.; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEK48898.1}. 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; ACLT01000089; EEK48898.1; -; Genomic_DNA. DR EMBL; JMPW01000022; KFL78105.1; -; Genomic_DNA. DR RefSeq; WP_000770356.1; NZ_KN050654.1. DR ProteinModelPortal; C2N6C5; -. DR EnsemblBacteria; EEK48898; EEK48898; bcere0002_41180. DR EnsemblBacteria; KFL78105; KFL78105; DJ50_3585. DR PATRIC; 24865737; VBIBacCer12024_5300. DR Proteomes; UP000001484; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001484}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:KFL78105.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:KFL78105.1}. SQ SEQUENCE 610 AA; 67237 MW; 10F373099941976F CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNVSDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTK INRAAVKLAK ASVTDKNAIL GTIGGMKHIG AVTTTDMERE FILLEQAGAL LEEQVDGLLL ETFYDEFELL HAVKVLRKQT NIPIVAQLAL HEAGTTQNGN DVNEILKQFI DYGANVVGLN CQLGPLHMTE AFKMISIPQN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPKFIEQGI RLLGGCCGTT PEHIQSMKRA VANITPVIEK ETIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRVSNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIK LIEEVYEATK HLEQPIFIGI MPLVSKRNAD FLHFEVPGIT LPEEIRERMD GHETKEAAIE EGIRISQELI DAAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID C2NMV2_BACCE Unreviewed; 1132 AA. AC C2NMV2; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 41. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEK54665.1}; GN ORFNames=bcere0004_40390 {ECO:0000313|EMBL:EEK54665.1}; OS Bacillus cereus BGSC 6E1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526970 {ECO:0000313|EMBL:EEK54665.1, ECO:0000313|Proteomes:UP000000284}; RN [1] {ECO:0000313|EMBL:EEK54665.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BGSC 6E1 {ECO:0000313|EMBL:EEK54665.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEK54665.1}. 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; ACLU01000092; EEK54665.1; -; Genomic_DNA. DR RefSeq; WP_000649730.1; NZ_CM000716.1. DR EnsemblBacteria; EEK54665; EEK54665; bcere0004_40390. DR PATRIC; 24935762; VBIBacCer134364_5556. DR Proteomes; UP000000284; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000284}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 125987 MW; 852AFF9A0546E6B6 CRC64; MKCIEEKLQN SILLLDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYELSHLDE ELNEKAARLA KQAVKESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGE VDVLLVETSQ DMRNVKAAYI GIQAAFDELK KIVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWVN IIGGCCGTTP EHIKAMKEAL ASLKPREHHE REGHGVSGLE ALQYDDSMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMENF LAEVTKVLKV PIMIDSTDEH VMERALTYIQ GKAVINSINL EDGEERFIKV TPLLQKYGAA IVVGTIDEDG MAVSAERKLE IAKRSYELLT TKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPDE EKRLADALLF ETTQETLEEF TNFYRVAKKK DVVVQETLTL DERLANYIVE GTKQGLHEDL SLALTEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILA NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAADIDIPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV TKEEKKVEIP AVIEPLPKSE VMVPDSTKRI VLRDVPALHL VPFLNRQMLL GHHLGLKGSV KKLLKEGDKR AHELNDLIDE LLQEGQSWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRVIE RFTFPRQGRA PYRTLGDYLR PIGDEMDYVA FLSVTVGEGV RDIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID C2NMV3_BACCE Unreviewed; 610 AA. AC C2NMV3; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 33. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=bcere0004_40400 {ECO:0000313|EMBL:EEK54666.1}; OS Bacillus cereus BGSC 6E1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526970 {ECO:0000313|EMBL:EEK54666.1, ECO:0000313|Proteomes:UP000000284}; RN [1] {ECO:0000313|EMBL:EEK54666.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BGSC 6E1 {ECO:0000313|EMBL:EEK54666.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEK54666.1}. 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; ACLU01000092; EEK54666.1; -; Genomic_DNA. DR RefSeq; WP_000770338.1; NZ_CM000716.1. DR ProteinModelPortal; C2NMV3; -. DR EnsemblBacteria; EEK54666; EEK54666; bcere0004_40400. DR PATRIC; 24935760; VBIBacCer134364_5555. DR Proteomes; UP000000284; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000284}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 610 AA; 67264 MW; 00A5EA30497F636A CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNISDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTE INRAAVKLAK ASVTDRNAIL GTIGGMKHIG AVTTTDMERE FMLLEQASAL LEEQVDGLLL ETFYDEFELL HAVQVLRKET NIPIVAQLAL HEAGTTQNGN DVNEILKQLL DYGANVVGLN CQLGPLHMTE ALKMISIPKN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPKFIEQGI RLLGGCCGTT PEHIESMKRA TLNVTPVIEK DTIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRISNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIA LIEEVYEATK HLEQPIFIGI MPLISKRNAD FLHFEVPGIT LPEAVRERMD GHETKEAAIE EGIRISQELI DETMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID C2P3L2_BACCE Unreviewed; 1132 AA. AC C2P3L2; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEK60435.1}; GN ORFNames=bcere0005_38770 {ECO:0000313|EMBL:EEK60435.1}; OS Bacillus cereus 172560W. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526967 {ECO:0000313|EMBL:EEK60435.1, ECO:0000313|Proteomes:UP000001752}; RN [1] {ECO:0000313|EMBL:EEK60435.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=172560W {ECO:0000313|EMBL:EEK60435.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEK60435.1}. 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; ACLV01000066; EEK60435.1; -; Genomic_DNA. DR RefSeq; WP_000649682.1; NZ_CM000717.1. DR EnsemblBacteria; EEK60435; EEK60435; bcere0005_38770. DR PATRIC; 24756928; VBIBacCer25702_4502. DR Proteomes; UP000001752; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001752}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 125958 MW; 078F3DCBEC854F2F CRC64; MKCIEEKLKN SILILDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYELSHLDE ELNEKAALLA KQAVKESGNE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGE VDVLLVETSQ DMRNVKAAYI GIQAAFEELK KTVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKLLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWVN IIGGCCGTTP EHIKAMKSAL ASLKPRDHHE REGHGISGLE ALQYDESMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMENF LAEVTKVLKV PIMIDSTDEN VMERALTYIQ GKAVINSINL EDGEERFKKV TPLLQKYGAA IVVGTIDEDG MAVSAERKIE IAKRSYELLT KKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPEE EKRLADALLF ETTKETLEEF TNFYRVAKKK DIVVQETLTL DERLANYIVE GTKQGLHEDL SLALEEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILA NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAANIDVPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV KKEEKKVEIP AVIEPLPKAE VIVPDSTKRI VLRDIPALHL APFLNRQMLL GHHLGLKGNV KKLLKEGDKR AHELNDLIDE LLQEGQSWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRVIE RFTFPRQGKA PYRTLGDYLR PIGDEMDYVA FLSVTVGEGV RDIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID C2P3L3_BACCE Unreviewed; 610 AA. AC C2P3L3; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 31. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=bcere0005_38780 {ECO:0000313|EMBL:EEK60436.1}; OS Bacillus cereus 172560W. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526967 {ECO:0000313|EMBL:EEK60436.1, ECO:0000313|Proteomes:UP000001752}; RN [1] {ECO:0000313|EMBL:EEK60436.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=172560W {ECO:0000313|EMBL:EEK60436.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEK60436.1}. 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; ACLV01000066; EEK60436.1; -; Genomic_DNA. DR RefSeq; WP_000770360.1; NZ_CM000717.1. DR ProteinModelPortal; C2P3L3; -. DR EnsemblBacteria; EEK60436; EEK60436; bcere0005_38780. DR PATRIC; 24756926; VBIBacCer25702_4501. DR Proteomes; UP000001752; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001752}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 610 AA; 67241 MW; 2994E829027824F4 CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNVSDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTK INRAAVKLAK ASVTDKNAIL GTIGGMKHIG AVTTTDMERE FMLLEQAGAL LEEQVDGLLL ETFYDEFELL HAVKVLRKQT NIPIVAQLAL HEAGTTQNGN DVNEILKQFI DYGANVVGLN CQLGPLHMTE AFKMISIPQN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPKFIEQGI RLLGGCCGTT PEHIQSMKRA VANITPVIEK ETIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRVSNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIK LIEEVYEATK HLEQPIFIGI MPLVSKRNAD FLHFEVPGIT LPEEIRERMD GHETKEAAIE EGIRISQELV DAAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID C2PJX1_BACCE Unreviewed; 1132 AA. AC C2PJX1; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 39. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEK65899.1}; GN ORFNames=bcere0006_40130 {ECO:0000313|EMBL:EEK65899.1}; OS Bacillus cereus MM3. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526971 {ECO:0000313|EMBL:EEK65899.1, ECO:0000313|Proteomes:UP000001751}; RN [1] {ECO:0000313|EMBL:EEK65899.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MM3 {ECO:0000313|EMBL:EEK65899.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEK65899.1}. 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; ACLW01000086; EEK65899.1; -; Genomic_DNA. DR RefSeq; WP_000649698.1; NZ_CM000718.1. DR ProteinModelPortal; C2PJX1; -. DR EnsemblBacteria; EEK65899; EEK65899; bcere0006_40130. DR PATRIC; 24985242; VBIBacCer63122_4939. DR Proteomes; UP000001751; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001751}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 126019 MW; AACB922B74B52100 CRC64; MKCIEEKLQN NILILDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYELSHLDE ELNEKAARLA KQAVKESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLNGD VDVLLVETSQ DMRNVKAAYI GIQAAFDELN KIVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWVN IIGGCCGTTP EHIKAMKSAL ASLKPREHHE RDGHGVSGLE ALQYDDSMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMENF LAEVTKVLKV PIMIDSTDEN VMERALTYIQ GKAVINSINL EDGEERFKKV TPLLRKYGAA IVVGTIDEDG MAVSAERKLE IAKRSYELLT TKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPEE EKRLADALLF ETTQETLEEF TNFYRAAKKK DVVIQETLTL DERLANYIVE GTKQGLQEDL SLALTEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS ESAKKGKVLL ATVKGDVHDI GKNLVEIILS NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAANIDIPIV VGGAALTRKF TDNRISPSYT GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV KKEEKKVEIP AVIEPLPKAE VMIPDSTKRI VLRDIPALHL APFLNRQMLL GHHLGLKGNV KKLLREGDKR AHELNDLIDE LLQEGKYWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRVIE RFTFPRQGKA PYRTLGDYLR PVGDEMDYVA FLSVTVGEGV RDIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSSEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID C2PJX2_BACCE Unreviewed; 610 AA. AC C2PJX2; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 31. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=bcere0006_40140 {ECO:0000313|EMBL:EEK65900.1}; OS Bacillus cereus MM3. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526971 {ECO:0000313|EMBL:EEK65900.1, ECO:0000313|Proteomes:UP000001751}; RN [1] {ECO:0000313|EMBL:EEK65900.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MM3 {ECO:0000313|EMBL:EEK65900.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEK65900.1}. 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; ACLW01000086; EEK65900.1; -; Genomic_DNA. DR RefSeq; WP_000770341.1; NZ_CM000718.1. DR ProteinModelPortal; C2PJX2; -. DR EnsemblBacteria; EEK65900; EEK65900; bcere0006_40140. DR PATRIC; 24985244; VBIBacCer63122_4940. DR Proteomes; UP000001751; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001751}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 610 AA; 67219 MW; 08862A4B3F77C4D2 CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNISDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVVQ INKAAVKIAK ASVTDRNAIL GTIGGMKHIG AVTTTDMERE FMLLEQASAL LEEQVDGLLL ETFYDEFELL HAVQVLRKQT NIPIVAQLAL HEAGTTQNGN DVNEILKQLL DYGANVVGLN CQLGPLHMTE AFKMISIPQN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPKFIEQGI RLLGGCCGTT PEHIESMKRA IANVTPVIEK DTIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLNTQRFFEG ARALKRAGAD AITLADNSLA SPRISNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIA LIEEVYEATK HLEQPIFIGI MPLISKRNAD FLHFEVPGIT LPEEIRERMD GHETKEAAIE EGIRISQELI DAAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID C2Q0V2_BACCE Unreviewed; 1132 AA. AC C2Q0V2; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 39. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEK71517.1}; GN ORFNames=bcere0007_39510 {ECO:0000313|EMBL:EEK71517.1}; OS Bacillus cereus AH621. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526972 {ECO:0000313|EMBL:EEK71517.1, ECO:0000313|Proteomes:UP000001909}; RN [1] {ECO:0000313|EMBL:EEK71517.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AH621 {ECO:0000313|EMBL:EEK71517.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEK71517.1}. 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; ACLX01000083; EEK71517.1; -; Genomic_DNA. DR RefSeq; WP_002015125.1; NZ_CM000719.1. DR ProteinModelPortal; C2Q0V2; -. DR EnsemblBacteria; EEK71517; EEK71517; bcere0007_39510. DR GeneID; 22938433; -. DR PATRIC; 24841830; VBIBacCer129149_5035. DR Proteomes; UP000001909; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001909}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 126128 MW; 780957A59CFC773A CRC64; MKRIEERLQH EILILDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVKTRP DVILNIHKVY IEAGADIIET NTFGATNIVL SDYALSHLDE ELNERAALLA KQAVKESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLRGE VDVLLVETSQ DMRNVKAAYI GIQSAFEELN KIVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR EHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPASLAEKV KRFAEEGWIN IIGGCCGTTP EHIRVMKSAL ASINPREHHE RVGHGISGLE ALQYDDSMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMERF LAEVTKVLKV PIMIDSTDEN VMAKALTYIQ GKGVINSINL EDGEERFEKV TPLLRKYGAA IVVGTIDEDG MAVSAERKIE IAKRSYELLT KKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYALIPEE EKRLADALLF GTTKETLEKF TNFYRVAKKK DVVIQETLTL DERLANYIVE GTKQGLQEDL SLALTEGRKP LDIINGPLMT GMDEVGRLFN GNELIVAEVL QSAESMKAAV SYLEPHMESS ESAKKGKVLL ATVKGDVHDI GKNLVEIILS NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAANIDIPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKR DKKERHLHIV KQEEKKIEIP AVIEPLPKAT VMIPDSTKRV VLRDVPALHL APFLNRQMLI GHHLGLKGNV KKLLQEGDKR AHELNDLIDE LLQEGQSWLR PKAVYQFFPA QSDGQNIIIY DPEDHTRIIE RFEFPRQGKA PYRTLGDYIR PIGDEMDYVA FLSVTVGEGV RDIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID C2Q0V3_BACCE Unreviewed; 610 AA. AC C2Q0V3; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 31. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=bcere0007_39520 {ECO:0000313|EMBL:EEK71518.1}; OS Bacillus cereus AH621. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526972 {ECO:0000313|EMBL:EEK71518.1, ECO:0000313|Proteomes:UP000001909}; RN [1] {ECO:0000313|EMBL:EEK71518.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AH621 {ECO:0000313|EMBL:EEK71518.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEK71518.1}. 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; ACLX01000083; EEK71518.1; -; Genomic_DNA. DR RefSeq; WP_002015127.1; NZ_CM000719.1. DR ProteinModelPortal; C2Q0V3; -. DR EnsemblBacteria; EEK71518; EEK71518; bcere0007_39520. DR GeneID; 22938434; -. DR PATRIC; 24841832; VBIBacCer129149_5036. DR Proteomes; UP000001909; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001909}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 610 AA; 67125 MW; 9C14592D213700CA CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNLSDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVVQ INKAAVNIAK ASVTDRNAIL GTIGGMKHIG AVTTTDIERE FMLLEQAGAL LEEQVDGLLL ETFYDEFELL HAVKVLRKQT NIPIVAQLAL HEAGTTQNGN DVNEILKRLL DYGANVVGLN CQLGPLHMTE AFKMISIPQN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEE MTPKFIEQGI RLLGGCCGTT PEHIEGMKRA IANVAPVIAK ETIQRPKVVH THEKRSRAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRVSNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDVA LIEEVYEATK HLEQPIFIGI MPLVSKRNAD FLHFEVPGIT LPEEIRQRMD GHETKEAAIE EGIRISQELI DAAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID C2Q483_BACCE Unreviewed; 308 AA. AC C2Q483; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 07-JAN-2015, entry version 17. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEK70409.1}; GN ORFNames=bcere0007_51430 {ECO:0000313|EMBL:EEK70409.1}; OS Bacillus cereus AH621. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526972 {ECO:0000313|EMBL:EEK70409.1, ECO:0000313|Proteomes:UP000001909}; RN [1] {ECO:0000313|EMBL:EEK70409.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AH621 {ECO:0000313|EMBL:EEK70409.1}; 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. {ECO:0000313|EMBL:EEK70409.1}. 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; ACLX01000114; EEK70409.1; -; Genomic_DNA. DR EnsemblBacteria; EEK70409; EEK70409; bcere0007_51430. DR PATRIC; 24844284; VBIBacCer129149_0484. DR Proteomes; UP000001909; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001909}; KW Methyltransferase {ECO:0000313|EMBL:EEK70409.1}; KW Transferase {ECO:0000313|EMBL:EEK70409.1}. SQ SEQUENCE 308 AA; 34400 MW; AD78C44C3336E868 CRC64; MLLDGALATE LEAHGCNLDD PLWSARVLLE NPELIYQVHS DYFRAGADCA ITASYQATIS GFSARGIQEQ EALELIKKTV LLARRARDDF WKENTQTNRP KPLVVASVGP YGAYLADGSE YVGNYGVTDK TLADFHRSRM SALIEAGADL LAFETIPSLQ EARVLDTLLR EFPETYAWLS FSLKNEKEIS EGMKLVECAR AFEKSEQIVA IGINCAPVTV VTGAIQELRA NTKKPIIVYP NSGETYNPES KTWHGHEQCN ALDIQSEEWY QAGARLIGGC CRTTPYHIEE ISNKWRSSEF FYSNEAKQ // ID C2QH46_BACCE Unreviewed; 1132 AA. AC C2QH46; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 39. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEK77134.1}; GN ORFNames=bcere0009_39680 {ECO:0000313|EMBL:EEK77134.1}; OS Bacillus cereus R309803. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526968 {ECO:0000313|EMBL:EEK77134.1, ECO:0000313|Proteomes:UP000006816}; RN [1] {ECO:0000313|EMBL:EEK77134.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=R309803 {ECO:0000313|EMBL:EEK77134.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEK77134.1}. 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; ACLY01000072; EEK77134.1; -; Genomic_DNA. DR RefSeq; WP_000649708.1; NZ_CM000720.1. DR ProteinModelPortal; C2QH46; -. DR EnsemblBacteria; EEK77134; EEK77134; bcere0009_39680. DR PATRIC; 25008454; VBIBacCer63003_4417. DR Proteomes; UP000006816; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006816}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 125793 MW; 148F48B7F7FFF2BC CRC64; MKCIEEKLQN NILILDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYELSHLDE KLNEKAARLA KQAVNESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGE VDVLLVETSQ DMRNVKAAYI GIQAAFDELN KIVPIMISGT IEPMGTTLAG QTIEAFYLSI EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEQGWVN IIGGCCGTTP EHIKAMKSAL ASLKPREHHE RAGHGVSGLE ALQYDDSMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMENF LAEVTKVLKV PIMIDSTDEN VMERALTYIQ GKAVINSINL EDGEERFKKV TPLLQKYGAA IVVGTIDEDG MAVSAERKLE IAKRSYDLLT TKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPEE EKRLADALLF ETTQGTLEEF TNFYRVAKKK DIVIQETLTL DERLANYIVE GTKQGLQEDL SLALTEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILS NNGYEIINLG INVRSDRIVQ EVQEKNPDII GLSGLLVKSA QQMVTTAEDL KAANIDIPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMQQ DKKERHLHIV KKEEKKVEIP AVIEPLAKAE VMIPDSTKRI VLRDIPALHL APFLNRQMLL GHHLGLKGNV KKLLLEGDKR AHELNDLIDE LLQEGQSWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRVIE RFTFPRQGKA PYRTLGDYLR PVGDEMDYVA FLSVTVGEGV RDIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID C2QH47_BACCE Unreviewed; 610 AA. AC C2QH47; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 31. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=bcere0009_39690 {ECO:0000313|EMBL:EEK77135.1}; OS Bacillus cereus R309803. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526968 {ECO:0000313|EMBL:EEK77135.1, ECO:0000313|Proteomes:UP000006816}; RN [1] {ECO:0000313|EMBL:EEK77135.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=R309803 {ECO:0000313|EMBL:EEK77135.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEK77135.1}. 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; ACLY01000072; EEK77135.1; -; Genomic_DNA. DR RefSeq; WP_000770369.1; NZ_CM000720.1. DR ProteinModelPortal; C2QH47; -. DR EnsemblBacteria; EEK77135; EEK77135; bcere0009_39690. DR PATRIC; 25008452; VBIBacCer63003_4416. DR Proteomes; UP000006816; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006816}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 610 AA; 67200 MW; 6229630F377B93C7 CRC64; MKLLDLLSKG TVIGDGAVGT LLHSHGLQSS FEELNISDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTE INRSAVKLAK ASVTEKNAIL GTIGGMKHIG AVTTTDMERE FMLLEQAGAL LEEQVDGLLL ETFYDEFELL HAVKVLRKQT NIPIVAQLAL HEAGTTQNGN DVNEILKQLL DYGANVVGLN CQLGPLHMTE ALKMISIPQN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MAPKFIEQGV RLLGGCCGTT PEHIESMKRA TLNVTPVIEK DTIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRVSNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIEAGAEY FLTQPIYDVA LIKEVYEATK HLEQPIFIGI MPLVSKRNAD FLHFEVPGIT LPEEIRHRMD GHETKEEAIE EGIRISQELI DAAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID C2QYA7_BACCE Unreviewed; 1132 AA. AC C2QYA7; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 41. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEK82575.1}; GN ORFNames=bcere0010_40470 {ECO:0000313|EMBL:EEK82575.1}; OS Bacillus cereus ATCC 4342. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526977 {ECO:0000313|EMBL:EEK82575.1, ECO:0000313|Proteomes:UP000001352}; RN [1] {ECO:0000313|EMBL:EEK82575.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 4342 {ECO:0000313|EMBL:EEK82575.1}; 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. {ECO:0000313|EMBL:EEK82575.1}. 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; ACLZ01000058; EEK82575.1; -; Genomic_DNA. DR RefSeq; WP_000649718.1; NZ_KN125577.1. DR EnsemblBacteria; EEK82575; EEK82575; bcere0010_40470. DR EnsemblBacteria; KFM88733; KFM88733; DJ86_639. DR PATRIC; 24878001; VBIBacCer13872_4024. DR Proteomes; UP000001352; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001352}. SQ SEQUENCE 1132 AA; 125869 MW; 8D35B43C378465FA CRC64; MKCIEEKLQN NILLLDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYELSYLDE ELNEKAARLA KQAVEESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGE VDVLLVETSQ DMRNVKAAYI GIQAAFDELN KIVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWVN IIGGCCGTTP EHIKAMKSAL ASLKPREQQE RAGHGVSGLE ALQYDDSMRP LFVGERTNVI GSHKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMENF LAEVTKVLKV PIMIDSTDEN VMERALTYIQ GKAVINSINL EDGEERFIKV TPLLQKYGAA IVVGTIDEDG MAVSAERKLE IAKRSYELLT TKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KDTLPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPEE EKRLADALLF ETTQETLEEF TNFYRAAKKK DVVIQETLTL DERLANYIVE GTKQGLHEDL SLALTEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILA NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAADIDIPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV TKEEKKVEIP AVIEPLPKSE VMVPDSTKRI VLRDIPALHL APFLNRQMLL GHHLGLKGSV KKLLREGDKR AHELNDLIDE LLQEGQSWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRVIE RFTFPRQGKA PYRTLGDYLR PIGDEMDYVA FLSVTVGEGV RDIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID C2QYA8_BACCE Unreviewed; 610 AA. AC C2QYA8; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 35. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=bcere0010_40480 {ECO:0000313|EMBL:EEK82576.1}; OS Bacillus cereus ATCC 4342. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526977 {ECO:0000313|EMBL:EEK82576.1, ECO:0000313|Proteomes:UP000001352}; RN [1] {ECO:0000313|EMBL:EEK82576.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 4342 {ECO:0000313|EMBL:EEK82576.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEK82576.1}. 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; ACLZ01000058; EEK82576.1; -; Genomic_DNA. DR RefSeq; WP_000770330.1; NZ_KN125577.1. DR ProteinModelPortal; C2QYA8; -. DR EnsemblBacteria; EEK82576; EEK82576; bcere0010_40480. DR EnsemblBacteria; KFM87407; KFM87407; DJ86_638. DR PATRIC; 24878003; VBIBacCer13872_4025. DR Proteomes; UP000001352; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001352}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 610 AA; 67210 MW; 2A5E2353CD2C989C CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNISDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTE INRAAVKLAK ASVTDRNAIL GTIGGMKHIG AVTTTDMERE FMLLEQASAL LEEQVDGLLL ETFYDEFELL HAVQVLRKET NIPIVAQLAL HEAGTTQNGN DVNEILKQLL DYGANVVGLN CQLGPLHMTE AFKMISIPKN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPKFIEQGI RLLGGCCGTT PEHIESMKRA TLNVTPVIEK DTIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRISNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIA LIEEVYEATK HLEQPIFIGI MPLISKRNAD FLHFEVPGIT LPEAVRERMD GHETKEAAIE EGIRISQELI DAAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID C2RD95_BACCE Unreviewed; 1132 AA. AC C2RD95; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEK87699.1}; GN ORFNames=bcere0011_39920 {ECO:0000313|EMBL:EEK87699.1}; OS Bacillus cereus m1550. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526969 {ECO:0000313|EMBL:EEK87699.1, ECO:0000313|Proteomes:UP000001371}; RN [1] {ECO:0000313|EMBL:EEK87699.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M1550 {ECO:0000313|EMBL:EEK87699.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEK87699.1}. 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; ACMA01000067; EEK87699.1; -; Genomic_DNA. DR RefSeq; WP_000649674.1; NZ_CM000722.1. DR EnsemblBacteria; EEK87699; EEK87699; bcere0011_39920. DR PATRIC; 25135958; VBIBacCer61419_4028. DR Proteomes; UP000001371; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001371}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 125918 MW; 0CA9E80CA7CEF3FF CRC64; MKCIEEKLKN SILILDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYDLSHLDE ELNEKAALLA KQAVKESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGA VDVLLVETSQ DMRNVKAAYI GIQAAFEELK KTVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWVN IIGGCCGTTP EHIKAMKSAL ASLRPRDHHE REGHGISGLE ALQYDESMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMENF LAEVTKVLKV PIMIDSTDEN VMERALTYIQ GKAVINSINL EDGEERFKKV TPLLQKYGAA IVVGTIDEDG MAVSAERKIE IAKRSYELLT KKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPEE EKRLADALLF ETTKETLEEF TNFYRVAKKK DVVVQETLTL DERLANYIVE GTKQGLHEDL SLALEEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILA NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAANIDVPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV KKEEKKVEIP AVIEPLPKSE VMVPDSTKRI VLRDVPALHL APFLNRQMLL GHHLGLKGNV KKLLKEGDKR AHELNDLIDE LLQEGQSWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRVIE RFTFPRQGKA PYRTLGDYLR PIGDEMDYVA FLSVTVGEGV RDIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID C2RD96_BACCE Unreviewed; 610 AA. AC C2RD96; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 33. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=bcere0011_39930 {ECO:0000313|EMBL:EEK87700.1}; OS Bacillus cereus m1550. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526969 {ECO:0000313|EMBL:EEK87700.1, ECO:0000313|Proteomes:UP000001371}; RN [1] {ECO:0000313|EMBL:EEK87700.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M1550 {ECO:0000313|EMBL:EEK87700.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEK87700.1}. 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; ACMA01000067; EEK87700.1; -; Genomic_DNA. DR RefSeq; WP_000770352.1; NZ_CM000722.1. DR ProteinModelPortal; C2RD96; -. DR EnsemblBacteria; EEK87700; EEK87700; bcere0011_39930. DR PATRIC; 25135960; VBIBacCer61419_4029. DR Proteomes; UP000001371; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001371}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 610 AA; 67207 MW; 6AAA70A0BB40008A CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNVSDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTE INRAAVKLAK ASVTDKNAIL GTIGGMKHIG AVTTTDMERE FMLLEQAGAL LEEQVDGLLL ETFYDEFELL HAVKVLRKQT NIPIVAQLAL HEAGTTQNGN DVNEILKQLI DYGANVVGLN CQLGPLHMTE AFKMISIPQN GYLSAYPNAG LPNYVDGRYV YEGSPAYFEA MTPRFIEQGI RLLGGCCGTT PEHIQSMKRA VANITPVIEK DTIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRVSNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIK LIEEVYEATK HLEQPIFIGI MPLVSKRNAD FLHFEVPGIT LPEEIRERMD GHETKEAAIE EGIRISQELV DAAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID C2S8Y9_BACCE Unreviewed; 1132 AA. AC C2S8Y9; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 39. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEK98711.1}; GN ORFNames=bcere0013_40840 {ECO:0000313|EMBL:EEK98711.1}; OS Bacillus cereus BDRD-ST26. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526975 {ECO:0000313|EMBL:EEK98711.1, ECO:0000313|Proteomes:UP000002291}; RN [1] {ECO:0000313|EMBL:EEK98711.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BDRD-ST26 {ECO:0000313|EMBL:EEK98711.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEK98711.1}. 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; ACMC01000085; EEK98711.1; -; Genomic_DNA. DR RefSeq; WP_000649709.1; NZ_CM000724.1. DR ProteinModelPortal; C2S8Y9; -. DR EnsemblBacteria; EEK98711; EEK98711; bcere0013_40840. DR PATRIC; 24923715; VBIBacCer77638_5261. DR Proteomes; UP000002291; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002291}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 125917 MW; CAF651DF42EF4C1F CRC64; MKCIEEKLQN NILLLDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYELSHLDE ELNEKAARLA KQAVEESGKE IYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGE VDVLLVETSQ DMRNVKAAYI GIQAAFDELN TVVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWVN IIGGCCGTTP EHIKAMKSAL TSLKPREQQE RAGHGVSGLE ALQYDDSMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEI ARAQVKKNAH IIDICMADPD RDEIEDMENF LAEVTKVLKV PIMIDSTDEH VMERALTYIQ GKAVINSINL EDGEERFEKV TPLLRKYGAA IVVGTIDEDG MAVSAERKLE IAKRSYELLT TKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPDE EKRLADALLF ETTQETLEKF TNFYRVAKKK DVVVQETLTL DERLANYIVE GTKQGLHEDL SLALTEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILA NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAADIDIPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV TKEEKKVEIP AVIEPLPKSE VMVPDSTKRI VLRDVPVSHL APFLNRQMLL GHHLGLKGSV KKLLREGDKR AHELNDLIDE LLQEGQSWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRIIE RFTFPRQGKA PYRTLGDYLR PVGDEMDYVA FLSVTVGEGV RDIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID C2S8Z0_BACCE Unreviewed; 610 AA. AC C2S8Z0; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 31. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=bcere0013_40850 {ECO:0000313|EMBL:EEK98712.1}; OS Bacillus cereus BDRD-ST26. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526975 {ECO:0000313|EMBL:EEK98712.1, ECO:0000313|Proteomes:UP000002291}; RN [1] {ECO:0000313|EMBL:EEK98712.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BDRD-ST26 {ECO:0000313|EMBL:EEK98712.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEK98712.1}. 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; ACMC01000085; EEK98712.1; -; Genomic_DNA. DR RefSeq; WP_000770335.1; NZ_CM000724.1. DR ProteinModelPortal; C2S8Z0; -. DR EnsemblBacteria; EEK98712; EEK98712; bcere0013_40850. DR PATRIC; 24923717; VBIBacCer77638_5262. DR Proteomes; UP000002291; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002291}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 610 AA; 67212 MW; C311353A7C332F2C CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNISDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTE INRAAVKLAK ASVTDRNAIL GTIGGMKHIG AVTTTDMERE FMLLEQASAL LEEQVDGLLL ETFYDEFELL HAVQVLRKET NIPIVAQLAL HEAGTTQNGN DVNEILKQLL DYGANVVGLN CQLGPLHMTE AFKMISIPKN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPKFIEQGI RLLGGCCGTT PEHIESMKRA TLNVTPVIEK DTVQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRISNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSVL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIA LIEEVYEATK HLEQPIFIGI MPLISKRNAD FLHFEVPGIT LPEAVRERMD GHETKETAIE EGIRISQELI DAAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID C2SQ64_BACCE Unreviewed; 1132 AA. AC C2SQ64; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEL04398.1}; GN ORFNames=bcere0014_39820 {ECO:0000313|EMBL:EEL04398.1}; OS Bacillus cereus BDRD-ST196. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526976 {ECO:0000313|EMBL:EEL04398.1, ECO:0000313|Proteomes:UP000002295}; RN [1] {ECO:0000313|EMBL:EEL04398.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BDRD-ST196 {ECO:0000313|EMBL:EEL04398.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEL04398.1}. 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; ACMD01000112; EEL04398.1; -; Genomic_DNA. DR RefSeq; WP_002034031.1; NZ_CM000725.1. DR EnsemblBacteria; EEL04398; EEL04398; bcere0014_39820. DR PATRIC; 24900231; VBIBacCer6084_0888. DR Proteomes; UP000002295; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002295}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 126214 MW; 506837A80CFC8E9E CRC64; MKRIEERLQH EILILDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVKTRP DVILNIHKVY IEAGADIIET NTFGATNIVL SDYALSHLDE ELNERAALLA KQAVKESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLRGE VDVLLVETSQ DMRNVKAAYI GIQSAFEELN KIVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR EHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPASLAEKV KRFAEEGWIN IIGGCCGTTP EHIRVMKSAL ASINPREHHE RVGHGISGLE ALQYDDSMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMERF LAEVTKVLKV PIMIDSTDEN VMAKALTYIQ GKGVINSINL EDGEERFEKV TPLLRKYGAA IVVGTIDEDG MAVSAERKIE IAKRSYELLT KKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYALIPEE EKRLADALLF ETTKETLEKF TNFYRVAKKK DVVIQETLTL DERLANYIVE GTKQGLQEDL SLALTEGRKP LDIINGPLMT GMDEVGRLFN GNELIVAEVL QSAESMKAAV SYLEPHMESS ESAKKGKVLL ATVKGDVHDI GKNLVEIILS NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAANIDIPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKR DKKERHLHIV KQEEKKIEIP AVIEPLPKAT VMIPDSTKRV VLRDIPALHL APFLNRQMLI GHHLGLKGNV KKLLQEGDKR AHELNDLIDE LLQEGQSWLR PKAVYQFFPA QSDGQNIIIY DPEDHTRIIE RFEFPRQGKA PYRTLGDYIR PIGDEMDYVA FLSVTVGEGV RDIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID C2SQ65_BACCE Unreviewed; 610 AA. AC C2SQ65; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 31. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=bcere0014_39830 {ECO:0000313|EMBL:EEL04399.1}; OS Bacillus cereus BDRD-ST196. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526976 {ECO:0000313|EMBL:EEL04399.1, ECO:0000313|Proteomes:UP000002295}; RN [1] {ECO:0000313|EMBL:EEL04399.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BDRD-ST196 {ECO:0000313|EMBL:EEL04399.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEL04399.1}. 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; ACMD01000112; EEL04399.1; -; Genomic_DNA. DR RefSeq; WP_002034032.1; NZ_CM000725.1. DR ProteinModelPortal; C2SQ65; -. DR EnsemblBacteria; EEL04399; EEL04399; bcere0014_39830. DR PATRIC; 24900233; VBIBacCer6084_0889. DR Proteomes; UP000002295; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002295}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 610 AA; 67083 MW; 2EF7BB867F436FFD CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNLSDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVVQ INKAAVNIAK ASVTDRNAIL GTIGGMKHIG AVTTTDIERE FMLLEQAGAL LEEQVDGLLL ETFYDEFELL HAVKVLRKQT NIPIVAQLAL HEAGTTQNGN DVNEILKQLL DYGANVVGLN CQLGPLHMTE AFKMISIPQN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEE MTPKFIEQGI RLLGGCCGTT PEHIEGMKRA IANVAPVIAK ETIQRPKVVH THEKRSRAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRVSNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDVA LIEEVYEATK HLEQPIFIGI MPLVSKRNAD FLHFEVPGIT LPEEIRQRMD GHETKDAAIE EGIRISQELI DAAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID C2T608_BACCE Unreviewed; 1132 AA. AC C2T608; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEL10005.1}; GN ORFNames=bcere0015_39760 {ECO:0000313|EMBL:EEL10005.1}; OS Bacillus cereus BDRD-Cer4. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526978 {ECO:0000313|EMBL:EEL10005.1, ECO:0000313|Proteomes:UP000001373}; RN [1] {ECO:0000313|EMBL:EEL10005.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BDRD-Cer4 {ECO:0000313|EMBL:EEL10005.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEL10005.1}. 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; ACME01000064; EEL10005.1; -; Genomic_DNA. DR RefSeq; WP_000649676.1; NZ_CM000726.1. DR EnsemblBacteria; EEL10005; EEL10005; bcere0015_39760. DR PATRIC; 24888569; VBIBacCer94942_3935. DR Proteomes; UP000001373; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001373}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 125831 MW; F65956F666CF92F4 CRC64; MKCIEEKLKN SILILDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYDLSHLDE ELNEKAALLA KQAVKESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGA VDVVLVETSQ DMRNVKAAYI GIQAAFEELK KTVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWVN IIGGCCGTTP EHIKAMKSAL ASLRPRDHHE REGHGISGLE ALQYDESMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMENF LAEVTKVLKV PIMIDSTDEN VMERALTYIQ GKAVINSINL EDGEERFKKV TPLLQKYGAA IVVGTIDEDG MAVSAERKIE IAKRSYELLT KKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPEE EKRLADALLF ETTKETLEEF TNFYRVAKKK DVVVQETLTL DERLANYIVE GTKQGLHEDL SLALEEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILA NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAANIDVPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV KKEEKKVEIP AVIEPLPKSE VMVPDSTKRI VLRDVPALHL APFLNRQMLL GHHLGLKGNV KKLLKEGDKR AHELNDLIDE LLQEGQSWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRVIE RFTFPRQGKA PYRTLGDYLR PIGDEMDYVA FLSVTVGEGV RDIAEELKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID C2T609_BACCE Unreviewed; 610 AA. AC C2T609; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 33. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=bcere0015_39770 {ECO:0000313|EMBL:EEL10006.1}; OS Bacillus cereus BDRD-Cer4. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526978 {ECO:0000313|EMBL:EEL10006.1, ECO:0000313|Proteomes:UP000001373}; RN [1] {ECO:0000313|EMBL:EEL10006.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BDRD-Cer4 {ECO:0000313|EMBL:EEL10006.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEL10006.1}. 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; ACME01000064; EEL10006.1; -; Genomic_DNA. DR RefSeq; WP_000770352.1; NZ_CM000726.1. DR ProteinModelPortal; C2T609; -. DR EnsemblBacteria; EEL10006; EEL10006; bcere0015_39770. DR PATRIC; 24888567; VBIBacCer94942_3934. DR Proteomes; UP000001373; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001373}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 610 AA; 67207 MW; 6AAA70A0BB40008A CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNVSDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTE INRAAVKLAK ASVTDKNAIL GTIGGMKHIG AVTTTDMERE FMLLEQAGAL LEEQVDGLLL ETFYDEFELL HAVKVLRKQT NIPIVAQLAL HEAGTTQNGN DVNEILKQLI DYGANVVGLN CQLGPLHMTE AFKMISIPQN GYLSAYPNAG LPNYVDGRYV YEGSPAYFEA MTPRFIEQGI RLLGGCCGTT PEHIQSMKRA VANITPVIEK DTIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRVSNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIK LIEEVYEATK HLEQPIFIGI MPLVSKRNAD FLHFEVPGIT LPEEIRERMD GHETKEAAIE EGIRISQELV DAAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID C2TLN8_BACCE Unreviewed; 1132 AA. AC C2TLN8; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEL15260.1}; GN ORFNames=bcere0016_40800 {ECO:0000313|EMBL:EEL15260.1}; OS Bacillus cereus 95/8201. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526979 {ECO:0000313|EMBL:EEL15260.1, ECO:0000313|Proteomes:UP000002293}; RN [1] {ECO:0000313|EMBL:EEL15260.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=95/8201 {ECO:0000313|EMBL:EEL15260.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEL15260.1}. 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; ACMF01000071; EEL15260.1; -; Genomic_DNA. DR RefSeq; WP_000649714.1; NZ_CM000727.1. DR EnsemblBacteria; EEL15260; EEL15260; bcere0016_40800. DR PATRIC; 24769465; VBIBacCer42905_4685. DR Proteomes; UP000002293; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002293}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 125942 MW; CFD6E26EBD6CBE3C CRC64; MKCIEEKLQN NILLLDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYELSHLDE ELNEKAARLA KQAVKESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGE VDVLLVETSQ DMRNVKAAYI GIQAAFDELK KIVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWVN IIGGCCGTTP EHIKAMKEAL ASLKPREHHE REGHGVSGLE ALQYDDSMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMENF LAEVTKVLKV PIMIDSTDEH VMERALTYIQ GKAVINSINL EDGEERFIKV TPLLQKYGAA IVVGTIDEDG MAVSAERKLE IAKRSYELLT TKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPDE EKRLADALLF ETTQETLEEF TNFYRVAKKK DVVVQETLTL DERLANYIVE GTKQGLHEDL SLALTEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILA NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAADIDIPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV TKEEKKIEIP AVIEPLPKSE VMVPDSTKRI VLRDVPALHL APFLNRQMLL GHHLGLKGSV KKLLKEGDKR AHELNDLIDE LLQEGQSWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRVIE RFTFPRQGRA PYRTLGDYLR PIGDEMDYVA FLSVTVGEGV RGIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID C2TLN9_BACCE Unreviewed; 610 AA. AC C2TLN9; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 33. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=bcere0016_40810 {ECO:0000313|EMBL:EEL15261.1}; OS Bacillus cereus 95/8201. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526979 {ECO:0000313|EMBL:EEL15261.1, ECO:0000313|Proteomes:UP000002293}; RN [1] {ECO:0000313|EMBL:EEL15261.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=95/8201 {ECO:0000313|EMBL:EEL15261.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEL15261.1}. 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; ACMF01000071; EEL15261.1; -; Genomic_DNA. DR RefSeq; WP_000770331.1; NZ_CM000727.1. DR ProteinModelPortal; C2TLN9; -. DR EnsemblBacteria; EEL15261; EEL15261; bcere0016_40810. DR PATRIC; 24769463; VBIBacCer42905_4684. DR Proteomes; UP000002293; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002293}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 610 AA; 67298 MW; 3F0A2353CD3128EB CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNISDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTE INRAAVKLAK ASVTDRNAIL GTIGGMKHIG AVTTTDMERE FMLLEQASAL LEEQVDGLLL ETFYDEFELL HAVQVLRKET NIPIVAQLAL HEAGTTQNGN DVNEILKQLL DYGANVVGLN CQLGPLHMTE AFKMISIPKN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPKFIEQGI RLLGGCCGTT PEHIESMKRA TLNVTPVIEK DTIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRISNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIA LIEEVYEATK HLEQPIFIGI MPLISKRNAD FLHFEVPGIT LPEAVRERMD GHETKEAAIE EGIRISQELI DETMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID C2UJ26_BACCE Unreviewed; 1132 AA. AC C2UJ26; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEL27017.1}; GN ORFNames=bcere0018_39720 {ECO:0000313|EMBL:EEL27017.1}; OS Bacillus cereus Rock1-15. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526982 {ECO:0000313|EMBL:EEL27017.1, ECO:0000313|Proteomes:UP000001923}; RN [1] {ECO:0000313|EMBL:EEL27017.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Rock1-15 {ECO:0000313|EMBL:EEL27017.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEL27017.1}. 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; ACMH01000091; EEL27017.1; -; Genomic_DNA. DR RefSeq; WP_000649674.1; NZ_CM000729.1. DR EnsemblBacteria; EEL27017; EEL27017; bcere0018_39720. DR PATRIC; 25020100; VBIBacCer37058_5454. DR Proteomes; UP000001923; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001923}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 125918 MW; 0CA9E80CA7CEF3FF CRC64; MKCIEEKLKN SILILDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYDLSHLDE ELNEKAALLA KQAVKESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGA VDVLLVETSQ DMRNVKAAYI GIQAAFEELK KTVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWVN IIGGCCGTTP EHIKAMKSAL ASLRPRDHHE REGHGISGLE ALQYDESMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMENF LAEVTKVLKV PIMIDSTDEN VMERALTYIQ GKAVINSINL EDGEERFKKV TPLLQKYGAA IVVGTIDEDG MAVSAERKIE IAKRSYELLT KKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPEE EKRLADALLF ETTKETLEEF TNFYRVAKKK DVVVQETLTL DERLANYIVE GTKQGLHEDL SLALEEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILA NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAANIDVPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV KKEEKKVEIP AVIEPLPKSE VMVPDSTKRI VLRDVPALHL APFLNRQMLL GHHLGLKGNV KKLLKEGDKR AHELNDLIDE LLQEGQSWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRVIE RFTFPRQGKA PYRTLGDYLR PIGDEMDYVA FLSVTVGEGV RDIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID C2UJ27_BACCE Unreviewed; 610 AA. AC C2UJ27; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 33. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=bcere0018_39730 {ECO:0000313|EMBL:EEL27018.1}; OS Bacillus cereus Rock1-15. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526982 {ECO:0000313|EMBL:EEL27018.1, ECO:0000313|Proteomes:UP000001923}; RN [1] {ECO:0000313|EMBL:EEL27018.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Rock1-15 {ECO:0000313|EMBL:EEL27018.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEL27018.1}. 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; ACMH01000091; EEL27018.1; -; Genomic_DNA. DR RefSeq; WP_000770352.1; NZ_CM000729.1. DR ProteinModelPortal; C2UJ27; -. DR EnsemblBacteria; EEL27018; EEL27018; bcere0018_39730. DR PATRIC; 25020102; VBIBacCer37058_5455. DR Proteomes; UP000001923; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001923}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 610 AA; 67207 MW; 6AAA70A0BB40008A CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNVSDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTE INRAAVKLAK ASVTDKNAIL GTIGGMKHIG AVTTTDMERE FMLLEQAGAL LEEQVDGLLL ETFYDEFELL HAVKVLRKQT NIPIVAQLAL HEAGTTQNGN DVNEILKQLI DYGANVVGLN CQLGPLHMTE AFKMISIPQN GYLSAYPNAG LPNYVDGRYV YEGSPAYFEA MTPRFIEQGI RLLGGCCGTT PEHIQSMKRA VANITPVIEK DTIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRVSNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIK LIEEVYEATK HLEQPIFIGI MPLVSKRNAD FLHFEVPGIT LPEEIRERMD GHETKEAAIE EGIRISQELV DAAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID C2V0K0_BACCE Unreviewed; 1132 AA. AC C2V0K0; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEL32816.1}; GN ORFNames=bcere0019_40230 {ECO:0000313|EMBL:EEL32816.1}; OS Bacillus cereus Rock3-28. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526983 {ECO:0000313|EMBL:EEL32816.1, ECO:0000313|Proteomes:UP000001379}; RN [1] {ECO:0000313|EMBL:EEL32816.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Rock3-28 {ECO:0000313|EMBL:EEL32816.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEL32816.1}. 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; ACMI01000161; EEL32816.1; -; Genomic_DNA. DR RefSeq; WP_000649702.1; NZ_CM000730.1. DR EnsemblBacteria; EEL32816; EEL32816; bcere0019_40230. DR PATRIC; 25044080; VBIBacCer113327_3316. DR Proteomes; UP000001379; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001379}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 125888 MW; 337B6A7C13718241 CRC64; MKCIEEKLQN NILILDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYELSHLDE ELNEKAARLA KQAVKESGNE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLNGE VDVLLVETSQ DMRNVKAAYI GIQAAFEELN KIVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWIN IIGGCCGTTP EHIRAMKEAL ASLTPRAQNE RAGHGISGLE ALQYDESMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMEKF LSEVTKVLKV PIMIDSTDEN VMARALTYIQ GKAVINSINL EDGEERFEKV TPLLRKYGAA IVVGTIDEDG MAVSAERKLE IAKRSYELLT TKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPEE EKRLADALLF ETTKETLEEF TNFYRVAKKK EVVVQETLTL DERLANYIVE GTKQGLHEDL SLALTEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILS NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAANIDIPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKK DKKERHLHIV KKEEKKVEIP AVIEPLPKSE VMVPDSTKRI VLRDVPVSHL APFLNRQMLL GHHLGLKGNV KKLLKEGDKR AHELNDLIDE LLVEGQSWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRVIE RFTFPRQGKA PYRTLGDYLR PIGDEMDYVA FLSVTVGEGV RDIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID C2V0K1_BACCE Unreviewed; 610 AA. AC C2V0K1; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 32. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=bcere0019_40240 {ECO:0000313|EMBL:EEL32817.1}; OS Bacillus cereus Rock3-28. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526983 {ECO:0000313|EMBL:EEL32817.1, ECO:0000313|Proteomes:UP000001379}; RN [1] {ECO:0000313|EMBL:EEL32817.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Rock3-28 {ECO:0000313|EMBL:EEL32817.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEL32817.1}. 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; ACMI01000161; EEL32817.1; -; Genomic_DNA. DR RefSeq; WP_000770364.1; NZ_CM000730.1. DR ProteinModelPortal; C2V0K1; -. DR EnsemblBacteria; EEL32817; EEL32817; bcere0019_40240. DR PATRIC; 25044078; VBIBacCer113327_3315. DR Proteomes; UP000001379; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001379}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 610 AA; 67151 MW; 02072EA4FF1537C2 CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNVSDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVVQ INKAAVKLAK ASVTNRNAIL GTIGGMKHIG AVTTTDMERE FMLLEQAGAL LEEQVDGLLL ETFYDEFELL HAVKVLRKQT NIPIVAQVAL HEAGTTQNGN DVNEILKQLI DYGANVVGLN CQLGPLHMTE AFKMISIPQN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPKFIEQGI RLLGGCCGTT PEHIQSMKRA VANVTPVIEK DTIQRPKVVH THEKRSKVQV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRVSNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDVV LIEEVYEATK HLEQPIFIGI MPLVSKRNAD FLHFEVPGIT LPEEIRERMD GHETKEAAIE EGIRISQELI DAAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID C2VGW9_BACCE Unreviewed; 1132 AA. AC C2VGW9; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 39. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEL38742.1}; GN ORFNames=bcere0020_39530 {ECO:0000313|EMBL:EEL38742.1}; OS Bacillus cereus Rock3-29. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526984 {ECO:0000313|EMBL:EEL38742.1, ECO:0000313|Proteomes:UP000006652}; RN [1] {ECO:0000313|EMBL:EEL38742.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Rock3-29 {ECO:0000313|EMBL:EEL38742.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEL38742.1}. 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; ACMJ01000069; EEL38742.1; -; Genomic_DNA. DR RefSeq; WP_000649707.1; NZ_CM000731.1. DR EnsemblBacteria; EEL38742; EEL38742; bcere0020_39530. DR PATRIC; 25055888; VBIBacCer100535_4533. DR Proteomes; UP000006652; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006652}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 125947 MW; C05E63049BDA07FA CRC64; MKCIEEKLQN NILILDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYELSHLDE ELNEKAARLA KQVVKESGNE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLNGE VDVLLVETSQ DMRNVKAAYI GIQAAFEELN KIVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWIN IIGGCCGTTP EHIRAMKEAL ASLTPRAQNE RAGHGISGLE ALQYDESMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMEKF LSEVTKVLKV PIMIDSTDEN VMARALTYIQ GKAVINSINL EDGEERFEKV TPLLRKYGAA IVVGTIDEDG MAVSAERKLE IAKRSYELLT TKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPEE EKRLADALLF ETTKETLEEF TNFYRVAKKK EVVVQEILTL DERLANYIVE GTKQGLHEDL SLALTEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILS NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAANIDIPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV KKEEKKVEIP AVIEPLPKSE VMVPDSTKRI VLRDVPVSHL APFLNRQMLL GHHLGLKGNV KKLLKEGDKR ARELNDLIDE LLVEGQSWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRVIE RFTFPRQGKA PYRTLGDYLR PIGDEMDYVA FLSVTVGEGV RDIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID C2VGX0_BACCE Unreviewed; 610 AA. AC C2VGX0; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 31. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=bcere0020_39540 {ECO:0000313|EMBL:EEL38743.1}; OS Bacillus cereus Rock3-29. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526984 {ECO:0000313|EMBL:EEL38743.1, ECO:0000313|Proteomes:UP000006652}; RN [1] {ECO:0000313|EMBL:EEL38743.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Rock3-29 {ECO:0000313|EMBL:EEL38743.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEL38743.1}. 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; ACMJ01000069; EEL38743.1; -; Genomic_DNA. DR RefSeq; WP_000770363.1; NZ_CM000731.1. DR EnsemblBacteria; EEL38743; EEL38743; bcere0020_39540. DR PATRIC; 25055886; VBIBacCer100535_4532. DR Proteomes; UP000006652; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006652}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 610 AA; 67123 MW; 396A987F8B877473 CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNVSDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVVQ INKAAVKLAK ASVTNRNAIL GTIGGMKHIG AVTTTDMERE FMLLEQAGAL LEEQVDGLLL ETFYDEFELL HAVKVLRKQT NIPIVAQVAL HEAGTTQNGN DVNEILKQLI DYGANVVGLN CQLGPLHMTE AFKMISIPQN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPKFIEQGI RLLGGCCGTT PEHIQSMKRA VANVTPVIEK DTIQRPKVVH THEKRSKVQV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRVSNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDVA LIEEVYEATK HLEQPIFIGI MPLVSKRNAD FLHFEVPGIT LPEEIRERMD GHETKEAAIE EGIRISQELI DAAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID C2VYW7_BACCE Unreviewed; 1132 AA. AC C2VYW7; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEL43846.1}; GN ORFNames=bcere0021_40500 {ECO:0000313|EMBL:EEL43846.1}; OS Bacillus cereus Rock3-42. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526985 {ECO:0000313|EMBL:EEL43846.1, ECO:0000313|Proteomes:UP000000325}; RN [1] {ECO:0000313|EMBL:EEL43846.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Rock3-42 {ECO:0000313|EMBL:EEL43846.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEL43846.1}. 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; ACMK01000122; EEL43846.1; -; Genomic_DNA. DR RefSeq; WP_000649731.1; NZ_CM000732.1. DR EnsemblBacteria; EEL43846; EEL43846; bcere0021_40500. DR PATRIC; 25068697; VBIBacCer34651_0703. DR Proteomes; UP000000325; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000325}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 125973 MW; CE416BF47A9053A3 CRC64; MKCIEEKLQN SILLLDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYELSHLDE ELNEKAARLA KQAVKESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGE VDVLLVETSQ DMRNVKAAYI GIQAAFDELK KIVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWVN IIGGCCGTTP EHIKAMKEAL ASLKPREHHE REGHGVSGLE ALQYDDSMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMENF LAEVTKVLKV PIMIDSTDEH VMERALTYIQ GKAVINSINL EDGEERFIKV TPLLQKYGAA IVVGTIDEDG MAVSAERKLE IAKRSYELLT TKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPDE EKRLADALLF ETTQETLEEF TNFYRVAKKK DVVVQETLTL DERLANYIVE GTKQGLHEDL SLALTEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILA NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAADIDIPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV TKEEKKVEIP AVIEPLPKSE VMVPDSTKRV VLRDVPALHL APFLNRQMLL GHHLGLKGSV KKLLKEGDKR AHELNDLIDE LLREGQSWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRVIE RFTFPRQGRA PYRTLGDYLR PIGDEMDYVA FLSVTVGEGV RDIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID C2VYW8_BACCE Unreviewed; 610 AA. AC C2VYW8; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 31. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=bcere0021_40510 {ECO:0000313|EMBL:EEL43847.1}; OS Bacillus cereus Rock3-42. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526985 {ECO:0000313|EMBL:EEL43847.1, ECO:0000313|Proteomes:UP000000325}; RN [1] {ECO:0000313|EMBL:EEL43847.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Rock3-42 {ECO:0000313|EMBL:EEL43847.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEL43847.1}. 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; ACMK01000122; EEL43847.1; -; Genomic_DNA. DR RefSeq; WP_000770339.1; NZ_CM000732.1. DR ProteinModelPortal; C2VYW8; -. DR EnsemblBacteria; EEL43847; EEL43847; bcere0021_40510. DR PATRIC; 25068699; VBIBacCer34651_0704. DR Proteomes; UP000000325; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000325}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 610 AA; 67229 MW; BE9C70CEB442A97B CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNISDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTE INRAAVKLAK ASVTDRNAIL GTIGGMKHIG AVTTTDMERE FMLLEQASAL LEEQVDGLLL ETFYDEFELL HAVQVLRKET NIPIVAQLAL HEAGTTQNGN DVNEILKQLL DYGTNVVGLN CQLGPLHMTE AFKMISIPKN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPKFIEQGI RLLGGCCGTT PEHIESMKRA TLNVTPVIEK DTIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRISNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATGF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIA LIEEVYEATK HLEQPIFIGI MPLISKRNAD FLHFEVPGIT LPEAVRERMD GHETKEAAIE EGIRISQELI DETMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID C2WC33_BACCE Unreviewed; 1133 AA. AC C2WC33; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEL49290.1}; GN ORFNames=bcere0022_34000 {ECO:0000313|EMBL:EEL49290.1}; OS Bacillus cereus Rock3-44. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526986 {ECO:0000313|EMBL:EEL49290.1, ECO:0000313|Proteomes:UP000006654}; RN [1] {ECO:0000313|EMBL:EEL49290.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Rock3-44 {ECO:0000313|EMBL:EEL49290.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEL49290.1}. 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; ACML01000201; EEL49290.1; -; Genomic_DNA. DR RefSeq; WP_001247363.1; NZ_CM000733.1. DR EnsemblBacteria; EEL49290; EEL49290; bcere0022_34000. DR PATRIC; 25078359; VBIBacCer125783_2272. DR Proteomes; UP000006654; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006654}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1133 AA; 125944 MW; 30FF8DFAEFDA45C3 CRC64; MRPIEERLRH DILILDGAMG TMIQQADLTA EDFGGEEYEG CNEYLVKTRP DVILHIHKAY IEAGADIIET NTFGATNIVL HDYELSHLDE ELNERAACLA KQAVRESGKE VYVAGAMGPT TKAISVTGGV TFEGLIEAYT RQARGLLRGG VDVLLVETSQ DMRNVKAAYL GIQQAFTEAN HTVPLMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR EHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPTSLAEKV KQFAEEGWIN IIGGCCGTTP DHIRAIKASL TSLKARKNHE REGHGISGLE ALQYDDSMRP LFVGERTNVI GSRKFKRLVA DGNFEEAAEI ARAQVKKNAH IIDICMADPD RDEVEDMENF LAEVTKVLKV PIMIDSTDEN VMAKALTYIQ GKGVINSINL ENGEERFEKV TPLLRKYGAA IVVGTIDEDG MAVCAERKLE IAKRSYELLT KKYGIRPSDI IFDALVFPVG TGDEEYIGSA EATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPEE EKKLADALLF ETTKETLEEF TNFYRVAKKK EGVIQETLTL DERLANYIVE GTKQGLQEDL SLALTEGRRP LDIINGPLMK GMDEVGRLFN NNELIVAEVL QSAESMKAAV AYLEPYMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILS NNGYDIVNLG INVRSDRIVQ EVKEKKPDII GLSGLLVKSA QQMVATAEDL QAANIDIPIV VGGAALTRKF TDNRISPSYN GLVLYASDAM TGLDLINRLQ KEEEREKMKQ EKKNRHLHAI VKQEEKKAEL PVVIEPLAPA EVMIPDSTKR VVLRDIPVSH LAPFLNRQML LGHHLGLKGN VKKLLREGDK RAHELNDLID ELLQEGQSWL RPKAVYQFFP AQSDGQTIII YDPEDHARVL ERFSFPRQGK APYRTLGDYL RPVGDEMDYV AFLSVTVGEG VRNIAEEWKE KGDYLRSHAI QSLALELAEG LAEKTHMLIR DRFGIPDSPE MTMEERFRTK YQGIRVSFGY PACPELADQE KLFRLIQPEE IGISLTEGFM MEPEASVTAM VFAHPEARYF SVL // ID C2WC34_BACCE Unreviewed; 610 AA. AC C2WC34; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 32. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=bcere0022_34010 {ECO:0000313|EMBL:EEL49291.1}; OS Bacillus cereus Rock3-44. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526986 {ECO:0000313|EMBL:EEL49291.1, ECO:0000313|Proteomes:UP000006654}; RN [1] {ECO:0000313|EMBL:EEL49291.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Rock3-44 {ECO:0000313|EMBL:EEL49291.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEL49291.1}. 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; ACML01000201; EEL49291.1; -; Genomic_DNA. DR RefSeq; WP_000697129.1; NZ_CM000733.1. DR ProteinModelPortal; C2WC34; -. DR EnsemblBacteria; EEL49291; EEL49291; bcere0022_34010. DR PATRIC; 25078357; VBIBacCer125783_2271. DR Proteomes; UP000006654; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006654}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 610 AA; 66908 MW; D0DFDA7C16FBEC07 CRC64; MKILDLLSKG IIIGDGAVGT LLHSHGLQSS FEELNLSDPD LIISIHKQYV AAGADIIQTN TYGANEAKLR TYGLENQVVQ INRAAVKLAK AAITDRNAIL GTIGGMKHIG AVTTTDMERE FMLLEQAGAL IEENVDGLLL ETFYDEFELL HAVKVLRKQT DIPIIAQLAL HEAGTTQNGN DVNEILEQLL DYGANVVGLN CQLGPLHMTE AFKMISIPKN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEE MTPKFIEQGI RLLGGCCGTT PAHIEAMKRA IANVTPVTEK QIVQRQQVVP MQTKRISTHV TLAEKAKKQT TVIVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRISNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNEGRSIL GKSIGSATRF SVGGAFNPHV RHLKAAVKRM ERKIAAGAEY FLTQPIYDVA LIGGVYEATK HLEQPIFIGI MPLVSKRNAD FLHFEVPGIT LPEEVRQRMD GHDTQESAIE EGIRISQELI DAAMKYFNGI YLITPFLKYE ITENLVNYVK EKQEVKEGVN // ID C2WM70_BACCE Unreviewed; 308 AA. AC C2WM70; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 07-JAN-2015, entry version 17. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEL56244.1}; GN ORFNames=bcere0023_21720 {ECO:0000313|EMBL:EEL56244.1}; OS Bacillus cereus Rock4-2. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526987 {ECO:0000313|EMBL:EEL56244.1, ECO:0000313|Proteomes:UP000001443}; RN [1] {ECO:0000313|EMBL:EEL56244.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Rock4-2 {ECO:0000313|EMBL:EEL56244.1}; 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. {ECO:0000313|EMBL:EEL56244.1}. 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; ACMM01000148; EEL56244.1; -; Genomic_DNA. DR EnsemblBacteria; EEL56244; EEL56244; bcere0023_21720. DR PATRIC; 25097834; VBIBacCer64089_1409. DR Proteomes; UP000001443; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001443}; KW Methyltransferase {ECO:0000313|EMBL:EEL56244.1}; KW Transferase {ECO:0000313|EMBL:EEL56244.1}. SQ SEQUENCE 308 AA; 34359 MW; 86157BFDBADD17A6 CRC64; MLLDGALATE LEAHGCNLDD PLWSARVLLE NPELIYQVHS DYFRAGADCA ITASYQATIS GFSARGIQEQ EALELIKKTV LLARRARDDF WKENTQTNRP KPLVVASVGP YGAYLADGSE YVGNYGVTDD TLADFHRSRM SALIEAGADL LAFETIPSLQ EARVLDTLLR EFPETYAWLS FSLKNEKEIS EGKKLVECAR AFEKSEQIVA IGINCAPVTV VTGAIQALRA NTKKSIIVYP NSGETYNPET KTWHGHEQCN TLNIQSEEWY QAGARLIGGC CRTTPYHIEE ISNKWRSSEF FYSNEAKQ // ID C2WSS5_BACCE Unreviewed; 856 AA. AC C2WSS5; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 01-APR-2015, entry version 35. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEL54307.1}; GN ORFNames=bcere0023_41470 {ECO:0000313|EMBL:EEL54307.1}; OS Bacillus cereus Rock4-2. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526987 {ECO:0000313|EMBL:EEL54307.1, ECO:0000313|Proteomes:UP000001443}; RN [1] {ECO:0000313|EMBL:EEL54307.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Rock4-2 {ECO:0000313|EMBL:EEL54307.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEL54307.1}. 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; ACMM01000188; EEL54307.1; -; Genomic_DNA. DR EnsemblBacteria; EEL54307; EEL54307; bcere0023_41470. DR PATRIC; 25101838; VBIBacCer64089_3418. DR Proteomes; UP000001443; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001443}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 856 AA; 94568 MW; A2469E3E0680363B CRC64; MKCIEEKLKN SILILDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYELSHLDE ELNEKAALLA KQAVKESGNE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGE VDVLLVETSQ DMRNVKAAYI GIQAAFEELK KTVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWVN IIGGCCGTTP EHIKAMKSAL ASLKPRDHHE REGHGISGLE ALQYDESMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMENF LAEVTKVLKV PIMIDSTDEN VMERALTYIQ GKAVINSINL EDGEERFKKV TPLLQKYGAA IVVGTIDEDG MAVSAERKIE IAKRSYELLT KKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPEE EKRLADALLF ETTKETLEEF TNFYRVAKKK DIVVQETLTL DERLANYIVE GTKQGLHEDL SLALEEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILA NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAANIDVPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV KKRRRK // ID C2WSS6_BACCE Unreviewed; 610 AA. AC C2WSS6; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 31. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=bcere0023_41480 {ECO:0000313|EMBL:EEL54308.1}; OS Bacillus cereus Rock4-2. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526987 {ECO:0000313|EMBL:EEL54308.1, ECO:0000313|Proteomes:UP000001443}; RN [1] {ECO:0000313|EMBL:EEL54308.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Rock4-2 {ECO:0000313|EMBL:EEL54308.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEL54308.1}. 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; ACMM01000188; EEL54308.1; -; Genomic_DNA. DR RefSeq; WP_000770357.1; NZ_CM000734.1. DR EnsemblBacteria; EEL54308; EEL54308; bcere0023_41480. DR PATRIC; 25101836; VBIBacCer64089_3417. DR Proteomes; UP000001443; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001443}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 610 AA; 67222 MW; 09DBD19A9941976F CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNVSDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTK INRAAVKLAK ASVTDKNAIL GTIGGMKHIG AVTTTDMERE FILLEQAGAL LEEQVDGLLL ETFYDEFELL HAVKVLRKQT NIPIVAQLAL HEAGTTQNGN DVNEILKQFI DYGANVVGLN CQLGPLHMTE AFKMISIPQN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPKFIEQGI RLLGGCCGTT PEHIQSMKRA VANITPVIEK ETIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRVSNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIK LIEEVYEATK HLEQPIFIGI MPLVSKRNAD FLHFEVPGIT LPEEIRERMD GHETKEAAIE EGIRISQELV DAAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID C2X2K1_BACCE Unreviewed; 1132 AA. AC C2X2K1; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEL59470.1}; GN ORFNames=bcere0024_39680 {ECO:0000313|EMBL:EEL59470.1}; OS Bacillus cereus Rock4-18. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526988 {ECO:0000313|EMBL:EEL59470.1, ECO:0000313|Proteomes:UP000001384}; RN [1] {ECO:0000313|EMBL:EEL59470.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Rock4-18 {ECO:0000313|EMBL:EEL59470.1}; 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 Bacillus cereus Rock4-18 genome."; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEL59470.1}. 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; ACMN01000074; EEL59470.1; -; Genomic_DNA. DR RefSeq; WP_000649699.1; NZ_CM000735.1. DR EnsemblBacteria; EEL59470; EEL59470; bcere0024_39680. DR GeneID; 23125961; -. DR PATRIC; 25089487; VBIBacCer120492_4658. DR Proteomes; UP000001384; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001384}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001384}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 125918 MW; EBBE986A6B85117F CRC64; MKCIEEKLQN NILILDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYELSHLDE ELNEKAARLA KQAVKESGNE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLNGE VDVLLVETSQ DMRNVKAAYI GIQAAFEELN KIVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWIN IIGGCCGTTP EHIKAMKEAL ASLTPREQNE RAGHGISGLE ALQYDESMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMEKF LSEVTKVLKV PIMIDSTDEN VMARALTYIQ GKAVINSINL EDGEERFEKV TPLLRKYGAA IVVGTIDEDG MAVSAERKLE IAKRSYELLT TKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPEE EKRLADALLF ETTKETLEEF TNFYRVAKKK EVVVQETLTL DERLANYIVE GTKQGLHEDL SLALTEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILS NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAANIDIPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV KKEEKKVEIP AVIEPLPKSE VMVPDSTKRI VLRDVPVSHL APFLNRQMLL GHHLGLKGNV KKLLKEGDKR AHELNDLIDE LLVEGQSWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRVIE RFTFPRQGKA PYRTLGDYLR PIGDEMDYVA FLSVTVGEGV RDIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID C2X2K2_BACCE Unreviewed; 610 AA. AC C2X2K2; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 30. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=bcere0024_39690 {ECO:0000313|EMBL:EEL59471.1}; OS Bacillus cereus Rock4-18. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526988 {ECO:0000313|EMBL:EEL59471.1, ECO:0000313|Proteomes:UP000001384}; RN [1] {ECO:0000313|EMBL:EEL59471.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Rock4-18 {ECO:0000313|EMBL:EEL59471.1}; 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 Bacillus cereus Rock4-18 genome."; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEL59471.1}. 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; ACMN01000074; EEL59471.1; -; Genomic_DNA. DR RefSeq; WP_000770362.1; NZ_CM000735.1. DR ProteinModelPortal; C2X2K2; -. DR EnsemblBacteria; EEL59471; EEL59471; bcere0024_39690. DR GeneID; 23125962; -. DR PATRIC; 25089489; VBIBacCer120492_4659. DR Proteomes; UP000001384; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001384}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000001384}. SQ SEQUENCE 610 AA; 67095 MW; EFB7C9453D5237C6 CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNVSDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVVQ INKAAVKLAK ASVTNRNAIL GTIGGMKHIG AVTTTDMERE FMLLEQAGAL LEEQVDGLLL ETFYDEFELL HAVKVLRKQT NIPIVAQVAL HEAGTTQNGN DVNEILKQLI DYGANVVGLN CQLGPLHMTE AFKMISIPQN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPKFIEQGI RLLGGCCGTT PEHIQSMKRA VANVTPVIEK DTIQRPKVVH THEKRSKAQV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRVSNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDVA LIEEVYEATK HLEQPIFIGI MPLVSKRNAD FLHFEVPGIT LPEEIRERMD GHETKEAAIE EGIRISQELI DAAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID C2X559_BACCE Unreviewed; 308 AA. AC C2X559; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 07-JAN-2015, entry version 16. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEL58513.1}; GN ORFNames=bcere0024_57130 {ECO:0000313|EMBL:EEL58513.1}; OS Bacillus cereus Rock4-18. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526988 {ECO:0000313|EMBL:EEL58513.1, ECO:0000313|Proteomes:UP000001384}; RN [1] {ECO:0000313|EMBL:EEL58513.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Rock4-18 {ECO:0000313|EMBL:EEL58513.1}; 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 Bacillus cereus Rock4-18 genome."; 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. {ECO:0000313|EMBL:EEL58513.1}. 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; ACMN01000156; EEL58513.1; -; Genomic_DNA. DR EnsemblBacteria; EEL58513; EEL58513; bcere0024_57130. DR PATRIC; 25093044; VBIBacCer120492_0657. DR Proteomes; UP000001384; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001384}; KW Methyltransferase {ECO:0000313|EMBL:EEL58513.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001384}; KW Transferase {ECO:0000313|EMBL:EEL58513.1}. SQ SEQUENCE 308 AA; 34394 MW; AE60BB021D3D3545 CRC64; MLLDGALATE LEAHGCNLDD PLWSARVLLE NPELIYQVHS DYFRAGADCA ITASYQATIS GFSARGIQEQ EALELIKKTV LLARRARDDF WKENTQTNRP KPLVVASVGP YGAYLADGSE YVGNYGVTDK TLADFHRSRM SALIEAGADL LAFETIPSLQ EARVLDTLLR EFPETYAWLS FSLKNEKEIS EGIKLVECAR AFEKSEQIVA IGINCAPVIV VTGAIQGLRA NTKKPIIVYP NSGETYNPET KTWHDHEQCN ALDIQSEEWY QAGARLIGGC CRTTPYHIEE ISNKWRSSEF FYSNEAKQ // ID C2XGQ9_BACCE Unreviewed; 1132 AA. AC C2XGQ9; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEL63312.1}; GN ORFNames=bcere0025_39260 {ECO:0000313|EMBL:EEL63312.1}; OS Bacillus cereus F65185. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526989 {ECO:0000313|EMBL:EEL63312.1, ECO:0000313|Proteomes:UP000000629}; RN [1] {ECO:0000313|EMBL:EEL63312.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F65185 {ECO:0000313|EMBL:EEL63312.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEL63312.1}. 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; ACMO01000104; EEL63312.1; -; Genomic_DNA. DR RefSeq; WP_000649688.1; NZ_CM000736.1. DR EnsemblBacteria; EEL63312; EEL63312; bcere0025_39260. DR PATRIC; 24947528; VBIBacCer123234_0341. DR Proteomes; UP000000629; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000629}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 126019 MW; 4496500B3180E385 CRC64; MKCIEEKLKN SILILDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYELSHLDE ELNEKAALLA KQAVKESGNE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGE VDVLLVETSQ DMRNVKAAYI GIQATFEELK KTVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWVN IIGGCCGTTP EHIKAMKSAL ASLKPRDHHE REGHGISGLE ALQYDESMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMENF LAEVTKVLKV PIMIDSTDEN VMERALTYIQ GKAVINSINL EDGEERFKKV TPLLQKYGAA IVVGTIDEDG MAVSAERKIE IAKRSYELLT KKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRFI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAILNTEK LERYASIPEE EKRLADALLF ETTKETLEEF TNFYRVAKKK DIVVQETLTL DERLANYIVE GTKQGLHEDL SLALEEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILA NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAANIDVPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV KKEEKKVEIP AVIEPLPKAE VIVPDSTKRI VLRDIPALHL APFLNRQMLL GHHLGLKGNV KKLLKEGDKR AHELNDLIDE LLQEGQSWLK PKAVYQFFPA QSDGQNIVIY NPEDHTRVIE RFTFPRQGKA PYRTLGDYLR PIGDEMDYVA FLSVTVGEGV RDIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID C2XGR0_BACCE Unreviewed; 610 AA. AC C2XGR0; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 31. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=bcere0025_39270 {ECO:0000313|EMBL:EEL63313.1}; OS Bacillus cereus F65185. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526989 {ECO:0000313|EMBL:EEL63313.1, ECO:0000313|Proteomes:UP000000629}; RN [1] {ECO:0000313|EMBL:EEL63313.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F65185 {ECO:0000313|EMBL:EEL63313.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEL63313.1}. 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; ACMO01000104; EEL63313.1; -; Genomic_DNA. DR RefSeq; WP_000770360.1; NZ_CM000736.1. DR ProteinModelPortal; C2XGR0; -. DR EnsemblBacteria; EEL63313; EEL63313; bcere0025_39270. DR PATRIC; 24947526; VBIBacCer123234_0340. DR Proteomes; UP000000629; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000629}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 610 AA; 67241 MW; 2994E829027824F4 CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNVSDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTK INRAAVKLAK ASVTDKNAIL GTIGGMKHIG AVTTTDMERE FMLLEQAGAL LEEQVDGLLL ETFYDEFELL HAVKVLRKQT NIPIVAQLAL HEAGTTQNGN DVNEILKQFI DYGANVVGLN CQLGPLHMTE AFKMISIPQN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPKFIEQGI RLLGGCCGTT PEHIQSMKRA VANITPVIEK ETIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRVSNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIK LIEEVYEATK HLEQPIFIGI MPLVSKRNAD FLHFEVPGIT LPEEIRERMD GHETKEAAIE EGIRISQELV DAAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID C2XK94_BACCE Unreviewed; 308 AA. AC C2XK94; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 07-JAN-2015, entry version 17. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEL62107.1}; GN ORFNames=bcere0025_51670 {ECO:0000313|EMBL:EEL62107.1}; OS Bacillus cereus F65185. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526989 {ECO:0000313|EMBL:EEL62107.1, ECO:0000313|Proteomes:UP000000629}; RN [1] {ECO:0000313|EMBL:EEL62107.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F65185 {ECO:0000313|EMBL:EEL62107.1}; 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. {ECO:0000313|EMBL:EEL62107.1}. 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; ACMO01000124; EEL62107.1; -; Genomic_DNA. DR EnsemblBacteria; EEL62107; EEL62107; bcere0025_51670. DR PATRIC; 24950073; VBIBacCer123234_1789. DR Proteomes; UP000000629; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000629}; KW Methyltransferase {ECO:0000313|EMBL:EEL62107.1}; KW Transferase {ECO:0000313|EMBL:EEL62107.1}. SQ SEQUENCE 308 AA; 34359 MW; 86157BFDBADD17A6 CRC64; MLLDGALATE LEAHGCNLDD PLWSARVLLE NPELIYQVHS DYFRAGADCA ITASYQATIS GFSARGIQEQ EALELIKKTV LLARRARDDF WKENTQTNRP KPLVVASVGP YGAYLADGSE YVGNYGVTDD TLADFHRSRM SALIEAGADL LAFETIPSLQ EARVLDTLLR EFPETYAWLS FSLKNEKEIS EGKKLVECAR AFEKSEQIVA IGINCAPVTV VTGAIQALRA NTKKSIIVYP NSGETYNPET KTWHGHEQCN TLNIQSEEWY QAGARLIGGC CRTTPYHIEE ISNKWRSSEF FYSNEAKQ // ID C2XZ88_BACCE Unreviewed; 1132 AA. AC C2XZ88; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEL69004.1}; GN ORFNames=bcere0026_40220 {ECO:0000313|EMBL:EEL69004.1}; OS Bacillus cereus AH603. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526990 {ECO:0000313|EMBL:EEL69004.1, ECO:0000313|Proteomes:UP000001753}; RN [1] {ECO:0000313|EMBL:EEL69004.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AH603 {ECO:0000313|EMBL:EEL69004.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEL69004.1}. 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; ACMP01000111; EEL69004.1; -; Genomic_DNA. DR RefSeq; WP_002067148.1; NZ_CM000737.1. DR EnsemblBacteria; EEL69004; EEL69004; bcere0026_40220. DR PATRIC; 24829923; VBIBacCer18372_0438. DR Proteomes; UP000001753; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001753}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 126106 MW; 620F3478F1814BD5 CRC64; MKRIEERLQH EILILDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVKTRP DVILNIHKVY IEAGADIIET NTFGATNIVL SDYALSHLDE ELNERAALLA KQAVKESGKA VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLRGE VDVLLVETSQ DMRNVKAAYI GIQSAFEELN KIVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR EHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPASLAEKV KRFAEEGWIN IIGGCCGTTP EHIRVMKSAL ASINPREHHE RVGHGISGLE ALQYDDSMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMERF LAEVTKVLKV PIMIDSTDEN VMAKALTYIQ GKGVINSINL EDGEERFEKV TPLLRKYGAA IVVGTIDEDG MAVSAERKIE IAKRSYELLT KKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYALIPEE EKRLADALLF ETTKETLEKF TNFYRVAKKK DVVIQETLTL DERLANYIVE GTKQGLQEDL SLALTEGRKP LDIINGPLMT GMDEVGRLFN GNELIVAEVL QSAESMKAAV SYLEPHMESS ESAKKGKVLL ATVKGDVHDI GKNLVEIILS NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAANIDIPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKR DKKERHLHIV KQEEKKIEIP AVIEPLPKAT VIVPDSTKRV VLRDIPALHL APFLNRQMLI GHHLGLKGNV KKLLQEGDKR AHELNDLIDE LLQEGQSWLR PKAVYQFFPA QSDGQNIIIY DPEDHTRIIE RFEFPRQGKA PYRTLGDYIR PIGDEIDYVA FLSVTVGEGV RDIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID C2XZ89_BACCE Unreviewed; 610 AA. AC C2XZ89; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 31. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=bcere0026_40230 {ECO:0000313|EMBL:EEL69005.1}; OS Bacillus cereus AH603. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526990 {ECO:0000313|EMBL:EEL69005.1, ECO:0000313|Proteomes:UP000001753}; RN [1] {ECO:0000313|EMBL:EEL69005.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AH603 {ECO:0000313|EMBL:EEL69005.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEL69005.1}. 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; ACMP01000111; EEL69005.1; -; Genomic_DNA. DR RefSeq; WP_002067147.1; NZ_CM000737.1. DR ProteinModelPortal; C2XZ89; -. DR EnsemblBacteria; EEL69005; EEL69005; bcere0026_40230. DR PATRIC; 24829921; VBIBacCer18372_0437. DR Proteomes; UP000001753; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001753}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 610 AA; 67037 MW; 5CDEE5A0A7F61E61 CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNLSDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVVQ INKAAVNIAK ASVTDRNAIL GTIGGMKHIG AVTTTDIERE FMLLEQAGAL LEEQVDGLLL ETFYDEFELL HAVKVLRKQT SIPIVAQLAL HEAGTTQNGN DVNEILKQLL DYGANVVGLN CQLGPLHMTE AFKMISIPQN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEE MTPNFIEQGI RLLGGCCGTT PEHIEGMKRA IANVAPVIAK ETIQRPKVVH THEKRSRAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRVSNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDVA LIEEVYEATK HLEQPIFIGI MPLVSKRNAD FLHFEVPGIT LPEEIRKRMD GHETKEAAIE EGIHISQELI DAAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID C2Y337_BACCE Unreviewed; 308 AA. AC C2Y337; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 07-JAN-2015, entry version 17. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEL67655.1}; GN ORFNames=bcere0026_53850 {ECO:0000313|EMBL:EEL67655.1}; OS Bacillus cereus AH603. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526990 {ECO:0000313|EMBL:EEL67655.1, ECO:0000313|Proteomes:UP000001753}; RN [1] {ECO:0000313|EMBL:EEL67655.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AH603 {ECO:0000313|EMBL:EEL67655.1}; 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. {ECO:0000313|EMBL:EEL67655.1}. 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; ACMP01000161; EEL67655.1; -; Genomic_DNA. DR EnsemblBacteria; EEL67655; EEL67655; bcere0026_53850. DR PATRIC; 24832671; VBIBacCer18372_1822. DR Proteomes; UP000001753; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001753}; KW Methyltransferase {ECO:0000313|EMBL:EEL67655.1}; KW Transferase {ECO:0000313|EMBL:EEL67655.1}. SQ SEQUENCE 308 AA; 34458 MW; 6E6062583331FDFB CRC64; MLLDGALATE LEAHGCNLDD PLWSARVLLE NPELIYQVHS DYFRAGADCA ITASYQATIS GFSARGIQEQ EALELIKKTV LLARRARDDF WKENTQTNRP KPLVVASVGP YGAYLADGSE YVGNYGVTDK TLADFHRSRM SALIEAGADL LAFETIPSLQ EARVLDTLLR EFPETYAWLS FSLKNEKEIS EGMKLVECAR AFEKSEQIVA IGINCAPVTV VTGAIQELRA NTKKPIIIYP NSGETYNPET KTWHGHEQCN TLDIQSEEWY QAGARLIGGC CRTTPYHIEE ISNKWRSSEF FYSNEAKQ // ID C2YWJ2_BACCE Unreviewed; 1132 AA. AC C2YWJ2; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEL80357.1}; GN ORFNames=bcere0028_39500 {ECO:0000313|EMBL:EEL80357.1}; OS Bacillus cereus AH1271. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526992 {ECO:0000313|EMBL:EEL80357.1, ECO:0000313|Proteomes:UP000001354}; RN [1] {ECO:0000313|EMBL:EEL80357.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AH1271 {ECO:0000313|EMBL:EEL80357.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEL80357.1}. 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; ACMR01000167; EEL80357.1; -; Genomic_DNA. DR RefSeq; WP_000649706.1; NZ_CM000739.1. DR EnsemblBacteria; EEL80357; EEL80357; bcere0028_39500. DR PATRIC; 24793397; VBIBacCer17091_1809. DR Proteomes; UP000001354; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001354}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 125763 MW; 7B22741CE7A7D955 CRC64; MKCIEEKLQN NILILDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYELSHLDE ELNEKAARLA KQAVNESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLNGG VDVLLVETSQ DMRNVKAAYI GIQAAFDELN KIVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWVN IIGGCCGTTP EHVKAMKSAL ASLKPREQQE RAGHGVSGLE ALQYDDSMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMENF LAEVTKVLKV PIMIDSTDEN VMERALTYIQ GKAVINSINL EDGEERFKKV TPLLRKYGAA IVVGTIDEDG MAVSAERKLE IAKRSYELLT TKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPEE EKRLADALLF ETTQETLEKF TNFYRVAKKK DVVIQETLTL DERLANYIVE GTKQGLQEDL SLALTEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILS NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAANIDVPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV EKEEKKVEIP AVIEPLPKAE VIVPDSTKRI VLRDIPALHL APFLNRQMLL GHHLGLKGSV KKLLREGDKR AHELNDLIDE LLQEGQSWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRVIE RFTFPRQGKA PYRTLGDYLR SVGDEMDYVA FLSVTVGEGV RDIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID C2YWJ3_BACCE Unreviewed; 610 AA. AC C2YWJ3; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 31. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=bcere0028_39510 {ECO:0000313|EMBL:EEL80358.1}; OS Bacillus cereus AH1271. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526992 {ECO:0000313|EMBL:EEL80358.1, ECO:0000313|Proteomes:UP000001354}; RN [1] {ECO:0000313|EMBL:EEL80358.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AH1271 {ECO:0000313|EMBL:EEL80358.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEL80358.1}. 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; ACMR01000167; EEL80358.1; -; Genomic_DNA. DR RefSeq; WP_000770325.1; NZ_CM000739.1. DR ProteinModelPortal; C2YWJ3; -. DR EnsemblBacteria; EEL80358; EEL80358; bcere0028_39510. DR PATRIC; 24793395; VBIBacCer17091_1808. DR Proteomes; UP000001354; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001354}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 610 AA; 67267 MW; 338DFBD8CDC81376 CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNISDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTE INRAAVKLAK ASVTDRNAIL GTIGGMKHIG AVTTTDMERE FMLLEQASAL LEEQVDGLLL ETFYDEFELL HAVQVIRKQT NIPIVAQLAL HEAGTTQNGN DVNEILKQLL DYGANVVGLN CQLGPLHMTE AFKMISIPQN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPKFIEQGI RLLGGCCGTT PEHIESMKRA TLNVTPVIEK DTIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRVSNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIA LIEEVYEATK HLEQPIFIGI MPLISKRNAD FLHFEVPGIT LPEEIRERMD GHETKEAAIE EGIRISQELI DAAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID C2ZCV0_BACCE Unreviewed; 1132 AA. AC C2ZCV0; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEL86184.1}; GN ORFNames=bcere0029_40110 {ECO:0000313|EMBL:EEL86184.1}; OS Bacillus cereus AH1272. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526993 {ECO:0000313|EMBL:EEL86184.1, ECO:0000313|Proteomes:UP000001750}; RN [1] {ECO:0000313|EMBL:EEL86184.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AH1272 {ECO:0000313|EMBL:EEL86184.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEL86184.1}. 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; ACMS01000184; EEL86184.1; -; Genomic_DNA. DR RefSeq; WP_000649666.1; NZ_CM000740.1. DR EnsemblBacteria; EEL86184; EEL86184; bcere0029_40110. DR PATRIC; 24805303; VBIBacCer63391_2097. DR Proteomes; UP000001750; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001750}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 126053 MW; CFFCC1982F5D3BC2 CRC64; MKCIEEKLKN NILILDGAMG TMIQQEDLTA EDFGGEDYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYELSHLDE ELNEKAALLA KQAVKESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGE IDVLLVETSQ DMRNVKAAYI GIQAAFDELN KTVPIMISGT IEPMGTTLAG QTIEAFYLSI EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWIN IIGGCCGTTP EHIRAMKSAL ASLKPREQHE REGHGVSGLE ALQYDDSMRP LFVGERTNVI GSRKFKRLIA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMERF LAEVTKVLKV PIMIDSTDEN VMARALTYIQ GKGVINSINL EDGEERFEKV TPLLRKYGAA IVVGTIDEDG MAVSAERKIE IAKRSYELLT KKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPEE EKRLADALLF ETTKETLEEF TNFYRVAKKK DVVVQETLTL DERLANYIVE GTKQGLHEDL SLALTEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKASV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILS NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAANIDIPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV KKEEKPVEIP AVIEPLPKAE VMIPDSTKRI VLRDIPVAHL APFLNRQMLL GHHLGLKGNV KKLLQEGDRR AHELNDLIDE LLQEGQSWLR PKAVYQFFPA QSDGQNIVIY DPEDHTRIIE RFTFPRQGKA PYRTLGDYLR PIGDEMDYVA FLSVTVGEGV RDIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIQPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID C2ZCV1_BACCE Unreviewed; 610 AA. AC C2ZCV1; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 31. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=bcere0029_40120 {ECO:0000313|EMBL:EEL86185.1}; OS Bacillus cereus AH1272. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526993 {ECO:0000313|EMBL:EEL86185.1, ECO:0000313|Proteomes:UP000001750}; RN [1] {ECO:0000313|EMBL:EEL86185.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AH1272 {ECO:0000313|EMBL:EEL86185.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEL86185.1}. 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; ACMS01000184; EEL86185.1; -; Genomic_DNA. DR RefSeq; WP_000770347.1; NZ_CM000740.1. DR EnsemblBacteria; EEL86185; EEL86185; bcere0029_40120. DR PATRIC; 24805301; VBIBacCer63391_2096. DR Proteomes; UP000001750; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001750}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 610 AA; 67224 MW; 94E935268693AF0F CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNLSDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVVQ INKAAVKIAK ASVTERNAIL GTIGGMKHIG AVTTTDMERE FMLLEQAGAL LEEQVDGLLL ETFYDEFELL HAVKVLRKQT NIPIVAQLAL HEAGTTQNGN DVNEILKQLI DYGANVVGLN CQLGPLHMTE AFKMISIPQN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTLKFIEQGI RLLGGCCGTT PEHIESMKRA TLNVTPVIEK DTIQRPKVVH THEKRSKSHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRVSNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDVA LIEEVYEATK HLEQPIFIGI MPLVSKRNAD FLHFEVPGIT LPEEIRERMD GHETKEAAIE EGIRISQELI DAAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID C3AQL7_BACMY Unreviewed; 1132 AA. AC C3AQL7; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 41. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEM04056.1}; GN ORFNames=bmyco0002_34990 {ECO:0000313|EMBL:EEM04056.1}; OS Bacillus mycoides Rock1-4. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526998 {ECO:0000313|EMBL:EEM04056.1, ECO:0000313|Proteomes:UP000001053}; RN [1] {ECO:0000313|EMBL:EEM04056.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Rock1-4 {ECO:0000313|EMBL:EEM04056.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEM04056.1}. 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; ACMV01000225; EEM04056.1; -; Genomic_DNA. DR RefSeq; WP_003200386.1; NZ_CM000743.1. DR EnsemblBacteria; EEM04056; EEM04056; bmyco0002_34990. DR GeneID; 23108257; -. DR PATRIC; 25173999; VBIBacMyc56145_2286. DR Proteomes; UP000001053; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001053}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001053}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 125864 MW; 46FDA7BA18FFCA55 CRC64; MRPIEERLQH DILILDGAMG TMIQQADLTA EDFGGEEYEG CNEYLVKTRP DVILGIHKAY IEAGADIIET NTFGATNIVL HDYELSHLDE ELNERAAFLA KQAVKESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLRGG VDVLLVETSQ DMRNVKAAYL GIQEAFTEAN HTVPLMISGT IEPMGTTLAG QTIEAFYLSI EHMKPLSVGL NCATGPEFMR EHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPTSLAEKV KQFAKEGWIN IIGGCCGTTP DHIRAIKVSL ESLEPRENHE REGHAISGLE ALQYDDSMRP LFVGERTNVI GSRKFKRLVA EGNFAEAAEI ARAQVKENAH IIDICMADPD RDEVEDMENF LAEVTKVLKV PIMIDSTDDN VMAKALTYIQ GKGVINSINL ENGEERFEKV TPLLHKYGAA IVVGTIDEEG MAVSAERKLE IAKRSYELLT KKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KESLPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPEE EKELADALLF ETTKETLEEF TNFYRVAKKK EAVIQETLTL DERLANYIVE GTKQGLHEDL SFALTEGRKP LDIINGPLMM GMDEVGRLFN NNELIVAEVL QSAESMKAAV AYLEPYMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILS NNGYDIVNLG INVRSDRIVQ EVKEKKPDII GLSGLLVKSA QQMVATAEDL QAANIDIPIV VGGAALTRKF TDNRISPSYN GLVLYASDAM TGLDLINRLQ KEEEREKMKQ DKKNRHIHVV KQEEKKVEKP AVIEPLPKAK VMVPDSTKRV VLRDIPVSHL APFLNRQMLI GHHLGLKGNV KKLLKEGDKR AHELNNLIDE LLQEGQSWLC SKAVYQFFPA QSDGQTIIIY DPEDRTRVLE RFSFPRQGKA PYRTLGDYLR PVGDEMDYVA FLSVTVGQGV RDIAEEWKEK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RFGIPDSPEM TMEERFRTKY QGIRVSFGYP ACPELADQEK LFRLIQPEEI GISLTEGFMM EPEASVTAMV FAHPEARYFS VL // ID C3AQL8_BACMY Unreviewed; 610 AA. AC C3AQL8; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 32. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=bmyco0002_35000 {ECO:0000313|EMBL:EEM04057.1}; OS Bacillus mycoides Rock1-4. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526998 {ECO:0000313|EMBL:EEM04057.1, ECO:0000313|Proteomes:UP000001053}; RN [1] {ECO:0000313|EMBL:EEM04057.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Rock1-4 {ECO:0000313|EMBL:EEM04057.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEM04057.1}. 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; ACMV01000225; EEM04057.1; -; Genomic_DNA. DR RefSeq; WP_003200385.1; NZ_CM000743.1. DR ProteinModelPortal; C3AQL8; -. DR EnsemblBacteria; EEM04057; EEM04057; bmyco0002_35000. DR GeneID; 23108256; -. DR PATRIC; 25173997; VBIBacMyc56145_2285. DR Proteomes; UP000001053; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001053}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000001053}. SQ SEQUENCE 610 AA; 66915 MW; 7B6454E3F0919BB3 CRC64; MKILDLVSKG IVIGDGAIGT LLHSHGLQSS FEELNLSDPD LIISIHKQYV AAGADIIQTN TYGANEAKLR MYGLENQVTQ INKAAVKLAK AAVTDKNAIL GTIGGMKHIG AVTTTDMERE FMLLEQAGAL LEEKVDGLLL ETFYDEFELL HAVKVLRKQT DIPIIAQLAL HEAGATQNGN DVNGILTQLL DYGANVVGLN CQLGPLHMTE AFKMISIPKN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEE MTPKFIEQGI RLLGGCCGTT PAHIEGMKRV IANVTPVTEK QIVQRQQVVH IQTKRASTHI TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRISNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIAAGAEY FLTQPIYDVA LIEEIYEATK HLEKPIFIGI MPLVSKRNAD FLHFEVPGIT LPEEVRQRMD GHETQESAIE EGIRISQELI NAAMKYFNGI YLITPFLKYE ITENLVKYVK EKQDVKEGIN // ID C3BPZ3_9BACI Unreviewed; 1132 AA. AC C3BPZ3; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEM15287.1}; GN ORFNames=bpmyx0001_37360 {ECO:0000313|EMBL:EEM15287.1}; OS Bacillus pseudomycoides DSM 12442. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=527000 {ECO:0000313|EMBL:EEM15287.1, ECO:0000313|Proteomes:UP000001378}; RN [1] {ECO:0000313|EMBL:EEM15287.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 12442 {ECO:0000313|EMBL:EEM15287.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEM15287.1}. 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; ACMX01000071; EEM15287.1; -; Genomic_DNA. DR RefSeq; WP_006096012.1; NZ_CM000745.1. DR EnsemblBacteria; EEM15287; EEM15287; bpmyx0001_37360. DR PATRIC; 25198221; VBIBacPse118422_4192. DR Proteomes; UP000001378; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001378}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 125862 MW; F9F7FA8352E4357E CRC64; MRPIEERLQH DILILDGAMG TMIQQADLTA EDFGGEEYEG CNEYLVKTRP DVILGIHKAY IEAGADIIET NTFGATNIVL HDYELSHLDE ELNERAAFLA KQAVKESDKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLRGG VDVLLVETSQ DMRNVKAAYL GIQEAFTEAN HTVPLMISGT IEPMGTTLAG QTIEAFYLSI EHMKPLSVGL NCATGPEFMR EHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPTSLAEKV KQFAKEGWIN IIGGCCGTTP DHIRAIKVSL ESLEPRENHE REGHGISGLE ALQYDDSMRP LFVGERTNVI GSRKFKRLVA EGNFAEAAEI ARAQVKENAH IIDICMADPD RDEVEDMENF LAEVTKVLKV PIMIDSTDDN VMAKALTYIQ GKGVINSINL ENGEERFEKV TPLLHKYGAA IVVGTIDEEG MAVSAERKLE IAKRSYELLT KKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KESLPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPEE EKELADALLF ETTKETLEEF TNFYRVAKKK EAVIQETLTL DERLANYIVE GTKQGLHEDL SFALTEGRKP LDIINGPLMM GMDEVGRLFN NNELIVAEVL QSAESMKAAV AYLEPYMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILS NNGYDILNLG INVRSDRIVQ EVKEKKPDII GLSGLLVKSA QQMVATAEDL QAANIDIPIV VGGAALTRKF TDNRISPSYN GLVLYASDAM TGLDLINQLQ KEEEREKMKQ DKKNRHIHVV KQEEKKVEKP AVIEPLPKAK VMVPDSTKRV VLRDIPVSHL APFLNRQMLI SHHLGLKGNV KKLLKEGDKR AHELNNLIDE LLQGGQSWLC PKAVYQFFPA QSDGQTIIIY DPEDRTRVLE RFSFPRQGKA PYRTLGDYLR PVGDEMDYVA FLSVTVGQGV RDIAEEWKEK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RFGIPDSPEM TMEERFRTKY QGIRVSFGYP ACPELADQEK LFRLIQPEEI GISLTEGFMM EPEASVTAMV FAHPEARYFS VL // ID C3BPZ4_9BACI Unreviewed; 610 AA. AC C3BPZ4; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 31. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=bpmyx0001_37370 {ECO:0000313|EMBL:EEM15288.1}; OS Bacillus pseudomycoides DSM 12442. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=527000 {ECO:0000313|EMBL:EEM15288.1, ECO:0000313|Proteomes:UP000001378}; RN [1] {ECO:0000313|EMBL:EEM15288.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 12442 {ECO:0000313|EMBL:EEM15288.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEM15288.1}. 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; ACMX01000071; EEM15288.1; -; Genomic_DNA. DR RefSeq; WP_006096011.1; NZ_CM000745.1. DR ProteinModelPortal; C3BPZ4; -. DR EnsemblBacteria; EEM15288; EEM15288; bpmyx0001_37370. DR PATRIC; 25198219; VBIBacPse118422_4191. DR Proteomes; UP000001378; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001378}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 610 AA; 66901 MW; 61E0395D39A6393F CRC64; MKILDLVSKG IVIGDGAIGT LLHSHGLQSS FEELNLSDPD LIISIHKQYV AAGADIIQTN TYGANEAKLR MYGLENQVTQ INKAAVKLAK AAVTDKNAIL GTIGGMKHIG AVTTTDMERE FMLLEQAGAL LEEKVDGLLL ETFYDEFELL HAVKVLRKQT DIPIIAQLAL HEAGATQNGN DVNGILTQLL DYGANVVGLN CQLGPLHMTE AFKMISIPKN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEE MTPKFIEQGI RLLGGCCGTT PAHIEGMKRV IANVTPVTEK QIVQRQQVVH IQTKRASTHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRISNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIAAGAEY FLTQPIYDVA LIEEIYEATK HLEKPIFIGI MPLVSKRNAD FLHFEVPGIT LPEEVRQRMD GHETQESAIE EGIRISQELI NAAMKYFNGI YLITPFLKYE ITENLVKYVK EKQDVKEGIN // ID C3C7X5_BACTU Unreviewed; 1132 AA. AC C3C7X5; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEM20681.1}; GN ORFNames=bthur0001_41740 {ECO:0000313|EMBL:EEM20681.1}; OS Bacillus thuringiensis serovar tochigiensis BGSC 4Y1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527024 {ECO:0000313|EMBL:EEM20681.1, ECO:0000313|Proteomes:UP000001913}; RN [1] {ECO:0000313|EMBL:EEM20681.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BGSC 4Y1 {ECO:0000313|EMBL:EEM20681.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEM20681.1}. 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; ACMY01000097; EEM20681.1; -; Genomic_DNA. DR RefSeq; WP_000649719.1; NZ_CM000746.1. DR EnsemblBacteria; EEM20681; EEM20681; bthur0001_41740. DR PATRIC; 31023233; VBIBacThu51894_5551. DR Proteomes; UP000001913; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001913}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 125902 MW; DBCA68F1295A27F5 CRC64; MKCIEEKLQN NILLLDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYELSYLDE ELNEKAARLA KQAVEESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGE VDVLLVETSQ DMRNVKAAYI GIQAAFDELN KIVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWVN IIGGCCGTTP EHIKAMKSAL ASLKPREQQE RAGHGVSGLE ALQYDDSMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMENF LAEVTKVLKV PIMIDSTDEN VMERALTYIQ GKAVINSINL EDGEERFIKV TPLLQKYGAA IVVGTIDEDG MAVSAERKLE IAKRSYELLT TKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KETLPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPEE EKRLADALLF ETTQETLEEF TNFYRAAKKK DVVIQETLTL DERLANYIVE GTKQGLHEDL SLALTEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILA NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAADIDIPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV TKEEKKVEIP AVIEPLPKSE VMVPDSTKRI VLRDIPALHL APFLNRQMLL GHHLGLKGSV KKLLREGDKR AHELNDLIDE LLQEGQSWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRVIE RFTFPRQGKA PYRTLGDYLR PIGDEMDYVA FLSVTVGEGV RDIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID C3C7X6_BACTU Unreviewed; 610 AA. AC C3C7X6; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 33. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=bthur0001_41750 {ECO:0000313|EMBL:EEM20682.1}; OS Bacillus thuringiensis serovar tochigiensis BGSC 4Y1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527024 {ECO:0000313|EMBL:EEM20682.1, ECO:0000313|Proteomes:UP000001913}; RN [1] {ECO:0000313|EMBL:EEM20682.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BGSC 4Y1 {ECO:0000313|EMBL:EEM20682.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEM20682.1}. 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; ACMY01000097; EEM20682.1; -; Genomic_DNA. DR RefSeq; WP_000770330.1; NZ_CM000746.1. DR ProteinModelPortal; C3C7X6; -. DR EnsemblBacteria; EEM20682; EEM20682; bthur0001_41750. DR PATRIC; 31023231; VBIBacThu51894_5550. DR Proteomes; UP000001913; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001913}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 610 AA; 67210 MW; 2A5E2353CD2C989C CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNISDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTE INRAAVKLAK ASVTDRNAIL GTIGGMKHIG AVTTTDMERE FMLLEQASAL LEEQVDGLLL ETFYDEFELL HAVQVLRKET NIPIVAQLAL HEAGTTQNGN DVNEILKQLL DYGANVVGLN CQLGPLHMTE AFKMISIPKN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPKFIEQGI RLLGGCCGTT PEHIESMKRA TLNVTPVIEK DTIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRISNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIA LIEEVYEATK HLEQPIFIGI MPLISKRNAD FLHFEVPGIT LPEAVRERMD GHETKEAAIE EGIRISQELI DAAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID C3CP28_BACTU Unreviewed; 1132 AA. AC C3CP28; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 43. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEM26996.1}; GN ORFNames=bthur0002_41040 {ECO:0000313|EMBL:EEM26996.1}; OS Bacillus thuringiensis Bt407. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527021 {ECO:0000313|EMBL:EEM26996.1, ECO:0000313|Proteomes:UP000001233}; RN [1] {ECO:0000313|EMBL:EEM26996.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Bt407 {ECO:0000313|EMBL:EEM26996.1}; 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. {ECO:0000313|EMBL:EEM26996.1}. 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; ACMZ01000101; EEM26996.1; -; Genomic_DNA. DR RefSeq; WP_000649720.1; NZ_CM000747.1. DR RefSeq; YP_006929016.1; NC_018877.1. DR EnsemblBacteria; AFV20079; AFV20079; BTB_c43970. DR EnsemblBacteria; EEM26996; EEM26996; bthur0002_41040. DR KEGG; btg:BTB_c43970; -. DR PATRIC; 26097767; VBIBacThu117809_0170. DR KO; K00548; -. DR Proteomes; UP000001233; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001233}; KW Reference proteome {ECO:0000313|Proteomes:UP000001233}. SQ SEQUENCE 1132 AA; 125985 MW; 3BA40F322F8A7B3F CRC64; MKCIEEKLQN SILILDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYELSHLDE ELNEKAALLA KQAVKESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGE VDVLLVETSQ DMRNVKAAYI GIQAAFEELK KTVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWIN IIGGCCGTTP EHIKAMKEAL ASLKPRDHHE REGHGISGLE ALQYDESMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMEKF LTEVTKVLKV PIMIDSTDEN VMARALTYIQ GKAVINSINL EDGEERFEKV TPLLRKYGAA IVVGTIDEDG MAVSAERKLE IAKRSYELLT TKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPEE EKHLADALLF ETTKETLEEF TNFYRVAKKK DVVVQETLTL DERLANYIVE GTKQGLHEDL SLALEEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILA NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAANIDVPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV KKEEKKVEIP AVIEPLPKAE VMVPDSTKRI VLRDIPALHL APFLNRQMLL GHHLGLKGNV KKLLKEGDKR AHELNDLIDE LLQEGQSWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRVIE RFTFPRQGKA PYRTLGDYLR PIGDEMDYVA FLSVTVGEGV RDIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID C3CP29_BACTU Unreviewed; 610 AA. AC C3CP29; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 35. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=bthur0002_41050 {ECO:0000313|EMBL:EEM26997.1}; OS Bacillus thuringiensis Bt407. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527021 {ECO:0000313|EMBL:EEM26997.1, ECO:0000313|Proteomes:UP000001233}; RN [1] {ECO:0000313|EMBL:EEM26997.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Bt407 {ECO:0000313|EMBL:EEM26997.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEM26997.1}. 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; ACMZ01000101; EEM26997.1; -; Genomic_DNA. DR RefSeq; WP_000770353.1; NZ_CM000747.1. DR RefSeq; YP_006929017.1; NC_018877.1. DR ProteinModelPortal; C3CP29; -. DR EnsemblBacteria; AFV20080; AFV20080; BTB_c43980. DR EnsemblBacteria; EEM26997; EEM26997; bthur0002_41050. DR KEGG; btg:BTB_c43980; -. DR PATRIC; 26097765; VBIBacThu117809_0169. DR KO; K00547; -. DR Proteomes; UP000001233; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001233}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000001233}. SQ SEQUENCE 610 AA; 67159 MW; D96AD95B688315AB CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNVSDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTE INRAAVKLAK ASVTDKNAIL GTIGGMKHIG AVTTTDMERE FMLLEQAGAL LEEQVDGLLL ETFYDEFELL HAVKVLRKQT NIPIVAQLAL HEAGTTQNGN DVNEILKQLI DYGANVVGLN CQLGPLHMTE AFKMISIPQN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPRFIEQGI RLLGGCCGTT PEHIQSMKHA VANVTPVIEK DTIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRISNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIA LIEEVYEATK HLEQPIFIGI MPLVSKRNAD FLHFEVPGIT LPEEIRERMD GHETKEAAIE EGIRISQELI DAAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID C3DQ64_BACTS Unreviewed; 709 AA. AC C3DQ64; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 38. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEM39920.1}; GN ORFNames=bthur0004_41210 {ECO:0000313|EMBL:EEM39920.1}; OS Bacillus thuringiensis serovar sotto str. T04001. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527026 {ECO:0000313|EMBL:EEM39920.1, ECO:0000313|Proteomes:UP000001375}; RN [1] {ECO:0000313|EMBL:EEM39920.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=T04001 {ECO:0000313|EMBL:EEM39920.1}; 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. {ECO:0000313|EMBL:EEM39920.1}. 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; ACNB01000131; EEM39920.1; -; Genomic_DNA. DR RefSeq; WP_003280029.1; NZ_CM000749.1. DR EnsemblBacteria; EEM39920; EEM39920; bthur0004_41210. DR PATRIC; 28960367; VBIBacThu7424_1486. DR Proteomes; UP000001375; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001375}. SQ SEQUENCE 709 AA; 78327 MW; 7F405812CE7F26D4 CRC64; MKCIEEKLQN SILILDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYELSHLDE ELNEKAALLA KQAVKESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGE VDVLLVETSQ DMRNVKAAYI GIQAAFEEMK KTVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWVN IIGGCCGTTP EHIKAMKSAL ASLKPRDHHE REGHGISGLE ALQYDESMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMEKF LTEVTKVLKV PIMIDSTDEN VMARALTYIQ GKAVINSINL EDGEERFEKV TPLLRKYGAA IVVGTIDEDG MAVSAERKLE IAKRSYELLT TKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPEE EKHLADALLF ETTKETLEEF TNFYRVAKKK DVVVQETLTL NERLANYIVE GTKQGLHEDL SLALEEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPYMESS DSDEKGKYY // ID C3DQ65_BACTS Unreviewed; 610 AA. AC C3DQ65; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 32. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=bthur0004_41220 {ECO:0000313|EMBL:EEM39921.1}; OS Bacillus thuringiensis serovar sotto str. T04001. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527026 {ECO:0000313|EMBL:EEM39921.1, ECO:0000313|Proteomes:UP000001375}; RN [1] {ECO:0000313|EMBL:EEM39921.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=T04001 {ECO:0000313|EMBL:EEM39921.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEM39921.1}. 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; ACNB01000131; EEM39921.1; -; Genomic_DNA. DR RefSeq; WP_000770367.1; NZ_CM000749.1. DR ProteinModelPortal; C3DQ65; -. DR EnsemblBacteria; EEM39921; EEM39921; bthur0004_41220. DR PATRIC; 28960365; VBIBacThu7424_1485. DR Proteomes; UP000001375; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001375}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 610 AA; 67232 MW; FAEE1FDEE089A711 CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNVSDPD LIISIHKQYV AAGADVIQTN TYGANETKLR MYGLENQVTE INRAAVKLAK ASVTDRNAIL GTIGGMKHIG AVTTTDMERE FMLLEQAGAL LEEQVDGLLL ETFYDEFELL HAVKVLRKQT NIPIVAQLAL HEAGTTQNGN DVNEILKQLI DCGANVVGLN CQLGPLHMTE AFKMISIPQN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPRFIEQGI RLLGGCCGTT PEHIQSMKRA VANITPVIEK DTIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRISNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIA LIEEVYEATK HLEQPIFIGI MPLVSKRNAD FLHFEVPGIT LPEEIRERMD GHETKEAAIE EGIRISQELI DIAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID C3E8J1_BACTU Unreviewed; 1132 AA. AC C3E8J1; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEM46088.1}; GN ORFNames=bthur0005_39860 {ECO:0000313|EMBL:EEM46088.1}; OS Bacillus thuringiensis serovar pakistani str. T13001. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527027 {ECO:0000313|EMBL:EEM46088.1, ECO:0000313|Proteomes:UP000001911}; RN [1] {ECO:0000313|EMBL:EEM46088.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=T13001 {ECO:0000313|EMBL:EEM46088.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEM46088.1}. 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; ACNC01000149; EEM46088.1; -; Genomic_DNA. DR RefSeq; WP_000649678.1; NZ_CM000750.1. DR EnsemblBacteria; EEM46088; EEM46088; bthur0005_39860. DR PATRIC; 28921895; VBIBacThu54181_1531. DR Proteomes; UP000001911; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001911}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 126089 MW; E7F963B91D38F6D4 CRC64; MKCIEEKLKN SILILDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYDLSHLDE ELNEKAALLA KQAVKESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGE VDVLLVETSQ DMRNVKAAYI GIQAAFEELK KTVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWIN IIGGCCGTTP EHIKAMKSAL ASLRPRDHHE REGHRISGLE ALQYDESMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMENF LAEVTKVLKV PIMIDSTDEN VMERALTYIQ GKAVINSINL EDGEERFKKV TPLLQKYGAA IVVGTIDEDG MAVSAERKIE IAKRSYELLT KKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPEE EKRLADALLF ETTKETLEEF TNFYRVAKKK DVVVQETLTL DERLANYIVE GTKQGLHEDL SLALEEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILA NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAANIDVPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV KKEEKKVEIP AVIEPLPKSE VMVPDSTKRI VLRDVPALHL APFLNRQMLL GHHLGLKGNV KKLLKEGDKR AHELNDLIDE LLQEGQSWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRVIE RFTFPRQGKA PYRTLGDYLR PIGDEMDYVA FLSVTVGEGV RDIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID C3E8J2_BACTU Unreviewed; 610 AA. AC C3E8J2; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 33. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=bthur0005_39870 {ECO:0000313|EMBL:EEM46089.1}; OS Bacillus thuringiensis serovar pakistani str. T13001. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527027 {ECO:0000313|EMBL:EEM46089.1, ECO:0000313|Proteomes:UP000001911}; RN [1] {ECO:0000313|EMBL:EEM46089.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=T13001 {ECO:0000313|EMBL:EEM46089.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEM46089.1}. 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; ACNC01000149; EEM46089.1; -; Genomic_DNA. DR RefSeq; WP_000770352.1; NZ_CM000750.1. DR ProteinModelPortal; C3E8J2; -. DR EnsemblBacteria; EEM46089; EEM46089; bthur0005_39870. DR PATRIC; 28921897; VBIBacThu54181_1532. DR Proteomes; UP000001911; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001911}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 610 AA; 67207 MW; 6AAA70A0BB40008A CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNVSDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTE INRAAVKLAK ASVTDKNAIL GTIGGMKHIG AVTTTDMERE FMLLEQAGAL LEEQVDGLLL ETFYDEFELL HAVKVLRKQT NIPIVAQLAL HEAGTTQNGN DVNEILKQLI DYGANVVGLN CQLGPLHMTE AFKMISIPQN GYLSAYPNAG LPNYVDGRYV YEGSPAYFEA MTPRFIEQGI RLLGGCCGTT PEHIQSMKRA VANITPVIEK DTIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRVSNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIK LIEEVYEATK HLEQPIFIGI MPLVSKRNAD FLHFEVPGIT LPEEIRERMD GHETKEAAIE EGIRISQELV DAAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID C3F1V8_BACTU Unreviewed; 236 AA. AC C3F1V8; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEM59820.1}; GN ORFNames=bthur0007_22700 {ECO:0000313|EMBL:EEM59820.1}; OS Bacillus thuringiensis serovar monterrey BGSC 4AJ1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527022 {ECO:0000313|EMBL:EEM59820.1, ECO:0000313|Proteomes:UP000000326}; RN [1] {ECO:0000313|EMBL:EEM59820.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BGSC 4AJ1 {ECO:0000313|EMBL:EEM59820.1}; 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. {ECO:0000313|EMBL:EEM59820.1}. 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; ACNE01000054; EEM59820.1; -; Genomic_DNA. DR RefSeq; WP_000420148.1; NZ_CM000752.1. DR EnsemblBacteria; EEM59820; EEM59820; bthur0007_22700. DR PATRIC; 28904831; VBIBacThu130558_5084. DR Proteomes; UP000000326; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000326}; KW Methyltransferase {ECO:0000313|EMBL:EEM59820.1}; KW Transferase {ECO:0000313|EMBL:EEM59820.1}. SQ SEQUENCE 236 AA; 26728 MW; 9E634A619380C898 CRC64; MELIGKTVLL ARRARDDFWK ENTQTNRPKR LVVASVGLYG AYLADGSEYV GNYGVTDKTL ADFHRSRMSA LIEAGADLLA FETIPSLQEA RVLDTLLREF PETYAWLSFS LKNEKEISQG IKLVECARAF EKSEQIVAIG INCAPVTVVT GAIQELRENT KKPIIVYPNS GETYNSETKT WHDHEQCNSL DIQSEEWYQA GARLIGGCCR TTPYHIEEIS NKWRSSEFFY SNEAKQ // ID C3F706_BACTU Unreviewed; 1132 AA. AC C3F706; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEM57993.1}; GN ORFNames=bthur0007_40950 {ECO:0000313|EMBL:EEM57993.1}; OS Bacillus thuringiensis serovar monterrey BGSC 4AJ1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527022 {ECO:0000313|EMBL:EEM57993.1, ECO:0000313|Proteomes:UP000000326}; RN [1] {ECO:0000313|EMBL:EEM57993.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BGSC 4AJ1 {ECO:0000313|EMBL:EEM57993.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEM57993.1}. 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; ACNE01000103; EEM57993.1; -; Genomic_DNA. DR RefSeq; WP_000649716.1; NZ_CM000752.1. DR EnsemblBacteria; EEM57993; EEM57993; bthur0007_40950. DR PATRIC; 28908693; VBIBacThu130558_0447. DR Proteomes; UP000000326; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000326}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 125970 MW; ED8E2640EF08987B CRC64; MKCIEEKLQN NILLLDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYELSHLDE ELNEKAARLA KQAVKESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGE VDVLLVETSQ DMRNVKAAYI GIQAAFDELK KIVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWVN IIGGCCGTTP EHIKAMKEAL ASLKPREHHE REGHGVSGLE ALQYDDSMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMENF LAEVTKVLKV PIMIDSTDEH VMERALTYIQ GKAVINSINL EDGEERFIKV TPLLQKYGAA IVVGTIDEDG MAVSAERKLE IAKRSYELLT TKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEVLPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPDE EKRLADALLF ETTQETLEEF TNFYRVAKKK DVVVQETLTL DERLANYIVE GTKQGLHEDL SLALTEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILA NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAADIDIPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV TKEEKKIEIP AVIEPLPKSE VMVPDSTKRI VLRDVPALHL APFLNRQMLL GHHLGLKGSV KKLLKEGDKR AHELNDLIDE LLQEGQSWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRVIE RFTFPRQGRA PYRTLGDYLR PIGDEMDYVA FLSVTVGEGV RGIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID C3F707_BACTU Unreviewed; 610 AA. AC C3F707; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 31. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=bthur0007_40960 {ECO:0000313|EMBL:EEM57994.1}; OS Bacillus thuringiensis serovar monterrey BGSC 4AJ1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527022 {ECO:0000313|EMBL:EEM57994.1, ECO:0000313|Proteomes:UP000000326}; RN [1] {ECO:0000313|EMBL:EEM57994.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BGSC 4AJ1 {ECO:0000313|EMBL:EEM57994.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEM57994.1}. 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; ACNE01000103; EEM57994.1; -; Genomic_DNA. DR RefSeq; WP_000770332.1; NZ_CM000752.1. DR ProteinModelPortal; C3F707; -. DR EnsemblBacteria; EEM57994; EEM57994; bthur0007_40960. DR PATRIC; 28908691; VBIBacThu130558_0446. DR Proteomes; UP000000326; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000326}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 610 AA; 67327 MW; 201A2B43DA3128EB CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNISDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTE INRAAVKLAK ASVTDRNAIL GTIGGMKHIG AVTTTDMERE FMLLEQASAL LEEQVDGLLL ETFYDEFELL HAVQVLRKET NIPIVAQLAL HEAGTTQNGN DVNEILKQLL DYGANVVGLN CQLGPLHMTE AFKMISIPKN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPKFIEQGI RLLGGCCGTT PEHIESMKRA TLNVTPVIEK DTIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRISNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGVEY FLTQPIYDIA LIEEVYEATK HLEQPIFIGI MPLISKRNAD FLHFEVPGIT LPEAVRERMD GHETKEAAIE EGIRISQELI DETMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID C3FQF3_BACTB Unreviewed; 1132 AA. AC C3FQF3; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 41. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEM64272.1}; GN ORFNames=bthur0008_40550 {ECO:0000313|EMBL:EEM64272.1}; OS Bacillus thuringiensis serovar berliner ATCC 10792. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527031 {ECO:0000313|EMBL:EEM64272.1, ECO:0000313|Proteomes:UP000001925}; RN [1] {ECO:0000313|EMBL:EEM64272.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 10792 {ECO:0000313|EMBL:EEM64272.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEM64272.1}. 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; ACNF01000095; EEM64272.1; -; Genomic_DNA. DR RefSeq; WP_000649720.1; NZ_CM000753.1. DR EnsemblBacteria; EEM64272; EEM64272; bthur0008_40550. DR PATRIC; 26150169; VBIBacThu124489_5977. DR Proteomes; UP000001925; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001925}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 125985 MW; 3BA40F322F8A7B3F CRC64; MKCIEEKLQN SILILDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYELSHLDE ELNEKAALLA KQAVKESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGE VDVLLVETSQ DMRNVKAAYI GIQAAFEELK KTVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWIN IIGGCCGTTP EHIKAMKEAL ASLKPRDHHE REGHGISGLE ALQYDESMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMEKF LTEVTKVLKV PIMIDSTDEN VMARALTYIQ GKAVINSINL EDGEERFEKV TPLLRKYGAA IVVGTIDEDG MAVSAERKLE IAKRSYELLT TKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPEE EKHLADALLF ETTKETLEEF TNFYRVAKKK DVVVQETLTL DERLANYIVE GTKQGLHEDL SLALEEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILA NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAANIDVPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV KKEEKKVEIP AVIEPLPKAE VMVPDSTKRI VLRDIPALHL APFLNRQMLL GHHLGLKGNV KKLLKEGDKR AHELNDLIDE LLQEGQSWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRVIE RFTFPRQGKA PYRTLGDYLR PIGDEMDYVA FLSVTVGEGV RDIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID C3FQF4_BACTB Unreviewed; 610 AA. AC C3FQF4; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 32. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=bthur0008_40560 {ECO:0000313|EMBL:EEM64273.1}; OS Bacillus thuringiensis serovar berliner ATCC 10792. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527031 {ECO:0000313|EMBL:EEM64273.1, ECO:0000313|Proteomes:UP000001925}; RN [1] {ECO:0000313|EMBL:EEM64273.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 10792 {ECO:0000313|EMBL:EEM64273.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEM64273.1}. 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; ACNF01000095; EEM64273.1; -; Genomic_DNA. DR RefSeq; WP_000770353.1; NZ_CM000753.1. DR ProteinModelPortal; C3FQF4; -. DR EnsemblBacteria; EEM64273; EEM64273; bthur0008_40560. DR PATRIC; 26150171; VBIBacThu124489_5978. DR Proteomes; UP000001925; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001925}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 610 AA; 67159 MW; D96AD95B688315AB CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNVSDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTE INRAAVKLAK ASVTDKNAIL GTIGGMKHIG AVTTTDMERE FMLLEQAGAL LEEQVDGLLL ETFYDEFELL HAVKVLRKQT NIPIVAQLAL HEAGTTQNGN DVNEILKQLI DYGANVVGLN CQLGPLHMTE AFKMISIPQN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPRFIEQGI RLLGGCCGTT PEHIQSMKHA VANVTPVIEK DTIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRISNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIA LIEEVYEATK HLEQPIFIGI MPLVSKRNAD FLHFEVPGIT LPEEIRERMD GHETKEAAIE EGIRISQELI DAAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID C3G865_BACTU Unreviewed; 1132 AA. AC C3G865; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEM69929.1}; GN ORFNames=bthur0009_40210 {ECO:0000313|EMBL:EEM69929.1}; OS Bacillus thuringiensis serovar andalousiensis BGSC 4AW1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527032 {ECO:0000313|EMBL:EEM69929.1, ECO:0000313|Proteomes:UP000001380}; RN [1] {ECO:0000313|EMBL:EEM69929.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BGSC 4AW1 {ECO:0000313|EMBL:EEM69929.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEM69929.1}. 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; ACNG01000094; EEM69929.1; -; Genomic_DNA. DR RefSeq; WP_000649715.1; NZ_CM000754.1. DR EnsemblBacteria; EEM69929; EEM69929; bthur0009_40210. DR PATRIC; 26138414; VBIBacThu67491_5566. DR Proteomes; UP000001380; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001380}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 125905 MW; B090E9D6AAEACC89 CRC64; MKCIEEKLQN NILLLDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYELSHLDE ELNEKAARLA KQAVKESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGE VDVLLVETSQ DMRNVKAAYI GIQAAFDELK KIVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWVN IIGGCCGTTP EHIKAMKEAL ASLKPREHHE REGHGVSGLE ALQYDDSMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMENF LAEVTKVLKV PIMIDSTDEH VMERALTYIQ GKAVINSINL EDGEERFIKV TPLLQKYGAA IVVGTIDEDG MAVSAERKLE IAKRSYELLT TKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPDE EKRLADALLF ETTQETLEEF TNFYRVAKKK DVVVQETLTL DERLANYIVE GTKQGLHEDL SLALTEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILA NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAADIDIPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV TKEEKKVEIP AVIEPLPKSE VMVPDSTKRV VLRDVPALHL APFLNRQMLL GHHLGLKGSV KKLLKEGDKR AQELNDLIDE LLQEGQSWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRVIE RFTFPRQGRA PYRTLGDYLR PIGDEMDYVA FLSVTVGEGV RGIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID C3G866_BACTU Unreviewed; 610 AA. AC C3G866; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 33. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=bthur0009_40220 {ECO:0000313|EMBL:EEM69930.1}; OS Bacillus thuringiensis serovar andalousiensis BGSC 4AW1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527032 {ECO:0000313|EMBL:EEM69930.1, ECO:0000313|Proteomes:UP000001380}; RN [1] {ECO:0000313|EMBL:EEM69930.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BGSC 4AW1 {ECO:0000313|EMBL:EEM69930.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEM69930.1}. 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; ACNG01000094; EEM69930.1; -; Genomic_DNA. DR RefSeq; WP_000770331.1; NZ_CM000754.1. DR ProteinModelPortal; C3G866; -. DR EnsemblBacteria; EEM69930; EEM69930; bthur0009_40220. DR PATRIC; 26138412; VBIBacThu67491_5565. DR Proteomes; UP000001380; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001380}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 610 AA; 67298 MW; 3F0A2353CD3128EB CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNISDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTE INRAAVKLAK ASVTDRNAIL GTIGGMKHIG AVTTTDMERE FMLLEQASAL LEEQVDGLLL ETFYDEFELL HAVQVLRKET NIPIVAQLAL HEAGTTQNGN DVNEILKQLL DYGANVVGLN CQLGPLHMTE AFKMISIPKN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPKFIEQGI RLLGGCCGTT PEHIESMKRA TLNVTPVIEK DTIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRISNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIA LIEEVYEATK HLEQPIFIGI MPLISKRNAD FLHFEVPGIT LPEAVRERMD GHETKEAAIE EGIRISQELI DETMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID C3GNZ7_BACTU Unreviewed; 1132 AA. AC C3GNZ7; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEM75925.1}; GN ORFNames=bthur0010_39860 {ECO:0000313|EMBL:EEM75925.1}; OS Bacillus thuringiensis serovar pondicheriensis BGSC 4BA1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527029 {ECO:0000313|EMBL:EEM75925.1, ECO:0000313|Proteomes:UP000006660}; RN [1] {ECO:0000313|EMBL:EEM75925.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BGSC 4BA1 {ECO:0000313|EMBL:EEM75925.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEM75925.1}. 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; ACNH01000075; EEM75925.1; -; Genomic_DNA. DR RefSeq; WP_000649713.1; NZ_CM000755.1. DR EnsemblBacteria; EEM75925; EEM75925; bthur0010_39860. DR PATRIC; 28934708; VBIBacThu130330_5099. DR Proteomes; UP000006660; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006660}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 125960 MW; AC6634065EF982D0 CRC64; MKCIEEKLQN NILLLDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYELSHLDE ELNEKAARLA KQAVKESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGE VDVLLVETSQ DMRNVKAAYI GIQAAFDELK KIVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWVN IIGGCCGTTP EHIKAMKEAL ASLKPREHHE REGHGVSGLE ALQYDDSMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMENF LAEVTKVLKV PIMIDSTDEH VMERALTYIQ GKAVINSINL EDGEERFIKV TPLLQKYGAA IVVGTIDEDG MAVSAERKLE IAKRSYELLT TKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPDE EKRLADALLF ETTQETLEEF TNFYRVAKKK DVVVQETLTL DERLANYIVE GTKQGLHEDL SLALTEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKILL ATVKGDVHDI GKNLVEIILA NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAADIDIPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV TKEEKKIEIP AVIEPLPKSE VMVPDSTKRI VLRDVPALHL APFLNRQMLL GHHLGLKGSV KKLLKEGDKR AHELNDLIDE LLQEGQSWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRIIE RFTFPRQGRA PYRTLGDYLR PIGDEMDYVA FLSVTVGEGV RGIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSSEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID C3GNZ8_BACTU Unreviewed; 610 AA. AC C3GNZ8; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 32. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=bthur0010_39870 {ECO:0000313|EMBL:EEM75926.1}; OS Bacillus thuringiensis serovar pondicheriensis BGSC 4BA1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527029 {ECO:0000313|EMBL:EEM75926.1, ECO:0000313|Proteomes:UP000006660}; RN [1] {ECO:0000313|EMBL:EEM75926.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BGSC 4BA1 {ECO:0000313|EMBL:EEM75926.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEM75926.1}. 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; ACNH01000075; EEM75926.1; -; Genomic_DNA. DR RefSeq; WP_000770328.1; NZ_CM000755.1. DR ProteinModelPortal; C3GNZ8; -. DR EnsemblBacteria; EEM75926; EEM75926; bthur0010_39870. DR PATRIC; 28934710; VBIBacThu130330_5100. DR Proteomes; UP000006660; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006660}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 610 AA; 67240 MW; 20E59FF319652DAE CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNISDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTE INRAAVKLAK ASVTDRNAIL GTIGGMKHIG AVTTTDMERE FMLLEQASAL LEEQVDGLLL ETFYDEFELL HAVQVLRKET NIPIVAQLAL HEAGTTQNGN DVNEILKQLL DYGANVVGLN CQLGPLHMTE AFKMISIPKN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPKFIEQGI RLLGGCCGTT PEHIESMKRA TLNVTPVIEK DTIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRISNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KAMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIA LIEEVYEATK HLEQPIFIGI MPLISKRNAD FLHFEVPGIT LPEAVRERMD GHETKEAAIE EGIRISQELI DETMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID C3H694_BACTU Unreviewed; 1132 AA. AC C3H694; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEM81987.1}; GN ORFNames=bthur0011_39870 {ECO:0000313|EMBL:EEM81987.1}; OS Bacillus thuringiensis serovar huazhongensis BGSC 4BD1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527030 {ECO:0000313|EMBL:EEM81987.1, ECO:0000313|Proteomes:UP000000627}; RN [1] {ECO:0000313|EMBL:EEM81987.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BGSC 4BD1 {ECO:0000313|EMBL:EEM81987.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEM81987.1}. 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; ACNI01000089; EEM81987.1; -; Genomic_DNA. DR RefSeq; WP_000649690.1; NZ_CM000756.1. DR EnsemblBacteria; EEM81987; EEM81987; bthur0011_39870. DR PATRIC; 26163075; VBIBacThu93808_5695. DR Proteomes; UP000000627; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000627}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 126000 MW; 6612FDDFD8E869B3 CRC64; MKCIEEKLKN SILILDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKTY IEAGADIIET NTFGATNIVL SDYELSHLDE ELNEKAALLA KQAVKESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGE VDVLLVETSQ DMRNVKAAYI GIQAAFEELK KTVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWVN IIGGCCGTTP EHIKAMKSAL APLKPRDHHE REGHGVSGLE ALQYDESMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMENF LAEVTKVLKV PIMIDSTDEN VMERALTYIQ GKAVINSINL EDGEERFKKV TPLLQKYGAA IVVGTIDEDG MAVSAERKIE IAKRSYELLT KKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPEE EKRLADALLF ETTKETLEEF TNFYRVAKKK DVVVQETLTL DERLANYIVE GTKQGLHEDL SLALEEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILA NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAANIDVPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV KKEEKKVEIP AVIELLPKAE VIVPDSTKRI VLRDIPALHL APFLNRQMLL GHHLGLKGNV KKLLKEGDKR AHELNDLIDE LLQEGQSWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRVIE RFTFPRQGKA PYRTLSDYLR PIGDEMDYVA FLSVTVGEGV RDIAEEWKGK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID C3H695_BACTU Unreviewed; 610 AA. AC C3H695; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 31. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=bthur0011_39880 {ECO:0000313|EMBL:EEM81988.1}; OS Bacillus thuringiensis serovar huazhongensis BGSC 4BD1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527030 {ECO:0000313|EMBL:EEM81988.1, ECO:0000313|Proteomes:UP000000627}; RN [1] {ECO:0000313|EMBL:EEM81988.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BGSC 4BD1 {ECO:0000313|EMBL:EEM81988.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEM81988.1}. 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; ACNI01000089; EEM81988.1; -; Genomic_DNA. DR RefSeq; WP_000770351.1; NZ_CM000756.1. DR ProteinModelPortal; C3H695; -. DR EnsemblBacteria; EEM81988; EEM81988; bthur0011_39880. DR PATRIC; 26163073; VBIBacThu93808_5694. DR Proteomes; UP000000627; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000627}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 610 AA; 67264 MW; D7973EE78D2E5458 CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNVSDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTE INRAAVKLAK ASVADKNAIL GTIGGMKHIG AVTTTDMERE FMLLEQAEAL LEEQVDGLLL ETFYDEFELL HTVKVLRKQT NIPIVAQLAL HEAGTTQNGN DVNEILKQLI DYGANVVGLN CQLGPLHMTE AFKMISIPQN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPRFIEQGI RLLGGCCGTT PEHIQSMKRA VANITPVIEK DTIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRVSNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNGGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIK LIEEVYEATK HLEQPIFIGI MPLVSKRNAD FLHFEVPGIT LPEEIRERMD GHETKEAAIE EGIRISQELI DAAMKYFNGI YLITPFLKYE ITEHLIKYVR EKQEVKEGIN // ID C3HNQ8_BACTU Unreviewed; 1132 AA. AC C3HNQ8; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEM87798.1}; GN ORFNames=bthur0012_41010 {ECO:0000313|EMBL:EEM87798.1}; OS Bacillus thuringiensis serovar pulsiensis BGSC 4CC1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527028 {ECO:0000313|EMBL:EEM87798.1, ECO:0000313|Proteomes:UP000006665}; RN [1] {ECO:0000313|EMBL:EEM87798.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BGSC 4CC1 {ECO:0000313|EMBL:EEM87798.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEM87798.1}. 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; ACNJ01000085; EEM87798.1; -; Genomic_DNA. DR RefSeq; WP_000649714.1; NZ_CM000757.1. DR EnsemblBacteria; EEM87798; EEM87798; bthur0012_41010. DR PATRIC; 28947734; VBIBacThu66700_5603. DR Proteomes; UP000006665; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006665}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 125942 MW; CFD6E26EBD6CBE3C CRC64; MKCIEEKLQN NILLLDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYELSHLDE ELNEKAARLA KQAVKESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGE VDVLLVETSQ DMRNVKAAYI GIQAAFDELK KIVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWVN IIGGCCGTTP EHIKAMKEAL ASLKPREHHE REGHGVSGLE ALQYDDSMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMENF LAEVTKVLKV PIMIDSTDEH VMERALTYIQ GKAVINSINL EDGEERFIKV TPLLQKYGAA IVVGTIDEDG MAVSAERKLE IAKRSYELLT TKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPDE EKRLADALLF ETTQETLEEF TNFYRVAKKK DVVVQETLTL DERLANYIVE GTKQGLHEDL SLALTEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILA NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAADIDIPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV TKEEKKIEIP AVIEPLPKSE VMVPDSTKRI VLRDVPALHL APFLNRQMLL GHHLGLKGSV KKLLKEGDKR AHELNDLIDE LLQEGQSWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRVIE RFTFPRQGRA PYRTLGDYLR PIGDEMDYVA FLSVTVGEGV RGIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID C3HNQ9_BACTU Unreviewed; 610 AA. AC C3HNQ9; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 33. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=bthur0012_41020 {ECO:0000313|EMBL:EEM87799.1}; OS Bacillus thuringiensis serovar pulsiensis BGSC 4CC1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527028 {ECO:0000313|EMBL:EEM87799.1, ECO:0000313|Proteomes:UP000006665}; RN [1] {ECO:0000313|EMBL:EEM87799.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BGSC 4CC1 {ECO:0000313|EMBL:EEM87799.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEM87799.1}. 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; ACNJ01000085; EEM87799.1; -; Genomic_DNA. DR RefSeq; WP_000770331.1; NZ_CM000757.1. DR ProteinModelPortal; C3HNQ9; -. DR EnsemblBacteria; EEM87799; EEM87799; bthur0012_41020. DR PATRIC; 28947732; VBIBacThu66700_5602. DR Proteomes; UP000006665; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006665}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 610 AA; 67298 MW; 3F0A2353CD3128EB CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNISDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTE INRAAVKLAK ASVTDRNAIL GTIGGMKHIG AVTTTDMERE FMLLEQASAL LEEQVDGLLL ETFYDEFELL HAVQVLRKET NIPIVAQLAL HEAGTTQNGN DVNEILKQLL DYGANVVGLN CQLGPLHMTE AFKMISIPKN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPKFIEQGI RLLGGCCGTT PEHIESMKRA TLNVTPVIEK DTIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRISNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIA LIEEVYEATK HLEQPIFIGI MPLISKRNAD FLHFEVPGIT LPEAVRERMD GHETKEAAIE EGIRISQELI DETMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID C3I653_BACTU Unreviewed; 1132 AA. AC C3I653; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEM94439.1}; GN ORFNames=bthur0013_42370 {ECO:0000313|EMBL:EEM94439.1}; OS Bacillus thuringiensis IBL 200. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527019 {ECO:0000313|EMBL:EEM94439.1, ECO:0000313|Proteomes:UP000001220}; RN [1] {ECO:0000313|EMBL:EEM94439.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=IBL 200 {ECO:0000313|EMBL:EEM94439.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEM94439.1}. 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; ACNK01000077; EEM94439.1; -; Genomic_DNA. DR RefSeq; WP_000649693.1; NZ_CM000758.1. DR EnsemblBacteria; EEM94439; EEM94439; bthur0013_42370. DR PATRIC; 26110859; VBIBacThu121489_5419. DR Proteomes; UP000001220; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001220}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 126082 MW; 99A637BA846947D7 CRC64; MKCIEEKLQN NILILDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYELSHLDE ELNEKAALLA KQAVKESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGE VDVLLVETSQ DMRNVKAAYI GIQAAFEEMK KTVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWVN IIGGCCGTTP EHIKAMKEAL ASLKPRDHHE REGHGISGLE ALQYDESMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMEKF LTEVTKVLKV PIMIDSTDEN VMARALTYIQ GKAVINSINL EDGEERFEKV TPLLRKYGAA IVVGTIDEDG MAVSAERKLE IAKRSYELLT TKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPEE EKHLADALLF ETTKETLEEF TNFYRVAKKK DVVVQETLTL DERLANYIVE GTKQGLHEDL SLALEEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILA NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAANIDVPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV KKEEKKVEIP AVIEPLPKTE VIVPDSTKRI VLRDIPALHL APFLNRQMLL GHHLGLKGNV KKLLKEGDKR AYELNDLIDE LLQEGQSWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRVIE RFTFPRQGKA PYRTLGDYLR PIGDEMDYVA FLSVTVGEGV RDIAEEWKAK GDYLRSHAIQ SLVLELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID C3I654_BACTU Unreviewed; 610 AA. AC C3I654; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 31. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=bthur0013_42380 {ECO:0000313|EMBL:EEM94440.1}; OS Bacillus thuringiensis IBL 200. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527019 {ECO:0000313|EMBL:EEM94440.1, ECO:0000313|Proteomes:UP000001220}; RN [1] {ECO:0000313|EMBL:EEM94440.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=IBL 200 {ECO:0000313|EMBL:EEM94440.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEM94440.1}. 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; ACNK01000077; EEM94440.1; -; Genomic_DNA. DR RefSeq; WP_000770355.1; NZ_CM000758.1. DR ProteinModelPortal; C3I654; -. DR EnsemblBacteria; EEM94440; EEM94440; bthur0013_42380. DR PATRIC; 26110857; VBIBacThu121489_5418. DR Proteomes; UP000001220; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001220}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 610 AA; 67235 MW; 8466E02FB2E625F3 CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNVSDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTE INRAAVKLAK ASVTDRNAIL GTIGGMKHIG AVTTTDMERE FMLLEQAGAL LEEQVDGLLL ETFYDEFELL HAVKVLRKQT NIPIVAQLAL HEAGTTQNGN DVNEILKQLI DYGANVVGLN CQLGPLHMTE AFKMISIPQN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPKFIEQGI RLLGGCCGTT PEHIESMKRA IANVTPVIEK DTIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRISNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIA LIEEVYEATK HLEQPIFIGI MPLISKRNAD FLHFEVPGIT LPEEIRERMD GHETKEAAIE EGIRISQELI DVAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID C3IB10_BACTU Unreviewed; 88 AA. AC C3IB10; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEM92681.1}; GN ORFNames=bthur0013_59770 {ECO:0000313|EMBL:EEM92681.1}; OS Bacillus thuringiensis IBL 200. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527019 {ECO:0000313|EMBL:EEM92681.1, ECO:0000313|Proteomes:UP000001220}; RN [1] {ECO:0000313|EMBL:EEM92681.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=IBL 200 {ECO:0000313|EMBL:EEM92681.1}; 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. {ECO:0000313|EMBL:EEM92681.1}. 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; ACNK01000146; EEM92681.1; -; Genomic_DNA. DR RefSeq; WP_003308554.1; NZ_CM000758.1. DR EnsemblBacteria; EEM92681; EEM92681; bthur0013_59770. DR PATRIC; 26114510; VBIBacThu121489_0667. DR Proteomes; UP000001220; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001220}; KW Methyltransferase {ECO:0000313|EMBL:EEM92681.1}; KW Transferase {ECO:0000313|EMBL:EEM92681.1}. SQ SEQUENCE 88 AA; 10153 MW; 6BE14B14B57D5187 CRC64; MTGAIQELRA NTKKPIIVYP NSGETYNPET KTWHGHEQCN ALNIQSEEWY QAGARLIGGC CRTTPYHIEE ISNKWRSSEF FYSNEAKQ // ID C3ICF7_BACTU Unreviewed; 140 AA. AC C3ICF7; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEM92181.1}; GN ORFNames=bthur0013_64930 {ECO:0000313|EMBL:EEM92181.1}; OS Bacillus thuringiensis IBL 200. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527019 {ECO:0000313|EMBL:EEM92181.1, ECO:0000313|Proteomes:UP000001220}; RN [1] {ECO:0000313|EMBL:EEM92181.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=IBL 200 {ECO:0000313|EMBL:EEM92181.1}; 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. {ECO:0000313|EMBL:EEM92181.1}. 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; ACNK01000214; EEM92181.1; -; Genomic_DNA. DR RefSeq; WP_003308812.1; NZ_CM000758.1. DR EnsemblBacteria; EEM92181; EEM92181; bthur0013_64930. DR PATRIC; 26115543; VBIBacThu121489_1556. DR Proteomes; UP000001220; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001220}; KW Methyltransferase {ECO:0000313|EMBL:EEM92181.1}; KW Transferase {ECO:0000313|EMBL:EEM92181.1}. SQ SEQUENCE 140 AA; 16069 MW; C31B58AFAADBFE3A CRC64; MREFPETYAW LSFSLKNEKE ISEGMKLVEC ARVFEKSEQI VAIGINCAPV TVVTGAIQEL RANIKKPIIV YPNSGETYNP ETKTWHGHEQ CNTLDIQSEE WYQAGARLIG GCCRTTPYHI EEISNKWRSS EFFYSNEAKQ // ID C3IJ95_BACTU Unreviewed; 308 AA. AC C3IJ95; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEN03159.1}; GN ORFNames=bthur0014_21400 {ECO:0000313|EMBL:EEN03159.1}; OS Bacillus thuringiensis IBL 4222. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527020 {ECO:0000313|EMBL:EEN03159.1, ECO:0000313|Proteomes:UP000006648}; RN [1] {ECO:0000313|EMBL:EEN03159.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=IBL 4222 {ECO:0000313|EMBL:EEN03159.1}; 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. {ECO:0000313|EMBL:EEN03159.1}. 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; ACNL01000071; EEN03159.1; -; Genomic_DNA. DR RefSeq; WP_003309453.1; NZ_CM000759.1. DR EnsemblBacteria; EEN03159; EEN03159; bthur0014_21400. DR PATRIC; 26120602; VBIBacThu2650_6314. DR Proteomes; UP000006648; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006648}; KW Methyltransferase {ECO:0000313|EMBL:EEN03159.1}; KW Transferase {ECO:0000313|EMBL:EEN03159.1}. SQ SEQUENCE 308 AA; 34471 MW; A41C510884CBCFEA CRC64; MLLDGALATE LEAHGCNLDD PLWSARVLLE NPELIYQVHS DYFRAGADCA ITASYQATIS GFSTRGIQEQ EALELIKKTV LLARRARDDF WKENTQTNRP KPLVVASVGP YGAYLADGSE YVGNYGVTDK TLADFHRSRM SALIEAGADL LAFETIPSLQ EARVLDTLLR EFPETYAWLS FSLKNEKEIS EGMKLVECAR VFEKSEQIVA IGINCAPVTV VTGAIQELRA NTKKPIIVYP NSGETYNPET KTWHGHEQCN ALNIQSEEWY QAGARLIGGC CRTTPYHIEE ISNKWRSSEF FYSNEAKQ // ID C3IPB1_BACTU Unreviewed; 610 AA. AC C3IPB1; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 31. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=bthur0014_39410 {ECO:0000313|EMBL:EEN01357.1}; OS Bacillus thuringiensis IBL 4222. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=527020 {ECO:0000313|EMBL:EEN01357.1, ECO:0000313|Proteomes:UP000006648}; RN [1] {ECO:0000313|EMBL:EEN01357.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=IBL 4222 {ECO:0000313|EMBL:EEN01357.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEN01357.1}. 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; ACNL01000139; EEN01357.1; -; Genomic_DNA. DR RefSeq; WP_000770367.1; NZ_CM000759.1. DR ProteinModelPortal; C3IPB1; -. DR EnsemblBacteria; EEN01357; EEN01357; bthur0014_39410. DR PATRIC; 26124272; VBIBacThu2650_1496. DR Proteomes; UP000006648; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006648}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 610 AA; 67232 MW; FAEE1FDEE089A711 CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNVSDPD LIISIHKQYV AAGADVIQTN TYGANETKLR MYGLENQVTE INRAAVKLAK ASVTDRNAIL GTIGGMKHIG AVTTTDMERE FMLLEQAGAL LEEQVDGLLL ETFYDEFELL HAVKVLRKQT NIPIVAQLAL HEAGTTQNGN DVNEILKQLI DCGANVVGLN CQLGPLHMTE AFKMISIPQN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPRFIEQGI RLLGGCCGTT PEHIQSMKRA VANITPVIEK DTIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRISNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIA LIEEVYEATK HLEQPIFIGI MPLVSKRNAD FLHFEVPGIT LPEEIRERMD GHETKEAAIE EGIRISQELI DIAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID C3JH75_RHOER Unreviewed; 340 AA. AC C3JH75; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEN89134.1}; DE Flags: Fragment; GN ORFNames=RHOER0001_0229 {ECO:0000313|EMBL:EEN89134.1}; OS Rhodococcus erythropolis SK121. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Nocardiaceae; Rhodococcus. OX NCBI_TaxID=596309 {ECO:0000313|EMBL:EEN89134.1}; RN [1] {ECO:0000313|EMBL:EEN89134.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK121 {ECO:0000313|EMBL:EEN89134.1}; 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. {ECO:0000313|EMBL:EEN89134.1}. 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; ACNO01000008; EEN89134.1; -; Genomic_DNA. DR RefSeq; WP_003941065.1; NZ_ACNO01000008.1. DR EnsemblBacteria; EEN89134; EEN89134; RHOER0001_0229. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEN89134.1}; KW Transferase {ECO:0000313|EMBL:EEN89134.1}. FT NON_TER 340 340 {ECO:0000313|EMBL:EEN89134.1}. SQ SEQUENCE 340 AA; 35531 MW; E81D306AC9B0EACC CRC64; MNRFEARNPI AAVSSKATAG GMSAPFNSAL LDALKQRVVI GDGAMGTMLQ AADLTLDDFL GLEGCNEILN DTRPDVLKDI HRAYFAAGAD AVETNTFGCN LPNLADYDIS HRIRELAEKG TALAREVADE MGPGRDGMAR FVLGSMGPGT KLPSLGHAPY AVLRDAYTEA ALGMIDGGAD AILVETCQDL LQVKAAILGS QRAMEQLGLR LPIITHVTVE TTGTMLLGSE IGAALTALEP LGIDMIGLNC ATGPAEMSEH LRHLSKYSTL PVSVMPNAGL PQLGPKGAEY PLTADELAEA LSGFVSEFGL GLVGGCCGTT PEHISAVADA VRQVEKAQRT // ID C3JX26_RHOER Unreviewed; 174 AA. AC C3JX26; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEN83940.1}; DE Flags: Fragment; GN ORFNames=RHOER0001_6210 {ECO:0000313|EMBL:EEN83940.1}; OS Rhodococcus erythropolis SK121. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Nocardiaceae; Rhodococcus. OX NCBI_TaxID=596309 {ECO:0000313|EMBL:EEN83940.1}; RN [1] {ECO:0000313|EMBL:EEN83940.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK121 {ECO:0000313|EMBL:EEN83940.1}; 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. {ECO:0000313|EMBL:EEN83940.1}. 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; ACNO01000119; EEN83940.1; -; Genomic_DNA. DR RefSeq; WP_003946329.1; NZ_ACNO01000119.1. DR EnsemblBacteria; EEN83940; EEN83940; RHOER0001_6210. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEN83940.1}; KW Transferase {ECO:0000313|EMBL:EEN83940.1}. FT NON_TER 1 1 {ECO:0000313|EMBL:EEN83940.1}. FT NON_TER 174 174 {ECO:0000313|EMBL:EEN83940.1}. SQ SEQUENCE 174 AA; 18336 MW; 363B43BC488D9183 CRC64; GCNEILNDTR PDVLKDIHRA YFAAGADAVE TNTFGCNLPN LADYDISHRI RELAEKGTAL AREVADEMGP GRDGMARFVL GSMGPGTKLP SLGHAPYAVL RDAYTEAALG MIDGGADAIL VETCQDLLQV KAAILGSQRA MEQLGLRLPI ITHVTVETTG TMLLGSEIGA ALTA // ID C3K933_PSEFS Unreviewed; 306 AA. AC C3K933; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 33. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CAY48463.1}; GN OrderedLocusNames=PFLU_2227 {ECO:0000313|EMBL:CAY48463.1}; OS Pseudomonas fluorescens (strain SBW25). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=216595 {ECO:0000313|EMBL:CAY48463.1, ECO:0000313|Proteomes:UP000002332}; RN [1] {ECO:0000313|EMBL:CAY48463.1, ECO:0000313|Proteomes:UP000002332} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SBW25 {ECO:0000313|EMBL:CAY48463.1, RC ECO:0000313|Proteomes:UP000002332}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; CAY48463.1; -; Genomic_DNA. DR RefSeq; WP_012723460.1; NC_012660.1. DR RefSeq; YP_002871839.1; NC_012660.1. DR STRING; 216595.PFLU2227; -. DR EnsemblBacteria; CAY48463; CAY48463; PFLU_2227. DR GeneID; 7820942; -. DR KEGG; pfs:PFLU2227; -. DR PATRIC; 19898678; VBIPseFlu98510_2442. DR eggNOG; COG2040; -. DR OMA; QPEVMAA; -. DR OrthoDB; EOG6Q5NS7; -. DR Proteomes; UP000002332; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002332}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000002332}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 206 206 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 282 282 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 306 AA; 32706 MW; DDB92D2024EDFA81 CRC64; MSQASLRLLD GGMGRELQRI GAPFRQPEWS ALALIEAPDY VLQAHQAFIE AGARIITTNS YAVVPFHIGD ERFAEQGRAL AERAGRLARQ AAAGSTEPVM VAGSLPPALG SYRPDLFDHQ RSVVIHRELI AGLQAHVDVW LAETQSSIAE VRAVVEALGA ESKPLWLSFT LLDEAGEPPR LRSSESVAQA VHVAVELGAR AVLFNCSQPE VMAAALAVAG DVLLRLDQSI ELGVYANAFP PVSTEAKANS TLLEIRRDLG PESYLHWSRT WVAAGASIVG GCCGIGPEHI AQLHAHLLPN EVVVSA // ID C3K9R8_PSEFS Unreviewed; 1236 AA. AC C3K9R8; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CAY48894.1}; GN OrderedLocusNames=PFLU_2662 {ECO:0000313|EMBL:CAY48894.1}; OS Pseudomonas fluorescens (strain SBW25). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=216595 {ECO:0000313|EMBL:CAY48894.1, ECO:0000313|Proteomes:UP000002332}; RN [1] {ECO:0000313|EMBL:CAY48894.1, ECO:0000313|Proteomes:UP000002332} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SBW25 {ECO:0000313|EMBL:CAY48894.1, RC ECO:0000313|Proteomes:UP000002332}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AM181176; CAY48894.1; -; Genomic_DNA. DR RefSeq; WP_012723855.1; NC_012660.1. DR RefSeq; YP_002872246.1; NC_012660.1. DR STRING; 216595.PFLU2662; -. DR EnsemblBacteria; CAY48894; CAY48894; PFLU_2662. DR GeneID; 7821828; -. DR KEGG; pfs:PFLU2662; -. DR PATRIC; 19899524; VBIPseFlu98510_2865. DR eggNOG; COG1410; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR Proteomes; UP000002332; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002332}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002332}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1236 AA; 135546 MW; 6C87ED472F9FF197 CRC64; MSDRSVRLQA LHQALKERIL ILDGGMGTMI QSYKLEEQDY RGKRFADWPS DVKGNNDLLV ITRPDVIGGI EKAYLDAGAD ILETNTFNAT RISMADYGME ELAYELNVEG ARLARKIADA KTLENPAKPR FVAGVLGPTS RTCSLSPDVN NPGYRNVTFD ELVENYTEAT QGLIEGGADL ILIETIFDTL NAKAAIFAVQ GVFETLNIEL PIMISGTITD ASGRTLSGQT TEAFWNSVAH AKPISVGLNC ALGASELRPY LEELSNKAST HVSAHPNAGL PNEFGEYDEL PSETAKVIEE FAQSGFLNIV GGCCGTTPGH IEAIAKAVAG YAPRVIPDIP KACRLSGLEP FTIDRSSLFV NVGERTNITG SARFARLIRE DNYTEALEVA LQQVEAGAQV IDINMDEGML DSKKAMVTFL NLIAGEPDIS RVPIMIDSSK WEVIEAGLKC IQGKGIVNSI SMKEGVEQFI HHAKLCKRYG AAVVVMAFDE AGQADTEARK KEICKRSYDI LVNEVGFPPE DIIFDPNIFA VATGIEEHNN YAVDFINACA YIRDELPYAL TSGGVSNVSF SFRGNNPVRE AIHSVFLLYA IRNGLTMGIV NAGQLEIYDQ IPAELRDAVE DVVLNRTPEG TDALLAIADK YKGDGSVKET ETEEWRGWPV NKRLEHALVK GITTHIVEDT EESRQSFARP IEVIEGPLMS GMNIVGDLFG AGKMFLPQVV KSARVMKQAV AHLIPFIELE KGDKPEAKGK ILMATVKGDV HDIGKNIVGV VLGCNGYDIV DLGVMVPAEK ILQVAKEQKC DIIGLSGLIT PSLDEMVHVA REMQRQDFHL PLMIGGATTS KAHTAVKIEP KYSNDAVIYV TDASRAVGVA TQLLSKELKA GFVEKTRLEY IDVRERTSNR SARTERLSYP AAIAKKPQFD WSTYTPVVPT FTGAKVLDNI DLKVLAEYID WTPFFISWDL AGKFPRILED EVVGEAATAL YADAQEMLNK LIDEKLISAR AVFGFWPTNQ VQDDDLEVYG DDGQPIAKLH HLRQQIIKTD GKPNFSLADF VAPKDSGVTD YIGGFITTAG IGAEEVAKAY QDAGDDYNSI MVKALADRLA EACAEWLHQQ VRKEHWGYAK DEQLDNEALI KEQYSGIRPA PGYPACPDHT EKAQLFQLLD PEAREMQAGR SGVFLTEHYA MFPAAAVSGW YFAHPQAQYF AVGKVDKDQV ASYTARKGQD LSVSERWLAP NLGYDN // ID C3KIA2_ANOFI Unreviewed; 366 AA. AC C3KIA2; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 04-MAR-2015, entry version 18. DE SubName: Full=Betaine--homocysteine S-methyltransferase 1 {ECO:0000313|EMBL:ACQ58374.1}; GN Name=BHMT1 {ECO:0000313|EMBL:ACQ58374.1}; OS Anoplopoma fimbria (Sablefish). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Cottioidei; Anoplopomatales; Anoplopomatidae; OC Anoplopoma. OX NCBI_TaxID=229290 {ECO:0000313|EMBL:ACQ58374.1}; RN [1] {ECO:0000313|EMBL:ACQ58374.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Brain {ECO:0000313|EMBL:ACQ58374.1}; RA Messmer A., Rondeau E., Sanderson D., Cooper G., Leong J., Koop B.F.; RT "Anoplopoma fimbria ESTs and full-length cDNAs."; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BT082667; ACQ58374.1; -; mRNA. DR UniPathway; UPA00051; UER00083. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000313|EMBL:ACQ58374.1}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000313|EMBL:ACQ58374.1}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 210 210 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 292 292 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 366 AA; 40518 MW; E2F9F15B811B7E6C CRC64; MENKRRGILE RLNAGEVVVG DGGYVMQLER RGYVKAGHWT PEAAVEHPEA VRQLHREFLR AGANVLQTFT FYCSEDKLEI SGNVTNITGA QINEAACDLA REVANEGDAL VAGGVSQTPC YVTSHSETEV KAIFKKQMDD FLKKDIDFFI VEYFEHVEEA VWAVEVLKTS GKPVGATLCI SPQGDMHGVP PGECAVRLVR AGADIVGINC HLDPLTCIRT VKLMKAGLEN AGLKAHLMIQ PLGFHTPECN HTGYLSLPEF PFALETRSMT RWDIHQYARE AYNAGIRYIG GCCGFEPYHI RAIAEEVAAE RGFLPPASEK HGLWGAALEM HTKPWVRARS RRDYWENLLP ASGRPKCPSM AIPADE // ID C3LRC1_VIBCM Unreviewed; 1226 AA. AC C3LRC1; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 45. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:ACP04701.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ACP04701.1}; GN Name=metH {ECO:0000313|EMBL:ACP04701.1}; GN OrderedLocusNames=VCM66_0375 {ECO:0000313|EMBL:ACP04701.1}; OS Vibrio cholerae serotype O1 (strain M66-2). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=579112 {ECO:0000313|EMBL:ACP04701.1, ECO:0000313|Proteomes:UP000001217}; RN [1] {ECO:0000313|EMBL:ACP04701.1, ECO:0000313|Proteomes:UP000001217} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M66-2 {ECO:0000313|EMBL:ACP04701.1, RC ECO:0000313|Proteomes:UP000001217}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001233; ACP04701.1; -; Genomic_DNA. DR RefSeq; WP_000514261.1; NC_012578.1. DR RefSeq; YP_002809152.1; NC_012578.1. DR ProteinModelPortal; C3LRC1; -. DR SMR; C3LRC1; 654-1224. DR STRING; 579112.VCM66_0375; -. DR PRIDE; C3LRC1; -. DR EnsemblBacteria; ACP04701; ACP04701; VCM66_0375. DR KEGG; vcm:VCM66_0375; -. DR PATRIC; 20064540; VBIVibCho108967_0355. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; VCHO579112:GJAW-411-MONOMER; -. DR Proteomes; UP000001217; Chromosome I. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001217}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACP04701.1}; KW Transferase {ECO:0000313|EMBL:ACP04701.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1226 AA; 135793 MW; 5CF4AB07A738D74F CRC64; MGKEVRQQLE QQLKQRILLI DGGMGTMIQS YKLQEEDYRG ARFVDWHCDL KGNNDLLVLT QPQIIKEIHS AYLEAGADIL ETNTFNSTTI AMADYDMQSL SAEINFAAAK LAREVADEWT AKDPSRPRYV AGVLGPTNRT CSISPDVNDP GFRNVTFDGL VEAYSESTRA LIKGGSDLIL IETIFDTLNA KACAFAVDSV FEELGISLPV MISGTITDAS GRTLSGQTTE AFYNALRHVR PISFGLNCAL GPDELRQYVE ELSRISECYV SAHPNAGLPN AFGEYDLSAE EMAEHIAEWA QAGFLNLVGG CCGTTPEHIA AIAKAVEGVK PRALPDLKVE CRLSGLEPLN IGPETLFVNV GERTNVTGSA RFKRLIKEEQ YDEALDVARE QVENGAQIID INMDEGMLDA EACMVRFLNL CASEPEISKV PVMVDSSKWE VIEAGLKCIQ GKGIVNSISL KEGKEKFIAQ AKLVRRYGAA VIVMAFDEVG QADTRERKLE ICRRAYHILV DEVGFPPEDI IFDPNIFAVA TGIDEHNNYA LDFINAVADI KRELPHAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK HGMDMGIVNA GQLEIYDNVP LKLREAVEDV ILNRRSDGTE RLLEIAEAYR ENSVGKEEDA SALEWRAWPV AKRLEHALVK GITEFIVQDT EEARQQASKP LEVIEGPLMD GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AYLEPFINAQ KSGSTSNGKI LLATVKGDVH DIGKNIVGVV LQCNNFEIID LGVMVPCEQI LKVAREQNVD IIGLSGLITP SLDEMVHVAK EMERQGFELP LLIGGATTSK AHTAVKIEQN YHAPVVYVNN ASRAVGVCTS LLSDEQRPGF IERLDLDYER TRDQHARKTP KSRPVTLEQA RANKAALDWA NYTPPAPAKP GVHVFENIAL ATLRPYIDWT PFFMTWSLMG KYPAILEHEE VGEEAKRLFH DANALLDKVE REGLLKASGM CALFPAASVG DDIEVYSDES RTQVAHVLYN LRQQTEKPKG ANYCLSDYVA PKESGKRDWI GAFAVTGGIG ERALADAYKA QGDDYNAIMI QAVADRLAEA FAEYLHEKVR KEIWGYASDE NLSNDDLIRE RYQGIRPAPG YPACPEHTEK ATLWQMLNVE ETIGMSLTTS YAMWPGASVS GWYFSHPDSR YFAVAQIQPD QLHSYAERKG WRLEEAEKWL APNLDA // ID C3M8I7_RHISN Unreviewed; 322 AA. AC C3M8I7; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 33. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACP24533.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ACP24533.1}; GN OrderedLocusNames=NGR_c07400 {ECO:0000313|EMBL:ACP24533.1}; OS Rhizobium sp. (strain NGR234). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24533.1, ECO:0000313|Proteomes:UP000001054}; RN [1] {ECO:0000313|EMBL:ACP24533.1, ECO:0000313|Proteomes:UP000001054} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NGR234 {ECO:0000313|EMBL:ACP24533.1, RC ECO:0000313|Proteomes:UP000001054}; 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-Roeser 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; ACP24533.1; -; Genomic_DNA. DR RefSeq; WP_012707318.1; NC_012587.1. DR RefSeq; YP_002825286.1; NC_012587.1. DR STRING; 394.NGR_c07400; -. DR EnsemblBacteria; ACP24533; ACP24533; NGR_c07400. DR GeneID; 7791966; -. DR KEGG; rhi:NGR_c07400; -. DR PATRIC; 32307865; VBIRhiSp122450_3556. DR eggNOG; COG2040; -. DR HOGENOM; HOG000179103; -. DR OMA; CCGTDHR; -. DR OrthoDB; EOG6R5C46; -. DR BioCyc; SFRE394:GBYN-739-MONOMER; -. DR Proteomes; UP000001054; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001054}; KW Methyltransferase {ECO:0000313|EMBL:ACP24533.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001054}; KW Transferase {ECO:0000313|EMBL:ACP24533.1}. SQ SEQUENCE 322 AA; 35489 MW; F184C68C9F1285AC CRC64; MQHEFAKYRH DLPLLQGGTF LSDGGMETAL IFQEGVELPH FASFVLLSSM EGRRQLLHYY TSYLEIARCR DTGFVLDTAT WRANADWGEK LGYDAEDLDQ VNRDAVYLLT ELRAQYERPQ VPIVFNGVIG PRGDGYKAGM MNAAEAEDYH AAQVAAFADS EADMVSAVTM TNVDEAIGVA RAARTHGMPC AISFTVETDG RLVTGRSLQE AVETVDAETE AYPHYYMVNC AHPSHFESSL DQDQAWVRRI GGIRANASTK SHAELDESET LDIGDINDLA RRYRSLTGRL PHLRVLGGCC GTDHRHIAAI CEACLPPVAL SA // ID C3M978_RHISN Unreviewed; 1256 AA. AC C3M978; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 29-APR-2015, entry version 51. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACP26789.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ACP26789.1}; GN Name=metH {ECO:0000313|EMBL:ACP26789.1}; GN OrderedLocusNames=NGR_c30540 {ECO:0000313|EMBL:ACP26789.1}; OS Rhizobium sp. (strain NGR234). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=394 {ECO:0000313|EMBL:ACP26789.1, ECO:0000313|Proteomes:UP000001054}; RN [1] {ECO:0000313|EMBL:ACP26789.1, ECO:0000313|Proteomes:UP000001054} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NGR234 {ECO:0000313|EMBL:ACP26789.1, RC ECO:0000313|Proteomes:UP000001054}; 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-Roeser 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001389; ACP26789.1; -; Genomic_DNA. DR RefSeq; WP_012709542.1; NC_012587.1. DR RefSeq; YP_002827542.1; NC_012587.1. DR STRING; 394.NGR_c30540; -. DR EnsemblBacteria; ACP26789; ACP26789; NGR_c30540. DR GeneID; 7792325; -. DR KEGG; rhi:NGR_c30540; -. DR PATRIC; 32312615; VBIRhiSp122450_5889. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SFRE394:GBYN-3042-MONOMER; -. DR Proteomes; UP000001054; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001054}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACP26789.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001054}; KW Transferase {ECO:0000313|EMBL:ACP26789.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 261 261 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 325 325 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 778 778 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1256 AA; 138181 MW; 6F69FB369EB4BC75 CRC64; MSAASLFGEL SPKPDGSEIF RALNQAAAER ILIMDGAMGT EIQQLGFVED HFRGERFGGC ACHQQGNNDL LTLTQPKAIE EIHYRYALAG ADILETNTFS STRIAQADYG MEDMVYDLNR DGARLARRAA KRAEAEDGRR RFVAGALGPT NRTASISPDV NNPGYRAVSF DDLRLAYAEQ VRGLIDGGAD IILIETIFDT LNAKAAIFAT QEVFAEKKIH LPVMVSGTIT DLSGRTLSGQ TPTAFWYSVR HAAPFTIGLN CALGADAMRA HIDELSTVAD TLVCAYPNAG LPNEFGRYDE SPETMAAQIE AFVRDGLVNI VGGCCGSTPA HIRAIAEAVQ KYPPRQVPEI ERRMRLSGLE PFTLTDEIPF VNVGERTNVT GSAKFRKLIT TGDYAAALDV ARDQVANGAQ IIDINMDEGL IDSTRAMVEF LNLVASEPDI ACVPVMIDSS KWEVIEAGLK CVQGKALVNS ISLKEGEEAF LHHARLVRAY GAAVVVMAFD EKGQADSRAR KVEICRRAYR LLTEEVGFPP EDIIFDPNIF AVATGIDEHN NYGVDFIEAT HEIIATLPHV HVSGGVSNLS FSFRGNEPVR EAMHAVFLYH AIQAGMDMGI VNAGQLAVYD AIDPELREAC EDVVLNRRPD ATERLLEIAE RYRGQGGAQG KEKDLAWRQW PVAKRLEHAL VNGITEFIEA DTEEARLAAE RPLHVIEGPL MAGMNVVGDL FGAGKMFLPQ VVKSARVMKQ AVAVLLPYME AEKLANGGEG TRASAGKILM ATVKGDVHDI GKNIVGVVLA CNNYEIIDLG VMVPSAKILE VARQEKVDAI GLSGLITPSL DEMVHVASEL EREGFDIPLL IGGATTSRVH TAVKINPRYG LGQTVYVTDA SRAVGVVSSL LSPEARDGYK ETVRAEYLKV ADAHARNEAE KRRLPLSQAR ANASKLDWDA YRPKTPSFLG TRVFESWDLA ELARYIDWTP FFQTWELKGV YPRILDDEHQ GPAARQLFAD AQAMLEKIIA EKWFAPKAVV GFWPAGSAGD DIRLFTDERR ERELATFFTL RQQLAKRDGR PNVALADFVA PVESGRRDYL GGFVVTAGIE EVAIAERFER ANDDYSSILV KALADRFAEA FAERMHEYVR KELWGYAPDE SFTPQELIAE PYTGIRPAPG YPAQPDHTEK ETLFRLLDAE AAIGVRLTEN YAMWPGSSVS GLYVGHPDAY YFGVAKIERD QVEDYATRKR MGVREVERWL SPILNYVPMR ETQAAE // ID C3MDS4_RHISN Unreviewed; 352 AA. AC C3MDS4; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 29-APR-2015, entry version 38. DE SubName: Full=Homocysteine S-methyltransferase, putative {ECO:0000313|EMBL:ACP25593.1}; GN OrderedLocusNames=NGR_c18290 {ECO:0000313|EMBL:ACP25593.1}; OS Rhizobium sp. (strain NGR234). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=394 {ECO:0000313|EMBL:ACP25593.1, ECO:0000313|Proteomes:UP000001054}; RN [1] {ECO:0000313|EMBL:ACP25593.1, ECO:0000313|Proteomes:UP000001054} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NGR234 {ECO:0000313|EMBL:ACP25593.1, RC ECO:0000313|Proteomes:UP000001054}; 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-Roeser 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; ACP25593.1; -; Genomic_DNA. DR RefSeq; WP_012708358.1; NC_012587.1. DR RefSeq; YP_002826346.1; NC_012587.1. DR STRING; 394.NGR_c18290; -. DR EnsemblBacteria; ACP25593; ACP25593; NGR_c18290. DR GeneID; 7791107; -. DR KEGG; rhi:NGR_c18290; -. DR PATRIC; 32310111; VBIRhiSp122450_4656. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265278; -. DR KO; K00548; -. DR OMA; GTNLFAM; -. DR OrthoDB; EOG693GKH; -. DR BioCyc; SFRE394:GBYN-1824-MONOMER; -. DR Proteomes; UP000001054; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001054}; KW Methyltransferase {ECO:0000313|EMBL:ACP25593.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001054}; KW Transferase {ECO:0000313|EMBL:ACP25593.1}. SQ SEQUENCE 352 AA; 36858 MW; 88D8D3B44643117C CRC64; MFISHYSLSS REMPMSIAAN ALSDLLAQKG VLLADGATGT SLFAMGLEAG EAPELWNETK PENITKLHQD FVDAGADIIL TNSFGGTRHR LKLHQAEDRV HALNKRAAEI ARAVADKAPR KVITAGSVGP TGELLIPLGA LSYEDAVSAF AEQIEGLKAG GAEVAWIETM SSPDEIRAAA EAATKVGLPF VYTGSFDTAG KTMMGLHPKD LHTVAAEIGE GPVAVGANCG VGASDILSSL LDMTAANPEG TVVVKGNCGI PEFRGSEIHY SGTPPLMAEY ARLAVDAGAR IIGGCCGTSC NHLAAMRLAL DNHTKGERPS LETIVEKIGP LRNKTANEGP VAPARERRSR RA // ID C3NS50_VIBCJ Unreviewed; 1226 AA. AC C3NS50; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 48. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:ACQ59406.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ACQ59406.1}; GN OrderedLocusNames=VCD_001233 {ECO:0000313|EMBL:ACQ59406.1}; OS Vibrio cholerae serotype O1 (strain MJ-1236). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=593588 {ECO:0000313|EMBL:ACQ59406.1, ECO:0000313|Proteomes:UP000001618}; RN [1] {ECO:0000313|Proteomes:UP000001618} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MJ-1236 {ECO:0000313|Proteomes:UP000001618}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001485; ACQ59406.1; -; Genomic_DNA. DR RefSeq; WP_000514261.1; NC_012668.1. DR RefSeq; YP_002876976.1; NC_012668.1. DR ProteinModelPortal; C3NS50; -. DR SMR; C3NS50; 654-1224. DR STRING; 593588.VCD_001233; -. DR PRIDE; C3NS50; -. DR EnsemblBacteria; ACQ59406; ACQ59406; VCD_001233. DR KEGG; vcj:VCD_001233; -. DR PATRIC; 20073703; VBIVibCho20143_1253. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; VCHO593588:GI2R-229-MONOMER; -. DR Proteomes; UP000001618; Chromosome 1. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001618}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACQ59406.1}; KW Transferase {ECO:0000313|EMBL:ACQ59406.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1226 AA; 135793 MW; 5CF4AB07A738D74F CRC64; MGKEVRQQLE QQLKQRILLI DGGMGTMIQS YKLQEEDYRG ARFVDWHCDL KGNNDLLVLT QPQIIKEIHS AYLEAGADIL ETNTFNSTTI AMADYDMQSL SAEINFAAAK LAREVADEWT AKDPSRPRYV AGVLGPTNRT CSISPDVNDP GFRNVTFDGL VEAYSESTRA LIKGGSDLIL IETIFDTLNA KACAFAVDSV FEELGISLPV MISGTITDAS GRTLSGQTTE AFYNALRHVR PISFGLNCAL GPDELRQYVE ELSRISECYV SAHPNAGLPN AFGEYDLSAE EMAEHIAEWA QAGFLNLVGG CCGTTPEHIA AIAKAVEGVK PRALPDLKVE CRLSGLEPLN IGPETLFVNV GERTNVTGSA RFKRLIKEEQ YDEALDVARE QVENGAQIID INMDEGMLDA EACMVRFLNL CASEPEISKV PVMVDSSKWE VIEAGLKCIQ GKGIVNSISL KEGKEKFIAQ AKLVRRYGAA VIVMAFDEVG QADTRERKLE ICRRAYHILV DEVGFPPEDI IFDPNIFAVA TGIDEHNNYA LDFINAVADI KRELPHAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK HGMDMGIVNA GQLEIYDNVP LKLREAVEDV ILNRRSDGTE RLLEIAEAYR ENSVGKEEDA SALEWRAWPV AKRLEHALVK GITEFIVQDT EEARQQASKP LEVIEGPLMD GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AYLEPFINAQ KSGSTSNGKI LLATVKGDVH DIGKNIVGVV LQCNNFEIID LGVMVPCEQI LKVAREQNVD IIGLSGLITP SLDEMVHVAK EMERQGFELP LLIGGATTSK AHTAVKIEQN YHAPVVYVNN ASRAVGVCTS LLSDEQRPGF IERLDLDYER TRDQHARKTP KSRPVTLEQA RANKAALDWA NYTPPAPAKP GVHVFENIAL ATLRPYIDWT PFFMTWSLMG KYPAILEHEE VGEEAKRLFH DANALLDKVE REGLLKASGM CALFPAASVG DDIEVYSDES RTQVAHVLYN LRQQTEKPKG ANYCLSDYVA PKESGKRDWI GAFAVTGGIG ERALADAYKA QGDDYNAIMI QAVADRLAEA FAEYLHEKVR KEIWGYASDE NLSNDDLIRE RYQGIRPAPG YPACPEHTEK ATLWQMLNVE ETIGMSLTTS YAMWPGASVS GWYFSHPDSR YFAVAQIQPD QLHSYAERKG WRLEEAEKWL APNLDA // ID C3PEG0_CORA7 Unreviewed; 292 AA. AC C3PEG0; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 30. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACP32214.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ACP32214.1}; GN Name=mmuM {ECO:0000313|EMBL:ACP32214.1}; GN OrderedLocusNames=cauri_0617 {ECO:0000313|EMBL:ACP32214.1}; 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 {ECO:0000313|EMBL:ACP32214.1, ECO:0000313|Proteomes:UP000002077}; RN [1] {ECO:0000313|EMBL:ACP32214.1, ECO:0000313|Proteomes:UP000002077} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700975 / DSM 44827 / CN-1 RC {ECO:0000313|Proteomes:UP000002077}; 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 ----------------------------------------------------------------------- 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; ACP32214.1; -; Genomic_DNA. DR RefSeq; WP_012714888.1; NC_012590.1. DR RefSeq; YP_002834152.1; NC_012590.1. DR STRING; 169292.cauri_0617; -. DR EnsemblBacteria; ACP32214; ACP32214; cauri_0617. DR KEGG; car:cauri_0617; -. DR PATRIC; 21477196; VBICorAur68407_0645. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; YGRSVTK; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; CAUR548476:GH9E-631-MONOMER; -. DR Proteomes; UP000002077; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002077}; KW Methyltransferase {ECO:0000313|EMBL:ACP32214.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002077}; KW Transferase {ECO:0000313|EMBL:ACP32214.1}. SQ SEQUENCE 292 AA; 30579 MW; D230FADE82C3F754 CRC64; MALFDAPLLL DGGLGTHLEA QGHDISGPLW SARVLRENPT LLESAHADFF AAGAQVATTA SYQVTFDVLG EDAEALLRRS VAVAREAVRV AVDKHTAHGD LLVAASIGPY GAGPGKGTDY DGAYDLRRGE LQRWHARRIA VLADTDADFL LAETIPNVDE AAALLELLKA QPKPFALSIT GAIAADQAKL SQVIELANQS SRLGALGVNC VSPSQARAVV ATLRAGTDKP LLACPNSGEV WDCTAHDWQP APADAMSLPE AALQLRAAGV SVLGGCCRVG PAEIRQLRRA IS // ID C3PZM5_9BACE Unreviewed; 917 AA. AC C3PZM5; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 01-APR-2015, entry version 34. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEO60774.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEO60774.1}; GN Name=metH {ECO:0000313|EMBL:EEO60774.1}; GN ORFNames=BSBG_01745 {ECO:0000313|EMBL:EEO60774.1}; OS Bacteroides sp. 9_1_42FAA. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=457395 {ECO:0000313|EMBL:EEO60774.1}; RN [1] {ECO:0000313|EMBL:EEO60774.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=9_1_42FAA {ECO:0000313|EMBL:EEO60774.1}; 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., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; EQ973127; EEO60774.1; -; Genomic_DNA. DR EnsemblBacteria; EEO60774; EEO60774; BSBG_01745. DR PATRIC; 30538170; VBIBacSp125524_1744. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEO60774.1}; KW Transferase {ECO:0000313|EMBL:EEO60774.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 243 243 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 917 AA; 100940 MW; B44B9CB82540F27B CRC64; MATLKQIINE RVLILDGAMG TMIQRYNLSE QDFRGERFAG IPGQMKGNND LLCLTRPDVI KDIHRKYLEA GADIIETNTF NAQRISMADY HMQDLCREIN LVAARLAREL ADEYTAKTPR KPRFVAGSVG PTNKTCSMSP DVNNPALRAL TYDELATAYQ EQMEALLEGG VDALLIETIF DSLNAKAAIY AAETAMKKTG REVPLMLSVT VSDIAGRTLS GQTLDAFLAS VQHAPIFSIG LNCSFGAKQL KPFLEGLAAR APYYISAYPN AGLPNSLGQY DQTPEEMASE VKEYIDEGLV NIIGGCCGTT EEYIAKYQEL IISGSAWVPP HIPATTPERL WLSGLELLEQ TPEMNFINVG ERCNVAGSRK FLRLINEKKY EEALSIARKQ VEDGALVIDV NMDDGLLDAR EEMTTFLNLV MSEPDIARVP IMIDSSKWEV IEAGLKCLQG KSIVNSISLK EGEEKFIEHA RLIKKLGAAT VVMAFDEKGQ ADTFERKIEV CARAYKILTE QVGFNPHDII FDPNVLAVAT GIEEHNNYAV DFINATGWIK KNLPGAHISG GVSNLSFSFR GNNYIREAMH AVFLYHAIRQ GMDMGIVNPA TSVLYTDIPA DVLERIEDVV LNRRPDAAER LIETAEALKN TATGTEAVKQ DVWREEPMVE KRLQYALIKG VGDHLEEDLA EAVKLYPKAV DIIEGPLMEG MNRVGELFGA GKMFLPQVVK TARTMKKAVA ILQPLIEADK QEGARSAGKV LMATVKGDVH DIGKNIVSVV MACNNYEIID LGVMVPAEMI VRKAIEEKVD IIGLSGLITP SLEEMAHVAV ELKRAGLDIP IMIGGATTSK LHTALKIAPV YGGPVIHMKD ASQNALVAAR LLNPESSSEF VERLNKEYEE LRLKNSTKQV KTVSLEEAQK NKLNLWS // ID C3QBI8_9BACE Unreviewed; 915 AA. AC C3QBI8; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 01-APR-2015, entry version 34. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEO49322.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEO49322.1}; GN Name=metH {ECO:0000313|EMBL:EEO49322.1}; GN ORFNames=BSAG_01033 {ECO:0000313|EMBL:EEO49322.1}; OS Bacteroides sp. D1. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=556258 {ECO:0000313|EMBL:EEO49322.1}; RN [1] {ECO:0000313|EMBL:EEO49322.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=D1 {ECO:0000313|EMBL:EEO49322.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEO49322.1}. 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; ACAB02000110; EEO49322.1; -; Genomic_DNA. DR EnsemblBacteria; EEO49322; EEO49322; BSAG_01033. DR PATRIC; 30546360; VBIBacSp27461_1000. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEO49322.1}; KW Transferase {ECO:0000313|EMBL:EEO49322.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 915 AA; 99932 MW; 18EED729F9367757 CRC64; MKKTISQVVS ERILILDGAM GTMIQQYNLK EEDFRGERFA HIPGQLKGNN DLLCLTRPDV IQDIHRKYLE AGADIIETNT FSSTTVSMAD YHVEEYVREM NLAAVKLARD LADEYTAKNP DKPRFVAGSV GPTNKTCSMS PDVNNPAYRA LSYDELAASY QQQMEAMLEG GVDAILIETI FDTLNAKAAI FAAEQAMKAT GVEVPVMLSV TVSDIGGRTL SGQTLDAFLA SMQHANIFSV GLNCSFGARQ LKPFLEQLAA RAPYYISAYP NAGLPNSLGK YDQTPADMAH EVREYIEEGL INIIGGCCGT TDAYIAEYPA LVKGAKPHIP ALAPDCMWLS GLELLEVKPE INFVNVGERC NVAGSRKFLR LINEKKYDEA LSIARQQVED GALVIDVNMD DGLLDAKTEM TTFLNLIMSE PEIARVPVMI DSSKWEVIEA GLKCLQGKSI VNSISLKEGE EVFLEHARII RQYGAATVVM AFDEKGQADT AARKIEVCER AYRLLVDKVG FNPHDIIFDP NVLAVATGIE EHNNYAVDFI EATAWIKKNL PGAHISGGVS NLSFSFRGNN YIREAMHAVF LYHAIQQGMD MGIVNPGTSV LYSDIPTDVL EKIEDVVLNR RPDAAERLIE LAESLKATMS GTAGQPAAKQ DAWREESVQE RLKYALMKGI GDFLEQDLAE ALPLYDKAVD VIEGPLMDGM NYVGELFGAG KMFLPQVVKT ARTMKKAVAI LQPIIESEKV EGSAAAGKVL LATVKGDVHD IGKNIVAVVM ACNGYDIVDL GVMVPAETIV QRAIEEKVDM IGLSGLITPS LEEMAHVALE LEKAGLDIPL LIGGATTSKM HTALKIAPVY HAPVVHLKDA SQNASVASKL LNPQLKAELV NELNSEYEAL REKSGLLKRE TVSLEEAQKN KLNLF // ID C3QPQ8_9BACE Unreviewed; 915 AA. AC C3QPQ8; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 01-APR-2015, entry version 33. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEO53942.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEO53942.1}; GN Name=metH {ECO:0000313|EMBL:EEO53942.1}; GN ORFNames=BSCG_00867 {ECO:0000313|EMBL:EEO53942.1}; OS Bacteroides sp. 2_2_4. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=469590 {ECO:0000313|EMBL:EEO53942.1}; RN [1] {ECO:0000313|EMBL:EEO53942.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=2_2_4 {ECO:0000313|EMBL:EEO53942.1}; 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., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; EQ973356; EEO53942.1; -; Genomic_DNA. DR EnsemblBacteria; EEO53942; EEO53942; BSCG_00867. DR PATRIC; 30505997; VBIBacSp4777_1012. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEO53942.1}; KW Transferase {ECO:0000313|EMBL:EEO53942.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 915 AA; 100038 MW; E55CC44564721482 CRC64; MKKTISQIVS ERILILDGAM GTMIQQYNLK EEDFRGERFA HIPGQLKGNN DLLCLTRPDV IQDIHRKYLE AGADIIETNT FSSTTVSMAD YHVEEYVREM NLAAVKLARD LADEYTAKNP DKPRFVAGSV GPTNKTCSMS PDVNNPAYRA LSYDELAASY QQQMEAMLEG GVDAILIETI FDTLNAKAAI FAAEQAMKMT GIEVPIMLSV TVSDIGGRTL SGQTLDAFLA SVQHANIFSV GLNCSFGARQ LKPFLEQLAS RAPYYISAYP NAGLPNSLGK YDQTPADMAH EVREYIEEGL INIIGGCCGT TDAYIAEYPA LVEGAKPHVP ASAPDCMWLS GLELLEVKPE INFVNVGERC NVAGSRKFLR LINEKKYDEA LSIARQQVED GALVIDVNMD DGLLEAKTEM TIFLNLIMSE PEIARVPIMI DSSKWEVIEA GLKCLQGKSI VNSISLKEGE EVFLEHARII RQYGAAAVVM AFDEKGQADT AARKIEVCQR AYRLLVDKIG FNPHDIIFDP NVLAVATGIE EHNNYAVDFI EATAWIKKNL PGAHISGGVS NLSFSFRGNN YIREAMHAVF LYHAIQQGMD MGIVNPGTSV LYTDIPADVL EKIEDVVLNR RLDAAERLIE LAESLKANMS ETAGQPAVKQ DAWREGTVQE RLKYALMKGI GDFLEQDLAE ALPLYDKAVD VIEGPLMDGM NHVGELFGAG KMFLPQVVKT ARTMKKAVAI LQPIIESEKV EGSASAGKVL LATVKGDVHD IGKNIVAVVM ACNGYDIVDL GVMVPAETIV QRAIEEKVDM IGLSGLITPS LEEMAHVAVE LEKAGLDIPL LIGGATTSKM HTALKIAPVY HAPVVHLKDA SQNASVASKL LNPQAKAELV NELETEYEAL REKSGLMKRE TVSLEEAQKN KLNLF // ID C3R639_9BACE Unreviewed; 917 AA. AC C3R639; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 37. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEO44506.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEO44506.1}; GN Name=metH {ECO:0000313|EMBL:EEO44506.1}; GN ORFNames=BSEG_00647 {ECO:0000313|EMBL:EEO44506.1}; OS Bacteroides dorei 5_1_36/D4. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=556260 {ECO:0000313|EMBL:EEO44506.1}; RN [1] {ECO:0000313|EMBL:EEO44506.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=5_1_36/D4 {ECO:0000313|EMBL:EEO44506.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEO44506.1}. 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; ACDI02000022; EEO44506.1; -; Genomic_DNA. DR RefSeq; WP_007842648.1; NZ_JH114322.1. DR EnsemblBacteria; EEO44506; EEO44506; BSEG_00647. DR PATRIC; 30565833; VBIBacSp91558_0135. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEO44506.1}; KW Transferase {ECO:0000313|EMBL:EEO44506.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 243 243 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 917 AA; 100966 MW; 9311B6D0DE4EEEFA CRC64; MATLKQIINE RVLILDGAMG TMIQRYNLSE QDFRGERFAG IPGQMKGNND LLCLTRPDVI KDIHRKYLEA GADIIETNTF NAQRISMADY HMQDLCREIN LAAARLAREL ADEYTAKTPR KPRFVAGSVG PTNKTCSMSP DVNNPALRAL TYDELATAYQ EQMEALLEGG VDALLIETIF DSLNAKAAIY AAETAMKKTG REVPLMLSVT VSDIAGRTLS GQTLDAFLAS VQHAPIFSIG LNCSFGAKQL KPFLEGLAAR APYYISAYPN AGLPNSLGQY DQTPEEMASE VKEYIDEGLV NIIGGCCGTT EEYIAKYQEL IISGSAWVPP HIPVTTPERL WLSGLELLEQ TPEMNFINVG ERCNVAGSRK FLRLINEKKY EEALSIARKQ VEDGALVIDV NMDDGLLDAR EEMTTFLNLV MSEPDIARVP IMIDSSKWEV IEAGLKCLQG KSIVNSISLK EGEEKFIEHA RLIKKLGAAT VVMAFDEKGQ ADTFERKIEV CARAYKILTE QVGFNPHDII FDPNVLAVAT GIEEHNNYAV DFINATGWIK KNLPGAHISG GVSNLSFSFR GNNYIREAMH AVFLYHAIRQ GMDMGIVNPA TSVLYTDIPA DVLERIEDVV LNRRPDAAER LIETAEALKN TATGTEAVKQ DVWREEPMVE KRLQYALIKG IGDHLEEDLA EAVKLYPKAV DIIEGPLMEG MNRVGELFGA GKMFLPQVVK TARTMKKAVA ILQPLIEADK QEGARSAGKV LMATVKGDVH DIGKNIVSVV MACNNYEIID LGVMVPAETI VRKAIEEKVD IIGLSGLITP SLEEMAHVAV ELQRAELDIP IMIGGATTSK LHTALKIAPV YGGPVIHMKD ASQNALVAAR LLNPESSSEF VERLNKEYEE LRLKNSAKQV KTVSLEEAQK NKLNLWS // ID C3SHY2_ECOLX Unreviewed; 1227 AA. AC C3SHY2; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 38. DE SubName: Full=B12-dependent homocysteine-N5-methyltetrahydrofolate transmethylase {ECO:0000313|EMBL:ACI74086.1}; DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:KIY29470.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:KIY29470.1}; GN Name=metH {ECO:0000313|EMBL:KIY29470.1}; GN ORFNames=ECs4937 {ECO:0000313|EMBL:ACI74086.1}, GN TB57_06515 {ECO:0000313|EMBL:KIY29470.1}, GN UC39_07360 {ECO:0000313|EMBL:KIZ11594.1}; OS Escherichia coli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562 {ECO:0000313|EMBL:ACI74086.1}; RN [1] {ECO:0000313|EMBL:ACI74086.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=493/89 {ECO:0000313|EMBL:ACI74086.1}, RC 86-24 {ECO:0000313|EMBL:ACI74087.1}, RC 87-14 {ECO:0000313|EMBL:ACI74088.1}, RC TB182A {ECO:0000313|EMBL:ACI74089.1}, and RC TW14359 {ECO:0000313|EMBL:ACI74090.1}; 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). RN [2] {ECO:0000313|EMBL:KIZ11594.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35150 NalR {ECO:0000313|EMBL:KIZ11594.1}; RA Markell J.A., Carrillo C.D., Koziol A., Manninger P., Blais B., RA Lambert D.; RT "Complete Genome Sequence of Escherichia coli O157:H7 ATCC 35150 RT Nalidixic Acid Resistant Mutant."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:KIY29470.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35150 {ECO:0000313|EMBL:KIY29470.1}; RA Markell J.A., Carrillo C.D., Manninger P., Koziol A.G., Lambert D., RA Blais B.; RT "Complete Genome Sequence of Escherichia coli O157:H7 ATCC 35150."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; EU891505; ACI74086.1; -; Genomic_DNA. DR EMBL; EU891506; ACI74087.1; -; Genomic_DNA. DR EMBL; EU891507; ACI74088.1; -; Genomic_DNA. DR EMBL; EU891508; ACI74089.1; -; Genomic_DNA. DR EMBL; EU891509; ACI74090.1; -; Genomic_DNA. DR EMBL; JXUS01000064; KIY29470.1; -; Genomic_DNA. DR EMBL; JYIO01000036; KIZ11594.1; -; Genomic_DNA. DR ProteinModelPortal; C3SHY2; -. DR SMR; C3SHY2; 651-1227. DR HOGENOM; HOG000251409; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACI74086.1}; KW Transferase {ECO:0000313|EMBL:ACI74086.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136040 MW; 8FB5738E12303E7E CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID C3WBE7_FUSMR Unreviewed; 1081 AA. AC C3WBE7; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 2. DT 27-MAY-2015, entry version 35. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEO35184.2}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEO35184.2}; GN Name=metH {ECO:0000313|EMBL:EEO35184.2}; GN ORFNames=FMAG_00746 {ECO:0000313|EMBL:EEO35184.2}; OS Fusobacterium mortiferum ATCC 9817. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=469616 {ECO:0000313|EMBL:EEO35184.2}; RN [1] {ECO:0000313|EMBL:EEO35184.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 9817 {ECO:0000313|EMBL:EEO35184.2}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEO35184.2}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACDB02000014; EEO35184.2; -; Genomic_DNA. DR RefSeq; WP_005884599.1; NZ_GL987988.1. DR EnsemblBacteria; EEO35184; EEO35184; FMAG_00746. DR PATRIC; 30259211; VBIFusMor134737_0035. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEO35184.2}; KW Transferase {ECO:0000313|EMBL:EEO35184.2}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 226 226 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 722 722 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1081 AA; 121863 MW; 59FBF3C8A4513131 CRC64; MDIKKELQKR ILVLDGAMGT AIQKYNLNSD DYLGKKGCNE ILNITRPDII KDIHLKYIEA GADIIETNSF NCNKISLNEY GFSERAYEIA KRSAELAKEV TTTSEKKIYI AGSIGPTNKT LTIPSGKNPY DRDLEFDYLK EAYSEQIEGL IDGGVDILLI ETIFDGLNAK CAVISAEEVM KRKNINLPIM ISATVNKEGK IFTGQSIESL IVALDRESII SYGFNCSFGA KELIPLTKKL GKFTKKPISL YPNAGLPNED GEYLESPDIT ANYLKELVDN QEVNILGGCC GTTFEHIKSI ANLVKNRAPR KFEENFKLEG FLSGNEILYF NDKFVDVGEK NNVAGSKIFK NLIADKNYIK ALEIAKKQIE NGAKVIDINM DDGLFESKIE MKNFLIVIQN DRFVSKIPIM IDSSDFEVIE TGLKNIAGKS IVNSISLKEG EEEFRKKAQV IKKYGASVVV MAFDEKGQGV SYERKIEICS RAYSILKEIG YSNSDIIFDL NILTIGTGME SDRYNGLNFL KACEWIRKNF KGVGIIGGLS NLSFAFRGNN DLRAGLHSIF LEEGKNRGLN FAILNPNENP PILSLEDKKI LRDLIFGEES SLEQILNLHI QRKKEVVIKE ELTLEQCIEN ALIFGETPEF INDINSALKI YSPLDIIQNI LMEGMKKLGV LFEKGEVYLP QLIRSSETMN KAVNIITPHL KSDEKVKAKG KILMATVEGD VHDIGKNIVG TVLKCNGYEI IDLGVMVPKE TILSTAKEQN VDIITLSGLI TPSLKEMEKV LKYFQENSMK TLILIAGATT SPLHTALRLE PLYSGKVLHV SEALDTLQSI NKLCSDEREE FLSEKLQNFK TLRKLYEKNK KENIEDTQEI LSPVIIPKEI GKKYLEISLE DIEKYINLDI LLHTLKVKNS NEELKIKEDL SFIFNKMKEN NLKVRGSYGI FSSKKIDGKL IIEDNIISTK EDFIYKFINN DDYIGAFALS YKSEIFKEKE YLKILEELLN NRIVEAGAEY LEDFVSKNIW KINIRPAIGY PSLPNHQLKE TVLKILDEDK LDIKLTSSYA MLPLSSVCGL YISNPKSFYK K // ID C3WSU1_FUSNV Unreviewed; 320 AA. AC C3WSU1; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEO40947.1}; GN ORFNames=FSCG_01660 {ECO:0000313|EMBL:EEO40947.1}; OS Fusobacterium nucleatum subsp. vincentii 4_1_13. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=469606 {ECO:0000313|EMBL:EEO40947.1}; RN [1] {ECO:0000313|EMBL:EEO40947.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=4_1_13 {ECO:0000313|EMBL:EEO40947.1}; 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., 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; GG658000; EEO40947.1; -; Genomic_DNA. DR RefSeq; WP_008803436.1; NZ_GG658000.1. DR EnsemblBacteria; EEO40947; EEO40947; FSCG_01660. DR PATRIC; 30298784; VBIFusSp49854_1780. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEO40947.1}; KW Transferase {ECO:0000313|EMBL:EEO40947.1}. SQ SEQUENCE 320 AA; 35394 MW; 00C4DBC0F774F139 CRC64; MKKIMFEIEK ELKERILVLD GAMGTVLQKY ELPAEDFNGT KGCYEILNET RPDIIFEVHK KYIEAGADII ETNSFNCNAI SLKNYHLEDK VYDLAKKSAE IAKDAVRKSG KKVYVFGSVG PTNKGLSFPE KDVSCKRAVS FDEMKEVIKV QVTGLIDGGV DGILLETIFD GLTAKAALLA IEEVFAEKNI KLPISISATV NKQGKLLTGQ SIESLIVDLD RDSVISFGFN CSFGAKDLVP FVLKIKELTT KFISLHANAG LPNQNGEYEE TAQKMRDDLL PLIENQAINI LGGCCGTDYE HIKLIAELIK GQKPRVLLEK // ID C3WZX5_FUSNU Unreviewed; 1081 AA. AC C3WZX5; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 37. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEO43501.1}; GN ORFNames=FSDG_02060 {ECO:0000313|EMBL:EEO43501.1}; OS Fusobacterium nucleatum subsp. animalis 7_1. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=457405 {ECO:0000313|EMBL:EEO43501.1, ECO:0000313|Proteomes:UP000002799}; RN [1] {ECO:0000313|EMBL:EEO43501.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=7_1 {ECO:0000313|EMBL:EEO43501.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP007062; EEO43501.1; -; Genomic_DNA. DR RefSeq; WP_008702444.1; NZ_AKBT01000001.1. DR EnsemblBacteria; EEO43501; EEO43501; FSDG_02060. DR GeneID; 23370356; -. DR PATRIC; 30304081; VBIFusSp38687_1866. DR Proteomes; UP000002799; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002799}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 723 723 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1081 AA; 120755 MW; B361E4114A49EE8A CRC64; MFEIEKELKE RILVLDGAMG TVLQKYELSA EDFNGAKGCY EILNETRPDI IFEVHKKYIE AGADIIETNS FNCNSISLKD YHLEDKVYDL AKKSAEIARD AVKESGKKVY IFGSVGPTNK SLSFPVGDIP FKRAVSFDEM KEVIKVQVAG LIDGGVDGIL LETIFDGLTA KAALLATEEV FEEKNIKLPI SISATVNKQG KLLTGQSMES LIVALDRDSV TSFGFNCSFG AKDLVPLVLK IKELTTKFVT LHANAGLPNQ NGDYVETAQK MKNDLLPLIE NQAINILGGC CGTSYDHIKA IAELVKGQKP RVLPEKNLLE TCLSGNEIYN FKDKFTCVGE RNNISGSKLF RTMIEEHNYL KALDVARQQI DAGAKVLDIN VDDAILDSVE EMKNFLRVLQ NDSFIAKVPI MIDSSDFAVI EEGLKNTAGK AIVNSISLKE GEENFLRKAK ITRKYGASII VMAFDENGQG VSAERKIEIC QRAYNLLKSI GVKNSDIVFD PNILSVGTGQ EADRYHAREF LKTIDYIHKN LKGCGIVGGL SNLSFAFRGN NILRAAFHHI FLEEAIPRGF NFAILNPKEK APQWTDEERE KIKSFIFGDS ANIEDLLSLN LVKRKEDAQI FAETPEDRIR KALIQGGSES LQEVIEELLK KYKALEILEN ILMSAMQEIG RLFEQGELYL PQLIRSASVM NNCVNILTPY LEKVDRTSSK GKILMATVDG DVHDIGKNIV KTVLECNGYE VIDLGVMVPR EKIVEVAKNN NVDIVTLSGL ISPSLKEMER VADSFQKVGM QIPILIAGAA TSKLHTGLKV LPNYDYSLHV TDAMDTITVV SQLLSTKRKD FLEAKQNQLR KIAKRYIENN DQTGEKKILP EVKKTVSYIP KVLGKQFLSL PVEILKDDLK WDIAFYALRV KNTPEEEKTL NDLKKIYEKL IEEKVEFKAA YGYFRCKKTE TFLEMEGMTF EVSPNIAQYI EKEDYLGAFV VSVKSEIFKD DKYLGLLETL LCNVIAEAAS EYMERRVSKD IVPTFLRPAV GYPILPDHSL KKVVFDLIDG EKTGAKLSPA FAMSPLSSVC GFYLCNDNAK Y // ID C3X5U7_OXAFO Unreviewed; 1253 AA. AC C3X5U7; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 39. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEO28583.1}; GN ORFNames=OFAG_01736 {ECO:0000313|EMBL:EEO28583.1}; OS Oxalobacter formigenes HOxBLS. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae; Oxalobacter. OX NCBI_TaxID=556268 {ECO:0000313|EMBL:EEO28583.1}; RN [1] {ECO:0000313|EMBL:EEO28583.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HOxBLS {ECO:0000313|EMBL:EEO28583.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEO28583.1}. 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; ACDP02000001; EEO28583.1; -; Genomic_DNA. DR RefSeq; WP_005878412.1; NZ_KI392030.1. DR EnsemblBacteria; EEO28583; EEO28583; OFAG_01736. DR PATRIC; 28553803; VBIOxaFor11927_2189. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 262 262 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 327 327 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 328 328 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 780 780 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1253 AA; 138708 MW; AEFD5735AA664AC4 CRC64; MTQMDINSTE NRLREIMSRR ILVLDGAMGT MIQRYGLTEE DYRGGPDGRF ADFVPPASAG DRELFVKGNN ELLSLTQPHI ISAIHEAYLK AGADVIETNT FGATAIAQDD YHMAHLVYEM NVQSARIARE ICDKYATPDR PRFVAGSMGP TPRTASISPD VNDPGARNIT FDQLVAAYSE QVRALVEGGV DLLLVETVFD TLNCKAALFA IDSFFETAGK KLPIMISGTV TDASGRILSG QTVTAFWHSI RHARPLTVGL NCALGAALMR PYVEELSRIA DTHICIYPNA GLPNPMSETG FDELPEDTSA FLKEFAESGF INVVGGCCGT TPDHIRAIAE AVAPLPPRKL PAIPPAMRLS GLEPFTIDED SLFVNVGERT NVTGSKAFAR MILNEEYDKA LAVARQQVEN GAQIIDINMD EAMLDSVSAM RRFLNLIASE PEIARVPVML DSSKWEVIET GLKCLQGKSI VNSISLKAGE AEFLRQAKLC RRYGAAVIVM AFDEQGQADT YERKISICRR AYDLLVNTIG FPAEDIIFDP NIFAVATGID EHNNYAVDFI EATRWIKANL PHAKVSGGVS NVSFSLRGNN PAREAIHTVF LYHAISAGMT MGIVNAGMIG VYDEIPEALR ERVEDVVLNR RPDATERLVE VANAFQAGAK KESDNLQWRT EPVGKRLTYA FVHGLTDFIT EDTDEALQEI LKKGGQPIEV IEGPLMDGMN AVGDLFGQGK MFLPQVVKSA RVMKQAVAYL VPYIEEQKRL SGNTQPKGKI VIATVKGDVH DIGKNIVAVV LQCNNFEVIN MGVMVPCEEI LAKAKEVNAD AIGLSGLITP SLEEMMHVAS EMQRDEYFRS RRIPLFVGGA TTSKTHTAIK IAPNYEGPVV QVPDASRTVT VIQALLSDSM REKYIKVLTD DYEHIRELHA QKKPKKLLSI EEARANKAKL SFKETNAPKK PIYLGQRFLR NIDLSVLTSY IDWSPFFRVW DLPGSYPDIL NDNAHGETAR KVFEDGQKML EKLIRGKWLT ANATIALMPA NSVNDDDIEI YTDETRSNVA FTYYGVRQQM EKPVVGGVSR PNQSLADFIA PKSSGIRDYI GMFGVTTGIG IERRLEEFDA ARNDYDSIML KALADRLVEA LAEYLHELVR KDLWGYAPNE HFTNEQLQKE LYSGIRPAPG YPSCPEHTVK SDLFRILRCE EIGMSLTESY AMLPTASITG FYFAHPDARY FTIGKIGKDQ VADMAKRRHV NEEKIAQWLA PVL // ID C3XC26_OXAFO Unreviewed; 1253 AA. AC C3XC26; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 35. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEO30752.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEO30752.1}; GN Name=metH {ECO:0000313|EMBL:EEO30752.1}; GN ORFNames=OFBG_01780 {ECO:0000313|EMBL:EEO30752.1}; OS Oxalobacter formigenes OXCC13. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae; Oxalobacter. OX NCBI_TaxID=556269 {ECO:0000313|EMBL:EEO30752.1}; RN [1] {ECO:0000313|EMBL:EEO30752.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=OXCC13 {ECO:0000313|EMBL:EEO30752.1}; 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., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG658170; EEO30752.1; -; Genomic_DNA. DR RefSeq; WP_005882192.1; NZ_GG658170.1. DR EnsemblBacteria; EEO30752; EEO30752; OFBG_01780. DR PATRIC; 25833429; VBIOxaFor91597_0924. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEO30752.1}; KW Transferase {ECO:0000313|EMBL:EEO30752.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 262 262 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 327 327 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 328 328 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 780 780 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1253 AA; 138887 MW; AF74AE45238AC79A CRC64; MTSTEKTSTE ARLREIMSKR ILVLDGAMGT MIQRYGLTEE DYRGGPEGRF ANFAPPASES ERELFVKGNN ELLSLTQPHI ISAIHEEYLK AGADVIETNT FGATSIAQSD YHMSHLVYEM NVQSAKIARE ICDKYSTPDH PRFVAGSIGP TPRTASISPD VSDPGARNVT FDQLVEAYLE QIRGLVEGGA DLLLVETVFD TLNCKAALFA IDTFFEESGK KLPIMISGTV TDASGRILSG QTVTAFWYSI RHARPLTVGL NCALGAALMR PYVEEISRIA DTHICIYPNA GLPNPMSETG FDELPEDTSA FLKEFAESGF INVVGGCCGT TPDHIRAIAK AVTPLPPRKV PTIPPAMRLS GLEPFTIDDS SLFVNVGERT NVTGSKAFAR MILNEEYDNA LAVARQQVEN GAQIIDINMD EAMLDSVSAM HRFLNLIASE PEISRVPVML DSSKWEVIEA GLKCLQGKSI VNSISLKNGE EEFIHHAKLC RRYGAAIIVM AFDEKGQADT YQRKIDICKR AYDLLVNQIG FPSEDIIFDP NIFAIATGIE EHNNYAVDFI EATRWIRDNL PNARISGGVS NVSFSLRGNN PAREAIHTVF LYHAISAGMT MGIVNAGMMG VYDEIPEALR ERVEDAVLNR REDATERLID VAGEFQSGAK KEGENLQWRE DSVNKRLSYA FVHGVTDFII EDTEEALQDT LKNGGKPIEV IEGPLMDGMN AVGDLFGQGK MFLPQVVKSA RVMKQAVAHL IPYIEEEKRQ SGSSQSNGKI VIATVKGDVH DIGKNIVAVV LQCNNFEVIN LGVMVPCEEI LAKAKEVNAD AIGLSGLITP SLEEMMYVAG EMQRDEYFRS RNIPLFIGGA TTSKTHTAVK IAPNYEGPVV HVTDASRTVT VIQALLSDSI REKYLKVLSD DYEHIRELHA QKKPQKLLSI EDARKNKAQL SFEGKDAPKR PTYLGQRFLK NIDLATLVDY IDWSPFFRVW DLSGSYPTIL NDAVHGEMAR KVFADGQKML EKLIKGKWLT ANATLALMPA NSVNDDDIEI YTDESRSKVA FTYYGVRQQN EKPVVDGVAR PNQCMSDFIA PKSSGIKDYI GMFGVTAGLG IEKHLEQFET ELDDYDAIML KALADRLVEA LAEYLHELVR KDLWGYSSNE TFTNEQLIKE QYRGIRPAPG YPSCPEHTVK DDLFRILRCE EIGMKLTESY AMLPTASITG FYFAHPDAHY FTIGKIGKDQ VSDMAKRRNV SEEQLAKWLA PIL // ID C3XLV5_9HELI Unreviewed; 1154 AA. AC C3XLV5; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAY-2015, entry version 35. DE SubName: Full=Vitamin B12 dependent methionine synthase, activation domain protein {ECO:0000313|EMBL:EEO25994.1}; GN ORFNames=HWAG_00786 {ECO:0000313|EMBL:EEO25994.1}; OS Helicobacter winghamensis ATCC BAA-430. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=556267 {ECO:0000313|EMBL:EEO25994.1}; RN [1] {ECO:0000313|EMBL:EEO25994.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-430 {ECO:0000313|EMBL:EEO25994.1}; 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., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG661974; EEO25994.1; -; Genomic_DNA. DR RefSeq; WP_006802480.1; NZ_GG661974.1. DR EnsemblBacteria; EEO25994; EEO25994; HWAG_00786. DR PATRIC; 27528403; VBIHelWin108846_1089. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 224 224 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 728 728 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1154 AA; 127964 MW; 56C141F3BD3448FF CRC64; MVLRNCIKER VLILDGAMGT EIQKHNIQTW GVNAKGEKLD GCSEALNLYA KDIIKAIHTS YLQAGANILK TNTFGVMPWV LAEYGLEEHC KEIAKTGVEL AKECIKKHSP LKNQNNALFV AASLGPGTKL PSLGHITYDS MEEGYALCVE GFKEADADVI LLETAQDPLQ IKAALNAIKN TAPEIPIMVS VTIETTGTML IGTDITTLFH ILEPYDLLSL GINCGLGPDL AHKHLVTLSE VCKFPISIHT NAGLPENRGG VTYYPMDAEE FSTIEKSFLE IPGVAFLGGC CGTTPEHIRQ LVQKTQSIIP KAPKCTYQPS ITSLFEAKEL KQFPAPLLIG ERSNATGSKA FRELLLNEDY EGALSVGSAQ VRSGAHCLDL SVAFAGRDES KDMQELITRY ATKITLPLMP DSTQVNALEI ALKHIGGRAI INSANLEDGI TKFDKVASLA KKFGAALICL TIDEEGMCKT FERKIACAKR MMERAITIHN LREEDIIFDP LTFTIGSGDA EYFDAGMQTL NTIKELSKLY PKAGTTLGLS NISFGLSKEG RICLNSIFLH HAIKNGLTSA IVNVSHIIPY NKLEADDIKV CENLIFNTEL SSAPLYAFIK HFESKNTLDL PKQEQDVHLS IEERIQKYLI DGELNAMLEL LPSAKDSISP EKIINEILID AMKIVGERFG NGEMQLPFVL QSAEVMKKSV DYLNAFLPKK QSTHKTTIVL GTVKGDVHDV GKNLVDIILT NNGFSVINIG IKAELEKFLE VLQTQKVDCI GMSGLLVKST LVMKENLEAL KKLDIKIPIM LGGAALNRNF VEEYCKPNYD GVIFYCKDAF DSVAAMQIIQ SGDFSDLTLP SQKGTKNKED IEENKITKQE ARLKKKLDST LDSKKESINK PTKCEITFEY ATHTPPFFGV KSLELNANDL DSVFDYIDKD LLFKHRWGYS KLKKEEYQIL KAKELEPLLK SLKEEFITKE IFKPVVLYGY FHTRTIAPKN LEDGLILEVS ATKDFIDSEQ FLFPRSTKKP YLCLSDYFNP QGDICAMHLV SSGNNFAPYE AELYKNAQYH KYYLAHTLGM DLAEALADFI HAKVRDALQL DAKCGQRYSF GYPACPDLAL SVGLFNLFKP ESFGITLSDT YQMSPEATTS ALIVPNKEAK YFAI // ID C3XT42_BRAFL Unreviewed; 122 AA. AC C3XT42; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 07-JAN-2015, entry version 28. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EEN68775.1}; GN ORFNames=BRAFLDRAFT_97253 {ECO:0000313|EMBL:EEN68775.1}; OS Branchiostoma floridae (Florida lancelet) (Amphioxus). OC Eukaryota; Metazoa; Chordata; Cephalochordata; Branchiostomidae; OC Branchiostoma. OX NCBI_TaxID=7739 {ECO:0000313|Proteomes:UP000001554}; RN [1] {ECO:0000313|EMBL:EEN68775.1, ECO:0000313|Proteomes:UP000001554} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN68775.1, RC ECO:0000313|Proteomes:UP000001554}; RC TISSUE=Testes {ECO:0000313|EMBL:EEN68775.1}; RX PubMed=18563158; DOI=10.1038/nature06967; RG US DOE Joint Genome Institute (JGI-PGF); RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U., RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K., RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., RA Gibson-Brown J.J., Grigoriev I.V., Horton A.C., de Jong P.J., RA Jurka J., Kapitonov V.V., Kohara Y., Kuroki Y., Lindquist E., RA Lucas S., Osoegawa K., Pennacchio L.A., Salamov A.A., Satou Y., RA Sauka-Spengler T., Schmutz J., Shin-I T., Toyoda A., RA Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H., RA Satoh N., Rokhsar D.S.; RT "The amphioxus genome and the evolution of the chordate karyotype."; RL Nature 453:1064-1071(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; GG666461; EEN68775.1; -; Genomic_DNA. DR RefSeq; XP_002612766.1; XM_002612720.1. DR STRING; 7739.JGI97253; -. DR GeneID; 7251059; -. DR KEGG; bfo:BRAFLDRAFT_97253; -. DR eggNOG; KOG1579; -. DR InParanoid; C3XT42; -. DR KO; K00544; -. DR Proteomes; UP000001554; Partially assembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001554}; KW Reference proteome {ECO:0000313|Proteomes:UP000001554}. SQ SEQUENCE 122 AA; 13912 MW; CA47C469BE106C7F CRC64; MAAKAKGLLE RFRDGETVIC AEGYLFEFER RGYLQAGGFV PEVVIEHPEL VEGLHREFVH AGSDVVLAFT FYAHREKLRL VGREADLEKM NRTALRLARK MSGKVSHAIL SPYVRPPEED RK // ID C3XWR6_BRAFL Unreviewed; 292 AA. AC C3XWR6; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 27-MAY-2015, entry version 31. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EEN67176.1}; GN ORFNames=BRAFLDRAFT_88435 {ECO:0000313|EMBL:EEN67176.1}; OS Branchiostoma floridae (Florida lancelet) (Amphioxus). OC Eukaryota; Metazoa; Chordata; Cephalochordata; Branchiostomidae; OC Branchiostoma. OX NCBI_TaxID=7739 {ECO:0000313|Proteomes:UP000001554}; RN [1] {ECO:0000313|EMBL:EEN67176.1, ECO:0000313|Proteomes:UP000001554} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN67176.1, RC ECO:0000313|Proteomes:UP000001554}; RC TISSUE=Testes {ECO:0000313|EMBL:EEN67176.1}; RX PubMed=18563158; DOI=10.1038/nature06967; RG US DOE Joint Genome Institute (JGI-PGF); RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U., RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K., RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., RA Gibson-Brown J.J., Grigoriev I.V., Horton A.C., de Jong P.J., RA Jurka J., Kapitonov V.V., Kohara Y., Kuroki Y., Lindquist E., RA Lucas S., Osoegawa K., Pennacchio L.A., Salamov A.A., Satou Y., RA Sauka-Spengler T., Schmutz J., Shin-I T., Toyoda A., RA Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H., RA Satoh N., Rokhsar D.S.; RT "The amphioxus genome and the evolution of the chordate karyotype."; RL Nature 453:1064-1071(2008). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG666471; EEN67176.1; -; Genomic_DNA. DR RefSeq; XP_002611166.1; XM_002611120.1. DR STRING; 7739.JGI88435; -. DR GeneID; 7247521; -. DR KEGG; bfo:BRAFLDRAFT_88435; -. DR eggNOG; COG0646; -. DR InParanoid; C3XWR6; -. DR KO; K00544; -. DR OMA; ARAMFKE; -. DR Proteomes; UP000001554; Partially assembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001554}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000001554}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 157 157 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 239 239 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 240 240 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 292 AA; 32121 MW; AD415DD9D7FEF969 CRC64; MKVGSLLQCS YFLQFYAHRE KLRLVGREAD LERMNRTALR LARKVADDTG TLMAGNICGT NIYDATDPAW EPKARAMFKE QIEWAVEGGA DFIYAETFFA YAEARLALEC VKQYGKGLPA VVGISKHRGD LLFDGVPLGD ALVRLAEAGA AAVGLNCGRG PPTMLPLLED LKDKIKVPLV AAPVPYRTHP DSPHFMTLKD PDGKVAFPLD LDPWLCSRSQ IAAFSRRARA LGARYLGLCC GNASHFTRAM AEALGRQPPA SRYTADMSKH AYYGTDPTLI DFNTQEVCKN NF // ID C3XWR7_BRAFL Unreviewed; 397 AA. AC C3XWR7; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 04-MAR-2015, entry version 32. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EEN67177.1}; GN ORFNames=BRAFLDRAFT_88434 {ECO:0000313|EMBL:EEN67177.1}; OS Branchiostoma floridae (Florida lancelet) (Amphioxus). OC Eukaryota; Metazoa; Chordata; Cephalochordata; Branchiostomidae; OC Branchiostoma. OX NCBI_TaxID=7739 {ECO:0000313|Proteomes:UP000001554}; RN [1] {ECO:0000313|EMBL:EEN67177.1, ECO:0000313|Proteomes:UP000001554} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN67177.1, RC ECO:0000313|Proteomes:UP000001554}; RC TISSUE=Testes {ECO:0000313|EMBL:EEN67177.1}; RX PubMed=18563158; DOI=10.1038/nature06967; RG US DOE Joint Genome Institute (JGI-PGF); RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U., RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K., RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., RA Gibson-Brown J.J., Grigoriev I.V., Horton A.C., de Jong P.J., RA Jurka J., Kapitonov V.V., Kohara Y., Kuroki Y., Lindquist E., RA Lucas S., Osoegawa K., Pennacchio L.A., Salamov A.A., Satou Y., RA Sauka-Spengler T., Schmutz J., Shin-I T., Toyoda A., RA Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H., RA Satoh N., Rokhsar D.S.; RT "The amphioxus genome and the evolution of the chordate karyotype."; RL Nature 453:1064-1071(2008). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG666471; EEN67177.1; -; Genomic_DNA. DR RefSeq; XP_002611167.1; XM_002611121.1. DR STRING; 7739.JGI88434; -. DR GeneID; 7246247; -. DR KEGG; bfo:BRAFLDRAFT_88434; -. DR eggNOG; COG0646; -. DR InParanoid; C3XWR7; -. DR KO; K00544; -. DR OMA; TVICADG; -. DR Proteomes; UP000001554; Partially assembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001554}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000001554}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 262 262 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 344 344 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 345 345 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 397 AA; 43525 MW; C7BA3B624AB0BD1C CRC64; MEEPKPKGLL AHLQAGETVI CADGYLLELG LLTRLQAGET VICAAPAGTC WSWVRGLLAR LKAGETVICA GGYLLELERR GYLQAGTFVP EVVVEHPDKV EALHREFVHA GSDVVLALTH YAHREKMRII GREADLERMN RTALRLARKV ADDTGTLMAG NICKLNLFDP NNSGWKEKAE VMFKEQLEWA VEGGADFVVA ESFFAHAEAM FALQCAKKYA KGLPVVVTLN LQRHSELIDG VPIQTALQEL AEAGADVVGL NCGRGPPTML PVLEEAKNNI KIPLAAVPVP YRTHEGDPNF LTLKDENGKV AFPLDLDPWL CSRSQIAAFS RRARALGVRY LGLCCGNASH FTRAMAEALG RQPPASRYTA DMSKHAYYGT DPTLIDFNTQ EVCKNKF // ID C3XWR8_BRAFL Unreviewed; 351 AA. AC C3XWR8; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 04-MAR-2015, entry version 32. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EEN67178.1}; GN ORFNames=BRAFLDRAFT_88433 {ECO:0000313|EMBL:EEN67178.1}; OS Branchiostoma floridae (Florida lancelet) (Amphioxus). OC Eukaryota; Metazoa; Chordata; Cephalochordata; Branchiostomidae; OC Branchiostoma. OX NCBI_TaxID=7739 {ECO:0000313|Proteomes:UP000001554}; RN [1] {ECO:0000313|EMBL:EEN67178.1, ECO:0000313|Proteomes:UP000001554} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN67178.1, RC ECO:0000313|Proteomes:UP000001554}; RC TISSUE=Testes {ECO:0000313|EMBL:EEN67178.1}; RX PubMed=18563158; DOI=10.1038/nature06967; RG US DOE Joint Genome Institute (JGI-PGF); RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U., RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K., RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., RA Gibson-Brown J.J., Grigoriev I.V., Horton A.C., de Jong P.J., RA Jurka J., Kapitonov V.V., Kohara Y., Kuroki Y., Lindquist E., RA Lucas S., Osoegawa K., Pennacchio L.A., Salamov A.A., Satou Y., RA Sauka-Spengler T., Schmutz J., Shin-I T., Toyoda A., RA Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H., RA Satoh N., Rokhsar D.S.; RT "The amphioxus genome and the evolution of the chordate karyotype."; RL Nature 453:1064-1071(2008). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG666471; EEN67178.1; -; Genomic_DNA. DR RefSeq; XP_002611168.1; XM_002611122.1. DR STRING; 7739.JGI88433; -. DR GeneID; 7246556; -. DR KEGG; bfo:BRAFLDRAFT_88433; -. DR eggNOG; COG0646; -. DR InParanoid; C3XWR8; -. DR KO; K00544; -. DR Proteomes; UP000001554; Partially assembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001554}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000001554}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 216 216 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 298 298 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 351 AA; 38822 MW; F2455F32FB2885B5 CRC64; MNIEKKVTTG LLARLQAEET VICAGGYLLE LERRGYLQAG TFVPEIVIEH PDKVEALHRE FVHAGSDVVL ALTHYAHREK MRIIGREADL ERMNRTALRL ARKVADDTGT LMAGNICKLN LFDPNSSGWK EKAEVMFKEQ LEWAVEGGAD FVVAESFFAH AEAMFALQCA KKYAKGLPLV VTLNLQRHSE LIDGVPIQTA LQELAEAGAD VVGLNCGRGP PTMLPVLEEA RNNIKIPLAA VPVPYRTHEG DPNFLTLKDE NGKVAFPLDL DPWLCSRSQI AAFSRRARAL GVRYLGLCCG NASHFTRAMA EALGRQPPAS RYTADMSKHA YYGTDPTLID FNTQEVCKNK F // ID C3XWR9_BRAFL Unreviewed; 683 AA. AC C3XWR9; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 07-JAN-2015, entry version 26. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EEN67179.1}; GN ORFNames=BRAFLDRAFT_88432 {ECO:0000313|EMBL:EEN67179.1}; OS Branchiostoma floridae (Florida lancelet) (Amphioxus). OC Eukaryota; Metazoa; Chordata; Cephalochordata; Branchiostomidae; OC Branchiostoma. OX NCBI_TaxID=7739 {ECO:0000313|Proteomes:UP000001554}; RN [1] {ECO:0000313|EMBL:EEN67179.1, ECO:0000313|Proteomes:UP000001554} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN67179.1, RC ECO:0000313|Proteomes:UP000001554}; RC TISSUE=Testes {ECO:0000313|EMBL:EEN67179.1}; RX PubMed=18563158; DOI=10.1038/nature06967; RG US DOE Joint Genome Institute (JGI-PGF); RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U., RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K., RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., RA Gibson-Brown J.J., Grigoriev I.V., Horton A.C., de Jong P.J., RA Jurka J., Kapitonov V.V., Kohara Y., Kuroki Y., Lindquist E., RA Lucas S., Osoegawa K., Pennacchio L.A., Salamov A.A., Satou Y., RA Sauka-Spengler T., Schmutz J., Shin-I T., Toyoda A., RA Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H., RA Satoh N., Rokhsar D.S.; RT "The amphioxus genome and the evolution of the chordate karyotype."; RL Nature 453:1064-1071(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; GG666471; EEN67179.1; -; Genomic_DNA. DR RefSeq; XP_002611169.1; XM_002611123.1. DR STRING; 7739.JGI88432; -. DR GeneID; 7247510; -. DR KEGG; bfo:BRAFLDRAFT_88432; -. DR eggNOG; COG0646; -. DR InParanoid; C3XWR9; -. DR KO; K00544; -. DR Proteomes; UP000001554; Partially assembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 2. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001554}; KW Reference proteome {ECO:0000313|Proteomes:UP000001554}. SQ SEQUENCE 683 AA; 76080 MW; B22CDAC143A598B4 CRC64; MVQCAHRPGE ADDETVICAE GYLFEFERRG YLQAGGYVPE VVIEHPELVE GLHREFVHAG SDVVLAFTYY AHREKMRLIG REEDLEKINR TALRLARKVA DDTGTLMAGN ICNLNIYDQA DPSWEGRAHA MFKEQLEWIM EEGGCDFIVA ETFFAFAEAK LALECVRKYA KGIPVVVSFN LKRGDDLIDG VLIQDALRRL AEAGADVVGL NCGRGPATTL PVLEEARRNG IKTPLSFVPV AYRTDDENPN MITLKDVDDK GKIAFPSDLD PWLCSRSQIA SYTRKAHALG VRFMGICCGN ASHFTRAMAE ALGRQPPASR YTADMTKHAY YGTDPTLIDF NTQEDDETII CAEGYLFEFE RRGFLKAGGF VPEVVIEHPE LVEGLHREFV HAGSDVVLAF TYYAHREKMR IIGREADLEK INRTALRLAR KVADDTGTLM AGNICNLNIY DQADPSWEGR AHGMFKEQLE WIMEEGGCDF ILAETFFAYA EAKLALECVR KYAKGIPVVV SFNLKRGDDL IDGVLIQDAL RRLAEAGADV VGLNCGRGPA TTLPVLEEAK QNGIKTPLAF VPVPYRTDDE NPNFMTLKDV NDNGKIAFPL DLDPWLCSRS QIASYTRKAH ALGVRFMGIC CGNASHFTRA MAEALGRQPP ASRYTADMSK HAYYGTDPTL IDFNTQEVCK NKF // ID C3Y1N2_BRAFL Unreviewed; 396 AA. AC C3Y1N2; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 04-MAR-2015, entry version 35. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EEN65772.1}; GN ORFNames=BRAFLDRAFT_78594 {ECO:0000313|EMBL:EEN65772.1}; OS Branchiostoma floridae (Florida lancelet) (Amphioxus). OC Eukaryota; Metazoa; Chordata; Cephalochordata; Branchiostomidae; OC Branchiostoma. OX NCBI_TaxID=7739 {ECO:0000313|Proteomes:UP000001554}; RN [1] {ECO:0000313|EMBL:EEN65772.1, ECO:0000313|Proteomes:UP000001554} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN65772.1, RC ECO:0000313|Proteomes:UP000001554}; RC TISSUE=Testes {ECO:0000313|EMBL:EEN65772.1}; RX PubMed=18563158; DOI=10.1038/nature06967; RG US DOE Joint Genome Institute (JGI-PGF); RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U., RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K., RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., RA Gibson-Brown J.J., Grigoriev I.V., Horton A.C., de Jong P.J., RA Jurka J., Kapitonov V.V., Kohara Y., Kuroki Y., Lindquist E., RA Lucas S., Osoegawa K., Pennacchio L.A., Salamov A.A., Satou Y., RA Sauka-Spengler T., Schmutz J., Shin-I T., Toyoda A., RA Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H., RA Satoh N., Rokhsar D.S.; RT "The amphioxus genome and the evolution of the chordate karyotype."; RL Nature 453:1064-1071(2008). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG666480; EEN65772.1; -; Genomic_DNA. DR RefSeq; XP_002609762.1; XM_002609716.1. DR UniGene; Bfl.3232; -. DR STRING; 7739.JGI78594; -. DR GeneID; 7215524; -. DR KEGG; bfo:BRAFLDRAFT_78594; -. DR eggNOG; COG0646; -. DR InParanoid; C3Y1N2; -. DR KO; K00544; -. DR OMA; WGVTKGT; -. DR Proteomes; UP000001554; Partially assembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001554}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000001554}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 212 212 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 396 AA; 43893 MW; 8C5A6A618A46163D CRC64; MVNGEKKGVL ERLRDGVVVG DGGFVFALEK RGYVKAGPWT PEATVEHPEA VRQLHREFVR AGADVCQTFT FYASDDKLEN RGNTANKTHT GSKINQAACD LAKEVADEGG CLIAGGISQT PTYLSGKGKE AVQAEFRKQI QIFVANNVDF LLAEYYEHVE EVEWAIEVLK ETGKPVAANM CIGPEGDMHG VSAGECAVRM AKAGADIVGI NCHFDPFVCL EGMKKMKAAL DKADLHPYLM VQPLAYMTPD AGKQGFIDLP EFPFALEPRV CSRWEIMKFA REAYEIGIRY IGGCCGFEPY HIRAISEELS KERGGFMPEG CQKHDMWGQG LRLHTKPWVR ARARREYWEN MKPASGRPFC PSCSKPDNWG VTAGDDMLKQ KTEATTDEEI KQLAAK // ID C3Y467_BRAFL Unreviewed; 339 AA. AC C3Y467; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 04-MAR-2015, entry version 33. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EEN65093.1}; GN ORFNames=BRAFLDRAFT_91053 {ECO:0000313|EMBL:EEN65093.1}; OS Branchiostoma floridae (Florida lancelet) (Amphioxus). OC Eukaryota; Metazoa; Chordata; Cephalochordata; Branchiostomidae; OC Branchiostoma. OX NCBI_TaxID=7739 {ECO:0000313|Proteomes:UP000001554}; RN [1] {ECO:0000313|EMBL:EEN65093.1, ECO:0000313|Proteomes:UP000001554} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN65093.1, RC ECO:0000313|Proteomes:UP000001554}; RC TISSUE=Testes {ECO:0000313|EMBL:EEN65093.1}; RX PubMed=18563158; DOI=10.1038/nature06967; RG US DOE Joint Genome Institute (JGI-PGF); RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U., RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K., RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., RA Gibson-Brown J.J., Grigoriev I.V., Horton A.C., de Jong P.J., RA Jurka J., Kapitonov V.V., Kohara Y., Kuroki Y., Lindquist E., RA Lucas S., Osoegawa K., Pennacchio L.A., Salamov A.A., Satou Y., RA Sauka-Spengler T., Schmutz J., Shin-I T., Toyoda A., RA Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H., RA Satoh N., Rokhsar D.S.; RT "The amphioxus genome and the evolution of the chordate karyotype."; RL Nature 453:1064-1071(2008). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG666484; EEN65093.1; -; Genomic_DNA. DR RefSeq; XP_002609083.1; XM_002609037.1. DR STRING; 7739.JGI91053; -. DR GeneID; 7210505; -. DR KEGG; bfo:BRAFLDRAFT_91053; -. DR eggNOG; COG0646; -. DR InParanoid; C3Y467; -. DR KO; K00544; -. DR OMA; NICNTNC; -. DR Proteomes; UP000001554; Partially assembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001554}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000001554}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 212 212 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 339 AA; 37311 MW; F4AB6D00C4A20BAD CRC64; MATKPKGLLD RLKAGETVIC AEGYLFEFER RGYLKAGPFA PEVVVEHPEL VKGLHREFAH AGSDVVLAFT YYGHRETLRA VGREDELETF NRTALKLARE VADETGTLMA GNICNTNCYN ADDPQALDRC RQIFKEQTEW AVSEGADFMV AETFHVLGEA LLALECVKQY GNGLPAVVTF SVSRNGLWCG NTVEEAMTAL EEAGAAVVGL NCGRGPATML PLMDKVVNKV KVPFAALPVV YRTTEQQPTM HSLISHKGSK AFIVDMDEFL CGRSMVADFG QRCKDLGVQY VGLCCGNAPH FTRTLAETMG RTPPASKYSP DMTKHFTYGT DRWYGNKSL // ID C3Y7W3_BRAFL Unreviewed; 415 AA. AC C3Y7W3; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 04-MAR-2015, entry version 33. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EEN63618.1}; GN ORFNames=BRAFLDRAFT_119742 {ECO:0000313|EMBL:EEN63618.1}; OS Branchiostoma floridae (Florida lancelet) (Amphioxus). OC Eukaryota; Metazoa; Chordata; Cephalochordata; Branchiostomidae; OC Branchiostoma. OX NCBI_TaxID=7739 {ECO:0000313|Proteomes:UP000001554}; RN [1] {ECO:0000313|EMBL:EEN63618.1, ECO:0000313|Proteomes:UP000001554} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN63618.1, RC ECO:0000313|Proteomes:UP000001554}; RC TISSUE=Testes {ECO:0000313|EMBL:EEN63618.1}; RX PubMed=18563158; DOI=10.1038/nature06967; RG US DOE Joint Genome Institute (JGI-PGF); RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U., RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K., RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., RA Gibson-Brown J.J., Grigoriev I.V., Horton A.C., de Jong P.J., RA Jurka J., Kapitonov V.V., Kohara Y., Kuroki Y., Lindquist E., RA Lucas S., Osoegawa K., Pennacchio L.A., Salamov A.A., Satou Y., RA Sauka-Spengler T., Schmutz J., Shin-I T., Toyoda A., RA Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H., RA Satoh N., Rokhsar D.S.; RT "The amphioxus genome and the evolution of the chordate karyotype."; RL Nature 453:1064-1071(2008). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG666490; EEN63618.1; -; Genomic_DNA. DR RefSeq; XP_002607608.1; XM_002607562.1. DR UniGene; Bfl.25201; -. DR STRING; 7739.JGI119742; -. DR GeneID; 7224874; -. DR KEGG; bfo:BRAFLDRAFT_119742; -. DR eggNOG; COG0646; -. DR InParanoid; C3Y7W3; -. DR KO; K00544; -. DR OMA; WITKLAT; -. DR Proteomes; UP000001554; Partially assembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001554}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000001554}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 255 255 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 339 339 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 340 340 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 415 AA; 45627 MW; A61A1C85B710223F CRC64; MHFLSRFSKI ARSPCLLQNT PLFTASHGVR KFSRSATRNK DGGPGQQKKK GLLERLGEGP VVGDGSYVFT LERRGYVLAG PWTPEVVIEH PEAVKSLHRE YLHAGADVLQ ASTFYSSDDK LTMPGHEASR TITCKELNDK ACTILKEVAG DADVLLCGAM SPVPSYLDGK GKEVVQREYA KQMEAFIEHD LDFLLAEFLG HVEEAEWVIE LMKTKGKPVA CTLRTGPKGD CAGVAAGECA VRMAEAGADV VGVNCQYDPN TCLKTMEAMK TELDKRGLSP YLMVQPLGFH CPEVENEDEG YQMLPECPFA LEPRQLTRFE AHAFARAAYD LGVRYIGGCC GFEPHHIRAI SEELSPERGG KLGEASKKHV PWGGALKNSM LVPNRTKGSR QHWEKTKPAS GRPGYPDVQP KLINQ // ID C3YH00_BRAFL Unreviewed; 1318 AA. AC C3YH00; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 27-MAY-2015, entry version 45. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EEN60471.1}; GN ORFNames=BRAFLDRAFT_122283 {ECO:0000313|EMBL:EEN60471.1}; OS Branchiostoma floridae (Florida lancelet) (Amphioxus). OC Eukaryota; Metazoa; Chordata; Cephalochordata; Branchiostomidae; OC Branchiostoma. OX NCBI_TaxID=7739 {ECO:0000313|Proteomes:UP000001554}; RN [1] {ECO:0000313|EMBL:EEN60471.1, ECO:0000313|Proteomes:UP000001554} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN60471.1, RC ECO:0000313|Proteomes:UP000001554}; RC TISSUE=Testes {ECO:0000313|EMBL:EEN60471.1}; RX PubMed=18563158; DOI=10.1038/nature06967; RG US DOE Joint Genome Institute (JGI-PGF); RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U., RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K., RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., RA Gibson-Brown J.J., Grigoriev I.V., Horton A.C., de Jong P.J., RA Jurka J., Kapitonov V.V., Kohara Y., Kuroki Y., Lindquist E., RA Lucas S., Osoegawa K., Pennacchio L.A., Salamov A.A., Satou Y., RA Sauka-Spengler T., Schmutz J., Shin-I T., Toyoda A., RA Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H., RA Satoh N., Rokhsar D.S.; RT "The amphioxus genome and the evolution of the chordate karyotype."; RL Nature 453:1064-1071(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; GG666512; EEN60471.1; -; Genomic_DNA. DR RefSeq; XP_002604460.1; XM_002604414.1. DR STRING; 7739.JGI122283; -. DR GeneID; 7217996; -. DR KEGG; bfo:BRAFLDRAFT_122283; -. DR eggNOG; COG1410; -. DR InParanoid; C3YH00; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR Proteomes; UP000001554; Partially assembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 2. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 2. DR Pfam; PF02574; S-methyl_trans; 2. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 2. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001554}; KW Reference proteome {ECO:0000313|Proteomes:UP000001554}. SQ SEQUENCE 1318 AA; 146190 MW; 1BCA5723F1FE1CFE CRC64; MPPASDSGVS CWSEYRDPEV AAKIAATLRE RIMILDGGMG TMIQGYHLEE DGYRGDEFKD WHKLLKGNND LLSLTQPNIV YDIHKAYLEA GADFAETNTF SGTRIAQADY GMEELVYRLN KVSAELAKKA ADKVTADTAW DELVDAYAEQ ARGLLDGGCD VLMVETIFDT ANSKAALFAL SQLFEEEYKP VPIFVSGTIV DRSGRTLSGQ TSEAFVISVS QAEPMCLGLN CALGATEMRP FIEAIGKNTT SYVLCYPNAG LPNALGGYDE TPEIMAEHLR VFAKDGLLNL VGGCCGTTPA HIKAIAEAVR PFRPRKVPSV LHEGHMLLSG LEPMYVGPHT LFVNIGERCN VAGSRAFNKM IQRGDYEKAL SVAKHQKALS MAKHQVEMGA PFRTQKALSV AKLQVEMGAQ VLDINMDEGM LDGKAAMARF LNLIATEPEI CKVPLCTDSS NFSVIEAGLK CAQGKCIVNS IRPLFLYIYS LLFSPPPQVP LCIDSSNFSV IEAGLKCAQG KCIVNSISLK EGEEDFLRKA RTIRRYGAAV VVMAFDETGQ ATDVEHKVQI CTRSYRLLVD KVGFNPCDII FDPNILTIAT GMEEHNEYAI NFIEATKIIK KTLPGCRVSG GLSNLSFSFR GMERIREAMH SVFLYHAIKA GMDMGIVNAG NLPLYDDISE ELLKLCEDLI WNKDPEATEK MLAYAQVHGK GAKKEQESEE WRSRTVEERL EHSLVKGIDK YVVEDTEEAR ANMELYPRPL NVIEGPLMKG MSIVGDLFGA GKMFLPQVIK SARVMKKAVA YLIPYMEEEK AQMKEQMMAE GTWDENAKYA GTIVLATVKG DVHDIGKNIV GVVLGCNNYR VIDLGVMTPC EKILKTAVEE NADIVGLSGL ITPSLDEMIF VAKEMQRVGL KLPLLIGGAT TSKTHTAVKI APRYKEPVIH VLDASKSVVV CSALMDEDQK EDLTEDVAEE YEEIREEHYD SLKDRKYLPI EKARTKKLEV DWASYEAVRP SFTGTMVFDD YDLGRLVDYI DWKPFFDVWQ LRGKYPNRGY PKIFKDKTVG EEARKVFDEA QAMLKKIMEE KLLTARGLLG FWPACSVGDD VQVFQEDSMP REGIPLATFY GLRQQAEKEP GVTDPYLCLS DCVAPKEAGV RDYCGLFAVS VFGAEDMCQK FKAEFDDYNI IMVKALADRL AEAFAEELHE RVRREFWGYS PEEHLDTSDL HRVRYEGIRP APGYPSQPDH TEKLTMWELA DIQNATGIVL TESLAMDPAA SVSGLYFAHP KAVYFAVGKI GKDQFEGLLS GMSSKFCRLF VSEAVVGVGT SVLQVRDN // ID C3YKD9_BRAFL Unreviewed; 376 AA. AC C3YKD9; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 04-MAR-2015, entry version 33. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EEN59300.1}; GN ORFNames=BRAFLDRAFT_60534 {ECO:0000313|EMBL:EEN59300.1}; OS Branchiostoma floridae (Florida lancelet) (Amphioxus). OC Eukaryota; Metazoa; Chordata; Cephalochordata; Branchiostomidae; OC Branchiostoma. OX NCBI_TaxID=7739 {ECO:0000313|Proteomes:UP000001554}; RN [1] {ECO:0000313|EMBL:EEN59300.1, ECO:0000313|Proteomes:UP000001554} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN59300.1, RC ECO:0000313|Proteomes:UP000001554}; RC TISSUE=Testes {ECO:0000313|EMBL:EEN59300.1}; RX PubMed=18563158; DOI=10.1038/nature06967; RG US DOE Joint Genome Institute (JGI-PGF); RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U., RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K., RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., RA Gibson-Brown J.J., Grigoriev I.V., Horton A.C., de Jong P.J., RA Jurka J., Kapitonov V.V., Kohara Y., Kuroki Y., Lindquist E., RA Lucas S., Osoegawa K., Pennacchio L.A., Salamov A.A., Satou Y., RA Sauka-Spengler T., Schmutz J., Shin-I T., Toyoda A., RA Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H., RA Satoh N., Rokhsar D.S.; RT "The amphioxus genome and the evolution of the chordate karyotype."; RL Nature 453:1064-1071(2008). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG666521; EEN59300.1; -; Genomic_DNA. DR RefSeq; XP_002603289.1; XM_002603243.1. DR STRING; 7739.JGI60534; -. DR GeneID; 7241294; -. DR KEGG; bfo:BRAFLDRAFT_60534; -. DR eggNOG; COG0646; -. DR InParanoid; C3YKD9; -. DR KO; K00544; -. DR Proteomes; UP000001554; Partially assembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001554}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000001554}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 214 214 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 298 298 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 376 AA; 41196 MW; 315E839A96792F0F CRC64; MVKKGLLERL QEGPVIGDGG YVFTLEKRGY VMAGPYTTEV VIEHPEAVKQ LHREFMRAGA DVLQAFTFWS TDDRLSLSGP DAPGNETGKS ITCKEMNDQA CTIVKEVVGD GDTLVCGGLS NTPSYAQGKG RAAVQKEFSK QVDSFMEQDV DFLLAEFIGN VEEAEWAIEV LKGKGKPVAC TLRIGPTGDD SGVPVGECAV RMAKAGADVV GLNCRFDANT CLKTIKMMKD ALEKAGLSPY LMVQPNGYHS PETEQTKNGW TILPEFPFAL GPRQMTRFEV HHFARAAFDL GVRYIGGCCG FEPHHIRAIS EELSPERGGK LGDASKKHLP WGGALKTDQS EKDFINGKDT REYWESVKPA LGRPGFPDVQ EKLFRQ // ID C3YKZ2_BRAFL Unreviewed; 369 AA. AC C3YKZ2; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 04-MAR-2015, entry version 35. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EEN58983.1}; GN ORFNames=BRAFLDRAFT_248283 {ECO:0000313|EMBL:EEN58983.1}; OS Branchiostoma floridae (Florida lancelet) (Amphioxus). OC Eukaryota; Metazoa; Chordata; Cephalochordata; Branchiostomidae; OC Branchiostoma. OX NCBI_TaxID=7739 {ECO:0000313|Proteomes:UP000001554}; RN [1] {ECO:0000313|EMBL:EEN58983.1, ECO:0000313|Proteomes:UP000001554} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN58983.1, RC ECO:0000313|Proteomes:UP000001554}; RC TISSUE=Testes {ECO:0000313|EMBL:EEN58983.1}; RX PubMed=18563158; DOI=10.1038/nature06967; RG US DOE Joint Genome Institute (JGI-PGF); RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U., RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K., RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., RA Gibson-Brown J.J., Grigoriev I.V., Horton A.C., de Jong P.J., RA Jurka J., Kapitonov V.V., Kohara Y., Kuroki Y., Lindquist E., RA Lucas S., Osoegawa K., Pennacchio L.A., Salamov A.A., Satou Y., RA Sauka-Spengler T., Schmutz J., Shin-I T., Toyoda A., RA Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H., RA Satoh N., Rokhsar D.S.; RT "The amphioxus genome and the evolution of the chordate karyotype."; RL Nature 453:1064-1071(2008). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG666525; EEN58983.1; -; Genomic_DNA. DR RefSeq; XP_002602971.1; XM_002602925.1. DR STRING; 7739.JGI248283; -. DR GeneID; 7223121; -. DR KEGG; bfo:BRAFLDRAFT_248283; -. DR eggNOG; COG0646; -. DR InParanoid; C3YKZ2; -. DR KO; K00544; -. DR OMA; VEECEWA; -. DR Proteomes; UP000001554; Partially assembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001554}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000001554}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 211 211 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 296 296 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 369 AA; 40797 MW; 10D706C99A044B41 CRC64; MGKKGLLERL AEGPVIGDGS YVFTLEKRGY VKGGPWTPEA VIEHPEGVKQ LHREFMRAGA DVLQAFTFYS TDDKLHLAGN LAGESVTCHD QNEAACKIVQ EVAAEGKDVL ICGGCSPTPS YMEKKGKEVV QQEFKKQVDV FAHREEVDFL LCEFMGHVEE CEWAIEAMKA AGKPVACTMR IGPKGDQNGV PTGECAVRMA KAGADVVGIN CLYDVNTSLK TIEMMKTALD KAGLSPYLMI QPLGYHCPEV ENMLEGYFHL PEAPFALEPR LLTRFDVQKF ARAAYELGVR YLGGCCGFEP YHIRALAEEL APERGRLPDA SAKHEPWGGA LKGSMFAFMR KRAGREHWEN IKPTLGRPDH PVLQDHLDE // ID C3YN41_BRAFL Unreviewed; 364 AA. AC C3YN41; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 04-MAR-2015, entry version 34. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EEN58147.1}; DE Flags: Fragment; GN ORFNames=BRAFLDRAFT_234263 {ECO:0000313|EMBL:EEN58147.1}; OS Branchiostoma floridae (Florida lancelet) (Amphioxus). OC Eukaryota; Metazoa; Chordata; Cephalochordata; Branchiostomidae; OC Branchiostoma. OX NCBI_TaxID=7739 {ECO:0000313|Proteomes:UP000001554}; RN [1] {ECO:0000313|EMBL:EEN58147.1, ECO:0000313|Proteomes:UP000001554} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN58147.1, RC ECO:0000313|Proteomes:UP000001554}; RC TISSUE=Testes {ECO:0000313|EMBL:EEN58147.1}; RX PubMed=18563158; DOI=10.1038/nature06967; RG US DOE Joint Genome Institute (JGI-PGF); RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U., RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K., RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., RA Gibson-Brown J.J., Grigoriev I.V., Horton A.C., de Jong P.J., RA Jurka J., Kapitonov V.V., Kohara Y., Kuroki Y., Lindquist E., RA Lucas S., Osoegawa K., Pennacchio L.A., Salamov A.A., Satou Y., RA Sauka-Spengler T., Schmutz J., Shin-I T., Toyoda A., RA Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H., RA Satoh N., Rokhsar D.S.; RT "The amphioxus genome and the evolution of the chordate karyotype."; RL Nature 453:1064-1071(2008). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG666533; EEN58147.1; -; Genomic_DNA. DR RefSeq; XP_002602135.1; XM_002602089.1. DR STRING; 7739.JGI234263; -. DR GeneID; 7255113; -. DR KEGG; bfo:BRAFLDRAFT_234263; -. DR eggNOG; COG0646; -. DR InParanoid; C3YN41; -. DR KO; K00544; -. DR Proteomes; UP000001554; Partially assembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001554}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000001554}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 205 205 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT NON_TER 1 1 {ECO:0000313|EMBL:EEN58147.1}. SQ SEQUENCE 364 AA; 40187 MW; D2C4D8CE2026236B CRC64; KKGLLQRLRE GPVIGDCSYV FTLEKRTYVK AGPWTPEVVV EHPDAVKQLH KEYIRAGADV VQALTFYSTD DKLNLPGHEA GRTITCKDLN RQACTIAEEV VGESDVLICG ALSPTPSYTE GKGKEAVQRE FSKQVEAFVE HDVDFLLAEV SHMGHDTLLQ RVQINSFPST STLNTSHFRD NSGVPPGECA VRMARAGADV IGVNCKFDPT TCLKTVRMMK EALDQEGLSP FLMVQPVGFH CPEVEMEHDG YAMLPENPFA LEPRQLTRFD VHKFARAAYE LGVRYIGGCC GFEPHHIRAI SEELSAERGG RLGEGSKKHV PWGGALTSSV LGTNRVKASR DHWERVQPAS GRPGHPNLQP KLMD // ID C3YN42_BRAFL Unreviewed; 369 AA. AC C3YN42; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 04-MAR-2015, entry version 32. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EEN58148.1}; GN ORFNames=BRAFLDRAFT_268352 {ECO:0000313|EMBL:EEN58148.1}; OS Branchiostoma floridae (Florida lancelet) (Amphioxus). OC Eukaryota; Metazoa; Chordata; Cephalochordata; Branchiostomidae; OC Branchiostoma. OX NCBI_TaxID=7739 {ECO:0000313|Proteomes:UP000001554}; RN [1] {ECO:0000313|EMBL:EEN58148.1, ECO:0000313|Proteomes:UP000001554} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN58148.1, RC ECO:0000313|Proteomes:UP000001554}; RC TISSUE=Testes {ECO:0000313|EMBL:EEN58148.1}; RX PubMed=18563158; DOI=10.1038/nature06967; RG US DOE Joint Genome Institute (JGI-PGF); RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U., RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K., RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., RA Gibson-Brown J.J., Grigoriev I.V., Horton A.C., de Jong P.J., RA Jurka J., Kapitonov V.V., Kohara Y., Kuroki Y., Lindquist E., RA Lucas S., Osoegawa K., Pennacchio L.A., Salamov A.A., Satou Y., RA Sauka-Spengler T., Schmutz J., Shin-I T., Toyoda A., RA Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H., RA Satoh N., Rokhsar D.S.; RT "The amphioxus genome and the evolution of the chordate karyotype."; RL Nature 453:1064-1071(2008). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG666533; EEN58148.1; -; Genomic_DNA. DR RefSeq; XP_002602136.1; XM_002602090.1. DR STRING; 7739.JGI268352; -. DR GeneID; 7250827; -. DR KEGG; bfo:BRAFLDRAFT_268352; -. DR eggNOG; COG0646; -. DR InParanoid; C3YN42; -. DR KO; K00544; -. DR OMA; CKELNER; -. DR Proteomes; UP000001554; Partially assembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001554}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000001554}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 209 209 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 369 AA; 40598 MW; D97E1794C81AC900 CRC64; MVKKGLLERL AEGPVVGDGS YVFTMEKRGY VMAGQWTPEV VIEHPEAVKQ LHREYLRAGA DILQAYTFFA SDDKLNLPGH AAGKITTCKE LNERAIDIVR EVAGDADVLI SGGVTMTPSY KQGKGKEAVQ AEYRKHAEVF IEKDVDFLLA EFINQIEEAE WAIKVLKSTG KPVACTMCIG PTGDFVDVPA GECAVRMAKA GADVVGLNCQ FDPNSGLKTM KLMKEALEKE GLSPFLMMQP LGFFCPEVEN EHPGYAMLPE CPFALEPRLL TRFDANRYAR AAYELGVRYI GGCCGFEPHH IRAISEELSP ERGGKLGEAS SKHIPWGEAL KTSTFLQNRM KATQEHWKTV KPASGRPGHP ALQPKLMGQ // ID C3YXS3_BRAFL Unreviewed; 891 AA. AC C3YXS3; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 07-JAN-2015, entry version 27. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EEN54882.1}; GN ORFNames=BRAFLDRAFT_125746 {ECO:0000313|EMBL:EEN54882.1}; OS Branchiostoma floridae (Florida lancelet) (Amphioxus). OC Eukaryota; Metazoa; Chordata; Cephalochordata; Branchiostomidae; OC Branchiostoma. OX NCBI_TaxID=7739 {ECO:0000313|Proteomes:UP000001554}; RN [1] {ECO:0000313|EMBL:EEN54882.1, ECO:0000313|Proteomes:UP000001554} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN54882.1, RC ECO:0000313|Proteomes:UP000001554}; RC TISSUE=Testes {ECO:0000313|EMBL:EEN54882.1}; RX PubMed=18563158; DOI=10.1038/nature06967; RG US DOE Joint Genome Institute (JGI-PGF); RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U., RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K., RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., RA Gibson-Brown J.J., Grigoriev I.V., Horton A.C., de Jong P.J., RA Jurka J., Kapitonov V.V., Kohara Y., Kuroki Y., Lindquist E., RA Lucas S., Osoegawa K., Pennacchio L.A., Salamov A.A., Satou Y., RA Sauka-Spengler T., Schmutz J., Shin-I T., Toyoda A., RA Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H., RA Satoh N., Rokhsar D.S.; RT "The amphioxus genome and the evolution of the chordate karyotype."; RL Nature 453:1064-1071(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; GG666563; EEN54882.1; -; Genomic_DNA. DR RefSeq; XP_002598870.1; XM_002598824.1. DR UniGene; Bfl.5785; -. DR STRING; 7739.JGI125746; -. DR GeneID; 7207645; -. DR KEGG; bfo:BRAFLDRAFT_125746; -. DR eggNOG; COG0646; -. DR Proteomes; UP000001554; Partially assembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008373; F:sialyltransferase activity; IEA:InterPro. DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR001675; Glyco_trans_29. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF00777; Glyco_transf_29; 2. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001554}; KW Reference proteome {ECO:0000313|Proteomes:UP000001554}. SQ SEQUENCE 891 AA; 101150 MW; 2E5D252F068DCE8C CRC64; MNIRRLIWFQ TAVPKARVPN RVVFNHPHHK IAAEKFWTDR GLDEKSFSSG FYMISSAFSF CEKITVYGFW PFNMDRNGKP LSYHYSQTGP KDGGVNNTWH RMDREFVKLV ELYKAGIIKL VTSPLESNDA MTAAPRTPVV PSKVQRNLLR EKPEDPAVST PAAVLPTDSR VFPKNNIRQG TSVESNNTKI PDPPMESEVV KTVVTYKMRG DKIIRIIKKY VRKRPKPPPA VDSNGQLNFD KPESKNNSDT RTSGSVAEDK NKTSNSEKRI DSPVVDSAIN NMLSSKVPAH VPKEANSDGQ SLLNNAQDGV NLDQTENTGD KKTEEDLKKT NEELRPNAEG NVPNANDKSD DSKDDHEEAA DPCKPKDEDY ERDITTIVTY AKKGTKTIKI IKKIIRKRLK PKRIWEEINN GTENNLPEYE QYDQEQIQDQ IDFKIENRCN TKRGFTQRFQ EEVAEIEEEM EVGSVNNRTS PRAHKRMTKK DLATKYILPD VLKFVTGNTS SWTFDYKALA QKRFDLERTC NARNHFFVTK KNIPLGSSLR YDVSNTTVKV NNTLFDTFPT AIPFADKMFP RCAVVGSSGI LMDSGCGREI DSSDFVIRFN MAPVGGRFRA DVGSKVDIVT VNGDSIKSRY DKLETNISRT MFAAYVRQYN RNTLLWSVPF TSLTHTAYVL RTYQVLKKAG APQAVVFANP GYMACTNTYW RQRGFTRAPR LSTGMFLTSA ALQFCEEVYL YGFWPFPVDT AGNVLPYHYY SKESSKGRSS TRKLCFSSTR SDYKMATTKP KGLLERLSND ETVIVAEGYL FEFERRGYLQ AGSYVPEVVL DHPEMVTSLH REFVHAGSDV VLAFTYYGHR EKMRLIGKEQ LLEPMNRNAL RLAREVADET GTLMAGNICN H // ID C3YXS5_BRAFL Unreviewed; 217 AA. AC C3YXS5; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 27-MAY-2015, entry version 30. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EEN54884.1}; GN ORFNames=BRAFLDRAFT_90102 {ECO:0000313|EMBL:EEN54884.1}; OS Branchiostoma floridae (Florida lancelet) (Amphioxus). OC Eukaryota; Metazoa; Chordata; Cephalochordata; Branchiostomidae; OC Branchiostoma. OX NCBI_TaxID=7739 {ECO:0000313|Proteomes:UP000001554}; RN [1] {ECO:0000313|EMBL:EEN54884.1, ECO:0000313|Proteomes:UP000001554} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN54884.1, RC ECO:0000313|Proteomes:UP000001554}; RC TISSUE=Testes {ECO:0000313|EMBL:EEN54884.1}; RX PubMed=18563158; DOI=10.1038/nature06967; RG US DOE Joint Genome Institute (JGI-PGF); RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U., RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K., RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., RA Gibson-Brown J.J., Grigoriev I.V., Horton A.C., de Jong P.J., RA Jurka J., Kapitonov V.V., Kohara Y., Kuroki Y., Lindquist E., RA Lucas S., Osoegawa K., Pennacchio L.A., Salamov A.A., Satou Y., RA Sauka-Spengler T., Schmutz J., Shin-I T., Toyoda A., RA Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H., RA Satoh N., Rokhsar D.S.; RT "The amphioxus genome and the evolution of the chordate karyotype."; RL Nature 453:1064-1071(2008). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG666563; EEN54884.1; -; Genomic_DNA. DR RefSeq; XP_002598872.1; XM_002598826.1. DR STRING; 7739.JGI90102; -. DR GeneID; 7206339; -. DR KEGG; bfo:BRAFLDRAFT_90102; -. DR eggNOG; COG0646; -. DR InParanoid; C3YXS5; -. DR KO; K00544; -. DR Proteomes; UP000001554; Partially assembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001554}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000001554}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 83 83 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 165 165 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 166 166 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 217 AA; 23703 MW; EAABA559BADFB616 CRC64; MVAAEQIEWA VEEGADFIVG ETFGFLGEAM LALECIKEYG KGLPAVITMV IHRDADHVAD GPTLVEAMQA LEQAGAAVVG FNCCRGPFTT LPLVEKVKGH VKVPIAVNPV LYRTDEEYPT MQSLKNHKGV RAFPVDLDAF LCSRSMIAEF GQRCRQLGLQ YVGLCCGNAS HFTRTLAESL GRTPPASKYS PDMSQHFAYG TDKKLHSLNT EKVVKLL // ID C3YXS7_BRAFL Unreviewed; 138 AA. AC C3YXS7; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 07-JAN-2015, entry version 26. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EEN54886.1}; GN ORFNames=BRAFLDRAFT_90100 {ECO:0000313|EMBL:EEN54886.1}; OS Branchiostoma floridae (Florida lancelet) (Amphioxus). OC Eukaryota; Metazoa; Chordata; Cephalochordata; Branchiostomidae; OC Branchiostoma. OX NCBI_TaxID=7739 {ECO:0000313|Proteomes:UP000001554}; RN [1] {ECO:0000313|EMBL:EEN54886.1, ECO:0000313|Proteomes:UP000001554} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN54886.1, RC ECO:0000313|Proteomes:UP000001554}; RC TISSUE=Testes {ECO:0000313|EMBL:EEN54886.1}; RX PubMed=18563158; DOI=10.1038/nature06967; RG US DOE Joint Genome Institute (JGI-PGF); RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U., RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K., RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., RA Gibson-Brown J.J., Grigoriev I.V., Horton A.C., de Jong P.J., RA Jurka J., Kapitonov V.V., Kohara Y., Kuroki Y., Lindquist E., RA Lucas S., Osoegawa K., Pennacchio L.A., Salamov A.A., Satou Y., RA Sauka-Spengler T., Schmutz J., Shin-I T., Toyoda A., RA Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H., RA Satoh N., Rokhsar D.S.; RT "The amphioxus genome and the evolution of the chordate karyotype."; RL Nature 453:1064-1071(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; GG666563; EEN54886.1; -; Genomic_DNA. DR RefSeq; XP_002598874.1; XM_002598828.1. DR STRING; 7739.JGI90100; -. DR GeneID; 7209182; -. DR KEGG; bfo:BRAFLDRAFT_90100; -. DR eggNOG; NOG307579; -. DR InParanoid; C3YXS7; -. DR KO; K00544; -. DR OMA; PETHEQT; -. DR Proteomes; UP000001554; Partially assembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001554}; KW Reference proteome {ECO:0000313|Proteomes:UP000001554}. SQ SEQUENCE 138 AA; 15568 MW; 3F7DABBEBEC009E6 CRC64; MAAKPRGLLE RLNAGETIIV AEGYLFEFER RGYLKAGAFV PEVVVEHPEL VKGLYREFVH AGSDVVLAFT YYGHREKLRV IGREADLEPM NRTALRLARE VADETGTLMA GNISNTTCYD PDKPETHEQT RQIFKVLS // ID C3YXS9_BRAFL Unreviewed; 399 AA. AC C3YXS9; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 04-MAR-2015, entry version 32. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EEN54888.1}; GN ORFNames=BRAFLDRAFT_90098 {ECO:0000313|EMBL:EEN54888.1}; OS Branchiostoma floridae (Florida lancelet) (Amphioxus). OC Eukaryota; Metazoa; Chordata; Cephalochordata; Branchiostomidae; OC Branchiostoma. OX NCBI_TaxID=7739 {ECO:0000313|Proteomes:UP000001554}; RN [1] {ECO:0000313|EMBL:EEN54888.1, ECO:0000313|Proteomes:UP000001554} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN54888.1, RC ECO:0000313|Proteomes:UP000001554}; RC TISSUE=Testes {ECO:0000313|EMBL:EEN54888.1}; RX PubMed=18563158; DOI=10.1038/nature06967; RG US DOE Joint Genome Institute (JGI-PGF); RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U., RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K., RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., RA Gibson-Brown J.J., Grigoriev I.V., Horton A.C., de Jong P.J., RA Jurka J., Kapitonov V.V., Kohara Y., Kuroki Y., Lindquist E., RA Lucas S., Osoegawa K., Pennacchio L.A., Salamov A.A., Satou Y., RA Sauka-Spengler T., Schmutz J., Shin-I T., Toyoda A., RA Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H., RA Satoh N., Rokhsar D.S.; RT "The amphioxus genome and the evolution of the chordate karyotype."; RL Nature 453:1064-1071(2008). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG666563; EEN54888.1; -; Genomic_DNA. DR RefSeq; XP_002598876.1; XM_002598830.1. DR STRING; 7739.JGI90098; -. DR GeneID; 7207640; -. DR KEGG; bfo:BRAFLDRAFT_90098; -. DR eggNOG; COG0646; -. DR InParanoid; C3YXS9; -. DR KO; K00544; -. DR OMA; REECITI; -. DR Proteomes; UP000001554; Partially assembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001554}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000001554}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 214 214 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 296 296 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 297 297 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 399 AA; 44071 MW; 093501A7D00063D1 CRC64; MPPKPKGLLE RLKAGETVIV AEGYLFEFER RGYLKAGAFV PEVVVEHPEL VKGLYREFVH AGSDVVLAFT YYGHREKLRV IGREADLEPM NRTALRLARE VADETGTLMA GNICNTTVFD PNVPSTREEC ITIFKEQIEW AVEEGADFIV AETYGMVAEA KLALECINKY GKGLPAVVCM TFHKDADRSV DGLSLLDSMR ALEEAGAAVV GLNCGRGPFT MLPLMERIKD KIKVPVAALP VPFRCDELRP TMQSLVNHKG ERAFPVDLDA FLCSRSMIAE FGQRCRQLGL QYVGLCCGNA SHFTRTLAES LGRTPPASKY SPDMSQHFAY GTDKKLHSLN TEKTIHNGLQ LQFSQRVHQD FYRGGVSFLR KPVVQHAAAA TLGIPLSPLN VVNVGLLKS // ID C3ZEE1_BRAFL Unreviewed; 315 AA. AC C3ZEE1; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 07-JAN-2015, entry version 31. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EEN49097.1}; GN ORFNames=BRAFLDRAFT_114091 {ECO:0000313|EMBL:EEN49097.1}; OS Branchiostoma floridae (Florida lancelet) (Amphioxus). OC Eukaryota; Metazoa; Chordata; Cephalochordata; Branchiostomidae; OC Branchiostoma. OX NCBI_TaxID=7739 {ECO:0000313|Proteomes:UP000001554}; RN [1] {ECO:0000313|EMBL:EEN49097.1, ECO:0000313|Proteomes:UP000001554} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN49097.1, RC ECO:0000313|Proteomes:UP000001554}; RC TISSUE=Testes {ECO:0000313|EMBL:EEN49097.1}; RX PubMed=18563158; DOI=10.1038/nature06967; RG US DOE Joint Genome Institute (JGI-PGF); RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U., RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K., RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., RA Gibson-Brown J.J., Grigoriev I.V., Horton A.C., de Jong P.J., RA Jurka J., Kapitonov V.V., Kohara Y., Kuroki Y., Lindquist E., RA Lucas S., Osoegawa K., Pennacchio L.A., Salamov A.A., Satou Y., RA Sauka-Spengler T., Schmutz J., Shin-I T., Toyoda A., RA Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H., RA Satoh N., Rokhsar D.S.; RT "The amphioxus genome and the evolution of the chordate karyotype."; RL Nature 453:1064-1071(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; GG666612; EEN49097.1; -; Genomic_DNA. DR RefSeq; XP_002593086.1; XM_002593040.1. DR STRING; 7739.JGI114091; -. DR GeneID; 7227867; -. DR KEGG; bfo:BRAFLDRAFT_114091; -. DR eggNOG; COG2040; -. DR InParanoid; C3ZEE1; -. DR KO; K00547; -. DR OMA; SEWCKDG; -. DR Proteomes; UP000001554; Partially assembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001554}; KW Reference proteome {ECO:0000313|Proteomes:UP000001554}. SQ SEQUENCE 315 AA; 34461 MW; 0C4D54B803F87A5B CRC64; METKVLDGGL ATELDFAGFD INNDPLWSAR LLATNPAAIK QVHKSFLSAG SDVIITATYQ ASVPGFQEYL GVSVEEAHKL MDHGVRIAKQ ACLEFCKEQD KGDFPGRRNP LAAGSVGPYG ACLHDASEYT GEYVDSMSIE ELQRWHRPRL GQLITSGADM VAIETIPAVK EAAALVQLLR EFPNTRAWVT FSCKDGLHTC HGESFPEAIA AVLKSPQVFA AGANCCMPEH VAPLLQKARE LCKDPAKFFI AYPNSGEKWA AGTGWHGKAD CRPLSTFVPE WLDHGARWIG GCCRTRPDDI KDIRSSIEQW KKTTG // ID C3ZH79_BRAFL Unreviewed; 414 AA. AC C3ZH79; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 04-MAR-2015, entry version 34. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EEN48226.1}; GN ORFNames=BRAFLDRAFT_123950 {ECO:0000313|EMBL:EEN48226.1}; OS Branchiostoma floridae (Florida lancelet) (Amphioxus). OC Eukaryota; Metazoa; Chordata; Cephalochordata; Branchiostomidae; OC Branchiostoma. OX NCBI_TaxID=7739 {ECO:0000313|Proteomes:UP000001554}; RN [1] {ECO:0000313|EMBL:EEN48226.1, ECO:0000313|Proteomes:UP000001554} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN48226.1, RC ECO:0000313|Proteomes:UP000001554}; RC TISSUE=Testes {ECO:0000313|EMBL:EEN48226.1}; RX PubMed=18563158; DOI=10.1038/nature06967; RG US DOE Joint Genome Institute (JGI-PGF); RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U., RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K., RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., RA Gibson-Brown J.J., Grigoriev I.V., Horton A.C., de Jong P.J., RA Jurka J., Kapitonov V.V., Kohara Y., Kuroki Y., Lindquist E., RA Lucas S., Osoegawa K., Pennacchio L.A., Salamov A.A., Satou Y., RA Sauka-Spengler T., Schmutz J., Shin-I T., Toyoda A., RA Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H., RA Satoh N., Rokhsar D.S.; RT "The amphioxus genome and the evolution of the chordate karyotype."; RL Nature 453:1064-1071(2008). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG666621; EEN48226.1; -; Genomic_DNA. DR RefSeq; XP_002592215.1; XM_002592169.1. DR UniGene; Bfl.13177; -. DR STRING; 7739.JGI123950; -. DR GeneID; 7242531; -. DR KEGG; bfo:BRAFLDRAFT_123950; -. DR eggNOG; NOG330803; -. DR InParanoid; C3ZH79; -. DR KO; K00544; -. DR Proteomes; UP000001554; Partially assembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001554}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000001554}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 254 254 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 338 338 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 339 339 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 414 AA; 45469 MW; A808485CFA43D1EB CRC64; MSFLSRVSKV ARSQCLLQNT PVLTVSHGVR KFSRSATRQD GGHGQQQKKG LLERLSEGPV VGDGSYVFTL ERRGYVLAGP WTPEVVIEHP EAVKSLHREY LHAGADVLQA STFYSSDDKL TMPGHEAGRT ITCKELNDKA CTILKEVAGD ADVLLCGAMS PVPSYLDGKG KEVVQREYAK QMEAFIEHDL DFLLAEFLGH VEEAEWVIEL MKTKGKPVAC TLRTGPKGDC AGIPAGECAV RMADAGADVV GVNCQYDPNT CLKTLEAMKT ELDKRGLSPY LMVQPLGFHC PEVENEDEGY QMLPECPFAL EPRHLTRFEA HAFARAAYDL GVRYIGGCCG FEPHHIRAIS EELSPERGGK LGEASKKHVP WGGALKNSML VPNRTKGSRQ HWEKTKPASG RPGYPDVQPK LINQ // ID C3ZZV0_BRAFL Unreviewed; 359 AA. AC C3ZZV0; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 04-MAR-2015, entry version 32. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EEN41931.1}; GN ORFNames=BRAFLDRAFT_90330 {ECO:0000313|EMBL:EEN41931.1}; OS Branchiostoma floridae (Florida lancelet) (Amphioxus). OC Eukaryota; Metazoa; Chordata; Cephalochordata; Branchiostomidae; OC Branchiostoma. OX NCBI_TaxID=7739 {ECO:0000313|Proteomes:UP000001554}; RN [1] {ECO:0000313|EMBL:EEN41931.1, ECO:0000313|Proteomes:UP000001554} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN41931.1, RC ECO:0000313|Proteomes:UP000001554}; RC TISSUE=Testes {ECO:0000313|EMBL:EEN41931.1}; RX PubMed=18563158; DOI=10.1038/nature06967; RG US DOE Joint Genome Institute (JGI-PGF); RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U., RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K., RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., RA Gibson-Brown J.J., Grigoriev I.V., Horton A.C., de Jong P.J., RA Jurka J., Kapitonov V.V., Kohara Y., Kuroki Y., Lindquist E., RA Lucas S., Osoegawa K., Pennacchio L.A., Salamov A.A., Satou Y., RA Sauka-Spengler T., Schmutz J., Shin-I T., Toyoda A., RA Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H., RA Satoh N., Rokhsar D.S.; RT "The amphioxus genome and the evolution of the chordate karyotype."; RL Nature 453:1064-1071(2008). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG666768; EEN41931.1; -; Genomic_DNA. DR RefSeq; XP_002585920.1; XM_002585874.1. DR STRING; 7739.JGI90330; -. DR GeneID; 7213742; -. DR KEGG; bfo:BRAFLDRAFT_90330; -. DR eggNOG; COG0646; -. DR InParanoid; C3ZZV0; -. DR KO; K00544; -. DR Proteomes; UP000001554; Partially assembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001554}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000001554}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 197 197 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 281 281 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 282 282 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 359 AA; 39111 MW; CCBB9A78E5994853 CRC64; MVKKGLLERL QEGPVIGDGG YVFTLEKRGY VMAGPYTTEV VIEHPEAGGY TGSSCAQAQM CARPSHSGRQ TTDFSCKEMN DQACTIVKEV VGDGDTLVCG GLSNTPSYAQ GKGKAAVQME FSKQVDSFME QDVDFLLAEF IGNVEEAEWA IEVLKGKGKP VACTLRIGPT GDDSGVPAGE CAVRMAKAGA DVVGLNCRFD ANTCLKTIKM MKDALEKAGL SPYLMVQPNG YHSPETEQTK NGWTILPEFP FALGPRQMTR FEVHHFARAA FDLGVRYIGG CCGFEPHHIR AISEEVVTER GGRLGEASKK HLPWGGALKT DQSEKDFING KDTREFWESV KPALGRPGFP DVQEKLFRQ // ID C4AXS9_BURML Unreviewed; 359 AA. AC C4AXS9; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEP85294.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEP85294.1}; GN ORFNames=BMAGB8_0081 {ECO:0000313|EMBL:EEP85294.1}; OS Burkholderia mallei GB8 horse 4. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=320390 {ECO:0000313|EMBL:EEP85294.1, ECO:0000313|Proteomes:UP000003995}; RN [1] {ECO:0000313|EMBL:EEP85294.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=GB8 horse 4 {ECO:0000313|EMBL:EEP85294.1}; 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. {ECO:0000313|EMBL:EEP85294.1}. 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; AAHO01000041; EEP85294.1; -; Genomic_DNA. DR RefSeq; WP_004197742.1; NZ_AAHO01000041.1. DR EnsemblBacteria; EEP85294; EEP85294; BMAGB8_0081. DR PATRIC; 26928633; VBIBurMal32783_3543. DR Proteomes; UP000003995; Unassembled WGS sequence. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000003995}; KW Methyltransferase {ECO:0000313|EMBL:EEP85294.1}; KW Transferase {ECO:0000313|EMBL:EEP85294.1}. SQ SEQUENCE 359 AA; 38489 MW; DE2A19E642A99A61 CRC64; MSEPTPIAPF ASSATPAAPY TRGAALPQLL RQRILILDGA MGTMIQRYKL DEAAYRGERF KDFPRDVKGN NELLSITQPR IIREIHDQYF AAGADIVETN TFGATAVAQA DYGMEALVVE MNVASAALAR ESAAKYATPE KPRFVAGAIG PTPKTASISP DVNDPGARNV TFDELRDAYY QQAKALLDGG VDLFLVETIF DTLNAKAALF ALDQLFDDTG ERLPIMISGT VTDASGRILS GQTVEAFWNS LRHAKPLTFG LNCALGAALM RPYIAELAKL CDTYVSCYPN AGLPNPMSDT GFDETPDVTS GLLKEFAQAG LVNLAGGCCG TTPEHIAAIA KALAEVKPRR WPSQYSEAA // ID C4FMM8_9FIRM Unreviewed; 813 AA. AC C4FMM8; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEP65995.1}; GN ORFNames=VEIDISOL_00058 {ECO:0000313|EMBL:EEP65995.1}; OS Veillonella dispar ATCC 17748. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Veillonella. OX NCBI_TaxID=546273 {ECO:0000313|EMBL:EEP65995.1}; RN [1] {ECO:0000313|EMBL:EEP65995.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 17748 {ECO:0000313|EMBL:EEP65995.1}; 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., 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEP65995.1}. 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; ACIK02000004; EEP65995.1; -; Genomic_DNA. DR RefSeq; WP_005384845.1; NZ_GG667604.1. DR EnsemblBacteria; EEP65995; EEP65995; VEIDISOL_00058. DR PATRIC; 29648432; VBIVeiDis1254_0543. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEP65995.1}; KW Transferase {ECO:0000313|EMBL:EEP65995.1}. SQ SEQUENCE 813 AA; 87242 MW; B7E563462CE1F3BC CRC64; MFMYIFDGAM GTMLQAAGLE EGYCPELFNV EKPEVVKNIH AQYLQHGSDV ITTNTFGACG LKLEDYDLQD RVREINIAAV KVAKDAIAEF KPSARVAGSM GPTGRFLQPL GNMSFDSIYD TYREQAEALI EGGVDFIIIE TIIDVQEMRA ALLASLDARE AAGKTKEDVQ IICQFSFSED GRTITGTPPA VATTIVEAMG ADIIGINCSL GPEQITPLIE EIASVTNLPI ICQPNAGMPQ LINKQTVFPL TAEEMGPLML PIVDAGASYV GGCCGTTPAH IQAISDAVKA HTPKERAHVE PKTIITSRTK LLELGHNTKP LIIGERINPT GRKVLAQELR DGSFIRVKRD ALDQVEAGAD ILDVNMGVAG MDQTPLMERA IFELSMLVET PLSIDTLDPA AMEVALKNYP GRALINSVNG EEESITHVMP LAKRYGAALL CLPICSGDLP EKAEDRVALA ESIVNRAYGY GLQPHDLLLD PLVLTLASGE DSARQTLRTL QLYKEKFGFP TVMGLSNISF GMPQRPYLNG QFLTMALACG LTTPIMNPLN YPAKKAFVSS TTLLGWDPGS AEFIKEYGYE DETSAPGNAA PKGPEKKSFD SNDPLANIRA CVEQGEKEAI VDLVKKALAD GMDPLDITKK GLSEAMNVVG DKFGSGKLFL PQVMLAAETM QAAFNTIKEI IPASESLDKG TVVVATVKGD IHDLGKNIVA ALLENNGYKI VDLGKDVDPE VIVQAIKDNK AALVGICSLM TTTMPQIDNT IAAIRAAGLK TKVMVGGAVV SQDYADQAGA DIYAKDGIAA VNHANDYFET LEK // ID C4FSL5_9FIRM Unreviewed; 341 AA. AC C4FSL5; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEP64843.1}; GN ORFNames=VEIDISOL_01905 {ECO:0000313|EMBL:EEP64843.1}; OS Veillonella dispar ATCC 17748. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Veillonella. OX NCBI_TaxID=546273 {ECO:0000313|EMBL:EEP64843.1}; RN [1] {ECO:0000313|EMBL:EEP64843.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 17748 {ECO:0000313|EMBL:EEP64843.1}; 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., 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEP64843.1}. 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; ACIK02000019; EEP64843.1; -; Genomic_DNA. DR RefSeq; WP_005387843.1; NZ_GG667605.1. DR EnsemblBacteria; EEP64843; EEP64843; VEIDISOL_01905. DR PATRIC; 29651962; VBIVeiDis1254_1768. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEP64843.1}; KW Transferase {ECO:0000313|EMBL:EEP64843.1}. SQ SEQUENCE 341 AA; 37228 MW; 1A76F160BEBB7CEE CRC64; MGDMMAKRRA FLDIIKEKGA LVLDGGLGSE LERYGCNLQH KLWSAKILMD QPDIIKKIHI SYLAAGADII QSSGYQATVA GFKGLGYGTE EAIELVKLSV RLAVQARNEF VEAKASGALT LRGITLGEET PDGVRYFSEG ALPKPLVAAS VGPYGAFLAD GSEYRGYPDV QTEYLEIFHI PRLALFCEEN PDILSFETIP SYDEAIAIAR AMSDPYTSRG IPGWIAFSCK DGHHVSSGET IIKCAEMIDK VRPITGIGVN CTKPEYVESL IKDIRTVTDK PIAVYPNLGE SYDSETKTWY GDPASFVDYV DVWRNAGADI IGGCCRTTPE IIGDIAKKIH K // ID C4GEB2_9FIRM Unreviewed; 841 AA. AC C4GEB2; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEP27364.1}; GN ORFNames=GCWU000342_02058 {ECO:0000313|EMBL:EEP27364.1}; OS Shuttleworthia satelles DSM 14600. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Shuttleworthia. OX NCBI_TaxID=626523 {ECO:0000313|EMBL:EEP27364.1}; RN [1] {ECO:0000313|EMBL:EEP27364.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 14600 {ECO:0000313|EMBL:EEP27364.1}; 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., 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEP27364.1}. 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; ACIP02000007; EEP27364.1; -; Genomic_DNA. DR RefSeq; WP_006907035.1; NZ_GG665867.1. DR EnsemblBacteria; EEP27364; EEP27364; GCWU000342_02058. DR PATRIC; 28587869; VBIShuSat84517_1682. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEP27364.1}; KW Transferase {ECO:0000313|EMBL:EEP27364.1}. SQ SEQUENCE 841 AA; 90573 MW; FD18D6A7F068764B CRC64; MDNKIIVLDG GMGTMLQAAG MPAGQHPEVF GHQHPEIVEQ IHRQYIEAGS NVIYANTFGA NARKLQGCSI DTGKAVFSAI RTAKRAAQKA AKETVRVALD LGPVGELLEP LGTLSFEEAY EIYREAVVAG YEAGADLIVA ETFTDLLDIK ALVLAAKENT PLPVWTTMTF ERSGRTFTGT TIASMALTLT GLGVDAIGIN CSLGPTEILP LIEELREWTH LPVIAKPNAG LPDPRTGVYD LTAEDFGKQM QAYAELGVSV LGGCCGTDPD YIRCLVSRLR EAGYISGWQD LSQASAGADR SKVRKGICST TNVCEFGGVR VIGERINPTG KKRFQQALRE HDMEYICKMA LDEEEAGADL LDVNVGLPGA EEKPLMLEVV RALQGVVSVP LQIDSSDPEV IEAALRIYAG KAIINSVNAD DAKLEAILPV ARKYGAAVIG LALDEGGIPQ TARERFEKAA YIKEKCLKAG MEADDIIIDA LTLTVSAQQE QARETLEAVE RISRELGLHT ALGVSNISFG LPAREHVTEN FLIQAMYCGL DFPIINPNIL SLMDAVASFK ALSGEDISCM HYIDRFAGRK EIKTSVSDSR PQAESAEGAV AGDASNGERG ISDQGKSSVG LSGKKEEDSF KTAIDQAILK GLKQETRKLA EGLLEQGLTE VEVINRYLIP ALDLVGDQYE KQTIFLPQLI NSANAASAAF DMIKDRIAAR GQGASGKEDK KIVVCTVKGD IHDIGKNIVK VILENYGYKV FDLGRDVPAG KVVDTVVAED VRLVGLSALM TTTLPAMQET IDRLREASPH TKVWVGGAVL TREYAREMGA DFYADDARES VEIAQRVLGE A // ID C4GEB4_9FIRM Unreviewed; 670 AA. AC C4GEB4; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 27-MAY-2015, entry version 28. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=GCWU000342_02060 {ECO:0000313|EMBL:EEP27366.1}; OS Shuttleworthia satelles DSM 14600. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Shuttleworthia. OX NCBI_TaxID=626523 {ECO:0000313|EMBL:EEP27366.1}; RN [1] {ECO:0000313|EMBL:EEP27366.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 14600 {ECO:0000313|EMBL:EEP27366.1}; 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., 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEP27366.1}. 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; ACIP02000007; EEP27366.1; -; Genomic_DNA. DR RefSeq; WP_006907037.1; NZ_GG665867.1. DR ProteinModelPortal; C4GEB4; -. DR EnsemblBacteria; EEP27366; EEP27366; GCWU000342_02060. DR PATRIC; 28587873; VBIShuSat84517_1684. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EEP27366.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EEP27366.1}. SQ SEQUENCE 670 AA; 74033 MW; 400A057D6CF8EA76 CRC64; MQIREYLKEH TLLFDGAFGT YYTKQFRPEK EESFFPEYVN VSRPDRVKAI HRKYLSAGAH AIKTNTFGAY PGILMKDAGE TKKLITAGFS LAEEALLNHL SKDVKNRPET TGEFARRAGQ ERSAEASGEE DYFIFADLGP APGEEEKERI LAYQMAIDSF LETGARYFLF ETLPEEKTVL EAIRYLKDQC PGAYTISSFA VMPDGFSSEG CNYRDMLAAA AGESAVDAVG LNCMSSVWHM DHLIRQIPDP GKPLLLMPNA GYPVVRGYRT VFEGNADYFA RILARDAGQG VAMVGGCCGT TPDHIRLLAD RLRENPVRHQ GGQGPVFKEP DPALGQDHGK RSDQHLYAAT GSDGNSSDKG SRDSGLSDRG LSVSKDQDAF YQKLMSGRKV VAVELDSPRG CDITRFMEAA ENLKEAGADI ITIADNPIAK ARMDSSIVAG IIRRQVGLDA LPHMTCRDRN LNATKSLLLG NYAQGIRNVL VITGDPIPSA RRDEVKVVYQ FNSRKLMAYM KALGQEEGTF PSPMHIFGAL NVNARNFEIE LDRAREKVQA GAVGFLTQPA LTTEAIANIC RASETLRAEN SRIRLLGGII PVISERNGRF MQSEISGIDV PDALIERYVG KDRADCEEIA VDSSLELAKT MEDAVDGYYL VTPFMRDYLI RRIMERLPGR // ID C4IFK5_CLOBU Unreviewed; 594 AA. AC C4IFK5; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 27-MAY-2015, entry version 30. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=CLP_1709 {ECO:0000313|EMBL:EEP54285.1}; OS Clostridium butyricum E4 str. BoNT E BL5262. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=632245 {ECO:0000313|EMBL:EEP54285.1, ECO:0000313|Proteomes:UP000003081}; RN [1] {ECO:0000313|EMBL:EEP54285.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BoNT E BL5262 {ECO:0000313|EMBL:EEP54285.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEP54285.1}. 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; ACOM01000005; EEP54285.1; -; Genomic_DNA. DR RefSeq; WP_003411215.1; NZ_ACOM01000005.1. DR ProteinModelPortal; C4IFK5; -. DR EnsemblBacteria; EEP54285; EEP54285; CLP_1709. DR PATRIC; 26458595; VBICloBut121738_2276. DR Proteomes; UP000003081; Unassembled WGS sequence. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003081}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EEP54285.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EEP54285.1}. SQ SEQUENCE 594 AA; 66530 MW; 42239028A183C567 CRC64; MIKEFLNNNI LICDGAMGTY YSEKTGNDIS YCEFGNLNDK NTIRRIHEEY IEAGAKLIRT NTFSANSKEL GVSRKTLKDI IESGIEIAKE AVYNKEVFIG ASIGPIRENG ADENFVEVLE EYKFIVDCFL DNNINVFIFE TLSNLDYLQE VSTYIKNKKP ESFILTQFAV KPDGFTRDGY SVSKIVGEVK KINTIDSYGF NCGSGPTHAL ELIKKIDIGD DIVSSLPNAG FPEIIHERTV YPNNPVYFAR KLKEIKKLGV SIIGGCCGTN PSYISKLRDT IDNKPEAGDK IKRYEHETYN EKNIIKNTFK EKVKNGDFVI AVELSAPVDT DINKIMTGAK VCKDNNIDIV TVPDSPMSKV RADSVVMSSK IKREIGIEAM PHMCCRDKNT NAIRSSLIGG HIEEIRNILA ITGDPISDAS RIETKSVFNL NSFKLIELIN DMNNEVFTSD DIFIGGALNL NVLNKEVEYG RMMKKVERGA KFFLTQPIYD DSAVEFLKSI KERTDVKILG GILPVVSYRN AMFLNNELPG VTIPQEILNR FSEDMSREEG QNIGIDIAVS MGKKLKGICD GLYFITPFGR VNMIVDIVNR IKEV // ID C4IG61_CLOBU Unreviewed; 307 AA. AC C4IG61; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEP53672.1}; GN ORFNames=CLP_2073 {ECO:0000313|EMBL:EEP53672.1}; OS Clostridium butyricum E4 str. BoNT E BL5262. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=632245 {ECO:0000313|EMBL:EEP53672.1, ECO:0000313|Proteomes:UP000003081}; RN [1] {ECO:0000313|EMBL:EEP53672.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BoNT E BL5262 {ECO:0000313|EMBL:EEP53672.1}; 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. {ECO:0000313|EMBL:EEP53672.1}. 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; ACOM01000005; EEP53672.1; -; Genomic_DNA. DR RefSeq; WP_003412687.1; NZ_ACOM01000005.1. DR ProteinModelPortal; C4IG61; -. DR EnsemblBacteria; EEP53672; EEP53672; CLP_2073. DR PATRIC; 26459305; VBICloBut121738_2631. DR Proteomes; UP000003081; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000003081}; KW Methyltransferase {ECO:0000313|EMBL:EEP53672.1}; KW Transferase {ECO:0000313|EMBL:EEP53672.1}. SQ SEQUENCE 307 AA; 34401 MW; 27F165946662E263 CRC64; MDFQTCFNTS SSILMDGALG ERLKREFNIK FDDKVAMANL IYDDKSRRAM EIIFQEYVKI AEIYSLPFIA TTPTRRANKE RVLQSNLSGK IIEDNVRFLQ EIKKNTSTNM FVGGLMGCKG DAYKGTEILS IEEAQEFHSW QADLFKNSGV DFLYAGIMPA LSEAIGMAKA MESTGLPYII SFMIKNNGKL IDGTTIHNAI INIDNATVHK PIGYMTNCVH PIVLRKALST QFNKTKLVRE RFCGIQANAS PLSPEELDNC SDLKSSDNVS LANEMMKLNQ YFNPKIFGGC CGTDNTHIEE IAKRIKN // ID C4IKP6_CLOBU Unreviewed; 803 AA. AC C4IKP6; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEP53597.1}; GN ORFNames=CLP_1226 {ECO:0000313|EMBL:EEP53597.1}; OS Clostridium butyricum E4 str. BoNT E BL5262. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=632245 {ECO:0000313|EMBL:EEP53597.1, ECO:0000313|Proteomes:UP000003081}; RN [1] {ECO:0000313|EMBL:EEP53597.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BoNT E BL5262 {ECO:0000313|EMBL:EEP53597.1}; 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. {ECO:0000313|EMBL:EEP53597.1}. 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; ACOM01000005; EEP53597.1; -; Genomic_DNA. DR RefSeq; WP_003407711.1; NZ_ACOM01000005.1. DR ProteinModelPortal; C4IKP6; -. DR EnsemblBacteria; EEP53597; EEP53597; CLP_1226. DR PATRIC; 26457639; VBICloBut121738_1799. DR Proteomes; UP000003081; Unassembled WGS sequence. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000003081}; KW Methyltransferase {ECO:0000313|EMBL:EEP53597.1}; KW Transferase {ECO:0000313|EMBL:EEP53597.1}. SQ SEQUENCE 803 AA; 88110 MW; 0C6835B3FC9FA1AB CRC64; MGLKELIKEK ILIFDGAMGT MLQKKGLKIG ENPEILNIKS PDIIEEIHRE YIESGANVIT TNTFGANERK LKLCNLEVEE AVDAAINIAK KARGEKEVYI ALDIGPIGEL LEPMGTLSFD EAYDIFKRQI IQGTKSGADV ILFETMTDLY ELKAAVLAAK ENSSLPILCT MTFEENGRTF TGCLPEAMVL VLEGLGVDAL GVNCSLGPKQ LKPVVEEICR LSNIPVMVQP NAGLPTLSVN NETKYDVTKE EFAETLCSFI DSGVSIIGGC CGTTPDYIRE LVKQTDGKSI LKREKNYYPA VCTPSKVVKI DGIRIVGERI NPTGKKLFKQ ALINDDLDYI LNTAVAQTEA GAHILDVNVG LPEINEPEMM QKVVKEIQGI LDIPLQIDSS DKNAIEKGLR YYNGKPILNS VNGEDKVLEN ILPMVKKYGA NVVGLTLSES GIPKKAEERF EIAKKIVDKA AQYGINKENV FIDCLVLTVS AQQEEVQETL KAVRMVKEKL GVKTLLGVSN ISFGLPNRKL INETFLALAL ANGLDLPIMN PNESGMVRVI DSYNVLYNYD KGSEHYIKNY ANVTIESNVE IKNADKTNII KSQSENGESN LKSIVIKGLK EEAKSATTNL LKKYEPLTIV NEYLIPALDE VGDKYEKGVL FLPQLIQAAE TVKNSFAVLK AEISKNNQET ISKGKIIVAT VKGDIHDIGK NIVKVILENY GYEMIDLGKD VPIETVVSEA KKHNVKLIGL SALMTTTLRS MEETIKALKE DGYEGKVFVG GAVLTPEYAD AIGADFYAKD ARESVEIAKE VLS // ID C4IR27_BRUAO Unreviewed; 1261 AA. AC C4IR27; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 27-MAY-2015, entry version 39. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEP63703.1}; DE EC=1.1.1.133 {ECO:0000313|EMBL:EEP63703.1}; GN Name=metH {ECO:0000313|EMBL:EEP63703.1}; GN ORFNames=BAAA_1000193 {ECO:0000313|EMBL:EEP63703.1}; OS Brucella abortus str. 2308 A. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=641140 {ECO:0000313|EMBL:EEP63703.1}; RN [1] {ECO:0000313|EMBL:EEP63703.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=2308 A {ECO:0000313|EMBL:EEP63703.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEP63703.1}. 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; ACOR01000001; EEP63703.1; -; Genomic_DNA. DR RefSeq; WP_002965438.1; NZ_ACOR01000001.1. DR ProteinModelPortal; C4IR27; -. DR SMR; C4IR27; 673-921. DR EnsemblBacteria; EEP63703; EEP63703; BAAA_1000193. DR GeneID; 3786978; -. DR PATRIC; 35201634; VBIBruAbo135566_0200. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008831; F:dTDP-4-dehydrorhamnose reductase activity; IEA:UniProtKB-EC. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Oxidoreductase {ECO:0000313|EMBL:EEP63703.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 263 263 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 326 326 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 327 327 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 783 783 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1261 AA; 138652 MW; B65506A5F8F0B796 CRC64; MASSLDDLFG ATAAKPDGSE VLAALTQAAR ERILILDGAM GTQIQGLGFH EEHFRGDRFA TCDCQLQGNN DLLTLTQPKA IEEIHYAYAM AGADILETNT FSSTSIAQAD YGMEAMVYDL NRDGARLARR AALRAEQKDG RRRFVAGALG PTNRTASLSP DVNNPGFRAV TFDDLRIAYS EQIRGLIDGG SDIILIETIF DTLNAKAAVF ATEEVFAEKG VRLPVMISGT ITDLSGRTLS GQTPTAFWYS LRHARPFTIG LNCALGANAM RAHLDELSGI ADTFICAYPN AGLPNEFGQY DETPEAMAAQ IEGFARDGLV NVVGGCCGST PDHIRAIAQA VAKYEPRKPA KVPPLMRLSG LEPFTLTKDI PFVNIGERTN VTGSARFRKL VKAGDFAAAL DVARDQVANG AQIIDINMDE GLIDSEKAMV EFLNLIAAEP DIARVPIMLD SSKWEVIEAG LKCVQGKAVV NSISLKEGEE AFLHHARLVR AYGAAVVIMA FDETGQADTQ ARKIEICTRA YKILTEQVGF PPEDIIFDPN IFAVATGIEE HNNYGVDFIE ATREIVRTLP HVHISGGVSN LSFSFRGNEP VREAMHAVFL YHAIQAGMDM GIVNAGQLAV YDTIDAELRE ACEDVVLNRP TKTGESATER LLEIAERFRD SGSREARTQD LSWREWPVEK RLEHALVNGI TEYIEADTEE ARLAAERPLH VIEGPLMAGM NVVGDLFGSG KMFLPQVVKS ARVMKQAVAV LLPFMEEEKR LNGGEGRQSA GKVLMATVKG DVHDIGKNIV GVVLACNNYE IIDLGVMVPS QKILQVARDE KVDIIGLSGL ITPSLDEMAH VAAEMEREGF DIPLLIGGAT TSRVHTAVKI HSRYERGQAV YVVDASRAVG VVSNLLSPEG KQAYIDGLRN EYAKVAAAHA RNEAEKQRLP IARARANPHQ LDWENYEPVK PAFTGTKVFE TYDLAEIARY IDWTPFFQTW ELRGRYPAIL EDEKQGEAAR QLWADAQAML RKIIDEKWFT PRAVVGFWPA NAVGDDIRLF TDESRKEELA TLFTLRQQLT KRDGRPNVAM ADFVAPVESG KQDYVGGFVV TAGIGEIAIA ERFERANDDY SAILVKALAD RFAEAFAELM HERVRKEFWA YAPDEAFTPE ELISEPYKGI RPAPGYPAQP DHTEKTTLFR LLDATANTGV ELTESYAMWP GSSVSGLYIG HPESYYFGVA KVERDQVEDY ARRKDMDVEA VERWLTPILN YVPGASKDEA A // ID C4KNR9_BURPE Unreviewed; 359 AA. AC C4KNR9; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 27-MAY-2015, entry version 35. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACQ97235.1}; GN ORFNames=GBP346_A0341 {ECO:0000313|EMBL:ACQ97235.1}; OS Burkholderia pseudomallei MSHR346. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=536230 {ECO:0000313|EMBL:ACQ97235.1, ECO:0000313|Proteomes:UP000002031}; RN [1] {ECO:0000313|EMBL:ACQ97235.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MSHR346 {ECO:0000313|EMBL:ACQ97235.1}; 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 ----------------------------------------------------------------------- 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; ACQ97235.1; -; Genomic_DNA. DR RefSeq; WP_004204527.1; NC_012695.1. DR RefSeq; YP_002895068.1; NC_012695.1. DR ProteinModelPortal; C4KNR9; -. DR STRING; 536230.GBP346_A0341; -. DR EnsemblBacteria; ACQ97235; ACQ97235; GBP346_A0341. DR KEGG; bpr:GBP346_A0341; -. DR PATRIC; 32569938; VBIBurPse130472_0311. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; BPSE536230:GHVQ-341-MONOMER; -. DR Proteomes; UP000002031; Chromosome I. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002031}; KW Methyltransferase {ECO:0000313|EMBL:ACQ97235.1}; KW Transferase {ECO:0000313|EMBL:ACQ97235.1}. SQ SEQUENCE 359 AA; 38459 MW; 1013B7D60E53B797 CRC64; MSEPTPIAPF ASSAAPAAPY TRGAALPQLL RQRILILDGA MGTMIQRYKL DEAAYRGERF KDFPRDVKGN NELLSITQPR IIREIHDQYF AAGADIVETN TFGATAVAQA DYGMEALVVE MNVASAALAR ESAAKYATPE KPRFVAGAIG PTPKTASISP DVNDPGARNV TFDELRDAYY QQAKALLDGG VDLFLVETIF DTLNAKAALF ALDQLFDDTG ERLPIMISGT VTDASGRILS GQTVEAFWNS LRHAKPLTFG LNCALGAALM RPYIAELAKL CDTYVSCYPN AGLPNPMSDT GFDETPDVTS GLLKEFAQAG LVNLAGGCCG TTPEHIAAIA KALAEVKPRR WPSQYSEAA // ID C4L805_TOLAT Unreviewed; 297 AA. AC C4L805; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 27-MAY-2015, entry version 31. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACQ91804.1}; GN OrderedLocusNames=Tola_0174 {ECO:0000313|EMBL:ACQ91804.1}; OS Tolumonas auensis (strain DSM 9187 / TA4). OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales; OC Aeromonadaceae; Tolumonas. OX NCBI_TaxID=595494 {ECO:0000313|EMBL:ACQ91804.1, ECO:0000313|Proteomes:UP000009073}; RN [1] {ECO:0000313|Proteomes:UP000009073} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 9187 / TA4 {ECO:0000313|Proteomes:UP000009073}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; ACQ91804.1; -; Genomic_DNA. DR RefSeq; WP_012728403.1; NC_012691.1. DR RefSeq; YP_002891390.1; NC_012691.1. DR STRING; 595494.Tola_0174; -. DR EnsemblBacteria; ACQ91804; ACQ91804; Tola_0174. DR KEGG; tau:Tola_0174; -. DR PATRIC; 23976931; VBITolAue42623_0177. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; PYVDVWL; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; TAUE595494:GHEF-187-MONOMER; -. DR Proteomes; UP000009073; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009073}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ACQ91804.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000009073}; KW Transferase {ECO:0000313|EMBL:ACQ91804.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 281 281 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 282 282 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 297 AA; 31653 MW; 2D846B4418CC42A7 CRC64; MSKVQILDGG MGRELKRIGA PFQQPEWSAL ALLDAPEYVT MAHNAFIGSG ADIITTNSYA VVPFHIGEVR FTERGHALAQ LAAEIARACA DKAAHPVTVA GSLSPVLGSY RPDLFQMEAA LRIYRVLIAA QEPFVDHWLA ETQSSIAEVK AVRQALGDNS KPLWVSFTLD DEPAGGQALL RSGETVTDAV AAAIGLNVSA ILFNCSQPEV MTNAVHDAVA EIQRQGKAIP VGVYANAFPA QSKEAEANAE LDEIRADLNP DAYLNWAKKW IAAGATIIGG CCGITPEHIA QLAKDLK // ID C4L880_TOLAT Unreviewed; 1237 AA. AC C4L880; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 01-APR-2015, entry version 46. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACQ93726.1}; GN OrderedLocusNames=Tola_2127 {ECO:0000313|EMBL:ACQ93726.1}; OS Tolumonas auensis (strain DSM 9187 / TA4). OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales; OC Aeromonadaceae; Tolumonas. OX NCBI_TaxID=595494 {ECO:0000313|EMBL:ACQ93726.1, ECO:0000313|Proteomes:UP000009073}; RN [1] {ECO:0000313|Proteomes:UP000009073} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 9187 / TA4 {ECO:0000313|Proteomes:UP000009073}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001616; ACQ93726.1; -; Genomic_DNA. DR RefSeq; WP_015879194.1; NC_012691.1. DR RefSeq; YP_002893312.1; NC_012691.1. DR STRING; 595494.Tola_2127; -. DR EnsemblBacteria; ACQ93726; ACQ93726; Tola_2127. DR KEGG; tau:Tola_2127; -. DR PATRIC; 23980899; VBITolAue42623_2111. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; TAUE595494:GHEF-2193-MONOMER; -. DR Proteomes; UP000009073; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000009073}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000009073}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 249 249 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1237 AA; 136654 MW; 1C6F6B7DEC1ACB44 CRC64; MVVKVNTSAL HQSLQERILL IDGGMGTMIQ SYQLQEADFR GERFADWPSD LKGNNDLLVL TKPDVIAAIH DAYLAAGADI LETNSFNATR IAMADYHMEE LSAEINREAA RLARKAADEW NAKTPQKPRF VAGVLGPTNR TASISPDVND PGKRNVTFDA LVEAYKESTE ALIEGGVDII MIETIFDTLN AKAAFFAVDT IFEKLGFKLP VMISGTITDA SGRTLSGQTT EAFYNSLRHA EPLSFGLNCA LGPKELRQYV QELARISETY VSVHPNAGLP NAFGGYDLEA DEMAEHIREW AESGFLNMVG GCCGTTPEHI RAMAKAVDGI KPRVLPELPV ACRLAGLEPL TIDENSMFVN VGERTNVTGS AKFKRLIKEE QYDEALDIAR QQVISGAQII DINMDEGMLD AQACMVRFLN LIASEPDISR VPIMIDSSKW EVIEAGLKCI QGKGIVNSIS MKEGEEKFIA QAKLLRRYGA AVIVMAFDEV GQADTRARKF EICQRAYKIL TEQVGFPPED IIFDPNIFAV ATGIDEHNNY AVDFIEAVKD IKTNLPHAMI SGGVSNVSFS FRGNDQVREA IHSVFLYYTI KNGMDMGIVN AGQLAIYEDI PAELKEKVEA VVLNTHPGAT EELLIIAEKY RGGAAQQAID PREQEWRSWP VGKRLEHALV KGITDFIDED TEEARQLAAR PIEVIEGPLM AGMNVVGDLF GAGKMFLPQV VKSARVMKRA VAYLQPYIEQ GKSAGQTNGK IVMATVKGDV HDIGKNIVGV VLQCNNYEIV DLGVMVSCEK ILQTAREVNA DIIGLSGLIT PSLDEMVHVA KEMERQGFKI PLMIGGATTS KAHTAVKIEQ NYSEPVVYVS NASRAVGVVQ NLLSQEQKAT FVERLRQEYV LVREQHSRKQ PRTPPVTLEE ARANALKLDW QNYQPPKPKQ LGVKVIDDVA IATLRDYIDW TQFFLSWELA GKFPRILEDE VVGEEAKRLY HDALAMLDRL QTSGEVKVSG IIGLFAANRV GDDVEIYTDE SRSQVAQTFH FLRQQTNKVM QARNGEVFPN YCLADFIAPK ESGVADYFGS FAVTGGIGEA ELAEQYKAAG DDYNAILIQA VCDRLAEAFA EYLHAQVRKE YWGYAADENL TNEELIRENY QGIRPAPGYP ACPEHTEKGT LWQLLGVEQA IGMKLTDSYA MLPAAAVSGF YFSHPQCKYF AVAGIQKDQV EDYAARKGMT LAEAERWLAP NLAYDVE // ID C4LIL8_CORK4 Unreviewed; 1240 AA. AC C4LIL8; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 27-MAY-2015, entry version 51. DE SubName: Full=5-methyltetrahydrofolate--homocysteinemethyltransferase {ECO:0000313|EMBL:ACR17673.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ACR17673.1}; GN Name=metH {ECO:0000313|EMBL:ACR17673.1}; GN OrderedLocusNames=ckrop_0919 {ECO:0000313|EMBL:ACR17673.1}; OS Corynebacterium kroppenstedtii (strain DSM 44385 / CCUG 35717). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=645127 {ECO:0000313|EMBL:ACR17673.1, ECO:0000313|Proteomes:UP000001473}; RN [1] {ECO:0000313|EMBL:ACR17673.1, ECO:0000313|Proteomes:UP000001473} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44385 / CCUG 35717 {ECO:0000313|Proteomes:UP000001473}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001620; ACR17673.1; -; Genomic_DNA. DR RefSeq; WP_012731560.1; NC_012704.1. DR RefSeq; YP_002906216.1; NC_012704.1. DR STRING; 645127.ckrop_0919; -. DR EnsemblBacteria; ACR17673; ACR17673; ckrop_0919. DR KEGG; ckp:ckrop_0919; -. DR PATRIC; 21517153; VBICorKro120627_0947. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CKRO645127:GI7D-909-MONOMER; -. DR Proteomes; UP000001473; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001473}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACR17673.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001473}; KW Transferase {ECO:0000313|EMBL:ACR17673.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 249 249 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 315 315 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 316 316 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 782 782 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1240 AA; 135518 MW; 0A62D47CEF74588F CRC64; MVEHPNSRLS CLSVNDERQP LNPKKSEFLQ ALHDRVLIGD GAMGTQLQAI DLDLDADFHG LEGCNEILNI TRPDILADIH RRYFEAGADA VETNTFGCNL PNFADYGIED RIEEIAYAGT QIARSVADDM GPGREGMKRF VLGSLGPGTK LPTLGNAPFS DLRDAYTEAA HGLVRGGADA ILIETAQDLL QVKAAVHGVQ QAFDDYGTTL PIMCHVTVET TGTMLLGSEI GAALTALERL GIDVIGMNCA TGPDEMNEHL RYLSAHAPMP VSVMPNAGLP ELGANGAVYP LTPDELAAAS VHFVRDYGLS MVGGCCGTTP EHITAVRDAV IGSPDSQEDA SESPAVTRPA RHHDFDDNVS SLYSTVPLTQ DTGITMIGER TNSNGSKAFR TAMLEGDWNK CLDIAKAQTR DGAHMIDLCV DYVGRDGTQD MAELASRLAT NSTLPIMLDS TEPDVIRMGL EHLGGRCAVN SVNFEDGDGP GSRYDRIMTL VKKHGAAVVA LTIDEEGQAR TAEKKVEIAE RLIADITTRW GLRESDIIVD CLTFPISTGQ VETRRDGIET INAIREITSR HPDIHTTLGL SNISFGLNPA ARQVLNSVFL NECIEAGLDT AIAHSSKIVP MNRIDDDQRD VALDMVYDRR GTEGRGGTAD EDYDPLQTFM ELFQGVSAAD AKDARAEALQ ALPLFKRLAQ RIIDGEKNGL EADLDLARDE KDPLEIINQD LLAGMKVVGD LFGSGQMQLP FVLQSAETMK AAVSHLEQFM EATDDSASKG KIILATVKGD VHDIGKNLVD IILSNNGYDV VNLGIKQPIS NILHAASEHQ ADVIGMSGLL VKSTVVMKDN LLEMNSAGAA NYPVLLGGAA LTRTYVENDL DELYQGDVHY ARDAFEGLNL MDQIMSMKRG SQRELTEEQI AAATRAQKKK EERKARHERS RKIAAKRKAE SAPAVIPDRS DVATDTPIAT PPFWGTRIVK GLPVRDYLTC LDERALFMGQ WGLRGTRGGD GPSYDELVET EGRPRLRAWI NDLKAEGILN HSAVVYGYFP AVSEGNTVHI LPVPNEAEEP DPTAQPVTSF EFPRQQRGRF LCIADFIRSR DEAQRTGHTD VFPLQLVTMG QSIADKANVL FKDNHYREYL ELHGIGVQLT EALAEYWHSR VRAELAFADG THAGDDDGTE DRAFFDLKYR GARYSFGYGS CPDLESRRAL VDLLRPERIG VELSEELQLH PEQSTDAFVL YHPEAKYFNV // ID C4R8J7_PICPG Unreviewed; 321 AA. AC C4R8J7; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 29-APR-2015, entry version 31. DE SubName: Full=Pichia pastoris GS115 chromosome 4, complete sequence {ECO:0000313|EMBL:CAY71922.1}; GN OrderedLocusNames=PAS_chr4_0664 {ECO:0000313|EMBL:CAY71922.1}; OS Komagataella pastoris (strain GS115 / ATCC 20864) (Yeast) (Pichia OS pastoris). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Phaffomycetaceae; Komagataella. OX NCBI_TaxID=644223 {ECO:0000313|EMBL:CAY71922.1, ECO:0000313|Proteomes:UP000000314}; RN [1] {ECO:0000313|EMBL:CAY71922.1, ECO:0000313|Proteomes:UP000000314} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GS115 / ATCC 20864 {ECO:0000313|Proteomes:UP000000314}; 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; FN392322; CAY71922.1; -; Genomic_DNA. DR RefSeq; XP_002494101.1; XM_002494056.1. DR STRING; 644223.PAS_chr4_0664; -. DR EnsemblFungi; CAY71922; CAY71922; PAS_chr4_0664. DR GeneID; 8201371; -. DR KEGG; ppa:PAS_chr4_0664; -. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR InParanoid; C4R8J7; -. DR KO; K00547; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000000314; Chromosome 4. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000314}; KW Reference proteome {ECO:0000313|Proteomes:UP000000314}. SQ SEQUENCE 321 AA; 35582 MW; B2A388041F969853 CRC64; MTPITKMDSW LKQKRCRVLD GALGTELEKL GIDIKSRLWS GKALFYSPET ITQIHSSYIQ AGAELILTCT YQLSDQGLKD LGIDDPDVYD RAVKLAKDAV DQNEGENKAK IVGSIGSYGA YLSGGEEYTG EYGAISKSEL EEFHRVRLQS LLTNPDVDLI GFETIPNILE AETLVVLFNA LATSLNVDKG YYMSFNCREE SNQSVIADGT SIPEVSDRLS KLDVSRMYAI GTNCCSISTA NGAVELFSKH TNLPLIVYPN SGERYDKTEK KWLPGECDQK ITDIVVNWLQ LNVKIIGGCC RTNPHFIRQL RDIVDNSSRS G // ID C4RMF4_9ACTO Unreviewed; 1167 AA. AC C4RMF4; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 01-APR-2015, entry version 36. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEP75155.1}; GN ORFNames=MCAG_05482 {ECO:0000313|EMBL:EEP75155.1}; OS Micromonospora sp. ATCC 39149. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micromonosporineae; Micromonosporaceae; Micromonospora. OX NCBI_TaxID=219305 {ECO:0000313|EMBL:EEP75155.1}; RN [1] {ECO:0000313|EMBL:EEP75155.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 39149 {ECO:0000313|EMBL:EEP75155.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG657738; EEP75155.1; -; Genomic_DNA. DR RefSeq; WP_007076417.1; NZ_GG657738.1. DR EnsemblBacteria; EEP75155; EEP75155; MCAG_05482. DR PATRIC; 26269286; VBIMicSp97049_4917. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 219 219 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 730 730 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1167 AA; 126772 MW; DFAC26DCEFC9E4CC CRC64; MLDVLSDRII VADGAMATML QAADLTLDDF EGHEGCNEIL NVTRPDVIHG VHDAYLAAGA DCVETNTFGA NLANLAEYDL QHRIRELSET GARIARRAAD AWSTAERPRF VLGAIGPGTK LPTLGHAAYA TLRDAYQENA AGLLAGGADA LIIETCQDLL QVKAAVVGSR RAMAEAGQSA PLICHVTVET TGTMLLGSEI GAALTALEPL GIDLIGLNCA TGPAEMSEHL RYLSQHARVP LSVMPNAGLP QLTADGAVYP LTPVELADAL ERFVAEYGVA LVGGCCGTTP EHIRMVAERL HGVRPGTREP RADAGVSSIY HHVPFAQDAS VLMVGERTNA NGSKAFREAM LAGDWQACVE IARSQARDGS HLLDLCVDYV GRDGTRDMRE LAGRFATAST LPIMLDSTEP QVIEAGLEML GGRCVVNSVN FEDGDGPGSR YARVMPVIAE HGAAVVALLI DEEGQARTTE WKVRVAQRLI EDLTGRWGLR RADILIDALT FPIATGQEET RRDGIATIEA IREIARRWPG VNFTLGISNV SFGLNPAARQ VLNSVFLHEC VQAGLTSAIV HASKILPMSK IPQEQREIAL DLVYDRRREG YDPVQRFIEV FEGVDASSAR ATRAEELAAL PLDERLRRRI VDGERNGLEA DLDAAMAGGR SPLSIINELL LDGMKVVGEL FGSGQMQLPF VLQSAEVMKT AVAYLEPHME KADDGGKGRI VLATVKGDVH DIGKNLVDII LSNNGYEVVN IGIKQPINAI LDAAEQHRAD AIGMSGLLVK STVIMKENLA EMAERGVAQR WPVLLGGAAL TRAYVEDDLR AMFPGQVHYA RDAFEGLSLM ERVMTAKRGG APVVDPQREA ALAARRQRRE RQRAMVGEAL PGLNDASVRS DVAVDVEVPT PPFFGTRVVK GLPLAEYAAL LDERATFLGQ WGLRGARGGK GPSYEELVES EGRPRLRYWL DRLTADKVLE AAVVYGYFPA YSEGNDLVVL DENGHAERAR FSFPRQRQER RLCLADFFRP KGDRLDVVAL QLVTVGQPIS EYTAKMFAGN AYRDYLEVHG LSVQLTEALA EYWHRRIRAE LTLPGGRTVG DDDPADLAGL LRTDYRGCRY AFGYPACPDL EDRAKIVDLL GADRIGVELS EEFQLVPEQA TDAIVVHHPE ANYFNAK // ID C4RNB1_9ACTO Unreviewed; 1214 AA. AC C4RNB1; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 01-APR-2015, entry version 38. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EEP75196.1}; GN ORFNames=MCAG_05523 {ECO:0000313|EMBL:EEP75196.1}; OS Micromonospora sp. ATCC 39149. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micromonosporineae; Micromonosporaceae; Micromonospora. OX NCBI_TaxID=219305 {ECO:0000313|EMBL:EEP75196.1}; RN [1] {ECO:0000313|EMBL:EEP75196.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 39149 {ECO:0000313|EMBL:EEP75196.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG657738; EEP75196.1; -; Genomic_DNA. DR EnsemblBacteria; EEP75196; EEP75196; MCAG_05523. DR PATRIC; 26269376; VBIMicSp97049_4963. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 258 258 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 767 767 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1214 AA; 130111 MW; BF028EFA6166C08E CRC64; MRTKGASETS GVVAMSSSVD RSDAVSALRR LLGERIAVLD GAWGTMLQGA RLSPADYRGD LIGDDHPCDV TGDPDLLNLT RPDLILDVHR QYLAAGADIT TTNTFTATSI GQADYGLEAL ARDMNVRGAQ LARQAADEAG GRFVAGSVGP LNVTLSLSPR VEDPAYRAVT FDDVKDAYAE QMAALAEGGV DLLLVETVFD TLNAKAAIAA AREAAPRLPL WISVTVVDLS GRTLSGQTVE AFWRSIAHAE PLVVGVNCAL GAAEMRPHVA ELSRLAGSYV AAHPNAGLPN AFGGYDQTPE EIGALLGEFA SDGLVNIVGG CCGTTPPHIA GIAAAVRGVA PRPVAREVPA TRFSGLEPFT IGPDTGFVMI GERTNVTGSA RFRRLVEADD YQAAVDVAVE QVRGGANLLD VNMDADLLDS EQAMVTFLNL IATEPEVARI PIMIDSSRWS VLEAGLKCVQ GKGVVNSISL KEGEEPFLAQ ARAIRGYGAG VVVMAFDEQG QADTSERKVQ ICGRAYDLLV GEAGFAPEDI IFDPNVLAVA TGMAEHNGYA KEFIDALPLI KARCPGARTS GGISNLSFAF RGNDVVREAM HSAFLFHAVR AGLDMGIVNA GQLSVYENIP ADLLELVEDV IFDRRPDATD RLVAFASTVT GSGTKREVDL SWRAAPVAER LKHALVHGIV DHVEADTEEA RLLLDRPLDV IEGPLMDGMR VVGDLFGAGK MFLPQVVKSA RVMKRSVAYL EPYMSKERAA GQGQGKVVLA TVKGDVHDIG KNIVGVVLGC NNYEVIDLGV MVPTARILDT AVAEGADAIG LSGLITPSLD EMVAVATEMQ RRGLRMPLLI GGATTSRQHT AVRIAPAYEG PTVHVLDASR VVGVVSDLLD AGRAQTLDTA NRAEQERLRA QHANRHAQPL LTLAQARANR ERVDFADLPV PAFTGVRTVE PTLAELREMI DWQFLFLAWE LKGKFPAILD QPVARELYDD ANTLLDAIIA DGSLRARGTY GFWTAHAEGD DIVLDDAGVR LPMLRQQTAK PAGRANRCLA DYVAPAGDHL GGFAVAVHGA EELAARYEAE HDDYRAIMVK ALADRLAEAF AEHLHLRARR DWFEPDAAPA LEDLHAERFR GIRPALGYPA SPDHSEKRDL FDLLGAETLG IGLTESYAMT PAASVSGLIF AHPDSRYFTV GRIGRDQAED YAARRRVALA EVERWLRPNL AYEP // ID C4RX31_YERBE Unreviewed; 1245 AA. AC C4RX31; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 01-APR-2015, entry version 34. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEQ08087.1}; GN ORFNames=yberc0001_520 {ECO:0000313|EMBL:EEQ08087.1}; OS Yersinia bercovieri ATCC 43970. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=349968 {ECO:0000313|EMBL:EEQ08087.1}; RN [1] {ECO:0000313|EMBL:EEQ08087.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43970 {ECO:0000313|EMBL:EEQ08087.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AALC02000004; EEQ08087.1; -; Genomic_DNA. DR EnsemblBacteria; EEQ08087; EEQ08087; yberc0001_520. DR PATRIC; 26363797; VBIYerBer741_0403. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 266 266 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 329 329 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 330 330 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 777 777 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1245 AA; 137719 MW; 606B04F975EDF22E CRC64; MSNGLFLQQG KEAAVVDIVT KNKVKELHQQ LAQRILVLDG GMGTMIQSYR LEEADYRGAR FADWPSDLKG NNDLLVLSKP EVITAIHNAY LEAGADILET NTFNSTTIAM ADYQMESLSA EINYEAARLA RICADEWTAR TPDKPRYVAG VLGPTNRTAS ISPKVNDPAF RNVSFDQLVE AYRESTCALI EGGADLIMIE TVFDTLNAKA ATFAVETEFE AMGVLLPVMI SGTITDASGR TLSGQTTEAF YNSLRHVKPL SFGLNCALGP DELRQYVAEL SRISEYYVSA HPNAGLPNAF GEYDLDAKEM AEQIGEWARA GFLNIVGGCC GTTPRHIAAM AKAVAGVPPR QLPDIPVACR LAGLEPLTID ANTLFVNVGE RTNVTGSARF KRLIKEEKYD EALEVALQQV ESGAQIIDIN MDEGMLDAEA AMVRFLNLIA GEPDIARVPI MIDSSKWEVI EKGLKCIQGK GIVNSISMKE GEEAFIHHAK LVRRYGAAMV VMAFDEAGQA DTRARKIEIC RRAYKILTET VGFPPEDIIF DPNIFAVATG IEEHNNYAVD FIEACADIKA ELPHAMISGG VSNVSFSFRG NDPVREAIHA VFLYYAIRNG MDMGIVNAGQ LAIYDDLSDE LRDAVEDVIL NRRSDSTERL LDLAEKYRSS KSGEVAIQQA EWRGWPVTKR LEYSLVKGIT EFIELDTEEA RQQADRPIEV IEGPLMAGMN VVGDLFGEGK MFLPQVVKSA RVMKQAVAYL EPYIEASKQK GTTAGKILLA TVKGDVHDIG KNIVGVVLQC NNYQIIDLGV MVPTEKILRT AREEQVDIIG LSGLITPSLD EMVNVAKEME RQGFTLPLLI GGATTSKAHT AVKIEQNYSG STTYVSNASR SVGVVSALLS DTQRDDFVAK TRKEYETVRI QHARKKPRTP PVSLPTARAN HTVIDWENYQ PPVAHKLGVQ VVEASIETLR NYIDWTPFFM TWSLAGKYPR ILEDEVVGEE AKRVFADANE LLDKLSAEDL LHPKGVVGLF PANSVGDDIE IYRDERRDEV LVVSHHLRQQ TEKTDFPNYC LADYVAPKSS GKADYFGAFA VTGGLEEDAL ADAYDAQHDD YNKIMIKALS DRLAEAFAEY LHERVRKVYW GFSPNENLSN EELVRENYQG IRPAPGYPAC PEHTEKGQIW QLLDVETHTG MKLTESFAMW PGASVSGWYF SHPESKYFAV AQIQRDQVED YAARKGMPVA EVERWLAPNL GYDAD // ID C4SHY9_YERMO Unreviewed; 1245 AA. AC C4SHY9; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 01-APR-2015, entry version 34. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEQ08831.1}; GN ORFNames=ymoll0001_40980 {ECO:0000313|EMBL:EEQ08831.1}; OS Yersinia mollaretii ATCC 43969. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=349967 {ECO:0000313|EMBL:EEQ08831.1}; RN [1] {ECO:0000313|EMBL:EEQ08831.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43969 {ECO:0000313|EMBL:EEQ08831.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AALD02000065; EEQ08831.1; -; Genomic_DNA. DR EnsemblBacteria; EEQ08831; EEQ08831; ymoll0001_40980. DR PATRIC; 29554875; VBIYerMol36980_3903. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 266 266 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 329 329 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 330 330 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 777 777 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1245 AA; 137703 MW; 9A6A3DD3D9C339BA CRC64; MSNGLFLQQG KEAAVVDTVT KNKVKELHQQ LAQRILVLDG GMGTMIQSYK LEEADYRGAR FADWPSDLKG NNDLLVLSKP EVITAIHNAY LEAGADILET NTFNSTTIAM ADYQMESLSA EINYEAARLA RLCADEWTAR TPDKPRYVAG VLGPTNRTAS ISPKVNDPAF RNVSFDQLVE AYRESTRALI EGGADLIMIE TVFDTLNAKA ATFAVETEFE AMGVLLPVMI SGTITDASGR TLSGQTTEAF YNSLRHVKPL SFGLNCALGP DELRQYVAEL SRISEYYVSA HPNAGLPNAF GEYDLEAKEM AEQIGEWARA GFLNIVGGCC GTTPRHIAAM VKAVAGVPPR QLPDIPVACR LAGLEPLTID ANTLFVNVGE RTNVTGSARF KRLIKEEKYD EALEVALQQV ESGAQIIDIN MDEGMLDAEA AMVRFLNLIA GEPDIARVPI MIDSSKWEVI EKGLKCIQGK GIVNSISMKE GEAAFIHHAK LVRRYGAAMV VMAFDETGQA DTRARKIEIC RRAYQILTET VGFPPEDIIF DPNIFAVATG IEEHNNYAVD FIEACADIKA ELPHAMISGG VSNVSFSFRG NDPVREAIHA VFLYYAIRNG MDMGIVNAGQ LAIYDDLSDE LRDAVEDVIL NRRSDSTERL LDLAEKYRSS KSGEVAIQQA EWRGWPVVKR LEYSLVKGIT EFIELDTEEA RQQADRPIEV IEGPLMAGMN VVGDLFGEGK MFLPQVVKSA RVMKQAVAYL EPYIEASKQK GTTAGKILLA TVKGDVHDIG KNIVGVVLQC NNYQIIDLGV MVPTEKILRT AREEKVDIIG LSGLITPSLD EMVNVAKEME RQGFTLPLLI GGATTSKAHT AVKIEQNYSG STTYVSNASR SVGVVSALLS DTQRDDFVAK TRKEYETVRI QHARKKPRTP PVSLPTARAN HTVIDWENYT PPVAHKLGVQ AVEASIETLR NYIDWTPFFM TWSLAGKYPR ILEDEVVGEE AKRVFADANE LLDKLSAEDL LHPKGVVGLF PANSVGDDIE IYRDERRDEV LVVSHHLRQQ TEKTDFPNYC LADYVAPKSS GKADYFGAFA VTGGLEEDAL ADAYDAQHDD YNKIMIKALS DRLAEAFAEY LHERVRKVYW GFSPNENLSN EELVRENYQG IRPAPGYPAC PEHTEKGQIW QLLEVETHTG MKLTESFAMW PGASVSGWYF SHPESKYFAV AQIQRDQVED YAARKGMPVA EVERWLAPNL GYDAD // ID C4T4W6_YERIN Unreviewed; 296 AA. AC C4T4W6; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 29-OCT-2014, entry version 14. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEQ18043.1}; GN ORFNames=yinte0001_3900 {ECO:0000313|EMBL:EEQ18043.1}; OS Yersinia intermedia ATCC 29909. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=349965 {ECO:0000313|EMBL:EEQ18043.1}; RN [1] {ECO:0000313|EMBL:EEQ18043.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29909 {ECO:0000313|EMBL:EEQ18043.1}; 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AALF02000025; EEQ18043.1; -; Genomic_DNA. DR EnsemblBacteria; EEQ18043; EEQ18043; yinte0001_3900. DR PATRIC; 36091282; VBIYerInt66761_3208. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEQ18043.1}; KW Transferase {ECO:0000313|EMBL:EEQ18043.1}. SQ SEQUENCE 296 AA; 32533 MW; 81B6735A148D8DFA CRC64; MILDGALATE LEARGCDLSD PLWSAKVLIE DPELIYQVHL DYFNAGAQCA ITASYQATPQ GFLQRGLDQQ QSLELITKSV QLAQQARKDF LNQHPQAEPL LIAGSVGPYG AYLADGSEYR GNYRLPQDEM IAFHRPRIAA LAEAGVDLLA CETLPSFHEL QALLTLLQEF PTLGGWFAFT LRDNQHLSDG TPLKDVLALL RGNQQVLAIG INCIALENVT PALQQFTALA DKPLLVYPNS GEHYDAVSKT WHACGGEHNH LIDLVGEWQR LGARLIGGCC RTTPKDIRII AEHCKP // ID C4T679_YERIN Unreviewed; 1231 AA. AC C4T679; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 27-MAY-2015, entry version 35. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEQ17542.1}; GN ORFNames=yinte0001_41740 {ECO:0000313|EMBL:EEQ17542.1}; OS Yersinia intermedia ATCC 29909. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=349965 {ECO:0000313|EMBL:EEQ17542.1}; RN [1] {ECO:0000313|EMBL:EEQ17542.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29909 {ECO:0000313|EMBL:EEQ17542.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AALF02000035; EEQ17542.1; -; Genomic_DNA. DR RefSeq; WP_005191511.1; NZ_AALF02000035.1. DR EnsemblBacteria; EEQ17542; EEQ17542; yinte0001_41740. DR PATRIC; 36092267; VBIYerInt66761_3689. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 252 252 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 315 315 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 316 316 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 763 763 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1231 AA; 136263 MW; E44B03C7BE241635 CRC64; MVDTILNNKV KQLHQQLAQR ILVLDGGMGT MIQSYRLEEA DYRGARFADW PSDLKGNNDL LVLSKPEVIT AIHNAYLEAG ADILETNTFN STTIAMADYQ MESLSAEINY EAARLARICA DEWTARTPEK PRYVAGVLGP TNRTASISPK VNDPAFRNVS FDQLVAAYRE STRALIEGGV DLIMIETVFD TLNAKAATFA VESEFEAMGV LLPVMISGTI TDASGRTLSG QTTEAFYNSL RHVKPLSFGL NCALGPDELR QYVAELSRIS EYYVSAHPNA GLPNAFGEYD LEAKEMAEQI GEWARAGFLN IVGGCCGTTP RHIAAMVKAV AGVPPRPLPD IAVACRLAGL EPLTIDANSL FVNVGERTNV TGSARFKRLI KEDKYDEALD VARQQVESGA QIIDINMDEG MLDAEAAMVR FLNLIAGEPD IARVPIMIDS SKWDVIEKGL KCIQGKGIVN SISMKEGEAA FIHHAKLVRR YGAAMVVMAF DETGQADTRA RKIEICRRAY KILTEIVGFP PEDIIFDPNI FAVATGIEEH NNYAVDFIEA CADIKAELPH AMISGGVSNV SFSFRGNDPV REAIHAVFLY YAIRNGMDMG IVNAGQLAIY DDLSDELRDA VEDVILNRRS DSTERLLDLA EKYRSSKSGE VAIQQAEWRG WAVGKRLEYS LVKGITEFIE LDTEEARQQA ERPIEVIEGP LMAGMNVVGD LFGEGKMFLP QVVKSARVMK QAVAYLEPYI EASKQKGTTA GKILLATVKG DVHDIGKNIV GVVLQCNNYE IIDLGVMVPT EKILRTAREE KVDIIGLSGL ITPSLDEMVN VAKEMERQGF TLPLLIGGAT TSKAHTAVKI EQNYSGSTTY VSNASRSVGV VSALLSDTQR DDFVAKTRKE YETVRIQHAR KKPRTPPVSL QVARDNQTII DWENYTPPVA HKLGVQPVEA SIETLRNYID WTPFFMTWSL AGKYPRILED EVVGEEAKRL FADANELLDK LSAENLLHPK GVVGIFPANS VGDDIEIYRD ERREDVLVVS HHLRQQTEKT DFPNYCLADY VAPKSSGKAD YYGAFAVTGG LEEDALADAY DAQHDDYNKI MIKALSDRLA EAFAEYLHER VRKVYWGFAP NENLSNEELV RENYQGIRPA PGYPACPEHT EKGQIWQLLD VETHTGMKLT ESYAMWPGAS VSGWYFSHPD SKYFAVAQIQ RDQVEDYAAR KGMPVAEVER WLAPNLGYDA D // ID C4TZC0_YERKR Unreviewed; 989 AA. AC C4TZC0; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 01-APR-2015, entry version 34. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEP90438.1}; GN ORFNames=ykris0001_24100 {ECO:0000313|EMBL:EEP90438.1}; OS Yersinia kristensenii ATCC 33638. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=527012 {ECO:0000313|EMBL:EEP90438.1}; RN [1] {ECO:0000313|EMBL:EEP90438.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33638 {ECO:0000313|EMBL:EEP90438.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; ACCA01000024; EEP90438.1; -; Genomic_DNA. DR EnsemblBacteria; EEP90438; EEP90438; ykris0001_24100. DR PATRIC; 26387430; VBIYerKri124070_3220. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 10 10 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 73 73 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 74 74 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 521 521 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 989 AA; 109692 MW; 7DF2703D79E6C9E0 CRC64; MKPLSFGLNC ALGPDELRQY VAELSRISEY YVSAHPNAGL PNAFGEYDLE AKEMAEQIGE WARAGFLNIV GGCCGTTPRH IAAMVKAVAG VAPRPLPDIP VACRLAGLEP LTIDANTLFV NVGERTNVTG SARFKRLIKE EKYDEALDVA RQQVESGAQI IDINMDEGML DAEAAMVRFL NLIAGEPDIA RVPIMIDSSK WDVIEKGLKC IQGKGIVNSI SMKEGEAAFI HHAKLVRRYG AAMVVMAFDE TGQADTRARK IEICRRAYKI LTETVGFPPE DIIFDPNIFA VATGIEEHNN YAVDFIEACA DIKAELPHAM ISGGVSNVSF SFRGNDPVRE AIHAVFLYYA IRNGMDMGIV NAGQLAIYDD LSDELRDAVE DVILNRRDDS TERLLDLAEK YRSSKSGEVA IQQAEWRGWA VGKRLEYSLV KGITEFIELD TEEARQQADR PIEVIEGPLM AGMNVVGDLF GEGKMFLPQV VKSARVMKQA VAYLEPYIEA SKQKGTTAGK ILLATVKGDV HDIGKNIVGV VLQCNNYEII DLGVMVPTEK ILRTAREEKV DIIGLSGLIT PSLDEMVNVA KEMERQGFTL PLLIGGATTS KAHTAVKIEQ NYSGSTTYVS NASRSVGVVS ALLSDTQRDD FIAKTRKEYE TVRIQHARKK PRTPPVSLQT ARANQTVIDW ANYTPPVAHK LGVQAVEASI ETLRNYIDWT PFFMTWALAG KYPRILEDEV VGEEAKRLFA DANEMLDKLS AEDLLHPKGV VGLFPANSVG DDIEIYRDER RDEVLVVSHH LRQQTEKTDF PNYCLADYIA PKSSGKADYY GAFAVTGGLE EDALAEAYDA QHDDYNKIMI KALSDRLAEA FAEYLHERVR KVYWGFSPNE NLSNEELVRE NYQGIRPAPG YPACPEHTEK GQIWQLLDVE THTGMKLTES YAMWPGASVS GWYFSHPDSK YFAVAQIQRD QVEDYAARKG MPVSEVERWL APNLGYDAD // ID C4TZC1_YERKR Unreviewed; 251 AA. AC C4TZC1; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 29-OCT-2014, entry version 21. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEP90439.1}; GN ORFNames=ykris0001_24110 {ECO:0000313|EMBL:EEP90439.1}; OS Yersinia kristensenii ATCC 33638. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=527012 {ECO:0000313|EMBL:EEP90439.1}; RN [1] {ECO:0000313|EMBL:EEP90439.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33638 {ECO:0000313|EMBL:EEP90439.1}; 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACCA01000024; EEP90439.1; -; Genomic_DNA. DR EnsemblBacteria; EEP90439; EEP90439; ykris0001_24110. DR PATRIC; 26387432; VBIYerKri124070_3221. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 251 AA; 28136 MW; A4470C073CFBC419 CRC64; MRQIMARQQG KEATVVDTVT NNKVKELHQQ LAQRILVLDG GMGTMIQSYR LEEEDYRGAR FADWPSDLKG NNDLLVLSKP EVIIAIHNAY LEAGADILET NTFNSTTIAM ADYQMESLSA EINYEAARLA RICADEWTAR TPEKPRYVAG VLGPTNRTAS ISPKVNDPAF RNVSFDQLVE AYRESTRALI EGGVDLIMIE TVFDTLNAKA ATFAVESEFE AMGGAVAGDD FRHHYRCIWP DFIRPNHRSF L // ID C4UDY5_YERAL Unreviewed; 1251 AA. AC C4UDY5; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 27-MAY-2015, entry version 35. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEP93801.1}; GN ORFNames=yaldo0001_37630 {ECO:0000313|EMBL:EEP93801.1}; OS Yersinia aldovae ATCC 35236. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=527002 {ECO:0000313|EMBL:EEP93801.1}; RN [1] {ECO:0000313|EMBL:EEP93801.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35236 {ECO:0000313|EMBL:EEP93801.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; ACCB01000057; EEP93801.1; -; Genomic_DNA. DR RefSeq; WP_004705327.1; NZ_ACCB01000057.1. DR EnsemblBacteria; EEP93801; EEP93801; yaldo0001_37630. DR PATRIC; 26362242; VBIYerAld45352_3869. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 272 272 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 335 335 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 336 336 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 783 783 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1251 AA; 138551 MW; 93D699E104920F4E CRC64; MHRVMARQQG KEAAVVDTVI SNRAFTKENV KELHQQLAQR ILVLDGGMGT MIQSYKLEEE DYRGARFADW PSDLKGNNDL LVLSQPDVII AIHNAYLEAG ADILETNTFN STPIAMADYQ MELLSAEINY EAARLARICA DEWTARTPDK PRYVAGVLGP TNRTASISPK VNDPAFRNVS FDQLVEAYRE STRALIEGGV DLIMIETVFD TLNAKAATFA VESEFEAMGV LLPVMISGTI TDASGRTLSG QTTEAFYNSL RHVNPLSFGL NCALGPDELR QYVAELSRIS EYYVSAHPNA GLPNAFGEYD LEAKEMADQI GEWARAGFLN IVGGCCGTTP RHIAAMVKAV AGVPPRQLPD IPVACRLAGL EPLTIDANSL FVNVGERTNV TGSARFKRLI KEDKYDEALD VARQQVESGA QIIDINMDEG MLDAEAAMVR FLNLIAGEPD IARVPIMIDS SKWDVIEKGL KCIQGKGIVN SISMKEGEAA FIHHAKLVRR YGAAMVVMAF DETGQADTRA RKIEICRRAY KILTETVGFP PEDIIFDPNI FAVATGIEEH NNYAVDFIEA CADIKAELPH AMISGGVSNV SFSFRGNDPV REAIHAVFLY YAIRNGMDMG IVNAGQLAIY DDLSDELRDA VEDVILNRRS DSTERLLDLA EKYRSSKSGE VAIQQAEWRG WEVKKRLEYS LVKGITEFIE RDTEEARQQA DRPIEVIEGP LMAGMNVVGD LFGEGKMFLP QVVKSARVMK QAVAYLEPYI EASKQKGTTA GKILLATVKG DVHDIGKNIV GVVLQCNNYE IIDLGVMVPT EKILRTAREE KVDIIGLSGL ITPSLDEMVN VAKEMERQGF TLPLLIGGAT TSKAHTAVKI EQNYSGSTTY VSNASRSVGV VSALLSDTQR DDFVAKTRKE YETVRIQHAR KKPRTPPVSL AAARDNHTVI DWENYTPPVA HKLGVQAVEA SIETLRNYID WTPFFMTWSL AGKYPRILAD EVVGEEAKRL LADANEMLDK LSAEGLLHPK GVVGLFPANS VGDDIEIYRD ERRDEVLVVS RHLRQQTEKT DFPNYCLADY VAPKSSGKAD YYGAFAVTGG LEEDALANAY DAQHDDYNKI MIKALSDRLA EAFAEYLHER VRKVYWGFAP HENLTNEELV RENYQGIRPA PGYPACPEHT EKGQIWQLLD VEAHTGMKLT ESYAMWPGAS VSGWYFSHPD SKYFAVAQIQ RDQVEDYAAR KGMPVAEVER WLAPNLGYDA D // ID C4ULI3_YERRU Unreviewed; 1257 AA. AC C4ULI3; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 27-MAY-2015, entry version 35. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEP98498.1}; GN ORFNames=yruck0001_1770 {ECO:0000313|EMBL:EEP98498.1}; OS Yersinia ruckeri ATCC 29473. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=527005 {ECO:0000313|EMBL:EEP98498.1}; RN [1] {ECO:0000313|EMBL:EEP98498.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29473 {ECO:0000313|EMBL:EEP98498.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; ACCC01000029; EEP98498.1; -; Genomic_DNA. DR RefSeq; WP_004721445.1; NZ_ACCC01000029.1. DR EnsemblBacteria; EEP98498; EEP98498; yruck0001_1770. DR PATRIC; 31313715; VBIYerRuc77443_2397. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 278 278 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 341 341 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 342 342 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 789 789 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1257 AA; 139234 MW; B430E1416D97C7C6 CRC64; MLAFAAIPIG WTALKYWLGR YLAGHSGEEA TVTNRVEKLH QQLAERILVL DGGMGTMIQS YRLEEADYRG ARFADWPSDL KGNNDLLVLS KPEVITAIHN AYLEAGADIL ETNTFNSTTI AMADYQMESL SAEINYEAAR LARLCADEWT ARTPDKPRYV AGVLGPTNRT ASISPKVNDP AFRNVSFDQL VEAYRESTRA LVEGGVDIIM IETVFDTLNA KAATFAVESE FEALGVMLPV MVSGTITDAS GRTLSGQTTE AFYHSLRHVK PLSFGLNCAL GPDELRQYIA ELSRISECYV SAHPNAGLPN AFGEYDLEAK EMAEQIGEWA RAGFLNIVGG CCGTTPRHIA AMVKAVAGVP PRPLPKIPVA CRLAGLEPLT IDASTLFVNV GERTNVTGSA RFKRLIKEEK YDEALDVARQ QVESGAQIID INMDEGMLDA EAAMVRFLNL IAGEPDIARV PIMIDSSKWD VIEKGLKCIQ GKGIVNSISM KEGEAAFIHH ARLVRRYGAA MVVMAFDEAG QADTRARKIE ICRRAYKILT ETVGFPPEDI IFDPNIFAVA TGIEEHNNYA VDFIEACADI KAELPHAMIS GGVSNVSFSF RGNDPVREAI HAVFLYYAIR NGMDMGIVNA GQLAIYDDLS DELRDAVEDV VLNRRDDSTE RLLDLAEKYR GSKSDEVAVL QAEWRGWPVA KRLEYSLVKG ITEFIELDTE EARQEATRPI EVIEGPLMAG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPYIEASK QRGTTAGKIL LATVKGDVHD IGKNIVGVVL QCNNYEIIDL GVMVPTEKIL RTAREENVDI IGLSGLITPS LDEMVNVAKE MERQGFTLPL LIGGATTSKA HTAVKIEQNY SGSTTYVSNA SRSVGVVSAL LSDTQRDEFI AKTRKEYETV RIQHARKKPR TPPVSLQAAR DNHTAIEWEN YTPPVAHKLG IQAVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEIVG EEARRLFADA NQMLDKLSAE DLLHPKGVVG LFPANRVGDD IEIYRDERRD EVLVVSHHLR QQTEKTDYPN YCLADYVAPK SSGKVDYLGA FAVTGGLEED ALADAYDAQH DDYNKIMIKA LSDRLAEAFA EYLHERVRKV YWGFAPNENL SNEELVRENY QGIRPAPGYP ACPEHTEKGQ IWQLLDVETH TGMKLTESYA MWPGASVSGW YFSHPDSKYF AVAQIQRDQV EDYAARKGMP LGEVERWLAP NLGYDAD // ID C4V3M8_9FIRM Unreviewed; 349 AA. AC C4V3M8; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEQ48642.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EEQ48642.1}; GN Name=mmuM {ECO:0000313|EMBL:EEQ48642.1}; GN ORFNames=HMPREF0908_1122 {ECO:0000313|EMBL:EEQ48642.1}; OS Selenomonas flueggei ATCC 43531. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Selenomonas. OX NCBI_TaxID=638302 {ECO:0000313|EMBL:EEQ48642.1}; RN [1] {ECO:0000313|EMBL:EEQ48642.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43531 {ECO:0000313|EMBL:EEQ48642.1}; 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 (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. {ECO:0000313|EMBL:EEQ48642.1}. 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; ACLA01000014; EEQ48642.1; -; Genomic_DNA. DR RefSeq; WP_006689856.1; NZ_GG694006.1. DR EnsemblBacteria; EEQ48642; EEQ48642; HMPREF0908_1122. DR PATRIC; 25816946; VBISelFlu67833_1017. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEQ48642.1}; KW Transferase {ECO:0000313|EMBL:EEQ48642.1}. SQ SEQUENCE 349 AA; 37552 MW; 149D17DF2EADD96A CRC64; MGCVPRAGGH FLAWRDGMNV LEVRLAAQDV LVLDGALATE LEARGFSVDD PLWSAKALFE RPDLVRDIHL DYLRAGADVL TSASYQATVD GFMQRGFTAE EAAELLRRSV RLAQEARGLY RAERSTGTAV PLVAASVGPY GAYLADGSEY RGDYDVEEDA LTAFHAQRLR ILASAAPDLL ACETLPCLHE ACAIVRSLRA EGIRIPAYFS FSCRDGAHIS DGTEIAECAR VLDAVPEAAA IGVNCTAPQY VSGLIRMIRQ ETDKPIVVYP NSGEYYDAAA RVWRGAAEDF GARSREYAAA GARIIGGCCR TTPHDTAAIA AWVKAGRKRG DGDGDRVRGG SSARRTRHA // ID C4V5G0_9FIRM Unreviewed; 595 AA. AC C4V5G0; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 27-MAY-2015, entry version 28. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HMPREF0908_1754 {ECO:0000313|EMBL:EEQ47937.1}; OS Selenomonas flueggei ATCC 43531. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Selenomonas. OX NCBI_TaxID=638302 {ECO:0000313|EMBL:EEQ47937.1}; RN [1] {ECO:0000313|EMBL:EEQ47937.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43531 {ECO:0000313|EMBL:EEQ47937.1}; 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 (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEQ47937.1}. 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; ACLA01000029; EEQ47937.1; -; Genomic_DNA. DR RefSeq; WP_006690882.1; NZ_GG694008.1. DR ProteinModelPortal; C4V5G0; -. DR EnsemblBacteria; EEQ47937; EEQ47937; HMPREF0908_1754. DR PATRIC; 25818994; VBISelFlu67833_1484. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EEQ47937.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EEQ47937.1}. SQ SEQUENCE 595 AA; 64257 MW; 184EE9C62771BE72 CRC64; MDMAQERVDI RGHIKKEPLI FDGGMGTYYA QKTHTRGKGV ELANIETPIV VEGIHTEYLR AGAQAIKTNT FAANRIVYQG EEALVQGILR TGWELAARAA ESFGAYVFAD IGPVAGLPPA DIAEEYRFLS DTFLALGAKN FLFETNSSME GLVETAAHIK QIVPDAFVLT SFAALSGGYT RDGLFVEELI RTAAESGYID AVGFNCVSGV QSMKELVHLI GTCPLPLSLM PNAGHPIVID GRTFYESAPD YFGKGLAAIV REGVSIAGGC CGTTPEHIRA LCKALEGGTA AEGERVRQER TELTPSRSPF FEALKAGEIP IAVELDPPDT GNADKFMAGA RELQAAGVHA ITIADNPIAR ARMDAAMLAG RVRRSLGIEP IPHMTCRDRN LNAIKSILLG LSAEGIHNMI AITGDPIPTA ERDEVKSVYQ FNSRKLSAFI KSLGERGDVI PFHVFGALNV NAKHFPSQLG LAKKKMEAGM TGFFTQPVLS AQAKENLRTA RDTLPGALIL GGIMPVVSER NARFMESEIT GIHVEERIIN AYHGLDREAA EELAVELSLG IARDIKPYID GYYIITPFSR TALVARIAAA MMKRQ // ID C4V5G1_9FIRM Unreviewed; 798 AA. AC C4V5G1; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEQ47938.1}; DE Flags: Fragment; GN ORFNames=HMPREF0908_1755 {ECO:0000313|EMBL:EEQ47938.1}; OS Selenomonas flueggei ATCC 43531. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Selenomonas. OX NCBI_TaxID=638302 {ECO:0000313|EMBL:EEQ47938.1}; RN [1] {ECO:0000313|EMBL:EEQ47938.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43531 {ECO:0000313|EMBL:EEQ47938.1}; 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 (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. {ECO:0000313|EMBL:EEQ47938.1}. 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; ACLA01000029; EEQ47938.1; -; Genomic_DNA. DR RefSeq; WP_006690883.1; NZ_GG694008.1. DR EnsemblBacteria; EEQ47938; EEQ47938; HMPREF0908_1755. DR PATRIC; 25818996; VBISelFlu67833_1485. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEQ47938.1}; KW Transferase {ECO:0000313|EMBL:EEQ47938.1}. FT NON_TER 1 1 {ECO:0000313|EMBL:EEQ47938.1}. SQ SEQUENCE 798 AA; 85484 MW; ACC8F02838CAC6B7 CRC64; IILDGGMGTQ LQARGLAPGE RPELFGLTHP DVIEEIHRNY IAAGSRVIYS NTFGANAHKL EGTGKTVAEV IGENVRTARR AAENSGTQGV RVALDIGPIG ELVEPLGTLS FEAAYELFRE MVAAGEEAGA DLVIFETLTD LYEVKAAVLA AKEHTKLPIW VTMTFEQNGR TFLGAAVPSV AVTLDALGVA ALGVNCSLGP VELVPIVDEL MEWTDLPIIV KPNAGLPDPR TGAYEMTAED FGREMTVFAQ RGALIMGGCC GTTPDFIRAL TAAVAAGAAD RPVRTKRKGI ASPGRVAEYG KLNVIGERIN PTGKKRLQQA LLEEDYGYIK KLAISQQEAG AQVLDINVGA QGVDEEKIIP YVVKAVQSVV DLPLQIDSAN PKVIEAALRV TNGRVIINSV SGERERMDAV FPLAKHYGAA VLGLAMDEKG LPETAAQRVA VAERIVAEAE KYGLEREDII IDCLTLTVSA QQAQAMETLR AVREVHERLG LHCALGVSNI SFGLPARGHM TENFLIQAMH VGLDFPIINP NTKGVMDAVV SFRAVSGEDA DCAAYIERFA PEQAEMRRRK ELGITGEEAA GAVQTASAER TDVVDPLMDA IIRGLSDDAE RITRKLLTEM APMDIIQEKV IPALDIVGDR YEKEIIFLPQ LINAANAATA GLELIKVRLA EEGQGVSKGK IILATVEGDI HDIGKNIVKV VLENYGYQII DLGRDVPVQR VVEVAIEKKV GLIGLSALMT TTVTAMKKTI EALHEAGLSC ETVVGGAVLT EDYAKEIGAD YYAGDARSIV EIARRVLG // ID C4WBD2_STAWA Unreviewed; 612 AA. AC C4WBD2; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 27-MAY-2015, entry version 28. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=STAWA0001_2461 {ECO:0000313|EMBL:EEQ79731.1}; OS Staphylococcus warneri L37603. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=596319 {ECO:0000313|EMBL:EEQ79731.1}; RN [1] {ECO:0000313|EMBL:EEQ79731.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=L37603 {ECO:0000313|EMBL:EEQ79731.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEQ79731.1}. 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; ACPZ01000041; EEQ79731.1; -; Genomic_DNA. DR RefSeq; WP_002451530.1; NZ_ACPZ01000041.1. DR ProteinModelPortal; C4WBD2; -. DR EnsemblBacteria; EEQ79731; EEQ79731; STAWA0001_2461. DR PATRIC; 31411884; VBIStaWar127182_1437. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EEQ79731.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EEQ79731.1}. SQ SEQUENCE 612 AA; 67968 MW; 8D865A1A01F7C408 CRC64; MSQFLNKLQN NVLVADGAIG TIFYSEGLDT CPEAYNLTHP EKVERIHRSY IDAGADVIQT NTYGANFEKL KAFGLEHKVK EIHKAAVQIA KKAANEDTFI LGTVGGFRGV KQDDLSLSTI QYHTEHQIDT LVDEGVDALL FETYYDLEEL KGIVVSTKRK HHIPIIAQLT ASNTNYLVDG TPINDALKQL VECGADIVGF NCHHGPHHMQ RSFSHIELPD KAFLSCYPNA SLLDIENSEF KYSDNAQYFG DVAQELINEG VRLIGGCCGT TPEHIRYIKT SVKNLRPVAH KNVIPINKKV NRKKDLNSKQ SLTSKVKQGP TVIVELDTPK HLDTDQFFNN IGKLDGADID AVTLADNSLA TVRVSNIAAA SIIKQRFNIE PLVHITCRDR NLIGLQSHLL GLSLIGVNEI LAITGDPSKV GHLPGATNVY DVNSKGLTEI ALRFNQGINT DGDALKKHTN FNIAGAFDPN VRKLDGAVKR LEKKVASGMS YFITQPVYSK EKIKQVYEAT KHLNTPFFIG IMPIASYNNA LFLHNEVPGI KMSEEVLNQF KAVKDDKEKT KELSLRLSKE LIDTVHEYFN GLYIITPFQK VDYSLELAAY SKSITTHKEA IL // ID C4WH05_9RHIZ Unreviewed; 1264 AA. AC C4WH05; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 27-MAY-2015, entry version 37. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEQ94869.1}; DE EC=1.1.1.133 {ECO:0000313|EMBL:EEQ94869.1}; GN Name=metH {ECO:0000313|EMBL:EEQ94869.1}; GN ORFNames=OINT_1000202 {ECO:0000313|EMBL:EEQ94869.1}; OS Ochrobactrum intermedium LMG 3301. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Ochrobactrum. OX NCBI_TaxID=641118 {ECO:0000313|EMBL:EEQ94869.1}; RN [1] {ECO:0000313|EMBL:EEQ94869.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 3301 {ECO:0000313|EMBL:EEQ94869.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEQ94869.1}. 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; ACQA01000001; EEQ94869.1; -; Genomic_DNA. DR RefSeq; WP_006465913.1; NZ_ACQA01000001.1. DR EnsemblBacteria; EEQ94869; EEQ94869; OINT_1000202. DR PATRIC; 28504598; VBIOchInt64846_0209. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008831; F:dTDP-4-dehydrorhamnose reductase activity; IEA:UniProtKB-EC. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Oxidoreductase {ECO:0000313|EMBL:EEQ94869.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 263 263 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 326 326 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 327 327 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 784 784 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1264 AA; 138493 MW; D877603E778AA68B CRC64; MASSLEGLFG ATAAQPDGSE VLAALTKAAR ERILILDGAM GTQIQGLGFH EEHFRGERFG ACDCQLQGNN DLLTLTQPKA IEEIHYAYAI AGADILETNT FSSTRIAQAD YGMEDQVYEL NRDGARLARR AALRAEQKDG RRRFVAGALG PTNRTASLSP DVNNPGFRAV TFDDLRIAYA EQIRGLIDGG SDIILIETIF DTLNAKAAVF ACEEVFAEKG IFLPVMISGT ITDLSGRTLS GQTPTAFWHS LRHAKPFTIG LNCALGANAM RAHLDELSSI ADTFVCAYPN AGLPNEFGQY DETPEAMAAQ IEGFARDGLV NVVGGCCGST PEHIRAIAEA VAKHPPRKPV KVAPLMRLSG LEPFTLTKDI PFVNVGERTN VTGSARFRKL IKAGDFSAAL DVARDQVANG AQIIDINMDE GLIDSEKAMV EFLNLIAAEP DIARVPIMID SSKWEVIEAG LKCVQGKAVV NSISMKEGEE AFIHHARLVR AYGAAVVVMA FDETGQADTE ARKVEICTRA YKILTEQVGF APEDIIFDPN IFAVATGIEE HNNYGVDFIE ATRQIIATLP HVHVSGGVSN LSFSFRGNEP VREAMHAVFL YHAIQAGMDM GIVNAGQLAV YDTIDPELRE ACEDVVLNRR SDSTERLLEI AERFRDSGSK EAKAQDLTWR EWPVEKRLEH ALVNGITEYI EADTEEARQS AERPLHVIEG PLMAGMNVVG DLFGAGKMFL PQVVKSARVM KQAVAVLLPY MEEEKRLNAE NGIGGGERQS AGKVLMATVK GDVHDIGKNI VGVVLACNNY EIIDLGVMVP SQKILQVARD EKVDVIGLSG LITPSLDEMV HVAAEMEREG FDIPLLIGGA TTSRVHTAVK IHPRYERGQA VYVIDASRAV GVVSSLLSPE GKKAYIDGLR GEYAKVAAAH ARNEAEKQRL PLARARANAH KLDWESFVPT KPTFTGTRTF DDYDLTEIAR YIDWTPFFQT WELKGRYPAI LEDEKQGEAA RQLWADAQAM LKKIIDEKWF TPKAVVGFWP ANAAGDDIRL FTDESRKQEL ATFFTLRQQL SKRDGRPNVA MSDFVAPVES GKQDYVGGFV VTAGIGEVAI AERFERANDD YSAILVKALA DRFAEAFAEL MHERVRKEFW AYASDETYTP EELIGEPYKG IRPAPGYPAQ PDHTEKTTLF RLLDATANTG VELTESYAMW PGSSVSGLYI GHPESYYFGV AKVERDQVED YAARKGMAVE EVERWLGPIL NYLPGAGKDE DAAA // ID C4WWI3_ACYPI Unreviewed; 199 AA. AC C4WWI3; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 01-OCT-2014, entry version 17. DE SubName: Full=ACYPI009247 protein {ECO:0000313|EMBL:BAH72253.1}; GN Name=ACYPI009247 {ECO:0000313|EMBL:BAH72253.1}; OS Acyrthosiphon pisum (Pea aphid). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Paraneoptera; Hemiptera; Sternorrhyncha; OC Aphidiformes; Aphidoidea; Aphididae; Macrosiphini; Acyrthosiphon. OX NCBI_TaxID=7029 {ECO:0000313|EMBL:BAH72253.1}; RN [1] {ECO:0000313|EMBL:BAH72253.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=LSR1 {ECO:0000313|EMBL:BAH72253.1}; RC TISSUE=Whole body {ECO:0000313|EMBL:BAH72253.1}; RA Shigenobu S., Nakabachi A., Richards S.; RT "A full-length cDNA resource of the pea aphid, Acyrthosiphon pisum."; 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; AK342079; BAH72253.1; -; mRNA. DR HOGENOM; HOG000265278; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; SQ SEQUENCE 199 AA; 22530 MW; 0823E0D00030AB1F CRC64; MQDSTVLNMK MYLLDGSFIS GILPYVEYDS VMKHPLWGSN LIFNNEEAVV KAHRDYIRAG AEFLTTNTYQ ASIEGFQKYL NLNYDQSFQL IKKSVTICRR AIMEESSGRT IRIMGSVGPY GASLCDGSEY NGNYIGKIDS KDLYDWHKPR IQALVEAGVD VVLFETIPSI IEANILLNIL AEYPIKKHAC RSRVRTVNT // ID C4XS82_DESMR Unreviewed; 805 AA. AC C4XS82; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 27-MAY-2015, entry version 44. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:BAH75604.1}; GN Name=metH {ECO:0000313|EMBL:BAH75604.1}; GN OrderedLocusNames=DMR_21130 {ECO:0000313|EMBL:BAH75604.1}; OS Desulfovibrio magneticus (strain ATCC 700980 / DSM 13731 / RS-1). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=573370 {ECO:0000313|EMBL:BAH75604.1, ECO:0000313|Proteomes:UP000009071}; RN [1] {ECO:0000313|EMBL:BAH75604.1, ECO:0000313|Proteomes:UP000009071} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700980 / DSM 13731 / RS-1 RC {ECO:0000313|Proteomes:UP000009071}; 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 ----------------------------------------------------------------------- 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; BAH75604.1; -; Genomic_DNA. DR RefSeq; WP_015860790.1; NC_012796.1. DR RefSeq; YP_002953490.1; NC_012796.1. DR STRING; 573370.DMR_21130; -. DR EnsemblBacteria; BAH75604; BAH75604; DMR_21130. DR KEGG; dma:DMR_21130; -. DR PATRIC; 21750503; VBIDesMag26496_2021. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; DMAG573370:GHJL-2136-MONOMER; -. DR Proteomes; UP000009071; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009071}; KW Reference proteome {ECO:0000313|Proteomes:UP000009071}. SQ SEQUENCE 805 AA; 83810 MW; 4F5A82119FDCFE81 CRC64; MGDFRKALAD DTLLLFDGAM GTLLQGRGLS AGQSPELFGL TNPDAIIGAH RDYVQAGSRV ITTNTFGGSR YKLPAGTDVA GLNREMARLA RQAAGPGVFV AGSVGPTGHF VAPLGKASLR DLVEAFAEQI RGLAEGGCDL IIGETHFDLA EAKAVILACR QVCSLPVAMC MTFEGAASLT GSSPEVFADA MENLGVALIG VNCGQGPDDM RLVGEAFSRR LKTPFFVKPN AGMPRLENGR TVFPMGPDEF AEKTARFVDL GAKALSGCCG TTPAHIAALG AALAPRSWKR VDTPDRPVLA VTSRSMVVPI GGGAPLAVIG ERINPTGKAE LAAELAAGEF AKALHFAEEQ TAAGAHILDV NVGAPMVDET AVLPGLALEL VKRQQLPLCL DSNNIDALTA GLWAYPGTPL VNSISGEPGR MERLGPVCRD HGAPFILLPL KGRKLPVSAA ERLAIIEELL LQAEALGIPR RLILVDALAL TVSSKPEAAL ACLEVIRTCR DKWGLPTVLG LSNISFGLPG RELVNSAFFA MCLGAGMAAA IANPNVPRLM ETLAAGEVLM GRDPQAGRYI AGYAGWKPSS GGGNGSPSGP ASGGADDGQS PLRRAVVYGR REEVLERIEK ALAEGADAAT LLGEELIPGI MSVGERYERK EFYLPQLLAA AEAMRAGFTR LEPLLTEAGA AAKARIVMAT VEGDIHDIGK NIVCLMLKNH GFEVIDLGKD VPAARIVEAA EEHKAAVIGL SALMTTTMVR MEDTVRLLRD KGLAIPVMVG GAVVTEAFAK SIGAAAYAAD AVDAVRQAKA LAGGA // ID C4XYV2_CLAL4 Unreviewed; 329 AA. AC C4XYV2; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 01-APR-2015, entry version 27. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EEQ37002.1}; GN ORFNames=CLUG_01125 {ECO:0000313|EMBL:EEQ37002.1}; 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 {ECO:0000313|EMBL:EEQ37002.1, ECO:0000313|Proteomes:UP000007703}; RN [1] {ECO:0000313|Proteomes:UP000007703} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 42720 {ECO:0000313|Proteomes:UP000007703}; 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; CH408076; EEQ37002.1; -; Genomic_DNA. DR RefSeq; XP_002619966.1; XM_002619920.1. DR GeneID; 8499765; -. DR KEGG; clu:CLUG_01125; -. DR InParanoid; C4XYV2; -. DR KO; K00547; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000007703; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007703}; KW Reference proteome {ECO:0000313|Proteomes:UP000007703}. SQ SEQUENCE 329 AA; 36272 MW; 0CFE282172056F39 CRC64; MSFKEALKKS VLVQDGALGT QLEALIPLDD PHSVKGSPLW STNALLYSPE LISSIHKQYV EAGADMIITA TYQASPQTLS KYENMDLAQA KKVWTKSVEC ALEATRTHPE KKIFIGGSIG PYGAYLANGA EYSGDYGDIS SDQLMDYHRD IVRFYAETKE VDVIAFETVP NFAEVQAIFS LIEQMFNANL HKEFYVSLSC KDADHLVDGT PLEQVIRYIL SKKSSQISDN LVGIGCNCVP FEIVSDFIET VNRVCQNNGS EQLSLLVYPN LGFEPTDTAN YAFRSSTEKW ASSVAKWALY SNVRVIGGCC STGPAEIAQI KDVVEKIKS // ID C4YDJ0_CANAW Unreviewed; 311 AA. AC C4YDJ0; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 07-JAN-2015, entry version 24. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EEQ42376.1}; GN ORFNames=CAWG_00585 {ECO:0000313|EMBL:EEQ42376.1}; OS Candida albicans (strain WO-1) (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Debaryomycetaceae; OC Candida/Lodderomyces clade; Candida. OX NCBI_TaxID=294748 {ECO:0000313|EMBL:EEQ42376.1, ECO:0000313|Proteomes:UP000001429}; RN [1] {ECO:0000313|Proteomes:UP000001429} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WO-1 {ECO:0000313|Proteomes:UP000001429}; 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; CH672346; EEQ42376.1; -; Genomic_DNA. DR HOGENOM; HOG000265278; -. DR OMA; SSVEGFM; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000001429; Chromosome 1, Supercontig 1.1. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001429}; KW Reference proteome {ECO:0000313|Proteomes:UP000001429}. SQ SEQUENCE 311 AA; 34314 MW; 3FFECAC35FD4C02D CRC64; MGRVQDILEK RKLVIDGALG TELERLLPTT STYLPSGSPL WSGQVLITNP ELVEQVHLDY INAGADMIIT STYQTSYASL HKYIGYDMDQ AIALWNSALN VAKNAVKKSG RDDVIIAGSI GPYATLLANG SEYNGDYQGV TDEELIEYHT PLFEFYENSD VDIICIETIP SFQELKVIIG LAKKYTSKEF FISINPQTGS ALSDGTSLIE VAQLFAEIND PRFVAVGINC TSYENVDQIS TYLTDFPLFI YPNLGFVYDT TVHKFVSKAL QESTWSKSVA KWLAFPNVKA IGGCCSTTPA EIKQVAQLIN Q // ID C4Z117_EUBE2 Unreviewed; 595 AA. AC C4Z117; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 27-MAY-2015, entry version 41. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=EUBELI_01283 {ECO:0000313|EMBL:ACR72280.1}; OS Eubacterium eligens (strain ATCC 27750 / VPI C15-48). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium. OX NCBI_TaxID=515620 {ECO:0000313|EMBL:ACR72280.1, ECO:0000313|Proteomes:UP000001476}; RN [1] {ECO:0000313|EMBL:ACR72280.1, ECO:0000313|Proteomes:UP000001476} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27750 / VPI C15-48 {ECO:0000313|Proteomes:UP000001476}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ACR72280.1; -; Genomic_DNA. DR RefSeq; WP_012739515.1; NC_012778.1. DR RefSeq; YP_002930727.1; NC_012778.1. DR ProteinModelPortal; C4Z117; -. DR STRING; 515620.EUBELI_01283; -. DR EnsemblBacteria; ACR72280; ACR72280; EUBELI_01283. DR KEGG; eel:EUBELI_01283; -. DR PATRIC; 21865718; VBIEubEli113401_1211. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; EELI515620:GH1N-1283-MONOMER; -. DR Proteomes; UP000001476; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001476}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ACR72280.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000001476}; KW Transferase {ECO:0000313|EMBL:ACR72280.1}. SQ SEQUENCE 595 AA; 65700 MW; 8BDFF7874FA4B4FD CRC64; MKYTGTAGIL YDRLKSEILV ADGAFGTYYA KKYDTGSLPE LANLQASDRV LAIHKEYIEA GAKIIRTNTF ASNTVCLGAG FDEVRNNIKN AVDIAREAVK GTDVLVAADI GPIPGENMIE KEHIEKEYVD IVNVFKECGV DIFVFETFPE LGFIDKAIEN AGENGFVITQ FAINQFGYSS AGFSARKLIE EAGKNSYIDA CGFNCGVGPG HMKKLVQSLI NRNDKYFAVL PNAGYPQVVS GRMVFDDNNA AYFSQIMHDL AEDGADIIGG CCGTTPEYIR QMVLKTADVV HMKNASIEEE ISEKKTANDV SFYKGKEGRK LIAVELAPPL GIDDEKIMDA AFLMKESGVD VLTFPDSPSG RTRADSILMA EKVSRETGMC VMPHICCRDK NAIAMRSQLL GAHINDINNF LVITGDPIPS VVRASVKSVF NFDSVGLMNI ISDMNQEQFA GKPVIYGGAI NQGRVNFKVE LERVKKKMEA GATFFMTQPV FSDEDIDRLR QIKEQTGARI LCGIMPFVSL RNATFMKNEM TGINVTDEIL SRYRADMSKE EGEETGIQIA REIIAKTTDF VDGYYFSFPF NRVHMLKKII GKNNQ // ID C4Z1L6_EUBE2 Unreviewed; 801 AA. AC C4Z1L6; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 27-MAY-2015, entry version 39. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:ACR72377.1}; GN OrderedLocusNames=EUBELI_01382 {ECO:0000313|EMBL:ACR72377.1}; OS Eubacterium eligens (strain ATCC 27750 / VPI C15-48). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium. OX NCBI_TaxID=515620 {ECO:0000313|EMBL:ACR72377.1, ECO:0000313|Proteomes:UP000001476}; RN [1] {ECO:0000313|EMBL:ACR72377.1, ECO:0000313|Proteomes:UP000001476} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27750 / VPI C15-48 {ECO:0000313|Proteomes:UP000001476}; 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; ACR72377.1; -; Genomic_DNA. DR RefSeq; WP_012739612.1; NC_012778.1. DR RefSeq; YP_002930824.1; NC_012778.1. DR STRING; 515620.EUBELI_01382; -. DR EnsemblBacteria; ACR72377; ACR72377; EUBELI_01382. DR KEGG; eel:EUBELI_01382; -. DR PATRIC; 21865910; VBIEubEli113401_1306. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; EELI515620:GH1N-1382-MONOMER; -. DR Proteomes; UP000001476; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001476}; KW Methyltransferase {ECO:0000313|EMBL:ACR72377.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001476}; KW Transferase {ECO:0000313|EMBL:ACR72377.1}. SQ SEQUENCE 801 AA; 86704 MW; 80766FF1F5510B50 CRC64; MADRFRELLK NRDYIIFDGA MGTMLQAAGM KMGETPEVLN ITRPELLVSI AEQYFNAGSD VVYANTFGAN RYKLEECGKS VEELVTAGIV NAKKARDAVK PDGLVALDVG PIGQLLEPTG VLSFEEAYDM YAEIVKAGAA AGADLVVFET MTDLLDVKAA VLAAKENSDL PIAATMTFEQ NMRTFTGCSI SAMALTLTGL GVDALGVNCS LGPKELEPVI EELVKWTNLP IIVKPNAGLP DPETNLYNVT AVQFADFMKD LRKYGIKIFG GCCGTNPEFI KELSEMLKRE GNPAAPHKYI PGAVCSATST VVVDEPRIIG ERINPTGKKL FKEALLRHDM DYILGQALEQ ISGGADILDV NVGLPGIDER EMMIDTIKSL QAVVDVPLQI DSTIPEVLEA ALRVYNGKPL VNSVNGEEES LNNVLPLVKK YGAGVIGLAL DKDGIPKKAE DRVAIAKKIM DRAVAMGIPK EDIYIDCLTL TASAEQEGVM ETLNALHTVK NELGLKTVLG VSNISFGLPN RVLVNHIFLT MALTNGLDLA IINPNIPEMT GAVRAYKLLA NIDKNSVDYI KNYGAMPNVS KIDPVKKEKK DGNYTGDDLF YAVEKGLKNE GAEITEALLK TMDSMEIVNQ VLIPALDKIG AEFEKGTLFL PQLIMAASVT QAAFEVIRKH MVMSDNAPVS KGKIVIATVK GDVHDIGKNI VKVLLENYGY DVIDLGKDVE YQTVVDAIRD NDVKLCGLSA LMTTTLVSMK ETIALIRENN LDCKVMVGGA VLTPEYAKEI DADFYAKDAK ESVDIAKRVL G // ID C4Z8W4_EUBR3 Unreviewed; 816 AA. AC C4Z8W4; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 01-APR-2015, entry version 36. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:ACR75195.1}; GN OrderedLocusNames=EUBREC_1436 {ECO:0000313|EMBL:ACR75195.1}; OS Eubacterium rectale (strain ATCC 33656 / VPI 0990). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium. OX NCBI_TaxID=515619 {ECO:0000313|EMBL:ACR75195.1, ECO:0000313|Proteomes:UP000001477}; RN [1] {ECO:0000313|EMBL:ACR75195.1, ECO:0000313|Proteomes:UP000001477} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33656 / VPI 0990 {ECO:0000313|Proteomes:UP000001477}; 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; ACR75195.1; -; Genomic_DNA. DR RefSeq; WP_012742294.1; NC_012781.1. DR RefSeq; YP_002937329.1; NC_012781.1. DR ProteinModelPortal; C4Z8W4; -. DR STRING; 515619.EUBREC_1436; -. DR EnsemblBacteria; ACR75195; ACR75195; EUBREC_1436. DR KEGG; ere:EUBREC_1436; -. DR PATRIC; 21871107; VBIEubRec107985_1214. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; EREC515619:GHMX-1430-MONOMER; -. DR Proteomes; UP000001477; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001477}; KW Methyltransferase {ECO:0000313|EMBL:ACR75195.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001477}; KW Transferase {ECO:0000313|EMBL:ACR75195.1}. SQ SEQUENCE 816 AA; 88823 MW; 5857886E4F222892 CRC64; MTREEFRKYI RENIVILDGA TGTNLMAAGM PVGVCPEEWV MEHPQVILDL QKAYVDNGTN IVYAPTFTGN RIKLLEYGLQ EKINEINTTL VGLSKQAVGD RALVAADMTM TGRQLFPLGD LMFEELLEVY KEQARILDEA GADVFVVETM MSLQECRAAV LAIKEVSDLP IMVTLTYNED GRTLFGTPPE TAVVVLQSLG VDAIGVNCST GPAEMIALVE KMAEYSTVPL IAKPNAGLPE LEDGKTVYKM TPDMFADAMR GLVKAGASIV GGCCGTTPEH IRALTEAVKT MPVHKPLEHH RRVLASERKN VEIDLDGNFT VVGERINPTG KKKLQAQLRE GKLDLVRQMA MEQETNGAGI LDINMGMNGI DEKEMMKSVI YEVSSTVDCP LCIDSSYVEV IEEALKIYPG RALINSISLE TEKMEKLLPL AAKYGAMFIL LPLSDAGLPK DVEEKKQIIN TIYDKALSLG MAHEDIVVDG LVATIGANPK AAIECYETIA YCKDEKKLPT ICGLSNISFG LPERMYVNTA FLTMAICKGL TMAIANPSQE LLMNAAFASD MLLDRPDSDI AYIERMSRLA EEKAQYETVV VKKSDNDASA SNGTCAAGSK DAVFQAVLKG NKGSIIDEVK KMLSDGAKPD EIINNSLIPA INEVGELFNQ KKYFLPQLIG SANTMKLAIE HLEPLLEKKD SGDDMPTLVI ATVEGDIHDI GKNLVVLMLK NYGYNVIDMG KDVPCEDIVN KAIETNAAVI GLSALMTTTM MRMKDVVEIC KEKGCKSKVV IGGACITQSF ADEIGADGYS KDAAECVKLV ERLLNS // ID C4ZMW7_THASP Unreviewed; 1232 AA. AC C4ZMW7; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 01-APR-2015, entry version 45. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACK53379.1}; GN OrderedLocusNames=Tmz1t_0606 {ECO:0000313|EMBL:ACK53379.1}; OS Thauera sp. (strain MZ1T). OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Rhodocyclaceae; Thauera. OX NCBI_TaxID=85643 {ECO:0000313|EMBL:ACK53379.1, ECO:0000313|Proteomes:UP000002186}; RN [1] {ECO:0000313|Proteomes:UP000002186} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MZ1T {ECO:0000313|Proteomes:UP000002186}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001281; ACK53379.1; -; Genomic_DNA. DR RefSeq; WP_012584533.1; NC_011662.2. DR RefSeq; YP_002354275.1; NC_011662.2. DR ProteinModelPortal; C4ZMW7; -. DR SMR; C4ZMW7; 659-1232. DR STRING; 85643.Tmz1t_0606; -. DR EnsemblBacteria; ACK53379; ACK53379; Tmz1t_0606. DR KEGG; tmz:Tmz1t_0606; -. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR Proteomes; UP000002186; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002186}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002186}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 770 770 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1232 AA; 133777 MW; 4FE07BFBD1DA4D54 CRC64; MQADRSIELR QLLAERILIL DGAMGTMIQQ EKLGEADYRG ERFLDHPKDL KGNNDLLVLT RPDVVAGIHR AYLEAGADLI ETNTFNATRV SQAEYGLEAL AYELNVEGAR LVRRLCDEYT AKDPARPRFC AGVLGPTSRT LSISPDVNDP GYRNISFDAL ADDYYASAKG LLEGGADILL IETIFDTLNA KAAVFAIEKL FEDLGRRWPV MISGTITDAS GRTLSGQTAE AFWNSLGHAQ PISFGLNCAL GADQLRQYVE ELSTACDTHV SAHPNAGLPN PLSPTGYDET PEHLAGQIRE WAQSGLVNIV GGCCGTTPAH IAAIAEAVRG LAPRAVPVLE KKLRLSGLEP FNVGGDSLFV NVGERTNVTG SKAFARMILE GRFDDALAVA RQQVENGAQV IDINMDEAML DSVAAMERFC KLIATEPDIS RVPIMLDSSK WSVIEAGLKC IQGKGVVNSI SMKEGEAEFL RQARLARRYG AAVIVMAFDE KGQADTFRRK TEICERAYRL LVKPVAEGGA GFPAEDIIFD PNIFAIATGI EEHDNYAVDF INAVAWIKEN LPYAKTSGGV SNVSFSFRGN DPVREAIHTV FLYHAIKAGL SMGIVNAGQL GVYDELAPEL RDKVEDVVMN RKPGAGEALV EFAQTVKGQA KESAQDLAWR EWAVEERLSH ALVKGITEFV VADTEEVRAK LEAAGKPPLA VIEGPLMAGM NVVGDLFGAG KMFLPQVVKS ARVMKQAVAH LIPYIEAEKL RTGASSKGRI VVATVKGDVH DIGKNIVGVV LGCNGYEVID LGVMVPAAKI LEAAKEHGAQ AIGLSGLITP SLEEMAHVAA EMKRQGFSVP LLIGGATTSR NHTAIKIAPH YDQPVVYVPD ASRAVGVVTA LLSEGRSEAF KAEVAADYEK IRALHANKKG MQLVSLEAAR ANAFRVASEY QPPRPNMLGV QAIDVELGEL VDYIDWGPFF QTWDLAGRFP AILDDEVVGE AARNVFADGK AMLDKIVAEE WLQAKAVFGL FPANAVGDDI ELYTGEDRKH LAMVWHGLRQ QHERPAGKPH WCLADFVAPK DSGVPDWVGA FAVTAGLGIE PRVAAFEAAH DDYHAIMLKS LADRLAEACA EWLHERVRRE CWGYAADETL DNAALIAEQY RGIRPAPGYP ACPDHTVKGP LFELLGARER IGMELTESYA MMPAAAVSGF YFAHPESHYF AISKIGRDQL EDWARRTGME VDEAARWLAP LL // ID C5ADV1_BURGB Unreviewed; 354 AA. AC C5ADV1; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 27-MAY-2015, entry version 43. DE SubName: Full=Cobalamin-dependent methionine synthase I {ECO:0000313|EMBL:ACR30291.1}; GN OrderedLocusNames=bglu_1g32280 {ECO:0000313|EMBL:ACR30291.1}; OS Burkholderia glumae (strain BGR1). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=626418 {ECO:0000313|EMBL:ACR30291.1, ECO:0000313|Proteomes:UP000002187}; RN [1] {ECO:0000313|EMBL:ACR30291.1, ECO:0000313|Proteomes:UP000002187} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGR1 {ECO:0000313|EMBL:ACR30291.1, RC ECO:0000313|Proteomes:UP000002187}; 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; CP001503; ACR30291.1; -; Genomic_DNA. DR RefSeq; WP_015877143.1; NC_012724.2. DR RefSeq; YP_002912995.1; NC_012724.2. DR STRING; 626418.bglu_1g32280; -. DR EnsemblBacteria; ACR30291; ACR30291; bglu_1g32280. DR GeneID; 7907732; -. DR KEGG; bgl:bglu_1g32280; -. DR PATRIC; 19114243; VBIBurGlu130723_6172. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; BGLU626418:GJI5-3279-MONOMER; -. DR Proteomes; UP000002187; Chromosome 1. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002187}; KW Reference proteome {ECO:0000313|Proteomes:UP000002187}. SQ SEQUENCE 354 AA; 38224 MW; ED4F6901C60799BB CRC64; MSSSPSVRPA LAASYTRGAD LPALLERRIL ILDGAMGTMI QRYKFDEAAY RGARFADFPR DIKGNNELLS LTQPDTIREI HDQYFAAGAD IVETNTFGAT AIAQADYGME HLVAEMNLAS AKLARESAQQ YSTPDKPRFV AGAIGPTPKT ASISPDVNDP GARNVTYDEL RDSYYEQAKA LLDGGVDLFL VETIFDTLNA KAALFALDQL FEDTGERLPI MISGTVTDAS GRILSGQTVE AFWNSLRHAR PLTFGLNCAL GAALMRPYIA ELAKLCDTYV SCYPNAGLPN PMAETGFDET PEVTSGLLRE FAQAGLVNLA GGCCGTTPEH IAEIAKALAD VKPRRWPSHY SEAA // ID C5AZM2_METEA Unreviewed; 1250 AA. AC C5AZM2; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 27-MAY-2015, entry version 49. DE SubName: Full=B12-dependent homocysteine-N5-methyltetrahydrofolate transmethylase {ECO:0000313|EMBL:ACS39356.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ACS39356.1}; GN Name=metH {ECO:0000313|EMBL:ACS39356.1}; GN OrderedLocusNames=MexAM1_META1p1494 {ECO:0000313|EMBL:ACS39356.1}; OS Methylobacterium extorquens (strain ATCC 14718 / DSM 1338 / AM1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=272630 {ECO:0000313|EMBL:ACS39356.1, ECO:0000313|Proteomes:UP000009081}; RN [1] {ECO:0000313|EMBL:ACS39356.1, ECO:0000313|Proteomes:UP000009081} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14718 / DSM 1338 / AM1 RC {ECO:0000313|Proteomes:UP000009081}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001510; ACS39356.1; -; Genomic_DNA. DR RefSeq; WP_012752514.1; NC_012808.1. DR RefSeq; YP_002962633.1; NC_012808.1. DR STRING; 272630.MexAM1_META1p1494; -. DR EnsemblBacteria; ACS39356; ACS39356; MexAM1_META1p1494. DR KEGG; mea:Mex_1p1494; -. DR PATRIC; 22508831; VBIMetExt101010_1492. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; MEXT272630:GBY6-1434-MONOMER; -. DR Proteomes; UP000009081; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000009081}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACS39356.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000009081}; KW Transferase {ECO:0000313|EMBL:ACS39356.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 254 254 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 318 318 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 771 771 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1250 AA; 137090 MW; C77D50DDEF3F7B86 CRC64; MTAFPPVDGT EIERALRQRA SEKILVLDGA MGTVIQRLKY TEEDFRGERF KDHSHDQKGN NDLLILTQPN AIRQIHLDYF LAGADVCETN TFSGTTIAQA DYGMESIIHE LNAEGARLAR EAAKLAEEQD GRRRFVAGAI GPTNRTLSIS PDVNNPGYRA VTFDGVKQAY VEQVRGLIDG GAELILIETI FDTLNAKAAI AAAWQVFDET GIRLPIQISG TITDLSGRTL SGQTPAAFWN SLRHSSPLTF GLNCALGAKE MRGHIAELSR ICDTLVCAYP NAGLPNEFGL YDESPEAMGK LVGEFAASGL VNMVGGCCGT TPDHIRAIAE AVADKKPREI PEIPRLMRLS GLEPFVLTKE IPFVNVGERT NVTGSAKFRK LITNNDYAAA LDVARDQVAA GAQVIDVNMD EGLLDSEKAM VEFLNLVAAE PDIARVPVMV DSSKFEVIEA GLKCIQGKPI VNSISMKEGE AKFIEAAKIC RSYGAAVVVM AFDEQGQADS YERKVEICTK AYKILTEQVG FPPEDIIFDP NIFAVATGIE EHNPYGVAFI EATRTIRETL PHAHISGGVS NLSFAFRGNE PVREAMHAVF LFHCIKAGMD MGIVNAGQLA VYDEIPAELR ELCEDVVLNR REDSTERLLE AAERFKTGAS AQAKTADLTW REAPVAKRIE HALVNGITEY IVADTEEARK EAARPLHVIE GPLMAGMNVV GDLFGSGKMF LPQVVKSARV MKQAVAYLEP FMEEEKRANG GDGKRQAAGK VLMATVKGDV HDIGKNIVGV VLACNNYEII DLGVMVPAAK ILETAKRENV DIVGLSGLIT PSLDEMVHVA AEMEREGMEM PLLIGGATTS RVHTAVKIHP AYAKGQAVYV TDASRAVGVV SSLISKETRG ATVEKVRAEY AKVADAHRRS EADKQRLPLA KARANAFKVD WSAYKPAKPS FTGTRVYGSY EVADLVPYID WTPFLQTYEF KGRYPAILDD PEQGPAARAL FEDAQVMLKQ IVEERWFNPK AVIGFWPANS VGDDIRLFTG ESRQETLATF HGLRQQLSKR DGRANTCISD FVAPAETGIA DYVGAFVVTA GLEEVRIAER FERANDDYRS ILVKALADRI AEAFAERMHE RVRKEFWGYA PDEAYAPEEL VSEKYDGIRP APGYPAQPDH TEKVQLFDLL KAESRIGVKL TESYAMWPGS SVSGLYLAHP DAHYFGVAKV ERDQVEDYAL RKGMDVSEVE RWLGPILNYD PVRYLKAAAE // ID C5B6Y7_EDWI9 Unreviewed; 1227 AA. AC C5B6Y7; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 29-APR-2015, entry version 45. DE SubName: Full=Methionine synthase, putative {ECO:0000313|EMBL:ACR67449.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ACR67449.1}; GN OrderedLocusNames=NT01EI_0206 {ECO:0000313|EMBL:ACR67449.1}; OS Edwardsiella ictaluri (strain 93-146). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Edwardsiella. OX NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67449.1, ECO:0000313|Proteomes:UP000001485}; RN [1] {ECO:0000313|Proteomes:UP000001485} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001600; ACR67449.1; -; Genomic_DNA. DR RefSeq; WP_015869660.1; NC_012779.2. DR RefSeq; YP_002931684.1; NC_012779.2. DR STRING; 634503.NT01EI_0206; -. DR EnsemblBacteria; ACR67449; ACR67449; NT01EI_0206. DR GeneID; 7958794; -. DR KEGG; eic:NT01EI_0206; -. DR PATRIC; 21833692; VBIEdwIct114273_0183. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; EICT634503:GCMY-205-MONOMER; -. DR Proteomes; UP000001485; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001485}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACR67449.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001485}; KW Transferase {ECO:0000313|EMBL:ACR67449.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 134310 MW; BD89282560F6C723 CRC64; MNTTCERLRR RLDKRILVLD GGMGTMIQRY GLSEQDFRAE RFVDWPCDLK GNNDLLALTR PDIISAIHYA YLEAGADILE TNTFNATRIA MADYRMEALA PEINYRAASL ARACADEWTA RTPHQPRFVA GVLGPTNRTA SISPEVNDPA CRNITFDQLV AAYRESARAL IEGGVDLLMI ETVFDTLNAK AAVYALECEF AALGVTLPVM ISGTITDASG RTLSGQTTEA FYNALRHARP LSFGLNCALG PEDLRQYVAE LSRVAECHVS AHPNAGLPNA FGEYDLSPQA MAQQIAEWAR AGYLNIVGGC CGTTPEHIAA ISRAVQGIAP RALPALPVAC RLSGLEPLTI DETSLFVNVG ERTNVTGSAK FKRLIKENKY DDALDVARQQ VASGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP LMIDSSRWSV IEAGLKCIQG KGVVNSLSLK EGEANFLQHA RQVRRFGAAL VVMAFDEQGQ ADTLARKVAI CRRAYQLLTE RIGFPPEDII FDPNIFAVAT GIEEHSNYAV DFIAACAEIK AQLPHALISG GVSNVSFSFR GNEAVREAIH AVFLYHAIRH GMDMGIVNAG QLAIYDDLPD DLRTAAEAVI LNQGSDATDR LLALAERYRD SQGSTQAEGQ QAEWRSWPVA QRLEYALVKG IGEFIAQDTE AARLEADRPI AVIEGPLMAG MNRVGDLFGD GKMFLPQVVK SARVMKQAVA YLSPFIEASK QRGSSAGKVL LATVKGDVHD IGKNIVGVVL QCNNYEIIDL GVMVPAERIL RVAREERVDI IGLSGLITPS LDEMVNVASE MERQGFTLPL LIGGATTSKA HTAVKIAPAY GGPTVYVQNA SRTVGVVAAL LSEAQRGPFI ERTRREYEAA RAQHGRQTPR TPPVTLAQAR ANGVVTDWSA CPPPVPQRLG VQTMQPGIAR LRDYIDWTPF FLTWSLAGKY PRILQDKVVG EEARRLLADA NGLLDRLEAS GSLTPRGVFG LFAANRRGDD VLIYRDESRR EVLAVSHHLR QQSDKSAGPN YCLADFIAAA DEGIADYIGA FAVTGGLEEE ALAQAFDAQH DDYHKIMVKA LADRLAEAFA EYLHQQVRKV HWGYAADEAL DNEQLIRENY RGIRPAPGYP ACPEHSEKAT LWRLLDVERH TGMRLTESYA MWPGASVSGW YFSHPHSKYF TVARVQRDQV ADYAARKGIP LAEAERWLAP NLGYEVE // ID C5BJB9_TERTT Unreviewed; 1229 AA. AC C5BJB9; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 27-MAY-2015, entry version 48. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACR11670.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ACR11670.1}; GN Name=metH {ECO:0000313|EMBL:ACR11670.1}; GN OrderedLocusNames=TERTU_2126 {ECO:0000313|EMBL:ACR11670.1}; OS Teredinibacter turnerae (strain ATCC 39867 / T7901). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadales genera incertae sedis; Teredinibacter. OX NCBI_TaxID=377629 {ECO:0000313|EMBL:ACR11670.1, ECO:0000313|Proteomes:UP000009080}; RN [1] {ECO:0000313|EMBL:ACR11670.1, ECO:0000313|Proteomes:UP000009080} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 39867 / T7901 {ECO:0000313|Proteomes:UP000009080}; 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.G., RA Elshahawi S., Hanora A., Schmidt E.W., Haygood M.G., Posfai J., RA Benner J., Madinger C., Nove J., Anton B., Chaudhary K., Foster J., RA Holman A., Kumar S., Lessard P.A., Luyten Y.A., Slatko B., Wood N., RA Wu B., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001614; ACR11670.1; -; Genomic_DNA. DR RefSeq; WP_015817782.1; NC_012997.1. DR RefSeq; YP_003073590.1; NC_012997.1. DR STRING; 377629.TERTU_2126; -. DR EnsemblBacteria; ACR11670; ACR11670; TERTU_2126. DR KEGG; ttu:TERTU_2126; -. DR PATRIC; 23871293; VBITerTur118718_1980. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; TTUR377629:GHSU-1920-MONOMER; -. DR Proteomes; UP000009080; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000009080}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACR11670.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000009080}; KW Transferase {ECO:0000313|EMBL:ACR11670.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 249 249 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1229 AA; 134839 MW; 5EDBCB3C1C75CB77 CRC64; MTKLVEDRLT ILQEALNQRI LILDGAMGTM IQRHKLQEND YRGERFASHH QDLIGNNDIL SLTRPDIIAG IHREYLEAGA DIIETNTFNA TRLSQSDYDT QSIAFELNKA SATLAREAAD AYATPEKPRF VAGILGPTSR TASISPDVND PGARNVTFDQ LVENYTEATH GLIEGGADIL MIETIFDTLN AKAAVFAVSS VFDALGYKLP IMISGTITDA SGRTLSGQTT EAFYNSLAHA EPLSIGLNCA LGASELEPYV KELARVANCR VSAHPNAGLP NEFGEYDQSA AEMAEIVIKF AENGYLNVVG GCCGTTPAHI AAIADAVASL PPREINPPPV SCRLAGLEPF NITADSLFVN VGERCNVTGS ARFKRLILEE DYATALDVAQ QQVTDGAQII DINMDEGMLD AEAAIVRFLN LIAGEPEIAR VPIMVDSSKW EVIEAGLKCI QGKPIVNSIS LKEGEAEFVE KARLCRRYGA AVIVMAFDEQ GQADTQARKI EICSRSYRIL TEELGFPPED IIFDPNIFAV ATGIDEHNNY AVDFIEATRW IRQNLPHAGV SGGVSNVSFS FRGNNPVREA IHSVFLYHAI RAGMNMGIVN AGQLAIYDDL PEELRTRVEA VISNTSADAT EALLSIAEKY RGDGSQQQSK EDLEWRTADV NKRLEHALVK GITSYIEADT EEARLQSSRP LDVIEGPLMD GMNVVGELFG SGKMFLPQVV KSARVMKQAV AWLQPYIEAE KSEGTRSNGK ILMATVKGDV HDIGKNIVGV VLQCNNFEVV DLGVMVPGEK ILETAKREGC DIIGLSGLIT PSLDEMVAVA REMETQGIDL PLMIGGATTS KAHTAVKIDP QFHLNQAVYV PDASRAVGVA TRLLSKDLRP DFIAALKTEY ETIRERRANR TSKRPATPYA EAVKLRKPLN WENYTPPKPQ FTGTQVWEDY PLTELVEYID WTPFFITWDL VGKFPAILTD KVVGEAATSL YQDARALLQD IVDGKLLQAK AILGFWEANT VDHDDIVLTH NAEPIATLHH IRQQVIKNDN DKHLLSLADF IAPQESGVTD FVGGFSVTAG IGADELAASY QAKGDDYNAI MVKALADRLA EAFAEHLHER VRKEFWGYDS AEALDKDELI REKYRGIRPA PGYPACPDHT EKATLFKLLQ ADRIGVSLTE HYAMFPAASV SGWYFSHPES QYFNVGKISR DQVESLAERK GLSVSDMEKW LQSVLAYDI // ID C5CX26_VARPS Unreviewed; 348 AA. AC C5CX26; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 27-MAY-2015, entry version 37. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACS16830.1}; GN OrderedLocusNames=Vapar_0167 {ECO:0000313|EMBL:ACS16830.1}; OS Variovorax paradoxus (strain S110). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Variovorax. OX NCBI_TaxID=543728 {ECO:0000313|EMBL:ACS16830.1, ECO:0000313|Proteomes:UP000000453}; RN [1] {ECO:0000313|Proteomes:UP000000453} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S110 {ECO:0000313|Proteomes:UP000000453}; 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 ----------------------------------------------------------------------- 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; ACS16830.1; -; Genomic_DNA. DR RefSeq; WP_012745332.1; NC_012791.1. DR RefSeq; YP_002942096.1; NC_012791.1. DR STRING; 543728.Vapar_0167; -. DR EnsemblBacteria; ACS16830; ACS16830; Vapar_0167. DR KEGG; vap:Vapar_0167; -. DR PATRIC; 24000716; VBIVarPar36677_0172. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; VPAR543728:GHLL-168-MONOMER; -. DR Proteomes; UP000000453; Chromosome 1. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000453}; KW Methyltransferase {ECO:0000313|EMBL:ACS16830.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000453}; KW Transferase {ECO:0000313|EMBL:ACS16830.1}. SQ SEQUENCE 348 AA; 37632 MW; F77DAE157383893B CRC64; MKPVIYTRGQ ALAGILEKRI AILDGAMGTM IQRFKLTEEQ YRGERFKDFE RDVKGNNELL SLTRPDVIRD IHEGYLAAGA DLIETNTFGA TTIAQEDYRM AHLAREMNLE SAKLARAACD KFSTPDKPRF VAGALGPTPK TASISPDVND PGARNVDFEQ LRAAYYEQTE ALVEGGADVI LVETIFDTLN AKAALFAVDE YFDNSGQRLP LIISGTVTDA SGRILSGQTV TAFWHSVRHA QPLAIGLNCA LGAALMRPYI QELAKVAGDT FISCYPNAGL PNPMSETGFD ETPDVTSRLL HEFAAEGLVN IVGGCCGTTP DHIAAIGKAV APMTGRLLNN NGFYREAA // ID C5D740_GEOSW Unreviewed; 1136 AA. AC C5D740; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 01-APR-2015, entry version 48. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACS23598.1}; GN OrderedLocusNames=GWCH70_0707 {ECO:0000313|EMBL:ACS23598.1}; OS Geobacillus sp. (strain WCH70). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=471223 {ECO:0000313|EMBL:ACS23598.1, ECO:0000313|Proteomes:UP000002386}; RN [1] {ECO:0000313|EMBL:ACS23598.1, ECO:0000313|Proteomes:UP000002386} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WCH70 {ECO:0000313|EMBL:ACS23598.1, RC ECO:0000313|Proteomes:UP000002386}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001638; ACS23598.1; -; Genomic_DNA. DR RefSeq; WP_012749399.1; NC_012793.1. DR RefSeq; YP_002948864.1; NC_012793.1. DR ProteinModelPortal; C5D740; -. DR STRING; 471223.GWCH70_0707; -. DR EnsemblBacteria; ACS23598; ACS23598; GWCH70_0707. DR KEGG; gwc:GWCH70_0707; -. DR PATRIC; 21970305; VBIGeoSp101709_0769. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; GSP471223:GH2C-792-MONOMER; -. DR Proteomes; UP000002386; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002386}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002386}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 724 724 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1136 AA; 126086 MW; 490C9D24E56A48AF CRC64; MGNITLEQQL EKKILIIDGA MGTMIQSAKL SADDFGGEAY EGCNEYLTLT APHVIERIHE AYLQAGADII ETNTFGATNV VLDEYHLGHL ALELNIEAAR LARKAADAYS TPEWPRFVAG SMGPTTKTLS VTGGITFEQL VAAYEEQARG LLLGGVDLLL LETCQDTLNV KAGFIGISKA FEAVGKQVPI MISGTIEPMG TTLAGQTIES FFISVQHMKP FAVGLNCATG PEFMTDHLRA LASLANTAVS CYPNAGLPDE EGCYHETPEM LAKKIRRFAE KGWINIVGGC CGTTPEHIRA IAEAVRDIPP RPIPKSFDVH AVSGIDPLIY DETMRPLFVG ERTNVIGSRK FKRLIAEGKY EEAAEIARAQ VKNGAHVIDI CLADPDRNEQ EDMEKFIQQV VKKVKVPLVI DSTDERVIER ALTYSQGKAI INSINLEDGE ERFEKVIPLL HKYGAAVVVG TIDEQGMAIH AERKLEIALR SHDLLVNKYG VSPHDIIFDP LVFPVGTGDE QYIGAAKETI EGIRLIKERL PQCLTILGIS NVSFGLPPVG REILNSVFLY HCTQAGLDYA IVNTEKLERF ASIPEEEVRL AEELLFNTND ETLNTFIQFY RDKTKEPKKI KTELSLEERL AGYVVEGTKE GLYADLEQAL QTYSDPLDII NGPLMEGMDE VGRLFNNNQL IVAEVLQSAE VMKAAVAFLE PYMEKKENST KGKVLLATVK GDVHDIGKNL VDIILSNNGF HVIDLGIKVA PQKLIEAVQA EKPDIIGLSG LLVKSAQQMV VTAQDLRQAG ISIPILVGGA ALSRKFTENK IAPEYDGIVL YAKDAMEGLA LANQLQQNEI EYTKTKKQET ETEKTTPTAI AAKSNVSTDV PVFVPTDLER HILKDISLSH IIPYVNWQMV LGHHLGLKGK VKRLLEEKDE KALMLKQVVD DLLDEAQRNN WITPAAVYQF FPAQSEGNRI YIYSPKDKRT IIEMFEFPRQ PREPYLCLAD YLKSTESGQI DYVGFFAVTA GKGIRELSQR WKESGEFLKS HAIQALALEI AEGLAELIHQ VMRDRWGFPD DPDFTMEQRF AAKYQGQRYS FGYPACPNLE DQEKLFRLLN PEEIGIHLTD GYMMEPEASV SAIVFAHPEA RYFNVL // ID C5D741_GEOSW Unreviewed; 616 AA. AC C5D741; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 01-APR-2015, entry version 42. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=GWCH70_0708 {ECO:0000313|EMBL:ACS23599.1}; OS Geobacillus sp. (strain WCH70). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=471223 {ECO:0000313|EMBL:ACS23599.1, ECO:0000313|Proteomes:UP000002386}; RN [1] {ECO:0000313|EMBL:ACS23599.1, ECO:0000313|Proteomes:UP000002386} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WCH70 {ECO:0000313|EMBL:ACS23599.1, RC ECO:0000313|Proteomes:UP000002386}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ACS23599.1; -; Genomic_DNA. DR RefSeq; WP_012749400.1; NC_012793.1. DR RefSeq; YP_002948865.1; NC_012793.1. DR ProteinModelPortal; C5D741; -. DR STRING; 471223.GWCH70_0708; -. DR EnsemblBacteria; ACS23599; ACS23599; GWCH70_0708. DR KEGG; gwc:GWCH70_0708; -. DR PATRIC; 21970307; VBIGeoSp101709_0770. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; GSP471223:GH2C-793-MONOMER; -. DR Proteomes; UP000002386; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002386}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ACS23599.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000002386}; KW Transferase {ECO:0000313|EMBL:ACS23599.1}. SQ SEQUENCE 616 AA; 68155 MW; 5823930A8D2FA3DE CRC64; MGLLEDLQER IVIADGAMGT LLYSHGVDRC FEELNLSKPE DIIHIHEAYI AAGAEVIQTN TYGANYVKLA RYGLEDEVPS INRAAVRLAK KAAGNKAYVL GTIGGLRSIN KSAVSIEEVK RTFREQLFVL LNEDVDGLLL ETYYDLEELE TVLAIARKET DKPIIAHVSL HEVGVLQDGT PLSEALARLE QLGADVVGLN CRLGPYHMIR SLEEVPLPKK AFLSAYPNAS LPDYRDGRLI YETNTDYFKE TALAFREQGV RLIGGCCGTT PKHIEAIANA LTDRTPITEK VVKQRHVPIS IQTNEPNAAP PLQDIVRKRR SVIVELDPPK KLGIAKFLEG AKALKEANID ALTLADNSLA TPRISNMALG SIVKEQLGIR PLIHITCRDR NLIGLQSHLM GLHTLGITDV LAITGDPSKI GDFPGATSVY DLSSFDLIRL IRQFNEGLSY SGKSLGQKTN FSIAAAFNPN VRHLDKAVER LEKKIQCGAH YFITQPLYSE QQIEEVYEAT KHLETPIYIG IMPLVSARNA DFLHHEVPGI TLSDEIRSRM AACANNPVQS AREGIAIAKS LIDAAFDLFN GIYLITPFLR YEMTVELVRY IHEKEQAAQE RKVLHG // ID C5DDU4_LACTC Unreviewed; 329 AA. AC C5DDU4; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 29-APR-2015, entry version 31. DE SubName: Full=Lachancea thermotolerans CBS 6340 chromosome C complete sequence {ECO:0000313|EMBL:CAR21955.1}; GN OrderedLocusNames=KLTH0C03850g {ECO:0000313|EMBL:CAR21955.1}; 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 {ECO:0000313|EMBL:CAR21955.1, ECO:0000313|Proteomes:UP000002036}; RN [1] {ECO:0000313|EMBL:CAR21955.1, ECO:0000313|Proteomes:UP000002036} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284 RC {ECO:0000313|Proteomes:UP000002036}; RX PubMed=19525356; DOI=10.1101/gr.091546.109; RG The Genolevures Consortium; RA Genolevures Consortium, Souciet J.L., Dujon B., Gaillardin C., RA Johnston M., Baret P.V., Cliften P., Sherman D.J., Weissenbach J., RA Westhof E., Wincker P., Jubin C., Poulain J., Barbe V., Segurens B., RA Artiguenave F., Anthouard V., Vacherie B., Val M.E., Fulton R.S., RA Minx P., Wilson R., Durrens P., Jean G., Marck C., Martin T., RA Nikolski M., Rolland T., Seret M.L., Casaregola S., Despons L., RA Fairhead C., Fischer G., Lafontaine I., Leh V., Lemaire M., RA de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I., RA Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A., RA Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L., RA Ozanne C., Richard G.F., Sacerdot C., 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; CU928167; CAR21955.1; -; Genomic_DNA. DR RefSeq; XP_002552393.1; XM_002552347.1. DR STRING; 559295.KLTH0C03850g; -. DR GeneID; 8291257; -. DR KEGG; lth:KLTH0C03850g; -. DR eggNOG; COG2040; -. DR HOGENOM; HOG000066018; -. DR InParanoid; C5DDU4; -. DR KO; K00547; -. DR OrthoDB; EOG7X9GHR; -. DR Proteomes; UP000002036; Chromosome C. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002036}; KW Reference proteome {ECO:0000313|Proteomes:UP000002036}. SQ SEQUENCE 329 AA; 36809 MW; F0E1FBA18A4BDEF2 CRC64; MPRPSVKEYL ASNPEEVLVL DGGQGTELEN RGIKVANPVW STIPFISDSF WTANDSSSKD RQIVKEMYED FLKAGARVLM TVTYQASFKS VSENTSITTL EEYDALLSRI VSFSRSCIGD DKWLVGCIGP WGAHNCSEFT GDYGSEPEKI DYLQYFKPQL DNFTVNDDLD LIGFETIPNI HELRAILSWD TTILPKPFYI GLSVHEHGVL RDGTTMHEVA ELIKSLGDKI NPNFVLLGIN CVSYNHSPEI LRSLHQEIPE LPLIAYPNSG EVYDTVKKIW NPKGDHTLTW DQVVKSYIDS GARIIGGCCR TSPKDIAAIN AAVNKYRPN // ID C5E0N3_ZYGRC Unreviewed; 325 AA. AC C5E0N3; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 27-MAY-2015, entry version 36. DE SubName: Full=Strain CBS732 chromosome G complete sequence {ECO:0000313|EMBL:CAR29667.1}; GN OrderedLocusNames=ZYRO0G14212g {ECO:0000313|EMBL:CAR29667.1}; 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 {ECO:0000313|Proteomes:UP000008536}; RN [1] {ECO:0000313|EMBL:CAR29667.1, ECO:0000313|Proteomes:UP000008536} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568 / NRRL Y-229 RC {ECO:0000313|Proteomes:UP000008536}; RX PubMed=19525356; DOI=10.1101/gr.091546.109; RG The Genolevures Consortium; RA Genolevures Consortium, Souciet J.L., Dujon B., Gaillardin C., RA Johnston M., Baret P.V., Cliften P., Sherman D.J., Weissenbach J., RA Westhof E., Wincker P., Jubin C., Poulain J., Barbe V., Segurens B., RA Artiguenave F., Anthouard V., Vacherie B., Val M.E., Fulton R.S., RA Minx P., Wilson R., Durrens P., Jean G., Marck C., Martin T., RA Nikolski M., Rolland T., Seret M.L., Casaregola S., Despons L., RA Fairhead C., Fischer G., Lafontaine I., Leh V., Lemaire M., RA de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I., RA Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A., RA Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L., RA Ozanne C., Richard G.F., Sacerdot C., Straub M.L., Talla E.; RT "Comparative genomics of protoploid Saccharomycetaceae."; RL Genome Res. 19:1696-1709(2009). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU928179; CAR29667.1; -; Genomic_DNA. DR RefSeq; XP_002498600.1; XM_002498555.1. DR STRING; 559307.ZYRO0G14212g; -. DR GeneID; 8206422; -. DR KEGG; zro:ZYRO0G14212g; -. DR eggNOG; COG2040; -. DR HOGENOM; HOG000066018; -. DR InParanoid; C5E0N3; -. DR KO; K00547; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000008536; Chromosome G. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008536}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000008536}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 235 235 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 325 AA; 36702 MW; E3A5ED0423465BD3 CRC64; MRQQLLEVLR DTDRVLVMDG GQGTELENRG MNISGPIWST VPFTKEEFWN FDQPYTDRDV VNSMFKAYVD AGAQLLSTVT YQTSYKTICA HTDIHTRTQY DQLLDRIVGF CRRCIGDDHY LVGSIGPYAA HVGAEYTGDY GPKPEEIDYW QYFEPQVANF NRNETIDIIG LETVPNVHEL KSILSWDETK ISKPFYVSLC VGDDGNLRDG TPLEQLVPLF ANRSNKNLLL VGINCCSLSV SSQALSHLNE ILASTPMGLL VYPNSGEIYD HKTQTWSRPT GLDSHRLSWP SLVQEYRKFG ARAIGGCCRT TPLDIQEICK VVDRN // ID C5E3E4_LACTC Unreviewed; 348 AA. AC C5E3E4; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 29-APR-2015, entry version 31. DE SubName: Full=Lachancea thermotolerans CBS 6340 chromosome H complete sequence {ECO:0000313|EMBL:CAR30555.1}; GN OrderedLocusNames=KLTH0H12716g {ECO:0000313|EMBL:CAR30555.1}; 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 {ECO:0000313|EMBL:CAR30555.1, ECO:0000313|Proteomes:UP000002036}; RN [1] {ECO:0000313|EMBL:CAR30555.1, ECO:0000313|Proteomes:UP000002036} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284 RC {ECO:0000313|Proteomes:UP000002036}; RX PubMed=19525356; DOI=10.1101/gr.091546.109; RG The Genolevures Consortium; RA Genolevures Consortium, Souciet J.L., Dujon B., Gaillardin C., RA Johnston M., Baret P.V., Cliften P., Sherman D.J., Weissenbach J., RA Westhof E., Wincker P., Jubin C., Poulain J., Barbe V., Segurens B., RA Artiguenave F., Anthouard V., Vacherie B., Val M.E., Fulton R.S., RA Minx P., Wilson R., Durrens P., Jean G., Marck C., Martin T., RA Nikolski M., Rolland T., Seret M.L., Casaregola S., Despons L., RA Fairhead C., Fischer G., Lafontaine I., Leh V., Lemaire M., RA de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I., RA Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A., RA Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L., RA Ozanne C., Richard G.F., Sacerdot C., 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; CAR30555.1; -; Genomic_DNA. DR RefSeq; XP_002556417.1; XM_002556371.1. DR STRING; 559295.KLTH0H12716g; -. DR GeneID; 8294758; -. DR KEGG; lth:KLTH0H12716g; -. DR eggNOG; COG2040; -. DR HOGENOM; HOG000066018; -. DR InParanoid; C5E3E4; -. DR KO; K00547; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000002036; Chromosome H. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002036}; KW Reference proteome {ECO:0000313|Proteomes:UP000002036}. SQ SEQUENCE 348 AA; 38952 MW; A72585E870FB3CD4 CRC64; MRKPLKEFFK NNILLLDGGQ GTELEKKGVS ISHPLWSTLP FIIKNKTHLE AIKEMYRDFA EAGSNALMTI TYQASFSSMK KYSEGLVNSE EDYAAFLDYV IGFTDRECIT PDKYLVGSVG PYAGLLSNGA EYSGYYGEGK IDFIDYYSPQ VKHFALSPRI DLIGIETIPN IDEFKALLSP EFSRLSFSKP YYISVTTDNN GCLRDGTSLN EICRAIKQSA SLLPDNFVFF AINCVEFLHC VEILQSLNDC LEMQGVDRRF RFRGAYPNSG EIYHGGTHSW SSNPYAGPED TWENLTLGLL SQECLMLGGC CRTGSEEIRQ MALTTKKNST VAAMKAFPSK ASNNYQSF // ID C5EEE3_9FIRM Unreviewed; 327 AA. AC C5EEE3; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 01-OCT-2014, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase domain family protein {ECO:0000313|EMBL:EEQ57034.1}; GN ORFNames=CBFG_00744 {ECO:0000313|EMBL:EEQ57034.1}; OS Clostridiales bacterium 1_7_47FAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales. OX NCBI_TaxID=457421 {ECO:0000313|EMBL:EEQ57034.1}; RN [1] {ECO:0000313|EMBL:EEQ57034.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_7_47_FAA {ECO:0000313|EMBL:EEQ57034.1}; 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; DS990260; EEQ57034.1; -; Genomic_DNA. DR RefSeq; WP_008717247.1; NZ_DS990260.1. DR EnsemblBacteria; EEQ57034; EEQ57034; CBFG_00744. DR PATRIC; 27115781; VBICloBac45081_2348. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEQ57034.1}; KW Transferase {ECO:0000313|EMBL:EEQ57034.1}. SQ SEQUENCE 327 AA; 37164 MW; A47B0F91BE6DF91A CRC64; MTTIQRREKF CNTFAQVPVM MLQGSVGERI KRNFTHQDPA PPLKLAGLYY TEDGHRGLDT VFHDYVQIAQ RYDLPMILHP YTRLTSPSMG KGTYWEDRDV SADNLNHCRS IVDGYPSIRD RIFIGTTMGF SGDSYDPLTG LEEEEAYLFY TDHAKMLEAS IVDHVRNGLT PCLTDAAGCA RALSETSVPY FITFLIRKDG KLMDGTWLND AIDYIDSRTV DHPPMFYQVN CVHPRNVMSA LDKQPNRTKL VRERFLGLEA NGSDMSPEEL DNSPVIYSSP ADEWAEEMME LHRNYGLKLL GGCCGTDHEH MEQLAMRIRG VYDGLQV // ID C5EJL8_9FIRM Unreviewed; 805 AA. AC C5EJL8; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 01-OCT-2014, entry version 23. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEQ56793.1}; GN ORFNames=CBFG_00503 {ECO:0000313|EMBL:EEQ56793.1}; OS Clostridiales bacterium 1_7_47FAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales. OX NCBI_TaxID=457421 {ECO:0000313|EMBL:EEQ56793.1}; RN [1] {ECO:0000313|EMBL:EEQ56793.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_7_47_FAA {ECO:0000313|EMBL:EEQ56793.1}; 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; DS990260; EEQ56793.1; -; Genomic_DNA. DR RefSeq; WP_008716831.1; NZ_DS990260.1. DR EnsemblBacteria; EEQ56793; EEQ56793; CBFG_00503. DR PATRIC; 27115313; VBICloBac45081_2118. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEQ56793.1}; KW Transferase {ECO:0000313|EMBL:EEQ56793.1}. SQ SEQUENCE 805 AA; 86457 MW; 8C7303EB8B312361 CRC64; MRILEEMKVR RLFCDGGMGS LLQAQGLKAG ELPELWNLTH PEVLRDIHRQ YLAAGADIMT TNTFGANGLK YRDNLEEIVA AAVGHARAAV EEAGHGYVAL DLGPTGKLLK PLGDLEFEAA VSLYKEVVTA GAKAGADLIL IETMSDSYEL KAAVLAAKEA GISREDGEPL PVFATVIYDE KGKLLTGGNV ESTVALLEGL RVDALGINCG LGPVQMKEIL RDIMKVTSLP VLVNPNAGLP RSEEGRTVYD IDEKQFALAM EEIAQLGAAV VGGCCGTTPA HIRETVKRCR DIPVRLPKPK KRTVISSYAQ AVVIDGKTVI IGERINPTGK SKFKQALRDH DLEYILREGV SQQDNGADVL DVNVGLPGID EPSMMEEVVK ELQSIIDLPL QIDTSDMEAM ERAMRAYNGK PLINSVNGKE EVMHQVFPLV AKYGGVVVGL CLDEGGIPET AGGRIEVGRK IIDTAASYGI GAEDIILDGL CMTVSSDSKG ALTTLDTLRR IRDELGGRSI LGVSNISFGL PQREIINAAF FTMAMEAGLN AAIINPNSEA MMRAFYSFNA LMDRDAQCSQ YIGVYSGQSA GLGQTIGKGG TAAAGESTDC SLSAAIERGL KDAAHQAVTA LLEEKEPLGI INEQMIPALD RVGKGFEKGT IFLPQLLMSA EAAKAAFEVI KTKMDAKGQV QEKKGTIVLA TVKGDIHDIG KNIVKVLLEN YGYEVVDLGK DVPPERIVEE TMGRKVQLVG LSALMTTTVP SMEETIRRLR TAAPWARVMV GGAVLTEEYA RTIDADMYCR DAMASVNYAE SIFVK // ID C5EY17_9HELI Unreviewed; 1142 AA. AC C5EY17; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 27-MAY-2015, entry version 36. DE SubName: Full=Vitamin B12 dependent methionine synthase, activation domain protein {ECO:0000313|EMBL:EEQ62787.1}; GN ORFNames=HPMG_00244 {ECO:0000313|EMBL:EEQ62787.1}; OS Helicobacter pullorum MIT 98-5489. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=537972 {ECO:0000313|EMBL:EEQ62787.1}; RN [1] {ECO:0000313|EMBL:EEQ62787.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MIT 98-5489 {ECO:0000313|EMBL:EEQ62787.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; DS990441; EEQ62787.1; -; Genomic_DNA. DR RefSeq; WP_005020774.1; NZ_DS990441.1. DR EnsemblBacteria; EEQ62787; EEQ62787; HPMG_00244. DR PATRIC; 27515792; VBIHelPul71015_0445. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 726 726 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1142 AA; 127937 MW; E50B813422014B25 CRC64; MQELIQKQVL ILDGAMGTEI QKRENIKWGR NAKGESLAGC TEALNLYSPQ IIYEIYTSYL QAGANIITSN TFGAMEWVLA EYEMQEHSKE IAKLGVQLAK EAILKHKPLE NQKDALFVAG SLGPGTKLPS LGHIDYDTMF LGYCKVVSGF KEANVDLILL ETAQDPLQIK AALHAIREID KEIPIMVSAT IETNGSMLIG TDIATLFYIL EPFDIFSLGI NCGLGPDLAK KYLLELSQVS KFPISIHANA GLPQNKGGVT YYPMEAEEFS EIESEFLKIS GVALLGGCCG TTPKHIQKLV EKTKDKIPSL PKGEYKPSIA SLFGAYELKQ NPAPLLIGER SNATGSKAFR ELLLNENYEG ALGVGSEQVK KGAHVLDVSV AFAGRDESKD MQELISLYAT KIPLPLMPDS TQVIALEIAL KLIGGRCIIN SANLEDGIEK FDKIAGLAKK FGCVLVCLTI DEKGMCKTKE RKVECAKRMM QRAIEVHHLR EEDIIFDPLT FTIGSGDEEY FTAGMETLGA IEEIMKIYPK AGSTLGLSNI SFGLSKEGRI CLNSVFLYHA IQKGLTSAIV NVAHIIPYAR LEREDIQVCE DLIFNTQKTS QPLYDFISYF EKKSGLDLDS KEDESHLSTQ ERISKYLIEG DLNAMQKILP VAKDEINPEV IVNEILIDAM KVVGERFGAG EMQLPFVLQS AEVMKKSVDY LNEFLPKKTN SHKTTIVIGT VKGDVHDVGK NLVDIILSNN GFNVINIGIK AELEKFLEVL KKEKVDCIGM SGLLVKSTLV MKENLEELKR LGIKIPIMLG GAALNRNFVD EYCRPNYDGV IFYCKDAFDS VAAMQIIQSG DFSDITLPSQ KNKNEDSKLE QRVAKKLEKQ LEVKEIFKPI KCELEFSYEV YKPPFFGRKV LQLSHQEILE VFDYLDKDLL FKHRWGYSKL KKDEYLKLKE NELEPMLESL KKEFIEQNIF APVALYGYYH TRTKIPEDKT QGLILEVSEN CDFKKVESFL FPRSSKKPYL CLGDYFNKEQ DICALHLVSS GLNLAPFEEK LYQESQYHKY YLVHALGVEL AEALADFVHQ RVRRELGLGE KEGQRYSFGY PACPDLALNE GLFNLLKPQE FGITLSETYQ MSPEATTSAL IVPHKEAKYF AL // ID C5K5V1_PERM5 Unreviewed; 1278 AA. AC C5K5V1; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 01-APR-2015, entry version 37. DE SubName: Full=Methionine synthase, putative {ECO:0000313|EMBL:EER20147.1}; GN ORFNames=Pmar_PMAR026737 {ECO:0000313|EMBL:EER20147.1}; OS Perkinsus marinus (strain ATCC 50983 / TXsc). OC Eukaryota; Alveolata; Perkinsea; Perkinsida; Perkinsidae; Perkinsus. OX NCBI_TaxID=423536 {ECO:0000313|Proteomes:UP000007800}; RN [1] {ECO:0000313|EMBL:EER20147.1, ECO:0000313|Proteomes:UP000007800} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 50983 / TXsc {ECO:0000313|Proteomes:UP000007800}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG670791; EER20147.1; -; Genomic_DNA. DR RefSeq; XP_002788351.1; XM_002788305.1. DR GeneID; 9053657; -. DR InParanoid; C5K5V1; -. DR Proteomes; UP000007800; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007800}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007800}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 266 266 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 329 329 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 330 330 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 795 795 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1278 AA; 142734 MW; 0BB976631F15EB4B CRC64; MGHSTAPKIG SHDDHPGGES ESTEYLRQLF SERIVLLDGG MGTRIQADRL QEEDFRGEIL KDHPKELKGD NDLLCLTRPD LVVKIHKEYL HAGADLIETN TFNGTTISQA EYQCESLVRD LNFQAAMLAK QACREVEAET GRRRLVAGAI GPTSRTLSVS PSVEDSSYRN VTWNELVKAY YEQVDALVAG GSDVLLVETI FDTLNAKAAL FAIDCYYEDH PRESRLPTII SATIVDQSGR TLSGQTIDAF LVSVMHARPL CVGINCALGA AQMRPFFETL AKLAPVYVHV YPNAGLPNAM GGYDETPESF GESLVLYAQD HLINMVGGCC GTFPAHIQAV HERLKSFPPR PLHVRRDPVM RLSGLEPLYL TPELGFVNVG ERCNLMGSLR FKKMVEQSRW DDALEVAKEQ VENGAQVLDF NFDADLIDGQ LAMGRFMRSC VTEPAIARVP FMIDSSKFKV IEEGLQAVQG RCIVNSLSLK VGEEDFIYHA RLVRKYGAAL VCMAFDEEGQ AATFDDKIRI CERTYKILTT KCGYEGHDII FDCNILTIAT GMEEHNNYGK DFIDAVEIVR QKCPGCYTSG GLSNLSFSFR GLNELREAMH SVFLYHAIPK GLSMAIVNAG ALPIYTDIPE DMRQLLEDVV MNVSPEATEK LLEFASELKE KKAQKGGASG VVKAVEEWRT EGVEKRLEHS LVKGIDKFIV DDVQECLDGL QLRPLEVIEG PLMAGMSVVG DLFGSGKMFL PQVIKSARVM KKAVAHLVPI METENRRKAL EEGLDPDRPN WAGTVLLATV KGDVHDIGKN IVGVVLGCNN FRVIDLGVMV PCDQILKRAR EEKADVIGLS GLITPSLDEM VFVAQQMRKE SMDVPLLIGG ATTSRKHTAV KIWPQYEASV VHVLDASRSV VVVNSLIQNP ERRIEYMEDI KEEYDGLRED YYSTLVDKRW LSLDEARKMR YTIDFEKYPP PPAPRRLGNK YLDEYPLEEL VEYIDWTPFF QVYQLRGRYP NKDYPKIFND KRVGEEAKKL FDDAQARTAR IRVVEWITAT AVVGVYRACS SGDDINVLSL DGSGEVLETF YGIRQQLDTE QDQTFALGDF IAPEASGLPD HIALFCCQAG IGVEERKKMY NATHDIDKSI MLEALADRLA EAFAELIHHK IRTDPDFWGY VPEEKLTLSD MLKVKYVGIR PAPGYPTQPD HREKDTLWRL LDAEKLSGGK MVLTESLMMM PAASVCALCF AHEKAKYFAV GQINKDQVAD YSARRGCTVE DSERWLGSST LGYEPQSQ // ID C5KDF9_PERM5 Unreviewed; 1282 AA. AC C5KDF9; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 01-APR-2015, entry version 38. DE SubName: Full=Methionine synthase, putative {ECO:0000313|EMBL:EER17470.1}; GN ORFNames=Pmar_PMAR025422 {ECO:0000313|EMBL:EER17470.1}; OS Perkinsus marinus (strain ATCC 50983 / TXsc). OC Eukaryota; Alveolata; Perkinsea; Perkinsida; Perkinsidae; Perkinsus. OX NCBI_TaxID=423536 {ECO:0000313|Proteomes:UP000007800}; RN [1] {ECO:0000313|EMBL:EER17470.1, ECO:0000313|Proteomes:UP000007800} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 50983 / TXsc {ECO:0000313|Proteomes:UP000007800}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG672080; EER17470.1; -; Genomic_DNA. DR RefSeq; XP_002785674.1; XM_002785628.1. DR GeneID; 9062697; -. DR InParanoid; C5KDF9; -. DR Proteomes; UP000007800; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007800}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007800}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 266 266 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 329 329 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 330 330 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 808 808 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1282 AA; 143277 MW; A34541E1651FE948 CRC64; MGHSTAPKIG SHDDHPGGES ESTEYLRQLF SERIVLLDGG MGTRIQADRL QEEDFRGEIL KDHPKELKGD NDLLCLTRPD LVVKIHKEYL HAGADLIETN TFNGTTISQA EYQCESLVRD LNFQAAMLAK QACREVEAET GRRRLVAGAI GPTSRTLSVS PSVEDSSYRN VTWNELVKAY YEQVDALVAG GSDVLLVETI FDTLNAKAAL FAIDCYYEDH PRESRLPTII SATIVDQSGR TLSGQTIDAF LVSVMHARPL CVGINCALGA AQMRPFFETL AKLAPVYVHV YPNAGLPNAM GGYDETPESF GESLVLYAQD HLINMVGGCC GTFPAHIQAV HERLKVERAK CPVSSHKRLS GLEPLYLTPE LGFVNVGERC NLMGSLRFKK MVEQSRWDDA LEVAKEQVSS RCQLLYNDFG CHQVENGAQV LDFNFDADLI DGQLAMGRFM RSCVTEPAIA RVPFMIDSSK FKVIEEGLQA VQGRCIVNSL SLKVGEEDFI YHARLVRKYG AALVCMAFDE EGQAATFDDK IRICERTYKI LTTKCGYEGH DIIFDCNILT IATGMEEHNN YGKDFIDAVE IVRQKCPGCY TSGGLSNLSF SFRGLNELRE AMHSVFLYHA IPKGLSMAIV NAGALPIYTD IPEDMRQLLE DVVMNVSPEA TEKLLEFASE LKEKKAQKGG ASGVVKAVEE WRTEGVEKRL EHSLVKGIDK FIVDDVQECL DGLQLRPLEV IEGPLMAGMS VVGDLFGSGK MFLPQVIKSA RVMKKAVAHL VPIMETENRR KALEEGLDPD RPNWAGTVLL ATVKGDVHDI GKNIVGVVLG CNNFRVIDLG VMVPCDQILK RAREEKADVI GLSGLITPSL DEMVFVAQQM RKESMDVPLL IGGATTSRKH TAVKIWPQYE ASVVHVLDAS RSVVVVNSLI QNPERRIEYM EDIKEEYDGL REDYYSTLVD KRWLSLDEAR KMRYTIDFEK YPPPPAPRRL GNKYLDEYPL EELVEYIDWT PFFQVYQLRG RYPNKDYPKI FNDKRVGEEA KKLFDDAQAR TARIRVVEWI TATAVVGVYR ACSSGDDINV LSLDGSGEVL ETFYGIRQQL DTEQDQTFAL GDFIAPEASG LPDHIALFCC QAGIGVEERK KMYNATHDID KSIMLEPWQI DWQSIRTDPD FWGYVPEEKL TLSDMLKVKY VGIRPAPGYP TQPDHREKDT LWRLLDAEKL SGGKMVLTES LMMMPAASVC ALCFAHEKAK YFAVGQINKD QVADYSARRG CTVEDSERWL GSSTLGYEPQ SQ // ID C5MAR2_CANTT Unreviewed; 312 AA. AC C5MAR2; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 07-JAN-2015, entry version 24. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EER32729.1}; GN ORFNames=CTRG_03154 {ECO:0000313|EMBL:EER32729.1}; OS Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Debaryomycetaceae; OC Candida/Lodderomyces clade; Candida. OX NCBI_TaxID=294747 {ECO:0000313|Proteomes:UP000002037}; RN [1] {ECO:0000313|Proteomes:UP000002037} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037}; 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; GG692398; EER32729.1; -; Genomic_DNA. DR RefSeq; XP_002548857.1; XM_002548811.1. DR GeneID; 8299782; -. DR KEGG; ctp:CTRG_03154; -. DR KO; K00547; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000002037; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002037}; KW Reference proteome {ECO:0000313|Proteomes:UP000002037}. SQ SEQUENCE 312 AA; 34524 MW; 9F16F7AA904AE5B8 CRC64; MGHFKEIFQQ KKLVIDGALG TELERLLPSS SASLPSNSPL WSGQALINNP ELVEQVHLDY INAGADIIIT STYQTSYASL NKYAGYDMKK SVELWNSALG AAKNAVNRSG RSDVIIAGSI GPYATVLANG SEYSGDYQGA TYDDLVEYHT PLFEFYDNSD VDVICIETIP NFTELKVVID MMKKYTKKEY FIAVNPQTAN ALSDGTTLDK VAEVFKTIED TSRFLGVGIN CTNYDLVNDI LKYFTDFPVL IYPNMGFVYD TETHKFVPEA NHELSWENAV KKWLNSDNVR AVGGCCSTGP SEISIVAKVL KH // ID C5NUG3_9BACL Unreviewed; 613 AA. AC C5NUG3; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 27-MAY-2015, entry version 28. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=GEMHA0001_0065 {ECO:0000313|EMBL:EER69149.1}; OS Gemella haemolysans ATCC 10379. OC Bacteria; Firmicutes; Bacilli; Bacillales; OC Bacillales Family XI. Incertae Sedis; Gemella. OX NCBI_TaxID=546270 {ECO:0000313|EMBL:EER69149.1}; RN [1] {ECO:0000313|EMBL:EER69149.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 10379 {ECO:0000313|EMBL:EER69149.1}; 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] {ECO:0000313|EMBL:EER69149.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 10379 {ECO:0000313|EMBL:EER69149.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EER69149.1}. 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; ACDZ02000004; EER69149.1; -; Genomic_DNA. DR RefSeq; WP_004263238.1; NZ_ACDZ02000004.1. DR ProteinModelPortal; C5NUG3; -. DR EnsemblBacteria; EER69149; EER69149; GEMHA0001_0065. DR PATRIC; 28763222; VBIGemHae122965_0098. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EER69149.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EER69149.1}. SQ SEQUENCE 613 AA; 68217 MW; 3800A9FDD7CC3921 CRC64; MRNLLERLEQ NVLVADGAMG TALYSNGLES CHEYNNISNP DSVEKIHKAY IEAGADIIQT NTYAAKKCQL KTYGYEDKFE EINIRAAEIA RKAAGENTFV FGTIGAIRGL RECELSLETI VNETIDQVKV LLSTNKVDAL LFETYYDQEE IRAVLTEARK LTDLPIITNI SLLEAGITQN GEKVTDALST LVNLGADIVG LNCHLGPYHM IKSLKQVPLF AQSYLSAYPN ASLLQLTQTI NGNEYRFRKN SAYFEQSAKL LVEEGVRLIG GCCGTTPEHI RAIKKGIKDL KPVKRKIITP LPAEEELVRV AHNEPTIVDK VKKQVTIIAE LDPPKHLNVD KFIEGAKAID KKNIEAITLA DNSLASTRIC NLAAATLLKE HISTPTLLHL TCRDHNLIGL QSRLMGFDLL GINNVLALTG DPSKLGDFPG ATSVYDMTSL KLIPFIKQLN EGLGYNGASL KKTTNFTVAA AYNPNVRDLS KTKRLVEKKI KAGTDYFITQ PVFEAEKIEQ LAEFAADYPD TPFFVGIMPI TSYNNAVFLH NEVPGIKLSE EFLAKLEEVK DDKELCQKIA LEESKKLLDV ALKHFKGIYL ITPFFRYDLT LELIDYVEEN KDK // ID C5P4X0_COCP7 Unreviewed; 363 AA. AC C5P4X0; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EER27760.1}; GN ORFNames=CPC735_030960 {ECO:0000313|EMBL:EER27760.1}; 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 {ECO:0000313|EMBL:EER27760.1, ECO:0000313|Proteomes:UP000009084}; RN [1] {ECO:0000313|EMBL:EER27760.1, ECO:0000313|Proteomes:UP000009084} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C735 {ECO:0000313|Proteomes:UP000009084}; 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. {ECO:0000313|EMBL:EER27760.1}. 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; ACFW01000025; EER27760.1; -; Genomic_DNA. DR RefSeq; XP_003069905.1; XM_003069859.1. DR UniGene; Cpo.217; -. DR STRING; 222929.C5P4X0; -. DR GeneID; 9695400; -. DR KEGG; cpw:CPC735_030960; -. DR EuPathDB; FungiDB:CPC735_030960; -. DR eggNOG; COG2040; -. DR KO; K00547; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000009084; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009084}; KW Methyltransferase {ECO:0000313|EMBL:EER27760.1}; KW Transferase {ECO:0000313|EMBL:EER27760.1}. SQ SEQUENCE 363 AA; 41205 MW; A1C0678CBB1530C8 CRC64; MGTVLEEPPY GFTFSAQTPL WSSHLLLSHP TTLSEIHRSY VDAGADIVLT ATYQASFEGF ARTAIVPANV PADHKQDERH GHATYRPMDA TRYMRSAIPL AYSSFNFSSK PPRVALSLGP YGATMCPVSA EYTGIYPEEM SNTAALEAWH AKRLEVYMED PETWRKIEFL GFETVRRWDE VLAIRGAMGK LLQIAESGQS RKWWISGVFP QEDIDEEDVR RWTSAAFGST SENGLHPWGI GVNCTRLENI ERIVDIMEDE LGREKLTDNG ERASVGSSWS SRPWLVLYPD GTQGEIYDPT LKTWVKKDEE EITESWPERC WRIVNHTWNR NAWNGILVGG CCRTRVHDIR ALRERIDSAW SGS // ID C5QPD0_9STAP Unreviewed; 612 AA. AC C5QPD0; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 27-MAY-2015, entry version 27. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HMPREF0793_1086 {ECO:0000313|EMBL:EES41300.1}; OS Staphylococcus caprae M23864:W1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=525378 {ECO:0000313|EMBL:EES41300.1}; RN [1] {ECO:0000313|EMBL:EES41300.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M23864:W1 {ECO:0000313|EMBL:EES41300.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EES41300.1}. 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; ACJB01000032; EES41300.1; -; Genomic_DNA. DR RefSeq; WP_002445126.1; NZ_GG696774.1. DR ProteinModelPortal; C5QPD0; -. DR EnsemblBacteria; EES41300; EES41300; HMPREF0793_1086. DR PATRIC; 31398552; VBIStaEpi14170_1886. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EES41300.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EES41300.1}. SQ SEQUENCE 612 AA; 68030 MW; 4232AD98060DB08A CRC64; MSQFLKHLQN NVLVADGAIG TILYSEGLDT CPEAYNLTHP DKVEHIHRSY IEAGADVIQT NTYGANFEKL KNFGLEHRVR EIHKAAVQIA KRAANEDTFI LGTVGGFRGV RQEEISLSTI QYHTELQIDT LINEGVDALL FETYYDLDEL KNIVVATRRK YNIPIIAQLT ASNTNYLVDG TEINEALKQL VECGADVVGL NCHHGPHHMQ RSFSHIELPE QAYLSCYPNA SLLDIENSEF KYSDNAQYFG DVAQELINEG VRLIGGCCGT TPEHIRYIKS AVQGLTPVKD KKVIPITKKS NRKPTSVMKQ NLTTKVKNGP TVIVELDTPK HLDTDTFFDN VGKLDEAGID AVTLADNSLA TVRVSNIAAA SLIKQRYDIE PLVHVTCRDR NLIGLQSHLL GLSLIGVNEI LAITGDPSKV GHLPGATNVY DVNSKGLTEL ALRFNQGINT DGDALKKHTN FNIAGAFDPN VRKLDGAVKR LEKKVASGMS YFITQPVYSK EKIKQVYEET KHLNTPFFIG IMPIASYNNA LFLHNEVPGI KMSEDVLNQF KAVKDDKEKT KELSLRLSKE LIDTVHEYFN GLYIITPFQK VDYSLELAAY SKSITANKEA IL // ID C5RZL1_9PAST Unreviewed; 296 AA. AC C5RZL1; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Homocysteine/selenocysteine methylase {ECO:0000313|EMBL:EER47866.1}; GN ORFNames=AM305_05519 {ECO:0000313|EMBL:EER47866.1}; OS Actinobacillus minor NM305. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=637911 {ECO:0000313|EMBL:EER47866.1}; RN [1] {ECO:0000313|EMBL:EER47866.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NM305 {ECO:0000313|EMBL:EER47866.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EER47866.1}. 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; ACQL01000055; EER47866.1; -; Genomic_DNA. DR RefSeq; WP_005822626.1; NZ_ACQL01000055.1. DR EnsemblBacteria; EER47866; EER47866; AM305_05519. DR PATRIC; 24361272; VBIActMin14942_0355. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EER47866.1}; KW Transferase {ECO:0000313|EMBL:EER47866.1}. SQ SEQUENCE 296 AA; 32494 MW; 99AA4D55527B6357 CRC64; MTITILDGGM SRELMRLNAP FRQPEWSALS LYEKPSAVQQ VHENFIQSGA EIITTNSYAV VPFHIGDQRF IADGKMLADL AGRLAKQAVK NSQKNVKIAG SLPPLFGSYR PDLFQAEKVK ETAQPLIDGL APYVDFWLCE TQSAIIEPQS IKPLLPDNRP LWVSFTLTDD EPTPEPQLRS GESVKMAVEK MIELGVQAIL FNCCQPEVIT EALNITRQAL AAHQATHIQI GAYANAFAPQ PKDATANDGL DEVRPDLDPQ AYLTWAQKWV ESGASIIGGC CGIGLEHIQA LSENLK // ID C5S2W6_9PAST Unreviewed; 1229 AA. AC C5S2W6; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 27-MAY-2015, entry version 33. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EER46721.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EER46721.1}; GN Name=metH {ECO:0000313|EMBL:EER46721.1}; GN ORFNames=AM305_11100 {ECO:0000313|EMBL:EER46721.1}; OS Actinobacillus minor NM305. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=637911 {ECO:0000313|EMBL:EER46721.1}; RN [1] {ECO:0000313|EMBL:EER46721.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NM305 {ECO:0000313|EMBL:EER46721.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EER46721.1}. 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; ACQL01000101; EER46721.1; -; Genomic_DNA. DR RefSeq; WP_005824570.1; NZ_ACQL01000101.1. DR EnsemblBacteria; EER46721; EER46721; AM305_11100. DR PATRIC; 24363584; VBIActMin14942_1475. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EER46721.1}; KW Transferase {ECO:0000313|EMBL:EER46721.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 246 246 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1229 AA; 136438 MW; 802FE6C99709744A CRC64; MQHNRIEQLK TALAQRILIL DGAMGTMIQQ FKLTEADFRG ERFKHSSVDL RGNNDLLTLT QPLVISSIHE KYLEAGADII ETNTFSSTTI AQADYDLQAV AYELNFAGAK LARIAADKYS TPEKPRFVAG ILGPTNRTAS ISPNVNDPGF RNITFMELVD AYAEATRGLI EGGSDIIMIE TIFDTLNAKA AAFAIDQVFE ELGVELPIMI SGTITDASGR TLSGQTTEAF YNSLRHAKPL SFGLNCALGP KELRPYVEVM SKICETYVSV HPNAGLPNAF GGYDLGADEM AAHIKEWAES GFLNIVGGCC GTTPEHIKAF ADVVAGIKPR ALPEIKTAMR LSGLEPLNID DESLFVNVGE RNNVTGSAKF KRLIKEEKFS EAIEIAIDQV ENGAQVIDVN MDEALLDSQK CMTRFLNIMA TEPDAAKVPV MIDSSKWEVI EAGLQSVQGK GIVNSISLKE GEEKFIHQAK LVRRYGAAVV VMAFDEVGQA DTEERKVEIC TRAYDILVNQ VGFPPEDIIF DPNIFAIGTG IEEHNNYGVD FINATGRIKR SLPHAKISGG VSNVSFSFRG NNVMREAIHA VFLYHAIKQG MDMGIVNAGQ LAIYDDLAPE LRDVIEDAVL NRRSDATDRL LDIAEKYRNV TASNSEDSGV AEWRTWAVEE RLKHALVKGI TNYIIEDTEE ARQKFPTPLE VIEGPLMDGM DVVGDLFGDG KMFLPQVVKS ARVMKQSVAY LEPFINATKQ KGSSSGKVVI ATVKGDVHDI GKNIVSVVLQ CNNFKVIDLG VMVPADKIIQ TAIDEKADII GLSGLITPSL DEMEYFLGEM NRLNLNIPVI IGGATTSKEH TAIKLYPKYK HEVIYTTNAS RAVTVCAALM NPDTKAELWE RMKKEYEQIQ EAFANKKAPR KQLPIEEARK NAFDAFSGEW ADYQVPTPKQ TGIVEYKNVP IATLRKFIDW SPFFRLWGLM GGYPDAFDYP EGGEEARRVW NDAQKVLDEL EQNHKLNPSG IMGIFPANSV GDDIEIYQNA DRTLVVGKVY NLRQQSERGR NSKSPYNLCL SDFIASKASG KQDWFGMFAV CAGIEEHDLV EGYKAAGDDY NAILLQAVGD RLAEAMAEYL HFELRTKVWG YSNETLDNDR LIREEYIGIR PAPGYPSCPE HTEKQIIWDL LEVEQRIGMK LTESYAMWPA ASVCGWYFTH PASNYFTLGR IDEDQAMDYA KRKGWNEREI VKWLGVAMK // ID C5T700_ACIDE Unreviewed; 354 AA. AC C5T700; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EER59738.1}; GN ORFNames=AcdelDRAFT_2680 {ECO:0000313|EMBL:EER59738.1}; OS Acidovorax delafieldii 2AN. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Acidovorax. OX NCBI_TaxID=573060 {ECO:0000313|EMBL:EER59738.1}; RN [1] {ECO:0000313|EMBL:EER59738.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=2AN {ECO:0000313|EMBL:EER59738.1}; 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. {ECO:0000313|EMBL:EER59738.1}. 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; ACQT01000100; EER59738.1; -; Genomic_DNA. DR RefSeq; WP_005797474.1; NZ_ACQT01000100.1. DR EnsemblBacteria; EER59738; EER59738; AcdelDRAFT_2680. DR PATRIC; 38321353; VBIAciDel137164_2598. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EER59738.1}; KW Transferase {ECO:0000313|EMBL:EER59738.1}. SQ SEQUENCE 354 AA; 38325 MW; 80B723A3E149099A CRC64; MSLPIYTRAA QLPDILAQRI VILDGAMGTM IQRFKLGEAQ YRGEGYSGAD GAGDRFKDFA YDVKGNNELL SLTRPDVIRD IHERYLAAGA DLIETNTFGA TTIAQEDYHM AHLAREMNLK SARLARAACD KYSTQDKPRF VAGALGPTPK TASISPDVND PGARNIDFET LRAAYYEQTE ALVEGGADVL LVETIFDTLN AKAALFAIDE FFEKSGERLP IIISGTVTDA SGRILSGQTV TAFWHSVRHA RPLAVGLNCA LGATLMRPYI QELNRVAEDT FISCYPNAGL PNPMSDTGFD ETPEVTSRLV HEFAAEGLVN IVGGCCGTTP DHIAAIGKAV APVKTRSLFY REAA // ID C5TJY8_NEIFL Unreviewed; 295 AA. AC C5TJY8; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EER56992.1}; GN ORFNames=NEIFL0001_2136 {ECO:0000313|EMBL:EER56992.1}; OS Neisseria flavescens SK114. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=596320 {ECO:0000313|EMBL:EER56992.1}; RN [1] {ECO:0000313|EMBL:EER56992.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK114 {ECO:0000313|EMBL:EER56992.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EER56992.1}. 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; ACQV01000010; EER56992.1; -; Genomic_DNA. DR RefSeq; WP_003683767.1; NZ_ACQV01000010.1. DR EnsemblBacteria; EER56992; EER56992; NEIFL0001_2136. DR PATRIC; 29958251; VBINeiFla25453_0445. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EER56992.1}; KW Transferase {ECO:0000313|EMBL:EER56992.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 204 204 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 277 277 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 278 278 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 295 AA; 32219 MW; 1D96C5636EE07F46 CRC64; MTVTILDGGM GRELHRRGAP FRQPEWSALA LMEAPDIVRE THLDFLRAGA QVVTTNSYAL VPFHIGQERF DAQAAEWARL AGRLAREAVE QSGTTAKVAA SLPPLFGSYR PDLFDKQVAP DLARPLISGL MPFADIWLAE TVSSLEEARF WRSSLPDDGK PFWVSFTLED TIPHDVPVLR SGENVHEAAD FAVEIGAAAM LFNCSQPEVM AEALKVAHEA QGRLKLGVYA NAFEPVQGQM NEANDGLDPI RADATPENYL SWARQWADLG AEIIGGCCGI APEHIRALAR GFKAV // ID C5UPQ0_CLOBO Unreviewed; 803 AA. AC C5UPQ0; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EES50079.1}; GN ORFNames=CLO_0798 {ECO:0000313|EMBL:EES50079.1}; OS Clostridium botulinum E1 str. 'BoNT E Beluga'. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=536233 {ECO:0000313|EMBL:EES50079.1, ECO:0000313|Proteomes:UP000005168}; RN [1] {ECO:0000313|EMBL:EES50079.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BoNT E Beluga {ECO:0000313|EMBL:EES50079.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EES50079.1}. 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; ACSC01000002; EES50079.1; -; Genomic_DNA. DR RefSeq; WP_003373180.1; NZ_ACSC01000002.1. DR ProteinModelPortal; C5UPQ0; -. DR EnsemblBacteria; EES50079; EES50079; CLO_0798. DR PATRIC; 26431584; VBICloBot69965_0754. DR Proteomes; UP000005168; Unassembled WGS sequence. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005168}; KW Methyltransferase {ECO:0000313|EMBL:EES50079.1}; KW Transferase {ECO:0000313|EMBL:EES50079.1}. SQ SEQUENCE 803 AA; 88398 MW; E9758494B5CF3AB4 CRC64; MGLREFIKDN ILVFDGAMGT MLQKEGLKLG ENPEIFNIEE SEKVKNVHKK YIENGAMVVT TNTFGANELK LDNTKYTVEE IIDAAISIAK DARGNKGIYI ALDIGPIGEL LEPMGTLSFE RAYDIFKRQM IQGEKSGADL ILIETMTDLY EAKAALLAAK ENTKLPVFCT MSFDESGRTF TGCTPESMAL TLGGIGADAI GINCSLGPKE LLPIVKRIKK ATNLPIMTQP NAGLPKLSFG EAIYDIIPEE FKYWVNEFIK EGVSIIGGCC GTNPEFIKEL RLLADSNKRL RRENIEFSAV CTPSKVVKIE GVKIIGERIN PTGKKLFKEA LKNNDIDYIL KQAIEQVEAG AEILDVNVGL PEINEKEMMV KVVKEIQGII DTPLQIDSSN VDVIEAGLRY YNGKCIVNSV NGEDDVLEKV LPLVKKYGAS VVGLTLDKRG IPKTAEERVE IAEKIINKAK EYGINKSDVF IDCLVLTASA QQAEVKETLK ALRKVKEELG VKTLLGVSNI SFGLPCRELI NETFLAMAIA SGLDLPIMNP NSTGMMDVIN SYNVLTNIDK GCERYISIYG NREIQSGVRY NSKGENKSDK NEEIQSNNSD LRYIVIKGLK DEAEEATKNI LESMNELDVV NEILIPSLDE VGLKYEKGEI FLPQLIQCAE TVKKSFEVIK KNIVINKSDN ISKGKIVLAT VKGDIHDIGK NIVKVILENY GYEIIDLGKD VPIETVVDAV LKNDIKLVGL SALMTTTLKS MKETIKALKD NGYSGKTFVG GAVLTSEYAK EICADYYAKD AKESVEIAKK ILG // ID C5VTW2_CLOBO Unreviewed; 788 AA. AC C5VTW2; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=MetH1 {ECO:0000313|EMBL:EES90498.1}; GN ORFNames=CLG_B0011 {ECO:0000313|EMBL:EES90498.1}; OS Clostridium botulinum D str. 1873. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=592027 {ECO:0000313|EMBL:EES90498.1, ECO:0000313|Proteomes:UP000006160}; RN [1] {ECO:0000313|EMBL:EES90498.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=1873 {ECO:0000313|EMBL:EES90498.1}; 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., Saunders E.S., RA Sims D.R., Smith L.A., Smith T.J., Sutton G., Brettin T.; 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. {ECO:0000313|EMBL:EES90498.1}. 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; ACSJ01000009; EES90498.1; -; Genomic_DNA. DR RefSeq; WP_003377396.1; NZ_ACSJ01000009.1. DR EnsemblBacteria; EES90498; EES90498; CLG_B0011. DR PATRIC; 26429816; VBICloBot14473_2127. DR Proteomes; UP000006160; Unassembled WGS sequence. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006160}. SQ SEQUENCE 788 AA; 87278 MW; E6E4FFF08E3092C2 CRC64; MIDINKILLK KHIFFDGAMG TMLQNRGISL GEIPPEIYNI LNPKVIKDIH KKYIDAGVDI ITTNTFGANE LKLKDSGYSV EEVIEAGVKL AKEVSNGNIV ALDIGPTGEM LEPIGNLKFN RAYEIFKRQV IAGVNAGCDI ILIETISDLY EAKAAILAAK ENSELPVFCT MTFGEDGRTF TGTDPLTMVS VLESLSVDAL GVNCSLGPKE ILGVVEEIIK YSSIPIIVQP NAGLPRVENN KTIFDITPKE FAFYGKVMAN KGVSILGGCC GTTDEYIKEV VKNLKYNVPL KIIKKNITMV SSSSKTIILG EGIKVVGERI NPTGKKEFRE ALKNNDINYI LKEAISQKKS GAHILDINLG LPEINEKDIM IRTIKELQGT INVPIQIDSS DTKVIEAAVR ICNGKPIINS VNGKEESMKS IFPIVKKYGT CVIALTLDEN GIPNTIEDRV KIAEKIINTA KTYGIDKKDI IVDCLALTAS AQQKEVMGTL DALEIIKKQF KVKTLLGISN ISFGLPKREL INRTFLTMAL TKGLDVPILN PKDREAMETI KSFEVLANID KNCENYIKEI DDFKKEKIDT REKMDLKHLV ISGLTEDVLK MTKTLLDKKN GIEIMDEYLI PALDEIGKEY EEGTIFLPQL IKCGETVKEA FNIIKKHMDK KNNDTVIRGK IVLATVKDDI HDIGKNIVKL LLENYGFEVI DLGKNVSVER ILEVVKKHNI KLVGLSALMT TTVKSMEETI LKLKETIPLC KVFVGGAVLN KEYAKQIGAD YYAKDARESV FIANEVFK // ID C5WSP6_SORBI Unreviewed; 323 AA. AC C5WSP6; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 07-JAN-2015, entry version 32. DE SubName: Full=Putative uncharacterized protein Sb01g042580 {ECO:0000313|EMBL:EER95257.1}; GN Name=Sb01g042580 {ECO:0000313|EMBL:EER95257.1}; GN ORFNames=SORBIDRAFT_01g042580 {ECO:0000313|EMBL:EER95257.1}; 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 {ECO:0000313|Proteomes:UP000000768}; RN [1] {ECO:0000313|EMBL:EER95257.1, ECO:0000313|Proteomes:UP000000768} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768}; 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; CM000760; EER95257.1; -; Genomic_DNA. DR RefSeq; XP_002468259.1; XM_002468214.1. DR UniGene; Sbi.7916; -. DR STRING; 4558.Sb01g042580.1; -. DR EnsemblPlants; Sb01g042580.1; Sb01g042580.1; Sb01g042580. DR GeneID; 8056874; -. DR KEGG; sbi:SORBI_01g042580; -. DR Gramene; C5WSP6; -. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR InParanoid; C5WSP6; -. DR KO; K00547; -. DR OMA; AINDPLW; -. DR Proteomes; UP000000768; Chromosome 1. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000768}; KW Reference proteome {ECO:0000313|Proteomes:UP000000768}. SQ SEQUENCE 323 AA; 34815 MW; 6F695C0B53ED530C CRC64; MGALEELVAK AGGCAVIDGG FATQLEALGA DINDPLWSAA CLITRPHLVK EVHMQYLEAG ADIIISSSYQ ATIPGFLARG MSVDEAEDLL RTSVKLAVEA RDEFWKSALR KAKPIYNRAL VAASVGSYGA YLADGSEYSG SYGADITAEK LKDFHRRRLQ VLASAGPDLI AFEAIPNKME AQALVELLEE EKVQVPSWIC FSSVDGKNLC SGESFADCLK ILDTSDKVAV VGVNCTPPQF IEGIICEFKK QTKKAIAVYP NSGEVWDGRA KRWLPVECLG HKSFDALAKR WQEAGASLIG GCCRTTPSTI RAVSKILKGK TGH // ID C5WSP7_SORBI Unreviewed; 91 AA. AC C5WSP7; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 07-JAN-2015, entry version 25. DE SubName: Full=Putative uncharacterized protein Sb01g042590 {ECO:0000313|EMBL:EER95258.1}; GN Name=Sb01g042590 {ECO:0000313|EMBL:EER95258.1}; GN ORFNames=SORBIDRAFT_01g042590 {ECO:0000313|EMBL:EER95258.1}; 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 {ECO:0000313|Proteomes:UP000000768}; RN [1] {ECO:0000313|EMBL:EER95258.1, ECO:0000313|Proteomes:UP000000768} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768}; 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; CM000760; EER95258.1; -; Genomic_DNA. DR RefSeq; XP_002468260.1; XM_002468215.1. DR STRING; 4558.Sb01g042590.1; -. DR EnsemblPlants; Sb01g042590.1; Sb01g042590.1; Sb01g042590. DR GeneID; 8085288; -. DR KEGG; sbi:SORBI_01g042590; -. DR Gramene; C5WSP7; -. DR eggNOG; NOG287390; -. DR Proteomes; UP000000768; Chromosome 1. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000768}; KW Reference proteome {ECO:0000313|Proteomes:UP000000768}. SQ SEQUENCE 91 AA; 9661 MW; EE46704F93D0EEB3 CRC64; MGALEELVAK AGGCAVIDGG FATELEALGA DINDLLWSAA CLITRPHLIK EARHGAAFQA GFRNRARVEL MTCEQPHRCA AGPAMGREVR T // ID C5XLK6_SORBI Unreviewed; 353 AA. AC C5XLK6; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 27-MAY-2015, entry version 34. DE SubName: Full=Putative uncharacterized protein Sb03g036040 {ECO:0000313|EMBL:EES03696.1}; GN Name=Sb03g036040 {ECO:0000313|EMBL:EES03696.1}; GN ORFNames=SORBIDRAFT_03g036040 {ECO:0000313|EMBL:EES03696.1}; 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 {ECO:0000313|Proteomes:UP000000768}; RN [1] {ECO:0000313|EMBL:EES03696.1, ECO:0000313|Proteomes:UP000000768} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000762; EES03696.1; -; Genomic_DNA. DR RefSeq; XP_002458576.1; XM_002458531.1. DR STRING; 4558.Sb03g036040.1; -. DR EnsemblPlants; Sb03g036040.1; Sb03g036040.1; Sb03g036040. DR GeneID; 8072141; -. DR KEGG; sbi:SORBI_03g036040; -. DR Gramene; C5XLK6; -. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR InParanoid; C5XLK6; -. DR KO; K00547; -. DR OMA; YGRSVTK; -. DR Proteomes; UP000000768; Chromosome 3. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000768}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000768}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 254 254 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 353 AA; 37522 MW; BE2DBD7F8D6F00E2 CRC64; MSLGGGGPIV DAAGALRGFV REAGGCAVVD GGLGTELEAH GADLHDALWS AKCLASAPHL IRKVHLDYLE AGADVIISAS YQATIEGFQS RGFSRDESEE LLRRSVHVAQ EARRVFVAEG DVDSSRSRRE RERERPPVLV AASIGSYGAY RADGSEYSGD YGKSVTKEAL KDFHRRRLQV LAGAGPDLIA FETIPNKLEA QAYAELLEEN GIRIPAWFSF TSKDGVHAAS GDPITECAAV ADSCQRVAAV GVNCTSPRLI HGLILSIKKV TSKPIVVYPN SGETYIADTN EWVDSDGATG TDFVSSVGEW RRAGAALIGG CCRTSPATVR AIARALREAD ADEYDDMPAV AVL // ID C5YRH9_SORBI Unreviewed; 331 AA. AC C5YRH9; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 07-JAN-2015, entry version 32. DE SubName: Full=Putative uncharacterized protein Sb08g020830 {ECO:0000313|EMBL:EES16331.1}; GN Name=Sb08g020830 {ECO:0000313|EMBL:EES16331.1}; GN ORFNames=SORBIDRAFT_08g020830 {ECO:0000313|EMBL:EES16331.1}; 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 {ECO:0000313|Proteomes:UP000000768}; RN [1] {ECO:0000313|EMBL:EES16331.1, ECO:0000313|Proteomes:UP000000768} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768}; 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; EES16331.1; -; Genomic_DNA. DR RefSeq; XP_002442493.1; XM_002442448.1. DR UniGene; Sbi.2124; -. DR STRING; 4558.Sb08g020830.1; -. DR EnsemblPlants; Sb08g020830.1; Sb08g020830.1; Sb08g020830. DR GeneID; 8070125; -. DR KEGG; sbi:SORBI_08g020830; -. DR Gramene; C5YRH9; -. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR InParanoid; C5YRH9; -. DR KO; K00547; -. DR OMA; SEWCKDG; -. DR Proteomes; UP000000768; Chromosome 8. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000768}; KW Reference proteome {ECO:0000313|Proteomes:UP000000768}. SQ SEQUENCE 331 AA; 35895 MW; 9F7010BD01C80022 CRC64; MVGTAAGAAE GAVRRWVDAA GGRLVLDGGL ATELEANGAD LNDPLWSAKC LLSSPHLIRK VHMDYLEAGA NILITASYQA TIQGFESKGF SKEQSENLLT KSVEIALEAR EMFLKEHLEK SIPIQHPILV AASIGSYGAY LADGSEYSGD YGEAGTKEFL KDFHRRRLQV LAEAGPDLIA FETIPNKLEA QAYVELLEEC NINIPAWLSF NSKDGVHIVS GDSVIECTTI ADKCAKVGAV GINCTPPRFI HGLILSIRKV TDKPILIYPN SGERYDGEKK EWVESTGVSD GDFVSYVNEW CKDGAALIGG CCRTTPNTIR AIQRTLNQGF N // ID C6AML8_AGGAN Unreviewed; 1229 AA. AC C6AML8; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 27-MAY-2015, entry version 49. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACS97075.1}; GN OrderedLocusNames=NT05HA_0674 {ECO:0000313|EMBL:ACS97075.1}; OS Aggregatibacter aphrophilus (strain NJ8700) (Haemophilus aphrophilus). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Aggregatibacter. OX NCBI_TaxID=634176 {ECO:0000313|EMBL:ACS97075.1, ECO:0000313|Proteomes:UP000002733}; RN [1] {ECO:0000313|EMBL:ACS97075.1, ECO:0000313|Proteomes:UP000002733} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NJ8700 {ECO:0000313|EMBL:ACS97075.1, RC ECO:0000313|Proteomes:UP000002733}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001607; ACS97075.1; -; Genomic_DNA. DR RefSeq; WP_005700366.1; NC_012913.1. DR RefSeq; YP_003007162.1; NC_012913.1. DR STRING; 634176.NT05HA_0674; -. DR EnsemblBacteria; ACS97075; ACS97075; NT05HA_0674. DR KEGG; aap:NT05HA_0674; -. DR PATRIC; 31916433; VBIAggAph86045_0629. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; AAPH634176:GHVL-660-MONOMER; -. DR Proteomes; UP000002733; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002733}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 757 757 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1229 AA; 136596 MW; 958AB71D73D55CFB CRC64; MKNTTELLKK SLAERILILD GAMGTMIQKY KLTEADFRGE RFKESAVDLR GNNDLLTLTQ PLLISAIHEK YLEAGADIIE TNTFSSTTIA QADYDLQSIA YELNFAGAKL ARLAADKYST QEKPRFVAGI LGPTNRTASI SPNVNDPGFR NVTFMELVDA YSEATRGLIK GGADLIMIET IFDTLNAKAA IFAIETVFEE LAVELPIMIS GTITDASGRT LSGQTTEAFY NSLRHAKPLT FGLNCALGPK ELRQYVEQLS KISETYVSVH PNAGLPNAFG GYDLGAEDMA AHLKEWAESG FVNIIGGCCG TTPEHIKAFA EAVENIPPRK LPQIKTAMRL SGLEPLNIDD ESLFVNVGER NNVTGSAKFK RLIKEDKFAE AIEIAIDQVK NGAQVIDVNM DEALLDSKKC MTRFLNIMAT EPDAAKVPVM IDSSKWEVIE AGLQSVQGKP IVNAISLKEG EEIFIEHAKL VRKYGAAVVV MAFDEVGQAD TEDRKVEICT RAYNILVNQV GFPPEDIIFD PNIFAIGTGI EEHNNYGVDF INATGRIKRS LPHAKISGGV SNVSFSFRGN NVMREAIHAV FLYHAIKQGM DMGIVNAGQL AIYDDLDPEL RNVIEDAVLN RTPDGTERLL DIAEKYRNQG NDESAVDSVA EWRTWPVEER LKHALVKGIT THIIEDTEEA RQKLPTPLEV IEGPLMAGMD VVGDLFGDGK MFLPQVVKSA RVMKQSVAYL EPFINATKQK GSSNGKVVIA TVKGDVHDIG KNIVSVVLQC NNFEVIDLGV MVPADKIIQT AIDEKADLIG LSGLITPSLD EMEYFLSEMM RLGLDLPVLI GGATTSKEHT AIKLYPKYKQ HGVFYTSNAS RAVTVCATLM NPEGRAALWE QFKKDYEKIQ QSFANRKPLR KQLSIEEARA NRFYGFSGEW ADYVPPTPKQ TGIVEFKNVP IAELRKFIDW SPFFRVWGLM GGYPDAFDHP ESGQEARRVW NDAQAMLDEF EKNHKLNPSG ILGIFPAERV GDDVVLFSDE DRTQAIGTAY GLRQQTERGK NSKSPFNFCL SDFIADRESG KKDWFGMFAV CAGVEEMDLV EGYKAAGDDY NAILLQAVGD RLAEAMAEYL HFELRTRIWS YTQEEFDNQR LINENYVGIR PAPGYPSCPE HTEKALIWDL LEVEQRIGMK LTESYAMWPA ASVCGWYFTH PASNYFTLGR IDEDQAQDYA NRKGWDERAM MKWLGVAMK // ID C6ASC4_RHILS Unreviewed; 1257 AA. AC C6ASC4; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 29-APR-2015, entry version 53. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACS57171.1}; GN OrderedLocusNames=Rleg_2911 {ECO:0000313|EMBL:ACS57171.1}; OS Rhizobium leguminosarum bv. trifolii (strain WSM1325). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS57171.1, ECO:0000313|Proteomes:UP000002256}; RN [1] {ECO:0000313|EMBL:ACS57171.1, ECO:0000313|Proteomes:UP000002256} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WSM1325 {ECO:0000313|EMBL:ACS57171.1, RC ECO:0000313|Proteomes:UP000002256}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001622; ACS57171.1; -; Genomic_DNA. DR RefSeq; WP_012758338.1; NC_012850.1. DR RefSeq; YP_002976710.1; NC_012850.1. DR STRING; 395491.Rleg_2911; -. DR EnsemblBacteria; ACS57171; ACS57171; Rleg_2911. DR KEGG; rlg:Rleg_2911; -. DR PATRIC; 23113247; VBIRhiLeg48398_3680. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; RLEG395491:GHX2-2942-MONOMER; -. DR Proteomes; UP000002256; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002256}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 260 260 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 776 776 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1257 AA; 138946 MW; 7DC2807977F25EEA CRC64; MFDNLFGPET GKRDGSEVFA ALKQAASERI LVLDGAMGTQ IQGLGYDEDQ FRGTRFIGCA CHQKGNNDLL ILTQPDAIEE IHYRYAKAGA DILETNTFSS TRIAQADYEM EGAVYDLNKE GAEIVRRAAQ RAEREDGRRR FVAGAIGPTN RTASISPDVN NPGFRAVTFD DLRSAYGEQI DGLIDGGADI ILIETIFDTL NAKAAIFACE ERFEAKGVRL PVMISGTITD LSGRTLSGQT PSAFWNSVRH ANPFTIGLNC ALGANAMRPH LQELSGVADT FICAYPNAGL PNEFGQYDET PELMAAQIDG FAREGLVNIV GGCCGSTPEH IKAIAETVAK YKPRPIPEHR PFMSLSGLEP FELTKDIPFV NVGERTNVTG SARFRKLITN ADFTAALDVA RDQVENGAQV IDINMDEGLI DSEKAMVEFL NLIAAEPDIA RVPVMIDSSK FSIIESGLKR VQGKPIVNSI SLKEGEENFL AQARLLHNYG AAVVVMAFDE TGQADSYERK VDICTRAYKL LTEKIGYPPE DIIFDPNIFA VATGIEEHNN YGVDFIEATR TIRERMPLVH ISGGVSNLSF SFRGNEPVRE AMHAVFLYHA IQAGMDMGIV NAGQLAVYDN IDPELREACE DVVLNRRPDG TERLLEVAEK FRGGAAREGR VQDLSWREWS VEKRLEHALV NGITEYIEAD TEEARQQAVR PLHVIEGPLM AGMNVVGDLF GSGKMFLPQV VKSARVMKQA VAVLLPYMEE EKRLNGGEER RSAGKILMAT VKGDVHDIGK NIVGVVLACN NYEIVDLGVM VPATKILETA IAEKVDVIGL SGLITPSLDE MVHVAAEMER QGFEIPLLIG GATTSRVHTA VKIHPGYNKG QTIYVTDASR AVGVVSALLS PENRQAYVDD IRAEYAKVAA AHARSEAEKV RLPLPRAREN AHKVDWSAYR PVKPQFFGTR VFEDYDLAEL AKYIDWTPFF QTWELRGRYP TILEDEKQGE AARALWADAQ AMLKKIIDEK WFRPRAVIGF WPAGAVGDDI RLFTDESRKH ELETFYTLRQ QLSKRDGRAN VALSDFVAPV TSGVQDYVGG FVVTAGIEEI AISERFERAN DDYSSILVKA LADRFAEAFA ERMHEQVRRE YWGYAKDETL SKEDLITEAY AGIRPAPGYP AQPDHTEKAT LFKLLDAEKA AGVKLTESYA MWPGSSVSGL YIGHPDSYYF GVAKVERDQV EDYAARKQMA VSEVERWLGP VLNYVPRKTD EQIEDAA // ID C6ASN0_RHILS Unreviewed; 315 AA. AC C6ASN0; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 27-MAY-2015, entry version 33. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACS55279.1}; GN OrderedLocusNames=Rleg_0984 {ECO:0000313|EMBL:ACS55279.1}; OS Rhizobium leguminosarum bv. trifolii (strain WSM1325). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS55279.1, ECO:0000313|Proteomes:UP000002256}; RN [1] {ECO:0000313|EMBL:ACS55279.1, ECO:0000313|Proteomes:UP000002256} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WSM1325 {ECO:0000313|EMBL:ACS55279.1, RC ECO:0000313|Proteomes:UP000002256}; 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; ACS55279.1; -; Genomic_DNA. DR RefSeq; WP_012756632.1; NC_012850.1. DR RefSeq; YP_002974818.1; NC_012850.1. DR STRING; 395491.Rleg_0984; -. DR EnsemblBacteria; ACS55279; ACS55279; Rleg_0984. DR KEGG; rlg:Rleg_0984; -. DR PATRIC; 23109332; VBIRhiLeg48398_1746. DR eggNOG; COG2040; -. DR HOGENOM; HOG000179103; -. DR OMA; CCGTDHR; -. DR OrthoDB; EOG6R5C46; -. DR BioCyc; RLEG395491:GHX2-992-MONOMER; -. DR Proteomes; UP000002256; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002256}; KW Methyltransferase {ECO:0000313|EMBL:ACS55279.1}; KW Transferase {ECO:0000313|EMBL:ACS55279.1}. SQ SEQUENCE 315 AA; 34336 MW; 20910862ACD91816 CRC64; MAKYRNCLPQ LKGGTFITDG GMETTMIFQE GIELPHFAAF ILLASEDGRQ RMRNYYRRYL DVSRRHGTGF VLDTATWRAN PDWGQKLGYT SEALKAVNEE AIDLLVGLRS AYERPEQPIV ISGAIGPRGD GYKAGFMDAA EAEDYHAFQI GAFAGTEADM VSAFTLTNID EAIGVARAAQ ALGMPSAISF TLETDGRLVT GRSIQEAIET TDAMTGGAPA YYMINCAHPT HFETALDPGS AWVRRISGIR ANASTMSHEQ LDNSETLDAG DPEDLGRRYR TLIDRMPELR VLGGCCGTDH RHIAAICEAC LPQAA // ID C6BAN4_RHILS Unreviewed; 302 AA. AC C6BAN4; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 27-MAY-2015, entry version 34. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACS61142.1}; GN OrderedLocusNames=Rleg_6392 {ECO:0000313|EMBL:ACS61142.1}; OS Rhizobium leguminosarum bv. trifolii (strain WSM1325). OG Plasmid pR132505 {ECO:0000313|EMBL:ACS61142.1, OG ECO:0000313|Proteomes:UP000002256}. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS61142.1, ECO:0000313|Proteomes:UP000002256}; RN [1] {ECO:0000313|EMBL:ACS61142.1, ECO:0000313|Proteomes:UP000002256} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001627; ACS61142.1; -; Genomic_DNA. DR RefSeq; WP_012760659.1; NC_012854.1. DR RefSeq; YP_002979387.1; NC_012854.1. DR ProteinModelPortal; C6BAN4; -. DR STRING; 395491.Rleg_6392; -. DR EnsemblBacteria; ACS61142; ACS61142; Rleg_6392. DR KEGG; rlg:Rleg_6392; -. DR PATRIC; 23118684; VBIRhiLeg48398_6367. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; DVITANS; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; RLEG395491:GHX2-7114-MONOMER; -. DR Proteomes; UP000002256; Plasmid pR132505. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002256}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ACS61142.1}; KW Plasmid {ECO:0000313|EMBL:ACS61142.1}; KW Transferase {ECO:0000313|EMBL:ACS61142.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 209 209 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 302 AA; 32855 MW; B76B95F92CF5D35C CRC64; MSTMRILDGG MSRELLRLGA ELKQPEWSAL ALINAPDIVR KVHQEFIAAG SEVVTTNSYA LVPFHIGEDR FWKEGPALIR LAGRLAREAA DAVTDRKVLV AGSLPPIFGS YEPQNFQPSR VQDYLEVLVE NLSPFVDIWL GETLSLIAEA EAVRKAVATS GKPLWISFTL ADNEVAIRGG EPKLRSEERV EDAASWVVSS GAEALLFNCS KPEVMQAAVE TAARVFRTMD ARIEIGVYAN AFEGEQGEAA ANEGLHKTRN DLNDDAYSRY ACSWAEAGAT IIGGCCGIGA AHIHRLKKTL LD // ID C6BKJ7_RALP1 Unreviewed; 346 AA. AC C6BKJ7; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACS61466.1}; GN OrderedLocusNames=Rpic12D_0156 {ECO:0000313|EMBL:ACS61466.1}; OS Ralstonia pickettii (strain 12D). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=428406 {ECO:0000313|EMBL:ACS61466.1, ECO:0000313|Proteomes:UP000008208}; RN [1] {ECO:0000313|EMBL:ACS61466.1, ECO:0000313|Proteomes:UP000008208} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=12D {ECO:0000313|EMBL:ACS61466.1, RC ECO:0000313|Proteomes:UP000008208}; 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; ACS61466.1; -; Genomic_DNA. DR RefSeq; WP_012760981.1; NC_012856.1. DR RefSeq; YP_002980138.1; NC_012856.1. DR STRING; 428406.Rpic12D_0156; -. DR EnsemblBacteria; ACS61466; ACS61466; Rpic12D_0156. DR KEGG; rpf:Rpic12D_0156; -. DR PATRIC; 20239275; VBIRalPic57998_0758. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; RPIC428406:GH9Y-156-MONOMER; -. DR Proteomes; UP000008208; Chromosome 1. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008208}; KW Methyltransferase {ECO:0000313|EMBL:ACS61466.1}; KW Transferase {ECO:0000313|EMBL:ACS61466.1}. SQ SEQUENCE 346 AA; 37526 MW; 47366F3BE7438800 CRC64; MTAPLPYTRA ANLPALLRER ILILDGAMGT MIQRYKLNEA QYRGERFADH PIDVKGNNEL LLLTRPDVIR EIHEQYLAAG ADLIETNTFG ATTIAQEDYK MAELAYEMNV VAARLAREAC DKYSTPDKPR FVAGAFGPTP KTASISPDVN DPGARNVSFD QLRDAYYEQG KALLEGGADV FLVETIFDTL NAKAALFAID QLFEDTGERV PVMISGTVTD ASGRILSGQT VEAFWNSLRH AKPITFGLNC ALGAALMRPY IAELAKICDA AVSCYPNAGL PNPMSDTGFD ETPEVTSSLV DEFASAGLVN LVGGCCGTTP EHIKAIAERV ANRKPRAWPG QYKEAA // ID C6BTZ8_DESAD Unreviewed; 806 AA. AC C6BTZ8; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 01-APR-2015, entry version 34. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACS81707.1}; GN OrderedLocusNames=Desal_3661 {ECO:0000313|EMBL:ACS81707.1}; 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 {ECO:0000313|EMBL:ACS81707.1, ECO:0000313|Proteomes:UP000002601}; RN [1] {ECO:0000313|EMBL:ACS81707.1, ECO:0000313|Proteomes:UP000002601} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14822 / DSM 2638 / NCIB 8403 / VKM B-1763 RC {ECO:0000313|Proteomes:UP000002601}; 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 ----------------------------------------------------------------------- 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; ACS81707.1; -; Genomic_DNA. DR RefSeq; WP_015853523.1; NC_012881.1. DR RefSeq; YP_002993246.1; NC_012881.1. DR STRING; 526222.Desal_3661; -. DR EnsemblBacteria; ACS81707; ACS81707; Desal_3661. DR KEGG; dsa:Desal_3661; -. DR PATRIC; 21762983; VBIDesSal121003_3677. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; DSAL526222:GHES-3766-MONOMER; -. DR Proteomes; UP000002601; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002601}; KW Methyltransferase {ECO:0000313|EMBL:ACS81707.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002601}; KW Transferase {ECO:0000313|EMBL:ACS81707.1}. SQ SEQUENCE 806 AA; 86812 MW; 9BCDA9F2C7CCBA06 CRC64; MPDFRKALSD DKIYFFDGGY GTFLQSRGLP AGMSPELFGL QSPEVIKSVH KDYVDAGANV LTTNTFGGSR PKLGADVDVI GLNREMALLA RSVGGDNVFI AGSVGPTGHF VQPLGEMTFK EMVEIYKEQI TGLVEGGVDL ILGETHFDLA EARAVVIAAR EVCDLPVALS MTFESPSACL TGTSPATFID TMQNMGVELM GTNCSAGPEQ ILEVLENMQP RLCSPLLVEA NAGLPELDEN RNTVFRLQPE PFAEQSAKFV DVGAKFIGGC CGTGPDHIRA LRNKVDGAKW KRAVPQEDCQ MVLTSRSQSV KIGFEQRGVI IGERINPTGK KQLIAELQKG QFTEAMKFAE EQIAVGAPVL DVNVGAPMVN EVEILPALVK EIFAQHSAPL SIDSTNPDAV EAALWEYPGS PLVNSISGEP GRMERLGPLC KKFGAPFILL PIVGSKLPIT CAEKVEVVSE LLKQADDLGI PRRLIMVDAL ALTVSSKPMA ARHCLDFIKH CKEEWNLPTV LGLSNISFGL PARELLNSSF LTLCQGQGMA AFISNPNSVR LREALYANEV MLCRDPQAEQ YIERYADWTP SGDGGQSGAA GGGKKADKSG AENLFDAVVK GDRGSIVALV ERDLEGGREP FAMVNEDLIP AIMEVGEKYE RKEYFLPQLL QSAETLQKGF EKIKPLLEAS GDMEEKATII MATVEGDIHD IGKNIVCLML KNHGYNVIDL GKDVPAETIV NAAEEHGAKI VGLSALMTTT MVRMEDTINL IKERNLDIKV MIGGAVITGG FCDSIGADGW STDAVAAVKV AKNLLQ // ID C6C8P4_DICDC Unreviewed; 1228 AA. AC C6C8P4; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 27-MAY-2015, entry version 45. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACS84265.1}; GN OrderedLocusNames=Dd703_0454 {ECO:0000313|EMBL:ACS84265.1}; OS Dickeya dadantii (strain Ech703). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Dickeya. OX NCBI_TaxID=579405 {ECO:0000313|EMBL:ACS84265.1, ECO:0000313|Proteomes:UP000002734}; RN [1] {ECO:0000313|EMBL:ACS84265.1, ECO:0000313|Proteomes:UP000002734} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ech703 {ECO:0000313|EMBL:ACS84265.1, RC ECO:0000313|Proteomes:UP000002734}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001654; ACS84265.1; -; Genomic_DNA. DR RefSeq; WP_012764084.1; NC_012880.1. DR RefSeq; YP_002986087.1; NC_012880.1. DR STRING; 579405.Dd703_0454; -. DR EnsemblBacteria; ACS84265; ACS84265; Dd703_0454. DR KEGG; dda:Dd703_0454; -. DR PATRIC; 21788066; VBIDicDad95084_0486. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; DDAD579405:GHJU-464-MONOMER; -. DR Proteomes; UP000002734; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002734}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1228 AA; 135386 MW; CAAECFF1D57FFA4F CRC64; MAKNRQQELQ QQLDQRIMIL DGGMGTMIQG YRLQEADYRG ARFADWHSDL KGNNDLLVLT KPDVIAAIHH DYLAAGADIL ETNTFNATRI AMADYDMEAL SAEINTVAAR LARTCADEWT ARTPERPRYV AGVLGPTNRT ASISPDVNDP AYRNVSFDQL VDAYRESTRA LIEGGVDLIL IETIFDTLNA KAAVYAVECE FEALGITLPV MISGTITDAS GRTLSGQTTE AFYNSLRHAR PLSFGLNCAL GPDELRQYVA ELARISECYV SAHPNAGLPN AFGEYDLDAR EMAQQVGEWA QSGFLNIIGG CCGTTPAHIA AMAQAVDGVP PRKLPQTPVA CRLSGLEPLN IGADTLFVNV GERTNVTGSA KFKRLIKEEK YNEALDVARQ QVENGAQIID INMDEGMLDA EAAMVRFLNL IAGEPDIARV PIMIDSSKWD VVEAGLKCIQ GKGIVNSISM KEGVDIFIEH AKKVRRYGAA VVVMAFDEVG QADTRERKID ICRRAYRILT EEVGFPPEDI IFDPNIFAVA TGIEEHNNYA VDFIGACDDI KTQLPHALIS GGVSNVSFSF RGNEPVREAI HAVFLYYAIR NGMDMGIVNA GQLAIYDDLP AELRDAVEDV VLNRRTDGTE RLLAIAEKYR GSKSDDDSNK GEAEWRGWPV KKRLEYALVK GITEFIEADT EEARAQAARP IEVIEGPLMD GMNVVGDLFG AGKMFLPQVV KSARVMKQAV AYLEPFIQAS KEAGSSAGKI LLATVKGDVH DIGKNIVGVV LQCNNYEIID LGVMVPSDKI LKTAREEKVD IIGLSGLITP SLDEMVNVAK EMERQGFTLP LLIGGATTSK AHTAVKIEQN YSGPTVYVQN ASRSVSVVSS LLSATQHDEF VARIRREYET VRIQHARKKP RTPPVSLDAA RENAQSFDWE SYTPPAAHRL GVHPVSAGID TLRHYIDWTP FFMTWSLAGK YPNILEDEVV GEEAKRLFAD ANAMLDQLSA DGTLNPRGVV GLFPANRVGD DIEIYTDERR DTVSALSCHL RQQTEKTDFP NYCLADFVAP KSSGKPDYIG AFAVTGGLEE DELAAQWEAQ HDDYNKIMLK ALADRLAEAF AEYLHERVRK VYWGYAPNEN LGNDELIREN YQGIRPAPGY PACPDHTEKA ILWQLLDVDN TVGMKLTESY AMWPGASVSG WYFSHPDSKY FAVAQIQRDQ VDDYAARKHM PVADVERWLA PNLGYDAD // ID C6CI13_DICZE Unreviewed; 1228 AA. AC C6CI13; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 27-MAY-2015, entry version 47. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACT05259.1}; GN OrderedLocusNames=Dd1591_0369 {ECO:0000313|EMBL:ACT05259.1}; OS Dickeya zeae (strain Ech1591). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Dickeya. OX NCBI_TaxID=561229 {ECO:0000313|EMBL:ACT05259.1, ECO:0000313|Proteomes:UP000002735}; RN [1] {ECO:0000313|EMBL:ACT05259.1, ECO:0000313|Proteomes:UP000002735} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ech1591 {ECO:0000313|EMBL:ACT05259.1, RC ECO:0000313|Proteomes:UP000002735}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001655; ACT05259.1; -; Genomic_DNA. DR RefSeq; WP_012768142.1; NC_012912.1. DR RefSeq; YP_003002738.1; NC_012912.1. DR STRING; 561229.Dd1591_0369; -. DR EnsemblBacteria; ACT05259; ACT05259; Dd1591_0369. DR KEGG; dze:Dd1591_0369; -. DR PATRIC; 21796590; VBIDicZea111179_0379. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; DZEA561229:GJ85-385-MONOMER; -. DR Proteomes; UP000002735; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002735}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1228 AA; 135422 MW; 3AE8B5AE892DCE39 CRC64; MMANRLQALQ QQLAQRIMVL DGGMGTMIQS YRLQEEDYRG ERFADWHCDL KGNNDLLVLS KPEVITAIHH DYLAAGADIL ETNTFNATRI AMADYEMEAL SAEINTVAAR LARACADEWT ARTPERPRYV AGVLGPTNRT ASISPDVNDP AYRNVSFDQL VDAYRESTRA LVEGGVDIIL IETIFDTLNA KAAIFAVETE FEALGVTLPV MLSGTITDAS GRTLSGQTTE AFYNSLRHAR PLSFGLNCAL GPDELRQYVA ELSRIAECYV TAHPNAGLPN AFGEYDLDAD EMARQIGEWA QSGFLNIIGG CCGTTPEHIA AMVNAVEGVA PRALPTLPVA CRLAGLEPLN IGDDTLFVNV GERTNVTGSA KFKRLIKEEK YNEALDVARQ QVESGAQIID INMDEGMLNA EAAMVRFLNL IAGEPDIARV PIMIDSSKWD VVEAGLKCIQ GKGIVNSISM KEGVDAFVHH ARLVRRYGAA VVVMAFDEVG QADTRARKIE ICRRAYHILT EEVGFPPEDI IFDPNIFAVA TGIDEHNNYA VDFIEACADI KAQLPHALIS GGVSNVSFSF RGNEPVREAI HAVFLYYAIR NGMDMGIVNA GQLAIYDDLP AELRDAVEDV ILNRRDDGTE RMLEIAEKYR GSKSDDDSNK GAAEWRGWPV RKRLEYALVK GITEFIEQDT EEARAESARP IEVIEGPLMD GMNVVGDLFG AGKMFLPQVV KSARVMKQAV AYLEPFIQAS KDQGSSAGKI LLATVKGDVH DIGKNIVGVV LQCNNYEIID LGVMVPTDKI LKTAREEKVD IIGLSGLITP SLDEMVNVAK EMERQGFTLP LLIGGATTSK AHTAVKIEQN YSGPTVYVQN ASRSVGVVSA LLSDTQRDDF VARIRKEYET VRIQHGRKKP RTPPVSLGVA RDNAMPIDWE SYTPPVAHRL GVQPVTASIE TLRNYIDWTP FFMTWSLAGK YPNILEDEVV GEEAKRLFAD ANAMLDTLSA SGTLNPRGVV GLFPANRVGD DVEIYTDERR TEVLTVSHHL RQQTEKTDFP NYCLADVVAP KASGKPDYLG AFAVTGGLEE DALAAQWEAQ HDDYNKIMLK ALADRLAEAF AEYLHERVRK VYWGYAPNEN LGNDELIREN YQGIRPAPGY PACPDHTEKA AIWQLLDVDN TVGMKLTESY AMWPGASVSG WYFSHPDSKY FAVAQIQRDQ VEDYAVRKQM PVEEIERWLA PNLGYDAD // ID C6CMA2_DICZE Unreviewed; 302 AA. AC C6CMA2; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACT08548.1}; GN OrderedLocusNames=Dd1591_3747 {ECO:0000313|EMBL:ACT08548.1}; OS Dickeya zeae (strain Ech1591). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Dickeya. OX NCBI_TaxID=561229 {ECO:0000313|EMBL:ACT08548.1, ECO:0000313|Proteomes:UP000002735}; RN [1] {ECO:0000313|EMBL:ACT08548.1, ECO:0000313|Proteomes:UP000002735} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ech1591 {ECO:0000313|EMBL:ACT08548.1, RC ECO:0000313|Proteomes:UP000002735}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; ACT08548.1; -; Genomic_DNA. DR RefSeq; WP_015848057.1; NC_012912.1. DR RefSeq; YP_003006027.1; NC_012912.1. DR STRING; 561229.Dd1591_3747; -. DR EnsemblBacteria; ACT08548; ACT08548; Dd1591_3747. DR KEGG; dze:Dd1591_3747; -. DR PATRIC; 21803589; VBIDicZea111179_3817. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; PYVDVWL; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; DZEA561229:GJ85-3829-MONOMER; -. DR Proteomes; UP000002735; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002735}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ACT08548.1}; KW Transferase {ECO:0000313|EMBL:ACT08548.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 302 AA; 32029 MW; A6479FD5DC63183D CRC64; MADNVLILDG GMGRELARIG APFRQPEWSA LALMESPQQV RQVHDSFIAA GAQVITSNSY AVVPFHIGDA EFSARGQALA ALAGQLARQA ADAAPHPVRV AGSLPPVLGS YRPDLFNAAA ATPILKTLID ALTPYVDVWL AETQSSLAEV ALVRELLADD PRELWLSFTL QDELDADGHA RLRSGETVAA AAQEAARLRA ANLLFNCSRP EVMAPAVAQA LATLNAQPAA IGVGVYANAF EPEDNQRGAN EGLSRLRTDT HPEGYLQWAQ EWVAQGASLV GGCCGIGPEH IARLAQAFNR QA // ID C6CUS8_PAESJ Unreviewed; 1148 AA. AC C6CUS8; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 01-APR-2015, entry version 47. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACT01281.1}; GN OrderedLocusNames=Pjdr2_2627 {ECO:0000313|EMBL:ACT01281.1}; OS Paenibacillus sp. (strain JDR-2). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=324057 {ECO:0000313|EMBL:ACT01281.1, ECO:0000313|Proteomes:UP000002510}; RN [1] {ECO:0000313|Proteomes:UP000002510} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JDR-2 {ECO:0000313|Proteomes:UP000002510}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001656; ACT01281.1; -; Genomic_DNA. DR RefSeq; WP_015844225.1; NC_012914.1. DR RefSeq; YP_003011367.1; NC_012914.1. DR STRING; 324057.Pjdr2_2627; -. DR EnsemblBacteria; ACT01281; ACT01281; Pjdr2_2627. DR KEGG; pjd:Pjdr2_2627; -. DR PATRIC; 22835779; VBIPaeSp118865_2611. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PSP324057:GH5H-2713-MONOMER; -. DR Proteomes; UP000002510; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002510}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002510}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 722 722 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1148 AA; 127041 MW; C444B041453BE8A9 CRC64; MLKPTIQEMM QQRILILDGA MGTMIQQADL TADDFGGEEL DGCNEMLVLT RPDVISTIHE KYLEAGADIL ETNTFGATSV VLAEYDIPEK AREINLAAAK LARDAADKFS TPDRPRYVAG ALGPTTKTLS VTGGVTFDEL VDSYYEQTVA LIEGDVDAIL LETSQDTLNV KAGSIGIRKA FAAMNRELPI MISGTIEPMG TTLAGQSIES FYISLEHLKP ISIGLNCATG PEFMRDHIRS LSEIADSAVS CYPNAGLPDE NGHYHESPES LARKMSAFAE QGWLNIAGGC CGTTPAHIKA LYDTMANYAP RTQYGTHPAA VSGIDTVYIE DENRPIMIGE RTNISGSRKF KRLIKEGKFD EASEIARSQV KGGAHIIDIN LQDTDIDEAY AVHEFLPQVV KKIKVPLMLD STYDHIIELG LKYSQGKAII NSINLEDGES KFEKILPLIH QYGAAVVMIL IDERGQAVSR EAKMEVAERS YNLLVNKYGM NPEDIIFDPN MFPVGSGDPQ YIGSAVETIE GIRMIKEKFP KAKTILGLSN ISFGLPDAGR EVLNSVYLYH CTKAGLDYAI VNTEKLERYA SIPEEERKLA EDLIYNTNDD TLAAFVAAFR EKKVVKKEKV SNLSLEERLA SYVVEGTKEG LIPDLDIALK KYTALEVING PLMRGMEEVG RLFNNNELIV AEVLQSAEVM KASVAHLEQF MEKNESSVKG KIILATVKGD VHDIGKNLVE IILSNNGYKI INLGIKVPPE QLIEAQRKEN ADIIGLSGLL VKSAQQMVVT AQDMRNAGIS APIMVGGAAL TRKFTKTRIG PEYDGLTLYA KDAMDGLDLA NKLMDKEHRG RMEEELRIYK ESGGDAEEEK KPQPQLTRVE RSKISVDAPV YIPPDTDRHI LRDVPIPHII PYVNMQMLLG HHLGLKGNVD NLLQEGNEKA VQLKETVDGI LQEGTTNGII KAHGMYRFFP AQSSGNDIII YDPQDHAKEI KRFTFPRQQV EPFLCLADYL KPVDSGIMDY VGFLVVTAGQ GIRDLANEWK ENGDYLRSHA LQSVALEVAE AMAERVHHMM RDIWGYPDPA TMTMKQRFGA RYQGIRVSFG YPACPNLEDQ GPLFELMKPE DIGVELTEGF MMEPEASVSA MVFAHPEAQY FNVEKVER // ID C6D4G9_PAESJ Unreviewed; 632 AA. AC C6D4G9; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 01-APR-2015, entry version 41. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=Pjdr2_3767 {ECO:0000313|EMBL:ACT02397.1}; OS Paenibacillus sp. (strain JDR-2). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=324057 {ECO:0000313|EMBL:ACT02397.1, ECO:0000313|Proteomes:UP000002510}; RN [1] {ECO:0000313|Proteomes:UP000002510} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JDR-2 {ECO:0000313|Proteomes:UP000002510}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ACT02397.1; -; Genomic_DNA. DR RefSeq; WP_015845337.1; NC_012914.1. DR RefSeq; YP_003012483.1; NC_012914.1. DR ProteinModelPortal; C6D4G9; -. DR STRING; 324057.Pjdr2_3767; -. DR EnsemblBacteria; ACT02397; ACT02397; Pjdr2_3767. DR KEGG; pjd:Pjdr2_3767; -. DR PATRIC; 22838061; VBIPaeSp118865_3748. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; PSP324057:GH5H-3856-MONOMER; -. DR Proteomes; UP000002510; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002510}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ACT02397.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000002510}; KW Transferase {ECO:0000313|EMBL:ACT02397.1}. SQ SEQUENCE 632 AA; 68554 MW; 55259CBDDCA9B2BC CRC64; MKPDLRTKLK QRILTGDGAM GTYLYQMGFP VGVSYEELNM TRPDVIEGVH RRYYEAGARV IETNTFSANL VKLSKYGLEP DMEAINRAGV RIAKAAAGED AYVVGAVGSI RAGKLKDVRT SEVSHAFERQ LDALLVEGVD GILFETFYDF DEMRLALGLA RKLTQLPVIC QFAAQDVGRT QDGTGLLDAF TLLKDEGADV VGFNCRSGPN GIMRAVESIG GPVELPLSIF PNAGIPDYVD GKYKYSAGPD YFAETALQFA DRGARIIGGC CGTTPEHIAA MAKALKDYKP QNGAAAVAIA DSPEAEIIVI EAEPAEVVKN ASGERADTPI NSEPSLVDTV RVRHAVIVEL DPPRDLDITK FMAGAAAIKA CGADAITMAD NSLAVTRMSN LALAALVKER IGLRPLVHIA CRDRNLIGTQ SHLMGLDALG IDHVLAVTGD PARFGDLPDS SSVYDLTSFE MIRMTKQLND GIAFSGKPLK QKAKFVVGAA FNPNVKHLDK AVQRLEKKIA SGADYIMTQP VYDPVLIEKI AEATKHLPVP VFIGIMPLAS GRNAEYLHNE VPGIQLSDEV RKRMAGLEGA EGRAEGVRIS RELLDTAIRH FKGIYFMTPF MFYEMAAELT DYVWAKTGVQ RR // ID C6DDW6_PECCP Unreviewed; 315 AA. AC C6DDW6; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 27-MAY-2015, entry version 33. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACT12578.1}; GN OrderedLocusNames=PC1_1535 {ECO:0000313|EMBL:ACT12578.1}; OS Pectobacterium carotovorum subsp. carotovorum (strain PC1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Pectobacterium. OX NCBI_TaxID=561230 {ECO:0000313|EMBL:ACT12578.1, ECO:0000313|Proteomes:UP000002736}; RN [1] {ECO:0000313|EMBL:ACT12578.1, ECO:0000313|Proteomes:UP000002736} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PC1 {ECO:0000313|EMBL:ACT12578.1, RC ECO:0000313|Proteomes:UP000002736}; 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 ----------------------------------------------------------------------- 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; ACT12578.1; -; Genomic_DNA. DR RefSeq; WP_015839803.1; NC_012917.1. DR RefSeq; YP_003017114.1; NC_012917.1. DR STRING; 561230.PC1_1535; -. DR EnsemblBacteria; ACT12578; ACT12578; PC1_1535. DR KEGG; pct:PC1_1535; -. DR PATRIC; 20487718; VBIPecCar70489_1548. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; PCAR561230:GKCK-1577-MONOMER; -. DR Proteomes; UP000002736; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002736}; KW Methyltransferase {ECO:0000313|EMBL:ACT12578.1}; KW Transferase {ECO:0000313|EMBL:ACT12578.1}. SQ SEQUENCE 315 AA; 33665 MW; 9E0EAA13E19CE0C4 CRC64; MRKNTVTELL ATAPTIVLDG ALATELEARG CDLTDPLWSA KVLVENPALI YQVHLDYFKA GAQCAITASY QATPQGFEAR GYSEAESLAL IAKSVQLAAQ ARDDYRHDNP QAGALLVAGS VGPYGAYLAD GSEYRGDYQL PQADMMAFHR PRMAALLEAG ADLLACETLP SFAEIETLIA LLAEFPQAQA WLSFTLRDSE HLSDGSPLRT VLARVNACSQ VVAVGINCIA LEKVTPALTY LSSLTDLPLV VYPNSGEQYD AVTKTWSSAH DAACSLTAYL PEWQAAGARL IGGCCRTTPA DIAGIARCCQ HEGQH // ID C6DFQ1_PECCP Unreviewed; 1227 AA. AC C6DFQ1; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 29-APR-2015, entry version 48. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACT14790.1}; GN OrderedLocusNames=PC1_3775 {ECO:0000313|EMBL:ACT14790.1}; OS Pectobacterium carotovorum subsp. carotovorum (strain PC1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Pectobacterium. OX NCBI_TaxID=561230 {ECO:0000313|EMBL:ACT14790.1, ECO:0000313|Proteomes:UP000002736}; RN [1] {ECO:0000313|EMBL:ACT14790.1, ECO:0000313|Proteomes:UP000002736} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PC1 {ECO:0000313|EMBL:ACT14790.1, RC ECO:0000313|Proteomes:UP000002736}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001657; ACT14790.1; -; Genomic_DNA. DR RefSeq; WP_015841901.1; NC_012917.1. DR RefSeq; YP_003019326.1; NC_012917.1. DR STRING; 561230.PC1_3775; -. DR EnsemblBacteria; ACT14790; ACT14790; PC1_3775. DR KEGG; pct:PC1_3775; -. DR PATRIC; 20492310; VBIPecCar70489_3802. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PCAR561230:GKCK-3859-MONOMER; -. DR Proteomes; UP000002736; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002736}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135503 MW; 57FF3AD35251B99F CRC64; MSNRVDELRR QLAQRIMVLD GGMGTMIQGY RLQEADYRGE RFADWPSDVK GNNDLLVLTR PQVISEIHDA YLEAGADILE TNTFNATTIA MADYDMQSLS AEINTVAAQL ARASADKWTA LTPDKPRYVA GVLGPTNRTA SISPDVNDPA FRNVSFDQLV DAYRESTRAL IAGGVDLIMI ETIFDTLNAK AASFAVESEF EALGIVLPVM ISGTITDASG RTLSGQTTEA FYNSLRHSRP LSFGLNCALG PDELRQYVAE LSRISECYVS AHPNAGLPNA FGEYDLDPAD MAKHIGEWAR SGFLNIVGGC CGSTPAHIAA MAKVVEGVPP RKLPEIPVAC RLSGLEPLTI DANTLFVNVG ERTNVTGSAR FKRLIKEEKY NEALDVARQQ VESGAQIIDI NMDEGMLDAE AAMIRFLNLI AGEPDIARVP IMIDSSKWDV VEKGLKCIQG KGIVNSISMK EGVEAFVHHA KLVRRYGAAV VVMAFDEVGQ ADTRARKIEI CRRAYRILTE EVGFPPEDII FDPNIFAVAT GIDEHNNYAV DFIEACADIK AQLPHAMISG GVSNVSFSFR GNDLVREAIH AVFLYHAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRSDATER MLELAEKYRG SKTDDEGSKT QAEWRGWDVK KRLEYSLVKG ITEFIELDTE EARQQAARPI EVIEGPLMDG MNVVGDLFGA GKMFLPQVVK SARVMKQAVA YLEPYIEASK AKGTSAGKIL LATVKGDVHD IGKNIVGVVL QCNNYEIIDL GVMVPTDKIL KTAREEKVDI IGLSGLITPS LDEMVNVAKE MERQGFTLPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRSVGVVSAL LSSTQHDDFV ARTRKEYETV RIQHARKKPR TPPVTLEAAR ANASDLDWES YTPPVAHRLG VQEVTASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG EEAKRLFADA NAMLDDLSAR GALNPRGVVG LFPANRVGDD VVIYTDERRE TVLSVSHHLR QQTEKTDFPN YCLSDFVAPK SSGKPDYLGA FAVTGGLEED TLADQWEALH DDYNKIMVKA ISDRLAEAFA EYLHERVRKV YWGYAPNENL SNELLIRENY QGIRPAPGYP ACPDHTEKVQ IWQLLDVEKH TGMKLTESYA MWPGASVSGW YFSHPDSKYF AVAQIQHDQV EDYAVRKGME VSDVERWLAP NLGYDAD // ID C6DY72_GEOSM Unreviewed; 813 AA. AC C6DY72; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 29-APR-2015, entry version 33. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACT16347.1}; GN OrderedLocusNames=GM21_0262 {ECO:0000313|EMBL:ACT16347.1}; OS Geobacter sp. (strain M21). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=443144 {ECO:0000313|EMBL:ACT16347.1, ECO:0000313|Proteomes:UP000002380}; RN [1] {ECO:0000313|EMBL:ACT16347.1, ECO:0000313|Proteomes:UP000002380} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M21 {ECO:0000313|EMBL:ACT16347.1, RC ECO:0000313|Proteomes:UP000002380}; 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; ACT16347.1; -; Genomic_DNA. DR RefSeq; WP_012773974.1; NC_012918.1. DR RefSeq; YP_003020105.1; NC_012918.1. DR STRING; 443144.GM21_0262; -. DR EnsemblBacteria; ACT16347; ACT16347; GM21_0262. DR KEGG; gem:GM21_0262; -. DR PATRIC; 22015026; VBIGeoSp56140_0267. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; GSP443144:GHKM-270-MONOMER; -. DR Proteomes; UP000002380; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002380}; KW Methyltransferase {ECO:0000313|EMBL:ACT16347.1}; KW Transferase {ECO:0000313|EMBL:ACT16347.1}. SQ SEQUENCE 813 AA; 84792 MW; 94830223D6697FFA CRC64; MKMSFMQAVK ERVLVLDGAM GTMLQERGLK PGQSPEEMNL TAAEVVAGVH QAYLDAGADI IVTNTFGGTK AKLEHYGLGD QVARINAEAV RIAREVAGEK AYVAGSIGPT GRFLEPVGDM SFDEAVSLFR EQAQALVDAG CDLISFETFL DIKEIRAGVI AVREISQEIP VIAMLTFEEK GISVLGTPPQ AAAITLEAVG ATIVGSNCGL GPDGIYQILS DMRDVTALPL ISQANAGLPI LKDGVTIFPA TPDEMTAYHD RLIELGVRII GGCCGTTPAH ISAIKKALAA KQAPFAPKKE DGTTWLSSRG SFAAVGAAHP VALIGERINP TGKKLYSQEL REAKVSYIRR EALEQAGLGA TLLDVNVGTP GIDEPAAMER AVFCITGAVQ TPLVLDSSSP EALEAGLKAA DGKVLVNSVN GEEKSLAAVL PLAKKYGAAL VCLTLDEAGI PAEAAGRVAV AEKIAAAALA AGVKRSDLVV DCLTLTVSAE PKGALVALEA VRQVSALSLN TTLGVSNISF GLPCRPLISS TFFSMAIAAG LTSAIVNVKE APMMAAWRSS MVLLEKDVNA AGYIEAYKGQ AVGATVEPAA AQGAAVARAA AVEPEGVRGR LSKAVINGEA DNVVALVEEA LSEGLTPMQI SSEALLVGLD EVGRRFGSGE FFLPQVMVSA DTMKTAFARL KMELSTGGLQ SIGKILMATV EGDIHDIGKN ILVTLLENNG FEVIDLGKNV PADRILYEAR AHQVDAVGLS ALMTTTMAQM DKVVKLLKAE GVKSFTMVGG AVVTQEYADE IGADLYAKDA MEAVARVKKL LAK // ID C6E085_GEOSM Unreviewed; 610 AA. AC C6E085; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 29-APR-2015, entry version 43. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=GM21_0627 {ECO:0000313|EMBL:ACT16701.1}; OS Geobacter sp. (strain M21). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=443144 {ECO:0000313|EMBL:ACT16701.1, ECO:0000313|Proteomes:UP000002380}; RN [1] {ECO:0000313|EMBL:ACT16701.1, ECO:0000313|Proteomes:UP000002380} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M21 {ECO:0000313|EMBL:ACT16701.1, RC ECO:0000313|Proteomes:UP000002380}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Note=FAD.; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {ECO:0000256|RuleBase:RU004255}. CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ACT16701.1; -; Genomic_DNA. DR RefSeq; WP_012774323.1; NC_012918.1. DR RefSeq; YP_003020459.1; NC_012918.1. DR ProteinModelPortal; C6E085; -. DR STRING; 443144.GM21_0627; -. DR EnsemblBacteria; ACT16701; ACT16701; GM21_0627. DR KEGG; gem:GM21_0627; -. DR PATRIC; 22015746; VBIGeoSp56140_0620. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; GSP443144:GHKM-643-MONOMER; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000002380; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004255}; KW Complete proteome {ECO:0000313|Proteomes:UP000002380}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ACT16701.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:ACT16701.1}. SQ SEQUENCE 610 AA; 64066 MW; 112C0C8952AC1396 CRC64; MGGSFLERVA HEVLIGDGAI GTMLYAKGVA LDANFEHLNL VRPQLVLDLH AEYLAAGAQV IETNTFGANY AKLSAIGIGG KVADINRQGA ILARRAAKGC DVFVAGSMGP MGRGKKEMSD DQVRDSFRLQ AAALAEGGVD LLILETFSEL DELETALAAA RETGLPVVAN LAFGEGSRLA GGIEAEDAAL RLAAAGASLV GANCGAGPLE LLATLKRMAA VTDLPLAAYP NSGFPEYVDG RYIYRTTPDY FAARAEEMVA AGAVLVGGCC GTTPEHIRVT ARRLKGARPA ARVAAGEVHR PPVAEKAQSA ASGFLDRWGK EMVVTVELDP PKGLDCSRIL AGSRALKEAG ADAINLAENP LARVRMGNLA LASLIRREVG IEVIAHITCR DRNLIGLQSD LMGASLLGVS SILAVTGDPA SLGEEAGASS VFDLNSFTLI KLLSDLNRGV NALGNPIGAG TGFTIGAAFN PNTQKMEVQV ARLAKKVENG ACFAQTQPIY DLERFEQMME QTAHLGIPIL PGVLPLVSGR NAEFLHNEVP GITIPDGIRA RMAGKVGEEG VREGLAIARE FIEATLGRVG GFYLIPPFGK YEIAVELVKF IKSKAEHRGL // ID C6EE05_ECOBD Unreviewed; 1227 AA. AC C6EE05; C5WBQ3; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 27-MAY-2015, entry version 48. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACT31003.1}; GN OrderedLocusNames=ECBD_4018 {ECO:0000313|EMBL:ACT31003.1}; OS Escherichia coli (strain B / BL21-DE3). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=469008 {ECO:0000313|Proteomes:UP000002032}; RN [1] {ECO:0000313|Proteomes:UP000002032} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B / BL21-DE3 [JGI] {ECO:0000313|Proteomes:UP000002032}; 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. CC ----------------------------------------------------------------------- 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; ACT31003.1; -; Genomic_DNA. DR RefSeq; WP_000095995.1; NC_012971.2. DR RefSeq; YP_003001580.1; NC_012892.2. DR RefSeq; YP_003038188.1; NC_012947.1. DR RefSeq; YP_003056453.1; NC_012971.2. DR ProteinModelPortal; C6EE05; -. DR SMR; C6EE05; 651-1227. DR STRING; 469008.ECBD_4018; -. DR EnsemblBacteria; ACT31003; ACT31003; ECBD_4018. DR EnsemblBacteria; ACT45682; ACT45682; ECD_03891. DR EnsemblBacteria; CAQ34368; CAQ34368; B21_03851. DR KEGG; ebd:ECBD_4018; -. DR KEGG; ebe:B21_03851; -. DR KEGG; ebl:ECD_03891; -. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR Proteomes; UP000002032; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002032}. SQ SEQUENCE 1227 AA; 135983 MW; 7250C9EE48BA453B CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LSFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAD // ID C6HW85_9BACT Unreviewed; 822 AA. AC C6HW85; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 01-APR-2015, entry version 19. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EES53190.1}; GN ORFNames=UBAL3_80290066 {ECO:0000313|EMBL:EES53190.1}; OS Leptospirillum ferrodiazotrophum. OC Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; Leptospirillum. OX NCBI_TaxID=412449 {ECO:0000313|EMBL:EES53190.1}; RN [1] {ECO:0000313|EMBL:EES53190.1} 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] {ECO:0000313|EMBL:EES53190.1} 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG693868; EES53190.1; -; Genomic_DNA. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EES53190.1}; KW Transferase {ECO:0000313|EMBL:EES53190.1}. SQ SEQUENCE 822 AA; 87679 MW; 91ED92A5EFD00616 CRC64; MIPLLERLKK DILILDGSMG ALLQGRGLPP GYAPDLWNLE RPKDIQAVHA EYRAAGSDIL LTNTFGASRR RLAEYQAEGR IREINHAGVE LARRAAQGKA YIAGDIGPFG STIAPFGDTT FEEAVGIFRE QASILAEAGV DLIAIETMFD IQEMRAALIG VREGAPGVPI MAFMTYNADG ITDSGSDPET VAAVLEGFSV EIMGLNCSVG PEAMLPVLER LGRATHTYLG IEPNAGLPVH RDGKTVYPLG ASEMASFAPA FADAGANIVG GCCGTTPDYI RLISKILKGR PPRLRTPSPH TRIASRTRVV PIGAGAPFVL IGEKINPTGK KLFSEAIAEG RTDMIVAEAR KEAAAGAHAL DVNVGVPLVD EALMMEKAVI AIGNVVSTPL VIDSSFASAL ESGLRIYPGR ALVNSVNAED ERLEEVLPLI RRYGASVIGL LSGDDIPEKA IDRMKNAEKI LKAAERFGLS PRDIVFDTLA LTVSAVQEAS RQTLETIRLL KSEWNAHTVV GLSNVSFGLP MRKTVHDTFL AMAIGAGLDG AICDPYDPLL HQTVAAASLF SGRDPECRVF ITKAESWTPL VPQGEKGAAA GSPAPGASPA TPDRPLTTRE RIERAIIEGE REAITPLVET ALAEGMAPFE IFVDVMTPAI RRLGDLFGAR QKFIPHLIAG ADTMKKGVEV LQPLLEAKGP TEPKGTIVFA TVKGDIHDIG KNICILMLRN FGYRVIDLGR NVPLETILET AEKEKAQIVA LSALMTTTMI QMKVAVDAIR EKSLPYKVMV GGAVVTPKFS AEIGADGYGK DVGEVVPLTE KILAALREIP AS // ID C6IR08_9BACE Unreviewed; 915 AA. AC C6IR08; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 01-APR-2015, entry version 36. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EES67028.1}; GN ORFNames=BSIG_4156 {ECO:0000313|EMBL:EES67028.1}; OS Bacteroides sp. 1_1_6. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=469586 {ECO:0000313|EMBL:EES67028.1}; RN [1] {ECO:0000313|EMBL:EES67028.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_1_6 {ECO:0000313|EMBL:EES67028.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EES67028.1}. 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; ACIC02000064; EES67028.1; -; Genomic_DNA. DR EnsemblBacteria; EES67028; EES67028; BSIG_4156. DR PATRIC; 30492986; VBIBacSp91036_3960. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 915 AA; 99969 MW; 186063120F6E0878 CRC64; MKKTISQIVS ERILILDGAM GTMIQQYNLK EEDFRGERFA HIPGQLKGNN DLLCLTRPDV IQDIHRKYLE AGADIIETNT FSSTTVSMAD YHVEEYVREI NLAATRLARE LADEYTAKSP DKPRFVAGSV GPTNKTCSMS PDVNNPAFRA LSYDELAASY QQQMEAMLEG GVDAILIETI FDTLNAKAAI FAAGQAMKVT GIEVPVMLSV TVSDIGGRTL SGQTLEAFLA SVQHANIFSV GLNCSFGARQ LKPFLEQLAS RAPYYISAYP NAGLPNSLGK YDQTPADMAH EVKEYIQEGL VNIIGGCCGT TDAYIAEYQA LIAGAKPHVP APKPDCMWLS GLELLEVKPE INFVNIGERC NVAGSRKFLR LVNEKKYDEA LSIARQQVED GALVIDVNMD DGLLDARTEM TTFLNLIMSE PEIARVPVMI DSSKWEVIEA GLKCLQGKSI VNSISLKEGE EVFLEHARII KQYGAATVVM AFDEKGQADT AARKIEVCER AYRLLVDKVG FNPHDIIFDP NVLAVATGIE EHNNYAVDFI EATGWIRKNL PGAHVSGGVS NLSFSFRGNN YIREAMHAVF LYHAIQQGMD MGIVNPGTSV LYSDIPADTL EKIEDVVLNR RPDAAERLIE LAEALKETMG GTSGQAAVKQ DAWREESVQE RLKYALMKGI GDYLEQDLAE ALPLYDKAVD VIEGPLMDGM NYVGELFGAG KMFLPQVVKT ARTMKKAVAI LQPIIESEKV EGSSSAGKVL LATVKGDVHD IGKNIVAVVM ACNGYDIVDL GVMVPAETIV QRAIEEKVDM IGLSGLITPS LEEMTHVAAE LEKAGLDIPL LIGGATTSKM HTALKIAPVY HAPVVHLKDA SQNASVASRL LNSQMKAELI NELDAEYQAL REKSGLLRRE TVSLEEAQKN KLNLF // ID C6J2A8_9BACL Unreviewed; 641 AA. AC C6J2A8; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 27-MAY-2015, entry version 25. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=POTG_02525 {ECO:0000313|EMBL:EES72825.1}; OS Paenibacillus sp. oral taxon 786 str. D14. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=621372 {ECO:0000313|EMBL:EES72825.1}; RN [1] {ECO:0000313|EMBL:EES72825.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=D14 {ECO:0000313|EMBL:EES72825.1}; 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., 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG695978; EES72825.1; -; Genomic_DNA. DR RefSeq; WP_009225244.1; NZ_GG695978.1. DR ProteinModelPortal; C6J2A8; -. DR EnsemblBacteria; EES72825; EES72825; POTG_02525. DR PATRIC; 25846302; VBIPaeSp50414_2567. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EES72825.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EES72825.1}. SQ SEQUENCE 641 AA; 69465 MW; 3DADEFC4AEBE7B2D CRC64; MKPDLRTTLE REIIVGDGAM GTYLYQLGFP VGISYEEFNL LRPDVIGDIH RRYLDAGARL LETNTFSANY YKLSKFGLEA KVEDINRAAV RIAKQAAGER AYVAGAVGSI RGGKRANVTV QELGKYFEQQ IAALLSEGVD ALLFETFYDL GEMRIALGQA RKLTDVPVIC QFAVDQIGRT LDGFTIPQAF GALVEEGADV VGFNCHSGPK GIMGVMDDVE GPLNVPMSVF PNAGLADYID GEYVYGATPD YFGECARAFA DLGARLIGGC CGTTPEHIAA MAKALEGYAA QPLAKERKLP EPHLSASVSL NEQPNAVPAG SSETGAVSGG GENRKLPSLT ELVKERHTVI VELDPPRDLD IGKFMEGAAA LKEAGIDALT LADNSLAVTR MSNMALGHLV QSQLGLRPLV HIACRDRNLI GTQSHMMGFD ALGIDHVLAV TGDPARFGDL PGASSVYDLT SFEIIRMIKQ LNEGISFSGK PLKQKAKFVV GAAFNPNVKH LHKAVERLEK KIASGADYIM TQPVYDPELI VAIKQATAHL DVPIFIGIMP LASGKNAEYL HNEVPGIQLS DEVRKRMEGL QGEEGRAMGV EIAKELLDTA MEHFNGIYLM TPFMFYEMNV ALTNYIREKS KRDSAHLSRL S // ID C6J513_9BACL Unreviewed; 1171 AA. AC C6J513; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 01-APR-2015, entry version 32. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EES71973.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EES71973.1}; GN Name=metH {ECO:0000313|EMBL:EES71973.1}; GN ORFNames=POTG_03490 {ECO:0000313|EMBL:EES71973.1}; OS Paenibacillus sp. oral taxon 786 str. D14. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=621372 {ECO:0000313|EMBL:EES71973.1}; RN [1] {ECO:0000313|EMBL:EES71973.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=D14 {ECO:0000313|EMBL:EES71973.1}; 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., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG695986; EES71973.1; -; Genomic_DNA. DR ProteinModelPortal; C6J513; -. DR EnsemblBacteria; EES71973; EES71973; POTG_03490. DR PATRIC; 25848252; VBIPaeSp50414_3534. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EES71973.1}; KW Transferase {ECO:0000313|EMBL:EES71973.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 251 251 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 315 315 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 746 746 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1171 AA; 129067 MW; 7E9C1F52AA6F005D CRC64; MELSFLQRFI LLNYILTFYG RDMNMSKPSL LERMKERILI LDGAMGTMIQ QENLTPADFG GEELDGCNEM LVLTRPDVIR GIHEKYLAAG ADLIETNTFG ATSVVLAEYD IPHKAREINM AAAKLAIEAA EKYSTPDHPR YVVGILGPTT KTLSVTGGVT FDELTASYAE QAAALIEAGV DALMLETSQD TLNVKAGSIG IKQAFAETGI TLPLMISGTI EPMGTTLAGQ NIEAFYISLE HLNPISIGLN CATGPEFMRD HIRTLSGLAK AAVSCHPNAG LPDENGIYHE SPDSLAQKMS AFAEQGWLNI AGGCCGTTPA HIAALANTLK DYRPRELTGS HLPALSGIEP VYIESANRPY LVGERTNVLG SRKFKRLIVE GKYEEASEIA RAQVKNGAQV VDVCVQDPDR DEAEDIKKFL ELVVKKVKVP LMIDTTDPKV LDIALQYCQG KSIINSINLE DGEEKFERVT PLIHKYGAAV VVGTIDERGQ AITREDKLEV AKRSYDLLVH KYGLQPEDII FDPLVFPVGT GDEQYIGSAK ETIEGIRLIK EALPKVHTVL GISNVSFGLP EAGREVLNSV FLYECTKAGL DYAIVNTEKL ERYAKIPEEE RRLAEELIYN TNDETLAAFV AAFRNKKVEK AETTTQLTLE ERLASYVVEG TKEGLIPDLD EALKKYTALE IINGPLMAGM EEVGRLFNNN ELIVAEVLQS AEVMKASVAY LEPFMEKNET SVKGKILLAT VKGDVHDIGK NLVEIILSNN GYQIVNLGIK VPPERIIEAY REEKADAIGL SGLLVKSAQQ MVTTAQDLRN AGIDVPILVG GAALTRKFTK TRIRPEYDGL VLYAKDAMDG LDLANKLMDP VAREQMRLEV DAEKEADRVV AVAEPLPELT RVERSKISTD APVFIPPDLE RHVLRDYPIG HITPYINMQM LLGHHLGLRG SVEQQLAAGE AKAVQLKETV DQILLEAVTD GIIRTQAMYR FFPAQSSGND ILIYDPAEPG KVIKRFSFPR QKVEPYLCLA DFLKSVDSGQ MDYVGFLVVT AGQGVRELSE KWKNEGEYLR SHVLQAVALE LAEALAERVH HIMRDTWGFP DPANMTMKQR HGARYQGIRV SFGYPACPDL EDQQLLFDLM HPEDIGVTLT EGFMMEPEAS VSAMVFAHPE AQYFNVDKAG I // ID C6JA88_9FIRM Unreviewed; 290 AA. AC C6JA88; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 2. DT 27-MAY-2015, entry version 24. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EES78381.2}; GN ORFNames=RSAG_00338 {ECO:0000313|EMBL:EES78381.2}; OS Ruminococcus sp. 5_1_39BFAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus. OX NCBI_TaxID=457412 {ECO:0000313|EMBL:EES78381.2}; RN [1] {ECO:0000313|EMBL:EES78381.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=5_1_39BFAA {ECO:0000313|EMBL:EES78381.2}; 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] {ECO:0000313|EMBL:EES78381.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=5_1_39BFAA {ECO:0000313|EMBL:EES78381.2}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EES78381.2}. CC ----------------------------------------------------------------------- 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; EES78381.2; -; Genomic_DNA. DR RefSeq; WP_020993961.1; NZ_ACII02000003.1. DR EnsemblBacteria; EES78381; EES78381; RSAG_00338. DR PATRIC; 29802527; VBIRumSp107365_0199. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 207 207 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 290 AA; 30634 MW; BA302E6A9E4B588A CRC64; MTREEFQKLT QDVVLLDGAT GSNLMAAGMP RGICTEAWIM EHKEVLQNLQ KAYVEAGSQI VYAPTFGGNR YSLGLHGLQD KLAEMNHALV NISREAVGHK VYVAGDITTT GKMMEPAGDL TYEMAYETYC EQIKVLEDAG VDLIAAETMI NIEETLAALD AAASVSSLPV MCTMTVEADG SIFSGGNAVE AAIALEGAGA VAVGINCSVG PDQLVSVVRN IKENVSIPVI AKPNAGMPTI DDQGNAIYSM DAKSFAEHMK VLIENGASVV GGCCGTTPEF IHEISRSLGR // ID C6JIG3_FUSVA Unreviewed; 1112 AA. AC C6JIG3; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 27-MAY-2015, entry version 33. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EES65080.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EES65080.1}; GN Name=metH {ECO:0000313|EMBL:EES65080.1}; GN ORFNames=FVAG_02060 {ECO:0000313|EMBL:EES65080.1}; OS Fusobacterium varium ATCC 27725. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=469618 {ECO:0000313|EMBL:EES65080.1}; RN [1] {ECO:0000313|EMBL:EES65080.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 27725 {ECO:0000313|EMBL:EES65080.1}; 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., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EES65080.1}. 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; ACIE02000025; EES65080.1; -; Genomic_DNA. DR RefSeq; WP_005951023.1; NZ_GL988001.1. DR EnsemblBacteria; EES65080; EES65080; FVAG_02060. DR PATRIC; 28748373; VBIFusVar73376_0139. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EES65080.1}; KW Transferase {ECO:0000313|EMBL:EES65080.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 228 228 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 292 292 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 736 736 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1112 AA; 124039 MW; 2AB036BC73919BB4 CRC64; MINELKKRIL VLDGATGTAI QKYNLSEIDF QGKKGCNEIL NISRPDIIKE IHTGYIKAGA DIIETNSFNC NRISLKDYGI EDMSYTLSKK GAELAREIAD NFYKTSGKKI YVAGSIGPTS KSLSLPVGDN PYERELNFDQ MKNIYSEQIE GVIDGGADCI LIETIFDGLN AKAALIAAEE LFEKKNIQLP IMISATVNKQ GKIFSGQSIE SLIVALDRPS IISFGLNCSF GAKDLIPMIK KIAAFTDKYI SLYPNAGLPN ENGEYEETPE ITTGYLKELV DKKQVNILGG CCGTHFSHIK AIADLVKNKE PRPIIVKENK CFLSGNEIYN FNNKFTVIGE RNNVAGSKIF KTLIEEKNYI KALEIARLQI EKGAAVLDIN LDDGLLIPHE EMEKFLRIIQ NDPIVSKVPI MIDSSDFLTI ETALKNIAGK SIVNSISLKE GEESFRKKAR IIKKYGAAVV VMAFDEKGQG ISFERKIEIC NRSYKLLKEE NFSDSDIIFD PNILAIGTGS KDDRYNGLNF LKTIQWLKEN LSYCGISGGL SNLSFAFRGN NSLRAAIHSL FIEAAKEKGM NFAIMNPGEK APQLTSDERD IILALINGNT ESLDSILELA AKLKNASVNL KPNSSSTNKM INNDFESLKD RIERALIYGG STTFDTDINT ALKNMTPLDI IQNILMKGMD KIGILFEKGE LYLPQLIRSA SVMNKAVDIL KPHMKVKADI RIKGKILMAT VEGDVHDIGK NIAGTVLKCN GYEVIDLGVM VSKEKILEEA IKNSVDIITL SGLISPSLKE MEKTLSLLNE NKISIPVLVA GAATSKLHTA VKLEPFYKKR TFHTTDALDT LTMINKLIYG DKEVFMEEKT KELENLCSIY LNTKKENSEK EICLKDNFSS EIVLPNQLGK QYLEFTLERI EKYINWNFLL HNMKVKNTPL EEQTLGDAKH IFDKMKENNI KIRCSFGIFP CVKNSDTLTI NDGDKSWSIS FTRGKIKNKD IGISDFFNKK DFIGAFVISV TSSLFLQDNY MSIMENILLT RIAEAASEFL ESYLKEKNIW IPNIRPAIGY PSIPDHSIKK TIFEIVDGEK TGASLTSNYA MLPLSTVCGI YISNPKSFYF SL // ID C6LEJ3_9FIRM Unreviewed; 291 AA. AC C6LEJ3; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EET60976.1}; GN ORFNames=BRYFOR_07043 {ECO:0000313|EMBL:EET60976.1}; OS Marvinbryantia formatexigens DSM 14469. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Marvinbryantia. OX NCBI_TaxID=478749 {ECO:0000313|EMBL:EET60976.1}; RN [1] {ECO:0000313|EMBL:EET60976.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 14469 {ECO:0000313|EMBL:EET60976.1}; 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., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EET60976.1}. 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; ACCL02000008; EET60976.1; -; Genomic_DNA. DR RefSeq; WP_006861836.1; NZ_ACCL02000008.1. DR EnsemblBacteria; EET60976; EET60976; BRYFOR_07043. DR PATRIC; 29034862; VBIBryFor99582_1809. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EET60976.1}; KW Transferase {ECO:0000313|EMBL:EET60976.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 207 207 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 291 AA; 31013 MW; 7924FE94D7D8E9BB CRC64; MTKKEFRKLA EDIIILDGAT GSNLMKAGMP RGICTEQWIL ENEQTLIELQ RAYVEAGSQI VCAPTFGANC RNLAAHGLRD KLADMNKRLV DISLRATEGR AYVAGDMSTG GVAIGSSPDA TYEEAFERYA EQITHLVNAG ADLLLAETMI SIDETVAAVE AAKEICDLPI LCSMTVEADG SLYFGGSALE ALETLQEVGA SAVGINCSVG PDQLEAVIAE MKKIARVPVI AKPNAGMPKI TEKGEALYSM TPEDFGKHME RLVEAGAGIV GGCCGTTPEY IREMCSRILS V // ID C6PZA9_9CLOT Unreviewed; 799 AA. AC C6PZA9; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EET85426.1}; GN ORFNames=CcarbDRAFT_4126 {ECO:0000313|EMBL:EET85426.1}; OS Clostridium carboxidivorans P7. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=536227 {ECO:0000313|EMBL:EET85426.1, ECO:0000313|Proteomes:UP000004198}; RN [1] {ECO:0000313|EMBL:EET85426.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=P7 {ECO:0000313|EMBL:EET85426.1}; 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. {ECO:0000313|EMBL:EET85426.1}. 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; ACVI01000091; EET85426.1; -; Genomic_DNA. DR RefSeq; WP_007063011.1; NZ_GG770696.1. DR EnsemblBacteria; EET85426; EET85426; CcarbDRAFT_4126. DR EnsemblBacteria; EFG86900; EFG86900; CLCAR_3857. DR PATRIC; 26470918; VBICloCar96475_4039. DR Proteomes; UP000004198; Unassembled WGS sequence. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000004198}; KW Methyltransferase {ECO:0000313|EMBL:EET85426.1}; KW Transferase {ECO:0000313|EMBL:EET85426.1}. SQ SEQUENCE 799 AA; 88170 MW; 5EBDEE2914D2C171 CRC64; MKIDDLVLEK FKDRFIIFDG AMGTMLQKSG LKVGDLPETL NITNPDIIRN IHKQYIDAGA DIIIANTFGA NELKYSSSKY SIEEVITAGV KIAKEAAQDK LVALDVSSIG QMMEPTGPLS FEAAYNLFKK QFVIGEKAGA DLILIETMSD LYETKAAVLA AKENSDLPVF CTMTFQDNGR TLMGTDPKTM VFVLEGLGVD VLGVNCSLGP KELMPIVEEI LKYASIPVMV QPNAGLPRYD GKNTVYDITA DEFVKYVKIM VEKGVRVLGG CCGTNPEFIK KLCEGLKDSK PLKIEEKNFS VVCSSTETVF LGEKVTIIGE RINPTGKSKY KEELKEKSVN FIQTQAVKQK EEGAHIIELN VGLPEIDEKE IMIKAVKSVQ KVVQLPITID SPNEEVLEAG ARVYNGKPII NSVNGKTEIM KKVFPVVKKY GGCVIGLTID ESGIPDTAEG RFKIAEKIVN TAKEYGIHKK NIIIDCLALT ASAQQKEVLE TIKAIKLVKE KLEVKTVLGV SNVSFGLPRR EILNRTFLSM ALYAGLDLPI MNTGDEGMKE VISSFEVLSN IDREGKNYVE KYGTKLVGKK EEAVTNIENI SSIKDLKQII VDGIEKDAIT STEVLLKTKE PLEVVNSYII PALDYVGEQY EEKEIFLPQL IQSAETVKKS FEVIKKKIVE QGEESISKGK IILATVKGDI HDIGKNIVKV LLENYGFEVI DLGKDVAIEK VVNTVKEHNV KLVGLSALMT TTVVNMKKTI EALRENNLQC KVFVGGAVLN EQYAEMIGAD FYAKDARESV RIAEEIFRN // ID C6Q231_9CLOT Unreviewed; 310 AA. AC C6Q231; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EET84445.1}; GN ORFNames=CcarbDRAFT_5099 {ECO:0000313|EMBL:EET84445.1}; OS Clostridium carboxidivorans P7. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=536227 {ECO:0000313|EMBL:EET84445.1, ECO:0000313|Proteomes:UP000004198}; RN [1] {ECO:0000313|EMBL:EET84445.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=P7 {ECO:0000313|EMBL:EET84445.1}; 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. {ECO:0000313|EMBL:EET84445.1}. 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; ACVI01000159; EET84445.1; -; Genomic_DNA. DR RefSeq; WP_007063982.1; NZ_ACVI01000159.1. DR EnsemblBacteria; EET84445; EET84445; CcarbDRAFT_5099. DR PATRIC; 26472885; VBICloCar96475_4972. DR Proteomes; UP000004198; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000004198}; KW Methyltransferase {ECO:0000313|EMBL:EET84445.1}; KW Transferase {ECO:0000313|EMBL:EET84445.1}. SQ SEQUENCE 310 AA; 34260 MW; F1980B32A75CF522 CRC64; MNPIENILKE FSPIILDGAL ATELENRGCN INDALWSAKI LAENPKMIEK VHYDYFCAGA DCAITSSYQA SIEGFIKKGF SKDEAVSLIK RSVTIAKKAR EDFWKEPSNR VNRAFPLIAG SVGPYGAYLA DGSEYRGYSS INEENLINFH RPRMEILVGE KVDILACETL PSLLEAKAIV KLLKEFPETY CWISFSCKNA LEISDGTPIS ECAKFLDSCE QVAAIGVNCT APQYVQSLIE EIKKNSNKPV VVYPNSGEEY DANSKTWHGN SSCKSYSCNA KGWFDKGASI IGGCCRTTPE DIKAIAKWAR // ID C6RQ71_ACIRA Unreviewed; 1228 AA. AC C6RQ71; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 27-MAY-2015, entry version 33. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EET81995.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EET81995.1}; GN Name=metH {ECO:0000313|EMBL:EET81995.1}; GN ORFNames=ACIRA0001_2753 {ECO:0000313|EMBL:EET81995.1}; OS Acinetobacter radioresistens SK82. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=596318 {ECO:0000313|EMBL:EET81995.1, ECO:0000313|Proteomes:UP000018419}; RN [1] {ECO:0000313|EMBL:EET81995.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK82 {ECO:0000313|EMBL:EET81995.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EET81995.1}. 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; ACVR01000060; EET81995.1; -; Genomic_DNA. DR RefSeq; WP_005019043.1; NZ_ACVR01000060.1. DR EnsemblBacteria; EET81995; EET81995; ACIRA0001_2753. DR PATRIC; 24341076; VBIAciRad20771_1959. DR Proteomes; UP000018419; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000018419}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EET81995.1}; KW Transferase {ECO:0000313|EMBL:EET81995.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1228 AA; 135508 MW; BF50AE6517A08EBD CRC64; MSTLATLKEL LAKRILIIDG AMGTMIQRHR LEEADYRGER FADWAHDLKG NNDLLVLTQP QIIQDIHEAY LDAGADIIET NSFNGTRVSM SDYHMEDLVP EINREAARLA KAACEKYSTP DKPRFVAGVL GPTSRTCSIS PDVNNPAFRN ITFDALKENY IEATHALIEG GADIILIETV FDTLNCKAAI FAVKEVFKEL GYELPLMISG TITDASGRTL TGQTAEAFWN SVRHGDLLSI GFNCALGADA MRPHVKTVAD VADVFVSAHP NAGLPNAFGG YDETPEETAA FLKEFAESGL INITGGCCGT TPDHIRAIYN AVKDIAPRQI PQIKPACRLS GLEPFNIYDE SLFVNVGERT NVTGSKKFAR LIREENYAEA LDVARQQVEG GAQIIDINMD EGMLDSQNAM VTFLNLIASE PDISRVPIMI DSSKWEIIEA GLKCVQGKAV VNSISLKEGY DEFVEKARLC RQYGAAVIVM AFDEKGQADT VERKKEICKR SYDVLVNEVG FPSEDIIFDP NVFAVATGIE EHNNYGVDFI EATGWIKQNL PNAMISGGIS NVSFSFRGNE PVREAIHAVF LYYAIKQGLT MGIVNAGQLA IYDDIPAELK DAVEDVVMNR NQGESGQEAT EKLLSIAEKY RGQGGTQREA ENLEWRNEPV EKRLEYALVK GITAFINEDT EEARLKSARP LDVIEGPLMA GMNVVGDLFG SGKMFLPQVV KSARVMKQAV AWLNPYIEAE KTAGEAKGKI LMATVKGDVH DIGKNIVGVV LGCNGYDIVD LGVMVPAEKI LQTAIDEKVD IIGLSGLITP SLDEMVFVAK EMQRKGFKIP LMIGGATTSK AHTAVKIDPQ YSNDAVIYVA DASRAVGVAT SLLSPEMKPA FVQGHRDEYV KVRERLANKQ PKAAKLSYAE SVKHGFKIAP DYVPPQPNFI GVQTITQYPL ETLVEYFDWT PFFISWSLAG KFPKILEDEV VGEAATDLYQ QAQIMLKDII ENKRFDARAV FGLYPAKRTA ADTVTVYDEQ GAATHHFEHL RQQSDKVTGK PNLSLADFIV TEENQAQDYL GGFTVSIFGA EELANEYKAK GDDYSAILVQ SLGDRFAEAF AEHLHERIRK EFWGYQASEQ LSNEELIKEK YIGIRPAPGY PACPEHSEKA VLFDWLGSTD KIGTQLTSSF AMWPPSSVSG FYYAHPESQY FNVGKISLDQ LEDYAKRKGW TLDEAKRWLA PNLDDSIV // ID C6TCM1_SOYBN Unreviewed; 341 AA. AC C6TCM1; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 01-OCT-2014, entry version 14. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:ACU19573.1}; 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 {ECO:0000313|EMBL:ACU19573.1}; RN [1] {ECO:0000313|EMBL:ACU19573.1} RP NUCLEOTIDE SEQUENCE. RA Cheung F., Xiao Y., Chan A., Moskal W., Town C.D.; 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; BT095312; ACU19573.1; -; mRNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; SQ SEQUENCE 341 AA; 37584 MW; 66EEE30407B0B69B CRC64; MGLEGKETPS FMRDFLDKCG GCAVIDGGFA TELERHGADL NDELWSAKCL ISSPHLVRRV HLDYLDAGAN IILTASYQAT IQGFEAKGFS REEGETMLRR SVEIAREARE IYYDRCTKDS SDFMRDERYR KRPILIAASV GSYGAYLADG SEYVGDYGDA VTVQTLKDFH RERVKILVEA GADLIAFETI PNKLEARAYA ELLEEEGIET PAWFSFSCKD ESNVVSGDSI FECASIADSC RQVVAVGVNC TAPRFIHGLI SFIKKATSKP VLVYPNSGET YIAESNQWVK SSGAAEHDFV SYIGKWRDAG ASLFGGCCRT TPNTIRGIAE ATYGKLKDKC I // ID C6TII2_SOYBN Unreviewed; 341 AA. AC C6TII2; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 01-OCT-2014, entry version 15. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:ACU22722.1}; 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 {ECO:0000313|EMBL:ACU22722.1}; RN [1] {ECO:0000313|EMBL:ACU22722.1} RP NUCLEOTIDE SEQUENCE. RA Cheung F., Xiao Y., Chan A., Moskal W., Town C.D.; 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; BT097465; ACU22722.1; -; mRNA. DR RefSeq; NP_001242352.1; NM_001255423.1. DR UniGene; Gma.398; -. DR GeneID; 100811127; -. DR KEGG; gmx:100811127; -. DR KO; K00547; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; SQ SEQUENCE 341 AA; 37542 MW; A4B3426997A817F6 CRC64; MGLEGKETPS FMRDFLDKCG GCAVIDGGFA TELERHGADL NDELWSAKCL ISSPHLVRRV HLDYLDAGAN IILTASYQAT IQGFEAKGFS REEGETMLRR SVEIAREARE IYYDRCTKDS SDFMRDERYR KRPILIAASV GSYGAYLADG SEYVGDYGDA VTVQTLKDFH RERVKILVEA GADLIAFETI PNKLEAQAYA ELLEEEGIET PAWFSFSCKD ESNVVSGDSI FECASIADSC RQVVAVGVNC TAPRFIHGLI SFIKKATSKP VLVYPNSGET YIAESNQWVK SSGAAEHDFV SYIGKWRDAG ASLFGGCCRT TPNTIRGVAE ATYGKLKDKC I // ID C6UN88_HODCD Unreviewed; 1185 AA. AC C6UN88; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 27-MAY-2015, entry version 42. DE SubName: Full=Putative B12-dependent methionine synthase {ECO:0000313|EMBL:ACT34338.1}; GN Name=metH {ECO:0000313|EMBL:ACT34338.1}; GN OrderedLocusNames=HCDSEM_166 {ECO:0000313|EMBL:ACT34338.1}; OS Hodgkinia cicadicola (strain Dsem). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Candidatus Hodgkinia. OX NCBI_TaxID=573234 {ECO:0000313|EMBL:ACT34338.1, ECO:0000313|Proteomes:UP000002741}; RN [1] {ECO:0000313|EMBL:ACT34338.1, ECO:0000313|Proteomes:UP000002741} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Dsem {ECO:0000313|EMBL:ACT34338.1, RC ECO:0000313|Proteomes:UP000002741}; RX PubMed=19609354; DOI=10.1371/journal.pgen.1000565; RA McCutcheon J.P., McDonald B.R., Moran N.A.; RT "Origin of an alternative genetic code in the extremely small and GC- RT rich genome of a bacterial symbiont."; RL PLoS Genet. 5:E1000565-E1000565(2009). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001226; ACT34338.1; -; Genomic_DNA. DR RefSeq; WP_012776147.1; NC_012960.1. DR STRING; 573234.HCDSEM_166; -. DR EnsemblBacteria; ACT34338; ACT34338; HCDSEM_166. DR KEGG; hci:HCDSEM_166; -. DR PATRIC; 31976641; VBICanHod64223_0156. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; TWTFPRQ; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CHOD573234:GI67-167-MONOMER; -. DR Proteomes; UP000002741; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002741}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002741}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 246 246 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 748 748 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1185 AA; 123935 MW; EE16B07B143E4FD0 CRC64; MCYSLRNASS ALKALTAISS KRALVLDGAM GTQIQKFKLK PKHYGVEASN GNNDALNMTQ PKVVEGVHAA YAAAGSDVLS TNTFCSCSVS QADYGTPYSC SDLNARGCLI ARRACLKAGF AQARRVFVAG VLGPTNKSAS IPADASRPSH RDVTFDDLVL SYRQQADALL ASGADALLVE TVFDTLNAKA GLKACIDASA SYRKRRALVA SATISDASGR TLSGQTIEAF WVSVKHANLA GVGLNCALGP AQLSRHAAAL ALAAEAPIWV YPNAGLPNEM GKYTQGAKAF AHALKRCFGV ASAVGGCCGS TPEHISELKA LKPKSASRKK LRQPLAVCGT DLVLAPTTRL CKVSERANVA GSSRFKTLIA RKNYSEALEV VRAQACGGAH AIDVNFDDAM LDPKAEMCRF LSLLAAEPDL AKMPVVIDSS SWDVLVAGMK LTQGRSIVNS ISLKDGSEPF VSKAQTIKTL GCVPITIAFD ELGQATTCER RLEICRRAFK LLTARAGYAP QDVIFDLNTF AVATGIPEHN ANAAMLLKAI KLVRCVFPSV TISAGVSNLS FAFRGDARIR RALHSAFLES ARGAGLNMAI VNTQEASSGE AATAEASQVC KALILNLRSV TPEEVIGAFA SAGVPRRQAS SAPTSWRSWS ARARVAHAVV SGTDKHVADD SVELAKSVGA LAVVEGALMD GMSVVGKLFE KGKMFLPQVV KSARVMKKAV QALAPMLAPR EAAKPHTVVL ATVKGDVHDI GKNIVATVLA CNSFRIVDLG IMAASDAIVS AAIAEDAVAI GLSGLISPSL DEMARVARKL QARGVTTPLL VGGATTSKLH TAIRLGPEYQ GGVVIHVSDA SKAVDVLTKL SSSNKAEFVA LVKAEQALTA EVYARAKACE ACVDHNKAAA LSACSSQHPV KAPSFVGLKL ACWACAGARY RTRSLARTPS NVLEAKASKI AERVSKLMEV ESWVSVRCRV GVFRATASNN TIALLTAKNK PVFGVQAPRR QRGSCLSLSD FVSKPSALAG AYCCVVGVEA SLIQQFFVKG GKLQAAAAFK TACDALAETC SEQLTRAMRH SVWGFVDAST QSLLKAGIAP APGYPVWPDH SAKPKLARAI GAERATALAI TSAWSLTPQS SVIAALLAGA PAAYFGVDGV SKQQVAAHAK AAKASVSKTE AALTSALSYV PSYLT // ID C6W4B8_DYAFD Unreviewed; 1274 AA. AC C6W4B8; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 27-MAY-2015, entry version 48. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACT94019.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ACT94019.1}; GN OrderedLocusNames=Dfer_2804 {ECO:0000313|EMBL:ACT94019.1}; OS Dyadobacter fermentans (strain ATCC 700827 / DSM 18053 / NS114). OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae; OC Dyadobacter. OX NCBI_TaxID=471854 {ECO:0000313|EMBL:ACT94019.1, ECO:0000313|Proteomes:UP000002011}; RN [1] {ECO:0000313|EMBL:ACT94019.1, ECO:0000313|Proteomes:UP000002011} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700827 / DSM 18053 / NS114 RC {ECO:0000313|Proteomes:UP000002011}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001619; ACT94019.1; -; Genomic_DNA. DR RefSeq; WP_015812269.1; NC_013037.1. DR RefSeq; YP_003087184.1; NC_013037.1. DR STRING; 471854.Dfer_2804; -. DR EnsemblBacteria; ACT94019; ACT94019; Dfer_2804. DR KEGG; dfe:Dfer_2804; -. DR PATRIC; 21827092; VBIDyaFer416_2894. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; DFER471854:GI24-2812-MONOMER; -. DR Proteomes; UP000002011; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 2. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 2. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002011}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACT94019.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002011}; KW Transferase {ECO:0000313|EMBL:ACT94019.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 263 263 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 326 326 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 327 327 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 774 774 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1274 AA; 141183 MW; F53FA78696967F3F CRC64; MVATQKADIR EILKNRILVL DGAMGTMIQR YKLQDHDYRG ERFADWPHDV KGNNDLLSLT RPDIIKEIHA AYFAAGADIA ETNTFSGTTI AMADYGMEEI VYELNYESAR LAREVADEFT EREPHKPRFV AGSIGPTNRT ASLSPDVNNP GFRAISFDQL VEAYYEQVKG LTDGGCDLLL VETIFDTLNA KAALFAIDQF FADAKAGKVE HLESWRIEPG QALPIMISGT ITDASGRTLS GQTTEAFLTS VSHLPLLSVG LNCALGADLM RPYVQIMAKE SPFYTSAHPN AGLPNEMGEY DETPEQMGEV IDGFLRDNLV NIIGGCCGTT PDHIRVIAEI AGKHSPRPLP ASETVMKLSG LEPVKINALT NFVNIGERCN VTGSKKFARL IRESKYDEAL SIAREQVESG AQVIDVNLDE GMIDGVEAMK TFVNLIASEP DISKVPLMID SSKWEVIESG LKCVQGKSIV NSISLKEGEE KFKESARTVL RYGAATVVMA FDEKGQADNY ERRIEICERA YRILVDEVGF PAEDIIFDPN ILTVATGMEE HNNYAVDFIN SVRWIKENLP HAKVSGGVSN VSFSFRGNEP VREAIHTAFL YHAIKAGMDM GIVNAGQIGI YDEIPKDVLE LVEDVLLNRR ADATERLVTY AETVKDKGKS QSGPDLSWRQ LPVKERISHA LVKGIADYVD EDTEECRLLF DRPLEVIEGP LMDGMSIVGD LFGEGKMFLP QVVKSARVMK KAVAYLQPFI EAEKQDGGSS AGKILLATVK GDVHDIGKNI VGVVLGCNNY EIIDLGVMVP TDKILAAAQE HNVDIIGLSG LITPSLDEMV GVAKEMERRS MKMPLLIGGA TTSRIHTAVK IDPNYSGPVI HVLDASRSVP VAGKLIQSEQ SQAEVLADIK AEYAKLRDDH SKRGGEKAHV AIGKARDNKA KIDWTNFQAV KPQFLGTRVY DDYDLAEISK YIDWTPFFQT WQLHGKYPKI FDDAVVGKEA QRLFEDAAVL LGEIIRDKTL KARAVVGFWP ANSIGDDIVL HHFNEETREV LCERHGSHQH IEYKISQQGV ENLNAGELVA DTAAVLHHLR QQSQKAANLP NYCLSDFVAP LESGHTDYVG GFAVTAGVGI EALLEKYEKD HDDYNSIMIK ALADRLVEAL AELMHEKVRK ELWGYAKEES FSNEELIKEE YKGIRPAPGY PACPDHTEKR HLFDLLNAEE LGITLTESFA MYPASSVSGW YFSHPDSRYF PVGKIYKDQV EDYARRKNMP VEEIEKWLSP VLAY // ID C6WIB0_ACTMD Unreviewed; 1178 AA. AC C6WIB0; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 27-MAY-2015, entry version 50. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACU36153.1}; GN OrderedLocusNames=Amir_2211 {ECO:0000313|EMBL:ACU36153.1}; 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 {ECO:0000313|EMBL:ACU36153.1, ECO:0000313|Proteomes:UP000002213}; RN [1] {ECO:0000313|EMBL:ACU36153.1, ECO:0000313|Proteomes:UP000002213} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU 3971 RC {ECO:0000313|Proteomes:UP000002213}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001630; ACU36153.1; -; Genomic_DNA. DR RefSeq; WP_015801042.1; NC_013093.1. DR RefSeq; YP_003099999.1; NC_013093.1. DR STRING; 446462.Amir_2211; -. DR EnsemblBacteria; ACU36153; ACU36153; Amir_2211. DR KEGG; ami:Amir_2211; -. DR PATRIC; 20767321; VBIActMir80567_2269. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; AMIR446462:GH7R-2256-MONOMER; -. DR Proteomes; UP000002213; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002213}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002213}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 737 737 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1178 AA; 128381 MW; 68DD97383375CDBB CRC64; MSDRVSSPLL DALTERVVVA DGAMGTMLQS FDLSLDDFAG HEGCNEILNT TRPDVVRAVH RGYLEAGADA VETNTFGANL SNFSDYGIQD RIFELSRLGA QLAREAADEH SEPGRPRFVL GSVGPGSKLP TLGHVAYSVL RDSYVEQIRG LLVGGSDAII VETSQDLLQT KAAIVGARRA MDAEGLRVPI IAQVTVETTG TMLLGSEIGA ALTALEPLGI DLVGLNCATG PAEMSEHLRH IAKHARIPLS VMPNAGLPQL GPNGAVYPLG PEELAQALRG FATEFGARLV GGCCGTTAEH VRQVAAAVRD LGPTTRRPRP EPGVSSLYQA VPFQQDASVL MIGERTNANG SKAFREAMLA DRWDDCVGIA RDQTRDGAHL IDLNIDYVGR DGVADMSALA SRLATASTLP IMLDSTEPEV LQAGLEHLGG RCAVNSVNYE DGDGPDSRFQ RIMRLVAEHG AAVVGLCIDE EGQARTAEWK VRVAIRIIED LVGNWGLRHG DIIIDCLTFP ISTGQEEVRR DGVETIEAIR ELKRRYPEVR TTLGLSNVSF GLNPAARQVL NSVFLHECVQ AGLDTAIVHA SKIVPMARIP DEQRAVALDL VYDRRREGYD PLQRLMELFE GVTTSASKAT RAQELAALPL FERLQRRIVD GERNGLEADL DEALTRRPAL QIINDTLLAG MKTVGELFGS GQMQLPFVLQ SAEVMKTAVA HLEPHMERSD DGGKGRIVLA TVKGDVHDIG KNLVDIILSN NGYEVINLGI KQPISAILDA AENHRADAIG MSGLLVKSTV IMKENLEEMN SRGVAARWPV LLGGAALTRA YVENDLTDTY LGEVRYARDA FEGLRLMDAV MAAKRGESPL IDPEAERKAA ERKARRERSL RIAAERKAAQ PEPEPVSRSD VAADLPVPTP PFWGTRVVKG VPLGDYSALL DERATFMGQW GLRGSRGSGP SYEELVETEG RPRLRYWLER LATEGVLAHA AVVYGYFPCV SEGDSLVILG EPSVDAPEVT RFAFPRQKRD RRLCLADFWR PRESGEVDVV PFQLVTMGQP IADYANELFA KDAYREYLEV HGLGVQLTEA LAEYWHKRVR EELTWPGGGV VAAEDPADVE EYFKLGYRGA RYSLGYGACP DMEDRTKVVA LLEPGRIGVK LSEELQLHPE QSTDAFIAHH PEAKYFNA // ID C6WTP7_METML Unreviewed; 1263 AA. AC C6WTP7; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 27-MAY-2015, entry version 46. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACT49188.1}; GN OrderedLocusNames=Mmol_2286 {ECO:0000313|EMBL:ACT49188.1}; OS Methylotenera mobilis (strain JLW8 / ATCC BAA-1282 / DSM 17540). OC Bacteria; Proteobacteria; Betaproteobacteria; Methylophilales; OC Methylophilaceae; Methylotenera. OX NCBI_TaxID=583345 {ECO:0000313|EMBL:ACT49188.1, ECO:0000313|Proteomes:UP000002742}; RN [1] {ECO:0000313|Proteomes:UP000002742} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JLW8 / ATCC BAA-1282 / DSM 17540 RC {ECO:0000313|Proteomes:UP000002742}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001672; ACT49188.1; -; Genomic_DNA. DR RefSeq; WP_015833223.1; NC_012968.1. DR RefSeq; YP_003049715.1; NC_012968.1. DR STRING; 583345.Mmol_2286; -. DR EnsemblBacteria; ACT49188; ACT49188; Mmol_2286. DR KEGG; mmb:Mmol_2286; -. DR PATRIC; 22614827; VBIMetMob89187_2303. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; MMOB583345:GHCF-2341-MONOMER; -. DR Proteomes; UP000002742; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002742}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002742}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 257 257 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 791 791 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1263 AA; 138430 MW; D3F8A09B366E00F3 CRC64; MAQLTISPIE TQLRALLAQR ILILDGAMGT MIQQYKLTEA DYRGERFVDF KAPAGERELF VKGNNELLTL TQPAIIQEIH EKYLAAGADI IETNTFGATA VAQDDYHMAH LVYEMNVEAA KLAKAACAKY STPDKPRFVA GALGPTPKTA SISPDVNDPA ARNVNFDQLV NAYLEQTRAL VEGGADILMV ETIFDTLNCK AALFAIDTYF EEVGRTLPIM ISGTVTDASG RILSGQTVTA FWHSVRHAKP LTIGLNCALG ATLMRPYVEE LSSIADTFVC IYPNAGLPNP MSDTGFDETP DVTSSLVKEF AQSNFLNIAG GCCGTTPAHI NAIYNEIKDL PPRQLPALPR TLKLSGLEPF VVDDDSLFVN VGERTNVTGS KAFARLIINE QYDEALTVAR QQVENGAQVI DINMDEGMLD AIKAMTHFLN LVASEPDIAR VPIMIDSSKW SVIEAGLKCV QGKAVVNSIS MKEGEEEFIR QAQLCKRYGA AAIVMAFDEK GQADTFERKI EICKRAYDLL VEKLDFPPED IIFDPNIFAI ATGIEEHNNY AVDFINATHW IKQHLPYAKI SGGVSNVSFS FRGNDPAREA IHTVFLYHAI KAGMTMGIVN AGMMGVYDDL APELKERVED VVLNRVVDPN NPLAATERMI EIASTLVAGG KKEAATLEWR GTPENPVPVE KRLSHAMVHG ITEFIVDDTE EARQKVAAAG GRPIHVIEGP LMDGMNVVGD LFGQGKMFLP QVVKSARVMK SAVAHLIPFI EAEKAADEAR TGIVAKPKGK MVIATVKGDV HDIGKNIVSV VLQCNNFEVV NMGVMVPASE ILAMAKAENA DIIGLSGLIT PSLEEMAHVA REMQRDPYFS EQKMPLLIGG ATTSRAHTAV KIAPHYDGPI VYVADASRSV TVMQNLLTPE TRGAYLAEIQ ADYEKARTQH ANKKGTPMLT IAEARANKAD LSFAGADAPV KPKFIGRREI KNADLSVIAQ YIDWTPFFQT WDLAGFYPAI LKDEVVGDAA TKLFNEAQMM LKKIIDGRWL TANGVVALHP ANRTGDDDIE IYTDETRTNI AFTYYGMRQQ TVKPVIDGIA RPNQCLADFI APKGTPDYIG LFAVTAGLGI EKHEQRFEAA HDDYSSIMLK ALADRLAEAF AEYMHERVRV DFWGYAPNEN VTKEGLIKEQ YQGIRPAPGY PACPDHTVKP DMFKLLQAEA ISMALTESFA MSPGAAVSGF YFAHPESKYF SVDKIGIDQL EDMAKRRGLT KEYLERWLAP NLS // ID C6X231_FLAB3 Unreviewed; 336 AA. AC C6X231; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 27-MAY-2015, entry version 36. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:ACU08494.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ACU08494.1}; GN OrderedLocusNames=FIC_02052 {ECO:0000313|EMBL:ACU08494.1}; OS Flavobacteriaceae bacterium (strain 3519-10). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae. OX NCBI_TaxID=531844 {ECO:0000313|EMBL:ACU08494.1, ECO:0000313|Proteomes:UP000001512}; RN [1] {ECO:0000313|EMBL:ACU08494.1, ECO:0000313|Proteomes:UP000001512} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3519-10 {ECO:0000313|EMBL:ACU08494.1, RC ECO:0000313|Proteomes:UP000001512}; RX PubMed=18622572; DOI=10.1007/s00792-008-0178-2; RA Raymond J.A., Christner B.C., Schuster S.C.; RT "A bacterial ice-binding protein from the Vostok ice core."; RL Extremophiles 12:713-717(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; CP001673; ACU08494.1; -; Genomic_DNA. DR RefSeq; WP_015806778.1; NC_013062.1. DR RefSeq; YP_003096556.1; NC_013062.1. DR STRING; 531844.FIC_02052; -. DR EnsemblBacteria; ACU08494; ACU08494; FIC_02052. DR KEGG; fba:FIC_02052; -. DR PATRIC; 21893136; VBIFlaBac12467_2039. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; FBAC531844:GHFZ-2052-MONOMER; -. DR Proteomes; UP000001512; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001512}; KW Methyltransferase {ECO:0000313|EMBL:ACU08494.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001512}; KW Transferase {ECO:0000313|EMBL:ACU08494.1}. SQ SEQUENCE 336 AA; 36896 MW; 8B896A1728DF683D CRC64; MISKKSIIPQ LNHRILVLDG AMGTMLQHYK FTEEDYRGDR FQTWAHSLKG NNDLLSLTQP LAIEEVHRKY LEAGADIIET NTFSATTIAM ADYHLEDFVY ELNFESAKIA RKICDEFTLS DPQKPRFVAG SIGPTNKTAS LSPDVNDPGY RAITFDELRI AYKQQSEALL DGGADILLVE TVFDTLNAKA ALFAIDEIRG ERGIDIPVMV SGTITDASGR TLSGQTAEAF LISVSHLDLL SIGFNCALGA QQLTPYLEEI AEKSGFYVSA YPNAGLPNAF GQYDESPERM AEQIKEYLDR KLVNIIGGCC GTTPAHIKAI ADLVKDYSPR QVGVSA // ID C6XB51_METGS Unreviewed; 1289 AA. AC C6XB51; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 01-APR-2015, entry version 47. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACT51821.1}; GN OrderedLocusNames=Msip34_2584 {ECO:0000313|EMBL:ACT51821.1}; OS Methylovorus glucosetrophus (strain SIP3-4). OC Bacteria; Proteobacteria; Betaproteobacteria; Methylophilales; OC Methylophilaceae; Methylovorus. OX NCBI_TaxID=582744 {ECO:0000313|EMBL:ACT51821.1, ECO:0000313|Proteomes:UP000002743}; RN [1] {ECO:0000313|Proteomes:UP000002743} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SIP3-4 {ECO:0000313|Proteomes:UP000002743}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001674; ACT51821.1; -; Genomic_DNA. DR RefSeq; WP_015831061.1; NC_012969.1. DR RefSeq; YP_003052348.1; NC_012969.1. DR STRING; 582744.Msip34_2584; -. DR EnsemblBacteria; ACT51821; ACT51821; Msip34_2584. DR KEGG; mei:Msip34_2584; -. DR PATRIC; 22620064; VBIMetSp110381_2503. DR eggNOG; COG1410; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; MGLU582744:GHXQ-2639-MONOMER; -. DR Proteomes; UP000002743; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 2. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002743}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002743}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 353 353 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 354 354 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 816 816 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1289 AA; 141001 MW; A59829FF3F99CC15 CRC64; MNQPSTLSTA IPISATEVRL RELLAERILI LDGAMGTMIQ RYKLTEEDYR GGPQGRFADF KPGLAFCPNG DGCGCGQPHA APAEGEAREL FVKGNNELLT LTQPHIIQEI HEQYLAAGAD IIETNTFGAT TVAQEDYHMA HLAFEMNVEA AKLARAACDK YSTPDKPRFV AGALGPTPKT ASISPDVNDP AARNITFDQL VKAYLEQTIA LVEGGADILL VETIFDTLNC KAALFAIDAY FEQSGKRLPI MISGTVTDAS GRILSGQTVP AFWHSVRHAR PLTIGLNCAL GAALMRPYAE ELSKIADTFV CIYPNAGLPN PMSDTGFDEE PQDTSSLLKE FAESGFVNVA GGCCGTTPAH IQAIAETVKN IAPRQVPAPR HATLLAGLEP FIIDDSSLFV NVGERTNVTG SKAFARMILN EQYEDALQVA RQQVENGAQV IDINMDEGML DAVKAMTHFL NLVASEPDIA RVPIMIDSSK WEVIEAGLKC VQGKSIVNSI SMKEGEAEFL RQARLCRRYG AAVIVMAFDE KGQADTYERK IEICKRAYDL LVNEASFPPE DIIFDPNIFA VATGIEEHNN YAVDFINATR WIKENLPYAK ISGGVSNVSF SFRGNDPARE AIHTVFLYHA IKAGMTMGIV NAGMVGVYDD LPAELRERVE DVVLNRREDA TERMIEFAAT LTAGGKKEAP TLEWRGTPEQ PVSVGKRLEH AMVHGITEFI VEDTEEARQQ VMAAGGRPIN VIEGPLMDGM NVVGDLFGQG KMFLPQVVKS ARVMKQAVAH LIPFIEEEKA AEEKRTGVAA KPKGKVVIAT VKGDVHDIGK NIVSVVLQCN NFEVVNMGVM VPCSEILATA KVENADIIGL SGLITPSLEE MAYVAKEMQR DPHFRMLKIP LLIGGATTSR AHTAVKIAPN YDGPVIYVPD ASRSVSVMQS LLTPEQRESY INEVAADYDR ARTQHANKKG PTMLTLAEAR ANKVKARFDG ANAPVKPKFI GRRVFKNIDL ATIAEYIDWG PFFQTWDLAG FYPAILTDSV VGEAATKLLA EGQAMLKKII EGRWLTANGV VALLPANTVN DDDIEIYTDD TRSQVAFTWY GMRQQTAKPV IDGVARPNQC LADYIAPKAS GVADYIGMFA VTGGLGIDKY LERFENDHDD YSSIMLKSLA DRLAEAFAEY LHARVRTDLW GYAADEQLDN DALIKEQYRG IRPAPGYPAC PDHTVKPDMF QVMQCDEIGM TLTESLAMMP AAAVSGFYLA HADAKYFSVD KIGQDQLKDM ATRRGLSEEY LERWLAPNL // ID C6XMD2_HIRBI Unreviewed; 350 AA. AC C6XMD2; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 27-MAY-2015, entry version 38. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACT58075.1}; GN OrderedLocusNames=Hbal_0373 {ECO:0000313|EMBL:ACT58075.1}; OS Hirschia baltica (strain ATCC 49814 / DSM 5838 / IFAM 1418). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Hyphomonadaceae; Hirschia. OX NCBI_TaxID=582402 {ECO:0000313|EMBL:ACT58075.1, ECO:0000313|Proteomes:UP000002745}; RN [1] {ECO:0000313|Proteomes:UP000002745} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49814 / DSM 5838 / IFAM 1418 RC {ECO:0000313|Proteomes:UP000002745}; 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; ACT58075.1; -; Genomic_DNA. DR RefSeq; WP_015826225.1; NC_012982.1. DR RefSeq; YP_003058772.1; NC_012982.1. DR STRING; 582402.Hbal_0373; -. DR EnsemblBacteria; ACT58075; ACT58075; Hbal_0373. DR KEGG; hba:Hbal_0373; -. DR PATRIC; 22128674; VBIHirBal9878_0382. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; HBAL582402:GHMV-376-MONOMER; -. DR Proteomes; UP000002745; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002745}; KW Methyltransferase {ECO:0000313|EMBL:ACT58075.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002745}; KW Transferase {ECO:0000313|EMBL:ACT58075.1}. SQ SEQUENCE 350 AA; 38269 MW; ADD544A32BDBC3AE CRC64; MNREQRLEKI TKIANERVLI LDGAMGTELQ TFKLTEEDFR GAQFKDVDRF LKGNNDLLNL TKPDVVKEVH RRYFNAGADI AETNTFSATT IAQADYALES LAAEIAREGA KIAREVADEF ETEDAPKAVW SAIGPTNKTL SLSPDVNDPG FREVTFEHVA KAYQEQIAAM AEFSDVFLIE TVFDTLNAKA AIKAVKDWEF ESGESRPIVL SGTITDASGR TLSGQTTEAF WYSVRHAKPW AIGLNCALGA DLMRQYVVAL SRVADTRVLA YPNAGLPNEF GEYDVTPDEQ AVHLKAWAQD GIVNVLGGCC GTTPAHIEAI AKAVKSSAPR KIPSIDPAMR LSGLEPFVLA // ID C6XUY2_PEDHD Unreviewed; 1219 AA. AC C6XUY2; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 27-MAY-2015, entry version 48. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACU05990.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ACU05990.1}; GN OrderedLocusNames=Phep_3799 {ECO:0000313|EMBL:ACU05990.1}; OS Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / NCIB 9290). OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Pedobacter. OX NCBI_TaxID=485917 {ECO:0000313|EMBL:ACU05990.1, ECO:0000313|Proteomes:UP000000852}; RN [1] {ECO:0000313|EMBL:ACU05990.1, ECO:0000313|Proteomes:UP000000852} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13125 / DSM 2366 / NCIB 9290 RC {ECO:0000313|Proteomes:UP000000852}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001681; ACU05990.1; -; Genomic_DNA. DR RefSeq; WP_015809599.1; NZ_AQGK01000003.1. DR RefSeq; YP_003094052.1; NC_013061.1. DR STRING; 485917.Phep_3799; -. DR EnsemblBacteria; ACU05990; ACU05990; Phep_3799. DR KEGG; phe:Phep_3799; -. DR PATRIC; 22884835; VBIPedHep98714_3866. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PHEP485917:GHL9-3850-MONOMER; -. DR Proteomes; UP000000852; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000852}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACU05990.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000852}; KW Transferase {ECO:0000313|EMBL:ACU05990.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 242 242 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 757 757 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1219 AA; 135259 MW; 5A8B9783105484B3 CRC64; MDIRKELEKR ILIIDGAMGT MIQRYTLTEE DFRGERFKDH PCDVKGNNDM LSITRPDVIK EIHTEYLKAG TDIIETNTFS TQRISLADYQ MEPLAYEMSF EGAKIAKEAV NEFMAANPDR KCFVAGAVGP TNRTLSISPD VNDPGFRAIT FDELVEAYDE QVRGLVDGGA DLLLIETIFD TLNAKAAIFS IKKYEAEIGR KIEIMISGTI TDASGRTLSG QTAEAFLNSV MHANPLSIGF NCALGAKDMR PHIEELSAKA GCYVSAYPNA GLPNEFGAYD EMPHETAHLV EDFIQHGFVN IVGGCCGTTP EHIGCIAKKA KNVAPRKIPH IEPYLRLSGL EPVTITPESI FVNIGERTNI TGSPKFSKLI LGGDFEAALA VARQQVEGGA QVIDVNMDEG MIDSEASMTK FLNLIASEPD ISKLPIMVDS SKWTVIEAGL KCLQGKGIVN SISLKEGEDK FRESARKIMT YGAAVVVMAF DELGQADNFE RRKEICKRSY DILVDEIGFP AQDIIFDPNI LTVATGLEEH NNYAVDFINA TRWIKENLPY AKVSGGVSNI SFSFRGNNTV REAMHSAFLY HAIKAGLDMG IVNAGMLEVY QEIPPELLVL VEDVLLNRRD DATERLVEFA DTIKSKGKEI VRDEEWRKTS VEERLSHALV KGIIEYLDAD VEEARQKYAR PIEVIEGPLM DGMNIVGDLF GAGKMFLPQV VKSARVMKKA VAYLLPFIEQ EKLDNPDQDQ NSSAGKILMA TVKGDVHDIG KNIVGVVLAC NNFEIVDMGV MVPAQDIIKK AKEINADIIG LSGLITPSLD EMVHFAKEME REGFTIPLMI GGATTSRIHA AVKVAPNYSG PAIHVLDASR SVTVASTLMN KDTRDEYIAG IRAEYDKARE AHLNKRSDKR FKTIEEARKD NFKIDTSLVA PAPTFTGTKV FDNYPLEELV PYIDWTPFFQ TWELRGSYPR ILEDKVVGDE AKKLFNDAKV LLKRIVEEKL LTARAVIGFW PANAVGDDIV LAVEGKEVVI HTLRQQAEKT ADQPYYALSD FIAQKETGIP DYFGGFALTT GIGCDELVAE FEAVYDDYNS IMAKALADRL AEAFAERMHE LVRKEYWGYA KDEHLDNEAL IKEEYSGIRP APGYPACPEH TEKGTLFELL DAEARIGLSL TESYAMYPTA AVSGFYFAHP QSRYFGLGKI TKDQVEDYAV RKNMPLEEVE RWLSPNLAY // ID C6YTC4_9GAMM Unreviewed; 348 AA. AC C6YTC4; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 29-APR-2015, entry version 22. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:AJI74255.1}; GN ORFNames=BZ13_1329 {ECO:0000313|EMBL:AJI74255.1}; OS Francisella philomiragia subsp. philomiragia ATCC 25015. OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Francisellaceae; Francisella. OX NCBI_TaxID=539329 {ECO:0000313|EMBL:AJI74255.1, ECO:0000313|Proteomes:UP000031897}; RN [1] {ECO:0000313|EMBL:AJI74255.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=O#319L {ECO:0000313|EMBL:AJI74255.1}; RA Daligault H.E., Bishop-Lilly K.A., Broomall S.M., Chain P.S., RA Chertkov O., Coyne S.R., Davenport K.W., Erkkila T., Frey K.G., RA Gibbons H.S., Gu W., Jaissle J., Johnson S.L., Koroleva G.I., RA Ladner J.T., Lo C.-C., Minogue T.D., Munk C., Palacios G.F., RA Redden C.L., Rosenzweig C.N., Scholz M.B., Teshima H., Xu Y.; RL Submitted (NOV-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; CP010019; AJI74255.1; -; Genomic_DNA. DR EnsemblBacteria; EET20478; EET20478; FTPG_01162. DR Proteomes; UP000031897; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000031897}; KW Methyltransferase {ECO:0000313|EMBL:AJI74255.1}; KW Transferase {ECO:0000313|EMBL:AJI74255.1}. SQ SEQUENCE 348 AA; 38711 MW; 38DA09AA2AB6F3E9 CRC64; MIERLNKGPV ICAEGFIFEL ERRGFLASGE FVPTVVLDHP EIVEGLHREF QHAGSDVVEA LTYYAHREKL KVAGQEHIIE DLNRQALRIA KKVADSAPKG VQPNLMAGNI CNSNIWKQGD RKAQLEVERM FDEMVTWAVE EGADMIIGET FSYAEEAFKA VEVIKKSGLP AVLTIAPMGQ NVMLDGWSIV DTCKELEQLG ADVVGLNCFR GPQTMLPYLK DIRKAVKCHV AALPVPYRTT DDHPTFFNLP DNNGCSCPSP HGRPFPTALD PLFCNRYEIR EFAKEAYDFG VNYLGVCCGA SPALIREVAE AVGLTVPASK YREKMQNHSM YGTHQRIAKH IQAYGDKA // ID C6Z5Z0_9BACE Unreviewed; 917 AA. AC C6Z5Z0; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 27-MAY-2015, entry version 31. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EET16299.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EET16299.1}; GN Name=metH {ECO:0000313|EMBL:EET16299.1}; GN ORFNames=BSFG_02446 {ECO:0000313|EMBL:EET16299.1}; OS Bacteroides sp. 4_3_47FAA. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=457394 {ECO:0000313|EMBL:EET16299.1}; RN [1] {ECO:0000313|EMBL:EET16299.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=4_3_47FAA {ECO:0000313|EMBL:EET16299.1}; 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., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EET16299.1}. 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; ACDR02000082; EET16299.1; -; Genomic_DNA. DR RefSeq; WP_008669919.1; NZ_JH114368.1. DR ProteinModelPortal; C6Z5Z0; -. DR EnsemblBacteria; EET16299; EET16299; BSFG_02446. DR PATRIC; 30530110; VBIBacSp78517_2512. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EET16299.1}; KW Transferase {ECO:0000313|EMBL:EET16299.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 243 243 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 917 AA; 100896 MW; E97F0983C01F0FDB CRC64; MATLKQLIDE RVLILDGAMG TMIQRYNLSE QDFRGERFAE MPGQMKGNND LLCLTRPDVI KDIHHKYLEA GADIIETNTF NAQRVSMADY HMQDLCREIN LAAAGLAREM ADEYTAKTPH KPRFVAGSVG PTNKTCSMSP DVNNPALRAL TYDELAAAYQ EQMEALLEGG VDALLIETIF DSLNAKAAIY AAETAMKKVG REVPLMLSVT VSDIAGRTLS GQTLDAFLAS VQHAPIFSIG LNCSFGAKQL KPFLEGLAAR APYYISAYPN AGLPNSLGQY DQTPEEMASE VKEYIDEGLV NIIGGCCGTT EEYIAKYQEL IVSGSAWVSP HIPATTPERL WLSGLELLEQ TPEMNFINVG ERCNVAGSRK FLRLINEKKY EEALSIARKQ VEDGALVIDV NMDDGLLDAR EEMTTFLNLV MSEPDIARVP VMIDSSKWEV IEAGLKCLQG KSIVNSISLK EGEEIFIEHA RLIKKLGAAV VVMAFDEKGQ ADTFERKIEV CARAYKILTE QVDFNPHDII FDPNVLAVAT GIEEHDNYAV DFIKATGWIK KNLPGAHVSG GVSNLSFSFR GNNYIREAMH AVFLYHAIRQ GMDMGIVNPA ASVLYTDIPA DVLERIEDVV LNRRPDAAER LIETAEALKR TSTGTEAVKQ DVWREEPMVE KRLQYALIKG IGDHLEEDLA EAVKLYPKAV DIIEGPLMEG MNKVGELFGA GKMFLPQVVK TARTMKKAVA ILQPLIEADK QEGVRSAGKV LMATVKGDVH DIGKNIVSVV MACNNYEIID LGVMVPAEMI VRKAIEEKVD IIGLSGLITP SLEEMAHVAV ELKRAGLDIP IMIGGATTSK LHTALKIAPV YGGPVIHMKD ASQNALVAAR LLNPESSSEF VERLNKEYED LRLKNSVRQV KTVSLEEAQK NKLNLWS // ID C7CDH6_METED Unreviewed; 1250 AA. AC C7CDH6; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 27-MAY-2015, entry version 49. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CAX23867.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAX23867.1}; GN Name=metH {ECO:0000313|EMBL:CAX23867.1}; GN OrderedLocusNames=METDI2267 {ECO:0000313|EMBL:CAX23867.1}; OS Methylobacterium extorquens (strain DSM 5838 / DM4) (Methylobacterium OS dichloromethanicum (strain DM4)). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=661410 {ECO:0000313|EMBL:CAX23867.1, ECO:0000313|Proteomes:UP000008070}; RN [1] {ECO:0000313|Proteomes:UP000008070} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 5838 / DM4 {ECO:0000313|Proteomes:UP000008070}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; FP103042; CAX23867.1; -; Genomic_DNA. DR RefSeq; WP_015822192.1; NC_012988.1. DR RefSeq; YP_003067816.1; NC_012988.1. DR STRING; 661410.METDI2267; -. DR EnsemblBacteria; CAX23867; CAX23867; METDI2267. DR KEGG; mdi:METDI2267; -. DR PATRIC; 22523145; VBIMetExt143287_2106. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; MEXT661410:GJA1-2214-MONOMER; -. DR Proteomes; UP000008070; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008070}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAX23867.1}; KW Transferase {ECO:0000313|EMBL:CAX23867.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 254 254 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 318 318 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 771 771 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1250 AA; 137107 MW; 63338FCE736E884C CRC64; MTAFPPVDGT EIERALRQRA SEKILVLDGA MGTVIQRLKY TEEDFRGERF KDHSHDQKGN NDLLILTQPD AIRQIHLDYF LAGADVCETN TFSGTTIAQA DYGMESIIHE LNAEGARLAR EAAKLAEEQD GRRRFVAGAI GPTNRTLSIS PDVNNPGYRA VTFDGVKQAY VEQVRGLIDG GAELILIETI FDTLNAKAAI AAAWQVFDET GIRLPIQISG TITDLSGRTL SGQTPAAFWN SLRHSSPLTF GLNCALGAKE MRGHIAELSR ICDTLVCAYP NAGLPNEFGL YDESPEAMGK LVGEFAASGL VNMVGGCCGT TPDHIRAIAE AVADKKPREI PEIPRLMRLS GLEPFVLTKE IPFVNVGERT NVTGSAKFRK LITNNDYAAA LDVARDQVAA GAQVIDVNMD EGLLDSEKAM VEFLNLVAAE PDIARVPVMV DSSKFEVIEA GLKCIQGKPI VNSISMKEGE AKFIEAAKIC RSYGAAVVVM AFDEQGQADS YERKVEICTK AYKILTEQVG FPPEDIIFDP NIFAVATGIE EHNPYGVAFI EATRTIRETL PHAHISGGVS NLSFAFRGNE PVREAMHAVF LFHCIKAGMD MGIVNAGQLA VYDEIPAELR ELCEDVVLNR REDSTERLLE AAERFKTGAS AQAKTADLTW REAPVAKRIE HALVNGITEY IVSDTEEARK EAARPLHVIE GPLMAGMNVV GDLFGSGKMF LPQVVKSARV MKQAVAYLEP FMEEEKRANG GDGKRQAAGK VLMATVKGDV HDIGKNIVGV VLACNNYEII DLGVMVPAAK ILETAKRENV DIVGLSGLIT PSLDEMVHVA AEMEREGMEM PLLIGGATTS RVHTAVKIHP AYAKGQAVYV TDASRAVGVV SSLISKETRG ATVEKVRAEY AKVADAHRRS EADKQRLPLA KARANAFKVD WSAYKPAKPS FTGTRVYGSY EVADLVPYID WTPFLQTYEF KGRYPAILDD PEQGPAARAL FEDAQVMLKQ IVEERWFNPK AVIGFWPANS VGDDIRLFTG ESRQETLATF HGLRQQLSKR DGRANTCISD FVAPAETGIA DYVGAFVVTA GLEEVRIAER FERANDDYRS ILVKALADRI AEAFAERMHE RVRKEFWGYA PDEAYAPEEL VSEKYDGIRP APGYPAQPDH TEKVQLFDLL KAESRIGVKL TESYAMWPGS SVSGLYIAHP DAHYFGVAKV ERDQVEDYAL RKGMDVSEVE RWLGPILNYD PVRYLKAAAE // ID C7D6E3_9RHOB Unreviewed; 338 AA. AC C7D6E3; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Methionine synthase I {ECO:0000313|EMBL:EET49324.1}; GN ORFNames=TR2A62_0862 {ECO:0000313|EMBL:EET49324.1}; OS Thalassobium sp. R2A62. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Thalassobium. OX NCBI_TaxID=633131 {ECO:0000313|EMBL:EET49324.1}; RN [1] {ECO:0000313|EMBL:EET49324.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=R2A62 {ECO:0000313|EMBL:EET49324.1}; 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 (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG697169; EET49324.1; -; Genomic_DNA. DR RefSeq; WP_009160380.1; NZ_GG697169.2. DR EnsemblBacteria; EET49324; EET49324; TR2A62_0862. DR PATRIC; 29912206; VBIThaSp99002_0838. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 212 212 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 278 278 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 279 279 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 338 AA; 35289 MW; 8188BB0AF6B6DE1E CRC64; MTNPLAQLLE TRDWLLADGA TGTNLFNMGL ESGDAPELWN VDHANRIKTL YSGAVDAGSD VFLTNTFGGN ASRLKLHNAQ SRVHELNRVG AEIAREVADA SGRTVIVAGS VGPTGDIMAP LGTLTHKSAV EMFHEQAEGL KAGGADVAWV ETISAPEEFE AAAKAFALAD MPWCGTMSFD TAGRTMMGLT SADMVKAVAK LDHQPIAFGA NCGVGASDLL RTIQGFAKAD APLPLISKGN AGIPKYHDGH IHYDGTPDLM ADYACLARDS GATIIGGCCG TTPEHLVAMR AALETRATTA RPSLDEIAQK LGAFSSASDG TDGAAPAPRR TRRRAKSA // ID C7DDC7_9RHOB Unreviewed; 288 AA. AC C7DDC7; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 01-OCT-2014, entry version 14. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EET49635.1}; GN ORFNames=TR2A62_2330 {ECO:0000313|EMBL:EET49635.1}; OS Thalassobium sp. R2A62. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Thalassobium. OX NCBI_TaxID=633131 {ECO:0000313|EMBL:EET49635.1}; RN [1] {ECO:0000313|EMBL:EET49635.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=R2A62 {ECO:0000313|EMBL:EET49635.1}; 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 (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; GG697169; EET49635.1; -; Genomic_DNA. DR RefSeq; WP_009160686.1; NZ_GG697169.2. DR EnsemblBacteria; EET49635; EET49635; TR2A62_2330. DR PATRIC; 29915118; VBIThaSp99002_2267. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EET49635.1}; KW Transferase {ECO:0000313|EMBL:EET49635.1}. SQ SEQUENCE 288 AA; 30304 MW; 12E3BCF00A0DE959 CRC64; MITLLDGGMG QELIARAGKA TGLWSVQALL DQPELVREVH DEYFAAGAQV ATTNTYSVLP DRLEKEGLGD HLHRLSDLAC RMAVEARDAH GSGMVAGSLG PIGFSYQPDK APPAERAAEV YADLAQAHAK FVDVHVLETM SSVDQARGGL MGCAVTDKPV WVAVSVDDNN GTRLRSGEPV VDVLTLLAEY KPAALFINCS LPEAVSQAIP LIAGQGVPVG AYANGFTGIS DSFDHIGSTV DVLKARTDLG PNQYADFAQG WVDAGATLIG GCCEVGPAHI AEMSRRFS // ID C7G6V2_9FIRM Unreviewed; 816 AA. AC C7G6V2; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEV02446.1}; GN ORFNames=ROSINTL182_05619 {ECO:0000313|EMBL:EEV02446.1}; OS Roseburia intestinalis L1-82. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Roseburia. OX NCBI_TaxID=536231 {ECO:0000313|EMBL:EEV02446.1}; RN [1] {ECO:0000313|EMBL:EEV02446.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=L1-82 {ECO:0000313|EMBL:EEV02446.1}; 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., 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. {ECO:0000313|EMBL:EEV02446.1}. 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; ABYJ02000033; EEV02446.1; -; Genomic_DNA. DR RefSeq; WP_006855754.1; NZ_GG692715.1. DR EnsemblBacteria; EEV02446; EEV02446; ROSINTL182_05619. DR PATRIC; 30038239; VBIRosInt114022_0625. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEV02446.1}; KW Transferase {ECO:0000313|EMBL:EEV02446.1}. SQ SEQUENCE 816 AA; 88671 MW; 422DBC832155113E CRC64; MTREAFRELV KKGPVLLDGA TGTNLQKAGM PVGVCPEQWI LENSEVLIDL QKQYVEAGTD ILFAPTFTAS RIKLKEYGLE DHLEEMNRKL VALSKEAAKG TNALVAGDLT MTGEQLYPLG DLMFEDLVDV YKEQAKIIAE AGADLFVVET MMSLQECRAA VLAIREVCDL PVMVSLTYNE DGRTLYGTDP VTAVVVMQSL GADAVGMNCS TGPEAMLEPI AKMAEYAAIP LLAKPNAGMP ELIDGQTVFN VEPEEFAEVG KKLVEEGAAI IGGCCGTTPE HIRALKEAVK GIPVKAPLQT KRRMLTSERK SVEITLDGRF MVIGERINPT GKKKLQAELK EGSLNLVRTM ALEQEENGAS ILDINMGMNG IDEKEMMLRT IYEVTSTVDC PLCIDSSHVD IIEAALRIYP GRALINSISL EKEKFEKLLP IAKKYGAMFI LLPLSDEGLP KDSAEKHGII RTIMDEAVRI GMAKEDIIVD GLVATIGANP NAALECFETF SYCKNELELP TACGLSNISF GLPERTYVNT AFLTMAIANG LTMAIANPSQ ELLMNAAFAS DMLLNKKESD IRYIERMNFL SEKYAGMERV MVQKTPAGTS AAGGETRKES TGSGVFQAVL KGNKEHVLEE VKKMLDGGAK PDEIINEHLI AAINEVGELF DKKKYFLPQL ISSANTMKLA IEYLEPMLER SNTEAMATIV VATVEGDIHD IGKNLVVLML KNYGYHVIDL GKDVPADVIV DTAMNEGAKV IGLSALMTTT MMRMKDVVEL AKEKGCTAKI VIGGAAITES FSDEIGADGY SKDAAECVKL VERLLA // ID C7GND5_YEAS2 Unreviewed; 324 AA. AC C7GND5; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 07-JAN-2015, entry version 23. DE SubName: Full=Mht1p {ECO:0000313|EMBL:EEU07680.1}; GN Name=MHT1 {ECO:0000313|EMBL:EEU07680.1}; GN ORFNames=C1Q_01791 {ECO:0000313|EMBL:EEU07680.1}; OS Saccharomyces cerevisiae (strain JAY291) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=574961 {ECO:0000313|EMBL:EEU07680.1, ECO:0000313|Proteomes:UP000008073}; RN [1] {ECO:0000313|EMBL:EEU07680.1, ECO:0000313|Proteomes:UP000008073} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JAY291 {ECO:0000313|EMBL:EEU07680.1, RC ECO:0000313|Proteomes:UP000008073}; 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., Missawa S.K., Galzerani F., Costa G.G., Vidal R.O., RA Noronha M.F., Dominska M., Andrietta M.G., Andrietta S.R., Cunha A.F., RA Gomes L.H., Tavares F.C., Alcarde A.R., Dietrich F.S., McCusker J.H., RA Petes T.D., Pereira G.A.; 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. {ECO:0000313|EMBL:EEU07680.1}. 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; ACFL01000073; EEU07680.1; -; Genomic_DNA. DR ProteinModelPortal; C7GND5; -. DR SMR; C7GND5; 3-313. DR OrthoDB; EOG7X9GHR; -. DR Proteomes; UP000008073; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008073}. SQ SEQUENCE 324 AA; 36715 MW; A77194694B6E5C14 CRC64; MKRIPIKELI VEHPGKVLIL DGGQGTELEN RGININSPVW SAAPFTSESF WEPSSQERKV VEEMYRDFMI AGANILMTIT YQANFQSISE NTSIKTLAAY KRFLDKIVSF TREFIGEERY LIGSIGPWAA HVSCEYTGDY GPHPENIDYY GFFKPQLENF NQNRDIDLIG FETIPNFHEL KAILSWDEDI ISKPFYIGLS VDDNSLLRDG TTLEEISVHI KGLGNKINKN LLLMGVNCVS FNQSALILKM LHEHLPGMPL LVYPNSGEIY NPKEKTWHRP TNKLDDWETT VKKFVDNGAR IIGGCCRTSP KDIAEIASAV DKYS // ID C7GSX0_YEAS2 Unreviewed; 325 AA. AC C7GSX0; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 07-JAN-2015, entry version 23. DE SubName: Full=Sam4p {ECO:0000313|EMBL:EEU06101.1}; GN Name=SAM4 {ECO:0000313|EMBL:EEU06101.1}; GN ORFNames=C1Q_03489 {ECO:0000313|EMBL:EEU06101.1}; OS Saccharomyces cerevisiae (strain JAY291) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=574961 {ECO:0000313|EMBL:EEU06101.1, ECO:0000313|Proteomes:UP000008073}; RN [1] {ECO:0000313|EMBL:EEU06101.1, ECO:0000313|Proteomes:UP000008073} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JAY291 {ECO:0000313|EMBL:EEU06101.1, RC ECO:0000313|Proteomes:UP000008073}; 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., Missawa S.K., Galzerani F., Costa G.G., Vidal R.O., RA Noronha M.F., Dominska M., Andrietta M.G., Andrietta S.R., Cunha A.F., RA Gomes L.H., Tavares F.C., Alcarde A.R., Dietrich F.S., McCusker J.H., RA Petes T.D., Pereira G.A.; 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. {ECO:0000313|EMBL:EEU06101.1}. 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; ACFL01000222; EEU06101.1; -; Genomic_DNA. DR ProteinModelPortal; C7GSX0; -. DR SMR; C7GSX0; 15-315. DR OrthoDB; EOG7X9GHR; -. DR Proteomes; UP000008073; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008073}. SQ SEQUENCE 325 AA; 36669 MW; 54658C7B92A610F0 CRC64; MARLPLKQFL ADNPKKVLVL DGGQGTELEN RGIKVANPVW STIPFISESF WSDESSANRK IVKEMFNDFL NAGAEILMTT TYQTSYKSVS ENTPIRTLSE YNNLLNRIVD FSRNCIGEDK YLIGCIGPWG AHICREFTGD YGAEPENIDF YQYFKPQLEN FNKNDKLDLI GFETIPNIHE LKAILSWDES ILSRPFYIGL SVHEHGVLRD GTTMEEIAQV IKDLGDKINP NFSFLGINCV SFNQSPDILE SLHQALPNMA LLAYPNSGEV YDTEKKIWLP NSDKLNSWDT VVKQYISSGA RIIGGCCRTS PKDIQEISAA VKKYT // ID C7H8B4_9FIRM Unreviewed; 809 AA. AC C7H8B4; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 01-OCT-2014, entry version 23. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEU95874.1}; GN ORFNames=FAEPRAA2165_02554 {ECO:0000313|EMBL:EEU95874.1}; OS Faecalibacterium prausnitzii A2-165. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Faecalibacterium. OX NCBI_TaxID=411483 {ECO:0000313|EMBL:EEU95874.1}; RN [1] {ECO:0000313|EMBL:EEU95874.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A2-165 {ECO:0000313|EMBL:EEU95874.1}; 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., 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. {ECO:0000313|EMBL:EEU95874.1}. 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; ACOP02000071; EEU95874.1; -; Genomic_DNA. DR EnsemblBacteria; EEU95874; EEU95874; FAEPRAA2165_02554. DR PATRIC; 30682197; VBIFaePra59507_2014. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEU95874.1}; KW Transferase {ECO:0000313|EMBL:EEU95874.1}. SQ SEQUENCE 809 AA; 85934 MW; 6713A28C34B7D058 CRC64; MQANELFDRP NTILLDGGMG TMLQAAGLKL GARPEELNIT DPALIESIHA RYAAAGSRII NANTFGASAH KLAGSEYTLE EIIAAGIANC KRACAPYGAL AALDVGPLGE LLEPNGTLAF EDAVAEYGRI VRAGVAAGAD LVFLETFTDL YELKAALLAV KENSSLPVLA SMSFEAGGRT FTGCTVESFA ATARGLGADA VGINCSLGPK EIFPMAKRLT EALPGSFPVF VKPNAGLPRA DGSGYDITPQ LYAMQMKPYR ELGLFAAGGC CGTTPEFIQL LNGVFADCRP GRPDHPMKSV VCSPMDCVDV DGITVVGERI NPTGKKRFQQ ALREGDMNYV LEQAVSQTEA GAQILDVNVG APGVDEPALM EQVVKALQSV VSLPLQLDSS HAEALERGLR VYNGKPIVNS VNGEEEKLNT ILPLCKKYGA AVVGLAIDER GILPKAEDRV AIARRIRDAA LAAGIPQEDI YIDCLTLTAS AQQEDVLATV QALHACKEEL GVRTILGVSN ISFGLPCRSY LNTTFLTMAM YAGLDLAIMN PSSEEMMAAV YAYNVLTNRD KQSTKYIERY ANRVPASAAL VQAVQNAQTA PAAGETPEAA GPYAPLMKAV EKGLKGEAAA RTRALLEEKE PLELVDEALI PALDIVGAKY EKGTLFLPQL LQAATAAQGA FEEIKTAIAQ KGEGSASKGR IVIATVKGDV HDIGKNIVRV ILENYGFEVI DLGRDVPVET VVNTVREKDV HLVGLSALMT TTLKSMEETI RALHDAKLDC KIMVGGAVLT PEYAKKIGAD WYAKDAKQSA DIAKEFFGV // ID C7HAY4_9FIRM Unreviewed; 596 AA. AC C7HAY4; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 27-MAY-2015, entry version 26. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=FAEPRAA2165_03498 {ECO:0000313|EMBL:EEU94967.1}; OS Faecalibacterium prausnitzii A2-165. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Faecalibacterium. OX NCBI_TaxID=411483 {ECO:0000313|EMBL:EEU94967.1}; RN [1] {ECO:0000313|EMBL:EEU94967.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A2-165 {ECO:0000313|EMBL:EEU94967.1}; 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., 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEU94967.1}. 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; ACOP02000095; EEU94967.1; -; Genomic_DNA. DR RefSeq; WP_005936540.1; NZ_GG697158.2. DR ProteinModelPortal; C7HAY4; -. DR EnsemblBacteria; EEU94967; EEU94967; FAEPRAA2165_03498. DR PATRIC; 30683742; VBIFaePra59507_2758. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EEU94967.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EEU94967.1}. SQ SEQUENCE 596 AA; 63995 MW; 4C60F2D2B1E5E5F3 CRC64; MKDIRELLQT RPLLFDGAMG TYYKAAPGVE CEQANLTDPA GVLAVHREYL AAGADAVKTN TFSLPRLAAA HTPGWEQLAQ AGWQLAVQAA GETGAAVFAD LGPAPDTEAV PAGQVYTAVA KQFAALGARN FLFETLSSDA GLLDAVGAIR AEVPDAFVLV SFAVLPDGYT REGMYCKDLA RRMQESGIVD AVGLNCVSAP GAMRTLAKQL GGTLPLSVMP NAGYPVVTRT QVKYQGRPEY FARELGRLAA EGTVQILGGC CGTTPAHIAA LRAELDSLTV VKKTAPAEEF STVKEQTVEN EDAFLRKLNA GEKVIAIELD SPRNADLTGY LEGAKKLQAA GADLLTIADC PIAQARMDSS LVACRVHREL GLCTLPHMTC RDRNLNATKA LLLGLYAEGV REVLAITGDP IPTAERDEVK NVYQFNSRKL AQYIVSLAGE GREMPGPMTV FGALNLNARN FDVELRRAKE KLENGMSGFL TQPVLSAQAV ENLKKSRETL GADARILAGI MPVVSQRNAI FMENEINGIH VEDWIIEKFA GLDRAQGEEL GLAISLEMAK AALPYADGLY LMTPFNRVAL MERLIGRLKQ EVLGAY // ID C7IU37_THEET Unreviewed; 807 AA. AC C7IU37; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEU61782.1}; GN ORFNames=TeCCSD1DRAFT_1801 {ECO:0000313|EMBL:EEU61782.1}; OS Thermoanaerobacter ethanolicus CCSD1. OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Thermoanaerobacter. OX NCBI_TaxID=589861 {ECO:0000313|EMBL:EEU61782.1}; RN [1] {ECO:0000313|EMBL:EEU61782.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCSD1 {ECO:0000313|EMBL:EEU61782.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEU61782.1}. 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; ACXY01000027; EEU61782.1; -; Genomic_DNA. DR RefSeq; WP_003868339.1; NZ_ACXY01000027.1. DR EnsemblBacteria; EEU61782; EEU61782; TeCCSD1DRAFT_1801. DR PATRIC; 30827374; VBITheEth125011_1872. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEU61782.1}; KW Transferase {ECO:0000313|EMBL:EEU61782.1}. SQ SEQUENCE 807 AA; 88096 MW; E9392E508311C63F CRC64; MLDIFKELSN RVIVFDGAMG TQLQDRGLKT GECPEYMNIT HPEVVFDIHR SYIEAGADVI ETNTFGANRI KLAKYGLENE VFNIVTQAVK IAKKASKDKP VALSIGPIGE LLTPYGDMTF DEAYDVFKEV VIAAERAGAD IVLIETMSDM LEAKAAILAA KENSSMKVIC TMTFQEDGRT LMGSDPITVV VSLQGLGLDA IGVNCSTGPD KMVSVVEKMS QVSRIPIIAQ PNAGMPVIRD GKTVYDLKPE EFASFFPSLV EKGASIVGGC CGTTPHYIRL VKEAVKNLKP KVKVNKFTAV ASNTKTVFIG HDYSLRVIGE RINPTGKKKL SEAFLAGDVG LAVEEGIKQQ KCGAEILDVN VGVPGVNEEE LLPKVVSEIQ NVVDLPLQID STNIKAVEKA IRILRGRPII NSVSAKEESL KEVLPIVKKY GACVVGLTVG DKGLPKDRHE RIENAKKIIK KAEEYGIPKE DILIDCIVLT VSSEQEAAIE TLEAIKLAKE ELGVNTVVGL SNVSFGLPER RLINSTFLAM AASYGLTTAI INPCDEAMMD TLRASMVLLN KDKGSVNYLK IYGNRQKEEG KEKEQQKIQE EDLKSKFYIQ ILEGKKSGVE DIVKNILDEE VQPLSIVDNI IIPALKEVGD RYEKGIYFLP QLLSSAEVVQ NAFRIIKEKL PKGSVSKGKI ILATVEGDVH DIGKNIVKVL LENYGYDVID LGKDVKGEVI LEEVKRTGAP LVGLSALMTT TLFNMEKIIK LLKANTDVKI MVGGAVLTEE YAYKIGADYY GKTAQDAVKI ADKFFLKNAL LCKTCGI // ID C7JFY7_ACEP3 Unreviewed; 1187 AA. AC C7JFY7; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 27-MAY-2015, entry version 49. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:BAI00557.1}; GN OrderedLocusNames=APA01_24490 {ECO:0000313|EMBL:BAI00557.1}; OS Acetobacter pasteurianus (strain NBRC 3283 / LMG 1513 / CCTM 1153). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acetobacter. OX NCBI_TaxID=634452 {ECO:0000313|EMBL:BAI00557.1, ECO:0000313|Proteomes:UP000000948}; RN [1] {ECO:0000313|EMBL:BAI00557.1, ECO:0000313|Proteomes:UP000000948} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 3283 / LMG 1513 / CCTM 1153 RC {ECO:0000313|Proteomes:UP000000948}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP011121; BAI00557.1; -; Genomic_DNA. DR RefSeq; WP_014457525.1; NC_013209.1. DR RefSeq; YP_003188936.1; NC_013209.1. DR STRING; 634452.APA01_24490; -. DR EnsemblBacteria; BAI00557; BAI00557; APA01_24490. DR KEGG; apt:APA01_24490; -. DR PATRIC; 20635394; VBIAcePas139226_2529. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; APAS634452:GI0T-2455-MONOMER; -. DR Proteomes; UP000000948; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000948}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000948}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 756 756 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1187 AA; 131110 MW; 00ECD8E9DBE8EBAF CRC64; MLCGVGKAPF PFLLYFMVAM SSRLPLLDAL RDQVLLCDGG MGSRIQMLDL DVQRDYWGQE NCTEILTLSR PELIREIHRG YFEAGADMVE TNTFGGSPIT LGEFSLTDKA REINKNSAIL AREAAESFAD SRTRYVLGSM GPGTKLPSLG NIDYDSLEAA LAEQARGLIE GGVDAILIET CQDTLQIKAA VNGVKIARKE LGTTTPIFVQ VTVETTGTLL VGPDIAAAAT VIHSLDVDLM GLNCATGPQE MAEHVKWLSE NWPRLISVQP NAGLPELVNG QTHYPLTPAE MATWVERFIT EDGLNLIGGC CGTSTPHTEA LDAMLRRRAE GTGRLRPAPV PRTSVWVPSV ASLYSQVPLR QENAYFSIGE RCNANGSKKW RELQEAHDWD GCVTVGREQI REGSNALDIC TAFVGRNERA EMDEVIKRFT SSVNAPLVID STETPVIEAA LKLHGGKPII NSINFEDGEG PASDRMELAR KFGAAVVALT IDEKGMARKP EDKLRIASRL VEFACEKYGL PQSDLMIDPL TFTIATGAED DRKLGQWTLE GIKMIRDAFP DIQIVLGLSN ISFGLNPAAR AVLNSVYLDH AVKAGMTAAI VHVSKIRPLH LIAPEEVKVA EDLIFDRRTE DYDPLQTLLA MFADRKAADA VKRKRAETAE ERLKDRIVDG DRKGLEADLE EAMQNMAPLD IINTVLLDGM KVVGELFGAG KMQLPFVLQS AETMKAAVAY LEPHMERIDG QQRGTIVLAT VKGDVHDIGK NLVDIILTNN GYRVVNLGIK VPVQDMIDAA RKEKADAIGM SGLLVKSTVI MRENLEEISR AGLDTPVLLG GAALTRNYVE EDCVAAYAPT GRVAYARDAF DGLTLMDQIS QKKFDDYLAA IQKRREGKAT RTNARTPETA ETRGFGPVDV AVARARRERL TADEPPMVPP FWGSRVLEAT PEAVLPFLNE RALYQFQWGF RKQGRSLDDF LVWARQELRP ILRRMLDLTA KENILKPQAI YGYWKAAGDG NDLVLFEEDG TTEACRFTLP RQPKVDGECI ADFVRDISEP ERDVIGLQVV TVGQKASDIA RDWFEENRYQ DYLYLHGLSV EMAEAMAEYT HKRIRAELGF AGEDARDMEK LLQQGYRGSR YSFGYPACPR LEDQHPILAL LDAERIGVSL TDGDQLHPEQ STSALVILNK HAKYFTI // ID C7LFP4_BRUMC Unreviewed; 1261 AA. AC C7LFP4; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 01-APR-2015, entry version 45. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:ACU47209.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ACU47209.1}; GN Name=metH {ECO:0000313|EMBL:ACU47209.1}; GN OrderedLocusNames=BMI_I191 {ECO:0000313|EMBL:ACU47209.1}; OS Brucella microti (strain CCM 4915). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=568815 {ECO:0000313|EMBL:ACU47209.1, ECO:0000313|Proteomes:UP000002188}; RN [1] {ECO:0000313|EMBL:ACU47209.1, ECO:0000313|Proteomes:UP000002188} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCM 4915 {ECO:0000313|EMBL:ACU47209.1, RC ECO:0000313|Proteomes:UP000002188}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001578; ACU47209.1; -; Genomic_DNA. DR RefSeq; WP_012783841.1; NC_013119.1. DR RefSeq; YP_003106158.1; NC_013119.1. DR STRING; 568815.BMI_I191; -. DR EnsemblBacteria; ACU47209; ACU47209; BMI_I191. DR KEGG; bmr:BMI_I191; -. DR PATRIC; 17805350; VBIBruMic92249_1402. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; BMIC568815:GJUE-191-MONOMER; -. DR PRO; PR:C7LFP4; -. DR Proteomes; UP000002188; Chromosome 1. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002188}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACU47209.1}; KW Transferase {ECO:0000313|EMBL:ACU47209.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 263 263 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 326 326 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 327 327 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 783 783 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1261 AA; 138662 MW; A4C5F997A553F534 CRC64; MASSLDDLFG ATAAKPDGSE VLAALTQAAR ERILILDGAM GTQIQGLGFH EEHFRGDRFA TCDCQLQGNN DLLTLTQPKA IEEIHYAYAM AGADILETNT FSSTSIAQAD YGMEAMVYDL NRDGARLARR AALRAEQKDG RRRFVAGALG PTNRTASLSP DVNNPGFRAV TFDDLRIAYS EQIRGLIDGG SDIILIETIF DTLNAKAAVF ATEEVFAEKG VRLPVMISGT ITDLSGRTLS GQTPTAFWYS LRHARPFTIG LNCALGANAM RAHLDELSGI ADTFICAYPN AGLPNEFGQY DETPEAMAAQ IEGFARDGLV NVVGGCCGST PDHIRAIAQA VAKYEPRKPA KVPPLMRLSG LEPFTLTKDI PFVNIGERTN VTGSARFRKL VKAGDFAAAL DVARDQVANG AQIIDINMDE GLIDSEKAMV EFLNLIAAEP DIARVPIMLD SSKWEVIEAG LKCVQGKAVV NSISLKEGEE AFLHHARLVR AYGAAVVIMA FDETGQADTQ ARKIEICTRA YKILTEQVGF PPEDIIFDPN IFAVATGIEE HNNYGVDFIE ATREIVRTLP HVHISGGVSN LSFSFRGNEP VREAMHAVFL YHAIQAGMDM GIVNAGQLAV YDTIDAELRE ACEDVVLNRP TKTGESATER LLEIAERFRD SGSREARTQD LSWREWPVEK RLEHALVNGI TEYIEADTEE ARLAAERPLH VIEGPLMAGM NVVGDLFGSG KMFLPQVVKS ARVMKQAVAV LLPFMEEEKR LNGGEGRQSA GKVLMATVKG DVHDIGKNIV GVVLACNNYE IIDLGVMVPS QKILQVARDE KVDIIGLSGL ITPSLDEMAH VAAEMEREGF DIPLLIGGAT TSRVHTAVKI HPRYERGQAV YVVDASRAVG VVSNLLSPEG KQAYIDGLRN EYAKVAAAHA RNEAEKQRLP IARARANPHQ LDWENYEPVK PAFTGTKVFE TYDLAEIARY IDWTPFFQTW ELRGRYPAIL EDEKQGEAAR QLWADAQAML RKIIDEKWFT PRAVVGFWPA NAVGDDIRLF TDESRKEELA TLFTLRQQLT KRDGRPNVAM ADFVAPVESG KQDYVGGFVV TAGIGEIAIA ERFERANDDY SAILVKALAD RFAEAFAELM HERVRKEFWA YAPDEAFTPE ELISEPYKGI RPAPGYPAQP DHTEKTTLFR LLDATANTGV ELTESYAMWP GSSVSGLYIG HPESYYFGVA KVERDQVEDY ARRKDMDVEA VERWLTPILN YVPGASKDEA A // ID C7LWR6_DESBD Unreviewed; 803 AA. AC C7LWR6; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 29-APR-2015, entry version 34. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACU89949.1}; GN OrderedLocusNames=Dbac_1858 {ECO:0000313|EMBL:ACU89949.1}; OS Desulfomicrobium baculatum (strain DSM 4028 / VKM B-1378) OS (Desulfovibrio baculatus). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfomicrobiaceae; Desulfomicrobium. OX NCBI_TaxID=525897 {ECO:0000313|EMBL:ACU89949.1, ECO:0000313|Proteomes:UP000002216}; RN [1] {ECO:0000313|EMBL:ACU89949.1, ECO:0000313|Proteomes:UP000002216} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 4028 / VKM B-1378 {ECO:0000313|Proteomes:UP000002216}; 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 ----------------------------------------------------------------------- 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; ACU89949.1; -; Genomic_DNA. DR RefSeq; WP_015774040.1; NC_013173.1. DR RefSeq; YP_003158365.1; NC_013173.1. DR STRING; 525897.Dbac_1858; -. DR EnsemblBacteria; ACU89949; ACU89949; Dbac_1858. DR KEGG; dba:Dbac_1858; -. DR PATRIC; 21706074; VBIDesBac69216_1874. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; DBAC525897:GI50-1900-MONOMER; -. DR Proteomes; UP000002216; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002216}; KW Methyltransferase {ECO:0000313|EMBL:ACU89949.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002216}; KW Transferase {ECO:0000313|EMBL:ACU89949.1}. SQ SEQUENCE 803 AA; 85173 MW; 4C601DACCCC46A15 CRC64; MRDFRQTLKG GNVLIFDGGM GSLLQRRGLQ AGQSPEEFGM GRPDVVASIH AEYARSGANV VTTNTFGATR YKLPQGFDVF EVNETMTRAA RQAVGDAVFV AGSVGPTGKM IKPLGDISFR GLVDVFKEQI RGLAAGGADL ILGETHFDLA EARAVVVAAR EVCDLPVGIS MTFEGGVSLT GTTPEVFAQT MENMGVDLIA SNCSAGPEQL IEVAKAMLRV SRTPVLIEPN AGLPELVDGA TVFRLPPDPF AATVSTLVDV GVSCLGGCCG TTPEHIKALT ALCAGKTVRR QEISAPPCLI VTSRSQAVEF GFDRPCRIIG ERINPTGKAE LTAELQRLET RRLMTYAEEQ VARGADLLDV NVGAPMVEEA RMLPLAVQAL TSAHAIPLCL DSSDISAIRA GLEAYPGSAL VNSISGEEER METLGPLCRD YGAPFILLPL KGRKLPVTAA ERLAIIEELL IKAESLRIPR RLILVDALAL TVSSKPEAAK ACLEVIRHCR ERWGLGSTMG LSNISFGLPA RDLINSTFLA MAMGVGMTSF IANPNAARIR ENLAAAEVLL GRDSQAAGFI ASYAGWNPGN PVAAVASTAV DEDGSPVAVA VIKGQKDRIV DLLRERIAAG EDPFVLVDGE MIPAIAKVGE KYEKKEYFLP QLLLCAETMQ IGFESIKHLL VREGQEAKAT IVMATVEGDI HDIGKNIVCL MLKNFGYDVV DLGKDVAAAD IVAAAMAHKA SVIGLSALMT TTMVRMEDTV RLVREQGLAC RVMIGGAVVS QSYADLIGAD GYADDAVAAV RVATRLCAEV RSA // ID C7LX76_DESBD Unreviewed; 599 AA. AC C7LX76; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 27-MAY-2015, entry version 42. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=Dbac_0626 {ECO:0000313|EMBL:ACU88749.1}; OS Desulfomicrobium baculatum (strain DSM 4028 / VKM B-1378) OS (Desulfovibrio baculatus). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfomicrobiaceae; Desulfomicrobium. OX NCBI_TaxID=525897 {ECO:0000313|EMBL:ACU88749.1, ECO:0000313|Proteomes:UP000002216}; RN [1] {ECO:0000313|EMBL:ACU88749.1, ECO:0000313|Proteomes:UP000002216} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 4028 / VKM B-1378 {ECO:0000313|Proteomes:UP000002216}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {ECO:0000256|RuleBase:RU004255}. CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ACU88749.1; -; Genomic_DNA. DR RefSeq; WP_015772849.1; NC_013173.1. DR RefSeq; YP_003157165.1; NC_013173.1. DR ProteinModelPortal; C7LX76; -. DR STRING; 525897.Dbac_0626; -. DR EnsemblBacteria; ACU88749; ACU88749; Dbac_0626. DR KEGG; dba:Dbac_0626; -. DR PATRIC; 21703594; VBIDesBac69216_0651. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; DBAC525897:GI50-648-MONOMER; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000002216; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004255}; KW Complete proteome {ECO:0000313|Proteomes:UP000002216}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ACU88749.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000002216}; KW Transferase {ECO:0000313|EMBL:ACU88749.1}. SQ SEQUENCE 599 AA; 63900 MW; 7C15446612ED0867 CRC64; MKKHIMTVLG ERVVVADGAM GSLLFDRGVD SSSCYDALNL TEPALVQSIH KAYADAGAEI LETNTFGANR VKLGRYDLAH TTREINLRGA ELARGEAGAG RWVAGAMGPL GRMGLDAVSQ EEMEDVFSQQ ALALVEGGVD FIMLETFASL SLLLTALRGV KACVSVPVAA QMVFTQRGRT HSGHTARECF DALIRAGADV VGLNCGIGPK NALEVVQGLG PVTVPLSVLP NAGFPESSGD RLIYASSPEY FARRTAACAT YGARLLGGCC GTAPEHIAAL VRALDAGSPE ARIISVSPDE IKTQTAAPTR LSRRLGEGKV ILVELDPPKH LDVEPVLAAA EALSAAGVDA ITIAENPLAV PRLSNIVLAG MVRARTGVDV VVHMTGRDRN LVGMQSTIMG LAASKLHNVL AVTGDPPSAG SAERVSGVYD LRSLELMELL AGFNQGRNHY GDSMRLPVNF CIGGAFNPNT RNMALQVGRM EKKMAAGASY FLTQPVYSRA RVDEILAATR HIKAPIVLGI MPLASSRNAE FLHNEFPGIE IPLETRERMA RAGDHGQEEG VDIAWELLEY AWSHFAGVYI IPPFNRHGMA LELMRRLGR // ID C7LY65_ACIFD Unreviewed; 1151 AA. AC C7LY65; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 29-APR-2015, entry version 49. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACU53673.1}; GN OrderedLocusNames=Afer_0723 {ECO:0000313|EMBL:ACU53673.1}; 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 {ECO:0000313|EMBL:ACU53673.1, ECO:0000313|Proteomes:UP000000771}; RN [1] {ECO:0000313|EMBL:ACU53673.1, ECO:0000313|Proteomes:UP000000771} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 10331 / JCM 15462 / NBRC 103882 / ICP RC {ECO:0000313|Proteomes:UP000000771}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001631; ACU53673.1; -; Genomic_DNA. DR RefSeq; WP_015798162.1; NC_013124.1. DR RefSeq; YP_003109346.1; NC_013124.1. DR ProteinModelPortal; C7LY65; -. DR STRING; 525909.Afer_0723; -. DR EnsemblBacteria; ACU53673; ACU53673; Afer_0723. DR KEGG; afo:Afer_0723; -. DR PATRIC; 20641101; VBIAciFer34262_0759. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; AFER525909:GHMR-733-MONOMER; -. DR Proteomes; UP000000771; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000771}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000771}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 224 224 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 731 731 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1151 AA; 125893 MW; 177A9EDF4689CCA3 CRC64; MRTYEELLRE RVVVFDGAMG TNLQLAGLGA DDFGGPALEG CNEILVVTRP EAVAAVHDSF LAVGVDVVET DTFGALAPVL AEYGIAERAY ELNLRAAQLA RDVASGYATP DHPRFVAGSM GPGTKLPSLG QIPFEDLRDA YEVQAEGLIA GGVDLLLVET VYDLLSAKAA VIGARRAMRR LGRSVPVQVQ VTIETTGRML PGTEVGAALA ALERLDPVAI GINCATGPEE MGEHLRYLSE HQRVPISCLP NAGMPHVVDG HMHYDLTPDA LAAAHRRFVD ELGVGIVGGC CGTRPEHLRA VVEAVGEAVP RERHPTPRAQ VASLYQAVEL RQDLAITAVG ERTNANGSRR FRDAMLARDW DTCVRMAQDQ VRDGAHMIDL CVDYTGEDGT VAMEELSSRL ATASTLPIMI DSTEAAVVET ALRHLGGRPI INSVNLEEGE GSNTRFDSFL RLAKDYGAAV VATCIDEEGQ ARTAARKVEI AKRIVALAVE RYGLATDDII IDPLVLPVTT GMEESRRDAL ETIEALRRIT AEMPGVSTLV GLSNVSFGIN AAAREALNSV FLAECQAAGL SMAILHPSRI QPLARIPEDV RAICLDLIYD RRGQGDPLAR LIERFADVQA VAVTGEELEA LSVPERLHRR IVDANRQGLE DDLAAALGEG MSALGVINDV LLPAMAEVGD LFGSGQMQLP FVLASAETMK QAVAWLEPYL DRASVNDRGT VVLATVQGDV HDIGKNLVDI ILTNNGYRVV NLGIKVALSE MLAAAEEHHA DAIGMSGLLV KSTLVMRDNL VEMNERGMAH LPVILGGAAL TRTFVERDLR QVYDGRVFYG KDAFEGLDVL ERLGRIRRGE LDDPEFGRSI RQSSTRTPRL LRRSTSERTE RSPTVAMDNP IFRPPFLGTR VVKGIALDDI AAYVNETALF RHQWGYRPEG DEDDAAFKQR LRAELRRQLD RALVDQSLVP QVVYGYFVAA SEGNDLVVFA DEAREHELAR FRFPRQEQEP YLCIADFFRP LAGPEIDYVA FHVVTMGPRI TEVAKRAFDE NRYQEYLLLH GLGVELTEAL AEYWHARIRA EWGFGDEDGP TLAGLFRQQY RGSRYSWGYP ACPDLEDNRT VVDLLDAGRI GVSVSDTFQL EPEQTTTAII VHHPQAKYFV A // ID C7MMT6_CRYCD Unreviewed; 298 AA. AC C7MMT6; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 27-MAY-2015, entry version 31. DE SubName: Full=Cobalamin-dependent methionine synthase I {ECO:0000313|EMBL:ACU94226.1}; GN OrderedLocusNames=Ccur_05050 {ECO:0000313|EMBL:ACU94226.1}; OS Cryptobacterium curtum (strain ATCC 700683 / DSM 15641 / 12-3). OC Bacteria; Actinobacteria; Coriobacteridae; Coriobacteriales; OC Coriobacterineae; Coriobacteriaceae; Cryptobacterium. OX NCBI_TaxID=469378 {ECO:0000313|EMBL:ACU94226.1, ECO:0000313|Proteomes:UP000000954}; RN [1] {ECO:0000313|EMBL:ACU94226.1, ECO:0000313|Proteomes:UP000000954} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700683 / DSM 15641 / 12-3 RC {ECO:0000313|Proteomes:UP000000954}; 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 ----------------------------------------------------------------------- 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; ACU94226.1; -; Genomic_DNA. DR RefSeq; WP_012802914.1; NC_013170.1. DR RefSeq; YP_003150908.1; NC_013170.1. DR STRING; 469378.Ccur_05050; -. DR EnsemblBacteria; ACU94226; ACU94226; Ccur_05050. DR KEGG; ccu:Ccur_05050; -. DR PATRIC; 21524823; VBICryCur116861_0487. DR eggNOG; NOG310274; -. DR HOGENOM; HOG000102398; -. DR KO; K00548; -. DR OMA; EIGPCGL; -. DR OrthoDB; EOG64FKJ0; -. DR BioCyc; CCUR469378:GH4Z-507-MONOMER; -. DR Proteomes; UP000000954; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000954}; KW Reference proteome {ECO:0000313|Proteomes:UP000000954}. SQ SEQUENCE 298 AA; 30824 MW; 930C696C919B8C92 CRC64; MPDIQMRFHH DMLTLSSPLE STLIAQGFDL SFGVSLLSVL EPEAVSAALR LQVAAGAPCL VAPTAGVTHA RLAHQRAADR DINIAQAAKS LATAFTTQHV LAEIGATGLP IDPNSKSSLT ANRDEYLRAA RAIGDADIDA FFVNGLTGAA DARCALMGVR QVFATPLIAS VDVNEEGIAN DGTGLEDIVA VMADLEADVV GFCTSADSEG AARLAQRAAH ACDRPLLVQL NVQKQPSSTL FSHARGQLDI PYADPSSMVQ AADCLRAAGA QFIRAVGAAT PAYAGALAAA LAGTEPIR // ID C7MR94_SACVD Unreviewed; 295 AA. AC C7MR94; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 27-MAY-2015, entry version 32. DE SubName: Full=Homocysteine/selenocysteine methylase (S-methylmethionine-dependent) {ECO:0000313|EMBL:ACU98680.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ACU98680.1}; GN OrderedLocusNames=Svir_37350 {ECO:0000313|EMBL:ACU98680.1}; 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 {ECO:0000313|EMBL:ACU98680.1, ECO:0000313|Proteomes:UP000000841}; RN [1] {ECO:0000313|EMBL:ACU98680.1, ECO:0000313|Proteomes:UP000000841} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15386 / DSM 43017 / JCM 3036 / NBRC 12207 / P101 RC {ECO:0000313|Proteomes:UP000000841}; RX PubMed=21304650; 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., Goker 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 ----------------------------------------------------------------------- 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; ACU98680.1; -; Genomic_DNA. DR RefSeq; WP_015787989.1; NC_013159.1. DR RefSeq; YP_003135507.1; NC_013159.1. DR STRING; 471857.Svir_37350; -. DR EnsemblBacteria; ACU98680; ACU98680; Svir_37350. DR KEGG; svi:Svir_37350; -. DR PATRIC; 23398066; VBISacVir111818_3798. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; SVIR471857:GHAV-3719-MONOMER; -. DR Proteomes; UP000000841; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000841}; KW Methyltransferase {ECO:0000313|EMBL:ACU98680.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000841}; KW Transferase {ECO:0000313|EMBL:ACU98680.1}. SQ SEQUENCE 295 AA; 31667 MW; A3C5EB177513197C CRC64; MIPFDGSAPL VSDGGLATEL EARGHDLGDA LWSARLLLDA PDEIVAVHRA FYEAGAVIAT TASYQASFSG FAERGIDRDT ATTLLRRSVE LARRARDEAP DDGRRRFVAA SVGPYGAALA DGSEYRGRYG LSVARLRRWH RPRLEVLAET SPDILALETV PDIDEAEALV EAVAGLGVPA WLTYTVDGER TRAGQPLTEA FAVAQSSPDI VAVGVNCCTP DDVSTALALA REVTTKPLVV YPNSGENWDP VRRTWWGPSR YSPELARRWT AEGAHVVGGC CRVGPADIAR VADVL // ID C7MUL0_SACVD Unreviewed; 1184 AA. AC C7MUL0; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 29-APR-2015, entry version 48. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ACU97686.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ACU97686.1}; GN OrderedLocusNames=Svir_27020 {ECO:0000313|EMBL:ACU97686.1}; 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 {ECO:0000313|EMBL:ACU97686.1, ECO:0000313|Proteomes:UP000000841}; RN [1] {ECO:0000313|EMBL:ACU97686.1, ECO:0000313|Proteomes:UP000000841} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15386 / DSM 43017 / JCM 3036 / NBRC 12207 / P101 RC {ECO:0000313|Proteomes:UP000000841}; RX PubMed=21304650; 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., Goker 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001683; ACU97686.1; -; Genomic_DNA. DR RefSeq; WP_015786998.1; NC_013159.1. DR RefSeq; YP_003134513.1; NC_013159.1. DR STRING; 471857.Svir_27020; -. DR EnsemblBacteria; ACU97686; ACU97686; Svir_27020. DR KEGG; svi:Svir_27020; -. DR PATRIC; 23395914; VBISacVir111818_2738. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SVIR471857:GHAV-2689-MONOMER; -. DR Proteomes; UP000000841; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000841}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACU97686.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000841}; KW Transferase {ECO:0000313|EMBL:ACU97686.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 225 225 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 292 292 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 735 735 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1184 AA; 130313 MW; 6BDB10084752EE65 CRC64; MTMDSRFLTE LDRRVLVADG GMGTALQGFD LTLDDFAQLE GCNEVLNDTR PDVVTAVYRS FLEAGSDAIE TNTFGTNYGN FGEYGILDRI RELAEKGTVL ARQCADEYST PDRPRFVLGS MGPGTKLPTL GHAPYAVLRD AYVENALGML DGGVDAVLVE TSQDLLQAKA AIVGAKRAMA RAGRRVPIIA QVTVEQTGTM LVGSEIGAAL TALEPLGIDL IGMNCATGPA EMSEHLRVLS EHARVPISVM PNAGLPELGP DGAVYPLRPD ELAEALATFV TEFGVRLVGG CCGTTPEHVR AVVEAVSSLR PKERRPEHTP AVSSVYQSVP FKQDASILNV GERTNANGSK AFRQAMLEGR YDDCVEIAKA QTREGAHVLD LCVDYVGRDG TTDMAELASR LATASTLPIM VDSTEPEVVR TGLEHFGGRC AINSVNYEDG TGPDSRYRRV LELAVEHGAA VVVTCIDEEG QARTAEWKLR VAERAISDLT TNWGLDKSSI IIDCLVFPIT TGQEEVRKDA LETINAIRQL KRRHPDVMTT LGLSNVSFGL NPAARQVLNS VFLHECREAG LDSAILNSSK ILPMNKIEDE PRQVALDLVY DRRRDGYDPL QRLMQLFEGK TASSARASRA EELAKLPLFE RLEKRIVEGE TTGLEEDLDA AMREKKPIDI INEHLLAGMK VVGDLFGSGQ MQLPFVLQSA ETMKAAVAYL EPHMEKTDAD GKGKLLLATV KGDVHDIGKN LVDIIVSNNG YDVVNIGIKQ PINAILEAAE EHQVDAIGMS GLLVKSTVVM KENLQEMNAR GVATKYPVLL GGAALTRTYV ENDLDEIYEG DVRYAKDAFE GLKLMDRIMA VKRGETPEED AAEEAKKAER KARRERSLRI AEKRRAEQGP EPDLYDTTRS DVDPDVPVPV PPFWGAKVVK GVAVADYLSL LDERATFFGQ WGLRGARKGE GPSYEELVES EGRPRLRAWI DELSTQGILA HAALVYGYFP CYSEGNDLVV LEKDEPDALE RLRFTFPRQR RDRRLCLADF FRSKEKAEQT GQVDVLPMQL VTMGQPIADY ANELFARNAY RDYLEVHGLG VQLTEALAEY WHRRIRQELR FPSGAPVAAE DPEDVQQFFR LGYRGARFSF GYGACPDLED RAKIVELLDA GRIGVTLSEE FQLHPEQSTD AIVAHHPEAK YFNT // ID C7N1R7_SLAHD Unreviewed; 820 AA. AC C7N1R7; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 27-MAY-2015, entry version 39. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ACV23358.1}; GN OrderedLocusNames=Shel_23490 {ECO:0000313|EMBL:ACV23358.1}; OS Slackia heliotrinireducens (strain ATCC 29202 / DSM 20476 / NCTC 11029 OS / RHS 1) (Peptococcus heliotrinreducens). OC Bacteria; Actinobacteria; Coriobacteridae; Coriobacteriales; OC Coriobacterineae; Coriobacteriaceae; Slackia. OX NCBI_TaxID=471855 {ECO:0000313|EMBL:ACV23358.1, ECO:0000313|Proteomes:UP000002026}; RN [1] {ECO:0000313|EMBL:ACV23358.1, ECO:0000313|Proteomes:UP000002026} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29202 / DSM 20476 / NCTC 11029 / RHS 1 RC {ECO:0000313|Proteomes:UP000002026}; RX PubMed=21304663; DOI=10.4056/sigs.37633; RA Pukall R., Lapidus A., Nolan M., Copeland A., Glavina Del Rio T., RA Lucas S., Chen F., Tice H., Cheng J.F., Chertkov O., Bruce D., RA Goodwin L., Kuske C., Brettin T., Detter J.C., Han C., Pitluck S., RA Pati A., Mavrommatis K., Ivanova N., Ovchinnikova G., Chen A., RA Palaniappan K., Schneider S., Rohde M., Chain P., D'haeseleer P., RA Goker M., Bristow J., Eisen J.A., Markowitz V., Kyrpides N.C., RA Klenk H.P., Hugenholtz P.; RT "Complete genome sequence of Slackia heliotrinireducens type strain RT (RHS 1)."; RL Stand. Genomic Sci. 1:234-241(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; CP001684; ACV23358.1; -; Genomic_DNA. DR RefSeq; WP_012799458.1; NC_013165.1. DR RefSeq; YP_003144707.1; NC_013165.1. DR STRING; 471855.Shel_23490; -. DR EnsemblBacteria; ACV23358; ACV23358; Shel_23490. DR KEGG; shi:Shel_23490; -. DR PATRIC; 23644284; VBISlaHel66389_2326. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SHEL471855:GH2I-2350-MONOMER; -. DR Proteomes; UP000002026; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002026}; KW Reference proteome {ECO:0000313|Proteomes:UP000002026}. SQ SEQUENCE 820 AA; 86225 MW; CAE083C8146A4B2F CRC64; MLAITDGIAK VRNRDQVRTK DEYLAAVLRG EAYLVFDGAM GTMLQASGME AGELPELLCL TDPAGVTAIH RQYVEAGSQA ITTNTFGANA RKLGDAATVE DVFAAAVACA RESGARYVAG DIGPTGGLLE PLGTMSFDEA YDLFAQEVRA ADAAGADLLV IETMADLLEM KAAVLAAKEN SDLPIFATMT FGEDGRTFLG TSPQIAALTL DALGVNVLGV NCSLGPSDLQ PIVSAMLETA TCPVMAQANA GLPSVVDGHT VYSIMPDEYA NAVQAMVDEG VSVIGGCCGT NPDYIRQLAA MVEGKRPPHR EVETPFSLTS AQNAVVLRGR EVAVIGERIN PTGKKRLKEA LRTKDYNYVL NEAISQTEAG ADVLDVNAGL PEIDEAATLV TLVGQIQGVS GLPLQIDSAD PAAVEAAVRV YSGKPLINSV NGKQESLDAV LPVAKHYGCA VVGLTLDENG IPPTGEERFA IAARIVEAAE AYGIPRSHVA IDCLVMAAST NQQEVVEILK GVTLVKERLG VRTVLGVSNV SFGLPLREIV NATFLSAAFA AGLDMPILNP MATRYKEVVD TWRVLCAQDE GAAGYIAEYA GKTLDAGAVA QAPAAEGAPG SSAEDDGSIR HLIITGRKGD MVQATQALLA DHDAMEVINE HLIPALDEVG ALFEKGTFFL PQLMASAEAA KAGFDVIRSN ASEGDVDEKG SVAVATVKGD IHDIGKNIVR MLLENYGYRV YDLGRDVDPE LIVQTVQEHD IKLVGLSALM TTTVHNMEEA IKLLREKAPD VKVMVGGAVL NPEYARMVGA DFYAKDAAES ARIAGEVLGS // ID C7N6G5_SLAHD Unreviewed; 296 AA. AC C7N6G5; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 29-APR-2015, entry version 32. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ACV22500.1}; GN OrderedLocusNames=Shel_14800 {ECO:0000313|EMBL:ACV22500.1}; OS Slackia heliotrinireducens (strain ATCC 29202 / DSM 20476 / NCTC 11029 OS / RHS 1) (Peptococcus heliotrinreducens). OC Bacteria; Actinobacteria; Coriobacteridae; Coriobacteriales; OC Coriobacterineae; Coriobacteriaceae; Slackia. OX NCBI_TaxID=471855 {ECO:0000313|EMBL:ACV22500.1, ECO:0000313|Proteomes:UP000002026}; RN [1] {ECO:0000313|EMBL:ACV22500.1, ECO:0000313|Proteomes:UP000002026} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29202 / DSM 20476 / NCTC 11029 / RHS 1 RC {ECO:0000313|Proteomes:UP000002026}; RX PubMed=21304663; DOI=10.4056/sigs.37633; RA Pukall R., Lapidus A., Nolan M., Copeland A., Glavina Del Rio T., RA Lucas S., Chen F., Tice H., Cheng J.F., Chertkov O., Bruce D., RA Goodwin L., Kuske C., Brettin T., Detter J.C., Han C., Pitluck S., RA Pati A., Mavrommatis K., Ivanova N., Ovchinnikova G., Chen A., RA Palaniappan K., Schneider S., Rohde M., Chain P., D'haeseleer P., RA Goker M., Bristow J., Eisen J.A., Markowitz V., Kyrpides N.C., RA Klenk H.P., Hugenholtz P.; RT "Complete genome sequence of Slackia heliotrinireducens type strain RT (RHS 1)."; RL Stand. Genomic Sci. 1:234-241(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; CP001684; ACV22500.1; -; Genomic_DNA. DR RefSeq; WP_012798602.1; NC_013165.1. DR RefSeq; YP_003143849.1; NC_013165.1. DR STRING; 471855.Shel_14800; -. DR EnsemblBacteria; ACV22500; ACV22500; Shel_14800. DR KEGG; shi:Shel_14800; -. DR PATRIC; 23642550; VBISlaHel66389_1463. DR eggNOG; NOG310274; -. DR HOGENOM; HOG000102398; -. DR KO; K00548; -. DR OMA; EIGPCGL; -. DR OrthoDB; EOG64FKJ0; -. DR BioCyc; SHEL471855:GH2I-1482-MONOMER; -. DR Proteomes; UP000002026; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002026}; KW Reference proteome {ECO:0000313|Proteomes:UP000002026}. SQ SEQUENCE 296 AA; 31467 MW; C2BC5076FBBCAD9B CRC64; MADIQLRFHK DMLVMSAPID YALTRQGVDL DNDAEFVSLF EGDTVHDALS MEQLAGAACL VTNTEGICKA RLAHKRMELH AQEIADSAIE AAQECTPQHI VFEIGPCGLP LDPESGASRK QSRKQYADAA SLVAGAEIDG VFLNGMRTAA DMQCAIAGVR DATDMPLFAS VTLDADGFFD GMPAHEAVSC MEGADVVGIR TAADTDAVAA IVAKMAQEID KPILVQVEIK QATEAEKRRA TLGPLPDNPY PTPDHLAQAA VQYFKAGAQF LRAVGEATPA YTGALAAVCY GLDARR // ID C7NB07_LEPBD Unreviewed; 1169 AA. AC C7NB07; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 27-MAY-2015, entry version 48. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACV39338.1}; GN OrderedLocusNames=Lebu_1463 {ECO:0000313|EMBL:ACV39338.1}; OS Leptotrichia buccalis (strain ATCC 14201 / DSM 1135 / JCM 12969 / NCTC OS 10249). OC Bacteria; Fusobacteria; Fusobacteriales; Leptotrichiaceae; OC Leptotrichia. OX NCBI_TaxID=523794 {ECO:0000313|EMBL:ACV39338.1, ECO:0000313|Proteomes:UP000001910}; RN [1] {ECO:0000313|EMBL:ACV39338.1, ECO:0000313|Proteomes:UP000001910} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14201 / DSM 1135 / JCM 12969 / NCTC 10249 RC {ECO:0000313|Proteomes:UP000001910}; RX PubMed=21304648; DOI=10.4056/sigs.1854; RA Ivanova N., Gronow S., Lapidus A., Copeland A., Glavina Del Rio T., RA Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E., RA Bruce D., Goodwin L., Brettin T., Detter J.C., Han C., Pitluck S., RA Mikhailova N., Pati A., Mavrommatis K., Chen A., Palaniappan K., RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Rohde C., RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Leptotrichia buccalis type strain (C- RT 1013-b)."; RL Stand. Genomic Sci. 1:126-132(2009). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001685; ACV39338.1; -; Genomic_DNA. DR RefSeq; WP_015769679.1; NC_013192.1. DR RefSeq; YP_003164329.1; NC_013192.1. DR STRING; 523794.Lebu_1463; -. DR EnsemblBacteria; ACV39338; ACV39338; Lebu_1463. DR KEGG; lba:Lebu_1463; -. DR PATRIC; 22402249; VBILepBuc70646_1483. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; LBUC523794:GHCR-1490-MONOMER; -. DR Proteomes; UP000001910; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001910}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001910}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 237 237 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 301 301 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 733 733 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1169 AA; 131585 MW; 72CD07076554DF6B CRC64; MQKNLYKNSY NLLQNDLKNK ILLLDGAMGT MIQQENLTAD DFGGEKYEGC NDYLVLQRPD VIKNIHKKYL EAGSDIIETN SFGALDIVLK DYDLEDTVFE MNKKAAELVN EAIAEYRSEH PEVTRNLYVA GALGPSNKSI SVTGGVTFEE LIHTYYTAVS GLMAGGVDLI LFETIQDTRN LKAAYLGLKK AMEENYTVPL MLSFTIESTG TTLAGQTADA FYYAVNHMNP FSVGLNCATG PEFMTQFLKT LNNISNTYIS VYPNAGLPNE DGEYEETPDT LSAKIEPFFQ NNYLNIVGGC CGTTPEHIQK IKEKSINYSP RVIDENKDFN DVSGLITLET PKDRPIYVGE RTNVIGSRIF KNLIASEKFD EATEVARLQI KGRADVIDIC LANPDRDEIA DMKAFLDKVA KFAKVPLMID STDINVVKEG LTYLQGKGII NSINLEDGEK KFTDMAKVIK DFGASVVVGL IDEEGMAVSV ERKLEIARRS YELLTKKYGI DERDIIFDTL VFPVATGDQK YIGSATATIE AIRQIKDEMP NVKTILGVSN ISFGLPIAGR EVLNTYYMQK AYEAGLDYAI VNTEKVIPMS EISDEEKELS ENILFHTDDE NVSKFANFYR EKKAIQKVVD TSNMTMEERV ANLVVEGSKK DLKICLDELL KKYSPIEIIN GPLMDGMDEV GRLFNNNDLI VAEVLQSAEV MKASVSHLEQ FMEKDESSVK GTVIMATVKG DVHDIGKNLV GIIIGNNGYK VIDLGINTPA EKIREAIIEH KADFLGLSGL LVKSATEMVN TMEVLHEAGI DIPIFVGGAA LTEKFTVNKI EPAYKNNIVI YSRDAMTALA DLNKMIDEIK FREFKEYLQK RRELVTIKDA KKLEQLKVKP TVSDIKDADG TFDFSKVELP KYDFEKIYKP QTLNKQIITN IKAKDVFPFI NLQMLIGKHL GMKWIVNNLI EKQDPRTIKL YNEILDIIEN GDEYFDIKAI YKFFPVRRKA GEKKEDFKIE VLSDDLSTVL ETFDFPRQKY GQYLSLNDYV NPDGIDYIGF FVATAGEKSR LVSNELKEKG EFYRGHIVNS VGLELAEAAS EYIHKMMRQD VGIIDKDISL NEILNAQYQG NRYSFGYPAC PDLSDQRKLF NLLKPERYGI SLTEEFMMYP EATVSAIVFS QPFCKYFNM // ID C7PK49_CHIPD Unreviewed; 339 AA. AC C7PK49; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 27-MAY-2015, entry version 35. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACU58390.1}; GN OrderedLocusNames=Cpin_0892 {ECO:0000313|EMBL:ACU58390.1}; 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 {ECO:0000313|EMBL:ACU58390.1, ECO:0000313|Proteomes:UP000002215}; RN [1] {ECO:0000313|Proteomes:UP000002215} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43595 / DSM 2588 / NCIB 11800 / UQM 2034 RC {ECO:0000313|Proteomes:UP000002215}; 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; ACU58390.1; -; Genomic_DNA. DR RefSeq; WP_012788566.1; NC_013132.1. DR RefSeq; YP_003120591.1; NC_013132.1. DR STRING; 485918.Cpin_0892; -. DR EnsemblBacteria; ACU58390; ACU58390; Cpin_0892. DR KEGG; cpi:Cpin_0892; -. DR PATRIC; 21350407; VBIChiPin99107_0882. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; CPIN485918:GHYR-909-MONOMER; -. DR Proteomes; UP000002215; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002215}; KW Methyltransferase {ECO:0000313|EMBL:ACU58390.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002215}; KW Transferase {ECO:0000313|EMBL:ACU58390.1}. SQ SEQUENCE 339 AA; 37144 MW; 608A0C2E507845C7 CRC64; MKKSLSQCAA ERILIIDGAM GTMIQRYKLE EADYRGERFK DYHLDVKGNN DLLCLTQPQI IEAIHKEYLD AGADIIETNT FSSTTIAMAD YDMQSLAFEM NVAAARIAKK AAQEYTAKNP DKPRFVAGAI GPLNKTLSLS PDVNNPGFRS VSFDEVVDAY YEQVKGLHEG GADILLIETI FDTLNSKAAI FAIKKYFSDI AQPELPVMIS GTITDASGRT LSGQTLEAFY ISVMHVKPFS VGLNCALGGE QMRPYISELS QIAACNVSCY PNAGLPNAFG EYDETPDHTA HIIEDFAKEG YVNIVGGCCG TTPDHIRHIA EHVKTVSPRR LPEMVDTLA // ID C7Q855_CATAD Unreviewed; 1169 AA. AC C7Q855; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 27-MAY-2015, entry version 49. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACU74222.1}; GN OrderedLocusNames=Caci_5363 {ECO:0000313|EMBL:ACU74222.1}; 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 {ECO:0000313|EMBL:ACU74222.1, ECO:0000313|Proteomes:UP000000851}; RN [1] {ECO:0000313|EMBL:ACU74222.1, ECO:0000313|Proteomes:UP000000851} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897 RC {ECO:0000313|Proteomes:UP000000851}; RX PubMed=21304647; 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., Ivanova N., Mavromatis K., Chen A., RA Palaniappan K., Chain 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001700; ACU74222.1; -; Genomic_DNA. DR RefSeq; WP_015793951.1; NC_013131.1. DR RefSeq; YP_003116063.1; NC_013131.1. DR STRING; 479433.Caci_5363; -. DR EnsemblBacteria; ACU74222; ACU74222; Caci_5363. DR KEGG; cai:Caci_5363; -. DR PATRIC; 21289425; VBICatAci36872_5465. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CACI479433:GI6Z-5393-MONOMER; -. DR Proteomes; UP000000851; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000851}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000851}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 237 237 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 747 747 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1169 AA; 127047 MW; 409B52014C2B17CA CRC64; MASTAAPSAH AGNARIAALR EALRTRVVVA DGAMGTMLQA QNPTLDDFQG HEGCNEILNI SRPDIVQTVH EEYFRAGVDC VETNTFGANH TNLGDYDISD RVFELSEAGA RLAREVADGF ATADKPRWVI GSIGPGTKLP SLGQIGYATL RDAYQAEAAG LIAGGADALL VETSQDLLQI KASVLGAKAA ARAAGIDVPV WASAAFETTG TMLLGTEVGA ALTALESLGI ERIGLNCSTG PAEMSEHLRY LAKHSTIGLS CMPNAGLPVL TSDGAHYPLS PEELVDWHAR FVDQFGIALI GGCCGTTPEH LRQLVESLGG REVPQRDPKR EPGASSLYQH VPFRQDISYL AIGERANTNG SKAFREALLA ENWDACVEIA RNQIRDGAHM LDLCVDYVGR DGVRDMQQVA SRFATASTLP IVLDSTEPQV LQAGLETLGG RAVINSVNYE DGDGPTSRFA RIMELVSAHG AGVIALTIDE QGQARTAEHK VAIAERLIED ITGNWGVPED SILVDCLTFT ICTGQEESRR DGLETIEGIR ELKRRHPDVQ TTLGLSNISF GLNPAARQVL NSVFLHECVE AGLDSAIVHA SKILPIARIP EEQRKTALDL VYDRRAEGYD PLTRLLELFE GVDAASLKAS RADELAALPL NERLKRRIID GERKGLEADL DEALGERPAL EIVNEVLLDG MKTVGELFGS GEMQLPFVLQ SAETMKTAVA HLEPHMEKSD STGKGTIVLA TVKGDVHDIG KNLVDIILSN NGYNVVNLGI KQPLQTILDA AEEHAADAIG MSGLLVKSTV VMKENLEEMN TRGVADRWPV LLGGAALTRA YVEQDLAELY DGEVRYARDA FEGLNLMDAV AAVKAGVPGA SLPALRPRRV KASGPLREIP DEPIPARSDV ALDNPIPAPP FWGDRMVKGI RLAEYAPYLD ERALFLGQWG LKPGRGSGGR SYEELVETEG RPRLRMWLER LQTENLLDAA VVYGYFPAVS KGDSLLILDE SGEQRTSFTF PRQRRDRHLC LSDFWRPQES GEVDVAPFQL VTVGARIAEA TGELFAANSY REYMELHGLS VQLAEALAEY WHARVRDELG YAAEDPESTE GLFKVEYRGC RYSFGYPACP DLEDRTKIVE LLKPERINVQ LSEEYQLHPE QSTDAIVAHH PEASYFNAG // ID C7R4L4_JONDD Unreviewed; 1181 AA. AC C7R4L4; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 29-APR-2015, entry version 49. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACV09071.1}; GN OrderedLocusNames=Jden_1418 {ECO:0000313|EMBL:ACV09071.1}; 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 {ECO:0000313|EMBL:ACV09071.1, ECO:0000313|Proteomes:UP000000628}; RN [1] {ECO:0000313|EMBL:ACV09071.1, ECO:0000313|Proteomes:UP000000628} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14870 / DSM 20603 / CIP 55134 RC {ECO:0000313|Proteomes:UP000000628}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001706; ACV09071.1; -; Genomic_DNA. DR RefSeq; WP_015771699.1; NC_013174.1. DR RefSeq; YP_003161374.1; NC_013174.1. DR STRING; 471856.Jden_1418; -. DR EnsemblBacteria; ACV09071; ACV09071; Jden_1418. DR KEGG; jde:Jden_1418; -. DR PATRIC; 22162989; VBIJonDen9837_1479. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; JDEN471856:GH77-1462-MONOMER; -. DR Proteomes; UP000000628; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000628}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000628}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 228 228 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 745 745 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1181 AA; 128904 MW; 6E945654E66D04FF CRC64; MDTPRASRLR QALTHRVVVA DGAMGTMLQA ASLTLEDFHG LEGCNEILNV TVPDVIESIH DAYFAVGVDC VESNTFGANW SNLSDYEIDD RIYELAYAGA SIARRSADRA ATEQQRDTWV LGSMGPGTKL PSLGHTTYAH LKTTFTQQAL GLLDGGADAF LIETAQDILQ AKAAINACHA AMEERGKRIL IMVSVTVETT GTMLMGSEIG AALTALSALN IDSIGLNCAT GPAEMSEHLR HLSKHAPIPV TCMPNAGLPV LGKNGAEYPL TPTELAAAHR QFVTEFGLGL VGGCCGTTPE HLGAVVAAVR DTSPAKRTVT VENGVASLYS HTDFHQDSSF LAIGERTNAN GSKAFREAML AENWDECVTI ARSQTRDGAH VLDVCVDYVG RDGVADVTNV VSRLASASTL PLVIDSTEPD VIKAALELIG GRPVVNSVNF EDGDGPTSRY ARIMPLVKEH GAAVVALTID EEGQARTRDA KVAIATRLIT DLTTRWGMSV TDIIVDTLTF PIATGQEETR RDAIETIHAI KDITTAFPGI HTTLGVSNVS FGLSPAARHV LNSVFLHEAV AAGLDSAIVH AAKIMPLKNI PDEQREAALD LIWDRRRYDD EGVMIHDPLA HFLNVFSGVD AASLNQSRAE ELAALPLTER LERRIIDGDN KGLTGDLDQA LSQGISALDI INDHLLAGMK VVGDLFGRGE MQLPFVLQSA ETMKAAVAWL EPHMERTESA GKGTMVLATV RGDVHDIGKN LVDIILTNNG YNVINIGIKQ SINAMIEAAE EHNADVIGMS GLLVKSTVVM KENLEELNSR GLARKYPVLL GGAALTRVYV EDDLDEVYDG VVRYARDAFE ALRLMDSLVA IARGANSNDV DLPPLKKRRH NVVTVTQTAE EDLPERSTIA ADNPIPTPPF WGTRVVKGIH LADYAAMLDE RATFMGQWGL KPTRSGDGPS YEELVEHEGR PRLRAWLDRI ATQDIFDPTV LYGYFPVYAE GNDVVLLHHE GPDGGSEGEP LTERMRFTFP RQRRDRHLCL ADFVQSRERF FETGTPDVVA VQLVTIGDKV SEHTARMYAD NQYRDYLELH GLSVQMTEAL AEFWHSRVRE ELGFADEEPD TTDGLFSLEY RGARFSLGYP ACPDMEDRRK IVRLLRARDY GVELSDELQL HPEQSTDAFV FHHPEAKYFS V // ID C7RCM5_KANKD Unreviewed; 1227 AA. AC C7RCM5; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 27-MAY-2015, entry version 47. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACV27017.1}; GN OrderedLocusNames=Kkor_1605 {ECO:0000313|EMBL:ACV27017.1}; OS Kangiella koreensis (strain DSM 16069 / KCTC 12182 / SW-125). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Alcanivoracaceae; Kangiella. OX NCBI_TaxID=523791 {ECO:0000313|EMBL:ACV27017.1, ECO:0000313|Proteomes:UP000001231}; RN [1] {ECO:0000313|EMBL:ACV27017.1, ECO:0000313|Proteomes:UP000001231} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16069 / KCTC 12182 / SW-125 RC {ECO:0000313|Proteomes:UP000001231}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001707; ACV27017.1; -; Genomic_DNA. DR RefSeq; WP_015780623.1; NC_013166.1. DR RefSeq; YP_003146785.1; NC_013166.1. DR STRING; 523791.Kkor_1605; -. DR EnsemblBacteria; ACV27017; ACV27017; Kkor_1605. DR KEGG; kko:Kkor_1605; -. DR PATRIC; 22168644; VBIKanKor123990_1578. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; KKOR523791:GHCO-1643-MONOMER; -. DR Proteomes; UP000001231; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001231}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001231}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 137515 MW; A9DEE17551546C4F CRC64; MNKSKQLQES LKQRILLLDG AMGTMIQQYE LTEADYRGER FADWPSDLKG NNDLLSLSQP QIISDIHKAY LEAGSDIIET NTFNATRVAM ADYGMQDLSA DINRESARLA RAVADQYSTP DKPRFVAGVI GPTNRTCSIS PDVNDPGFRN IYFDELADAY YESTHALIEG GADIILIETV FDTLNAKAAI FAVKKYFDDH QIDYPIMLSG TITDASGRTL TGQTTEAFYN SIRHANPISV GLNCALGPKD LRAYIEELSR ISEFAVSAHP NAGLPNEFGG YDETPDDMSR EMSEWIEKGF INIIGGCCGT TPEHIARFND MIAGAKPRTK FNQEPRCRLS GLEALNLDAK SLFVNVGERT NVTGSAKFLR LIKEDDFETA IEVALEQVEN GAQVIDINMD EGMLDSKAAM QRFLNLIASE PDISRVPIML DSSKWDIIEA GLKCVQGKGI VNSISLKEGE PQFLEQAHLA QRYGAAVIVM AFDEDGQADT FERKTEICRR AYDLLIKELN FDPQDIIFDP NIFAIATGIE EHNNYAVDFI EATRWIKQNL PGARVSGGVS NVSFSFRGNN TVREAIHAVF LYHAIRAGMD MGIVNAGQLE VYSAIPEDLK EAVENVVLNR SPEATEKLLE LAEQYRGSGQ EVKEKETQEW RQWPVNKRLE HSLVKGITEF IDDDVEEARQ QAERPLHVIE GPLMDGMNVV GDLFGSGQMF LPQVVKSARV MKKAVAYLFP YMEEEKKRLK LADKPKGKIV LATVKGDVHD IGKNIVGVVL QCNGYEVINL GVMVACDKIL DTAIEQNCDI VGLSGLITPS LEEMVHVAKE MQRRGLDLPL LIGGATTSKI HTAVKIEPHY EHPAMYVMDA SRVVGVVNKL LGEHKDEFVS EIKAEYHKLR TEREKRQKKS SLASLEKARQ FAANIDWSQA NITKPSFLGT KVFSDYPLED LLPRIDWTPF FRSWQLAGKF PNILDDEIVG ETARKLYADA QTMLKSIVEE QWLTARAVIG FYPANAQGDD IEIYADDSRK TIIHRLHHLR QQKQTRDGKF NYCLSDFIAP KETGLKDYIG GFAVTSGIGI DEHVKAFEAK HDDYNAILLK ALADRLAEAF AERMHELVRK DYWGYVPDEK LDNAELISEQ YQGIRPAPGY PACPDHTEKG TLWTMLKPDA EIELNITEHF AMYPTAAVSG WYFAHPESRY FGVGKIEKDQ VKDYAQRKGW DLELAEKWLA PTLNYDN // ID C7RJK8_ACCPU Unreviewed; 1238 AA. AC C7RJK8; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 27-MAY-2015, entry version 45. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACV33572.1}; GN OrderedLocusNames=CAP2UW1_0214 {ECO:0000313|EMBL:ACV33572.1}; OS Accumulibacter phosphatis (strain UW-1). OC Bacteria; Proteobacteria; Betaproteobacteria; OC Candidatus Accumulibacter. OX NCBI_TaxID=522306 {ECO:0000313|EMBL:ACV33572.1, ECO:0000313|Proteomes:UP000001619}; RN [1] {ECO:0000313|EMBL:ACV33572.1, ECO:0000313|Proteomes:UP000001619} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UW-1 {ECO:0000313|EMBL:ACV33572.1, RC ECO:0000313|Proteomes:UP000001619}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001715; ACV33572.1; -; Genomic_DNA. DR RefSeq; WP_012807023.1; NC_013194.1. DR RefSeq; YP_003165501.1; NC_013194.1. DR ProteinModelPortal; C7RJK8; -. DR STRING; 522306.CAP2UW1_0214; -. DR EnsemblBacteria; ACV33572; ACV33572; CAP2UW1_0214. DR KEGG; app:CAP2UW1_0214; -. DR PATRIC; 21256420; VBICanAcc132554_0479. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; APHO522306:GHXL-216-MONOMER; -. DR Proteomes; UP000001619; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001619}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001619}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 767 767 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1238 AA; 133775 MW; A56AB2C263B80F89 CRC64; MQLDRTAELK ARLEHDILVL DGAMGTMIQR RGLREADYRG TRFAAHPHDL KGNNDLLLLT RPDIIRAIHA EYLAAGADII ETNTFNSTSA SQADYRLEAI VYELNVAGAQ LARAVCDEFT AGNPAKPRFV AGVLGPTSRT ASISPDVNDP GYRNTSFDEL VDTYAEAIRG LCDGGADILL VETVFDTLNA KAALFAIERH FDEVGRRWPV MISGTITDAS GRTLSGQTAE AFWNSLNHIR PLCFGLNCAL GAADLRQYVE ELSHLCECFV SAHPNAGLPN AFGGYDETPE QLAAEIGDWA RKGFVNIVGG CCGTSPAHIA AIAASVAGVQ PRVIPERERK LRLSGLEPFN VGRDSLFVNV GERTNVTGSR AFARMILEGR FDDALAVARQ QVENGAQVID INMDEAMLDS QAAMDRFLKL IASEPDISRV PIMLDSSKWE VIEAGLKCIQ GKGIVNSISM KEGEAEFLRQ ARLARRYGAA VVVMAFDETG QADTYTRKTE ICARAYRLLT EQAAFPPEDI IFDPNIFAIA TGIEEHNNYA VDFIEACAWI RAHLPGAQIS GGVSNVSFSF RGNDAVREAI HTVFLYHAVK AGLSMGIVNA GMLGVYDDLD PALRDKVEDV VLNRRPDAGE ALVEFAQTVK EGRSREGGMG GPDLAWRDFE VEARLTHALV KGINDFVVAD TEECRATVES AGKPPLSVIE GPLMNGMNVV GDLFGAGKMF LPQVVKSARV MKQAVAHLIP YIEAEKLRTG VSSKGKIVIA TVKGDVHDIG KNIVGVVLGC NGYDVVDLGV MVGCDKILHA AREHGAQAIG LSGLITPSLE EMSHVAAEME RLGFATGTDG SPPVPLLIGG ATTSRAHTAI KIAPNYSGPV VYVPDASRAV GVVTKLLSID NADAFKAGLA ADYEKLRAQH AGKKGTTLLA LEAARDNRFV WNGEATYRPS APKRPGLHVL RAIDLATLAG FIDWAPFFQT WDLAGSYPKI LDDPLVGATA RAVFSDAQAM LDKVIAENWL SANAVFGIFP ANSVGDDIEI YADETRAKTL MTWHNLRQQH ERPAGKPHYC LSDFVAERGT PDWIGAFAVS AGFGIEEKLA EFAAAHDDYH AIMLKAIADR LAEACAEWLH ARVRREYWAY AGDEGLDPEA LIREAYRGIR PAPGYPACPD HTAKGALFAM LDAPRNAGIE LTESFAMTPA AAVSGFYLAH PQARYFAISK IAGDQLADWA QRAGFSVPEA QRWLAPLL // ID C7X9A0_9PORP Unreviewed; 1230 AA. AC C7X9A0; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 27-MAY-2015, entry version 35. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEU50827.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEU50827.1}; GN Name=metH {ECO:0000313|EMBL:EEU50827.1}; GN ORFNames=HMPREF0619_02042 {ECO:0000313|EMBL:EEU50827.1}; OS Parabacteroides sp. D13. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Parabacteroides. OX NCBI_TaxID=563193 {ECO:0000313|EMBL:EEU50827.1}; RN [1] {ECO:0000313|EMBL:EEU50827.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=D13 {ECO:0000313|EMBL:EEU50827.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG698740; EEU50827.1; -; Genomic_DNA. DR RefSeq; WP_009017548.1; NZ_GG698740.1. DR EnsemblBacteria; EEU50827; EEU50827; HMPREF0619_02042. DR PATRIC; 25881828; VBIParSp13980_2058. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEU50827.1}; KW Transferase {ECO:0000313|EMBL:EEU50827.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1230 AA; 136493 MW; D75F2DFCDABFFE08 CRC64; MNKERFLRLL NERILILDGG MGTMIQSFKL NEQDYRGERF ADFPGQLKGN NDLLCITRPD VIQSIHRQYL DAGADIFATN TFNANAISMA DYAMEAYVRE INLAAGRLSR EVADTYMAEH PDRTIFVAGS IGPTNKTASM SPDVSDPAYR AVTYKDLYNA YKEQVEGLVD GGVDIILFET TFDTLNVKAG LEAAEVVLKE KEKDLPIMLS LTLSAQGGRT FSGQTLLAFL ASIQHTHIVS VGLNCSFGAA DMKPYLQELA KYAPYYISAY PNAGLPNSFG TYDETPDKMA QHVKPFVEEG LVNIIGGCCG TTPAHISRYP ELVKGAKPHI PAPKPDCLWL SGLELLEVKP ENNFVNVGER CNVAGSRKFL RLIKEGSYEE ALTIARKQVE DGAQVIDINM DDGMLDAVKE MKTFLNLIAS EPDIARVPVM IDSSKWEVIE EGLMCVQGKS IVNSISLKEG EEVFVKHAAR IKRLGAAAVV MAFDEKGQAD TYERKIEICE RAYRLLTEKI DFNPQDIIFD PNVLAIATGM EEHNGYGLAF IRAVEWIKKN LPGAKVSGGV SNLSFSFRGN NHVREAMHSV FLYHAIGKGM DMGIVNPSTS VLYEDIEPEF RTLLEDVILA RRPEAAEELI TYAQNLHVQA SGETPEKHEA WRELSLKERL EHALIKGIGD YLEDDLQEAL RTYPHAVDII DGPLMSGMNK VGELFGAGKM FLPQVVKTAR TMKKAVAILQ PAIESEKKAS GSAKAGKVIF ATVKGDVHDI GKNIVSIVLS CNNYEVIDLG VMVPADVIIK KAIEEKPDLV CLSGLITPSL EEMAHVADEM QKAGLTIPMM VGGATTSKLH TAVKIAPHYD YPVIHVLDAS QNPLIAAKLL NPDTRDAYIM ELEQEQEALR ASLGQKKEVL VSLSEARKHP IEIDWTGYTP VVPARMGVHV IPYIPLEKVI PYIHWTFFFS AWKLNGRFSE ISQIHGCDSC RASWLAGFPE KDRAKATEAM QLYKDAVRLL DRLVNMKVEY CKAIYGFFSA NSEGDTIRMG DIALPLLRQQ VKKEENIYKC LSDYVIPVSE ERTDYVGAFV VTAGAGADCL KDKFEEEGDT YNSMLLQTLT DRLAEATAEY LHEKVRKEYW GYAKDESLSI PDLYKVKYQG IRPAIGYPSL PDQLLNFTLD GLLDMSRIGV SLTENGAMYP TASVSGIYIA HPSSQYFMIG SIDEEQMRDY ASRRNLTEEQ ARKLLSKNIG // ID C7XGN2_9LACO Unreviewed; 329 AA. AC C7XGN2; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Putative homocysteine S-methyltransferase {ECO:0000313|EMBL:EEU19804.1}; GN ORFNames=HMPREF5045_00482 {ECO:0000313|EMBL:EEU19804.1}; OS Lactobacillus crispatus 125-2-CHN. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=575595 {ECO:0000313|EMBL:EEU19804.1, ECO:0000313|Proteomes:UP000005083}; RN [1] {ECO:0000313|EMBL:EEU19804.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=125-2-CHN {ECO:0000313|EMBL:EEU19804.1}; 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., Liu Y., Xu Q., Lander E., Nusbaum C., RA Galagan J., Birren B.; RT "The Genome Sequence of Lactobacillus crispatus strain 125-2-CHN."; 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; GG698760; EEU19804.1; -; Genomic_DNA. DR RefSeq; WP_005723036.1; NZ_GG698760.1. DR EnsemblBacteria; EEU19804; EEU19804; HMPREF5045_00482. DR PATRIC; 30705963; VBILacCri66009_0314. DR OrthoDB; EOG6C019S; -. DR Proteomes; UP000005083; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005083}; KW Methyltransferase {ECO:0000313|EMBL:EEU19804.1}; KW Transferase {ECO:0000313|EMBL:EEU19804.1}. SQ SEQUENCE 329 AA; 37143 MW; A3AA6C0F4E93C998 CRC64; MNLLKQIRDR GLILDGAMST ALEKLGIDTN NELWTAIALE HNLAQIYQVH MNYFKAGAQM AITDTYQANI PAFEKHGFTQ DQATKLITNA VQIAKKARDD FAKTTGIHNY VAASVGPYGA YLAQGDEFRG DYSLTTEEYL NFHLPRLKIL LANKPDCLAL ETQPKLDEVV AILDWLKENA PEFPVYVSFT LHDTTKISDG TPLKRVVQKL NEYDQVFAIG ANCFKPFLAT AVIDKIHDFT DKQIVIYPNL GGVYNEFERN WIPFNAKFDF KKLSQEWYEH GARIIGGCCS TTEKEIGQIS AFFKTINNTK SKSVKSELKK VKNDSNIQI // ID C7XRK9_FUSNV Unreviewed; 320 AA. AC C7XRK9; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EEU31664.1}; GN ORFNames=HMPREF0946_01525 {ECO:0000313|EMBL:EEU31664.1}; OS Fusobacterium nucleatum subsp. vincentii 3_1_36A2. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=469604 {ECO:0000313|EMBL:EEU31664.1, ECO:0000313|Proteomes:UP000016231}; RN [1] {ECO:0000313|EMBL:EEU31664.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_36A2 {ECO:0000313|EMBL:EEU31664.1}; 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; EEU31664.1; -; Genomic_DNA. DR RefSeq; WP_008800178.1; NC_022196.1. DR RefSeq; YP_008476071.1; NC_022196.1. DR EnsemblBacteria; EEU31664; EEU31664; HMPREF0946_01525. DR KEGG; fnc:HMPREF0946_01525; -. DR PATRIC; 30290127; VBIFusSp42159_1623. DR KO; K00548; -. DR Proteomes; UP000016231; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000016231}. SQ SEQUENCE 320 AA; 35466 MW; 4784FA778200128E CRC64; MKKIMFEIEK ELKERILVLD GAMGTVLQKY ELPAEDFNGT KGCYEILNET RPDIIFEVHK KYIEAGADII ETNSFNCNAI SLKNYHLEDK VYDLAKKSAE IAKDAVRKSE KKVYVFGSVG PTNKGLSFPE KDVSCKRAVS FDEMKEVIKV QVTGLIDGGV DGILLETIFD GLTAKAALLA IEEVFAEKNI KLPISISATV NKQGKLLTGQ SIESLIVDLD RDSVISFGFN CSFGAKDLVP FVLKIKELTT KFISLHANAG LPNQNGEYEE TAQKMRDDLL PLIENQAINI LGGCCGTDYE HIKLIAELIK GQKPRVLLEK // ID C7YSG1_NECH7 Unreviewed; 342 AA. AC C7YSG1; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 07-JAN-2015, entry version 30. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EEU45630.1}; GN ORFNames=NECHADRAFT_40637 {ECO:0000313|EMBL:EEU45630.1}; 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 {ECO:0000313|Proteomes:UP000005206}; RN [1] {ECO:0000313|EMBL:EEU45630.1, ECO:0000313|Proteomes:UP000005206} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI RC {ECO:0000313|Proteomes:UP000005206}; 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; GG698899; EEU45630.1; -; Genomic_DNA. DR RefSeq; XP_003051343.1; XM_003051297.1. DR EnsemblFungi; NechaT40637; NechaP40637; NechaG40637. DR GeneID; 9666199; -. DR KEGG; nhe:NECHADRAFT_40637; -. DR InParanoid; C7YSG1; -. DR KO; K00547; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000005206; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005206}; KW Reference proteome {ECO:0000313|Proteomes:UP000005206}. SQ SEQUENCE 342 AA; 37426 MW; D08198325CB76975 CRC64; MPSKTLILDG GLGTSLESKY SVSFSRSTPL WSSHLLISDP ATLESCQSDF GAVPVDVLLT ATYQVSAKGF ADTRTEEFPD GIGRDTVPRF LDDAVNIAQR AVGDKAQVAL SYGPYGACLI PSQEYSGKYD DAHDSESTLE EWHRERLGLF AEVPDVGKRV SHVALETIPR VDEIIAMRKA LAATPALSDL PYWTSCLSPG SDLTLPDGNS IEAAVEAMLD SSVSVKTPWG IGINCTKVDK LDRLLQIFES TVARLIEQGR LDDWPALVLY PDGTNGEVYN TTTQKWELLD DAKDQVRSSW ESQVESVVRA TESRGKWPVI LVGGCCKARS EDIKRLRDRL LG // ID C8CGW4_9FABA Unreviewed; 338 AA. AC C8CGW4; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 01-OCT-2014, entry version 12. DE SubName: Full=Selenocysteine methyltransferase {ECO:0000313|EMBL:ACV03420.1}; GN Name=SMT {ECO:0000313|EMBL:ACV03420.1}; OS Astragalus racemosus. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; OC Galegeae; Astragalus. OX NCBI_TaxID=668559 {ECO:0000313|EMBL:ACV03420.1}; RN [1] {ECO:0000313|EMBL:ACV03420.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=19309459; DOI=10.1111/j.1365-313X.2009.03855.x; RA Sors T.G., Martin C.P., Salt D.E.; RT "Characterization of selenocysteine methyltransferases from Astragalus RT species with contrasting selenium accumulation capacity."; RL Plant J. 59:110-122(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; GQ398501; ACV03420.1; -; mRNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Methyltransferase {ECO:0000313|EMBL:ACV03420.1}; KW Transferase {ECO:0000313|EMBL:ACV03420.1}. SQ SEQUENCE 338 AA; 36691 MW; 7DE215F0EFD72AB2 CRC64; MSSSLITDFL HQAGRTAIIA GGLGTELGRH GADLNDPLWS AKCLLSSPHL IRQVHLDYLE NGADIIITAS YQATIQGFKA KGFSDEEGEA LLRRSVEIAR EARDLYYQRC AESSSDNGDD SRILKQRPIL IAGSVGSYGA YLADGSEFSG NYGDAIKLET LKDFHRRKVQ ILADSGVDLL AFEAVPNKLE AQAYADLLEE ENMITPAWFA FNSKDGTNVV SGDSIEECGS IAESCDKVVA VGINCTPPRF IHDLILLLKK VTAKPIVIYP NSGETYDGIR KEWGQNSGVT DEDFVSYVDK WCESGASLVG GCCRTTPDTI RGIYKILSSG QSPTFSAK // ID C8CGW5_9FABA Unreviewed; 338 AA. AC C8CGW5; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 01-OCT-2014, entry version 12. DE SubName: Full=Selenocysteine methyltransferase {ECO:0000313|EMBL:ACV03421.1}; GN Name=SMT {ECO:0000313|EMBL:ACV03421.1}; OS Astragalus pectinatus. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; OC Galegeae; Astragalus. OX NCBI_TaxID=668558 {ECO:0000313|EMBL:ACV03421.1}; RN [1] {ECO:0000313|EMBL:ACV03421.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=19309459; DOI=10.1111/j.1365-313X.2009.03855.x; RA Sors T.G., Martin C.P., Salt D.E.; RT "Characterization of selenocysteine methyltransferases from Astragalus RT species with contrasting selenium accumulation capacity."; RL Plant J. 59:110-122(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; GQ398502; ACV03421.1; -; mRNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Methyltransferase {ECO:0000313|EMBL:ACV03421.1}; KW Transferase {ECO:0000313|EMBL:ACV03421.1}. SQ SEQUENCE 338 AA; 36611 MW; ABB42E28374D19B7 CRC64; MSSSLITDFL RQAGRPAIIA GGLGTELERH GADLNDPLWS AKCLYSSPHL IHQVHLDYLE NGADIILTAS YQATIQGFKA KGFSDEEGEA LLRRSVEIAR EARDLYYQRC AESSSDNGDD SRILKPRPIL IAGSIGSYGA YLADGSEFSG NYGDAIKLET LKDFHRRRVQ ILADSGVDLL AFGAVPNKLE AQAYADLLEE ENIITPAWFA FNSKDGTNVV SGDSIEECGS IAESCDKVVA VGISCTPPRF IHDLIHLLKK VTAKPVVIYP NSGETYDGIR KEWGQNSGVT DGDFVSYVDK WCESGASIVG GCCRTAPDTI RGIYKILSSG QSPTFSAK // ID C8CGW6_9FABA Unreviewed; 337 AA. AC C8CGW6; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 01-OCT-2014, entry version 12. DE SubName: Full=Selenocysteine methyltransferase {ECO:0000313|EMBL:ACV03422.1}; GN Name=SMT {ECO:0000313|EMBL:ACV03422.1}; OS Astragalus ceramicus. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; OC Galegeae; Astragalus. OX NCBI_TaxID=90165 {ECO:0000313|EMBL:ACV03422.1}; RN [1] {ECO:0000313|EMBL:ACV03422.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=19309459; DOI=10.1111/j.1365-313X.2009.03855.x; RA Sors T.G., Martin C.P., Salt D.E.; RT "Characterization of selenocysteine methyltransferases from Astragalus RT species with contrasting selenium accumulation capacity."; RL Plant J. 59:110-122(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; GQ398503; ACV03422.1; -; mRNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Methyltransferase {ECO:0000313|EMBL:ACV03422.1}; KW Transferase {ECO:0000313|EMBL:ACV03422.1}. SQ SEQUENCE 337 AA; 36656 MW; 33E0E0ABCBF1E283 CRC64; MSSSLITDFL HQAGRTAVIA GGLATELERH GADLNDPLWS AKCLLSSPHL IRQVHLDYLE NGADIIITAS YQATIQGFKA KGFSDEEGEA LLRRSVEIAR EARDLYYQRC AESSSDNGDD SRILKQRPIL IAGSVGSYGA YLADGSEYSG NYGDAIKLET LKDFHRRRVQ ILADSGVDLL AFEAVPNKPE AQAYADLLEE ENIITPAWFA FNSKDGTNVV SGDSIEECGS IAESCDKVVA VGINCTPPRF IHDLILLPKK VTAKPIVIYP NSGETYDGIR KEWGQNSGVT DEDFVSYVDK WCESGASLVG GCCRTTPDTI RGIYKILSSG QSPFSAK // ID C8CGW7_9FABA Unreviewed; 337 AA. AC C8CGW7; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 01-OCT-2014, entry version 12. DE SubName: Full=Selenocysteine methyltransferase-like protein {ECO:0000313|EMBL:ACV03423.1}; GN Name=SMT {ECO:0000313|EMBL:ACV03423.1}; OS Astragalus drummondii. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; OC Galegeae; Astragalus. OX NCBI_TaxID=668556 {ECO:0000313|EMBL:ACV03423.1}; RN [1] {ECO:0000313|EMBL:ACV03423.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=19309459; DOI=10.1111/j.1365-313X.2009.03855.x; RA Sors T.G., Martin C.P., Salt D.E.; RT "Characterization of selenocysteine methyltransferases from Astragalus RT species with contrasting selenium accumulation capacity."; RL Plant J. 59:110-122(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; GQ398504; ACV03423.1; -; mRNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Methyltransferase {ECO:0000313|EMBL:ACV03423.1}; KW Transferase {ECO:0000313|EMBL:ACV03423.1}. SQ SEQUENCE 337 AA; 36674 MW; 1BD9CE615D4CCB07 CRC64; MSSSLITDFL HQAGRTAVIG GGLATELERH GADLNDPLWS AKCLLSSPHL IRQVHLDYLE NGADIIITAS YQATIQGFKA KGFSDEEGEA LLRRSVEIAR EARDLYYQRC AESSSDNGDD SRILKQRPIL IAGSVGSYGA YLADGSEYSG NYGDAIKLET LKDFHRRRVQ ILADSGVDLL AFEAVPNKLE AQAYADLLEE ENIITPAWFA FNSKDGTNVV SGDSIEECGS IAESCDKVVA VGINCTPPRF IHDLILLLKK VTAKPIVIYP NSGETYDGIR KEWGQNSGVT DEDFVSYVDK WCESGASLVG GCCRTTPDTI RGIYKILSSG QSPFSAK // ID C8CGW8_9FABA Unreviewed; 337 AA. AC C8CGW8; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 01-OCT-2014, entry version 12. DE SubName: Full=Selenocysteine methyltransferase {ECO:0000313|EMBL:ACV03424.1}; GN Name=SMT {ECO:0000313|EMBL:ACV03424.1}; OS Astragalus leptocarpus. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; OC Galegeae; Astragalus. OX NCBI_TaxID=668557 {ECO:0000313|EMBL:ACV03424.1}; RN [1] {ECO:0000313|EMBL:ACV03424.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=19309459; DOI=10.1111/j.1365-313X.2009.03855.x; RA Sors T.G., Martin C.P., Salt D.E.; RT "Characterization of selenocysteine methyltransferases from Astragalus RT species with contrasting selenium accumulation capacity."; RL Plant J. 59:110-122(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; GQ398505; ACV03424.1; -; mRNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Methyltransferase {ECO:0000313|EMBL:ACV03424.1}; KW Transferase {ECO:0000313|EMBL:ACV03424.1}. SQ SEQUENCE 337 AA; 36558 MW; EB50919CD008B1F4 CRC64; MSSSLITDFL HQAGRTAVIA GGLATELERH GADLNDPLWS AKCLLSSPHL IRQVHLDYLE NGADIIITAS YQATIQGFKA KGFSGEEGEA LLRRSVGIAR EARDLYYQRC AESSSDNGDD SRILKQRPIL IAGSVGSYGA YLADGSEYSG NYGDAIKLET LKDFHRRRVQ ILADSGVDLL AFEAVPNKLE AQAYADLLEE ENIITPAWFA FNSKDGTNVV SGDSIEECGS IAESCDKVVA VGINCTPPRF IHDLILLLKK VTAKPIVIYP NSGETYDGIR KEWGQNSGVT DEDFVSYVDK WCESGASLVG GCCRTTPDTI RGIYKILSSG QSPFSAK // ID C8KXT7_9PAST Unreviewed; 837 AA. AC C8KXT7; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EEV24616.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEV24616.1}; DE Flags: Fragment; GN Name=metH {ECO:0000313|EMBL:EEV24616.1}; GN ORFNames=AM202_00280 {ECO:0000313|EMBL:EEV24616.1}; OS Actinobacillus minor 202. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=591023 {ECO:0000313|EMBL:EEV24616.1}; RN [1] {ECO:0000313|EMBL:EEV24616.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=202 {ECO:0000313|EMBL:EEV24616.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEV24616.1}. 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; ACFT01000068; EEV24616.1; -; Genomic_DNA. DR RefSeq; WP_005819996.1; NZ_ACFT01000068.1. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEV24616.1}; KW Transferase {ECO:0000313|EMBL:EEV24616.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 246 246 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. FT NON_TER 837 837 {ECO:0000313|EMBL:EEV24616.1}. SQ SEQUENCE 837 AA; 91499 MW; 1399F55069060F58 CRC64; MQHNRIEQLK TALTQRILIL DGAMGTMIQQ FKLTEADFRG ERFKNSSVDL RGNNDLLTLT QPLVISSIHE KYLEAGADII ETNTFSSTTI AQADYDLQAV AYELNFAGAK LARIAADKYS TPEKPRFVAG ILGPTNRTAS ISPNVNDPGF RNITFMELVD AYAEATRGLI DGGSDIIMIE TIFDTLNAKA AAFAIDQVFE ELGVELPIMI SGTITDASGR TLSGQTTEAF YNSLRHAKPL SFGLNCALGP KELRPYVEVM SKICETYVSV HPNAGLPNAF GGYDLGAEEM ATHIKEWAES GFLNIVGGCC GTTPEHIKAF ADVVTGIKPR TLPEIKTAMR LSGLEPLNID DESLFVNVGE RNNVTGSAKF KRLIKEEKFS EAIEIAIDQV ENGAQVIDVN MDEALLDSQK CMTRFLNIMA TEPDAAKVPV MIDSSKWEVI EAGLQSVQGK GIVNSISLKE GEEKFIHQAK LVRRYGAAVV VMAFDEVGQA DTEERKVEIC TRAYDILVNQ VGFPPEDIIF DPNIFAIGTG IEEHNNYGVD FINATGRIKR SLPHAKISGG VSNVSFSFRG NNVMREAIHA VFLYHAIKQG MDMGIVNAGQ LAIYDDLDPE LRDVIEDAVL NRRPDATDRL LDIAEKYRNV TASNSEDSGV AEWRTWVVEE RLKHALVKGI TNYIIEDTEE ARQKFPTPLE VIEGPLMDGM DVVGDLFGDG KMFLPQVVKS ARVMKQSVAY LEPFINATKQ KGSSSGKVVI ATVKGDVHDI GKNIVSVVLQ CNNFEVIDLG VMVPADKIIQ TAIDEKADII GLSGLITPSL DEMEYFLGEM NRLNLNIPVI IGGGGGG // ID C8KZR0_9PAST Unreviewed; 296 AA. AC C8KZR0; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Homocysteine/selenocysteine methylase {ECO:0000313|EMBL:EEV25289.1}; GN ORFNames=AM202_03675 {ECO:0000313|EMBL:EEV25289.1}; OS Actinobacillus minor 202. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=591023 {ECO:0000313|EMBL:EEV25289.1}; RN [1] {ECO:0000313|EMBL:EEV25289.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=202 {ECO:0000313|EMBL:EEV25289.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEV25289.1}. 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; ACFT01000106; EEV25289.1; -; Genomic_DNA. DR RefSeq; WP_005821263.1; NZ_ACFT01000106.1. DR PATRIC; 24360181; VBIActMin123628_1849. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEV25289.1}; KW Transferase {ECO:0000313|EMBL:EEV25289.1}. SQ SEQUENCE 296 AA; 32469 MW; CFD85A3596BD7E6E CRC64; MTITILDGGM SRELMRLNAP FRQPEWSALS LYEKPSAVQQ VHENFIQSGA EIITTNSYAV VPFHIGDQRF IADGKMLADL AGRLAKQAVK NSQKDVKIAG SLPPLFGSYR PDLFQADKVK ETAQPLIDGL APYVDFWLCE TQSAIIEPQS IKPLLPDNRP LWVSFTLTDD EPTPEPQLRS GESVKMAVEK MIELGVQAIL FNCCQPEVIT EALNITRQTL AAHQATHIQI GAYANAFAPQ PKDATANDGL DEVRPDLDPQ AYLTWAQKWV DCGATIIGGC CGIGLEHIQA LSANLK // ID C8N8Q6_9GAMM Unreviewed; 305 AA. AC C8N8Q6; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEV88982.1}; GN ORFNames=HMPREF0198_0883 {ECO:0000313|EMBL:EEV88982.1}; OS Cardiobacterium hominis ATCC 15826. OC Bacteria; Proteobacteria; Gammaproteobacteria; Cardiobacteriales; OC Cardiobacteriaceae; Cardiobacterium. OX NCBI_TaxID=638300 {ECO:0000313|EMBL:EEV88982.1}; RN [1] {ECO:0000313|EMBL:EEV88982.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 15826 {ECO:0000313|EMBL:EEV88982.1}; 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 (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEV88982.1}. 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; ACKY01000043; EEV88982.1; -; Genomic_DNA. DR RefSeq; WP_004140399.1; NZ_GG694026.1. DR EnsemblBacteria; EEV88982; EEV88982; HMPREF0198_0883. DR PATRIC; 30389152; VBICarHom6741_1253. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EEV88982.1}; KW Transferase {ECO:0000313|EMBL:EEV88982.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 207 207 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 287 287 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 305 AA; 32378 MW; 92896D567D884EBD CRC64; MTHPHPLHLL DGGMGRELLR RGAPFAQPEW SALALIQAPA TVQDVHAAYI AAGAETLTTN SYALVPFHIG EERFRARAGE LAALAGKLAR QAVKKSGKTV HIAGSLPPLF GSYRPDLFDP ARAAEIARPL IDGQAPYVDY WLAETQSSIA EVRALHALTA RDRPFWASFT LEDEPPAEPP RLRSGETVAA AVAAALELKL DALLFNCSHP EAMTAALKTA RATIDAAGSA MRLGVYANAF AAHGTDEEAL PANDGLDEIR TDLTPTAYLD WAKHWCAAGA DIIGGCCGVG PEHIAALAAW RAQNA // ID C8Q0K3_9GAMM Unreviewed; 1255 AA. AC C8Q0K3; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 32. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEV21971.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEV21971.1}; GN Name=metH {ECO:0000313|EMBL:EEV21971.1}; GN ORFNames=ENHAE0001_0681 {ECO:0000313|EMBL:EEV21971.1}; OS Enhydrobacter aerosaccus SK60. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Enhydrobacter. OX NCBI_TaxID=553217 {ECO:0000313|EMBL:EEV21971.1}; RN [1] {ECO:0000313|EMBL:EEV21971.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK60 {ECO:0000313|EMBL:EEV21971.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEV21971.1}. 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; ACYI01000068; EEV21971.1; -; Genomic_DNA. DR RefSeq; WP_007117125.1; NZ_ACYI01000068.1. DR EnsemblBacteria; EEV21971; EEV21971; ENHAE0001_0681. DR PATRIC; 29274490; VBIEnhAer50137_2180. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEV21971.1}; KW Transferase {ECO:0000313|EMBL:EEV21971.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 280 280 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 343 343 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 344 344 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 794 794 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1255 AA; 138772 MW; 17EF5CE0BD4244F5 CRC64; MSISTSNAPT SHKPHDPTNF KLTPPTSFPY QDRQATNKAR LAELLKQRIL FLDGAMGTEI QNYKLIEADY RGERFANFGR DVKGNNDLLV LTQPHIIRDI HRSYLEAGAD IIETNSFNGT QISMADYGME NLAYEINKSA AALARQVCDE VTATNPDKPR FVAGVIGPTS RTCSISPDVN DPAFRNVTFD ELVDNYTEAT YALIEGGADI ILIETVFDTL NAKAAIFAVT GVFETIGFEL PIMISGTITD ASGRTLSGQT AEAFYNSIRH AKPISIGFNC ALGADALKPH IKTLSDVCET FVSAHPNAGL PNEFGEYDET PEQTATMVAD YAKSGLVNIV GGCCGTTPKH IAKIVEMTSP FAPRQLPDYK PACRLSGLEA FNITRDSLFV NVGERTNVTG SKKFLRLIKN EEYTEALDVA RDQVEGGAQV VDINMDEAML DSKAAMIHFV NLVASEPDIS RVPLMIDSSK WDIIEAGLKC TQGKSVVNSI SLKEGKTEFV QKAKLCQRYG AAIIVMAFDE DGQADSFERK IEICKRSYDI LVDEVGFPSE DIIFDPNIFA VATGIEEHNN YGLDFINATR WITDNLPNAM VSGGVSNVSF SFRGNPIREA IHAVFLYHAI KNGMTMGIVN PAMLELYDDI DPDVRNAIED VILNRNQGES GQDATDHLMQ VAENYLSGKK KDSTVDLSWR ELPVEKRIEH ALVKGITTYI NEDTEEARLK FPRPLDVIEG PLMDGMNVVG DLFGAGKMFL PQVVKSARVM KQAVAWLNPY IEKEKVAGET KGKVLMATVK GDVHDIGKNI VGVVLGCNGY DIIDLGVMVP CEKILQVAKD ENVDIIGLSG LITPSLDEMV YVAKQMQEQG FNLPLLIGGA TTSKAHTAVK IEPNYQNDAV VYVADASRAV GVATTLLSKE KRVDFISELR QEYGEVRERL ANRQPKAAKL SYAESIKQGF QYDWANYTPP KPNQLGQVIL DDYPLQNLLP YIDWTPFFIS WGLVGKYPKI FDDSIVGEEA KDLFANAQTM IDKLIKEKLV TAKAVFRLSP AQRPSSDTVQ VLDEQGHVTH TFEHLRQQSD KASGKPNYSL ADFISPEKTD YLGGFTVSLF GAEALANDYK AKGDDYSAIM VQALCDRFAE AFAEHLHELI RKQYWGYQSD ENLTNEELIK EKYVGIRPAP GYPACPDHTE KGKLFDWLDT TNAIGTYLTE SYAMYPASSV SGFYYSHPES EYFNVGKISE DQLLDYAARK GWDKATAEKW LNPNL // ID C8RXE5_9RHOB Unreviewed; 297 AA. AC C8RXE5; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEW26670.1}; GN ORFNames=Rsw2DRAFT_0473 {ECO:0000313|EMBL:EEW26670.1}; OS Rhodobacter sp. SW2. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=371731 {ECO:0000313|EMBL:EEW26670.1}; RN [1] {ECO:0000313|EMBL:EEW26670.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SW2 {ECO:0000313|EMBL:EEW26670.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEW26670.1}. 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; ACYY01000002; EEW26670.1; -; Genomic_DNA. DR RefSeq; WP_008027664.1; NZ_ACYY01000002.1. DR EnsemblBacteria; EEW26670; EEW26670; Rsw2DRAFT_0473. DR PATRIC; 28437594; VBIRhoSp55960_0481. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EEW26670.1}; KW Transferase {ECO:0000313|EMBL:EEW26670.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 201 201 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 274 274 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 275 275 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 297 AA; 30739 MW; 3FAD079D7D2B658B CRC64; MQITLLDGGM GQELLARTGD APTPLWATQV MLDHPDVVRQ IHADYFAAGA TVATTNTYAI HHDRLERFGV DHLFGALHAK ALAQAQEARA AHGSGRIAGS LGPLVASYRP ETCPPVAEAA VKYAEIAALL APGVDFFLCE TMASVQQAEG ALAGALTAGK PVWLSVTVDD ADGSRLRSGE AVADLAPLVA RYKPAAVLVN CSVPEAMAAA LAQVAGFGVP FGAYANGFTH INAAFKADAP TVDVLEHRHD LTPAKYADFA MFWVAQGATI VGGCCEVGPA HIAALAAALR AAGHEIV // ID C8S4S6_9RHOB Unreviewed; 336 AA. AC C8S4S6; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 01-OCT-2014, entry version 17. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEW23985.1}; GN ORFNames=Rsw2DRAFT_3054 {ECO:0000313|EMBL:EEW23985.1}; OS Rhodobacter sp. SW2. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=371731 {ECO:0000313|EMBL:EEW23985.1}; RN [1] {ECO:0000313|EMBL:EEW23985.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SW2 {ECO:0000313|EMBL:EEW23985.1}; 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. {ECO:0000313|EMBL:EEW23985.1}. 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; ACYY01000028; EEW23985.1; -; Genomic_DNA. DR RefSeq; WP_008032534.1; NZ_ACYY01000028.1. DR EnsemblBacteria; EEW23985; EEW23985; Rsw2DRAFT_3054. DR PATRIC; 28442864; VBIRhoSp55960_3075. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEW23985.1}; KW Transferase {ECO:0000313|EMBL:EEW23985.1}. SQ SEQUENCE 336 AA; 34988 MW; 07E3A04A4F7C0730 CRC64; MTNALSRLLS THDWLMADGA TGTNLFNMGL SSGEAPEFWN ADQPDNIRKL YQWAVDAGSD IFLTNSFGGN ASRLKLHGAQ GRVHELNRLA ASLGREVADK AGRPVVVAGS VGPTGEIMAP MGTLTHAIAV EMFHEQAEGL KAGGADVLWV ETISAAAEYQ AAAEAAALAG MPWCGTMSFD TAGRTMMGVT SAAMVEMVEK LANPPLAFGA NCGVGSSDLL RTVLGFAAQG SERPVIAKGN AGIPKYKDGA IHYDGTPALM ADYAVLARDA GARIIGGCCG TMPEHLRAMR QALETRPKGP RPTLEAISAA LGAFSSASDG TGDDSGAPKR ERRRGR // ID C8T4K8_KLEPR Unreviewed; 310 AA. AC C8T4K8; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEW41387.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EEW41387.1}; GN Name=mmuM {ECO:0000313|EMBL:EEW41387.1}; GN ORFNames=HMPREF0484_2550 {ECO:0000313|EMBL:EEW41387.1}; OS Klebsiella pneumoniae subsp. rhinoscleromatis ATCC 13884. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=667127 {ECO:0000313|EMBL:EEW41387.1}; RN [1] {ECO:0000313|EMBL:EEW41387.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 13884 {ECO:0000313|EMBL:EEW41387.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEW41387.1}. 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; ACZD01000123; EEW41387.1; -; Genomic_DNA. DR RefSeq; WP_004144601.1; NZ_GG703526.1. DR EnsemblBacteria; EEW41387; EEW41387; HMPREF0484_2550. DR PATRIC; 35968088; VBIKlePne146004_2571. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEW41387.1}; KW Transferase {ECO:0000313|EMBL:EEW41387.1}. SQ SEQUENCE 310 AA; 33155 MW; E47269D621DA3F0A CRC64; MSQTNPFTAL LAAQPFVLLD GAMATELEAR GCDLADSLWS AKVLLENPQL IRDVHLDYFR AGAQVAITAS YQATPAGFAA RGLDEAQSRA LIGKSVELAR KAREAYLAEN PQAGTLLVAG SVGPYGAFLA DGSEYRGDYQ RSAAEFQAFH RPRVEALLDA GADLLACETL PSFAEIQALA ALLQEYPRAR AWYSFTLRDA EHLSDGTPLR EVMAALADNP QVVAVGINCI ALENTPAALA HLHSLTALPL VVYPNSGEHY DAVSKTWHHH GEACASLADY LPQWLAAGAK LIGGCCRTTP KDIAALNAKR // ID C8TDD5_KLEPR Unreviewed; 674 AA. AC C8TDD5; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEW38337.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEW38337.1}; GN Name=metH2 {ECO:0000313|EMBL:EEW38337.1}; GN ORFNames=HMPREF0484_5629 {ECO:0000313|EMBL:EEW38337.1}; OS Klebsiella pneumoniae subsp. rhinoscleromatis ATCC 13884. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=667127 {ECO:0000313|EMBL:EEW38337.1}; RN [1] {ECO:0000313|EMBL:EEW38337.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 13884 {ECO:0000313|EMBL:EEW38337.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEW38337.1}. 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; ACZD01000265; EEW38337.1; -; Genomic_DNA. DR EnsemblBacteria; EEW38337; EEW38337; HMPREF0484_5629. DR PATRIC; 35971325; VBIKlePne146004_3874. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEW38337.1}; KW Transferase {ECO:0000313|EMBL:EEW38337.1}. SQ SEQUENCE 674 AA; 73965 MW; 47E214FF382BEAAA CRC64; MVCWLFGLSR ALSGASVSSK VEQLHQQLKE RILVLDGGMG TMIQGYRLSE QDFRGERFAD WPCDLKGNND LLVLSKPEVI REIHDAYFEA GADIVETNTF NSTTIAMADY QMESLSAEIN FAAAKLARAS ADAWTARTPE KPRYVAGVLG PTNRTASISP DVNDPAFRNI TFDQLVAAYR ESTRALVEGG VDLILIETVF DTLNAKAAIY AAKEELEALG VDLPLMISGT ITDASGRTLS GQTTEAFYNS LRHAEALSFG LNCALGPDEL RQYVQELSRI AECYVTAHPN AGLPNAFGEY DLDADTMATQ IREWAEAGFL NIVGGCCGTT PEHIAAMSRA VAGLPPRQLP EIAVACRLAG LEPLNIGDDS LFVNVGERTN VTGSAKFKRL IKEEKYSEAL DVARQQVESG AQIIDINMDE GMLDAEAAMV RFLNLIAGEP DIARVPIMID SSKWEVIEKG LKCIQGKGIV NSISMKEGVE SFIHHAKLVR RYGAAVVVMA FDEVGQADTR ERKIEICRRA YKVLTEEVGF PPEDIIFDPN IFAVATGIEE HNNYAQDFIG ACEDIKRELP HALISGGVSN VSFSFRGNDP VREAIHAVFL YYAIRNGMDM GIVNAGQLAI YDDLPGELRD AVEDVILNRR DDSTERLLEL AEKYRGSKAD DGANAQQAEW RTWR // ID C8TMQ3_ECO26 Unreviewed; 1227 AA. AC C8TMQ3; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 44. DE SubName: Full=Homocysteine-N5-methyltetrahydrofolate transmethylase, B12-dependent {ECO:0000313|EMBL:BAI28274.1}; GN Name=metH {ECO:0000313|EMBL:BAI28274.1}; GN OrderedLocusNames=ECO26_5123 {ECO:0000313|EMBL:BAI28274.1}; OS Escherichia coli O26:H11 (strain 11368 / EHEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=573235 {ECO:0000313|EMBL:BAI28274.1, ECO:0000313|Proteomes:UP000001617}; RN [1] {ECO:0000313|EMBL:BAI28274.1, ECO:0000313|Proteomes:UP000001617} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=11368 / EHEC {ECO:0000313|Proteomes:UP000001617}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP010953; BAI28274.1; -; Genomic_DNA. DR RefSeq; WP_000096053.1; NC_013361.1. DR RefSeq; YP_003232014.1; NC_013361.1. DR STRING; 573235.ECO26_5123; -. DR EnsemblBacteria; BAI28274; BAI28274; ECO26_5123. DR KEGG; eoj:ECO26_5123; -. DR PATRIC; 18406226; VBIEscCol24965_5282. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; ECOL573235:GCY7-5308-MONOMER; -. DR Proteomes; UP000001617; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001617}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAI28274.1}; KW Transferase {ECO:0000313|EMBL:BAI28274.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136040 MW; D1A76336C7330E3D CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID C8TZU5_ECO10 Unreviewed; 1227 AA. AC C8TZU5; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 45. DE SubName: Full=Homocysteine-N5-methyltetrahydrofolate transmethylase, B12-dependent {ECO:0000313|EMBL:BAI33457.1}; GN Name=metH {ECO:0000313|EMBL:BAI33457.1}; GN OrderedLocusNames=ECO103_4764 {ECO:0000313|EMBL:BAI33457.1}; OS Escherichia coli O103:H2 (strain 12009 / EHEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI33457.1, ECO:0000313|Proteomes:UP000000959}; RN [1] {ECO:0000313|EMBL:BAI33457.1, ECO:0000313|Proteomes:UP000000959} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP010958; BAI33457.1; -; Genomic_DNA. DR RefSeq; WP_000096076.1; NC_013353.1. DR RefSeq; YP_003224591.1; NC_013353.1. DR STRING; 585395.ECO103_4764; -. DR EnsemblBacteria; BAI33457; BAI33457; ECO103_4764. DR KEGG; eoh:ECO103_4764; -. DR PATRIC; 32101752; VBIEscCol146794_4994. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; ECOL585395:GJA9-4947-MONOMER; -. DR Proteomes; UP000000959; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000959}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAI33457.1}; KW Transferase {ECO:0000313|EMBL:BAI33457.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135996 MW; 510CD94298D08EAE CRC64; MSSKVEQLRA QLNQRILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAD // ID C8UKR6_ECO1A Unreviewed; 1227 AA. AC C8UKR6; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 43. DE SubName: Full=Homocysteine-N5-methyltetrahydrofolate transmethylase, B12-dependent {ECO:0000313|EMBL:BAI38576.1}; GN Name=metH {ECO:0000313|EMBL:BAI38576.1}; GN OrderedLocusNames=ECO111_4831 {ECO:0000313|EMBL:BAI38576.1}; OS Escherichia coli O111:H- (strain 11128 / EHEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=585396 {ECO:0000313|EMBL:BAI38576.1, ECO:0000313|Proteomes:UP000001614}; RN [1] {ECO:0000313|EMBL:BAI38576.1, ECO:0000313|Proteomes:UP000001614} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=11128 / EHEC {ECO:0000313|Proteomes:UP000001614}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP010960; BAI38576.1; -; Genomic_DNA. DR RefSeq; WP_000096053.1; NC_013364.1. DR RefSeq; YP_003237127.1; NC_013364.1. DR STRING; 585396.ECO111_4831; -. DR EnsemblBacteria; BAI38576; BAI38576; ECO111_4831. DR KEGG; eoi:ECO111_4831; -. DR PATRIC; 32113282; VBIEscCol143187_5015. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; ECOL585396:GJCW-5020-MONOMER; -. DR Proteomes; UP000001614; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001614}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAI38576.1}; KW Transferase {ECO:0000313|EMBL:BAI38576.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136040 MW; D1A76336C7330E3D CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID C8W2L3_DESAS Unreviewed; 801 AA. AC C8W2L3; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 38. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACV63697.1}; GN OrderedLocusNames=Dtox_2941 {ECO:0000313|EMBL:ACV63697.1}; OS Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM OS B-1644). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfotomaculum. OX NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV63697.1, ECO:0000313|Proteomes:UP000002217}; RN [1] {ECO:0000313|EMBL:ACV63697.1, ECO:0000313|Proteomes:UP000002217} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49208 / DSM 771 / VKM B-1644 RC {ECO:0000313|Proteomes:UP000002217}; 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 ----------------------------------------------------------------------- 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; ACV63697.1; -; Genomic_DNA. DR RefSeq; WP_015758389.1; NC_013216.1. DR RefSeq; YP_003192320.1; NC_013216.1. DR ProteinModelPortal; C8W2L3; -. DR STRING; 485916.Dtox_2941; -. DR EnsemblBacteria; ACV63697; ACV63697; Dtox_2941. DR KEGG; dae:Dtox_2941; -. DR PATRIC; 21722767; VBIDesAce42372_2988. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; DACE485916:GHUF-3012-MONOMER; -. DR Proteomes; UP000002217; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002217}; KW Methyltransferase {ECO:0000313|EMBL:ACV63697.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002217}; KW Transferase {ECO:0000313|EMBL:ACV63697.1}. SQ SEQUENCE 801 AA; 85944 MW; 848B45DE57E28682 CRC64; MRFIDKLAEK ILVFDGAMGT MLQAAGLRAG ECPELINLKN PETVKNIHRQ YVKAGADIVE TNTFGGSRLK LLEYGLADKV AEINASAVRL AKESADGQAL VALSVGPTGK LMFPNGPLTF DEAHHVFSEQ ISAGAAAGAD MICIETMSDL GEIRAALLAA KDAAPGVPVI CSMTFEPNKR TLMGTDPVAA VITLQALGAD IIGANCSGGP GELLEVIEEM ARYARVPLIV QPNAGMPMLE GDRTVFPLSA AEMGEYVPKL AAAGASLIGG CCGTSPEYIR VIKERSTGLK PLPRNITPVT AITSARQTLF IGSGHPVRIV GERINPTGRK ELSEQLRKGD MSLILREAVE QVERGANLLD VNMGLPEIDE AALMEKAVNS LQKVISVPLQ LDSTDPKVLE AGLKAYHGKA IINSVNGKEE SLKTILPLAK RYGACILGLA LDDKGIPKTS EGRLAAAEKI MQRALALGIP KEDIIIDSLV LTASAQQDTA LACVECTRLV KEELGLSALL GVTNISYGLP NRSLIDNTFL AMCLAGGVDV VIFNVENQDM VNTVRASEVL TARDKHSRNY INLFAAGEAQ GAVLEEQAVE EDRKPADCLY RDIINGFKEN TVPLLEEVLK QGMMPLQIVD DLLVPALDEV GGKYDRGEFF LPQLMQSAEV VQAAFARLKQ ELKVAGDSGK GTVLLATVKG DIHDIGKNIV KVLLENYGYE VVDMGKDVPP EEIVRAAKEK DIRLIGLSAL MTTTVVFMKE TIDLLRQEKP DCKVVVGGAV LNEKYAENIR ADFYARDARE GVAVAREVFG R // ID C8WLR3_EGGLE Unreviewed; 300 AA. AC C8WLR3; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Methionine synthase I (Cobalamin-dependent) methyltransferase domain-like protein {ECO:0000313|EMBL:ACV56526.1}; GN OrderedLocusNames=Elen_2573 {ECO:0000313|EMBL:ACV56526.1}; 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 {ECO:0000313|EMBL:ACV56526.1, ECO:0000313|Proteomes:UP000001377}; RN [1] {ECO:0000313|EMBL:ACV56526.1, ECO:0000313|Proteomes:UP000001377} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25559 / DSM 2243 / JCM 9979 / NCTC 11813 / VPI 0255 RC {ECO:0000313|Proteomes:UP000001377}; 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; ACV56526.1; -; Genomic_DNA. DR RefSeq; WP_009609446.1; NC_013204.1. DR RefSeq; YP_003182915.1; NC_013204.1. DR STRING; 479437.Elen_2573; -. DR EnsemblBacteria; ACV56526; ACV56526; Elen_2573. DR KEGG; ele:Elen_2573; -. DR PATRIC; 21845907; VBIEggLen106823_2637. DR eggNOG; NOG310274; -. DR HOGENOM; HOG000102398; -. DR KO; K00548; -. DR OMA; EIGPCGL; -. DR OrthoDB; EOG64FKJ0; -. DR BioCyc; ELEN479437:GHWY-2623-MONOMER; -. DR Proteomes; UP000001377; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001377}; KW Methyltransferase {ECO:0000313|EMBL:ACV56526.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001377}; KW Transferase {ECO:0000313|EMBL:ACV56526.1}. SQ SEQUENCE 300 AA; 31671 MW; 81831A2FE3F06721 CRC64; MPDIALRFHK DMLVLSSPVA VVLARQGFDV EHDLEFANLV EPEAVRDALR LNKMAGAQCL VANTEGIAPA RLAHRGMEDR AAEIVRTGLS LARELKSQHV LVEIGPCGLP LDAASKSSLN ENRDQYARAA HACDGQEFDA FFLNGFANPA DLKCALMGVR QVSGAPVFAS VDVDADGMLA DGRHTLEDAL AVMVDYEASV VGFATAAPLD AAVTFARRAS GAGRLPVLAQ LIVREHNPKQ GDVTHENPYY CPDVLVGAAV QLRAAGAQFL RAAGAATPAY AGALAAASEG FDVVRSDVEE // ID C8WWX3_ALIAD Unreviewed; 637 AA. AC C8WWX3; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 38. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=Aaci_1583 {ECO:0000313|EMBL:ACV58595.1}; OS Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC OS 27009 / DSM 446 / JCM 5260 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / OS 104-1A) (Bacillus acidocaldarius). OC Bacteria; Firmicutes; Bacilli; Bacillales; Alicyclobacillaceae; OC Alicyclobacillus. OX NCBI_TaxID=521098 {ECO:0000313|EMBL:ACV58595.1, ECO:0000313|Proteomes:UP000001917}; RN [1] {ECO:0000313|Proteomes:UP000001917} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27009 / DSM 446 / JCM 5260 / NBRC 15652 / NCIMB 11725 / RC NRRL B-14509 / 104-1A {ECO:0000313|Proteomes:UP000001917}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ACV58595.1; -; Genomic_DNA. DR RefSeq; WP_012810901.1; NC_013205.1. DR RefSeq; YP_003184984.1; NC_013205.1. DR ProteinModelPortal; C8WWX3; -. DR STRING; 521098.Aaci_1583; -. DR EnsemblBacteria; ACV58595; ACV58595; Aaci_1583. DR KEGG; aac:Aaci_1583; -. DR PATRIC; 20846582; VBIAliAci73240_1531. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; AACI521098:GCIO-1635-MONOMER; -. DR Proteomes; UP000001917; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001917}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ACV58595.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000001917}; KW Transferase {ECO:0000313|EMBL:ACV58595.1}. SQ SEQUENCE 637 AA; 69061 MW; 4093297FAB3A8EA0 CRC64; MWRQWRRPPR DVEGPLGAYV IFDGAMSTYL HQLGVPIGTP VEQLNLTSPD LVARVHRRYV ESGCTVLQTN TFMGNRIALE RHGLTVDVQS LNRRGVEIAR SAARDEASVY GTMGPAMGGY RYGALLQDEE RDLLARVYAE QAEALVSAGI DGLILETFPD LEEALVAIAA VRPILGDLPL VVNLSPEEIG VTRDGVPLAE AFRRIKAAGA DVVGLNCRLG PYGILRSYEQ AGVAADGPYA AVPNAGILQR SEGDEIAYTG DTADFSRLML RIAQLGVRWL GGCCGTTPEY IRTLRDALMR ADREPHGAAI QAETHATSRP SAVTTGAGAY HDGMSVVDIA REKKAIVVEL DPPKHLSIAR FLEGAEALAG AGADLITMAD NSLGSVRVSN MALASLLKQR GIEPLVHVTC RDRNLIGQQS HLMGLAVLGI RNVLLVTGDP SRYGELPGAT SVYDVSSMDL TKMVRRLNEG IGFSGQPLKQ PSRFVIGTAF NPHVHNFRKA VERLRRKVEA GADFVMTQPV FDPNLMAAIA EATRDLGVPV FVGIMPLTSA RNAEFLHHQV PGIRLSEQAL RRMQEAAPEE APAVGEAIAR ELVEVAIRLF PGIYLVTPFL RYEMTVRLTE YARSLEATLV SRPHGHA // ID C8X153_DESRD Unreviewed; 804 AA. AC C8X153; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 29-APR-2015, entry version 37. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACV68150.1}; GN OrderedLocusNames=Dret_0859 {ECO:0000313|EMBL:ACV68150.1}; OS Desulfohalobium retbaense (strain DSM 5692). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfohalobiaceae; Desulfohalobium. OX NCBI_TaxID=485915 {ECO:0000313|EMBL:ACV68150.1, ECO:0000313|Proteomes:UP000001052}; RN [1] {ECO:0000313|Proteomes:UP000001052} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 5692 {ECO:0000313|Proteomes:UP000001052}; 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. RN [2] {ECO:0000313|EMBL:ACV68150.1, ECO:0000313|Proteomes:UP000001052} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 5692 {ECO:0000313|EMBL:ACV68150.1, RC ECO:0000313|Proteomes:UP000001052}; RX PubMed=21304676; RA Spring S., Nolan M., Lapidus A., Glavina Del Rio T., Copeland A., RA Tice H., Cheng J.F., Lucas S., Land M., Chen F., Bruce D., Goodwin L., RA Pitluck S., Ivanova N., Mavromatis K., Mikhailova N., Pati A., RA Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., RA Munk C., Kiss H., Chain P., Han C., Brettin T., Detter J.C., RA Schuler E., Goker M., Rohde M., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Desulfohalobium retbaense type strain RT (HR(100))."; RL Stand. Genomic Sci. 2:38-48(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; CP001734; ACV68150.1; -; Genomic_DNA. DR RefSeq; WP_015751308.1; NC_013223.1. DR RefSeq; YP_003197728.1; NC_013223.1. DR STRING; 485915.Dret_0859; -. DR EnsemblBacteria; ACV68150; ACV68150; Dret_0859. DR KEGG; drt:Dret_0859; -. DR PATRIC; 21698670; VBIDesRet71890_0922. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; DRET485915:GHRJ-875-MONOMER; -. DR Proteomes; UP000001052; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001052}; KW Methyltransferase {ECO:0000313|EMBL:ACV68150.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001052}; KW Transferase {ECO:0000313|EMBL:ACV68150.1}. SQ SEQUENCE 804 AA; 84958 MW; 270094E3A83EDDD9 CRC64; MSAFRKALQG NKVLIFDGAM GTLLQSRGLV PGQSPEQFGR SNPEAVAAAH RDYLEAGADV ITTNTFGGTA YKLGTDIDVR AFNAQMAAVA RKEAGDKHFV AGSVGPTGHM VRPLGNVGFT DLVQAFRTQI RGLVEGGVDC ILAETHFDLA EAKAVVVAAR QECDLPVGVS MTFEGGCSLT GTPPHCFVDT MQNLDVDLLA TNCSAGPEQL VEVVRDMLPR LQTPLLVEPN AGLPELIDGE TVFNLGPEAF AQQMRQFVEL GVGCVGGCCG TSPDHIRALG RECPEKSAAA NSVFSPCPPV VVTSRFGSVT LGPKSPLALI GERINPTGKK DLTAELQAGE LQRACALAAE QVQAGATVLD INVGAPLVEE SQLIPELVLE LSRRQQVPLC LDSADPDAIE LGLQAAPGSP LVNSISGEEG KMERLAPLCV RYGAPFILLP LEGGALPVSA ESRLSIIQRL IDKALALGVP KRLIVVDALA LTVSSKPEAA RACLETIRAC QERWAVPSVL GLSNISFGLP ARELLNSTFL TMATGAGLSG CIANPGSVRL QEALAASEVL LGRDPQAQHF IQGYAEWTPG TGAVPARATA SGGGEEERTV LQRAVIKGET EVVTREVQEA LRQGSQPFEL VNNELIPGIM AVGEKYEKKE YFLPQLLLSA EAMQAGFELL RPLLEAAKDQ EKPKKIILAT VEGDIHDIGK NIVALLLRNH GFEVVDLGKD VPAETIVQAA EEHEAELIGL SALMTTTMVK MEQTLELVRK RGLSTQVLVG GAVVTPEYAR VIGAHGYAAD AVGAVKKAKE LVAE // ID C8X542_DESRD Unreviewed; 350 AA. AC C8X542; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACV69539.1}; GN OrderedLocusNames=Dret_2255 {ECO:0000313|EMBL:ACV69539.1}; OS Desulfohalobium retbaense (strain DSM 5692). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfohalobiaceae; Desulfohalobium. OX NCBI_TaxID=485915 {ECO:0000313|EMBL:ACV69539.1, ECO:0000313|Proteomes:UP000001052}; RN [1] {ECO:0000313|Proteomes:UP000001052} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 5692 {ECO:0000313|Proteomes:UP000001052}; 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. RN [2] {ECO:0000313|EMBL:ACV69539.1, ECO:0000313|Proteomes:UP000001052} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 5692 {ECO:0000313|EMBL:ACV69539.1, RC ECO:0000313|Proteomes:UP000001052}; RX PubMed=21304676; RA Spring S., Nolan M., Lapidus A., Glavina Del Rio T., Copeland A., RA Tice H., Cheng J.F., Lucas S., Land M., Chen F., Bruce D., Goodwin L., RA Pitluck S., Ivanova N., Mavromatis K., Mikhailova N., Pati A., RA Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., RA Munk C., Kiss H., Chain P., Han C., Brettin T., Detter J.C., RA Schuler E., Goker M., Rohde M., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Desulfohalobium retbaense type strain RT (HR(100))."; RL Stand. Genomic Sci. 2:38-48(2010). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; ACV69539.1; -; Genomic_DNA. DR RefSeq; WP_015752680.1; NC_013223.1. DR RefSeq; YP_003199117.1; NC_013223.1. DR STRING; 485915.Dret_2255; -. DR EnsemblBacteria; ACV69539; ACV69539; Dret_2255. DR KEGG; drt:Dret_2255; -. DR PATRIC; 21701646; VBIDesRet71890_2373. DR eggNOG; COG0646; -. DR HOGENOM; HOG000231636; -. DR OMA; PEGDMHD; -. DR OrthoDB; EOG6NSGDJ; -. DR BioCyc; DRET485915:GHRJ-2311-MONOMER; -. DR Proteomes; UP000001052; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001052}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ACV69539.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001052}; KW Transferase {ECO:0000313|EMBL:ACV69539.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 211 211 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 350 AA; 38382 MW; 1559A85666985188 CRC64; MHKRNLEQRL ADGPVICAEG YLFEMERRGY LQAGSFVPEV ALEHPEVLRQ LHQDFCFCGS DVAVAFTYNG HREKMRLIGK EDLLEPLNRH ALRLAKEVAD AQRPEPALVA GNISNTNVYD PDDAGSHHEA RSMFAEMAGW AVEEGADFIL AETMYYHGEA VLALEAIQEA GLPAVVTLGL MGENVLRDGW SAEASCKALE DRGATVVGMN CFRGPATMMP YLRKIRAAVQ GPVAGLPVPF RTTEDHPTFF NLPDPGNTAP LPHPTPFPTA LEPLSCNRYE LAQWAATAQN EGIKYLGLCC GATPAQIRAV AEAVGKTTPA SRYSPDMSKH FLFGDDARLR RHMTSYAEKA // ID C8X6V8_NAKMY Unreviewed; 320 AA. AC C8X6V8; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 29-APR-2015, entry version 30. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACV80856.1}; GN OrderedLocusNames=Namu_4577 {ECO:0000313|EMBL:ACV80856.1}; 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 {ECO:0000313|EMBL:ACV80856.1, ECO:0000313|Proteomes:UP000002218}; RN [1] {ECO:0000313|Proteomes:UP000002218} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700099 / DSM 44233 / JCM 9543 / Y-104 RC {ECO:0000313|Proteomes:UP000002218}; 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 ----------------------------------------------------------------------- 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; ACV80856.1; -; Genomic_DNA. DR RefSeq; WP_015749671.1; NC_013235.1. DR RefSeq; YP_003203845.1; NC_013235.1. DR STRING; 479431.Namu_4577; -. DR EnsemblBacteria; ACV80856; ACV80856; Namu_4577. DR KEGG; nml:Namu_4577; -. DR PATRIC; 22666818; VBINakMul62011_4620. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; NMUL479431:GHQL-4613-MONOMER; -. DR Proteomes; UP000002218; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002218}; KW Methyltransferase {ECO:0000313|EMBL:ACV80856.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002218}; KW Transferase {ECO:0000313|EMBL:ACV80856.1}. SQ SEQUENCE 320 AA; 32947 MW; 3BE0D0F6BBC81F59 CRC64; MTAAAGLARA MADRPLVLDG GLATLLEAHG HDLTSALWSA QLLVQNPGAI TAAHREYFRA GAQVAITASY QASLPGLAAI GLGRVEAEQA LRRSVDLART AAADGVNEAT APGSGPRWVA TSVGPYGAAL ADGSEYRGDY GLTVRQLRDW HRPRLEILAD AGGDVLAIET IPCAAEVEAL LTEIQALDAP AWLSLTCQDG RTRAGERVDE VFAMAAGVDQ VIAVGVNCVE SAEAADLVAA AAENSGKPAV VYPNSGEDWD AQARAWAGRA TFGPEHAAVW VASGARLVGG CCRVGPQAIR RLARSAPGWP AGTPGSVSSR // ID C8X8S7_NAKMY Unreviewed; 1195 AA. AC C8X8S7; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 01-APR-2015, entry version 45. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACV79132.1}; GN OrderedLocusNames=Namu_2786 {ECO:0000313|EMBL:ACV79132.1}; 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 {ECO:0000313|EMBL:ACV79132.1, ECO:0000313|Proteomes:UP000002218}; RN [1] {ECO:0000313|Proteomes:UP000002218} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700099 / DSM 44233 / JCM 9543 / Y-104 RC {ECO:0000313|Proteomes:UP000002218}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001737; ACV79132.1; -; Genomic_DNA. DR RefSeq; WP_015748011.1; NC_013235.1. DR RefSeq; YP_003202121.1; NC_013235.1. DR STRING; 479431.Namu_2786; -. DR EnsemblBacteria; ACV79132; ACV79132; Namu_2786. DR KEGG; nml:Namu_2786; -. DR PATRIC; 22663158; VBINakMul62011_2803. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; NMUL479431:GHQL-2815-MONOMER; -. DR Proteomes; UP000002218; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002218}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002218}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 236 236 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 302 302 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 746 746 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1195 AA; 129392 MW; C7220A4CDE9DB7B5 CRC64; MCYSTYSVPV TAAPRHPLLT ALSERVLVAD GAMGTMLQAQ DPSLDDFAGL EGCNEILNVT RPDIVRAVHR AYLEVGVDAI ETNTFGANLA NLAEYDIPDR IYELSRAGAA LARAEADEFS TPDHPRFVLG SVGPGTKLPT LGHAGYVTLR DAYQQEVAGL LDGGSDAIIV ETCQDLLQAK SAILAAKRAM TASGIVVPII VHVTVETTGT MLLGSEIGAA LTALEPLGVD YIGLNCATGP AEMSEHLRYL SRHATVGVSV MPNAGLPQLG PNGAVYPLSP AELAQALSGF VTEFGLGLVG GCCGTTPEHL RQVVEAVRDL RAAGRRPRRE PGLSSLYQAV PFQQDASVLM VGERTNANGS KAFREAMLAQ DWQACIEIAR AQTRDGAHVL DLNVDYVGRD GAADMASLAS RLATASTLPI MIDSTEPEVI GAGLEHLGGR SIVNSVNFED GDGPTSRYTR IMNLVAEHGA AVVALTIDEQ GQARTREHKV AIAERLIADL TGTWGMAESD IVVDCLTFPI ATGQEETRRD GIETIEAIRE LKRRHPDLHF TLGISNVSFG LNPAARQVLN SVFLAECTAA GLDSAIVHPS KILPMARIPE EQRTVALDLV WDRRREGYDP LQRVLEMFEG ATTAAGRATR AAEMAALPLD ERLQRRIIDG ERNGLEADLD EALTMRSALE IINDTLLEGM KTVGELFGSG AMQLPFVLTS AEVMKTAVAY LEPHMEKADS GGKGTIVLAT VKGDVHDIGK NLVDIILSNN GYSVVNLGIK QPIATILSAA QDSGADAIGM SGLLVKSTVI MKENLEEMNA RGIAEKYPVL LGGAALTRSY VENDLSSVFK GDVRYARDAF EGLRLMDGVM SRKRGLDPVA AAAETAKIAE RKARHERSKR IAEKRKAAAA EEEQVDVPAR SDVATDNPVP TPPFWGSRVI KGIALADYST MLDERATFMG QWGLRGSKGG QGPSYEELVE KEGRPRLRYW LDRLHTDKVL EAAVVYGYFP CVSEGDDVVV LAEPTPDAAE LCRFTFPRQR RDRHLCLSDF YRSRESARQT GQVDVIAFTV VTMGQRIADF ANELFAANAY RDYLEVHGLS VQLTEALAEF WHQRIRSELV FPDGSNAAAE DSAEIEKFFD LEYRGARYSF GYPACPDLTD QTKVMALLEP ERIGVELSEE FQLHPEQSTS ALVAHHPEAK YFAAR // ID C8ZCR5_YEAS8 Unreviewed; 324 AA. AC C8ZCR5; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 29-APR-2015, entry version 23. DE SubName: Full=Chromosome XII, EC1118_1L10 genomic scaffold, whole genome shotgun sequence {ECO:0000313|EMBL:CAY81181.1}; GN ORFNames=EC1118_1L10_0001g {ECO:0000313|EMBL:CAY81181.1}; 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 {ECO:0000313|EMBL:CAY81181.1, ECO:0000313|Proteomes:UP000000286}; RN [1] {ECO:0000313|EMBL:CAY81181.1, ECO:0000313|Proteomes:UP000000286} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Lalvin EC1118 / Prise de mousse RC {ECO:0000313|Proteomes:UP000000286}; RX PubMed=19805302; DOI=10.1073/pnas.0904673106; RA Novo M., Bigey F., Beyne E., Galeote V., Gavory F., Mallet S., RA Cambot 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; FN393078; CAY81181.1; -; Genomic_DNA. DR ProteinModelPortal; C8ZCR5; -. DR SMR; C8ZCR5; 3-313. DR OrthoDB; EOG7X9GHR; -. DR Proteomes; UP000000286; Chromosome XII, Scaffold EC1118_1L10. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000286}. SQ SEQUENCE 324 AA; 36715 MW; A77194694B6E5C14 CRC64; MKRIPIKELI VEHPGKVLIL DGGQGTELEN RGININSPVW SAAPFTSESF WEPSSQERKV VEEMYRDFMI AGANILMTIT YQANFQSISE NTSIKTLAAY KRFLDKIVSF TREFIGEERY LIGSIGPWAA HVSCEYTGDY GPHPENIDYY GFFKPQLENF NQNRDIDLIG FETIPNFHEL KAILSWDEDI ISKPFYIGLS VDDNSLLRDG TTLEEISVHI KGLGNKINKN LLLMGVNCVS FNQSALILKM LHEHLPGMPL LVYPNSGEIY NPKEKTWHRP TNKLDDWETT VKKFVDNGAR IIGGCCRTSP KDIAEIASAV DKYS // ID C8ZIA6_YEAS8 Unreviewed; 325 AA. AC C8ZIA6; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 29-APR-2015, entry version 23. DE SubName: Full=Chromosome XVI, EC1118_1P2 genomic scaffold, whole genome shotgun sequence {ECO:0000313|EMBL:CAY86687.1}; GN ORFNames=EC1118_1P2_0012g {ECO:0000313|EMBL:CAY86687.1}; 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 {ECO:0000313|EMBL:CAY86687.1, ECO:0000313|Proteomes:UP000000286}; RN [1] {ECO:0000313|EMBL:CAY86687.1, ECO:0000313|Proteomes:UP000000286} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Lalvin EC1118 / Prise de mousse RC {ECO:0000313|Proteomes:UP000000286}; RX PubMed=19805302; DOI=10.1073/pnas.0904673106; RA Novo M., Bigey F., Beyne E., Galeote V., Gavory F., Mallet S., RA Cambot 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; CAY86687.1; -; Genomic_DNA. DR ProteinModelPortal; C8ZIA6; -. DR SMR; C8ZIA6; 15-315. DR OrthoDB; EOG7X9GHR; -. DR Proteomes; UP000000286; Chromosome XVI, Scaffold EC1118_1P2. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000286}. SQ SEQUENCE 325 AA; 36669 MW; 54658C7B92A610F0 CRC64; MARLPLKQFL ADNPKKVLVL DGGQGTELEN RGIKVANPVW STIPFISESF WSDESSANRK IVKEMFNDFL NAGAEILMTT TYQTSYKSVS ENTPIRTLSE YNNLLNRIVD FSRNCIGEDK YLIGCIGPWG AHICREFTGD YGAEPENIDF YQYFKPQLEN FNKNDKLDLI GFETIPNIHE LKAILSWDES ILSRPFYIGL SVHEHGVLRD GTTMEEIAQV IKDLGDKINP NFSFLGINCV SFNQSPDILE SLHQALPNMA LLAYPNSGEV YDTEKKIWLP NSDKLNSWDT VVKQYISSGA RIIGGCCRTS PKDIQEISAA VKKYT // ID C9CS97_9RHOB Unreviewed; 349 AA. AC C9CS97; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEW60760.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEW60760.1}; GN ORFNames=SCH4B_0323 {ECO:0000313|EMBL:EEW60760.1}; OS Silicibacter sp. TrichCH4B. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Ruegeria. OX NCBI_TaxID=644076 {ECO:0000313|EMBL:EEW60760.1}; RN [1] {ECO:0000313|EMBL:EEW60760.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TrichCH4B {ECO:0000313|EMBL:EEW60760.1}; 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; GG703515; EEW60760.1; -; Genomic_DNA. DR RefSeq; WP_009175613.1; NZ_GG703515.1. DR EnsemblBacteria; EEW60760; EEW60760; SCH4B_0323. DR PATRIC; 28602019; VBISilSp32447_0237. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEW60760.1}; KW Transferase {ECO:0000313|EMBL:EEW60760.1}. SQ SEQUENCE 349 AA; 37406 MW; DA1DBA458EB0D37E CRC64; MHNFSLPKSK AFEALTRTAQ ERILILDGAM GTQIQTLGLD EEAFRGHGGH TCAYHSDHPQ KGNNDLLILT QPEAVEQIHY DFAMAGADIV ETNTFSSTTI AQADYALEDA VHDLNAEGAR VARRAMDRAT AEDGKPRWVA GAVGPTNRTA SISPDVNDPG YRAVTFDELR IAYGQQIRGL IAGGSDLILI ETIFDTLNAK AAIFACFEAF AEHGERLPIM ISGTITDASG RTLSGQTPTA FWHSVCHARP FTVGLNCALG ADAMRPHLTE LAGVAESLVC AYPNAGLPNA FGQYDEEPED TAAKVEIFAK EGLVNVVGGC CGTTPEHIRA IAEHVASYAP RQIRETANV // ID C9CXE7_9RHOB Unreviewed; 344 AA. AC C9CXE7; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 01-OCT-2014, entry version 16. DE SubName: Full=Methionine synthase I {ECO:0000313|EMBL:EEW59215.1}; GN ORFNames=SCH4B_2169 {ECO:0000313|EMBL:EEW59215.1}; OS Silicibacter sp. TrichCH4B. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Ruegeria. OX NCBI_TaxID=644076 {ECO:0000313|EMBL:EEW59215.1}; RN [1] {ECO:0000313|EMBL:EEW59215.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TrichCH4B {ECO:0000313|EMBL:EEW59215.1}; 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; EEW59215.1; -; Genomic_DNA. DR RefSeq; WP_009176408.1; NZ_GG703517.1. DR EnsemblBacteria; EEW59215; EEW59215; SCH4B_2169. DR PATRIC; 28605613; VBISilSp32447_1653. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 344 AA; 36731 MW; 50A00F1CC8AA159F CRC64; MDKSMSNSFL ELLESREVLL ADGATGTNLF NMGLQSGDAP ELWNTDEPEK IKALYKGSVD AGSDLFLTNS FGGTAARLKL HDAQGRVREL NRVAAELGRE VADKSERKIA VAGSVGPTGE IMQPVGELSH ALAVEMFHEQ ADALKEGGVD VLWLETISAP EEFAAAAEAF KLADMPWCGT MSFDTAGRTM MGVTSADLAK LVEDYDVPPL AFGANCGTGA SDILRTVLGF AAQGTERPII SKGNAGIPKY VDGHIHYDGT PELMGEYAVL ARDAGAKIIG GCCGTMPDHL RKMREALDSR PRGDRPTLEQ IVEVLGPFTS ANDGTEEGSD AGSERRGRRG RRRN // ID C9D0M7_9RHOB Unreviewed; 69 AA. AC C9D0M7; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 01-OCT-2014, entry version 18. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEW58553.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEW58553.1}; GN ORFNames=SCH4B_2883 {ECO:0000313|EMBL:EEW58553.1}; OS Silicibacter sp. TrichCH4B. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Ruegeria. OX NCBI_TaxID=644076 {ECO:0000313|EMBL:EEW58553.1}; RN [1] {ECO:0000313|EMBL:EEW58553.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TrichCH4B {ECO:0000313|EMBL:EEW58553.1}; 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; GG703518; EEW58553.1; -; Genomic_DNA. DR RefSeq; WP_009178007.1; NZ_GG703518.1. DR EnsemblBacteria; EEW58553; EEW58553; SCH4B_2883. DR PATRIC; 28607023; VBISilSp32447_2326. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEW58553.1}; KW Transferase {ECO:0000313|EMBL:EEW58553.1}. SQ SEQUENCE 69 AA; 7477 MW; D681C94DFB9E1995 CRC64; MTQPEAVEQI HYDFAMAGAD IVETNTFSST TIAQADYALE DAVHDLNAEG ARVARRATRG SGRSGRKHL // ID C9KQ22_9FIRM Unreviewed; 315 AA. AC C9KQ22; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEX68327.1}; GN ORFNames=MITSMUL_05330 {ECO:0000313|EMBL:EEX68327.1}; OS Mitsuokella multacida DSM 20544. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Mitsuokella. OX NCBI_TaxID=500635 {ECO:0000313|EMBL:EEX68327.1}; RN [1] {ECO:0000313|EMBL:EEX68327.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 20544 {ECO:0000313|EMBL:EEX68327.1}; 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., 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. {ECO:0000313|EMBL:EEX68327.1}. 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; ABWK02000020; EEX68327.1; -; Genomic_DNA. DR RefSeq; WP_005842524.1; NZ_GG697142.2. DR EnsemblBacteria; EEX68327; EEX68327; MITSMUL_05330. DR PATRIC; 37044645; VBIMitMul54707_1961. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEX68327.1}; KW Transferase {ECO:0000313|EMBL:EEX68327.1}. SQ SEQUENCE 315 AA; 34683 MW; E20520DE193888D0 CRC64; MEIMDTIARD LAKYPLLVLD GAFGTELARR GFDTNDELWS AKALFEKPEL VEAVHRDYYE AGADISTSAS YQATVEGFEK KGFTREQAKE LIVRSVRLVQ QARDAFWQQR AKRVGRPQPL AAASVGPYGA YLADGSEYRG DYGASRAELA DFHAERLAIL VSAGPDILAC ETLPLLDEAR AILDDLRRYP DAGAWISFSC KDAEHTCGGD AIADCARLLD KESQVAAIGV NCTAPQYVAD LIRNIRAHTA KPVVVYPNTG ETYDAVTKTW HGSPTPYHDF VRQWYEAGAR LIGGCCRTTP DDIRGIAAFR ASLQR // ID C9KQD5_9FIRM Unreviewed; 815 AA. AC C9KQD5; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEX67926.1}; GN ORFNames=MITSMUL_05450 {ECO:0000313|EMBL:EEX67926.1}; OS Mitsuokella multacida DSM 20544. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Mitsuokella. OX NCBI_TaxID=500635 {ECO:0000313|EMBL:EEX67926.1}; RN [1] {ECO:0000313|EMBL:EEX67926.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 20544 {ECO:0000313|EMBL:EEX67926.1}; 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., 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. {ECO:0000313|EMBL:EEX67926.1}. 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; ABWK02000023; EEX67926.1; -; Genomic_DNA. DR RefSeq; WP_005842739.1; NZ_GG697143.2. DR EnsemblBacteria; EEX67926; EEX67926; MITSMUL_05450. DR PATRIC; 37044856; VBIMitMul54707_2057. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEX67926.1}; KW Transferase {ECO:0000313|EMBL:EEX67926.1}. SQ SEQUENCE 815 AA; 86092 MW; E55A9C3BDDB20133 CRC64; MSIESLSKNI RNHVSGTTLE ELAMIHIFDG AMGTMLQAGG LEAGGCPELM NIDHPEVVRH IHEAYIEAGA TIIETNTFGA SRLKLDHYGL EDRVEELNTA AVRIAKEAAG TRAKVAGSMG PTGRFISPLG DLDFEEAYAC FKEQASALAK AGVDFFIIET CIDIQEMRAA LLASKEVAPA IPVICQLTYS DDGRTVTGTD PQSAAIILSH MGADIIGVNC SLGPEQLVPI VKTLAASCDC PISVQPNAGM PQLVDGVTHF PMGPEDFGSW GPKLLAAGAT YLGGCCGTTP AHIRALRAAL EGQAEPVREP LPKRLWLASR SRSVCVDKDL PTVLIGERIN PTGRKKLAAE IREGSLLSVK KEAVNQVKAG ARLLDVNMGV AGIDATKAMK QAVTEIAQLT DAPLAIDTSD AAALEAGLRA YPGRALINSV TAEDDRIRDF LPLAKKYGAA ILCLPITEDG VPKTAEDRLK AIEYIVGKAK ENGLNDGDFL LDALVMTVSA DKNACREVLK TLQLYRQRLG YPSTMGLSNI SFGLPNRPLI NSTFFAMCLA AGLDAPIMNP YDESMQKALK ASAALLGDDP CGLAFSQDEA NLAVPKKAAV MKTTDLPILD AIKQAVIEGE KDVIVGLVVQ ALQEGKSSNE ITEKGLTAAM TEIGEDFGSG RMFLPQVLLS AETMRAAFDK LKELIPASAE ADKGTFVIAT VKGDVHDLGK NITGALLANS GFKVIDLGKD VEADTIVETA LEQNADVVGL AALMTTTMPQ IDKVIDKLRR AGARAKVMIG GAAVTQDYAD SCGADAYAAD GVKAVKLAKQ IVGVE // ID C9KYF1_9BACE Unreviewed; 915 AA. AC C9KYF1; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 01-APR-2015, entry version 34. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEX44984.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEX44984.1}; GN Name=metH {ECO:0000313|EMBL:EEX44984.1}; GN ORFNames=BACFIN_07352 {ECO:0000313|EMBL:EEX44984.1}; OS Bacteroides finegoldii DSM 17565. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=483215 {ECO:0000313|EMBL:EEX44984.1}; RN [1] {ECO:0000313|EMBL:EEX44984.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17565 {ECO:0000313|EMBL:EEX44984.1}; 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., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEX44984.1}. 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; ABXI02000049; EEX44984.1; -; Genomic_DNA. DR PRIDE; C9KYF1; -. DR EnsemblBacteria; EEX44984; EEX44984; BACFIN_07352. DR PATRIC; 27014805; VBIBacFin117758_2487. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEX44984.1}; KW Transferase {ECO:0000313|EMBL:EEX44984.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 915 AA; 99997 MW; 9DC54358028CCA0A CRC64; MKKTISQIVS ERILILDGAM GTMIQQYNLK EEDFRGERFA HIPGQLKGNN DLLCLTRPDV IQDIHRKYLE AGADIIETNT FSSTTVSMAD YHVEEYVREM NLAAVKLARE LADEYTAKNP EKPRFVAGSV GPTNKTCSMS PDVNNPAYRA LSYDELAASY QQQMEAMLEG GVDAILIETI FDTLNAKAAI FAAGQAMKTT GVKVPVMLSV TVSDIGGRTL SGQTLDAFLA SVQHADIFSV GLNCSFGARQ LKPFLEQLAA RAPYYISAYP NAGLPNSLGK YDQTPADMAH EVKEYIHEGL VNIIGGCCGT TDAYIAEYPA LVEGAKPHIP VAKPECMWLS GLELLEVKPE INFVNVGERC NVAGSRKFLR LINEKKYDEA LSIARQQVED GALVIDVNMD DGLLDAKSEM TTFLNLIMSE PEIARVPVMI DSSKWEVIEA GLKCLQGKSV VNSISLKEGE EVFLEHARIV KQYGAAAVVM AFDEKGQADT AVRKIEVCQR AYHLLVDKVG FNPHDIIFDP NVLAVATGIE EHNNYAVDFI EATGWIKRNL PGAHISGGVS NLSFSFRGNN YIREAMHAVF LYHAIQLGMD MGIVNPGTSV LYSDIPTDVL EKIEDVVLNR RPDAAERLIE LAESLKATMN GTTGQTAVKQ DAWREDSVQE RLKYALMKGI GDYLEQDLAE ALPLYNKAVD VIEGPLMDGM NYVGELFGAG KMFLPQVVKT ARTMKKAVAI LQPIIESEKT EGTTSAGKIL LATVKGDVHD IGKNIVAVVM ACNGYDIVDL GVMVTAETIV QRAIEEKVDM IGLSGLITPS LEEMAHVAGE LEKAGLDIPL LIGGATTSKM HTALKIAPVY HAPVVHLKDA SQNAGVAARL LNPQAKAELV NELETEYRAL REKSGLLRRE TVSLEEAQKN RLNLF // ID C9L9P7_BLAHA Unreviewed; 287 AA. AC C9L9P7; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEX21393.1}; GN ORFNames=BLAHAN_06132 {ECO:0000313|EMBL:EEX21393.1}; OS Blautia hansenii DSM 20583. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Blautia. OX NCBI_TaxID=537007 {ECO:0000313|EMBL:EEX21393.1}; RN [1] {ECO:0000313|EMBL:EEX21393.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 20583 {ECO:0000313|EMBL:EEX21393.1}; 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., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEX21393.1}. 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; ABYU02000027; EEX21393.1; -; Genomic_DNA. DR RefSeq; WP_003022344.1; NZ_GG698590.1. DR EnsemblBacteria; EEX21393; EEX21393; BLAHAN_06132. DR PATRIC; 36960188; VBIBlaHan43885_2275. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EEX21393.1}; KW Transferase {ECO:0000313|EMBL:EEX21393.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 203 203 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 287 AA; 30865 MW; 497B5867DD114AD9 CRC64; MTREEFRELI GREIVILDGA TGSNLMKAGM PKGICTEKWI CENPQPLMNL QSAYQQAGSQ IVYAPTFSAN KISLANHGLE NQVHSLNKQL VEISRSAVGE NCMVAGDLTT TGKQDAEYET LLDAYKEQIE AQLEAGVDLL VAETMLGVTE PMAVLDAARE LCSLPVLCTL TVESDGSLFF GGNIYDSAEL LEEMGADAVG INCSTGPDQL LSVVENIRKR IHIPLIVKPN AGNPVIDAMG NPVYSMGAEE FARHIKRLID AGANLVGGCC GTTPAYIEQL VKLKSSF // ID C9LV24_SELS3 Unreviewed; 790 AA. AC C9LV24; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 33. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEC01231.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEC01231.1}; DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEX77258.1}; GN ORFNames=Selsp_2287 {ECO:0000313|EMBL:AEC01231.1}, GN SELSPUOL_01314 {ECO:0000313|EMBL:EEX77258.1}; OS Selenomonas sputigena (strain ATCC 35185 / DSM 20758 / VPI D19B-28). OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Selenomonas. OX NCBI_TaxID=546271 {ECO:0000313|EMBL:EEX77258.1, ECO:0000313|Proteomes:UP000011124}; RN [1] {ECO:0000313|EMBL:EEX77258.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35185 {ECO:0000313|EMBL:EEX77258.1}; 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., 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] {ECO:0000313|EMBL:AEC01231.1, ECO:0000313|Proteomes:UP000011124} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35185 {ECO:0000313|EMBL:AEC01231.1}, and RC ATCC 35185 / DSM 20758 / VPI D19B-28 RC {ECO:0000313|Proteomes:UP000011124}; 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; AEC01231.1; -; Genomic_DNA. DR EMBL; ACKP02000023; EEX77258.1; -; Genomic_DNA. DR RefSeq; WP_006192615.1; NZ_GG698597.1. DR RefSeq; YP_004414690.1; NC_015437.1. DR EnsemblBacteria; AEC01231; AEC01231; Selsp_2287. DR EnsemblBacteria; EEX77258; EEX77258; SELSPUOL_01314. DR KEGG; ssg:Selsp_2287; -. DR PATRIC; 25826612; VBISelSpu76100_1658. DR KO; K00548; -. DR BioCyc; SSPU546271:GCBU-2355-MONOMER; -. DR Proteomes; UP000003505; Unassembled WGS sequence. DR Proteomes; UP000011124; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000011124}; KW Methyltransferase {ECO:0000313|EMBL:EEX77258.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000011124}; KW Transferase {ECO:0000313|EMBL:EEX77258.1}. SQ SEQUENCE 790 AA; 84154 MW; 3691E8D9ABBB30E5 CRC64; MIHIFDGAMG TMLQEGGLKP GGCPELMNLE QPDVVQKIHE AYIEAGATMI ETNTFGASAL KLDHYGLEDR VKEINEAAVK IAREASKGRA KIVGSLGPTG RFIVPLGDLE FEDAYRAFYE QAKALADAGA DYLLFETCID IQEMRAGLLA AKDATSLPII CQLSYSEDGR TVTGTDPQTA AITLEALGAD IIGVNCSLGP KELVPIVKTL AENCSVPISV LPNAGMPRLE NGRTIFPMGP EEFASWGAKL VAAGATYLGG CCGTTPAHIK ALAAAVKDLP LTERKSPDNR LRLTSRSKTV IIDKDLATTL IGERINPTGR KKLAEEIKNG SLFSVKREAI DQVRAGARLL DVNMGVGGID QVKAMHDAIR EVSQITDAPL AIDTSDTKTL EAGLRAYPGR ALINSVSAEK ERIEEFLPLA KKYGAAILCL PITEDGVPKT AEDRINVING IIKEAKKNGL KDGDFLLDAL VMTISADQNA CLEVLNTLRL YRKHFGYPAT MGLSNISFGL PNRPLINSTF FAMCLAAGLD APIMNPYDEK MQEALMASAA LLGKDPRGID FSRNEVNLKT PKKAAEAKPI EGDVLAAIKQ AVIDGASESI AMLTERAIRE GHSSNEITEK ALTAAMNDIG IDFGAGRVFL PQVLLSAEAM RASFQKIKEL LPAQQEADKG TVVMATVKGD VHDLGKNIVS ALLSNSGFKL IDLGKDVDAD TIVRTALEKE ADIVGLSALM TTTMTQIDKV IKKLREAGSE ARVIVGGAAV TEDYATSAGA DAYANDGVSA VKIAKDFVGE // ID C9M596_9BACT Unreviewed; 808 AA. AC C9M596; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEX49264.1}; GN ORFNames=GCWU000246_00352 {ECO:0000313|EMBL:EEX49264.1}; OS Jonquetella anthropi E3_33 E1. OC Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae; OC Jonquetella. OX NCBI_TaxID=645512 {ECO:0000313|EMBL:EEX49264.1, ECO:0000313|Proteomes:UP000003290}; RN [1] {ECO:0000313|EMBL:EEX49264.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=E3_33 E1 {ECO:0000313|EMBL:EEX49264.1}; 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., 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. {ECO:0000313|EMBL:EEX49264.1}. 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; ACOO02000004; EEX49264.1; -; Genomic_DNA. DR RefSeq; WP_008520046.1; NZ_GG697147.2. DR EnsemblBacteria; EEX49264; EEX49264; GCWU000246_00352. DR PATRIC; 27566843; VBIJonAnt83004_1465. DR Proteomes; UP000003290; Unassembled WGS sequence. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000003290}; KW Methyltransferase {ECO:0000313|EMBL:EEX49264.1}; KW Transferase {ECO:0000313|EMBL:EEX49264.1}. SQ SEQUENCE 808 AA; 84453 MW; 83B31690D5653101 CRC64; MAVEFTSPSR RLTLGRDRII FDGAMGTALG SRGLRRGSLP EELNLSSPET VAAVHRSFLE AGSDFITTNT FGAFPSRLAH AGLSVGPVVR SACQIARREA ERFGGFVALD IGPSGRLMEP LGDATFDEIY QGVCEVLHAG AAYCDAVLLE TFTDLAEIRA AALAVRENCG LPLLATMSFE PSGRTFSGAS AEACSLVLSG LGASAFGTNC SAGPRALRET VRQICGACPV PVIVQPNAGL PEFSGSSVVY SAGPDEFQSV MGEFARWGVA VLGGCCGTTP DYIRRLSSLR GDVPPRSVPL GPAACSASQV VRFDMFVPVG ERINPTGKPV LADAYASRLP SPLLEDAIKQ TQEGAVMLDV NAGVPGVDEA AALSWAVQTL QEGVTCPLQL DSANPKALEA ALRACVGLPM INSASARPES LEPAIRLAKK YGVSILGLPM DETGVPERAA DRLAVAARIK ERWTAAGLAA EKLLFDPLVM AAAAGPERVS ETLNTLSALK ERLGAKTMAG ISNVSFGLPA RGAVNRTMLA ACLDRGLDAA ILNPGDLGMM DTVAVWNLLS GRDADASGYL AYCAARPEEL EPESRDALPV PEANQDDNED ELGRAVRLGL VQEARRAAAE LCKGVSAMTV VEEYLVPALD RVGDDYEAGR IFLPGLLKAA SAASAAFDEI RQALPAGSGA RDKGPIVLAT VQGDVHDIGK NIAGTVLESY GFRVIDLGKN VPAETVVRTV VENRAPLVGL SALMTATVAS MEDTVAALRR AAPGVKIIVG GAVLSRVLAR SIGADYYAAT AMETVRLAEK AIKLKERE // ID C9MVF0_9FUSO Unreviewed; 997 AA. AC C9MVF0; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 31. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEX75372.1}; GN ORFNames=GCWU000323_00621 {ECO:0000313|EMBL:EEX75372.1}; OS Leptotrichia hofstadii F0254. OC Bacteria; Fusobacteria; Fusobacteriales; Leptotrichiaceae; OC Leptotrichia. OX NCBI_TaxID=634994 {ECO:0000313|EMBL:EEX75372.1}; RN [1] {ECO:0000313|EMBL:EEX75372.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0254 {ECO:0000313|EMBL:EEX75372.1}; 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., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEX75372.1}. 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; ACVB02000007; EEX75372.1; -; Genomic_DNA. DR RefSeq; WP_006803958.1; NZ_GG700632.1. DR EnsemblBacteria; EEX75372; EEX75372; GCWU000323_00621. DR PATRIC; 29260851; VBILepHof63998_0842. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEX75372.1}; KW Transferase {ECO:0000313|EMBL:EEX75372.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 237 237 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 301 301 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 733 733 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 997 AA; 111620 MW; 3AC0784F05A7C616 CRC64; MTKNKYKNSY NLLQNDLKNK ILLLDGAMGT MIQQEKLTAN DFGGEKYEGC NDYLVLQRPD VIKNIHKRYL EAGSDIIETN SFGALDIVLK DYDLEDKVFE MNKAAAELVN EAIAEYRSEH PEVTRNLYVA GALGPSNKSI SVTGGVTFEE LIHSYYTAVS GLMAGGVDLI LFETIQDTRN LKAAYLGLKK AMEENYTVPL MLSFTIESTG TTLAGQTADA FYYAVNHMNP FSVGLNCATG PEFMTQFLKT LNNISNTYIS VYPNAGLPNE DGEYEETPDT LSAKIEPFFQ NNYLNIVGGC CGTTPEHIQK IKEKSVNYSP RVIDENKDFN DVSGLIALET PKNRPIYVGE RTNVIGSRIF KNLIASEKFD EATEVARLQI KGRADVIDIC LANPDRDEVA DMKAFLDKVA KFAKVPLMID STDINVIKEG LTYLQGKGII NSINLEDGEK KFADMAKVIK DFGASVVVGL IDEEGMAVSV EKKLKVARRS YELLTKKYGI DERDIIFDTL VFPVATGDQK YIGSATATIE AIKQIKAEMP NVKTILGVSN VSFGLPIAGR EVLNTYYMQK AYEAGLDYAI VNTEKVMPMD EISDEEKELA ENLLFHTNDE NVSKFANFYR EKKAIQKVVD TSNLTTEEKV SNLVVEGSKK DLIVYLDELL QKYSPIDIIN GPLMTGMDEV GRLFNNNDLI VAEVLQSAEV MKASVSHLEQ FMEKDESSVK GKVIMATVKG DVHDIGKNLV GIIIGNNGYE VIDLGINTPA EKIREAIIEH KADFLGLSGL LVKSATEMVN TMGVLHEAGI DIPIFVGGAA LTEKFTVNKI EPAYKNNIVI YSRDAMTALA DLNKMIDEKK FEEFKEYLQK RRELVTIKDA KKLEQLKVKP TVSDIKDADG TFDFSKVELP KYDFEKIYKP QTLNKQIITN IKAKDVFPFI NLQMLIGKHL GMKWIVNNLI EKQDPRTIKL YNEILDIIEN GDEYFDIKAI YKFFPVRRKV GERKEDF // ID C9P2V8_VIBME Unreviewed; 1203 AA. AC C9P2V8; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 34. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEX38006.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEX38006.1}; GN ORFNames=VIB_002140 {ECO:0000313|EMBL:EEX38006.1}; OS Vibrio metschnikovii CIP 69.14. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=675813 {ECO:0000313|EMBL:EEX38006.1}; RN [1] {ECO:0000313|EMBL:EEX38006.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIP 69.14 {ECO:0000313|EMBL:EEX38006.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; ACZO01000006; EEX38006.1; -; Genomic_DNA. DR RefSeq; WP_004396121.1; NZ_ACZO01000006.1. DR EnsemblBacteria; EEX38006; EEX38006; VIB_002140. DR PATRIC; 30108977; VBIVibMet139223_2349. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEX38006.1}; KW Transferase {ECO:0000313|EMBL:EEX38006.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 225 225 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 737 737 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1203 AA; 133263 MW; 6CBDCAC1A996349E CRC64; MGTMIQSYQL QEQDYRGNRF ADWHCDLKGN NDLLVLSQPS LIKEIHHAYL AAGADILETN TFNSTTIAMA DYDMQSLSAE INYVAAQLAR QVADEWTEKT PDKPRYVAGV LGPTNRTCSI SPDVNDPGYR NVSFDQLVDA YSESTRALIE GGCDLIMIET VFDTLNAKAC AFAVDCIFDE LGYALPVMIS GTITDASGRT LSGQTTEAFY HSLRHVRPLS FGLNCALGPD ELRPYVAELS RISESYVSAH PNAGLPNAFG DYDLGPEEMA EHIAEWAQAG FLNLVGGCCG TTPEHIAAMA KAVEGVVPRR LPELNVACRL SGLEPLTIAK GTLFVNVGER TNVTGSARFK RLIREELYDE ALDVAREQVA NGAQIIDINM DEGMLDAKAC MVRFLQLCAS EPEISKVPIM VDSSKWEVIE AGLKCIQGKG IVNSISLKEG KAKFIEQAKL VRRYGAAVIV MAFDEVGQAD TRERKVAICS NAYRILVDEV GFPPEDIIFD PNIFAIATGI DEHNNYAVDF IEAIADIKRD LPYAMISGGV SNVSFSFRGN NYVREAIHAV FLYHCFKHGM DMGIVNAGQL EIYDNVPVSL REAVEDVVLN RRPDATERLL EMAEQYRDNA VGKVDDPALL EWRSWPVAKR LEHALVKGIT EFIIEDTEDA RQQSSRPLDV IEGPLMDGMN VVGDLFGEGK MFLPQVVKSA RVMKQAVAYL EPYINALKQA SSANGKILLA TVKGDVHDIG KNIVGVVLQC NNYEIIDLGV MVPCEQILKV AKEQQVDIIG LSGLITPSLD EMVHVAKEME RQGFNLPLLI GGATTSKAHT AVKIEQNYRH PVVYVNNASR AVGVCSALLS DELRPAFVEK LDLDYQRTRE QHARKTPKTR PISLDKARAN KVAIDWQTYT PPTPAKPGIH VFDNCSIAVL RQYIDWTPFF MTWSLMGKYP AILQHEEVGE EAQRLFHDAN TLLDRVEREG LLQAKGICGL FPAASVGDDI EVYADETRTE VVHVLHHLRQ QTEKPKGANY CLADYIAPKS SAKRDWIGAF AVTGGIGERE LADAYKAQGD DYNAIMIQAV ADRLAEAFAE YLHDRVRKEI WGYAVEEDLA CDDLIREKYQ GIRPAPGYPA CPEHTEKGTL WQLLSVEENI GMSLTSSYAM WPGSSVSGWY FSHPDSRYFA IAQIQEDQVQ SYAERKGWDK LTAEKWLGPN ING // ID C9P5E9_VIBME Unreviewed; 299 AA. AC C9P5E9; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EEX37403.1}; GN ORFNames=VIB_001524 {ECO:0000313|EMBL:EEX37403.1}; OS Vibrio metschnikovii CIP 69.14. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=675813 {ECO:0000313|EMBL:EEX37403.1}; RN [1] {ECO:0000313|EMBL:EEX37403.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIP 69.14 {ECO:0000313|EMBL:EEX37403.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACZO01000006; EEX37403.1; -; Genomic_DNA. DR RefSeq; WP_004395506.1; NZ_ACZO01000006.1. DR EnsemblBacteria; EEX37403; EEX37403; VIB_001524. DR PATRIC; 30107579; VBIVibMet139223_1675. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EEX37403.1}; KW Transferase {ECO:0000313|EMBL:EEX37403.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 203 203 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 278 278 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 279 279 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 299 AA; 32151 MW; 091C2599F84F45AB CRC64; MSTFTLLDGG MGRELKRIGA PFSQPLWSAQ ALIESPEHVR LAHQSFIDAG ADIITVNSYA CVPFHLGEAL YRSDGARLAR LAAQIAAEVA QQAPHTVQVA GSIPPAMGSY RPDLFQAQPA QAITQTLYAA QDPYVDIWIA ETIASLEELS MIQQVLEQSS KPCYYAFTLQ DDSDVALLRS GESVGDAAQQ VAATGGAGIL FNCSVPEVMA DAISQAKSAL NGREKEIEIG VYANSFAPIK AQHAANQTVQ AMREFSAQDY VEFAQQWYGL GATVIGGCCG ITPTHIRALQ DWRQALEKS // ID C9PPY3_9PAST Unreviewed; 1232 AA. AC C9PPY3; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 32. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEX50434.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEX50434.1}; GN Name=metH {ECO:0000313|EMBL:EEX50434.1}; GN ORFNames=HMPREF0621_1057 {ECO:0000313|EMBL:EEX50434.1}; OS Pasteurella dagmatis ATCC 43325. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Pasteurella. OX NCBI_TaxID=667128 {ECO:0000313|EMBL:EEX50434.1}; RN [1] {ECO:0000313|EMBL:EEX50434.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43325 {ECO:0000313|EMBL:EEX50434.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEX50434.1}. 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; ACZR01000011; EEX50434.1; -; Genomic_DNA. DR RefSeq; WP_005764604.1; NZ_GG704813.1. DR EnsemblBacteria; EEX50434; EEX50434; HMPREF0621_1057. DR PATRIC; 25898637; VBIPasDag141287_1475. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEX50434.1}; KW Transferase {ECO:0000313|EMBL:EEX50434.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1232 AA; 136962 MW; B36D53DC60492094 CRC64; MDTILLKNQT QQLTDLLAQR ILILDGAMGT MIQKYKLTEA DFRGERFKNS PVDLRGNNDL LTLTQPLLIK AIHEKYLAAG ADIIETNTFS STTIAQADYE LQAVAYELNF AGAKLARLAA DKYSTPEKPR FVAGILGPTN RTASISPNVN DPGFRNVTFM ELVDAYAEAT RGLIEGGSDL IMIETIFDTL NAKAAAFAID QVFEELGVIL PIMISGTITD ASGRTLSGQT TEAFYNSLRH VKPLTFGLNC ALGPKELRQY VEAMSKISET YVSVHPNAGL PNAFGGYDLG AEEMAAHLKE WAEQGFVNIV GGCCGTTPEH IKAFSEAMEG IKPRQLPEIK TAMRLSGLEP LTVDEDSLFV NVGERNNVTG SAKFKKLIKE EKFAEAIEIA IQQVENGAQV IDVNMDEALL DSEKCMVRFL NIMATEPDAA KVPVMIDSSK WEVIEAGLQA VQGKAIVNSI SLKEGEEKFI QQAKLVRRYG AAVVVMAFDE VGQADTEDRK VEICTRAYRI LVDQVGFPPE DIIFDPNIFA IGTGIEEHNN YGVDFINAVG RIKQSLPHAK ISGGVSNVSF SFRGNNVMRE AIHAVFLYHA IKQGMDMGIV NAGQLAIYDD LDPEMRNIIE DAVLNRHPDA TEQLIELAEK YRNSTARQED NSVAEWRTWS VEERLKYALV KGITNHIIED TEEARLKFSS PLEVIEGPLM DGMDVVGELF GDGKMFLPQV VKSARVMKQS VAYLEPFINA TKQKGSSAGK VVIATVKGDV HDIGKNIVSV VMQCNNFEVI DLGVMVPADK IIDTAIREKA DVIALSGLIT PSLDEMEYFL GEMTRLGLNL PVMIGGATTS KEHTAIKLYP KYKHEVVYTT NASRAVTVCA ALMNPETKAE LWERMKKEYE QIQHAFANKK APRKQLPIEE ARANRFDAFA GEWADYQVPQ PKQTGIIEYK NVPIATLRKF IDWSPFFMLW GLMGGYPDAF DYPEGGEEAR RVWNDAQKVL DELEQNGKLN PSGVMGIFPA CRAGDDIEIF ANSGRTSPVG KVYNLRQQTE RGKNSKSPYN LCLSDFIADK ESGQQDWFGM FAVCAGIEEH DLVEGYKAAG DDYNAILLQA VGDRLAEAMA EYLHFELRTK VWGYSDETMD NERLIREEYI GIRPAPGYPS CPEHTEKQII WDLLEVEQRI GMKLTESYAM WPAASVCGWY FSHPASNYFT LGRIDEDQAV DYAKRKGWDE KMMLKWLSVA MK // ID C9PYM3_9BACT Unreviewed; 921 AA. AC C9PYM3; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 32. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEX52469.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEX52469.1}; GN Name=metH {ECO:0000313|EMBL:EEX52469.1}; GN ORFNames=HMPREF6745_2046 {ECO:0000313|EMBL:EEX52469.1}; OS Prevotella sp. oral taxon 472 str. F0295. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=619693 {ECO:0000313|EMBL:EEX52469.1}; RN [1] {ECO:0000313|EMBL:EEX52469.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0295 {ECO:0000313|EMBL:EEX52469.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEX52469.1}. 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; ACZS01000129; EEX52469.1; -; Genomic_DNA. DR RefSeq; WP_009235308.1; NZ_GG704824.1. DR EnsemblBacteria; EEX52469; EEX52469; HMPREF6745_2046. DR PATRIC; 29541931; VBIPreSp61738_0138. DR OrthoDB; EOG6091CH; -. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEX52469.1}; KW Transferase {ECO:0000313|EMBL:EEX52469.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 240 240 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 763 763 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 921 AA; 101460 MW; DA70C5F5727C2565 CRC64; MKIQDIIKQR IMILDGALGT MIQDYNLEEK DFRNADLAHH EGQLKGNNDV LNITRPDLIL DIHRRYLAAG ADLIETNTFS SQIISQADYQ LEHLSRPMAL AGARLARKAA DEFSTPQWPR FVCGSVGPTN KTCSMSPNVS DAAARDITYD QIFDAYREQV GALIEGGVDA ILIETIFDTL NAKAAIDATM TEMQMQGVDL PIMLSMTVSD LAGRTLSGQT IEGFLASISS YPIFSVGLNC SFGADQMKPF LKELASKAPY YISAYPNAGL PNTMGQYDET VESMSPQIAQ FINEGLVNII GGCCGTDDKF IASYAALAKG KTPHVVVSKP TSLWLSGLEM LNVTPEVNFV NVGERCNVAG SKKFLRLIKE GLYDEAISIA RKQVTDGALV LDINMDDGLL DAEKEMTTFL NMIAAEPDIA RVPIMIDSSK WEVIMAGLKC AQGKCIVNSI SLKEGEELFI EHGRALKRFG AACVVMCFDE QGQATTFERR IEIAQRAYRI LTQEVGMNPL DIIFDPNILA IATGIEEHDN YAHEFIRSIA WIRKNLPGTH ISGGVSNLSF SFRGNNYIRE AMHAVFLYHA INEGMDFGIV NPSSKITYSD IPTDELEIIE DVILNRKPNA AEALIELANK KKEEEERRKA GIASGDNSVQ KQEEEQWRSL ELDERLKYAL RKGIGDHLDE DLHLALAHFP HAVDIIEGPL MAGMNEVGEL FGAGKMFLPQ VVKTARTMKQ AVAILHPYIE KEKKVGATKA GKVILATVKG DVHDIGKNIV AVVMACNNYE VIDLGVMVPA EQIIKKAIEE KADIIGLSGL ITPSLEEMIN VAQEMEKAGL DIPIMIGGAT TSQLHVALKI APVYGGPVVW MKDASQNSLA AARLLNKNEE PAYINELNDK YESLRASYQD KQQKLLPIEE ARKNRLRLFD D // ID C9Q269_9VIBR Unreviewed; 1224 AA. AC C9Q269; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 01-APR-2015, entry version 34. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEX67555.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEX67555.1}; GN ORFNames=VCJ_000200 {ECO:0000313|EMBL:EEX67555.1}; OS Vibrio sp. RC341. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=675810 {ECO:0000313|EMBL:EEX67555.1}; RN [1] {ECO:0000313|EMBL:EEX67555.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=RC341 {ECO:0000313|EMBL:EEX67555.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; ACZT01000010; EEX67555.1; -; Genomic_DNA. DR RefSeq; WP_000453920.1; NZ_ACZT01000010.1. DR EnsemblBacteria; EEX67555; EEX67555; VCJ_000200. DR PATRIC; 25642764; VBIVibSp138932_0204. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEX67555.1}; KW Transferase {ECO:0000313|EMBL:EEX67555.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 246 246 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1224 AA; 135644 MW; 0049F4A6F672265A CRC64; MEVRQQLEQQ LKQRILLIDG GMGTMIQSYK LQEEDYRGAR FVDWHCDLKG NNDLLVLTQP QIIKEIHSAY LEAGADILET NTFNSTTIAM ADYDMQSLSA EINFAAAKLA REVADEWTAK DPSRPRYVAG VLGPTNRTCS ISPDVNDPGF RNVTFDGLVE AYSESTRALI KGGSDLILIE TIFDTLNAKA CAFAVDSVFE ELGISLPVMI SGTITDASGR TLSGQTTEAF YNALRHVRPI SFGLNCALGP DELRQYVEEL SRISECYVSA HPNAGLPNAF GEYDLSAEEM AEHIAEWAQA GFLNLVGGCC GTTPEHIAAI AKAVEGVKPR ALPDLKVECR LSGLEPLNIG PETLFVNVGE RTNVTGSARF KRLIKEEQYD EALDVAREQV ENGAQIIDIN MDEGMLDAEA CMVRFLNLCA SEPEISKVPV MVDSSKWEVI EAGLKCIQGK GIVNSISLKE GKEKFIAQAK LVRRYGAAVI VMAFDEVGQA DTRERKLEIC RRAYHILVDE VGFPPEDIIF DPNIFAVATG IDEHNNYALD FINAVADIKR ELPHAMISGG VSNVSFSFRG NNYVREAIHA VFLYHCFKHG MDMGIVNAGQ LEIYDNVPLK LREAVEDVIL NRRNDGTERL LEIAEAYREN SVGKEEDASA LEWRTWPVAK RLEHALVKGI TEFIVQDTEE ARQQASKPLE VIEGPLMDGM NVVGDLFGEG KMFLPQVVKS ARVMKQAVAY LEPFINAQKS GSTSNGKILL ATVKGDVHDI GKNIVGVVLQ CNNFEIIDLG VMVPCEQILK VAREQNVDII GLSGLITPSL DEMVHVAKEM ERQGFELPLL IGGATTSKAH TAVKIEQNYH APVVYVNNAS RAVGVCTSLL SDELRPGFIE RLDLDYERTR DQHARKTPKS RPVTLEQARA NKAAIDWASY TPPMPAKPGV HVFENIALAT LRPYIDWTPF FMTWSLMGKY PAILEHEEVG EEAKRLFHDA NALLDKVERE GLLKASGMCA LFPAASVGDD IEVYSDESRT QVAHVLYNLR QQTEKPKGAN YCLSDYVAPK ESGKRDWIGA FAVTGGIGER ALADAYKAQG DDYNAIMIQA VADRLAEAFA EYLHEKVRKE IWGYASDENL SNDELIRERY QGIRPAPGYP ACPEHTEKAT LWQMLNVEES IGMSLTTSYA MWPGASVSGW YFSHPDSRYF AVAQIQQDQL HSYAERKGWS LQEAEKWLAP NLDA // ID C9QC35_VIBOR Unreviewed; 1226 AA. AC C9QC35; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 37. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EGU52270.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGU52270.1}; GN Name=metH {ECO:0000313|EMBL:EGU52270.1}; GN ORFNames=VIOR3934_09400 {ECO:0000313|EMBL:EGU52270.1}; OS Vibrio orientalis CIP 102891 = ATCC 33934. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=675816 {ECO:0000313|EMBL:EGU52270.1, ECO:0000313|Proteomes:UP000002817}; RN [1] {ECO:0000313|EMBL:EGU52270.1, ECO:0000313|Proteomes:UP000002817} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIP 102891 {ECO:0000313|EMBL:EGU52270.1}; 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. {ECO:0000313|EMBL:EGU52270.1}. 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; AFWH01000013; EGU52270.1; -; Genomic_DNA. DR RefSeq; WP_004409802.1; NZ_AFWH01000013.1. DR EnsemblBacteria; EEX95231; EEX95231; VIA_000149. DR EnsemblBacteria; EGU52270; EGU52270; VIOR3934_09400. DR PATRIC; 35987017; VBIVibOri138666_0150. DR Proteomes; UP000002817; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002817}; KW Methyltransferase {ECO:0000313|EMBL:EGU52270.1}; KW Transferase {ECO:0000313|EMBL:EGU52270.1}. SQ SEQUENCE 1226 AA; 136512 MW; 17B88189D7F31A70 CRC64; MGSNVRQQIE AQLKQRILLI DGGMGTMIQD YKLEEHDYRS ERFADWHCDL KGNNDLLVLS QPKLIKDIHL EYLEAGADIL ETNTFNATTI AMADYDMESL SEEINFAAAK LARQAADEWT AKTPDKPRYV AGVLGPTNRT CSISPDVNDP GYRNVSFDEL VTAYSESTRA LIKGGSDLIL IETIFDTLNA KACAFAVDSV FEELGIALPV MISGTITDAS GRTLSGQTTE AFYNSLRHVQ PISFGLNCAL GPDELRPYVE ELSRISESFV SAHPNAGLPN AFGEYDLSPQ DMAIHVKEWA ESGFLNLIGG CCGTTPEHIR HMAEAVKDVI PRVLPELTVA CRLSGLEPLT IEKESLFINV GERTNVTGSA RFKRLIKEEL YDEALDVARQ QVENGAQIID INMDEGMLDA EACMVRFLNL CASEPEISKV PIMVDSSKWE VIEAGLKCIQ GKGIVNSISL KEGKEKFVEQ AKLIRRYGAA VIVMAFDEVG QAETRERKLQ ICTNAYNILV DEVGFPPEDV IFDPNIFAVA TGIEEHNNYA VDFIEAVADI KRDLPHAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK NGMDMGIVNA GQLEIYDNVP DKLREAVEDV VLNRRDDSTE RLLDIAAEYA GKGVGKEEDA SALEWRTWPV EKRLEHALVK GITEFIVDDT EEARVNASKP LEVIEGPLMD GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AHLEPYINKE KQAGSSNGKI LLATVKGDVH DIGKNIVGVV LQCNNYEIID LGVMVPCEKI LKVAKEENVD IIGLSGLITP SLDEMVHVAK EMERLDFDLP LLIGGATTSK AHTAVKIEQN YSKPVVYVNN ASRAVGVCTS LLSDELRPAF VEKLDVDYER VRDQHNRKKP RTKPVTLEQA RANKVDIDWD NYTPPVPVKP GVHVFDDFDI ATLRNYIDWT PFFMTWSLVG KYPKIFEHEE VGEEAKRLFN DANELLDRVE KEGLMQARGM CALFPAASVG DDIEVYTDES RTEVAKLLCN LRQQTEKPKG FNYCLSDYIA PKESGKKDWI GAFAVTGGIN ERELADEYKA QGDDYNAIMI QAVADRLAEA FAECLHERVR KEIWGYAADE NLSNDELIRE KYQGIRPAPG YPACPEHTEK GPLWELMKVE ETIGMTLTSS YAMYPGASVS GWYFSHPDSR YFAIAQIQQD QVKSYADRKG WDMLEAEKWL GPNING // ID C9QGC6_VIBOR Unreviewed; 299 AA. AC C9QGC6; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGU53060.1}; GN ORFNames=VIOR3934_05564 {ECO:0000313|EMBL:EGU53060.1}; OS Vibrio orientalis CIP 102891 = ATCC 33934. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=675816 {ECO:0000313|EMBL:EGU53060.1, ECO:0000313|Proteomes:UP000002817}; RN [1] {ECO:0000313|EMBL:EGU53060.1, ECO:0000313|Proteomes:UP000002817} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIP 102891 {ECO:0000313|EMBL:EGU53060.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGU53060.1}. 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; AFWH01000010; EGU53060.1; -; Genomic_DNA. DR RefSeq; WP_004412869.1; NZ_AFWH01000010.1. DR EnsemblBacteria; EEX94808; EEX94808; VIA_001970. DR EnsemblBacteria; EGU53060; EGU53060; VIOR3934_05564. DR PATRIC; 35990749; VBIVibOri138666_1987. DR Proteomes; UP000002817; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002817}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EGU53060.1}; KW Transferase {ECO:0000313|EMBL:EGU53060.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 204 204 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 279 279 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 280 280 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 299 AA; 32637 MW; 140A03452E5A64A8 CRC64; MNKLTILDGG MGRELKRMGA PFSQPLWSAQ ALIESPEIVA LAHKNFIHAG AEIIIANSYA CVPFHLGQEL YESDGARLAK EAAILAHDAA VQTEQRVKVA GALPPAFGSY RPDLFNAVEG EKIFRTLFEA QDPYVDIWLA ETISSIEEFD VIQSILSQTA KTCYYAFSLQ DAPSNTASIR SGQSVREATK RVCESGGQGV YFNCSVPEVM AQAIQEAKQV IDELNAEVEI GVYANNFAPI GSDHEANDTI QTMRELSPQD YLAYSKQWHQ LGATTIGGCC GIGPEHIQAL SDWKLSQYG // ID C9RQ92_FIBSS Unreviewed; 1217 AA. AC C9RQ92; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 51. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:ADL26256.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADL26256.1}; GN Name=metH {ECO:0000313|EMBL:ADL26256.1}; GN OrderedLocusNames=FSU_1627 {ECO:0000313|EMBL:ADL26256.1}; OS Fibrobacter succinogenes (strain ATCC 19169 / S85). OC Bacteria; Fibrobacteres; Fibrobacterales; Fibrobacteraceae; OC Fibrobacter. OX NCBI_TaxID=59374 {ECO:0000313|EMBL:ADL26256.1, ECO:0000313|Proteomes:UP000000517}; RN [1] {ECO:0000313|Proteomes:UP000000517} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19169 / S85 {ECO:0000313|Proteomes:UP000000517}; 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002158; ADL26256.1; -; Genomic_DNA. DR RefSeq; WP_014545890.1; NC_017448.1. DR RefSeq; YP_003249251.1; NC_013410.1. DR RefSeq; YP_005821604.1; NC_017448.1. DR STRING; 59374.Fisuc_1165; -. DR EnsemblBacteria; ACX74769; ACX74769; Fisuc_1165. DR EnsemblBacteria; ADL26256; ADL26256; FSU_1627. DR KEGG; fsc:FSU_1627; -. DR KEGG; fsu:Fisuc_1165; -. DR PATRIC; 32142101; VBIFibSuc28982_1144. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR Proteomes; UP000000517; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000517}; KW Methyltransferase {ECO:0000313|EMBL:ADL26256.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000517}; KW Transferase {ECO:0000313|EMBL:ADL26256.1}. SQ SEQUENCE 1217 AA; 133046 MW; 97DF0BF70041AF59 CRC64; MTLREAFESK MMLLDGGMGS VIQTYGIKGA NNDMLSIEKP EIILDIQRRY VDAGVDCLTT NTFSSQRVSQ HEYHQEHRIA EMNRASVKIA KQAAEEGFKK YGRKVYILGD VGPTSKMLSM SEDVNDPASR AITFDELEDA YLEQISVLME EGVDAILIET IFDTLNAKAA LSAYSKANDA RIEAAKAAGT PEAEIKPIEV MLSMTVSDAS GRTLSGQTVE AFAVSVMHMH PLSIGLNCGL GADGMVPYLR RMGAIAPCYL SCHPNAGLPN QFGGYDDTPE DMVRLMRVYL DDKLVNMIGG CCGTTPEHIA AMRQMLDALP ADYKRREPAP KYVTSPRLRL AGLEPLFREQ VRPSNGADSC NADDFVKVGE RCNVAGSKKF LRLINEKNYE EALDIARKQV DDGADVIDVN MDDGLLDATA EMRTFLNLIA SDPAVSRVPI MVDSSRFEVI EEGLKCIQGK SIVNSISLKM GEKAFIEHAL TVKRLGAAVI VMLFDEEGQA TNYERRVQIA SRAYDIMVKQ LHFDPSDIIY DPNVLTVATG MAEHNAYAID FIRAVRWIMD NLPGVRISGG LSNLSFAFRG NNYLREAMHT TFLHYAIPNG MGMAIMNPSA IIKYKTIPLE LRMAITEVIF NTEPEASEEL IEIASRMTAA QAKAKETGAK YDPKAIFAVS TGAGSATSDA NEKAADAKPT TPEERLQEAL LKGTSTTLQP DLMELINRGD SPVGIISGPL MDGMNEVGRR FGEGKMFLPQ VVKTARTMKK AVEILQPYIE AGKDANASSR GKIVIATVKG DVHDIGKNIV SVIMACNGYD MVDLGVMVPE DVIVKAAIEN KADILSLSGL ITPSLEEMCT VAKAMQAAGQ RIPIIVGGAT TSPTHTAVKI APCYDGPVFH VRDAASNPGL AQKLLDPATR EQTIQENREE QQRIRDKQNG IKTEAANAMA AAASTPEERR FQYDWSKYQP VQPPFMGESK LPPIPIEKII PLISWEYFFF TWKIKPDEEE AKKLKADAEA LIKSLTKPEY ALRAVQAFYP AAGTEKSVIF NTGRTGTDAD LIEVLTARQQ NPEGTCLSLC DYVAPANANT ASVFASPAGK DVFRDIVGAF AVTMSDTFVK RLEKLKAEQG GSDYDVLLMQ TVADRLAEAG AEYLSQELDR TSGWKGIRPA VGYPVLPNIK EIFNVAKLID FKSVGISLTE NGAMYPQASV SGLYISHPEI DYFQVKL // ID C9SAQ6_VERA1 Unreviewed; 355 AA. AC C9SAQ6; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 07-JAN-2015, entry version 24. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEY16345.1}; GN ORFNames=VDBG_02454 {ECO:0000313|EMBL:EEY16345.1}; OS Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136) OS (Verticillium wilt of alfalfa) (Verticillium albo-atrum). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Hypocreomycetidae; Glomerellales; OC Plectosphaerellaceae; mitosporic Plectosphaerellaceae; Verticillium. OX NCBI_TaxID=526221 {ECO:0000313|Proteomes:UP000008698}; RN [1] {ECO:0000313|Proteomes:UP000008698} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136 RC {ECO:0000313|Proteomes:UP000008698}; RX PubMed=21829347; DOI=10.1371/journal.ppat.1002137; RA Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E., RA Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J., RA Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., RA Santhanam P., Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., RA Inderbitzin P., Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., RA Galagan J., Cuomo C.A., Dobinson K.F., Ma L.-J.; RT "Comparative genomics yields insights into niche adaptation of plant RT vascular wilt pathogens."; RL PLoS Pathog. 7:E1002137-E1002137(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; DS985215; EEY16345.1; -; Genomic_DNA. DR RefSeq; XP_003008266.1; XM_003008220.1. DR GeneID; 9533960; -. DR KEGG; val:VDBG_02454; -. DR KO; K00547; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000008698; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008698}; KW Methyltransferase {ECO:0000313|EMBL:EEY16345.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008698}; KW Transferase {ECO:0000313|EMBL:EEY16345.1}. SQ SEQUENCE 355 AA; 38265 MW; FF9BDDC0E53B291E CRC64; MSSSASNKVL ILDGGLGTSL GDKYGVRFDK STPLWSSHML VSDQDTLLAC QKDFGDVPVD IILTATYQFS IHGFANTRTA QFPDGIDRTK IASYARDAIA IAHSAGKENG GQVALSVGPY GACMIPGQEY TGKYDLEHDT PEDLAAWHLE RFRIFEEAGG FSSPVSYIAV ETMPRLDEIV AARKALDDLG AKAANTPFWI ACVFPGEEMA LPDGASISSA VDAMLNPAVA RSQPWGIGIN CTKIWKLKEL IAHFEAAVAD QVQAGHVNEA PALVLYPDGT DGEVYNTTTQ TWELPAGGKV QGAPWEEQLA EIVRDANTRG KWKQIVVGGC CKASHAHLAR LRDCVLNNNE QAKNE // ID C9U7C5_BRUAO Unreviewed; 1261 AA. AC C9U7C5; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 37. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEX62974.1}; GN ORFNames=BAAG_02388 {ECO:0000313|EMBL:EEX62974.1}; OS Brucella abortus bv. 6 str. 870. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520454 {ECO:0000313|EMBL:EEX62974.1}; RN [1] {ECO:0000313|EMBL:EEX62974.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=870 {ECO:0000313|EMBL:EEX62974.1}; 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 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; DS999867; EEX62974.1; -; Genomic_DNA. DR RefSeq; WP_002965438.1; NZ_DS999867.1. DR ProteinModelPortal; C9U7C5; -. DR SMR; C9U7C5; 673-921. DR EnsemblBacteria; AIJ63724; AIJ63724; DO74_1679. DR EnsemblBacteria; EEX62974; EEX62974; BAAG_02388. DR GeneID; 3786978; -. DR PATRIC; 24190182; VBIBruAbo118911_1666. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; SQ SEQUENCE 1261 AA; 138652 MW; B65506A5F8F0B796 CRC64; MASSLDDLFG ATAAKPDGSE VLAALTQAAR ERILILDGAM GTQIQGLGFH EEHFRGDRFA TCDCQLQGNN DLLTLTQPKA IEEIHYAYAM AGADILETNT FSSTSIAQAD YGMEAMVYDL NRDGARLARR AALRAEQKDG RRRFVAGALG PTNRTASLSP DVNNPGFRAV TFDDLRIAYS EQIRGLIDGG SDIILIETIF DTLNAKAAVF ATEEVFAEKG VRLPVMISGT ITDLSGRTLS GQTPTAFWYS LRHARPFTIG LNCALGANAM RAHLDELSGI ADTFICAYPN AGLPNEFGQY DETPEAMAAQ IEGFARDGLV NVVGGCCGST PDHIRAIAQA VAKYEPRKPA KVPPLMRLSG LEPFTLTKDI PFVNIGERTN VTGSARFRKL VKAGDFAAAL DVARDQVANG AQIIDINMDE GLIDSEKAMV EFLNLIAAEP DIARVPIMLD SSKWEVIEAG LKCVQGKAVV NSISLKEGEE AFLHHARLVR AYGAAVVIMA FDETGQADTQ ARKIEICTRA YKILTEQVGF PPEDIIFDPN IFAVATGIEE HNNYGVDFIE ATREIVRTLP HVHISGGVSN LSFSFRGNEP VREAMHAVFL YHAIQAGMDM GIVNAGQLAV YDTIDAELRE ACEDVVLNRP TKTGESATER LLEIAERFRD SGSREARTQD LSWREWPVEK RLEHALVNGI TEYIEADTEE ARLAAERPLH VIEGPLMAGM NVVGDLFGSG KMFLPQVVKS ARVMKQAVAV LLPFMEEEKR LNGGEGRQSA GKVLMATVKG DVHDIGKNIV GVVLACNNYE IIDLGVMVPS QKILQVARDE KVDIIGLSGL ITPSLDEMAH VAAEMEREGF DIPLLIGGAT TSRVHTAVKI HSRYERGQAV YVVDASRAVG VVSNLLSPEG KQAYIDGLRN EYAKVAAAHA RNEAEKQRLP IARARANPHQ LDWENYEPVK PAFTGTKVFE TYDLAEIARY IDWTPFFQTW ELRGRYPAIL EDEKQGEAAR QLWADAQAML RKIIDEKWFT PRAVVGFWPA NAVGDDIRLF TDESRKEELA TLFTLRQQLT KRDGRPNVAM ADFVAPVESG KQDYVGGFVV TAGIGEIAIA ERFERANDDY SAILVKALAD RFAEAFAELM HERVRKEFWA YAPDEAFTPE ELISEPYKGI RPAPGYPAQP DHTEKTTLFR LLDATANTGV ELTESYAMWP GSSVSGLYIG HPESYYFGVA KVERDQVEDY ARRKDMDVEA VERWLTPILN YVPGASKDEA A // ID C9UGJ9_BRUAO Unreviewed; 1261 AA. AC C9UGJ9; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 37. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEX56527.1}; GN ORFNames=BABG_02384 {ECO:0000313|EMBL:EEX56527.1}; OS Brucella abortus bv. 4 str. 292. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520452 {ECO:0000313|EMBL:EEX56527.1, ECO:0000313|Proteomes:UP000003810}; RN [1] {ECO:0000313|EMBL:EEX56527.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=292 {ECO:0000313|EMBL:EEX56527.1}; 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 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; DS999879; EEX56527.1; -; Genomic_DNA. DR RefSeq; WP_002965438.1; NZ_JMSB01000021.1. DR ProteinModelPortal; C9UGJ9; -. DR SMR; C9UGJ9; 673-921. DR EnsemblBacteria; EEX56527; EEX56527; BABG_02384. DR EnsemblBacteria; KFJ59588; KFJ59588; DK59_2479. DR GeneID; 3786978; -. DR PATRIC; 24183187; VBIBruAbo93713_2144. DR Proteomes; UP000003810; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000003810}. SQ SEQUENCE 1261 AA; 138652 MW; B65506A5F8F0B796 CRC64; MASSLDDLFG ATAAKPDGSE VLAALTQAAR ERILILDGAM GTQIQGLGFH EEHFRGDRFA TCDCQLQGNN DLLTLTQPKA IEEIHYAYAM AGADILETNT FSSTSIAQAD YGMEAMVYDL NRDGARLARR AALRAEQKDG RRRFVAGALG PTNRTASLSP DVNNPGFRAV TFDDLRIAYS EQIRGLIDGG SDIILIETIF DTLNAKAAVF ATEEVFAEKG VRLPVMISGT ITDLSGRTLS GQTPTAFWYS LRHARPFTIG LNCALGANAM RAHLDELSGI ADTFICAYPN AGLPNEFGQY DETPEAMAAQ IEGFARDGLV NVVGGCCGST PDHIRAIAQA VAKYEPRKPA KVPPLMRLSG LEPFTLTKDI PFVNIGERTN VTGSARFRKL VKAGDFAAAL DVARDQVANG AQIIDINMDE GLIDSEKAMV EFLNLIAAEP DIARVPIMLD SSKWEVIEAG LKCVQGKAVV NSISLKEGEE AFLHHARLVR AYGAAVVIMA FDETGQADTQ ARKIEICTRA YKILTEQVGF PPEDIIFDPN IFAVATGIEE HNNYGVDFIE ATREIVRTLP HVHISGGVSN LSFSFRGNEP VREAMHAVFL YHAIQAGMDM GIVNAGQLAV YDTIDAELRE ACEDVVLNRP TKTGESATER LLEIAERFRD SGSREARTQD LSWREWPVEK RLEHALVNGI TEYIEADTEE ARLAAERPLH VIEGPLMAGM NVVGDLFGSG KMFLPQVVKS ARVMKQAVAV LLPFMEEEKR LNGGEGRQSA GKVLMATVKG DVHDIGKNIV GVVLACNNYE IIDLGVMVPS QKILQVARDE KVDIIGLSGL ITPSLDEMAH VAAEMEREGF DIPLLIGGAT TSRVHTAVKI HSRYERGQAV YVVDASRAVG VVSNLLSPEG KQAYIDGLRN EYAKVAAAHA RNEAEKQRLP IARARANPHQ LDWENYEPVK PAFTGTKVFE TYDLAEIARY IDWTPFFQTW ELRGRYPAIL EDEKQGEAAR QLWADAQAML RKIIDEKWFT PRAVVGFWPA NAVGDDIRLF TDESRKEELA TLFTLRQQLT KRDGRPNVAM ADFVAPVESG KQDYVGGFVV TAGIGEIAIA ERFERANDDY SAILVKALAD RFAEAFAELM HERVRKEFWA YAPDEAFTPE ELISEPYKGI RPAPGYPAQP DHTEKTTLFR LLDATANTGV ELTESYAMWP GSSVSGLYIG HPESYYFGVA KVERDQVEDY ARRKDMDVEA VERWLTPILN YVPGASKDEA A // ID C9UQU0_BRUAO Unreviewed; 1261 AA. AC C9UQU0; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 35. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEX83789.1}; GN ORFNames=BACG_02411 {ECO:0000313|EMBL:EEX83789.1}; OS Brucella abortus bv. 3 str. Tulya. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520451 {ECO:0000313|EMBL:EEX83789.1}; RN [1] {ECO:0000313|EMBL:EEX83789.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tulya {ECO:0000313|EMBL:EEX83789.1}; 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 abortus bv. 3 str. Tulya."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; DS999890; EEX83789.1; -; Genomic_DNA. DR RefSeq; WP_002965438.1; NZ_DS999890.1. DR ProteinModelPortal; C9UQU0; -. DR SMR; C9UQU0; 673-921. DR EnsemblBacteria; EEX83789; EEX83789; BACG_02411. DR GeneID; 3786978; -. DR PATRIC; 24176065; VBIBruAbo20544_2190. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 263 263 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 326 326 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 327 327 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 783 783 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1261 AA; 138652 MW; B65506A5F8F0B796 CRC64; MASSLDDLFG ATAAKPDGSE VLAALTQAAR ERILILDGAM GTQIQGLGFH EEHFRGDRFA TCDCQLQGNN DLLTLTQPKA IEEIHYAYAM AGADILETNT FSSTSIAQAD YGMEAMVYDL NRDGARLARR AALRAEQKDG RRRFVAGALG PTNRTASLSP DVNNPGFRAV TFDDLRIAYS EQIRGLIDGG SDIILIETIF DTLNAKAAVF ATEEVFAEKG VRLPVMISGT ITDLSGRTLS GQTPTAFWYS LRHARPFTIG LNCALGANAM RAHLDELSGI ADTFICAYPN AGLPNEFGQY DETPEAMAAQ IEGFARDGLV NVVGGCCGST PDHIRAIAQA VAKYEPRKPA KVPPLMRLSG LEPFTLTKDI PFVNIGERTN VTGSARFRKL VKAGDFAAAL DVARDQVANG AQIIDINMDE GLIDSEKAMV EFLNLIAAEP DIARVPIMLD SSKWEVIEAG LKCVQGKAVV NSISLKEGEE AFLHHARLVR AYGAAVVIMA FDETGQADTQ ARKIEICTRA YKILTEQVGF PPEDIIFDPN IFAVATGIEE HNNYGVDFIE ATREIVRTLP HVHISGGVSN LSFSFRGNEP VREAMHAVFL YHAIQAGMDM GIVNAGQLAV YDTIDAELRE ACEDVVLNRP TKTGESATER LLEIAERFRD SGSREARTQD LSWREWPVEK RLEHALVNGI TEYIEADTEE ARLAAERPLH VIEGPLMAGM NVVGDLFGSG KMFLPQVVKS ARVMKQAVAV LLPFMEEEKR LNGGEGRQSA GKVLMATVKG DVHDIGKNIV GVVLACNNYE IIDLGVMVPS QKILQVARDE KVDIIGLSGL ITPSLDEMAH VAAEMEREGF DIPLLIGGAT TSRVHTAVKI HSRYERGQAV YVVDASRAVG VVSNLLSPEG KQAYIDGLRN EYAKVAAAHA RNEAEKQRLP IARARANPHQ LDWENYEPVK PAFTGTKVFE TYDLAEIARY IDWTPFFQTW ELRGRYPAIL EDEKQGEAAR QLWADAQAML RKIIDEKWFT PRAVVGFWPA NAVGDDIRLF TDESRKEELA TLFTLRQQLT KRDGRPNVAM ADFVAPVESG KQDYVGGFVV TAGIGEIAIA ERFERANDDY SAILVKALAD RFAEAFAELM HERVRKEFWA YAPDEAFTPE ELISEPYKGI RPAPGYPAQP DHTEKTTLFR LLDATANTGV ELTESYAMWP GSSVSGLYIG HPESYYFGVA KVERDQVEDY ARRKDMDVEA VERWLTPILN YVPGASKDEA A // ID C9V867_BRUNE Unreviewed; 1261 AA. AC C9V867; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 35. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEY03779.1}; GN ORFNames=BANG_00490 {ECO:0000313|EMBL:EEY03779.1}; OS Brucella neotomae 5K33. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520456 {ECO:0000313|EMBL:EEY03779.1, ECO:0000313|Proteomes:UP000005727}; RN [1] {ECO:0000313|EMBL:EEY03779.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=5K33 {ECO:0000313|EMBL:EEY03779.1}; 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 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; EQ999582; EEY03779.1; -; Genomic_DNA. DR RefSeq; WP_004687894.1; NZ_KN046827.1. DR EnsemblBacteria; EEY03779; EEY03779; BANG_00490. DR EnsemblBacteria; KFJ56113; KFJ56113; DK64_1246. DR PATRIC; 24245207; VBIBruNeo114381_1343. DR Proteomes; UP000005727; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005727}. SQ SEQUENCE 1261 AA; 138640 MW; F6BF48DC1F9E7D87 CRC64; MASSLDDLFG ATAAKPDGSE VLAALTQAAR ERILILDGAM GTQIQGLGFH EEHFRGDRFA TCDCQLQGNN DLLTLTQPKA IEEIHYAYAM AGADILETNT FSSTSIAQAD YGMEAMVYDL NRDGARLARR AALRAEQKDG RRRFVAGALG PTNRTASLSP DVNNPGFRAV TFDDLRIAYS EQIRGLIDGG SDIILIETIF DTLNAKAAVF ATEEVFAEKG VRLPVMISGT ITDLSGRTLS GQTSTAFWYS LRHARPFTIG LNCALGANAM RAHLDELSGI ADTFICAYPN AGLPNEFGQY DETPEAMAAQ IEGFARDGLV NVVGGCCGST PDHIRAIAQA VAKYEPRKPA KVPPLMRLSG LEPFTLTKDI PFVNIGERTN VTGSARFRKL VKAGDFAAAL DVARDQVANG AQIIDINMDE GLIDSEKAMV EFLNLIAAEP DIARVPIMLD SSKWEVIEAG LKCVQGKAVV NSISLKEGEE AFLHHARLVR AYGAAVVIMA FDETGQADTQ ARKIEICTRA YKILTEQVGF PPEDIIFDPN IFAVATGIEE HNNYGVDFIE ATREIVRTLP HVHISGGVSN LSFSFRGNEP VREAMHAVFL YHAIQAGMDM GIVNAGQLAV YDTIDAELRE ACEDVVLNRP TKTGESATER LLEIAERFRD SGSREARTQD LSWREWPVEK RLEHALVNGI TEYIEADTEE ARLAAERPLH VIEGPLMAGL NVVGDLFGSG KMFLPQVVKS ARVMKQAVAV LLPFMEEEKR LNGGEGRQSA GKVLMATVKG DVHDIGKNIV GVVLACNNYE IIDLGVMVPS QKILQVARDE KVDIIGLSGL ITPSLDEMAH VAAEMEREGF DIPLLIGGAT TSRVHTAVKI HSRYERGQAV YVVDASRAVG VVSNLLSPEG KQAYIDGLRN EYAKVAAAHA RNEAEKQRLP IARARANPHQ LDWENYEPVK PAFTGTKVFE TYDLAEIARY IDWTPFFQTW ELRGRYPAIL EDEKQGEAAR QLWADAQAML RKIIDEKWFT PRAVVGFWPA NAVGDDIRLF TDESRKEELA TLFTLRQQLT KRDGRPNVAM ADFVAPVESG KQDYVGGFVV TAGIGEIAIA ERFERANDDY SAILVKALAD RFAEAFAELM HERVRKEFWA YAPDEAFTPE ELISELYKGI RPAPGYPAQP DHTEKTTLFR LLDATANTGV ELTESYAMWP GSSVSGLYIG HPESYYFGVA KVERDQVEDY ARRKDMDVEA VERWLTPILN YVPGASKDEA A // ID C9VVT4_BRUAO Unreviewed; 1261 AA. AC C9VVT4; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 37. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEX81662.1}; GN ORFNames=BARG_02351 {ECO:0000313|EMBL:EEX81662.1}; OS Brucella abortus bv. 9 str. C68. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520455 {ECO:0000313|EMBL:EEX81662.1}; RN [1] {ECO:0000313|EMBL:EEX81662.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C68 {ECO:0000313|EMBL:EEX81662.1}; 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 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; EQ999642; EEX81662.1; -; Genomic_DNA. DR RefSeq; WP_002965438.1; NZ_EQ999642.1. DR ProteinModelPortal; C9VVT4; -. DR SMR; C9VVT4; 673-921. DR EnsemblBacteria; AIJ61854; AIJ61854; DK53_198. DR EnsemblBacteria; EEX81662; EEX81662; BARG_02351. DR GeneID; 3786978; -. DR PATRIC; 24199563; VBIBruAbo122389_3305. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; SQ SEQUENCE 1261 AA; 138652 MW; B65506A5F8F0B796 CRC64; MASSLDDLFG ATAAKPDGSE VLAALTQAAR ERILILDGAM GTQIQGLGFH EEHFRGDRFA TCDCQLQGNN DLLTLTQPKA IEEIHYAYAM AGADILETNT FSSTSIAQAD YGMEAMVYDL NRDGARLARR AALRAEQKDG RRRFVAGALG PTNRTASLSP DVNNPGFRAV TFDDLRIAYS EQIRGLIDGG SDIILIETIF DTLNAKAAVF ATEEVFAEKG VRLPVMISGT ITDLSGRTLS GQTPTAFWYS LRHARPFTIG LNCALGANAM RAHLDELSGI ADTFICAYPN AGLPNEFGQY DETPEAMAAQ IEGFARDGLV NVVGGCCGST PDHIRAIAQA VAKYEPRKPA KVPPLMRLSG LEPFTLTKDI PFVNIGERTN VTGSARFRKL VKAGDFAAAL DVARDQVANG AQIIDINMDE GLIDSEKAMV EFLNLIAAEP DIARVPIMLD SSKWEVIEAG LKCVQGKAVV NSISLKEGEE AFLHHARLVR AYGAAVVIMA FDETGQADTQ ARKIEICTRA YKILTEQVGF PPEDIIFDPN IFAVATGIEE HNNYGVDFIE ATREIVRTLP HVHISGGVSN LSFSFRGNEP VREAMHAVFL YHAIQAGMDM GIVNAGQLAV YDTIDAELRE ACEDVVLNRP TKTGESATER LLEIAERFRD SGSREARTQD LSWREWPVEK RLEHALVNGI TEYIEADTEE ARLAAERPLH VIEGPLMAGM NVVGDLFGSG KMFLPQVVKS ARVMKQAVAV LLPFMEEEKR LNGGEGRQSA GKVLMATVKG DVHDIGKNIV GVVLACNNYE IIDLGVMVPS QKILQVARDE KVDIIGLSGL ITPSLDEMAH VAAEMEREGF DIPLLIGGAT TSRVHTAVKI HSRYERGQAV YVVDASRAVG VVSNLLSPEG KQAYIDGLRN EYAKVAAAHA RNEAEKQRLP IARARANPHQ LDWENYEPVK PAFTGTKVFE TYDLAEIARY IDWTPFFQTW ELRGRYPAIL EDEKQGEAAR QLWADAQAML RKIIDEKWFT PRAVVGFWPA NAVGDDIRLF TDESRKEELA TLFTLRQQLT KRDGRPNVAM ADFVAPVESG KQDYVGGFVV TAGIGEIAIA ERFERANDDY SAILVKALAD RFAEAFAELM HERVRKEFWA YAPDEAFTPE ELISEPYKGI RPAPGYPAQP DHTEKTTLFR LLDATANTGV ELTESYAMWP GSSVSGLYIG HPESYYFGVA KVERDQVEDY ARRKDMDVEA VERWLTPILN YVPGASKDEA A // ID C9XX22_CROTZ Unreviewed; 310 AA. AC C9XX22; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 31. DE SubName: Full=MmuM protein {ECO:0000313|EMBL:CBA28467.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:CBA28467.1}; GN Name=mmuM {ECO:0000313|EMBL:CBA28467.1}; GN OrderedLocusNames=Ctu_09370 {ECO:0000313|EMBL:CBA28467.1}; OS Cronobacter turicensis (strain DSM 18703 / LMG 23827 / z3032). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Cronobacter. OX NCBI_TaxID=693216 {ECO:0000313|EMBL:CBA28467.1, ECO:0000313|Proteomes:UP000002069}; RN [1] {ECO:0000313|Proteomes:UP000002069} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18703 / LMG 23827 / z3032 RC {ECO:0000313|Proteomes:UP000002069}; 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 ----------------------------------------------------------------------- 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; CBA28467.1; -; Genomic_DNA. DR RefSeq; WP_012815476.1; NC_013282.2. DR RefSeq; YP_003209300.1; NC_013282.2. DR STRING; 413502.Ctu_09370; -. DR EnsemblBacteria; CBA28467; CBA28467; CTU_09370. DR KEGG; ctu:CTU_09370; -. DR PATRIC; 20402562; VBICroTur2449_0897. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; CTUR693216:GI0P-979-MONOMER; -. DR Proteomes; UP000002069; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002069}; KW Methyltransferase {ECO:0000313|EMBL:CBA28467.1}; KW Transferase {ECO:0000313|EMBL:CBA28467.1}. SQ SEQUENCE 310 AA; 33075 MW; C148CA8A67B29251 CRC64; MSLNNPLTPL LNQQPFVVLD GALATELEAR GCNLADSLWS AKVLMEQPEL IYAVHLDYFR AGAQCAITAS YQATPAGFAA RGLDEAQSRA LIARSVELAR QAREAFYKEQ PDAGPLLVAG SVGPYGAYLA DGSEYRGDYA LSAAEFADFH RPRVEALLAA GVDLLACETL PSLSEARALA VLLESYPQAR AWLTFTLRDS GHISDGTPLA DVAAALAPYP QIVALGINCV ALEKTTAALA HLHDATRLPL VVYPNSGEQY DAVSKTWRHD GHACQTLAHY LDEWRAAGAA LIGGCCRTTP ADIAALNAQR // ID C9Y1X5_CROTZ Unreviewed; 1227 AA. AC C9Y1X5; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 48. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CBA34117.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CBA34117.1}; GN Name=metH {ECO:0000313|EMBL:CBA34117.1}; GN OrderedLocusNames=Ctu_38000 {ECO:0000313|EMBL:CBA34117.1}; OS Cronobacter turicensis (strain DSM 18703 / LMG 23827 / z3032). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Cronobacter. OX NCBI_TaxID=693216 {ECO:0000313|EMBL:CBA34117.1, ECO:0000313|Proteomes:UP000002069}; RN [1] {ECO:0000313|Proteomes:UP000002069} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18703 / LMG 23827 / z3032 RC {ECO:0000313|Proteomes:UP000002069}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; FN543093; CBA34117.1; -; Genomic_DNA. DR RefSeq; WP_015742687.1; NC_013282.2. DR RefSeq; YP_003212163.1; NC_013282.2. DR STRING; 413502.Ctu_38000; -. DR EnsemblBacteria; CBA34117; CBA34117; CTU_38000. DR KEGG; ctu:CTU_38000; -. DR PATRIC; 20408063; VBICroTur2449_3592. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CTUR693216:GI0P-3896-MONOMER; -. DR Proteomes; UP000002069; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002069}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CBA34117.1}; KW Transferase {ECO:0000313|EMBL:CBA34117.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135907 MW; C97814EB7E872B42 CRC64; MSSKSEQLRQ QLAERIMVLD GGMGTMIQSY RLDEEDFRGE RFADWPCDLK GNNDLLVLTR PDIIAAIHYA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINYEAARL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNVTFDQLV DAYRESTRAL IEGGSDLILI ETVFDTLNAK AAIFAVKTEF EALGVELPMM ISGTITDASG RTLSGQTTEA FYNSLRHADA LTFGLNCALG PDELRQYVAE LSRIAECYVT AHPNAGLPNA FGEYDLDADV MAAQIREWAE SGFLNIVGGC CGTTPAHIAA MSRAVEGLPP RKLPEIPVAC RLAGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VESGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVEAFVHHA RLVRRYGAAV VVMAFDEVGQ ADTRERKIEI CRRAYNILTE EVGFPPEDII FDPNIFAVAT GIDEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRADGTER LLALAEKYRG SKADSAADAQ QAEWRSWDVK KRLEYSLVKG ITEFIEQDTE EARQQAERPI QVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPYIQASK EVGKSNGKIV LATVKGDVHD IGKNIVGVVL QCNNYEIIDL GVMVPTDKIL KTAREVNADI IGLSGLITPS LDEMVNVAKE MERQGFTLPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVSSL LSDTLRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLAAAR ENDLAFDWES YTPPAAHRLG VEEVVASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG EEAQRLFKDA NEMLDALSAE KSLTPRGVVG IFPANRVGDD IEIYRDETRT QVLSVSHHLR QQTEKVGFAN YCMADFVAPK HSGKADYLGA FAVTGGLEED ALAEAFDAQH DDYNKIMVKA VADRLAEAFA EYLHERVRKV LWGYAPYENL SNEELIRENY QGIRPAPGYP ACPEHTEKSA IWELLDVENR IGMKLTESYA MWPGASVSGW YFSHPESKYF AVAQIQRDQV EDYARRKGMS VSEVERWLAA NLGYDAD // ID C9YBV3_9BURK Unreviewed; 317 AA. AC C9YBV3; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 01-OCT-2014, entry version 10. DE SubName: Full=Homocysteine S-methyltransferase ybgG {ECO:0000313|EMBL:CBA31253.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:CBA31253.1}; GN Name=ybgG {ECO:0000313|EMBL:CBA31253.1}; GN ORFNames=Csp_C27620 {ECO:0000313|EMBL:CBA31253.1}; OS Curvibacter putative symbiont of Hydra magnipapillata. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Curvibacter. OX NCBI_TaxID=667019 {ECO:0000313|EMBL:CBA31253.1}; RN [1] {ECO:0000313|EMBL:CBA31253.1} 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN543105; CBA31253.1; -; Genomic_DNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:CBA31253.1}; KW Transferase {ECO:0000313|EMBL:CBA31253.1}. SQ SEQUENCE 317 AA; 34189 MW; EC188B862158EE4C CRC64; MIPMMLNPLN SFLAHDRLMV LDGALATELE RRGAYLNDGL WSAKLLIEQP ELIRAVHADY FAAGADVATT ASYQATFEAF TRRGMSRTEA ADLMRLSVTL ACEARDAFWA EPANRVGRLR PLVAASVGPY GAMLADGSEY RGNYGLSRAA LADFHRERMQ VLSTSGADLL ACETIPGLDE ALAIADVLAE QNNITAWISF SCKDGEHNVQ GERLADCVAA LEAYPHIVAI GVNCTAPEHV ASLVEQAKAR TTKPVLVYPN SGEHYDAEGK VWTGACDPAD AYAEMAARWQ AKGARMIGGC CRTGPDDIRA VRHMAAT // ID C9YC11_9BURK Unreviewed; 371 AA. AC C9YC11; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:CBA30209.1}; GN ORFNames=Csp_C22400 {ECO:0000313|EMBL:CBA30209.1}; OS Curvibacter putative symbiont of Hydra magnipapillata. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Curvibacter. OX NCBI_TaxID=667019 {ECO:0000313|EMBL:CBA30209.1}; RN [1] {ECO:0000313|EMBL:CBA30209.1} 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN543105; CBA30209.1; -; Genomic_DNA. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:CBA30209.1}; KW Transferase {ECO:0000313|EMBL:CBA30209.1}. SQ SEQUENCE 371 AA; 39824 MW; 2837F29905F7E15A CRC64; MRSLVSIHIV SRTMKPITYT RAQELPGILA SRIAILDGAM GTMIQRFKLG EAQYRGEGYA GPGSQGDRFK DFPKDVKGNN ELLSLTRPDV ITDIHEAYLA AGADMIETNT FGATTVAQAD YDMADLAIEM NFVSAKLARA ACDKFSTPEK PRFVCGALGP TPKTASISPD VNDPGARNVT FEELRAAYYA QTKALVEGGA DVILVETIFD TLNAKAALFA VDEYFEASGE RLPIIISGTV TDASGRILSG QTVTAFWHSV RHAQPLAIGL NCALGAALMR PYIQELNKVA TDTFISCYPN AGLPNPMSDT GFDETPDVTS RLVREFAEEG LVNIVGGCCG TTPDHIGAIA HAVNPIATRN VQRGYFYKDA A // ID C9YS66_PEPDR Unreviewed; 793 AA. AC C9YS66; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 38. DE SubName: Full=Clostridium difficile R20291 complete genome {ECO:0000313|EMBL:CBE07519.1}; GN OrderedLocusNames=CDR20291_3434 {ECO:0000313|EMBL:CBE07519.1}; OS Peptoclostridium difficile (strain R20291) (Clostridium difficile). OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Peptoclostridium. OX NCBI_TaxID=645463 {ECO:0000313|EMBL:CBE07519.1, ECO:0000313|Proteomes:UP000002070}; RN [1] {ECO:0000313|EMBL:CBE07519.1, ECO:0000313|Proteomes:UP000002070} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R20291 {ECO:0000313|EMBL:CBE07519.1, RC ECO:0000313|Proteomes:UP000002070}; 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; CBE07519.1; -; Genomic_DNA. DR RefSeq; WP_009892182.1; NC_013316.1. DR STRING; 645463.CDR20291_3434; -. DR EnsemblBacteria; CBE07519; CBE07519; CDR20291_3434. DR KEGG; cdl:CDR20291_3434; -. DR PATRIC; 19461005; VBICloDif78408_3641. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CDIF645463:GJP4-3521-MONOMER; -. DR Proteomes; UP000002070; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002070}. SQ SEQUENCE 793 AA; 86553 MW; 440779456A8E3971 CRC64; MEIRQYLKNN ILIFDGAMGT MLQQKGLKLG ENPEVFGLQN PDKLIEIHTA YLEAGSNVIL TNTFGCNELK LDSKYTVEEV IDNAVLVARK AIENVDNTKP RYVALDIGPI GEMLEPMGTL SFDNAYEIFK RQVLQGVKSG VDVIVIETMM DLYEAKVAVL AAKENSDLPI FCTMTFDEGG RSFTGCMPEC MVATIEGLGV DAIGVNCSLG PKQLLPIVEK IASRATVPVM VQANAGLPNI VDGEAIYDVD AKEFFEGVKK FVEVGATIIG GCCGTNPSFI KEISENINSV TKGCIEKIDK CVVCSPSKFV EVQSPTVVGE RLNPTGRKSL QEALKNENVD YAINLGLEQV NAGAQILGVN VGLPEIDEKK LMPKLIREIQ AVVDTPLQVD SSNVEALEQG LRYYNGRTIV NSVNGKEESL ESILPIVKKY GSCVVGLTLD EKGIPKKAEE RFEIAKRIVN RAVSCGIKPK DIFIDCLSLT VSAQQEEAIE TIKAITMVKT LGVKTILGVS NISFGLPNRK ALNASFLTLA LGAGLDLAII NPNEYSMMEA INSFKILNNT DKGCINYINQ YSNINNSKKS DSSTKIDKDL PLDILVERGL KDEAKNVTLN LLKEKDENYI LDEILIPALD KVGKRYDSGD IFLPQLIQSA ETVKVSLNTI KETLLSKSSN NVSKGKIIVA TVKGDIHDIG KNIVKIMLEN YGYEVIDLGK DVPIEEVVEV AKKRNIKLVG LSALMTTTVQ SMKDTIQALR DNEINAKVFV GGAVLTEEYA EEMGADYYSK DAKSAVEIAK LNF // ID C9YT67_STRSW Unreviewed; 317 AA. AC C9YT67; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 29-APR-2015, entry version 34. DE SubName: Full=Streptomyces scabiei 87.22 complete genome {ECO:0000313|EMBL:CBG69081.1}; GN OrderedLocusNames=SCAB_19601 {ECO:0000313|EMBL:CBG69081.1}; OS Streptomyces scabies (strain 87.22) (Streptomyces scabiei). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG69081.1, ECO:0000313|Proteomes:UP000001444}; RN [1] {ECO:0000313|EMBL:CBG69081.1, ECO:0000313|Proteomes:UP000001444} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=87.22 {ECO:0000313|EMBL:CBG69081.1, RC ECO:0000313|Proteomes:UP000001444}; 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 ----------------------------------------------------------------------- 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; CBG69081.1; -; Genomic_DNA. DR RefSeq; WP_012999805.1; NC_013929.1. DR RefSeq; YP_003487646.1; NC_013929.1. DR EnsemblBacteria; CBG69081; CBG69081; SCAB_19601. DR KEGG; scb:SCAB_19601; -. DR PATRIC; 35319616; VBIStrSca144334_1922. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR BioCyc; SSCA680198:GJ76-1859-MONOMER; -. DR Proteomes; UP000001444; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001444}; KW Reference proteome {ECO:0000313|Proteomes:UP000001444}. SQ SEQUENCE 317 AA; 32740 MW; F14B6159F7459A1B CRC64; MTSNASGSPS PVPGPPSGRF AAALAADVLV LDGGMSNQLE SAGHDLSDEL WSARLLAESP KAITEAHLAY FEAGANVAIT ASYQATFDGF AKRGIDGDRA AELMALSIGL AADAAAEAGT RGEARPLLVA ASVGPYGAML ADGSEYRGRY GLGVAELERF HRPRLEVLAA ARPDVLALET IPDTDEAEAL LRAVRGLDVP AWLSYTVAGD RTRAGQPLEE AFALAADAEE IVAVGVNCCA SEDVDGAIET AVRVTGKPVV VYPNSGETWD AAARSWTGRS TFTTEQVLGW RAAGARLIGG CCRVGPEAVS AIARTLA // ID C9Z309_STRSW Unreviewed; 1175 AA. AC C9Z309; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 29-APR-2015, entry version 47. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CBG74318.1}; GN Name=metH {ECO:0000313|EMBL:CBG74318.1}; GN OrderedLocusNames=SCAB_73321 {ECO:0000313|EMBL:CBG74318.1}; OS Streptomyces scabies (strain 87.22) (Streptomyces scabiei). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG74318.1, ECO:0000313|Proteomes:UP000001444}; RN [1] {ECO:0000313|EMBL:CBG74318.1, ECO:0000313|Proteomes:UP000001444} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=87.22 {ECO:0000313|EMBL:CBG74318.1, RC ECO:0000313|Proteomes:UP000001444}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; FN554889; CBG74318.1; -; Genomic_DNA. DR RefSeq; WP_013004859.1; NC_013929.1. DR RefSeq; YP_003492853.1; NC_013929.1. DR EnsemblBacteria; CBG74318; CBG74318; SCAB_73321. DR KEGG; scb:SCAB_73321; -. DR PATRIC; 35330365; VBIStrSca144334_7226. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; SSCA680198:GJ76-7181-MONOMER; -. DR Proteomes; UP000001444; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001444}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001444}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 241 241 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 751 751 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1175 AA; 128151 MW; 853367FC4122C1C3 CRC64; MASLPNPSPS SAAAGRARSD ALREALATRV VVADGAMGTM LQAQDPTLED FQQLEGCNEV LNATRPDIVR SVHAAYFDAG VDCVETNTFG ANLTALGEYD ISERTAELSE AGARIARETA DEYTARDGRP RWVLGSIGPG TKLPTLGHTT FTAIRDAYRQ NAEGLLAGGA DALLVETTQD LLQTKASVIA ARRAMETAGY DVPLIVSVTV ETTGTMLLGS EIGAALTALE PLGIDMIGLN CATGPAEMSE HLRYLARHSR IQLSCMPNAG LPVLTKDGAH YPLTAPELAD AQENFVREYG LSLIGGCCGT TPEHLRQVVE RVRDLTPTVR DPRPEPGAAS LYQTVPFRQD TSYMAIGERT NANGSKKFRE AMLEARWDDC VEMARDQIRE GAHMLDLCVD YVGRDGVADM AELAGRFATA STLPIVLDST EVDVIRAGLE KLGGRAVINS VNYEDGDGPE SRFAKVTALA QEHGAALIAL TIDEEGQART PEKKVEIAER LIDDLTGNWG IHESDILIDT LTFTICTGQE ESRKDGIATI EAIRELKRRH PEVQTTLGLS NISFGLNPAA RILLNSVFLD ECAKAGLDSA IVHASKILPI ARFSEEEVQT ALDLIHDRRA EGYDPLTKLM ALFEGATAKS LKAGKAEELA ALPLEERLKR RIIDGEKNGL EADLDEALQT RPALDIVNDT LLDGMKVVGE LFGSGQMQLP FVLQSAEVMK SAVAHLEPHM EKSDDEGKGT IVLATVRGDV HDIGKNLVDI ILSNNGYNVV NLGIKQPVSA ILDAAREHRA DVIGMSGLLV KSTVIMKENL QELNQRGLAA DYPVILGGAA LTRAYVEQDL HEIYEGEVRY ARDAFEGLRL MDALIGVKRG VPGAVLPELR QRRVRAAAGV TAVEERPEEG HVRSDVATDN PVPAPPFRGT RVIKGIQLKE YATWLDEGAL FKGQWGLKQA RTGDGPTYEE LVETEGRPRL RGLLDRLQTD NLLEAAVVYG YFPCVSKDDD LIILDDDGNE RTRFSFPRQR RGRRLCLADF FRPEESGETD VVGLQVVTVG SRIGEETAKL FEADSYRDYL ELHGLSVQLA EALAEYWHAR VRSELGFAGE DPAAIEDMFD LKYRGARFSL GYGACPDLED RAKIAELLEP ERIGVRLSEE FQLHPEQSTD AIVIHHPEAK YFNAR // ID C9ZI75_TRYB9 Unreviewed; 433 AA. AC C9ZI75; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 29-APR-2015, entry version 13. DE SubName: Full=Chromosome 1, complete sequence {ECO:0000313|EMBL:CBH08867.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:CBH08867.1}; GN ORFNames=TbgDal_I590 {ECO:0000313|EMBL:CBH08867.1}; OS Trypanosoma brucei gambiense (strain MHOM/CI/86/DAL972). OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Trypanosoma. OX NCBI_TaxID=679716 {ECO:0000313|EMBL:CBH08867.1, ECO:0000313|Proteomes:UP000002316}; RN [1] {ECO:0000313|Proteomes:UP000002316} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MHOM/CI/86/DAL972 {ECO:0000313|Proteomes:UP000002316}; RX PubMed=20404998; DOI=10.1371/journal.pntd.0000658; RA Jackson A.P., Sanders M., Berry A., McQuillan J., Aslett M.A., RA Quail M.A., Chukualim B., Capewell P., MacLeod A., Melville S.E., RA Gibson W., Barry J.D., Berriman M., Hertz-Fowler C.; RT "The genome sequence of Trypanosoma brucei gambiense, causative agent RT of chronic human african trypanosomiasis."; RL PLoS Negl. Trop. Dis. 4:E658-E658(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; FN554964; CBH08867.1; -; Genomic_DNA. DR Proteomes; UP000002316; Chromosome 1. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002316}; KW Methyltransferase {ECO:0000313|EMBL:CBH08867.1}; KW Transferase {ECO:0000313|EMBL:CBH08867.1}. SQ SEQUENCE 433 AA; 48262 MW; FC9A286EAF7C7938 CRC64; MKDISCPTGE TGSIFEKSKK FHHFFTMDGA VGTLVERCGL DPSKMGSMWS TSALITDEEI VRYVHKSYLD VGADVILTNT YQMHAAGCAQ AGVTMNEVVN TAVRVLCDGI TPERAAATKE AKVWAQHVMN NKRSEFVDVF APLFYGPRDD ASKCPVLVGG SLGSYGASLG NAQEYRGEYE VNEDIIRDYY VGRFMAFVNH VDEKEAHLKV DFIMIETIPL LNEAIEIFTW LKYQKEDETL RSAPVCLSFI SCLREPRPDV TVDDATLNEW WLAAESNIRL IDGNTFEKAF NSLMELQLPQ LVGFGTNCCS PLEASVVASA FLKKKKHKVT DPSLALFLYS NSGENFKEGE WHWGGQLPRG SHSPTSSPKE TLPFTTLQRL MLCCEADVRT AAFFAHQLLL QRPEADDWLF DIIICGGCCR STPEDIAMIR SLV // ID D0B4P4_BRUME Unreviewed; 1261 AA. AC D0B4P4; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 38. DE SubName: Full=MetH family protein {ECO:0000313|EMBL:EEW88368.1}; GN ORFNames=BAWG_0476 {ECO:0000313|EMBL:EEW88368.1}; OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=224914 {ECO:0000313|Proteomes:UP000000419, ECO:0000313|Proteomes:UP000008511}; RN [1] {ECO:0000313|EMBL:EEW88368.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=16M {ECO:0000313|EMBL:EEW88368.1}; 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. 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; GG703778; EEW88368.1; -; Genomic_DNA. DR RefSeq; WP_004684692.1; NZ_GG703778.1. DR EnsemblBacteria; AIJ88965; AIJ88965; DK63_1726. DR EnsemblBacteria; EEW88368; EEW88368; BAWG_0476. DR PATRIC; 17796387; VBIBruMel146950_1467. DR eggNOG; COG1410; -. DR Proteomes; UP000008511; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008511}. SQ SEQUENCE 1261 AA; 138682 MW; B3587ED5F18F1BE6 CRC64; MASSLDDLFG ATAAKPDGSE VLAALTQAAR ERILILDGAM GTQIQGLGFH EEHFRGDRFA TCDCQLQGNN DLLTLTQPKA IEEIHYAYAM AGADILETNT FSSTSIAQAD YGMEAMVYDL NRDGARLARR AALRAEQKDG RRRFVAGALG PTNRTASLSP DVNNPGFRAV TFDDLRIAYS EQIRGLIDGG SDIILIETIF DTLNAKAAVF ATEEVFAEKG VRLPVMISGT ITDLSGRTLS GQTPTAFWYS LRHARPFTIG LNCALGANAM RAHLDELSGI ADTFICAYPN AGLPNEFGQY DETPEAMAAQ IEGFARDGLV NVVGGCCGST PDHIRAIAQA VAKYEPRKPA KVPPLMRLSG LEPFTLTKDI PFVNIGERTN VTGSARFRKL VKAGDFAAAL DVARDQVANG AQIIDINMDE GLIDSEKAMV EFLNLIAAEP DIARVPIMLD SSKWEVIEAG LKCVQGKAVV NSISLKEGEE AFLHHARLVR AYGAAVVIMA FDETGQADTQ ARKIEICTRA YKILTEQVGF PPEDIIFDPN IFAVATGIEE HNNYGVDFIE ATREIVRTLP HVHISGGVSN LSFSFRGNEP VREAMHAVFL YHAIQAGMDM GIVNAGQLAV YDTIDAELRE ACEDVVLNRP TKTGESATER LLEIAERFRD SGSREARTQD LSWREWPVEK RLEHALVNGI TEYIEADTEE ARLAAERPLH VIEGPLMAGM NVVGDLFGSG KMFLPQVVKS ARVMKQAVAV LLPFMEEEKR LNGGEGRQSA GKVLMATVKG DVHDIGKNIV GVVLACNNYE IIDLGVMVPS QKILQVARDE KVDIIGLSGL ITPSLDEMAH VAAEMEREGF DIPLLIGGAT TSRVHTAVKI HSRYERGQAV YVVDASRAVG VVSNLLSPEG KQAYIDGLRN EYAKVAAAHA RNEAEKQRLP IARARANPHQ LDWENYEPVK PTFTGTKVFE TYDLAEIARY IDWTPFFQTW ELRGRYPAIL EDEKQGEAAR QLWADAQAML RKIIDEKWFT PRAVVGFWPA NAVGDDIRLF TDESRKEELA TLFTLRQQLT KRDGRPNVAM ADFVAPVESG KQDYVGGFVV TAGIGEIAIA ERFERANDDY SAILVKALAD RFAEAFAELM HERVRKEFWA YAPDEAFTPE ELISEPYKGI RPAPGYPAQP DHTEKTTLFR LLDATANTGV ELTESYAMWP GSSVSGLYIG HPESYYFGVA KVERDQVEDY ARRKDMDVEA VERWLTPILN YVPGASKDEA A // ID D0C9Z4_ACIBA Unreviewed; 292 AA. AC D0C9Z4; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEX04063.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ENW74502.1}; GN ORFNames=F911_03012 {ECO:0000313|EMBL:ENW74502.1}, GN HMPREF0010_01457 {ECO:0000313|EMBL:EEX04063.1}; 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 {ECO:0000313|EMBL:EEX04063.1}; RN [1] {ECO:0000313|EMBL:EEX04063.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 19606 {ECO:0000313|EMBL:EEX04063.1}; 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] {ECO:0000313|EMBL:ENW74502.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIP 70.34 {ECO:0000313|EMBL:ENW74502.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG704573; EEX04063.1; -; Genomic_DNA. DR EMBL; APRG01000015; ENW74502.1; -; Genomic_DNA. DR RefSeq; WP_000697114.1; NZ_KL810966.1. DR EnsemblBacteria; EEX04063; EEX04063; HMPREF0010_01457. DR EnsemblBacteria; ENW74502; ENW74502; F911_03012. DR EnsemblBacteria; KFC03956; KFC03956; DJ41_2612. DR PATRIC; 24332450; VBIAciBau3967_1429. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EEX04063.1}; KW Transferase {ECO:0000313|EMBL:EEX04063.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 202 202 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 275 275 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 276 276 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 292 AA; 31992 MW; 391AD506B8C20EE9 CRC64; MKILDGGLGR ELARRGAPFR QPEWSALALI EAPETVKEVH LDFINAGAEV ITTNNYAVVP FHIGQERFET DGVRLIKVAI EQAKNAVKES GKNVKIAGCL PPLFGSYRAD LFQPGQAKNL AEPIINTLAP EVDFWLAETQ SCLKEVETVH ALLPQDGKDY WVSFTLQDEI KQEQALLRSG ENMQQVADFI KQSNAKAVLF NCCQPEVILQ AINEIKGLIP ESVQIGAYAN AFPPQDESAT ANDGLDEIRK DLDAPAYLGF AKQWQQAGAS LVGGCCGIGP EHIAELSQFF KE // ID D0CA43_ACIBA Unreviewed; 745 AA. AC D0CA43; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 31. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEX04112.1}; GN ORFNames=HMPREF0010_01506 {ECO:0000313|EMBL:EEX04112.1}; 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 {ECO:0000313|EMBL:EEX04112.1}; RN [1] {ECO:0000313|EMBL:EEX04112.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 19606 {ECO:0000313|EMBL:EEX04112.1}; 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG704573; EEX04112.1; -; Genomic_DNA. DR EnsemblBacteria; EEX04112; EEX04112; HMPREF0010_01506. DR PATRIC; 24332552; VBIAciBau3967_1480. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEX04112.1}; KW Transferase {ECO:0000313|EMBL:EEX04112.1}. SQ SEQUENCE 745 AA; 81936 MW; 6B8D3E121208CF45 CRC64; MSTLATLKAL LAKRILIIDG AMGTMIQRHK LEEADYRGER FADWAHDLKG NNDLLVLTQP QIIQGIHEAY LDAGADIIET NSFNGTRVSM SDYHMEELVP EINREAARLA KAACEKYSTP DKPRFVAGVL GPTSRTCSIS PDVNNPAFRN ISFDELKENY IEATHALIEG GADIILIETV FDTLNCKAAI FAVKEVFKQI GRELPIMISG TITDASGRTL TGQTAEAFWN SVRHGDLLSI GFNCALGADA MRPHVKTISD VADTFVSAHP NAGLPNAFGE YDETPEQTAA FLKEFAESGL INITGGCCGT TPDHIRAIAN AVKDIAPRQV PETVPACRLS GLEPFNIYDD SLFVNVGERT NVTGSKKFLR LIREENFAEA LEVAQQQVEA GAQIIDINMD EGMLDSQNAM VHFLNLVASE PDISRVPIMI DSSKWEIIEA GLKCVQGKPV VNSISLKEGY DEFVEKARLC RQYGAAIIVM AFDEVGQADT AERKREICKR SYDILVNEVG FPAEDIIFDP NVFAVATGIE EHNNYAVDFI EATGWIKQNL PHAMISGGVS NVSFSFRGNE PVREAIHSVF LYHAIKQGMT MGIVNAGQMA IYDDIPTELK EAVEDVILNQ NQGESGQAAT EKLLEVAEKY RGQGGATKEA ENLEWRNESV EKRLEYALVK GITTYIDQDT EEARLKSKRP LDVIEGPLMD GMNVVGDLFG SGKMFLPQVV KSARVMKQAV AWLNPYIEAE KTRTV // ID D0CRG9_9RHOB Unreviewed; 337 AA. AC D0CRG9; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Methionine synthase I {ECO:0000313|EMBL:EEX10925.1}; GN ORFNames=SL1157_2996 {ECO:0000313|EMBL:EEX10925.1}; OS Silicibacter lacuscaerulensis ITI-1157. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Ruegeria. OX NCBI_TaxID=644107 {ECO:0000313|EMBL:EEX10925.1}; RN [1] {ECO:0000313|EMBL:EEX10925.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ITI-1157 {ECO:0000313|EMBL:EEX10925.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; EEX10925.1; -; Genomic_DNA. DR RefSeq; WP_005983376.1; NZ_GG704596.1. DR EnsemblBacteria; EEX10925; EEX10925; SL1157_2996. DR PATRIC; 28600711; VBISilLac12138_2758. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 212 212 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 278 278 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 279 279 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 337 AA; 35605 MW; AAE88E532A733ECC CRC64; MTNALTRLLE TTDAILADGA TGTNLFNMGL QSGDAPELWN TEQPDKIRAL YRGSVDAGSD LFLTNTFGGT AARLKLHDAH TRVAELNRVG AELAREVADA AGRPVVVAGS VGPTGEILEP VGSLTHAEAV EMFHEQAEAL KAGGVDVLWL ETISAPEEFR AAAEAFALAD MPWCGTMSFD TAGRTMMGVT SADLAQLVET LPNPPIAFGA NCGTGASDIL RTVLGFVAQG TERPLISKGN AGIPKYVDGH IHYDGTPELM GRYAAMARDA GATIIGGCCG TMPEHLREMR KALDTTPRGA RPTLDQITEA LGSFSSANDG TGENSQPERR ARRRRRA // ID D0CUB1_9RHOB Unreviewed; 298 AA. AC D0CUB1; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EEX09434.1}; GN ORFNames=SL1157_1472 {ECO:0000313|EMBL:EEX09434.1}; OS Silicibacter lacuscaerulensis ITI-1157. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Ruegeria. OX NCBI_TaxID=644107 {ECO:0000313|EMBL:EEX09434.1}; RN [1] {ECO:0000313|EMBL:EEX09434.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ITI-1157 {ECO:0000313|EMBL:EEX09434.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; EEX09434.1; -; Genomic_DNA. DR RefSeq; WP_005980514.1; NZ_GG704596.1. DR EnsemblBacteria; EEX09434; EEX09434; SL1157_1472. DR PATRIC; 28597746; VBISilLac12138_1179. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EEX09434.1}; KW Transferase {ECO:0000313|EMBL:EEX09434.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 202 202 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 275 275 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 276 276 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 298 AA; 31828 MW; 424A45EA8CD526E6 CRC64; MTDITLMDGS IGQELVKRSG DRATPLWSTR VMIDHPDLVG EVHADYFRRG ATIATTNTYA VHRSRLARVG MEDQLPALID TALAQAERAR AQFPQGRIAG ALGPLLASYR PDLSPDPTEA AEKFRELVQM MADRVDLFLI ETVSSVQEAE GALRGTQGCG KPAWLALTVM DDDGTRLRSG EALGDIAPLV DRFGPEAVLI NCSRPEAIPA ALGIIKGLGR PFGAYANGFT CISEGFLQDA PTVDALEQRQ DLGPDAYADH AMGWVAQGAT IVGGCCEVGP DHIEALAGRL RAAGHRIV // ID D0D0L1_9RHOB Unreviewed; 349 AA. AC D0D0L1; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEX16640.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEX16640.1}; GN ORFNames=CSE45_4360 {ECO:0000313|EMBL:EEX16640.1}; OS Citreicella sp. SE45. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Citreicella. OX NCBI_TaxID=501479 {ECO:0000313|EMBL:EEX16640.1}; RN [1] {ECO:0000313|EMBL:EEX16640.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SE45 {ECO:0000313|EMBL:EEX16640.1}; 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; GG704598; EEX16640.1; -; Genomic_DNA. DR RefSeq; WP_008883160.1; NZ_GG704598.1. DR EnsemblBacteria; EEX16640; EEX16640; CSE45_4360. DR PATRIC; 27085569; VBICitSp11713_0237. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEX16640.1}; KW Transferase {ECO:0000313|EMBL:EEX16640.1}. SQ SEQUENCE 349 AA; 37392 MW; FEA6B39134DA3850 CRC64; MHSFILPPTK TVADLTRAAR ERILILDGAM GTQIQTLGLD EDDFRGHGGQ CCSFHSDHPQ KGNNDLLILT QPKAIEDIHY AFAMAGADIV ETNTFSSTTI AQADYAMEQA VFDLNVEGAR VARRALDRAT AEDGRPRWVA GAVGPTNRTA SISPDVNDPG YRAVTFDDLR RAYGQQIRGL IVGGADLILI ETIFDTLNAK AAIFACFEAF AEHGARLPIM ISGTITDASG RTLSGQTPTA FWHSVRHARP FSVGLNCALG ADAMRPHLAE LAGVADTLIC AYPNAGLPNA FGKYDEEPED TAAKVEVFAR EGLVNLVGGC CGTTPEHIRA IAEHVASYAP RQIEETADA // ID D0DAY2_9RHOB Unreviewed; 320 AA. AC D0DAY2; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 01-OCT-2014, entry version 12. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEX13412.1}; GN ORFNames=CSE45_3694 {ECO:0000313|EMBL:EEX13412.1}; OS Citreicella sp. SE45. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Citreicella. OX NCBI_TaxID=501479 {ECO:0000313|EMBL:EEX13412.1}; RN [1] {ECO:0000313|EMBL:EEX13412.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SE45 {ECO:0000313|EMBL:EEX13412.1}; 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; GG704601; EEX13412.1; -; Genomic_DNA. DR RefSeq; WP_008887231.1; NZ_GG704601.1. DR EnsemblBacteria; EEX13412; EEX13412; CSE45_3694. DR PATRIC; 27092955; VBICitSp11713_3827. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEX13412.1}; KW Transferase {ECO:0000313|EMBL:EEX13412.1}. SQ SEQUENCE 320 AA; 34107 MW; 2005ECB62F405E62 CRC64; MVIQMTTYRN NLPQFDGTIL LTDSGLETTL IFHDGIDLPA FAAYPLMETE PGRETLARYY RRHLSIAADH GTGFVLEAPT WRASRDWGAE LGHSPEDLAR LNQAAIGFLS DLRASARGVR PVVISGNIGP RGDGYVADTA MTAAEAEAYH AEQIGWFAET DVDMVTAVTL STVAEGVGAI RAACKRGLPV VVSYTVETDG RLPDGTPLGT AFEQTDAETD GAAAYFMVNC AHPDHFRDAL AAGSGWLERI GGVRANASRL SHAELDAAEE LDAGNPAELG HDYARLRRLL PNLVVLGGCC GTDHRHVEAI ADCCVASTAA // ID D0DGE7_9LACO Unreviewed; 329 AA. AC D0DGE7; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Putative homocysteine S-methyltransferase {ECO:0000313|EMBL:EEX29819.1}; GN ORFNames=HMPREF0508_00696 {ECO:0000313|EMBL:EEX29819.1}; OS Lactobacillus crispatus MV-3A-US. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=575597 {ECO:0000313|EMBL:EEX29819.1, ECO:0000313|Proteomes:UP000003974}; RN [1] {ECO:0000313|EMBL:EEX29819.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MV-3A-US {ECO:0000313|EMBL:EEX29819.1}; 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 crispatus strain MV-3A-US."; 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; GG704608; EEX29819.1; -; Genomic_DNA. DR RefSeq; WP_005719570.1; NZ_GG704608.1. DR EnsemblBacteria; EEX29819; EEX29819; HMPREF0508_00696. DR GeneID; 9107864; -. DR PATRIC; 35687927; VBILacCri90530_0813. DR OrthoDB; EOG6C019S; -. DR Proteomes; UP000003974; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000003974}; KW Methyltransferase {ECO:0000313|EMBL:EEX29819.1}; KW Transferase {ECO:0000313|EMBL:EEX29819.1}. SQ SEQUENCE 329 AA; 37079 MW; AC5A97247149A998 CRC64; MNLLKQIRDR GLILDGAMST ALEKLGIDTN NELWTAIALE HNLAQIYQVH MNYFKAGAQM AITDTYQANI PAFEKHGFTQ DQATKLITNA VQIAKKARDD FAKTTGIHNY VAASVGPYGA YLAQGDEFRG DYSLTTEEYL NFHLPRLKIL LANKPDCLAL ETQPKLDEVV AILDWLKENA PEIPVYVSFT LHDTTKISDG TPLKRVVQKL NEYDQVFAIG ANCFKPFLAT AVIDKIHDFT DKQIVIYPNL GGVYNEFERN WIPFNAKFDF KKLSQEWYEH GARIIGGCCS TTEKEIGQIS AFFKTINNAK SKSVKSELKK VKNDSNIQI // ID D0DRI1_LACFE Unreviewed; 310 AA. AC D0DRI1; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEX26457.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EEX26457.1}; GN Name=mmuM {ECO:0000313|EMBL:EEX26457.1}; GN ORFNames=HMPREF0513_00195 {ECO:0000313|EMBL:EEX26457.1}; OS Lactobacillus fermentum 28-3-CHN. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=575599 {ECO:0000313|EMBL:EEX26457.1}; RN [1] {ECO:0000313|EMBL:EEX26457.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=28-3-CHN {ECO:0000313|EMBL:EEX26457.1}; 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 ----------------------------------------------------------------------- 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; EEX26457.1; -; Genomic_DNA. DR RefSeq; WP_003681749.1; NZ_GG704699.1. DR EnsemblBacteria; EEX26457; EEX26457; HMPREF0513_00195. DR GeneID; 6232276; -. DR PATRIC; 30718583; VBILacFer94112_0291. DR OrthoDB; EOG6C019S; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEX26457.1}; KW Transferase {ECO:0000313|EMBL:EEX26457.1}. SQ SEQUENCE 310 AA; 33675 MW; 7DA01ED5B30D73D5 CRC64; MKLLERLAQG PLVLDGSMST PLEVAGAKTN SDLWTSQTLI DNPDLVYQVH LDYFKAGADL TITDTYQTNV DALVRHGLSE EEARNLIKRA VQLANQARDD YEKETGKHNY VAGSIGPYGA YLADGSEYRG DYDLTAIQLQ NFHLPRLAAI LATGVDCLAL ETQPKLTEVV AILALLKTLE PTMPVYVSFS LRDAEHLSDG TSLKEAVQVV TKDPQVFAVG VNCVGLDLVT PAIKAIKEVT DKPVIVYPNS GATYDPTVKQ WRFEEGTPRF VNAIDDWITA GAAIIGGCCT TLPQDIAVVA EKLRGVGNNR // ID D0GK40_9FUSO Unreviewed; 1165 AA. AC D0GK40; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 27-MAY-2015, entry version 33. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEY35554.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEY35554.1}; GN Name=metH {ECO:0000313|EMBL:EEY35554.1}; GN ORFNames=HMPREF0554_0246 {ECO:0000313|EMBL:EEY35554.1}; OS Leptotrichia goodfellowii F0264. OC Bacteria; Fusobacteria; Fusobacteriales; Leptotrichiaceae; OC Leptotrichia. OX NCBI_TaxID=596323 {ECO:0000313|EMBL:EEY35554.1}; RN [1] {ECO:0000313|EMBL:EEY35554.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0264 {ECO:0000313|EMBL:EEY35554.1}; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Strausberg R.L., Nelson K.E.; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEY35554.1}. 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; ADAD01000059; EEY35554.1; -; Genomic_DNA. DR RefSeq; WP_006806845.1; NZ_ADAD01000059.1. DR EnsemblBacteria; EEY35554; EEY35554; HMPREF0554_0246. DR PATRIC; 36036520; VBILepGoo29969_0623. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEY35554.1}; KW Transferase {ECO:0000313|EMBL:EEY35554.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 237 237 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 301 301 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 734 734 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1165 AA; 130649 MW; A9FFB47B9F5875D2 CRC64; MSDIKYKDSF YELKKDLNGK IVLLDGAMGT MIQKQNLTAE DFGGEKYEGC NDYLVLTKPE VIKNIHKMYL EAGSDIIETN TFGALDIVLR DYELEDKVFE MNKSAAELVR KAIEEYREEN PNEKRNLYVA GALGPSNKSI SVTGGVTFDE LIHTYYTATS GLLAGNVDII LFETIQDTRN LKAAYLGLQK AMEEHYNVPL MLSFTIESTG TTLAGQTADA FYYAVNHMHP LSVGLNCATG PEFMTQFLKI LNNVSNTYIS VYPNAGLPNE EGKYEETPDT LSAKIEPFFQ NKYLNIVGGC CGTTPEHIKQ IKEKSIKYTP RVIEEHSETK NEVSGLITLN PPQNRPVYVG ERTNVIGSRI FKNLIVNEKF DEATEVARLQ IKGDADVIDV CLANPDRDEI NDMKAFLEKV SKFAKVPIML DSTDINVIKE GLTYLQGKGI INSINLEDGE KKFVDMSELI KKFGASVVVG LIDEEGMAVS LEKKIKVAKR SYELLTKKYG IDERDIIFDT LVFPVATGDQ KYIGSAAATI EAIREIKKEM PNVKTILGVS NISFGLPVAG REVLNSYYMQ KAYETGLDYA IVNTEKLIPL SEISDKEKEL SEALLFNTND DTVADFVAFY REKKGVEKKA DTTNMTPEEQ VSNLVVEGSK KDLIPLLDTL LQKYAPLDII NGPLMDGMDE VGKLFNNNDL IVAEVLQSAE VMKASVSHLE QFMEKSESST KGKVIMATVK GDVHDIGKNL VGIIIGNNGY DVVDLGINTP AEKIREAIIN EKADFVGLSG LLVKSAAEMV NTVAVLREAG IKIPIFVGGA ALTEKFTVNK IEPSYENNIV IYSKDAMTAL ADLNKMIVPE KFEEFKQYLQ SRRDMLLLKD KDAIEKLNVR QTVGDVKNAD GSFDITKVKL PEYNFEKIYK PSTLNKQIIT NIPAKEVFKY LNLQMLIGKH LGMKWVVREL LEKGDPKATK MYNEILDIIN HGDEYFDIKA VYKYFPCRKK DGKIEILSDD LKETVETFDF PRQTWGQHLS LNDYIHPAEI DYIGMFVVSA GEKSRIVSNE LKEKGEFYKG HLVNSIGLEL AESTAEYAHY LMRKDVGIID DENLTVDEIH RAKYHGKRYS FGYPACPDLS DQDKLFNLLK PERFGIKLTL GHMMYPEASV SAIVFSQPFA KYFNM // ID D0GK41_9FUSO Unreviewed; 137 AA. AC D0GK41; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EEY35542.1}; GN ORFNames=HMPREF0554_0247 {ECO:0000313|EMBL:EEY35542.1}; OS Leptotrichia goodfellowii F0264. OC Bacteria; Fusobacteria; Fusobacteriales; Leptotrichiaceae; OC Leptotrichia. OX NCBI_TaxID=596323 {ECO:0000313|EMBL:EEY35542.1}; RN [1] {ECO:0000313|EMBL:EEY35542.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0264 {ECO:0000313|EMBL:EEY35542.1}; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Strausberg R.L., Nelson K.E.; 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. {ECO:0000313|EMBL:EEY35542.1}. 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; ADAD01000059; EEY35542.1; -; Genomic_DNA. DR RefSeq; WP_006806833.1; NZ_ADAD01000059.1. DR EnsemblBacteria; EEY35542; EEY35542; HMPREF0554_0247. DR PATRIC; 36036522; VBILepGoo29969_0624. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 137 AA; 15473 MW; 1FC322BC521348AE CRC64; MKEYYYVPLM LSFALKDTGT TFTGQTIQEL YDTAYYMNPI SLGFNCAVGG EHTEKFIETL NSISNIYTSF YPNAGLPDKN GKYEKTPDVL ASETELFFQN NCLNIIGGCC GTTPEHIRQI KEKSIKYLPR SIELPVL // ID D0GNI0_9FUSO Unreviewed; 148 AA. AC D0GNI0; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EEY34350.1}; DE Flags: Fragment; GN ORFNames=HMPREF0554_1991 {ECO:0000313|EMBL:EEY34350.1}; OS Leptotrichia goodfellowii F0264. OC Bacteria; Fusobacteria; Fusobacteriales; Leptotrichiaceae; OC Leptotrichia. OX NCBI_TaxID=596323 {ECO:0000313|EMBL:EEY34350.1}; RN [1] {ECO:0000313|EMBL:EEY34350.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0264 {ECO:0000313|EMBL:EEY34350.1}; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Strausberg R.L., Nelson K.E.; 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. {ECO:0000313|EMBL:EEY34350.1}. 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; ADAD01000168; EEY34350.1; -; Genomic_DNA. DR RefSeq; WP_006808039.1; NZ_ADAD01000168.1. DR EnsemblBacteria; EEY34350; EEY34350; HMPREF0554_1991. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; FT NON_TER 148 148 {ECO:0000313|EMBL:EEY34350.1}. SQ SEQUENCE 148 AA; 16820 MW; 2DDEA19242AF8CB9 CRC64; MPDNIKYKNS FYQLKKDLES KIVLLDGAMG TMIMNFDNFR EEKYKGCIDY LVLRKPETVK NIHKMYLEAG SDIIETNTFG ALDITLKDYG LENKAFEINK AAALLARKAV KEYRKENPFE SRNLYVAGAL GPSNKSLSSG NITFEEMA // ID D0HCA4_VIBMI Unreviewed; 1226 AA. AC D0HCA4; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 27-MAY-2015, entry version 34. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEY46351.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEY46351.1}; GN ORFNames=VMA_000598 {ECO:0000313|EMBL:EEY46351.1}; OS Vibrio mimicus VM223. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=675820 {ECO:0000313|EMBL:EEY46351.1}; RN [1] {ECO:0000313|EMBL:EEY46351.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=VM223 {ECO:0000313|EMBL:EEY46351.1}; 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] {ECO:0000313|EMBL:EEY46351.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=VM223 {ECO:0000313|EMBL:EEY46351.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEY46351.1}. 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; ADAJ01000006; EEY46351.1; -; Genomic_DNA. DR RefSeq; WP_000510784.1; NZ_ADAJ01000006.1. DR EnsemblBacteria; EEY46351; EEY46351; VMA_000598. DR PATRIC; 36148451; VBIVibMim144207_0784. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEY46351.1}; KW Transferase {ECO:0000313|EMBL:EEY46351.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1226 AA; 136022 MW; DDC370F3843A5826 CRC64; MGIEVRQQLE QQLKQRILLI DGGMGTMIQS YKLQEEDYRG ARFADWHCDL KGNNDLLVLT QPQIIKDIHS AYLEAGADIL ETNTFNSTTI AMADYDMQSF SDEINFAAAK LAREVAYEWT TKDPSRPRYV AGVLGPTNRT CSISPDVNDP GFRNVTFDQL VQAYSESTRA LIKGGSDLIL IETIFDTLNA KACAFAVDSV FEELGISLPV MISGTITDAS GRTLSGQTTE AFYNALRHVR PISFGLNCAL GPDELRQYVE ELSRISECYV SAHPNAGLPN AFGEYDLSAE DMAEHIAEWA QAGFLNLVGG CCGTTPEHIA AMAKAVDGVK PRALPELKVE CRLSGLEPLN IGPETLFVNV GERTNVTGSA RFKRLIKEEK YDEALDVARE QVENGAQIID INMDEGMLDA EACMVRFLNL CASEPEISKV PVMVDSSKWE VIEAGLKCIQ GKGIVNSISL KEGKEKFIAQ AKLVRRYGAA VIVMAFDEVG QADTRERKLE ICSRAYHILV DEVGFPPEDI IFDPNIFAVA TGIDEHNNYA LDFINAVADI KRELPHAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK HGMDMGIVNA GQLEIYDNVP LKLREAVEDV ILNRRNDGTE RLLEIAEAYR ENSVGKEEDA SALEWRTWPV AKRLEHALVK GITEFIVQDT EEARQQASKP LEVIEGPLMD GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AYLEPFINAQ KSGSTSNGKI LLATVKGDVH DIGKNIVGVV LQCNNFEIID LGVMVPCEQI LKVAREENVD IIGLSGLITP SLDEMVHVAK EMERQGFELP LLIGGATTSK AHTAVKIEQN YHAPVVYVNN ASRAVGVCTS LLSDELRPGF IERLDLDYER TRDQHARKTP KSRPVTLEQA RANKAAIDWA SYTPPFPAKP GVHVFENIQL ATLRPYIDWT PFFMTWSLMG KYPAILEHEE VGEEAKRLFH DANALLDKVE REGLLKASGM CALFPAASVG DDIEVYSDES RTQVAHVLYN LRQQTEKPKG ANYCLSDYVA PKESGKRDWI GAFAVTGGIG ERALADAYKA QGDDYNAIMI QAVADRLAEA FAEYLHEKVR KEIWGYASDE NLSNDELIRE RYQGIRPAPG YPACPEHTEK ATLWQMLNVE ETIGMSLTTS YAMWPGASVS GWYFSHPDSR YFAVAQIQQD QLHSYAERKG WSLEEAEKWL APNLDA // ID D0I572_GRIHO Unreviewed; 1224 AA. AC D0I572; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 27-MAY-2015, entry version 33. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEY73639.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEY73639.1}; GN ORFNames=VHA_000889 {ECO:0000313|EMBL:EEY73639.1}; OS Grimontia hollisae CIP 101886. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Grimontia. OX NCBI_TaxID=675812 {ECO:0000313|EMBL:EEY73639.1}; RN [1] {ECO:0000313|EMBL:EEY73639.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIP 101886 {ECO:0000313|EMBL:EEY73639.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEY73639.1}. 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; ADAQ01000009; EEY73639.1; -; Genomic_DNA. DR RefSeq; WP_005502300.1; NZ_ADAQ01000009.1. DR EnsemblBacteria; EEY73639; EEY73639; VHA_000889. DR PATRIC; 36171777; VBIGriHol144062_0896. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEY73639.1}; KW Transferase {ECO:0000313|EMBL:EEY73639.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 246 246 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1224 AA; 136008 MW; 810B57AA3E3E879E CRC64; MSSRETLEKL LAERILIIDG GMGTMIQSYK LEESDYRGER FADWHCDLKG NNDLLVLTQP NMIKDIHAEY LEAGADILET NTFNATTIAM ADYDMESLSE EINFSAAKLA REAADEWTAK TPDKPRFVAG VLGPTNRTCS ISPDVNDPGY RNVSFDELVT AYSESTRALI KGGSDLILIE TIFDTLNAKA CSFAVQSVFE ELGVTLPVMI SGTITDASGR TLSGQTTEAF YNSLRHVKPI SFGLNCALGP DELRPYVEEL SRISETYVST HPNAGLPNAF GEYDLSPEDM AAHVKEWAES GFLNLVGGCC GTTPEHIRQM HEATQSIKPR TLPELPVACR LSGLEPLTID KETLFVNVGE RTNVTGSARF KRLIKEEQYD EALEVARQQV ENGAQIIDIN MDEGMLDAKA CMVRFLNLCA TEPEIAKVPI MVDSSKWEVI EAGLKCIQGK GIVNSISLKE GKAKFVEQAK LIRRYGAAVI VMAFDEVGQA DTRERKLEIC TNAYRILVDE VGFPPEDIIF DPNIFAIATG IEEHNNYAVD FIEAVADIKR DLPHAMISGG VSNVSFSFRG NNYVREAIHA VFLYHCFKNG MDMGIVNAGQ LEIYDNVPEK LREAVEDVVL NRRDDSTERL LDIAAEYANK GVGKEEDASA LEWRTWPVEK RLEHALVKGI TEFIVDDTEE ARVNASKPLE VIEGPLMDGM NVVGDLFGEG KMFLPQVVKS ARVMKQAVAH LEPFINAEKQ AGSTNGKILL ATVKGDVHDI GKNIVGVVLQ CNNYEIIDLG VMVPCEKILK VAKEENVDII GLSGLITPSL DEMVHVAKEM ERLGFDLPLL IGGATTSKAH TAVKIEQNYN QPVVYVNNAS RAVGVCSSLL SETLKPAFVE KLQADYDVVR EQHARKRPRT KPVTLEKARA NKVAIDWDSY TPPVPAKPGV HVFEDFDVAT LRQYIDWTPF FMTWSLVGKY PAILDHEEVG EEARRLFKDA NDLLDRVERE GLMKASGMCA LFPAASVGDD IEVYTDESRT EVAHVLYHLR QQTEKPKGFN YCLSDYIAPK ESGKKDWIGA FAVTGGIGER ELADAYKAQG DDYNAIMIQA VADRLAEAFA EHLHERVRKE IWGYATDENL SNDDLIREKY QGIRPAPGYP ACPEHTEKGT LWEMLKVEET IGMSLTSSYA MWPGASVSGW YFSHPESRYF AVAQIQEDQR DSYADRKGWD LIDAEKWLGP NLND // ID D0I954_GRIHO Unreviewed; 299 AA. AC D0I954; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EEY71969.1}; GN ORFNames=VHA_002391 {ECO:0000313|EMBL:EEY71969.1}; OS Grimontia hollisae CIP 101886. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Grimontia. OX NCBI_TaxID=675812 {ECO:0000313|EMBL:EEY71969.1}; RN [1] {ECO:0000313|EMBL:EEY71969.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIP 101886 {ECO:0000313|EMBL:EEY71969.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEY71969.1}. 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; ADAQ01000012; EEY71969.1; -; Genomic_DNA. DR RefSeq; WP_005504773.1; NZ_ADAQ01000012.1. DR EnsemblBacteria; EEY71969; EEY71969; VHA_002391. DR PATRIC; 36174894; VBIGriHol144062_2408. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EEY71969.1}; KW Transferase {ECO:0000313|EMBL:EEY71969.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 202 202 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 277 277 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 278 278 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 299 AA; 32778 MW; 28B98042543D2F1C CRC64; MFVLLDGGMG RELQRIGAPF SQPLWSAQAL IEAPEFVYQA HQNFIDAGCD VITVNSYACV PFHLGEQRYK EQGFTLAERA AQIARRAADD SEQEVKVAGC IPPALGSYRP DLFNARQAKP ILQTLVEAQV GYCDFWLAET ISSIEEFQTI HGVLRTTNQP AYYAFSLMDT EVDQPRLRSG ESVIDAIHAV CTAGVDGVLF NCSQPEVMLD AIGVSKGIID DEGKAISLGA YANGFTVIHQ DHEANDALTT MRDLPADEYA AFVRAWLDAG SNIVGGCCAI FPEHIAYLDA LRKRPKNDR // ID D0ICZ2_9VIBR Unreviewed; 1226 AA. AC D0ICZ2; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 01-APR-2015, entry version 33. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEZ01368.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEZ01368.1}; GN ORFNames=VOA_003071 {ECO:0000313|EMBL:EEZ01368.1}; OS Vibrio sp. RC586. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=675815 {ECO:0000313|EMBL:EEZ01368.1}; RN [1] {ECO:0000313|EMBL:EEZ01368.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=RC586 {ECO:0000313|EMBL:EEZ01368.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; ADBD01000003; EEZ01368.1; -; Genomic_DNA. DR RefSeq; WP_000510785.1; NZ_ADBD01000003.1. DR EnsemblBacteria; EEZ01368; EEZ01368; VOA_003071. DR PATRIC; 36177436; VBIVibSp142240_0039. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEZ01368.1}; KW Transferase {ECO:0000313|EMBL:EEZ01368.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1226 AA; 135938 MW; 1BD48DDAB9F3FC05 CRC64; MGIEVRQQLE QQLKQRILLI DGGMGTMIQS YKLQEEDYRG ARFADWHCDL KGNNDLLVLT QPQIIKDIHS AYLEAGADIL ETNTFNSTTI AMADYDMQSL SDEINFAAAK LAREVADEWT TKDPSRPRYV AGVLGPTNRT CSISPDVNDP GFRNVTFDQL VQAYSESTRA LIKGGSDLIL IETIFDTLNA KACAFAVDSV FEELGIRLPV MISGTITDAS GRTLSGQTTE AFYNALRHVR PISFGLNCAL GPDELRQYVE ELSRISECYV SAHPNAGLPN AFGEYDLSAK EMAEHIAEWA QAGFLNLVGG CCGTTPEHIA AMAKAVEGVK PRALPELKVE CHLSGLEPLN IGPETLFVNV GERTNVTGSA RFKRLIKEEQ YDEALDVARE QVENGAQIID INMDEGMLDA EACMVRFLNL CASEPEISKV PVMVDSSKWE VIEAGLKCIQ GKGIVNSISL KEGKEKFIAQ AKLVRRYGAA VIVMAFDEVG QADTRERKLE ICRRAYHILV DEVGFPPEDI IFDPNIFAVA TGIDEHNNYA LDFINAVADI KRELPHAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK HGMDMGIVNA GQLEIYDNVP LKLREAVEDV ILNRRSDGTE RLLEIAEAYR ENSVGKEEDA SALEWRAWPV AKRLEHALVK GITEFIVQDT EEARQQASKP LEVIEGPLMD GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AYLEPFINAQ KSGSTSNGKI LLATVKGDVH DIGKNIVGVV LQCNNFEIID LGVMVPCEQI LKVAREKNVD IIGLSGLITP SLDEMVHVAK EMERQGFELP LLIGGATTSK AHTAVKIEQN YHAPVVYVNN ASRAVGVCTS LLSDELRPGF IERLDLDYER TRDQHARKTP KSRPVTLEQA RANKAAIDWA SYTPPAPAKP GVHVFENIPL ATLRPYIDWT PFFMTWSLMG KYPAILDHEE VGEEAKRLFH DANALLDKVE REGLLKASGM CALFPAASVG DDIEVYSDES RTQVAHVLYN LRQQTEKPKG ANYCLSDYVA PKESGKRDWI GAFAVTGGIG ERALADAYKA QGDDYNAIMI QAVADRLAEA FAEYLHEKMR KEIWGYASDE NLSNDELIRE RYQGIRPAPG YPACPEHTEK ATLWQMLNVE ETIGMSLTTS YAMWPGASVS GWYFSHPDSR YFAVAQIQQD QLHSYAERKG WSLQEAEKWL APNLDA // ID D0IWA9_COMT2 Unreviewed; 358 AA. AC D0IWA9; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 27-MAY-2015, entry version 35. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACY30927.1}; GN OrderedLocusNames=CtCNB1_0181 {ECO:0000313|EMBL:ACY30927.1}; OS Comamonas testosteroni (strain CNB-2). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Comamonas. OX NCBI_TaxID=688245 {ECO:0000313|EMBL:ACY30927.1, ECO:0000313|Proteomes:UP000002360}; RN [1] {ECO:0000313|EMBL:ACY30927.1, ECO:0000313|Proteomes:UP000002360} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CNB-2 {ECO:0000313|Proteomes:UP000002360}; 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 ----------------------------------------------------------------------- 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; ACY30927.1; -; Genomic_DNA. DR RefSeq; WP_003071808.1; NC_013446.2. DR RefSeq; YP_003276223.1; NC_013446.2. DR STRING; 688245.CtCNB1_0181; -. DR EnsemblBacteria; ACY30927; ACY30927; CtCNB1_0181. DR GeneID; 8565368; -. DR KEGG; ctt:CtCNB1_0181; -. DR PATRIC; 35261151; VBIComTes153857_0287. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; CTES543891:GJCV-182-MONOMER; -. DR Proteomes; UP000002360; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002360}; KW Methyltransferase {ECO:0000313|EMBL:ACY30927.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002360}; KW Transferase {ECO:0000313|EMBL:ACY30927.1}. SQ SEQUENCE 358 AA; 38453 MW; B2BF22F3E2C5C011 CRC64; MSQSHPTPAY TRAQELPATL AKRLVILDGA MGTMIQRFKL GEAQYRGEGY AGAEGAGERF KDFAHDVKGN NELLSLTRPD VIRDIHEKYL AAGADLIETN TFGATTIAQE DYHMADLAYE MNLKSAQLAR AACDKYSTPD HKRYVAGALG PTPKTASISP DVNDPAARNI TFEQLRQAYL EQTLALIEGG ADVILVETIF DTLNAKAALF AVDEAFEQTG ERLPIMISGT VTDASGRILS GQTVTAFWHS VRHSNPLSVG LNCALGATLM RPYVQELAKA APDTFISCYP NAGLPNPMSD TGFDETPEIT SRLVHEFAAE GLVNIVGGCC GTTPDHIGAI AKAVQATATR KLFYPAEA // ID D0KAM6_PECWW Unreviewed; 1227 AA. AC D0KAM6; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 29-APR-2015, entry version 45. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACX89682.1}; GN OrderedLocusNames=Pecwa_3951 {ECO:0000313|EMBL:ACX89682.1}; OS Pectobacterium wasabiae (strain WPP163). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Pectobacterium. OX NCBI_TaxID=561231 {ECO:0000313|EMBL:ACX89682.1, ECO:0000313|Proteomes:UP000000315}; RN [1] {ECO:0000313|EMBL:ACX89682.1, ECO:0000313|Proteomes:UP000000315} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WPP163 {ECO:0000313|EMBL:ACX89682.1, RC ECO:0000313|Proteomes:UP000000315}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001790; ACX89682.1; -; Genomic_DNA. DR RefSeq; WP_015731321.1; NC_013421.1. DR RefSeq; YP_003261289.1; NC_013421.1. DR STRING; 561231.Pecwa_3951; -. DR EnsemblBacteria; ACX89682; ACX89682; Pecwa_3951. DR KEGG; pwa:Pecwa_3951; -. DR PATRIC; 32282206; VBIPecWas23660_3901. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PWAS561231:GHO0-4030-MONOMER; -. DR Proteomes; UP000000315; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000315}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135618 MW; D89D6E9A436BE128 CRC64; MSNRLDELRR QLAQRIMVLD GGMGTMIQGY RLQEADYRGE RFADWPSDVK GNNDLLVLTK PQVISEIHDA YLEAGADILE TNTFNATTIA MADYDMASLS AEINTVAAQL ARASADKWTS LTPDKPRYVA GVLGPTNRTA SISPDVNDPA FRNVSFDQLV EAYRESTRAL IAGGVDLIMI ETIFDTLNAK AASFAVESEF EALGIVLPVM ISGTITDASG RTLSGQTTEA FYHSLRHSRP LSFGLNCALG PDELRQYVAE LSRISECYVS AHPNAGLPNA FGEYDLDPAD MAKHIGEWAR SGFLNIVGGC CGSTPAHIAA MAKVVDGVPP RKLPDIPVAC RLSGLEPLII DANTLFVNVG ERTNVTGSAR FKRLIKEEKY NEALDVARQQ VESGAQIIDI NMDEGMLDAE AAMIRFLNLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVEAFIHHA KLVRRYGAAV VVMAFDEVGQ ADTRARKIEI CRRAYRILTE EVGFPPEDII FDPNIFAVAT GIDEHNNYAV DFIEACADIK AELPHAMISG GVSNVSFSFR GNDLVREAIH AVFLYYAIRN GMDMGIVNAS QLAIYDDLPA ELRDAVEDVI LNRRADATER MLELAEKYRG SKTEDEGSKT QAEWRGWDVK KRLEYSLVKG ITEFIELDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGA GKMFLPQVVK SARVMKQAVA YLEPYIEASK DKGSSAGKIL LATVKGDVHD IGKNIVGVVL QCNNYEIIDL GVMVPTDKIL KTAREEKVDI IGLSGLITPS LDEMVNVAKE MERQGFTLPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRSVGVVSAL LSSTQYDDFV ARTRKEYETV RIQHARKKPR TPPVTLEAAR ANASDLDWEN YTPPVAHRLG VQAVTASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG EEAKRLFADA NAMLDDLSTR GALNPRGVVG LFPANRVGDD VVIYTDERRE TVLSVSHHLR QQTEKTDFPN YSLSDFVAPK SSGKPDYLGA FAVTGGLEED TLADQWEAQH DDYNKIMVKA ISDRLAEAFA EYLHERVRKV YWGYAPNENL SNELLIRENY QGIRPAPGYP ACPDHTEKVP IWQLLDVEKH TGMKLTESYA MWPGASVSGW YFSHPDSKYF AVAQIQHDQV KDYAVRKGMD VSEVERWLAP NLGYDAD // ID D0KHG8_PECWW Unreviewed; 313 AA. AC D0KHG8; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 29-APR-2015, entry version 28. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACX88676.1}; GN OrderedLocusNames=Pecwa_2926 {ECO:0000313|EMBL:ACX88676.1}; OS Pectobacterium wasabiae (strain WPP163). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Pectobacterium. OX NCBI_TaxID=561231 {ECO:0000313|EMBL:ACX88676.1, ECO:0000313|Proteomes:UP000000315}; RN [1] {ECO:0000313|EMBL:ACX88676.1, ECO:0000313|Proteomes:UP000000315} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WPP163 {ECO:0000313|EMBL:ACX88676.1, RC ECO:0000313|Proteomes:UP000000315}; 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 ----------------------------------------------------------------------- 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; ACX88676.1; -; Genomic_DNA. DR RefSeq; WP_015730809.1; NC_013421.1. DR RefSeq; YP_003260283.1; NC_013421.1. DR STRING; 561231.Pecwa_2926; -. DR EnsemblBacteria; ACX88676; ACX88676; Pecwa_2926. DR KEGG; pwa:Pecwa_2926; -. DR PATRIC; 32280060; VBIPecWas23660_2845. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; PWAS561231:GHO0-2983-MONOMER; -. DR Proteomes; UP000000315; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000315}; KW Methyltransferase {ECO:0000313|EMBL:ACX88676.1}; KW Transferase {ECO:0000313|EMBL:ACX88676.1}. SQ SEQUENCE 313 AA; 33499 MW; B8B4A9A39A2F64C4 CRC64; MRKNTVTNML ATASTIVLDG ALATELEARG CDLTDPLWSA KVLVENPALI YQVHLDYFNA GAQCAITASY QATPQGFKAR GYSEAESLTL IAKSVQLAAQ ARDDYRRDNS QAGVLLVAGS VGPYGAYLAD GSEYRGDYQL PQAEMMAFHR PRIAALHEAG ADLLACETLP SFAEVEALIA LLAEFPQAQA WFSFTLRDSE HLSDGTPLHT VLERVNACPQ VVAVGINCIA LENVTPALTY LSLLTNLPLV VYPNSGEQYD AVTKTWSSAH DAACSLAAYL PEWQAAGARL IGGCCRTTPA DIAGIARCCQ HEG // ID D0KYI6_HALNC Unreviewed; 1238 AA. AC D0KYI6; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 29-APR-2015, entry version 44. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACX95509.1}; GN OrderedLocusNames=Hneap_0657 {ECO:0000313|EMBL:ACX95509.1}; OS Halothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus OS neapolitanus). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Halothiobacillaceae; Halothiobacillus. OX NCBI_TaxID=555778 {ECO:0000313|EMBL:ACX95509.1, ECO:0000313|Proteomes:UP000009102}; RN [1] {ECO:0000313|EMBL:ACX95509.1, ECO:0000313|Proteomes:UP000009102} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23641 / c2 {ECO:0000313|Proteomes:UP000009102}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001801; ACX95509.1; -; Genomic_DNA. DR RefSeq; WP_012823545.1; NC_013422.1. DR RefSeq; YP_003262556.1; NC_013422.1. DR STRING; 555778.Hneap_0657; -. DR EnsemblBacteria; ACX95509; ACX95509; Hneap_0657. DR KEGG; hna:Hneap_0657; -. DR PATRIC; 32205152; VBIHalNea120669_0662. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; HNEA555778:GIVV-681-MONOMER; -. DR Proteomes; UP000009102; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000009102}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000009102}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 253 253 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 316 316 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 769 769 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1238 AA; 136282 MW; 69899BAAF3724A7C CRC64; MTQKIIEQPV FAQLRALMHE RILILDGAMG TMIQKRRLSE SEFRGERFAD WPVDLKGNND LLVLTQPKVI SDIHRAYLDA GADIIEANTF NATRISMADY QMQELAYEIN VAAARLAREC ADAKTLETPE KPRFVAGIIG PTSRTGSISP DVNDPGFRNV TFEELSSAYR ESAEGLIEGG VDILLIETIF DTLNAKAAVF ALEQLFADRG QRWPVMISGT ITDASGRTLS GQTTEAFYNS LRHAQPLSIG LNCALGPDLL RQYVAELSRV SEFPVSVHPN AGLPNELGEY DLEADPMAQQ IGEWARSGLI NIVGGCCGTT PEHIAYMAQQ VAPHPPRVPP KPEPACRLSG LEPFNITPES LFVNVGERTN VTGSARFRRL IKEGDFTTAL DVARQQVEAG AQIIDINMDE GLIDGEAAME RFLKLIASEP DISRVPIMID SSKFAVIEKG LQWVQGKPIV NSISMKEGED IFLEHARLVR RYGAAAVVMA FDEHGQADTV QRRIEICSRA YKLLTEEVGF PAEDIIFDPN IFAIATGIEE HNNYAVDFIE GTRWIKQNLP HALISGGVSN VSFSFRGNEP VREAIHSVFL NHAVAAGMDM GIVNAGQLVI VDDIPAELRE AVEDIVLNRR DDATDRMLDI AEKYRGSGTG EAKSGADLAW RELPVNKRLS HSLIKGIDQF VIEDTEEARL AAERPLHVIE GPLMDGMNIV GDLFGAGKMF LPQVVKSARV MKKAVAHLLP FMEAEAAAGG CAAETAGKIL MATVKGDVHD IGKNIVGVVL QCNGFEIVDL GVMVPTQKIL DTAIAEQCDI IGLSGLITPS LDEMVTVASE MQRQGFTLPL MIGGATTSKL HTALKIAPVY EQPVVHVLDA SRAVGVAASL LGENKAVYVQ GIANEYAELV ARRKANQKEA KRANLAEARA NKQVMDYSNY TPVAPKTPGI TVFEDYPLED ILPFIDWTPF FQSWQLFGKY PAILDDEKVG LEARKLFDDA QAMLKTMVEE KWVKASGVIG FWPAASIDDD IRVFTDEKRQ SVLTTLHHIR QQMPRSGGKP NQCLADFVAP TGKKIKDWIG GFAVTTGHGI EPHIERFEKA MDDYHAILLK ALADRLAEAF AEHLHYRVRT EFWGYAPDEP MDNDAMIAEQ YQGIRPAPGY PACPDHTEKG TLWSLLEPET RAGISLTENF AMYPGAAVSG WYFAHPDARY FGTGKIGRDQ VHDYAERKGW SLKESERWLA PILGYEPE // ID D0LDR3_GORB4 Unreviewed; 1199 AA. AC D0LDR3; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 27-MAY-2015, entry version 44. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACY21686.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ACY21686.1}; GN OrderedLocusNames=Gbro_2445 {ECO:0000313|EMBL:ACY21686.1}; 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 {ECO:0000313|EMBL:ACY21686.1, ECO:0000313|Proteomes:UP000001219}; RN [1] {ECO:0000313|Proteomes:UP000001219} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25592 / DSM 43247 / JCM 3198 / NCTC 10667 RC {ECO:0000313|Proteomes:UP000001219}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001802; ACY21686.1; -; Genomic_DNA. DR RefSeq; WP_012834241.1; NC_013441.1. DR RefSeq; YP_003273579.1; NC_013441.1. DR STRING; 526226.Gbro_2445; -. DR EnsemblBacteria; ACY21686; ACY21686; Gbro_2445. DR KEGG; gbr:Gbro_2445; -. DR PATRIC; 32184503; VBIGorBro114338_2502. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; GBRO526226:GHJF-2478-MONOMER; -. DR Proteomes; UP000001219; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001219}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACY21686.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001219}; KW Transferase {ECO:0000313|EMBL:ACY21686.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 240 240 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 750 750 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1199 AA; 130734 MW; 4F71BBF1480F805E CRC64; MSSVSRPDHS TDPADFDTTF MSAMSRRVLI GDGAMGTMLQ AADLTLDDFN GLEGCNEILN DARPDVLEGI HRAYFEAGAD AVETNTFGCN LSNLGDYDIA DRIRELAYKG TGIARGVADE MGPTANGTDR FVLGSIGPGT KLPSLGHTTF AVIRDAYFEC VAGMLDGGAD AILIETSQDL LQVKAAVVAA RRAMDKLGRR IPIISHVTVE TTGTMLLGSE IGAALTAIEP LGVDMIGLNC ATGPAEMSEH LRYLSRHARI PVSVMPNAGL PVLGPNGAEY PLSPEELAQA LHGFVAEFGL DFVGGCCGTT PEHIRQVAEA VHGATPAART PEHASETSSL YTAVPFDQDA SFLVIGERTN TNGSKAFREA MIAGDYQRCL DIAKDQTRDG AHMLDLNVDY VGRDGAVDMT ALASRFATSS TLPIMLDSTE PEVIRAGLET LGGRCAVNSV NYEDGDGPNS RFTRIMQLVV EHGAAVVALT IDEEGQARTA DWKVRIAERL IADITGNWGL AEEDIIIDAL TFPISTGQEE VRRDGIETIE AIRRIHEAHP EVHFTLGISN ISFGLNPAAR QVLNSVFLHE CVQAGLDTAI VHASKILPMA RIPEEHRKVA LDLVYDRRAP GYDPLQKLME LFEGVSAASA RESRAAELAK LPLFERLERR IVDGERNGLE DDLDEAMTTV PPLKIINETL LSGMKTVGEL FGSGQMQLPF VLQSAEVMKT AVAHLEPHME STGEDGKGRI VLATVKGDVH DIGKNLVDII LSNNGYEVVN IGIKQPITNI LDVAADKKVD VIGMSGLLVK STVVMKENLE EINARGLADE YPVLLGGAAL TRSYVENDLS ETYEGDVHYA RDAFEGLRLM DEIMATKRGE GPDPDSPEAI AAAEKAAERK ARHDRSKRIA AKRKAAEEPV EVPARSDVAA DNDIPAPPFW GTRIVKGVPV ADYLQLLDER ALFLGQWGLR GARGGDGPSY EDLVESEGRP RLRYWIDRLA TEGILQHAAV VYGYFPAVSD GDTVHVLTEP RPDAPVRYSF GFPRQQRSRF LCIADFIRSR EDAIRDGHVD VLPFQLVTMG QPIADFANEL FAADAYRDYL EVHGIGVQLT EALAEYWHQR VRSELRFGER TMDSEDPDEA QGFFDLEYRG ARFSFGYGAC PDLDDRAKMM ELLQPERIGV HLSEELQLHP EQSTDAFVLH HPEAKYFNT // ID D0LSQ2_HALO1 Unreviewed; 643 AA. AC D0LSQ2; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 27-MAY-2015, entry version 42. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=Hoch_4784 {ECO:0000313|EMBL:ACY17274.1}; OS Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Nannocystineae; Kofleriaceae; Haliangium. OX NCBI_TaxID=502025 {ECO:0000313|EMBL:ACY17274.1, ECO:0000313|Proteomes:UP000001880}; RN [1] {ECO:0000313|EMBL:ACY17274.1, ECO:0000313|Proteomes:UP000001880} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14365 / JCM 11303 / SMP-2 RC {ECO:0000313|Proteomes:UP000001880}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {ECO:0000256|RuleBase:RU004255}. CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ACY17274.1; -; Genomic_DNA. DR RefSeq; WP_012829872.1; NC_013440.1. DR RefSeq; YP_003269167.1; NC_013440.1. DR ProteinModelPortal; D0LSQ2; -. DR STRING; 502025.Hoch_4784; -. DR EnsemblBacteria; ACY17274; ACY17274; Hoch_4784. DR KEGG; hoh:Hoch_4784; -. DR PATRIC; 32199405; VBIHalOch22000_4826. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; HOCH502025:GI43-4821-MONOMER; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000001880; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004255}; KW Complete proteome {ECO:0000313|Proteomes:UP000001880}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ACY17274.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000001880}; KW Transferase {ECO:0000313|EMBL:ACY17274.1}. SQ SEQUENCE 643 AA; 68442 MW; 63F33DE4996966ED CRC64; MSGTSCLKPF LEALAQGPLL FDGAMGSLLY DRGVFHTRNY DELSLSQPKL IRAVHREYLE AGAQILETNT FGANRIKLTA HGHSERVADI NRAAVEMARS VADDRAYVAG AVGPTGIRYT IAPAAERKRA IEALGEQIDY LVEAGVDLLC LETFGAILEL EAAIELARQI APEMPVVAHL VFDADGLVEG ELDGATVAQR LIAAGANAVG ANCGVGPPEL YAVGTKMSDV GAPVSIQPNA GFPSNIDGRT IYVANPEHFG VFARRMLKSG VRMVGGCCGT TPEHVRAMLG AVRMCGGADI FRPASAPVTV SVRAATEPPV PREVVVPLAM RSRLGARLAA GQFAVSVELT APAGTDDSKL LGNIRTLLEA GVDVVNIADG PRASARTGNL AVCTKLQATT GVEPILHVCT RDRNYLGLIA HLLGAHALGI RNMVIITGDP PKMGDYPFAT PVYDVDSIGL LRMARTLNEG YDPAGKEIDG HTSFVLATGA EPAATDYERE MRRLEDKRAA GAELVMTQPV YDPRVLERFL DDAEPLGLPV MVGILPLASH RNAEFLHNEV PGMQIPQSYR DRMEKVGSGP EARAEGVRIA QEALEAVKHR VAGVYIMPPF NRVSSAIEVL DVVRDRWQPA PLPAPGGPLR GPA // ID D0LTG7_HALO1 Unreviewed; 311 AA. AC D0LTG7; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACY13862.1}; GN OrderedLocusNames=Hoch_1304 {ECO:0000313|EMBL:ACY13862.1}; OS Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Nannocystineae; Kofleriaceae; Haliangium. OX NCBI_TaxID=502025 {ECO:0000313|EMBL:ACY13862.1, ECO:0000313|Proteomes:UP000001880}; RN [1] {ECO:0000313|EMBL:ACY13862.1, ECO:0000313|Proteomes:UP000001880} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14365 / JCM 11303 / SMP-2 RC {ECO:0000313|Proteomes:UP000001880}; 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 ----------------------------------------------------------------------- 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; ACY13862.1; -; Genomic_DNA. DR RefSeq; WP_012826471.1; NC_013440.1. DR RefSeq; YP_003265755.1; NC_013440.1. DR STRING; 502025.Hoch_1304; -. DR EnsemblBacteria; ACY13862; ACY13862; Hoch_1304. DR KEGG; hoh:Hoch_1304; -. DR PATRIC; 32192270; VBIHalOch22000_1280. DR eggNOG; COG2040; -. DR HOGENOM; HOG000179103; -. DR OrthoDB; EOG6R5C46; -. DR BioCyc; HOCH502025:GI43-1316-MONOMER; -. DR Proteomes; UP000001880; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001880}; KW Methyltransferase {ECO:0000313|EMBL:ACY13862.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001880}; KW Transferase {ECO:0000313|EMBL:ACY13862.1}. SQ SEQUENCE 311 AA; 33117 MW; F42B6423D4621115 CRC64; MKGFAVSTLF SNAPVWLTWT GMETDLIFNK GVDLPGFAAF TLLKTEEGRE RIARYYDEIA ALARKTGVGA LIETVTWMAN PDRAVGIGYS PEDLDRFNAE AVAIARAAKE RAKDVPLLVS LQIGPRGDGY AAGMATADEA QEYHGRQIAV GAKAGVDVAS AYTLGSAEEA IGVIRAAKAV GLPVTVSFTV ETDGKLADGS RLEDAILRTD AETDSAAIAY AVNCAHPDHI APALTEGPWS ERLMGVVANA SRQSHEELDN SEELDDGDPQ ELGQQIASMK QQLPRVQLVG GCCGTDMRHL EQIATRAMAA R // ID D0LXL7_HALO1 Unreviewed; 1266 AA. AC D0LXL7; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 27-MAY-2015, entry version 45. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACY17772.1}; GN OrderedLocusNames=Hoch_5287 {ECO:0000313|EMBL:ACY17772.1}; OS Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Nannocystineae; Kofleriaceae; Haliangium. OX NCBI_TaxID=502025 {ECO:0000313|EMBL:ACY17772.1, ECO:0000313|Proteomes:UP000001880}; RN [1] {ECO:0000313|EMBL:ACY17772.1, ECO:0000313|Proteomes:UP000001880} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14365 / JCM 11303 / SMP-2 RC {ECO:0000313|Proteomes:UP000001880}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001804; ACY17772.1; -; Genomic_DNA. DR RefSeq; WP_012830364.1; NC_013440.1. DR RefSeq; YP_003269665.1; NC_013440.1. DR STRING; 502025.Hoch_5287; -. DR EnsemblBacteria; ACY17772; ACY17772; Hoch_5287. DR KEGG; hoh:Hoch_5287; -. DR PATRIC; 32200473; VBIHalOch22000_5355. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; HOCH502025:GI43-5329-MONOMER; -. DR Proteomes; UP000001880; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001880}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001880}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 353 353 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 354 354 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 802 802 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1266 AA; 139299 MW; 633CF0B328FEA21C CRC64; MAARSDGSIS VPTVGRRSAF PGDFELPLEL DGVSVQSSQH MASNEETTTA LLHKLMRERI LVIDGAMGTM IQRQGLDEDD YRGTRFQDHP SSLKGCNDLL GLTQPKLIEE LHLQFLRAGA DIIETNTFNA NAVAMADYAM EAQVREMNLA SAQVARRAVE RFASESERVC MIAGSMGPTT KTASLSPDVN DPGARGITYD ELVTIYYEQA QALLEGGVDL LLAETSFDTL NMRAALFAIQ KLFADGGRRV PVMSSATITD RSGRTLSGQT IAAYYQSVAH VDLSYIGINC ALGADEMRPY VEELAGLSRF PVACVPNAGL PNELGEYDET PESMGALLGE FANNGWLNFA GGCCGTRPEH IAAIADAVAG VAPRKPAEPK PFTSLSGLEP LVITPESNFT MIGERTNVTG SRKFKRLIMN DHYEEAVEVA RQQVEGGANI IDVCMDEGML ESEAAMTRFL NLIAAEPDIA RVPVMIDSSK FTVIEAGLKC IQGKGVVNSI SLKEGEEAFK EHASLIRRYG AAVVVMAFDE TGQATTVDHR LTIARRAYRI LTEELGFPPE DIIFDPNILT VGTGIEEHAD YAVSFIEAVR QIKAEMPLCK VSGGVSNISF SFRGNDPVRE AMHAAFLYHA IKAGLDMGIV NAGQLEVYDE IEPELRERVE DVLLNRRADA TERLIDFASS YTREETEKQD VKQWRTGTLE ERMSHALVKG IADHVDEDVA EALEKYPSPL SIIEGPLMDG MNVVGGLFGE GKMFLPQVVK SARVMKKAVA ILEPLMEEEK RKSGKTHAKG KMVIATVKGD VHDIGKNIVG VVLRCNGYEV EDLGVMVPAK QILDAAREMK ADVVGLSGLI TPSLDEMIHV AKEMKRLKMN IPLLIGGATT SGKHTAVKIA PVYDGPSVHV GDASLAVGVL GKLLSSTQRD GFVAANADKQ ATLRENFERT QKQRTLLPLA EARARKVEVE WRAEDVAKPA FVGTRTLTED DIPVSDLVPW IDWSPFFHAW ELKGLYPAIL DHERYGERAR ELFDDGQKLL RRICDEKLLR ARGVYGFFPA ASEGEDIVIY DQERENERAR FYFLRQQEDK RPCFCLADYV APASSQLQDH IGGFTVTAGL GTDELVAEFE RDHDDYQAIM VKALADRLAE AFAEMLHKRV RDEWGYGKQE DIDFQSVLSE NYRGIRPAFG YPACPDHSDK STLFSLLDAT EATGVSLTES MAMTPTAAVS GIYLGHPQSR YFAVRRLGRD QVEDYAARKG ISRQEAERWL APYLTY // ID D0M6H6_VIBSE Unreviewed; 1226 AA. AC D0M6H6; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 01-APR-2015, entry version 41. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:ACY50517.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ACY50517.1}; GN OrderedLocusNames=VEA_002355 {ECO:0000313|EMBL:ACY50517.1}; OS Vibrio sp. (strain Ex25). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=150340 {ECO:0000313|EMBL:ACY50517.1, ECO:0000313|Proteomes:UP000002571}; RN [1] {ECO:0000313|Proteomes:UP000002571} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ex25 {ECO:0000313|Proteomes:UP000002571}; 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. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001805; ACY50517.1; -; Genomic_DNA. DR RefSeq; WP_012841363.1; NC_013456.1. DR RefSeq; YP_003284982.1; NC_013456.1. DR STRING; 150340.VEA_002355; -. DR EnsemblBacteria; ACY50517; ACY50517; VEA_002355. DR KEGG; vex:VEA_002355; -. DR PATRIC; 32534667; VBIVibSp203755_0744. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; VSP150340:GJJG-813-MONOMER; -. DR Proteomes; UP000002571; Chromosome 1. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002571}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ACY50517.1}; KW Transferase {ECO:0000313|EMBL:ACY50517.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1226 AA; 136418 MW; C114AFD1DAC3F8D0 CRC64; MGSNVRQQIE AQLKQRILLI DGGMGTMIQG YKLEEQDYRG TRFADWHCDL KGNNDLLVLS QPQLIKEIHA AYLGAGADIL ETNTFNATTI AMADYEMESL SEEINFAAAK LAREVADEWT AKTPDKPRYV AGVLGPTNRT CSISPDVNDP GYRNVSFDEL VEAYSESTRA LIKGGSDLIL IETIFDTLNA KACSFAVESV FEEMGIELPV MISGTITDAS GRTLSGQTTE AFYNSLRHVK PISFGLNCAL GPDELRPYVE DLSRISESFV SAHPNAGLPN AFGEYDLSPE DMAKHVQEWA QSGFLNLIGG CCGTTPEHIR QMALAVENVA PRQLPDLPVA CRLSGLEPLA IDKDSLFINV GERTNVTGSA RFKRLIKEEL YDEALDVARQ QVENGAQIID INMDEGMLDA QACMVRFLNL CASEPEISKV PIMVDSSKWE VIEAGLKCIQ GKGIVNSISL KEGKEKFVEQ AKLIRRYGAA VIVMAFDEIG QADTRERKVE ICTNAYRILV DEVGFPPEDI IFDPNIFAIA TGIEEHNNYA VDFIEAVGDI KRDLPHAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK NGMDMGIVNA GQLEIYDNVP ETLREAVEDV VLNRRDDATE RLLDIAAEYA GKGVGKEEDA SALEWRTWPV EKRLEHALVK GITEFIVDDT EEARVNASKP LEVIEGPLMD GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AHLEPYINAE KQVGQTNGKI LLATVKGDVH DIGKNIVGVV LQCNNYEIID LGVMVPCEKI LKVAQEENVD IIGLSGLITP SLDEMVHVAK EMERLDFNLP LLIGGATTSK AHTAVKIEQN YKHPVVYVNN ASRAVGVCTS LLSDERRPEF VEKLEADYER VRDQHNRKKP RTKPVTLEAA RANKVAIDWE AYTPPVPVKP GIHIFDDFDV AILRQYIDWT PFFMTWSLVG KYPTIFQHEE VGEEAKRLFE DANELLDRVE REGLLKARGM CGLFPAASVG DDIEVYADET RTDVVKVLRN LRQQTEKPKG FNYCLSDYIA PKESGKHDWI GAFAVTGGIG ERELADEYKA QGDDYNAIMI QAVADRLAEA FAEYLHERVR KEIWGYAADE DLSNNDLIRE KYQGIRPAPG YPACPEHTEK GPLWELLNVE ENIGMTLTSS YAMYPGASVS GWYFSHPDSR YFAIAQIQED QLESYADRKG WDRIEAEKWL GPNING // ID D0MF55_RHOM4 Unreviewed; 1236 AA. AC D0MF55; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 29-APR-2015, entry version 45. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACY49311.1}; GN OrderedLocusNames=Rmar_2433 {ECO:0000313|EMBL:ACY49311.1}; 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 {ECO:0000313|EMBL:ACY49311.1, ECO:0000313|Proteomes:UP000002221}; RN [1] {ECO:0000313|EMBL:ACY49311.1, ECO:0000313|Proteomes:UP000002221} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43812 / DSM 4252 / R-10 RC {ECO:0000313|Proteomes:UP000002221}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001807; ACY49311.1; -; Genomic_DNA. DR RefSeq; WP_012844921.1; NC_013501.1. DR RefSeq; YP_003291699.1; NC_013501.1. DR STRING; 518766.Rmar_2433; -. DR EnsemblBacteria; ACY49311; ACY49311; Rmar_2433. DR KEGG; rmr:Rmar_2433; -. DR PATRIC; 32319009; VBIRhoMar93821_2460. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; RMAR518766:GJJ8-2480-MONOMER; -. DR Proteomes; UP000002221; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002221}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002221}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1236 AA; 138337 MW; 9A6C65379DDB7E0E CRC64; MLDTHPLARL LQERILILDG AMGTLIQRHR LAEEDFRGAR FADHPHPLRG NNDLLVLTQP ELIRDIHRAY LEAGADLIET NTFNANAISQ ADYGLEHLVY ELNVAAARLA REVADEYTRR APERPRFVAG AIGPTNKTLS ISPDVNNPAY RAVTFDEMVA VYREQVRGLL DGGVDVLLVE TVFDTLNCKA ALFAIQEEFH VRGRAVPVMV SGTIVDQSGR TLSGQTPEAF WISIAHMPHL LSVGLNCALG SGQMRPFIEE LARVATVFTS LYPNAGLPDE LGQYREMPEY MAAQLADYAR EGWLNLAGGC CGTTPEHIRA IAEALEGLPP RRIPEVPRTL RLSGLEPLVF RPDLNFVNIG ERTNVTGSRR FARLIREGRY EEALDVAREQ VENGAQMIDV NMDEGLLDGV QAMTTFLNLI ATEPEIARVP VVIDSSKWEV IEAGLKCLQG KGVVNSLSLK DGEEVFKERA RRVRQYGAAV IVMAFDEQGQ ADTLERRIEI CRRAYRILTE EVGFPPEDII FDPNIYAVAT GIPEHNRYAI DFLEATRWIK ANLPYARVSG GISNLSFSFR GNEPVRQAMH TVFLYHAVQA GMDMGIVNPG QLGIYEEIDP ELRERIEDVL FDRRPDATER LIALAQTLTQ SAADAAESEM LAWRQAPVEE RLRHALVKGI TEFIEEDVEE ARQKYGSPLA VIEGPLMDGM NVVGDLFGAG KMFLPQVVKS ARVMKKAVAY LVPFLEAEKQ KLGDTRPRAR ILLATVKGDV HDIGKNIVGV VLQCNGFEVI DLGVMVPADR ILEEARRHRV DLIGLSGLIT PSLDEMVHVA RELERAGFDT PLLIGGATTS KVHTALKIDP CYHAPVVHVL DASRAVPVAS ALVDPDRRDA FAEEIRQEYE AIRRRHGRRT DEQLLTLEEA RANRFTCDWS AVPITRPNRP GLTVFRNYPL AEIRRYIDWT PFFQAWELRG KYPRILDDPV KGPEARRLFA DANRLLDEII AHGWLQAHGV VGLFPANSRG DDVLVFADEA RREVRAVLHF LRQQTPKRTG QPNRSLADYV APVESGRADY IGAFAVTAGH GLEELVARFE RAHDDYQAIL AKALADRLAE AFAELLHERV RRELWGYAPD ERLTNEELIA ERYRGIRPAP GYPACPDHTE KWTLWELLEA ERHTGIRLTE HLAMHPAASV CGYYLAHPEA SYFNVGHLGM DQIEDYARRK GMTVEEVERW LAPRLAYDPA ARADAA // ID D0MU48_PHYIT Unreviewed; 1203 AA. AC D0MU48; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 27-MAY-2015, entry version 45. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEY61495.1}; GN ORFNames=PITG_01804 {ECO:0000313|EMBL:EEY61495.1}; OS Phytophthora infestans (strain T30-4) (Potato late blight fungus). OC Eukaryota; Stramenopiles; Oomycetes; Peronosporales; Phytophthora. OX NCBI_TaxID=403677 {ECO:0000313|Proteomes:UP000006643}; RN [1] {ECO:0000313|Proteomes:UP000006643} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T30-4 {ECO:0000313|Proteomes:UP000006643}; RX PubMed=19741609; DOI=10.1038/nature08358; RG The Broad Institute Genome Sequencing Platform; RA Haas B.J., Kamoun S., Zody M.C., Jiang R.H., Handsaker R.E., RA Cano L.M., Grabherr M., Kodira C.D., Raffaele S., Torto-Alalibo T., RA Bozkurt T.O., Ah-Fong A.M., Alvarado L., Anderson V.L., RA Armstrong M.R., Avrova A., Baxter L., Beynon J., Boevink P.C., RA Bollmann S.R., Bos J.I., Bulone V., Cai G., Cakir C., Carrington J.C., RA Chawner M., Conti L., Costanzo S., Ewan R., Fahlgren N., RA Fischbach M.A., Fugelstad J., Gilroy E.M., Gnerre S., Green P.J., RA Grenville-Briggs L.J., Griffith J., Grunwald N.J., Horn K., RA Horner N.R., Hu C.H., Huitema E., Jeong D.H., Jones A.M., Jones J.D., RA Jones R.W., Karlsson E.K., Kunjeti S.G., Lamour K., Liu Z., Ma L., RA Maclean D., Chibucos M.C., McDonald H., McWalters J., Meijer H.J., RA Morgan W., Morris P.F., Munro C.A., O'Neill K., Ospina-Giraldo M., RA Pinzon A., Pritchard L., Ramsahoye B., Ren Q., Restrepo S., Roy S., RA Sadanandom A., Savidor A., Schornack S., Schwartz D.C., Schumann U.D., RA Schwessinger B., Seyer L., Sharpe T., Silvar C., Song J., RA Studholme D.J., Sykes S., Thines M., van de Vondervoort P.J., RA Phuntumart V., Wawra S., Weide R., Win J., Young C., Zhou S., Fry W., RA Meyers B.C., van West P., Ristaino J., Govers F., Birch P.R., RA Whisson S.C., Judelson H.S., Nusbaum C.; RT "Genome sequence and analysis of the Irish potato famine pathogen RT Phytophthora infestans."; RL Nature 461:393-398(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; DS028119; EEY61495.1; -; Genomic_DNA. DR RefSeq; XP_002908412.1; XM_002908366.1. DR UniGene; Pin.3643; -. DR EnsemblProtists; PITG_01804T0; PITG_01804T0; PITG_01804. DR GeneID; 9469275; -. DR KEGG; pif:PITG_01804; -. DR EuPathDB; FungiDB:PITG_01804; -. DR HOGENOM; HOG000251409; -. DR InParanoid; D0MU48; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR Proteomes; UP000006643; Partially assembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006643}; KW Reference proteome {ECO:0000313|Proteomes:UP000006643}. SQ SEQUENCE 1203 AA; 133946 MW; 758FCBA5827F8374 CRC64; MRSNVTAEEV AMLQRPFVRG ETDIFAYLTA LMKQRTLIFD GGMGTMIQVH KFTEEDFRSE RFKDSPCLVK GNNDLLSITQ PHIIKEIHKQ YMQIGRAQLI GTNTFSGTTI AQADYQMEHL VYELNYESAK LAREAADEVT QLDPLLPRFV AGSIGPTNRT LSISPNVEDP GFRNVTFDEL VDAYYTQVEG LVDGGSDVLL VETIFDTLNA KAAVFAINKY QEATGRKLPL FISGTIVDMS GRTLSGQTTE AFYVSLRHSK PFCIGLNCAL GANQMKPFLQ RLANVAECFV SVYANAGLPN AMGGYDDTPA MMAEYCEEFS KDRLVNMMGG CCGTTPQHIQ AIAKMTTKYD PRPLPELKEP FMWLSGLEDM VVTKERFSFL NVGERCNISG SIRFKRLIMK SDYGTAMDVA RQQVEDGAMV IDVNVDDGML DGVAAMERFL KIAVTEPDVS KVPFMIDSSK FHIVEAGLKC VQGKCIVNSI SLKVGKELFM EHARIVKNHG AAVVVMAFDE EGQAATEAEK VRICKRSYDI LVNEVGFPPE DIIFDPNILT VATGMEEHNN YGVDFINACR IIKEQNPYCG AVAAAGNKQE WRSKPIGERL TYSLVKGISE FIDQDVEEMR KVADKPLDVI EGPLMDGMNV VGELFGSGKM FLPQVIKSAR VMKKAVAYLL PFMEEEKNKR RLANAANGIA NEEEDEDSQY AGKVLIATVK GDVHDIGKNI VGVVLGCNNY KIIDLGVMVP CENILAAAKE YNVDVIGLSG LITPSLDEMV HVAREMSKAG LNIPLIVGGA TTSKMHAAVK IAPHYSTPEH PVMHVLDASR SVVVVGNLLR QDEERDEFVE EVMEEYEEMQ EDYYASLDDI KLVGFQDAKT KSYQIDYTAS PPFQKINRVG LHVIEDLPLE ELVPIIDWNP FFQTWELRGR YPNRGYPKIF DDEAVGAEAR KVFDEAQKLL QEIMDKKLLR VRGVSGIFPA YRDGDDVVVC DPKNTDQDIS KFCMLRQQAE KETSDPYMSL ADFIAPKGVG QDYIGGFAVG VFGVEEMAAK FEADHDDFNK IMSQAIGDRL AEAFAEYIHR EMRVKDWGYA ADEVLDKEDL LKVKYDGIRP APGYPSQPDH TEKRALWDLL KADELIDLNL TDSYMMLPGS AVSALCFAHP DSQYFAVGKI GKDQVVEYAK RKGQTLEETE RWLAPILGYD RSARPALEGD TQG // ID D0NMR7_PHYIT Unreviewed; 319 AA. AC D0NMR7; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 29-APR-2015, entry version 24. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EEY61824.1}; GN ORFNames=PITG_13769 {ECO:0000313|EMBL:EEY61824.1}; OS Phytophthora infestans (strain T30-4) (Potato late blight fungus). OC Eukaryota; Stramenopiles; Oomycetes; Peronosporales; Phytophthora. OX NCBI_TaxID=403677 {ECO:0000313|Proteomes:UP000006643}; RN [1] {ECO:0000313|Proteomes:UP000006643} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T30-4 {ECO:0000313|Proteomes:UP000006643}; RX PubMed=19741609; DOI=10.1038/nature08358; RG The Broad Institute Genome Sequencing Platform; RA Haas B.J., Kamoun S., Zody M.C., Jiang R.H., Handsaker R.E., RA Cano L.M., Grabherr M., Kodira C.D., Raffaele S., Torto-Alalibo T., RA Bozkurt T.O., Ah-Fong A.M., Alvarado L., Anderson V.L., RA Armstrong M.R., Avrova A., Baxter L., Beynon J., Boevink P.C., RA Bollmann S.R., Bos J.I., Bulone V., Cai G., Cakir C., Carrington J.C., RA Chawner M., Conti L., Costanzo S., Ewan R., Fahlgren N., RA Fischbach M.A., Fugelstad J., Gilroy E.M., Gnerre S., Green P.J., RA Grenville-Briggs L.J., Griffith J., Grunwald N.J., Horn K., RA Horner N.R., Hu C.H., Huitema E., Jeong D.H., Jones A.M., Jones J.D., RA Jones R.W., Karlsson E.K., Kunjeti S.G., Lamour K., Liu Z., Ma L., RA Maclean D., Chibucos M.C., McDonald H., McWalters J., Meijer H.J., RA Morgan W., Morris P.F., Munro C.A., O'Neill K., Ospina-Giraldo M., RA Pinzon A., Pritchard L., Ramsahoye B., Ren Q., Restrepo S., Roy S., RA Sadanandom A., Savidor A., Schornack S., Schwartz D.C., Schumann U.D., RA Schwessinger B., Seyer L., Sharpe T., Silvar C., Song J., RA Studholme D.J., Sykes S., Thines M., van de Vondervoort P.J., RA Phuntumart V., Wawra S., Weide R., Win J., Young C., Zhou S., Fry W., RA Meyers B.C., van West P., Ristaino J., Govers F., Birch P.R., RA Whisson S.C., Judelson H.S., Nusbaum C.; RT "Genome sequence and analysis of the Irish potato famine pathogen RT Phytophthora infestans."; RL Nature 461:393-398(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; DS028147; EEY61824.1; -; Genomic_DNA. DR RefSeq; XP_002899464.1; XM_002899418.1. DR UniGene; Pin.10365; -. DR EnsemblProtists; PITG_13769T0; PITG_13769T0; PITG_13769. DR GeneID; 9461332; -. DR KEGG; pif:PITG_13769; -. DR EuPathDB; FungiDB:PITG_13769; -. DR HOGENOM; HOG000265278; -. DR InParanoid; D0NMR7; -. DR Proteomes; UP000006643; Partially assembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006643}; KW Reference proteome {ECO:0000313|Proteomes:UP000006643}. SQ SEQUENCE 319 AA; 34830 MW; DD9AB9B146371971 CRC64; MESKKIEIIA GGMLHELLRR ELPNDRNMLS ASALVSPAHH RLIVQAHEAY LKAGATMIVT NNYYVTPGVG FTSDEIREYS QTAGELAVGA LARTNRQDAK ICGSLPPLMH SLRSDRTIER QKGLDMYLLI GEALFPSVDV FLAETMSSLA EAKMAFEGVQ PLQKPVMVSF ALNSTGQLRS GEDVIESVKS LIKFCTRSME MLPGEAEGKT DLLQGILFNC SQPEDIAKAL SQLKGNQAVM EALQQHNIRI GGYGDRISPM SKAGIMEESL VPGALQSVMD MEVYSKFTTR WIEDGASIVG GCCGISPEYL QRIAEVLSE // ID D0NMR8_PHYIT Unreviewed; 305 AA. AC D0NMR8; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 29-APR-2015, entry version 25. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EEY61825.1}; GN ORFNames=PITG_13770 {ECO:0000313|EMBL:EEY61825.1}; OS Phytophthora infestans (strain T30-4) (Potato late blight fungus). OC Eukaryota; Stramenopiles; Oomycetes; Peronosporales; Phytophthora. OX NCBI_TaxID=403677 {ECO:0000313|Proteomes:UP000006643}; RN [1] {ECO:0000313|Proteomes:UP000006643} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T30-4 {ECO:0000313|Proteomes:UP000006643}; RX PubMed=19741609; DOI=10.1038/nature08358; RG The Broad Institute Genome Sequencing Platform; RA Haas B.J., Kamoun S., Zody M.C., Jiang R.H., Handsaker R.E., RA Cano L.M., Grabherr M., Kodira C.D., Raffaele S., Torto-Alalibo T., RA Bozkurt T.O., Ah-Fong A.M., Alvarado L., Anderson V.L., RA Armstrong M.R., Avrova A., Baxter L., Beynon J., Boevink P.C., RA Bollmann S.R., Bos J.I., Bulone V., Cai G., Cakir C., Carrington J.C., RA Chawner M., Conti L., Costanzo S., Ewan R., Fahlgren N., RA Fischbach M.A., Fugelstad J., Gilroy E.M., Gnerre S., Green P.J., RA Grenville-Briggs L.J., Griffith J., Grunwald N.J., Horn K., RA Horner N.R., Hu C.H., Huitema E., Jeong D.H., Jones A.M., Jones J.D., RA Jones R.W., Karlsson E.K., Kunjeti S.G., Lamour K., Liu Z., Ma L., RA Maclean D., Chibucos M.C., McDonald H., McWalters J., Meijer H.J., RA Morgan W., Morris P.F., Munro C.A., O'Neill K., Ospina-Giraldo M., RA Pinzon A., Pritchard L., Ramsahoye B., Ren Q., Restrepo S., Roy S., RA Sadanandom A., Savidor A., Schornack S., Schwartz D.C., Schumann U.D., RA Schwessinger B., Seyer L., Sharpe T., Silvar C., Song J., RA Studholme D.J., Sykes S., Thines M., van de Vondervoort P.J., RA Phuntumart V., Wawra S., Weide R., Win J., Young C., Zhou S., Fry W., RA Meyers B.C., van West P., Ristaino J., Govers F., Birch P.R., RA Whisson S.C., Judelson H.S., Nusbaum C.; RT "Genome sequence and analysis of the Irish potato famine pathogen RT Phytophthora infestans."; RL Nature 461:393-398(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; DS028147; EEY61825.1; -; Genomic_DNA. DR RefSeq; XP_002899465.1; XM_002899419.1. DR UniGene; Pin.1244; -. DR EnsemblProtists; PITG_13770T0; PITG_13770T0; PITG_13770. DR GeneID; 9461333; -. DR KEGG; pif:PITG_13770; -. DR EuPathDB; FungiDB:PITG_13770; -. DR HOGENOM; HOG000265278; -. DR InParanoid; D0NMR8; -. DR OMA; DVITANS; -. DR Proteomes; UP000006643; Partially assembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006643}; KW Reference proteome {ECO:0000313|Proteomes:UP000006643}. SQ SEQUENCE 305 AA; 33971 MW; 0751DB1536E39662 CRC64; MTTTTRRIPC VTLLDGGTGE ELFARGLPDD RFIWSATALV HEQHHKLLRE VHTSFLDANA DYITCNNYGV TPGVGFRDEE IVRYTAVAGR VARDACDRWT KTYPTSPKPK ICGSLPPLLE SYRADKVPEH EEGVRLYAMI ARTLKPFVDC YLAETLSSTQ EAKMALLGVQ QAKENVCKVV ENVLSFTAGT SRTELQAILF NCSQPEDICK ALKELHDDDN TQASLRSRGV RLGAYANRLT VIPDDWALAE SSEPQAMRKD LAVERYRDFV SQWVELGADV VGGCCGIGPE YIASIHDMLQ QQGRR // ID D0NSW2_PHYIT Unreviewed; 332 AA. AC D0NSW2; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 29-APR-2015, entry version 22. DE SubName: Full=Homocysteine S-methyltransferase, putative {ECO:0000313|EMBL:EEY64674.1}; GN ORFNames=PITG_16102 {ECO:0000313|EMBL:EEY64674.1}; OS Phytophthora infestans (strain T30-4) (Potato late blight fungus). OC Eukaryota; Stramenopiles; Oomycetes; Peronosporales; Phytophthora. OX NCBI_TaxID=403677 {ECO:0000313|Proteomes:UP000006643}; RN [1] {ECO:0000313|Proteomes:UP000006643} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T30-4 {ECO:0000313|Proteomes:UP000006643}; RX PubMed=19741609; DOI=10.1038/nature08358; RG The Broad Institute Genome Sequencing Platform; RA Haas B.J., Kamoun S., Zody M.C., Jiang R.H., Handsaker R.E., RA Cano L.M., Grabherr M., Kodira C.D., Raffaele S., Torto-Alalibo T., RA Bozkurt T.O., Ah-Fong A.M., Alvarado L., Anderson V.L., RA Armstrong M.R., Avrova A., Baxter L., Beynon J., Boevink P.C., RA Bollmann S.R., Bos J.I., Bulone V., Cai G., Cakir C., Carrington J.C., RA Chawner M., Conti L., Costanzo S., Ewan R., Fahlgren N., RA Fischbach M.A., Fugelstad J., Gilroy E.M., Gnerre S., Green P.J., RA Grenville-Briggs L.J., Griffith J., Grunwald N.J., Horn K., RA Horner N.R., Hu C.H., Huitema E., Jeong D.H., Jones A.M., Jones J.D., RA Jones R.W., Karlsson E.K., Kunjeti S.G., Lamour K., Liu Z., Ma L., RA Maclean D., Chibucos M.C., McDonald H., McWalters J., Meijer H.J., RA Morgan W., Morris P.F., Munro C.A., O'Neill K., Ospina-Giraldo M., RA Pinzon A., Pritchard L., Ramsahoye B., Ren Q., Restrepo S., Roy S., RA Sadanandom A., Savidor A., Schornack S., Schwartz D.C., Schumann U.D., RA Schwessinger B., Seyer L., Sharpe T., Silvar C., Song J., RA Studholme D.J., Sykes S., Thines M., van de Vondervoort P.J., RA Phuntumart V., Wawra S., Weide R., Win J., Young C., Zhou S., Fry W., RA Meyers B.C., van West P., Ristaino J., Govers F., Birch P.R., RA Whisson S.C., Judelson H.S., Nusbaum C.; RT "Genome sequence and analysis of the Irish potato famine pathogen RT Phytophthora infestans."; RL Nature 461:393-398(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; DS028158; EEY64674.1; -; Genomic_DNA. DR RefSeq; XP_002897874.1; XM_002897828.1. DR UniGene; Pin.8363; -. DR EnsemblProtists; PITG_16102T0; PITG_16102T0; PITG_16102. DR GeneID; 9475261; -. DR KEGG; pif:PITG_16102; -. DR EuPathDB; FungiDB:PITG_16102; -. DR HOGENOM; HOG000265278; -. DR InParanoid; D0NSW2; -. DR OMA; ICETIPC; -. DR Proteomes; UP000006643; Partially assembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006643}; KW Methyltransferase {ECO:0000313|EMBL:EEY64674.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006643}; KW Transferase {ECO:0000313|EMBL:EEY64674.1}. SQ SEQUENCE 332 AA; 36313 MW; BDDB935252167A99 CRC64; MSTPALTGLQ QLLADKSRVV VLDGGFATEL EKDPRVDLSA SSLWSGSLLL DQNQHLQDVV VNAHTNYFLA GADVATTVSY QASVDGFKRE GVTALEDVEK LFAKSIDLGA QARDAAWNEL QQSKRIKPLV GASIGCYGAA LADGSEYRGD YGKTKNELVA WHKHRFAFFT SYAPANFLIC ETIPCLVEVE AFVDLLNEFP TAHAIVAVAC HNGKELNSGE PIARIPEILA KLNNPSQLLA IGINCTPPQY VESLLLELDC PWPKAVYPNS GEGWDGVNKK WLPADNTGGP SSWEEYLPKW YDAGARFFGG CCRTSPDDIR AIREYFASRQ LL // ID D0PAL9_BRUSS Unreviewed; 1261 AA. AC D0PAL9; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 27-MAY-2015, entry version 34. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEY29193.1}; GN ORFNames=BAEG_00501 {ECO:0000313|EMBL:EEY29193.1}; OS Brucella suis bv. 5 str. 513. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520489 {ECO:0000313|EMBL:EEY29193.1, ECO:0000313|Proteomes:UP000002782}; RN [1] {ECO:0000313|EMBL:EEY29193.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=513 {ECO:0000313|EMBL:EEY29193.1}; 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 suis bv. 5 str. 513."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; DS999724; EEY29193.1; -; Genomic_DNA. DR RefSeq; WP_002965438.1; NZ_DS999724.1. DR ProteinModelPortal; D0PAL9; -. DR SMR; D0PAL9; 673-921. DR EnsemblBacteria; EEY29193; EEY29193; BAEG_00501. DR GeneID; 3786978; -. DR PATRIC; 24301113; VBIBruSui73489_1619. DR Proteomes; UP000002782; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002782}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 263 263 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 326 326 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 327 327 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 783 783 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1261 AA; 138652 MW; B65506A5F8F0B796 CRC64; MASSLDDLFG ATAAKPDGSE VLAALTQAAR ERILILDGAM GTQIQGLGFH EEHFRGDRFA TCDCQLQGNN DLLTLTQPKA IEEIHYAYAM AGADILETNT FSSTSIAQAD YGMEAMVYDL NRDGARLARR AALRAEQKDG RRRFVAGALG PTNRTASLSP DVNNPGFRAV TFDDLRIAYS EQIRGLIDGG SDIILIETIF DTLNAKAAVF ATEEVFAEKG VRLPVMISGT ITDLSGRTLS GQTPTAFWYS LRHARPFTIG LNCALGANAM RAHLDELSGI ADTFICAYPN AGLPNEFGQY DETPEAMAAQ IEGFARDGLV NVVGGCCGST PDHIRAIAQA VAKYEPRKPA KVPPLMRLSG LEPFTLTKDI PFVNIGERTN VTGSARFRKL VKAGDFAAAL DVARDQVANG AQIIDINMDE GLIDSEKAMV EFLNLIAAEP DIARVPIMLD SSKWEVIEAG LKCVQGKAVV NSISLKEGEE AFLHHARLVR AYGAAVVIMA FDETGQADTQ ARKIEICTRA YKILTEQVGF PPEDIIFDPN IFAVATGIEE HNNYGVDFIE ATREIVRTLP HVHISGGVSN LSFSFRGNEP VREAMHAVFL YHAIQAGMDM GIVNAGQLAV YDTIDAELRE ACEDVVLNRP TKTGESATER LLEIAERFRD SGSREARTQD LSWREWPVEK RLEHALVNGI TEYIEADTEE ARLAAERPLH VIEGPLMAGM NVVGDLFGSG KMFLPQVVKS ARVMKQAVAV LLPFMEEEKR LNGGEGRQSA GKVLMATVKG DVHDIGKNIV GVVLACNNYE IIDLGVMVPS QKILQVARDE KVDIIGLSGL ITPSLDEMAH VAAEMEREGF DIPLLIGGAT TSRVHTAVKI HSRYERGQAV YVVDASRAVG VVSNLLSPEG KQAYIDGLRN EYAKVAAAHA RNEAEKQRLP IARARANPHQ LDWENYEPVK PAFTGTKVFE TYDLAEIARY IDWTPFFQTW ELRGRYPAIL EDEKQGEAAR QLWADAQAML RKIIDEKWFT PRAVVGFWPA NAVGDDIRLF TDESRKEELA TLFTLRQQLT KRDGRPNVAM ADFVAPVESG KQDYVGGFVV TAGIGEIAIA ERFERANDDY SAILVKALAD RFAEAFAELM HERVRKEFWA YAPDEAFTPE ELISEPYKGI RPAPGYPAQP DHTEKTTLFR LLDATANTGV ELTESYAMWP GSSVSGLYIG HPESYYFGVA KVERDQVEDY ARRKDMDVEA VERWLTPILN YVPGASKDEA A // ID D0RLI4_9RHIZ Unreviewed; 1261 AA. AC D0RLI4; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 27-MAY-2015, entry version 34. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EEY27283.1}; GN ORFNames=BATG_02403 {ECO:0000313|EMBL:EEY27283.1}; OS Brucella sp. F5/99. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=437701 {ECO:0000313|EMBL:EEY27283.1}; RN [1] {ECO:0000313|EMBL:EEY27283.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F5/99 {ECO:0000313|EMBL:EEY27283.1}; 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 sp. F5/99."; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG663486; EEY27283.1; -; Genomic_DNA. DR RefSeq; WP_002965438.1; NZ_GG663486.1. DR ProteinModelPortal; D0RLI4; -. DR SMR; D0RLI4; 673-921. DR EnsemblBacteria; EEY27283; EEY27283; BATG_02403. DR GeneID; 3786978; -. DR PATRIC; 24282953; VBIBruSp65954_3291. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 263 263 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 326 326 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 327 327 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 783 783 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1261 AA; 138652 MW; B65506A5F8F0B796 CRC64; MASSLDDLFG ATAAKPDGSE VLAALTQAAR ERILILDGAM GTQIQGLGFH EEHFRGDRFA TCDCQLQGNN DLLTLTQPKA IEEIHYAYAM AGADILETNT FSSTSIAQAD YGMEAMVYDL NRDGARLARR AALRAEQKDG RRRFVAGALG PTNRTASLSP DVNNPGFRAV TFDDLRIAYS EQIRGLIDGG SDIILIETIF DTLNAKAAVF ATEEVFAEKG VRLPVMISGT ITDLSGRTLS GQTPTAFWYS LRHARPFTIG LNCALGANAM RAHLDELSGI ADTFICAYPN AGLPNEFGQY DETPEAMAAQ IEGFARDGLV NVVGGCCGST PDHIRAIAQA VAKYEPRKPA KVPPLMRLSG LEPFTLTKDI PFVNIGERTN VTGSARFRKL VKAGDFAAAL DVARDQVANG AQIIDINMDE GLIDSEKAMV EFLNLIAAEP DIARVPIMLD SSKWEVIEAG LKCVQGKAVV NSISLKEGEE AFLHHARLVR AYGAAVVIMA FDETGQADTQ ARKIEICTRA YKILTEQVGF PPEDIIFDPN IFAVATGIEE HNNYGVDFIE ATREIVRTLP HVHISGGVSN LSFSFRGNEP VREAMHAVFL YHAIQAGMDM GIVNAGQLAV YDTIDAELRE ACEDVVLNRP TKTGESATER LLEIAERFRD SGSREARTQD LSWREWPVEK RLEHALVNGI TEYIEADTEE ARLAAERPLH VIEGPLMAGM NVVGDLFGSG KMFLPQVVKS ARVMKQAVAV LLPFMEEEKR LNGGEGRQSA GKVLMATVKG DVHDIGKNIV GVVLACNNYE IIDLGVMVPS QKILQVARDE KVDIIGLSGL ITPSLDEMAH VAAEMEREGF DIPLLIGGAT TSRVHTAVKI HSRYERGQAV YVVDASRAVG VVSNLLSPEG KQAYIDGLRN EYAKVAAAHA RNEAEKQRLP IARARANPHQ LDWENYEPVK PAFTGTKVFE TYDLAEIARY IDWTPFFQTW ELRGRYPAIL EDEKQGEAAR QLWADAQAML RKIIDEKWFT PRAVVGFWPA NAVGDDIRLF TDESRKEELA TLFTLRQQLT KRDGRPNVAM ADFVAPVESG KQDYVGGFVV TAGIGEIAIA ERFERANDDY SAILVKALAD RFAEAFAELM HERVRKEFWA YAPDEAFTPE ELISEPYKGI RPAPGYPAQP DHTEKTTLFR LLDATANTGV ELTESYAMWP GSSVSGLYIG HPESYYFGVA KVERDQVEDY ARRKDMDVEA VERWLTPILN YVPGASKDEA A // ID D0RN80_9PROT Unreviewed; 296 AA. AC D0RN80; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Homocysteine/selenocysteine methylase (S-methylmethionine-dependent) {ECO:0000313|EMBL:EMH79874.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EMH79874.1}; DE Flags: Precursor; GN ORFNames=HIMB114_00002450 {ECO:0000313|EMBL:EMH79874.1}; OS alpha proteobacterium HIMB114. OC Bacteria; Proteobacteria; Alphaproteobacteria; SAR11 cluster. OX NCBI_TaxID=684719 {ECO:0000313|EMBL:EMH79874.1}; RN [1] {ECO:0000313|EMBL:EMH79874.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HIMB114 {ECO:0000313|EMBL:EMH79874.1}; 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] {ECO:0000313|EMBL:EMH79874.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HIMB114 {ECO:0000313|EMBL:EMH79874.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EMH79874.1}. 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; ADAC02000001; EMH79874.1; -; Genomic_DNA. DR RefSeq; WP_009359959.1; NZ_ADAC02000001.1. DR EnsemblBacteria; EMH79874; EMH79874; HIMB114_00002450. DR PATRIC; 36032932; VBIAlpPro140191_0323. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EMH79874.1}; KW Transferase {ECO:0000313|EMBL:EMH79874.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 281 281 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 282 282 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 296 AA; 33139 MW; B1C25A24BFF95E85 CRC64; MKNIFTKNFI ILDGGMGQEL LARGVKPVSN LWSATALMEK KYHQIIKDCH LDFINAGAEI ILTNTFGSRR RRLEDNQIEN RFEELNFTAL KLAKESVKES GRKVLIAGSL PPQNFTYLPE LGDIDKMKKN FFDQAKILNE GVDLFYLDVL SSSEEIEIGI QSIQTFNKPF VVGIHFKKNG LLPSGEKIKN VINKIKSYNP LAITGSCVAY EDVIDAKNGF IESGLPFGFK VNAFKEIPKG WKPDSSNPNL ALGKNEDLTA FKFQEISKEF IDMGAKLIGG CCEITPSHIS KIQDLR // ID D0S0C8_ACICA Unreviewed; 1228 AA. AC D0S0C8; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 27-MAY-2015, entry version 33. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEY79011.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEY79011.1}; GN Name=metH {ECO:0000313|EMBL:EEY79011.1}; GN ORFNames=HMPREF0012_01880 {ECO:0000313|EMBL:EEY79011.1}; OS Acinetobacter calcoaceticus RUH2202. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=575585 {ECO:0000313|EMBL:EEY79011.1, ECO:0000313|Proteomes:UP000005126}; RN [1] {ECO:0000313|Proteomes:UP000005126} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG704949; EEY79011.1; -; Genomic_DNA. DR RefSeq; WP_003653087.1; NZ_GG704949.1. DR EnsemblBacteria; EEY79011; EEY79011; HMPREF0012_01880. DR PATRIC; 35595728; VBIAciCal110308_1632. DR Proteomes; UP000005126; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000005126}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEY79011.1}; KW Transferase {ECO:0000313|EMBL:EEY79011.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1228 AA; 135809 MW; 8C5865FAE34E05B7 CRC64; MSTLATLKAL LAKRILIIDG AMGTMIQRHK LEEADYRGER FADWAHDLKG NNDLLVLTQP EIIQGIHEAY LDAGADIIET NSFNGTRVSM SDYHMEDLVP EINREAARLA KAACEKYSTP DKPRFVAGVL GPTSRTCSIS PNVNDPAFRN ITFDALKENY IEATHALIEG GADIILIETV FDTLNCKAAI FAVKEVFKQI GHELPLMISG TITDASGRTL TGQTAEAFWN SVRHGDLLSI GFNCALGADA MRPHVKTVSD VADTFISAHP NAGLPNAFGE YDETPEQTAA FLKEFAESGL INITGGCCGT TPDHIRAIAN AVKDIAPRQI PETKPACRLS GLEPFNIYDD SLFVNVGERT NVTGSKKFLR LIREENFAEA LEVAQQQVEA GAQIIDINMD EGMLDSQNAM VHFLNLVASE PDISRVPIMI DSSKWEIIEA GLKCVQGKPV VNSISLKEGY DEFVEKARLC RQYGAAIIVM AFDETGQADT AARKREICKR SYDVLVNDVG FPAEDIIFDP NVFAVATGIE EHNNYGVDFI EATGWIKQNL PHAMISGGVS NVSFSFRGNE PVREAIHSVF LYHAIKQGMT MGIVNAGQMA IYDDIPKELK DAVEDVVLNQ NQGESGQNAT EKLLEVAEKY RGHSGTQREA ENLEWRNEPV EKRLEYALVK GITTYIDEDT EEARLKAKRP LDVIEGALMD GMNVVGDLFG SGKMFLPQVV KSARVMKQAV AWLNPYIEAE KTGSQSKGKV LMATVKGDVH DIGKNIVGVV LGCNGYDIVD LGVMVPCEKI LQTAIDEKCD IIGLSGLITP SLDEMVFVAK EMQRKGFDIP LLIGGATTSK AHTAVKIDPQ YHNDAVIYVA DASRAVGVAT TLLSKEMRGK FIEEHRAEYV KIRERLANKQ PKAAKLTYAE SIKNGFKIDE SYVPAKPNLL GTQVLTNYPL ETLVEYFDWT PFFISWSLAG KFPKILQDEV VGEAATDLYN QAQAMLKDII DNNLFDARAV FGMFPAQRTD ADTVSVFDEA SQNVTHTFEH LRQQSDKVTG KPNLSLADYI RTDREQQDYL GGFTVSIFGA EELANEYKAK GDDYSAILVQ SLADRFAEAF AEHLHERIRK EFWGYKADEQ LSNEELIKEK YVGIRPAPGY PACPEHSEKA VLFDWLGSTD KIGTKLTEHF AMMPPSSVSG FYYSHPQSEY FNVGKISQDQ LEDYAKRKGW TLDEAKRWLG PNLDDSVS // ID D0S0H7_ACICA Unreviewed; 292 AA. AC D0S0H7; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEY79060.1}; GN ORFNames=HMPREF0012_01929 {ECO:0000313|EMBL:EEY79060.1}; OS Acinetobacter calcoaceticus RUH2202. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=575585 {ECO:0000313|EMBL:EEY79060.1, ECO:0000313|Proteomes:UP000005126}; RN [1] {ECO:0000313|Proteomes:UP000005126} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; EEY79060.1; -; Genomic_DNA. DR RefSeq; WP_003653169.1; NZ_GG704949.1. DR EnsemblBacteria; EEY79060; EEY79060; HMPREF0012_01929. DR PATRIC; 35595828; VBIAciCal110308_1682. DR Proteomes; UP000005126; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005126}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EEY79060.1}; KW Transferase {ECO:0000313|EMBL:EEY79060.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 202 202 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 275 275 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 276 276 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 292 AA; 31985 MW; 9EBEF65B079FEEB4 CRC64; MKILDGGLGR ELARRGAPFR QPEWSALALI EAPETVKEVH LDFINAGSEV ITTNNYAVVP FHIGQERFET DGVRLIQVAI EQAKNAVKES GKNVKIAGCL PPLFGSYRAD LFQAEQAKDL AEPIINTLAP EVDFWLAETQ SCLKEVETVH ALLPKDGKDY WVSFTLQDEI KQEQALLRSG ENMQQVADFI KQSNANAVLF NCCQPEVILQ AINEIKGLIP ESVQIGAYAN AFPPQDSSAT ANDGLDEVRK DLDAPAYLGF AKQWQQAGAS LVGGCCGIGP EHIAELSQFF KE // ID D0SAS6_ACIJO Unreviewed; 1228 AA. AC D0SAS6; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 27-MAY-2015, entry version 32. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEY97513.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEY97513.1}; GN Name=metH {ECO:0000313|EMBL:EEY97513.1}; GN ORFNames=HMPREF0016_00596 {ECO:0000313|EMBL:EEY97513.1}; OS Acinetobacter johnsonii SH046. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=575586 {ECO:0000313|EMBL:EEY97513.1}; RN [1] {ECO:0000313|EMBL:EEY97513.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SH046 {ECO:0000313|EMBL:EEY97513.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG704964; EEY97513.1; -; Genomic_DNA. DR RefSeq; WP_005399886.1; NZ_GG704964.1. DR EnsemblBacteria; EEY97513; EEY97513; HMPREF0016_00596. DR PATRIC; 35600336; VBIAciJoh101986_0517. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEY97513.1}; KW Transferase {ECO:0000313|EMBL:EEY97513.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1228 AA; 135684 MW; ED3AF8644B557AC2 CRC64; MSTLATLKAL LAERILIIDG AMGTMIQRHK LEEEDYRGER FVDWASDLKG NNDLLVLTQP QIIQGIHEAY LDAGADIIET NSFNGTRVSM SDYHMEDLVP EINREAARLA KAACEKYSTP DKPRFVAGVL GPTSRTCSIS PNVNDPAFRN ITFDELKENY IEATHALIEG GADIILIETV FDTLNCKAAI FAVKEVFKQL GRELPLMISG TITDASGRTL TGQTAEAFWN SVRHGDLLSI GFNCALGADA MRPHVKTIAD VADTFVSAHP NAGLPNAFGE YDETPEQTAA FIKEFAESGL INITGGCCGT TPDHIRAIYN AVKDIQPRQV PETKPACRLS GLEPFNIYDD SLFVNVGERT NVTGSKKFLR LIREEKFAEA LEVAQQQVEA GAQIIDINMD EGMLDSQNAM VHFLNLVASE PDISRVPIMI DSSKWEIIEA GLKCVQGKPV VNSISLKEGY DEFVEKARLC RQYGAAIIVM AFDETGQADT AKRKREICKR SYDVLVNDVG FPAEDIIFDP NVFAVATGIE EHNNYGVDFI EATGWIKQNL PHAMISGGVS NVSFSFRGNE PVREAIHSVF LYYAIKQGMT MGIVNAGQMA IYDDIPKELK DAVEDVVLNQ NQGESGQNAT EKLLEVAEKF RGHSGAQREA ENLEWRNESV EKRLEYALVK GITTYIDEDT EEARLKAKRP LDVIEGALMD GMNVVGDLFG SGKMFLPQVV KSARVMKQAV AWLNPYIEAE KGNAQSKGRV LMATVKGDVH DIGKNIVGVV LGCNGYDIVD LGVMVPAEKI LQTAIDEKCD IIGLSGLITP SLDEMVFVAK EMQRKGFDIP LLIGGATTSK AHTAVKIDPQ YSNDAVIYVA DASRAVGVAT TLLSKEMRSN FIAEHRAEYA KIRERLANKQ PKAAKLSYAD SVENGFKIDE NYMPPKPNAL GTQVITNYPL ATLVEYFDWT PFFISWSLAG KFPKILEDEV VGEAATDLYN QAQAMLKDII DNDRFDARAV FGLYPAQRTG ADTVSVFDET AQNVTHTFEH LRQQSDKVTG KPNLSLADFI STSKDNTDYL GGFTVSIFGA EELANEYKAK GDDYSAILVQ SLADRFAEAF AEHLHERIRK EFWGYKADET LGNEELIKEK YVGIRPAPGY PACPEHSEKA VLFDWLGSEE KIGTKLTEHF AMMPPSSVSG FYYSHPESEY FNVGKISQDQ LEDYAKRKGW SLDVAKRWLA PNLDDSIV // ID D0SKA4_ACIJU Unreviewed; 1228 AA. AC D0SKA4; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 27-MAY-2015, entry version 32. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEY94276.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEY94276.1}; GN Name=metH {ECO:0000313|EMBL:EEY94276.1}; GN ORFNames=HMPREF0026_01552 {ECO:0000313|EMBL:EEY94276.1}; OS Acinetobacter junii SH205. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=575587 {ECO:0000313|EMBL:EEY94276.1}; RN [1] {ECO:0000313|EMBL:EEY94276.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SH205 {ECO:0000313|EMBL:EEY94276.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG705011; EEY94276.1; -; Genomic_DNA. DR RefSeq; WP_005403036.1; NZ_GG705011.1. DR EnsemblBacteria; EEY94276; EEY94276; HMPREF0026_01552. DR PATRIC; 35609035; VBIAciJun5570_1486. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEY94276.1}; KW Transferase {ECO:0000313|EMBL:EEY94276.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1228 AA; 135705 MW; F0C15FFCADCCD084 CRC64; MSTLATLKSL LAQRILIIDG AMGTMIQRHK LEEEDYRGER FADWASDLKG NNDLLVLTQP QIIQGIHEAY LDAGADIIET NSFNGTRVSM SDYHMEDLVP EINREAARLA RAACDKYSTP DKPRFVAGVL GPTSRTCSIS PNVNDPAFRN ITFDELKENY IEATHALIEG GADILLIETV FDTLNCKAAI FAVKEVFKQI GYELPLMISG TITDASGRTL TGQTAEAFWN SVRHGDLLSI GFNCALGADA MRPHVKTISD VADTFVSAHP NAGLPNAFGE YDETPEQTAA FIKEFAESGL INITGGCCGT TPDHIRAIYQ AVKDIPPRKI PETVHACRLS GLEPLNIYDD SLFVNVGERT NVTGSKKFLR LIREENFAEA LEVAQQQVEA GAQIIDINMD EGMLDSQGAM VHFLNLVASE PDISRVPIMI DSSKWEIIEA GLKCVQGKPV VNSISLKEGY DEFVEKARLC RQYGAAVIVM AFDEVGQADT AERKREICKR SYDILVNEVG YPAEDIIFDP NVFAVATGIE EHNNYAVDFI EATGWIKQNL PHAMISGGVS NVSFSFRGNE PVREAIHSVF LYHAIKQGMT MGIVNAGQMA IYDDINKELK DAVEDVVLNQ NQGETGQAAT EKLLEVAEKY RGQAGATKEA ENLEWRNESV EKRLEYALVK GITTYIDQDT EEARLKSKRP LDVIEGPLMD GMNVVGDLFG SGKMFLPQVV KSARVMKQAV AWLNPYIEAE KSEGQSKGKV LMATVKGDVH DIGKNIVGVV LGCNGYDIVD LGVMVPAEKI LQTAIDEKCD IIGLSGLITP SLDEMVFVAK EMQRKGFNIP LLIGGATTSK AHTAVKIDPQ YSNDAVIYVA DASRAVGVAT TLLSPEMRGN FIAEHRAEYA KIRERLANKQ PKAAKLSYAE SVENGFKIDN HYVPPKPNAL GTQVIKNYPL ETLVKYFDWT PFFISWSLAG KFPKILEDEV VGEAATDLYN QAQAMLKDII ENKRFDARAV FGLYPAQRTG ADTVSVFDES GQHHTHTFEH VRQQSDKVTG KPNLSLADYI KPSEQPEDYL GGFTVSIFGA EELANEYKAK GDDYSAILVQ SLADRFAEAF AEHLHERIRK EFWGYKADET LSNEELIKEK YVGIRPAPGY PACPEHSEKA VLFDWLGSEA KIGTKLTEHF AMMPPSSVSG FYYSHPQSEY FNVGKISQDQ LEDYAKRKGW TLDEAKRWLA PNLDDSIG // ID D0SUJ6_ACILW Unreviewed; 1228 AA. AC D0SUJ6; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 27-MAY-2015, entry version 32. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEY90551.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEY90551.1}; GN Name=metH {ECO:0000313|EMBL:EEY90551.1}; GN ORFNames=HMPREF0017_00970 {ECO:0000313|EMBL:EEY90551.1}; OS Acinetobacter lwoffii SH145. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=575588 {ECO:0000313|EMBL:EEY90551.1}; RN [1] {ECO:0000313|EMBL:EEY90551.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SH145 {ECO:0000313|EMBL:EEY90551.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG705057; EEY90551.1; -; Genomic_DNA. DR RefSeq; WP_004279396.1; NZ_GG705057.1. DR EnsemblBacteria; EEY90551; EEY90551; HMPREF0017_00970. DR PATRIC; 35614308; VBIAciLwo61775_0757. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEY90551.1}; KW Transferase {ECO:0000313|EMBL:EEY90551.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1228 AA; 135313 MW; E80B78EA014EAACC CRC64; MSTLTTLKEL LAKRILIIDG AMGTMIQRHK LEEADYRGER FADWAYDLKG NNDLLVLTQP QIIQGIHEAY LEAGADIIET NTFNGTRVSM SDYHMEDLVP EINREAARLA KEACAKYSTP EKPRFVAGVI GPTSRTTSIS PNVNDPAFRN ITFDALKVDY IESTKALIEG GADIILIETV FDTLNAKAAI FAVKEVFKEL GYELPIMISG TITDASGRTL TGQTAEAFWN SMRHAEPLSI GFNCALGADA MRPHVKTVSD VANTFVSAHP NAGLPNAFGG YDETPEETAA FIKEFAESGL INITGGCCGT TPDHIRAIAN AVAGITPRQI PEIEPACRLS GLEPFNITKD SLFVNVGERT NVTGSKKFLR LIREENFAEA LDVARQQVEA GAQIIDINMD EGMLDSQGAM VHFLNLIASE PDISRVPIML DSSKWEIIEA GLKCVQGKAV VNSISLKEGH DEFVERARLC RQYGAAVIVM AFDEDGQADT ATRKKEICKR SYDVLVNEVG FPSEDIIFDP NVFAIATGIE EHNNYGVDFI EATGWIKQNL PNAMISGGVS NVSFSFRGNE PVREAIHSVF LYHAIQQGMT MGIVNAGQMA IYDDIDKELK EAVEDVVLNQ NQGESGQEAT EKLLAVAEKY RGQSGTQKAE ENLEWRNESV EKRLEYALVK GITTYIDQDT EEARLNSTRP LDVIEGPLMA GMNVVGDLFG AGKMFLPQVV KSARVMKQAV AWLNPFIEAE KTQAEAKGKI LLATVKGDVH DIGKNIVGVV LGCNGYDIVD LGVMVPCEKI LQTAIDEKVD IIGLSGLITP SLDEMVFVAK EMQRKGFNIP LMIGGATTSK AHTAVKISPQ YHNDGVLYTA DASRAVGVAT QLLSPEMKPK LLADYAADYE KIRTRLANKQ PKAAKLSYQD SVENGFKIDF DKNAPVKPNF IGSETFTNYP LETLVEYFDW TPFFISWSLA GKFPKILEDE VVGEAARDLY EQAQAMLKDI IENKRFDARA TFSIYPANRV AADTVAVVDE TGNVTHSFEH LRQQSDKVTG KANYSLADFV APKDVAQDYL GGFTVSIFGA EELSQEYKAK GDDYNAIMVQ ALGDRFAEAF AEHLHERIRK EFWGYQADEQ LSNDDLIKEK YVGIRPAPGY PACPEHSEKA PLFDWLGTTD KIGTYLTTSF AMWPPSSVSG FYYANPETEY FNVGKISGDQ LEDYAKRKGW TLDEAKRWLA PNLDDSVV // ID D0TAB1_9BACE Unreviewed; 1230 AA. AC D0TAB1; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 01-APR-2015, entry version 32. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEY84174.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEY84174.1}; GN Name=metH {ECO:0000313|EMBL:EEY84174.1}; GN ORFNames=HMPREF0103_0118 {ECO:0000313|EMBL:EEY84174.1}; OS Bacteroides sp. 2_1_33B. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=469589 {ECO:0000313|EMBL:EEY84174.1}; RN [1] {ECO:0000313|EMBL:EEY84174.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=2_1_33B {ECO:0000313|EMBL:EEY84174.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG705149; EEY84174.1; -; Genomic_DNA. DR RefSeq; WP_008771641.1; NZ_GG705149.1. DR EnsemblBacteria; EEY84174; EEY84174; HMPREF0103_0118. DR PATRIC; 35643548; VBIBacSp88625_0982. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEY84174.1}; KW Transferase {ECO:0000313|EMBL:EEY84174.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1230 AA; 136502 MW; CD7A8336EE6DBDD6 CRC64; MNKERFLRLL NERILILDGG MGTMIQSFKL NEQDYRGERF ADFPGQLKGN NDLLCITRPD VIQSIHRQYL DAGADIFATN TFNANAISMA DYAMEAYVRE INLAAGRLSR EVADTYMAEH PDRTIFVAGS IGPTNKTASM SPDVSDPAYR AVTYKDLYNA YKEQVEGLVD GGVDIILFET TFDTLNVKAG LEAAEVVLKE KEKDLPIMLS LTLSAQGGRT FSGQTLLAFL ASIQHTHIVS VGLNCSFGAA DMKPYLQELA KYAPYYISAY PNAGLPNSFG TYDETPDKMA QHVKPFVEEG LVNIIGGCCG TTPAHISRYP ELVKGAKPHI PAPKPDCLWL SGLELLEVKP ENNFVNVGER CNVAGSRKFL RLIKEGSYEE ALTIARKQVE DGAQVIDINM DDGMLDAVKE MKTFLNLIAS EPDIARVPVM IDSSKWEVIE EGLMCVQGKS IVNSISLKEG EEVFLKHAAR IKQLGAAAVV MAFDEKGQAD TYERKIEICE RAYRLLIEKI DFNPQDIIFD PNVLAIATGM EEHNGYGLAF IRAVEWIKKN LPGAKVSGGV SNLSFSFRGN NHVREAMHSV FLYHAIGKGM DMGIVNPSTS VLYEDIEPEF RTLLEDVILA RRPEAAEELI TYAQNLHVQA SGETPEKHEA WRELSLKERL EHALIKGIGD YLEDDLQEAL RIYPHAVDII DGPLMSGMNK VGELFGAGKM FLPQVVKTAR TMKKAVAILQ PAIESEKKAS GSAKAGKVIF ATVKGDVHDI GKNIVSIVLS CNNYEVIDLG VMVPADVIIK KAIEEKPDLV CLSGLITPSL EEMAHVADEM QKAGLTIPMM VGGATTSKLH TAVKIAPHYD YPVIHVLDAS QNPLIAAKLL NPDTRDAYIR ELEQEQEALR ASLGQKKETL ASLSEARKHP IEIDWTGYTP VVPARMGVHV IPYIPLEEVI PYIHWTFFFS AWKLNGRFSE ISQIHGCDSC RASWLAGFPE KDRAKATEAM QLYKDAVRLL DRLVNMKVEY CKAIYGFFSA NSEGDTIRMG DIALPLLRQQ VKKEENIYKC LSDYVIPVSE ERTDYVGAFV VTAGAGADCL KDKFEEEGDT YNSMLLQTLT DRLAEATAEY LHEKVRKEYW GYAKDESLSI PDLYKVKYQG IRPAIGYPSL PDQLLNFTLD GLLDMSRIGV SLTENGAMYP TASVSGIYIA HPSSQYFMIG SIDEEQMRDY ASRRNLTEEQ ARKLLSKNIG // ID D0TTH2_9BACE Unreviewed; 915 AA. AC D0TTH2; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 01-APR-2015, entry version 31. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEZ03398.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEZ03398.1}; GN Name=metH {ECO:0000313|EMBL:EEZ03398.1}; GN ORFNames=HMPREF0102_02460 {ECO:0000313|EMBL:EEZ03398.1}; OS Bacteroides sp. 2_1_22. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=469588 {ECO:0000313|EMBL:EEZ03398.1}; RN [1] {ECO:0000313|EMBL:EEZ03398.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=2_1_22 {ECO:0000313|EMBL:EEZ03398.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG705175; EEZ03398.1; -; Genomic_DNA. DR EnsemblBacteria; EEZ03398; EEZ03398; HMPREF0102_02460. DR PATRIC; 35638734; VBIBacSp133744_2568. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEZ03398.1}; KW Transferase {ECO:0000313|EMBL:EEZ03398.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 915 AA; 99932 MW; 18EED729F9367757 CRC64; MKKTISQVVS ERILILDGAM GTMIQQYNLK EEDFRGERFA HIPGQLKGNN DLLCLTRPDV IQDIHRKYLE AGADIIETNT FSSTTVSMAD YHVEEYVREM NLAAVKLARD LADEYTAKNP DKPRFVAGSV GPTNKTCSMS PDVNNPAYRA LSYDELAASY QQQMEAMLEG GVDAILIETI FDTLNAKAAI FAAEQAMKAT GVEVPVMLSV TVSDIGGRTL SGQTLDAFLA SMQHANIFSV GLNCSFGARQ LKPFLEQLAA RAPYYISAYP NAGLPNSLGK YDQTPADMAH EVREYIEEGL INIIGGCCGT TDAYIAEYPA LVKGAKPHIP ALAPDCMWLS GLELLEVKPE INFVNVGERC NVAGSRKFLR LINEKKYDEA LSIARQQVED GALVIDVNMD DGLLDAKTEM TTFLNLIMSE PEIARVPVMI DSSKWEVIEA GLKCLQGKSI VNSISLKEGE EVFLEHARII RQYGAATVVM AFDEKGQADT AARKIEVCER AYRLLVDKVG FNPHDIIFDP NVLAVATGIE EHNNYAVDFI EATAWIKKNL PGAHISGGVS NLSFSFRGNN YIREAMHAVF LYHAIQQGMD MGIVNPGTSV LYSDIPTDVL EKIEDVVLNR RPDAAERLIE LAESLKATMS GTAGQPAAKQ DAWREESVQE RLKYALMKGI GDFLEQDLAE ALPLYDKAVD VIEGPLMDGM NYVGELFGAG KMFLPQVVKT ARTMKKAVAI LQPIIESEKV EGSAAAGKVL LATVKGDVHD IGKNIVAVVM ACNGYDIVDL GVMVPAETIV QRAIEEKVDM IGLSGLITPS LEEMAHVALE LEKAGLDIPL LIGGATTSKM HTALKIAPVY HAPVVHLKDA SQNASVASKL LNPQLKAELV NELNSEYEAL REKSGLLKRE TVSLEEAQKN KLNLF // ID D0WFU5_9ACTN Unreviewed; 297 AA. AC D0WFU5; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EEZ61358.1}; GN ORFNames=HMPREF0762_00695 {ECO:0000313|EMBL:EEZ61358.1}; OS Slackia exigua ATCC 700122. OC Bacteria; Actinobacteria; Coriobacteridae; Coriobacteriales; OC Coriobacterineae; Coriobacteriaceae; Slackia. OX NCBI_TaxID=649764 {ECO:0000313|EMBL:EEZ61358.1}; RN [1] {ECO:0000313|EMBL:EEZ61358.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 700122 {ECO:0000313|EMBL:EEZ61358.1}; 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., 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEZ61358.1}. 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; ACUX02000006; EEZ61358.1; -; Genomic_DNA. DR RefSeq; WP_006361940.1; NZ_GG700630.1. DR EnsemblBacteria; EEZ61358; EEZ61358; HMPREF0762_00695. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; SQ SEQUENCE 297 AA; 31088 MW; F0E0E23CF73F3F2E CRC64; MADIEFRFHR DMLVLSAPID YRLAERGVDV DADMEFMSLF EDDTVSDLLS MEQIAGAACL VTNTEGICRA RLAHRRMEDA AADIASSALA AATGLAPQHV ICAIGPCGLP LDPSDEASLE RTRAQYEGAV RAFGGAPFDA ILLDGMRTVH DMACAIEGAR RATDRPVLAS VTLGADGTFD GAPLENAASC MAAADVVGIR SSLGIDALTD AVATLARVCT QPLLVQIDVA QPTEAERRMR KLGRTIEGNP YPDPDSLADV AVALRAAGAQ FLRAVGEATP AYTGALAVVC AGAQSVR // ID D0X0X3_VIBAL Unreviewed; 805 AA. AC D0X0X3; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 04-FEB-2015, entry version 28. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEZ82070.1}; GN Name=metH {ECO:0000313|EMBL:EEZ82070.1}; GN ORFNames=VMC_30730 {ECO:0000313|EMBL:EEZ82070.1}; OS Vibrio alginolyticus 40B. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=674977 {ECO:0000313|EMBL:EEZ82070.1}; RN [1] {ECO:0000313|EMBL:EEZ82070.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=40B {ECO:0000313|EMBL:EEZ82070.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEZ82070.1}. 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; ACZB01000068; EEZ82070.1; -; Genomic_DNA. DR EnsemblBacteria; EEZ82070; EEZ82070; VMC_30730. DR PATRIC; 35948072; VBIVibAlg143054_3440. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEZ82070.1}; KW Transferase {ECO:0000313|EMBL:EEZ82070.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 805 AA; 89038 MW; 3F26CA99B261516B CRC64; MGSNVRQQIE AQLKQRILLI DGGMGTMIQG YKLEEQDYRG TRFADWHCDL KGNNDLLVLS QPQLIKEIHA AYLEAGADIL ETNTFNATTI AMADYEMESL SEEINFAAAK LAREVADEWT AKTPDKPRYV AGVLGPTNRT CSISPDVNDP GYRNVSFDEL VEAYSESTRA LIKGGSDLIL IETIFDTLNA KACSFAVESV FEEMGIELPV MISGTITDAS GRTLSGQTTE AFYNSLRHVK PISFGLNCAL GPDELRPYVE ELSRISESFV SAHPNAGLPN AFGEYDLSPE DMAKHVKEWA QSGFLNLIGG CCGTTPEHIR QMALAVENIA PRQLPELPVA CRLSGLEPLA IDKDSLFINV GERTNVTGSA RFKRLIKEEL YDEALDVARQ QVENGAQIID INMDEGMLDA QACMVRFLNL CASEPEISKV PIMVDSSKWE VIEAGLKCIQ GKGIVNSISL KEGKEKFVEQ AKLIRRYGAA VIVMAFDEIG QADTRERKVE ICTNAYRILV DEVGFPPEDI IFDPNIFAIA TGIEEHNNYA VDFIEAVGDI KRDLPHAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK NGMDMGIVNA GQLEIYDNVP EKLREAVEDV VLNRRDDATE RLLDIAAEYA GKGVGKEEDA SALEWRTWPV EKRLEHALVK GITEFIVDDT EEARVKASKP LEVIEGPLMD GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AHLEPYINAE KQVGQTNGKI LLATVKGDVH DIGKNIVGVV LQCNNYEIID LGVMVPCEKI LKVAQEENVV YYWFI // ID D0X2S6_VIBAL Unreviewed; 300 AA. AC D0X2S6; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EEZ81435.1}; GN ORFNames=VMC_37260 {ECO:0000313|EMBL:EEZ81435.1}; OS Vibrio alginolyticus 40B. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=674977 {ECO:0000313|EMBL:EEZ81435.1}; RN [1] {ECO:0000313|EMBL:EEZ81435.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=40B {ECO:0000313|EMBL:EEZ81435.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEZ81435.1}. 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; ACZB01000093; EEZ81435.1; -; Genomic_DNA. DR RefSeq; WP_005388906.1; NZ_ACZB01000093.1. DR EnsemblBacteria; EEZ81435; EEZ81435; VMC_37260. DR PATRIC; 35949646; VBIVibAlg143054_4196. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 204 204 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 279 279 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 280 280 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 300 AA; 32969 MW; 8935B6BF195DDA69 CRC64; MKKVTILDGG MGRELKRIGA PFSQPLWSAQ ALIESPQHVK MAHENFIDAG AEIITVNSYA CVPFHLGEEL YAKRGTELAK SAAKIARDVV TSSNDRVLVA GSLPPVMGSY RPELFEPKRA LEVASELFEA QDQYVDIWLA ETVSSLAEVE VLSIILAKTD KPNYIAFTLM DEPNSLARLR SGESLKVAVN TLLKTNVSGI FFNCSIPEVV EQAIIDTQAV LSESGRELTI GVFANSFAPI KQAHQANETI QEVRHFSPTE YLEYAKKWHA QGASIIGGCC GIEPRHIKLL ATWRDTLENA // ID D0XAC0_VIBHA Unreviewed; 1226 AA. AC D0XAC0; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 27-MAY-2015, entry version 31. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEZ88042.1}; GN Name=metH {ECO:0000313|EMBL:EEZ88042.1}; GN ORFNames=VME_20330 {ECO:0000313|EMBL:EEZ88042.1}; OS Vibrio harveyi 1DA3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=673519 {ECO:0000313|EMBL:EEZ88042.1}; RN [1] {ECO:0000313|EMBL:EEZ88042.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=1DA3 {ECO:0000313|EMBL:EEZ88042.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEZ88042.1}. 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; ACZC01000019; EEZ88042.1; -; Genomic_DNA. DR RefSeq; WP_005438086.1; NZ_ACZC01000019.1. DR EnsemblBacteria; EEZ88042; EEZ88042; VME_20330. DR PATRIC; 35955860; VBIVibHar146073_2174. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEZ88042.1}; KW Transferase {ECO:0000313|EMBL:EEZ88042.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1226 AA; 136637 MW; E134DA5012FE0782 CRC64; MGSNVRQQIE AQLKQRILLI DGGMGTMIQG YKLEEQDYRG ERFADWHCDL KGNNDLLVLT QPQLIKEIHS AYLEAGADIL ETNTFNATTI AMADYEMESL SEEINFAAAK LAREAADEWT AKTPERPRYV AGVLGPTNRT CSISPDVNDP GYRNVSFDEL VEAYSESTRA LIKGGSDLIL IETIFDTLNA KACAFAVDSV FEELGIELPV MISGTITDAS GRTLSGQTTE AFYNSLRHVN PISFGLNCAL GPDELRPYVE ELSRISESFV STHPNAGLPN AFGEYDLSPE DMAEHVKEWA ESGFLNLIGG CCGTTPEHIR HMAMAVEGVK PRDLPELTVA CRLSGLEPLT IEKETLFINV GERTNVTGSA RFKRLIKEEL YDEALEVARQ QVENGAQIID INMDEGMLDA EACMVRFLNL CASEPEISKV PIMVDSSKWE VIEAGLKCIQ GKGIVNSISL KEGKEKFVEQ AKLIRRYGAA VIVMAFDEVG QAETRERKLE ICTNAYRILV DEVGFPPEDI IFDPNIFAVA TGIEEHNNYA VDFIEAVADI KRDLPHAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK NGMDMGIVNA GQLEIYDNVP DKLREAVEDV VLNRRDDSTE RLLDIAAEYA GKGVGKEEDA SALEWRTWAV EKRLEHALVK GITEFIVEDT EEARLNASKP LEVIEGPLMD GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AHLEPFINKE KQAGSSNGKI LLATVKGDVH DIGKNIVGVV LQCNNYEIID LGVMVPCEKI LKVAKEENVD IIGLSGLITP SLDEMVHVAK EMERLDFDLP LLIGGATTSK AHTAVKIEQN YKHPVVYVNN ASRAVGVCTS LLSDELRPGF VEKLDVDYER VRDQHNRKKP RTKPVTLEEA RANKVAIDWD KYTPPAPVKP GIHIFDDFEV STLRKYIDWT PFFMTWSLVG KYPTVFDHEE VGEEAQRLYK DANELLDRVE REGLLKARGM CGLFPAASVG DDIEVYTDES RTEVAKVLHN LRQQTEKPKG FNYCLSDYVA PKESGKRDWV GAFAVTGGIG ERELADEYKA QGDDYNAIMI QAVADRLAEA FAEYLHERVR KEIWGYAVDE ALSNEELIRE KYQGIRPAPG YPACPEHTEK GPLWELMNVE ENIGMSLTSS YAMYPGASVS GWYFSHPDSR YFAIAQIQED QLQSYADRKG WDRIEAEKWL GPNING // ID D0XFR2_VIBHA Unreviewed; 305 AA. AC D0XFR2; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EEZ86137.1}; GN ORFNames=VME_39250 {ECO:0000313|EMBL:EEZ86137.1}; OS Vibrio harveyi 1DA3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=673519 {ECO:0000313|EMBL:EEZ86137.1}; RN [1] {ECO:0000313|EMBL:EEZ86137.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=1DA3 {ECO:0000313|EMBL:EEZ86137.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEZ86137.1}. 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; ACZC01000051; EEZ86137.1; -; Genomic_DNA. DR EnsemblBacteria; EEZ86137; EEZ86137; VME_39250. DR PATRIC; 35960071; VBIVibHar146073_4211. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 212 212 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 287 287 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 305 AA; 33400 MW; 2BCC4ACBE0D23190 CRC64; MDCSMKKLTI LDGGMGRELK RMGAPFSQPL WSAQALIESP EFVYQAHNNF IHAGAEIIIA NSYACVPFHL GQALYDQKGS DLARYAAQIA RECADKSSTL VQVAGCIPPA FGSYRPDLFE PKLGEIIFRT LFDAQEDYVD LWLAETICSL EELTCLQSVF ASSTKPTAYA FSLNDDSLET ALLRSGETVI QAIEHVAQSA DNTNTISVYF NCSVPEVMAK AVSDTKAVLN QHKLDIAIGV YANNFTAIQS NHEANSALQS MRELSPEEYL TFAQEWHQRG ATIIGGCCGI GPEHIKALSD WKASL // ID D0Z1R6_LISDA Unreviewed; 1221 AA. AC D0Z1R6; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 27-MAY-2015, entry version 32. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEZ42447.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEZ42447.1}; GN ORFNames=VDA_003480 {ECO:0000313|EMBL:EEZ42447.1}; OS Photobacterium damselae subsp. damselae CIP 102761. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Photobacterium. OX NCBI_TaxID=675817 {ECO:0000313|EMBL:EEZ42447.1}; RN [1] {ECO:0000313|EMBL:EEZ42447.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIP 102761 {ECO:0000313|EMBL:EEZ42447.1}; 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., Huq A., Grim C.J., Hasan N.A., Vonstein V., RA Bartels D.; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; ADBS01000001; EEZ42447.1; -; Genomic_DNA. DR RefSeq; WP_005303565.1; NZ_ADBS01000001.1. DR EnsemblBacteria; EEZ42447; EEZ42447; VDA_003480. DR PATRIC; 36217023; VBIPhoDam144561_2733. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEZ42447.1}; KW Transferase {ECO:0000313|EMBL:EEZ42447.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 756 756 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1221 AA; 135207 MW; AC6BAC3A58293568 CRC64; MVKGLNLLQQ RLAEQILIID GGMGTMIQGY KLAESDYRGE RFANWHCDVK GNNDLLVLTQ PQIITDIHQQ YLAAGADILE TNTFNATTIA MADYEMADFS AEINLVAAQL ARQAADEWST PDKPRFVAGV LGPTNRTCSI SPDVNDPGFR NITFEQLVIA YSESTRALIK GGVDLILIET IFDTLNAKAC AFAVESVFDE LGYQLPIMIS GTITDASGRT LSGQTTEAFY NALRHVKPIS FGLNCALGPD ELRQYVAELS RLAECSVSAH PNAGLPNAFG EYDLEPEEMA EHIAEWAQSG FLNLVGGCCG TTPEHIRQMA AVTQNIKPRT PPSIPVACRL SGLEPLNIEK NSLFINVGER TNVTGSARFK RLIKEELYDE ALEVARQQVE AGAQIIDINM DEGMLDAKAA MVRFLNLCAT EPEIAKVPIM VDSSKWEVIE AGLQCVQGKP IVNSISLKEG KAKFIEQAKL IQRYGAAVIV MAFDEEGQAD TRERKVEICT QAYRILVDEV GFAPEDIIFD PNIFAVATGI EEHNNYAVDF IEAVGEIKAT LPHAMISGGV SNVSFSFRGN DPVREAIHAV FLYYCFQKGM DMGIVNAGQL AIYDDLPQEL RQAVEDVVLN LREDSTERLL DIAEKYRGTG KVEEDRSAQE WRSWPVEKRL EHALVKGITE FIVEDTEQAR ALAAKPLEVI EGPLMAGMNV VGDLFGEGRM FLPQVVKSAR VMKQAVAYLE PFINAEKQAG SSNGKILLAT VKGDVHDIGK NIVGVVLQCN NYEIIDLGVM VSCEQILKVA KEEQVDIVGL SGLITPSLDE MVHVAKEMER QGFELPLLIG GATTSKAHTA VKIEQNYHAP VVYVSNASRA VGVCSALLSE TQREDFIARL DKEYEVVRDQ HSRKKPRSAP ITLEQARENC AHIDWQAYQP PQPKSKGIHT IIDCSVATLR QYIDWTPFFM TWSLSGKYPT ILRHEVVGEE ATKLFNEANV LLDKIEQEGI IKANGVCGFF PANSVGDDIE VYTDESRQHV LTRLHHLRQQ TAKPKGANYC LSDFIAPKSS QHPDWIGAFA VTGGIGESEL AAQFKAQGDD YNAILIQAVA DRLAEAFAEY LHQQVRTQLW GYSPKEDLSN DDLIREKYQG IRPAPGYPAC PEHTEKGTLW QLLEVEERTG MSLTESYAMW PGASVSGWYF SHPEARYFAV AQIQQDQALD YANRKGWNER EIEKWLGPNL N // ID D0Z9V7_EDWTE Unreviewed; 1227 AA. AC D0Z9V7; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 27-MAY-2015, entry version 44. DE SubName: Full=12-dependent methionine synthase {ECO:0000313|EMBL:ACY83047.1}; GN Name=metH {ECO:0000313|EMBL:ACY83047.1}; GN OrderedLocusNames=ETAE_0200 {ECO:0000313|EMBL:ACY83047.1}; OS Edwardsiella tarda (strain EIB202). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Edwardsiella. OX NCBI_TaxID=498217 {ECO:0000313|EMBL:ACY83047.1, ECO:0000313|Proteomes:UP000002634}; RN [1] {ECO:0000313|EMBL:ACY83047.1, ECO:0000313|Proteomes:UP000002634} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EIB202 {ECO:0000313|EMBL:ACY83047.1, RC ECO:0000313|Proteomes:UP000002634}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001135; ACY83047.1; -; Genomic_DNA. DR RefSeq; WP_012847078.1; NC_013508.1. DR RefSeq; YP_003294258.1; NC_013508.1. DR EnsemblBacteria; ACY83047; ACY83047; ETAE_0200. DR KEGG; etr:ETAE_0200; -. DR PATRIC; 32075719; VBIEdwTar116525_0186. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; ETAR498217:GJC4-216-MONOMER; -. DR Proteomes; UP000002634; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002634}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 134523 MW; F2149E84A9F1E0E6 CRC64; MNTTLERLRR RLEKRILVLD GGMGTMIQRY GLSEQDFRAE RFADWPCDLK GNNDLLALTR PDIISAIHYA YLEAGADILE TNTFNATRIA MADYRMEALA PEINYRAACL ARACADEWTA RTPHQPRFVA GVLGPTNRTA SISPEVNDPA CRNITFDQLV AAYRESARAL IEGGVDLLMI ETVFDTLNAK AAVYALECEF AALGVTLPVM ISGTITDASG RTLSGQTTEA FYNALRHARP LSFGLNCALG PEDLRQYVAE LSRVAECHVS AHPNAGLPNA FGEYDLSPQA MAQQIAEWAR AGYLNIVGGC CGTTPEHIAA ISRAVQGITP RALPTLPVAC RLSGLEPLTI DETSLFVNVG ERTNVTGSAK FKRLIKENKY DEALDVARQQ VASGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP LMIDSSRWSV IEAGLKCIQG KGIVNSLSLK EGEANFLEHA RQVRRFGAAL VVMAFDEQGQ ADTRERKVAI CRRAYQLLTE RIGFPPEDII FDPNIFAVAT GIEEHSNYAV DFIASCAEIK AQLPHALISG GVSNVSFSFR GNEAVREAIH AVFLYHAIRH GMDMGIVNAG QLAIYDDLPD DLRTAAEAVI LNQSPDATDR LLALAERYRD TQGSAQAEAQ QAEWRSWPVA QRLEYALVKG IGEFIAQDTE AARLEADRPI AVIEGPLMAG MNRVGDLFGD GKMFLPQVVK SARVMKQAVA YLSPFIEASK QRGSSAGKVL LATVKGDVHD IGKNIVGVVL QCNNYEIIDL GVMVPAERIL RVAREERVDI IGLSGLITPS LDEMVNVASE MERQGFTLPL LIGGATTSKA HTAVKIAPAY GGPTVYVQNA SRTVGVVAAL LSEAQRGPFI DRTRREYEAA RAQHGRQTPR TPPVTLAQAR ANGVVTDWSA CPPPVPLRLG VQTVQPGIAR LRDYIDWTPF FLTWSLAGKY PRILQDEVVG EEARRLLADA NGLLDRLEAS GSLTPRGVFG LFAANRRGDD VLIYRDESRR EVLAVSHHLR QQSDKRVGPN YCLADFVAAA DEGIADYIGA FAVTGGLEEE ALAQAFDAQH DDYHKIMVKA LADRLAEAFA EYLHQQVRKV HWGYAADEAL DNEQLIRENY RGIRPAPGYP ACPEHSEKAT LWRLLDVERH TGMRLTESYA MWPGASVSGW YFSHPHSKYF AVARVQRDQV ADYAARKGMT LAEAERWLAP NLGYEVA // ID D1A2R0_THECD Unreviewed; 1157 AA. AC D1A2R0; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 01-APR-2015, entry version 42. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACY97858.1}; GN OrderedLocusNames=Tcur_2292 {ECO:0000313|EMBL:ACY97858.1}; 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 {ECO:0000313|EMBL:ACY97858.1, ECO:0000313|Proteomes:UP000001918}; RN [1] {ECO:0000313|Proteomes:UP000001918} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19995 / DSM 43183 / JCM 3096 / NCIMB 10081 RC {ECO:0000313|Proteomes:UP000001918}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001738; ACY97858.1; -; Genomic_DNA. DR RefSeq; WP_012852642.1; NC_013510.1. DR RefSeq; YP_003299896.1; NC_013510.1. DR EnsemblBacteria; ACY97858; ACY97858; Tcur_2292. DR KEGG; tcu:Tcur_2292; -. DR PATRIC; 32514248; VBITheCur33965_2343. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; TCUR471852:GHHD-2339-MONOMER; -. DR Proteomes; UP000001918; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001918}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001918}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 226 226 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 292 292 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 736 736 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1157 AA; 126842 MW; 1E0A45635261AE9D CRC64; MSATPQSLRQ ALRERVVVAD GAMGTMLQAH NPTLDDFQGY EGCNEILNVT RPDIVRAVHA AYLDAGVDCV ETNTFGANLG NLGEYGITDR IEELAEAGAR IAREVADSYS TPERPRWVIG SIGPGTKLPT LGHVSYGELR ESYRRTAAGL IAGGAHALLV ETCQDLLQVK AALNGAKQAV AEAGADVVLI AQVTIEQNGA MLLGSEIGAA LTALEPLGID LIGLNCATGP AEMSEHLRYL SRHARVGLSC MPNAGLPELT PDGARYPLTP QELADAHDAF TRDYGLSLVG GCCGTTPEHL RLVVERVRGR ELAPRRPRPE PGASSLYQHV PFKQDTSYLA IGERTNANGS KAFREAMLAE RWDDCVRIAR DQARDGAHMI DLCVDYVGRD GVADMKELAF RLATASTLPI MLDSTEPAVL RAGLEMLGGR AVVNSVNYED GRGPGSRFHR TMTAVREHGA AVVAMCIDEG GQARTREDKV RIACEIIEDL TGNWGMRLED IVVDCLTFPI ATGQEETRRD ALETIEAIAE LKRRYPQVQT TLGISNVSFG LNPAARVVLN SVFLNECVNA GLDSAIVHAS KILPMNRIPD EQRQVALDMV YDRRREGYDP LQRFMELFEG VSAKELRASR AQELAALPLW ERLKRRIIDG EANGMEADLD EALQSRPALE IINDVLLDGM KTVGDLFGSG QMQLPFVLQS AEVMKAAVAY LEPHMEKSAD GGKGRIVLAT VKGDVHDIGK NLVDIILSNN GYEVINLGIK QPISAIVEAA KEHRADVIGM SGLLVKSTVV MKENLEELNA RGLARQWPVL LGGAALTRAY VEQDLAELFD GEVRYARDAF EGLRLMDAFM AVKRGEEGAQ LPPLRKRRVA SGAKLKVTAP EDMPARSDVA TDNPVPEPPF WGDRIVKGIP LADYAAFLDE RATFMGQWGL KPARGGDGPS YEELVETEGR PRLRMWLDRI QSEGLIEAAV VYGYFPAVSE GDDLVILNDD GSERERITFP RQRRDRHLCL ADFFRPRESG ETDVVAFQLV TVGAKVSQAT AELFAKNSYR EYLELHGLSV QLTEALAEYW HARVREEIGF GDQDPADLDG FFKVDYRGAR YSFGYPACPD LENRAVVMRL LRPERIGVTL SEEFQLVPEQ STDALIAHHP EAKYFNV // ID D1AP89_SEBTE Unreviewed; 791 AA. AC D1AP89; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 27-MAY-2015, entry version 35. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACZ09923.1}; GN OrderedLocusNames=Sterm_3081 {ECO:0000313|EMBL:ACZ09923.1}; OS Sebaldella termitidis (strain ATCC 33386 / NCTC 11300). OC Bacteria; Fusobacteria; Fusobacteriales; Leptotrichiaceae; Sebaldella. OX NCBI_TaxID=526218 {ECO:0000313|EMBL:ACZ09923.1, ECO:0000313|Proteomes:UP000000845}; RN [1] {ECO:0000313|Proteomes:UP000000845} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33386 / NCTC 11300 {ECO:0000313|Proteomes:UP000000845}; 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. RN [2] {ECO:0000313|EMBL:ACZ09923.1, ECO:0000313|Proteomes:UP000000845} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33386 / NCTC 11300 {ECO:0000313|Proteomes:UP000000845}; RX PubMed=21304705; RA Harmon-Smith M., Celia L., Chertkov O., Lapidus A., Copeland A., RA Glavina Del Rio T., Nolan M., Lucas S., Tice H., Cheng J.-F., Han C., RA Detter J.C., Bruce D., Goodwin L., Pitluck S., Pati A., Mavromatis K., RA Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L., RA Chang Y.-J., Jeffries C.D., Brettin T., Goeker M., Beck B., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., RA Klenk H.-P., Chen F.; RT "Complete genome sequence of Sebaldella termitidis type strain (NCTC RT 11300)."; RL Stand. Genomic Sci. 2:220-227(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; CP001739; ACZ09923.1; -; Genomic_DNA. DR RefSeq; WP_012862505.1; NC_013517.1. DR RefSeq; YP_003309854.1; NC_013517.1. DR EnsemblBacteria; ACZ09923; ACZ09923; Sterm_3081. DR KEGG; str:Sterm_3081; -. DR PATRIC; 32410162; VBISebTer81212_3122. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; STER526218:GHLD-3107-MONOMER; -. DR Proteomes; UP000000845; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000845}; KW Methyltransferase {ECO:0000313|EMBL:ACZ09923.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000845}; KW Transferase {ECO:0000313|EMBL:ACZ09923.1}. SQ SEQUENCE 791 AA; 87188 MW; EE187DF59B3A6957 CRC64; MGIREKLGKE ILFFDGAMGT MLQKKGLKLG KMPEDLNIDN PEIIEEIHRL YAKSGADIIT TNTFGANRLK LEHSSYSQEE IIKSGISIAK KANPDGYVAL DIGPLGQLLE PLGVLPFEEA YEIFKEQIIL GEKYGADIII IETMVDIYEA KAAILAAKEN SSLPVICTVT FQEDKRMLTG TSILGAVTIL ESLGVDALGV NCSLGPKELI PIVDELLQYS KTPVIVQPNA GLPKMIGGNT VFDLSAEEYS SIMEDFVHKG ISIIGGCCGT DERFIKSIHD KLIDFSPVPR KIKPRSIIAT ATKCVDLDEG IKVIGERINP TGKKKLKEAL INNNMEYILR EAVTQKEKGA DILDVNVGLP EINESEVITG VVKEIQSIID LPLQIDSSDA GAIEAALRIY NGKAVINSVN GKAEIMDTIF KIARKYGACV VGLTLDENGI PSSAEERFKI AEKIVNTAEK YGIPKENLLI DCLVLTASAQ QKEVSETLKA ITMVREKLGV KTVLGVSNVS FGLPDRALLN RTFLTMALHS GLTTPILNPQ SEEMMHIIKA FNVLTNQDKD SAEYIDFFNN SDTKKEIIKN TDLELPDIIR LGLKEEGKSK IYSLLKEYQP MYIIDNYLIP VLDTIGIKFE KGEIFLPQLI QTAETVKYFF EILKGEMIKE KKEFVNKGDI ILATVKGDIH DIGKNIVKIV LENYGYNIID LGKDVPVEKV VNTAKEKNIQ LIGLSALMTT TVKSMEETIK ALRTSNIKCK VFVGGAVLTQ EYADMIGADF YAEDAQESVR IADKFFNNTS K // ID D1B2D3_SULD5 Unreviewed; 311 AA. AC D1B2D3; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACZ12253.1}; GN OrderedLocusNames=Sdel_1230 {ECO:0000313|EMBL:ACZ12253.1}; OS Sulfurospirillum deleyianum (strain ATCC 51133 / DSM 6946 / 5175). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Sulfurospirillum. OX NCBI_TaxID=525898 {ECO:0000313|EMBL:ACZ12253.1, ECO:0000313|Proteomes:UP000002222}; RN [1] {ECO:0000313|Proteomes:UP000002222} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51133 / DSM 6946 / 5175 RC {ECO:0000313|Proteomes:UP000002222}; 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; ACZ12253.1; -; Genomic_DNA. DR RefSeq; WP_012857010.1; NC_013512.1. DR RefSeq; YP_003304288.1; NC_013512.1. DR EnsemblBacteria; ACZ12253; ACZ12253; Sdel_1230. DR KEGG; sdl:Sdel_1230; -. DR PATRIC; 32483259; VBISulDel109514_1253. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; SDEL525898:GHVA-1260-MONOMER; -. DR Proteomes; UP000002222; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002222}; KW Methyltransferase {ECO:0000313|EMBL:ACZ12253.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002222}; KW Transferase {ECO:0000313|EMBL:ACZ12253.1}. SQ SEQUENCE 311 AA; 34262 MW; DE39000F00EC52F9 CRC64; MNPLTPFLEN QFVFILDGAF GTELERKGYD INDSLWSAKF LMEKPEAIAE VHLDYLRAGS DCITTASYQA SFEGFMKRGM SEEEAKALIA SSVQIAKKVR DDFWADETNR TKRLKPLVAA SVGPYGAYLA DGSEFRGDYA LDVEALQAFH AKRLLTLIEA KPDLLACETI PCLKEAKALC TLLEDYPDVS AWMSFSAKDG EHINSGESVR ECAQFLENQK NIVAIGINCT APEFIESLIG EIKAVSSKLI IVYPNGGATY NALTKTWNGL SKNASYGKMA YGWYQKGARL IGGCCQTTPE DIAQIAKWVR G // ID D1B335_SULD5 Unreviewed; 1156 AA. AC D1B335; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 27-MAY-2015, entry version 44. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACZ12505.1}; GN OrderedLocusNames=Sdel_1488 {ECO:0000313|EMBL:ACZ12505.1}; OS Sulfurospirillum deleyianum (strain ATCC 51133 / DSM 6946 / 5175). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Sulfurospirillum. OX NCBI_TaxID=525898 {ECO:0000313|EMBL:ACZ12505.1, ECO:0000313|Proteomes:UP000002222}; RN [1] {ECO:0000313|Proteomes:UP000002222} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51133 / DSM 6946 / 5175 RC {ECO:0000313|Proteomes:UP000002222}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001816; ACZ12505.1; -; Genomic_DNA. DR RefSeq; WP_012857256.1; NC_013512.1. DR RefSeq; YP_003304540.1; NC_013512.1. DR EnsemblBacteria; ACZ12505; ACZ12505; Sdel_1488. DR KEGG; sdl:Sdel_1488; -. DR PATRIC; 32483777; VBISulDel109514_1511. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SDEL525898:GHVA-1519-MONOMER; -. DR Proteomes; UP000002222; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002222}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002222}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 726 726 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1156 AA; 128025 MW; 8851D01326579EDC CRC64; MATLQELISE KILIIDGAMG TQIQALQIPL EKWEGKEGCN ELLNVTCKDE ISKIHRGYLL AGADIIKTNT FGALPWVLDD YGIGDRTYEL ARTGVEIVKE ACLAFSSEDK PRFCAAAFGP GTKLPSLGHI GYDEMYAGYR VAATGAIEGG CDVFLIETAQ DPLQIKAALH AIFDAQTSLH VKLPVMVSVT IELSGTMLIG TDATTIATIL EPFDIMSLGF NCGTGPEQVE KHVKTLSSVW SKPISVHANA GLPQNRGGYT FYPMGPREFA ELQEKFTQIA GVAILGGCCG TTPQHILELS KRVEGKKLLA PQGEMARSIA SLFEVRALKQ DPAPFLIGER SNATGSKAFR ELLLAEDYDG TLSVAQQQVR SGAHGIDVSV GFAGRDEIKD TTAVVGRYVQ KILLPLMPDT TQVPALECAL KLIGSKPIIN SVNLEDGIEK FDKVCSLAKR FGCALVCLTI DEQGMAKTKA QKVAIAERIF QLATTKHGIN AGDLVFDLLT FTVGSGDAEY HTAAIETIEA IREFHAMHPE VGFVLGISNI SFGLAKHARE YLNSVFLHHC VEAGLSMAIV NVKNTLPMHK ISDIDKKVCE DLLFNRREEG DPLFKFISHF EGVVENKDES DAAYLAMSTK EKIATLLIDG DKERMLALLP TAKEEIAAEV IVNEILIDAM KVVGELFGSG KMQLPFVLQS AEVMKASVDY LQPYLPKTEK STTTTLIIGT VKGDVHDVGK NLVDIILSNN GFKVVNIGIK ADLEQFLEAL KEHKADAIGM SGLLVKSTNV MKENLEAMQK MGLNIPVILG GAALTDNFVE DFCRPIYEGP IFYCKDAFEG ITAMSRIEAK NYDTDFGRKV LENAVVRANK ETKEIPPFSE IKMPSRELKI PTPPFWGRRV LKTDVKELAY SWINHKILFA QRWGYSGKGQ SKEEKQKQLD EVLYPTYERV KADIERLGLF EPTLIYGYYP ARSHENKLYL FDESEGYFSK EQVCRERVDV VAKRALKTFD FPRQNRNPYR SLSDFIAPDR HDVLALTCVS AGAKFSAYEK ELYDAGNFKE YFFVHGLGVE LAEALAEIVH KQIRLDLGVA QHEGHSLRDV QMKRYHGCRY SFGYPACPNL EDTRVIFDLL KPEEFGIELS ETFQIHPEQS TTAIVMHHKE ALYFNV // ID D1B7X8_THEAS Unreviewed; 816 AA. AC D1B7X8; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 29-APR-2015, entry version 35. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACZ18381.1}; GN OrderedLocusNames=Taci_0141 {ECO:0000313|EMBL:ACZ18381.1}; OS Thermanaerovibrio acidaminovorans (strain ATCC 49978 / DSM 6589 / OS Su883) (Selenomonas acidaminovorans). OC Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae; OC Thermanaerovibrio. OX NCBI_TaxID=525903 {ECO:0000313|EMBL:ACZ18381.1, ECO:0000313|Proteomes:UP000002030}; RN [1] {ECO:0000313|EMBL:ACZ18381.1, ECO:0000313|Proteomes:UP000002030} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49978 / DSM 6589 / Su883 RC {ECO:0000313|Proteomes:UP000002030}; 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 ----------------------------------------------------------------------- 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; ACZ18381.1; -; Genomic_DNA. DR RefSeq; WP_012868897.1; NC_013522.1. DR RefSeq; YP_003316663.1; NC_013522.1. DR EnsemblBacteria; ACZ18381; ACZ18381; Taci_0141. DR GeneID; 8629951; -. DR KEGG; tai:Taci_0141; -. DR PATRIC; 32491567; VBITheAci125881_0144. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; TACI525903:GH4K-141-MONOMER; -. DR Proteomes; UP000002030; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002030}; KW Methyltransferase {ECO:0000313|EMBL:ACZ18381.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002030}; KW Transferase {ECO:0000313|EMBL:ACZ18381.1}. SQ SEQUENCE 816 AA; 86264 MW; 6C81D7299311769F CRC64; MLLDRGRVRS LLGEVRSPLV MDGGMGTQLA ERGWHPPMLP EEMCLHMPQA VREVHESYVE SGAAVLETNS FGGSVRKLSM RGLGHLAEEL ALRSAQIARQ AAGDALVAGS VGPTGEMLAP LGEMSFEEAV KSFEPQVRGL IRGGADLILI ETMLDLKEAA AAVEAVKRVD PLFPFVVSFT FDRDGRTVTG TTPEAAACWA QAVGALGVGA NCGLGPRGYV PVVRRLAEAS PLPVWVYPNA GVPSAGDYLG PDEFVGECEE LLKAGASVIG GCCGTTPDHV RALAALARGR RVTRLHCDLG GVRLSSRSRV ISAGAGLPLA MIGERINVSR KSPLREQVGE YRYGEVKREA KAQTVAGAAV IDVNVGLPQI DQVRAIREAI WAVESVTHLP ISIDSDAPAV LEAGLAEAVG VPLMNSVTAK EESLELGIRL ALRYGAVLAV LLIDQRGILE DGLERARIAQ RVLDVASSRG LGPNRIVFDP LTLTLGASQS NGLETLRAVE AVSRMGGHTM LGISNVSHGL PARGLLNRTF LAMAMERGLD MVICNPLDRE LLGVVRAADA LRGRDRGLGA FMAFGPSWRE PERGAVQAAE ASAGEVCSGL SELSRRVMEG DRDGALAEAL TVMAQEGPME VISGHLIPAL DEVGRRYETG EFFLPQLMEA AEAASAVCRL AEEELLRLGR SANRGTVVLA TVEGDLHDLG KNLVGTVLKS HGYRVVDLGK DVKAEVILEA AQREGAQVVG LSALMTSTVP RMREFIEEAR RRGAGFKVIV GGAAVSPAYA RSIGADGMSY DAVGAARLVE RLLSGLPCDW EGLGCS // ID D1BG25_SANKS Unreviewed; 1176 AA. AC D1BG25; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 29-APR-2015, entry version 42. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ACZ21536.1}; GN OrderedLocusNames=Sked_16010 {ECO:0000313|EMBL:ACZ21536.1}; OS Sanguibacter keddieii (strain ATCC 51767 / DSM 10542 / NCFB 3025 / OS ST-74). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Sanguibacteraceae; Sanguibacter. OX NCBI_TaxID=446469 {ECO:0000313|EMBL:ACZ21536.1, ECO:0000313|Proteomes:UP000000322}; RN [1] {ECO:0000313|EMBL:ACZ21536.1, ECO:0000313|Proteomes:UP000000322} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51767 / DSM 10542 / NCFB 3025 / ST-74 RC {ECO:0000313|Proteomes:UP000000322}; RX PubMed=21304646; RA Ivanova N., Sikorski J., Sims D., Brettin T., Detter J.C., Han C., RA Lapidus A., 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 Pati A., Mavromatis K., Chen A., Palaniappan K., D'haeseleer P., RA Chain P., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Goker M., Pukall R., Klenk H.P., Kyrpides N.C.; RT "Complete genome sequence of Sanguibacter keddieii type strain (ST- RT 74)."; RL Stand. Genomic Sci. 1:110-118(2009). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001819; ACZ21536.1; -; Genomic_DNA. DR RefSeq; WP_012866605.1; NC_013521.1. DR RefSeq; YP_003314370.1; NC_013521.1. DR EnsemblBacteria; ACZ21536; ACZ21536; Sked_16010. DR KEGG; ske:Sked_16010; -. DR PATRIC; 32391644; VBISanKed123513_1579. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; SKED446469:GHD3-1598-MONOMER; -. DR Proteomes; UP000000322; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000322}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000322}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 744 744 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1176 AA; 126708 MW; 2CEB04D51B018E4F CRC64; MLTARAAALK SAIATRVVVA DGAMGTMLQA ADLSLDDFQG LEGCNEILNV TRPDVVESVH DAYFAVGVDC VETNTFGANW SNLGDYGIDD RIFELAEAGA RVARRSADKH ATPDKPRWVL GSMGPGTKLP SLGHTSYAHL RDTFAQQAAG LVAGGADAIL VETSQDLLQT KAAVNGSKKA MAESGVEVPI FVQVTVEATG TMLMGSEIGA ALTTLAALGI DSIGLNCATG PAEMSEHLRH LAKHSAVPVT CMPNAGLPVL GANGAHYPLS PAELAVAHQQ FVREFGLGLV GGCCGTTPEH LRAVVDAVGG APVVERTPEP EKGVASLYTH VDFDQDASFL AIGERTNANG SKAFREAMLA EDWDECVQIA RAQTRDGAHL LDVCVDYVGR DGVADVRSVV SRLASASTLP LVIDSTEPPV IQAGLELVGG RGVVNSVNFE DGDGETSRYG RIMPLVKEHG AAVIALTIDE EGQARTAKTK LAIASRLVDD LTGRWGMDVA DIIVDTLTFP IATGQEETRR DAIETIEAIR ALKAKYPGVH TTLGVSNVSF GLNPAARVVL NSVFLHEAVQ AGLDSAIVHA AKILPLAKIP DEQRKAALDL VWDRREYDAD GAMTFDPLAR LLDLFAGVDT AALKDQRAAE LAALPLGERL ERRILDGDLK GLDTDLDLAL GEGMTALAII NDHLLEGMKV VGELFGKGEM QLPFVLQSAE AMKTAVAYLE PHMEKTDEAG KGTIVLATVR GDVHDIGKNL VDIILTNNGY TVVNIGIKQT IAAMIEAAEE HHADVIGMSG LLVKSTVVMR ENLEELNARG LAQKYPVLLG GAALTRTYVE DDLDAVYDGQ VRYARDAFEG LRLMEPLVRV ARGEDVAAVG LPALKKRRHA TVTVTQTADE DLPPRSDIAS DNPVPTPPFW GSRIVKGIQL ADYAAFLDER ATFMGQWGLK PSRADDSASY EELVEVEGRP RLRDWLDRIK TEDMFDPSVV YGYFPAVADG DDMVILHHEG PDGGSGGEPG TERMRFTFPR QRRDRHLCLA DFVRPKDSGE VDVVAFQLVT VGASVDPHTA RLFAENRYRE YMELHGLSVQ LTESLAEFWH SRVREELGFA AEDPADLDGM FKVDYRGARF SLGYPACPDM EDRRKVMELL RAERVGVVLS DELQLHPEQS TDAIVFHHPA AKYFSV // ID D1BKY6_VEIPT Unreviewed; 341 AA. AC D1BKY6; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 29-APR-2015, entry version 28. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACZ24043.1}; GN OrderedLocusNames=Vpar_0359 {ECO:0000313|EMBL:ACZ24043.1}; 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 {ECO:0000313|EMBL:ACZ24043.1, ECO:0000313|Proteomes:UP000007968}; RN [1] {ECO:0000313|Proteomes:UP000007968} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10790 / DSM 2008 / JCM 12972 / Te3 RC {ECO:0000313|Proteomes:UP000007968}; 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 ----------------------------------------------------------------------- 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; ACZ24043.1; -; Genomic_DNA. DR RefSeq; WP_012863924.1; NC_013520.1. DR RefSeq; YP_003311323.1; NC_013520.1. DR EnsemblBacteria; ACZ24043; ACZ24043; Vpar_0359. DR KEGG; vpr:Vpar_0359; -. DR PATRIC; 32529998; VBIVeiPar80537_0350. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; VPAR479436:GHOS-363-MONOMER; -. DR Proteomes; UP000007968; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007968}; KW Methyltransferase {ECO:0000313|EMBL:ACZ24043.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007968}; KW Transferase {ECO:0000313|EMBL:ACZ24043.1}. SQ SEQUENCE 341 AA; 37166 MW; ADEFCDED443A69A6 CRC64; MGDMMAKRSA FLDIIKEKDA LVLDGALGTE LERYGCDIQH KLWSAKVLMD QPDIIKKIHI SYLAAGADII QSSGYQATVA GFKGLGYGTE EAIELVKLSV RLAVQARNEF LEAKASGALT LRGIKLGEET PEGVKYFSEG ALPKPLVAAS VGPYGAFLAD GSEYRGYPDV QTEYLEVFHI PRLALFCEEN PDILSFETIP SYAEAIAIAR AMSDPFTSKG IPAWIAFSCK DGHHVSSGET IIKCAQMIDK VHPITGIGIN CTKPEYVESL IKDIRTVTDK PIAVYPNLGE SYDSKTKTWY GDAASFVDYV EVWRKAGAEI IGGCCRTTPE IIGDIAKKIH N // ID D1BQ67_VEIPT Unreviewed; 811 AA. AC D1BQ67; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 29-APR-2015, entry version 34. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACZ25524.1}; GN OrderedLocusNames=Vpar_1850 {ECO:0000313|EMBL:ACZ25524.1}; 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 {ECO:0000313|EMBL:ACZ25524.1, ECO:0000313|Proteomes:UP000007968}; RN [1] {ECO:0000313|Proteomes:UP000007968} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10790 / DSM 2008 / JCM 12972 / Te3 RC {ECO:0000313|Proteomes:UP000007968}; 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 ----------------------------------------------------------------------- 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; ACZ25524.1; -; Genomic_DNA. DR RefSeq; WP_012865040.1; NC_013520.1. DR RefSeq; YP_003312804.1; NC_013520.1. DR EnsemblBacteria; ACZ25524; ACZ25524; Vpar_1850. DR GeneID; 8637354; -. DR KEGG; vpr:Vpar_1850; -. DR PATRIC; 32533026; VBIVeiPar80537_1809. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; VPAR479436:GHOS-1915-MONOMER; -. DR Proteomes; UP000007968; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007968}; KW Methyltransferase {ECO:0000313|EMBL:ACZ25524.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007968}; KW Transferase {ECO:0000313|EMBL:ACZ25524.1}. SQ SEQUENCE 811 AA; 87070 MW; 2A164090936CA51B CRC64; MYIFDGAMGT MLQAAGLEEG YCPELFNVER PEVVKNIHAQ YLQHGSDVIT TNTFGACGLK LEDYDLQDRV REINIAAVKV AKEAIAEVKP SARIAGSMGP TGRFLQPLGN MSFDDIYDTY REQAEALIEG GVDFIIIETI IDVQEMRAAL LASLDAREAA GKTKEDVQII CQFSFSEDGR TITGTPPAVA TSIVEAIGAD IIGINCSLGP EQITPLIKEI ASVTNLPISC QPNAGMPQLI NKQTVFPLTA EEMGPLMLDI VDAGTSYVGG CCGTTPAHIQ SISNAVKAHT PKERAHIEPK TIITSRTRLL ELGHNTKPLI IGERINPTGR KVLAQELRDG SFIRVKRDAL DQVEAGADIL DVNMGVAGMD QSPLMERAIF ELSMLVETPL SIDTLDPVAM EVALKNYPGR ALINSVNGEE ESITHVMPLA KRYGAALLCL PICSGDLPEK AEDRVALAES IVNRAYGYGL QPHDLLLDPL VLTLASGEDS ARQTLRTLQL YKEKFGFPTV MGLSNISFGM PQRPYLNGQF LTMALACGLT TPIMNPLNYP AKKAFVSSTT LLGWDPGSAE FIKEYGYEDE TTAPGNSAPK GPEKKSFDSN DPLANIRACV EQGEKEAIID LVKKALADGI DPLDLTKKGL SEAMNVVGDK FGSGKLFLPQ VMLAAETMQA AFNTIKEIIP ASESLDKGTV VVATVKGDIH DLGKNIVAAL LENNGYKIVD LGKDVDPEVI VQAIKDNKAA LVGICSLMTT TMPQIDNTIA AIRAAGLKTK VMVGGAVVSQ DYADQAGADI YAKDGIAAVN HANDFFETLE K // ID D1BTI0_XYLCX Unreviewed; 1193 AA. AC D1BTI0; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 29-APR-2015, entry version 45. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACZ30959.1}; GN OrderedLocusNames=Xcel_1940 {ECO:0000313|EMBL:ACZ30959.1}; 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 {ECO:0000313|EMBL:ACZ30959.1, ECO:0000313|Proteomes:UP000002255}; RN [1] {ECO:0000313|Proteomes:UP000002255} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15894 / CECT 5975 / LMG 20990 / XIL07 RC {ECO:0000313|Proteomes:UP000002255}; 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. RN [2] {ECO:0000313|EMBL:ACZ30959.1, ECO:0000313|Proteomes:UP000002255} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15894 / CECT 5975 / LMG 20990 / XIL07 RC {ECO:0000313|Proteomes:UP000002255}; RX PubMed=21304672; DOI=10.4056/sigs.571102; RA Foster B., Pukall R., Abt B., Nolan M., Glavina Del Rio T., Chen F., RA Lucas S., Tice H., Pitluck S., Cheng J.-F., Chertkov O., Brettin T., RA Han C., Detter J.C., Bruce D., Goodwin L., Ivanova N., Mavromatis K., RA Pati A., Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L., RA Chang Y.-J., Jeffries C.D., Chain P., Rohde M., Goeker 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 Xylanimonas cellulosilytica type strain RT (XIL07)."; RL Stand. Genomic Sci. 2:1-8(2010). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001821; ACZ30959.1; -; Genomic_DNA. DR RefSeq; WP_012878701.1; NC_013530.1. DR RefSeq; YP_003326517.1; NC_013530.1. DR EnsemblBacteria; ACZ30959; ACZ30959; Xcel_1940. DR KEGG; xce:Xcel_1940; -. DR PATRIC; 32552899; VBIXylCel24446_1980. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; XCEL446471:GHA2-1977-MONOMER; -. DR Proteomes; UP000002255; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002255}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002255}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 239 239 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 757 757 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1193 AA; 128363 MW; B5B04ECE36115B01 CRC64; MTIEAPAPTV DPVADARAAA LLDAVRSRVV VADGAMGTMI QEQDPTLEDY EGHEGCNEVL NVSRPDIIGA VHDAYLEAGV DAIETNTFGA NWSNLGDYGI DHRIRELARA GAAIARSRAD AFATPDRPRW VLGSMGPGTK LPSLGHTTYA HLRSTFAEQA AGLLEGGADA LLIETSQDLL QAKAAVTAAH DAFAAVGRRV PVMVSVTVET TGTMLMGSEI GAALTALQAI GVDTIGLNCA TGPDKMSEHL RYLSQHSEMP VTSMPNAGLP ELGPHGAVYP LSATELAAAH AQFVREFGLG LVGGCCGTTP EHLAAVVDAV RGADLPPREP QRENAVASLY SPTDLTQELS YLAIGERTNA NGSKAFREAM LEGRWDDIVD LARAQTREGA HLLDVCVDYV GRDGVADVRE VVSRLASAST LPLVIDSTEP AVLQAGLELV GGRAVVNSVN FEDGEGPGSR FARIMPLVKE HGTAVVALTI DEEGQARTTD HKVAIASRLI DTLVQKWGMR VDDIIVDALT FPIATGQEET RRDAIETIEA IRQITAKYPG VHTTLGVSNV SFGLNPAART VLNSVFLHEA VAAGLDSAIV HAAKILPRTA IPDEQWDAAL ALVWDKRVYD DAGELVHDPL SHLLSLFEGV DAAALRDARE AELSALPIGE RLARRIIDGN KKGLEADVDE ALADRMKALD IVNDHLLSGM QVVGELFGSG QMQLPFVLQS AEVMKTAVAL LEPHMEKVAG EATKGTIVLA TVRGDVHDIG KNLVDIILTN NGYKVVNIGI KQPISAMIEA AEEHDADVIG MSGLLVKSTV VMKENLQELA SRGLASRWPV LLGGAALTRT YVEDDLASQF PGTVRYARDA FEGLRLMEPL VAIARGAAPD AVGLPPLKKR RHAAVTLAET APENLPARSD VAADNEVPEP PFWGTRIVKG MPLADYAAFL DERAVFLGQW GLKPGRGDDG ASYEELRQTE GLPRLAMWLD RIRTERILDP SVIYGYFPAW SEGDDVVVAH HAGPDGGSGG VAGTERLRFT FPRQRRDRHL CLADFIRPRS YYEETGSFDV LPVQLVTVGS TVAEHTAKMF AANEYRDYME LHGLSVQLTE ALAEYWHSRV RAELGFAAEE PTDVDGLFKL DYRGARMSLG YPACPNMEDR HKVVELLRPG RVGVELSEEL QLHPEASTDA FVFHHPEAKY FSV // ID D1CBD0_THET1 Unreviewed; 629 AA. AC D1CBD0; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 27-MAY-2015, entry version 38. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=Tter_1187 {ECO:0000313|EMBL:ACZ42095.1}; OS Thermobaculum terrenum (strain ATCC BAA-798 / YNP1). OC Bacteria; Thermobaculum. OX NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ42095.1, ECO:0000313|Proteomes:UP000000323}; RN [1] {ECO:0000313|Proteomes:UP000000323} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ACZ42095.1; -; Genomic_DNA. DR RefSeq; WP_012875130.1; NC_013525.1. DR RefSeq; YP_003322917.1; NC_013525.1. DR ProteinModelPortal; D1CBD0; -. DR EnsemblBacteria; ACZ42095; ACZ42095; Tter_1187. DR KEGG; ttr:Tter_1187; -. DR PATRIC; 32502570; VBITheTer68767_1266. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; TTER525904:GHMJ-1227-MONOMER; -. DR Proteomes; UP000000323; Chromosome 1. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000323}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ACZ42095.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000000323}; KW Transferase {ECO:0000313|EMBL:ACZ42095.1}. SQ SEQUENCE 629 AA; 68098 MW; 46C6589A781CAAA6 CRC64; MKDPFVERLE KGPILSDGAI GTQLYERGVP YGKSFDELNI VDPSLVSGVH IDYLRAGAEI ITTNTFGANR IRLKEFGLEK KVRDINLRGV KIAREAREIV GVPAFIAGSV GPIGRPATEY NSLTDRVIGD TFREQIEALL EGGADVIMFE TFSELEELLI AIEVAKEVCE LPIIAQMSFG EDELTHGGDT PEDFVRALKD SDVDVIGVNC SVGPQGTLDV VMRLIAAGAH RVSAQPNAGL PSRRGQHFVY ISTPEYFAEY AKKFVSAGAV IVGGCCGTTP AHISAMAAAI KDGNRATTVT VNIEQKSPHI TAIPSGEPEP TKLAQAIKRG EFIVSVEVDP PKGLSARKTL EGAKMLAEKG VKWINIGDSP MARVRMSCIA LAKLIQETTP IEAIIHFTTR DRNVMAIQSD LIGAHAMGIR NVIALTGDPP SLGDYPDATG VWDIDSVGLI KALSRMNEGF DLAGKQIGAK AGFCIAAAVD PTAKDIEFQI DRMWQKIEAG AHLIMSQPLY DVEDLQKFLD RVGNIPVPFI LGVLPLQSYK HAEFMHNEVP GIYVPEHILD AMRRAGSNGL QEGVRLAQEL VHQAQHLVQG IYLMPSFGRY DVCAQVFEAL DIDKRPTASN SSEAQAANK // ID D1CH13_THET1 Unreviewed; 319 AA. AC D1CH13; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 27-MAY-2015, entry version 30. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACZ43034.1}; GN OrderedLocusNames=Tter_2133 {ECO:0000313|EMBL:ACZ43034.1}; OS Thermobaculum terrenum (strain ATCC BAA-798 / YNP1). OC Bacteria; Thermobaculum. OX NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ43034.1, ECO:0000313|Proteomes:UP000000323}; RN [1] {ECO:0000313|Proteomes:UP000000323} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001826; ACZ43034.1; -; Genomic_DNA. DR RefSeq; WP_012876065.1; NC_013526.1. DR RefSeq; YP_003323856.1; NC_013526.1. DR EnsemblBacteria; ACZ43034; ACZ43034; Tter_2133. DR KEGG; ttr:Tter_2133; -. DR PATRIC; 32504639; VBITheTer68767_2279. DR HOGENOM; HOG000231636; -. DR OMA; VLTCTFN; -. DR OrthoDB; EOG6NSGDJ; -. DR BioCyc; TTER525904:GHMJ-2194-MONOMER; -. DR Proteomes; UP000000323; Chromosome 2. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000323}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ACZ43034.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000323}; KW Transferase {ECO:0000313|EMBL:ACZ43034.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 221 221 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 297 297 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 298 298 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 319 AA; 34700 MW; 089675B2BE60437C CRC64; MARNPLEIIR HQGYILGDGG YLIELERRGY VQSGSDREKV GTGKGSGQYT PEVAIEHPDA LRELHTEFLM AGSQVLQALT FFATREKLSR AGYGPQTEAI NIAAVRIARE VAGERALVAA SVARTQLFER EGPAAREHAR DLIAEQIRIL TSAGVDFLIL ETFFHLQEML IALECARDCG LPVMATMSFR PKTTESSDGY TPAECARAMV DAGADIVGAN CEQEPSRMLP IVLQMRAAVD VPIAAQPAAF RTSDDTPCFT RMPQFPDDLE TIQVSRREFA DFATQAISQG VQYIGGCCGA NAAYIRAMAK ALSRAPELA // ID D1CVC6_9RHIZ Unreviewed; 297 AA. AC D1CVC6; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 29-OCT-2014, entry version 20. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEZ32219.1}; DE Flags: Fragment; GN ORFNames=BAKG_01479 {ECO:0000313|EMBL:EEZ32219.1}; OS Brucella sp. 83/13. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520449 {ECO:0000313|EMBL:EEZ32219.1}; RN [1] {ECO:0000313|EMBL:EEZ32219.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=83/13 {ECO:0000313|EMBL:EEZ32219.1}; 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 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; DS999649; EEZ32219.1; -; Genomic_DNA. DR EnsemblBacteria; EEZ32219; EEZ32219; BAKG_01479. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; FT NON_TER 297 297 {ECO:0000313|EMBL:EEZ32219.1}. SQ SEQUENCE 297 AA; 32066 MW; 9436678F33AFB362 CRC64; MASSLDDLFG ATAAKPDGSE VLAALTQAAR ERILILDGAM GTQIQGLGFH EEHFRGDRFA TCDCQLQGNN DFLTLTQPKA IEEIHYAYAM AGADILETNT FSSTSIAQAD YGMEAMVYDL NRDGARLARR AALRAEQKDG RRRFVAGALG PTNRTASLSP DVNNPGFRAV TFDDLRIAYS EQIRGLIDGG SDIILIETIF DTLNAKAAVF ATEEVFAEKG VRLPVMISGT ITDLSGRTLS GQTPTAFWYS LRHARPFTIG LNCALGANAM RAHLDELSGI ADTFICAYPN AGLPNEF // ID D1CVC7_9RHIZ Unreviewed; 955 AA. AC D1CVC7; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 01-APR-2015, entry version 31. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEZ32220.1}; GN ORFNames=BAKG_01480 {ECO:0000313|EMBL:EEZ32220.1}; OS Brucella sp. 83/13. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520449 {ECO:0000313|EMBL:EEZ32220.1}; RN [1] {ECO:0000313|EMBL:EEZ32220.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=83/13 {ECO:0000313|EMBL:EEZ32220.1}; 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 sp. 83/13."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; DS999649; EEZ32220.1; -; Genomic_DNA. DR EnsemblBacteria; EEZ32220; EEZ32220; BAKG_01480. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 20 20 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 21 21 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 477 477 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 955 AA; 105517 MW; B5959FE9DA02C236 CRC64; MAAQIEGFAR DGLVNVVGGC CGSTPDHIRA IAQAVAKYEP RKPAKVPPLM RLSGLEPFTL TKDIPFVNIG ERTNVTGSAR FRKLVKAGDF AAALDVARDQ VANGAQIIDI NMDEGLIDSE KAMVEFLNLI AAEPDIARVP IMLDSSKWEV IEAGLKCVQG KAVVNSISLK EGEEAFLHHA RLVRAYGAAV VIMAFDETGQ ADTQARKIEI CTRAYKILTE QVGFPPEDII FDPNIFAVAT GIEEHNNYGV DFIEATREIV RTLPHVHISG GVSNLSFSFR GNEPVREAMH AVFLYHAIQA GMDMGIVNAG QLAVYDTIDA ELREACEDVV LNRPTKTGES ATERLLEIAE RFRDSGSREA RTQDLSWREW PVEKRLEHAL VNGITEYIEA DTEEARLAAE RPLHVIEGPL MAGMNVVGDL FGSGKMFLPQ VVKSARVMKQ AVAVLLPFME EEKRLNGGEG CQSAGKVLMA TVKGDVHDIG KNIVGVVLAC NNYEIIDLGV MVPSQKILQV ARDEKVDIIG LSGLITPSLD EMAHVAAEME REGFDIPLLI GGATTSRVHT AVKIHPRYER GQAVYVVDAS RAVGVVSNLL SPEGKQAYID GLRNEYAKVA AAHARNEAEK QRLPIARARA NPHQLDWENY EPVKPAFTGT KVFETYDLAE IARYIDWTPF FQTWELRGRY PAILEDEKQG EAARQLWADA QAMLQKIIDE KWFTPRAVVG FWPANAVGDD IRLFTDKSRK EELATLFTLR QQLTKRDGRP NVAMADFVAP VESGKQDYVG GFVVTAGIGE IAIAERFERA NDDYSAILVK ALADRFAEAF AELMHERVRK EFWAYAPDEA FTPEELISEP YKGIRPAPGY PAQPDHTEKT TLFRLLDATA NTGVELTESY AMWPGSSVSG LYIGHPESYY FGVAKVERDQ VEDYARRKGM DVEAVERWLT PILNYVPGAS KDEAA // ID D1F6F3_BRUML Unreviewed; 1261 AA. AC D1F6F3; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 27-MAY-2015, entry version 36. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEZ11035.1}; GN ORFNames=BAOG_02924 {ECO:0000313|EMBL:EEZ11035.1}; OS Brucella melitensis bv. 3 str. Ether. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520466 {ECO:0000313|EMBL:EEZ11035.1, ECO:0000313|Proteomes:UP000005102}; RN [1] {ECO:0000313|EMBL:EEZ11035.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Ether {ECO:0000313|EMBL:EEZ11035.1}; 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. 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; EQ999591; EEZ11035.1; -; Genomic_DNA. DR RefSeq; WP_004684692.1; NZ_EQ999591.1. DR EnsemblBacteria; AIJ85097; AIJ85097; DK62_1225. DR EnsemblBacteria; EEZ11035; EEZ11035; BAOG_02924. DR PATRIC; 24238189; VBIBruMel115656_1638. DR Proteomes; UP000005102; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005102}. SQ SEQUENCE 1261 AA; 138682 MW; B3587ED5F18F1BE6 CRC64; MASSLDDLFG ATAAKPDGSE VLAALTQAAR ERILILDGAM GTQIQGLGFH EEHFRGDRFA TCDCQLQGNN DLLTLTQPKA IEEIHYAYAM AGADILETNT FSSTSIAQAD YGMEAMVYDL NRDGARLARR AALRAEQKDG RRRFVAGALG PTNRTASLSP DVNNPGFRAV TFDDLRIAYS EQIRGLIDGG SDIILIETIF DTLNAKAAVF ATEEVFAEKG VRLPVMISGT ITDLSGRTLS GQTPTAFWYS LRHARPFTIG LNCALGANAM RAHLDELSGI ADTFICAYPN AGLPNEFGQY DETPEAMAAQ IEGFARDGLV NVVGGCCGST PDHIRAIAQA VAKYEPRKPA KVPPLMRLSG LEPFTLTKDI PFVNIGERTN VTGSARFRKL VKAGDFAAAL DVARDQVANG AQIIDINMDE GLIDSEKAMV EFLNLIAAEP DIARVPIMLD SSKWEVIEAG LKCVQGKAVV NSISLKEGEE AFLHHARLVR AYGAAVVIMA FDETGQADTQ ARKIEICTRA YKILTEQVGF PPEDIIFDPN IFAVATGIEE HNNYGVDFIE ATREIVRTLP HVHISGGVSN LSFSFRGNEP VREAMHAVFL YHAIQAGMDM GIVNAGQLAV YDTIDAELRE ACEDVVLNRP TKTGESATER LLEIAERFRD SGSREARTQD LSWREWPVEK RLEHALVNGI TEYIEADTEE ARLAAERPLH VIEGPLMAGM NVVGDLFGSG KMFLPQVVKS ARVMKQAVAV LLPFMEEEKR LNGGEGRQSA GKVLMATVKG DVHDIGKNIV GVVLACNNYE IIDLGVMVPS QKILQVARDE KVDIIGLSGL ITPSLDEMAH VAAEMEREGF DIPLLIGGAT TSRVHTAVKI HSRYERGQAV YVVDASRAVG VVSNLLSPEG KQAYIDGLRN EYAKVAAAHA RNEAEKQRLP IARARANPHQ LDWENYEPVK PTFTGTKVFE TYDLAEIARY IDWTPFFQTW ELRGRYPAIL EDEKQGEAAR QLWADAQAML RKIIDEKWFT PRAVVGFWPA NAVGDDIRLF TDESRKEELA TLFTLRQQLT KRDGRPNVAM ADFVAPVESG KQDYVGGFVV TAGIGEIAIA ERFERANDDY SAILVKALAD RFAEAFAELM HERVRKEFWA YAPDEAFTPE ELISEPYKGI RPAPGYPAQP DHTEKTTLFR LLDATANTGV ELTESYAMWP GSSVSGLYIG HPESYYFGVA KVERDQVEDY ARRKDMDVEA VERWLTPILN YVPGASKDEA A // ID D1JSZ5_9BACE Unreviewed; 916 AA. AC D1JSZ5; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 01-APR-2015, entry version 31. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEZ25188.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEZ25188.1}; GN Name=metH {ECO:0000313|EMBL:EEZ25188.1}; GN ORFNames=HMPREF0101_03096 {ECO:0000313|EMBL:EEZ25188.1}; OS Bacteroides sp. 2_1_16. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=469587 {ECO:0000313|EMBL:EEZ25188.1}; RN [1] {ECO:0000313|EMBL:EEZ25188.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=2_1_16 {ECO:0000313|EMBL:EEZ25188.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG705211; EEZ25188.1; -; Genomic_DNA. DR EnsemblBacteria; EEZ25188; EEZ25188; HMPREF0101_03096. DR PATRIC; 35630763; VBIBacSp133054_3062. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEZ25188.1}; KW Transferase {ECO:0000313|EMBL:EEZ25188.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 916 AA; 100392 MW; 97E88A639A98A3DE CRC64; MKKTIQQLVL ERILILDGAM GTMIQQYNLR EEDFRNERFA HIPGQLKGNN DLLCLTRPDV IRDIHRKYLE AGADIIETNT FSSTTISMAD YHVQEYVREM NQAAVKLARE VADEYTALNP DKPRFVAGSV GPTNKTCSMS PDVNNPAYRA VTYDEMADAY QQQMEAMLES GVDALLIETI FDTLNAKAAI LAAERAMKAT GVKVPVMLSV TVSDTGGRTL SGQTLEAFLA SVQHADIFSV GLNCSFGARQ LKPFLEQLAA RAPYYISAYP NAGLPNSLGK YDQTPADMAH EVKEYVHEGL INIIGGCCGT TDAYIAEYPA LIAGAKPHIP VCKPDCMWLS GLELLEVKPE INFVNVGERC NVAGSRKFLR LINEKKYDEA LSIARKQVED GALIIDVNMD DGLLDAKEEM TTFLNLVASE PEIARVPVMI DSSKWEVIEA GLKCLQGKSI VNSISLKEGE EKFLEHARTV RQYGAAVVVM AFDEKGQADT ATRKIEVCER AYHLLVDKIG FNPHDIIFDP NVLAVATGIE EHNNYAVDFI EATAWIKKNL PGAHISGGVS NLSFSFRGNN YIREAMHAVF LYHAIQKGMD MGIVNPGTSV LYTDIPADVL ERIEDVVLNR RSDAAERLIE LADRLKEASA GNTSAGQPVK HDAWRDGTVE ERLQYALVKG IGDFLEEDLA EALPKYDKAV DVIERPLMNG MNHVGELFGA GKMFLPQVVK TARTMKKAVA ILQPIIESEK VEGTASAGKV LLATVKGDVH DIGKNIVSVV MACNGYDIID LGVMVPAESI VQKAIEEKVD MIGLSGLITP SLEEMVHVAM ELEKAGLDIP LLIGGATTSK LHTALKIAPV YHAPVVHLKD ASQNAGVAAR LMSPKSKEEL AKELSGEYEA LRDKSGMMKR ETVSLKEAQE NRLKLF // ID D1JU12_9BACE Unreviewed; 318 AA. AC D1JU12; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase domain family protein {ECO:0000313|EMBL:EEZ24487.1}; GN ORFNames=HMPREF0101_03463 {ECO:0000313|EMBL:EEZ24487.1}; OS Bacteroides sp. 2_1_16. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=469587 {ECO:0000313|EMBL:EEZ24487.1}; RN [1] {ECO:0000313|EMBL:EEZ24487.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=2_1_16 {ECO:0000313|EMBL:EEZ24487.1}; 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; GG705212; EEZ24487.1; -; Genomic_DNA. DR RefSeq; WP_005802500.1; NZ_GG705212.1. DR EnsemblBacteria; EEZ24487; EEZ24487; HMPREF0101_03463. DR PATRIC; 35631488; VBIBacSp133054_3421. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEZ24487.1}; KW Transferase {ECO:0000313|EMBL:EEZ24487.1}. SQ SEQUENCE 318 AA; 36046 MW; E9087F2732D7AAE9 CRC64; MEQLSFIESF RTSPFILTEG AIVERLRHEF HISPDKHIAH AALIYDDSHR EILASIYRQY LQIATEFRLP LMLMTPTRRA NIEQIATSDY RHKNVLADTM AFLSRFRDEA STPVYIGGLA GCRGNAYDGR YYLSVEEAME FHFPTVRTLA QSGADYLFAG IMPQLTEAIG MANAMAATGL PYIISFMICR DGRLIDGTFI HDAIDAIEKE TSTRPLCYMA NCVHPDVLHQ ALLHPRNDTP LVRQRFQGIQ ANAANLSPEE LDGCDHLISS SPEELADRLM TLLWDFPLKI CGGCCGTNQQ HMHRFAEMLA YRRDNKAW // ID D1JYT7_9BACE Unreviewed; 917 AA. AC D1JYT7; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 27-MAY-2015, entry version 30. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEZ23146.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEZ23146.1}; GN Name=metH {ECO:0000313|EMBL:EEZ23146.1}; GN ORFNames=HMPREF0105_0529 {ECO:0000313|EMBL:EEZ23146.1}; OS Bacteroides sp. 3_1_33FAA. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=457391 {ECO:0000313|EMBL:EEZ23146.1}; RN [1] {ECO:0000313|EMBL:EEZ23146.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_33FAA {ECO:0000313|EMBL:EEZ23146.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG705227; EEZ23146.1; -; Genomic_DNA. DR RefSeq; WP_007837694.1; NZ_GG705227.1. DR EnsemblBacteria; EEZ23146; EEZ23146; HMPREF0105_0529. DR PATRIC; 35652414; VBIBacSp128056_0542. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEZ23146.1}; KW Transferase {ECO:0000313|EMBL:EEZ23146.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 243 243 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 917 AA; 100924 MW; 505D6BDEA9B137EE CRC64; MATLKQIINE RVLILDGAMG TMIQRYNLSE QDFRGERFAG IPGQMKGNND LLCLTRPDVI KDIHRKYLEA GADIIETNTF NAQRISMADY HMQDLCREIN LAAARLAREL ADEYTAKTPR KPRFVAGSVG PTNKTCSMSP DVNNPALRAL TYDELATAYQ EQMEALLEGG VDALLIETIF DSLNAKAAIY AAETAMKKTG REVPLMLSVT VSDIAGRTLS GQTLDAFLAS VQYAPIFSIG LNCSFGAKQL KPFLEGLAAR APYYISAYPN AGLPNSLGQY DQTPEEMASE VKEYIDEGLV NIIGGCCGTT EEYIAKYQEL IVSGSAWVPP HIPATTPERL WLSGLELLEQ TPEMNFINVG ERCNVAGSRK FLRLINEKKY EEALSIARKQ VEDGALVIDV NMDDGLLDAR EEMTTFLNLV MSEPDIARVP IMIDSSKWEV IEAGLKCLQG KSIVNSISLK EGEEKFIEHA RLIKKLGAAT VVMAFDEKGQ ADTFERKIEV CARAYKILTE QVGFNPHDII FDPNVLAVAT GIEEHNNYAV DFINATGWIK KNLPGAHISG GVSNLSFSFR GNNYIREAMH AVFLYHAIRQ GMDMGIVNPA TSVLYTDIPA DVLERIEDVV LNRRPDAAER LIETAEALKN TATGTEAVKQ DVWREEPMVE KRLQYALIKG VGDHLEEDLA EAVKLYPKAV DIIEGPLMEG MNRVGELFGA GKMFLPQVVK TARTMKKAVA ILQPLIEADK QEGARSAGKV LMATVKGDVH DIGKNIVSVV MACNNYEIID LGVMVPAEMI VRKAIEEKVD IIGLSGLITP SLEEMAHVAV ELKRAGLDIP IMIGGATTSK LHTALKIAPV YGGPVIHMKD ASQNALVAAR LLNPESSSEF VERLNKEYEE LRLKNSTKQV KTVSLEEAQK NKLNLWS // ID D1P758_9ENTR Unreviewed; 1227 AA. AC D1P758; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 27-MAY-2015, entry version 30. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFB70905.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFB70905.1}; GN Name=metH {ECO:0000313|EMBL:EFB70905.1}; GN ORFNames=PROVRUST_08078 {ECO:0000313|EMBL:EFB70905.1}; OS Providencia rustigianii DSM 4541. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Providencia. OX NCBI_TaxID=500637 {ECO:0000313|EMBL:EFB70905.1}; RN [1] {ECO:0000313|EMBL:EFB70905.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 4541 {ECO:0000313|EMBL:EFB70905.1}; 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., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFB70905.1}. 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; ABXV02000046; EFB70905.1; -; Genomic_DNA. DR RefSeq; WP_006816073.1; NZ_GG703821.1. DR EnsemblBacteria; EFB70905; EFB70905; PROVRUST_08078. DR PATRIC; 36130776; VBIProRus116159_6930. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFB70905.1}; KW Transferase {ECO:0000313|EMBL:EFB70905.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136954 MW; D758E216563A6B57 CRC64; MSSKKNQLEQ QLKNRILVLD GAMGTMIQRH KLTEEQFRGE RFADWPSDVK GNNDLLVLTQ PDIIRDIHHQ YFAAGADIIE TNTFNSTTIA MADYKMESLS AEINEVAARI ARECADEWSR KTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNVTFDRLV EAYRESTRAL IKGGADLIMI ETIFDTLNAK AAIFAVETEF EALGTHLPVM ISGTITDASG RTLSGQTTEA FYNSLRHSQP LSFGLNCALG PDELRQYIAE LSRISDCYVS AHPNAGLPNA FGEYDLDAQN MAQQIREWAE AGFLNIVGGC CGTTPLHIQK MAEAVEGIKP RPLPELPVEC RLSGLEPLNI GAQSLFVNVG ERTNVTGSAK FKRLIKEENY QEALDIARQQ VESGAQIIDI NMDEGMLDSH AAMVRFLNLI AGEPDIARVP IMIDSSKWSV IEDGLKCIQG KGIVNSISMK EGVDTFIEHA KLVRKYGAAM VVMAFDEVGQ ADTRERKIEI CRRAYQILTE TVGFPPEDII FDPNIFAVAT GIEEHNNYAV DFIEVCKDIK QQLPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELKDAVEDVI LNRREDGTER LLDLAEKYRG TGGQEQQVQQ AEWRSWEVEK RLEYSLVKGI TEFIIQDTEE TRQRAASPIE VIEGPLMNGM NVVGDLFSDG KMFLPQVVKS ARVMKQAVAY LEPYIQELKQ SGSSAGKVLL ATVKGDVHDI GKNIVGVVLQ CNNYEIIDLG VMVPCETILK TARERNVDII GLSGLITPSL DEMVHVAKEM ERQGFTLPLL IGGATTSKAH TAVKIEQNYS GPTTYVQNAS RTVGVVAALL SDTQKEEFVA RTRREYETVR QQYARKKPRT PPVELEVARA NGVKIDWENY QPPTPKFLGV QEVTASIKTL REYIDWTPFF MTWSLAGKYP RILQDEVVGE EARRVLADAN AMLDELDRQK LLTPRGIFGI FPANRVQDDI EIYASSARDS VKAVSLNLRQ QTLKTDFPNY CLSDFVAPKE SGKADYIGAF AVTGGLEEDA LAEQYENAHD DYNKIMLKAL ADRLAEAFAE YLHQQVRIHY WGYAEEESLS NEELIRENYQ GIRPAPGYAA CPEHTEKEKI WQLLNVEENI GMQLTSSYAM WPGASVSGWY FSHPDSKYFA VAQVQKDQIE DYAKRKGMSV TELERWLAPN LGYDPED // ID D1PGK1_9BACT Unreviewed; 927 AA. AC D1PGK1; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFB34198.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFB34198.1}; GN Name=metH {ECO:0000313|EMBL:EFB34198.1}; GN ORFNames=PREVCOP_06366 {ECO:0000313|EMBL:EFB34198.1}; OS Prevotella copri DSM 18205. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=537011 {ECO:0000313|EMBL:EFB34198.1}; RN [1] {ECO:0000313|EMBL:EFB34198.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 18205 {ECO:0000313|EMBL:EFB34198.1}; 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., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFB34198.1}. 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; ACBX02000044; EFB34198.1; -; Genomic_DNA. DR RefSeq; WP_006849039.1; NZ_GG703861.1. DR EnsemblBacteria; EFB34198; EFB34198; PREVCOP_06366. DR OrthoDB; EOG6091CH; -. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFB34198.1}; KW Transferase {ECO:0000313|EMBL:EFB34198.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 241 241 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 771 771 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 927 AA; 102114 MW; 75B8A05A941319A0 CRC64; MKNLREIVKE KILILDGAMG TEIQKYNLTE EDFRGERFRD LPGMMKGNND MLNITRPDVI SDIYRRYLEA GADIITANTF SCQRISQADY HLENCAREMA FEGARLARIE CDKFSTPDKP RFVAGDVGPT NKTCSMSPDV SNPAAREITY DELFTDVCEQ VDGLIEGGAD VILIETIFDT LNCKAMIDAA LTMMKKHGVE LPVMISLTVS DLAGRTLSGQ TVDAFLASLS PYPIFSVGMN CAFGAPQMKP FIEHMAQVAP YYISAHPNAG LPNEMGEYDE TAESMAPQIA EFIDEGIVNI IGGCCGTSPE FIAHYARIAE GKKPHQVVEK PKYMWLSGLD LLQVDDSVHL PVDAIRFVNV GERCNVAGSR KFLRLINEKN YEEAIGIARK QVADGAAVVD VNMDDGLLDA KAEMVNFLNM IAAEPDIAKV PVMIDSSKWD VIVVGLKCCQ GKCIVNSISL KEGEEVFLSH ARDVLRYGAA VVVMCFDEVG QATTFERRIE IAERAYHLLV DKLGMNPLDI IFDPNVLAIA TGMEEHDNYA VEFIRATEWI HQNLPGAHVS GGVSNLSFSF RGNTYIREAI HCVFLHHAQQ VGMDFGIVNA KARMDYNKIP EEQLHLIEDV VLNRRKGAAD ELIELAAEIK AQADAAKAAA KAGGVAPKKP AAPEWRKESV EERLKYALRK GITDFLQQDI DEALAKYPHA VNVIEGPLMD GMNLVGELFG KGEMFLPQVV KTARTMKSAV SILQPHIEAE KQGGATTAGK ILMATVKGDV HDIGKNIVCV VMSCNNYEII DLGVMVPAEQ IVQKAIDEKV DAIGLSGLIT PSLEEMVHVA REMQKAGLRI PIMVGGATTS ELHVALKIAP EYDGPVIWVK DASLNAGICA RFLNEAECPK FESELKERYE KLRQNYHEEQ AKIASLSEAR KNKLELF // ID D1PMD8_9FIRM Unreviewed; 780 AA. AC D1PMD8; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFB75723.1}; GN ORFNames=SUBVAR_05498 {ECO:0000313|EMBL:EFB75723.1}; OS Subdoligranulum variabile DSM 15176. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Subdoligranulum. OX NCBI_TaxID=411471 {ECO:0000313|EMBL:EFB75723.1}; RN [1] {ECO:0000313|EMBL:EFB75723.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 15176 {ECO:0000313|EMBL:EFB75723.1}; 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., 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFB75723.1}. 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; ACBY02000023; EFB75723.1; -; Genomic_DNA. DR RefSeq; WP_007046883.1; NZ_GG704769.1. DR EnsemblBacteria; EFB75723; EFB75723; SUBVAR_05498. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFB75723.1}; KW Transferase {ECO:0000313|EMBL:EFB75723.1}. SQ SEQUENCE 780 AA; 81711 MW; 2C9CD3DDBAFE3292 CRC64; MGTQLQKHGL KPGQKPELAA LEMPETVTAI HAAYAAAGAD LLLANTFGAN ARKLAETGYS VAEVVKASLH CARTAAEPTG ALVGLDIGPL GELLAPAGTL PFEDAYTAFA EIVQAGVEAG ADFVFLETMT DLYELKAAIL AAKEHSRLPV FVSMSFESRG RTFTGCTVES YGATAAGLGA DAIGINCSLG PAEILPFAQR LCRTVPAGTP VFVKPNAGLP NPDGSYNLDA EEFAREMEAY AAIGVSMVGG CCGTTPEYIA RLRDVFSSLT PAQKIPLRRS CLCTPVRFVE VDGITVVGER INPTGKKRLQ QALREGDSAY PCTQAVAQAE AGAEVLDVNA GLPGIDEAAT LERLVRDLQA VTDLPLQLDS SNPEALARAL RVYNGKPIVN SVNGEQKTLE AILPLCKKYG AAVVGLTMDE QGIPSSAEGR FAIAQKIVEA AAAVGIPRED IYIDCLTLTA SAQQEGAAQT LAALTRCKEE LGVRTILGVS NISFGLPCRG YLNTTFLTMA MAAGLDLAIM NPNTPEMMAA VRAYRVLTAQ DKQSAAYVAA YADVQIQTQQ VSKNVEAAPA QSSEDPLFDA VRRGLKAEAH EAAEAALAVK APLEVVNASL IPALDVVGDG FEKGTIFLPQ LLQAATAAQA AFEAVKAKIA AQGQPQTTGK GKIVVATVKG DVHDIGKNIV RVILENYGYD VLDLGRDVPP ERVVEAVRTT GAKLVGLSAL MTTTVPNMKA TIDALHEANL DCQVWVGGAV LTPGYAKEIG ADFYCKDAKA SADLAKQILG // ID D1QMD2_9BACT Unreviewed; 60 AA. AC D1QMD2; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFB33402.1}; GN ORFNames=HMPREF0971_00165 {ECO:0000313|EMBL:EFB33402.1}; OS Prevotella oris F0302. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=649760 {ECO:0000313|EMBL:EFB33402.1}; RN [1] {ECO:0000313|EMBL:EFB33402.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0302 {ECO:0000313|EMBL:EFB33402.1}; 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., 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. {ECO:0000313|EMBL:EFB33402.1}. 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; ACUZ02000003; EFB33402.1; -; Genomic_DNA. DR RefSeq; WP_004370996.1; NZ_GG703883.1. DR EnsemblBacteria; EFB33402; EFB33402; HMPREF0971_00165. DR OrthoDB; EOG6091CH; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; SQ SEQUENCE 60 AA; 6651 MW; 6B5BF348003786E7 CRC64; MELYDETAES MLSQLAEFMT EGLVNIVGGC CGTTDEFVRC CAEQVKGKRP HQPMKRPNGL // ID D1Y627_9BACT Unreviewed; 798 AA. AC D1Y627; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFB90221.1}; GN ORFNames=HMPREF7215_2692 {ECO:0000313|EMBL:EFB90221.1}; OS Pyramidobacter piscolens W5455. OC Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae; OC Pyramidobacter. OX NCBI_TaxID=352165 {ECO:0000313|EMBL:EFB90221.1}; RN [1] {ECO:0000313|EMBL:EFB90221.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=W5455 {ECO:0000313|EMBL:EFB90221.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFB90221.1}. 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; ADFP01000090; EFB90221.1; -; Genomic_DNA. DR RefSeq; WP_009165308.1; NZ_ADFP01000090.1. DR EnsemblBacteria; EFB90221; EFB90221; HMPREF7215_2692. DR PATRIC; 36441291; VBIPyrPis26956_1665. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFB90221.1}; KW Transferase {ECO:0000313|EMBL:EFB90221.1}. SQ SEQUENCE 798 AA; 84795 MW; 5EFFA1436FDC37D0 CRC64; MMKEFDRVVM FDGAMGTMLQ KKGLKLREIP ESLNVSRPDL IESIHREYFA AGCDFVQTNT FGANPYKLEG TAYETEQVIG AAVKIARRAA DAFSGKGILL DVGPSGRAMA PVGDADFDEI YGSVARQVRA GAELCDGILL ETFTDLLEAK ASALAALENS DKPVFLTMSF QEDGRTFFGT PVEAMIMTFE GLGLSGLGVN CSLGPAQLAP IVKKLTAHSR VPVIVQPNAG LPVVRDGVSG WDVSPGEFAN WLGQFVDWGT AFVGGCCGTT PEFLSAANDM IGNRRLRPRK VAPLRGVCSA TRVEPFDRTV IIGERLNPTG KKRLKQALYE HDFDYVVLEA QKQKEQGAGV LDVNVGLPDV DEPAMLREVV AELQGAVDLP LQLDSANAAA LEAGARRYAG KPLLNSVSGK ESSLASVLPV AKKYGACVLG LCLDDGGIPQ TAEARFAVAQ KILDRAAALG IPKDDVFIDC LTLTASAQQD LALETIKAVR MVSERLAVKT TLGVSNVSFG LPRRPLINRT MLAAALANGL SAAIVNPGEK SVQETLAAWR VLSAQDRDAK EYIDFCAANP EETAFAPRAV AAVSERGKFS GGLGEAVARG LKDEARACAA ELVKKQPPLE IVEKTLIPAL DAVGRDYEAQ KIYLPQLIKS ADAAKAALEV VKGVLAGDQG GAPRSGPKVI VATVYGDVHD IGKNIVKVIM ENYNFDVIDL GKDVSSDAIV AAVKKTGAAV VGLSALMTTT VASMKETIAA LRRECPEVRV IVGGAVLTPD LARHVGADRY ARDAMDTVRA VEEFLSRE // ID D1YM31_9FIRM Unreviewed; 811 AA. AC D1YM31; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFB86949.1}; GN ORFNames=HMPREF1035_0495 {ECO:0000313|EMBL:EFB86949.1}; OS Veillonella parvula ATCC 17745. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Veillonella. OX NCBI_TaxID=686660 {ECO:0000313|EMBL:EFB86949.1}; RN [1] {ECO:0000313|EMBL:EFB86949.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 17745 {ECO:0000313|EMBL:EFB86949.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFB86949.1}. 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; ADFU01000001; EFB86949.1; -; Genomic_DNA. DR RefSeq; WP_004692954.1; NZ_ADFU01000001.1. DR EnsemblBacteria; EFB86949; EFB86949; HMPREF1035_0495. DR PATRIC; 36455283; VBIVeiPar156829_0058. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFB86949.1}; KW Transferase {ECO:0000313|EMBL:EFB86949.1}. SQ SEQUENCE 811 AA; 87156 MW; 123D4CB621DF1E54 CRC64; MYIFDGAMGT MLQAAGLEEG YCPELFNVER PKVVKNIHAQ YLQHGSDVIT TNTFGACGLK LEDYDLQDRV REINIAAVKV AKEAIAEVKP SARVAGSMGP TGRFLQPLGN MSFDDIYDTY REQAEALIEG GVDFIIIETI IDVQEMRAAL LASLDAREAA GKTKEDIQII CQFSFSEDGR TITGTPPAVA TTIVEAIGAD IIGINCSLGP EQITPLIEEI ASVTNLPISC QPNAGMPQLI NKQTVFPLTA EEMGPLMLDI VDAGASYIGG CCGTTPAHIQ SISDAVKAHT PKERAHITPK TIITSRTKLL ELGHHTKPLI IGERINPTGR KVLAQELRDG SFIRVKRDAL DQVEAGTDIL DVNMGVAGMD QTPLMERAIF ELSMLVETPL SIDTLDPAAM EVALKNYPGR ALINSVNGEE ESITHVMPLA KRYGAALLCL PICSGDLPEK AEDRVALAES IINRAYGYGL QPHDLLLDPL VLTLASGEDS ARQTLRTLQL YKEKFGFPTV MGLSNISFGM PQRPYLNGQF LTMALACGLT TPIMNPLNYP AKKAFVSSTT LLGWDPGSAE FIKEYGYEDE TTAPGNFAPK GPDKKSFDSN DPLANIRTCV EQGEKEAIID LVKKALADGI DPLDLTKKGL SEAMNVVGDK FGSGKLFLPQ VMLAAETMQA AFNTIKEIIP ASESLDKGTV VVATVKGDIH DLGKNIVAAL LENNGYKIID LGKDVDPEVI VQAIKDNKAA LVGICSLMTT TMPQIDNTIA AIRAAGLKTK VMVGGAVVSQ DYADQAGADI YAKDGIAAVN HANDFFETLE K // ID D1YN72_9FIRM Unreviewed; 341 AA. AC D1YN72; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 01-OCT-2014, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFB86278.1}; GN ORFNames=HMPREF1035_0123 {ECO:0000313|EMBL:EFB86278.1}; OS Veillonella parvula ATCC 17745. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Veillonella. OX NCBI_TaxID=686660 {ECO:0000313|EMBL:EFB86278.1}; RN [1] {ECO:0000313|EMBL:EFB86278.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 17745 {ECO:0000313|EMBL:EFB86278.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFB86278.1}. 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; ADFU01000011; EFB86278.1; -; Genomic_DNA. DR EnsemblBacteria; EFB86278; EFB86278; HMPREF1035_0123. DR PATRIC; 36456085; VBIVeiPar156829_0437. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFB86278.1}; KW Transferase {ECO:0000313|EMBL:EFB86278.1}. SQ SEQUENCE 341 AA; 37045 MW; 47E07936E3E92509 CRC64; MGGMMAKRSA FLDIIKEKGA LVLDGALGTE LERYGCDIQH KLWSAKVLMD QPDIIKKIHI SYLAAGADII QSSGYQATVA GFKGLGYGTE EAIELVKLSV RLAVQARNEF LEAKASGALT LDGIKLGEET PEGVRYFSEG ALPKPLVAAS VGPYGAFLAD GSEYRGYPDV QTEYLEIFHI PRLALFCEEH PDILSFETIP SYAEAIAIAR AMSDPFTSKG IPGWIAFSCK DGHHVSSGET IIKCAQMIDK VHPITGIGIN CSKPEYVESL IKDIRTVTDK PIAVYPNLGE SYDSKTKTWY GDAASFVDYV EVWRKAGAEI IGGCCRTTPE IIGDIAKKIH N // ID D1ZZE7_TRICA Unreviewed; 313 AA. AC D1ZZE7; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 07-JAN-2015, entry version 29. DE SubName: Full=Putative uncharacterized protein GLEAN_07465 {ECO:0000313|EMBL:EFA01862.1}; GN Name=GLEAN_07465 {ECO:0000313|EMBL:EFA01862.1}; GN ORFNames=TcasGA2_TC007465 {ECO:0000313|EMBL:EFA01862.1}; OS Tribolium castaneum (Red flour beetle). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Coleoptera; Polyphaga; OC Cucujiformia; Tenebrionidae; Tenebrionidae incertae sedis; Tribolium. OX NCBI_TaxID=7070 {ECO:0000313|Proteomes:UP000007266}; RN [1] {ECO:0000313|EMBL:EFA01862.1, ECO:0000313|Proteomes:UP000007266} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA01862.1, RC ECO:0000313|Proteomes:UP000007266}; RX PubMed=18362917; DOI=10.1038/nature06784; RG Tribolium Genome Sequencing Consortium; RA Richards S., Gibbs R.A., Weinstock G.M., Brown S.J., Denell R., RA Beeman R.W., Gibbs R., Beeman R.W., Brown S.J., Bucher G., RA Friedrich M., Grimmelikhuijzen C.J., Klingler M., Lorenzen M., RA Richards S., Roth S., Schroder R., Tautz D., Zdobnov E.M., Muzny D., RA Gibbs R.A., Weinstock G.M., Attaway T., Bell S., Buhay C.J., RA Chandrabose M.N., Chavez D., Clerk-Blankenburg K.P., Cree A., Dao M., RA Davis C., Chacko J., Dinh H., Dugan-Rocha S., Fowler G., Garner T.T., RA Garnes J., Gnirke A., Hawes A., Hernandez J., Hines S., Holder M., RA Hume J., Jhangiani S.N., Joshi V., Khan Z.M., Jackson L., Kovar C., RA Kowis A., Lee S., Lewis L.R., Margolis J., Morgan M., Nazareth L.V., RA Nguyen N., Okwuonu G., Parker D., Richards S., Ruiz S.J., RA Santibanez J., Savard J., Scherer S.E., Schneider B., Sodergren E., RA Tautz D., Vattahil S., Villasana D., White C.S., Wright R., Park Y., RA Beeman R.W., Lord J., Oppert B., Lorenzen M., Brown S., Wang L., RA Savard J., Tautz D., Richards S., Weinstock G., Gibbs R.A., Liu Y., RA Worley K., Weinstock G., Elsik C.G., Reese J.T., Elhaik E., Landan G., RA Graur D., Arensburger P., Atkinson P., Beeman R.W., Beidler J., RA Brown S.J., Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H., RA Lorenzen M., Maselli V., Osanai M., Park Y., Robertson H.M., Tu Z., RA Wang J.J., Wang S., Richards S., Song H., Zhang L., Sodergren E., RA Werner D., Stanke M., Morgenstern B., Solovyev V., Kosarev P., RA Brown G., Chen H.C., Ermolaeva O., Hlavina W., Kapustin Y., RA Kiryutin B., Kitts P., Maglott D., Pruitt K., Sapojnikov V., RA Souvorov A., Mackey A.J., Waterhouse R.M., Wyder S., Zdobnov E.M., RA Zdobnov E.M., Wyder S., Kriventseva E.V., Kadowaki T., Bork P., RA Aranda M., Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F., RA Bopp D., Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E., RA Ferrier D.E., Friedrich M., Gordon C.M., Jindra M., Klingler M., RA Lan Q., Lattorff H.M., Laudet V., von Levetsow C., Liu Z., Lutz R., RA Lynch J.A., da Fonseca R.N., Posnien N., Reuter R., Roth S., RA Savard J., Schinko J.B., Schmitt C., Schoppmeier M., Schroder R., RA Shippy T.D., Simonnet F., Marques-Souza H., Tautz D., Tomoyasu Y., RA Trauner J., Van der Zee M., Vervoort M., Wittkopp N., Wimmer E.A., RA Yang X., Jones A.K., Sattelle D.B., Ebert P.R., Nelson D., Scott J.G., RA Beeman R.W., Muthukrishnan S., Kramer K.J., Arakane Y., Beeman R.W., RA Zhu Q., Hogenkamp D., Dixit R., Oppert B., Jiang H., Zou Z., RA Marshall J., Elpidina E., Vinokurov K., Oppert C., Zou Z., Evans J., RA Lu Z., Zhao P., Sumathipala N., Altincicek B., Vilcinskas A., RA Williams M., Hultmark D., Hetru C., Jiang H., Grimmelikhuijzen C.J., RA Hauser F., Cazzamali G., Williamson M., Park Y., Li B., Tanaka Y., RA Predel R., Neupert S., Schachtner J., Verleyen P., Raible F., Bork P., RA Friedrich M., Walden K.K., Robertson H.M., Angeli S., Foret S., RA Bucher G., Schuetz S., Maleszka R., Wimmer E.A., Beeman R.W., RA Lorenzen M., Tomoyasu Y., Miller S.C., Grossmann D., Bucher G.; RT "The genome of the model beetle and pest Tribolium castaneum."; RL Nature 452:949-955(2008). RN [2] {ECO:0000313|EMBL:EFA01862.1, ECO:0000313|Proteomes:UP000007266} RP GENOME REANNOTATION. RC STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA01862.1, RC ECO:0000313|Proteomes:UP000007266}; RX PubMed=19820115; DOI=10.1093/nar/gkp807; RA Kim H.S., Murphy T., Xia J., Caragea D., Park Y., Beeman R.W., RA Lorenzen M.D., Butcher S., Manak J.R., Brown S.J.; RT "BeetleBase in 2010: revisions to provide comprehensive genomic RT information for Tribolium castaneum."; RL Nucleic Acids Res. 38:D437-D442(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; CM000279; EFA01862.1; -; Genomic_DNA. DR RefSeq; XP_971795.1; XM_966702.2. DR EnsemblMetazoa; TC007465-RA; TC007465-PA; TC007465. DR GeneID; 660474; -. DR KEGG; tca:660474; -. DR InParanoid; D1ZZE7; -. DR KO; K00547; -. DR OMA; SEWCKDG; -. DR OrthoDB; EOG7GQXW0; -. DR PhylomeDB; D1ZZE7; -. DR Proteomes; UP000007266; Linkage group 4. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007266}; KW Reference proteome {ECO:0000313|Proteomes:UP000007266}. SQ SEQUENCE 313 AA; 34840 MW; 8B32E37F45767346 CRC64; MSDRKKKIVL LDGSFGFQLS KYVSKSLDGD PLWSARSLAS DPEAVIRVHL DYIKAGCDII ETNSYQASVP GFMKYLNLSK EESYNLVKKS VVLAKTAIER AQKEGILQGD AKPLIAGSVG PYGAYLHDGS EYNGYYTDRI SREEFVDYHK SRIDALIEGG VDLLAIETIP SKKEAEIIVQ LIKEYPDIKA WLSFSCQTEG ACTAHGDNFK DAATSCYKLN PDQILAVGVN CIAPHAVEPL LKEITDIPLI VYANSGEKYD PDLGWDNNCE KLEEYVPVWL NLGVKYIGGC CRVCDNYITK IADEVRKWEE NNS // ID D2AD89_SHIF2 Unreviewed; 1227 AA. AC D2AD89; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 27-MAY-2015, entry version 42. DE SubName: Full=B12-dependent homocysteine-N5-methyltetrahydrofolate transmethylase {ECO:0000313|EMBL:ADA76380.1}; GN Name=metH {ECO:0000313|EMBL:ADA76380.1}; GN OrderedLocusNames=SFxv_4455 {ECO:0000313|EMBL:ADA76380.1}; OS Shigella flexneri serotype X (strain 2002017). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=591020 {ECO:0000313|EMBL:ADA76380.1, ECO:0000313|Proteomes:UP000001884}; RN [1] {ECO:0000313|EMBL:ADA76380.1, ECO:0000313|Proteomes:UP000001884} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2002017 {ECO:0000313|EMBL:ADA76380.1, RC ECO:0000313|Proteomes:UP000001884}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001383; ADA76380.1; -; Genomic_DNA. DR RefSeq; WP_000096021.1; NC_017328.1. DR RefSeq; YP_005729673.1; NC_017328.1. DR ProteinModelPortal; D2AD89; -. DR SMR; D2AD89; 651-1227. DR EnsemblBacteria; ADA76380; ADA76380; SFxv_4455. DR KEGG; sfe:SFxv_4455; -. DR PATRIC; 36751064; VBIShiFle60233_4780. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR BioCyc; SFLE591020:GLK5-4360-MONOMER; -. DR Proteomes; UP000001884; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001884}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADA76380.1}; KW Transferase {ECO:0000313|EMBL:ADA76380.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135857 MW; DA24CC6AD801C059 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLA AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKADDTANAQ QAEWRSWDVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RIAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFAIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTCKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDHARRKGMS VSDVERWLAP NLGYDAD // ID D2ATZ7_STRRD Unreviewed; 1154 AA. AC D2ATZ7; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 29-APR-2015, entry version 44. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACZ88652.1}; GN OrderedLocusNames=Sros_5917 {ECO:0000313|EMBL:ACZ88652.1}; 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 {ECO:0000313|EMBL:ACZ88652.1, ECO:0000313|Proteomes:UP000002029}; RN [1] {ECO:0000313|EMBL:ACZ88652.1, ECO:0000313|Proteomes:UP000002029} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100 RC {ECO:0000313|Proteomes:UP000002029}; RX PubMed=21304675; 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 9100)."; RL Stand. Genomic Sci. 2:29-37(2010). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001814; ACZ88652.1; -; Genomic_DNA. DR RefSeq; WP_012892387.1; NC_013595.1. DR RefSeq; YP_003341395.1; NC_013595.1. DR EnsemblBacteria; ACZ88652; ACZ88652; Sros_5917. DR KEGG; sro:Sros_5917; -. DR PATRIC; 32473677; VBIStrRos112010_5824. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; ILESWIT; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SROS479432:GI0V-5947-MONOMER; -. DR Proteomes; UP000002029; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002029}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002029}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 225 225 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 292 292 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 735 735 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1154 AA; 126417 MW; 030F13E49EFA6081 CRC64; MTSRPSFREV LAERVMVADG AMGTMLQAHD VTLDDFEGHE GCNEVLNATR PDIVRAVHDA YFEVGVDCVE TNTFGANLAA LGEYDISERT HELSEAGARV AREAADHWST PDHPRYVLGS IGPGTKLPTL GHKPYGVLRD AYYDNAAGLI AGGADALIIE TCQDLLQVKA AVIGAKRAIT DSGRDVPVIA QVTVETNGAM LLGSEIGAAL TAIEPLGVDV IGLNCATGPA EMSEHLRYLS RHARLQLSCM PNAGLPQLTS DGAYYPLTPD ELADAHENFT RSFGLSLVGG CCGTTPEHLR KVVERVRGNG HSPRRPRPEA GAASLYQHVP FRQDTSYLAI GERTNANGSK AFREAMLAEN WEECVEIARA QARDGAHMLD LCIDYVGRDG VRDMKELAFR FATASTLPIV LDSTEPAVLE AGLEMIGGRA IINSVNYEDG DGPDSRFTRI MKLVRSHGAA VMALTIDEEG QARTAEWKLR IATRLIEDLT ANWGMNVEDI IIDALTFPIA TGQEETRRDG VETIEAIREL KRRYPGVQTV LGLSNISFGL NPAARIVLNS VFLNECVNAG LDSAIVHASK ILPMARIPDE QRQVALDMVY DRRREGYDPL QRFMELFEGV DAASIKADRA AELLGLPLWE RLKRRIIDGE RKGLEADLDE ALAQRPALEI VNDVLLDGMK TVGELFGSGQ MQLPFVLQSA EVMKTSVAYL EPHMDRVEGE NKGRIVLATV KGDVHDIGKN LVDIILSNNG YEVVNLGIKQ PVSAILEAAE EQKADVIGMS GLLVKSTVIM KENLEEMNSR GMSERFPVLL GGAALTRAYV EQDLAELFQG DVRYARDAFE GLRLMDAFMA VKRGEAGASL PPLRERRVKT GATLVRTPEA ELPARSDVAA DNPVPTAPFL GERIIKGIPL ADYAAFLDER ATFMGQWGLK AARGGDGPSY EELVETEGRP RLRMWLERMQ TEGLLEAAVA YGYFPCVSDG DSLIILDDAG NERTRFTFPR QRRDRHLCLS DFFRSKDSGE VDVVALQVAT MGNRVSEAAA ELFAKDAYRD YLELHGLSVQ LTEALAEYWH ARVRSELGIG GDESLEDMLK VNVTGCRYSF GYPACPNLED QVQLMELIDP SRIGVNLSEE FQLHPEQSTS ALVVHHPEAS YFNV // ID D2AXV0_STRRD Unreviewed; 1245 AA. AC D2AXV0; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 27-MAY-2015, entry version 44. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACZ85121.1}; GN OrderedLocusNames=Sros_2137 {ECO:0000313|EMBL:ACZ85121.1}; 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 {ECO:0000313|EMBL:ACZ85121.1, ECO:0000313|Proteomes:UP000002029}; RN [1] {ECO:0000313|EMBL:ACZ85121.1, ECO:0000313|Proteomes:UP000002029} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100 RC {ECO:0000313|Proteomes:UP000002029}; RX PubMed=21304675; 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 9100)."; RL Stand. Genomic Sci. 2:29-37(2010). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001814; ACZ85121.1; -; Genomic_DNA. DR RefSeq; WP_012888866.1; NC_013595.1. DR RefSeq; YP_003337864.1; NC_013595.1. DR EnsemblBacteria; ACZ85121; ACZ85121; Sros_2137. DR KEGG; sro:Sros_2137; -. DR PATRIC; 32466221; VBIStrRos112010_2108. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; QPFFNAW; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SROS479432:GI0V-2155-MONOMER; -. DR Proteomes; UP000002029; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002029}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002029}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 271 271 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 334 334 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 335 335 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 789 789 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1245 AA; 134149 MW; 28D6F82E562BFD5D CRC64; MDTSLNHGDE HGQGAVRHAP GAGDPGAPGA HPAEAAGRTQ ALRELLDQRI VVLDGAWGTM LQGAELTAAD YRGERFKDHP RDVTGDPDLL NLTRPDVVLD VHRQYLAAGA DITTTNTFTA TSIGQADYGL ESLVREMNLR GAQLARQAAD EAGGRFVAGS IGPLNVTLSL SPRVEDPAYR AVSFDEVRAA YAEQIQALAD GGVDLLLIET IFDTLNAKAA IAAARDVAPH LPLWISVTIV DLSGRTLSGQ TVEAFWSSIE HAAPLVVGVN CSLGAEEMRP HVAELSRLAG VYTASHPNAG LPNAFGGYDQ TPDETARLLG EFAGSGMVNV VGGCCGTTPA HIARIAAEVS ALPPRPIPAP PARTRFSGLE PFEIGADTGF VMIGERTNVT GSARFRRLVE GGDHQGAVDV ALEQVRGGAN LLDVNMDADL LDSEQAMTTF LNLIATEPEV ARIPVMIDSS RWSVLEAGLK CVQGRGVVNS ISLKEGEEPF LEQARRIRDY GAGVVVMAFD EQGQADTVER KVAICARAYD LLTQRAGFPA EDIVFDPNVL AVATGIAEHN GYAKAFIDAL PLIKQRCPGA RTSGGISNLS FSFRGNDVVR EAMHSAFLFH AVRAGLDMGI VNAGQLAVYQ DIPADLLELV EDVIFDRRAD ATDRLVAFAE TVSGSGTRRT VDLSWRDAPV EQRLAYALVQ GIVDFIDADT EEARQRAARP LDVIEGPLMD GMKIVGDLFG AGKMFLPQVV KSARVMKRSV AYLEPYMEAE KEQARLEGRV DAGRGQGKVV LATVKGDVHD IGKNIVGVVL GCNNYQVIDL GVMVPAAVVL DTAIAEGADA VGLSGLITPS LDEMVTVAAE MQRRGLKLPL LIGGATTSRQ HTAVRIAPAY DGTTVHVLDA SRVVGVVSDL LHADRAEKLA VSNRAEQERL REQHATRERR PLLTLAQARA NREQVPFDDL PVPDFTGLRT VQPDLTTLRG MIDWQFLFLA WELKGKYPAI LDQPVARELY DDANTLLDQI IAEGHFQARG AYGFWPAHSE GDDILIDAGP PAAGGRGILR LPMLRQQTAK PTGRANRCLA DYVAPAGDHI GGFAVAVHGA EDLATAFEAR HDDYRAIMVK ALADRLAEAF AEHIHLQARR AWYEPDADPL IEDLHAERFR GIRPALGYPA SPDHSQKQDL FDLLDAKRLD MALTESFAMT PAASVSGLLF AHPESRYFTV GRLGRDQIED YALRRGLGLP EVERWLRPNL AYEPG // ID D2B6D6_STRRD Unreviewed; 287 AA. AC D2B6D6; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 27-MAY-2015, entry version 32. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:ACZ85700.1}; GN OrderedLocusNames=Sros_2740 {ECO:0000313|EMBL:ACZ85700.1}; 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 {ECO:0000313|EMBL:ACZ85700.1, ECO:0000313|Proteomes:UP000002029}; RN [1] {ECO:0000313|EMBL:ACZ85700.1, ECO:0000313|Proteomes:UP000002029} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100 RC {ECO:0000313|Proteomes:UP000002029}; RX PubMed=21304675; 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 9100)."; RL Stand. Genomic Sci. 2:29-37(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; CP001814; ACZ85700.1; -; Genomic_DNA. DR RefSeq; WP_012889445.1; NC_013595.1. DR RefSeq; YP_003338443.1; NC_013595.1. DR EnsemblBacteria; ACZ85700; ACZ85700; Sros_2740. DR KEGG; sro:Sros_2740; -. DR PATRIC; 32467441; VBIStrRos112010_2714. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; SROS479432:GI0V-2762-MONOMER; -. DR Proteomes; UP000002029; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002029}; KW Methyltransferase {ECO:0000313|EMBL:ACZ85700.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002029}; KW Transferase {ECO:0000313|EMBL:ACZ85700.1}. SQ SEQUENCE 287 AA; 30343 MW; 3634D037570DD973 CRC64; MVILDGGLAT HLEALGADLR DELWSAKLLL ENPSVIRQAH LDYFTAGAEV ATTASYQASI PAFVRRGLSA REAEELIVLS VRLAAEARDS HGTGTVAASV GPYGAYLANG AEYTGDYDLD EDGLADWHRD RWHILAGSGA DLLACETIPS YAEARALGRL LAETPGTRAW VSFSCRDGEH ISDGTPLKDA AALFAGNPQV IAVGVNCTAP RHITSLIGRI EGKPVMVYPN SGETWDAANR RWLGLADPAE FGAAAAGWHA AGSAFVGGCC RTTPEHIRQI GEHLKAG // ID D2BXE5_DICD5 Unreviewed; 1227 AA. AC D2BXE5; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 29-APR-2015, entry version 41. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACZ78520.1}; GN OrderedLocusNames=Dd586_3690 {ECO:0000313|EMBL:ACZ78520.1}; OS Dickeya dadantii (strain Ech586). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Dickeya. OX NCBI_TaxID=590409 {ECO:0000313|EMBL:ACZ78520.1, ECO:0000313|Proteomes:UP000001446}; RN [1] {ECO:0000313|EMBL:ACZ78520.1, ECO:0000313|Proteomes:UP000001446} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ech586 {ECO:0000313|EMBL:ACZ78520.1, RC ECO:0000313|Proteomes:UP000001446}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001836; ACZ78520.1; -; Genomic_DNA. DR RefSeq; WP_012886318.1; NC_013592.1. DR RefSeq; YP_003335226.1; NC_013592.1. DR EnsemblBacteria; ACZ78520; ACZ78520; Dd586_3690. DR KEGG; ddc:Dd586_3690; -. DR PATRIC; 32074216; VBIDicDad110536_3722. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; DDAD590409:GHDW-3773-MONOMER; -. DR Proteomes; UP000001446; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001446}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135471 MW; 689BB277BFA8E8B3 CRC64; MANRLQALQQ QLAQRIMILD GGMGTMIQSY RLQEEDYRGE RFADWHCDLK GNNDLLVLSK PEVITAIHHD YLAAGADILE TNTFNATRIA MADYEMQALS AEINTVAARL ARACADEWTA RTPDRPRYVA GVLGPTNRTA SISPDVNDPA YRNVSFDQLV EAYRESTRAL IDGGVDIILI ETIFDTLNAK AAIFAVETEF EALGVTLPVM ISGTITDASG RTLSGQTTEA FYNSLRHARP LSFGLNCALG PDELRQYVAE LSRIAECYVT AHPNAGLPNA FGEYDLDADE MARQIGEWAQ SGFLNIIGGC CGTTPEHIAA MVKAVEGVAP RALPTLPVAC RLSGLEPLNI GDDTLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VESGAQIIDI NMDEGMLNAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV VEAGLKCIQG KGIVNSISMK EGVEAFVHHA RLVRRYGAAV VVMAFDEVGQ ADTRARKIEI CRRAYHILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAV DFIEACADIK AQLPHALISG GVSNVSFSFR GNEPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLEIAEKYRG SKSDDDSNKG AAEWRGWPVK KRLEYALVKG ITEFIEQDTE EARAESARPI EVIEGPLMDG MNVVGDLFGA GKMFLPQVVK SARVMKQAVA YLEPFIQASK DQGSSAGKIL LATVKGDVHD IGKNIVGVVL QCNNYEIIDL GVMVPTDKIL KTAREENVDI IGLSGLITPS LDEMVNVAKE MERQGFTLPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRSVGVVSAL LSDTQHDDFV ARIRKEYETV RIQHGRKKPR TPPVSLEVAR DNAMPIDWES YTPPVAHRLG VQPVTASIET LRNYIDWTPF FMTWSLAGKY PNILEDEVVG EEATRLFADA NAMLDTLSAN GTLNPRGVVG LFPANRVGDD VEIYTDERRT EVLTVSHHLR QQTEKTDFPN YCLADVVAPK TSGKPDYLGA FAVTGGLEED ELAAQWEAQH DDYNKIMLKA LADRLAEAFA EYLHERVRKV YWGYVPNENL GNDELIRENY QGIRPAPGYP ACPDHTEKAV IWQLLDVDNT VGMKLTESYA MWPGASVSGW YFSHPDSKYF AVAQIQRDQV EDYAVRKQMP VEQIERWLAP NLGYDAD // ID D2C2L5_DICD5 Unreviewed; 302 AA. AC D2C2L5; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ACZ75258.1}; GN OrderedLocusNames=Dd586_0361 {ECO:0000313|EMBL:ACZ75258.1}; OS Dickeya dadantii (strain Ech586). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Dickeya. OX NCBI_TaxID=590409 {ECO:0000313|EMBL:ACZ75258.1, ECO:0000313|Proteomes:UP000001446}; RN [1] {ECO:0000313|EMBL:ACZ75258.1, ECO:0000313|Proteomes:UP000001446} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ech586 {ECO:0000313|EMBL:ACZ75258.1, RC ECO:0000313|Proteomes:UP000001446}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; ACZ75258.1; -; Genomic_DNA. DR RefSeq; WP_012883110.1; NC_013592.1. DR RefSeq; YP_003331963.1; NC_013592.1. DR EnsemblBacteria; ACZ75258; ACZ75258; Dd586_0361. DR KEGG; ddc:Dd586_0361; -. DR PATRIC; 32067385; VBIDicDad110536_0369. DR HOGENOM; HOG000265278; -. DR OMA; PYVDVWL; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; DDAD590409:GHDW-376-MONOMER; -. DR Proteomes; UP000001446; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001446}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ACZ75258.1}; KW Transferase {ECO:0000313|EMBL:ACZ75258.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 207 207 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 302 AA; 31925 MW; FCE489652CF1D2DA CRC64; MADNVLILDG GMGRELARIG APFRQPEWSA LALIESPQHV RQVHDSFIAA GAQVITSNSY AVVPFHIGEA EFSARGQALA ALAGQLARQA ADAASHPVRV AGSLPPVLGS YRPDLFNAEA ATPILKTLID ALNPYVDVWL AETQSSLAEV ALVRELLASD PRELWLSFTL QDELDADGHA RLRSGETVAA AAQEAARLGA ANLLFNCSRP EVMAPAVAQA SATLSALSAP IGVGVYANAF EPDDNQRGAN EGLSRLRTDT HPEGYLQWAQ EWVAQGASLV GGCCGIGPEH IARLAQAFHR QA // ID D2C7Q3_THENR Unreviewed; 768 AA. AC D2C7Q3; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 27-MAY-2015, entry version 35. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADA66989.1}; GN OrderedLocusNames=Tnap_0898 {ECO:0000313|EMBL:ADA66989.1}; OS Thermotoga naphthophila (strain ATCC BAA-489 / DSM 13996 / JCM 10882 / OS RKU-10). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=590168 {ECO:0000313|EMBL:ADA66989.1, ECO:0000313|Proteomes:UP000000940}; RN [1] {ECO:0000313|EMBL:ADA66989.1, ECO:0000313|Proteomes:UP000000940} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-489 / DSM 13996 / JCM 10882 / RKU-10 RC {ECO:0000313|Proteomes:UP000000940}; 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., Munk A.C., Brettin T., RA Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Nelson K.E., Gogarten J.P., Noll K.M.; RT "Complete sequence of Thermotoga petrophila RKU-1."; 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; CP001839; ADA66989.1; -; Genomic_DNA. DR RefSeq; WP_012896217.1; NC_013642.1. DR RefSeq; YP_003346403.1; NC_013642.1. DR ProteinModelPortal; D2C7Q3; -. DR EnsemblBacteria; ADA66989; ADA66989; Tnap_0898. DR KEGG; tnp:Tnap_0898; -. DR PATRIC; 32521597; VBITheNap72244_0911. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; TNAP590168:GC5O-928-MONOMER; -. DR Proteomes; UP000000940; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000940}; KW Methyltransferase {ECO:0000313|EMBL:ADA66989.1}; KW Transferase {ECO:0000313|EMBL:ADA66989.1}. SQ SEQUENCE 768 AA; 85637 MW; A7E14E54AADEB5C0 CRC64; MRNRREVSKL LSERVLLLDG AYGTEFMKYG YDDLPEELNI KAPDVVLKVH GSYIESGSDV ILTNTFGATR MKLRKHGLED KLDPIVRNAV RIARRAAGEK LVFGDIGPTG ELPYPLGNTL FEEFYENFRE TVKIMVEEGV DGIIFETFSD ILELKAAVLA AREVSRDVFL IAHMTFDEKG RSLTGTDPAN FAITFDELDV DALGINCSLG PEEILPIFQE LSQYTDKFLV VEPNAGKPIV ENGKTVYPLK PHDFAVHIDS YYELGVNIFG GCCGTTPEHV KLFRKVLGNR KPLKRKKKRI FAVSSPSKLV TFDHFVVIGE RINPAGRKKL WAEMQKGNEE IVINEAKTQV EKGAEVLDVN FGIESQIDVR YVEKIVQALP YVSNVPLSLD IQSVDLTEKA LRTYPGRPLF NSSKVDEEEL EKKINLLKKY GGTLIVLLMG KDVPKSFEER KEYFEKALKI LERHNFSDRV IFDPGVLPLG AEGKPVEVLK TIEFISNRGF NTTVGLSNLS FGLPDRSYYN TAFLVLGISK GLSSAIMNPL DEILMKTLNA TLVILEKKEL PRAEVKEEKL VEVILSGNQS ELEKLVEDFL KKKDPLSIIE EHLRPAMERI GELYDKGKIF LPQLILAAQT VKPVFDKLTS MLPSDSQGET FVIATVKGDV HDIGKNIVAS VIRSSGYRVV DLGKDVDTSK IVEAVERERP VALGLSAMMT TTVSRIKEVV EKLKEKNLKI PVIAGGASLN EKLAKELGAD YYAKNASEAV KILKSLGR // ID D2F015_9BACE Unreviewed; 921 AA. AC D2F015; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 01-APR-2015, entry version 30. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFA19483.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFA19483.1}; GN Name=metH {ECO:0000313|EMBL:EFA19483.1}; GN ORFNames=HMPREF0969_02737 {ECO:0000313|EMBL:EFA19483.1}; OS Bacteroides sp. D20. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=585543 {ECO:0000313|EMBL:EFA19483.1}; RN [1] {ECO:0000313|EMBL:EFA19483.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=D20 {ECO:0000313|EMBL:EFA19483.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG730107; EFA19483.1; -; Genomic_DNA. DR EnsemblBacteria; EFA19483; EFA19483; HMPREF0969_02737. DR PATRIC; 35666094; VBIBacSp64485_2702. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFA19483.1}; KW Transferase {ECO:0000313|EMBL:EFA19483.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 243 243 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 765 765 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 921 AA; 101047 MW; 5E789CDA52AA0F2A CRC64; MSKLGSLVRE RILILDGAMG TMIQQYNLTE GDFRGERFSQ IPGQMKGNND LLCLTRPDVI QDIHRKYLAA GADIIETNTF SSTRVSMADY HVQDYVREMN LAAVRLARKV ADEFTSLTPD KPRFVAGSVG PTNKTCSMSP DVNNPAFRAL SYDELADAYR EQMEALLEGG VDALLIETIF DTLNAKAAIF AAGQAMETVG VHVPLMLSVT VSDIGGRTLS GQTLDAFLAS VQHADIFSVG LNCSFGARQL KPFLEQLAVR APYYISAYPN AGLPNSLGTY DQTPADMAHE VKEYIHEGLV NIIGGCCGTT DAYIAEYSSL IAGATPHQPV PRPENLWLSG LELLEVKPEN NFVNVGERCN VAGSRKFLRL INEKKYDEAL SIARRQVEDG AQVIDINMDD GLLDARTEMT TFLHLIASEP EIARVPVMID SSKWEVIVAG LKCLQGKSIV NSISLKEGED KFLEHARTIK QYGAATVVMA FDEKGQADTY ERKIEVCERA YRLLVDKIGF NPHDIIFDPN VLAVATGMDE HNNYAVDFIR ATGWIRKNLP GAHVSGGVSN LSFSFRGNNY IREAMHAVFL YYAIREGMDM GIVNPATSVL YTDIPADILE RIEDVVLNRR PDAAERLIET AERLKAEAEA AKTSGGERQA AAHSQLAWRE ETSVEERLKY ALTKGIGDYL EEDLAEALKL YPKAVSIIEG PLMAGMNHVG DLFGAGKMFL PQVVKTARTM KRAVAILQPV IESEKEEGAT AAGKVLLATV KGDVHDIGKN IVSVVMACNG YEIIDLGVMV PAETIVQHAI EEKVDMIGLS GLITPSLDEM VHVAIELEKA GLDVPLLIGG ATTSPLHTAL KIAPVYHAPV IHLKDASQNA TVAAKLMNPK TKEELEEELH EKYRQLCEKN REKQVTTVSL EEARKNKLNL F // ID D2HE48_AILME Unreviewed; 392 AA. AC D2HE48; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EFB29051.1}; DE Flags: Fragment; GN ORFNames=PANDA_009043 {ECO:0000313|EMBL:EFB29051.1}; OS Ailuropoda melanoleuca (Giant panda). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; OC Ailuropoda. OX NCBI_TaxID=9646; RN [1] {ECO:0000313|EMBL:EFB29051.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20010809; DOI=10.1038/nature08696; RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., RA Li B., Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., RA Jian M., Li J., Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., RA Ryder O.A., Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., RA Guo X., Wang B., Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., RA Wang G., Yu C., Nie W., Wang J., Wu Z., Liang H., Min J., Wu Q., RA Cheng S., Ruan J., Wang M., Shi Z., Wen M., Liu B., Ren X., Zheng H., RA Dong D., Cook K., Shan G., Zhang H., Kosiol C., Xie X., Lu Z., RA Zheng H., Li Y., Steiner C.C., Lam T.T., Lin S., Zhang Q., Li G., RA Tian J., Gong T., Liu H., Zhang D., Fang L., Ye C., Zhang J., Hu W., RA Xu A., Ren Y., Zhang G., Bruford M.W., Li Q., Ma L., Guo Y., An N., RA Hu Y., Zheng Y., Shi Y., Li Z., Liu Q., Chen Y., Zhao J., Qu N., RA Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X., Vinar T., Wang Y., RA Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y., Wang X., RA Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L., RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., RA Wang J., Wang J.; RT "The sequence and de novo assembly of the giant panda genome."; RL Nature 463:311-317(2010). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL192742; EFB29051.1; -; Genomic_DNA. DR HOGENOM; HOG000231636; -. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006577; P:amino-acid betaine metabolic process; IEA:Ensembl. DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 206 206 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT NON_TER 1 1 {ECO:0000313|EMBL:EFB29051.1}. FT NON_TER 392 392 {ECO:0000313|EMBL:EFB29051.1}. SQ SEQUENCE 392 AA; 43484 MW; 9B9ABD841E3AF431 CRC64; GILERLNAGE VVIGDGGFVF ALEKRGYVKA GPWTPEAAVE HPEAVRQLHR EFLRAGSNVM QTFTFYASED KLENRGNYVA EKISGQKVNE AACDIARQVA DEGDALVAGG VSQTPSYLSC KSETEVKKVF QQQLEVFMKK NVDFLIAEYF EHVEEAVWAV ETLKTSGKPV AATMCIGPEG DLHGVSPGEC AVRLVKAGAS IVGVNCHFDP TISLQTVKLM KEGLEAARLK GHLMSQPLAY HTPDCSKQGF IDLPEFPFGL EPRVATRWDI QKYAREAYNL GVRYIGGCCG FEPYHIRAIA EELAPERGFL PPASDKHGSW GSGLDMHTKP WIRARARKEY WENLRIASGR PYNPSMSKPD AWGVTKGTAE LMQQKEATTE QQLKELFEKQ KF // ID D2HE49_AILME Unreviewed; 352 AA. AC D2HE49; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 04-MAR-2015, entry version 24. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EFB29052.1}; DE Flags: Fragment; GN ORFNames=PANDA_009044 {ECO:0000313|EMBL:EFB29052.1}; OS Ailuropoda melanoleuca (Giant panda). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; OC Ailuropoda. OX NCBI_TaxID=9646; RN [1] {ECO:0000313|EMBL:EFB29052.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20010809; DOI=10.1038/nature08696; RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., RA Li B., Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., RA Jian M., Li J., Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., RA Ryder O.A., Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., RA Guo X., Wang B., Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., RA Wang G., Yu C., Nie W., Wang J., Wu Z., Liang H., Min J., Wu Q., RA Cheng S., Ruan J., Wang M., Shi Z., Wen M., Liu B., Ren X., Zheng H., RA Dong D., Cook K., Shan G., Zhang H., Kosiol C., Xie X., Lu Z., RA Zheng H., Li Y., Steiner C.C., Lam T.T., Lin S., Zhang Q., Li G., RA Tian J., Gong T., Liu H., Zhang D., Fang L., Ye C., Zhang J., Hu W., RA Xu A., Ren Y., Zhang G., Bruford M.W., Li Q., Ma L., Guo Y., An N., RA Hu Y., Zheng Y., Shi Y., Li Z., Liu Q., Chen Y., Zhao J., Qu N., RA Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X., Vinar T., Wang Y., RA Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y., Wang X., RA Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L., RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., RA Wang J., Wang J.; RT "The sequence and de novo assembly of the giant panda genome."; RL Nature 463:311-317(2010). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL192742; EFB29052.1; -; Genomic_DNA. DR HOGENOM; HOG000231636; -. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 198 198 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 280 280 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 281 281 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT NON_TER 1 1 {ECO:0000313|EMBL:EFB29052.1}. FT NON_TER 352 352 {ECO:0000313|EMBL:EFB29052.1}. SQ SEQUENCE 352 AA; 38831 MW; 758CE5D7434E9797 CRC64; QGILERLESG EVVVGDGSFL LTLEKRGYVK AGLWTPEAVV DHPDAVRQLH TEFLRAGSNV MQTFTFSASE DNMESKWEAV NEAACDLARE VAGKGDALVA GGICQTSLYR HHKDEVRVKK LFQLQLEVFI KKNMDFLIAE YFEHAEEAVW AVEVLKESGK PVAATMCIGP DGDMHGVTPG ECAVKLVKAG AAIVGVNCRF GPSTSLKTMR LMKEGLRAAG LKAHLIVQSL GFHTPDCGKG GFVDLPEYPF GLEPRVATRW DIQKYAREAY NLGVRYIGGC CGFEPYHIRA IAEELAPERG FLPPASDKHG SWGSSLNMHT KPWIRARARR EYWENLLPAS GRPFCPSLSR PD // ID D2I0F1_AILME Unreviewed; 1261 AA. AC D2I0F1; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 01-APR-2015, entry version 35. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EFB19906.1}; DE Flags: Fragment; GN ORFNames=PANDA_018634 {ECO:0000313|EMBL:EFB19906.1}; OS Ailuropoda melanoleuca (Giant panda). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; OC Ailuropoda. OX NCBI_TaxID=9646; RN [1] {ECO:0000313|EMBL:EFB19906.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20010809; DOI=10.1038/nature08696; RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., RA Li B., Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., RA Jian M., Li J., Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., RA Ryder O.A., Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., RA Guo X., Wang B., Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., RA Wang G., Yu C., Nie W., Wang J., Wu Z., Liang H., Min J., Wu Q., RA Cheng S., Ruan J., Wang M., Shi Z., Wen M., Liu B., Ren X., Zheng H., RA Dong D., Cook K., Shan G., Zhang H., Kosiol C., Xie X., Lu Z., RA Zheng H., Li Y., Steiner C.C., Lam T.T., Lin S., Zhang Q., Li G., RA Tian J., Gong T., Liu H., Zhang D., Fang L., Ye C., Zhang J., Hu W., RA Xu A., Ren Y., Zhang G., Bruford M.W., Li Q., Ma L., Guo Y., An N., RA Hu Y., Zheng Y., Shi Y., Li Z., Liu Q., Chen Y., Zhao J., Qu N., RA Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X., Vinar T., Wang Y., RA Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y., Wang X., RA Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L., RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., RA Wang J., Wang J.; RT "The sequence and de novo assembly of the giant panda genome."; RL Nature 463:311-317(2010). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GL193880; EFB19906.1; -; Genomic_DNA. DR HOGENOM; HOG000251409; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 781 781 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. FT NON_TER 1 1 {ECO:0000313|EMBL:EFB19906.1}. FT NON_TER 1261 1261 {ECO:0000313|EMBL:EFB19906.1}. SQ SEQUENCE 1261 AA; 140526 MW; 6CB382FD27B4FD67 CRC64; GVKKSLQDEI EAILRERIMV LDGGMGTMIQ RHKLSEEDFR GHEFQDHARP LKGNNDILSI TQPSVIYQIH KDYLLAGADI IETNTFSSTN IAQADYGLEH LAYRMNKCSA GLARKAAEEV SFQTGIKRFV AGALGPTNKT LSVSPSVEKP DYRNITFDEL VEAYQEQAKG LLDGGADILL IETIFDTANA KAALFALQTL FEEEYSPRPI FISGTIIDKS GRTLSGQMGE AFVISVSHAD PLCIGLNCAL GAAEMRPFIE TIGKCTTAYV LCYPNAGLPN TFGDYDETPH MMATQLKDFA MDGLVNIVGG CCGTTPDHIR EIAKAVRNCK PRVPPATVFE EHMLLSGLEP FRIGPYTNFV NIGERCNVAG SRRFAKLIMA GNYEEALSVA KVQVEMGAQV LDINMDDGML DGSSAMTRFC NFIASEPDIA KVPLCIDSSN FAVIEAGLKC CQGKCIVNSI SLKEGEEDFL EKARKIKKFG AAVVVMAFDE EGQATETDTK ISVCMRAYRL LVKKLGFNPN DIIFDPNILT IGTGMEEHNL YAVNFIRATK IIKETLPGAR VSGGLSNLSF SFRGMEAIRE AMHGVFLYHA IKFGMDMGIV NAGNLPVYDD IHKELLQLCE DLIWNKDPEA TEKLLRYAQT HGKGGKKVIQ TDEWRNGPIE ERLEYALVKG IEKYIIEDTE EARLNQEKYP RPLNIIEGPL MNGMKVVGDL FGAGKMFLPQ VIKSARVMKK AVGHLIPFME KEREENKMHA GTEEKEATVW LTPQDPYQGT IVLATVKGDV HDIGKNIVGV VLGCNNFRVI DLGVMTPCDK ILKAALDHKA DIIGLSGLIT PSLDEMIFVA KEMERLAIKI PLLIGGATTS RTHTAVKIAP RYSAPVIHVL DASKSVVVCS QLLDENLKDE FFEEILEEYE DIRQDHYESL KERRYLTLSQ ARKNGFHIDW LSEPPPVKPT FLGTRVFEDY DLRKLVAYID WKPFFDVWQL RGKYPNRSFP KIFKDKTVGE EARKVYDDAQ NMLEVLISQK KLRARGVVGF WPAQSVEDDI HLYAEGATPQ AAEPIATFHG LRQQAEKDSA STDPYHCLSD FIAPLHSGVR DYLGLFAVAC FGVEELSKAY EQECDDYSSI MVKALGDRLA EAFAEELHER VRRELWAYCS CEQLDVADLR RLRYEGIRPA PGYPSQPDHS EKLTMWKLAD VERCTGIRLT ESLAMAPASA VSGLYFSNLK SKYFAVGKIS KDQIEDYAVR KNMSVAEVEK WLGPILGYDI E // ID D2PQB9_KRIFD Unreviewed; 1199 AA. AC D2PQB9; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADB34821.1}; GN OrderedLocusNames=Kfla_5817 {ECO:0000313|EMBL:ADB34821.1}; OS Kribbella flavida (strain DSM 17836 / JCM 10339 / NBRC 14399). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Nocardioidaceae; Kribbella. OX NCBI_TaxID=479435 {ECO:0000313|EMBL:ADB34821.1, ECO:0000313|Proteomes:UP000007967}; RN [1] {ECO:0000313|Proteomes:UP000007967} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17836 / JCM 10339 / NBRC 14399 RC {ECO:0000313|Proteomes:UP000007967}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001736; ADB34821.1; -; Genomic_DNA. DR RefSeq; WP_012923375.1; NC_013729.1. DR RefSeq; YP_003383620.1; NC_013729.1. DR EnsemblBacteria; ADB34821; ADB34821; Kfla_5817. DR KEGG; kfl:Kfla_5817; -. DR PATRIC; 32242146; VBIKriFla67707_5819. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; QPFFNAW; -. DR BioCyc; KFLA479435:GI0F-5870-MONOMER; -. DR Proteomes; UP000007967; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007967}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007967}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 234 234 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 297 297 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 298 298 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 751 751 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1199 AA; 130516 MW; 6A6393391200136C CRC64; MTTSSLRDLL DRRIAVLDGA WGTMLQAANL TSEDYQGDRF LDHSHDVSGD PDLLNLMRPD LILDVHRQYL DAGADITTTN TFTATSIGQA DYGLQSLVRE MNLEGARLAR QAADEAGGRF VAGSVGPLNV TLSLSPRVED PAYRAVSFEQ VRDSYAEQIT ALRDGGVDLL LIETIFDTLN CKAAIAAARE AAPELPLWIS LFVDLSGRTL SGQTVEAWWN SIEHAEPLVV GVNCSLGARE LRPHVADLAR FADTYVASHP NAGLPNAFGG YDETPEQTAG MIGEFAESGL VNIVGGCCGT TPAHIAKIAQ AVAGAAPRTV VPPAGTTRFS GLEPFKIGAD TGFVMIGERT NVTGSARFRR LIESDDFQAA VDVALDQVRG GANLLDVNMD ADLLDSEQAM TTFLNLIATE PEVARIPIMI DSSKWTVLEA GLKCVQGKGV VNSISLKEGE QEFLERARRI RDYGAGAVVM AFDEQGQADT VERKVDICGR AYDLLTGIGF PAEDIIFDPN VLAVATGMSE HNGYAKNFID ALPLIKQRCP GVHISGGISN LSFSFRGNDI VREAMHSAFL YHAGKAGLDM GIVNAGQLAV YEDIPKDLLE LVEDVIFNRR DDATDRLVSF AENVKGKGTQ RVVDLSWREG TVEQRLSHAL VHGIVDYVEA DTEEARQQFA RPLEVIEGPL MDGMKIVGDL FGAGKMFLPQ VVKSARVMKR SVAYLEPFME AEKELARQEG RTEDVRDQGK VVLATVKGDV HDIGKNIVGV VLGCNNYEVI DLGVMVPAAK ILDTAIAEGA DVVGLSGLIT PSLDEMVTVA AEMQRRGLEL PLLIGGATTS KQHTAVRIAP AYDQTTVHVL DASRVVGVVS DLLDKDRSQT LALSNREDQD RLREQHASKQ RAPLLSIDDA RANREPVEYG ELPVPAFTGL RREAPSLETL RAMIDWQFLF LAWELKGKYP AILEQPVARE LFDDANTLLD QIVADKSFTA EGAYGFWPAH SEGDDIVLDG LGVSFPMLRQ QTQKPAGRYN RCLADYVAPA GDHLGGFGVA IHGAEELAAR YEAQNDDYRA IMVKALADRL AEAFAEWIHL EARKAWFEPD AEPVLEDLHA ERFRGIRPAL GYPASPDHSE KKELFDLIEA EKLGLGLTTS YAMTPAAAVS GLIFASPSAR YFSVGRLGRD QIEDYAKRRG LPVAEIERWL RPNLAYDPQ // ID D2QKR8_SPILD Unreviewed; 1261 AA. AC D2QKR8; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 27-MAY-2015, entry version 41. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADB40234.1}; GN OrderedLocusNames=Slin_4250 {ECO:0000313|EMBL:ADB40234.1}; OS Spirosoma linguale (strain ATCC 33905 / DSM 74 / LMG 10896). OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae; OC Spirosoma. OX NCBI_TaxID=504472 {ECO:0000313|EMBL:ADB40234.1, ECO:0000313|Proteomes:UP000002028}; RN [1] {ECO:0000313|Proteomes:UP000002028} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33905 / DSM 74 / LMG 10896 RC {ECO:0000313|Proteomes:UP000002028}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001769; ADB40234.1; -; Genomic_DNA. DR RefSeq; WP_012928742.1; NC_013730.1. DR RefSeq; YP_003389033.1; NC_013730.1. DR EnsemblBacteria; ADB40234; ADB40234; Slin_4250. DR KEGG; sli:Slin_4250; -. DR PATRIC; 32438433; VBISpiLin97822_4244. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; SLIN504472:GHKB-4281-MONOMER; -. DR Proteomes; UP000002028; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 2. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 2. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002028}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002028}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 756 756 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1261 AA; 140476 MW; F67A314EAADA0566 CRC64; MKTIYELLHE RILVLDGAMG TMIQRYNLTD ADYRGERFRD WPHDLKGNND LLSLTKPEII QAIHKQYLEA GADIIETNTF SGTSIAMADY RMEELAYELN YESARIAKEV AVEITRQNPD KPRFVAGAMG PTNRTASLSP DVNNPAYRAV TFDELVNAYY EQVSGLVDGG ADLLLVETIF DTLNAKAAMF AIDKYFNLNP QKTALPIMIS GTITDASGRT LSGQTTEAFL YSVSHLPLLS VGLNCALGAQ LMRPYIQTLA KEAPFFTSAY PNAGLPNEFG EYDETPDMMA LQIEDFVKSN FVNIVGGCCG STPDHIRAIA DVAAKYPPRQ LPQPEPYQKL SGLEPLKITE QTNFLNVGER TNVTGSKKFA RLIKEGNFDE ALSIARGQVE GGAQVIDINM DEGMLDSVEA MKTFLNLIAA EPDIARVPIM VDSSKWEVIE AGLKCVQGKA IVNSISLKEG EEAFIERANL VKRYGAAAVV MAFDENGQAD SYERRIEICE RAYRILVDKV QFAPQDIIFD PNILTVATGI EEHNNYAVDF INATRWIKQN LPLAKVSGGV SNISFSFRGN DVVREAMHSA FLYHAIRAGL DMGIVNAGQL EVYDSIPKDL LERCEDVLLN RRDDATERLV EFAETVKAKG KAIVQDESWR LEPVRERLKH ALIKGITDYI DQDVEEIRQQ VERPLHVIEG PLMDGMNVVG DLFGAGKMFL PQVVKSARVM KKAVAYLTPF IEAEKSGTGS SNAGKILLAT VKGDVHDIGK NIVGVVLGCN NYEIIDLGVM VPTQKILDAA REHNVDIIGL SGLITPSLDE MVGVAKEMER QGFKLPLLIG GATTSRIHTA VKIDPHYSGP VVHVLDASRS VPVAGRLVSE TDGTKEKIFT DIKAEYVKLR EEHTKRQKDK ASLTISQARD NRTKIDWSTF EPTKPAFLGN RYFDDYSIAE LVDYIDWTPF FQTWQLHGKY PAIFDDAVVG KEAKQLFDDA NRLLQEIVDK KLLKAKAVVG FFPANSADDD VLLHDFEEHV RETACERHGS HQHIEYKISK AQSQAAVSPA GELIYDTKTV LHFLRQQNQK APGLPNFCLS DFIAPLESGR EDYIGGFAVT AGIGIETLLE KYERDHDDYN SIMVKALADR LAEAFAERMH ERVRKEFWPY AVNENLSNEQ LVKEAYQGIR PAPGYPACPD HTEKGTLFNL LDANKIDIEL TESYAMYPAS SVSGFYFSHP ESKYFALGKI NKDQILDYAQ RKDMPVEEIE KWLSPVLSYD A // ID D2QXK9_PIRSD Unreviewed; 1234 AA. AC D2QXK9; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 27-MAY-2015, entry version 37. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADB16194.1}; GN OrderedLocusNames=Psta_1519 {ECO:0000313|EMBL:ADB16194.1}; 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 {ECO:0000313|EMBL:ADB16194.1, ECO:0000313|Proteomes:UP000001887}; RN [1] {ECO:0000313|EMBL:ADB16194.1, ECO:0000313|Proteomes:UP000001887} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27377 / DSM 6068 / ICPB 4128 RC {ECO:0000313|Proteomes:UP000001887}; RX PubMed=21304671; DOI=10.4056/sigs.51657; RA Clum A., Tindall B.J., Sikorski J., Ivanova N., Mavrommatis K., RA Lucas S., Glavina del Rio T., Nolan M., 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., Ovchinikova G., Pati A., Mikhailova N., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., RA Chain P., Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.; RT "Complete genome sequence of Pirellula staleyi type strain (ATCC RT 27377)."; RL Stand. Genomic Sci. 1:308-316(2009). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001848; ADB16194.1; -; Genomic_DNA. DR RefSeq; WP_012910457.1; NC_013720.1. DR RefSeq; YP_003370054.1; NC_013720.1. DR EnsemblBacteria; ADB16194; ADB16194; Psta_1519. DR KEGG; psl:Psta_1519; -. DR PATRIC; 32286692; VBIPirSta4342_1581. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR BioCyc; PSTA530564:GHPR-1529-MONOMER; -. DR Proteomes; UP000001887; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001887}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001887}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 253 253 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 316 316 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 768 768 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1234 AA; 136572 MW; 9D63F92D105D708B CRC64; MTDIRRSKTY DLLESLLEDR VLVLDGAMGT MIQRLDLDEA AVRGDRFADH TKDLARFSDI LCLTRANDIT EIHRKYLAAG ADIIETNTFG ASVIGMEEFD LPNELVREIN FAAVKCARIA CDEFTSRDPS RPRFVAGSIG PTTKQTAIST RVEDPAYRAV TFEQMVESYS GQIEALVEAG VDIILPETVI DTLNLKACLF ALERHFKKVG ERTAVMVSGT FNAAGVTFVS SQNVEAFWNS IAHVPLLSVG MNCALGPDVM RPHLEELQRV SGAKISCYPN AGLPNEMGQY DLGPAGMANI IGEFLDERWL NIVGGCCGTT PDHIAAIAER TRRAKPHKIA EKPAWLRLSG TEAFTLRPES NFVMVGERTN VTGSKAFARL IRDEKYEEAV DVARQQVAGG ATIIDVNMDD ALLDGEAAMT RFLRLIAGDG EASKVPVMID SSKWSVLEAG LRCVQGKAIV NSISLKDGEE EFLRRAELVR RYGASAVVMA FDEGGQAVEI DHKVSICKRA YDLLTQKIGF PPEDIIFDPN ILTVATGIEE HNNYAVNFIE ATRIIKQVCP GAKVSGGVSN ISFSFRGNDV VREAMHSAFL YHAIRAGLDM GIVNAGQLAV YEEIPPALLK AVEDVLLNRS DDATEKLVAL AETVKGKGKV AAGEDLTWRE ENVEGRLRHA LVKGIDRFVE TDVEEARQKY PKCLSIIEGP LMDGMTVVGD LFGEGKMFLP QVVKSARVMK KAVNYLLPFM EQEKLLAGNE SQGARARVLM ATVKGDVHDI GKNIVGVVLA CNNYEVIDLG VMVPCEKILQ TAVEKKCDII GLSGLITPSL DEMVHVAKEM SRQNIKIPLL IGGATTSAKH TAVKIAPSYA EPVVHVLDAS RCVGVVDKLL SENLRAQMVA DNKKLQLDLA TSYQARQQKL VPFKEAQSRK FVTDWSTVQI DEPTFLGTRV IEAQSLELLR GYIDWSPFFS TWELKGKFPK IFDDPKVGPQ AKELYQDAEQ LLDKIIQFNL LKAKAVYGFW PANSDGDDII LYTDDTRTAE LCRFYTLRQQ WERQGQNDFK ALADFVAPVA SGRKDYLGAF AVTAGVGCDE LAKEFDKKFD DYNSIMVKAL ADRLAEAFAE QLHQQARREW RYGAGEQLTS EQLIAEEYRG IRPAPGYPSQ PDHTEKRTLF DLLGVEKSIG MSLTESFAMW PAASVCGLYF GHPDARYFAL DRITRDQVED YARRKHLPVK EVERWLSPNL GYDP // ID D2R929_PIRSD Unreviewed; 293 AA. AC D2R929; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADB15856.1}; GN OrderedLocusNames=Psta_1177 {ECO:0000313|EMBL:ADB15856.1}; 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 {ECO:0000313|EMBL:ADB15856.1, ECO:0000313|Proteomes:UP000001887}; RN [1] {ECO:0000313|EMBL:ADB15856.1, ECO:0000313|Proteomes:UP000001887} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27377 / DSM 6068 / ICPB 4128 RC {ECO:0000313|Proteomes:UP000001887}; RX PubMed=21304671; DOI=10.4056/sigs.51657; RA Clum A., Tindall B.J., Sikorski J., Ivanova N., Mavrommatis K., RA Lucas S., Glavina del Rio T., Nolan M., 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., Ovchinikova G., Pati A., Mikhailova N., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., RA Chain P., Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.; RT "Complete genome sequence of Pirellula staleyi type strain (ATCC RT 27377)."; RL Stand. Genomic Sci. 1:308-316(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; CP001848; ADB15856.1; -; Genomic_DNA. DR RefSeq; WP_012910121.1; NC_013720.1. DR RefSeq; YP_003369716.1; NC_013720.1. DR EnsemblBacteria; ADB15856; ADB15856; Psta_1177. DR KEGG; psl:Psta_1177; -. DR PATRIC; 32285986; VBIPirSta4342_1229. DR HOGENOM; HOG000265278; -. DR BioCyc; PSTA530564:GHPR-1186-MONOMER; -. DR Proteomes; UP000001887; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001887}; KW Methyltransferase {ECO:0000313|EMBL:ADB15856.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001887}; KW Transferase {ECO:0000313|EMBL:ADB15856.1}. SQ SEQUENCE 293 AA; 31511 MW; FFC92E22185D63C8 CRC64; MNRNWKLLNG ELLLLDGATG TELNRRGLDT GLPMWSANAL TTDTGLNVLR QIHLDYLQAG ADILTANTFR THRRALASKV HAARELTMRA VATAQEAIAE FGQAAQVAGS VSPLEDCYRP DLVPPDDMCR AEHSERIQHL VDAGVDLLLI ETMSSIREAV IAAKLATITG LPTLVSFVCD GEGRILSGEP VAVAAELLLP LGVKALGVNC GPAHTLAKPL VELRRICGPD FPLIAYGNIG YADEAQGWIN TDAESPESYL HHAETWPAQI LGGCCGTTPA HIRRLRVRSN DTT // ID D2RKX3_ACIFV Unreviewed; 317 AA. AC D2RKX3; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADB47725.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ADB47725.1}; GN OrderedLocusNames=Acfer_1365 {ECO:0000313|EMBL:ADB47725.1}; OS Acidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / VR4). OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; OC Acidaminococcaceae; Acidaminococcus. OX NCBI_TaxID=591001 {ECO:0000313|EMBL:ADB47725.1, ECO:0000313|Proteomes:UP000001902}; RN [1] {ECO:0000313|EMBL:ADB47725.1, ECO:0000313|Proteomes:UP000001902} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25085 / DSM 20731 / VR4 RC {ECO:0000313|Proteomes:UP000001902}; RX PubMed=21304687; RA Chang Y.J., Pukall R., Saunders E., Lapidus A., Copeland A., Nolan M., RA Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J.F., Han C., RA Detter J.C., 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.D., Brettin T., RA 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 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; ADB47725.1; -; Genomic_DNA. DR RefSeq; WP_012938712.1; NC_013740.1. DR RefSeq; YP_003399040.1; NC_013740.1. DR EnsemblBacteria; ADB47725; ADB47725; Acfer_1365. DR KEGG; afn:Acfer_1365; -. DR PATRIC; 31909261; VBIAciFer109666_1342. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR BioCyc; AFER591001:GHUL-1420-MONOMER; -. DR Proteomes; UP000001902; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001902}; KW Methyltransferase {ECO:0000313|EMBL:ADB47725.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001902}; KW Transferase {ECO:0000313|EMBL:ADB47725.1}. SQ SEQUENCE 317 AA; 34849 MW; A2E62DCE5B76492D CRC64; MRQTLKNILD QNKILVIDGS MGTALENLGA DLNNSLWTAR VLANRPELVK QVHLDYFRAG ADAGITCSYQ ASIPGLVANG FTEQEAEELI TRSVTIFQEA RQEWWDREGK AAGRAWPLCL AGVGPYGAYL ADGSEYRGHY GVSREDLEKF HRRRAELLWQ AGADVLLFET QPSLEEALVE VSIAKDLGAA FWVSFSCRDG LHICEGTPIR EAAAEVVRQF PEVEALGVNC TKPEYLVSLI GELKTASDRP IFVYPNSGEE YDPVTKTWHG VGTDRKFGDY ALEYMKAGAV AVGGCCTTVA DHVRQVAAAR EQFLGEA // ID D2RMA2_ACIFV Unreviewed; 805 AA. AC D2RMA2; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 27-MAY-2015, entry version 34. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADB48204.1}; GN OrderedLocusNames=Acfer_1850 {ECO:0000313|EMBL:ADB48204.1}; OS Acidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / VR4). OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; OC Acidaminococcaceae; Acidaminococcus. OX NCBI_TaxID=591001 {ECO:0000313|EMBL:ADB48204.1, ECO:0000313|Proteomes:UP000001902}; RN [1] {ECO:0000313|EMBL:ADB48204.1, ECO:0000313|Proteomes:UP000001902} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25085 / DSM 20731 / VR4 RC {ECO:0000313|Proteomes:UP000001902}; RX PubMed=21304687; RA Chang Y.J., Pukall R., Saunders E., Lapidus A., Copeland A., Nolan M., RA Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J.F., Han C., RA Detter J.C., 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.D., Brettin T., RA 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 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; ADB48204.1; -; Genomic_DNA. DR RefSeq; WP_012939187.1; NC_013740.1. DR RefSeq; YP_003399519.1; NC_013740.1. DR EnsemblBacteria; ADB48204; ADB48204; Acfer_1850. DR KEGG; afn:Acfer_1850; -. DR PATRIC; 31910293; VBIAciFer109666_1842. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR BioCyc; AFER591001:GHUL-1923-MONOMER; -. DR Proteomes; UP000001902; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001902}; KW Methyltransferase {ECO:0000313|EMBL:ADB48204.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001902}; KW Transferase {ECO:0000313|EMBL:ADB48204.1}. SQ SEQUENCE 805 AA; 85036 MW; 3291D9A82729D28B CRC64; MNFTEALHTR RLFFDGAMGT MLQEAGLQPG ELPETWNLLH PEKVRAIHQA YVRAGVDILK TNTFGANGLK FGAAHGQPEV EELVRAGVEN ARAAFAAEVR DGFVALDLGP TGKLLQPFGD LPFAEAVALY AAQVKAGAAA GADLILIETM SDSYEAKAAI LAAKENADLP IVCTFTFDED GKLLNGADVT TALVMAESLG VSAVGFNCGQ GPDTLVKLVP QALQAVDIPL VANPNAGLPV QKDGKTVFHI DGEGYAPLMV PFAEAGVSVL GGCCGTTPDH IARLIEACRD IPLPAPRSGA PCAIAGYGRA VDFEGMPVII GERINPTGKP RLKEALKSQN MDYVCQLALE QLDKGAQVLD VNVGVPGVDE PALIEKVILT LQSITSVPLQ IDTSNIEAME RALRIYNGRP LLNSVNGKAE NMADVLPLAK KYGAALVGLC LDEGGIADTA KGRLEVADKV IAEAGKYGIP ARDMVMDPLA MTISTGGQNA RIDLEVIRQL KARNIKTVMG VSNISFGLPS RDAVNSAFFA LAMEAGLSAG IINPNSGAMM GAYIAYGALS GKDEGCKKYV EYFADAPQMV AVAKSQGGAK PAAKGPQKEY PLEEAIVKGL TSQVENGVRK QLAEGKPALD IINESMIPGL NIVGDLFEKK KLFLPQLLVS ADAAKAGFEI LKQSIAKGAS TEKGDPIVIC TVKGDIHDIG KNIVKVLLEN YGYQVIDLGK DVPPEEVVKA AREHDARLVG LSALMTTTVG SMEETIRQLR QALPDCRVMV GGAVMTEEYA RTIGADFYGA NAVASVHYAN QLFHK // ID D2S6D2_GEOOG Unreviewed; 1269 AA. AC D2S6D2; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 27-MAY-2015, entry version 41. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADB75306.1}; GN OrderedLocusNames=Gobs_2671 {ECO:0000313|EMBL:ADB75306.1}; 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 {ECO:0000313|EMBL:ADB75306.1, ECO:0000313|Proteomes:UP000001382}; RN [1] {ECO:0000313|Proteomes:UP000001382} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25078 / DSM 43160 / JCM 3152 / G-20 RC {ECO:0000313|Proteomes:UP000001382}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001867; ADB75306.1; -; Genomic_DNA. DR RefSeq; WP_012948739.1; NC_013757.1. DR RefSeq; YP_003409677.1; NC_013757.1. DR EnsemblBacteria; ADB75306; ADB75306; Gobs_2671. DR KEGG; gob:Gobs_2671; -. DR PATRIC; 32174470; VBIGeoObs49253_2648. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; QPFFNAW; -. DR BioCyc; GOBS526225:GI00-2700-MONOMER; -. DR Proteomes; UP000001382; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001382}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001382}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 257 257 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 320 320 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 774 774 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1269 AA; 138966 MW; 8E56CC822260B88B CRC64; MPSRIVSPDL RPDATAELTA VLGQRILVLD GAMGTAIQRD RPDEAGYRGE RFADWPTDVQ GNNDLLSITR PEIIAGIHRE YLEAGADLVE TNTFNATAIS LRDYGMSDLA YEINVAAARL ARAEADAMTA RTPDRPRYVA GALGPTSRTA SISPNVNDPG ARNVTFDELA LAYLEQADGL VDGGVDVLLI ETVFDTLNAK AAIYALETLF EQRGRRWPVM VSGTITDASG RTLSGQVTEA FWHSIRHVRP LLVGLNCALG AAEMRPYLAE LSRVADTYVS CYPNAGLPNA FGEYDESPEE TAAVLAEFAD AGFVNTVGGC CGTTPAHIAV IAATVEGRAP RTPPRVRPAL RLSGLEPLVV DEDSLFVNVG ERTNITGSAR FRNLIRAGDY PTALAVARQQ VEAGAQVIDV NMDEGMIDGV EAMDRFLKLV AAEPDICRVP VMVDSSKWEV IEAGLKCVQG KSIVNSISLK AGEEEFVQQA RLCRKHGAAV VVMAFDEQGQ ADSLQRRQEI CRRAYDILVE QVGFPAEDVI FDPNVFAVAT GIEEHARYGL DFIEATRWIK QHLPGALVSG GVSNVSFSFR GNNRVREAIH AVFLFHAIAA GMNMGIVNAG ALEVYDEVPE RLRERIEDVV LARRPDATER LLEIAAEYAG DGAQKEVASE EWRSLPVEER IAHALVKGID GFVEADTEEL RAQIAARGGR PIEVIEGPLM GGMNVVGDLF GAGKMFLPQV VKSARVMKKA VAYLVPFIEA EKQPGDVERS NGKVVMATVK GDVHDIGKNI VGVVLQCNNY DVVDLGVMVP AQKVLDTAKQ EGADVIGLSG LITPSLDEMS NLAAEMERQG FDIPLLIGGA TTSRAHTAVK VAPRYHGPVI WVKDASRSVP VVAALLSNEQ RPKLLADVET EYAGLRERHA ARQDTRALLP LEAARAAAPP VDWSSYAPPR PRMLLQQARD VCSGADCDHL HGRATQFTRV LDDYPLEELR RYVDWQPFFN AWEMRGRFPD ILHNPATGEA ARRLYEDAQE MLDRVVAERW LQARGVFGLF PANRVDGEDI EVYTDESRTT VRTTLHQLRQ QTQGRDGSPR KSLADFVAPK ETGLRDYVGA FAVTAGLGSA ERVAAFKAAN DDYSAIMLEA LADRLAEAFA ERLHERVRRE FWGYAADEHL DNDALIAEQY RGIRPAPGYP ACPEHTEKRT IWELLDVEAT TGITLTESMA MWPGAAVSGL YLAHPQSRYF VLGRLGRDQV EDYARRKGWT LAEAERWLSP NLGYRTDDE // ID D2S8U0_GEOOG Unreviewed; 314 AA. AC D2S8U0; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADB75671.1}; GN OrderedLocusNames=Gobs_3061 {ECO:0000313|EMBL:ADB75671.1}; 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 {ECO:0000313|EMBL:ADB75671.1, ECO:0000313|Proteomes:UP000001382}; RN [1] {ECO:0000313|Proteomes:UP000001382} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25078 / DSM 43160 / JCM 3152 / G-20 RC {ECO:0000313|Proteomes:UP000001382}; 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; ADB75671.1; -; Genomic_DNA. DR RefSeq; WP_012949101.1; NC_013757.1. DR RefSeq; YP_003410042.1; NC_013757.1. DR EnsemblBacteria; ADB75671; ADB75671; Gobs_3061. DR KEGG; gob:Gobs_3061; -. DR PATRIC; 32175259; VBIGeoObs49253_3039. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; YGRSVTK; -. DR BioCyc; GOBS526225:GI00-3094-MONOMER; -. DR Proteomes; UP000001382; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001382}; KW Methyltransferase {ECO:0000313|EMBL:ADB75671.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001382}; KW Transferase {ECO:0000313|EMBL:ADB75671.1}. SQ SEQUENCE 314 AA; 32118 MW; 4C3A79C972FC04D5 CRC64; MPDFPLATAL AAGPVVLDGG LATQLEAQGH DLSSELWSSR LLHDAPEAVV AAHAAFAAAG AQVATTASYQ VSVEGLAAAG LDATEARRLV VRSVHLAERG APDAWIAGSV GPYGAALADG SEYTGAYADE IGVDRLRQWH RPRMEWLAEA GADVLACETV PAAAEAEALL EEADMLGMPV WLSLTTVLDS DGVVRTRRGE PAGEVFAMAR DLDAVVAVGV NCTDPDGVLA AVTAAGVAGR PVVVYPNSGE RWDAAGRRWT GTAGLSPHNA LTWVHAGARL VGGCCRVGPR SIGALAAALR PAPSGEPVGP HNGH // ID D2T3W4_ERWP6 Unreviewed; 300 AA. AC D2T3W4; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Erwinia pyrifoliae DSM 12163 complete genome, culture collection DSM:12163 {ECO:0000313|EMBL:CAY75121.1}; DE EC=2.1.1.- {ECO:0000313|EMBL:CAY75121.1}; GN OrderedLocusNames=EPYR_02741 {ECO:0000313|EMBL:CAY75121.1}; OS Erwinia pyrifoliae (strain DSM 12163 / CIP 106111 / Ep16/96). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Erwinia. OX NCBI_TaxID=644651 {ECO:0000313|EMBL:CAY75121.1, ECO:0000313|Proteomes:UP000008690}; RN [1] {ECO:0000313|Proteomes:UP000008690} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 12163 / CIP 106111 / Ep16/96 RC {ECO:0000313|Proteomes:UP000008690}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; CAY75121.1; -; Genomic_DNA. DR RefSeq; WP_012668798.1; NC_017390.1. DR RefSeq; YP_005803492.1; NC_017390.1. DR EnsemblBacteria; CAY75121; CAY75121; EPYR_02741. DR KEGG; epr:EPYR_02741; -. DR PATRIC; 36678922; VBIErwPyr40668_2493. DR HOGENOM; HOG000265278; -. DR BioCyc; EPYR644651:GLCX-2807-MONOMER; -. DR Proteomes; UP000008690; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008690}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:CAY75121.1}; KW Transferase {ECO:0000313|EMBL:CAY75121.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 208 208 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 300 AA; 31777 MW; 0472DF4F6B45796D CRC64; MTQQIKILDG GMGRELARVG APFRQPEWSA LALYEAPQRV REVHDSFISA GAGTITTNSY AVVPFHIGEA RFNADGEHLA ALAGQLARQA ANAATHPVQV AGSLPPALGS YRPDLFDAQQ ALKIYRVLVA AQAPYVDVWL GETISSLAEA VAIHQAVADQ PQPLWLSFSL QDGPDKTRRD SRLRSGESVS AAVELAVESG ATHILFNCSN PEVMLSAVQQ AAATLRRLGS GAGIGVYANA FEHGSNEGGA NEGLSDLRQD THPEGYLRWA REWVAAGATL VGGCCGIGPE HIQCLASAFK // ID D2TSQ2_CITRI Unreviewed; 1205 AA. AC D2TSQ2; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 27-MAY-2015, entry version 39. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CBG90443.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CBG90443.1}; GN Name=metH {ECO:0000313|EMBL:CBG90443.1}; GN OrderedLocusNames=ROD_37381 {ECO:0000313|EMBL:CBG90443.1}; OS Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype OS 4280). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Citrobacter. OX NCBI_TaxID=637910 {ECO:0000313|EMBL:CBG90443.1, ECO:0000313|Proteomes:UP000001889}; RN [1] {ECO:0000313|EMBL:CBG90443.1, ECO:0000313|Proteomes:UP000001889} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ICC168 {ECO:0000313|EMBL:CBG90443.1, RC ECO:0000313|Proteomes:UP000001889}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; FN543502; CBG90443.1; -; Genomic_DNA. DR RefSeq; WP_012907731.1; NC_013716.1. DR RefSeq; YP_003367178.1; NC_013716.1. DR EnsemblBacteria; CBG90443; CBG90443; ROD_37381. DR KEGG; cro:ROD_37381; -. DR PATRIC; 32031144; VBICitRod33214_3557. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; CROD637910:GJIG-3757-MONOMER; -. DR Proteomes; UP000001889; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001889}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CBG90443.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001889}; KW Transferase {ECO:0000313|EMBL:CBG90443.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 225 225 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 737 737 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1205 AA; 133298 MW; 8B16F7FD20C3012F CRC64; MGTMIQSYRL SEADFRGERF ADWPCDLKGN NDLLVLSKPD VISAIHNAYF AAGADIIETN TFNSTTIAMA DYQMESLSAE INLAAAKLAR ACADEWTART PEKPRYVAGV LGPTNRTASI SPDVNDPAFR NISFDRLVAA YRESTRALVE GGADLILIET VFDTLNAKAA VFAVKEEFDA LGVELPIMIS GTITDASGRT LSGQTTEAFY NSLRHAEALT FGLNCALGPD ELRQYVQELS RIAECYVTAH PNAGLPNAFG EYDLDADTMA KQIREWAQAG FLNIVGGCCG TTPEHIAAMS RAVEGLPPRK LPEIEIACRL SGLEPLNIGE DSLFVNVGER TNVTGSAKFK RLIKEEKYSE ALDVARQQVE SGAQIIDINM DDGMLDAEAA MVRFLNLIAG EPDIARVPIM IDSSKWEVIE KGLKCIQGKG IVNSISMKEG VETFIHHAKL LRRYGAAVVV MAFDEQGQAD TRARKIEICR RAYKILTEEV GFPPEDIIFD PNIFAVATGI DEHNNYAQDF IGACEDIKRE LPHALISGGV SNVSFSFRGN DPVREAIHAV FLYYAIRNGM DMGIVNAGQL AIYDDLPAEL RDAVEDVILN RRDDGTERLL ALAEKYRGSK ADDTANAQQA EWRSWEVKKR LEYSLVKGIT EFIEQDTEEA RQQAARPIEV IEGPLMDGMN VVGDLFGEGK MFLPQVVKSA RVMKQAVAYL EPFIEASKEQ GTSNGKMVIA TVKGDVHDIG KNIVGVVLQC NNYEIVDLGV MVPAEKILKT AKEVNADLIG LSGLITPSLD EMVNVAKEME RQGFTIPLLI GGATTSKAHT AVKIEQNYSG PTVYVQNASR TVGVVAALLS ATQRDEFVAR TRKEYETVRI QHGRKKPRTP PVTLAAARDN DLAFDWASYT PPVAHRLGVQ EVEASIETLR NYIDWTPFFM TWSLAGKYPR ILEDEVVGEE ARRLFQDANE MLDKLSVEKA LNPRGVVGLF PANRIGDDIE IYRDETRTHV LTVSHHLRQQ TEKVGFANYC LADFVAPKLS GKADYIGAFA VTGGLEEDAL AEAFAAQRDD YNKIMVKAIA DRLAEAFAEY LHERVRKVYW GYAPNENLSN EELIRENYQG IRPAPGYPAC PEHTEKGTIW QLLDVEKHTG MKLTESFAMW PGASVSGWYF SHPDSKYFAV AQIQRDQVED YAFRKGMSVT EVERWLAPNL GYDAD // ID D2U9L3_XANAP Unreviewed; 316 AA. AC D2U9L3; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 27-MAY-2015, entry version 30. DE SubName: Full=MmuM protein {ECO:0000313|EMBL:CBA16965.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:CBA16965.1}; GN Name=mmuM {ECO:0000313|EMBL:CBA16965.1}; GN OrderedLocusNames=XALc_2486 {ECO:0000313|EMBL:CBA16965.1}; OS Xanthomonas albilineans (strain GPE PC73 / CFBP 7063). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=380358 {ECO:0000313|EMBL:CBA16965.1, ECO:0000313|Proteomes:UP000001890}; RN [1] {ECO:0000313|EMBL:CBA16965.1, ECO:0000313|Proteomes:UP000001890} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GPE PC73 / CFBP 7063 {ECO:0000313|Proteomes:UP000001890}; 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 ----------------------------------------------------------------------- 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; CBA16965.1; -; Genomic_DNA. DR RefSeq; WP_012916960.1; NC_013722.1. DR EnsemblBacteria; CBA16965; CBA16965; XALC_2486. DR KEGG; xal:XALc_2486; -. DR PATRIC; 32547427; VBIXanAlb89132_2439. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR BioCyc; XALB29447:GJN1-2477-MONOMER; -. DR BioCyc; XALB380358:GLMQ-2477-MONOMER; -. DR Proteomes; UP000001890; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001890}; KW Methyltransferase {ECO:0000313|EMBL:CBA16965.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001890}; KW Transferase {ECO:0000313|EMBL:CBA16965.1}. SQ SEQUENCE 316 AA; 33970 MW; 256F73177F78FCAC CRC64; MPMPHNPLTA LLAEGRCIVL DGALATELER FGCDLDDPLW SAKVLLEQPE RIRQVHLDYF VAGAQCAITA SYQATLQGLA ARGIDPAQAR RLIARSAELA QQARRDYRAA HPQAGTLLVA GSVGPYGAYL ADGSEYRGDY VVAPARMRDF HRPRITALVD AGVDLLAFET QPSSAEIAAL LALLEEFPQS VAWFACTLRD PTHLSDGTPL RETVALLDGH PQVVALGVNC IAPALAAAAL EHLSTLTRLP LVVYPNSGER YDAGDKRWKA DGAVACALVE HIDRWRAAGA RLIGGCCRTT PQQIAQLARC LAMPHG // ID D2UDY2_XANAP Unreviewed; 380 AA. AC D2UDY2; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 27-MAY-2015, entry version 34. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CBA16262.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CBA16262.1}; GN OrderedLocusNames=XALc_1766 {ECO:0000313|EMBL:CBA16262.1}; OS Xanthomonas albilineans (strain GPE PC73 / CFBP 7063). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=380358 {ECO:0000313|EMBL:CBA16262.1, ECO:0000313|Proteomes:UP000001890}; RN [1] {ECO:0000313|EMBL:CBA16262.1, ECO:0000313|Proteomes:UP000001890} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GPE PC73 / CFBP 7063 {ECO:0000313|Proteomes:UP000001890}; 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 ----------------------------------------------------------------------- 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; CBA16262.1; -; Genomic_DNA. DR RefSeq; WP_012916262.1; NC_013722.1. DR EnsemblBacteria; CBA16262; CBA16262; XALC_1766. DR KEGG; xal:XALc_1766; -. DR PATRIC; 32545985; VBIXanAlb89132_1727. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR BioCyc; XALB29447:GJN1-1763-MONOMER; -. DR BioCyc; XALB380358:GLMQ-1763-MONOMER; -. DR Proteomes; UP000001890; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001890}; KW Methyltransferase {ECO:0000313|EMBL:CBA16262.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001890}; KW Transferase {ECO:0000313|EMBL:CBA16262.1}. SQ SEQUENCE 380 AA; 40477 MW; B8AFC419705EBA20 CRC64; MTTVTSPQSP GQPWLHPQRA QALLQALSER ILIIDGAMGT MIQRHGLQEA DYRGDRFAAG YDSAQPPHVH GPGCDHAMHG HDLKGNNDLL LLTRPEVIAE IHSAYLEAGA DLLETNTFNA TAISQADYHL EHLVYELNKA GARVARDCCD AVEAQQARAG GPDKPRFVIG VLGPTSRTAS ISPDVNDPGY RNTSFDELRA TYREAIDGLI DGGADTLMVE TIFDTLNAKA ALYAIEEVFD ARGGRLPVMI SGTITDASGR TLSGQTAEAF YASVAHGRPL SVGLNCALGA KDLRPHVETL ARIADGYVST HPNAGLPNAF GEYDETPEEM AATLKEFAEA GLLNLVGGCC GTTPAHIRAI AEAVRGLRPR VPLAAQRQAA // ID D2UYB1_NAEGR Unreviewed; 1254 AA. AC D2UYB1; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 01-APR-2015, entry version 37. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|EMBL:EFC50443.1}; GN ORFNames=NAEGRDRAFT_34723 {ECO:0000313|EMBL:EFC50443.1}; OS Naegleria gruberi (Amoeba). OC Eukaryota; Heterolobosea; Schizopyrenida; Vahlkampfiidae; Naegleria. OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671}; RN [1] {ECO:0000313|EMBL:EFC50443.1, ECO:0000313|Proteomes:UP000006671} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC50443.1, RC ECO:0000313|Proteomes:UP000006671}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG738845; EFC50443.1; -; Genomic_DNA. DR InParanoid; D2UYB1; -. DR OMA; DYNSIMV; -. DR Proteomes; UP000006671; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006671}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFC50443.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006671}; KW Transferase {ECO:0000313|EMBL:EFC50443.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 246 246 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 774 774 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1254 AA; 140483 MW; C2C573F6DF5ADC8F CRC64; MVTRKELEEI FKERILIIDG AMGTMIQKYK LSEADFRGEE FKDWNCDLKG NNDMLCITRP EIIVEIHEKY LEAGADIIET NTFSSTVISQ ADYNAQSLAY RLNFCAAQCA KKAATKYTQL TPEKPRFVAG ALGPTNKTGS ISPSVEDPGF RNISFDELYE AYFEQVRGLV DGGADILLIE TIFDTLNAKA AAFACMDYLE KFNIDMPIII SGTITDQTGR TLSGQTTEAF YISMMHSNML CMGLNCALGT VQMKPFVKAL SNIAECFTHA YPNAGLPDEM GQYRQTPEEM ARQVKDFLDE KLVNMIGGCC GTTPDHIRAL AQLAAQYKPN QIRKPQEPTH DMKLSGLEPM IYSKNSNFIN VGERCNVAGS IRFKKLIMEN KFEDALSIAR NQVEAGAQVI DVNMDEGLLD SKNVMKKFLY LIMSEPEISK IPIMVDSSKF EVVEQGLKCI QGKCIVNSLS LKEGEEDFIA KAKKVKKYGA AVVVMAFDEQ GQAAECARKV EICTRAYKIL TEKVGFPPED IIFDPNILTI ATGIEEHNNY GVEFINTIKI IKETLPYAKV SGGVSNLSFS FRGLTLVRES MHSAFLYHAI KAGMDMGIVN AGALPIYDEI TPKILQLCED AILNRNENAT ENLLSFASEL REKQAHGEDI EGPKQKEVLA WRTGSVQERL KHALIKGIVD FIDSDVEEAR QNLPSPLSVI EGPLMNGMNV VGDLFGAGKM FLPQVIKSAR VMKKAVKYLI PYLEKDKEEK RLRGEATSSS AGRILLATVK GDVHDIGKNI VGVVLACNNF EVIDLGVMIP PDVIVREAKE KNVDIVGLSG LITPSLDEMA TVAKEMQKGG LTCPLLIGGA TTSRTHTAVK ICPQYDQPCI HVLDASRSVV VASSLLDNRL REEYMEEINE LYEELREEHY DSLLERKFEN IQHARQSRLA IDWEKQPPAK SPTFLGEKVL DNFPLDQLVS HIDWSPFFSV WQIKGKYPHR GYPKIFNDPD VGEEAKKLFD NATKMLKSII EEKKLVARGI VGFYPANTND SKSLDDIEIY DPTCPEEKKQ IGTFYGLRQQ AEKENDEEPF MCISDFIAPK TTGLNDYIGQ FAVSIFGAEE LAAKYQEDDD DYSSIMVKAL ADRLAEAFAE LLHELVRKDY WGYSPEEKLD TEDLLRVKYQ GIRPAPGYPS QPDHTEKETM WRIGQITEKT GIKLIEESLA MWPPASVSGL YFAHPEAKYF AVGKISKDQV EDYMKRKEWA DMDYAEKKLS TMLF // ID D2VNT9_NAEGR Unreviewed; 342 AA. AC D2VNT9; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 07-JAN-2015, entry version 23. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFC41473.1}; GN ORFNames=NAEGRDRAFT_80673 {ECO:0000313|EMBL:EFC41473.1}; OS Naegleria gruberi (Amoeba). OC Eukaryota; Heterolobosea; Schizopyrenida; Vahlkampfiidae; Naegleria. OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671}; RN [1] {ECO:0000313|EMBL:EFC41473.1, ECO:0000313|Proteomes:UP000006671} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC41473.1, RC ECO:0000313|Proteomes:UP000006671}; 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; GG738885; EFC41473.1; -; Genomic_DNA. DR InParanoid; D2VNT9; -. DR Proteomes; UP000006671; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 2. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006671}; KW Methyltransferase {ECO:0000313|EMBL:EFC41473.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006671}; KW Transferase {ECO:0000313|EMBL:EFC41473.1}. SQ SEQUENCE 342 AA; 38839 MW; 82190710ED98BAFC CRC64; MTELGLELNG SLWGANYLLE NPKAIAKVHS DYVHEGLCDI CTSSSYQISQ EGLAADHVSM KEEERIELAS RMFRDSVQIA RKVVREKEKL VAASVSCFGA SISNLLGEAK EYFGDYLDED ADSNSGHYVH KFVKQLSEKL GETLEKSGME QVIYDFHYPR VRELILAEPD FILLETMPVL KEVEILCDRV IPDILKELNK KGIKVMISFY CKDGLHTGHG ESIEKCVEYV NQDRFNPSLF EIFAVGANCI SPSIVPILIE NIHTHLRKDI SIILYPNSGE IYDNLTKSWS IPQGGLDWLY DRDFIPFIKK WSENHPERKL VIGGCCRTNP RNIKKLANSL NH // ID D2W5I3_NAEGR Unreviewed; 661 AA. AC D2W5I3; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 07-JAN-2015, entry version 24. DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EFC35669.1}; DE Flags: Fragment; GN ORFNames=NAEGRDRAFT_60084 {ECO:0000313|EMBL:EFC35669.1}; OS Naegleria gruberi (Amoeba). OC Eukaryota; Heterolobosea; Schizopyrenida; Vahlkampfiidae; Naegleria. OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671}; RN [1] {ECO:0000313|EMBL:EFC35669.1, ECO:0000313|Proteomes:UP000006671} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC35669.1, RC ECO:0000313|Proteomes:UP000006671}; 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; GG739079; EFC35669.1; -; Genomic_DNA. DR InParanoid; D2W5I3; -. DR Proteomes; UP000006671; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 2. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006671}; KW Reference proteome {ECO:0000313|Proteomes:UP000006671}. FT NON_TER 661 661 {ECO:0000313|EMBL:EFC35669.1}. SQ SEQUENCE 661 AA; 75242 MW; B488C65693F02FD3 CRC64; MLVAPEVITP DNSELLSFQS LKIYRSQYNI ALKVVEKWLQ SSLAGYKETK FKSINLCIIG PTFTALRNQT SDDFELFKEA IGLSAFTSVI VNSDNVGKEK TNSFIERFDN ENELHLLVHD EAHWGIAKNS TINDFLKQIN EKRKKVLQKG KKLYLGILLV TATANVLLFG NYDFRIENNV DWNHLRTTSP ERYGTPSYRS IEELEFKQDK IIGNTNTMKE ASNAVVKEYE EAINKINESK TTSAEIIRNI YLSEEPVMGV IRLKSKDHAD MLSSSLINYL KNRSKKVYVV KLTDNTPNIS KQLEQQGYGP NSMNTLIELD KLSVILVLVD RKILILDGGI STYMTELGLE LNGSLWGANY LLENPKAIAK VHSDYVHEGL CDICTSSSYQ ISQEGLAADH VSMKEEERIE LASRMFRDSV QIARKVVREK EKLVAASVSC FGASISNLLG EAKEYFGDYL DKDVDSNSGH YVHKFVKQLS EKLGETLEKS GMEQVIYDFH YPRVRELILA EPDFILLETM PVLKEVEILC DRVIPDILKE LNKKGIKVMI SFYCKDGLHT GHGESIEKCV EYVNQDRFNP SLFEIFAVGA NCISPSIVPI LIENIHTHLR KDISIILYPN SGEIYDNLTK SWSIPQGGLD WLYDRDFIPF IKKWSENHPE R // ID D2YHU0_VIBMI Unreviewed; 1226 AA. AC D2YHU0; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEW05613.1}; GN Name=metH {ECO:0000313|EMBL:EEW05613.1}; GN ORFNames=VMB_30870 {ECO:0000313|EMBL:EEW05613.1}; OS Vibrio mimicus VM603. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=671074 {ECO:0000313|EMBL:EEW05613.1, ECO:0000313|Proteomes:UP000004827}; RN [1] {ECO:0000313|EMBL:EEW05613.1, ECO:0000313|Proteomes:UP000004827} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VM603 {ECO:0000313|EMBL:EEW05613.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEW05613.1}. 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; ACYU01000169; EEW05613.1; -; Genomic_DNA. DR RefSeq; WP_000510780.1; NZ_ACYU01000169.1. DR EnsemblBacteria; EEW05613; EEW05613; VMB_30870. DR PATRIC; 28330029; VBIVibMim145354_3227. DR Proteomes; UP000004827; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000004827}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEW05613.1}; KW Transferase {ECO:0000313|EMBL:EEW05613.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1226 AA; 135933 MW; C5C3BBCA31CFCEA0 CRC64; MGIEVREQLE QQLKQRILLI DGGMGTMIQS YKLQEEDYRG ARFADWHCDL KGNNDLLVLT QPQIIKDIHS AYLEAGADIL ETNTFNSTTI AMADYDMQLL SDEINFAAAK LAREVADEWT AKDPSRPRYV AGVLGPTNRT CSISPDVNDP GFRNVTFDQL VQAYSESTRA LIKGGSDLIL IETIFDTLNA KACAFAVDSV FEELGISLPV MISGTITDAS GRTLSGQTTE AFYNALRHVR PISFGLNCAL GPDELRQYVE ELSRISECYV SAHPNAGLPN AFGEYDLSAE DMAEHIAEWA QAGFLNLVGG CCGTTPEHIA AMAKAVEGVK PRALPELKVE CRLSGLEPLN IGPETLFVNV GERTNVTGSA RFKRLIKEEQ YDEALDVARD QVENGAQIID INMDEGMLDA EACMVRFLNL CASEPEISKV PVMVDSSKWE VIEAGLKCIQ GKGIVNSISL KEGKEKFIAQ AKLVRRYGAA VIVMAFDEVG QADTRERKLE ICSRAYHILV DEVGFPPEDI IFDPNIFAVA TGIDEHNNYA LDFINAVADI KRELPHAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK HGMDMGIVNA GQLEIYDNVP LKLREAVEDV ILNRRHDGTE RLLEIAEAYR ENSVGKEEDA SALEWRTWPV AKRLEHALVK GITEFIVQDT EEARQQASKP LEVIEGPLMD GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AYLEPFINAQ KSGSTSNGKI LLATVKGDVH DIGKNIVGVV LQCNNFEIID LGVMVPCEQI LKVAREENVD IIGLSGLITP SLDEMVHVAK EMERQGFELP LLIGGATTSK AHTAVKIEQN YHAPVVYVNN ASRAVGVCTS LLSDELRPGF IERLDLDYER TRDQHARKTP KSRPVTLEQA RANKAAIDWA SYTPPAPAKP GVHVFENIPL ATLRPYIDWT PFFMTWSLMG KYPAILEHEE VGEEAKRLFH DANALLDKVE REGLLKASGM CALFPAASVG DDIEVYSDES RMQVAHMLYN LRQQTEKPKG ANYCLSDYVA PKESGKRDWI GAFAVTGGIG ERALADAYKA QGDDYNAIMI QAVADRLAEA FAEYLHEKMR KEIWGYASDE NLSNDELIRE RYQGIRPAPG YPACPEHTEK ATLWQMLNVE ESIGMSLTTS YAMWPGASVS GWYFSHPDSR YFAVAQIQQD QLHSYAERKG WSLEEAEKWL APNLDA // ID D2YUG0_VIBMI Unreviewed; 1227 AA. AC D2YUG0; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEW09055.1}; GN Name=metH {ECO:0000313|EMBL:EEW09055.1}; GN ORFNames=VMD_33940 {ECO:0000313|EMBL:EEW09055.1}; OS Vibrio mimicus VM573. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=671076 {ECO:0000313|EMBL:EEW09055.1, ECO:0000313|Proteomes:UP000003714}; RN [1] {ECO:0000313|EMBL:EEW09055.1, ECO:0000313|Proteomes:UP000003714} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VM573 {ECO:0000313|EMBL:EEW09055.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEW09055.1}. 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; ACYV01000038; EEW09055.1; -; Genomic_DNA. DR RefSeq; WP_000510783.1; NZ_ACYV01000038.1. DR EnsemblBacteria; EEW09055; EEW09055; VMD_33940. DR PATRIC; 30118799; VBIVibMim144731_3690. DR Proteomes; UP000003714; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000003714}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEW09055.1}; KW Transferase {ECO:0000313|EMBL:EEW09055.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135974 MW; CBCA214B02E07949 CRC64; MGIEVRQQLE QQLKQRILLI DGGMGTMIQS YKLQEEDYRG ARFADWHCDL KGNNDLLVLT QPQIIKDIHS AYLEAGADIL ETNTFNSTTI AMADYDMQLL SDEINFAAAK LAREVADEWT AKDPSRPRYV AGVLGPTNRT CSLSPDVNDP GFRNVTFDQL VQAYSESTRA LIKGGSDLIL IETIFDTLNA KACAFAVDSV FEELGISLPV MISGTITDAS GRTLSGQTTE AFYNALRHVR PISFGLNCAL GPDELRQYVE ELSRISECYV SAHPNAGLPN AFGEYDLSAE DMAEHIAEWA QAGFLNLVGG CCGTTPEHIA AMAKAVDGVK PRALPELKVE CRLSGLEPLN IGPETLFVNV GERTNVTGSA RFKRLIKEEQ YDEALDVARE QVENGAQIID INMDEGMLDA EACMVRFLNL CASEPEISKV PVMVDSSKWE VIEAGLKCIQ GKGIVNSISL KEGKEKFIAQ AKLVRRYGAA VIVMAFDEVG QADTRERKLE ICSRAYHILV DEVGFPPEDI IFDPNIFAVA TGIDEHNNYA LDFINAVADI KRELPHAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK HGMDMGIVNA GQLEIYDNVP LKLREAVEDV ILNRRNDGTE RLLEIAEAYR ENSVGKEEDA SALEWRTWPV AKRLEHALVK GITEFIVQDT EEARQQASKP LEVIEGPLMD GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AYLEPFINAQ KSGSTSNGKI LLATVKGDVH DIGKNIVGVV LQCNNFEIID LGVPCVPCEQ ILKVAREENV DIIGLSGLIT PSLDEMVHVA KEMERQGFEL PLLIGGATTS KAHTAVKIEQ NYHAPVVYVN NASRAVGVCT SLLSDELRPG FIERLDLDYE RTRDQHARKT PKSRPVTLEQ ARANKAAIDW VSYTPPVPAK PGVHVFENIA LATLRPYIDW TPFFMTWSLM GKYPAILEHE EVGEEAKRLF HDANVLLDKV EREGLLKASG MCALFPAASV GDDIEVYSDE SRTQVAHVLY NLRQQTEKPK GANYCLSDYV APKESGKRDW IGAFAVTGGI GERALADAYK AQGDDYNAIM IQAVADRLAE AFAEYLHEKM RKEIWGYASD ENLSNDELIR ERYQGIRPAP GYPACPEHTE KATLWQMLNV EESIGMSLTT SYAMWPGASV SGWYFSHPDS RYFAVAQIQQ DQLHSYAERK GWSLEEAEKW LAPNLDA // ID D2ZFT6_9ENTR Unreviewed; 310 AA. AC D2ZFT6; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFC55755.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EFC55755.1}; GN Name=mmuM {ECO:0000313|EMBL:EFC55755.1}; GN ORFNames=ENTCAN_07350 {ECO:0000313|EMBL:EFC55755.1}; OS Enterobacter cancerogenus ATCC 35316. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex. OX NCBI_TaxID=500639 {ECO:0000313|EMBL:EFC55755.1}; RN [1] {ECO:0000313|EMBL:EFC55755.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35316 {ECO:0000313|EMBL:EFC55755.1}; 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., 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFC55755.1}. 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; ABWM02000017; EFC55755.1; -; Genomic_DNA. DR RefSeq; WP_006176817.1; NZ_GG704864.1. DR EnsemblBacteria; EFC55755; EFC55755; ENTCAN_07350. DR PATRIC; 29279413; VBIEntCan670_2825. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFC55755.1}; KW Transferase {ECO:0000313|EMBL:EFC55755.1}. SQ SEQUENCE 310 AA; 33545 MW; EFFABA9A0C0D18E2 CRC64; MSQNNPLTAL LETQPYVVLD GAMATELEAR GCNLADSLWS AKVLVENPEL IREVHLDYYR AGAQVAITAS YQATPAGFAA RGLDEAQSRV LIGKSVELAR KAREAYLAEN ANAGTLLVAG SVGPYGAYLA DGSEYRGDYV RSAEEFTRFH RPRVEALLDA GADLLACETL PSFAEIKALA SLLAEYPRAR AWFSFTLRDS EHLSDGTALR EVVSALSHYP QIVALGINCI ALENTTAALK HLNSLTALPL VVYPNSGEHY DAVTKTWHHH GEACETLAGY LPQWLEAGAK LIGGCCRTTP KDIAELNAQR // ID D2ZHQ8_9ENTR Unreviewed; 1227 AA. AC D2ZHQ8; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFC55323.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFC55323.1}; GN Name=metH {ECO:0000313|EMBL:EFC55323.1}; GN ORFNames=ENTCAN_08038 {ECO:0000313|EMBL:EFC55323.1}; OS Enterobacter cancerogenus ATCC 35316. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex. OX NCBI_TaxID=500639 {ECO:0000313|EMBL:EFC55323.1}; RN [1] {ECO:0000313|EMBL:EFC55323.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35316 {ECO:0000313|EMBL:EFC55323.1}; 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., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFC55323.1}. 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; ABWM02000022; EFC55323.1; -; Genomic_DNA. DR RefSeq; WP_006177530.1; NZ_GG704864.1. DR EnsemblBacteria; EFC55323; EFC55323; ENTCAN_08038. DR PATRIC; 29280665; VBIEntCan670_2505. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFC55323.1}; KW Transferase {ECO:0000313|EMBL:EFC55323.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135673 MW; E6AE84B537F2A9AE CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQGY RLSEDDFRGE RFADWPCDLK GNNDLLVLSK PQVIADIHNA YFEAGADIVE TNTFNSTTIA MADYQMESLS AEINFEATKL ARACADEWTA RTPDKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV VAYRESTKAL VEGGSDLILI ETVFDTLNAK AAIYAVKAEF EALGVDLPIM ISGTITDASG RTLSGQTTEA FYNSLRHADA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MASQIREWAE SGFLNIVGGC CGTTPAHIAA MSNAVAGLPP RKLPELPVAC RLSGLEPLTI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VESGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVESFIHHA KQVRRYGAAV VVMAFDEVGQ ADTRERKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDATER MLDLAEKYRG SKSDEAVNVQ QAEWRAWDVK KRLEYSLVKG ITEFIEFDTE EARQQAARPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLAPYIEASK EKGSSNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIIDL GVMVPADKIL KTAREVNADL IGLSGLITPS LDEMVFVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVSAL LSDTQRDEFV ARTRKEYETV RIQHGRKKPH TPPVSLQAAR ENDLAFDWSA YTPPVAHRLG VQDVTASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG EEAKRLFNDA NDMLDRLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVLAVSHHLR QQTEKVGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALAEAFDAQH DDYNKIMIKA IADRLAEAFA EYLHERVRKV HWGYAANENL SNEELIRENY QGIRPAPGYP ACPEHTEKGT IWKLLDVEAH TGMKLTESFA MWPGASVSGW YFSHPDSKYF AVAQLQRDQV EDYALRKGMS VSEVERWLAP NLGYDAD // ID D3A227_NEISU Unreviewed; 307 AA. AC D3A227; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFC53265.1}; GN ORFNames=NEISUBOT_03267 {ECO:0000313|EMBL:EFC53265.1}; OS Neisseria subflava NJ9703. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=546268 {ECO:0000313|EMBL:EFC53265.1}; RN [1] {ECO:0000313|EMBL:EFC53265.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NJ9703 {ECO:0000313|EMBL:EFC53265.1}; 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., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFC53265.1}. 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; ACEO02000001; EFC53265.1; -; Genomic_DNA. DR RefSeq; WP_004519018.1; NZ_ACEO02000001.1. DR EnsemblBacteria; EFC53265; EFC53265; NEISUBOT_03267. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EFC53265.1}; KW Transferase {ECO:0000313|EMBL:EFC53265.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 216 216 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 307 AA; 33711 MW; BA89A6E79E8BC9EA CRC64; MAILKIHHWR SIMTVTILDG GMGRELHRRG APFRQPEWSA LALMETPEIV RETHLDFLRA GAQVITTNSY ALVPFHIGQE RFDAQAAEWA RLSGRLAREA VEQSGTTAKV AASLPPLFGS YRPDLFDKQV APALARPLIS GLMPFADIWL AETVSSLEEA RFWRSSLPDD GKPFWVSFTL EDTMPHDVPV LRSGETVHEA ADFAVEIGAA AMLFNCSQPE VMAEALKVAH EAQGRLKLGV YANAFEPVQG QMNEANDGLD PIRSDATPKN YLAWARQWAD LGAEIIGGCC GIAPEHIRAL AQGFKAV // ID D3AMZ6_9FIRM Unreviewed; 305 AA. AC D3AMZ6; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFC96809.1}; GN ORFNames=CLOSTHATH_04996 {ECO:0000313|EMBL:EFC96809.1}; OS [Clostridium] hathewayi DSM 13479. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=566550 {ECO:0000313|EMBL:EFC96809.1}; RN [1] {ECO:0000313|EMBL:EFC96809.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 13479 {ECO:0000313|EMBL:EFC96809.1}; 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., 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFC96809.1}. 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; ACIO01000495; EFC96809.1; -; Genomic_DNA. DR RefSeq; WP_006775426.1; NZ_GG667727.1. DR EnsemblBacteria; EFC96809; EFC96809; CLOSTHATH_04996. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFC96809.1}; KW Transferase {ECO:0000313|EMBL:EFC96809.1}. SQ SEQUENCE 305 AA; 34333 MW; C742868F77E23E9D CRC64; MDFKTSFYHH QAFLMEGALG ERLKREYGLM PDKSLALAKH VYSLKGRNAL KELWLEYGAI ADRYQLPFLA VTPTRRVNQE RVRSRSDEGV IGDNVSFLQR IKRECRAEMY AGGMIGSRGD AYTGRGALGE NESRMFHRWE LDQFSEAGVD FLYAALIPTL PEAAGMAWAM AETGIPYIVS FTIQRSGTLI DGTPICDAIT YIDNRVSDPP VCYMTNCVHP RIAYEALSQP FQDKELLKRR FLGIQANTAQ LSYEELDNAA ELVTSEPEAL AEDMMALKDI CCLKIFGGCC GTDGRHMREI ARRLD // ID D3ATI6_9FIRM Unreviewed; 725 AA. AC D3ATI6; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFC94871.1}; DE Flags: Fragment; GN ORFNames=CLOSTHATH_06945 {ECO:0000313|EMBL:EFC94871.1}; OS [Clostridium] hathewayi DSM 13479. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=566550 {ECO:0000313|EMBL:EFC94871.1}; RN [1] {ECO:0000313|EMBL:EFC94871.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 13479 {ECO:0000313|EMBL:EFC94871.1}; 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., 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFC94871.1}. 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; ACIO01000901; EFC94871.1; -; Genomic_DNA. DR RefSeq; WP_006777349.1; NZ_GG667928.1. DR EnsemblBacteria; EFC94871; EFC94871; CLOSTHATH_06945. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFC94871.1}; KW Transferase {ECO:0000313|EMBL:EFC94871.1}. FT NON_TER 725 725 {ECO:0000313|EMBL:EFC94871.1}. SQ SEQUENCE 725 AA; 78229 MW; 43C191E85B2AF8B2 CRC64; MFENRLRVQE RIRDMTELME EIRKRIVFFD GGTGSLLQAN GLKPGELPET WNILHPEIVT KLHYDYLEAG ADIVKTNTFG ANGLKFNDAG EYGLDEIVAA AMENAKKAVS KAGDKGYIAL DIGPTGKLLK PLGDLGFEEA YRLFSDVVAI GAREGADLVL IETMSDSYEV KAAVLAAKEN CNLPVFATMI FDSKGKLLTG GTVESTVALL EGLGVDALGI NCGLGPVQMK GILADIMKAA SVPVIVNPNA GLPRSEGGRT FYDIDADEFA GTMREIVEMG ACVVGGCCGT TPEHIRKTIA LCKDQPARMP EKKNRTVISS YAQAVEIDKN PVLIGERINP TGKSKFKQAL RDHNLEYILR EGVAQQDNGA HVLDVNVGLP EIDEAAMMEE VVMELQSIID LPLQIDTSNI QAMERALRVY NGKPLINSVN GKQEVMEAVF PLVKRYGGVV VALALDEDGI PETADGRLKV AEKIYAKASE YGIERKDIVI DALCMTVSSD SRGAITTLET VRRVRDELGG KTILGVSNIS FGLPQREIVN AAFFTMALQN GLNAAIINPN SEAMMRSYYS FRVLADLDPQ CSEYISVYSG QVATLGQTVR QGGGSGKADG SGSAMSASLA ESIERGLKES AHQAVTELLK TLEPLVIINE EMIPALDRVG KGFEKGTVFL PQLLMSAEAA KAAFEVIKEQ LAKSGREEEK KGKIILATVK GDIHDIGKNI VKVLL // ID D3BM55_POLPA Unreviewed; 1231 AA. AC D3BM55; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 01-APR-2015, entry version 30. DE SubName: Full=Cobalamin-dependent methionine synthase {ECO:0000313|EMBL:EFA77656.1}; GN Name=mtr {ECO:0000313|EMBL:EFA77656.1}; GN ORFNames=PPL_12264 {ECO:0000313|EMBL:EFA77656.1}; OS Polysphondylium pallidum (Cellular slime mold). OC Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; Polysphondylium. OX NCBI_TaxID=13642 {ECO:0000313|Proteomes:UP000001396}; RN [1] {ECO:0000313|Proteomes:UP000001396} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PN500 {ECO:0000313|Proteomes:UP000001396}; RA Gloeckner G., Schaap P., Noegel A.A., Felder M., Eichinger L., RA Heidel A.J., Platzer M.; RT "Living fossils from the dawn of multicellularity."; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFA77656.1}. 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; ADBJ01000042; EFA77656.1; -; Genomic_DNA. DR ProteinModelPortal; D3BM55; -. DR InParanoid; D3BM55; -. DR Proteomes; UP000001396; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001396}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001396}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 230 230 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 751 751 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1231 AA; 136418 MW; 89536E0CE1A8E49C CRC64; MILDGAMGTE IQKFKLKDAD YRGQEFVDFP HELGGNNDLL VLTQPHIIKE IHKKYLEAGA DIIETNTFNG NIFSQADYKM EHLVKRINRE AARIAKEAAQ EVMAADPSKP RFVAGAVGPT NKTASISPSV ERPEARNVLF DELVDGYFEQ VEALVEGGID ILLVETVFDS LNCKAALFAI ENFFKNHPRI PVFVSGTIVD KSGRTLSGQT GEAFYTSTAH ADPMVFGLNC ALGANEMRPF LQNISKCAEC FVLCYPNAGL PNTFGGYDET PEMMAVQIQE FAESGLLNIV GGCCGTSPDH IREFARVTKG VQPRQIPSLP PYTTLSGLEP LAFTPTLNFV NVGERCNVSG SRRFANLIKA NKYEEAISVA RQQVEAGAQI IDINMDEGMI DAVAAIQKFL FFIGSEPEIS KVPIMLDSSN FAVVEAGLKC VQGKCIVNSI SLKVGEELFM EQARICKQYG ASVVVMAFDE QGQATSKEEK VRICYRSYKI LVERVGFKPQ DIIFDPNILT IATGLEEHNN YGVEFIEATR EIKRLMPLTK VSGGVSNLSF SFRGNEPLRE AMHSAFLFHA IKAGMDMGIV NAGQLPIYDD IEKDLLTMVE DAILNRTNDA TERLLEHAQK NAKTEKATTE VEEWRTKDVS SRITHALVKG ITNFITEDTE EARNTLPSSL SVIEGPLMSG MNVVGDLFGA GKMFLPQVIK SARVMKKAVA YLIPFMEEEK AAKRALNADA VVEEAENAGV CVLATVKGDV HDIGKNIVGV VLGCNNYKVI DLGVMCPCEK ILAAAIEHKA DIVGLSGLIT PSLDEMIYVA SEMERMKFKV PLLIGGATTS QIHTAVKIAP HYSQPTVHVL DASRSVTVVS SLLDVNNKEN FADDVATQYQ ELREKHYASL KDRKYMTLEK ARALKPKTEW KSLTTPTVPS FLGQKIIKDY PLEKLLAKID WNPFFATWQL RGKYPNRGYP RIFNDATVGA EAQKLFDDAQ AMLKEIIEKK LLNARGVIGF YPAASQNEDV ILYTDESRTT PLATLYGLRQ QSEKEVDEPY ISMGDFVAPH DSGVNDYIGL FALSSGFGLE EMVERYKQEN DDYSSIMAKA LADRLAEALA EHVHEDVRKE HWGYEKNEQL TAEDLFKVKY RGIRPAPGYP VQPDHTEMKT IWKVMNVQET TGIELTDHMA MLPGAAVCGI YFGNENSKYF SVGKISKDQV ESYATRKGIP IEEAERWLST ILSYDRLPLA K // ID D3DA68_9ACTO Unreviewed; 653 AA. AC D3DA68; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFC80204.1}; DE Flags: Fragment; GN ORFNames=FrEUN1fDRAFT_6690 {ECO:0000313|EMBL:EFC80204.1}; OS Frankia sp. EUN1f. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Frankineae; Frankiaceae; Frankia. OX NCBI_TaxID=102897 {ECO:0000313|EMBL:EFC80204.1}; RN [1] {ECO:0000313|EMBL:EFC80204.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=EUN1f {ECO:0000313|EMBL:EFC80204.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFC80204.1}. 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; ADGX01000169; EFC80204.1; -; Genomic_DNA. DR RefSeq; WP_006544554.1; NZ_ADGX01000169.1. DR EnsemblBacteria; EFC80204; EFC80204; FrEUN1fDRAFT_6690. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFC80204.1}; KW Transferase {ECO:0000313|EMBL:EFC80204.1}. FT NON_TER 653 653 {ECO:0000313|EMBL:EFC80204.1}. SQ SEQUENCE 653 AA; 69095 MW; 3396FEEB3AC3B1B5 CRC64; MAVSGTLDNL VSGASADSPD ADTSGASGAP GARAVTAGER ALRELLGQRV AVLDGAWGTM LQNAGLTPAD YRTERFADHP KDVTGDPDLL NLTRPDIILD VHRQYLAAGA DITTTNTFTA TSIGQADYGL ESLVREMNVQ GARLAREAAD EAAQKTGTRR FVAGSIGPLN VTLSLSPRVE DPAYRAVTFD QVKASYAEQI AALAEGGVDL LLIETIFDTL NAKAAIAAAR EVAPQLPLWI SVTIVDMSGR TLSGQTVEAF WSSIAHAEPL VVGVNCSLGA EEMRPHVADL ARLAGTFTAC HPNAGLPNAF GGYDQTPEEA GRLIGGFASE GLVNVVGGCC GTTPAHIARI AESVRGTAPR ALPELPATTR FSGLEPFEIG PDTGFVMIGE RTNVTGSARF RRLIEADDYQ AAIDVALEQV RGGANLLDVN MDADLLDSER AMTTFLNLLA TEPEAARLPI MIDSSRWSVL EAGLRCVQGK GVVNSISLKE GEEPFLAQAR RIRDFGAGVV VMAFDEQGQA DTTERKVAIC ARAYDLLTQK VGFPATDIIF DPNVLAVATG IAEHNGYAKA FVDALPLIKQ RCPGVRISGG ISNLSFSFRG NDVVREAMHS AFLLHAVRAG LDMGIVNAGQ LAVYADIPAD LLELVEDVLF DRR // ID D3E5S5_GEOS4 Unreviewed; 623 AA. AC D3E5S5; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 27-MAY-2015, entry version 35. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=GYMC10_1943 {ECO:0000313|EMBL:ACX64225.1}; OS Geobacillus sp. (strain Y412MC10). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=481743 {ECO:0000313|EMBL:ACX64225.1, ECO:0000313|Proteomes:UP000002381}; RN [1] {ECO:0000313|Proteomes:UP000002381} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Y412MC10 {ECO:0000313|Proteomes:UP000002381}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ACX64225.1; -; Genomic_DNA. DR RefSeq; WP_015734328.1; NC_013406.1. DR RefSeq; YP_003242032.1; NC_013406.1. DR ProteinModelPortal; D3E5S5; -. DR EnsemblBacteria; ACX64225; ACX64225; GYMC10_1943. DR KEGG; gym:GYMC10_1943; -. DR PATRIC; 32152489; VBIGeoSp56627_1956. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; PSP481743:GH8K-1990-MONOMER; -. DR Proteomes; UP000002381; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002381}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ACX64225.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000002381}; KW Transferase {ECO:0000313|EMBL:ACX64225.1}. SQ SEQUENCE 623 AA; 68426 MW; C1E5540B4F4CB6F6 CRC64; MKPNLRQAWE NQVLVGDGAM GTYLYQKGFP VGISYEELNL TSPEVIGNVH RQYVEAGAQV IETNTFSANY DKLSKYGLEA RVGEINRAGV RIAREAAGDQ GYVVGAVGSI RAGKRSNIST SELKRYFEEQ LSVLISEGVD GILLETFYDV DEMQLALAQA RMLSDLPVIC QFAVEDIART LDGFTMPDAY RILSHEGADV IGFNCRTGPN GIMRALETLN GIMNLPASVY PNAGIADYVD GEYRYGASPE YFGKTALEFA DRGARIIGGC CGTTPEHIAE ISSALSGYVP SPLPAVEEAE INRIVIHETA QEQFYERSGE PTIVDIVKER HTVIVELDPP RDLDITKFMK GAEALKKAGA DALTLADNSL AVTRMSNMAL GHLVQARTGL RPLIHIACRD RNLIGTQSHM MGFDALGIDH VLAVTGDPAR FGDLPDSSSV YDMTSFEIIR MIKQLNDGIA FSGKPLKQKA KFVVGAAFNP NVRHLDKAVA RLEKKIASGA DYVMTQPVYD PELMVRLREA TAHLDIPIFI GIMPLASGRN AEYLHNEVPG IQLSDEVRSR MAGLEGEAGR AMGVKIGKEL LDVATEHFNG IYLMTPFMFY EMSVQLMEYV WEKSGRRLTP LFH // ID D3E8S3_GEOS4 Unreviewed; 1146 AA. AC D3E8S3; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 27-MAY-2015, entry version 42. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ACX64650.1}; GN OrderedLocusNames=GYMC10_2372 {ECO:0000313|EMBL:ACX64650.1}; OS Geobacillus sp. (strain Y412MC10). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=481743 {ECO:0000313|EMBL:ACX64650.1, ECO:0000313|Proteomes:UP000002381}; RN [1] {ECO:0000313|Proteomes:UP000002381} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Y412MC10 {ECO:0000313|Proteomes:UP000002381}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001793; ACX64650.1; -; Genomic_DNA. DR RefSeq; WP_015734674.1; NC_013406.1. DR RefSeq; YP_003242457.1; NC_013406.1. DR EnsemblBacteria; ACX64650; ACX64650; GYMC10_2372. DR KEGG; gym:GYMC10_2372; -. DR PATRIC; 32153375; VBIGeoSp56627_2399. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PSP481743:GH8K-2419-MONOMER; -. DR Proteomes; UP000002381; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002381}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002381}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 722 722 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1146 AA; 126038 MW; 8266E9A4CDD6A08C CRC64; MNKPSLQEVL KERILILDGA MGTMIQQEDL SAEDFGGPEL DGCNEMLVIH RPDVIQKIHE QYLEAGADLI ETNTFGATSV VLAEYDIPEL AREINLKAAH LARAAVEKYS TPDSPRYVVG AMGPTTKTLS VTGGVTFAEL IESYEEQAVA LIEGGVDALL LETSQDTLNV KAGSIGIRQA FDKTGVTLPI MISGTIEPMG TTLAGQNIEA FYISLEHLNP VSIGLNCATG PEFMRDHIRS LSEMSRSAIS CYPNAGLPDE NGQYHESPES LAQKMGAFAE KGWLNIAGGC CGTTPDHIRA LKQTMDGFTP RPLEGGHLPA LSGIEPVYIE QENRPYMVGE RTNVLGSRKF KRLIVEGKYE EASEIARAQV KNGAHVIDVC VQDPDREEAE DMIQFLELVV KKVKVPLMID TTDPAVIDLA LQYSQGKAII NSINLEDGEE KFEHVTPLVH KYGAAVVVGT IDESGQAIHR DDKLKVAQRS YDLLVNKYGI SPEDIIFDTL VFPVGTGDEQ YIGSAKETIE GIRMIKEAMP KVHTILGISN VSFGLPEAGR EVLNSVYLYE CTKAGLDYAI VNTEKLERYA SIPEEERRLA EDLIYRTNDE TLAAFVAAFR HKKVEKKVKV SNLTLEERLA SYVVEGSKEG LIPDLDEALT KYGALEIING PLMAGMTEVG RLFNNNELIV AEVLQSAEVM KASVAYLESF MEKNESSVKG KIMLATVKGD VHDIGKNLVE IILSNNGYQI INLGIKVPPE QIIEAYRREQ PDAIGLSGLL VKSAQQMVST AQDLKNAGIS VPIMVGGAAL TRKFTKTRIR PEYDGMVLYA KDAMDGLALA NQLSDPVLRT QMAEEIKAEQ EADAAAPQVV KVMPKLSEGL RSKISTEAPV YIPPDMERHV LRNYPISHIL PYINMQMLLG HHLGLKGSVE QLLKANDPKA VSLKETVDGI LEEAVQSGII QAHAMYRFFP AQSRGNDIII YDPKDASKIL HTFTFPRQQV EPYLCLADFL KSVESGVMDY VGFLVVTAGH GVGKLSGEWK DKGDYLRSHA LQSVALETAE GLAERIHHMM RDTWGYPDPA DMTMKQRLGA RYQGIRVSFG YPACPDLEDQ EPLFKLMQPE DIGVHLTEGF MMEPEASVSA MVFSHPEAHY FNVDKA // ID D3F0W9_CONWI Unreviewed; 1189 AA. AC D3F0W9; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 01-APR-2015, entry version 35. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADB50045.1}; GN OrderedLocusNames=Cwoe_1617 {ECO:0000313|EMBL:ADB50045.1}; OS Conexibacter woesei (strain DSM 14684 / JCM 11494 / NBRC 100937 / OS ID131577). OC Bacteria; Actinobacteria; Rubrobacteridae; Solirubrobacterales; OC Conexibacteraceae; Conexibacter. OX NCBI_TaxID=469383 {ECO:0000313|EMBL:ADB50045.1, ECO:0000313|Proteomes:UP000008229}; RN [1] {ECO:0000313|Proteomes:UP000008229} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14684 / JCM 11494 / NBRC 100937 / ID131577 RC {ECO:0000313|Proteomes:UP000008229}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001854; ADB50045.1; -; Genomic_DNA. DR RefSeq; WP_012933096.1; NC_013739.1. DR RefSeq; YP_003393420.1; NC_013739.1. DR ProteinModelPortal; D3F0W9; -. DR EnsemblBacteria; ADB50045; ADB50045; Cwoe_1617. DR KEGG; cwo:Cwoe_1617; -. DR PATRIC; 32045212; VBIConWoe21639_1619. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; CWOE469383:GH82-1629-MONOMER; -. DR Proteomes; UP000008229; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008229}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADB50045.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008229}; KW Transferase {ECO:0000313|EMBL:ADB50045.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 223 223 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 728 728 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1189 AA; 129805 MW; 742E7018C63C0A7B CRC64; MRDYLDAIRS RVVVFDGGMG ATLEQFELTE KDYGGLQGKC HEALILHRPD VIEGVHTTML DAGADVVETD TFQASRLKLE EWGLGEHTLE INRRGAEIAR KAAGEHRYVA GSIGPTGFLP ASDDPTLGNI SFRALVEVFA EQAQGLIEGG ADLLMIETAQ DILEVKASVF GAREAFKTTG RKIPIQVSVS LLPNGGKMLL GTDISAVLTT LTALDVDALG LNCSTGPEDM RDAIRFLGEF SPVPVHCIPN AGLPLQGPDG ETIFPEKPEP LAASLTEFVE RYGVSIVGGC CGTTAAHIRA IADSVKGHPV APRPAAPIPH VSSMIAATPL AQEPRPTIVG ERVNSQGSRK AKELLLADDY DGLLQIAENQ VELGAHVLDL CVALTERQDE DVQMRTLAKR VSLSLPAPIQ VDSTEPEVME AALEQIPGRA IVNSVNLEAG RDKLDRVVPI CLQHGAALIA LTIDEESMAK TAQRKLDVAK RIHGYVCDEH GMAPELLIFD ALTFTLATGS DEFKTSAVET IEGIRLIKAE LPGVLTSLGV SNVSFGFGRA AREVLNSVFL HHCVEAGLDL AMVHPKDVTP YSEIPGNERE LADDLVFNRR DDATQRFIEH FEEKGESAED ESADPTAGME PEEALHFHIL RRKKDGVEDW IDRSVEKIGA VPTLNDVLLP AMKEVGDKFG AGELILPFVL QSAEVMKKAV ARLENYLDRL EGYTKGTVVL ATVFGDVHDI GKSLVNTILT NNGYTVVDLG KQVPVSTILD AAQEHRANAI GLSALLVSTS KQMPLAVQEL HQRELPYPVL IGGAAINRDF GLRILYPHGR ESDDVYEPGV FYCKDAFEGL AKMDEIVDDE ARSALVEKTR VAAKRLREKV VVVDDGPPVT DDSVRSAALT DNPVPTPPWW GVREVDVPLD EVWHHLDTHV LFKLHWGGRG VKGDAWTELL RDNFQPRLER MWREQDYLHP RAKLGYFPCN SEGNEVIVFD PENPDRELHR LVFPRQPKHD RICLADLYRP LDSGERDVVA LQVVTAGDQV TELMAQLERD GEFAEQLFVH GLGVQTAEGM AEWLHAKVRT DLGIDLDEGR RYSWGYPACP DQSEHEKVFD LLDAQSIGMR LSGGYAVEPE QSTVAIVAHH PQAVYFGMRS GFLPKEKAPD DIIAGSDRDP GLLDAGSLES DPRDGAVEEE AAPDAAARS // ID D3F6Z9_CONWI Unreviewed; 578 AA. AC D3F6Z9; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADB52797.1}; GN OrderedLocusNames=Cwoe_4383 {ECO:0000313|EMBL:ADB52797.1}; OS Conexibacter woesei (strain DSM 14684 / JCM 11494 / NBRC 100937 / OS ID131577). OC Bacteria; Actinobacteria; Rubrobacteridae; Solirubrobacterales; OC Conexibacteraceae; Conexibacter. OX NCBI_TaxID=469383 {ECO:0000313|EMBL:ADB52797.1, ECO:0000313|Proteomes:UP000008229}; RN [1] {ECO:0000313|Proteomes:UP000008229} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14684 / JCM 11494 / NBRC 100937 / ID131577 RC {ECO:0000313|Proteomes:UP000008229}; 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 ----------------------------------------------------------------------- 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; ADB52797.1; -; Genomic_DNA. DR RefSeq; WP_012935848.1; NC_013739.1. DR RefSeq; YP_003396172.1; NC_013739.1. DR ProteinModelPortal; D3F6Z9; -. DR EnsemblBacteria; ADB52797; ADB52797; Cwoe_4383. DR KEGG; cwo:Cwoe_4383; -. DR PATRIC; 32050831; VBIConWoe21639_4406. DR BioCyc; CWOE469383:GH82-4417-MONOMER; -. DR Proteomes; UP000008229; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008229}; KW Methyltransferase {ECO:0000313|EMBL:ADB52797.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008229}; KW Transferase {ECO:0000313|EMBL:ADB52797.1}. SQ SEQUENCE 578 AA; 61833 MW; 5A902FDF06A8E9AF CRC64; MTALLGTPPA YDRITAAVQA GRCVILDGGV GTELAPRTDS DDRQWAGRAL VAPEQSVRAV HRRYAEAGCD VISTNTWALA GAARDGAPVG AGGAPPRHWM DLARTAVRAA RAAIDEAGRS GEVAVAFSLN DEIDTRDGLD TVRLLTRVFE DDPPDLLLLE TLSSVRGSTY GTVETLLETG LPVWLGFQRC RHGLCGVYGQ HWGGPEGDAF GRAARRFEQM GVGALLINCV PPDHVDGMLP WLRDFTDLPL GVSPNLGHLS AAGWQRHGSV EAEQYAQWAL RWRAEGAQLV GGCCGVRPEH VHSAREALDG TTPGTAPPPG AAHADGARPA GDAPRWTDGR GRSLFPLDVP ELVIEPGVQA VTQSSLLVWE YLDRERVGAH RRCLDVGCGS GLLAVQLARN GATHVHALDA DPAAVKNTLT NAFRNGVADR VTAHAADLYP WVPDERYDVI VANLCQLPAD PSGAPGRGRT ADFWGRTLID HLIRLLPEAL ADDGAAYLLQ LSIVGERRTA EQLEALGYEA RVVAYSLCEL RGLLDGDAEQ IAHVENRSDA YHVSLGGEDL LVAYLLEVTR KGAESWTA // ID D3FFF0_CONWI Unreviewed; 319 AA. AC D3FFF0; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADB53743.1}; GN OrderedLocusNames=Cwoe_5337 {ECO:0000313|EMBL:ADB53743.1}; OS Conexibacter woesei (strain DSM 14684 / JCM 11494 / NBRC 100937 / OS ID131577). OC Bacteria; Actinobacteria; Rubrobacteridae; Solirubrobacterales; OC Conexibacteraceae; Conexibacter. OX NCBI_TaxID=469383 {ECO:0000313|EMBL:ADB53743.1, ECO:0000313|Proteomes:UP000008229}; RN [1] {ECO:0000313|Proteomes:UP000008229} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14684 / JCM 11494 / NBRC 100937 / ID131577 RC {ECO:0000313|Proteomes:UP000008229}; 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 ----------------------------------------------------------------------- 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; ADB53743.1; -; Genomic_DNA. DR RefSeq; WP_012936794.1; NC_013739.1. DR RefSeq; YP_003397118.1; NC_013739.1. DR EnsemblBacteria; ADB53743; ADB53743; Cwoe_5337. DR KEGG; cwo:Cwoe_5337; -. DR PATRIC; 32052753; VBIConWoe21639_5360. DR HOGENOM; HOG000179103; -. DR OMA; CCGTDHR; -. DR BioCyc; CWOE469383:GH82-5381-MONOMER; -. DR Proteomes; UP000008229; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008229}; KW Methyltransferase {ECO:0000313|EMBL:ADB53743.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008229}; KW Transferase {ECO:0000313|EMBL:ADB53743.1}. SQ SEQUENCE 319 AA; 34011 MW; E3E976DBF0C00FD1 CRC64; MLRDVLRDLI ESGTPILADA GIETRIMFET DLELDPHIEV TALLDQRDGR EVLRDVYATY VDVAWAHGLP AIIGTPTFRA SLRYVEGAGR GGVEAVRRLN SEAVAFLHEI RSGGDHEPVF IAGVIGPYGD AYRPEDCLSH LDGADYHAAQ AEALAEAGVD LLFAPTFPSV EEAHGAAVAM SQTSVPYAVS FVLNQRGRLL DGTYLHDAIE RIDDAVVPAP THYGISCVHP TVVRTALQDL HVASARGAAR LREVKANGSS LAPGQLVALD HAESDPPEVF GESMHQLGID FGVSILGGCC GTDAKHLAAL ARRLEAKAA // ID D3G024_BACPE Unreviewed; 608 AA. AC D3G024; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 29-APR-2015, entry version 36. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN Name=yitJ {ECO:0000313|EMBL:ADC51109.1}; GN OrderedLocusNames=BpOF4_15300 {ECO:0000313|EMBL:ADC51109.1}; OS Bacillus pseudofirmus (strain OF4). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=398511 {ECO:0000313|EMBL:ADC51109.1, ECO:0000313|Proteomes:UP000001544}; RN [1] {ECO:0000313|EMBL:ADC51109.1, ECO:0000313|Proteomes:UP000001544} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OF4 {ECO:0000313|EMBL:ADC51109.1, RC ECO:0000313|Proteomes:UP000001544}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ADC51109.1; -; Genomic_DNA. DR RefSeq; WP_012958471.1; NC_013791.2. DR RefSeq; YP_003428001.1; NC_013791.2. DR ProteinModelPortal; D3G024; -. DR EnsemblBacteria; ADC51109; ADC51109; BpOF4_15300. DR KEGG; bpf:BpOF4_15300; -. DR PATRIC; 31948652; VBIBacPse80461_2991. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR BioCyc; BPSE398511:GJI9-1530-MONOMER; -. DR Proteomes; UP000001544; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001544}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ADC51109.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000001544}; KW Transferase {ECO:0000313|EMBL:ADC51109.1}. SQ SEQUENCE 608 AA; 67175 MW; 93DED4E0F7725A03 CRC64; MTFIEKMKNE VLVGDGAMGT LLYEQGISKC FEELNLSDPN RIIDAHKQYI EAGAVIIQTN TYAANRLKLE KYGLGEKVKI INQEAVKLAK EAGPNGIFIV GTVGGLQNFH QEEWTKEEVL EALEEQIEAL LASNVDGILL ETFYDLDELL GAINIVRNQS ELPIIANVSL GEIGVLHGGV SLKEAIGELE KAGADVVGVN CRMGPSHMLR SLEDVPLPKR AYLSVYPNAS LPEYQDGRLF YHSNPEYFES MGEQFVNQGV RLLGGCCGTT PEHIRAFSQV AERRTPVEEK WVTPSLEKVT KKIEFPRSLV PLSDIAKKRR SVIVELDPPK KLSTEKFIKG AKVLKEAGVD AVTLADNSLA SPRIDNMALA AQIKEDVRPL VHVTCRDRNL IGLQSHLMGL HALGINDVLA VTGDPTKVGD FPGATSVYDV TSFQLISLMK QLNEGISFSG KDLGQKANFS IAAASNPNVR HLDKAVQRME KKIESGADFF MTQPMYSEEQ IEAFYHETKH LDTPIYVGIM PLTSSRNAEF LHNEVPGIKL TDSIRRSMAS CETKDSAQLE GIKIAKSLID TATQYFNGIY LITPFLRYEI TAELTAYIEQ KSTAKLMN // ID D3G025_BACPE Unreviewed; 1148 AA. AC D3G025; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 27-MAY-2015, entry version 36. DE SubName: Full=5-methyltetrahydrofolate S-homocysteine methyltransferase {ECO:0000313|EMBL:ADC51110.1}; GN Name=metH {ECO:0000313|EMBL:ADC51110.1}; GN OrderedLocusNames=BpOF4_15305 {ECO:0000313|EMBL:ADC51110.1}; OS Bacillus pseudofirmus (strain OF4). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=398511 {ECO:0000313|EMBL:ADC51110.1, ECO:0000313|Proteomes:UP000001544}; RN [1] {ECO:0000313|EMBL:ADC51110.1, ECO:0000313|Proteomes:UP000001544} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OF4 {ECO:0000313|EMBL:ADC51110.1, RC ECO:0000313|Proteomes:UP000001544}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001878; ADC51110.1; -; Genomic_DNA. DR RefSeq; WP_012958472.1; NC_013791.2. DR RefSeq; YP_003428002.1; NC_013791.2. DR ProteinModelPortal; D3G025; -. DR EnsemblBacteria; ADC51110; ADC51110; BpOF4_15305. DR KEGG; bpf:BpOF4_15305; -. DR PATRIC; 31948654; VBIBacPse80461_2992. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR BioCyc; BPSE398511:GJI9-1531-MONOMER; -. DR Proteomes; UP000001544; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001544}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADC51110.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001544}; KW Transferase {ECO:0000313|EMBL:ADC51110.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 724 724 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1148 AA; 126789 MW; 798F283F9B7A5871 CRC64; MPKSLLEQQL KERILVLDGA MGTMLQQANL TAEDFGGEEY EGCNEYLNET APHVIEGIHR AYFEAGADIV ETNTFGATDI VLDDYDLGFK AEELNRVAVE IAKKAAKEFS APEKPRFVAG AMGPTTKSLS VTGGTTFDAL INSYHEQARG LLSGGADLLL LETSQDMRNV KAAYVGIERA FSELDVKVPI MVSGTIEPMG TTLAGQTIEA FYLSLEHMKP TVVGLNCATG PEFMRDHIRS LSELSNTFVS CYPNAGLPDE EGHYHESPSS LSKKLMGFAE KGWLNIVGGC CGTTPEHIRA MVEAVDGFAP RKLEEKRGHA VSGIEPLIYD DSMRPLFVGE RTNVIGSRKF KRLIAEGKYE EASEIARAQV KRGAHVIDIC LADPDREELE DMEAFLSHVV NKVKVPLMID STDEAVIEKS LTYSQGKAII NSINLEDGEE RFEAIVPLIK RYGAAVVVGT IDEEGMAVSA KRKLEVAKRS YDLLVNKHGL KPSDIIFDPL VFPVGTGDAQ YIGSAEATVE GIRLIKEELP ECLTILGVSN VSFGLPPVGR EVLNAVYLYH CTQAGLDYAI VNTEKLERYA SIPEEEKEMA KTLLFKTTDE SLAEFTAFYR GKKQEKKVEA SSMTLEERLA AYVVEGTKEG LYKDLDQALK SYSDALDIIN GPLMDGMDEV GRLFNNNELI VAEVLQSAEV MKASVAHLEP HMEKKADDDG KGKILLATVK GDVHDIGKNL VEIILGNNGF KIVNLGIKVT SNELIEAIKK ENPKAVGLSG LLVKSAQQMV LTAQDLRQQN ISIPILVGGA ALTRKFTDTK IAAEYDGLVL YAKDAMNGLE LANKLVKPED QQKLALEISE KRSLKEQVRP QREAAVQVLE KPVRSKVAAD GPLFIPEDLD EHILRDYDLS HLEPYVNLQM LLGKHLGLQG KVSRLLEEGD SRAVELKEKV DELFKRIKKE GIIKANGMYR FFPAQADGND VIIYDPNDKK TEINRFSFPR QNHEPFLCLA DYLRPKESGE MDYVGFLSVT AGNGVRDLAE EAKENGDYLF SHLIQAAALE IAEGFAERVH QLMRDKWGFP DSTDFTMAER FAAKYQGVRV SFGYPACPNL EDQEKLFDLI KPEKIGVQLT DGFMMEPEAS VTAMVFAHPE GRYFNVLA // ID D3GSZ3_ECO44 Unreviewed; 1227 AA. AC D3GSZ3; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 27-MAY-2015, entry version 38. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CBG37205.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CBG37205.1}; GN Name=metH {ECO:0000313|EMBL:CBG37205.1}; GN OrderedLocusNames=EC042_4381 {ECO:0000313|EMBL:CBG37205.1}; OS Escherichia coli O44:H18 (strain 042 / EAEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=216592 {ECO:0000313|EMBL:CBG37205.1, ECO:0000313|Proteomes:UP000001407}; RN [1] {ECO:0000313|EMBL:CBG37205.1, ECO:0000313|Proteomes:UP000001407} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=042 / EAEC {ECO:0000313|Proteomes:UP000001407}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; FN554766; CBG37205.1; -; Genomic_DNA. DR RefSeq; WP_000095993.1; NC_017626.1. DR RefSeq; YP_006098662.1; NC_017626.1. DR KEGG; elo:EC042_4381; -. DR PATRIC; 36690565; VBIEscCol52250_4547. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; ECOL216592:GCV7-4451-MONOMER; -. DR Proteomes; UP000001407; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001407}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CBG37205.1}; KW Transferase {ECO:0000313|EMBL:CBG37205.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135927 MW; E8811A9EC2746346 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV AAYQESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID D3HVY9_9BACT Unreviewed; 882 AA. AC D3HVY9; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFC76514.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFC76514.1}; DE Flags: Fragment; GN Name=metH {ECO:0000313|EMBL:EFC76514.1}; GN ORFNames=HMPREF0649_00421 {ECO:0000313|EMBL:EFC76514.1}; OS Prevotella buccae D17. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=575611 {ECO:0000313|EMBL:EFC76514.1}; RN [1] {ECO:0000313|EMBL:EFC76514.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=D17 {ECO:0000313|EMBL:EFC76514.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG739927; EFC76514.1; -; Genomic_DNA. DR RefSeq; WP_004340625.1; NZ_GG739927.1. DR EnsemblBacteria; EFC76514; EFC76514; HMPREF0649_00421. DR OrthoDB; EOG6091CH; -. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFC76514.1}; KW Transferase {ECO:0000313|EMBL:EFC76514.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 241 241 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 774 774 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. FT NON_TER 882 882 {ECO:0000313|EMBL:EFC76514.1}. SQ SEQUENCE 882 AA; 96341 MW; 3485BB532D240E7E CRC64; MKTIQELVKE RILILDGAMG TMIQNYHLTE EDFRGELFRR QPGVMKGNND MLNITRPDVV KDIFRQYIEA GADIITTNTF SSQRISQADY LLEDYAGEMA LQGARIAREV ADEYASEKHP CFVAGSVGPT NKTCSMSPDV SNPAARNLTY DQLFDAYCEQ IDGLVEGGVD VILIETIFDT LNAKVAIDAA LTIMARREVE LPIMLSLTIA DLAGRTLSGQ TIEAFLASVS SYPIFSVGLN CSFGAPQMKP FLEQMAKVAP YYVSVYPNAG IPNELGLYDE TAGTMAPQIG DFVNEGLVNF VGGCCGTTPE FIAAYRPFVE GKTPRRVPSP TRRMCLSGLD VLVPLDNIPG EDEQSAISGF TNIGERCNVA GSRKFLRLIK EKQYEEAVAI ARKQVDDGAL ILDINMDDGL LDAKAEMVNF LNMIASDPDI ARVPVMIDSS KWEVIVAGLK CVQGKSIVNS ISLKEGEEQF LAHARDIKRY GAACVVMCFD EQGQATTFDR RIEIAQRAYD LLTRKVGIQP QDIIFDPNVL AIATGMEEHD DYAMDFIRAT RWIKEHLPGA HVSGGVSNLS FSFRGNNYIR EAMHAVFLYH AISNGMDFGI VNPSAKITYA DIPQAELEVI EDVVLNRRRG AGEDLIALAQ RILDVKTVAT EGPQKGSDAS GTNGTPEWRS TPLDERLEYA LRKGVADFLE EDLREAMDEY PKAVDIIEGP LMHGMNVVGE LFGAGKMFLP QVVKTARTMK RAVAILQPAI EAERREGATK AGKVLLATVK GDVHDIGKNI VSVVMSCNNY EVIDMGVMVP ADQIVKKAVA EHVDIIGLSG LVTPSLDEMV NVATELHKAG LHVPIMIGGA TTSKLHVALK IAPVYSGPVI WMKDASQNPI VA // ID D3I4Q7_9BACT Unreviewed; 915 AA. AC D3I4Q7; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 01-APR-2015, entry version 26. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFC73392.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFC73392.1}; GN Name=metH {ECO:0000313|EMBL:EFC73392.1}; GN ORFNames=HMPREF0660_00872 {ECO:0000313|EMBL:EFC73392.1}; OS Prevotella melaninogenica D18. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=575612 {ECO:0000313|EMBL:EFC73392.1}; RN [1] {ECO:0000313|EMBL:EFC73392.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=D18 {ECO:0000313|EMBL:EFC73392.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG740013; EFC73392.1; -; Genomic_DNA. DR EnsemblBacteria; EFC73392; EFC73392; HMPREF0660_00872. DR PATRIC; 35831649; VBIPreMel53552_0860. DR OrthoDB; EOG6091CH; -. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFC73392.1}; KW Transferase {ECO:0000313|EMBL:EFC73392.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 240 240 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 915 AA; 100742 MW; 3DE5F8B7FFC7D7D6 CRC64; MKLRDNIKDR ILILDGAMGT MIQGYNLTEK DFRGNLELLQ MLNYQGNNDM LNLSRPDIIE DIHRRYLEAG ADIISTNTFS AQRVSQADYH MESFSRDIAF AGAKLARQCA DEYSTVDKPR FVAGSIGPTN KTCSMSPDVS DPAKRDLTYD TLFDTYSEQV AAMIEGGIDA VLIETIFDTL NAKVAIDASL SEMKKAGVDL PIMLSVTITD LSGRTLSGQT LDAFLASVSS YPIFSVGLNC SFGAEQMRPY LKELAAKAPY YISIHPNVGL PNSMGEYDET PDIMVPQMAS FVDEGLVNII GGCCGTTEEF IAGYVKVVEG KKPHIPVDAP KEMILSGLEQ FRLTPEISFV NVGERCNVAG SRKFLRLVKE KNYEEALTIA RKQVDDGALV LDINMDDGLL EAKDEMAHFV NMISSEPEIA RVPLMIDSSD WEVVVSALKC VQGKAIVNSI SLKEGEELFI QHAKDVLRFG AAVVVMCFDE EGQATSYERR IEIANRAYKI LTEKVGFPPQ DIIFDPNILA ICTGMKEHNS YAVDFIRATE WIKKNLPGAH VSGGVSNLSF SFRGNNYIRE AMHAVFLYHA IQVGMDFGIV NPATKVTYAD IPEDHLKIIE DVVLDRVEGA DELLIELANK ILEEKEAQKN GGATQDVAQE AWRNDALEDR LKYALRKGIS TYLNEDIHEA LEKYPHAVNI IEGPLMQGMN EVGDLFGAGK MFLPQVVKTA RTMKDAVAIL QPYIEKEKVD GKAIAGKVLL ATVKGDVHDI GKNIVGVVMA CNNYEVIDLG VMVPADQIIK KAKEENVDLI GLSGLITPSL QEMVNSVVAF KEAGLNIPVM IGGATTSQLH VALKIAPLYD APVVWVKDAS VNPSIAAALL NDKDRERFCK NLGATYEELR AGYKEEQQKV LSLSKARENK LNLFD // ID D3IGH8_9BACT Unreviewed; 921 AA. AC D3IGH8; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFC69124.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFC69124.1}; GN Name=metH {ECO:0000313|EMBL:EFC69124.1}; GN ORFNames=HMPREF0670_00447 {ECO:0000313|EMBL:EFC69124.1}; OS Prevotella sp. oral taxon 317 str. F0108. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=575615 {ECO:0000313|EMBL:EFC69124.1}; RN [1] {ECO:0000313|EMBL:EFC69124.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0108 {ECO:0000313|EMBL:EFC69124.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG740072; EFC69124.1; -; Genomic_DNA. DR RefSeq; WP_009229552.1; NZ_GG740072.1. DR EnsemblBacteria; EFC69124; EFC69124; HMPREF0670_00447. DR PATRIC; 35692302; VBIPreSp57183_0350. DR OrthoDB; EOG6091CH; -. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFC69124.1}; KW Transferase {ECO:0000313|EMBL:EFC69124.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 240 240 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 763 763 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 921 AA; 101488 MW; D448E6E4549B0B74 CRC64; MKIQDIIKQR IMILDGALGT MIQDYNLEEK DFRNADLAEH KGQLKGNNDV LNITRPDLIL DIHRRYLAAG ADLIETNTFS SQVVSQADYQ LEHLSRPMAL AGARLARKAA DEFSTPQWPR FVCGSVGPTN KTCSMSPDVS DAAARDITYD QLFDAYREQV GALIEGGVDA ILIETIFDTL NAKAAIDATM TEMQAQGLEL PIMLSMTVSD LAGRTLSGQT IEGFLASISS YPIFSVGLNC SFGADQMKPF LKELASKAPY YISAYPNAGL PNTMGQYDET AESMSPQIAQ FINEGLVNII GGCCGTDDKF IASYAALAKG KTPHAVVNKP TTLWLSGLEM LNVTPEVNFV NVGERCNVAG SKRFLRLIKE GQYDEAISIA RKQVTDGALV LDINMDDGLL DAEKEMTTFL NMIAAEPDIA RVPIMIDSSK WDVIMAGLKC VQGKCIVNSI SLKEGEEQFI EHARALKRFG AACVVMCFDE QGQATTFERR IEIAQRAYRI LTQEVGMNPL DIIFDPNILA IATGIEEHDN YAYEFIRSIA WIRKNLPGTH ISGGVSNLSF SFRGNNYIRE AMHAVFLYHA INEGMDFGIV NPSSKVTYSD IPIDELEIIE DVILNRKPNA AEALIELANK KKEEEEQRKA GLANGDSSVL KQEEEQWRSM ELDERLKYAL RKGIGDHLDE DLHLALEHYP HAVDIIEGPL MAGMNEVGEL FGAGKMFLPQ VVKTARTMKQ AVAILQPYIE KEKKVGATKA GKVILATVKG DVHDIGKNIV AVVMACNNYE VIDLGVMVPA EQIIRKAIEE KADIIGLSGL ITPSLEEMIN VAQEMEKAGL DIPIMIGGAT TSQLHVALKI APVYGGPVVW MKDASQNSLA AARLLNKSEE TAYVNELNDK YESLRAGYQD KQQKLLPIEE ARKNRLRLFD D // ID D3KZ43_ARTPT Unreviewed; 1182 AA. AC D3KZ43; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 01-APR-2015, entry version 27. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:BAI81897.1}; GN Name=MS {ECO:0000313|EMBL:BAI81897.1}; OS Arthrospira platensis (Spirulina platensis). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Arthrospira. OX NCBI_TaxID=118562 {ECO:0000313|EMBL:BAI81897.1}; RN [1] {ECO:0000313|EMBL:BAI81897.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NIES-39 {ECO:0000313|EMBL:BAI81897.1}; RX PubMed=20558164; DOI=10.1016/j.febslet.2010.06.013; RA Tanioka Y., Miyamoto E., Yabuta Y., Ohnishi K., Fujita T., Yamaji R., RA Misono H., Shigeoka S., Nakano Y., Inui H., Watanabe F.; RT "Methyladeninylcobamide functions as the cofactor of methionine RT synthase in a Cyanobacterium, Spirulina platensis NIES-39."; RL FEBS Lett. 584:3223-3226(2010). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AB548759; BAI81897.1; -; Genomic_DNA. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 228 228 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 737 737 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1182 AA; 130970 MW; CD972F795DB20EBD CRC64; MESLFLQRLH SPQRPVIIFD GAMGTNLQVQ NLTAEDFGGK EYEGCNEYLV HTKPEAVATV HRQFLQAGAD VIETDTFGGT SIVLAEYDLA DQAYQLNQTA ATLAKSVAAE FSTPEKPRFV AGSMGPGTKL PTLGHIDFDT LERAFCQQAE GLFDGGVDLF IVETCQDVLQ IKAALNGIEE VFKMKGERRP IMVSVTMEAF GTMLVGSEIN AALTILEPYQ IDILGLNCAT GPDLMKEHIA YLSEHSPFVV SCIPNAGLPE NVGGQAHYKL TPLELKMALM HFIEDLGVQV IGGCCGTRPD HIKALAEIAQ TLTPKPRHPQ ITPSAASIYS TISYEQENSF LIVGERLNAS GSKKCRDLLN AEDWDGLVAL AKTQVKEGAQ ILDVNVDYVG RNGVRDMHEL VSRLVTNVNL PLMLDSTEWE KMEAGLKVAG GKCLLNSTNY EDGEPRFYKV LELAKKYGAG VVVGTIDEEG MARTAAKKFA IAQTAYNDAI AFGIPATEIF FDPLALPIST GIEEDRENGK ATIEAIHQMR QQLPGCHILL GISNISFGLN PAARPVLNSV FLHETMAVGL DAAIVTANKI LPLAKIEPEH QEVCHHLIYD QRQFDGDVCT YDPLTKLTTL FEGKTTKRDR SGDANLPIEE RLKQHIIDGE RIGLEDALAE AIKKYPPLDI INIFLLDGMK VVGELFGSGQ MQLPFVLQSA QTMKAAVAYL EPFMEKSESG NNAKGTFVIA TVKGDVHDIG KNLVEIILSN NGYKVVNLGI KQPVDNIISA YREHNADCIA MSGLLVKSTA FMKDNLEVFN QEGITVPVIL GGAALTSKFV YEDCQNTYKG RVIYGKDAFS DLTFMDKLMP AKKAGKWEDF KGFLDEFVQD ETITTNGQSQ QSPPQTDQPE PDTPKVVDTR RSEAVAVDIE RPTPPFWGVK VLEPVDMPFD ELFWYLDLQA LTAGQWQFRK PQGQPREEYN QFLEAKVYPI LAEWKQRIIA ENLLQPRAVY GYFPCQSEGN TLLIYDPEKI KAGEISEPIT SFEFPRQRSG RRLCIADFFA PKDSGKIDVF PMHAVTVGQI ATDYAQKLFA ADDYTNYLYF HGMAVQTAEA MAEWLHARIR RELGFGGEDA DNIRDILKQR YRGSRYSFGY PACPNMQDQY KQLDLLKAEV IGLYMDESEQ LYPEQSTTAI ITYHPAAKYF SA // ID D3L3E4_9BACT Unreviewed; 815 AA. AC D3L3E4; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFD24474.1}; GN ORFNames=HMPREF1705_01562 {ECO:0000313|EMBL:EFD24474.1}; OS Anaerobaculum hydrogeniformans ATCC BAA-1850. OC Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae; OC Anaerobaculum. OX NCBI_TaxID=592015 {ECO:0000313|EMBL:EFD24474.1}; RN [1] {ECO:0000313|EMBL:EFD24474.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-1850 {ECO:0000313|EMBL:EFD24474.1}; 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., 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFD24474.1}. 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; ACJX02000007; EFD24474.1; -; Genomic_DNA. DR RefSeq; WP_009201735.1; NZ_GG705294.1. DR EnsemblBacteria; EFD24474; EFD24474; HMPREF1705_01562. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFD24474.1}; KW Transferase {ECO:0000313|EMBL:EFD24474.1}. SQ SEQUENCE 815 AA; 87769 MW; FBE1F7FF3800AE6D CRC64; MTIYHSRERC DFDLPLKFVD LITSLDRVLV LDGGMGTMLS EKGWRPPMLP EEMNLIAPDV VLDIHKEYLR SGASVVETNS FGASPIKLSY RGMGEKARRI NEEAARIARR AAEGWDAYVA GSMGPLGELI RPLGNLSFEE AYEAYKEQAI GLRDGGVDFF LIETQMDIKE AKAAVLAIKD VAAHIPFVVS FTFERNGRTI TGSPPEVVAH WARMIGACAV GVNCGFGPDL AREIVKKLYL NAGIPIFAYP NAGTPGKEDF DPREFAEEGR ELIRAGASVV GGCCGTTPEH IAHLKGVASQ EKPLRPRKVE KAALASRSRL VFAGAGEPIV VVGERINVSR KSPIRDEVAQ YKWDALSEEA RRQSSSGSQV IDVNISLPGI DRKRAIREAV EAVESACTLP ISIDADEADV LEEGLIHVAG IPLINSVTAE REKLIKGIEL AKRYGACLVV LAIDEDGISE TVEGRIKAVE KVCALADEMS FSKSRLFVDP LTMSVAADGR AGVVTLEALR AFKKLDLFTI MGVSNVSHGL PNRPLLNNAF LTMAAGAGLD SVIANPLDES FASLMMACNL LVGRDKGASG YITWARSLKS EEKDTSSPEK KEGASSPIEQ MKGMIVQGDR GGVLAVARRF LSEGGEPLAL INDVVLPALE EVGRLYECGD YFLPQLISSA EAAQGVCDLV EQAVLSRGGT LKDRGCILMA TVAGDIHDIG KNIVSMVLKS HGYRVIDLGK DVALEKILEE ARRGEAQIVG LSALMTTTMS EMERVTRKIK EENLSVKVII GGAAVSQNYA DHIGADGYAP DALSAVRLVE KLLGR // ID D3NT31_AZOS1 Unreviewed; 1163 AA. AC D3NT31; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 29-APR-2015, entry version 37. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:BAI71560.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:BAI71560.1}; GN Name=metH {ECO:0000313|EMBL:BAI71560.1}; GN OrderedLocusNames=AZL_009220 {ECO:0000313|EMBL:BAI71560.1}; OS Azospirillum sp. (strain B510). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Azospirillum. OX NCBI_TaxID=137722 {ECO:0000313|EMBL:BAI71560.1, ECO:0000313|Proteomes:UP000002040}; RN [1] {ECO:0000313|EMBL:BAI71560.1, ECO:0000313|Proteomes:UP000002040} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B510 {ECO:0000313|EMBL:BAI71560.1, RC ECO:0000313|Proteomes:UP000002040}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP010946; BAI71560.1; -; Genomic_DNA. DR RefSeq; WP_012973546.1; NC_013854.1. DR RefSeq; YP_003448104.1; NC_013854.1. DR EnsemblBacteria; BAI71560; BAI71560; AZL_009220. DR KEGG; azl:AZL_009220; -. DR PATRIC; 31930753; VBIAzoSp82869_1017. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR BioCyc; ASP137722:GBYD-938-MONOMER; -. DR Proteomes; UP000002040; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002040}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAI71560.1}; KW Transferase {ECO:0000313|EMBL:BAI71560.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 733 733 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1163 AA; 127650 MW; DD10C2984618944D CRC64; MPHILDTLRD RVLLCDGGFG SRIQALDLDV EKDYWGHENC TDILPLSRPD IVRDIHRGYF EAGADMVETD TFGASPVTLG EFGISEKAFE INRRAVELAR EAAESFTDGQ PRFVIGSIGP GTKLPSLGHI AYQPAEDSFH VQAAGLIAGG ADAILVETCQ DPLQIKAAVN GIKRARLEAK SDTPVFVQVT VETTGTLLVG TDIAAAATII QALDVPLMGL NCATGPLEMS EHVRWLAQNW PGLISVQPNA GLPELVDGKT HYPLLAGDFA HWLERFVVED GVNLVGGCCG TNVPHIAAAN QMLRKLAPAG SHRPNPKGRT VHWVPAVASL YSQVTLRQEN AFFAIGERCN ANGSKKWREL QERNDWDGCV EMAREQVKEG SHSLDVCTAF VGRDEVAEMN AVISRFAGSV TAPLVIDSTE YKVLEQALAL YGGKAILNSI NFEDGEEPAR LRLELAKKFG AAVIALTIDE EGMAKTPDRK LAIAKRLYDL AVTEYGLAPS DLLFDPLTFT IATGNEDDRK LAIWTLEGIE AISREMPGCQ IILGLSNVSF GLNAAARHVL NSVFLDHAVK KGMTGAIVHV SKILPLHQIP EKEVKTAEDL IFDRRSEGYD PLQAFIALFE GRKAADAKKK ARAETVEERL KERIVDGDRT GLEDDLAEAM KTHPPLEIIN TYLLDGMKVV GELFGAGKMQ LPFVLQSAET MKAAVAWLEP HMEKVEGQQK GTLVLATVKG DVHDIGKNLV DIILTNNGYK VVNLGIKQPV SAIIQAAKEH KATAVGMSGL LVKSTVVMRE NLEEMTREGL EVPVLLGGAA LTRAYVEGDC VASYGSGRVA YAGDAFDGLT LMDKVVEGSF DQQLAIQQAK RAGKATNRRR VLGQATSAAT GPVDKDAVRA RRHRLAEGVP VPTPPFWGPK LIDHVPLKTL VTYLNERMLY QLQWGYRKDG KSFEEFKEWA KKELRPVLDR ILQIAAKEEI LRPTAVYGYW KAAADGNDVI LFEEDGTTEA ARFSLPRQAK EDGECIADFL RDVTDPERDV IGLQVVTMGQ HCADVARDWF AENRYQDYLY LHGLSVEMTE AMAEYVHARI RAELGYGAED SRDKEKLLQQ AYRGSRYSFG YPACPNLKDQ EQLLKLLDAG RIGIEMSDED QLHPEQSTSA IVLHHPRAKY FSV // ID D3P3X9_AZOS1 Unreviewed; 307 AA. AC D3P3X9; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=Betaine-homocysteine S-methyltransferase {ECO:0000313|EMBL:BAI75358.1}; DE EC=2.1.1.5 {ECO:0000313|EMBL:BAI75358.1}; GN Name=bhmT {ECO:0000313|EMBL:BAI75358.1}; GN OrderedLocusNames=AZL_c00650 {ECO:0000313|EMBL:BAI75358.1}; OS Azospirillum sp. (strain B510). OG Plasmid pAB510c {ECO:0000313|EMBL:BAI75358.1, OG ECO:0000313|Proteomes:UP000002040}. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Azospirillum. OX NCBI_TaxID=137722 {ECO:0000313|EMBL:BAI75358.1, ECO:0000313|Proteomes:UP000002040}; RN [1] {ECO:0000313|EMBL:BAI75358.1, ECO:0000313|Proteomes:UP000002040} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP010949; BAI75358.1; -; Genomic_DNA. DR RefSeq; WP_012977189.1; NC_013857.1. DR RefSeq; YP_003451902.1; NC_013857.1. DR EnsemblBacteria; BAI75358; BAI75358; AZL_c00650. DR KEGG; azl:AZL_c00650; -. DR PATRIC; 31939024; VBIAzoSp82869_5084. DR HOGENOM; HOG000265278; -. DR BioCyc; ASP137722:GBYD-4808-MONOMER; -. DR Proteomes; UP000002040; Plasmid pAB510c. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002040}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:BAI75358.1}; KW Plasmid {ECO:0000313|EMBL:BAI75358.1}; KW Transferase {ECO:0000313|EMBL:BAI75358.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 307 AA; 32328 MW; B01E26A0300EDAF2 CRC64; MTEETIILDG GMGRELQRIG APFRQPEWSA LALIESPDHV RQAHESFARA GADMLTSNSY AVVPFHIGRD RFDAQGLALA DRAGRLARSV ADAHGVKAAG SLPPVFGSYR PDLFLPEQVD AILRVLVDGL APHVDVWLAE TQSALDEARA VRRVLGDDAR PLWLSFTLDD TDAGAVAAGR SAPALRSGES VADAARTAAG LGARALLFNC SQPEVMRAAV ETARAQPEAA ALRIGVYANA FPPQPKTAEA NDGLDPIRDD LDPASYLRWA ESWVEAGASI VGGCCGIGPD HIAALAGRLT PGGTRIG // ID D3P8U9_DEFDS Unreviewed; 1126 AA. AC D3P8U9; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 29-APR-2015, entry version 38. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:BAI81139.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:BAI81139.1}; GN Name=metH {ECO:0000313|EMBL:BAI81139.1}; GN OrderedLocusNames=DEFDS_1683 {ECO:0000313|EMBL:BAI81139.1}; OS Deferribacter desulfuricans (strain DSM 14783 / JCM 11476 / NBRC OS 101012 / SSM1). OC Bacteria; Deferribacteres; Deferribacterales; Deferribacteraceae; OC Deferribacter. OX NCBI_TaxID=639282 {ECO:0000313|EMBL:BAI81139.1, ECO:0000313|Proteomes:UP000001520}; RN [1] {ECO:0000313|Proteomes:UP000001520} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14783 / JCM 11476 / NBRC 101012 / SSM1 RC {ECO:0000313|Proteomes:UP000001520}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP011529; BAI81139.1; -; Genomic_DNA. DR RefSeq; WP_013008385.1; NC_013939.1. DR RefSeq; YP_003496895.1; NC_013939.1. DR EnsemblBacteria; BAI81139; BAI81139; DEFDS_1683. DR KEGG; ddf:DEFDS_1683; -. DR PATRIC; 35337329; VBIDefDes107323_1686. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; DDES639282:GJ90-1671-MONOMER; -. DR Proteomes; UP000001520; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001520}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAI81139.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001520}; KW Transferase {ECO:0000313|EMBL:BAI81139.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 216 216 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 282 282 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 716 716 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1126 AA; 126771 MW; 9E351B0247539B95 CRC64; MLRNYTSDKI LLFDGGMGTT IQQYDIPSDK WSGKQGCNEI LNLTYPELIE EIHTKFYEAG ADIVETNSFG ASRLVLSEYG LEDKVYEINL NAAKIARKAA NKFNNKFVAG SIGPGTKLPS LSQISFDDLY KMYKEQILGL IDGGVDLLLI ETCQDLLQVK SVVIAAFDLL DEKNLDIPVS VSVTIEQNGT MLLGTDLSAV ITVLRDYPIF SLGINCAVGP DLMYEPLSQL AKLWDRKISC IPNAGLPQNI NGKFIYDLTP EKMAEIMADL CEQFNLDFIG GCCGTTYEHI AALRMVANSF KPKPKVKYEY QGEVSSLYTS TKLRQEPPPT LIGERANANG SKAFRELLIA EDFDGMLAVA KEQENNGAHL LDVCVAYAGR DETKDMAKFV SMLNNAINIP LVIDSTEPKV LEEALKRYAG KPVINSINLE DGGTKLHQIL EIVRKHPAAV IALTIDEEGM AMTAEKKFEI AKKIYNIWTQ DYNFNPEDII FDPLTFSIGS GDETLKTAAK ETLEAIKKIK SELKGAKTVL GVSNVSFGLS PNAREVLNSV FLQEAVKYGL DLAIVNPAKI IPIHKINEKE LNLCLDLIYN KENALTNFLE YFSKRTDIKE DNDSINIPPE EQLKNKLISG DKSKLESLLD NLLVKYKPIE IINKILIPAM KEVGDLFGAG KMLLPFVLQS AEVMKKSVLY LEKFMDKKDD ENKGVIVLAT VKGDVHDIGK NLVDIILSNN GYKVYNLGIK VPVEEMIKKA KEVNADAIGM SGLLVKSTIV MKENIEEIRR SQLKTKILLG GAALTEGYVK NECEPILKGK VFYCRDAFDA IKFLSDNNGK SDEKITPVKN VKQNNVTINE EDIEMRSDIK PVENPPKPPF YGTKIVKDID FNEVVKFMNL NTLFNTRWSY KKKDMSDEEY TNLLKKVAYP ELEKIKKNVT ENKICNLQVA YGYFRVKSNG NYLLVFDENE KNISTIKFPR QKVEPYLCIA DYFNDIESEI YDVLPLQLVT IGDKAVEYTQ SLFKSNKYKE YFLYHGFFTE LTEALAEYWH SVIRKELNIE KENLSVEQIL NMKYQGKRYS FGYPSCPDLE GNLLICNLLN SKEIGVTITE NYEMVPEYST SAVIVYHPEA KYFVIK // ID D3PJG0_LEPSM Unreviewed; 392 AA. AC D3PJG0; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 01-OCT-2014, entry version 11. DE SubName: Full=Homocysteine S-methyltransferase 4 {ECO:0000313|EMBL:ADD38696.1}; GN Name=HMT4 {ECO:0000313|EMBL:ADD38696.1}; OS Lepeophtheirus salmonis (Salmon louse). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Maxillopoda; OC Copepoda; Siphonostomatoida; Caligidae; Lepeophtheirus. OX NCBI_TaxID=72036 {ECO:0000313|EMBL:ADD38696.1}; RN [1] {ECO:0000313|EMBL:ADD38696.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Atlantic form {ECO:0000313|EMBL:ADD38696.1}; RC TISSUE=Mixed tissue {ECO:0000313|EMBL:ADD38696.1}; RA Yasuike M., von Schalburg K., Cooper G., Leong J., Nilsen F., RA Jones S.R.M., Koop B.F.; RT "Atlantic Lepeophtheirus salmonis ESTs and full-length cDNAs."; 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; BT121766; ADD38696.1; -; mRNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Methyltransferase {ECO:0000313|EMBL:ADD38696.1}; KW Transferase {ECO:0000313|EMBL:ADD38696.1}. SQ SEQUENCE 392 AA; 44316 MW; 363AD25CD53711E3 CRC64; MTDIFYPIFP RVLGKRDEFF VLDGGFSTQC VSHVSAESFT GRAHWTSELI DENPEAVVET HKDFLSHGSV DLISTNTYQA HCGTIEKAVE LADQAIFETH AIPRKAGIVG SLGPYAAFLA SGSEYNGDKS TSYPLSEEEL KTWHKERIRH MMIGGVDVIA FETIPSIKEA ILILDLIDNT LNAKCWISFQ CKDSKSLAYG DSYKEAVRSL MCHPAYAKRK LLSIGINCTS PKYISPLLKL AEEVNNKSNF PDMYGYWRIP YVVYPNRGVY CKKKTCYIED KDDILGGGDN AILKRIHEWM SLGARIIGGC CGVNAQLIQK IKDQISEHIL DVLDKEEDCQ CHYFVDDEVL ENSLRKADPK SKSERRNKTN DFTDNLWMIC EMPYKNTGWS ND // ID D3PR18_MEIRD Unreviewed; 1215 AA. AC D3PR18; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 01-APR-2015, entry version 42. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AGK04370.1}; GN ORFNames=K649_05340 {ECO:0000313|EMBL:AGK04370.1}; 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 {ECO:0000313|EMBL:AGK04370.1, ECO:0000313|Proteomes:UP000013026}; RN [1] {ECO:0000313|EMBL:AGK04370.1, ECO:0000313|Proteomes:UP000013026} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 1279 {ECO:0000313|EMBL:AGK04370.1}; 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP005385; AGK04370.1; -; Genomic_DNA. DR RefSeq; WP_013013420.1; NC_021081.1. DR RefSeq; YP_003506921.1; NC_013946.1. DR RefSeq; YP_007879867.1; NC_021081.1. DR EnsemblBacteria; ADD27901; ADD27901; Mrub_1138. DR EnsemblBacteria; AGK04370; AGK04370; K649_05340. DR KEGG; mrb:Mrub_1138; -. DR KEGG; mre:K649_05340; -. DR PATRIC; 35358424; VBIMeiRub128672_1147. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; MRUB504728:GI6U-1162-MONOMER; -. DR Proteomes; UP000013026; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000013026}; KW Reference proteome {ECO:0000313|Proteomes:UP000013026}. SQ SEQUENCE 1215 AA; 134541 MW; 3001E6F8A6614A62 CRC64; MSVSAPRDFF AEQGVEPLTA QGYAREARAQ AFPYLKTLSE RVLVYDGAMG TEIFKYNLGD ADFGGPQYNG CPEILNRTRP DVIAAIHRSY LEAGADVIET NSFGSMPHVL AEYGLEAEAE DLAYAAAQIA RSEADKKSAE KPRFVAGSLG PGTKLISLGQ IGWKEMFESY RTAARGLIRG GVDLLIIETC QDVLQVRCAV LASRQAMQDL GREVPLQVQV TFEATGTLLV GSDDGAALTV LESLPVDVVG INCAVGPDLM DSHIRHFCQH STRWVACLPN AGLPRNEGGR AVFDLTPAEL ARWQLKFVRE YGLNVVGGCC GTGPEHIRAL VEALGGCHTP PLRSSQQAQT PSPLGQVASL YQSVPLRQDT GILIVGERTN ATGSKKFREL LFAGDFDGME ALANEQVAEG AHVLDVSVAW TGRDEVRDMR EVLKRFATSV PIPIMVDTTQ PEVMEEALKH LGGRAILNSI NLEDGLEKFD RVAALAKRHG AALVALTIDE DKEAGMAKTV ERKVEIALRI YERLTQVHGI AGESILFDLL TFPITQGDED TRKLALWTIE GIRQLRQQLP EVGFILGISN VSFGLSPQAR VVLNSVFLDE CIRAGLTAAI LNAGKILPIN QIPQEQYQLA LDLIYDRRQF GPAGEVIHDP LFAYVDYFAK NKVDKAQARD PLAGLELEER LKKRIIEGRK VGLEADLEQA LGKYSPVEII NQILLEGMKV VGDLFGAGKM QLPFVLQAAE TMKAAVRYLE PRMEKLEGVH KGTMVIATVK GDVHDIGKNL VDIILSNNGY KVINLGIKKP IEEILAAVEE HRPDVVGMSG LLVKSTVVMK ENLEYMAARG ISLPVVLGGA ALNRHYVEND LRRVYTTGQV YYASDAFDGL QLMEELTGHA PPRLTSREVS GHKYKTAYEI LQEKLMAGSE YIPSNTPPAP RIPRPPFWGR RVVDKSELEI GVISRYVNKN ALFRGQWGFR KGEMSQPEYE AYLERLAEPM FEEMVLQAMA EGWLEPAVVY GYWPVASDKN ELIVFDPDSG AELFRFNFPR QMGAGSRHLC IADFFRPRHA PPIGDEQGWF PPAAWANGAR DVLAAQVVTM GRKVSQVAQE LFQSDAYQDY LYLHGFSVEM AEALAEYWHK RIRQQLDIAQ DDATSLEELF RQGYQGSRYS FGYPACPRLE DQKYLQELLQ WQEIGVELSE EYQLHPEQST SAIVVHHPAA KYFNL // ID D3Q595_STANL Unreviewed; 1173 AA. AC D3Q595; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 01-APR-2015, entry version 40. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADD44144.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADD44144.1}; GN OrderedLocusNames=Snas_4499 {ECO:0000313|EMBL:ADD44144.1}; 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 {ECO:0000313|EMBL:ADD44144.1, ECO:0000313|Proteomes:UP000000844}; RN [1] {ECO:0000313|EMBL:ADD44144.1, ECO:0000313|Proteomes:UP000000844} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44728 / NRRL B-16338 / NBRC 102104 / LLR-40K-21 RC {ECO:0000313|Proteomes:UP000000844}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001778; ADD44144.1; -; Genomic_DNA. DR RefSeq; WP_013019715.1; NC_013947.1. DR RefSeq; YP_003513237.1; NC_013947.1. DR EnsemblBacteria; ADD44144; ADD44144; Snas_4499. DR KEGG; sna:Snas_4499; -. DR PATRIC; 35371299; VBIStaNas43420_4453. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; SNAS446470:GHHC-4531-MONOMER; -. DR Proteomes; UP000000844; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000844}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADD44144.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000844}; KW Transferase {ECO:0000313|EMBL:ADD44144.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 224 224 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 734 734 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1173 AA; 128296 MW; FCEDD5CECEE74B2A CRC64; MSENPFLSAL KHRILVADGA MGTMLQDAQL EIDDFEGLEG CNEILNVSRP DVVRDIHDAY FAAGADMVET NSFGSNMTNL GEYDIADRIR ELSQRSAELA KEVASGHSTP DRPRFVLGSI GPGTKLPTLG HAPYAVLRDA YLENAAGLIL GGADALIVET SQDLLQTKAA IVGAQRAMKA EGIQVPIIAS VAVETTGTML VGSEIGAALT ALAALKVDLI GLNCSTGPAE MSEHLRYLSQ YSRIPLSVMP NAGLPELGPN GAIFPMTPPK FTEAIDEFAQ EFGVALVGGC CGTTPEHIRQ VYERVGQREP VRRTIADEPG VSSVYHHVPF KQDASILNVG ERTNANGSKA FREAMLAADW DKCVDIARDQ ARAGSHLLDL CVDYVGRDGR DDMRELAGRF ATASTLPIML DSTEPGVIEA GLESLGGRCI VNSVNFEDGD GPNSRYAKAM PAIVEHGAAV VVMCIDEEGQ ARTADRKIEI AARTIDDLVD NWGMRVSDIF VDALTFPIST GQEETRRDGI ETIDAIRGIA ERYPGINFTL GISNVSFGLN PASRQVLNSV FLHECVEAGL TSAIVHASKI LPMSKIEEEH RQVALDMVYD RRREGYDPLQ RFIELFEGVD MASARASRAE ELAALPLNER LERRVIDGER NGLEADLDAA LVERSALDIV NDTLLNGMKT VGELFGSGQM QLPFVLQSAE VMKTAVAYLE PHMEKADSEG KGTIVLATVK GDVHDIGKNL VDIILSNNGY SVVNIGIKQP INAIVDAAEQ HNADAIGMSG LLVKSTVIMK ENLAEMMSRG VAGRWPVLLG GAALTRSYVE DDLREMFAEG EVHYAKDAFE GLSLMERVMT ARRTGVAVVD EEREAKIAQR RERRARHAAV KAESGPSLDD DSVRSDVATD NPVPRPPFFG TRVIKGVPTA DYAAMLDERA TFLGQWGLKP SRGKDGPSYE ELVETEGRPR LRYWMDRLAT DKVLDPSVVY GYFPCYSEGN TLVVLDENGH SERARFAFPR QRRERRLCIA DFFRPKESGE LDVIGMQLVT IGSAASDYTA KLFAQHAYRD YLEVHGLSVQ LTEALAEYWH KRMRAEWTRP DGKSVADFDP NDLDGMLKVD YHGCRYSFGY AACPDLEDRA KTVAILRPDR IGVELTEEFQ LTPEQSTDAI VVHHPEASYF NAK // ID D3QK18_ECOCB Unreviewed; 1227 AA. AC D3QK18; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADD59262.1}; GN Name=metH {ECO:0000313|EMBL:ADD59262.1}; GN OrderedLocusNames=G2583_4836 {ECO:0000313|EMBL:ADD59262.1}; OS Escherichia coli O55:H7 (strain CB9615 / EPEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=701177 {ECO:0000313|EMBL:ADD59262.1, ECO:0000313|Proteomes:UP000001521}; RN [1] {ECO:0000313|EMBL:ADD59262.1, ECO:0000313|Proteomes:UP000001521} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CB9615 / EPEC {ECO:0000313|Proteomes:UP000001521}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001846; ADD59262.1; -; Genomic_DNA. DR RefSeq; WP_000096047.1; NC_013941.1. DR RefSeq; YP_003502246.1; NC_013941.1. DR ProteinModelPortal; D3QK18; -. DR SMR; D3QK18; 651-1227. DR EnsemblBacteria; ADD59262; ADD59262; G2583_4836. DR KEGG; eok:G2583_4836; -. DR PATRIC; 35348851; VBIEscCol154499_4833. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; ECOL701177:GI1N-4837-MONOMER; -. DR Proteomes; UP000001521; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001521}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136040 MW; 8FB5738E12303E7E CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID D3RA44_KLEVT Unreviewed; 310 AA. AC D3RA44; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADC59951.1}; GN OrderedLocusNames=Kvar_4072 {ECO:0000313|EMBL:ADC59951.1}; OS Klebsiella variicola (strain At-22). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=640131 {ECO:0000313|EMBL:ADC59951.1, ECO:0000313|Proteomes:UP000001907}; RN [1] {ECO:0000313|Proteomes:UP000001907} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=At-22 {ECO:0000313|Proteomes:UP000001907}; 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 ----------------------------------------------------------------------- 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; ADC59951.1; -; Genomic_DNA. DR RefSeq; WP_012968857.1; NC_013850.1. DR RefSeq; YP_003440983.1; NC_013850.1. DR EnsemblBacteria; ADC59951; ADC59951; Kvar_4072. DR KEGG; kva:Kvar_4072; -. DR PATRIC; 32228226; VBIKleVar54872_4033. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR BioCyc; KVAR640131:GHXG-4138-MONOMER; -. DR Proteomes; UP000001907; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001907}; KW Methyltransferase {ECO:0000313|EMBL:ADC59951.1}; KW Transferase {ECO:0000313|EMBL:ADC59951.1}. SQ SEQUENCE 310 AA; 33245 MW; B6FE0C75F88F3DAB CRC64; MSQTNPFTAL LAAQPYVLLD GAMATELEAR GCDLADSLWS AKVLLENPQL IRDVHLDYFR AGAQVAITAS YQATPAGFAA RGLDDAQSRA LIGKSVELAR KAREAYLAEN PQAGTLLVAG SIGPYGAFLA DGSEYRGDYQ RSAAEFQDFH RPRVEALLDA GADLLACETL PSFAEIQALT ALLQDYPRAR AWYSFTLRDA EHLSDGTPLR EVMAALADNP QVVAVGINCI ALENTPAALA HLHSLTALPL VVYPNSGEHY DAVSKTWHHH GEACATLADY LPQWLAAGAK LIGGCCRTTP KDIAALNAKR // ID D3RG91_KLEVT Unreviewed; 1227 AA. AC D3RG91; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 27-MAY-2015, entry version 39. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADC60718.1}; GN OrderedLocusNames=Kvar_4847 {ECO:0000313|EMBL:ADC60718.1}; OS Klebsiella variicola (strain At-22). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=640131 {ECO:0000313|EMBL:ADC60718.1, ECO:0000313|Proteomes:UP000001907}; RN [1] {ECO:0000313|Proteomes:UP000001907} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=At-22 {ECO:0000313|Proteomes:UP000001907}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001891; ADC60718.1; -; Genomic_DNA. DR RefSeq; WP_012969169.1; NC_013850.1. DR RefSeq; YP_003441750.1; NC_013850.1. DR EnsemblBacteria; ADC60718; ADC60718; Kvar_4847. DR KEGG; kva:Kvar_4847; -. DR PATRIC; 32229832; VBIKleVar54872_4815. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; KVAR640131:GHXG-4932-MONOMER; -. DR Proteomes; UP000001907; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001907}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135805 MW; C38527E9CC161766 CRC64; MSSKVEQLHQ QLKERILVLD GGMGTMIQGY RLSEQDFRGE RFADWPCDLK GNNDLLVLSK PEVIREIHDA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARASADAWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTRAL VEGGVDLILI ETVFDTLNAK AAIYAVKEEL EALGVDLPLM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LSFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MATQIREWAE AGFLNIVGGC CGTTPEHIAA MSRAVAGLPP RQLPELPVAC RLAGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VESGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVEPFIHHA KLVRRYGAAV VVMAFDEVGQ ADTRERKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPG ELRDAVEDVI LNRRDDSTER LLELAEKYRG SKADDGANAQ QAEWRSWDVK KRLEYSLVKG ITEFIEQDTE EARQQAARPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPYIEASK EQGSSNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIIDL GVMVPADKIL KTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLAAAR ENDLAFDWES YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG EEAQRLFKDA NDLLDKLSAE KTLNPRGVIG LFPANRVGDD IEIYRDETRT HVLTVSHHLR QQTEKVGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAYEAQH DDYNKIMIKA IADRLAEAFA EYLHEKVRKV YWGYAANENL SNEELIRENY QGIRPAPGYP ACPEHTEKGT IWQLLDVEAH TGMKLTESFA MWPGASVSGW YFSHPDSKYF AVAQIQRDQV EDYALRKGMT PAEVERWLAP NLGYDAD // ID D3RTP5_ALLVD Unreviewed; 1253 AA. AC D3RTP5; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 27-MAY-2015, entry version 39. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADC62554.1}; GN OrderedLocusNames=Alvin_1622 {ECO:0000313|EMBL:ADC62554.1}; OS Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / OS NCIMB 10441 / D) (Chromatium vinosum). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Allochromatium. OX NCBI_TaxID=572477 {ECO:0000313|EMBL:ADC62554.1, ECO:0000313|Proteomes:UP000001441}; RN [1] {ECO:0000313|Proteomes:UP000001441} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D RC {ECO:0000313|Proteomes:UP000001441}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001896; ADC62554.1; -; Genomic_DNA. DR RefSeq; WP_012970828.1; NC_013851.1. DR RefSeq; YP_003443586.1; NC_013851.1. DR EnsemblBacteria; ADC62554; ADC62554; Alvin_1622. DR KEGG; alv:Alvin_1622; -. DR PATRIC; 31923007; VBIAllVin64954_1612. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR BioCyc; AVIN572477:GCJK-1647-MONOMER; -. DR Proteomes; UP000001441; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001441}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001441}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1253 AA; 137113 MW; 49A776C4EF857A43 CRC64; MTDSNALIRE RLARSILILD GAMGTMIQRH GLTEADYRGA RFADWPSDLK GNNDLLVLTR PDVIGGIHRA YLEAGADIVE TNSFNATRIA MADYGMEDLA YEINVAAARL ALAAADDYST PEKPRFVAGV LGPTNRTASI SPDVNDPGAR NVDFDTLVAA YAESTRGLIE GGADLILIET IFDTLNAKAA IFAVKQVFDE DGVERPTMIS GTITDQSGRT LTGQTTEAFY NALRHAEPIS IGLNCALGPF ELRQYVEELA RISETHVSAH PNAGLPNELG GYDLGPDEMA EEIAEWARSG FLNIVGGCCG TTPDHIRAIA QAVAGIAPRA RPEIAPACRL SGLEPCNIDA GSFFVNVGER TNVTGSARFR RLIKEGDYDT ALSVAQEQVE NGAQVIDVNM DEGLLDAVAA MKRFLNLVAA EPEIARVPVM IDSSKWEVIE TGLKCVQGKP IVNSISIKEG EEKFLQQARL CRRYGAAVIV MAFDEAGQAD TQARKIEICT RAYRLLTEQV GFPPEDIIFD PNIFAVATGI EEHDNYAVDF IEATREIKRT LPHALVSGGV SNVSFSFRGN DPVREAIHAV FLYHAVKAGM DMGIVNAGQL AIYDDLPEEL REAVEDVILN RRPDGTERLL DLAPKYKGDG GGVENKADLE WRGWPVEKRI EHALIKGITD FIDEDTEAAR QALGRPLEVI EGPLMRGMNI VGDLFGEGKM FLPQVVKSAR VMKKAVAYLQ PFLEAEKAES GAVASSNGKF LIATVKGDVH DIGKNIVAVV LQCNSYEVID LGVMVPTETI LQRAREVGAD VIGLSGLITP SLDEMVHVAK EMQRQGMNVP LLIGGATTSK LHTALKIAPQ REAPVIYVPD ASRAVGVVSS LLSETQRPGY VAAIAEEYER LRVEREGRST TRKSVSIAEA RANRLALDWA GYEPPKPALL DAGFSDTASW SLRLERTGET VIATLDDFPL DDLVRTIDWL PFFRAWELAH KHFPGILDDA VIGEEARKLY ADAQAFLERL VSERWLQARA VLGFFPANGV GADDIALYRD EARTQPLATL HNLRQQMPRD GGRNQANFCL SDFIAPAESG RPDWIGAFAV TAGVGIEEHL ARFEADHDDY SAIMLKALAD RLAESFAERL HQLVRTRYWG YAAGETLSND ELIAEKYQGI RPAPGYAACP DHTEKGILWS LLEPDQRIGL TLTENYAMWP TAAVSGWYFA HPEARYFGVG RIQRDQVEDY AQRKGMTLAE AERWLAPVLG YEA // ID D3SCH9_THISK Unreviewed; 1263 AA. AC D3SCH9; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 27-MAY-2015, entry version 36. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADC70698.1}; GN OrderedLocusNames=TK90_0182 {ECO:0000313|EMBL:ADC70698.1}; OS Thioalkalivibrio sp. (strain K90mix). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Thioalkalivibrio. OX NCBI_TaxID=396595 {ECO:0000313|EMBL:ADC70698.1, ECO:0000313|Proteomes:UP000009099}; RN [1] {ECO:0000313|Proteomes:UP000009099} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K90mix {ECO:0000313|Proteomes:UP000009099}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001905; ADC70698.1; -; Genomic_DNA. DR RefSeq; WP_012981597.1; NC_013889.1. DR RefSeq; YP_003459434.1; NC_013889.1. DR EnsemblBacteria; ADC70698; ADC70698; TK90_0182. DR KEGG; tkm:TK90_0182; -. DR PATRIC; 32523890; VBIThiSp13812_0183. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR BioCyc; TSP396595:GH8D-183-MONOMER; -. DR Proteomes; UP000009099; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000009099}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000009099}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 757 757 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1263 AA; 140733 MW; 43BDBF5409C2DCCE CRC64; MTATRNDIEK ALKERILILD GGMGTTIQLY KLEEADYRGE RFKDWESDLK GNNDLLSLTR PDIIEQIHND YLEAGADIIE ANTFNGTRIA MADYHMEDLV PELNRESAKL ARKAADAWTE KTPDKPRYVA GILGPTNRTA SISPDVNDPG ARNVDFDTLV ESYKEAAEAL VEGGVDILLI ETVFDTLNAK AAIFAVKTLE DELGKELPIM ISGTITDASG RTLSGQTTEA FWNSVRHANP VSIGLNCALG AKEMRQYVEE LSRIADTHVS AHPNAGLPNE FGDYDESPEQ MAADVGPWAE QGLLNIIGGC CGTLPEHIRA MREAVEKFPP RKVPEIAPAC RLSGLEPCNI TDDSLFVNVG ERTNVTGSRK FLRLIQNEEY DVALEVALNQ VEGGAQIIDI NMDEGMLESQ DAMVRFLNLL AGEPDIARVP VMIDSSKFEI IEAGLKCVQG KAVVNSISMK EGEENFIKQA QLCRRYGAAI VVMAFDEDGQ ADNEDRRVEI CTRAYRLLTE KVGFPAEDII FDPNIFAVAT GIEEHNNYGV DFIEATRRIK QDLPHALVSG GVSNVSFSFR GNEPVREAIH AVFLYHAIKA GMDMGIVNAG QLAVYDDIDE KLKEAVEDVV LNRRDDATER LLDLSEEYKG QGGGKKEENL EWREWEVTKR LEHSLVKGID TYVVEDTEEA RQQYDRPIQV IEGPLMDGMN VVGDLFGEGK MFLPQVVKSA RVMKKAVAHL IPYIEAEKTG TENNGKILMA TVKGDVHDIG KNIVGVVLQC NNFEVIDIGV MQPGAEILKA AKEHDVDVIG LSGLITPSLE EMANFAADLE REGMTTPLMI GGATTSRAHT AVKIEPNYSG PVVWVKDASR AVGVAQSLIS PELRENYAAE IREEYEKLRV QNAGRKKKTQ WVTLEKARAN KPQIDWSSYT PTKPKALETD KLPGEPKVLH PHGDGSVLLR FDDFDLNEVR NFIDWTPFFH SWQLHAAYPR ILDDEKVGEE ARKLFKDGQE MLDRMIEEKW VTLRGVVGFF PANTVNDDDI EVYTDESRSK VLKKLHHLRQ QTEKRRGQPS HSLADFLMPK EAGGPDYLGA FAVSAGGDVD AKAEEYEKAN DDYHAILVKS LADRLAEAFA ECMHQYVRKH YWGYVPDEAL ENEDLIDEKY QGIRPAPGYP ACPEHTEKGT LWELLQADEH ADMTLTESYA MLPVSAVSGW YFAHPESRYF GLGKVNRDQV EDYAKRKGMS FEEAERWLAP NIGYDDSDEA KAEARAEREA RSA // ID D3T3Q0_THEIA Unreviewed; 807 AA. AC D3T3Q0; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 27-MAY-2015, entry version 33. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADD02852.1}; GN OrderedLocusNames=Thit_1600 {ECO:0000313|EMBL:ADD02852.1}; OS Thermoanaerobacter italicus (strain DSM 9252 / Ab9). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Thermoanaerobacter. OX NCBI_TaxID=580331 {ECO:0000313|EMBL:ADD02852.1, ECO:0000313|Proteomes:UP000001552}; RN [1] {ECO:0000313|EMBL:ADD02852.1, ECO:0000313|Proteomes:UP000001552} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 9252 / Ab9 {ECO:0000313|Proteomes:UP000001552}; 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 ----------------------------------------------------------------------- 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; ADD02852.1; -; Genomic_DNA. DR RefSeq; WP_012995580.1; NC_013921.1. DR RefSeq; YP_003477414.1; NC_013921.1. DR ProteinModelPortal; D3T3Q0; -. DR EnsemblBacteria; ADD02852; ADD02852; Thit_1600. DR KEGG; tit:Thit_1600; -. DR PATRIC; 32498280; VBITheIta22270_1640. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR BioCyc; TITA580331:GHTM-1655-MONOMER; -. DR Proteomes; UP000001552; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001552}; KW Methyltransferase {ECO:0000313|EMBL:ADD02852.1}; KW Transferase {ECO:0000313|EMBL:ADD02852.1}. SQ SEQUENCE 807 AA; 88176 MW; CF3BCFB433B65093 CRC64; MLDIFKELSK RVIIFDGAMG TQLQERGLKT GECPEYMNIT HPEVVFDIHR AYIEAGADVV ETNTFGANRI KLAKYGLENE VFNIVTQAVK IAKEVAKDKP VALSIGPTGE LLTPYGDMTF DEAYEVFKEV VVAGEKAGAD IVLIETMSDI LEAKAAILAA KENSNMKVIC TMTFQEDGRT LMGSDPITVI VSLQGLGLDA IGVNCSTGPD KMINVVEKMS QVSRIPIIAQ PNAGMPVIRD GKTVYDLKPE EFASFFPSLV EKGASIVGGC CGTTPHYIKL VKEAVKDLKP KVKINKFTAV ASNTKTVFIG DDYPLRIIGE RINPTGKKKL SEAFLVGDVS LAVEEAIKQQ KCGAEILDVN VGVPGIDEEQ LLPKVVSEIQ NVVDLPLQID STNIKAVEKA IRILRGRPII NSVSAKEESL KEVLPIVKKY GACVVGLTVG DKGLPKDRHE RIENAKKIIK KAEEYGIPKE DILIDCIVLT VSSEQEAAIE TLEAIKLAKE ELGVNTVVGL SNVSFGLPER KLINSAFLAM AASYGLTTAI INPCDETMMD TLRATMVLLN KDKGSVNYLN IYGKKQKEEL REKEQPKIQE EDLKSKFYIQ ILEGKKSGVE DIVKNILEEE IQPLSIVDNI IIPALKEVGD RYEKGVYFLP QLLSSAEVVQ SAFKIIKEKL PKGSVSKGKI ILATVEGDVH DIGKNIVKVL LENYGYDVID LGKDVKGEVI LEEVKRTGAP LVGLSALMTT TLFNMEKIIK LLKANTDVKI MVGGAVLTEE YAYKIGADYY GKTAQDAVKI ADKFFLKNAL LCKTCGI // ID D3TPQ2_GLOMM Unreviewed; 331 AA. AC D3TPQ2; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 01-OCT-2014, entry version 10. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADD19680.1}; OS Glossina morsitans morsitans (Savannah tsetse fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Hippoboscoidea; Glossinidae; Glossina. OX NCBI_TaxID=37546 {ECO:0000313|EMBL:ADD19680.1}; RN [1] {ECO:0000313|EMBL:ADD19680.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Salivary gland {ECO:0000313|EMBL:ADD19680.1}; RX PubMed=20353571; DOI=10.1186/1471-2164-11-213; RA Alves-Silva J., Ribeiro J.M., Van Den Abbeele J., Attardo G., Hao Z., RA Haines L.R., Soares M.B., Berriman M., Aksoy S., Lehane M.J.; RT "An insight into the sialome of Glossina morsitans morsitans."; RL BMC Genomics 11:213-213(2010). RN [2] {ECO:0000313|EMBL:ADD19680.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Salivary gland {ECO:0000313|EMBL:ADD19680.1}; RG International Glossina Genome Initiative; RA da Silva J., Ribeiro J.M.C., Abbeele J.V., Attardo G., Hao Z., RA Haines L.R., Soares M.B., Berriman M., Aksoy S., Lehane M.J.; 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; EZ423404; ADD19680.1; -; mRNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Methyltransferase {ECO:0000313|EMBL:ADD19680.1}; KW Transferase {ECO:0000313|EMBL:ADD19680.1}. SQ SEQUENCE 331 AA; 36853 MW; 2F52594831C875A9 CRC64; MDLTSILVKD GGFGTQMTVH VGDAVDGDPL WSARFNATKP AAIINTHLDF LQNGADIILT NTYQTSVEGY MEYMELNEEQ SVELIKNTVR LAHIAKEKYL SECCQAGLNI TEGFPMIIAS IGPYGAHLHD GSEYTGSYAD YLSAKDITDW HRVRIDACLD AGIDALAIET IPCQMEAEAL VDMLCEDYAD VKFWISFQCK DEKTLAHGEV FAEAALSVWD LLRNRNAQKN CLAIGANCVH PKFVTPLLQS VNAHKKPEEK IPLVVYPNSG EIYDVDKGWL GKEHCVPLAD YVPEWAHLGA KIIGGCCRTY ARDIRLIKEA VQDYNKCEDW N // ID D3TRN2_GLOMM Unreviewed; 333 AA. AC D3TRN2; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 01-OCT-2014, entry version 10. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADD20360.1}; OS Glossina morsitans morsitans (Savannah tsetse fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Hippoboscoidea; Glossinidae; Glossina. OX NCBI_TaxID=37546 {ECO:0000313|EMBL:ADD20360.1}; RN [1] {ECO:0000313|EMBL:ADD20360.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Salivary gland {ECO:0000313|EMBL:ADD20360.1}; RX PubMed=20353571; DOI=10.1186/1471-2164-11-213; RA Alves-Silva J., Ribeiro J.M., Van Den Abbeele J., Attardo G., Hao Z., RA Haines L.R., Soares M.B., Berriman M., Aksoy S., Lehane M.J.; RT "An insight into the sialome of Glossina morsitans morsitans."; RL BMC Genomics 11:213-213(2010). RN [2] {ECO:0000313|EMBL:ADD20360.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Salivary gland {ECO:0000313|EMBL:ADD20360.1}; RG International Glossina Genome Initiative; RA da Silva J., Ribeiro J.M.C., Abbeele J.V., Attardo G., Hao Z., RA Haines L.R., Soares M.B., Berriman M., Aksoy S., Lehane M.J.; 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; EZ424084; ADD20360.1; -; mRNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Methyltransferase {ECO:0000313|EMBL:ADD20360.1}; KW Transferase {ECO:0000313|EMBL:ADD20360.1}. SQ SEQUENCE 333 AA; 37325 MW; E33317584E5FB43A CRC64; MSPLHLKGLV LVKSGGFSTQ LAKHVGDKID GDPLWGSRFD KENPEAVIQT HLDFLEVGAD IIVTNTYQSS VEGFTKHLNL TKEESIDLMR ESVKLAMQAK NKYIERLKDC NRHKEPGLPL IMGSIGPYGA MLHDGSEYNG SYTEQLTKQD IQQWHRTRIE AVLSGGVDGL AVETIPCQME AEAVTEMLLK DYPDVKFWVS FQCKDELHLA HGENFANAAK SVWELVRKAN AVDRLYGIGV NCVNPKFVST LFQSLHKLLN HEQIPQLIVY SNRGEIYDAT KGEWTGHDKC VPLASYVPEW VQLQAKIIGG CCRVYPEDIL AIRKCIDNIG NNN // ID D3UNW4_LISSS Unreviewed; 617 AA. AC D3UNW4; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 27-MAY-2015, entry version 36. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=lse_1646 {ECO:0000313|EMBL:CBH27797.1}; OS Listeria seeligeri serovar 1/2b (strain ATCC 35967 / DSM 20751 / CIP OS 100100 / SLCC 3954). OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=683837 {ECO:0000313|EMBL:CBH27797.1, ECO:0000313|Proteomes:UP000002044}; RN [1] {ECO:0000313|EMBL:CBH27797.1, ECO:0000313|Proteomes:UP000002044} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35967 / DSM 20751 / CIP 100100 / SLCC 3954 RC {ECO:0000313|Proteomes:UP000002044}; RX PubMed=20061480; DOI=10.1128/JB.01415-09; RA Steinweg C., Kuenne C.T., Billion A., Mraheil M.A., Domann E., RA Ghai R., Barbuddhe S.B., Karst U., Goesmann A., Puhler A., RA Weisshaar B., Wehland J., Lampidis R., Kreft J., Goebel W., RA Chakraborty T., Hain T.; RT "Complete genome sequence of Listeria seeligeri, a nonpathogenic RT member of the genus Listeria."; RL J. Bacteriol. 192:1473-1474(2010). CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN557490; CBH27797.1; -; Genomic_DNA. DR RefSeq; WP_012985848.1; NC_013891.1. DR RefSeq; YP_003464883.1; NC_013891.1. DR ProteinModelPortal; D3UNW4; -. DR EnsemblBacteria; CBH27797; CBH27797; lse_1646. DR KEGG; lsg:lse_1646; -. DR PATRIC; 32263185; VBILisSee138575_1639. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR BioCyc; LSEE683837:GI10-1669-MONOMER; -. DR Proteomes; UP000002044; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002044}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 617 AA; 68592 MW; 873759CBCB163714 CRC64; MNLRKDLSEK VLIADGAMGT LLYSYGVDRS FEELNLSHPE DIIAIHKAYI GAGADIIQTN TYGANYIKLS RYGLEDQVKR INQAAIRLAK EAARGTGTYI FGTIGGINGA VDAKLPATPL EEIKRSFREQ LYCFLLEGVD AILLETYYDL DELKTVLKII RETTDLPVVA NVSMHEPGLL QNGQKLSDAL EELIALGADV VGVNCRLGPY HMARALETVP LYDHAYLAVY PNASLPEMQE GKVIYQSDTD YFEHYGEVFR QGGARIIGGC CGTTPDHIRA LRKGLKSIKP VLTKEVRPIL ELVPEEVVDE DSGERLLDKV KERLTILVEL DPPRTFDTTK FFEGAKALDE AGVDAITISD NSLATPRISN MALASILKHE YGIKPLIHLT TRDHNLVGMH SHVMGFHKLG LHDVLAITGD PTKVGDFPGA SSVFDLRSVE LVQLIKKFND GISYTGKSLK EKARFHVGAA FNPNVLNLEK AIRLIERKVE YGADYIITQP IYDVNKAVLL KEALQKANIK VPLFIGVMPL LSSRNAEFLH NEVPGIRLTD EVRERMREAE EHGSANEEGM QIARELIDSI CTCFQGIYII TPFLRYDLSI ELAKYVQSKQ QVQIVSK // ID D4BDB6_9ENTR Unreviewed; 310 AA. AC D4BDB6; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 27-MAY-2015, entry version 11. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFE07965.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EFE07965.1}; GN Name=mmuM {ECO:0000313|EMBL:EFE07965.1}; GN ORFNames=CIT292_08483 {ECO:0000313|EMBL:EFE07965.1}; OS Citrobacter youngae ATCC 29220. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Citrobacter; Citrobacter freundii complex. OX NCBI_TaxID=500640 {ECO:0000313|EMBL:EFE07965.1}; RN [1] {ECO:0000313|EMBL:EFE07965.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29220 {ECO:0000313|EMBL:EFE07965.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFE07965.1}. 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; ABWL02000009; EFE07965.1; -; Genomic_DNA. DR RefSeq; WP_006685795.1; NZ_GG730299.1. DR EnsemblBacteria; EFE07965; EFE07965; CIT292_08483. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFE07965.1}; KW Transferase {ECO:0000313|EMBL:EFE07965.1}. SQ SEQUENCE 310 AA; 33467 MW; EA5720AE8EAC72E2 CRC64; MSQHNPLRAL LEKQDFLLLD GAMATELEAR GCNLADSLWS AKVLVENPQL IREVHLDYYR AGAQCAITAS YQATPAGLAA RGLDEAQSKA LIGKSVELAR KAREAYLAEN PQAGTLLVAG SVGPYGAYLA DGSEYRGDYQ RSVGALQAFH RPRVEALLDA GADLLACETL PNFTEIGALA ELLTAYPRAR AWFSFTLRDS EHLSDGTPLR DVVALLAGYP QVVALGINCI ALEKTTAALQ HLHGLTALPL VVYPNSGEQY DAASKTWHHH GEHCAHLADY LPQWRAAGAR LIGGCCRTTP KDIAELNAQR // ID D4BKX9_9ENTR Unreviewed; 1227 AA. AC D4BKX9; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFE05555.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFE05555.1}; GN Name=metH {ECO:0000313|EMBL:EFE05555.1}; GN ORFNames=CIT292_11209 {ECO:0000313|EMBL:EFE05555.1}; OS Citrobacter youngae ATCC 29220. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Citrobacter; Citrobacter freundii complex. OX NCBI_TaxID=500640 {ECO:0000313|EMBL:EFE05555.1}; RN [1] {ECO:0000313|EMBL:EFE05555.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29220 {ECO:0000313|EMBL:EFE05555.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFE05555.1}. 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; ABWL02000036; EFE05555.1; -; Genomic_DNA. DR RefSeq; WP_006688340.1; NZ_GG730304.1. DR EnsemblBacteria; EFE05555; EFE05555; CIT292_11209. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFE05555.1}; KW Transferase {ECO:0000313|EMBL:EFE05555.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135790 MW; 4D57CCF65EC1577D CRC64; MSSKVEQLRQ QLNERILVLD GGMGTMIQGY RLNEEDFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA YRNITFDQLV AAYRESTKAL VEGGCDLILI ETVFDTLNAK AAIFAVKTEF EALGVELPIM LSGTITDASG RTLSGQTTEA FYNSLRHADA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAAQIREWAE AGFLNVVGGC CGTTPEHIAA MSRAVDGLPP RKLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VESGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVEAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ MAEWRSWDVK KRLEYSLVKG ITEFIELDTE EARLQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EKGSSNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIIDL GVMVPAEKIL KTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLAAAR ENDLAFDWES YTPPVAHRLG VQAVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG EEAKRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKVGFAN YCLSDFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA IADRLAEAFA EYLHERVRKV YWGYAANENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLDVEAH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYALRKGMS VAEVERWLAP NLGYDAD // ID D4BZU0_PRORE Unreviewed; 1227 AA. AC D4BZU0; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFE53464.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFE53464.1}; GN Name=metH {ECO:0000313|EMBL:EFE53464.1}; GN ORFNames=PROVRETT_07843 {ECO:0000313|EMBL:EFE53464.1}; OS Providencia rettgeri DSM 1131. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Providencia. OX NCBI_TaxID=521000 {ECO:0000313|EMBL:EFE53464.1}; RN [1] {ECO:0000313|EMBL:EFE53464.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 1131 {ECO:0000313|EMBL:EFE53464.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFE53464.1}. 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; ACCI02000055; EFE53464.1; -; Genomic_DNA. DR RefSeq; WP_004261329.1; NZ_GG705263.1. DR EnsemblBacteria; EFE53464; EFE53464; PROVRETT_07843. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFE53464.1}; KW Transferase {ECO:0000313|EMBL:EFE53464.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136398 MW; 7953201DC83823C0 CRC64; MSAKVNQLEQ ELKKRILVLD GAMGTMIQQH KLSEAQFRGE RFADWPSDLK GNNDLLVLTQ PDIIRDIHSQ YFEAGADIVE TNTFNSTSIA MADYKMESLS AEINEVAARL ARECADEWTR KTPDQPRYVA GVLGPTNRTA SISPDVNDPA YRNITFDQLV EAYRESTRSL VKGGVDLIMI ETIFDTLNAK AAIFAVETEL EALGVSLPIM ISGTITDASG RTLSGQTTEA FYNSLRHAQP ISFGLNCALG PDELRQYIAE LSRIAECYVS AHPNAGLPNA FGEYDLDAQN MAEQIHEWAT AGFLNIVGGC CGTTPLHIKK MAEAVKGIAP RQLPSLPVEC RLSGLEPLNI GEKSLFVNVG ERTNVTGSAK FKRLIKEENY QEALDVARQQ VENGAQIIDI NMDEGMLDSH AAMVRFLNLI AGEPDIARVP IMIDSSKWEV IEAGLKCIQG KGIVNSISMK EGVEAFIEHA KLLRKYGAAV VVMAFDEVGQ ADTRERKIEI CRRAYQILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAV DFIEVCKDIK AQLPHAMISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPT ELKDAVEDVI LNRRDDSTEC LLELAEKYRG AGAGEQQVQQ AEWRSWEVEK RLEYALVKGI TEFIIEDTEE TRQRASSPIE VIEGPLMNGM NVVGDLFGEG KMFLPQVVKS ARVMKQAVAY LEPYIQELKQ SGSSAGKILL ATVKGDVHDI GKNIVGVVLQ CNNYEIIDLG VMVPCETILK TAREENVDII GLSGLITPSL DEMVHVAKEM ERQGFTLPLL IGGATTSKAH TAVKIEPNYS GPTTYVQNAS RTVGVVAALL SATQKADFVA RTRREYETVR QQHGRRRPKT PPVALDVARA NAVNIDWQHY QPPVPKFLGI QEVTASISTL RNYIDWTPFF MTWSLAGKYP RILEDEVVGS EARKLLKDAN NMLDKLDKEN LLTPKGIFGL FPANRVGDDI EIYTDESRNH VQVMGLNLRQ QTLKTEFPNY CLSDFVAPKD SGKADYIGAF AVTGGLEEDA LADAYEQQHD DYNKIMVKAL ADRLAEAFAE YLHQQVRMQY WGYADDENLS NEELIRENYQ GIRPAPGYPA CPEHTEKAKI WQLLDVETQI GMQLTSSYAM WPGASVSGWY FSHPESKYFA VAQLQKDQIE DYAKRKGMSV TELERWLAPN LAYDPED // ID D4C7Y5_9CLOT Unreviewed; 835 AA. AC D4C7Y5; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 01-OCT-2014, entry version 19. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFE14673.1}; GN ORFNames=CLOM621_05504 {ECO:0000313|EMBL:EFE14673.1}; OS Clostridium sp. M62/1. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=411486 {ECO:0000313|EMBL:EFE14673.1}; RN [1] {ECO:0000313|EMBL:EFE14673.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M62/1 {ECO:0000313|EMBL:EFE14673.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFE14673.1}. 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; ACFX02000003; EFE14673.1; -; Genomic_DNA. DR RefSeq; WP_008395107.1; NZ_GG730309.1. DR EnsemblBacteria; EFE14673; EFE14673; CLOM621_05504. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFE14673.1}; KW Transferase {ECO:0000313|EMBL:EFE14673.1}. SQ SEQUENCE 835 AA; 90294 MW; D03E07878FB890BB CRC64; MSIAERQTGK KSRLLHELAE RILFFDGGTG SLLQAAGLKP GELPETWNIR RPEVIVKLHR DYLDAGCDII NTNTFGANRL KFNENTEFGL KEIIEAAVRN AREAVNLAGH GYIALDLGPT GRLLKPMGDL DFETAVEIYR EAAGIGIRAG VDLVLIETMS DSYELKAAVL GVKEALAGDG ISGEQADLPV FATTIFDEKG KLLTGGTPRT VIALLEGLGV DAVGINCGLG PVQMKEFVRE FAKYASVPII VNPNAGLPRS VEGRTVYDID EDQFAKTMAE IVDMGASVVG GCCGTTPEYI RKLCLACREK KQKLPSKKAE TVVTSYSQLV EIASDPVIIG ERINPTGKPK FKQALRDHDM EYILREGLAQ QDSGAQVLDV NVGLPEIDEP SMMEEAVREL QSILDLPLQI DTSNIEAMER AMRIYNGKPL INSVNGKAES MDAIFPLVKK YGGVVVALTL DEEGIPDTAD GRIRVAEKIY RRAAQYGIDK KDILIDTLCM TISSDSQGAL TTLEAVRRIR DELHGKTILG VSNVSFGLPQ RESINAAFFT MAMMNGLSAA IINPNSDAMM RSWRSFRALA ALDENCGDYI SAYGGQTKQQ PSDTVFGKGE AVSEKAPEEV QEIHESHKSQ VQLWESVVRG LKEQAARAAA AALKEASPLE VINACMIPAL DCVGKGFEQG TVFLPQLLMS AEAAKAAFEV LKAAMAGSGK SQEKKGVIIL ATVRGDIHDI GKNIVKVLLE NYSYEVVDLG KDVPPERIAE ETVKHRAPLV GLSALMTTTV PSMEETIRLL RKEAGWAKIM VGGAVLTPEY ADSIGADAYC KDAMASVNYA QKVIG // ID D4CWW1_9FUSO Unreviewed; 1081 AA. AC D4CWW1; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Vitamin B12 dependent methionine synthase, activation domain protein {ECO:0000313|EMBL:EFE86176.1}; GN ORFNames=FUSPEROL_01920 {ECO:0000313|EMBL:EFE86176.1}; OS Fusobacterium periodonticum ATCC 33693. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=546275 {ECO:0000313|EMBL:EFE86176.1}; RN [1] {ECO:0000313|EMBL:EFE86176.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33693 {ECO:0000313|EMBL:EFE86176.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFE86176.1}. 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; ACJY01000096; EFE86176.1; -; Genomic_DNA. DR RefSeq; WP_005974395.1; NZ_GG665898.1. DR EnsemblBacteria; EFE86176; EFE86176; FUSPEROL_01920. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 723 723 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1081 AA; 120693 MW; DE8BEF932F0F4922 CRC64; MFEFEKELRE RILVLDGAMG TVLQKYELTP EDFNGAKGCY EILNETRPDI IFEVHKKYIE AGADIIETNS FNCNAISLKD YHLEDKVYDL AKKSAEIARD AVKESGKKVY VFGAIGPTNK SLSFPVGDVP YKRAVSFDEM KEVIKVQVAG LIDGGVDGIL LETIFDGLTA KAALLATEEV FEEKNVKLPI SISATVNRQG KLLTGQSIES LIVALDRDSV TSFGFNCSFG AKDLVPLVIK IKELTTKFVS LHANAGLPNQ NGDYVETAQK MRDDLLPLIE NQAINILGGC CGTNYDHIRA IAELVKDQKP RVLPKENLLE TCLSGNEIYN FNDKFTCVGE RNNISGSKLF RTMIEEHNYL KALEVARQQI DAGAKVLDIN VDDGILDSVE EMKNFLRVLQ NDSFIAKIPI MIDSSDFAVI EEGLKNTSGK AIVNSISLKE GTEEFLRKAK IIRNFGASIV VMAFDEKGQG VSAERKIEIC QRAYDLLKSI GVKNSDIVFD PNILSVGTGQ EADRYHAREF IKTIDYIHEN LKGCGVVGGL SNLSFAFRGN NVLRAAFHHI FLEEAVPRGF NFAILNPKEK APQWTDEERE KIKSFIFGDS TDMEALLSLN LVKRKEDAQI FAETPEDKIR KALIQGGSES LQEVIGDLLK KYKALEILEN ILMSAMQEIG RLFEQGELYL PQLIRSASVM NNCVDILTPY LDKVDKASSK GKILMATVDG DVHDIGKNIV GTVLECNGYE VIDLGVMVPR DKIVEKAKEI NADVVTLSGL ISPSLKEMER VADLFQKVGM QVPILIAGAA TSKLHTGLKV LPNYDYSLHV TDAMDTITVV SQLLSTKRKD FLETKQTQLR KIAKRYMDNN NETEEKKVFT EVKKTVSYIP KVLGKQFLSL PVEIFKDNLK WDIALYALRV KNTPEEEKTL SDLKKIYEKL IEEKVEFRAA YGYFRCKKTE TFLEMEGMTF EISPNLAQYI EKEDYVGGFV ISVGSKIFKD DKYLGLLETL LCNAIAETAS EYMETRVSED IVPTFLRPAV GYPILPDHSL KKVVFDLIDG ERTGAKLSPA FAMTPLSTVC GFYLCNDNAK Y // ID D4E0I9_SEROD Unreviewed; 1226 AA. AC D4E0I9; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFE96638.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFE96638.1}; GN Name=metH {ECO:0000313|EMBL:EFE96638.1}; GN ORFNames=HMPREF0758_1689 {ECO:0000313|EMBL:EFE96638.1}; OS Serratia odorifera DSM 4582. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Serratia. OX NCBI_TaxID=667129 {ECO:0000313|EMBL:EFE96638.1}; RN [1] {ECO:0000313|EMBL:EFE96638.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 4582 {ECO:0000313|EMBL:EFE96638.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFE96638.1}. 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; ADBY01000029; EFE96638.1; -; Genomic_DNA. DR RefSeq; WP_004957823.1; NZ_GG753567.1. DR EnsemblBacteria; EFE96638; EFE96638; HMPREF0758_1689. DR PATRIC; 36061244; VBISerOdo144996_0949. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFE96638.1}; KW Transferase {ECO:0000313|EMBL:EFE96638.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1226 AA; 135629 MW; F46821EBA3542829 CRC64; MTNRVEQLRQ QLAQRILLLD GGMGTMIQSY GLLEEDYRGE RFADWQSDLK GNNDLLVLTR PEIITAIHDG YLAAGADILE TNTFNATPIA MADYHMESLS AEINYQAACL ARACADAWTA RTPQRPRYVA GVLGPTNRTA SISPNVNDPA FRNVSFDELV AAYRESTRAL VAGGVDLIMI ETIFDTLNAK AAAFAVETEF EALGVTLPIM ISGTITDASG RTLSGQTTEA FYNSLRHVKP LSFGLNCALG PDELRQYVAE LARISESYVT AHPNAGLPNA FGEYDLDAEE MAKQVSEWAH AGFLNIIGGC CGTTPAHIAA MAKAVEGVPP RRLPDIPVAC RLSGLEPLNI DAKSLFVNVG ERTNVTGSAR FKRLIKEEKY NEALDVARQQ VESGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWQV IEKGLKCIQG KGIVNSISMK EGEEAFIHHA KLVRRYGAAV VVMAFDEVGQ ADTRERKFDI CRRAYKILTE RVGFPPEDII FDPNIFAVAT GIDEHNNYAV DFIEACADIK THLPHAMISG GVSNVSFSFR GNDPVREAIH AVFLYHAIRN GMDMGIVNAG QLAIYDDLSA ELRDAVEDVV LNRRPDGTER LLELAEKYRG SKDNEVAVQQ AEWRGWPVAK RLEYSLVKGI TEFIELDTEE ARQQATRPIE VIEGPLMAGM NVVGDLFGEG KMFLPQVVKS ARVMKQAVAY LEPYIQASKQ QGSSAGKILL ATVKGDVHDI GKNIVGVVLQ CNNYEIIDLG VMVPTDKILK TARDENVDII GLSGLITPSL DEMVNVAKEM ERQGFTLPLL IGGATTSKAH TAVKIEQNYS GSTTYVQNAS RTVGVVSALL SDTQRDAFVA RTRKEYETVR IQHGRKKPRT PPVSLEKARA NAMALDWDSY SPPVPRQLGV FPVEADIATL RHYIDWTPFF MTWSLAGKYP RILQDEVVGE EAKRLFDDAN QMLDMLAARH SLNPRGVYGL FPANSVGDDV EIYRDERRDE VLVVSRHLRQ QTEKTDFPNY CLADFVAPKS SGKADYFGAF AVTGGLEEDD LAAAYDAQHD DYNKIMVKAL SDRLAEAFAE YLHEQVRKLH WGFAADENLN NEELIRENYQ GIRPAPGYPA CPEHTEKAEI WQLLDVNRHT GMVLTESFAM WPGAAVSGWY FSHPQSKYFA VAQIQRDQVE DYAARKGMSV SEVERWLAPN LGYDAD // ID D4E388_SEROD Unreviewed; 318 AA. AC D4E388; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 27-MAY-2015, entry version 12. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFE95664.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EFE95664.1}; GN Name=mmuM {ECO:0000313|EMBL:EFE95664.1}; GN ORFNames=HMPREF0758_2638 {ECO:0000313|EMBL:EFE95664.1}; OS Serratia odorifera DSM 4582. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Serratia. OX NCBI_TaxID=667129 {ECO:0000313|EMBL:EFE95664.1}; RN [1] {ECO:0000313|EMBL:EFE95664.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 4582 {ECO:0000313|EMBL:EFE95664.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFE95664.1}. 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; ADBY01000045; EFE95664.1; -; Genomic_DNA. DR RefSeq; WP_004960084.1; NZ_GG753567.1. DR EnsemblBacteria; EFE95664; EFE95664; HMPREF0758_2638. DR PATRIC; 36062985; VBISerOdo144996_1836. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFE95664.1}; KW Transferase {ECO:0000313|EMBL:EFE95664.1}. SQ SEQUENCE 318 AA; 34460 MW; 3F1DF82C680433BE CRC64; MQEKNMSVNN PLAPLLADGR SLILDGALAT ELETRGCDLS DPLWSAKVLI ENPELIYQVH LDYFNAGAQC AITASYQATP QGFLRRGLDE QQSLALIAKS VQLAQQARRD YLAQRPQAEP LLIAGSVGPY GAFLADGSEY RGDYRLPAAE MIAFHRPRIA ALAQAGVDLL ACETLPSFDE LHALLTLLRD FPSLGAWFSF TLRDSHHLSD GTPLTEVIAL LNHNPQVLAI GVNCIALENV TPALQTLATL TSLPLLVYPN SGEHYDAVSK TWHACGGEYG SLSEQAGDWQ QIGARLIGGC CRTTPKDIRA IAEQLASR // ID D4F072_EDWTA Unreviewed; 1229 AA. AC D4F072; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 01-APR-2015, entry version 24. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFE24837.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFE24837.1}; GN Name=metH {ECO:0000313|EMBL:EFE24837.1}; GN ORFNames=EDWATA_00095 {ECO:0000313|EMBL:EFE24837.1}; OS Edwardsiella tarda ATCC 23685. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Edwardsiella. OX NCBI_TaxID=500638 {ECO:0000313|EMBL:EFE24837.1}; RN [1] {ECO:0000313|EMBL:EFE24837.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 23685 {ECO:0000313|EMBL:EFE24837.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFE24837.1}. 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; ADGK01000007; EFE24837.1; -; Genomic_DNA. DR EnsemblBacteria; EFE24837; EFE24837; EDWATA_00095. DR PATRIC; 36078133; VBIEdwTar109008_0103. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFE24837.1}; KW Transferase {ECO:0000313|EMBL:EFE24837.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 249 249 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1229 AA; 135429 MW; A04929D214BB16FA CRC64; MRVNTTLERL RRRLEKRILL LDGGMGTMIQ RYGLSEQDFR ADRFADWPCD LKGNNDLLVL TRPDIISAIH YAYLEAGADI LETNTFNATR IAMADYRMEA LAPEINYQAA CLARACADEW TARTPHQPRF VAGILGPTNR TASISPEVND PACRNITFDQ LVDAYRESAR ALIEGGVDLL MIETVFDTLN AKAAVYALEC EFAELGVTLP VMISGTITDA SGRTLSGQTT EAFYNSLRHA RPLSFGLNCA LGPEDLRQYV AELSRIAECY VSAHPNAGLP NAFGEYDLSP QAMAQQIAEW AQAGYLNIVG GCCGTTPEHI AAISQAVRDI APRTRPLPAR ACRLAGLEPL TIDEQTLFVN VGERTNVTGS ARFKRLIKEN NYDEALEVAR QQVESGAQII DINMDEGMLD AEAAMVRFLN LIAGEPDIAR VPLMIDSSRW SVIEAGLKCI QGKGIVNSLS LKEGEAAFLE HARQVRRYGA ALVVMAFDEQ GQADSRERKV AICRRAYQLL TERLDFPPED IIFDPNIFAV ATGIEEHSNY ALDFIDACAE IKAQLPHALI SGGVSNVSFS FRGNETVREA IHAVFLYHAI RHGMDMGIVN AGQLAIYDSL PDDLRAAAEA VILNQSPDAT EHLLALAERY RGVPGEGSGE AQRAEWRDWP VAQRLEYALV KGIGEFVEQD TEEARQQVDR PIAVIEGPLM AGMNRVGDLF GDGKMFLPQV VKSARVMKQA VAYLSPFIEA SKQRGSSAGK VLLATVKGDV HDIGKNIVGV VLQCNNYEII DLGVMVPAER ILRVAREEQV DIIGLSGLIT PSLDEMVNVA SEMERQGFTL PLLIGGATTS KAHTAVKIAP AYSGPTVYVQ NASRTVGVVA ALLSEVQRPA FLARISAEYE TARAQHGRRT PRTPPLPLAQ ARANALATDW THYTPPRPPQ LGVQTVQPGI ATLRRYIDWT PFFLTWSLAG KYPRILEDEV VGEEARRLLA DANHLLDDLV ANASLTPRGV FGLFAANRCG DDVLIYRDDT RREVLAVSHH LRQQSSKPSG ANYCLADFVA TKESGIADYI GAFAVTGGLE EERLAQAFEA QHDDYHKIMV KALADRLAEA FAEYLHEQVR KVHWGYAADE ALDNEQLIRE NYRGIRPAPG YPACPEHSEK ATLWRLLDVE AQCGMRLTES YAMWPGASVS GWYFSHPESK YFAVARIQRD QVEDYAARKG IRLAEAEYWL APNLGYDPE // ID D4FLW9_STAEP Unreviewed; 612 AA. AC D4FLW9; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 27-MAY-2015, entry version 25. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HMPREF0794_1557 {ECO:0000313|EMBL:EFE58587.1}; OS Staphylococcus epidermidis M23864:W2(grey). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=525375 {ECO:0000313|EMBL:EFE58587.1, ECO:0000313|Proteomes:UP000004733}; RN [1] {ECO:0000313|EMBL:EFE58587.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M23864:W2 {ECO:0000313|EMBL:EFE58587.1}; 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 (NOV-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFE58587.1}. 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; ADMU01000038; EFE58587.1; -; Genomic_DNA. DR RefSeq; WP_002456825.1; NZ_GG749255.1. DR ProteinModelPortal; D4FLW9; -. DR EnsemblBacteria; EFE58587; EFE58587; HMPREF0794_1557. DR PATRIC; 36660640; VBIStaEpi43789_1210. DR Proteomes; UP000004733; Unassembled WGS sequence. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004733}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EFE58587.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EFE58587.1}. SQ SEQUENCE 612 AA; 67913 MW; 1635B2791B471D29 CRC64; MSHLLNQLKS NVLVADGAIG TIFYSEGLDT CPEAYNLTHP DKVERIHRSY IEAGADVIQT NTYGANFEKL KSFGLEHKVK EIHQAAVQIA KRAANEDTII LGTVGGFRGV RQEDISLSTI QYHTELQIDT LIDEGVDALL FETYYDLDEL TRIVTATRQK YDIPIIAQLT ASNTNYLVDG TEINAALKYV VECGANVVGL NCHHGPHHMQ RSFSHIELPK HAYLSCYPNA SLLDIENSEF KYSDNAQYFG DIAQELINEG VRLIGGCCGT TPEHIRYIKS AVKHLKPVKD KKVIPINKAS SQKQTRVLKQ NLTSKVKNGP TVIVELDTPK HLDTDTFFDN VGKLDEAGID AVTLADNSLA TVRVSNIAAA SLIKQRYDIE PLVHVTCRDR NLIGLQSHLL GLSLIGVNEI LAITGDPSKV GHLPGATNVY DVNSKGLTEL ALRFNKGINT DGDALKKHTN FNIAGAFDPN VRKLDGAIKR LEKKVASGMS YFITQPVYSK EKIIQVYEET KHLNTPFFIG IMPIASYNNA LFLHNEVPGI KMSDDVLNQF KAVKDDKEKT KELSLRLSKE LIDTVHEYFN GLYIITPFQK VDYSLELAAY SKSITANKEA IL // ID D4FUX2_BACNB Unreviewed; 612 AA. AC D4FUX2; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 27-MAY-2015, entry version 29. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN Name=yitJ {ECO:0000313|EMBL:BAI84653.1}; GN ORFNames=BSNT_07540 {ECO:0000313|EMBL:BAI84653.1}; OS Bacillus subtilis subsp. natto (strain BEST195). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=645657 {ECO:0000313|EMBL:BAI84653.1, ECO:0000313|Proteomes:UP000006805}; RN [1] {ECO:0000313|EMBL:BAI84653.1, ECO:0000313|Proteomes:UP000006805} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BEST195 {ECO:0000313|EMBL:BAI84653.1, RC ECO:0000313|Proteomes:UP000006805}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; BAI84653.1; -; Genomic_DNA. DR RefSeq; WP_014479414.1; NC_017196.2. DR RefSeq; YP_005560356.1; NC_017196.2. DR ProteinModelPortal; D4FUX2; -. DR EnsemblBacteria; BAI84653; BAI84653; BSNT_07540. DR KEGG; bso:BSNT_01860; -. DR PATRIC; 42729781; VBIBacSub97792_2069. DR KO; K00547; -. DR Proteomes; UP000006805; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006805}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:BAI84653.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:BAI84653.1}. SQ SEQUENCE 612 AA; 68028 MW; 9962F24A2390F2B3 CRC64; MGLLEDLQRQ VLIGDGAMGT LLYSYGIDRC FEELNISKPE EIQRIHKAYV EAGANIIQTN TYGANYIKLS RHGLEDDIKK MNQEAVKIAR ASAGDAYVLG TMGGIRTFNK NAYSLDEIKR SFREQLYLLL HEEPDGLLLE TYYDLEEARE VLKIARKETD LPIMLNVSMH EQGVLQDGTP LSDALRSIAD LGADIVGINC RLGPYHMIEA LSEVPIFDDV FLSVYPNSSL PSLEEGRLVY ETDDTYFQNS ASEFRKQGAR IIGGCCGTTP NHIRAMAEAV GGLVPIKEKE VKTRAKEFIS VHHERTEPGL DEIAAKKRSI IVELDPPKKL SFDKFLSAAA ELKEAGIDAL TLADNSLATP RISNVACGAL IKQQLDMRSL VHITCRDRNI IGLQSHLMGL DTLGLNDVLA ITGDPSKIGD FPGATSVYDL TSFDLIRLIK QFNEGLSLSG KPLGKKTNFS VAAAFNPNVR HLDKAVKRLE KKIDCGADYF VSQPVYSEQQ LVDIHNEIKH LKTPIYIGIM PLTSSRNAEF IHNEIPGIKL SDTIREKMAR AGEDKEKQKA EGLAIARSLL DTACELFNGI YLITPFLRSD LTAELTSYIQ QKDEQRQNIF LH // ID D4G4N3_BACNB Unreviewed; 315 AA. AC D4G4N3; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:BAI83689.1}; GN Name=mmuM {ECO:0000313|EMBL:BAI83689.1}; GN ORFNames=BSNT_06549 {ECO:0000313|EMBL:BAI83689.1}; OS Bacillus subtilis subsp. natto (strain BEST195). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=645657 {ECO:0000313|EMBL:BAI83689.1, ECO:0000313|Proteomes:UP000006805}; RN [1] {ECO:0000313|EMBL:BAI83689.1, ECO:0000313|Proteomes:UP000006805} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BEST195 {ECO:0000313|EMBL:BAI83689.1, RC ECO:0000313|Proteomes:UP000006805}; 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; BAI83689.1; -; Genomic_DNA. DR RefSeq; WP_014478701.1; NC_017196.2. DR RefSeq; YP_005559392.1; NC_017196.2. DR EnsemblBacteria; BAI83689; BAI83689; BSNT_06549. DR KEGG; bso:BSNT_00427; -. DR PATRIC; 42727789; VBIBacSub97792_1115. DR KO; K00547; -. DR Proteomes; UP000006805; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006805}; KW Methyltransferase {ECO:0000313|EMBL:BAI83689.1}; KW Transferase {ECO:0000313|EMBL:BAI83689.1}. SQ SEQUENCE 315 AA; 34707 MW; 1918D5EC2BB37B4C CRC64; MNPIQHILDT YPLIVLDGAM ATELERKGCN LNDSLWSAKI LMEEPNLIKQ VHTDYFAAGA DCAITASYQS TFEGFAARGL SEAEARRLIE LSVSIAAEAR DEFWSLEENR LNRPKPIIAA SVGPYGAYLA DGSEYRGNYA ISEDELIEFH RPRMKALIEA GADVLACETI PCLTEAKAIV RLLKEFPETY AWISFSAKDG LHISDGTPAA DCASWLDEHR QIAALGINCT PLQHIPSLIE ELKKNTSKPI IVYPNSGEQY DPETKTWNGA ACAESYGASA RTWHEKGARL IGGCCRTKPE NIQEIAAWAR SLKTT // ID D4GH93_PANAM Unreviewed; 1248 AA. AC D4GH93; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 27-MAY-2015, entry version 38. DE SubName: Full=MetH {ECO:0000313|EMBL:ADD75408.1}; GN Name=metH {ECO:0000313|EMBL:ADD75408.1}; GN OrderedLocusNames=PANA_0241 {ECO:0000313|EMBL:ADD75408.1}; OS Pantoea ananatis (strain LMG 20103). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Pantoea. OX NCBI_TaxID=706191 {ECO:0000313|EMBL:ADD75408.1, ECO:0000313|Proteomes:UP000001702}; RN [1] {ECO:0000313|EMBL:ADD75408.1, ECO:0000313|Proteomes:UP000001702} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 20103 {ECO:0000313|EMBL:ADD75408.1, RC ECO:0000313|Proteomes:UP000001702}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001875; ADD75408.1; -; Genomic_DNA. DR RefSeq; WP_013024141.1; NC_013956.2. DR RefSeq; YP_003518536.1; NC_013956.2. DR EnsemblBacteria; ADD75408; ADD75408; PANA_0241. DR KEGG; pam:PANA_0241; -. DR PATRIC; 35381253; VBIPanAna151616_0254. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; PANA706191:GJNK-260-MONOMER; -. DR Proteomes; UP000001702; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001702}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 268 268 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 331 331 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 332 332 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 780 780 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1248 AA; 137977 MW; 829BE3FCA4C7F358 CRC64; MTLCKNDWLV FHQRIDVDEI TVSNLTDALH QQLAHRIMVL DGGMGTMIQS YKLDEHDFRG SRFADWPCDL KGNNDLLVLS KPEVIREIHD AYLAAGADIL ETNTFNATSI AMADYQMEAL SAEINFAAAK LARTCADAWT AKTPDKPRYV AGVLGPTNRT CSISPDVNDP AFRNITFNQL VDAYRESTRA LVEGGCHIIM IETVFDTLNA KAAVFAVKAE MEALGVALPL MISGTITDAS GRTLSGQTTE AFYNSLRHAE PLSFGLNCAL GPDELRQYVA ELSRIAEGYV TAHPNAGLPN AFGEYDLDAE VMAQQIGEWA NAGFLNIVGG CCGTTPQHIA AMAAAVEGVA PRQRPKLPVA CRLSGLEPLN ISAESLFVNV GERTNVTGSA KFKRLIKEDK YHEALEVALQ QVESGAQIID INMDEGMLDA EAAMVRFLNL IAGEPDIARV PIMIDSSKWE VIEKGLQCIQ GKGIVNSVSM KEGEAVFIHH ARLIRRYGAA MVVMAFDEVG QADTRERKIE ICRRAYQILT QQVGFPPEDI IFDPNIFAVA TGINEHNNYA MDFIGACEDI KRELPHAMIS GGVSNVSFSF RGNDPVREAI HAVFLYYAIR NGMDMGIVNA GQLAIYDDLS DELRESVEDV ILNRRADGTE RLLALAEKYR RNKSDSADEK QQAEWRGWDV VKRLEYSLVK GITEFIEQDT EEARQQAARP IDVIEGPLMS GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AWLEPYIQAS KEAGRSNGKV VLATVKGDVH DIGKNIVGVV LQCNNYEIID LGVMVPGEKI LKTAREVKAD IIGLSGLITP SLDEMVNMAK EMERQGFTLP LLIGGATTSK AHTAVKIEQH YSGPTVYVQN ASRTVGVVSS LLSDTLRDDF VARTRKEYET VRIQHARKKP RTPPVSLSAA RDNATKIDWD SYTPPVAKHV GVRRVDAGID VLRNYIDWTP FFMTWSLAGK YPRILEDEVV GDEAKRLFAD ANAMLDKLSD EKALTPRGVV GLFPANRVGD DIHIFADEQR DTLLNISHHL RQQTEKTDFA NYCLADFVAP KSSGKADYIG AFAVTGGLEE DALAEAYDKQ QDDYNKIMVK AIADRLAEAF AEYLHEQVRK TIWGFAPDEH LSNEALIREN YQGIRPAPGY PACPEHTEKA TIWALLDVET HAGMKLTESF AMWPGASVSG WYFSHPDSRY FAVAQIQRDQ VEDYAARKRM SVSEVERWLA PNLGYDAD // ID D4GKW3_PANAM Unreviewed; 341 AA. AC D4GKW3; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 01-APR-2015, entry version 25. DE SubName: Full=MmuM {ECO:0000313|EMBL:ADD78152.1}; GN Name=mmuM {ECO:0000313|EMBL:ADD78152.1}; GN OrderedLocusNames=PANA_2985 {ECO:0000313|EMBL:ADD78152.1}; OS Pantoea ananatis (strain LMG 20103). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Pantoea. OX NCBI_TaxID=706191 {ECO:0000313|EMBL:ADD78152.1, ECO:0000313|Proteomes:UP000001702}; RN [1] {ECO:0000313|EMBL:ADD78152.1, ECO:0000313|Proteomes:UP000001702} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 20103 {ECO:0000313|EMBL:ADD78152.1, RC ECO:0000313|Proteomes:UP000001702}; 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 ----------------------------------------------------------------------- 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; ADD78152.1; -; Genomic_DNA. DR RefSeq; WP_013026857.1; NC_013956.2. DR RefSeq; YP_003521280.1; NC_013956.2. DR EnsemblBacteria; ADD78152; ADD78152; PANA_2985. DR KEGG; pam:PANA_2985; -. DR PATRIC; 35387046; VBIPanAna151616_3104. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR BioCyc; PANA706191:GJNK-3062-MONOMER; -. DR Proteomes; UP000001702; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001702}. SQ SEQUENCE 341 AA; 36915 MW; 39CEFE9207A8A3A2 CRC64; MPCGAEFRLC CFAMALTMSR TKKHRLRRPG MSHNPVSRAL QQSAPLILDG ALATELEARG CDLADALWSA KVLVENPELI YQVHYDYFAA GARCAITASY QATPQGFAAR GLNETQSLAL IAQSVELAKR ARADYLATQA EAKILLVAGS VGPYGAFLAD GSEYRGDYAL PETEMMAFHR PRINALLTAG VDVLACETLP SFAEAQALVA LLGEFPDSRA WFSFTLRDAE HISDGTPLRE VAAYLNAQPQ VVALGINCIA LESVTPALQQ LQRLTDKPLV VYPNSGEQYD ASSKTWHSAP SGCTLHDKFS EWQQAGARLI GGCCRTSPKD IAAIARHCQP Q // ID D4H5Z8_DENA2 Unreviewed; 1116 AA. AC D4H5Z8; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 27-MAY-2015, entry version 37. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADD67644.1}; GN OrderedLocusNames=Dacet_0864 {ECO:0000313|EMBL:ADD67644.1}; OS Denitrovibrio acetiphilus (strain DSM 12809 / N2460). OC Bacteria; Deferribacteres; Deferribacterales; Deferribacteraceae; OC Denitrovibrio. OX NCBI_TaxID=522772 {ECO:0000313|EMBL:ADD67644.1, ECO:0000313|Proteomes:UP000002012}; RN [1] {ECO:0000313|EMBL:ADD67644.1, ECO:0000313|Proteomes:UP000002012} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 12809 / N2460 {ECO:0000313|Proteomes:UP000002012}; RX PubMed=21304711; RA Kiss H., Lang E., Lapidus A., Copeland A., Nolan M., RA Glavina Del Rio T., Chen F., Lucas S., Tice H., Cheng J.F., Han C., RA Goodwin L., Pitluck S., Liolios K., Pati A., Ivanova N., RA Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., RA Chang Y.J., Jeffries C.D., Detter J.C., Brettin T., Spring S., RA Rohde M., 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 Denitrovibrio acetiphilus type strain RT (N2460)."; RL Stand. Genomic Sci. 2:270-279(2010). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001968; ADD67644.1; -; Genomic_DNA. DR RefSeq; WP_013010175.1; NC_013943.1. DR RefSeq; YP_003503600.1; NC_013943.1. DR EnsemblBacteria; ADD67644; ADD67644; Dacet_0864. DR KEGG; dap:Dacet_0864; -. DR PATRIC; 35351660; VBIDenAce54242_0849. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR BioCyc; DACE522772:GHC2-877-MONOMER; -. DR Proteomes; UP000002012; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002012}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002012}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 215 215 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 281 281 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 282 282 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 715 715 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1116 AA; 123057 MW; 458C66F658835922 CRC64; MFNEFAKNRI ILFDGAMGTS IQNYEITDEI WQGYNGCSEW LNVAAPEIIQ QIHEQYFEAG ADVVETNTFG GTELVMSEYD LQDRTYELNL LGAQIARRAA DKYGKYTAGS IGPGTKLPSL GQISYDDLYT MYHSQAEALL EGGVDLFIIE TCQDLLQIKS ALNAVIDVKA EKNSDAPVMV SITVEQNGTM LMGTDISAAV TLLREYPVFS LGLNCSTGPD LMHNPINDLA QNFNGRISCI PNAGLPENRG GQMVYDMTPD KMAKIVEGMV QEFPIGVLGG CCGTTPEHIK ALRPIADKYK PNKPQAKEYT GESSSLYVST TLMQTPPPAL IGERANANGS KAFRELLLAE DFDGMLAVAK EQEETGAHFI DACVAYAGRD EKADMAKFMH LLNKTLTAPV VIDSTEPDVV ETALKSCAGK PVINSINFED GGEKLHIILR AVKKHPASVI ALTIDEDGMA MTAEKKFEIA ERIYNIFTKE YGLNPNDLIF DPLTFSIGSG DKTLVDAAIQ TNKAIKMIKE KLTGAKTALG LSNISFGLSK DSRPILNSVF LHEAVEHGLD MAIVHASKVM PQAAIPEEDI KVSKDLLAGQ EGALSAFIEH FSKKEGIVQQ EEKTDLPPDE MLKNLIKKGR KAGLEETLTA LMQTMKPIEI INNIMLDTMK EIGELFGAGK MLLPFVLQSA ETMKTAVTVL EPFMEKSDTE TRGRIVLATV KGDVHDIGKN LVDIILSNNG YEVYNLGIKV SVEEMIAKAV EMDADAIGMS GLLVKSTNIM RENIAEINRQ GLSKKVLLGG AALTEKFVKN DCMPIMPGMV SYCRDAFDAL KVLSGESEGS IAPEKTYADI SAKPKKVQSP KLETPPAPPF FGVKTAENYT ADDILEYMNK LALFSHRWGY SKKNMPDYEY EELLTKTVIP EFNETVQEIK DKELLEMGIR YAYFPCNSDG EELIVYNEDG SELTRFVFPR QNLENGVCLA DYFHPVSSGV KDVVAFHIVT AGSKPAEYCQ QLFKNNEYKK YYQFHGFFTE FAEAMAEYAH KMIRTDLKID HADAKTAHGI ISLGYSGRRY SFGYPSCPDL AQNNQLDSIL DFSQIGVSIT ENHEMVSEYT TCAIIIHNSS AEYFTT // ID D4HR74_KLEPN Unreviewed; 331 AA. AC D4HR74; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 01-APR-2015, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADD63670.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ADD63670.1}; GN ORFNames=pKF140-191 {ECO:0000313|EMBL:ADD63670.1}; OS Klebsiella pneumoniae. OG Plasmid pKF3-140 {ECO:0000313|EMBL:ADD63670.1}. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=573 {ECO:0000313|EMBL:ADD63670.1}; RN [1] {ECO:0000313|EMBL:ADD63670.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=KF3 {ECO:0000313|EMBL:ADD63670.1}; RC PLASMID=pKF3-140 {ECO:0000313|EMBL:ADD63670.1}; RA Zhao F., Bai J., Wu J., Liu J., Zhou M., Xia S., Wang S., Yao X., RA Yi H., Lin M., Gao S., Zhou T., Xu Z., Niu Y., Bao Q.; RT "Sequencing and Genetic Variation of Multidrug Resistance Plasmids in RT Klebsiella pneumoniae."; RL PLoS ONE 5:E10141-E10141(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; FJ876827; ADD63670.1; -; Genomic_DNA. DR RefSeq; WP_013023898.1; NC_013951.1. DR RefSeq; YP_003517716.1; NC_013951.1. DR GeneID; 8877705; -. DR KEGG; pg:8877705; -. DR KO; K00547; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:ADD63670.1}; KW Plasmid {ECO:0000313|EMBL:ADD63670.1}; KW Transferase {ECO:0000313|EMBL:ADD63670.1}. SQ SEQUENCE 331 AA; 35824 MW; C5392BE664E00B68 CRC64; MRCAMVLISL LNPETQNRSQ NMSQNNPLRA LLDKQDILLL DGAMATELEA RGCNLADSLW SAKVLVENPE LIREVHLDYY RAGAQCAITA SYQATPAGFA ARGLDEAQSK ALIGKSVELA RKAREAYLAE NPQAGTLLVA GSVGPYGAYL ADGSEYRGDY HCSVEAFQAF HRPRVEALLD AGADLLACET LPNFSEIEAL AELLTAYPRA RAWFSFTLRD SEHLSDGTPL RDVVALLAGY PQVVALGINC IALENTTAAL QHLHGLTVLP LVVYPNSGEH YDAVSKTWHH HGEHCAQLAD YLPQWQAAGA RLIGGCCRTT PADIAALKAR S // ID D4HYP6_ERWAC Unreviewed; 300 AA. AC D4HYP6; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CBA20021.1}; DE EC=2.1.1.- {ECO:0000313|EMBL:CBA20021.1}; GN OrderedLocusNames=EAMY_1071 {ECO:0000313|EMBL:CBA20021.1}; OS Erwinia amylovora (strain CFBP1430). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Erwinia. OX NCBI_TaxID=665029 {ECO:0000313|EMBL:CBA20021.1, ECO:0000313|Proteomes:UP000001841}; RN [1] {ECO:0000313|EMBL:CBA20021.1, ECO:0000313|Proteomes:UP000001841} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CFBP1430 {ECO:0000313|Proteomes:UP000001841}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; CBA20021.1; -; Genomic_DNA. DR RefSeq; WP_004156536.1; NC_013961.1. DR RefSeq; YP_003530429.1; NC_013961.1. DR EnsemblBacteria; CBA20021; CBA20021; EAMY_1071. DR GeneID; 8911456; -. DR KEGG; eam:EAMY_1071; -. DR PATRIC; 35406296; VBIErwAmy142366_1054. DR HOGENOM; HOG000265278; -. DR OMA; PYVDVWL; -. DR BioCyc; EAMY665029:GCM3-1115-MONOMER; -. DR Proteomes; UP000001841; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001841}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:CBA20021.1}; KW Transferase {ECO:0000313|EMBL:CBA20021.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 208 208 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 300 AA; 31866 MW; D59BC17EC77FA4CC CRC64; MTQQIKILDG GMGRELARAG APFRQPEWSA LALYEAPQRV REVHDSFISA GAGTITTNSY AVVPFHIGQA RFHADGEYLA ALAGQLARQA ANAATHPVQV AGSLPPALGS YRPDLFDAQQ ALKIYRLLVA AQAPYVDIWL GETISSLAEA VAIHQAVADQ PHPLWLSFSL EDDPDKTRRD STLRSGESVS AAVELAVESG ATHILFNCSN PEVMLSAVQQ AAATLRRLGS EAGIGVYANA FEHGSNGGGA NEGLSDLRQD THPEGYLRWA REWVAAGATL VGGCCGIGPE HIRCLASAFK // ID D4IP79_9BACT Unreviewed; 1204 AA. AC D4IP79; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 27-MAY-2015, entry version 31. DE SubName: Full=Draft genome {ECO:0000313|EMBL:CBK64741.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CBK64741.1}; GN ORFNames=AL1_25320 {ECO:0000313|EMBL:CBK64741.1}; OS Alistipes shahii WAL 8301. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Rikenellaceae; OC Alistipes. OX NCBI_TaxID=717959 {ECO:0000313|EMBL:CBK64741.1, ECO:0000313|Proteomes:UP000008794}; RN [1] {ECO:0000313|EMBL:CBK64741.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=WAL 8301 {ECO:0000313|EMBL:CBK64741.1}; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J.; RT "The genome sequence of Alistipes shahii WAL 8301."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CBK64741.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=WAL 8301 {ECO:0000313|EMBL:CBK64741.1}; RA Pajon A.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; FP929032; CBK64741.1; -; Genomic_DNA. DR RefSeq; WP_015547552.1; NC_021030.1. DR RefSeq; YP_007817502.1; NC_021030.1. DR EnsemblBacteria; CBK64741; CBK64741; AL1_25320. DR KEGG; ash:AL1_25320; -. DR PATRIC; 42710953; VBIAliSha154597_1035. DR KO; K00548; -. DR BioCyc; ASHA717959-WGS:GSEZ-2023-MONOMER; -. DR Proteomes; UP000008794; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008794}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CBK64741.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008794}; KW Transferase {ECO:0000313|EMBL:CBK64741.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 754 754 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1204 AA; 131071 MW; D0174966BD0A7AC8 CRC64; MTTTLYDQLE RRILLLDGGF GTMVQGYGLQ EEDYRGRRFA GWPVQLKGCN DLLALTRPDV VREIHEKYLR AGADIIETDS FNANAVSLAD YRLEECAYEI SKVAAGIARS AADEFTARNP QKPRFVAGSV GPTNRTASMS ADVQNPAARE VTFAQLVEAY TDQVRGLVDG GADILLVETV FDTLNAKAAL WAIDTLCERL GRAIPVMVSG TLADASGRTL SGQTVEAFAV SVSHANLLSV GLNCAYGAKQ LLPYLERLAA VAGTRISAHP NAGLPNVMGG YDETPEMFAG DVGEYMRRGL VNIVGGCCGT TPAHIFELSK ISGDYAPRPV PAPKHITTLS GLEPLRIVPE ANFINVGERT NVAGSARFAR LIREANYEEA LSVARAQVDA GAQIVDVCMD DGLIDGPAAM RTFLNLMASE PEIARVPVMI DSSKWEVLQA GLEVTQGKSV VNSISLKEGE AEFLRRAAEI HRFGASAVVM LFDERGQADT FERKAEVAER AYKLLTDNGF PPEDIIFDPN VLAVATGIAE HDGYAKAFID ATRWIKEHLP HAKVSGGVSN LSFAFRGNNT VREAMHSAFL YHAIRAGMDM GIVNPQMLKV YSQIEPELLC RVEDVILCRR ADAAERLAEY AHGVQQTAQA QPQAPDAWRA GTLGERIAHA MLKGVADYVE QDALEGYEAL GSPMAVIDTL LMPAMEQVGT LFGEGKMFLP QVVKTARVMK RAVAALTPYI EQGSAANAHN SGKVLIATVK GDVHDIGKNI VAVVMACNGY EIRDLGVMVE PERIVEEAVA WGAQCICLSG LITPSLDEMA RVCEELERRG LRIPVIIGGA TTSDLHTAVK IAPVYSGVAV HSANASRNSQ ILAQLLGPDG DLYADKVKVD QQVLREEYAR RLRERDLIPI AEARAARRGA AQHEPVVPLH TGRMVFPDFD VADAEPYIDW SFFFAAWGLK GRYPEILDHP EKGAEARKVF ADAQALLARI RDERLLTLQG VAGIFPARSE GDDILVTDAK GREKRLPMLR NQTRGEENLS LADFIAPDGD WIGCFALTAG IGLKELAEKF RAGGDDYSAI MAKLLADRLT EAFAEAVHAF MRREMWGYET GTPPTPEQAV RGQYRGRRMA FGYPASPDHS LKREVFDLLA VEVTTGMQLT ENWMIDPGEA LCGLMFSDAD YFSVGTIGAE QLLDYARRRG MEAETVKKII PNNV // ID D4IVX3_BUTFI Unreviewed; 505 AA. AC D4IVX3; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Draft genome {ECO:0000313|EMBL:CBK74916.1}; GN ORFNames=CIY_22400 {ECO:0000313|EMBL:CBK74916.1}; OS Butyrivibrio fibrisolvens 16/4. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Butyrivibrio. OX NCBI_TaxID=657324 {ECO:0000313|EMBL:CBK74916.1, ECO:0000313|Proteomes:UP000008796}; RN [1] {ECO:0000313|EMBL:CBK74916.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=16/4 {ECO:0000313|EMBL:CBK74916.1}; 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. RN [2] {ECO:0000313|EMBL:CBK74916.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=16/4 {ECO:0000313|EMBL:CBK74916.1}; RA Pajon A.; 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; FP929036; CBK74916.1; -; Genomic_DNA. DR RefSeq; WP_015550009.1; NC_021031.1. DR EnsemblBacteria; CBK74916; CBK74916; CIY_22400. DR KEGG; bfi:CIY_22400; -. DR PATRIC; 42804357; VBIButFib8520_2032. DR KO; K00548; -. DR BioCyc; BFIB657324-WGS:GSIP-1926-MONOMER; -. DR Proteomes; UP000008796; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008796}; KW Reference proteome {ECO:0000313|Proteomes:UP000008796}. SQ SEQUENCE 505 AA; 56049 MW; 2E51B39FB3AF92F1 CRC64; MTRNDFRQLL ETRTVFIDGA TGTELQKRGM AAGVCPEKWI IDNPWAIQEV QKAYYEAGSD IVLAPTFTGT RIKLDEYGLA DDLVNINRTL VRLTKEICPE GKFVAADISM TGKQLYPLGD LMFEDLVDCY KEQVNAILEE GVDLFVVETM MSLQECRAAV LAIKETCDLP IIVSLTYNPD GKTLYGTSPD TATIVLQSMG IDCIGMNCST GPDAMLELVN QIARVATVPI MVKPNAGLPE LENGKTVYKM GPKEFADASE KLYEAGASLF GGCCGSTPEH IKELVLRLKD KACHKVVDKP LRVVTSERMN TWIDLDGPFM VIGERINPTG KKKFQETLRN GSLSMVVDFA REQEERGANI LDVNMGMNGI DEKKMMIESI YEVTSSVDLP LCIDTSHVDV MEAALRIYPG RALINSISAE EEKMEPMLKL AKKYGAMFIT LPLSGAGLPK DIEEKKQHIN TVLIKAIELG LKKKMLLWTC WCRLLELKEQ QACNVLKLLI IVNTN // ID D4JC63_9FIRM Unreviewed; 603 AA. AC D4JC63; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 27-MAY-2015, entry version 29. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=CC1_34080 {ECO:0000313|EMBL:CBK81934.1}; OS Coprococcus catus GD/7. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Coprococcus. OX NCBI_TaxID=717962 {ECO:0000313|EMBL:CBK81934.1, ECO:0000313|Proteomes:UP000008798}; RN [1] {ECO:0000313|EMBL:CBK81934.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=GD/7 {ECO:0000313|EMBL:CBK81934.1}; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Coprococcus catus GD/7."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CBK81934.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=GD/7 {ECO:0000313|EMBL:CBK81934.1}; RA Pajon A.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; CBK81934.1; -; Genomic_DNA. DR RefSeq; WP_015515454.1; NC_021009.1. DR ProteinModelPortal; D4JC63; -. DR EnsemblBacteria; CBK81934; CBK81934; CC1_34080. DR KEGG; cct:CC1_34080; -. DR PATRIC; 42888303; VBICopCat158046_3281. DR KO; K00547; -. DR BioCyc; CCAT717962-WGS:GSLR-2986-MONOMER; -. DR Proteomes; UP000008798; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008798}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:CBK81934.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000008798}; KW Transferase {ECO:0000313|EMBL:CBK81934.1}. SQ SEQUENCE 603 AA; 67673 MW; 4BC7CC609E43C097 CRC64; MDIREYLANN RLITDGAMGT WYDRLTGYKG KLAERANLDD LQQIRDIHRA YIEAGARLIR TNTFAVNSMF FSADEIEAVL KAAWENACQA VSDSGRDVWI AADMGPIDEN ETKSAADVEN EYIHLADCFL GLGAKIFVFE TLSEFRSVKK AIAYIKAECP DAFIVTQFSF NRNGYTRSGL SVRALLLEAA AMKELDAVGF NCGVGPLHLY ELLKNQSFPE GKYMTVLPNA GYPTELRGRT FYSENVPYYV DMMGRIAALG FDIIGGCCGT TPEHIRGLHD LLVNDVRPPK KLMPAVYSAD GKENCAEEAV EEKTDFIQKL ERGEKVFVVE LDPPFDVNDT KLMEGAALLR DINVDMITLA DSPLARPRAD SIASAIKMRY TRQMEAMPHI CCRDKNMIAH RSQLLGMQMN GLRHALIVTG DPIARGDRES IKSVFNFNSI KLMKYIQTMN QEVFGSRPIY YGGALNHNNG SIDNIAARMC QKMEAGAQWF LTQPVYGQED IDRLKELKEK SGGRIIAGIM PLVSRKNALF IKNEMPGIHV PDQVLERYEA GMSREAYEDV AEAISVDLMK RLEDVCDGYY MMTPFNRAAL IKRIILQAKK ELR // ID D4JC64_9FIRM Unreviewed; 802 AA. AC D4JC64; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Draft genome {ECO:0000313|EMBL:CBK81935.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CBK81935.1}; GN ORFNames=CC1_34090 {ECO:0000313|EMBL:CBK81935.1}; OS Coprococcus catus GD/7. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Coprococcus. OX NCBI_TaxID=717962 {ECO:0000313|EMBL:CBK81935.1, ECO:0000313|Proteomes:UP000008798}; RN [1] {ECO:0000313|EMBL:CBK81935.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=GD/7 {ECO:0000313|EMBL:CBK81935.1}; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Coprococcus catus GD/7."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CBK81935.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=GD/7 {ECO:0000313|EMBL:CBK81935.1}; RA Pajon A.; 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; CBK81935.1; -; Genomic_DNA. DR RefSeq; WP_015515455.1; NC_021009.1. DR ProteinModelPortal; D4JC64; -. DR EnsemblBacteria; CBK81935; CBK81935; CC1_34090. DR KEGG; cct:CC1_34090; -. DR PATRIC; 42888305; VBICopCat158046_3282. DR KO; K00548; -. DR BioCyc; CCAT717962-WGS:GSLR-2987-MONOMER; -. DR Proteomes; UP000008798; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008798}; KW Methyltransferase {ECO:0000313|EMBL:CBK81935.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008798}; KW Transferase {ECO:0000313|EMBL:CBK81935.1}. SQ SEQUENCE 802 AA; 87409 MW; 47E5A558EF29D413 CRC64; MTREEFQRLC RERIVFLDGA TGTNLQKAGM PTGVCPEAWI LEHPDTMMQL QKAYFEAGSD IVLAPTFTAN RIKLDEYGLV DKIEEMNHQL VAISKAAAGD RGLVAGDMTM TGRQLAPMGD MGFEELIDIY KEQAGYLVDA GVDLFVVETM MSLNECRAAL IAIREVTDLP VCVTLSFNED GRTLFGTDAC TAMVVLQSLG ADAVGINCST GPEQMAELVR EMKAYANIPI IAKPNDGMPE VIDGETVYRM TPEEFAAEAR LLLEAGAGIV GGCCGTTPEH IRAFKEAAKA YPVPEVSQTY KRVLASERQT LEIGLDAGFK IVGERINPTG KKKLQAALRE GQMDMVMDMA LAQEEKGASI LDVNMGMNGI DEKAMMLKSI EIVTQAVNLP LCIDSSHVDI IEAALRVYPG RALINSISLE KEKFEHLLPI ARKYGAMFIL LPLSDEGLPK NIDEKIQIIH TIMDRALELG FHKEDIVVDG LVATIGANKN AAIETLDTIS YCHDQLELAT ICGLSNISFG LPERSYVNTA FLTMAISRGL TMAIANPSQD LLMHAAFASD LLMNHPGADI RYINRMNAVK EQQSGESTAA AVVLTPGEKI FEAVMKGSQG SIINLVKEGL DAGIMPDDMI QKHLITAIQK VGVLFEEKKY YLPQLIASAE TMEKAINYLE PMLIKDDEEE KATIIMATVE GDIHDIGKNL VVLMLKNYGY RVIDLGKDVS AECIIETAVK EHAAIIGLSA LMTTTMMRMR DVVELAQAKH CSSKIIIGGA VTTQSFADEI GADGYSRDAA EAVHLVERLL NK // ID D4JIZ9_9FIRM Unreviewed; 816 AA. AC D4JIZ9; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Draft genome {ECO:0000313|EMBL:CBK93596.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CBK93596.1}; GN ORFNames=ERE_16450 {ECO:0000313|EMBL:CBK93596.1}; OS Eubacterium rectale M104/1. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium. OX NCBI_TaxID=657317 {ECO:0000313|EMBL:CBK93596.1, ECO:0000313|Proteomes:UP000008802}; RN [1] {ECO:0000313|EMBL:CBK93596.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M104/1 {ECO:0000313|EMBL:CBK93596.1}; 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. RN [2] {ECO:0000313|EMBL:CBK93596.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M104/1 {ECO:0000313|EMBL:CBK93596.1}; RA Pajon A.; 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; CBK93596.1; -; Genomic_DNA. DR RefSeq; WP_015568715.1; NC_021044.1. DR EnsemblBacteria; CBK93596; CBK93596; ERE_16450. DR KEGG; era:ERE_16450; -. DR PATRIC; 42990212; VBIEubRec155814_2315. DR KO; K00548; -. DR BioCyc; EREC657317-WGS:GSND-1441-MONOMER; -. DR Proteomes; UP000008802; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008802}; KW Methyltransferase {ECO:0000313|EMBL:CBK93596.1}; KW Transferase {ECO:0000313|EMBL:CBK93596.1}. SQ SEQUENCE 816 AA; 88821 MW; 95A9AD2676163BE4 CRC64; MTREEFRKYI RENIVILDGA TGTNLMAAGM PVGVCPEEWV MEHPQVILDL QKAYVDNGTN IVYAPTFTGN RIKLLEYGLQ EKINEINTTL VGLSKQAVGD RALVAADMTM TGRQLFPLGD LMFEELLEVY KEQARILDAA GADVFVVETM MSLQECRAAV LAIKEVSDLP IMVTLTYNED GRTLFGTPPE TAVVVLQSLG VDAIGVNCST GPAEMIALVE KMAEYSTVPL IAKPNAGLPE LEDGKTVYKM TPDMFADAMR GLVEAGASIV GGCCGTTPEH IRALTEAVKS MPVHKPLEHH RRVLASERKN VEIDLDGNFT VVGERINPTG KKKLQAQLRE GKLDLVRQMA MEQETNGARI LDINMGMNGI DEKEMMKSVI YEVSSTVDCP LCIDSSYVEV IEEALKIYPG RALINSISLE TEKMEKLLPL AAKYGAMFIL LPLSDAGLPK DVEEKKQIIN TIYDKALSLG MAHEDIVVDG LVATIGANPK AAIECYETIA YCKDEKKLPT ICGLSNISFG LPERMYVNTA FLTMAICKGL TMAIANPSQE LLMNAAFASD MLLDRPDGDI AYIERMSRLA EEKAQYETVV VKKSDNDASA SNGTCAAGSK DAVFQAVLKG NKGSIIDEVK KMLSDGAKPD EIINNSLIPA INEVGELFNQ KKYFLPQLIG SANTMKLAIE HLEPLLEKKD SGDDMPTLVI ATVEGDIHDI GKNLVVLMLK NYGYNVIDMG KDVPCEDIVN KAIETNAAVI GLSALMTTTM MRMKDVVEIC KEKGCKSKVV IGGACITQSF ADEIGADGYS KDAAECVKLV ERLLNS // ID D4JSB0_9FIRM Unreviewed; 414 AA. AC D4JSB0; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Draft genome {ECO:0000313|EMBL:CBK95979.1}; GN ORFNames=EUS_07220 {ECO:0000313|EMBL:CBK95979.1}; OS [Eubacterium] siraeum 70/3. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminiclostridium. OX NCBI_TaxID=657319 {ECO:0000313|EMBL:CBK95979.1, ECO:0000313|Proteomes:UP000008803}; RN [1] {ECO:0000313|EMBL:CBK95979.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=70/3 {ECO:0000313|EMBL:CBK95979.1}; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Eubacterium siraeum 70/3."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CBK95979.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=70/3 {ECO:0000313|EMBL:CBK95979.1}; RA Pajon A.; 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; FP929044; CBK95979.1; -; Genomic_DNA. DR RefSeq; WP_015518314.1; NC_021011.1. DR EnsemblBacteria; CBK95979; CBK95979; EUS_07220. DR KEGG; esu:EUS_07220; -. DR PATRIC; 42995483; VBIEubSir135646_0971. DR KO; K00548; -. DR BioCyc; ESIR657319-WGS:GSO8-615-MONOMER; -. DR Proteomes; UP000008803; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008803}; KW Reference proteome {ECO:0000313|Proteomes:UP000008803}. SQ SEQUENCE 414 AA; 45042 MW; CD2ED01E4DAC84BD CRC64; MDSNPVSQDI PIRLPILLDG GTGTGLEKYG YDHTVSTAQF VCEHPEALTQ LQQGFIDAGS QILYTATHGA NRENLKAYGV EDKTEQLNAA AAKITYDSFH EKALIAGCLS STGLYIEPYG DYTFTEIMSV YRQQVKALSP YCDMFVIETV PALWNMRAAV LACKKENKPI IATMKVDEDG ETAIGTNVLC TLLVLQAMGI SAFGLNCTSA DLCPDIISEI APYAKIPLIV KPSAVYEQDG ERLSISPEEF AFAVKKSVLS GAEIAGGCCG TGKEHIAALR EMFASLDASE INPVEKQDTS LALATENQMF FLDPETTEFS PAVECGPYME DDIAQMCGES YDVLTVSINS PDDAIDFGRN MHMATLPVAF LSDDEISLKM ALMLYQGRAI IDRKSLIEPE KLEAMAEKYG AVLY // ID D4K157_9FIRM Unreviewed; 597 AA. AC D4K157; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 27-MAY-2015, entry version 31. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=FP2_27030 {ECO:0000313|EMBL:CBL00006.1}; OS Faecalibacterium prausnitzii L2-6. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Faecalibacterium. OX NCBI_TaxID=718252 {ECO:0000313|EMBL:CBL00006.1, ECO:0000313|Proteomes:UP000008804}; RN [1] {ECO:0000313|EMBL:CBL00006.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=L2/6 {ECO:0000313|EMBL:CBL00006.1}; 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. RN [2] {ECO:0000313|EMBL:CBL00006.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=L2/6 {ECO:0000313|EMBL:CBL00006.1}; RA Pajon A.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; CBL00006.1; -; Genomic_DNA. DR RefSeq; WP_015565623.1; NC_021042.1. DR ProteinModelPortal; D4K157; -. DR EnsemblBacteria; CBL00006; CBL00006; FP2_27030. DR KEGG; fpr:FP2_27030; -. DR PATRIC; 43010175; VBIFaePra154692_0898. DR KO; K00547; -. DR BioCyc; FPRA718252-WGS:GSNH-2326-MONOMER; -. DR Proteomes; UP000008804; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008804}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:CBL00006.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000008804}; KW Transferase {ECO:0000313|EMBL:CBL00006.1}. SQ SEQUENCE 597 AA; 64022 MW; F0568F6F72CE53A0 CRC64; MTDIREYLAH KPLLFDGGMG TYYKAAPGAD CEMANLTDPE GVKKVHAEYL AAGAQAIKTN TFGLPRMAAA QTPGWEELAE AGWKLACDAA AEKDAAVFAD LGPAPDTEAA PASSAYGLVA QQFAALGAKN FLFETLSSDV GIVEAVKALR VAVPDAFVMV SFAVLPDGYT REGLLFRDLL RRMEQSGVVD AVGLNCVSAP GAMKKLVQGL GETLLPLSVM PNAGYPVVTR ARVLYQGKPA YFAREMGQIA AAGVRILGGC CGTTPAHIAA LRAELDALPQ RTEAAPAAKL STGTAPAVEK DDAFLRKLNA GEKVIAIELD SPRVADLSGY LDGARRLQAA GADLLTIADC PIAQARMDSS LVACRVHREL GMCALPHMTC RDRNLNATKA LLLGLYAEGV REVLAITGDP IPTAERDEVK NVYQFNSRKL AQYIVSLAGE GREMPSAMTV LGALNLNARN FDVELRRAVE KLENGMSGFL TQPVLSAQAV ENLRKARQTL GERAKILAGI MPVVSQRNAI FMENEINGIH VEEDIIQRFA GLDREQGEAL GLEVSMQMAR EALPYADGFY LMTPFNRVAL MERLIARLKT ELLDAED // ID D4K7S2_9FIRM Unreviewed; 579 AA. AC D4K7S2; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 27-MAY-2015, entry version 30. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=FPR_04840 {ECO:0000313|EMBL:CBL00885.1}; OS Faecalibacterium prausnitzii SL3/3. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Faecalibacterium. OX NCBI_TaxID=657322 {ECO:0000313|EMBL:CBL00885.1, ECO:0000313|Proteomes:UP000007059}; RN [1] {ECO:0000313|EMBL:CBL00885.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SL3/3 {ECO:0000313|EMBL:CBL00885.1}; 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. RN [2] {ECO:0000313|EMBL:CBL00885.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SL3/3 {ECO:0000313|EMBL:CBL00885.1}; RA Pajon A.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; CBL00885.1; -; Genomic_DNA. DR RefSeq; WP_015536795.1; NC_021020.1. DR ProteinModelPortal; D4K7S2; -. DR EnsemblBacteria; CBL00885; CBL00885; FPR_04840. DR KEGG; fpa:FPR_04840; -. DR PATRIC; 43012170; VBIFaePra148460_0162. DR KO; K00547; -. DR Proteomes; UP000007059; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007059}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:CBL00885.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000007059}; KW Transferase {ECO:0000313|EMBL:CBL00885.1}. SQ SEQUENCE 579 AA; 62102 MW; 9ACA53BB9132B847 CRC64; MLDVRKLLAQ RPLLFDGGMG TYYKAKPGQE CEQANLTDPE GILAVHRAYL AAGADAIKTN TFSLPRLAAA QQPGWEQLAD AGWQLAVKAA GETGAAVFAD LGPAPDTENL PAEQVYLAVA KRFALLGARN FLFETLSAED GVLEAIRALK QTVPEAFVLV SFAVLPDGYT REGRYCAELV RRVAQSGVVD AVGLNCVSAP GAMRALVQQL GDAGLPLSVM PNAGYPVVAR AQVRYQGKPE YFARELSRLA SEGVRILGGC CGTTPQHIAA LRTALDALPE VLPAAPAAKP AVAAKPAVET DDAFLRKLRA GQRVIAVELD SPKDADLTAY LEGARRLQAA GADLLTIADC PIARARMDSS LVACRVHREL GMNVLPHMTC RDRNLNATKA LLLGLYAEGV REVLAITGDP IPTAERDEVK NVYQFNSRKL AQYIVSLAGE GREMPSPITV FGALNLNARN FEVELRRAAE KLENGMSGFL TQPVLSAQAV ENLKKTRETL GERAKILAGI LPVVSQRNAI FMENEVNGIH VDDAIIQRFE GLDRAAGEEL GLEVSVQAAK AAAPYVDGFY LMTPLTGWR // ID D4KHC2_9FIRM Unreviewed; 790 AA. AC D4KHC2; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Draft genome {ECO:0000313|EMBL:CBL05651.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CBL05651.1}; GN ORFNames=MHY_05560 {ECO:0000313|EMBL:CBL05651.1}; OS Megamonas hypermegale ART12/1. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Megamonas. OX NCBI_TaxID=657316 {ECO:0000313|EMBL:CBL05651.1, ECO:0000313|Proteomes:UP000008806}; RN [1] {ECO:0000313|EMBL:CBL05651.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ART12/1 {ECO:0000313|EMBL:CBL05651.1}; 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. RN [2] {ECO:0000313|EMBL:CBL05651.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ART12/1 {ECO:0000313|EMBL:CBL05651.1}; RA Pajon A.; 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; FP929048; CBL05651.1; -; Genomic_DNA. DR RefSeq; WP_015561950.1; NC_021041.1. DR ProteinModelPortal; D4KHC2; -. DR EnsemblBacteria; CBL05651; CBL05651; MHY_05560. DR KEGG; mhg:MHY_05560; -. DR PATRIC; 43122035; VBIMegHyp147215_0330. DR KO; K00548; -. DR BioCyc; MHYP657316-WGS:GSQ8-399-MONOMER; -. DR Proteomes; UP000008806; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008806}; KW Methyltransferase {ECO:0000313|EMBL:CBL05651.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008806}; KW Transferase {ECO:0000313|EMBL:CBL05651.1}. SQ SEQUENCE 790 AA; 84209 MW; 1FE1FB7E660DC51C CRC64; MIHIFDGATG TMLQKSVLKP GMCPELLNIE APEAIQNVHR AYVEAGSNIV ETNTFGASRI KLNEYNLGDK VEAINIAAVK NAKIATAGKA KVAGSMGPTG AFIEPLGELT FDKVYANYYE QAKILADAGV DYILIETCIE IQEMRAALLA AKDACDLPVI CQLSFSEDGR TVTGTDPQSA AIILEAMGAD IIGANCSLGP EQLVPIIKEL ADNCSCPISV QANAGMPHLE NGQTIFPLTP EDMAKWAPKL VEAGATYIGG CCGTTPAHIK AIKEALANVS EPIRKAPNPN LALASRSKTV FIGKDLPTRL IGERINPTGR KKLAEEIKNG SFISVKREAI EQTQAGAQIL DVNMGVAGID QAKAMHKAIT EISQLVNTPL AIDTSDVKAL EAGLKAYPGR ALINSVSAEP DRLKYFIPLA RRYGAAILCL PLSDEGIPKT AKERLALAQK IIAEAKAQGL KDNDFLLDAL VMTIAADKNA CNEVLNTLKL YREHIGAPST MGLSNISFGL PNRPLINSTF FTMCLAMGLD APIMNPYDDS MQNALSASNA LLAKDPNGRD YSLNHSGQNI PVAKAKNTVS SGDIIEDIKS AIISGEKESI AQMVEQALTE GHKPNEITDK ALSAAMNVVG KDFGAKKIFL PQVMLSAEAM REAFIKIKER IPSDSVSNKG TIVIATVKGD IHDLGKNIVS ALLENNGFKV IDLGKDIDKE EIIKAAIDNK ADMIGLCSLM TTTITQIDEV IAELNKSDYS TKVMIGGAVV TQEYADNVGA NAYAPDGVEA VEIAKKLINK // ID D4KMW9_9FIRM Unreviewed; 787 AA. AC D4KMW9; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Draft genome {ECO:0000313|EMBL:CBL08221.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CBL08221.1}; GN ORFNames=ROI_10180 {ECO:0000313|EMBL:CBL08221.1}; OS Roseburia intestinalis M50/1. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Roseburia. OX NCBI_TaxID=657315 {ECO:0000313|EMBL:CBL08221.1, ECO:0000313|Proteomes:UP000008807}; RN [1] {ECO:0000313|EMBL:CBL08221.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M50/1 {ECO:0000313|EMBL:CBL08221.1}; 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. RN [2] {ECO:0000313|EMBL:CBL08221.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M50/1 {ECO:0000313|EMBL:CBL08221.1}; RA Pajon A.; 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; CBL08221.1; -; Genomic_DNA. DR RefSeq; WP_015559896.1; NC_021040.1. DR EnsemblBacteria; CBL08221; CBL08221; ROI_10180. DR KEGG; rim:ROI_10180; -. DR PATRIC; 43140413; VBIRosInt153491_2108. DR KO; K00548; -. DR BioCyc; RINT657315-WGS:GSTX-866-MONOMER; -. DR Proteomes; UP000008807; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008807}; KW Methyltransferase {ECO:0000313|EMBL:CBL08221.1}; KW Transferase {ECO:0000313|EMBL:CBL08221.1}. SQ SEQUENCE 787 AA; 85599 MW; 6E794CF6C820D27B CRC64; MPVGVCPEQW ILENSEVLID LQKQYVEAGT DILFAPTFTA SRIKLKEYGL EDHLEEMNRK LVALSKEAAK GTNALVAGDL TMTGEQLYPL GDLMFEDLVD VYKEQAKIIA EAGADLFVVE TMMSLQECRA AVLAIREVCD LPVMVSLTYN EDGRTLYGTD PVTAVVVMQS LGADAVGMNC STGPEAMLEP IAKMAEYAAI PLLAKPNAGM PELIDGQTVF NVEPEEFAEV GKKLVEEGAA IIGGCCGTTP EHIRALKEAV KGIPVKAPLQ TKRRMLTSER KSVEITLDGR FMVIGERINP TGKKKLQAEL KEGSLNLVRT MALEQEENGA SILDINMGMN GIDEKEMMLR TIYEVTSTVD CPLCIDSSHV DIIEAALRIY PGRALINSIS LEKEKFEKLL PIAKKYGAMF ILLPLSDEGL PKDSAEKHGI IRTIMDEAVR IGMAKEDIIV DGLVATIGAN PNAALECFET FSYCKNELEL PTACGLSNIS FGLPERTYVN TAFLTMAIAN GLTMAIANPS QELLMNAAFA SDMLLNKKES DIRYIERMNF LSEKYAGMER VMVQKTPAGT SAAGGEIRKE STGSGVFQAV LKGNKEHVLE EVKKMLDGGA KPDEIINEHL IAAINEVGEL FDKKKYFLPQ LISSANTMKL AIEYLEPMLE RSNTEAMATI VVATVEGDIH DIGKNLVVLM LKNYGYHVID LGKDVPADVI VDTAMNEGAK VIGLSALMTT TMMRMKDVVE LAKEKGCTAK IVIGGAAITE SFSDEIGADG YSKDAAECVK LVERLLA // ID D4KZF5_9FIRM Unreviewed; 816 AA. AC D4KZF5; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Draft genome {ECO:0000313|EMBL:CBL12745.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CBL12745.1}; GN ORFNames=RO1_22390 {ECO:0000313|EMBL:CBL12745.1}; OS Roseburia intestinalis XB6B4. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Roseburia. OX NCBI_TaxID=718255 {ECO:0000313|EMBL:CBL12745.1, ECO:0000313|Proteomes:UP000008953}; RN [1] {ECO:0000313|EMBL:CBL12745.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=XB6B4 {ECO:0000313|EMBL:CBL12745.1}; 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. RN [2] {ECO:0000313|EMBL:CBL12745.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=XB6B4 {ECO:0000313|EMBL:CBL12745.1}; RA Pajon A.; 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; CBL12745.1; -; Genomic_DNA. DR RefSeq; WP_015521258.1; NC_021012.1. DR EnsemblBacteria; CBL12745; CBL12745; RO1_22390. DR KEGG; rix:RO1_22390; -. DR PATRIC; 43150806; VBIRosInt152332_3402. DR KO; K00548; -. DR BioCyc; RINT718255-WGS:GSUO-1920-MONOMER; -. DR Proteomes; UP000008953; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008953}; KW Methyltransferase {ECO:0000313|EMBL:CBL12745.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008953}; KW Transferase {ECO:0000313|EMBL:CBL12745.1}. SQ SEQUENCE 816 AA; 88723 MW; 15C5A7925910074D CRC64; MTREAFRELV KKGPVLLDGA TGTNLQKAGM PVGVCPEQWI LENSEVLIDL QKRYVEAGTD ILFAPTFTAS RIKLKEYGLE DHLEEMNRKL VALSKEAAKG TNALVAGDLT MTGEQLYPLG DLMFEDLVDV YKEQAKIIAE AGADLFVVET MMSLQECRAA VLAIREVCDL PVMVSLTYNE DGRTLYGTDP VTAVVVMQSL GADAVGMNCS TGPEAMLEPI AKMAEYATIP LLAKPNAGMP ELIDGQTVFN VEPEEFAEVG KKLVEEGAAI IGGCCGTTPE HIRALKEAVK GIPVKAPLQT KRRMLTSERK SVEITLDGRF MVIGERINPT GKKKLQAELK EGSLNLVRTM ALEQEENGAS ILDINMGMNG IDEKEMMLRT IYEVTSTVDC PLCIDSSHVD IIEAALRIYP GRALINSISL EKEKFEKLLP IAKKYGAMFI LLPLSDEGLP KDSAEKHGII RTIMDEAVRI GMAKEDIIVD GLVATIGANP NAALECFETF SYCKNELELP TACGLSNISF GLPERTYVNT AFLTMAIANG LTMAIANPSQ ELLINAAFAS DMLLNKKESD IRYIERMNFL SEKYAGMERV MVQKTPAGTS AAGGEIRKES TGSGVFQAVL KGNKEHVLEE VKKMLDGGAK PDEIINEHLI AAINEVGELF DKKKYFLPQL ISSANTMKLA IEYLEPMLER SNTEAMATIV VATVEGDIHD IGKNLVVLML KNYGYHVIDL GKDVPADVIV DTAMNEGAKV IGLSALMTTT MMRMKDVVEL AKEKGCTAKI VIGGAAITES FSDEIGADGY SKDAAECVKL VERLLA // ID D4LF38_RUMC1 Unreviewed; 785 AA. AC D4LF38; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Ruminococcus champanellensis type strain 18P13T draft genome {ECO:0000313|EMBL:CBL18233.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CBL18233.1}; GN OrderedLocusNames=RUM_22270 {ECO:0000313|EMBL:CBL18233.1}; OS Ruminococcus champanellensis (strain DSM 18848 / JCM 17042 / 18P13). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus. OX NCBI_TaxID=213810 {ECO:0000313|EMBL:CBL18233.1, ECO:0000313|Proteomes:UP000007054}; RN [1] {ECO:0000313|Proteomes:UP000007054} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18848 / JCM 17042 / 18P13 RC {ECO:0000313|Proteomes:UP000007054}; 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 ----------------------------------------------------------------------- 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; CBL18233.1; -; Genomic_DNA. DR RefSeq; WP_015559139.1; NC_021039.1. DR RefSeq; YP_007830241.1; NC_021039.1. DR EnsemblBacteria; CBL18233; CBL18233; RUM_22270. DR KEGG; rch:RUM_22270; -. DR PATRIC; 43170681; VBIRumSp55702_2114. DR KO; K00548; -. DR BioCyc; RCHA213810-WGS:GSU3-1972-MONOMER; -. DR Proteomes; UP000007054; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007054}; KW Methyltransferase {ECO:0000313|EMBL:CBL18233.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007054}; KW Transferase {ECO:0000313|EMBL:CBL18233.1}. SQ SEQUENCE 785 AA; 83950 MW; 8912BEE134C8CB5C CRC64; MTFAELLQNN YIFLDGGMGT MLQANGMQAG ERPELLNLKD PALVEQVQRA YVEAGSNIIC SNTFGANRAK LTGSGATVQQ VIPAAIQCAR RAAAGKALVA LDLGPTGQML EPTGSLTFEQ AYDLYAEQVD AGQEADLILI ETMTDLYEIR AAVLAAKEHG NGKPVIALMT FEHTGRTFTG CSVSAMALTL EGLGVDAMGI NCSIGPDELY PVVEELCRWT TLPLLIKPNA GLPDPVTNQY NVSPAEFARS MTRIAKLGVK LLGGCCGTTP DYIRAVREAV ADLPFTPRQV QVPAAVCSYS RTVVIDRPRV IGERINPTGK KLFKEALLRG DIDYILGQAI TQVHGGADIL DVNVGLPSID ERDMMVRTVK ALQGVVDVPL QLDSTMPQVL EAALRIYNGK PIVNSVNGEE KSLSTVLPLV KKYGAAVVGL TLDEQGIPKT AEGRFQIAKR ILDRALALGI RREDVYIDCL TLTVSAEQDG AVQTLSALHR VKQELGLKTV LGVSNISFGL PNRELVNHSF LLMALQNGLD LPIMNPNVAS MMDAVRSYCL LANIDKNAVD FIAAYGSAEP KAKPAAAPAD MTLSFAIENG LKQEGARITR QLLEQMDSME IVNGQLIPAL DKAGAAFEQG KLFLPQLIQA AGVAQAAFGE IRSYLTAHNA VPVSRGKVIL ATVKGDIHDI GKNIVKVLME NYGYQVIDLG RDVPPETIVA AALEHQVKLV GLSALMTTTL GAMEETIRQL HANNVPCKVV VGGAVLTADY AAQIGADYYA KDAKESVDIA KQVVG // ID D4LJ07_9FIRM Unreviewed; 292 AA. AC D4LJ07; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Draft genome {ECO:0000313|EMBL:CBL19818.1}; GN ORFNames=CK1_17470 {ECO:0000313|EMBL:CBL19818.1}; OS Ruminococcus sp. SR1/5. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus. OX NCBI_TaxID=657323 {ECO:0000313|EMBL:CBL19818.1, ECO:0000313|Proteomes:UP000007055}; RN [1] {ECO:0000313|EMBL:CBL19818.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SR1/5 {ECO:0000313|EMBL:CBL19818.1}; 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. RN [2] {ECO:0000313|EMBL:CBL19818.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SR1/5 {ECO:0000313|EMBL:CBL19818.1}; RA Pajon A.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; CBL19818.1; -; Genomic_DNA. DR RefSeq; WP_015525685.1; NC_021014.1. DR EnsemblBacteria; CBL19818; CBL19818; CK1_17470. DR KEGG; rum:CK1_17470; -. DR PATRIC; 43174452; VBIRumSp156992_1326. DR KO; K00548; -. DR Proteomes; UP000007055; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007055}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000007055}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 208 208 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 274 274 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 275 275 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 292 AA; 30942 MW; 203ADD277CB8533E CRC64; MTKQEFQKLT EDHVLLLDGA TGSNLMKAGM PRGVCTESWV LEHKDVIQSL QKAYIEAGSH IIYAPTFGGN RINLTMHGLE DQIEQINHTL AGYSKEIAPE GVFVAGDITT TGKMMSPAGD MTYEKAFEVY QEQIGYLRDA GVDLIVAETM INIEETLAAV DACQSVCELP IICTVTVEAD GSIFSGGNAI EAAMSLEAAG ADAVGINCSV GPDQLVSVIR NIKENVSIPV IAKPNAGMPQ IDDLGNAVYS MTPADFAGYM KVLVDNGASV IGGCCGTTPE FISETAQVLG LR // ID D4LSD8_9FIRM Unreviewed; 289 AA. AC D4LSD8; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Draft genome {ECO:0000313|EMBL:CBL23696.1}; GN ORFNames=CK5_23710 {ECO:0000313|EMBL:CBL23696.1}; OS Ruminococcus obeum A2-162. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Blautia. OX NCBI_TaxID=657314 {ECO:0000313|EMBL:CBL23696.1, ECO:0000313|Proteomes:UP000008955}; RN [1] {ECO:0000313|EMBL:CBL23696.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A2-162 {ECO:0000313|EMBL:CBL23696.1}; 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. RN [2] {ECO:0000313|EMBL:CBL23696.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A2-162 {ECO:0000313|EMBL:CBL23696.1}; RA Pajon A.; 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; CBL23696.1; -; Genomic_DNA. DR RefSeq; WP_015542480.1; NC_021022.1. DR EnsemblBacteria; CBL23696; CBL23696; CK5_23710. DR KEGG; rob:CK5_23710; -. DR PATRIC; 43163784; VBIRumObe156199_2223. DR KO; K00548; -. DR Proteomes; UP000008955; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008955}; KW Reference proteome {ECO:0000313|Proteomes:UP000008955}. SQ SEQUENCE 289 AA; 30524 MW; B8D8BD4B8584E390 CRC64; MTKEEFQKLA EQTLILDGAT GSNLMASGMP RGICTETWVI DHKDIIQDLQ RAYIKAGSQV IYAPTFGGNR LNLEKHGLAD RIKEINRTLV SYSKELAGNG VYVAGDITTS GSFITADGDY TYAEAFDMYQ EQIRILADAG IDLIAAETMI NIEETLAAVD AAASVCDLPI MCTMTVEADG SIFSGGNAIE AAVSLEAAGA DAVGINCSVG PDQLVSVVRN IRENVSIPVI AKPNAGMPVI DDSGNAVYSM HAGDFARHMK VLIKSGASVV GGCCGTTPAF IKALHDIIR // ID D4M5L1_9FIRM Unreviewed; 798 AA. AC D4M5L1; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Draft genome {ECO:0000313|EMBL:CBL26523.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CBL26523.1}; GN ORFNames=RTO_19850 {ECO:0000313|EMBL:CBL26523.1}; OS Ruminococcus torques L2-14. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Blautia. OX NCBI_TaxID=657313 {ECO:0000313|EMBL:CBL26523.1, ECO:0000313|Proteomes:UP000008956}; RN [1] {ECO:0000313|EMBL:CBL26523.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=L2-14 {ECO:0000313|EMBL:CBL26523.1}; 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. RN [2] {ECO:0000313|EMBL:CBL26523.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=L2-14 {ECO:0000313|EMBL:CBL26523.1}; RA Pajon A.; 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; CBL26523.1; -; Genomic_DNA. DR RefSeq; WP_015529111.1; NC_021015.1. DR EnsemblBacteria; CBL26523; CBL26523; RTO_19850. DR KEGG; rto:RTO_19850; -. DR PATRIC; 43182810; VBIRumTor148568_1812. DR KO; K00548; -. DR Proteomes; UP000008956; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008956}; KW Methyltransferase {ECO:0000313|EMBL:CBL26523.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008956}; KW Transferase {ECO:0000313|EMBL:CBL26523.1}. SQ SEQUENCE 798 AA; 86859 MW; 29FEC20D2296AD92 CRC64; MIRERLGKEL LYFDGGMGTL LQAKGLQPGE LPETWNVTHA DEIKNIHKQY ISAGSDIVLA NTFGANALKF HCDDFPLEEI IRLAIRHVKD AAEEASGGRR IYTALDVGPT GKLLKPMGDL DFETAYETFK EVMILGEKAG ADLIHIETMS DTYELKAAVL AAKENTSLPV FATTIFDERG KLLTGADVPS VVAMLEGLRI DALGINCGMG PEQMLPILEQ IMKYSSVPVI VKPNAGLPKQ KDGETYYDVS PEEFASVMRH VVDLGAVVIG GCCGTTPAHI AEMVKQCKDI PVKPIEKKSY TVVSSYGQSV FLGTGSKIIG ERINPTGKKR FKQALKEHDL DYILKEGIAQ QDNGAHILDV NVGLPDIDEP TLMKEVVQEL QSVTNLPLQI DTVDTVAMEN ALRIYNGKAM VNSVSGKQES MDAVFPLIRK YGGVVIGLAL DEDGIPATAE GRVQIAKKII AEAAKYGIEK KDIVIDALAM TISSEPEGAK VTLETLRRLR DEVGVCTVLG VSNISFGLPS RPIVNSIFYT MAMQNGLSVG IINPNSEDMM KAWYAYHALM NLDSNCENYI NKYAQQPGTA PVSATGSAHK MTLKSAIERG LREEANSITS EMIQEKDGLE IINEELIPAL NTVGEGFEKG TVFLPQLLMS AEAAKTAFAV LKEKMDSSGE VQEKKGKIIL ATVKGDIHDI GKNIVKVLLE NYSFDVIDLG KDVPPETIVD TVLEQDIHLV GLSALMTTTV VSMEETIRQL REKAPHCLVM VGGAVLNQDY ADMIGADFYG KDAMQSVHYA QRVFGTEE // ID D4MKU1_9FIRM Unreviewed; 414 AA. AC D4MKU1; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Draft genome {ECO:0000313|EMBL:CBL34374.1}; GN ORFNames=ES1_14000 {ECO:0000313|EMBL:CBL34374.1}; OS [Eubacterium] siraeum V10Sc8a. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminiclostridium. OX NCBI_TaxID=717961 {ECO:0000313|EMBL:CBL34374.1, ECO:0000313|Proteomes:UP000007050}; RN [1] {ECO:0000313|EMBL:CBL34374.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=V10Sc8a {ECO:0000313|EMBL:CBL34374.1}; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Eubacterium siraeum V10Sc8a."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CBL34374.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=V10Sc8a {ECO:0000313|EMBL:CBL34374.1}; RA Pajon A.; 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; FP929059; CBL34374.1; -; Genomic_DNA. DR RefSeq; WP_015567006.1; NC_021043.1. DR EnsemblBacteria; CBL34374; CBL34374; ES1_14000. DR KEGG; esr:ES1_14000; -. DR PATRIC; 43002202; VBIEubSir152769_1482. DR KO; K00548; -. DR BioCyc; ESIR717961-WGS:GSNG-1149-MONOMER; -. DR Proteomes; UP000007050; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007050}. SQ SEQUENCE 414 AA; 44975 MW; 9F70E7F274C0AEFA CRC64; MDSNPVSQDI PIRLPILLDG GTGTGLEKYG YDHTVSTAQF VCANPEALIE LQQGFVDAGS QILYTATHGA NRENLKAYGV EDKTEQLNAA AAKITYDSFH EKALIAGCLS STGLYIEPYG DYTFTEIMSV YRQQVKALSP YCDMFVIETV PALWNMRAAV LACKKENKPI IATMKVDEDG ETAIGTNVLC TLLVLQAMGI SAFGLNCTSA DLCPDIISEI APYAKIPLIV KPSAVYEQDG ERQSISPEEF AFAVKKSVLS GAEIAGGCCG TGKEHIAALR EMFASLDASE INPVEKQDTS LALATENQMF FLDPETTEFS PAVECGPYME DDIAQMCGES YDVLTVSINS PDDAIDFGRN MHMATLPVAF LSDDEISLKM ALMLYQGRAI IDRKSLIEPE KLEAMAEKYG AVLY // ID D4MTN1_9FIRM Unreviewed; 677 AA. AC D4MTN1; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 29-APR-2015, entry version 26. DE SubName: Full=Clostridiales sp. SM4/1 draft genome {ECO:0000313|EMBL:CBL37117.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CBL37117.1}; GN ORFNames=CL3_34960 {ECO:0000313|EMBL:CBL37117.1}; OS butyrate-producing bacterium SM4/1. OC Bacteria; Firmicutes; Clostridia; Clostridiales. OX NCBI_TaxID=245012 {ECO:0000313|EMBL:CBL37117.1, ECO:0000313|Proteomes:UP000008959}; RN [1] {ECO:0000313|EMBL:CBL37117.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SM4/1 {ECO:0000313|EMBL:CBL37117.1}; 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. RN [2] {ECO:0000313|EMBL:CBL37117.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SM4/1 {ECO:0000313|EMBL:CBL37117.1}; RA Pajon A.; 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; FP929060; CBL37117.1; -; Genomic_DNA. DR EnsemblBacteria; CBL37117; CBL37117; CL3_34960. DR PATRIC; 42787126; VBIButBac39087_2802. DR Proteomes; UP000008959; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008959}; KW Methyltransferase {ECO:0000313|EMBL:CBL37117.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008959}; KW Transferase {ECO:0000313|EMBL:CBL37117.1}. SQ SEQUENCE 677 AA; 72938 MW; 17E535718BB77BA2 CRC64; MSDSYELKAA VLGVKEALAG DGISGEQADL PVFATTIFDE KGKLLTGGTP RTVIALLEGL GVDAVGINCG LGPVQMKEFV REFAKYASVP IIVNPNAGLP RSVEGRTVYD IDEDQFAKAM AEIVDMGASV VGGCCGTTPE YIRKLCLACR EKKQKLPSKK AETVVTSYSQ LVEIASDPVI IGERINPTGK PKFKQALRDH DMEYILREGL AQQDSGAQVL DVNVGLPEID EPSMMEEAVR ELQSILDLPL QIDTSNIEAM ERAMRIYNGK PLINSVNGKA ESMDAIFPLV KKYGGVVVAL TLDEEGIPDT ADGRIRVAEK IYRRAAQYGI DKKDILIDTL CMTISSDSQG ALTTLEAVRR IRDELHGKTI LGVSNVSFGL PQRESINAAF FTMAMMNGLS AAIINPNSDA MMRSWRSFRA LAALDENCGD YISAYGGQTK QQPSDTVFGK GEAVSEKAPE EVQEIHESHK SQVQLWESVV RGLKEQAARA AAAALKEASP LEVINACMIP ALDCVGKGFE QGTVFLPQLL MSAEAAKAAF EVLKAAMAGS GKSQEKKGVI ILATVRGDIH DIGKNIVKVL LENYSYEVVD LGKDVPPERI AEETVKHRAP LVGLSALMTT TVPSMEETIR LLRKEAGWAK IMVGGAVLTP EYADSIGADA YCKDAMASVN YAQKVIG // ID D4MY48_9FIRM Unreviewed; 318 AA. AC D4MY48; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Clostridiales sp. SSC/2 draft genome {ECO:0000313|EMBL:CBL37543.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:CBL37543.1}; GN ORFNames=CL2_04730 {ECO:0000313|EMBL:CBL37543.1}; OS butyrate-producing bacterium SSC/2. OC Bacteria; Firmicutes; Clostridia; Clostridiales. OX NCBI_TaxID=245018 {ECO:0000313|EMBL:CBL37543.1, ECO:0000313|Proteomes:UP000008960}; RN [1] {ECO:0000313|EMBL:CBL37543.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SSC/2 {ECO:0000313|EMBL:CBL37543.1}; 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. SSC/2."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CBL37543.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SSC/2 {ECO:0000313|EMBL:CBL37543.1}; RA Pajon A.; 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; CBL37543.1; -; Genomic_DNA. DR RefSeq; WP_015530253.1; NC_021016.1. DR EnsemblBacteria; CBL37543; CBL37543; CL2_04730. DR KEGG; bprl:CL2_04730; -. DR PATRIC; 42794820; VBIButBac135163_0651. DR KO; K00547; -. DR BioCyc; BBAC245018-WGS:GSIN-422-MONOMER; -. DR Proteomes; UP000008960; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008960}; KW Methyltransferase {ECO:0000313|EMBL:CBL37543.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008960}; KW Transferase {ECO:0000313|EMBL:CBL37543.1}. SQ SEQUENCE 318 AA; 35669 MW; 5B678CE3D89DDDA3 CRC64; MKNSIENIIK ENKIMVIDGS MSTPLENRGV SLNSKLWTAK ILAEQPELIK QVHKNYFKAG ADCGITCSYQ ASIPGLMENG YTLEEAENLI RSAVKIFCEA RDEWWEEEGR EARRAWPLCL GAAGPYGAYL ADGSEYRGNY GITDEQLKEF HKRRVELLHE AGADIILFET VPSLKEAKVE AEIAEEYGYD YWISFSCLSE NIICEGTPIA ECATTFAKGY PHLKMIGVNC TKPEYITGLI HKIKENCDIP IGVYPNSGEE YDAVKKVWFG KQSALSFEQY AYNYMKSGAS AVGGCCTTVA KHVEEVVRAK KRFSEEQK // ID D4N1A5_9FIRM Unreviewed; 791 AA. AC D4N1A5; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=Clostridiales sp. SSC/2 draft genome {ECO:0000313|EMBL:CBL38650.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CBL38650.1}; GN ORFNames=CL2_17300 {ECO:0000313|EMBL:CBL38650.1}; OS butyrate-producing bacterium SSC/2. OC Bacteria; Firmicutes; Clostridia; Clostridiales. OX NCBI_TaxID=245018 {ECO:0000313|EMBL:CBL38650.1, ECO:0000313|Proteomes:UP000008960}; RN [1] {ECO:0000313|EMBL:CBL38650.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SSC/2 {ECO:0000313|EMBL:CBL38650.1}; 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. SSC/2."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CBL38650.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SSC/2 {ECO:0000313|EMBL:CBL38650.1}; RA Pajon A.; 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; CBL38650.1; -; Genomic_DNA. DR RefSeq; WP_008392153.1; NC_021016.1. DR ProteinModelPortal; D4N1A5; -. DR EnsemblBacteria; CBL38650; CBL38650; CL2_17300. DR KEGG; bprl:CL2_17300; -. DR PATRIC; 42797220; VBIButBac135163_2023. DR KO; K00548; -. DR BioCyc; BBAC245018-WGS:GSIN-1534-MONOMER; -. DR Proteomes; UP000008960; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008960}; KW Methyltransferase {ECO:0000313|EMBL:CBL38650.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008960}; KW Transferase {ECO:0000313|EMBL:CBL38650.1}. SQ SEQUENCE 791 AA; 86556 MW; CF2CEBDABBF04460 CRC64; MLQNRLGKEL LIFDGAMGTQ LQNAGLSAGD IPEELNIDRP DLLRSIHKNY LKAGADFITT NTFGCNRLKM EEAKYEAKDM LLAAVENARV ARTEAGREDD SYIVLDIGPI GQLLEPMGTL TFDEAYDIIL EQVETVKDQV DLVLFETMSD LYEVKAGVLA VKEHTDLPVF VTMTFEQNGR TLSGNDPETF INVAEGLGVD ALGVNCSLGP DELKPIIDEI LEKASIPVML QPNAGLPCLE HGETHYHVTP EEYVESMKDY MARGAAIVGG CCGTTPEFIG KLAEAAPKAV AERTVEKKTR VSSQTQTVTF GDHVIVCGER LNPTGKKKMK KALLEERYDE LVVEAVKQVE AGAEVLDVNV GLPGIDEPET MKRVVRLLQE VVTLPLQIDS SEADAIENAC RYYNGKPLIN SVNGKDEVME KIFPIAKKYG GVVIGLTLED GIPLKAEERF EIAKKIVNKA AEYGIGKENI IIDCLTLTAS AQQKEVKETL RAIKMVKKEL GVNTVLGVSN VSFGLPNRPL LNRTFLALAM EAGLDLPIIN PLDAELMGTI DAFHVLFYKD VDSQTYIKNQ SKDKETKPAA AAATTNFTLK DVIIHGLKDE VEKVTKEELK DKEALTVINE VIIPALNIVG KDYETGKIFL PQLIQSAETT KKAFEVVKET FSANDGEEKG PIIIATVEGD IHDIGKNIVK VVLESYGYKI IDLGKDVKVE KVVEAYKKYK PKAIGLSALM TTTVASMERT IKALHEAGCS EPIWVGGAVV TEDIAHNIGA DYYTEDAMAA VNLLENEILI L // ID D4S1Z9_9FIRM Unreviewed; 789 AA. AC D4S1Z9; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFF67701.1}; GN ORFNames=BUTYVIB_02121 {ECO:0000313|EMBL:EFF67701.1}; OS Butyrivibrio crossotus DSM 2876. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Butyrivibrio. OX NCBI_TaxID=511680 {ECO:0000313|EMBL:EFF67701.1}; RN [1] {ECO:0000313|EMBL:EFF67701.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 2876 {ECO:0000313|EMBL:EFF67701.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFF67701.1}. 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; ABWN01000036; EFF67701.1; -; Genomic_DNA. DR RefSeq; WP_005604105.1; NZ_GG663524.1. DR EnsemblBacteria; EFF67701; EFF67701; BUTYVIB_02121. DR PATRIC; 30456205; VBIButCro39456_2169. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFF67701.1}; KW Transferase {ECO:0000313|EMBL:EFF67701.1}. SQ SEQUENCE 789 AA; 85416 MW; 392D32F89FDCD643 CRC64; MNILDELGRR ILFFDGGLSS LLQERGLEPG ELPETWNLTR PEILIDIHKA YINAGADIIN ANTFGANRFK FDNLEEIITA GIANAKKAVA ETGKKAYVAL DIGSCGKLLK PMGTLDFADA VDVFAEIVRI GDKAGADLIL IETMSDTYEL KAAVLAAKEN SDLPVFATVI FDESHKMLTG ATPAAVVALL EGLNVDAIGM NCGLGPEQMK PIFEEMAEYA SVPLIINPNA GLPRSENGRT VYDVGPEEFA GYMELLVKDG AWIIGGCCGT TPEHIMATYD RCKDLKPIPI VEKDITLVSS YSHAVEIGKV PVIIGERINP TGKSKFKQAL RDHNMTYILE EGTKQADSGA HILDVNVGLP EIDETAMMKD TVFELQSILD LPLQIDTTDM NAMETAMRIY NGKPMVNSVN GKKEVMEQVF PLVKKYGGAV VALCLDEDGI PDTAEGRIKI AEKIYATAAT YGIKAKDIVI DALTMTMSTD NESANITLDT VREIKARGGR TVLGVSNISF GLPQRELITS TFFTMALQAG LSAGIINPNA KAMMQSYDTY MVLSGNDSQC TKYIEKYAVA PETAETKPKT TANFSLSDCI VKGLKENAYT ETVELLKTKA PMDIINGDLV PALDIVGKGF EKGTMFLPQL LMSAEAAKAG FEAIKEYMKK SGSSEEKKAT VVIATVKGDI HDIGKNIVKV ILENYSYNVI DLGKDVPPED VVDAVIANDA KLVGLSALMT TTVVNMEATI KLLREKCPDC KIMVGGAVLT QEYADMIGAD FYGKDAMQSV YYAESLFNK // ID D4S4K6_9FIRM Unreviewed; 325 AA. AC D4S4K6; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 27-MAY-2015, entry version 11. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFF66842.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EFF66842.1}; GN Name=mmuM {ECO:0000313|EMBL:EFF66842.1}; GN ORFNames=HMPREF7545_0471 {ECO:0000313|EMBL:EFF66842.1}; OS Selenomonas noxia ATCC 43541. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Selenomonas. OX NCBI_TaxID=585503 {ECO:0000313|EMBL:EFF66842.1}; RN [1] {ECO:0000313|EMBL:EFF66842.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43541 {ECO:0000313|EMBL:EFF66842.1}; 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-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. {ECO:0000313|EMBL:EFF66842.1}. 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; ACKT01000013; EFF66842.1; -; Genomic_DNA. DR RefSeq; WP_006695467.1; NZ_GG749282.1. DR EnsemblBacteria; EFF66842; EFF66842; HMPREF7545_0471. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFF66842.1}; KW Transferase {ECO:0000313|EMBL:EFF66842.1}. SQ SEQUENCE 325 AA; 34696 MW; A3CF0ED64D3DBE16 CRC64; MTAVGQKAYG GGTGLNVIEE RLAVQDVIVL DGAFATELEA RGFSVNDALW SAKALFERPD LVREVHLDYL RAGADVVTSA SYQATVEGFQ KRGFSAEEAA ALLQTSVHLA QEARDLYLAE HGAGGSAPLV AASVGPYGAY LADGSEYRGN YGIDEDALTA FHAERLAILA AAHPDLLACE TLPCLVEARA VVRALREKEI CIPAWFSFSC RDAAHISDGT PIAVCARWLD SVPEAAAVGL NCTAPQHVEE LIRAIRRETE KPIVIYPNSG ESYDASDKTW HGAAENFAAA ARRWRAAGAR IIGGCCRTGP RDIAAIAVWA KEKAE // ID D4S4M6_9FIRM Unreviewed; 597 AA. AC D4S4M6; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 27-MAY-2015, entry version 24. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HMPREF7545_0491 {ECO:0000313|EMBL:EFF66708.1}; OS Selenomonas noxia ATCC 43541. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Selenomonas. OX NCBI_TaxID=585503 {ECO:0000313|EMBL:EFF66708.1}; RN [1] {ECO:0000313|EMBL:EFF66708.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43541 {ECO:0000313|EMBL:EFF66708.1}; 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-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFF66708.1}. 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; ACKT01000015; EFF66708.1; -; Genomic_DNA. DR RefSeq; WP_006694381.1; NZ_GG749280.1. DR ProteinModelPortal; D4S4M6; -. DR EnsemblBacteria; EFF66708; EFF66708; HMPREF7545_0491. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EFF66708.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EFF66708.1}. SQ SEQUENCE 597 AA; 64527 MW; 1FEC478FD9B7504E CRC64; MAQNSADIRE HIKKEPLVFD GGMGTYYAQK THTHGKGVEL ANIETPAVVG AIHTEYLQAG AQAIKTNTFA ANRIVYQGDE SLVRRIIRAG WEIAARAAEP FGAYVFADIG PVTGLPHTDI IAEYRFLADT FLACGATHFL FETNASIEGL IETAAHIKRI CPHAFILASF SALPGGYTRD GRFAEDLIHE AAESGSIDAV GFNCVNGVRQ MRELGHHLGM TSLPLSLMPN AGHPIVVDGR TFYESAPEYF GTSLAAIVRD GISIVGGCCG TTPEHIRALC AALADGTGEI DEEGEETRVQ PMEVPLSPFF DALKSGGKPI AVELDPPETG NADKFLVGVR ELQAAGISAI TIADNPIARA RMDAAMLAGR VHRELGIEPI PHMTCRDRNL NAIKSILLGL SAEGVHNMIA ITGDPIPTAE RDEVKSVYQF NSRKLASFVT SLGSRGDIVP FHVFGALNVN AKHFPSQLGL ARKKMEAGMT GFFTQPVLSE RAKENLQTAR DMLPGAFILG GIMPVVSERN ARFMESEIVG IHVEERIISA YRGLDRTAAE ELAVRLSLAI AKDIEPYIDG YYIITPFSRT ALIARIVEGI KERGEIR // ID D4S4M7_9FIRM Unreviewed; 802 AA. AC D4S4M7; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFF66709.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFF66709.1}; GN Name=metH {ECO:0000313|EMBL:EFF66709.1}; GN ORFNames=HMPREF7545_0492 {ECO:0000313|EMBL:EFF66709.1}; OS Selenomonas noxia ATCC 43541. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Selenomonas. OX NCBI_TaxID=585503 {ECO:0000313|EMBL:EFF66709.1}; RN [1] {ECO:0000313|EMBL:EFF66709.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43541 {ECO:0000313|EMBL:EFF66709.1}; 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-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. {ECO:0000313|EMBL:EFF66709.1}. 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; ACKT01000015; EFF66709.1; -; Genomic_DNA. DR RefSeq; WP_006694382.1; NZ_GG749280.1. DR EnsemblBacteria; EFF66709; EFF66709; HMPREF7545_0492. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFF66709.1}; KW Transferase {ECO:0000313|EMBL:EFF66709.1}. SQ SEQUENCE 802 AA; 86066 MW; 8C7382C79220E63F CRC64; MKDIIILDGG MGTELQARGL APGERPELFG IEHPEVVEEI HRNYIAAGSR VIYSNTFGAN GHKLAGTGKT VAEVIGANVQ IARRAAEHSG VEGVRVALDV GPIGELVEPL GTLSFEAAYE LFREMAVAGE EAGADLIIFE TLTDLYEAKA AVLAAKEHTK LPIWVTMTFE QNGRTFLGAA VPSVAVTLDA LGVAAIGVNC SLGPVELLPI VDELMEWTDL PVIVKPNAGL PDPRTGAYEM TAEEFGREMA EFARRGAVIM GGCCGTNPEF IRALAASVAS GAAERPERRK RKGIASPGRV AEYGKLNVIG ERINPTGKKR LQQALLEEDY GYIKKLAISQ QEAGAQVLDI NVGAQGVDEE KIIPYVVKAV QSVVDLPLQI DSANPKVIAA ALRVTNGRVI INSVSGERER MDAIFPLAKH YGAAVLGLAM DEKGLPETAA DRIAVAERIV AEAERYGIER EDIIIDCLTL TVSAQQNQAM ETLRAVREVH ERLGLHCALG VSNISFGLPA RVHMTENFLI QAMHVGLDFP IVNPNTKEIM DAVISFRAVS GEDVDCAAYI ARFAPEQAEI RRRKELGITG SESPDAVQTA AADGADDVDP LMDAIIRGLS DDAERITRKL LTEKAPMEII QEKVIPALDI VGDRYEKEII FLPQLINAAN AATAGLELIK ARLAEEGQGV SKGKIILATV EGDIHDIGKN IVKVVLENYG YQIIDLGRDV PVTRVVEVAI EKQVGLIGLS ALMTTTVTAM KRTIDALHEA GHECETVVGG AVLTEDYARE IGADHYAGDA RSIVEIARRV LG // ID D4SR65_9XANT Unreviewed; 379 AA. AC D4SR65; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|EMBL:EFF45340.1}; GN Name=metH {ECO:0000313|EMBL:EFF45340.1}; GN ORFNames=XAUB_05600 {ECO:0000313|EMBL:EFF45340.1}; OS Xanthomonas fuscans subsp. aurantifolii str. ICPB 11122. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=427081 {ECO:0000313|EMBL:EFF45340.1}; RN [1] {ECO:0000313|EMBL:EFF45340.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ICPB 11122 {ECO:0000313|EMBL:EFF45340.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFF45340.1}. 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; ACPX01000108; EFF45340.1; -; Genomic_DNA. DR RefSeq; WP_007962623.1; NZ_ACPX01000108.1. DR EnsemblBacteria; EFF45340; EFF45340; XAUB_05600. DR PATRIC; 35668825; VBIXanFus92710_0387. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFF45340.1}; KW Transferase {ECO:0000313|EMBL:EFF45340.1}. SQ SEQUENCE 379 AA; 40536 MW; 4DE616A884C4988B CRC64; MTLVRIPDPE SPIQFALPWL HPERAAKLTA ALAERILIID GAMGTMIQRH DLQEPDYRGT RFADGYDSAH VHGPGCDHAH VPQGHDLKGN NDLLLLTRPE IIAGIHRAYL EAGADLLETN TFNATSVSQA DYHLEHLVYE LNKAGAQVAR ACCDDVEALT PHKPRFVIGV LGPTSRTASI SPDVNDPGYR NTSFDALRAA YREAIEGLID GGADTLMVET IFDTLNAKAA LYAIEEVFDA RGGRLPVMVS GTITDASGRT LSGQTAEAFY ASVAHGRPLS IGLNCALGAR DLRPHVETLA QIADAYVSAH PNAGLPNAFG EYDETPEEMA QTLREFAQAG LLNLVGGCCG TSPDHIRAIA EAVADLPPRQ LPGAQELAA // ID D4SVC1_9XANT Unreviewed; 321 AA. AC D4SVC1; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 27-MAY-2015, entry version 12. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:EFF43865.1}; GN Name=mmuM {ECO:0000313|EMBL:EFF43865.1}; GN ORFNames=XAUB_20430 {ECO:0000313|EMBL:EFF43865.1}; OS Xanthomonas fuscans subsp. aurantifolii str. ICPB 11122. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=427081 {ECO:0000313|EMBL:EFF43865.1}; RN [1] {ECO:0000313|EMBL:EFF43865.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ICPB 11122 {ECO:0000313|EMBL:EFF43865.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFF43865.1}. 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; ACPX01000187; EFF43865.1; -; Genomic_DNA. DR RefSeq; WP_007965586.1; NZ_ACPX01000187.1. DR EnsemblBacteria; EFF43865; EFF43865; XAUB_20430. DR PATRIC; 35672348; VBIXanFus92710_2089. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFF43865.1}; KW Transferase {ECO:0000313|EMBL:EFF43865.1}. SQ SEQUENCE 321 AA; 34232 MW; 58F7BF64A7AA8430 CRC64; MTILPRQPRP NAPFSQALQH DGYVVLDGAL ATELEQRGCD LNDALWSARV LMEQPELIYQ VHRDYFAAGA QCAITASYQA TPLGFAARGL DVAQAQALIA RSVALAVQAR ADHLTLHPHA APLWVAGLVG PYGAYLADGS EYRGDYVLPI EQLMDFHRPR IAALAEAGVD LLACETLPSV SEIVALRQLL QHDFPQLHAW FSFTLRDAAH LSDGTPLAQV VPALDACAQV IAVGVNCIAL DQATAALHSL SALTALPLVV YPNSGEHYDA SDKRWHAGRG AALTLADQHA HWLAAGARLI GGCCRTAPRD IAALAAARAA E // ID D4T404_9XANT Unreviewed; 321 AA. AC D4T404; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 27-MAY-2015, entry version 12. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:EFF48564.1}; GN Name=mmuM {ECO:0000313|EMBL:EFF48564.1}; GN ORFNames=XAUC_10490 {ECO:0000313|EMBL:EFF48564.1}; OS Xanthomonas fuscans subsp. aurantifolii str. ICPB 10535. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=427082 {ECO:0000313|EMBL:EFF48564.1}; RN [1] {ECO:0000313|EMBL:EFF48564.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ICPB 10535 {ECO:0000313|EMBL:EFF48564.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFF48564.1}. 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; ACPY01000152; EFF48564.1; -; Genomic_DNA. DR RefSeq; WP_007971186.1; NZ_ACPY01000152.1. DR EnsemblBacteria; EFF48564; EFF48564; XAUC_10490. DR PATRIC; 35679557; VBIXanFus21887_1145. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFF48564.1}; KW Transferase {ECO:0000313|EMBL:EFF48564.1}. SQ SEQUENCE 321 AA; 34206 MW; 405E9EFE8C03A5A0 CRC64; MTILPRQPRP NAPFSQALQH DGYVVLDGAL ATELEQRGCD LNDALWSARV LMEQPELIYQ VHRDYFAAGA QCAITASYQA TPLGFAARGL DVAQAQALIA RSVALAVQAR ADHLTLHPHA APLWVAGSVG PYGAYLADGS EYRGDYVLPI EQLMDFHRPR IAALAEAGVD LLACETLPSV SEIVALRQLL QHDFPQLHAW FSFTLRDAAH LSDGTPLAQV VPALDACAQV IAVGVNCIAL DQATAALHSL SALTALPLVV YPNSGEHYDA SDKRWHAGRG AALTLADQHA HWLAAGARLI GGCCRTAPRD IAALAAARAA E // ID D4T5M2_9XANT Unreviewed; 379 AA. AC D4T5M2; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|EMBL:EFF48020.1}; GN Name=metH {ECO:0000313|EMBL:EFF48020.1}; GN ORFNames=XAUC_16200 {ECO:0000313|EMBL:EFF48020.1}; OS Xanthomonas fuscans subsp. aurantifolii str. ICPB 10535. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=427082 {ECO:0000313|EMBL:EFF48020.1}; RN [1] {ECO:0000313|EMBL:EFF48020.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ICPB 10535 {ECO:0000313|EMBL:EFF48020.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFF48020.1}. 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; ACPY01000181; EFF48020.1; -; Genomic_DNA. DR RefSeq; WP_007972015.1; NZ_ACPY01000181.1. DR EnsemblBacteria; EFF48020; EFF48020; XAUC_16200. DR PATRIC; 35680881; VBIXanFus21887_1783. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFF48020.1}; KW Transferase {ECO:0000313|EMBL:EFF48020.1}. SQ SEQUENCE 379 AA; 40536 MW; 38C5F8DA61BC231E CRC64; MTLVRIPDAE SPIQFALPWL HPERAAKLTA ALAERILIID GAMGTMIQRH DLQEPDYRGT RFADGYDSAH VHGPGCDHAH VPQGHDLKGN NDLLLLTRPE IIAGIHRAYL EAGADLLETN TFNATSVSQA DYHLEHLVYE LNKAGAQVAR ACCDDVEALP PHKPRFVIGV LGPTSRTASI SPDVNDPGYR NTSFDALRAT YREAIEGLID GGADTLMVET IFDTLNAKAA LYAIEEVFDA RGGRLPVMVS GTITDASGRT LSGQTAEAFY ASVAHGRPLS IGLNCALGAR DLRPHVETLA QIADAYVSAH PNAGLPNAFG EYDETPEEMA QTLREFAQAG LLNLVGGCCG TSPDHIRAIA EAVADLPPRQ LPGAQELAA // ID D4TCX6_9NOST Unreviewed; 1177 AA. AC D4TCX6; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFA71197.1}; GN ORFNames=CRC_00051 {ECO:0000313|EMBL:EFA71197.1}; OS Cylindrospermopsis raciborskii CS-505. OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Cylindrospermopsis. OX NCBI_TaxID=533240 {ECO:0000313|EMBL:EFA71197.1}; RN [1] {ECO:0000313|EMBL:EFA71197.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CS-505 {ECO:0000313|EMBL:EFA71197.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFA71197.1}. 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; ACYA01000002; EFA71197.1; -; Genomic_DNA. DR RefSeq; WP_006275777.1; NZ_ACYA01000002.1. DR EnsemblBacteria; EFA71197; EFA71197; CRC_00051. DR PATRIC; 35893258; VBICylRac118657_0258. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFA71197.1}; KW Transferase {ECO:0000313|EMBL:EFA71197.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 228 228 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 737 737 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1177 AA; 130781 MW; 389F489A93F7DFCD CRC64; MTHSFLERLH SPEHPVIVFD GAMGTNLQIQ NLTAEDFGGP EYEGCNEYLI HTKPEAVAKV HRDFLLAGAD VIETDTFGGT SIVLAEYDLA DQAYYLSKNA AELAKRVAAE FSTPEKPRFV AGSIGPTTKL PTLGHIDFDT MKSAFAEQVT ALFDGGVDLF IVETCQDVLQ IKAALNGIEE VFSQKGERRP VMVSVTMESM GTMLVGTEIA AVLTILAPYS IDILGLNCAT GPDLMKPHIK YLSEHSPFVV SCIPNAGLPE NIGGQAHYKL TPLELRIALM HFVEDLGVQV IGGCCGTRPD HIQQLAEIAK DLKPKVRQPS LEPAAASIYS TQNYTQDNSF LIVGERLNAS GSKKCRDLLN AEDWDGLVSI ARSQVKEGAH ILDVNVDYVG RDGVHDMHEL VSRVVNNVTL PLMLDSTEWE KMEAGLKVAG GKCLLNSTNY EDGEPRFLKV LELGKKYGAG VVIGTIDEEG MARTAQKKFE IAQRAYRQAV EYGIPASEIF FDTLALPIST GIEEDRKNGS ATIESIRRIR EELPECHVIL GVSNISFGLN PAARIVLNSM FLHEAMEAGM DAAIVSASKI LPLAKIDPQH QEVCKQLIYD QRRFNGDVCV YDPLAELTRL FAGVKAKQNR GIDESLPIEE RLKLHIIDGE RIGLEAQLAK ALEQYPPLDI INTFLLDGMK VVGELFGAGQ MQLPFVLQSA ETMKAAVAYL EPYMEKSGAG SNAKGIFVIA TVKGDVHDIG KNLVDIILSN NGYKVINLGI KQPVENIIQA YEKHQPDCIA MSGLLVKSTA FMKENLEVFN EKGITVPVIL GGAALTPKFV NQDCQNTYHG KVIYGKDAFD DLNFMDKLMP AKAAGKWDDL QGFLDEVKGD LPEINPQIKE RIKEEVKQQP TEVDTRRSEA VNANIERPQP PFWGSRFLQP QDIPLEEVLY YLDLQALIVG QWQFRKPKEK SQAEHQEFLI DTVYPLLENW KQRVIQEKLL HPQVIYGYFP CQAVGNSLLI YETTHINSKN PVITTTFEFP RQRSGRRYCI ADFFAPKESG LIDVFPMQAV TVGEVATKFA QNLFGENKYT DYLYFHGIAV QVAEALAEWI HAKIRQELGF GDVEPDNIRD ILAQRYQGSR YSFGYPACPN ISDQHKQLQL LDANRMGMYM DESEQLYPEQ STTAIIAYHP TAKYFTA // ID D4TN20_9NOST Unreviewed; 1177 AA. AC D4TN20; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFA74114.1}; GN ORFNames=CRD_00798 {ECO:0000313|EMBL:EFA74114.1}; OS Raphidiopsis brookii D9. OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Raphidiopsis. OX NCBI_TaxID=533247 {ECO:0000313|EMBL:EFA74114.1}; RN [1] {ECO:0000313|EMBL:EFA74114.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=D9 {ECO:0000313|EMBL:EFA74114.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFA74114.1}. 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; ACYB01000007; EFA74114.1; -; Genomic_DNA. DR RefSeq; WP_009341691.1; NZ_ACYB01000007.1. DR EnsemblBacteria; EFA74114; EFA74114; CRD_00798. DR PATRIC; 35901249; VBIRapBro106515_0373. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFA74114.1}; KW Transferase {ECO:0000313|EMBL:EFA74114.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 228 228 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 737 737 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1177 AA; 130876 MW; 9C07372E4CDA15E8 CRC64; MTYSFLERLH SPEHPVIVFD GAMGTNLQIQ NLKAEDFGGP EYEGCNEYLI HTKPEAVAKV HRDFLLAGAD VIETDTFGGT SIVLAEYDLA DQAYYLSKKA AELAKRVAGE FSTPEKPRFV AGSIGPTTKL PTLGHIDFDT MKSAFAEQVT ALFDGGVDLF IVETCQDVLQ IKAALNGIEE VFSQKGERRP VMVSVTMESM GTMLVGTEIA AVLTILAPYS IDILGLNCAT GPDLMKPHIK YLSEHSPFVV SCIPNAGLPE NIGGQAHYKL TPLELRMALM HFVEDLGVQV IGGCCGTRPD HIQQLAEIAK DLKPKVRQPS LEPAAASIYS TQNYTQDNSF LIVGERLNAS GSKKCRDLLN TEDWDGLVSI ARSQVKEGAH ILDVNVDYVG RDGVRDMHEL VSRVVNNVTL PLMLDSTEWE KMEAGLKVAG GKCLLNSTNY EDGEPRFLKV LELGKKYGAG VVIGTIDEEG MARTAQKKFE IAQRAYRQAV EYGIAPSEIF FDTLALPIST GIEEDRKNGS ATIESIRRIR EELPDCHVIL GVSNISFGLN PAARIVLNSM FLHEAMGAGM DAAIVSASKI LPLAKIDPQH QEVCKQLIYD QRRFEGNVCV YDPLAELTRL FAGVKAKQNR GIDESLPIEE RLKLHIIDGE RIGLEAQLAK ALEQYPPLDI INTFLLDGMK VVGELFGAGQ MQLPFVLQSA ETMKAAVAYL EPFMEKSGAG SNGKGIFVIA TVKGDVHDIG KNLVDIILSN NGYKVINLGI KQPVENIIQA YEKHQPDCIA MSGLLVKSTA FMKENLEVFN EKGITVPVIL GGAALTPKFV NQDCQNTYHG KVIYGKDAFD DLNFMDKLMP AKAAGKWDDL QGFLDEVKGD LPEINTQIKE QIKEEVKQQP REVDTQRSEA VNANIERPQP PFWGSRFLQP QDIPLEEVLY YLDLQALIVG QWQFRKPKEK SQAEHQQFLI DTVYPLLENW KQRVIQEKLL HPQVIYGYFP CQAVGNSLWI YETTQINGKD PVISTTFKFP RQRSGRRYCI ADFFAPKESG LIDVFPMQAV TVGEVATQFA QKLFAEDKYT DYLYFHGIAV QVAEALAEWT HAKIRQELGF GNVEPNNIRD ILAQRYQGSR YSFGYPACPN ISDQYKQLQL LDAKRMGMYM DESEQLYPEQ STTAIIAYHP TAKYFTA // ID D4VEJ9_BACVU Unreviewed; 917 AA. AC D4VEJ9; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFG15764.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFG15764.1}; GN Name=metH {ECO:0000313|EMBL:EFG15764.1}; GN ORFNames=CUU_2614 {ECO:0000313|EMBL:EFG15764.1}; OS Bacteroides vulgatus PC510. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=702446 {ECO:0000313|EMBL:EFG15764.1}; RN [1] {ECO:0000313|EMBL:EFG15764.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PC510 {ECO:0000313|EMBL:EFG15764.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFG15764.1}. 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; ADKO01000117; EFG15764.1; -; Genomic_DNA. DR RefSeq; WP_005847467.1; NZ_ADKO01000117.1. DR ProteinModelPortal; D4VEJ9; -. DR SMR; D4VEJ9; 652-894. DR EnsemblBacteria; EFG15764; EFG15764; CUU_2614. DR GeneID; 5303492; -. DR PATRIC; 36608137; VBIBacVul154801_4026. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFG15764.1}; KW Transferase {ECO:0000313|EMBL:EFG15764.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 243 243 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 917 AA; 100856 MW; E91AC6CE0F06EA5A CRC64; MATLKQLIDE RVLILDGAMG TMIQRYNLSE QDFRGERFAE MPGQMKGNND LLCLTRPDVI KDIHHKYLEA GADIIETNTF NAQRVSMADY HMQDLCREIN LAAAGLAREM ADEYTAKTPH KPRFVAGSVG PTNKTCSMSP DVNNPALRAL TYDELAAAYQ EQMEALLEGG VDALLIETIF DSLNAKAAIY AAETAMKKIG REVPLMLSVT VSDIAGRTLS GQTLDAFLAS VQHAPIFSIG LNCSFGAKQL KPFLEGLAAR APYYISAYPN AGLPNSLGQY DQTPEEMASE VKEYIDEGLV NIIGGCCGTT EEYIAKYQEL IVSGSAWVSP HIPATTPERL WLSGLELLEQ TPEMNFINVG ERCNVAGSRK FLRLINEKKY EEALSIARKQ VEDGALVIDV NMDDGLLDAR EEMTTFLNLV MSEPDIARVP VMIDSSKWEV IEAGLKCLQG KSIVNSISLK EGEEIFIEHA RLIKKLGAAV VVMAFDEKGQ ADTFERKIEV CARAYKILTE QVDFNPHDII FDPNVLAVAT GIEEHDNYAV DFIKATGWIK KNLPGAHVSG GVSNLSFSFR GNNYIREAMH AVFLYHAIRQ GMDMGIVNPA ASVLYTDIPA DVLERIEDVV LNRRPDAAER LIETAEALKN TATGTEAVKQ DVWREEPMVE KRLQYALIKG IGDHLEEDLA EAVKLYPKAV DIIEGPLMEG MNKVGELFGA GKMFLPQVVK TARTMKKAVA ILQPLIEADK QEGVRSAGKV LMATVKGDVH DIGKNIVSVV MACNNYEIID LGVMVPAEMI VRKAIEEKVD IIGLSGLITP SLEEMAHVAV ELKRAGLDIP IMIGGATTSK LHTALKIAPV YGGPVIHMKD ASQNALVAAR LLNPESSFEF VERLNKEYED LRLKNSAKQV KTVSLEEAQK NKLNLWS // ID D4VNA7_9BACE Unreviewed; 915 AA. AC D4VNA7; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:CDM06832.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CDM06832.1}; GN ORFNames=BN890_44500 {ECO:0000313|EMBL:CDM06832.1}; OS Bacteroides xylanisolvens SD CC 1b. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=702447 {ECO:0000313|EMBL:CDM06832.1, ECO:0000313|Proteomes:UP000019380}; RN [1] {ECO:0000313|EMBL:CDM06832.1} 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. {ECO:0000313|EMBL:CDM06832.1}. 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; CBXG010000049; CDM06832.1; -; Genomic_DNA. DR EnsemblBacteria; CDM06832; CDM06832; BN890_44500. DR EnsemblBacteria; EFG12659; EFG12659; CW3_0955. DR PATRIC; 36614426; VBIBacXyl153952_3031. DR Proteomes; UP000019380; Unassembled WGS sequence. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000019380}; KW Methyltransferase {ECO:0000313|EMBL:CDM06832.1}; KW Transferase {ECO:0000313|EMBL:CDM06832.1}. SQ SEQUENCE 915 AA; 99932 MW; 18EED729F9367757 CRC64; MKKTISQVVS ERILILDGAM GTMIQQYNLK EEDFRGERFA HIPGQLKGNN DLLCLTRPDV IQDIHRKYLE AGADIIETNT FSSTTVSMAD YHVEEYVREM NLAAVKLARD LADEYTAKNP DKPRFVAGSV GPTNKTCSMS PDVNNPAYRA LSYDELAASY QQQMEAMLEG GVDAILIETI FDTLNAKAAI FAAEQAMKAT GVEVPVMLSV TVSDIGGRTL SGQTLDAFLA SMQHANIFSV GLNCSFGARQ LKPFLEQLAA RAPYYISAYP NAGLPNSLGK YDQTPADMAH EVREYIEEGL INIIGGCCGT TDAYIAEYPA LVKGAKPHIP ALAPDCMWLS GLELLEVKPE INFVNVGERC NVAGSRKFLR LINEKKYDEA LSIARQQVED GALVIDVNMD DGLLDAKTEM TTFLNLIMSE PEIARVPVMI DSSKWEVIEA GLKCLQGKSI VNSISLKEGE EVFLEHARII RQYGAATVVM AFDEKGQADT AARKIEVCER AYRLLVDKVG FNPHDIIFDP NVLAVATGIE EHNNYAVDFI EATAWIKKNL PGAHISGGVS NLSFSFRGNN YIREAMHAVF LYHAIQQGMD MGIVNPGTSV LYSDIPTDVL EKIEDVVLNR RPDAAERLIE LAESLKATMS GTAGQPAAKQ DAWREESVQE RLKYALMKGI GDFLEQDLAE ALPLYDKAVD VIEGPLMDGM NYVGELFGAG KMFLPQVVKT ARTMKKAVAI LQPIIESEKV EGSAAAGKVL LATVKGDVHD IGKNIVAVVM ACNGYDIVDL GVMVPAETIV QRAIEEKVDM IGLSGLITPS LEEMAHVALE LEKAGLDIPL LIGGATTSKM HTALKIAPVY HAPVVHLKDA SQNASVASKL LNPQLKAELV NELNSEYEAL REKSGLLKRE TVSLEEAQKN KLNLF // ID D4WIN0_BACOV Unreviewed; 915 AA. AC D4WIN0; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 01-APR-2015, entry version 23. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFF51597.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFF51597.1}; GN Name=metH {ECO:0000313|EMBL:EFF51597.1}; GN ORFNames=CUY_3999 {ECO:0000313|EMBL:EFF51597.1}; OS Bacteroides ovatus SD CMC 3f. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=702443 {ECO:0000313|EMBL:EFF51597.1}; RN [1] {ECO:0000313|EMBL:EFF51597.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SD CMC 3f {ECO:0000313|EMBL:EFF51597.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; ADMO01000099; EFF51597.1; -; Genomic_DNA. DR EnsemblBacteria; EFF51597; EFF51597; CUY_3999. DR PATRIC; 36636543; VBIBacOva158973_3390. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFF51597.1}; KW Transferase {ECO:0000313|EMBL:EFF51597.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 915 AA; 100038 MW; E55CC44564721482 CRC64; MKKTISQIVS ERILILDGAM GTMIQQYNLK EEDFRGERFA HIPGQLKGNN DLLCLTRPDV IQDIHRKYLE AGADIIETNT FSSTTVSMAD YHVEEYVREM NLAAVKLARD LADEYTAKNP DKPRFVAGSV GPTNKTCSMS PDVNNPAYRA LSYDELAASY QQQMEAMLEG GVDAILIETI FDTLNAKAAI FAAEQAMKMT GIEVPIMLSV TVSDIGGRTL SGQTLDAFLA SVQHANIFSV GLNCSFGARQ LKPFLEQLAS RAPYYISAYP NAGLPNSLGK YDQTPADMAH EVREYIEEGL INIIGGCCGT TDAYIAEYPA LVEGAKPHVP ASAPDCMWLS GLELLEVKPE INFVNVGERC NVAGSRKFLR LINEKKYDEA LSIARQQVED GALVIDVNMD DGLLEAKTEM TIFLNLIMSE PEIARVPIMI DSSKWEVIEA GLKCLQGKSI VNSISLKEGE EVFLEHARII RQYGAAAVVM AFDEKGQADT AARKIEVCQR AYRLLVDKIG FNPHDIIFDP NVLAVATGIE EHNNYAVDFI EATAWIKKNL PGAHISGGVS NLSFSFRGNN YIREAMHAVF LYHAIQQGMD MGIVNPGTSV LYTDIPADVL EKIEDVVLNR RLDAAERLIE LAESLKANMS ETAGQPAVKQ DAWREGTVQE RLKYALMKGI GDFLEQDLAE ALPLYDKAVD VIEGPLMDGM NHVGELFGAG KMFLPQVVKT ARTMKKAVAI LQPIIESEKV EGSASAGKVL LATVKGDVHD IGKNIVAVVM ACNGYDIVDL GVMVPAETIV QRAIEEKVDM IGLSGLITPS LEEMAHVAVE LEKAGLDIPL LIGGATTSKM HTALKIAPVY HAPVVHLKDA SQNASVASKL LNPQAKAELV NELETEYEAL REKSGLMKRE TVSLEEAQKN KLNLF // ID D4X6S4_9BURK Unreviewed; 1281 AA. AC D4X6S4; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFF77441.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFF77441.1}; GN Name=metH {ECO:0000313|EMBL:EFF77441.1}; GN ORFNames=HMPREF0004_1171 {ECO:0000313|EMBL:EFF77441.1}; OS Achromobacter piechaudii ATCC 43553. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Achromobacter. OX NCBI_TaxID=742159 {ECO:0000313|EMBL:EFF77441.1}; RN [1] {ECO:0000313|EMBL:EFF77441.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43553 {ECO:0000313|EMBL:EFF77441.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFF77441.1}. 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; ADMS01000026; EFF77441.1; -; Genomic_DNA. DR RefSeq; WP_006217147.1; NZ_GG770409.1. DR EnsemblBacteria; EFF77441; EFF77441; HMPREF0004_1171. DR PATRIC; 36775490; VBIAchPie159143_2044. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFF77441.1}; KW Transferase {ECO:0000313|EMBL:EFF77441.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 280 280 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 345 345 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 346 346 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 813 813 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1281 AA; 141635 MW; B1672F099777A58F CRC64; MFFRRFSLFS HIRAAVGQLY PDLPVSYPRL PYPPEAYTHG GDFARLLGKR ILILDGAMGT MIQRYKLGEA DFRGERFKDH GKDVKGNNEL LSLVRPDVIS EIHRQYLEAG ADVIETNTFG ATTIAQGDYD LPELAYELNL VSAKLAREAC EAYSTPDKPR FVAGALGPQP KTASISPDVN DPGARNVTFD ELRVAYIEQL NGLLDGGIDI VLIETIFDTL NAKAAIFATE EVFEARGIRL PVMISGTVTD ASGRILSGQT VEAFWNSVRH ARPVTIGLNC ALGAALMRPY VAELSKICDT YVCVYPNAGL PNPMAETGFD ETPADTSALL EEFARAGLVN MSGGCCGTTP DHIRAIADKV TSLTPRVVPD IPVKTRLSGL EPLNIDEDTL YVNVGERTNV TGSKMFARLI REEKYDEALA VARQQVENGA QIIDINMDEA MLDSVACMHR FLNLIASEPD IARVPVMIDS SKWEVIETGL KCVQGKAVVN SISMKEGLEP FRHHARLCRR YGAAVVVMAF DELGQADTLE RRKEICGRAY KILVEEEGFP PEDIIFDPNV FAVATGIDEH NHYAVDFIEG TRWIRENLPH ARISGGVSNV SFSFRGNEPM REAIHTVFLY YAVKEGMTMG IVNAGQLGVY ADLDPKLRDL VEDVVLDRPE PVGKTDPDDE RTPTERLVQF ADSVKGSGAK REEDLTWRKA EVEQRLSHAL VHGITTFIVE DTEEVRQKIA ARGGRPIEVI EGPLMDGMNV VGDLFGEGKM FLPQVVKSAR VMKQAVAHLI PFIEEEKRQI AAAGGDVRAK GKIVIATVKG DVHDIGKNIV SVVLQCNNFE VVNMGVMVPC AQILEKAKEE NADIVGLSGL ITPSLEEMAY VASEMQRDEY FRSRKLPLMI GGATTSRVHT AVKIAPNYEG PVIYVPDASR SVGVATNLMS DQSETYLAEL AQDYEEVRRR HANRKATPIL PLADARASRP VIDWDNYTPP RPKFIGRRTF KSYDLAEIAK YVDWGPFFQT WSLFGPFPAI LDDKVVGEQA RKVYADGLAM MKRIIEGRWL TANGVVGFYP ANSVNDEDIE IYKDETRSEV LFTYRNLRQQ GAKREGVSNK SLSDFIAPKS SGKLDYIGMF AVTAGIGIEK KEAEFEKALD DYSSIMLKSL ADRLAEGFAE CLHARVRQDL WGYAPDEALS NEDMIAEKYV GIRPAPGYPA CPEHVVKSDM FRVLDGADIG MMLTDSYAMY PASSVSGFYF SHPQSQYFNV GVIGEDQLLD YAKRSGRSIE DLKRTLAPNL G // ID D4XSH8_ACIHA Unreviewed; 1228 AA. AC D4XSH8; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFF81886.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFF81886.1}; GN Name=metH {ECO:0000313|EMBL:EFF81886.1}; GN ORFNames=HMP0015_2670 {ECO:0000313|EMBL:EFF81886.1}; OS Acinetobacter haemolyticus ATCC 19194. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=707232 {ECO:0000313|EMBL:EFF81886.1}; RN [1] {ECO:0000313|EMBL:EFF81886.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 19194 {ECO:0000313|EMBL:EFF81886.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFF81886.1}. 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; ADMT01000199; EFF81886.1; -; Genomic_DNA. DR RefSeq; WP_004640198.1; NZ_GG770435.1. DR EnsemblBacteria; EFF81886; EFF81886; HMP0015_2670. DR PATRIC; 36655911; VBIAciHae153512_0894. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFF81886.1}; KW Transferase {ECO:0000313|EMBL:EFF81886.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1228 AA; 135750 MW; D6EA1475ED03546D CRC64; MSTLATLKSL LAQRILIIDG AMGTMIQRHK LEEEDYRGER FADWASDLKG NNDLLVLTQP QIIQGIHEAY LDAGADIIET NSFNGTRVSM SDYHMEDLVP EINREAARLA RAACDKYSTP EKPRFVAGVL GPTSRTCSIS PNVNDPAFRN ITFDELKENY IEATHALIEG GADILLIETV FDTLNCKAAI FAVKEVFKQI GYELPLMISG TITDASGRTL TGQTAEAFWN SVRHGDLLSI GFNCALGADA MRPHVKTISD VADTFVSAHP NAGLPNAFGE YDETPEQTAA FIKEFAESGL INITGGCCGT TPDHIRAIYQ AVKDIPPRKI PETVHACRLS GLEPFNIYDD SLFVNVGERT NVTGSKKFLR LIREENFAEA LEVAQQQVEA GAQIIDINMD EGMLDSQGAM VHFLNLVASE PDISRVPIMI DSSKWEIIEA GLKCVQGKPV VNSISLKEGY DEFVEKARLC RQYGAAVIVM AFDEVGQADT AERKREICKR SYDILVNEVG YPAEDIIFDP NVFAVATGIE EHNNYAVDFI EATGWIKQNL PHAMISGGVS NVSFSFRGNE PVREAIHSVF LYHAIKQGMT MGIVNAGQMA IYDDINKELK DAVEDVVLNQ NQGETGQAAT EKLLEVAEKY RGQAGATKEA ENLEWRNESV EKRLEYALVK GITTYIDQDT EEARLKSKRP LDVIEGPLMD GMNVVGDLFG SGKMFLPQVV KSARVMKQAV AWLNPYIEAE KSEGQSKGKV LMATVKGDVH DIGKNIVGVV LGCNGYDIVD LGVMVPAEKI LQTAIDEKCD IIGLSGLITP SLDEMVFVAK EMQRKGFNIP LLIGGATTSK AHTAVKIDPQ YSNDAVIYVA DASRAVGVAT TLLSPEMRGN FIAEHRAEYA KIRERLANKQ PKAAKLSYAE SVENGFKIDN HYVPPKPNAL GTQVIKNYPL ETLVEYFDWT PFFISWSLAG KFPKILTDEV VGEAATDLYN QAQAMLKDII ENKRFDARAV FGLYPAQRTG ADTVSVFDES GQNRTHTFEH VRQQSDKVTG KPNLSLADYI KPSEQPEDYL GGFTVSIFGA EELANEYKAK GDDYSAILIQ SLADRFAEAF AEHLHERIRK EFWGYKADET LTNEELIKEK YVGIRPAPGY PACPEHSEKA VLFDWLGSEA KIGTKLTEHF AMMPPSSVSG FYYSHPQSEY FNVGKISQDQ LEDYAKRKGW TLDEAKRWLA PNLDDSIG // ID D4Z567_SPHJU Unreviewed; 348 AA. AC D4Z567; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 27-MAY-2015, entry version 30. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:BAI97749.1}; DE EC=2.1.1.- {ECO:0000313|EMBL:BAI97749.1}; GN OrderedLocusNames=SJA_C1-29150 {ECO:0000313|EMBL:BAI97749.1}; OS Sphingobium japonicum (strain NBRC 101211 / UT26S). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingobium. OX NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI97749.1, ECO:0000313|Proteomes:UP000007753}; RN [1] {ECO:0000313|EMBL:BAI97749.1, ECO:0000313|Proteomes:UP000007753} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753}; 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; BAI97749.1; -; Genomic_DNA. DR RefSeq; WP_013041049.1; NC_014006.1. DR RefSeq; YP_003546361.1; NC_014006.1. DR EnsemblBacteria; BAI97749; BAI97749; SJA_C1-29150. DR KEGG; sjp:SJA_C1-29150; -. DR PATRIC; 35437978; VBISphJap147895_2763. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR BioCyc; SJAP452662:GHEL-2966-MONOMER; -. DR Proteomes; UP000007753; Chromosome 1. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007753}; KW Methyltransferase {ECO:0000313|EMBL:BAI97749.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007753}; KW Transferase {ECO:0000313|EMBL:BAI97749.1}. SQ SEQUENCE 348 AA; 37371 MW; F607CA82CDFCC1BD CRC64; MTPEQQFRAV AAEKIMIFDG GYGTSIQKHG LTEADYRGSL DLAKDQKGNN DLLCLTRPDI VEGIHAAYLD AGADMIETNT FSSTKIAMAD YGCEHLVRDI NVAAARIARK ACEAASAKDG RPRFVAGSIG PTNKTLSISP DVNDPAYREV DYDTLKADYR EQCDALIEGG VDFLLVETCF DTLNAKAAGM AAREAEAAAG RPVPLMLSFT ITDMSGRNLS GHTINAFWYS LRHLKPLTIG VNCAFGADLL RPYLSELAKN ADTLILAYPN AGLPNELGQY DELPETTAKL IRQWVDEGLV NMVGGCCGTT PAHIGAVAKA LAGQKPRQVP ELPVVTRLAG LEPMHIAA // ID D4ZG22_SHEVD Unreviewed; 1256 AA. AC D4ZG22; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 27-MAY-2015, entry version 38. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:BAJ00621.1}; GN Name=metH {ECO:0000313|EMBL:BAJ00621.1}; GN OrderedLocusNames=SVI_0650 {ECO:0000313|EMBL:BAJ00621.1}; OS Shewanella violacea (strain JCM 10179 / CIP 106290 / LMG 19151 / OS DSS12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=637905 {ECO:0000313|EMBL:BAJ00621.1, ECO:0000313|Proteomes:UP000002350}; RN [1] {ECO:0000313|Proteomes:UP000002350} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 10179 / CIP 106290 / LMG 19151 / DSS12 RC {ECO:0000313|Proteomes:UP000002350}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP011177; BAJ00621.1; -; Genomic_DNA. DR RefSeq; WP_013049934.1; NC_014012.1. DR RefSeq; YP_003555399.1; NC_014012.1. DR EnsemblBacteria; BAJ00621; BAJ00621; SVI_0650. DR KEGG; svo:SVI_0650; -. DR PATRIC; 35457525; VBISheVio92117_0636. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; SVIO637905:GCRO-675-MONOMER; -. DR Proteomes; UP000002350; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002350}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAJ00621.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002350}; KW Transferase {ECO:0000313|EMBL:BAJ00621.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 261 261 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 325 325 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 782 782 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1256 AA; 139042 MW; E7653FFC6727FE69 CRC64; MANDTLSTPI ITKEKGQELT LKLTRQLEQE ILILDGAMGT MIQDLKLEEE DFRGEQFKDW HKDVKGNNDM LVLTQPAAIK GIHKQYLLAG ADIIETNTFN STRIAMADYD MQEFSAQINL EGARLARAAA DEVEQETGRS CYVAGVLGPT NRTCSISPDV NDPGYRNVSF DELVEAYVES INALIEGGAD IIMVETIFDT LNAKAALFAV ETVYDDLGAR LPIMISGTIT DASGRTLTGQ TTEAFYNSLR HVKPLSIGLN CALGPKELRP YVEELSKISE CFVSAHPNAG LPNEFGGYDE TPKQMADIIG EWAEEGFLNI IGGCCGTTPD HIRVIREAVI KHPARQLPDI PVACRLSGLE PLTIDENSLF LNVGERTNVT GSAKFLRLIK TGEFEEALSV ARDQVENGAQ IIDINMDEGM LDGVEIMHKF LNLIASEPDI SRVPIMIDSS KWEVIEAGLK CIQGKGIVNS ISLKEGEEKF IQQATLVKRY GAAAIIMAFD EQGQADTKAR KIEICTRAYR VLVDKVGFPP EDIIFDPNIF AIATGIEEHD NYAVDFIEAT AEIKRTLPHA MISGGVSNVS FSFRGNNPVR EAIHAVFLYH AIQAGMDMGI VNAGQLSIYD DIDPELKERV EAIVGNLPCT AVDKNGDATN NTELLLEVAE KFRGDGSQTA KKEDLEWRSW EVNKRLSHAL VKGITDYIVQ DTEEARAASS RPLDVIEGAL MDGMNVVGDL FGSGKMFLPQ VVKSARVMKK AVAYLNPYIE EEKTPGQSNG KILMVTVKGD VHDIGKNIVG VVLACNGYDV IDLGVMVPVE KIIDVAITEN VDIIGMSGLI TPSLDEMVHN VKSFHKAGLT IPTIIGGATC SKIHTAVKIA PHSPTGAIYI ADASRAVPMV SKLINNETRQ ATIDAAYEEY DVMREKRLSQ TKRKIITTIE AARDNRCKYD WDNYTPFIPN QLGRQVFDDY PLEDLVDRID WTPFFRSWEL HGHFPKILTD KVVGEEATKL FADGKAMLKR IIDEKWLTAK GVIGLFPANT VNHDDIELYS CDGTDESRDK PIITLHHLRM QIERVGNDNF CLADFVAPKD SGVADYMGGF AVTAGHGIDE HIARFEADHD DYSAIMLKCL ADRLAEAFAE RMHERVRKEF WGYASDEVLD NEALIREKYK GIRPAPGYPA CPDHTEKGLL WDLLKPDETI GLNITESYAM YPTAAVSGWY FAHPKSRYFG VTNIGKDQVE DYAQRKGMSI EETERWLSPV LDYDPE // ID D4ZXI4_ARTPN Unreviewed; 1182 AA. AC D4ZXI4; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 29-APR-2015, entry version 30. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:BAI92259.1}; GN Name=metH {ECO:0000313|EMBL:BAI92259.1}; GN ORFNames=NIES39_L00980 {ECO:0000313|EMBL:BAI92259.1}; OS Arthrospira platensis (strain NIES-39 / IAM M-135) (Spirulina OS platensis). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Arthrospira. OX NCBI_TaxID=696747 {ECO:0000313|EMBL:BAI92259.1, ECO:0000313|Proteomes:UP000006803}; RN [1] {ECO:0000313|EMBL:BAI92259.1, ECO:0000313|Proteomes:UP000006803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NIES-39 / IAM M-135 {ECO:0000313|Proteomes:UP000006803}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP011615; BAI92259.1; -; Genomic_DNA. DR RefSeq; WP_006617814.1; NC_016640.1. DR RefSeq; YP_005070797.1; NC_016640.1. DR EnsemblBacteria; BAI92259; BAI92259; NIES39_L00980. DR KEGG; arp:NIES39_L00980; -. DR PATRIC; 42722307; VBIArtPla153080_2373. DR KO; K00548; -. DR Proteomes; UP000006803; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006803}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAI92259.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006803}; KW Transferase {ECO:0000313|EMBL:BAI92259.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 228 228 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 737 737 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1182 AA; 131042 MW; 513F4B1AFE578AEA CRC64; MESLFLQRLH SPQRPVIIFD GAMGTNLQVQ NLTAEDFGGK EYEGCNEYLV HTKPEAVATV HRQFLQAGAD VIETDTFGGT SIVLAEYDLA DQAYQLNQTA ATLAKSVAAE FSTPEKPRFV AGSMGPGTKL PTLGHIDFDT LERAFCQQAE GLFDGGVDLF IVETCQDVLQ IKAALNGIEE VFKMKGERRP IMVSVTMEAF GTMLVGSEIN AALTILEPYQ IDILGLNCAT GPDLMKEHIA YLSEHSPFVV SCIPNAGLPE NVGGQAHYKL TPLELKMALM HFIEDLGVQV IGGCCGTRPD HIKALAEIAQ TLTPKPRHPQ ITPSAASIYS TISYEQENSF LIVGERLNAS GSKKCRDLLN AEDWDGLVAL AKTQVKEGAQ ILDVNVDYVG RNGVRDMHEL VSRLVTNVNL PLMLDSTEWE KMEAGLKVAG GKCLLNSTNY EDGEPRFYKV LELAKKYGAG VVVGTIDEEG MARTAAKKFA IAQRAYNDAI AFGIPATEIF FDPLALPIST GIEEDRENGK ATIEAIHQMR QQLPGCHILL GISNISFGLN PAARQVLNSV FLHETMAVGL DAAIVTANKI LPLAKIEPEH QEVCHHLIYD QRQFDGDVCT YDPLTKLTTL FEGKTTKRDR SGDANLPIEE RLKQHIIDGE RIGLEDALAE AIKKYPPLDI INIFLLDGMK VVGELFGSGQ MQLPFVLQSA QTMKAAVAYL EPFMEKSESG NNAKGTFVIA TVKGDVHDIG KNLVDIILSN NGYKVVNLGI KQPVDNIISA YREHNADCIA MSGLLVKSTA FMKDNLEVFN QEGITVPVIL GGAALTSKFV YEDCQNTYKG RVIYGKDAFS DLTFMDKLMP AKKAGKWEDF KGFLDEFVQD ETITTNGQSQ QSPPQTDQPE PDTPKVVDTR RSEAVAVDIE RPTPPFWGVK VLEPVDMPFD ELFWYLDLQA LTAGQWQFRK PQGQPREEYN QFLEAKVYPI LAEWKQRIIA ENLLQPRAVY GYFPCQSEGN TLLIYDPEKI KAGEISEPIT SFEFPRQRSG RRLCIADFFA PKDSGKIDVF PMHAVTVGQI ATDYAQKLFA ADDYTNYLYF HGMAVQTAEA MAEWLHARIR RELGFGGEDA DNIRDILKQR YRGSRYSFGY PACPNMQDQY KQLDLLKAEV IGLYMDESEQ LYPEQSTTAI ITYHPAAKYF SA // ID D5AKC8_STRGZ Unreviewed; 315 AA. AC D5AKC8; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:ADE32293.1}; GN OrderedLocusNames=SSGZ1_1837 {ECO:0000313|EMBL:ADE32293.1}; OS Streptococcus suis (strain GZ1). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=423211 {ECO:0000313|EMBL:ADE32293.1, ECO:0000313|Proteomes:UP000002359}; RN [1] {ECO:0000313|EMBL:ADE32293.1, ECO:0000313|Proteomes:UP000002359} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GZ1 {ECO:0000313|EMBL:ADE32293.1, RC ECO:0000313|Proteomes:UP000002359}; 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 ----------------------------------------------------------------------- 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; ADE32293.1; -; Genomic_DNA. DR RefSeq; WP_012775454.1; NC_017617.1. DR RefSeq; YP_006075235.1; NC_017617.1. DR EnsemblBacteria; ADE32293; ADE32293; SSGZ1_1837. DR KEGG; ssw:SSGZ1_1837; -. DR PATRIC; 36798268; VBIStrSui127079_1809. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR BioCyc; SSUI423211:GLLL-1893-MONOMER; -. DR Proteomes; UP000002359; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002359}; KW Methyltransferase {ECO:0000313|EMBL:ADE32293.1}; KW Transferase {ECO:0000313|EMBL:ADE32293.1}. SQ SEQUENCE 315 AA; 34868 MW; AAC726145F5E324F CRC64; MGRFKELLEQ KEYIILHGAL GTELEFRGHD VSGKLWSAKY LLENPQYIKD IHKDYIRAGA DLVTTSTYQA TFEGLAEVGL SQAEAEELIR LTVDLAKEAR DEVWAELSEA EKVQRTYPLI SGDVGPYAAY LANGAEYTGD YGNISLSELK DFHRRRIELL LEQEAELLAL ETIPNVLEAQ ALVELLAEDF PEAEAYISFT SQDGQSISDG TSIEKIAELV NSSEQILAVG LNCTAPSLYP AFLSQLREKT DKPFVTYPNS GEVYDGATQT WKEKADDSHS LLDNTLEWHE LGAKVVGGCC RTRPADIADL VAGLK // ID D5AS55_RHOCB Unreviewed; 345 AA. AC D5AS55; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 27-MAY-2015, entry version 31. DE SubName: Full=Methionine synthase, A subunit-1 {ECO:0000313|EMBL:ADE87077.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADE87077.1}; GN Name=metH1 {ECO:0000313|EMBL:ADE87077.1}; GN OrderedLocusNames=RCAP_rcc03353 {ECO:0000313|EMBL:ADE87077.1}; OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=272942 {ECO:0000313|EMBL:ADE87077.1, ECO:0000313|Proteomes:UP000002361}; 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] {ECO:0000313|EMBL:ADE87077.1, ECO:0000313|Proteomes:UP000002361} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003 RC {ECO:0000313|Proteomes:UP000002361}; 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; ADE87077.1; -; Genomic_DNA. DR RefSeq; WP_013069049.1; NC_014034.1. DR RefSeq; YP_003579484.1; NC_014034.1. DR EnsemblBacteria; ADE87077; ADE87077; RCAP_rcc03353. DR KEGG; rcp:RCAP_rcc03353; -. DR PATRIC; 35506924; VBIRhoCap134200_3396. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR BioCyc; RCAP272942:GJIY-3397-MONOMER; -. DR Proteomes; UP000002361; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002361}; KW Methyltransferase {ECO:0000313|EMBL:ADE87077.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002361}; KW Transferase {ECO:0000313|EMBL:ADE87077.1}. SQ SEQUENCE 345 AA; 36339 MW; BECDA07ADC5122F0 CRC64; MLTQTLPRSA AFAAIEALSR QRILILDGAM GTQIQQLGLS EDDFLGHGSG CACRHATDHP QKGNNDLLVL TQPQAIEEIH FRYAMAGADI VETNTFSATT IAQADYGLES AVFDLNAAGA RVARAAMDRA EATDGRRRFV AGAVGPTNRT ASLSPDVNDP GFRAVTFDDL RTAYGQQVRG LIAGGADILL IETIFDTLNA KAAIFACFEA FAERGERLPV MISGTITDAS GRTLSGQTPT AFWHSVAHAR PFTVGLNCAL GASAMRPHLA ELAGVAPCAI CAYPNAGLPN AFGQYDETPD RTAAQVAEFA REGLVNVVGG CCGTTPDHIR AIAEAVKPFP PRALP // ID D5AVC1_RHOCB Unreviewed; 338 AA. AC D5AVC1; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=Methionine synthase, A subunit-2 {ECO:0000313|EMBL:ADE85903.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADE85903.1}; GN Name=metH3 {ECO:0000313|EMBL:ADE85903.1}; GN OrderedLocusNames=RCAP_rcc02173 {ECO:0000313|EMBL:ADE85903.1}; OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=272942 {ECO:0000313|EMBL:ADE85903.1, ECO:0000313|Proteomes:UP000002361}; 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] {ECO:0000313|EMBL:ADE85903.1, ECO:0000313|Proteomes:UP000002361} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003 RC {ECO:0000313|Proteomes:UP000002361}; 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; ADE85903.1; -; Genomic_DNA. DR RefSeq; WP_013067882.1; NC_014034.1. DR RefSeq; YP_003578310.1; NC_014034.1. DR EnsemblBacteria; ADE85903; ADE85903; RCAP_rcc02173. DR KEGG; rcp:RCAP_rcc02173; -. DR PATRIC; 35504528; VBIRhoCap134200_2215. DR HOGENOM; HOG000265278; -. DR KO; K00548; -. DR OMA; GTNLFAM; -. DR BioCyc; RCAP272942:GJIY-2201-MONOMER; -. DR Proteomes; UP000002361; Chromosome. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002361}; KW Methyltransferase {ECO:0000313|EMBL:ADE85903.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002361}; KW Transferase {ECO:0000313|EMBL:ADE85903.1}. SQ SEQUENCE 338 AA; 35581 MW; E3A6A4FA4F2C5713 CRC64; MTNTLSRLLK SRDWLLADGA TGTNLFNMGL SSGEPPELWN VEHPDRIAKL YGFAVEAGSD LFLTNSFGGN SARLKLHNAQ GRVRELNRIA AEIGRNVADK AGRPVAVCGS VGPTGEIFAP MGTLTHELAV EIFHEQAEGL KEGGADVLWV ETISAPEEYK AAAEAARLAG MDWCGTMSFD TAGRTMMGVT SAQLAALVEK LPNPPLAFGA NCGVGAADLL RTLMGFVATG TERPLIAKGN AGIPKYHDGH IHYDGTPELM GDYACLARDA GATIIGGCCG TMPVHLQAMH EALSTRPRGP RPSLEEIAAK LGAFSSASDG TGDDDGGPAR ERRGRRRG // ID D5BKM4_ZUNPS Unreviewed; 339 AA. AC D5BKM4; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 27-MAY-2015, entry version 33. DE SubName: Full=Methionine synthase-like protein {ECO:0000313|EMBL:ADF53936.1}; GN OrderedLocusNames=ZPR_3626 {ECO:0000313|EMBL:ADF53936.1}; OS Zunongwangia profunda (strain DSM 18752 / CCTCC AB 206139 / SM-A87). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Zunongwangia. OX NCBI_TaxID=655815 {ECO:0000313|EMBL:ADF53936.1, ECO:0000313|Proteomes:UP000001654}; RN [1] {ECO:0000313|EMBL:ADF53936.1, ECO:0000313|Proteomes:UP000001654} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18752 / CCTCC AB 206139 / SM-A87 RC {ECO:0000313|Proteomes:UP000001654}; 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; ADF53936.1; -; Genomic_DNA. DR RefSeq; WP_013073020.1; NC_014041.1. DR RefSeq; YP_003586132.1; NC_014041.1. DR EnsemblBacteria; ADF53936; ADF53936; ZPR_3626. DR KEGG; zpr:ZPR_3626; -. DR PATRIC; 37236572; VBIZunPro130839_3490. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR BioCyc; ZPRO655815:GI6J-3621-MONOMER; -. DR Proteomes; UP000001654; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001654}; KW Reference proteome {ECO:0000313|Proteomes:UP000001654}. SQ SEQUENCE 339 AA; 36968 MW; 616CBA219104AAA4 CRC64; MSKLEELLAE KILILDGAMG TMLQEYKFTE EDFRGDRFKD WPVSLQGNND LLSITQPEAI ATIHKKYFQA GADIVETNTF SGTTIAMADY QMEELVDELN YESAKIAKQV ATELTEANPD QPKFVAGAMG PTNKTASMSP DVNDPGYRAI SFDELRVAYK QQARALIKGG VDILLVETVF DTLNAKAALF AIDELKEELD LDIPVMVSGT ITDASGRTLS GQTAEAFLIS VSHIPLLSIG FNCALGAKQL TPHLEVLSYK TQYGVSAYPN AGLPNAFGEY DESPDEMAIQ TKEYLDKSLV NILGGCCGTT PDHIKAIANI AKDYKPRPIK SLQHKKASA // ID D5BMT9_PUNMI Unreviewed; 373 AA. AC D5BMT9; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADE40132.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADE40132.1}; GN OrderedLocusNames=SAR116_1889 {ECO:0000313|EMBL:ADE40132.1}; OS Puniceispirillum marinum (strain IMCC1322). OC Bacteria; Proteobacteria; Alphaproteobacteria; SAR116 cluster; OC Candidatus Puniceispirillum. OX NCBI_TaxID=488538 {ECO:0000313|EMBL:ADE40132.1, ECO:0000313|Proteomes:UP000007460}; RN [1] {ECO:0000313|EMBL:ADE40132.1, ECO:0000313|Proteomes:UP000007460} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IMCC1322 {ECO:0000313|EMBL:ADE40132.1, RC ECO:0000313|Proteomes:UP000007460}; 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 ----------------------------------------------------------------------- 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; ADE40132.1; -; Genomic_DNA. DR RefSeq; WP_013046759.1; NC_014010.1. DR RefSeq; YP_003552216.1; NC_014010.1. DR EnsemblBacteria; ADE40132; ADE40132; SAR116_1889. DR KEGG; apb:SAR116_1889; -. DR PATRIC; 35450761; VBIAlpPro78664_1913. DR HOGENOM; HOG000265278; -. DR KO; K00548; -. DR OMA; GTNLFAM; -. DR BioCyc; PMAR488538:GI1I-1913-MONOMER; -. DR Proteomes; UP000007460; Chromosome. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007460}; KW Methyltransferase {ECO:0000313|EMBL:ADE40132.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007460}; KW Transferase {ECO:0000313|EMBL:ADE40132.1}. SQ SEQUENCE 373 AA; 39058 MW; AC436871C72A80B4 CRC64; MSVVQQKPVS ADALHGVERL LVKDKPRQNM SSKFHDMLAE RSYLIADGAT GTNLFGRGLE TGYPPELWNV ERPDDILWLH DSFLQAGSNL ILTNSFGGTS FRLKLHDAQD RVEELNHAAA VNAVTAVTNH RDKTGIDAIV AGSIGPTGEL FEPLGALTPD SACEAFTKQA SALSEGGVDM LWVETMSSTE EVDAAVTAAK TTGLPVAVTM TFDTASRTMM GITPQQFAEQ AVALGVDVLG ANCGIGPAEL MHSMTGMTAT ALAANIPMVA KGNCGIPAYV EGAIHYHGTP ELMASYALFA RDAGISIIGG CCGTTPAHVA AMSAALASRP AGVLDEDDMQ AVLGTPWADV QTSSDATDDG AGGRRGRRGR RRS // ID D5BPU7_PUNMI Unreviewed; 317 AA. AC D5BPU7; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADE40599.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ADE40599.1}; GN OrderedLocusNames=SAR116_2356 {ECO:0000313|EMBL:ADE40599.1}; OS Puniceispirillum marinum (strain IMCC1322). OC Bacteria; Proteobacteria; Alphaproteobacteria; SAR116 cluster; OC Candidatus Puniceispirillum. OX NCBI_TaxID=488538 {ECO:0000313|EMBL:ADE40599.1, ECO:0000313|Proteomes:UP000007460}; RN [1] {ECO:0000313|EMBL:ADE40599.1, ECO:0000313|Proteomes:UP000007460} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IMCC1322 {ECO:0000313|EMBL:ADE40599.1, RC ECO:0000313|Proteomes:UP000007460}; 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 ----------------------------------------------------------------------- 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; ADE40599.1; -; Genomic_DNA. DR RefSeq; WP_013047226.1; NC_014010.1. DR RefSeq; YP_003552683.1; NC_014010.1. DR EnsemblBacteria; ADE40599; ADE40599; SAR116_2356. DR KEGG; apb:SAR116_2356; -. DR PATRIC; 35451719; VBIAlpPro78664_2386. DR HOGENOM; HOG000265278; -. DR OMA; PYVDVWL; -. DR BioCyc; PMAR488538:GI1I-2386-MONOMER; -. DR Proteomes; UP000007460; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007460}; KW Methyltransferase {ECO:0000313|EMBL:ADE40599.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007460}; KW Transferase {ECO:0000313|EMBL:ADE40599.1}. SQ SEQUENCE 317 AA; 34175 MW; EEF92C89D4445E71 CRC64; MIILDGGLGR QLAAVGAPFR QPEWSALALM EAPQYVRDVH DSFIAAGADV ITTNSYAIVP FHIGQDRFDE LAPQLLTLSG TLAQAAAEAA DRQVKVAASI PPMFGSYEPD KFDPQTGQQM MQLFQRHLAP SADIFLAETL GSVIEAKIFL ESFVDCAADL WLSVTLEDVK PVPGAPRLRS GEPLSALLDV IASKRLDGLL FNCSQPEVMH DAVTCVSEFR ARQPSRPAGM GLQIGVYANA FPLMNDDYEH ANSTLHQIRH DITPQNYAKY AVQWAAAGAD IIGGCCGISP EHIEILAAAL KNNQAAQLSS STFARQA // ID D5BWG1_NITHN Unreviewed; 1231 AA. AC D5BWG1; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 27-MAY-2015, entry version 37. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADE15618.1}; GN OrderedLocusNames=Nhal_2538 {ECO:0000313|EMBL:ADE15618.1}; OS Nitrosococcus halophilus (strain Nc4). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Nitrosococcus. OX NCBI_TaxID=472759 {ECO:0000313|EMBL:ADE15618.1, ECO:0000313|Proteomes:UP000001844}; RN [1] {ECO:0000313|Proteomes:UP000001844} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nc4 {ECO:0000313|Proteomes:UP000001844}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001798; ADE15618.1; -; Genomic_DNA. DR RefSeq; WP_013033478.1; NC_013960.1. DR RefSeq; YP_003528005.1; NC_013960.1. DR EnsemblBacteria; ADE15618; ADE15618; Nhal_2538. DR KEGG; nhl:Nhal_2538; -. DR PATRIC; 35395096; VBINitHal115488_2670. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; NHAL472759:GHH2-2574-MONOMER; -. DR Proteomes; UP000001844; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001844}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001844}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1231 AA; 137617 MW; 1CBACADD1EA39FD6 CRC64; MSLKSPRIAA LKDQLAKRIL MLDGALGTMI QSYELVEEQY RGERFADWPC DLKGNNDLLV LTQPQILREI YRDYLEAGAD IIETNTFNAT RIAMADYQME ALVVEINQAA AQLAREMADE MTAKTPDRPR FVAGVLGPTN RTASISPDVN DPGFRNTSFD KLVEAYRESI HGLVQGGVDI LLIETIFDTL NAKAAVYAVE QYFEDQEVRL PIMISGTITD ASGRTLSGQT TEAFWNSLRH GEPLAFGLNC ALGPKQLRQY VEELSGLADT YVSAHPNAGL PNEFGGYDET PEEMAKEIGE WAREGFLNIV GGCCGTTPEH IRVIREAVEK YPPRKIPQRP EACRLSGLEP SNIDEHSLFV NVGERTNITG SARFRRLIKE EDYETALEVA RQQVENGAQI IDVNMDEGLL DSQKAMVRFL NLIAAEPDIS RVPIMIDSSK WEVIEAGLKC IQGKGVVNSI SLKEGEEPFI QQAKQVRRYG AAAVIMAFDE QGQAETKERK VEICARAYKL LTEKVGFPAE DIIFDPNIFA VATGIEEHDN YAVTFIEATR EIKRTLAPAL VSGGVSNVSF SFRGNDTVRE AIHAVFLYHA IQAGMDMGIV NAGQLAVYDE IPSDLRERVE DVILNRRSDA TERLLDIAEK YRGAGGAAER KEDLAWRELP VNERLAHALI KGVTDFVEED TEEARLAAKR PLDVIEGPLM DGMNVVGDLF GSGKMFLPQV VKSARVMKKA VAYLLPYMEK EKESYKSHGK LVLATVKGDV HDIGKNIVAV VLQCNGFEVI DLGVMVPSEK ILQTAKEQSC DFVGLSGLIT PSLDEMVHVA KEMERQSFNV PLLIGGATTS KMHTAVRIEP QYAQPVVYVP DASRVVGIAQ RLLNPTIKAE YAAEIAEEYG QMRQRRAEQQ TERSHTPLAQ ARANKLETDW AAYTPPQPTF LGLKTFEDYP LEELAARIDW TPFFHAWELA GKYPKILEDE VVGEEARKLL ADAKAMLKRV MEEKWLQARA VIGFFPANTV NDDDIELYTD ESRGEVLTTL HHIRQQMARR GGQPNYCLAD FIAPKETGVA DYLGAFAVTA GLGIDERLQE FMEHHDDYNN ILLKAVADRL AEAFAERMHE RVRKEFWRYA PDEAFTNEEL INENYRGVRP APGYPACPDH TEKATLWQLI QPDENAGIIL TESYAMVPTA AVSGWYFSHP EARYFGTGKI QKDQVEDYAR RKGMSVEQVE RWLRSILGYE P // ID D5BYS5_NITHN Unreviewed; 319 AA. AC D5BYS5; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 29-APR-2015, entry version 23. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADE16063.1}; GN OrderedLocusNames=Nhal_3006 {ECO:0000313|EMBL:ADE16063.1}; OS Nitrosococcus halophilus (strain Nc4). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Nitrosococcus. OX NCBI_TaxID=472759 {ECO:0000313|EMBL:ADE16063.1, ECO:0000313|Proteomes:UP000001844}; RN [1] {ECO:0000313|Proteomes:UP000001844} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nc4 {ECO:0000313|Proteomes:UP000001844}; 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 ----------------------------------------------------------------------- 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; ADE16063.1; -; Genomic_DNA. DR RefSeq; WP_013033913.1; NC_013960.1. DR RefSeq; YP_003528450.1; NC_013960.1. DR EnsemblBacteria; ADE16063; ADE16063; Nhal_3006. DR KEGG; nhl:Nhal_3006; -. DR PATRIC; 35396074; VBINitHal115488_3157. DR HOGENOM; HOG000179103; -. DR OMA; CCGTDHR; -. DR BioCyc; NHAL472759:GHH2-3044-MONOMER; -. DR Proteomes; UP000001844; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001844}; KW Methyltransferase {ECO:0000313|EMBL:ADE16063.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001844}; KW Transferase {ECO:0000313|EMBL:ADE16063.1}. SQ SEQUENCE 319 AA; 35560 MW; 19796C5F2A51B8B2 CRC64; MSQYRNRLPQ LREDLFITDG GLETTLVFHE GIDLPYFAAF HLLKDDAGFD TLHHYFARYV KIARRWGFGI VLEAPTWRAN PDWGAKLGYD AVTLADANRK AIGLLLEIRA AYETLETPVV ISGNLGPRGD GYLAASRMSI EVAREYHRPQ METFAQTDAD MVSALTLNYV EEAIGIVQAA RDAAMPVAIS FTVETDGRLP SGDQLAEAIQ RTDDETNAYA AYYMINCAHP THFEQVLQEG GHWRERIRGL RANASKRSHA ELDESTELDI GNPQELGEQY CALRTLLPRL TVLGGCCGTD HRHVEAICDA CHAYVETSL // ID D5CTJ6_SIDLE Unreviewed; 1239 AA. AC D5CTJ6; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 29-APR-2015, entry version 33. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADE10302.1}; GN OrderedLocusNames=Slit_0060 {ECO:0000313|EMBL:ADE10302.1}; OS Sideroxydans lithotrophicus (strain ES-1). OC Bacteria; Proteobacteria; Betaproteobacteria; Gallionellales; OC Gallionellaceae; Sideroxydans. OX NCBI_TaxID=580332 {ECO:0000313|EMBL:ADE10302.1, ECO:0000313|Proteomes:UP000001625}; RN [1] {ECO:0000313|EMBL:ADE10302.1, ECO:0000313|Proteomes:UP000001625} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ES-1 {ECO:0000313|EMBL:ADE10302.1, RC ECO:0000313|Proteomes:UP000001625}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001965; ADE10302.1; -; Genomic_DNA. DR RefSeq; WP_013028201.1; NC_013959.1. DR RefSeq; YP_003522689.1; NC_013959.1. DR EnsemblBacteria; ADE10302; ADE10302; Slit_0060. DR KEGG; slt:Slit_0060; -. DR PATRIC; 35398200; VBISidLit69165_0060. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; SLIT580332:GH9F-60-MONOMER; -. DR Proteomes; UP000001625; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001625}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001625}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 256 256 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 770 770 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1239 AA; 136558 MW; 50A6D861BC0A1210 CRC64; MSQATHPIEQ LLQRRILILD GAMGTMIQRY KLTEAHYRGT ELFGNYQGER RTFADHPVDL KGCNDLLLLT QPHIIGGIHR EYLEAGADIL ETCTFNSTSV SMEDYELERL AYELNVAGAK LARGLCDEFS TADKPRFVAG VLGPTGKTAS ISPDVNDPGA RNITFDQLVE SYAEAVRGLL DGGADMLMVE TIFDTLNAKA ALFAIERHFE QHGVRVPILI SGTITDASGR TLSGQTTEAF YNSLAHARPL SIGLNCALGA ELMRPYVEEL ARVAGCYVSA HPNAGLPNPL SETGYDEVPE TTARLVKEFA TSGFLNIAGG CCGTSPAHIK AIAEALRDVP PRKLPDIEHK CRLSGLEPFN IGDDSLFVNV GERANVTGSA KFKRLILEGN YDEALEVAKQ QVETGAQVID INMDEAMLDG EATMVKFLNL IASEPDISKV PLMIDSSKWS IIEAGLKCVQ GKSIVNSISL KEGEENFIRH ATLVRRYGAA AVVMAFDEQG QADTYKRKTE ICKRSYDILV DKVGFPPEDI IFDPNIFAVA TGIEEHNNYA VDFIEATAWI RKNLPFAKIS GGVSNVSFSF RGNDPVREAI HTVFLYHAIK AGMNMGIVNA GQLGVYEEIP RELRDAVENV VLNRHPDAGE KLVKLADSVK GGSKEQVEDL EWRKGTVQER LTHALVRGIT TFIVEDTEEA RLQARFPVEV IEGPLMTGMN VVGDLFGAGK MFLPQVVKSA RVMKQAVAHL IPFIEAEKLR SGDTSTKGKI VMATVKGDVH DIGKNIVTVV LQCNNFEVVN MGVMVPCQQI LDTAREHNAD VIGLSGLITP SLEEMAHVAK EMERQGFRIP LLIGGATTSR VHTAVKIEPN YPSGTTVYVN DASRAVGVCS NLLSSTLRDD YVAEIKADYA AAREQHEGKK GKASYVTLAE ARAHGVKTDW KKYTPPKPKL LGVQKLENYP LDILVDFIDW TPFFQAWELA GRYPKILQDE VVGSEARKLF ADAQAMLKKI VKEKWLTANA VFGLFPANTV NSDDIEIYTD DKRNKIAMTW HNLRQQTKKP DDIPNYCLAD YIAPKESKVK DYIGAFAVTT GIGIDARVAE FEKQNDDYNA IMLKSLADRL AEAFAEHLHL RVRREFWGYA ADEQLGNEDI IAEKYRGIRP APGYPACPEH TEKGPLFELL QAPQNAGITI TESFAMLPTA AVSGFYFSHP QAQYFATGKV DKDQVADYAK RKSWTVEEAE KWLAPVLSY // ID D5DB60_BACMD Unreviewed; 311 AA. AC D5DB60; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADF37711.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ADF37711.1}; GN Name=ybgG {ECO:0000313|EMBL:ADF37711.1}; GN OrderedLocusNames=BMD_0849 {ECO:0000313|EMBL:ADF37711.1}; OS Bacillus megaterium (strain DSM 319). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=592022 {ECO:0000313|EMBL:ADF37711.1, ECO:0000313|Proteomes:UP000002365}; RN [1] {ECO:0000313|Proteomes:UP000002365} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 319 {ECO:0000313|Proteomes:UP000002365}; 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; ADF37711.1; -; Genomic_DNA. DR RefSeq; WP_013081876.1; NC_014103.1. DR RefSeq; YP_003596061.1; NC_014103.1. DR EnsemblBacteria; ADF37711; ADF37711; BMD_0849. DR GeneID; 9116240; -. DR KEGG; bmd:BMD_0849; -. DR PATRIC; 37251681; VBIBacMeg104484_0767. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR BioCyc; BMEG592022:GIVX-849-MONOMER; -. DR Proteomes; UP000002365; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002365}; KW Methyltransferase {ECO:0000313|EMBL:ADF37711.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002365}; KW Transferase {ECO:0000313|EMBL:ADF37711.1}. SQ SEQUENCE 311 AA; 34457 MW; F18E332FE54D8BB8 CRC64; MNPIQQILHT FPVIVLDGAM ATELERYSCD LNDSLWSAKV LMEQPELIKR VHQDYFAAGA DCAITASYQS TFEGFAKRGL SEAEARELIQ ASVKIAAESR DEFWHQEENR LNRPKPIVAA SVGPYGAFLA NGSEYTGQYD VTEEELMEFH RPRMKALIEA GADVLACETI PNLMEARAIA KLLEEFEGAY AWITFSAKDD LHISSGTLIS ECARYLDSYE QVAALGVNCT PPQYISSLIK EIKSQTDKPV IVYPNSGEHY DAESKTWNGT SAGETYGCSA HSWYEAGAQL IGGCCRTTPD DIKGITKWAR K // ID D5DBM3_BACMD Unreviewed; 1147 AA. AC D5DBM3; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 27-MAY-2015, entry version 34. DE SubName: Full=Methionine synthase, vitamin-B12 dependent {ECO:0000313|EMBL:ADF38134.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADF38134.1}; GN Name=metH {ECO:0000313|EMBL:ADF38134.1}; GN OrderedLocusNames=BMD_1273 {ECO:0000313|EMBL:ADF38134.1}; OS Bacillus megaterium (strain DSM 319). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=592022 {ECO:0000313|EMBL:ADF38134.1, ECO:0000313|Proteomes:UP000002365}; RN [1] {ECO:0000313|Proteomes:UP000002365} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 319 {ECO:0000313|Proteomes:UP000002365}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001982; ADF38134.1; -; Genomic_DNA. DR RefSeq; WP_013082255.1; NC_014103.1. DR RefSeq; YP_003596484.1; NC_014103.1. DR EnsemblBacteria; ADF38134; ADF38134; BMD_1273. DR GeneID; 9116664; -. DR KEGG; bmd:BMD_1273; -. DR PATRIC; 37252547; VBIBacMeg104484_1200. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; BMEG592022:GIVX-1273-MONOMER; -. DR Proteomes; UP000002365; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002365}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADF38134.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002365}; KW Transferase {ECO:0000313|EMBL:ADF38134.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 226 226 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 724 724 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1147 AA; 126620 MW; 634FC8C3E39C0352 CRC64; MSSLIEQQLK KRILVIDGAM GTMIQDADLT AEDFGGEEYE GCNEYLTRTA PHVIQRIHEE YFAAGADIIE TNTFGSTSTV LDEYDLGHLA YELNIEAVKL ACAARDKYST PEWPRFVAGA IGPTTKTLSV TGGITFPELV ESYEEQARGL LDGGVDLLLV ETCQDMLNVK AAFLGITAAF EKLKIEVPIM ISGTIEPMGT TLAGQDIESF YLSLEHMKPL SVGLNCATGP EFMTDHIRSL SDLATSAVSC YPNAGLPDEE GNYHESPELL AQKIKGFADK GWLNFVGGCC GTTPAHIKAL AEAVKEVAPR SLDRSEHNHA VTGIEPLVYD DSMRPLFVGE RTNVIGSRKF KRLIAEGKIE EASEIARAQV KNGAHVIDIC LADPDREEME DMEEFIQEVV KKVKVPLVID STDEKVIEKA LTYSQGKVII NSINLEDGEE RFDAILPLVK KFGAALVVGT IDETGMAVTA ERKVEIAKRS HDLLVEKHGF NPKDIIFDPL VFPVGTGDEQ YIGSAEETVK GIKMIKEALP DCLTILGVSN VSFGLPPVGR EVLNAVYLYH CTQAGLDYAI VNTEKLERYA SIPEAEIELA NALLFNTTDE TLSTFTDFYR DKKKEAKVEI STLTLEERLA MYIVEGTKEG LLPDLEQALA QYDDPLDIIN GPLMKGMAEV GRLFNDNQLI VAEVLQSAEV MKASVAFLEP HMEATENDSG KGKVILATVK GDVHDIGKNL VDIILSNNGF KVIDLGIKVT PQQLIEAVKE EKPDIIGLSG LLVKSAQQMV LTAQDLTQSS IDVPIMVGGA ALSRKFTDFK IAPEYEGAVL YAKDAMDGLA LANKLQNKEE VIQLLADLKT RQEKKVTVRE RQPQTAQAAT AVLERSAIST DAPVFVPADL KRHVVKHYDL AQVLPYINWQ MLLGHHLGLK GKVNKLLAEK DERAVQLKET VDDLLELALK ENLIKPAVIY QFFPAQADGN DLIIYDPADE KTEIERFTFP RQTKGQFLCL SDFAKPKEKE MDYVCFFSVT AGTGIRERAA KFKENGEFLK SHVFQALALE LAEGLAERVH QQIRDRWGFP DSPDFTMAER FSAKYQGQRF SFGYPACPDL EDQAKLFKLL KPEDIGIQLT DGFMMEPEAS VTALVFAHPE AKYFNVL // ID D5DBM4_BACMD Unreviewed; 612 AA. AC D5DBM4; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 27-MAY-2015, entry version 30. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN Name=yitJ {ECO:0000313|EMBL:ADF38135.1}; GN OrderedLocusNames=BMD_1274 {ECO:0000313|EMBL:ADF38135.1}; OS Bacillus megaterium (strain DSM 319). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=592022 {ECO:0000313|EMBL:ADF38135.1, ECO:0000313|Proteomes:UP000002365}; RN [1] {ECO:0000313|Proteomes:UP000002365} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 319 {ECO:0000313|Proteomes:UP000002365}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ADF38135.1; -; Genomic_DNA. DR RefSeq; WP_013082256.1; NC_014103.1. DR RefSeq; YP_003596485.1; NC_014103.1. DR ProteinModelPortal; D5DBM4; -. DR EnsemblBacteria; ADF38135; ADF38135; BMD_1274. DR GeneID; 9116665; -. DR KEGG; bmd:BMD_1274; -. DR PATRIC; 37252549; VBIBacMeg104484_1201. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR BioCyc; BMEG592022:GIVX-1274-MONOMER; -. DR Proteomes; UP000002365; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002365}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ADF38135.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862, KW ECO:0000313|EMBL:ADF38135.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002365}; KW Transferase {ECO:0000313|EMBL:ADF38135.1}. SQ SEQUENCE 612 AA; 68083 MW; 983D91F2ECBE047A CRC64; MGLLEDLKSK ILIGDGATGT LLYSHGIDSC FEELNITKPE EVSRIHRAYV EAGANVIQTN TYAANYQKLA RYGLEDSVKD INVAGVKLAK QAAKDQAYVV GTLGGIRSFQ KNAISLEEVK RSIREQMFWL LNEGVDGLLF ETYYDFEELK TVLTLARKET DKPIITHVSL HDIGVLQDGR PLADALKELE ALGADVVGLN CRLGPYHMIQ SLEEVPLPDR AFLSAYPNAS LPAYVEGKLE YETNEDYFVE SARLFREQGV RLIGGCCGTT PAHVRAMSSA LKDLPPITSK VVKMRPAVTV QEREQQDKPH MHEIVKKRRS VIVELDPPKQ LGPTKFLEGA KALDKVGVDA ITLADNSLAS PRISNLAMAT LMQQETKARP LIHITCRDRN LIGLQSHLMG LHTLGMNQVL AITGDPSKVG DFPGATSVYD LSSFDLISLI AQFNEGLSYS GKPLGQKTNF SIAAAFNPNV RHLDRAVQRL EKKIDCGAHY FITQPLYSTK QIEEVYEATK HLTTPVYIGI MPLTSARNAR FIHHEVPGIK LSEDILERMD ATGNDRIRGE VEGLAIAKNL IDTAYELFDG IYLITPFMRY EMTEILTRYI HDKQLVTSER KI // ID D5E063_BACMQ Unreviewed; 1147 AA. AC D5E063; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 01-APR-2015, entry version 34. DE SubName: Full=Methionine synthase, vitamin-B12 dependent {ECO:0000313|EMBL:ADE68326.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADE68326.1}; GN Name=metH {ECO:0000313|EMBL:ADE68326.1}; GN OrderedLocusNames=BMQ_1293 {ECO:0000313|EMBL:ADE68326.1}; OS Bacillus megaterium (strain ATCC 12872 / QMB1551). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=545693 {ECO:0000313|EMBL:ADE68326.1, ECO:0000313|Proteomes:UP000000935}; RN [1] {ECO:0000313|Proteomes:UP000000935} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12872 / QMB1551 {ECO:0000313|Proteomes:UP000000935}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001983; ADE68326.1; -; Genomic_DNA. DR RefSeq; WP_013056001.1; NC_014019.1. DR RefSeq; YP_003561760.1; NC_014019.1. DR ProteinModelPortal; D5E063; -. DR EnsemblBacteria; ADE68326; ADE68326; BMQ_1293. DR KEGG; bmq:BMQ_1293; -. DR PATRIC; 35479233; VBIBacMeg35839_1291. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR BioCyc; BMEG545693:GHSY-1293-MONOMER; -. DR Proteomes; UP000000935; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000935}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADE68326.1}; KW Transferase {ECO:0000313|EMBL:ADE68326.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 226 226 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 724 724 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1147 AA; 126576 MW; 675AA82252CC93D6 CRC64; MSSLIEQQLK KRILVIDGAM GTMIQDADLT AEDFGGEEYE GCNEYLTRTA PHVIQRIHEE YFAAGADIIE TNTFGSTSTV LDEYDLGHLA YELNIEAVKL ACAARDKYST PEWPRFVAGA IGPTTKTLSV TGGITFPELV ESYEEQVRGL LDGGVDLLLV ETCQDMLNVK AAFLGITAAF EKLKTEVPIM ISGTIEPMGT TLAGQDIESF YLSLEHMKPL SVGLNCATGP EFMTDHIRSL SDLATSAVSC YPNAGLPDEE GNYHESPELL AQKIKGFADK GWLNFVGGCC GTTPAHIKAL AEAVKEVAPR SLDRSEHNHA VTGIEPLVYD DSMRPLFVGE RTNVIGSRKF KRLIAEGKIE EASEIARAQV KNGAHVIDIC LADPDREEME DMEEFIQEVV KKVKVPLVID STDEKVIEKA LTYSQGKVII NSINLEDGEE RFDAILPLVK KFGAALVVGT IDETGMAVTA ERKVEIAKRS HDLLVEKHGF NPKDIIFDPL VFPVGTGDEQ YIGSAEETVK GIKMIKEALP DCLTILGVSN VSFGLPPVGR EVLNAVYLYH CTQAGLDYAI VNTEKLERYA SIPEAEIELA NALLFNTTDE TLSTFTDFYR DKKKEAKVEI STLTLEERLA MYIVEGTKEG LLPDLEQALA QYDDPLDIIN GPLMKGMAEV GRLFNDNQLI VAEVLQSAEV MKASVAFLEP HMEATENDSG KGKVILATVK GDVHDIGKNL VDIILSNNGF KVIDLGIKVT PQQLIEAVKE EKPDIIGLSG LLVKSAQQMV LTAQDLTQSS IDVPIMVGGA ALSRKFTDFK IAPEYEGAVL YAKDAMDGLA LANKLQNKEE VIQLLADLKT RQEKKVAVRE RQPQTAQAAT AVLERSAIST DAPVFVPADL KRHVVKHYDL AQVLPYINWQ MLLGHHLGLK GKVNKLLAEK DERAVQLKET VDDLLELALK ENLIKPAVIY QFFPAQADGN DLIIYDPADE KTEIERFTFP RQAKGQFLCL SDFAKPKEKE MDYVCFFSVT AGTGIRERAA KFKENGEFLK SHVFQALALE LAEGLAERVH QQIRDRWGFP DSPDFTMAER FSAKYQGQRF SFGYPACPDL EDQAKLFKLL KPEDIGIQLT DGFMMEPEAS VTALVFAHPE AKYFNVL // ID D5E064_BACMQ Unreviewed; 612 AA. AC D5E064; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 29-APR-2015, entry version 34. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN Name=yitJ {ECO:0000313|EMBL:ADE68327.1}; GN OrderedLocusNames=BMQ_1294 {ECO:0000313|EMBL:ADE68327.1}; OS Bacillus megaterium (strain ATCC 12872 / QMB1551). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=545693 {ECO:0000313|EMBL:ADE68327.1, ECO:0000313|Proteomes:UP000000935}; RN [1] {ECO:0000313|Proteomes:UP000000935} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12872 / QMB1551 {ECO:0000313|Proteomes:UP000000935}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ADE68327.1; -; Genomic_DNA. DR RefSeq; WP_013056002.1; NC_014019.1. DR RefSeq; YP_003561761.1; NC_014019.1. DR ProteinModelPortal; D5E064; -. DR EnsemblBacteria; ADE68327; ADE68327; BMQ_1294. DR KEGG; bmq:BMQ_1294; -. DR PATRIC; 35479235; VBIBacMeg35839_1292. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR BioCyc; BMEG545693:GHSY-1294-MONOMER; -. DR Proteomes; UP000000935; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000935}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ADE68327.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862, KW ECO:0000313|EMBL:ADE68327.1}; KW Transferase {ECO:0000313|EMBL:ADE68327.1}. SQ SEQUENCE 612 AA; 68030 MW; DAFF583B99BA0907 CRC64; MGLLEDLKSK ILIGDGATGT LLYSHGIDSC FEELNITKPE EVSRIHRAYV EAGANVIQTN TYAANYQKLA RYGLEDSVKD INVAGVKLAK QAAKDQAYVV GTLGGIRSFQ KNAISLEEVK RSIREQMFWL LNEGVDGLLF ETYYDFEELK TVLTLARKET DKPIITHVSL HDIGVLQDGR PLADALKELE ALGADVVGLN CRLGPYHMIQ SLEEVPLPDC AFLSAYPNAS LPAYVEGKLE YETNEDYFVE SARLFREQGV RLIGGCCGTT PAHVRAMSSA LKDLPPITSK VVKMRPAVTV QEREQQDKPH MHEIVKKRRS VIVELDPPKQ LGPTKFLEGA KALDKVGVDA ITLADNSLAS PRISNLAMAT LMQQETKARP LIHITCRDRN LIGLQSHLMG LHTLGMNQVL AITGDPSKVG DFPGATSVYD LSSFDLISLI AQFNEGLSYS GKPLGQKTNF SIAAAFNPNV RHLDRAVQRL EKKIDCGAHY FITQPLYSTK QIEEVYEATK HLTTPVYIGI MPLTSARNAR FIHHEVPGIK LSEDILERMD ATGNDRIRGE VEGLAIAKNL IDTAYELFDG IYLITPFMRY EMTEILTRYI HDKQLVTSER KI // ID D5E174_BACMQ Unreviewed; 311 AA. AC D5E174; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADE67880.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ADE67880.1}; GN Name=ybgG {ECO:0000313|EMBL:ADE67880.1}; GN OrderedLocusNames=BMQ_0847 {ECO:0000313|EMBL:ADE67880.1}; OS Bacillus megaterium (strain ATCC 12872 / QMB1551). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=545693 {ECO:0000313|EMBL:ADE67880.1, ECO:0000313|Proteomes:UP000000935}; RN [1] {ECO:0000313|Proteomes:UP000000935} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12872 / QMB1551 {ECO:0000313|Proteomes:UP000000935}; 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; ADE67880.1; -; Genomic_DNA. DR RefSeq; WP_013055555.1; NC_014019.1. DR RefSeq; YP_003561314.1; NC_014019.1. DR EnsemblBacteria; ADE67880; ADE67880; BMQ_0847. DR KEGG; bmq:BMQ_0847; -. DR PATRIC; 35478349; VBIBacMeg35839_0849. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR BioCyc; BMEG545693:GHSY-847-MONOMER; -. DR Proteomes; UP000000935; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000935}; KW Methyltransferase {ECO:0000313|EMBL:ADE67880.1}; KW Transferase {ECO:0000313|EMBL:ADE67880.1}. SQ SEQUENCE 311 AA; 34459 MW; 2EE0D4B56598AD1E CRC64; MNPIQQILHT FPVIVLDGAM ATELERYGCD LNDSLWSAKV LMEQPELIKR VHQDYFAAGA DCAITASYQS TFEGFAKRGL SEAEARELIQ ASVKIAAEAR DEFWQQEENR RNRPKPIVAA SVGPYGAFLA NGSEYTGQYD VTEEELMEFH RPRMKALIEA GADVLACETI PNVMEARAIA RLLEEFEGAY AWITFSAKDD LHISSGTLIS ECARYLDSYE QVAALGVNCT PPQYISSLIK EIKSQTDKPV IVYPNSGEHY DAESKTWNGT SAGETYGCSA HSWYEAGAQL IGGCCRTTPD DIKGITKWAR K // ID D5EM00_CORAD Unreviewed; 1292 AA. AC D5EM00; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 27-MAY-2015, entry version 39. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADE55160.1}; GN OrderedLocusNames=Caka_2142 {ECO:0000313|EMBL:ADE55160.1}; 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 {ECO:0000313|EMBL:ADE55160.1, ECO:0000313|Proteomes:UP000000925}; RN [1] {ECO:0000313|EMBL:ADE55160.1, ECO:0000313|Proteomes:UP000000925} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 45221 / IAM 15411 / JCM 23193 / KCTC 12865 RC {ECO:0000313|Proteomes:UP000000925}; 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; ADE55160.1; -; Genomic_DNA. DR RefSeq; WP_013043882.1; NC_014008.1. DR RefSeq; YP_003549330.1; NC_014008.1. DR EnsemblBacteria; ADE55160; ADE55160; Caka_2142. DR KEGG; caa:Caka_2142; -. DR PATRIC; 35444918; VBICorAka2911_2115. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; CAKA583355:GI4D-2182-MONOMER; -. DR Proteomes; UP000000925; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000925}; KW Reference proteome {ECO:0000313|Proteomes:UP000000925}. SQ SEQUENCE 1292 AA; 141284 MW; 131E819C534C92E1 CRC64; MSTTVSNPPL TAKGQQLADL FAQRILFLDG AMGTMIQQHS LEEADFRDDS FANVEGDLKG NNDLLSITRP DIIADIHRAF LEAGADIIET NTFSGTTIAQ ADYGLESRVR DINLASAKLA RQVADEVSAK EGRPTFVAGA IGPTNRTASL SPDVNRPEYR ATNYDELYTA YYEQVEALVE GGVDLLLPET VFDTLNLKAC LHAIEDFFDT QNERLPVIVS VTITDQSGRT LSGQTVEACW NSIRHAKPLC VGLNCALGAD LMRPFLQELS RVADSYVHVY PNAGLPNPLA PTGYDETPET TGSAVGGFAK DGLVNLVGGC CGTTPGHIAA VVKEVSQYAP RPIPVTTPAQ RLSGLEALNI EADTGFINVG ERTNVTGSPR FKKLIKADDF TAALAIAQSQ VDKGAQIIDI NFDEGMLDGE ACMTRFLNLV ASEPDISRVP IMIDSSKWSV IEAGLKCVQG KCIVNSISLK GGEDEFKAQA KKILRYGASV IVMAFDEKGQ AANQADKVAI AERSFKILTE EVGMDPQDII FDLNILTVAT GMEEHNNYAV DFIEAVREVK QKCPGARCSG GLSNISFSFR GNNPVREAMH AAFLHHACEA GLDMAIVNPG LLMDYQEMDP TLKTLVEDVL LNRNDEATEK LIEHAEAIKE GKITLGAGTP EERINAAMVQ GMETLRALFE RATAEKNPEI LERFLTSGTD AVPAAAEKKT ADVASDWRSG TVEERLSHAL VKGIVAHVDA DTEEARQKYA RPLEVIEGPL MDGMKVVGEL FGAGKMFLPQ VVKSARVMKK AVAYLLPYME AEKEGSSGSS AGKFLIATVK GDVHDIGKNI VAVVLACNNY EVKDLGVMVD CETILKEAEE WGADIIGLSG LITPSLDEMI FNAQEMQKRG FKQPLLIGGA TTSKAHTAIK IAPHYEQPIV RVGDASLVTE VCNNLLTEDS DRRTAYIAEV AAEQEKQRQR FAARAKDTEF LSLEDARAKR FTCDWSKAQL KAPNRPGITV DDHIDLEALS EYFDYSPLFW TWELKGVYPY ILEHKKYGEE AQKIYADAQA LLKRIIAEKR FRARSVVGLF PANSVGDDIE LYTDTERSGV LNTLHSLRQQ KKKDKGDTYF ALADFVAPKD SGQVDACGAF AACIEGVDAF AQEFEDAHDD YSSIMVKAIG DRFAEALAEY THARVRKELW GYAPDEALDN DQLIQEEYRG IRPAAGYPSQ PDHTEKAIIW DLLQAEANTG ATLTESFAMH PGSAVSGLYF GHPDAKYFQV GPMAKDQFED YAQRKGFNLE KTEKWLAPNK GY // ID D5EZ62_PRER2 Unreviewed; 902 AA. AC D5EZ62; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 29-APR-2015, entry version 33. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:ADE81124.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADE81124.1}; GN Name=metH {ECO:0000313|EMBL:ADE81124.1}; GN OrderedLocusNames=PRU_0799 {ECO:0000313|EMBL:ADE81124.1}; OS Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=264731 {ECO:0000313|EMBL:ADE81124.1, ECO:0000313|Proteomes:UP000000927}; RN [1] {ECO:0000313|EMBL:ADE81124.1, ECO:0000313|Proteomes:UP000000927} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19189 / JCM 8958 / 23 {ECO:0000313|Proteomes:UP000000927}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002006; ADE81124.1; -; Genomic_DNA. DR RefSeq; WP_013063111.1; NC_014033.1. DR RefSeq; YP_003574153.1; NC_014033.1. DR EnsemblBacteria; ADE81124; ADE81124; PRU_0799. DR KEGG; pru:PRU_0799; -. DR PATRIC; 35495749; VBIPreRum14515_0768. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR BioCyc; PRUM264731:GHX6-774-MONOMER; -. DR Proteomes; UP000000927; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000927}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADE81124.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000927}; KW Transferase {ECO:0000313|EMBL:ADE81124.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 225 225 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 747 747 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 902 AA; 99002 MW; 205686A3797021AD CRC64; MKKLNEIIKQ RILILDGGMG TMIGAVMGKV GNSDELNLTH PEIVSDIYRK YLEAGADIIT TNTFSSQRIS QAEYHLEDRA HEMACESARL ARQLANEYST DDKPRFVAGS IGPTNKTLSM SPDVSNPAFR DVTYDEMLEA YQEQADGLIE GGVDTLLIET IFDSLNAKCA IDACMRAMEA RGVELPIMVS VTVSDLAGRT LSGQTLEAFL ASVSTYPIFS IGLNCSFGAT QMKPFIRELA QKAPYYISCH PNAGLPNALG LYDETAESMA PKMGELVDEG IVNIIGGCCG TTDEFIRLYG PLVVGKKPHV PAPKPHSMWL SGLELLEVLE NLEARFTNVG ERCNVAGSRK FLRLIKEKKY NEAISIARKQ VADGALVIDI NMDDGLLDAK QEMTTFLNMI AAEPDIAKVP VMIDSSNWEV IKAGLKCVQG KSIVNSISLK EGEQKFIEHA QDVMRYGAAV VVMCFDEEGQ ATTYERRIEI ASRAYKILTE QVGMNPLDII FDPNILAIAT GMEEHDAYAI DFIRATEWIK QNLPGAHVSG GVSNLSFSFR GNNYIREAMH AVFLYHAIQV GMDFGIVNPS TKVTYADIPQ DQLEVIEDVV LNRKKGASEV LIELAGKILE EELAKKEAGG ATSENTPFQD RAQTPVEERL AQALIKGDGT FLEEDLKEAL PKFTHAVQII EGPLMAGMNT VGTLFGEGKM FLPQVVKTAR TMKQAVDILQ PYIEAEKNES TTSAGKVLLA TVKGDVHDIG KNIVNVVMAC NGYEVLDMGV MVPAEQIVKK AQEEHVDMIG LSGLITPSLE EMVNVAEELK KAGLDIPIMI GGATTSELHV ALKIAPVYGG PVVWMKDASQ NALVAQKLLT DKQAVEHELD QKYETLREEY HQEQAQIVSL EEARKNKYKY EE // ID D5H3E0_LACCS Unreviewed; 329 AA. AC D5H3E0; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=MmuM protein {ECO:0000313|EMBL:CBL50525.1}; GN Name=mmuM {ECO:0000313|EMBL:CBL50525.1}; GN OrderedLocusNames=LCRIS_01078 {ECO:0000313|EMBL:CBL50525.1}; OS Lactobacillus crispatus (strain ST1). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=748671 {ECO:0000313|EMBL:CBL50525.1, ECO:0000313|Proteomes:UP000002371}; RN [1] {ECO:0000313|EMBL:CBL50525.1, ECO:0000313|Proteomes:UP000002371} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ST1 {ECO:0000313|EMBL:CBL50525.1, RC ECO:0000313|Proteomes:UP000002371}; RX PubMed=20435723; DOI=10.1128/JB.00399-10; RA Ojala T., Kuparinen V., Koskinen J.P., Alatalo E., Holm L., RA Auvinen P., Edelman S., Westerlund-Wikstrom B., Korhonen T.K., RA Paulin L., Kankainen M.; RT "Genome sequence of Lactobacillus crispatus ST1."; RL J. Bacteriol. 192:3547-3548(2010). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ST1; RA Ojala T., Kuparinen V., Koskinen J.P., Alatalo E., Holm L., RA Auvinen P., Edelman S., Westerlund-Wikstroem B., Korhonen T.K., RA Paulin L., Kankainen M.; RT "Genome Sequence of Lactobacillus crispatus ST1."; 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; FN692037; CBL50525.1; -; Genomic_DNA. DR RefSeq; WP_005719570.1; NC_014106.1. DR RefSeq; YP_003601550.1; NC_014106.1. DR EnsemblBacteria; CBL50525; CBL50525; LCRIS_01078. DR GeneID; 9107864; -. DR KEGG; lcr:LCRIS_01078; -. DR PATRIC; 37240975; VBILacCri149433_1054. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; SSVEGFM; -. DR BioCyc; LCRI748671:GIX1-1142-MONOMER; -. DR Proteomes; UP000002371; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002371}. SQ SEQUENCE 329 AA; 37079 MW; AC5A97247149A998 CRC64; MNLLKQIRDR GLILDGAMST ALEKLGIDTN NELWTAIALE HNLAQIYQVH MNYFKAGAQM AITDTYQANI PAFEKHGFTQ DQATKLITNA VQIAKKARDD FAKTTGIHNY VAASVGPYGA YLAQGDEFRG DYSLTTEEYL NFHLPRLKIL LANKPDCLAL ETQPKLDEVV AILDWLKENA PEIPVYVSFT LHDTTKISDG TPLKRVVQKL NEYDQVFAIG ANCFKPFLAT AVIDKIHDFT DKQIVIYPNL GGVYNEFERN WIPFNAKFDF KKLSQEWYEH GARIIGGCCS TTEKEIGQIS AFFKTINNAK SKSVKSELKK VKNDSNIQI // ID D5H4Z3_SALRM Unreviewed; 320 AA. AC D5H4Z3; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 29-APR-2015, entry version 24. DE SubName: Full=Chromosome, complete genome {ECO:0000313|EMBL:CBH23098.1}; GN OrderedLocusNames=SRM_00177 {ECO:0000313|EMBL:CBH23098.1}; OS Salinibacter ruber (strain M8). OC Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis; OC Rhodothermaceae; Salinibacter. OX NCBI_TaxID=761659 {ECO:0000313|EMBL:CBH23098.1, ECO:0000313|Proteomes:UP000000933}; 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] {ECO:0000313|Proteomes:UP000000933} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M8 {ECO:0000313|Proteomes:UP000000933}; 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; CBH23098.1; -; Genomic_DNA. DR RefSeq; WP_013060666.1; NC_014032.1. DR RefSeq; YP_003570050.1; NC_014032.1. DR EnsemblBacteria; CBH23098; CBH23098; SRM_00177. DR KEGG; srm:SRM_00177; -. DR PATRIC; 35488322; VBISalRub49863_0170. DR HOGENOM; HOG000265278; -. DR PhylomeDB; D5H4Z3; -. DR BioCyc; SRUB761659:GHC6-182-MONOMER; -. DR Proteomes; UP000000933; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000933}. SQ SEQUENCE 320 AA; 33903 MW; 336E3D6EE890916B CRC64; MRDLSTRLSG GPVLLDGGLG QELIRRGMPG TEPSLWSANA LTEAPDLVQE VHEEYLRAGA DVITTNTYAT PPERLSEAGL DGRAEALNRE AGRLAERARA AVGRDALIAG SLPPIRGSYR PDLVGEAGEI EPQYREQAGY LAPHVDLFLC ETMSTPGEAQ AAARGAASTG LPVLVSYTIA DPSSPEDAEP RLRNGESLEE AVEALSGLPV EGVLLNCSHP ESISAAVPVL RQLTDRAVGA YANAFTHIPD GFDERADALD SDARPDRRED FAPEAYGRHV EDWLSAGADI VGGCCEVRPG HIAHLRTTVD GAADARRAAE // ID D5HGD3_9FIRM Unreviewed; 808 AA. AC D5HGD3; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Draft genome {ECO:0000313|EMBL:CBK83966.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CBK83966.1}; GN ORFNames=CCU_26970 {ECO:0000313|EMBL:CBK83966.1}; OS Coprococcus sp. ART55/1. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Coprococcus. OX NCBI_TaxID=751585 {ECO:0000313|EMBL:CBK83966.1, ECO:0000313|Proteomes:UP000008799}; RN [1] {ECO:0000313|EMBL:CBK83966.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ART55/1 {ECO:0000313|EMBL:CBK83966.1}; 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. RN [2] {ECO:0000313|EMBL:CBK83966.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ART55/1 {ECO:0000313|EMBL:CBK83966.1}; RA Pajon A.; 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; FP929039; CBK83966.1; -; Genomic_DNA. DR RefSeq; WP_015534959.1; NC_021018.1. DR EnsemblBacteria; CBK83966; CBK83966; CCU_26970. DR KEGG; coo:CCU_26970; -. DR PATRIC; 42893246; VBICopSp152499_1850. DR KO; K00548; -. DR Proteomes; UP000008799; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008799}; KW Methyltransferase {ECO:0000313|EMBL:CBK83966.1}; KW Transferase {ECO:0000313|EMBL:CBK83966.1}. SQ SEQUENCE 808 AA; 87305 MW; 6D1F8612BB7BB720 CRC64; MKKTDFRKLF DDKILILDGA TGTNLMNAGM PLGVCPEKWI LEHPQIMFDL QVAYLNAGTD ILYAPTFTCN RIKLNEYGLA DDLEDMNRRL VKLSKEAVKA AGHGLVAGDI TMTGEMLYPM GKLKFEELVD VYKEQIKVID ESGCDLLVVE TMMSLAETRA AVIAANEVSD LPIIASLTFN EDGRTLYGTD PVTAVNVLQN LGVAAIGVNC STGPDKMVEL VRQMKSIAFI PVFAKPNAGM PELVNDKSVY RMTPEEFAED MKMIIEAGAG MVGGCCGTRP EHIKALADMA SKMPVPEISS EHVRCISSER SSLIIDLDAP FKVVGERINP TGKKKLQAEL REGSLELVMN MAEEQVDKGA SILDINVGMN GIDERDMMLK VVYQVSQAVN LPLCLDSSSP EVLEAALRIY PGRALVNSVS LEKVKMEEIL PLVKKYGAMF ILLPLSDKGL PESPQEKEDI INTVLGTAYE MGFTKNDVVV DGLVATVGAQ KDAAINCLKT INYCYNNGLA TICGLSNISF GLPERMFVNT AFLTMAISRG LTMAIANPSQ TMLMNAAFAS DMLLFKEESD VRYIENVKPL ELASPGAGAS GGKAGSDLEG KSQIYIDVLK GNKRSILDDV HAVLDSGADP QSIIDNDLIG AINEVGRLFE KKKYFLPQLI SSAETMEMAI GVISPLVLKD KDSSDMPTIV VATVEGDIHD IGKNLVVLML RNYGFNVIDL GKDVPCDVII QAAKDNNASI IGLSALMTTT MVKMKDVVEA VKENGLDSKV VIGGAVITES YAEEIGADGY SEDAANCVVV VKNLLGIE // ID D5MGY5_9BACT Unreviewed; 1227 AA. AC D5MGY5; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 29-APR-2015, entry version 29. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CBE69016.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CBE69016.1}; GN Name=metH {ECO:0000313|EMBL:CBE69016.1}; GN ORFNames=DAMO_1966 {ECO:0000313|EMBL:CBE69016.1}; OS Candidatus Methylomirabilis oxyfera. OC Bacteria; candidate division NC10; Candidatus Methylomirabilis. OX NCBI_TaxID=671143 {ECO:0000313|EMBL:CBE69016.1, ECO:0000313|Proteomes:UP000006898}; RN [1] {ECO:0000313|EMBL:CBE69016.1, ECO:0000313|Proteomes:UP000006898} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; FP565575; CBE69016.1; -; Genomic_DNA. DR RefSeq; WP_015744510.1; NC_013260.1. DR RefSeq; YP_003206847.1; NC_013260.1. DR KEGG; mox:DAMO_1966; -. DR KO; K00548; -. DR BioCyc; CMET671143-WGS:GSII-1918-MONOMER; -. DR Proteomes; UP000006898; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006898}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CBE69016.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006898}; KW Transferase {ECO:0000313|EMBL:CBE69016.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 762 762 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136020 MW; 8B937642C556D78F CRC64; MTDTFGRFAE LEQMLRHRIV ILDGAMGTMI QMHNLTEADF RGQKFADHPC DLKGCNDLLA ITQPAIIEAI HCQYLDAGAD IIETNTFNST SISMADYRLE SLAYDLNLSG ARAARSAVES TMAKDPNHPR FVAGSIGPTN RTASMPSDIH NPAFRAVTFD RLVAAYTEQV RGLLDGGVDL LLVETVFDTL NCKAALFAID QYFEEVGRRV PIMVSVTIAD RSGRTLSGQT VEAFWNSIAH MPLFSVGINC AFGAKQMRPY LEELAQIASV FLSCYPNAGL PNAFGGFDET PAIMAADLGD FAKSGWLNIV GGCCGSTPDH IRAIAKAVRE YQPRVPPHPQ PHTRLSGLEP VTICPEVGFV NIGERTNIAG SAAFAKLIRS GEYEAAASIA RQQVEGGAQI IDVNMDEAML DAKAAMIQFL NLVACEPDIA RVPVMIDSSD WSVIEAGLKC AQGKPVVNSI SLKEGEETFI QRARLIKRYG AAVVVMAFDE RGQADTLERK TEICARAYRI LTGTVGMPPQ DIIFDPNILT VATGLEEHNR YAVDFIEATR WIKANLPYCK VSGGVSNVSF SFRGNNAVRE AMHSAFLYHA VHAGLDMGIV NAGQLTVYAD ITKDLLEVVE DVLLNRRPDA TDRLVEFAKT MKAQERAVVK DEAWRQGSVE ERLTHALVKG ITDYIESDVE EARQRYDRPL QVIEGPLMAG MNLVGELFGS GKMFLPQVVK TARVMKKAVA YLLPFIEVER LTSDRKRTQR KVLMATVKGD VHDIGKNIVG VVLGCNDYEV IDLGVMAPCD TILKTAREQQ VDMIGLSGLI TPSLNEMMHV AREMMREGLK IPLLIGGATT SRTHTAVKIA PLYDQPVVHV ADASRAVVVA GHLSSRDQRS AFIENNRLDQ ERVRQAYEDR EPRALLTLTQ ARDRKLLLDW RAADIPTPSS IGIRMLDEFP LDQIVPYIDW TPFFHAWEMR GRYPEILQKP KARELFDDGQ HLLEQIVRDR RLIARAVYGF FPANSVDDDI ELYTDDSRSQ VLATFHTLRQ QLPKAEGQCN LALADFIAPR LPGRPDYLGA FAVTTGHGLD ALCAQYEASH DDYTSILAKA LADRLAEAFA ECLHRRVRAE WGYGVGEQLT NEDLIRERYR GIRPAPGYPA CPDHSEKRTL FDLLQVERNA GIRLTDSCAM VPTSSVSGLY FAHREATYFA VGKIGRDQVL DYAQRKRMDV RTVERWLAAN LNYDVDT // ID D5P4V6_9MYCO Unreviewed; 1277 AA. AC D5P4V6; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFG78860.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFG78860.1}; GN Name=metH {ECO:0000313|EMBL:EFG78860.1}; GN ORFNames=HMPREF0591_1200 {ECO:0000313|EMBL:EFG78860.1}; OS Mycobacterium parascrofulaceum ATCC BAA-614. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=525368 {ECO:0000313|EMBL:EFG78860.1}; RN [1] {ECO:0000313|EMBL:EFG78860.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-614 {ECO:0000313|EMBL:EFG78860.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFG78860.1}. 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; ADNV01000091; EFG78860.1; -; Genomic_DNA. DR RefSeq; WP_007170398.1; NZ_GG770555.1. DR EnsemblBacteria; EFG78860; EFG78860; HMPREF0591_1200. DR PATRIC; 37986190; VBIMycPar21360_3782. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFG78860.1}; KW Transferase {ECO:0000313|EMBL:EFG78860.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 282 282 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 345 345 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 346 346 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 806 806 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1277 AA; 140093 MW; 2F738F9E1F8924D4 CRC64; MGDRGPLVSA TLGRVKDAFR YGRNYVNAAE SDFAPNIRPD CTDELSAALR RRIMVIDGAM GTAIQRDRPD EAGYRGDRFT EWPTALQGNN DLLNLTQPQI IEGIHREYLE AGADILETNT FNANAISLSD YGMADLAYEL NYAGAALARK AADEYSTPDK PRYVAGAIGP TTRTASISPD VNDPGARNIS YDELVAAYLE SANGLVDGGV DLLIIETIFD SLNAKAAVFA VETLFEERGR RWPMIISGTI TDASGRTLSG QVTEAFWNSI RHAKPIAVGL NCALGAPEMR PYIAEVSRIA DTFVSCYPNA GLPNAFGEYD ESPERQATYI ADFAEAGLVN LVGGCCGTAP PHIAEIAKVV EGLRPREVPH IAVATRLSGL EPLNITDDSL FVNIGERTNI TGSARFRNLI KAEDYDTALS VALQQVEVGA QVIDINMDEG MIDGVAAMDR FTKLVAAEPD ISRVPVMIDS SKWEVIEAGL KNVQGKPIVN SISMKEGEEK FIREARLCRK YGAAVVVMAF DEQGQADNLE RRKEICGRAY RILTEQVGFP PEDIIFDPNC FALATGIEEH ATYGIDFIEA CAWIKENLPG VHISGGISNV SFSFRGNNPV REAIHAVFLY HAIKAGLDMG IVNAGALVPY DSIDPELRDR IEDVVLNRRD DAAERLLEIA ERFNKTDKAE DPKAAEWRSL PVRERITHAL VKGIDAHVDA DTEELRAEIA AAGGRPIEVI EGPLMDGMNV VGDLFGSGKM FLPQVVKSAR VMKKAVAYLL PFIEAEKEQN GASQNGGAGK DTNGTIVMAT VKGDVHDIGK NIVGVVLQCN NFEVIDLGVM VPAEKILAAA KEHDADIIGL SGLITPSLDE MANFAVEMER EGLEIPLLIG GATTSRAHTA VKISPRRSGP VVWVKDASRS VPVAAALLDD KQRPALLEAT EKDYASLRER HSQKNERPMV TLEKARANRT PIEWDGYTPP VPAMGAGVRE FQDYDLAELR EYIDWQPFFN AWEMKGRFPD ILNNPGTGEA ARKLYDDAQE MLDTLIKEKW LTANGVIGFF PANAVGDDIE VYTDDTRTEV LTTLHNLRQQ GEHRDGIPNR SLGDYIAPKD TGLADYVGAF AVTAGLGSQE KIAEFKAALD DYSAILLESI ADRLAEAFAE RMHQRVRKEF WGFQPDEQLD NDALIDEKYV GIRPAPGYPA CPEHTEKVTL WKLLDVRERT GIELTESMAM WPGAAVSGWY FSHPQSQYFV IGRLAQDQVA DYARRKGWTL QEAERWLAPN LGYNPED // ID D5PH58_9MYCO Unreviewed; 133 AA. AC D5PH58; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 27-MAY-2015, entry version 11. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFG74665.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EFG74665.1}; GN Name=mmuM {ECO:0000313|EMBL:EFG74665.1}; GN ORFNames=HMPREF0591_5502 {ECO:0000313|EMBL:EFG74665.1}; OS Mycobacterium parascrofulaceum ATCC BAA-614. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=525368 {ECO:0000313|EMBL:EFG74665.1}; RN [1] {ECO:0000313|EMBL:EFG74665.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-614 {ECO:0000313|EMBL:EFG74665.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFG74665.1}. 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; ADNV01000353; EFG74665.1; -; Genomic_DNA. DR RefSeq; WP_007169490.1; NZ_GG770554.1. DR EnsemblBacteria; EFG74665; EFG74665; HMPREF0591_5502. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFG74665.1}; KW Transferase {ECO:0000313|EMBL:EFG74665.1}. SQ SEQUENCE 133 AA; 14226 MW; 0182F339D9E99CFB CRC64; MELAPISESV LINDGGLATE LEARGHDLSD PLWSARLLAD DPHEIVAVHA AYFRAGATIA AAHAFRTARR AVGGRRGAHR RRLLPGAPGR HCGAAPSVHW RRKISEKLAV SSRSANVAKR SARKASGTPA RCR // ID D5Q9X5_PEPDI Unreviewed; 811 AA. AC D5Q9X5; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 01-OCT-2014, entry version 24. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFH05298.1}; GN ORFNames=HMPREF0220_3709 {ECO:0000313|EMBL:EFH05298.1}; OS Peptoclostridium difficile NAP08. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Peptoclostridium. OX NCBI_TaxID=525259 {ECO:0000313|EMBL:EFH05298.1}; RN [1] {ECO:0000313|EMBL:EFH05298.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NAP08 {ECO:0000313|EMBL:EFH05298.1}; 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 (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. {ECO:0000313|EMBL:EFH05298.1}. 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; ADNX01000103; EFH05298.1; -; Genomic_DNA. DR EnsemblBacteria; EFH05298; EFH05298; HMPREF0220_3709. DR PATRIC; 37996657; VBICloDif41119_3128. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFH05298.1}; KW Transferase {ECO:0000313|EMBL:EFH05298.1}. SQ SEQUENCE 811 AA; 88681 MW; F6BDEAF8DABEF887 CRC64; MKIVKTIETV HIEKERTLVE IRQYLKNNIL IFDGAMGTML QQKGLKLGEN PEVFGIQNPE KLIEIHTAYL EAGSNVILTN TFGCNELKLD SEYTVEEVID NAVLVARKAI ENVDNTKPRY VALDIGPIGE MLEPMGTLSF DKAYEIFKRQ VLQGVKSGVD VIVIETMMDL YEAKVAVLAA KENSDLPIFC TMTFDEGGRS FTGCMPECMV ATIEGLGVDA IGVNCSLGPK QLLPIVEKIA SRATVPVMVQ ANAGLPNIVD GEAIYDVDAK EFFEGVKKFV EVGATIIGGC CGTNPSFIKE ISENINSVTK GCIEKIDKCV VCSPSKFVEV ESPTVVGERL NPTGRKALQE ALKNENVDYA INLGLEQVNA GAQILGVNVG LPEIDEKKLM PKLIREIQAV VDTPLQVDSS NVEALEQGLR YYNGRTIVNS VNGKEESLKS ILPIVKKYGS CVVGLTLDEK GIPKKAEERF EIAKRIVDRA VSYGIKPKDI FIDCLSLTVS AQQEEAIETI KAIAMVKTLG VKTILGVSNI SFGLPNRKAL NASFLTLALG AGLDLAIINP NECSMMEAIN SFKILNNTDK GCINYINQYS NINNSKKLDS STKIDKDLPL DILVERGLKD EAKNVTLNLL KEKDENYILD KILIPALDKV GKRYDSGDIF LPQLIQSAET VKVSLNTIKE TLLSKSSNNV SKGKIIVATV KGDIHDIGKN IVKIMLENYG YEVIDLGKDV PIEEVVEVAK KRNIKLVGLS ALMTTTVQSM KDTIQALRDN EINAKVFVGG AVLTEEYAEE MGADYYSKDA KSAVEIAKLN F // ID D5QB96_KOMHA Unreviewed; 1169 AA. AC D5QB96; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 27-MAY-2015, entry version 32. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFG85582.1}; GN ORFNames=GXY_01936 {ECO:0000313|EMBL:EFG85582.1}; OS Komagataeibacter hansenii ATCC 23769. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Komagataeibacter. OX NCBI_TaxID=714995 {ECO:0000313|EMBL:EFG85582.1, ECO:0000313|Proteomes:UP000006468}; RN [1] {ECO:0000313|EMBL:EFG85582.1, ECO:0000313|Proteomes:UP000006468} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23769 {ECO:0000313|EMBL:EFG85582.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFG85582.1}. 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; ADTV01000004; EFG85582.1; -; Genomic_DNA. DR RefSeq; WP_003617214.1; NZ_CM000920.1. DR EnsemblBacteria; EFG85582; EFG85582; GXY_01936. DR PATRIC; 37998519; VBIGluHan153203_1464. DR Proteomes; UP000006468; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006468}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006468}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 225 225 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 292 292 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 738 738 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1169 AA; 128646 MW; D13DCB3E2E214444 CRC64; MTTRPHLLDA LRDQVLLCDG GMGSRVQLLD LEVERDYWGQ ENCTEILNLS RPELVREIHR GYFEAGADMV ETNSFGGSPI TLGEFGLSDR AREINRTAAH LAREAAEQFS DGRHRYVVGS VGPGTKLPSL GNIDYDTLES GLAEQCRGLI EGGVDCLLIE TCQDTLQIKA AVNAGKIARA ELGTDTPIFV QVTVETTGTL LVGPDIGAAA TVVNALDVPV MGLNCATGPQ EMAEHVRWLS ENWPGMISVQ PNAGLPELVN GKTHYPLTPQ DMATWVERFI VEDGLNLIGG CCGTSTPHTQ ALDAMLRRRA QEAGGSLRPA PVPRRPVWIP SVASLYSQVP LRQENSYFSI GERCNANGSK KWRQLQEAGD WDGCVAVGRE QAAEGSNALD ICTAFVGRDE MREMNEVITR FTSSVNAPLV IDSTETPVIE AALKLHGGKP IINSINFEDG EAAANDRLKL ARKFGASVIA LTIDEVGMAK TAEDKLRIAT RLVDYACNQH GLPQADLMID PLTFTIGTGV EDDRKLGLWT LEGIRLIHER FPDIQIVLGL SNISFGLNPA ARAVLNSVFL DHAVRAGMTA AIVHVSKIRP LHLIAEEEVK VAEDLIFDRR APGYDPLQRM LELFADRKAA DAVKKVRAET AAERLKDRIV DGDRKGLEDD LAEAMRDMAP LDIINTVLLD GMKVVGELFG SGKMQLPFVL QSAETMKAAV AWLEPHMERK EGQARGTMVL ATVKGDVHDI GKNLVDIILT NNGYRVINLG IKVPVADMIA AVREHGADAI GMSGLLVKST VIMRENLEEM NRQGIETPIL LGGAALTRNY VEEDCVAAYG EDGRVAYARD AFDGLSLMDK VVKGEFDAYI AAIQSRRATK AARSTPRDLE QAENRGFAPA DIPAARARRE RLTRDEPVIA PPFWGARVLE ATPEAVLPFL NERSLYQFQW GFRKQGRSLD EFMVWARQEL RPVMRRMLAM CAQDDILRPQ ASYGYWKAAG EGNDLILFDA DGTTPVARFT LPRQPRADGE CIADFVRDID DAQRDVIGLQ VVTVGQKASD IARQWFEADR YQDYLYLHGL SVEMAEAMAE YTHKRIRAEL GFAAEDARDM NKLLQQGYRG SRYSFGYPAC PRLEEQEPIL KLLDAEKIGV TLTDGFQLHP EQSTSALVIL NPHAKYFSI // ID D5RC65_FUSNC Unreviewed; 320 AA. AC D5RC65; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFG95632.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFG95632.1}; GN Name=metH {ECO:0000313|EMBL:EFG95632.1}; GN ORFNames=HMPREF0397_0800 {ECO:0000313|EMBL:EFG95632.1}; OS Fusobacterium nucleatum subsp. nucleatum ATCC 23726. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=525283 {ECO:0000313|EMBL:EFG95632.1}; RN [1] {ECO:0000313|EMBL:EFG95632.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 23726 {ECO:0000313|EMBL:EFG95632.1}; 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 (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. {ECO:0000313|EMBL:EFG95632.1}. 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; ADVK01000022; EFG95632.1; -; Genomic_DNA. DR RefSeq; WP_005902716.1; NZ_ADVK01000022.1. DR EnsemblBacteria; EFG95632; EFG95632; HMPREF0397_0800. DR PATRIC; 38046718; VBIFusNuc129935_0798. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFG95632.1}; KW Transferase {ECO:0000313|EMBL:EFG95632.1}. SQ SEQUENCE 320 AA; 35401 MW; F219F640C4AF6A62 CRC64; MKKMMFELEK ELEERILVLD GAMGTVLQKY ELTLEDFNGA KGCYEILNET RPDIIFEVHK KYIEAGADII ETNSFNCNAI SLKDYHLEDK VYDLAKKSAE IARDAVKKSG KKVYVFGSVG PTNKGLSFSV GDVPFKRAVS FDEMKEVIKV QVAGLIDGGV DGILLETIFD GLTAKAALLA IEEVFEEKNI KLPVSISATV NKQGKLSTGQ SIESLMVDLD RDFVISFGFN CSFGAKNLVP LVIKIKELTT KFVSLHANAG LPNQNGEYEE TAQKMRDDLL PLIENQAINI LGGCCGTDYE HIKLIAELVK GQKPRILPKR // ID D5RLA8_9PROT Unreviewed; 1166 AA. AC D5RLA8; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFH11912.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFH11912.1}; GN Name=metH {ECO:0000313|EMBL:EFH11912.1}; GN ORFNames=HMPREF0731_1869 {ECO:0000313|EMBL:EFH11912.1}; OS Roseomonas cervicalis ATCC 49957. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Roseomonas. OX NCBI_TaxID=525371 {ECO:0000313|EMBL:EFH11912.1}; RN [1] {ECO:0000313|EMBL:EFH11912.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 49957 {ECO:0000313|EMBL:EFH11912.1}; 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 (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFH11912.1}. 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; ADVL01000305; EFH11912.1; -; Genomic_DNA. DR RefSeq; WP_007004286.1; NZ_GG770779.1. DR EnsemblBacteria; EFH11912; EFH11912; HMPREF0731_1869. DR PATRIC; 38053783; VBIRosCer132485_2360. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFH11912.1}; KW Transferase {ECO:0000313|EMBL:EFH11912.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 224 224 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 735 735 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1166 AA; 127979 MW; 9C62DD099AD01CC4 CRC64; MARPTLLEAL RDRVLLCDGG MGSRVQALTL DVEKDYWGKE NCTEVLNLSR PELVREIHRG YYEAGSDMVL TNSFGGSPIT LEEFELGAKA FEINKLSVEL AREAAESFAD GRDRWVIGDI GPGTKLPSLG HIDYDTLEAA LTEQCRGLIA GGADALLTET NQDTLFIKAA VNAAKIALRE AQKEIPIFVQ VTVETTGTLL VGADIAAATT VVQALDVPLI GLNCATGPQE MAEHVRYLAQ NWPGLVSVQP NAGLPELVDG KTHYPLGAAE MASWMERFVT EDGVNLIGGC CGTSTPHIQA LDAMLRKVGG SRFRPAPVAR RVHWVPAVAS LYGATTLRQE NAYFSIGERC NANGSKAWRE RQAAHDWDGC VAMGREQVGE GSNSLDICTA FVGRDEMAEM NEVVRRFTGS VNAPLVIDST ETPVIEAALK LHGGKPIINS INFEDGEGHA TDRMKLAKKF GAAVIALTID EVGMAKTAED KLRIAERLVD FACNKHGLPQ SDLLIDPLTF TIATGNEDDR KLGLWTLEGI RMIRERFPDI QIILGLSNIS FGLNPAARHV LNSVFLDHAV KAGMTGAIVH VSKIKPLHSI PPEEVKVAED LIFDRRSEGY DPLQKLLEIF AGRKAADAAK KVKAETVEGR LKDRIVDGDR KGLDDELADA LAKGIKPLDI INGILLDGMK VVGELFGAGK MQLPFVLQSA ETMKAAVAYL EPFMEKIEGQ EKGTIVLATV KGDVHDIGKN LVDIILTNNG YKVVNLGIKV PLTEMVAAVR EHRANAIGMS GLLVKSTVVM KENLEEMSRL GVEVPVLLGG AALTRNFVEE DCVRAYASGR VAYARDAFDG LHLMDRVMGN DFDGYIAALQ SKRAGKSKNT TRTLGTADPR GFAPVDVNYA QARRRRVTQG EAVPVPPFWG ARVMEAAPKA IIPFINERSL YQFQWGFRKQ GRSLEDFIGW AKQELRPVLK RMLALAEQEK ILRPQAIYGY WKCAGQGNDV ILFEEDGVTE AARFTLPRQP KEDGECIADF LRDIEDGPEG RDVIGLQVVT VGQKASDVAR EWFEGNRYQD YLYLHGLSVE MAEAMAEYIH KRIRAELGYA GEDDRDMEKM LAQGYRGGRY SFGYPACPRL EDQEPLLRLL QAERIGVSIS DEWQLHPEQS TSAIVLHHPR AKYFSV // ID D5S1N7_PEPDI Unreviewed; 811 AA. AC D5S1N7; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 01-OCT-2014, entry version 24. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFH14829.1}; GN ORFNames=HMPREF0219_2468 {ECO:0000313|EMBL:EFH14829.1}; OS Peptoclostridium difficile NAP07. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Peptoclostridium. OX NCBI_TaxID=525258 {ECO:0000313|EMBL:EFH14829.1}; RN [1] {ECO:0000313|EMBL:EFH14829.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NAP07 {ECO:0000313|EMBL:EFH14829.1}; 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 (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. {ECO:0000313|EMBL:EFH14829.1}. 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; ADVM01000064; EFH14829.1; -; Genomic_DNA. DR EnsemblBacteria; EFH14829; EFH14829; HMPREF0219_2468. DR PATRIC; 38059861; VBICloDif89320_0659. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFH14829.1}; KW Transferase {ECO:0000313|EMBL:EFH14829.1}. SQ SEQUENCE 811 AA; 88681 MW; F6BDEAF8DABEF887 CRC64; MKIVKTIETV HIEKERTLVE IRQYLKNNIL IFDGAMGTML QQKGLKLGEN PEVFGIQNPE KLIEIHTAYL EAGSNVILTN TFGCNELKLD SEYTVEEVID NAVLVARKAI ENVDNTKPRY VALDIGPIGE MLEPMGTLSF DKAYEIFKRQ VLQGVKSGVD VIVIETMMDL YEAKVAVLAA KENSDLPIFC TMTFDEGGRS FTGCMPECMV ATIEGLGVDA IGVNCSLGPK QLLPIVEKIA SRATVPVMVQ ANAGLPNIVD GEAIYDVDAK EFFEGVKKFV EVGATIIGGC CGTNPSFIKE ISENINSVTK GCIEKIDKCV VCSPSKFVEV ESPTVVGERL NPTGRKALQE ALKNENVDYA INLGLEQVNA GAQILGVNVG LPEIDEKKLM PKLIREIQAV VDTPLQVDSS NVEALEQGLR YYNGRTIVNS VNGKEESLKS ILPIVKKYGS CVVGLTLDEK GIPKKAEERF EIAKRIVDRA VSYGIKPKDI FIDCLSLTVS AQQEEAIETI KAIAMVKTLG VKTILGVSNI SFGLPNRKAL NASFLTLALG AGLDLAIINP NECSMMEAIN SFKILNNTDK GCINYINQYS NINNSKKLDS STKIDKDLPL DILVERGLKD EAKNVTLNLL KEKDENYILD KILIPALDKV GKRYDSGDIF LPQLIQSAET VKVSLNTIKE TLLSKSSNNV SKGKIIVATV KGDIHDIGKN IVKIMLENYG YEVIDLGKDV PIEEVVEVAK KRNIKLVGLS ALMTTTVQSM KDTIQALRDN EINAKVFVGG AVLTEEYAEE MGADYYSKDA KSAVEIAKLN F // ID D5SPE9_PLAL2 Unreviewed; 1261 AA. AC D5SPE9; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 27-MAY-2015, entry version 40. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADG68293.1}; GN OrderedLocusNames=Plim_2467 {ECO:0000313|EMBL:ADG68293.1}; OS Planctomyces limnophilus (strain ATCC 43296 / DSM 3776 / IFAM 1008 / OS 290). OC Bacteria; Planctomycetes; Planctomycetia; Planctomycetales; OC Planctomycetaceae; Planctomyces. OX NCBI_TaxID=521674 {ECO:0000313|EMBL:ADG68293.1, ECO:0000313|Proteomes:UP000002220}; RN [1] {ECO:0000313|EMBL:ADG68293.1, ECO:0000313|Proteomes:UP000002220} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43296 / DSM 3776 / IFAM 1008 / 290 RC {ECO:0000313|Proteomes:UP000002220}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001744; ADG68293.1; -; Genomic_DNA. DR RefSeq; WP_013110724.1; NC_014148.1. DR RefSeq; YP_003630492.1; NC_014148.1. DR EnsemblBacteria; ADG68293; ADG68293; Plim_2467. DR KEGG; plm:Plim_2467; -. DR PATRIC; 38241508; VBIPlaLim6916_2990. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; PLIM521674:GKE7-2526-MONOMER; -. DR Proteomes; UP000002220; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002220}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002220}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 246 246 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 789 789 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1261 AA; 139893 MW; BF372762531981C9 CRC64; MVDISRPGLF ESLLDDRILI LDGAMGSMIH RFEPTEADYR GERFKSHSID LKNASDVLVL TQPQMIQSIH RQYLEAGADI IETNTFGATE LMLDEFHLGH LTHEMNIAAA TLARDVCDEF TKKNPAKPRF VAGSIGPTKF QLSFNADKPG YRPVTFEQLA ASYAGQVRAL LDGGVDLLLP ETSFDTLNMK ACLYAIEQVF AERGVRIPVM VSGTIFQGGV TLTGQTMEAF WAAVSHNPMT SVGLNCALGP KQMRQYVETL ANTATRYISC YPNAGMPDGM GGFDSTPSEF SGVIREFAEN GWVNIVGGCC GTTPEFIHAV ANVVKGVAPR KVPHENHWSV YSGSDVLKIP AADAVFDEGQ SAPNRSFLMI GERTNVTGSK KFARLIREKK YEEALTIAAQ QVENGANMID VNMDEGLLDS KAEMVHFLNL ISDDPAISKV PVMVDSSKFD VIEAGLKCLS GKGVVNSISL KEGEEKFLEH AGIIRKYGAA VVVMAFDEEG QAADQVNKVR ICQRAYKLLT EKAGFPPEDI IFDCNILTVG TGMEEHANYA VEFIEAVREI KATCPYARTS GGVSNVSFSF RGNEHVREAM NAAFLYHAIN AGLDMGIVNA GQLAVYDEIE KELLTYVEDV LLNRRPDATE RLIAYSEELK ARETRTDDSG PVVEAWRSES VEERLKHALL KGIADFIDED TEEARLKYSR PLNVIQGPLM DGMNVVGKLF GEGKMFLPQV VKSARVMKKS VAYLQPFMEA EKEALAASSE AAGETTVAAQ PTSTSRGKIL IATVKGDVHD IGKNIVAVVL RCNNFEVLDL GVMVPCDKIL DTAIAEGCQI IGLSGLITPS LDEMTTVAKE MERRGFKIPL LIGGATTSAK HTAVKIAPHY SAPTVHIVDA SLSVPVVENL LDDERRDEYL KQLAANQQRD RDTYGHLQKR TLVPFEEACR RRFETDWKTV KIDTPDFWGA KVLDDFPLEK LVPYIDWSPF FMTWELRGKY PKILHDPVVG EEASRVFSDA QKLLDRILKE KLLQAKGVYG FWPAQADGED IVLYSPESVA AGKPEIIQRF PMLRQQWERV GQKEFRSLAD YIAPIESGRM DSLGAFAVTT GIGCDELADE FLHKQHDDYL SIMTKALADR LAEAFAEYLH HEARQHWGFG KEESLSKEEM IEEKYRGIRP AYGYPACPDH TEKVPLFELL DVEKNTGIKL TESYAMHPGA AVSGLYFAHP ESRYFSVDKV TKDQIEDYAR RKEMSVAEIE KWLMPNLGYD N // ID D5T144_LEUKI Unreviewed; 306 AA. AC D5T144; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=YbgG {ECO:0000313|EMBL:ADG39993.1}; GN OrderedLocusNames=LKI_02250 {ECO:0000313|EMBL:ADG39993.1}; OS Leuconostoc kimchii (strain IMSNU 11154 / KCTC 2386 / IH25). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostocaceae; OC Leuconostoc. OX NCBI_TaxID=762051 {ECO:0000313|EMBL:ADG39993.1, ECO:0000313|Proteomes:UP000002362}; RN [1] {ECO:0000313|EMBL:ADG39993.1, ECO:0000313|Proteomes:UP000002362} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IMSNU 11154 / KCTC 2386 / IH25 RC {ECO:0000313|Proteomes:UP000002362}; 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 ----------------------------------------------------------------------- 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; ADG39993.1; -; Genomic_DNA. DR RefSeq; WP_013102591.1; NC_014136.1. DR RefSeq; YP_003620962.1; NC_014136.1. DR EnsemblBacteria; ADG39993; ADG39993; LKI_02250. DR KEGG; lki:LKI_02250; -. DR PATRIC; 38185513; VBILeuKim161478_0487. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR BioCyc; LKIM762051:GJOL-452-MONOMER; -. DR Proteomes; UP000002362; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002362}. SQ SEQUENCE 306 AA; 33801 MW; 6440C804DFDFA3BA CRC64; MTKFESYIES GTVILDGGMG SELEKRQIDV NNSWWSASAL IQSPEDVREI HKNYFDSGAD LAITDTYQAH VKSFTDQGLS EQKAYELIDS AVALAKLGLT DSNRSDGLIA GSVGPYGAYL ANGAEYTGDY HLSEFEFQAF HRPRIVRLID DGVDVLALET IPNFEEAKAL GHLLQQEFPT VNAYLSFSTE NGDHLWDGTR LSEAVAYFES ISQIKAIGVN CTAPQNILPA IKNITPNTSK KIIVYPNAGD EYDPETKRWV SQHGPIKWDE LVPLWQEAGA NLIGGCCRTS PDDINDIVQA TINQRH // ID D5TXN6_BACT1 Unreviewed; 1132 AA. AC D5TXN6; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 27-MAY-2015, entry version 33. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:ADH08731.1}; GN Name=metH {ECO:0000313|EMBL:ADH08731.1}; GN OrderedLocusNames=BMB171_C3922 {ECO:0000313|EMBL:ADH08731.1}; OS Bacillus thuringiensis (strain BMB171). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=714359 {ECO:0000313|EMBL:ADH08731.1, ECO:0000313|Proteomes:UP000001658}; RN [1] {ECO:0000313|EMBL:ADH08731.1, ECO:0000313|Proteomes:UP000001658} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BMB171 {ECO:0000313|EMBL:ADH08731.1, RC ECO:0000313|Proteomes:UP000001658}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001903; ADH08731.1; -; Genomic_DNA. DR RefSeq; WP_000649677.1; NC_014171.1. DR RefSeq; YP_003666451.1; NC_014171.1. DR EnsemblBacteria; ADH08731; ADH08731; BMB171_C3922. DR KEGG; btb:BMB171_C3922; -. DR PATRIC; 38134833; VBIBacThu148000_4201. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR BioCyc; BTHU714359:GJBQ-4038-MONOMER; -. DR Proteomes; UP000001658; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001658}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADH08731.1}; KW Transferase {ECO:0000313|EMBL:ADH08731.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 125990 MW; CE3D831A3277C6EF CRC64; MKCIEEKLKN SILILDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYDLSHLDE ELNEKAALLA KQAVKESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGE VDVLLVETSQ DMRNVKAAYI GIQAAFEELK KTVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWIN IIGGCCGTTP EHIKAMKSAL ASLRPRDHHE REGHGISGLE ALQYDESMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMENF LAEVTKVLKV PIMIDSTDEN VMERALTYIQ GKAVINSINL EDGEERFKKV TPLLQKYGAA IVVGTIDEDG MAVSAERKIE IAKRSYELLT KKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPEE EKRLADALLF ETTKETLEEF TNFYRVAKKK DVVVQETLTL DERLANYIVE GTKQGLHEDL SLALEEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILA NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAANIDVPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV KKEEKKVEIP AVIEPLPKSE VMVPDSTKRI VLRDVPALHL APFLNRQMLL GHHLGLKGNV KKLLKEGDKR AHELNDLIDE LLQEGQSWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRVIE RFTFPRQGKA PYRTLGDYLR PIGDEMDYVA FLSVTVGEGV RDIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID D5TXN7_BACT1 Unreviewed; 610 AA. AC D5TXN7; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 27-MAY-2015, entry version 31. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=BMB171_C3923 {ECO:0000313|EMBL:ADH08732.1}; OS Bacillus thuringiensis (strain BMB171). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=714359 {ECO:0000313|EMBL:ADH08732.1, ECO:0000313|Proteomes:UP000001658}; RN [1] {ECO:0000313|EMBL:ADH08732.1, ECO:0000313|Proteomes:UP000001658} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BMB171 {ECO:0000313|EMBL:ADH08732.1, RC ECO:0000313|Proteomes:UP000001658}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ADH08732.1; -; Genomic_DNA. DR RefSeq; WP_000770352.1; NC_014171.1. DR RefSeq; YP_003666452.1; NC_014171.1. DR ProteinModelPortal; D5TXN7; -. DR EnsemblBacteria; ADH08732; ADH08732; BMB171_C3923. DR KEGG; btb:BMB171_C3923; -. DR PATRIC; 38134835; VBIBacThu148000_4202. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR BioCyc; BTHU714359:GJBQ-4039-MONOMER; -. DR Proteomes; UP000001658; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001658}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ADH08732.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:ADH08732.1}. SQ SEQUENCE 610 AA; 67207 MW; 6AAA70A0BB40008A CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNVSDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTE INRAAVKLAK ASVTDKNAIL GTIGGMKHIG AVTTTDMERE FMLLEQAGAL LEEQVDGLLL ETFYDEFELL HAVKVLRKQT NIPIVAQLAL HEAGTTQNGN DVNEILKQLI DYGANVVGLN CQLGPLHMTE AFKMISIPQN GYLSAYPNAG LPNYVDGRYV YEGSPAYFEA MTPRFIEQGI RLLGGCCGTT PEHIQSMKRA VANITPVIEK DTIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRVSNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIK LIEEVYEATK HLEQPIFIGI MPLVSKRNAD FLHFEVPGIT LPEEIRERMD GHETKEAAIE EGIRISQELV DAAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID D5UPJ9_TSUPD Unreviewed; 1243 AA. AC D5UPJ9; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 29-APR-2015, entry version 33. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADG78755.1}; GN OrderedLocusNames=Tpau_2144 {ECO:0000313|EMBL:ADG78755.1}; 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 {ECO:0000313|EMBL:ADG78755.1, ECO:0000313|Proteomes:UP000001213}; RN [1] {ECO:0000313|Proteomes:UP000001213} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8368 / DSM 20162 / JCM 10117 / NBRC 16120 / NCTC 13040 RC {ECO:0000313|Proteomes:UP000001213}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001966; ADG78755.1; -; Genomic_DNA. DR RefSeq; WP_013126777.1; NC_014158.1. DR RefSeq; YP_003647094.1; NC_014158.1. DR EnsemblBacteria; ADG78755; ADG78755; Tpau_2144. DR KEGG; tpr:Tpau_2144; -. DR PATRIC; 38307585; VBITsuPau718_2143. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR BioCyc; TPAU521096:GI2W-2165-MONOMER; -. DR Proteomes; UP000001213; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001213}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001213}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 253 253 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 316 316 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 772 772 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1243 AA; 136304 MW; 5AE5C46AE7C859C8 CRC64; MSSFEPNIRP DCTDELAATL RRRIMVIDGA MGTAIQRDRP DEDGYRGERF TEWPTALQGN NDLLNLTQPQ IIEGIHREYL EAGADILETN TFNANAISLS DYDMGELSYE LNFVGAALAR KVCDEFSTAD KPRYVAGALG PTTRTASISP EVNDPGARNV SYDQLVAAYL EAVNGLVDGG SDVILIETIF DSLNAKAAVF AVETLFEDRG RRWPVIISGT ITDGSGRTLS GQVTEAFWNA IRHAKPIAVG LNCALGAPEM RPYIAEMARI SDTFVSCYPN AGLPNAFGEY DESPEHQAAY LAEFAEAGLV NLVGGCCGTA PAHIAEIARV VEGTPPREIP QLSVATRLSG LEPLNITADS LFVNIGERTN ITGSARFRNL IKAEDYDTAL SVALQQVEVG AQVIDINMDE GMIDGVAAMD RFTKLIAAEP DISRVPVMID SSKWEVIEAG LKNVQGKPIV NSISLKEGEE KFIREARLCR KYGAAVVVMA FDEQGQADNL ERRKEICGRA YRILTEEVGF PAEDIIFDPN CFALATGIEE HATYGIDFIE ACAWIKENLP GVHISGGISN VSFSFRGNNP VREAIHAVFL FHAIKAGLDM GIVNAGALVP YDAIDPELRD RIEDVVLNRR EDAAERLLEI AEQFNKSEKA EDPKAAEWRG LPVRERITHA LVKGIDADVE TDTEELRAEI AAAGGRPIEV IEGPLMDGMN VVGDLFGAGK MFLPQVVKSA RVMKKAVAYL LPYIEAEKDE SGAASKDTNG TIIMATVKGD VHDIGKNIVG VVLQCNNYEV IDLGVMVPAE KILAAAKEYD ADIIGLSGLI TPSLDEMVNF AVAMEREGLD IPLLIGGATT SRAHTAVKVS PRRSGPVVWV KDASRSVPVA AALLDDRQRP ALLEATEADY AALRERHAQK SERPMLTLEK ARANRTPIEW AAYTPPVPAQ GLGVREFLDY DLAELREYID WQPFFNAWEM KGRFPDILNN PVSGETARKL YDDAQTMLDT LIKEKWLTAN GVIGFFPANA VGDDIEVYTD ETRTDVLTRL HNLRQQGEHR DGIPNRSLGD FVAPKDTGLA DYVGAFAVTT GLGSAAKIVE FKAANDDYNA ILLESLADRL AEAFAERMHQ RVRTEFWGFQ PDEDLDNEAL IDEKYVGIRP APGYPACPEH TEKATLWELM NVHERTGIEL TESMAMWPGA AVSGWYFSHP QSQYFVVGRL AQDQVADYAK RKGWTLQEAE RWLSPNLGYN PED // ID D5V4W3_ARCNC Unreviewed; 1157 AA. AC D5V4W3; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 29-APR-2015, entry version 36. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADG91925.1}; GN OrderedLocusNames=Arnit_0259 {ECO:0000313|EMBL:ADG91925.1}; 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 {ECO:0000313|EMBL:ADG91925.1, ECO:0000313|Proteomes:UP000000939}; RN [1] {ECO:0000313|EMBL:ADG91925.1, ECO:0000313|Proteomes:UP000000939} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33309 / DSM 7299 / LMG 7604 / NCTC 12251 / CI RC {ECO:0000313|Proteomes:UP000000939}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001999; ADG91925.1; -; Genomic_DNA. DR RefSeq; WP_013134070.1; NC_014166.1. DR RefSeq; YP_003654431.1; NC_014166.1. DR EnsemblBacteria; ADG91925; ADG91925; Arnit_0259. DR KEGG; ant:Arnit_0259; -. DR PATRIC; 38113122; VBIArcNit33843_0257. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR BioCyc; ANIT572480:GJ62-266-MONOMER; -. DR Proteomes; UP000000939; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000939}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000939}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 223 223 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 727 727 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1157 AA; 128915 MW; 7DE8258833CB1D05 CRC64; MKNRINEIIQ NKVLIIDGAM GTQLQNAEIK PEAWKYENQD LEGCNELLNE TAPEILEGIH DAYAKAGANL ISTNTFGTMP WVLDEYGISS KAYELSKLGA ELVKKSCKKY ETEDEPRFCL GSIGPGTKLP SLGHIRYDEM YEGYKEVANG LADGGCDIYL LETCQDPLQI KAALHALTDT HPEIPVMVSV TIELSGTMLI GTDAMTIAAI MSPFNILSLG FNCGTGPKQV HKHVKTLSEV CKFPISVHAN AGLPQNKGGV SYYPMGPEEF TQLQSSFLEI NGVSFLGGCC GTTPEHIEAL ANKVRGIKPK APSGFLKASL ASLFNTVPLK QDPAPLLIGE RSNATGSKAF RDLLKDNNYE GTLSVGQQQV RAGAHIIDVS VGFAGRDETG DMDKVVELYS QKVSLPLMPD STQIKALEAA LKQIGGRCII NSVNLEDGEE KFDAVCKLAK KFGAALVCLV IDEVGMAKTK EDKIRIAERI YDLCVNRHGF NPEDLVFDML TFTIGSGDDE YRTAGVETME AIREFQILHP EVGTTLGLSN ISFGLDIKAR VYLNSIYLDH CVKAGLTSAI VNVKHILPLN KITEEDRKAC DDLIFNNQED GDPLFKFIDH FSNVEAQEDQ SDEEYLKMEP IDKVKKLLLD GDKDRLLPLV DELRHTIKAE MIVNEWLIDG MKIIGELFGS GQMQLPFVLQ SAETMKATVD ALNPYLPKEE KASETVLVIG TVKGDVHDVG KNLVDIILSN NGFKVINIGI KADINDFIIA VQKHKAQAIG MSGLLVKSTA VMKENLEELK RQGIDIPVLL GGAALTKSFV NEYCRPLYEG PIFYCRDAFD GVVSMQRIES GDSFNTKLAA DLIKDADDIK KEKKEVIIPP YEEIELPPKA EFTFPPLWGR VTQNKTLLNK DLIFSWINHR VLFRQRWGYK KGAMKADEFL AHEEDVVKPL YEKYKEEFFE KDIFDPIAIY GYYPCISHDN KLYIFDNEYA FNSLKEAQNV PPLEKAIKVF EFPRQTKAPY RCIADFFAND RLDVVAFTLA SSGLKITSYE SELYQNSEFS KYHQIHGLGV ELAEALAEVI HKQIRLDLDI VPKEGHTLYD VQMKQYVGCR YSPGYAACPD LEQSRDIFDL LKPEEFGITL SETFQIDPEQ STCAIVVPHN KANYYNI // ID D5V5I1_ARCNC Unreviewed; 310 AA. AC D5V5I1; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADG93116.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ADG93116.1}; GN OrderedLocusNames=Arnit_1459 {ECO:0000313|EMBL:ADG93116.1}; 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 {ECO:0000313|EMBL:ADG93116.1, ECO:0000313|Proteomes:UP000000939}; RN [1] {ECO:0000313|EMBL:ADG93116.1, ECO:0000313|Proteomes:UP000000939} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33309 / DSM 7299 / LMG 7604 / NCTC 12251 / CI RC {ECO:0000313|Proteomes:UP000000939}; 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; ADG93116.1; -; Genomic_DNA. DR RefSeq; WP_013135261.1; NC_014166.1. DR RefSeq; YP_003655623.1; NC_014166.1. DR EnsemblBacteria; ADG93116; ADG93116; Arnit_1459. DR KEGG; ant:Arnit_1459; -. DR PATRIC; 38115538; VBIArcNit33843_1446. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR BioCyc; ANIT572480:GJ62-1486-MONOMER; -. DR Proteomes; UP000000939; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000939}; KW Methyltransferase {ECO:0000313|EMBL:ADG93116.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000939}; KW Transferase {ECO:0000313|EMBL:ADG93116.1}. SQ SEQUENCE 310 AA; 34460 MW; 7915E8EFED7EE903 CRC64; MNKIKEILKS QKIVIIDGAT GTELERKGYD INDSLWSAKF LMENPKAIYE VHKDYLEAGS DCITTLSYQA TFEGFKERGL NEVQAKELLQ SSIKLAIEAR DEFWASNESK SRIKPLVAAS VGPYGAYLAD GSEFRGNYGL SQEELVNFHR KRMQALIEAK PDLLACETVP CLIEAKAYVK LLEEFPSTQA WITFSAKDGK HINSGESIKE CAKFLDNKEQ VVAIGINCTA PQYIESLISQ IKEVSTKPII VYPNGGAAYD GATKTWSTQA NTKDYGKMAH LWYEKGASVI GGCCQTTPND IEQISSWVRN // ID D5VFP8_CAUST Unreviewed; 358 AA. AC D5VFP8; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADG09780.1}; GN OrderedLocusNames=Cseg_1282 {ECO:0000313|EMBL:ADG09780.1}; 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 {ECO:0000313|EMBL:ADG09780.1, ECO:0000313|Proteomes:UP000002629}; RN [1] {ECO:0000313|Proteomes:UP000002629} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 21756 / DSM 7131 / JCM 7823 / NBRC 15250 / LMG 17158 / RC TK0059 {ECO:0000313|Proteomes:UP000002629}; 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; ADG09780.1; -; Genomic_DNA. DR RefSeq; WP_013078447.1; NC_014100.1. DR RefSeq; YP_003592398.1; NC_014100.1. DR EnsemblBacteria; ADG09780; ADG09780; Cseg_1282. DR KEGG; cse:Cseg_1282; -. DR PATRIC; 37202596; VBICauSeg118057_1313. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR BioCyc; CSEG509190:GHVG-1304-MONOMER; -. DR Proteomes; UP000002629; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002629}; KW Methyltransferase {ECO:0000313|EMBL:ADG09780.1}; KW Transferase {ECO:0000313|EMBL:ADG09780.1}. SQ SEQUENCE 358 AA; 39224 MW; 35FA3E1CADBA943C CRC64; MTDLSIRANR VAALKAAAKE RILILDGSWG VMFQKKGLTE ADYRADRFAA HDGQMKGNND ILCLTRPDLV AELHDAYFSA GADISETNTF SGTTIAQADY HLSAQDVWDI NLEGARIGRS VADRWNAENP ERPKFIAGSI GPLNVMLSMS SDVNDPGARK VTFDQVYEAY RQQVDALYQG GVDLFLIETI TDTLNCKAAI KAILDWRDEG HEELPIWISG TITDRSGRTL SGQTAEAFWN SVKHAKPFAV GFNCALGADL MRPHIAEMAR VADTLVAAYP NAGLPNAMGQ YDEEPHQTGH ALHEWAKDGL VNILGGCCGT TPDHIRHVAD EVRGVKPRQI PERPKAMRLA GLEPFELA // ID D5WAL6_BURSC Unreviewed; 356 AA. AC D5WAL6; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADG14319.1}; GN OrderedLocusNames=BC1002_0212 {ECO:0000313|EMBL:ADG14319.1}; OS Burkholderia sp. (strain CCGE1002). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=640511 {ECO:0000313|EMBL:ADG14319.1, ECO:0000313|Proteomes:UP000002190}; RN [1] {ECO:0000313|EMBL:ADG14319.1, ECO:0000313|Proteomes:UP000002190} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCGE1002 {ECO:0000313|EMBL:ADG14319.1, RC ECO:0000313|Proteomes:UP000002190}; 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; ADG14319.1; -; Genomic_DNA. DR RefSeq; WP_013088222.1; NC_014117.1. DR RefSeq; YP_003603830.1; NC_014117.1. DR EnsemblBacteria; ADG14319; ADG14319; BC1002_0212. DR KEGG; bge:BC1002_0212; -. DR PATRIC; 37209165; VBIBurSp41388_0200. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR BioCyc; BSP640511:GJ7J-216-MONOMER; -. DR Proteomes; UP000002190; Chromosome 1. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002190}; KW Methyltransferase {ECO:0000313|EMBL:ADG14319.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002190}; KW Transferase {ECO:0000313|EMBL:ADG14319.1}. SQ SEQUENCE 356 AA; 38246 MW; 0FA04EC7CCE8A692 CRC64; MTQPAQSITP VRSEPAYTRG AALPALLNSR ILILDGAMGT MIQRYKLDEA SYRGERFKDY PRDIKGNNEL LSITQPQIIS EIHEQYLAAG ADIIETNTFG ATTVAQADYG MESLAVEMNI ESAKLARAAC DKYATPDKPR FVAGAIGPTP KTASISPDVN DPGARNVTFD ELHAAYYEQA KALLDGGADL FLVETIFDTL NAKAALFALD ELFENTGERL PIMISGTVTD ASGRILSGQT VEAFWNSLRH AKPLTFGLNC ALGAALMRPY IAELAKLCDT YVSCYPNAGL PNPMSDTGFD ELPADTSGLL KEFAEAGLVN IAGGCCGTTP EHIAAIAKAL AELKPRKWPS QYRDAA // ID D5WSZ6_KYRT2 Unreviewed; 1159 AA. AC D5WSZ6; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 29-APR-2015, entry version 35. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADG05100.1}; GN OrderedLocusNames=Btus_0327 {ECO:0000313|EMBL:ADG05100.1}; OS Kyrpidia tusciae (strain DSM 2912 / NBRC 15312 / T2) (Bacillus OS tusciae). OC Bacteria; Firmicutes; Bacilli; Bacillales; Alicyclobacillaceae; OC Kyrpidia. OX NCBI_TaxID=562970 {ECO:0000313|EMBL:ADG05100.1, ECO:0000313|Proteomes:UP000002368}; RN [1] {ECO:0000313|Proteomes:UP000002368} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2912 / NBRC 15312 / T2 {ECO:0000313|Proteomes:UP000002368}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002017; ADG05100.1; -; Genomic_DNA. DR RefSeq; WP_013074393.1; NC_014098.1. DR RefSeq; YP_003588244.1; NC_014098.1. DR ProteinModelPortal; D5WSZ6; -. DR EnsemblBacteria; ADG05100; ADG05100; Btus_0327. DR KEGG; bts:Btus_0327; -. DR PATRIC; 37243568; VBIBacTus29608_0341. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; KTUS562970:GHUX-341-MONOMER; -. DR Proteomes; UP000002368; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002368}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002368}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 241 241 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 736 736 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1159 AA; 126720 MW; DE1922ED8CC3E2F3 CRC64; MTLGQNIQSV QLAKRRPELL ERRLKEAILV LDGAMGTMIQ QQGLTAADFG GEAQEGCNEV LNLTRPDVIT SIHEAYLEAG ADIIETNTFG ATRVVLAEYG LEGKAYAINR TAAELARRAA DGYSTPDRPR FVAGAMGPTT KTLSVTGGID FDTLAAAYAE QAKGLLDGGV DLLLVETAQD TLNVKAAGVG IHRAFAELGF EVPVMISGTI EPMGTTLAGQ GIDAFYVSVE HLHPVAVGLN CATGPEFMTD HLRTLSGLAK TAVSCYPNAG LPDEEGHYHE SPQSLAEKMA GFARQGWVNV VGGCCGTTPE HIRALAQAVR GLPPRTPAAD HPPAVSGVEA VFLEGDNRPL LVGERTNVIG SRKFRELIQS GRFEEAAEIA RAQVRGGAQI IDVCLADPDR DEYADMDQFL KYVTRMVKVP LMIDSTDPRV VELALQRSQG KAIINSINLE DGEKRFAQVA PLARRYGAAV VVGTIDEEGM AVTRERKLAV AQRSYQLLTE EYGIPPEDLI FDPLVFPVGT GDENYVGAAA ETVAALRMLK ERFPRSATIL GISNVSFGLP PAGREVLNAV FLYHCTKAGL DYAIVNPEKL QRYASIPEEE RRLAEALLFE TGQETLARFH DRFKDRPAGP PVRRETLSLN ERLARCVVEG SKEGLLDDLS EALQSASPIE IINGPLMAGM DEVGRLFNDN QLIVAEVLQS AEVMKAAVAY LEPHMEKAET AKKAKILLAT VKGDVHDIGK NLVEIILSNN GFEVVNLGIK VAPEVLIEAV RREEPDAIGL SGLLVKSAQQ MVVTAQDLRA AGVSLPLLVG GAALTAKFAY TRIAPEYEGL VLYAKDAMEG LEIANRLVDP EGRPELERKT AELRASLTDR PAAPAVSTGS RPRRSSVSRT VPVAVPPDCR RHLWRDYPFD HVQPYINLQM LLGRHMGLRG NVDKLLAERD PKAVEWVERL NALIAEAKGE GLLRLHAVYQ FFPSQSEGDD ILIYDPEQPG RVIERFTFPR QGREPYLCLS DYVRPVESGE MDYVAFFAVT AGAGIRDKAE EWKARGEYVK SHFLQALALE TAEAFAERLH GMIRDLWGFP DPPDMTMRER FQAKYRGIRV SFGYPACPNL EDQAKLFRLL RPEEIGIRLT DGFMMDPEAS VSALVFSHPE AVYFRADVT // ID D5X044_THIK1 Unreviewed; 354 AA. AC D5X044; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADG32472.1}; GN OrderedLocusNames=Tint_3145 {ECO:0000313|EMBL:ADG32472.1}; OS Thiomonas intermedia (strain K12) (Thiobacillus intermedius). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Thiomonas. OX NCBI_TaxID=75379 {ECO:0000313|EMBL:ADG32472.1, ECO:0000313|Proteomes:UP000002185}; RN [1] {ECO:0000313|EMBL:ADG32472.1, ECO:0000313|Proteomes:UP000002185} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 {ECO:0000313|EMBL:ADG32472.1, RC ECO:0000313|Proteomes:UP000002185}; 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; ADG32472.1; -; Genomic_DNA. DR RefSeq; WP_013124548.1; NC_014153.1. DR RefSeq; YP_003644802.1; NC_014153.1. DR EnsemblBacteria; ADG32472; ADG32472; Tint_3145. DR KEGG; tin:Tint_3145; -. DR PATRIC; 38296901; VBIThiInt85915_3178. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR BioCyc; TINT75379:GH6C-3198-MONOMER; -. DR Proteomes; UP000002185; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002185}; KW Methyltransferase {ECO:0000313|EMBL:ADG32472.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002185}; KW Transferase {ECO:0000313|EMBL:ADG32472.1}. SQ SEQUENCE 354 AA; 38065 MW; 34FC160E3EE1F88E CRC64; MQTAHPLAPK PYTRAAQLPA LLKQRIVILD GAMGTMIQRF KLSEAQYRGE RFKDWPRDVK GNNELLSLTQ PQIIRDIHEG YLAAGADLVE TNTFGATTVA QDDYGMAELV DEMNEASARL ARAACDKFST PDKPRFVAGA LGPTPKTASI SPDVNDPGAR NVDFETLRAA YAQQTRALMR GGADVILVET IFDTLNAKAA LFAVDEVFEQ TGERLPIIIS GTVTDASGRV LSGQTVTAFW ASVRHAQPLA IGLNCALGAA LMRPYLQELA KAAPDTFISC YPNAGLPNPM SDTGFDETPE VTSRLLHEFA AEGLVNIVGG CCGTTPEHIA AIQSAVKDEA PRARRRAGFY ADAD // ID D5ZP92_9ACTO Unreviewed; 304 AA. AC D5ZP92; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:EFE66325.2}; GN ORFNames=SSFG_01575 {ECO:0000313|EMBL:EFE66325.2}; OS Streptomyces ghanaensis ATCC 14672. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=566461 {ECO:0000313|EMBL:EFE66325.2}; RN [1] {ECO:0000313|EMBL:EFE66325.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 14672 {ECO:0000313|EMBL:EFE66325.2}; 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 ghanaensis ATCC 14672."; 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; DS999641; EFE66325.2; -; Genomic_DNA. DR RefSeq; WP_004981760.1; NZ_DS999641.1. DR EnsemblBacteria; EFE66325; EFE66325; SSFG_01575. DR PATRIC; 25316589; VBIStrGha89667_0344. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFE66325.2}; KW Transferase {ECO:0000313|EMBL:EFE66325.2}. SQ SEQUENCE 304 AA; 31767 MW; 519FF8CC7C327299 CRC64; MSSTPPALTD ALADGTVVLD GGMSNQLASA GHDLSDELWS ARLLAEDPEA VTAAHLAYFE AGADVAITAS YQATFEGFAR RGIGRGRAAE LLALSVECAR EAARRARAAR PLWVAASVGP YGAMLADGSE YRGRYGLSVA ELERFHRPRT EVLAAARPDV LALETIPDTD EAEALLRVLR GLGTPAWLSY SAAGDRTRAG QPLEDAFALA ADADEVIAVG VNCCTPEDAD RAVALAARVT GKPVVVYPNS GETWDTGARA WTGRPTFTAG RVAGWRESGA RLVGGCCRVG PETISAIAKA VRAT // ID D5ZRG9_9ACTO Unreviewed; 1170 AA. AC D5ZRG9; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFE70476.2}; GN ORFNames=SSFG_05719 {ECO:0000313|EMBL:EFE70476.2}; OS Streptomyces ghanaensis ATCC 14672. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=566461 {ECO:0000313|EMBL:EFE70476.2}; RN [1] {ECO:0000313|EMBL:EFE70476.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 14672 {ECO:0000313|EMBL:EFE70476.2}; 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 ghanaensis ATCC 14672."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; DS999641; EFE70476.2; -; Genomic_DNA. DR RefSeq; WP_004990250.1; NZ_DS999641.1. DR EnsemblBacteria; EFE70476; EFE70476; SSFG_05719. DR PATRIC; 25325077; VBIStrGha89667_5072. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 238 238 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 748 748 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1170 AA; 128159 MW; 770858F3680AE830 CRC64; MASLPLTPSA DSRTRVSALR EALATRVVVA DGAMGTMLQA QDPTLEDFEN LEGCNEILNL TRPDIVRSVH REYFDAGVDC VETNTFGANL TALGEYDIAE RVMELSEAGA RIAREVADEF GARDGRQRWV LGSMGPGTKL PTLGHTTFAA IRDAYQQNAE GLLAGGADAL LVETTQDLLQ TKASVIAARR AMEATGHEVP LVVSVTVETT GTMLLGSEIG AALTALEPLG IDMIGLNCAT GPAEMSEHLR YLARHARVPL SCMPNAGLPV LTADGAHYPL TPGELADAQE TFVRDYGLSL VGGCCGTTPE HLRRLVERVR DVTPPERDPR PEPGAASLYQ SVPFRQDTSY LAIGERTNAN GSKKFREAML EGRWDDCVEM AREQIREGAH MLDLCVDYVG RDGVADMEEL AGRFATASTL PIVLDSTEVD VIRAGLEKLG GRAVINSVNY EDGDGPESRF ARVARLARDH GAALVALTID EEGQARTAEK KVEIAERLID DLTGNWGIRE EDILVDCLTF TICTGQEESR KDGLATIEGI RELKRRRPRV QTTLGLSNIS FGLNPAARIL LNSVFLDECV KAGLDSAIVH ASKILPIARF SEEEVRTALD LIHDRRSEGY DPLQKLMQLF EGATAKSLKA GKAEELAALP LEERLKRRII DGERNGLEAD LDEALETRKA LDIVNDTLLD GMKVVGELFG SGQMQLPFVL QSAEVMKAAV AHLEPYMEKT DEAGKGTIVL ATVRGDVHDI GKNLVDIILS NNGYNVVNLG IKQPVSAILE AAEEHRADVI GMSGLLVKST VIMKENLEEL NQRGLAADYP VILGGAALTR AYVEQDLHEI YQGEVRYARD AFEGLRLMDA LIGIKRGVPG AKLPELRQRR VRAATVEIEE RPETGHVRSD VATDNPVPAP PFWGTRVIKG IQLKEYASWL DEGALFKGQW GLKQARTGEG PTYEELVETE GRPRLRGLLE RLQTENLLEA AVVYGYFPCV SKDDDLIILD EAGNERTRFT FPRQRRGRRL CLADFFRPEE SGETDVVGLQ VVTVGSRIGE ETARMFAANA YRDYLELHGL SVQLAEALAE YWHARVRGEL GFAGEDPAAM EDMFALKYRG ARFSLGYGAC PDLEDRAKIA DLLEPGRIGV ELSEEFQLHP EQSTDAIVIH HPEAKYFNAR // ID D6AMW7_STRFL Unreviewed; 1170 AA. AC D6AMW7; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=5-methyltetrahydrofolate:homocysteine S-methyltransferase {ECO:0000313|EMBL:EFE73394.2}; GN ORFNames=SSGG_00760 {ECO:0000313|EMBL:EFE73394.2}; OS Streptomyces roseosporus NRRL 15998. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=457431 {ECO:0000313|EMBL:EFE73394.2}; RN [1] {ECO:0000313|EMBL:EFE73394.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NRRL 15998 {ECO:0000313|EMBL:EFE73394.2}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; DS999644; EFE73394.2; -; Genomic_DNA. DR RefSeq; WP_006123392.1; NZ_DS999644.1. DR EnsemblBacteria; EFE73394; EFE73394; SSGG_00760. DR PATRIC; 25405478; VBIStrRos54375_5900. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFE73394.2}; KW Transferase {ECO:0000313|EMBL:EFE73394.2}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 237 237 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 747 747 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1170 AA; 127921 MW; 23E37629C30E402F CRC64; MASLPTSAAD SRNRAEALRE ALATRVVVAD GAMGTMLQAQ DPTLEDFENL EGCNEILNIT RPDIVRSVHE EYFAVGVDCV ETNTFGANHS AANEYEIADR IFELSESGAR IAREVADEFG AKDGRQRWVL GSIGPGTKLP SLGHTTYDIL RDGYQQNAEG LLAGGSDALI VETTQDLLQT KASIIGARRA MDALGLQVPL ICSLAFETTG VMLLGSEIGA ALTALEPLGI DLIGLNCSTG PDEMSEHLRY LARHSRTPLM CMPNAGLPVL TKDGAHFPLG PDGLADSQEH FVRDYGLSLI GGCCGTTPAH MKAVVERSQG LTPPERDPRP EPGAASLYQH IPFRQDTAYL AIGERTNANG SKKFREAMLE ARWDDCVEMA RDQIREGAHM LDLCVDYVGR DGVADMTELA GRFATASTLP IVLDSTELDV LRAGLEKLGG RAVLNSVNYE DGDGPESRFA QVSALAAEHG AALIALTIDE EGQARTVEHK VAIAERLIED LTTNWGIRES DILIDTLTFT ICTGQEESRG DGIATIGAIR ELKQRHPDVQ TTLGLSNISF GLNPAARVVL NSVFLDECVK AGLDSAIVHA SKILPIARLE EEQVKVALDL IYDRRAEGYD PLQKLMELFE GVNMKSMKAG KAEELMALPL DERLQRRIID GEKNGLEADL DEALQDTPAL DIVNNTLLEG MKVVGELFGS GQMQLPFVLQ SAEVMKSAVA HLEPHMEKSD DEGKGTIVLA TVRGDVHDIG KNLVDIILSN NGYNVVNLGI KQPVSAILEA AEEHRADVIG MSGLLVKSTV IMKENLQELN QRKMAADFPV ILGGAALTRA YVEQDLHEIY EGEVRYARDA FEGLRLMDAL IGVKRGVPGA ALPELKQRRV PKKDVAVLEV EEPEGSVRSD VSITNPIPEP PFRGTRVIKG IPLKEYASWL DEGALFKGQW GLKQNRTGDG PTYEELVETE GRPHLRGWLD HLQSNNLLEA AVVYGYFPCV SKGEDLILLH EDGSERTRFT FPRQRRGRRL CLADFFRPEE SGETDVIGLQ IVTVGSRIGE ATAELFAANS YRDYLELHGL SVQLAEALAE YWHARVRSEL GFGGEDPDDV EDMFALKYRG ARFSLGYGAC PELEDRAKIA DLLQPERIGV HLSEEFQLHP EQSTDAIVIH HPEAKYFNAR // ID D6AUB3_STRFL Unreviewed; 323 AA. AC D6AUB3; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:EFE78273.2}; GN ORFNames=SSGG_05640 {ECO:0000313|EMBL:EFE78273.2}; OS Streptomyces roseosporus NRRL 15998. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=457431 {ECO:0000313|EMBL:EFE78273.2}; RN [1] {ECO:0000313|EMBL:EFE78273.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NRRL 15998 {ECO:0000313|EMBL:EFE78273.2}; 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 ----------------------------------------------------------------------- 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; EFE78273.2; -; Genomic_DNA. DR RefSeq; WP_006128245.1; NZ_DS999644.1. DR EnsemblBacteria; EFE78273; EFE78273; SSGG_05640. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFE78273.2}; KW Transferase {ECO:0000313|EMBL:EFE78273.2}. SQ SEQUENCE 323 AA; 33621 MW; 13D68CF7896523CB CRC64; MSTGGTLADA LDAGPVLLDG GLSNQLEAQG CDLSDALWSA RLLADAPEQI EAAHLAYLRA GARVLITASY QATFEGFGRY GLDRSGTEAL FARSVELARS AADAARRAGP GRKTWVAASV GPYGAMLADG SEYRGRYGLS VGELERFHRP RVAALAAAGP DVLALETVPD LDEAEALVRV AEETGLPYWL SYSVAGGRTR AGQPLEEAFA VAAGRESVLA VGVNCCDPDE AQAAVELAVA VTGRPAVVYP NSGEGWDAGA RGWTGRSTFD PDRVRAWTRA GARLVGGCCR VGPDLIAELA GQLEKPGEPG ARGEPEKPEG VEK // ID D6AWL9_9ACTO Unreviewed; 306 AA. AC D6AWL9; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 01-OCT-2014, entry version 13. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:EFE84782.2}; GN ORFNames=SSHG_05224 {ECO:0000313|EMBL:EFE84782.2}; OS Streptomyces albus J1074. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=457425 {ECO:0000313|EMBL:EFE84782.2}; RN [1] {ECO:0000313|EMBL:EFE84782.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=J1074 {ECO:0000313|EMBL:EFE84782.2}; 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999645; EFE84782.2; -; Genomic_DNA. DR EnsemblBacteria; EFE84782; EFE84782; SSHG_05224. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFE84782.2}; KW Transferase {ECO:0000313|EMBL:EFE84782.2}. SQ SEQUENCE 306 AA; 31318 MW; E16A8B25006389C9 CRC64; MGGAGSFVAA LGERAVVVDG GLSEQLAARG NDLSDALWSA RLLADAPEEV VAAHRAYYAA GAEVAITASY QATFEGFARR GVGRVAAARL LGDSVGLARR AADEAREADG VTGPLWVAAS AGPYGAMLAD GSEYRGRYGL SVAELERFHR PRLEVLAAAG PDVLALETVP DADEARALLR AVRGLGVPAW LSYSVAGGRT RAGDRLADAF ALAADAPEVV AVGVNCCDPR EVEPAVRLAA HVTGKPVVAY PNSGERWDAA ARAWRGPAQP LAGLAGEWVA AGARLVGGCC RVGAQAVREV AGAVRG // ID D6BAE7_9ACTO Unreviewed; 1174 AA. AC D6BAE7; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 27-MAY-2015, entry version 35. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFE80334.2}; GN ORFNames=SSHG_00776 {ECO:0000313|EMBL:EFE80334.2}, GN XNR_5171 {ECO:0000313|EMBL:AGI91487.1}; OS Streptomyces albus J1074. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=457425 {ECO:0000313|EMBL:EFE80334.2, ECO:0000313|Proteomes:UP000012184}; RN [1] {ECO:0000313|EMBL:EFE80334.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=J1074 {ECO:0000313|EMBL:EFE80334.2}; 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] {ECO:0000313|EMBL:AGI91487.1, ECO:0000313|Proteomes:UP000012184} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=J1074 {ECO:0000313|EMBL:AGI91487.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP004370; AGI91487.1; -; Genomic_DNA. DR EMBL; DS999645; EFE80334.2; -; Genomic_DNA. DR RefSeq; WP_003947215.1; NZ_DS999645.1. DR RefSeq; YP_007748490.1; NC_020990.1. DR EnsemblBacteria; AGI91487; AGI91487; XNR_5171. DR EnsemblBacteria; EFE80334; EFE80334; SSHG_00776. DR GeneID; 15148995; -. DR KEGG; salb:XNR_5171; -. DR PATRIC; 29730956; VBIStrAlb121414_5823. DR KO; K00548; -. DR Proteomes; UP000012184; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000012184}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 239 239 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 751 751 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1174 AA; 127830 MW; 3F71D890AE67BFE1 CRC64; MASSPTHRTA LSAAARADAL REALATRVVV ADGAMGTMLQ AQDPTLDDFQ QLEGCNEILN LTRPDIVTSV HDAYFAVGVD CVETNTFGAN HAALGEYDIP ERVFELSEAG ARVARESADR FTVETGQQRW VLGSMGPGTK LPTLGHAPYT TLRDAYQRNA EGMIAGGADA LLVETTQDLL QTKASVIGAR RALEATGANL PVIVSVTVET TGTMLLGSEI GAALTALEPL GIDMIGLNCA TGPAEMSEHL RHLARHSRVP ISCMPNAGLP VLGKDGAHYP LTASELADAQ EGFVREYGLS LVGGCCGTTP EHLRQVVERV RGAVPGERDP RPEPGAASLY QTVPFRQDTS YLAIGERTNA NGSKKFRTAM LEGRWDDCVE MAREQIREGA HLLDLCVDYV GRDGVADMTE LAGRFATAST LPLVLDSTEV DVLRAGLEKL GGRAVINSVN YEDGDGPDSR FAKVTALAQE HGAALMALTI DEEGQARTTE HKVAVAERLI EDLTGNWGIH ESDILIDTLT FTICTGQEES RRDGVHTIEA IRELKRRHPD VQTTLGLSNI SFGLNPAARI VLNSVFLDEC VKAGLDSAIV HASKILPIAR LEEEHVKVAL DLIHDRRSEG YDPLQTFLEL FEGVDTKSMK AGKAEELLAL PLDERLKRRI IDGEKNGLHE DLDEALTERP ALDIVNDTLL DGMKVVGELF GSGQMQLPFV LQSAEVMKDA VAHLEPHMEK AEGDEEGKGT IVLATVRGDV HDIGKNLVDI ILSNNGYNVV NLGIKQPVSA ILEAAEEHRA DVIGMSGLLV KSTVIMKENL EELNQRGLAS GYPVILGGAA LTRAYVEQDL HEIYEGEVRY ARDAFEGLRL MDALIAVKRG VPGATLPELK QRRVRATASA TVTEEREEGP VRSETATDNP VPTPPFWGTR VAKGIPLKDY ASWLDEGALF KGQWGLKQNR AGDGPSYEEL VETEGRPRLR GWLDELHTRN LLEAAVIHGY FPCVSKGDDL IVLDDAGNER TRFSFPRQRR GKRLCLADFF RPEESGESDV VGFQVVTVGS RIGEATAELF AANSYRDYLE LHGLSVQLAE ALAEYWHARV RAELGFGGED PVDVEDMFAL KYRGARFSLG YGACPNLEDR AKIADLLQPE RIGVHLSEEF QLHPEQSTDA IVIHHPEAKY FNAR // ID D6BEM0_FUSNU Unreviewed; 1081 AA. AC D6BEM0; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFD80617.2}; GN ORFNames=PSAG_00652 {ECO:0000313|EMBL:EFD80617.2}; OS Fusobacterium nucleatum subsp. animalis D11. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=556264 {ECO:0000313|EMBL:EFD80617.2}; RN [1] {ECO:0000313|EMBL:EFD80617.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=D11 {ECO:0000313|EMBL:EFD80617.2}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; EQ999804; EFD80617.2; -; Genomic_DNA. DR RefSeq; WP_009006830.1; NZ_EQ999804.1. DR EnsemblBacteria; EFD80617; EFD80617; PSAG_00652. DR PATRIC; 28733522; VBIFusSp99290_0614. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 723 723 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1081 AA; 120858 MW; 979F5EA21472F528 CRC64; MFEIEKDLKE RILVLDGAMG TVLQKYELSA EDFNGAKGCY EILNESRPDI IFEVHKKYIE AGADIIETNS FNCNSISLKD YHLEDKVYDL AKKSAEIARD AVKESGKKVY IFGSVGPTNK SLSFPVGDTP FKRAVSFDEM KEVIKVQVAG LIDGGVDGIL LETIFDGLTA KAALLATEEV FKEKNIKLPI SISATVNKQG KLLTGQSMES LIVALDRDSV TSFGFNCSFG AKDLVPLVIK IKELTTKFVT LHANAGLPNQ NGDYVETAQK MKNDLLPLIE NQAINILGGC CGTSYDHIKA IAELVKGQKP RVFPEKNLLE TCLSGNEIYN FKDKFTCVGE RNNISGSKLF RTMIEEHNYL KALDVARQQI DAGAKVLDIN VDDAILDSVE EMKNFLRVLQ NDSFIAKVPI MIDSSDFAVI EEGLKNTVGK AIVNSISLKE GEENFLRKAK ITRKYGASII VMAFDENGQG VSAERKIEIC QRAYNLLKSI GIKNSDIVFD PNILSVGTVQ EADRYHAREF LKTIDYIHKN LKGCGIVGGL SNLSFAFRGN NILRAAFHHI FLEEAIPRGF NFAILNPKEK APQWTDEERE KIKSFIFGDS TNIEDLLSLN LVKRKEDAQI FAETPEDRIR KALIQGGSES LQEVIEELLK KYKALEILEN ILMSAMQEIG RLFEQGELYL PQLIRSASVM NNCVNILTPY LEKVDRTSSK GKILMATVDG DVHDIGKNIV KTVLECNGYE VIDLGVMVPR KKIVEVAKNN NVDIVTLSGL ISPSLKEMER VADSFQKVGM QIPILIAGAA TSKLHTGLKV LPNYDYSLHV TDAMDTITVV SQLLSTKRKD FLEAKQNQLR KIAKRYIENN DQTGEKKVLP EVKKTVSYIP KVLGKQFLSL PVEILKDDLK WDIAFYALRV KNTPEEEKTL NDLKKIYEKL IEEKVEFRAA YGYFRCKKTE TFLEIEGMTF EVSPNIAQYI EKEDYLGAFV VSVKSEIFKD DKYLGLLETL LCNVIAEAAS EYMERRVSKD IVPTFLRPAV GYPILPDHSL KKVVFDLIDG EKTGAKLSPA FAMSPLSSVC GFYLCNDNAK Y // ID D6CP78_THIA3 Unreviewed; 354 AA. AC D6CP78; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=Thiomonas sp. str. 3As chromosome, complete genome {ECO:0000313|EMBL:CAZ90356.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAZ90356.1}; GN OrderedLocusNames=THI_3781 {ECO:0000313|EMBL:CAZ90356.1}; OS Thiomonas arsenitoxydans (strain DSM 22701 / CIP 110005 / 3As). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Thiomonas. OX NCBI_TaxID=426114 {ECO:0000313|EMBL:CAZ90356.1, ECO:0000313|Proteomes:UP000002372}; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3As; RA Genoscope - CEA; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000002372} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22701 / CIP 110005 / 3As RC {ECO:0000313|Proteomes:UP000002372}; 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; CAZ90356.1; -; Genomic_DNA. DR RefSeq; WP_013107565.1; NC_014145.1. DR RefSeq; YP_003626124.1; NC_014145.1. DR EnsemblBacteria; CAZ90356; CAZ90356; THI_3781. DR KEGG; thi:THI_3781; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR BioCyc; TARS426114-WGS:GSYJ-3641-MONOMER; -. DR Proteomes; UP000002372; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002372}; KW Methyltransferase {ECO:0000313|EMBL:CAZ90356.1}; KW Transferase {ECO:0000313|EMBL:CAZ90356.1}. SQ SEQUENCE 354 AA; 38049 MW; 005A9D30C4DF0E33 CRC64; MQTAHPPAPK PYTRAAQLPA LLKQRIVILD GAMGTMIQRF KLSEAQYRGE RFKDWPRDVK GNNELLSLTQ PQIIRDIHEG YLAAGADLVE TNTFGATTVA QDDYGMAELV DEMNEASARL ARAACDKFST PDKPRFVAGA LGPTPKTASI SPDVNDPGAR NVDFETLRAA YAQQTRALMR GGADVILVET IFDTLNAKAA LFAVDEVFEQ TGERLPIIIS GTVTDASGRV LSGQTVTAFW ASVRHAQPLA IGLNCALGAA LMRPYLQELA KAAPDTFISC YPNAGLPNPM SDTGFDETPE VTSRLLHEFA AEGLVNIVGG CCGTTPEHIA AIQSAVKDEA PRARRRAGFY ADAD // ID D6D3U0_9BACE Unreviewed; 915 AA. AC D6D3U0; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=Bacteroides xylanisolvens XB1A draft genome {ECO:0000313|EMBL:CBK69092.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CBK69092.1}; GN ORFNames=BXY_41870 {ECO:0000313|EMBL:CBK69092.1}; OS Bacteroides xylanisolvens XB1A. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=657309 {ECO:0000313|EMBL:CBK69092.1, ECO:0000313|Proteomes:UP000008795}; RN [1] {ECO:0000313|EMBL:CBK69092.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=XB1A {ECO:0000313|EMBL:CBK69092.1}; 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. RN [2] {ECO:0000313|EMBL:CBK69092.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=XB1A {ECO:0000313|EMBL:CBK69092.1}; RA Pajon A.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; FP929033; CBK69092.1; -; Genomic_DNA. DR RefSeq; WP_015532797.1; NC_021017.1. DR EnsemblBacteria; CBK69092; CBK69092; BXY_41870. DR KEGG; bxy:BXY_41870; -. DR PATRIC; 42760871; VBIBacXyl109951_3177. DR KO; K00548; -. DR Proteomes; UP000008795; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008795}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CBK69092.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008795}; KW Transferase {ECO:0000313|EMBL:CBK69092.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 915 AA; 99884 MW; FC37141F06D82B15 CRC64; MKKTISQVVS ERILILDGAM GTMIQQYNLK EEDFRGERFA HIPGQLKGNN DLLCLTRPDV IQDIHRKYLE AGADIIETNT FSSTTVSMAD YHVEEYVREM NLAAVKLARD LADEYTAKNP DKPRFVAGSV GPTNKTCSMS PDVNNPAYRA LSYDELAASY QQQMEAMLEG GVDAILIETI FDTLNAKAAI FAAEQAMKAT GVEVPVMLSV TVSDIGGRTL SGQTLDAFLA SVQHANIFSV GLNCSFGARQ LKPFLEQLAA RAPYYISAYP NAGLPNSLGK YDQTPADMAH EVREYIEEGL INIIGGCCGT TDAYIAEYPA LVKGAKPHVP ALAPDCMWLS GLELLEVKPE INFVNVGERC NVAGSRKFLR LVNEKKYDEA LSIARQQVED GALVIDVNMD DGLLDAKTEM TTFLNLIMSE PEIARVPVMI DSSKWEVIEA GLKCLQGKSI VNSISLKEGE DVFLEHARII RQYGAAAVVM AFDEKGQADT AARKIEVCER AYRLLVDKVG FNPHDIIFDP NVLAVATGIE EHNNYAVDFI EATAWIKKNL PGAHISGGVS NLSFSFRGNN YIREAMHAVF LYHAIQRGMD MGIVNPGTSV LYSDIPTDVL EKIEDVVLNR RPDAAERLIE LAESLKATMS GTAGQPAAKQ DAWREESVQE RLKYALMKGI GDFLEQDLAE ALPLYDKAVD VIEGPLMDGM NYVGELFGAG KMFLPQVVKT ARTMKKAVAI LQPIIESEKV EGSAAAGKVL LATVKGDVHD IGKNIVAVVM ACNGYDIVDL GVMVPAETIV QRAIEEKVDM IGLSGLITPS LEEMAHVALE LEKAGLDIPL LIGGATTSKM HTALKIAPVY HAPVVHLKDA SQNASVASKL LNPQLKAELV NELNSEYEVL REKSGLLKRE TVSLEEAQKN KLNLF // ID D6DIA6_CLOSC Unreviewed; 835 AA. AC D6DIA6; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=Draft genome {ECO:0000313|EMBL:CBK77430.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CBK77430.1}; GN ORFNames=CLS_19140 {ECO:0000313|EMBL:CBK77430.1}; OS [Clostridium] cf. saccharolyticum K10. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=717608 {ECO:0000313|EMBL:CBK77430.1, ECO:0000313|Proteomes:UP000008797}; RN [1] {ECO:0000313|EMBL:CBK77430.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=K10 {ECO:0000313|EMBL:CBK77430.1}; 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. RN [2] {ECO:0000313|EMBL:CBK77430.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=K10 {ECO:0000313|EMBL:CBK77430.1}; RA Pajon A.; 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; FP929037; CBK77430.1; -; Genomic_DNA. DR RefSeq; WP_015573810.1; NC_021047.1. DR EnsemblBacteria; CBK77430; CBK77430; CLS_19140. DR KEGG; cso:CLS_19140; -. DR PATRIC; 42837834; VBICloCf158569_3559. DR KO; K00548; -. DR Proteomes; UP000008797; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008797}; KW Methyltransferase {ECO:0000313|EMBL:CBK77430.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008797}; KW Transferase {ECO:0000313|EMBL:CBK77430.1}. SQ SEQUENCE 835 AA; 90280 MW; D03E0780FFBAE0BE CRC64; MSIAERQTGK KSRLLHELAE RILFFDGGTG SLLQAAGLKP GELPETWNIR RPEVIVKLHR DYLDAGCDII NTNTFGANRL KFNENTEFGL KEIIEAAVRN AREAVNLAGH GYIALDLGPT GRLLKPMGDL DFETAVEIYR EAAGIGIRAG VDLVLIETMS DSYELKAAVL GVKEALAGDG ISGEQADLPV FATTIFDEKG KLLTGGTPRT VIALLEGLGV DAVGINCGLG PVQMKEFVRE FAKYASVPII VNPNAGLPRS VEGRTVYDID EDQFAKTMAE IVDMGASVVG GCCGTTPEYI RKLCLACREK KQKLPSKKAE TVVTSYSQLV EIASDPVIIG ERINPTGKPK FKQALRDHDM EYILREGLAQ QDSGAQVLDV NVGLPEIDEP SMMEEAVREL QSILDLPLQI DTSNIEAMER AMRIYNGKPL INSVNGKAES MDAIFPLVKK YGGVVVALTL DEEGIPDTAD GRIRVAEKIY RRAAQYGIDK KDILIDTLCM TISSDSQGAL TTLEAVRRIR DELHGKTILG VSNVSFGLPQ RESINAAFFT MAMMNGLSAA IINPNSDAMM RSWRSFRALA ALDENCGDYI SAYGGQTKQQ PSDTVFGKGE AVSEKAPEEV QEIHESHKSQ VQLWESVVRG LKEQAARAAA AALKEASPLE VINACMIPAL DCVGKGFEQG TVFLPQLLMS AEAAKAAFEV LKAAMAGSGN SQEKKGVIIL ATVRGDIHDI GKNIVKVLLE NYSYEVVDLG KDVPPERIAE ETVKHRAPLV GLSALMTTTV PSMEETIRLL RKEAGWAKIM VGGAVLTPEY ADSIGADAYC KDAMASVNYA QKVIG // ID D6E430_9FIRM Unreviewed; 816 AA. AC D6E430; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Eubacterium rectale DSM 17629 draft genome {ECO:0000313|EMBL:CBK90170.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CBK90170.1}; GN ORFNames=EUR_10190 {ECO:0000313|EMBL:CBK90170.1}; OS Eubacterium rectale DSM 17629. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium. OX NCBI_TaxID=657318 {ECO:0000313|EMBL:CBK90170.1, ECO:0000313|Proteomes:UP000007057}; RN [1] {ECO:0000313|EMBL:CBK90170.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17629 {ECO:0000313|EMBL:CBK90170.1}; 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 A1-86 (DSM 17629)."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CBK90170.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17629 {ECO:0000313|EMBL:CBK90170.1}; RA Pajon A.; 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; CBK90170.1; -; Genomic_DNA. DR RefSeq; WP_015516174.1; NC_021010.1. DR ProteinModelPortal; D6E430; -. DR EnsemblBacteria; CBK90170; CBK90170; EUR_10190. DR KEGG; ert:EUR_10190; -. DR PATRIC; 42982791; VBIEubRec131464_0761. DR KO; K00548; -. DR BioCyc; EREC657318-WGS:GSNC-921-MONOMER; -. DR Proteomes; UP000007057; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007057}; KW Methyltransferase {ECO:0000313|EMBL:CBK90170.1}; KW Transferase {ECO:0000313|EMBL:CBK90170.1}. SQ SEQUENCE 816 AA; 88806 MW; 9080BA134491DCDF CRC64; MTREEFRKYI RENIVILDGA TGTNLMAAGM PVGVCPEKWV MEHPQVILDL QKAYVDNGTN IVYAPTFTGN RIKLLEYGLQ EKINEINTTL VGLSKQAVGD RALVAADMTM TGRQLFPLGD LMFEELLEVY KEQARILDAA GADVFVVETM MSLQECRAAV LAIKEVSDLP IMVTLTYNED GRTLFGTPPE TAVVVLQSLG VDAIGVNCST GPTEMIALVE KMAEYSTVPL IAKPNAGLPE LEDGKTVYKM TPDMFADAMR GLVEAGASIV GGCCGTTPEH IRALTEAVKS MPVHKPLEHH RRVLASERKN VEIDLDGNFT VVGERINPTG KKKLQAQLRE GKLDLVRQMA MEQETNGARI LDINMGMNGI DEKEMMKSVI YEVSSTVDCP LCIDSSYVEV IEEALKIYPG RALINSISLE TEKMEKLLPL AAKYGAMFIL LPLSDAGLPK DVEEKKQIIN TIYDKALSLG MAHEDIVVDG LVATIGANPK AAIECYETIA YCKDEKKLPT ICGLSNISFG LPERMYVNTA FLTMAICKGL TMAIANPSQE LLMNAAFASD MLLDRPDSDI AYIERMSRLA EEKAQYETVV VKKSDNAASA SNGTCAAGGK DAVFQAVLKG NKGSIIDEVK KMLSDGAKPD EIINNSLIPA INEVGELFNQ KKYFLPQLIG SANTMKLAIE HLEPLLEKKD SGDDMPTLVI ATVEGDIHDI GKNLVVLMLK NYGYNVIDMG KDVPCEDIVN KAIETNAAVI GLSALMTTTM MRMKDVVEIC KEKGCKSKVV IGGACITQSF ADEIGADGYS KDAAECVKLV ERLLNS // ID D6EKS1_STRLI Unreviewed; 304 AA. AC D6EKS1; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 29-APR-2015, entry version 18. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:AIJ12505.1}; GN ORFNames=SLIV_07450 {ECO:0000313|EMBL:AIJ12505.1}; OS Streptomyces lividans TK24. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=457428 {ECO:0000313|EMBL:AIJ12505.1, ECO:0000313|Proteomes:UP000028682}; RN [1] {ECO:0000313|EMBL:AIJ12505.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TK24 {ECO:0000313|EMBL:AIJ12505.1}; RG StrepSynth; RA Ruckert C., Fridjonson O.H., Lambert C., van Wezel G.P., Bernaerts K., RA Anne J., Economou A., Kalinowski J.; RT "Complete genome sequence of Streptomyces lividans TK24."; RL Submitted (AUG-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; CP009124; AIJ12505.1; -; Genomic_DNA. DR RefSeq; WP_003972785.1; NZ_GG657756.1. DR EnsemblBacteria; AIJ12505; AIJ12505; SLIV_07450. DR EnsemblBacteria; EFD65851; EFD65851; SSPG_01491. DR PATRIC; 25365435; VBIStrLiv48540_6949. DR Proteomes; UP000028682; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000028682}; KW Methyltransferase {ECO:0000313|EMBL:AIJ12505.1}; KW Transferase {ECO:0000313|EMBL:AIJ12505.1}. SQ SEQUENCE 304 AA; 32335 MW; D09D163E3D828BAD CRC64; MTSDFADALA SGPLVLDGGL SNQLEAAGHD LGDALWSARL LAEDPEAITR AHLAYFEAGA EVAITSSYQA TFEGFARRGI GRERAAELLA LSVASAREAA RRARTARPER ALWVAASAGP YGAMLADGSE YRGRYGLGRG ALERFHRPRL EVLAAARPDV LALETVPDTD EAAALLRAVR GLDVPAWLSY TVAGDRTRAG QPLDEAFALA ADADEVIAVG VNCCAPEDVS GAVETAARVT GKPVVAYPNS GETWDARSRG WRGRSSYTAE RVRDWWERGA RLVGGCCRVG PETITSIARA LPRE // ID D6ENK0_STRLI Unreviewed; 1170 AA. AC D6ENK0; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 29-APR-2015, entry version 29. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AIJ16791.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AIJ16791.1}; GN Name=metH {ECO:0000313|EMBL:AIJ16791.1}; GN ORFNames=SLIV_29460 {ECO:0000313|EMBL:AIJ16791.1}; OS Streptomyces lividans TK24. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=457428 {ECO:0000313|EMBL:AIJ16791.1, ECO:0000313|Proteomes:UP000028682}; RN [1] {ECO:0000313|EMBL:AIJ16791.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TK24 {ECO:0000313|EMBL:AIJ16791.1}; RG StrepSynth; RA Ruckert C., Fridjonson O.H., Lambert C., van Wezel G.P., Bernaerts K., RA Anne J., Economou A., Kalinowski J.; RT "Complete genome sequence of Streptomyces lividans TK24."; RL Submitted (AUG-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; CP009124; AIJ16791.1; -; Genomic_DNA. DR RefSeq; WP_003977168.1; NZ_GG657756.1. DR EnsemblBacteria; AIJ16791; AIJ16791; SLIV_29460. DR EnsemblBacteria; EFD70257; EFD70257; SSPG_05897. DR PATRIC; 25374563; VBIStrLiv48540_4149. DR Proteomes; UP000028682; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000028682}; KW Methyltransferase {ECO:0000313|EMBL:AIJ16791.1}; KW Transferase {ECO:0000313|EMBL:AIJ16791.1}. SQ SEQUENCE 1170 AA; 128290 MW; 703E8D01EBD5E29B CRC64; MASSPSTPPA NTRTRVSALR EALATRVVVA DGAMGTMLQA QNPTLDDFQQ LEGCNEVLNL TRPDIVRSVH EEYFAAGVDC VETNTFGANH SALGEYDIPE RVHELSEAGA RVAREVADEF GARDGRQRWV LGSMGPGTKL PTLGHAPYTV LRDAYQRNAE GLVAGGADAL LVETTQDLLQ TKASVLGARR ALDALGLDLP LIVSVTVETT GTMLLGSEIG AALTALEPLG IDMIGLNCAT GPAEMSEHLR YLARHSRIPL TCMPNAGLPV LGKDGAHYPL TAPELADAHE TFVREYGLSL VGGCCGTTPE HLRQVVERVR DTAPTARDPR PEPGAASLYQ TVPFRQDTSY LAIGERTNAN GSKKFREAML DGRWDDCVEM VRDQIREGAH MLDLCVDYVG RDGVADMEEL AGRFATASTL PIVLDSTEVD VIRAGLEKLG GRAVINSVNY EDGAGPESRF ARVTKLAREH GAALIALTID EVGQARTAEK KVEIAERLID DLTGNWGIHE SDILVDCLTF TICTGQEESR KDGLATIEGI RELKRRHPDV QTTLGLSNIS FGLNPAARIL LNSVFLDECV KAGLDSAIVH ASKILPIARF DEEQVTTALD LIYDRRREGY DPLQKLMQIF EGATAKSLKA SKAEELAALP LEERLKRRII DGEKNGLEQD LDEALRERPA LEIVNDTLLD GMKVVGELFG SGQMQLPFVL QSAEVMKTAV AHLEPHMEKT DDDGKGTIVL ATVRGDVHDI GKNLVDIILS NNGYNVVNLG IKQPVSAILE AADEHRADVI GMSGLLVKST VIMKENLEEL NQRKLAADYP VILGGAALTR AYVEQDLHEI YDGEVRYARD AFEGLRLMDA LIGIKRGVPG AKLPELKQRR VRAATVEIDE RPEEGHVRSD VATDNPVPTP PFRGTRVVKG IQLKEYASWL DEGALFKGQW GLKQARTGEG PSYEELVESE GRPRLRGLLD RLQTDNLLEA AVVYGYFPCV SKDDDLIVLD DDGNERTRFT FPRQRRGRRL CLADFFRPEE SGETDVVGFQ VVTVGSRIGE ETARMFEANA YRDYLELHGL SVQLAEALAE YWHARVRSEL GFAGEDPAEM EDMFALKYRG ARFSLGYGAC PDLEDRAKIA ALLEPERIGV HLSEEFQLHP EQSTDAIVIH HPEAKYFNAR // ID D6FI18_MYCTX Unreviewed; 497 AA. AC D6FI18; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|EMBL:EFD17909.1}; DE Flags: Fragment; GN ORFNames=TBNG_03692 {ECO:0000313|EMBL:EFD17909.1}; OS Mycobacterium tuberculosis CPHL_A. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=611303 {ECO:0000313|EMBL:EFD17909.1}; RN [1] {ECO:0000313|EMBL:EFD17909.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CPHL_A {ECO:0000313|EMBL:EFD17909.1}; 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 CPHL_A."; 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; GG663498; EFD17909.1; -; Genomic_DNA. DR EnsemblBacteria; EFD17909; EFD17909; TBNG_03692. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFD17909.1}; KW Transferase {ECO:0000313|EMBL:EFD17909.1}. FT NON_TER 497 497 {ECO:0000313|EMBL:EFD17909.1}. SQ SEQUENCE 497 AA; 53061 MW; 6171D6C841E6B816 CRC64; MLNETRPDVL ETIHRNYFEA GADAVETNTF GCNLSNLGDY DIADRIRDLS QKGTAIARRV ADELGSPDRK RYVLGSMGPG TKLPTLGHTE YAVIRDAYTE AALGMLDGGA DAILVETCQD LLQLKAAVLG SRRAMTRAGR HIPVFAHVTV ETTGTMLLGS EIGAALTAVD PLGVDMIGLN CATGPAEMSE HLRHLSRHAR IPVSVMPNAG LPVLGAKGAE YPLLPDELAE ALAGFIAEFG LSLVGGCCGT TPAHIREVAA AVANIKRPER QVSYEPSVSS LYTAIPFAQD ASVLVIGERT NANGSKGFRE AMIAEDYQKC LDIAKDQTRD GAHLLDLCVD YVGRDGVADM KALASRLATS STLPIMLDST ETAVLQAGLE HLGGRCAINS VNYEDGDGPE SRFAKTMALV AEHGAAVVAL TIDEEGQART AQKKVEIAER LINDITGNWG VDESSILIDT LTFTIATGQE ESRRDGIETI EAIRELKKRH PDVQTTL // ID D6FJ19_MYCTX Unreviewed; 302 AA. AC D6FJ19; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Homocysteine S-methyltransferase mmuM {ECO:0000313|EMBL:EFD18260.1}; GN ORFNames=TBNG_04043 {ECO:0000313|EMBL:EFD18260.1}; OS Mycobacterium tuberculosis CPHL_A. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=611303 {ECO:0000313|EMBL:EFD18260.1}; RN [1] {ECO:0000313|EMBL:EFD18260.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CPHL_A {ECO:0000313|EMBL:EFD18260.1}; 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 CPHL_A."; 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; GG663498; EFD18260.1; -; Genomic_DNA. DR RefSeq; WP_003412639.1; NZ_KK338573.1. DR ProteinModelPortal; D6FJ19; -. DR EnsemblBacteria; EFD18260; EFD18260; TBNG_04043. DR EnsemblBacteria; KBF62169; KBF62169; BO02_01360. DR PATRIC; 26060055; VBIMycTub38905_3310. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFD18260.1}; KW Transferase {ECO:0000313|EMBL:EFD18260.1}. SQ SEQUENCE 302 AA; 31533 MW; D8174BFD6FDE55BD CRC64; MELVSDSVLI SDGGLATELE ARGHDLSDPL WSARLLVDAP HAITAVHTAY FRAGAQIATT ASYQASFEGF AARGIGHDDA TVLLRRSVEL AQAARDEVGV GGLSVAASVG PYGAALADGS EYRGCYGLSV AALMKWHLPR LEVLVDAGAD MLALETIPDI DEAEALVNLV RRLATPAWLS YTINGTRTRA GQPLTDAFAV AAGVPEIVAV GVNCCAPDDV LPAIAFAVAH TGKPVIVYPN SGEGWDGRRR AWVGPRRFSG SSGQLAREWV AAGARIVGGC CRVRPIDIAE IGRALTTAPP RG // ID D6I3Q6_ECOLX Unreviewed; 1227 AA. AC D6I3Q6; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 27-MAY-2015, entry version 30. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFE60217.2}; GN ORFNames=ECCG_02638 {ECO:0000313|EMBL:EFE60217.2}; OS Escherichia coli B088. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=550672 {ECO:0000313|EMBL:EFE60217.2}; RN [1] {ECO:0000313|EMBL:EFE60217.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=B088 {ECO:0000313|EMBL:EFE60217.2}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG749153; EFE60217.2; -; Genomic_DNA. DR RefSeq; WP_000096010.1; NZ_GG749153.1. DR ProteinModelPortal; D6I3Q6; -. DR SMR; D6I3Q6; 651-1227. DR EnsemblBacteria; EFE60217; EFE60217; ECCG_02638. DR PATRIC; 35861519; VBIEscCol142334_4093. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135969 MW; 31A0CAA1E9127CD9 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID D6IGV2_ECOLX Unreviewed; 1227 AA. AC D6IGV2; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFF03233.2}; GN ORFNames=ECDG_02432 {ECO:0000313|EMBL:EFF03233.2}; OS Escherichia coli B185. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=550676 {ECO:0000313|EMBL:EFF03233.2}; RN [1] {ECO:0000313|EMBL:EFF03233.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=B185 {ECO:0000313|EMBL:EFF03233.2}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG749190; EFF03233.2; -; Genomic_DNA. DR RefSeq; WP_000096025.1; NZ_GG749190.1. DR EnsemblBacteria; EFF03233; EFF03233; ECDG_02432. DR PATRIC; 35871435; VBIEscCol145366_4275. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136049 MW; F03A2CAA1484F834 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKHIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID D6J4Z8_ECOLX Unreviewed; 1227 AA. AC D6J4Z8; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFF14480.2}; GN ORFNames=ECEG_02665 {ECO:0000313|EMBL:EFF14480.2}; OS Escherichia coli B354. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=550677 {ECO:0000313|EMBL:EFF14480.2}; RN [1] {ECO:0000313|EMBL:EFF14480.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=B354 {ECO:0000313|EMBL:EFF14480.2}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG749326; EFF14480.2; -; Genomic_DNA. DR RefSeq; WP_000096062.1; NZ_GG749326.1. DR EnsemblBacteria; EFF14480; EFF14480; ECEG_02665. DR PATRIC; 35872749; VBIEscCol143929_0008. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136027 MW; 675F26160C078038 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MTRAVEGLAP RKLPEIPVAC RLSGLEPLSI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID D6JRT8_ACIPI Unreviewed; 1228 AA. AC D6JRT8; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EFF87853.2}; GN ORFNames=HMPREF0013_01056 {ECO:0000313|EMBL:EFF87853.2}; OS Acinetobacter sp. SH024. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=575565 {ECO:0000313|EMBL:EFF87853.2, ECO:0000313|Proteomes:UP000004924}; RN [1] {ECO:0000313|Proteomes:UP000004924} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG753600; EFF87853.2; -; Genomic_DNA. DR RefSeq; WP_005802991.1; NZ_GG753600.1. DR EnsemblBacteria; EFF87853; EFF87853; HMPREF0013_01056. DR PATRIC; 36269443; VBIAciSp53575_0572. DR Proteomes; UP000004924; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000004924}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1228 AA; 135576 MW; CAD3E7CEE8BA379D CRC64; MSTLATLKAL LAKRILIIDG AMGTMIQRHK LEEADYRGER FADWAHDLKG NNDLLVLTQP QIIQGIHEAY LDAGADIIET NSFNGTRVSM SDYHMEDLVP EINREAARLA KAACEKYSTP EKPRFVAGVL GPTSRTCSIS PNVNDPAFRN ITFDELKENY IEATHALIEG GADIILIETV FDTLNCKAAI FAVKEVFKEI GRELPIMISG TITDASGRTL TGQTAEAFWN SVRHGDLLSI GFNCALGADA MRPHVKTISD VADTFVSAHP NAGLPNAFGE YDETPEQTAA FLKEFAESGL INITGGCCGT TPDHIRAIAN AVKDIAPRQV PETVPACRLS GLEPFNIYDD SLFVNVGERT NVTGSKKFLR LIREENFAEA LEVAQQQVEA GAQIIDINMD EGMLDSQNAM VHFLNLVASE PDISRVPIMI DSSKWEIIEA GLKCVQGKPV VNSISLKEGY DEFVEKARLC RQYGAAIIVM AFDETGQADT AARKREICKR SYDILVNDVG FPAEDIIFDP NVFAVATGIE EHNNYGVDFI EATGWIKQNL PHAMISGGVS NVSFSFRGNE PVREAIHSVF LYHAIKQGMT MGIVNAGQMA IYDDIPAELK QAVEDVILNQ NQGESGQAAT EKLLEVAEKY RGQGGATKEA ENLEWRNESV EKRLEYALVK GITTYIDEDT EEARLKAKRP LDVIEGALMD GMNVVGDLFG SGKMFLPQVV KSARVMKQAV AWLNPYIEAE KTGSQSKGKV LMATVKGDVH DIGKNIVGVV LGCNGYDIVD LGVMVPCEKI LQTAIDEKCD IIGLSGLITP SLDEMVFVAK EMQRKGFNIP LLIGGATTSK AHTAVKIDPQ YQNDAVIYVA DASRAVGVAT TLLSKEMRGN FIAEHRAEYA KIRERLANKQ PKAAKLTYAE SVENGFKIDE SYVPPKPNLL GTQVLTNYPL ATLVEYFDWT PFFISWSLAG KFPKILEDEV VGEAATDLYN QAQAMLKDII DNNRFDARAV FGMFPAQRTD ADTVSVFDEA GQNVTHTFEH LRQQSDKVTG KPNLSLADYI RNDREQQDYL GGFTVSIFGA EELANEYKAK GDDYSAILVQ SLADRFAEAF AEHLHERIRK EFWGYKADEQ LSNEELIKEK YVGIRPAPGY PACPEHSEKA VLFDWLGSTD KIGTKLTEHF AMMPPSSVSG FYYSHPQSEY FNVGKISQDQ LEDYAKRKGW TLDEAKRWLA PNLDDSIV // ID D6JRY1_ACIPI Unreviewed; 292 AA. AC D6JRY1; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EFF87896.2}; GN ORFNames=HMPREF0013_01100 {ECO:0000313|EMBL:EFF87896.2}; OS Acinetobacter sp. SH024. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=575565 {ECO:0000313|EMBL:EFF87896.2, ECO:0000313|Proteomes:UP000004924}; RN [1] {ECO:0000313|Proteomes:UP000004924} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG753600; EFF87896.2; -; Genomic_DNA. DR RefSeq; WP_005803054.1; NZ_GG753600.1. DR EnsemblBacteria; EFF87896; EFF87896; HMPREF0013_01100. DR PATRIC; 36269533; VBIAciSp53575_0617. DR Proteomes; UP000004924; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000004924}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 202 202 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 275 275 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 276 276 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 292 AA; 32067 MW; 12DD35C42BC90C38 CRC64; MKILDGGLGR ELARRGAPFR QPEWSALALI EAPETVKEVH LDFINAGSEV ITTNNYAVVP FHIGQERFET DGVRLIKVAI EQAKNAVKES GKNVKIAGCL PPLFGSYRAD LFQPEQAKSL AEPIINTLAP EVDFWLAETQ SCLKEVETVH ALLPQDGKDY WVSFTLQDEI KQEQALLRSG ENMQQVAEFI KQSNAKAVLF NCCQPEVILQ AINEIKGLIP ESVQIGAYAN AFPPQDESAT ANDGLDEIRK DLDAPAYLGF AKQWQQAGAS LVGGCCGIGP EHIAELSQFF KE // ID D6K526_9ACTO Unreviewed; 309 AA. AC D6K526; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 01-OCT-2014, entry version 16. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFF93773.2}; GN ORFNames=SSTG_04092 {ECO:0000313|EMBL:EFF93773.2}; OS Streptomyces sp. e14. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=645465 {ECO:0000313|EMBL:EFF93773.2}; RN [1] {ECO:0000313|EMBL:EFF93773.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=E14 {ECO:0000313|EMBL:EFF93773.2}; 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 ----------------------------------------------------------------------- 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; EFF93773.2; -; Genomic_DNA. DR RefSeq; WP_009191314.1; NZ_GG753626.1. DR EnsemblBacteria; EFF93773; EFF93773; SSTG_04092. DR PATRIC; 35776183; VBIStrSp49670_3833. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 2. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFF93773.2}; KW Transferase {ECO:0000313|EMBL:EFF93773.2}. SQ SEQUENCE 309 AA; 32399 MW; 64D1876ABAD8D588 CRC64; MTSETSPDLA AALAAGTLVL DGGLSNQLET AGHDLGDALW SARLLAERPE AVTEAHLAYF TAGADVVITA SYQATFEGFR PARGSAGSGR PRSSRPAWTS PGTRYGGHAP RASHGRCGWP RRPGPYGAML ADGSEYRGRY GLTAGELERF HRPRLEVLAA ARPDVLALET VPDADEARAL LRAVRGLGVP AWLSYTVAGP RTRAGQPLEE AFAPAAAADE VIAVGVNCCD PEDADAAVAT AARVTGKPVV VYPNSGEAWD AGARAWSGRP SFHADRVTRW RAFGARLIGG CCRVGPETIT EIARTLSDG // ID D6K8M6_9ACTO Unreviewed; 1172 AA. AC D6K8M6; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 01-APR-2015, entry version 28. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFF90171.2}; GN ORFNames=SSTG_00489 {ECO:0000313|EMBL:EFF90171.2}; OS Streptomyces sp. e14. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=645465 {ECO:0000313|EMBL:EFF90171.2}; RN [1] {ECO:0000313|EMBL:EFF90171.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=E14 {ECO:0000313|EMBL:EFF90171.2}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG753626; EFF90171.2; -; Genomic_DNA. DR RefSeq; WP_009187749.1; NZ_GG753626.1. DR EnsemblBacteria; EFF90171; EFF90171; SSTG_00489. DR PATRIC; 35768552; VBIStrSp49670_4662. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 238 238 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 748 748 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1172 AA; 128385 MW; 88C3D80ACAB493C8 CRC64; MASLPPSPSA DSRTRVSALR EALATRVVVA DGAMGTMLQA QDPTLEDFQN LEGCNEILNV TRPDIVRSVH AAYFDAGVDC VETNTFGANH TAASEYEIAD RVHELSEAGA RLARELADEY TGRDGRTRWV LGSIGPGTKL PTLGHVGYPT IRDGYQANAE GLLAGGADAL IVETTQDLLQ TKASVLGARR AMEATGADVP LLVSMAFETT GTMLLGSEIG AALTALEPLG IDMIGLNCST GPAEMSEHLR YLTRHSRIPL LCMPNAGLPI LTKDGAHFPL DPEGLADAQE NFVRDYGLSL VGGCCGTTPE HLRRLVERVR DVAPVERDPR PEPGAASLYQ TVPFRQDTSY LAIGERTNAN GSKKFREAML EGRWDDCVEM ARDQIREGAH MLDLCVDYVG RDGVADMAEL AGRFATASTL PIVLDSTEVE VIRAGLEKLG GRAVINSVNY EDGDGPESRF AKVTALAREH GAALIALTID EEGQARTAEK KVEIAERLIE DLTGNWGIHE EDILVDCLTF TICTGQEESR KDGIATIEGI RELKRRHPKV QTTLGLSNIS FGLNPAARIL LNSVFLDECV KAGLDSAIVH ASKILPIARF DEEQVTTALD LIYDRRREGY DPLQKLMQLF EGATAKSLKA GKAEELAALP LDERLKRRII DGEKNGLEAD LDEALTQRPA LDIVNDTLLD GMKVVGELFG SGQMQLPFVL QSAEVMKTAV AHLEPHMEKS DEAGKGTIVL ATVRGDVHDI GKNLVDIILS NNGYNVVNLG IKQPVSAILE AADEHKADVI GMSGLLVKST VIMKENLEEL NQRGLAATYP VILGGAALTR AYVEQDLHEI YEGEVRYARD AFEGLRLMDA LIGVKRGVPG AKLPELKQRR VRSTAAVQVE EQRPEEGHVR SDVATDNPVP EPPFWGTRVI KGIQLKEYAS WLDEGALFKG QWGLKQARTG DGPTYEELVE TEGRPRLRGL LDRLHTENLL EAAVVYGYFP CVSKDDDLIV LDERGNERTR FTFPRQRRGR RLCLADFFRP EESGERDVVG FQVVTVGSRI GEETARLFAS DAYREYLELH GLSVQLAEAL AEYWHARVRA ELGFGGEDPA DVEDMFALKY RGARFSLGYG ACPDLEDRAK FADLLQPERI GVHLSEEFQL HPEQSTDAIV IHHPEAKYFN AR // ID D6KJ57_9FIRM Unreviewed; 811 AA. AC D6KJ57; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 01-APR-2015, entry version 21. DE SubName: Full=Vitamin B12-dependent methionine synthase family protein {ECO:0000313|EMBL:EFG22916.2}; GN ORFNames=HMPREF0873_00810 {ECO:0000313|EMBL:EFG22916.2}; OS Veillonella sp. 3_1_44. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Veillonella. OX NCBI_TaxID=457416 {ECO:0000313|EMBL:EFG22916.2}; RN [1] {ECO:0000313|EMBL:EFG22916.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_44 {ECO:0000313|EMBL:EFG22916.2}; 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG770200; EFG22916.2; -; Genomic_DNA. DR RefSeq; WP_008714555.1; NZ_GG770200.1. DR ProteinModelPortal; D6KJ57; -. DR EnsemblBacteria; EFG22916; EFG22916; HMPREF0873_00810. DR PATRIC; 36276439; VBIVeiSp18830_0817. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; SQ SEQUENCE 811 AA; 86936 MW; 652E01902A484577 CRC64; MYIFDGAMGT MLQAAGLEEG YCPELFNIER PEVVKDIHAQ YLQHGSDVIT TNTFGACGLK LEDYDLQDRV REINIAAVKV AKEAIAETKP TARVAGSMGP TGRFLQPLGN MSFDSIYDTY REQAEALIEG GVDFIIIETI IDVQEMRAAL LASLDAREAA GKTKDDVQII CQFSFSEDGR TITGTPPAVA TTIVEAIGAD IIGINCSLGP EQITPLIEEI ASVTNLPISC QPNAGMPQLI NKQTVFPLSA EEMGPLMLPI VDAGASYVGG CCGTTPAHIQ SISDAVKAHT PKERAHIAPK TIITSRTKLL ELGHHTKPLI IGERINPTGR KVLAQELRDG SFIRVKRDAL DQVEAGADIL DVNMGVAGMD QSPLMERAIF ELSMLVETPL SIDTLDPVAM EIALKNYPGR ALINSVNGEE ESITHVMPLA KRYGAALLCL PICSGDLPEK AEDRVALAES IVNRAYGYGL KPHDLLLDPL VLTLASGEDS ARQTLRTLQL YKEKFGFPTV MGLSNISFGM PQRPYLNGQF LTMALACGLT TPIMNPLNYP AKKAFVSSTT LLGWDPGSAE FIKEYGYEDE TTAPGNSAPK GPDKKSFDSN DPLANIRACV EQGEKEAIID LVKKALADGI DPLDLTKKGL SEAMNVVGDK FGSGKLFLPQ VMLAAETMQA AFNTIKEIIP ASESLDKGTV VVATVKGDIH DLGKNIVAAL LENNGYKIVD LGKDVDPEVI VQAIKDNKAA LVGICSLMTT TMPQIDNTIA AIRAAGLKTK VMVGGAVVSQ DYADQAGADI YAKDGIAAVN HANDFFETLE K // ID D6KLA6_9FIRM Unreviewed; 337 AA. AC D6KLA6; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 01-OCT-2014, entry version 14. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFG22699.2}; GN ORFNames=HMPREF0873_01579 {ECO:0000313|EMBL:EFG22699.2}; OS Veillonella sp. 3_1_44. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Veillonella. OX NCBI_TaxID=457416 {ECO:0000313|EMBL:EFG22699.2}; RN [1] {ECO:0000313|EMBL:EFG22699.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_44 {ECO:0000313|EMBL:EFG22699.2}; 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 ----------------------------------------------------------------------- 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; EFG22699.2; -; Genomic_DNA. DR RefSeq; WP_008715448.1; NZ_GG770201.1. DR EnsemblBacteria; EFG22699; EFG22699; HMPREF0873_01579. DR PATRIC; 36278013; VBIVeiSp18830_1578. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFG22699.2}; KW Transferase {ECO:0000313|EMBL:EFG22699.2}. SQ SEQUENCE 337 AA; 36673 MW; 19E21F0B3524BDF2 CRC64; MAKRSAFLDI IKEKGALVLD GALGTELERY GCDIQHKLWS AKVLMDQPDI IKKIHISYLA AGADIIQSSG YQATVAGFKG LGYGTEEAIE LVKLSVRLAV QARNEFLEAK ASGALTLRGI TLGEETPKGI RYFSEGALPK PLVAASVGPY GAFLADGSEY RGYPDVQTEY LEVFHIPRLA LFCEENPDIL SFETIPSYAE AIAIARAMSD PFTSKGIPAW IAFSCKDGHH VSSGETIIKC AQMIDKVHPI TGIGINCSKP EYVESLIKDI RTVTDKPIAV YPNLGESYDS KTKTWYGDAA SFVDYVEVWR KAGAEIIGGC CRTTPEIIGD IAKKIHN // ID D6KPH1_9FIRM Unreviewed; 811 AA. AC D6KPH1; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 01-APR-2015, entry version 21. DE SubName: Full=Vitamin B12-dependent methionine synthase family protein {ECO:0000313|EMBL:EFG24669.2}; GN ORFNames=HMPREF0874_00855 {ECO:0000313|EMBL:EFG24669.2}; OS Veillonella sp. 6_1_27. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Veillonella. OX NCBI_TaxID=450749 {ECO:0000313|EMBL:EFG24669.2}; RN [1] {ECO:0000313|EMBL:EFG24669.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=6_1_27 {ECO:0000313|EMBL:EFG24669.2}; 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; GG770216; EFG24669.2; -; Genomic_DNA. DR RefSeq; WP_008601894.1; NZ_GG770216.1. DR ProteinModelPortal; D6KPH1; -. DR EnsemblBacteria; EFG24669; EFG24669; HMPREF0874_00855. DR PATRIC; 36280400; VBIVeiSp6271_0855. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; SQ SEQUENCE 811 AA; 86934 MW; 22238914489C8A6D CRC64; MYIFDGAMGT MLQAAGLEEG YCPELFNIER PEVVKDIHAQ YLLHGSDVIT TNTFGACGLK LEDYDLQDRV REINIAAVKV AKEAIAENKP TARVAGSMGP TGRFLQPLGN MSFDSIYDTY REQAEALIEG GVDFIIIETI IDVQEMRAAL LASLDAREAA GKTKDDVQII CQFSFSEDGR TITGTPPAVA TTIVEAMGAD IIGINCSLGP EQITPLIEEI ASVTNLPISC QPNAGMPQLI NKQTVFPLTA EEMGPLMLAI VDAGASYVGG CCGTTPAHIQ SISNAVKAHT PKERAHIAPK TIITSRTKLL ELGHHTKPLI IGERINPTGR KVLAQELRDG SFIRVKRDAL DQVEAGADIL DVNMGVAGMD QSPLMERAIF ELSMLVETPL SIDTLDPAAM EIALKNYPGR ALINSVNGEE ESITHVMPLA KRYGAALLCL PICSGDLPEK AEDRVALAES IVNRAYGYGL HPHDLLLDPL VLTLASGEDS ARQTLRTLQL YKEKFGFPTV MGLSNISFGM PQRPYLNGQF LTMALACGLT TPIMNPLNYP AKKAFVSSTT LLGWDPGSAE FIKEYGYEDE TTAPGNTAPK GPDKKSFDSN DPLANIRACV EQGEKEAIID LVKKALADGI DPLDLTKKGL SEAMNVVGDK FGSGKLFLPQ VMLAAETMQA AFNTIKEIIP ASESLDKGTV VVATVKGDIH DLGKNIVAAL LENNGYKIVD LGKDVDPEVI VQAIKDNKAA LVGICSLMTT TMPQIDNTIA AIRAAGLKTK VMVGGAVVSQ DYADQAGADI YAKDGIAAVN HANDFFETLE K // ID D6KR58_9FIRM Unreviewed; 337 AA. AC D6KR58; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFG24304.2}; GN ORFNames=HMPREF0874_01461 {ECO:0000313|EMBL:EFG24304.2}; OS Veillonella sp. 6_1_27. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Veillonella. OX NCBI_TaxID=450749 {ECO:0000313|EMBL:EFG24304.2}; RN [1] {ECO:0000313|EMBL:EFG24304.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=6_1_27 {ECO:0000313|EMBL:EFG24304.2}; 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; EFG24304.2; -; Genomic_DNA. DR RefSeq; WP_008602832.1; NZ_GG770217.1. DR EnsemblBacteria; EFG24304; EFG24304; HMPREF0874_01461. DR PATRIC; 36281650; VBIVeiSp6271_1448. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFG24304.2}; KW Transferase {ECO:0000313|EMBL:EFG24304.2}. SQ SEQUENCE 337 AA; 36691 MW; 304844BC9E9B72B3 CRC64; MAKRSAFLDI IKEKGALVLD GALGTELERY GCDIQHKLWS AKVLMDQPDI IKKIHISYLA AGADIIQSSG YQATVAGFKG LGYGTEEAIE LVKLSVRLAV QARNEFLEAK ASGALTLHGI KLGEETPEGV RYFSEGALPK PLVAASVGPY GAFLADGSEY RGYPDVQTEY LEIFHIPRLA LFCEEHPDIL SFETIPSYAE AIAIARAMSD PFTSKGIPGW IAFSCKDGHH VSSGETIIKC AQMIDKVHPI TGIGINCSKP EYVESLIKDI RTVTDKPIAV YPNLGESYDS KTKTWYGDAA SFVDYVEVWR KAGAEIIGGC CRTTPEIIGD IAKKIHN // ID D6LF05_9FUSO Unreviewed; 1081 AA. AC D6LF05; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFG28740.2}; GN ORFNames=HMPREF0400_00293 {ECO:0000313|EMBL:EFG28740.2}; OS Fusobacterium periodonticum 1_1_41FAA. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=469621 {ECO:0000313|EMBL:EFG28740.2}; RN [1] {ECO:0000313|EMBL:EFG28740.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_1_41FAA {ECO:0000313|EMBL:EFG28740.2}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG770381; EFG28740.2; -; Genomic_DNA. DR RefSeq; WP_008820311.1; NZ_GG770381.1. DR EnsemblBacteria; EFG28740; EFG28740; HMPREF0400_00293. DR PATRIC; 36482854; VBIFusSp71368_0616. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFG28740.2}; KW Transferase {ECO:0000313|EMBL:EFG28740.2}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 723 723 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1081 AA; 120788 MW; D3C13B3E586011EE CRC64; MFEFEKELRE RILVLDGAMG TVLQKYELTP EDFNGAKGCY EILNETRPDI IFEVHKKYIE AGADIIETNS FNCNAISLKD YHLEDKVYDL AKKSAEIARD AVKQSGKKVY VFGSIGPTNK SLSFPVGDVP FKRAVSFDEM KEVIKVQVAG LIDGGVDGIL LETIFDGLTA KAALLATEEV FEEKNVKLPI SISATVNRQG KLLTGQSMES LIVALDRDSV TSFGFNCSFG AKDLVPLILK IKELTTKFVS LHANAGLPNQ NGDYVETAQK MRDDLLPLIE NQAINILGGC CGTNYDHIRA IAELVKDQKP RVLPEENLLE TCLSGNEIYN FNDKFTCVGE RNNISGSKLF RTMIEEHNYL KALEVARQQI DAGAKVLDIN VDDGILDSVE EMKNFLRVLQ NDSFIAKVPI MIDSSDFAVI EEGLKNTSGK AIVNSISLKE GTEEFLRKAK IIRKFGASII VMAFDEKGQG VSAERKIEIC QRAYDLLKSI GVKNSDIVFD PNILSVGTGQ EADRYHAREF IKTIDYIHEN LKGCGVVGGL SNLSFAFRGN NVLRAAFHHI FLEEAVPRGF NFAILNPKEK APQWTDDERE KIKSFIFGES TDMEALLSLN LIKRKEEAQI FAETPEDKIR KALIQGGSES LQEVIGDLLK KYKALEILEN ILMSAMQEIG RLFEQGELYL PQLIRSASVM NNCVDILTPY LDKVDKTSSK GKILMATVDG DVHDIGKNIV GTVLECNGYE VIDLGVMVPR DKIVEKAKEI NADVVTLSGL ISPSLKEMER VADLFQKVGM QVPILIAGAA TSKLHTGLKV LPNYDYSLHV TDAMDTITVV SQLLSTKRKD FIETKQNQLR KIAKRYIDNN NETEEKKVFP EVKKTVSYIP KVLGKQFLSL PVEIFKDTLK WDIALYALRV KNTPEEEKTL NDLKKIYEKL IEEKVEFRAA YGYFRCKKTE TFLEMEGMTF EVSPNLAQYI EKEDYVGGFV ISVGSKIFKD DKYLGLLETL LCNAIAETAS EYMETRVSED IVPTFLRPAV GYPILPDHSL KKVVFDLIDG ERTGAKLSPA FAMTPLSTVC GFYLCNDNAK Y // ID D6LLC2_9RHIZ Unreviewed; 1300 AA. AC D6LLC2; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 01-APR-2015, entry version 28. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFG37176.2}; GN ORFNames=BAZG_00497 {ECO:0000313|EMBL:EFG37176.2}; OS Brucella sp. NVSL 07-0026. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520448 {ECO:0000313|EMBL:EFG37176.2}; RN [1] {ECO:0000313|EMBL:EFG37176.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NVSL 07-0026 {ECO:0000313|EMBL:EFG37176.2}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG770510; EFG37176.2; -; Genomic_DNA. DR EnsemblBacteria; EFG37176; EFG37176; BAZG_00497. DR PATRIC; 35168236; VBIBruSp103899_0388. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 263 263 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 326 326 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 327 327 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 783 783 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1300 AA; 143052 MW; 473E3E2836E15F28 CRC64; MASSLDDLFG ATAAKPDGSE VLAALTQAAR ERILILDGAM GTQIQGLGFH EEHFRGDRFA TCDCQLQGNN DLLTLTQPKA IEEIHYAYAM AGADILETNT FSSTSIAQAD YGMEAMVYDL NRDGARLARR AALRAEQKDG RRRFVAGALG PTNRTASLSP DVNNPGFRAV TFDDLRIAYS EQIRGLIDGG SDIILIETIF DTLNAKAAVF ATEEVFAEKG VRLPVMISGT ITDLSGRTLS GQTPTAFWYS LRHARPFTIG LNCALGANAM RAHLDELSGI ADTFICAYPN AGLPNEFGQY DETPEAMAAQ IEGFARDGLV NVVGGCCGST PDHIRAIAQA VAKYEPRKPA KVPPLMRLSG LEPFTLTKDI PFVNIGERTN VTGSARFRKL VKAGDFAAAL DVARDQVANG AQIIDINMDE GLIDSEKAMV EFLNLIAAEP DIARVPIMLD SSKWEVIEAG LKCVQGKAVV NSISLKEGEE AFLHHARLVR AYGAAVVIMA FDETGQADTQ ARKIEICTRA YKILTEQVGF PPEDIIFDPN IFAVATGIEE HNNYGVDFIE ATREIVRTLP HVHISGGVSN LSFSFRGNEP VREAMHAVFL YHAIQAGMDM GIVNAGQLAV YDTIDAELRE ACEDVVLNRP TKTGESATER LLEIAERFRD SGSREARTQD LSWREWPVEK RLEHALVNGI TEYIEADTEE ARLAAERPLH VIEGPLMAGM NVVGDLFGSG KMFLPQVVKS ARVMKQAVAV LLPFMEEEKR LNGGEGRQSA GKVLMATVKG DVHDIGKNIV GVVLACNNYE IIDLGVMVPS QKILQVARDE KVDIIGLSGL ITPSLDEMAH VAAEMEREGF DIPLLIGGAT TSRVHTAVKI HSRYERGQAV YVVDASRAVG VVSNLLSPEG KQAYIDGLRN EYAKVAAAHA RNEAEKQRLP IARARANPHQ LDWENYEPVK PAFTGTKVFE TYDLAEIARY IDWTPFFQTW ELRGRYPAIL EDEKQGEAAR QLWADAQAML RKIIDEKWFT PRAVVGFWPA NAVGDDIRLF TDESRKEELA TLFTLRQQLT KRDGRPNVAM ADFVAPVESG KQDYVGGFVV TAGIGEIAIA ERFERANDDY SAILVKALAD RFAEAFAELM HERVRKEFWA YAPDEAFTPE ELISEPYKGI RPAPGYPAQP DHTEKTTLFR LLDATANTGV ELTESYAMWP GSSVSGLYIG HPESYYFGVA KVERDQVEDY ARRKDMDVEA VERWLTPILN YVPGGIERRS GLTADRSRGN GKTALMEQTS TRAVCFKLCG GVFRFYFSSK // ID D6TJM7_9CHLR Unreviewed; 1194 AA. AC D6TJM7; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFH89634.1}; GN ORFNames=Krac_11199 {ECO:0000313|EMBL:EFH89634.1}; OS Ktedonobacter racemifer DSM 44963. OC Bacteria; Chloroflexi; Ktedonobacteria; Ktedonobacterales; OC Ktedonobacteraceae; Ktedonobacter. OX NCBI_TaxID=485913 {ECO:0000313|EMBL:EFH89634.1}; RN [1] {ECO:0000313|EMBL:EFH89634.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SOSP1-21 {ECO:0000313|EMBL:EFH89634.1}; RX PubMed=22180814; RA Chang Y.J., Land M., Hauser L., Chertkov O., Del Rio T.G., Nolan M., RA Copeland A., Tice H., Cheng J.F., Lucas S., Han C., Goodwin L., RA Pitluck S., Ivanova N., Ovchinikova G., Pati A., Chen A., RA Palaniappan K., Mavromatis K., Liolios K., Brettin T., Fiebig A., RA Rohde M., Abt B., Goker M., Detter J.C., Woyke T., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., RA Lapidus A.; RT "Non-contiguous finished genome sequence and contextual data of the RT filamentous soil bacterium Ktedonobacter racemifer type strain (SOSP1- RT 21)."; RL Stand. Genomic Sci. 5:97-111(2011). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFH89634.1}. 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; ADVG01000001; EFH89634.1; -; Genomic_DNA. DR RefSeq; WP_007906375.1; NZ_ADVG01000001.1. DR EnsemblBacteria; EFH89634; EFH89634; Krac_11199. DR PATRIC; 38025365; VBIKteRac14625_1796. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 229 229 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 296 296 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 756 756 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1194 AA; 132888 MW; 18163C2D0E301041 CRC64; MSQFLSALAR RPLIFDGAMG SNIQLYQLTA EDYGGQQTEG CNEYLVLTKP QVIEEIHTGF FEAGCDVIET DSFTASRLKL DEYQIGHLTY EVNFEAARLA RRLADRYSTA SQPRFVAGSV GPTGMLPSSD DPMLSNITYQ QLAAIFHEQA IPLLKGGVDV LLIETSQDIL EVRAAITGLR RAMQEVGRRV PIQAQVSLDT SGRMLLGTDI AAVTTTLTAL RVDIIGLNCS TGPEYMREPV RYLSENCRLP ISTIPNAGIP LNVNGQAVYP LEPEPMAQAM REFIEEFGVN IVGGCCGSSH EHLQAIVRAC RPVTRKPRPQ ADQNIEHKDF KQIMPPLVSS AIRSVEMQQD PAPLLIGERV NAQGSKKAKQ ALLKDDYDTL LGIGREQVEG GAHVLDVQVA VTERTDEPEQ MHKIVKKLSM GIEAPLVIDS TEADVIQAAL EIYPGRVIIN SINMENGRQR IEKVVPLALE HGSALVALTI DEEGMAKSIE RKVEIARKIY DICVNEYDLS PNALIFDPLT FTITTGQEEL QTAGIDTLEG IRRIKSELPG VMTVLGVSNV SFGLKPHARA VLNSVFLYHA IKAGLDMAIV NPTHIKPYAE IDTEQRQLAE DLIFNRTEAL PRFIEYFESH GPQKNEGEAK VDPTEGMNTA ERIHWQILHR RKEGIEPLID AIIQERTEAS DTPISEAAVE VLNTVLLPAM KDVGDRFGAG ELILPFVLQS AEVMKKSVAH LENYLEKKEG YTKGKVVLAT VFGDVHDIGK NLVNTILTNN GYTVYDLGKQ VPLNTIIDKA IEVNADAIGL SALLVSTSKQ MPLCVKELHK RGYSFPVIIG GAAINRSFGR RILFVDEQNA EAAPLPYAPG VFYARDAFEG LDIMDRLTSV PEQRSTFVEK IQQEALNERQ RKARGQEETA NSQSQVDTRP STSIQPARSL PTPPFWGPRV LDRIGLEDVA ECMDFKTLYR LHWGGKTHGE EFERLVERDF KPRLERMLQE ARRLRYLQPR VVYGYYPCQS SGNDLIVYEP GEVESGKPLS QWRELTRFSF PRQRERERLC LADYFASVKS GKIDVVPLQV VTMGRAASEY IDQLQQAGSY SEGYFVHGLA VEMAEGLAEY TNRLVRHELG LEEDRGRRYS WGYPAIPDLV DHEKLFKVLP VTESIGINLT EAHQLVPEQS TAAIIVHHQQ SSYFSVRANE AALV // ID D6TL89_9CHLR Unreviewed; 641 AA. AC D6TL89; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 27-MAY-2015, entry version 23. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=Krac_7841 {ECO:0000313|EMBL:EFH86539.1}; OS Ktedonobacter racemifer DSM 44963. OC Bacteria; Chloroflexi; Ktedonobacteria; Ktedonobacterales; OC Ktedonobacteraceae; Ktedonobacter. OX NCBI_TaxID=485913 {ECO:0000313|EMBL:EFH86539.1}; RN [1] {ECO:0000313|EMBL:EFH86539.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SOSP1-21 {ECO:0000313|EMBL:EFH86539.1}; RX PubMed=22180814; RA Chang Y.J., Land M., Hauser L., Chertkov O., Del Rio T.G., Nolan M., RA Copeland A., Tice H., Cheng J.F., Lucas S., Han C., Goodwin L., RA Pitluck S., Ivanova N., Ovchinikova G., Pati A., Chen A., RA Palaniappan K., Mavromatis K., Liolios K., Brettin T., Fiebig A., RA Rohde M., Abt B., Goker M., Detter J.C., Woyke T., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., RA Lapidus A.; RT "Non-contiguous finished genome sequence and contextual data of the RT filamentous soil bacterium Ktedonobacter racemifer type strain (SOSP1- RT 21)."; RL Stand. Genomic Sci. 5:97-111(2011). CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFH86539.1}. 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; ADVG01000002; EFH86539.1; -; Genomic_DNA. DR RefSeq; WP_007910951.1; NZ_ADVG01000002.1. DR ProteinModelPortal; D6TL89; -. DR EnsemblBacteria; EFH86539; EFH86539; Krac_7841. DR PATRIC; 38030298; VBIKteRac14625_4234. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EFH86539.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EFH86539.1}. SQ SEQUENCE 641 AA; 70344 MW; 6DF49A751241892A CRC64; MRRTSPFIER LVQGPILCDG GMGTQLYARG ISYERCFEQL NLTSPELIKT IHLEYVAAGA EIIETNTFGA NRFRLREHGL EEQVHAINRA GAKIAREARE LSEQPIFLAG NIGPLGSHLA PLGDITPEEA RNAFQEQAAA LLESGVDLLI IETITNLEEM REALSAIRGM TDLPIVALMS FDEENTVSSG EEPLLVAQTM QELGADVVGV NCALGPAGTF SVIEGMSTGE HEHFLLAAQP NAGLPKRVGN RFIYGASPDY FADYARRFLE IGVSLLGGCC GTTPQHIAAM RKVLAEYAPE LGTREITVPK RQPRLETIFE RDPESSSGTQ THSTYLSQRL ATGHFVVSAE MRPPRSVKFT RFLQNAEYLR DIGVDTINIT DNAMARVRMS NVAAARLIQQ QVGVETIVHF TPRDRNLMAV QSDLIGAHAT DIRNVLAVTG DPPTHGDFPN ATGIWDVDSI GLIAILNNLN QGLDGRGRKL GTPGSFCIGC AATPPATDIA LDLERLHRKI EAGAQFIMTQ PVYDPETLIS YFERYKQEYG PLTIPILVGL QPLHSYQQAE KFHNEVPGIV IPEAVRERLR LAGDQACDTG LEIIKELFDA TLPYIQGTYI MPLDRYDLVG ELLPYIRQQT VDRGSESAIS S // ID D6V3W2_9BRAD Unreviewed; 1282 AA. AC D6V3W2; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 01-APR-2015, entry version 25. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFI52642.1}; GN ORFNames=AfiDRAFT_0629 {ECO:0000313|EMBL:EFI52642.1}; OS Afipia sp. 1NLS2. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Afipia. OX NCBI_TaxID=666684 {ECO:0000313|EMBL:EFI52642.1}; RN [1] {ECO:0000313|EMBL:EFI52642.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=1NLS2 {ECO:0000313|EMBL:EFI52642.1}; 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., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFI52642.1}. 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; ADVZ01000001; EFI52642.1; -; Genomic_DNA. DR RefSeq; WP_009337628.1; NZ_ADVZ01000001.1. DR EnsemblBacteria; EFI52642; EFI52642; AfiDRAFT_0629. DR PATRIC; 38093209; VBIAfiSp150213_0631. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 767 767 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1282 AA; 140709 MW; 3761C9BD9C595CB5 CRC64; MTSSTADKFR ALARERILVL DGAMGTMIQR LELDEAAFRG ERFKDFHRDV RGNNDLLILT QPQAIEDIHY EYLKAGADIV ETNTFSSTSI AQADYDMSNL AYELNREGAR LARNAANRAE ADDGKPRFVA GALGPTNRTA SISPDVANPG YRAVTFDGLR IAYSEQINGL LDGGADLLLV ETIFDTLNAK AALYAIAEIC EARGIDVPVM ISGTITDKSG RLLSGQMPEA FWYSVQHANP ITIGFNCALG AEDLRAHIAD IGRVADTLVC AYPNAGLPNE FGQYDETPEY MARLVGEFAR DGLVNVVGGC CGTTPDHIKA IAQAVAPHKP RIVPAIEPRL RLSGLEPFVL TNDIPFVNVG ERTNVTGSAR FRKLIKEGNY TAALQVARDQ VENGAQVIDV NMDEGLLDSK QAMIDFLNLV ASEPDIAKVP VMVDSSKFEV IEAGLQCIQG KSILNSISMK EGEEKFLHEA AIARRHGAAV VVMAFDEIGQ ADTYQRKIDI CKRAYDLLTT KLNFPPQDII FDPNIFAIAT GLEEHNNYGV DFIEATRWIR QNLPHVHISG GVSNLSFSFR GNEPVREAMH SVFLYHAIKA GMDMGIVNAG QMVIYDDIDP ELREVCEDVI LNRDPGAPER LLQLAEKFRG QGKQVKEQDL AWREWSVEKR LSHALVNGIT EYIEVDTEDA RLTVERPLNV IEGPLMAGMN VVGDLFGSGK MFLPQVVKSA RVMKQAVAYL MPFMEEEKER NKAAGLTEGQ RSSAGKIVMA TVKGDVHDIG KNIVGIVLQC NNFEVVDLGV MVPAAKILET AKKENADLIG LSGLITPSLD EMAFVASEME REGFDIPLLI GGATTSRVHT AVKIDPRYRK GAVVHVNDAS RAVGVASSLL SAEKRDEYIA EVRADYAKIA DAHFRAQQNK KRLSLAAARA NHLKIDWSKT KPVKPSFLGL KTFTNYSLAE LAECIDWTPF FQAWELSGRF PAILKDPNVG EVAQSLYNDA RKMLDTIIKE NWFTANATIG FWPANADGDD VTLYSDEART KPLATLHTLR QQLERRAGVP NLALADFIAP KGSGVADYIG AFVVTAGIGE EAITMRFKKS NDDYSSIIVK ALADRLAEAF AERMHQRVRM EFWGYAADEA LSNDDLILEK YQGIRPAPGY PAQPDHNEKT TIFKLLDAER NAGVTLTESL AMWPGSSVSG IYYSHPQSEY FGVGKIERDQ VEDYAERVGA TVAETERSLA SVLNYIPASE PQPPAPADDD ITSLPPAQHP PGCGCAIHMR LNVKSRTDAR PD // ID D6WLX1_TRICA Unreviewed; 348 AA. AC D6WLX1; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 07-JAN-2015, entry version 28. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EFA03390.1}; GN ORFNames=TcasGA2_TC013376 {ECO:0000313|EMBL:EFA03390.1}; OS Tribolium castaneum (Red flour beetle). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Coleoptera; Polyphaga; OC Cucujiformia; Tenebrionidae; Tenebrionidae incertae sedis; Tribolium. OX NCBI_TaxID=7070 {ECO:0000313|Proteomes:UP000007266}; RN [1] {ECO:0000313|EMBL:EFA03390.1, ECO:0000313|Proteomes:UP000007266} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA03390.1, RC ECO:0000313|Proteomes:UP000007266}; RX PubMed=18362917; DOI=10.1038/nature06784; RG Tribolium Genome Sequencing Consortium; RA Richards S., Gibbs R.A., Weinstock G.M., Brown S.J., Denell R., RA Beeman R.W., Gibbs R., Beeman R.W., Brown S.J., Bucher G., RA Friedrich M., Grimmelikhuijzen C.J., Klingler M., Lorenzen M., RA Richards S., Roth S., Schroder R., Tautz D., Zdobnov E.M., Muzny D., RA Gibbs R.A., Weinstock G.M., Attaway T., Bell S., Buhay C.J., RA Chandrabose M.N., Chavez D., Clerk-Blankenburg K.P., Cree A., Dao M., RA Davis C., Chacko J., Dinh H., Dugan-Rocha S., Fowler G., Garner T.T., RA Garnes J., Gnirke A., Hawes A., Hernandez J., Hines S., Holder M., RA Hume J., Jhangiani S.N., Joshi V., Khan Z.M., Jackson L., Kovar C., RA Kowis A., Lee S., Lewis L.R., Margolis J., Morgan M., Nazareth L.V., RA Nguyen N., Okwuonu G., Parker D., Richards S., Ruiz S.J., RA Santibanez J., Savard J., Scherer S.E., Schneider B., Sodergren E., RA Tautz D., Vattahil S., Villasana D., White C.S., Wright R., Park Y., RA Beeman R.W., Lord J., Oppert B., Lorenzen M., Brown S., Wang L., RA Savard J., Tautz D., Richards S., Weinstock G., Gibbs R.A., Liu Y., RA Worley K., Weinstock G., Elsik C.G., Reese J.T., Elhaik E., Landan G., RA Graur D., Arensburger P., Atkinson P., Beeman R.W., Beidler J., RA Brown S.J., Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H., RA Lorenzen M., Maselli V., Osanai M., Park Y., Robertson H.M., Tu Z., RA Wang J.J., Wang S., Richards S., Song H., Zhang L., Sodergren E., RA Werner D., Stanke M., Morgenstern B., Solovyev V., Kosarev P., RA Brown G., Chen H.C., Ermolaeva O., Hlavina W., Kapustin Y., RA Kiryutin B., Kitts P., Maglott D., Pruitt K., Sapojnikov V., RA Souvorov A., Mackey A.J., Waterhouse R.M., Wyder S., Zdobnov E.M., RA Zdobnov E.M., Wyder S., Kriventseva E.V., Kadowaki T., Bork P., RA Aranda M., Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F., RA Bopp D., Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E., RA Ferrier D.E., Friedrich M., Gordon C.M., Jindra M., Klingler M., RA Lan Q., Lattorff H.M., Laudet V., von Levetsow C., Liu Z., Lutz R., RA Lynch J.A., da Fonseca R.N., Posnien N., Reuter R., Roth S., RA Savard J., Schinko J.B., Schmitt C., Schoppmeier M., Schroder R., RA Shippy T.D., Simonnet F., Marques-Souza H., Tautz D., Tomoyasu Y., RA Trauner J., Van der Zee M., Vervoort M., Wittkopp N., Wimmer E.A., RA Yang X., Jones A.K., Sattelle D.B., Ebert P.R., Nelson D., Scott J.G., RA Beeman R.W., Muthukrishnan S., Kramer K.J., Arakane Y., Beeman R.W., RA Zhu Q., Hogenkamp D., Dixit R., Oppert B., Jiang H., Zou Z., RA Marshall J., Elpidina E., Vinokurov K., Oppert C., Zou Z., Evans J., RA Lu Z., Zhao P., Sumathipala N., Altincicek B., Vilcinskas A., RA Williams M., Hultmark D., Hetru C., Jiang H., Grimmelikhuijzen C.J., RA Hauser F., Cazzamali G., Williamson M., Park Y., Li B., Tanaka Y., RA Predel R., Neupert S., Schachtner J., Verleyen P., Raible F., Bork P., RA Friedrich M., Walden K.K., Robertson H.M., Angeli S., Foret S., RA Bucher G., Schuetz S., Maleszka R., Wimmer E.A., Beeman R.W., RA Lorenzen M., Tomoyasu Y., Miller S.C., Grossmann D., Bucher G.; RT "The genome of the model beetle and pest Tribolium castaneum."; RL Nature 452:949-955(2008). RN [2] {ECO:0000313|EMBL:EFA03390.1, ECO:0000313|Proteomes:UP000007266} RP GENOME REANNOTATION. RC STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA03390.1, RC ECO:0000313|Proteomes:UP000007266}; RX PubMed=19820115; DOI=10.1093/nar/gkp807; RA Kim H.S., Murphy T., Xia J., Caragea D., Park Y., Beeman R.W., RA Lorenzen M.D., Butcher S., Manak J.R., Brown S.J.; RT "BeetleBase in 2010: revisions to provide comprehensive genomic RT information for Tribolium castaneum."; RL Nucleic Acids Res. 38:D437-D442(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; CM000280; EFA03390.1; -; Genomic_DNA. DR RefSeq; XP_008193878.1; XM_008195656.1. DR RefSeq; XP_966501.1; XM_961408.2. DR EnsemblMetazoa; TC013376-RA; TC013376-PA; TC013376. DR GeneID; 662176; -. DR KEGG; tca:662176; -. DR InParanoid; D6WLX1; -. DR KO; K00547; -. DR OMA; QCKDENT; -. DR OrthoDB; EOG7GQXW0; -. DR PhylomeDB; D6WLX1; -. DR Proteomes; UP000007266; Linkage group 5. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007266}; KW Reference proteome {ECO:0000313|Proteomes:UP000007266}. SQ SEQUENCE 348 AA; 38979 MW; 7BDF2994A554D30C CRC64; MAPPGVGSSS EKRHNDTMSA NERDIVVLDG GFATQLSCHV SQQIDGDVLW SARFLATDKE AIIDAHLDFL RAGADLVITN SYQASIGGFM EHLKLTKDQS YELIKESVKL ARIACQRYNK EFPNSTPPMV VGSVGPYGAS LHDGSEYTGS YAKTTPVETM REWHIPRIRA LVEAGVDLLA LETIPCKIEA EMLVELLKKE FPNTKAWLSF SVRQDGKSLA YGESFQEVAR YCYDLNPQQL VAVGVNCVAP RLVETLISGI NKDRKNPVPL VVYPNSGESY KVELGWIDRD KCEPVDTYVQ KWLDLGVTWV GGCCRTYATD VSRIRQEVEK WKRNKEEKRH QNGQCTQK // ID D6XXG6_BACIE Unreviewed; 1158 AA. AC D6XXG6; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 01-APR-2015, entry version 34. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADH98023.1}; GN OrderedLocusNames=Bsel_0486 {ECO:0000313|EMBL:ADH98023.1}; OS Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10). OC Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae; OC unclassified Sporolactobacillaceae. OX NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH98023.1, ECO:0000313|Proteomes:UP000000271}; RN [1] {ECO:0000313|EMBL:ADH98023.1, ECO:0000313|Proteomes:UP000000271} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700615 / DSM 15326 / MLS10 RC {ECO:0000313|Proteomes:UP000000271}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001791; ADH98023.1; -; Genomic_DNA. DR RefSeq; WP_013171452.1; NC_014219.1. DR RefSeq; YP_003698589.1; NC_014219.1. DR ProteinModelPortal; D6XXG6; -. DR EnsemblBacteria; ADH98023; ADH98023; Bsel_0486. DR KEGG; bse:Bsel_0486; -. DR PATRIC; 38120103; VBIBacSel78655_0528. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; BSEL439292:GHLG-516-MONOMER; -. DR Proteomes; UP000000271; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000271}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000271}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 232 232 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 296 296 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 730 730 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1158 AA; 127811 MW; 2E856EFB9A493A1E CRC64; MTVTTKQASA FRDALKERIL VLDGAMGTML QNANLTPEQF GGEAYEGCNE YLNITAPEVI RTIYHDYLEA GADIIETNTF GATDLVLDDY DLGHLAYELN KAAASIAVEE ARAFSTDSEP RFVAGAMGPT TKSLSVTGGT TFEELSSAYK EQVEGLLDGG VDLLLLETSQ DMRNVKAAYT AIEEVLSERD LDVPLIISGT IEPMGTTLAG QTIESFYISL EHMKPTVVGL NCATGPEFMQ DHLRSLSELS TGFVHCYPNA GLPDEEGHYH ETPSSLASKL RDFAEKGWLN VVGGCCGTTP EHIRAMKEAV RGFAPRQPAQ ETHHSISGIE PLIYDESLRP ILVGERTNVI GSKKFKRLIA DGKFEEASEI ARAQVKRGAM VVDVCLADPD RDEMADMEQF LHYVINKVKV PLMIDSTDEH VIEKALTYSQ GKAIINSINL EDGEERFEAV CPLIRRYGAA VVVGTIDEEG MGVSAERKLA IAKRSYELLT GKYGIAPEDI IFDPLVFPVG TGDEQYIGSA EATVEGIRLI KKAFPRTMTI LGVSNVSFGL PPLGREVLNA AFVYHCTKAG LDYAIVNTEK LERYGSVSED EKKLADELLF RTSDETLAEF TAFYRAKKPQ QKVEASKRTL EERLANYIIE GTKEGLYTDL DEALAKYPDP LDIINGPLMD GMDEVGKLFN NNELIVAEVL QSAEAMKAAV AHLEPHMEKK ESDDRGKGKI LLATVKGDVH DIGKNLVEII LSNNGFQVVN LGIKVASHEL IEAVEREDPD YIGLSGLLVK STQQMVITAN DLRERGIDIP ILVGGAALTR KFTETKITRQ YNGLVLYAKD AMNGLSLANK LAKPETRDEL VAVQHEKQLK LNEAEAAGDG MASKGKTNTA TADPAQSEVS RDHKVYQPED FEPHILRDFR LTHLQPYLNL QTLLGSHLGV NGNVRRKLES GDERTKELLD KVNALIQKGE QEKLLRADGM YQFFPAQSNG NDILIYDPND ESSVIERFTF PRQTQAPYMC LSDFLKSVDS GEMDRVGFLA VTAGKGIRKL AEAAKESGDY LDSYLVQAVA LELAEGFAER VHQQMRDKWG FSDPVDLTMQ DRFSARYQGV RVSYGYPACP NLEDQKKLFG LLKPEKIGIE LTDEYMMEPE ASVTAMVFSH PEGRYFNV // ID D6XXS9_BACIE Unreviewed; 352 AA. AC D6XXS9; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADI00122.1}; GN OrderedLocusNames=Bsel_2622 {ECO:0000313|EMBL:ADI00122.1}; OS Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10). OC Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae; OC unclassified Sporolactobacillaceae. OX NCBI_TaxID=439292 {ECO:0000313|EMBL:ADI00122.1, ECO:0000313|Proteomes:UP000000271}; RN [1] {ECO:0000313|EMBL:ADI00122.1, ECO:0000313|Proteomes:UP000000271} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700615 / DSM 15326 / MLS10 RC {ECO:0000313|Proteomes:UP000000271}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; ADI00122.1; -; Genomic_DNA. DR RefSeq; WP_013173543.1; NC_014219.1. DR RefSeq; YP_003700687.1; NC_014219.1. DR EnsemblBacteria; ADI00122; ADI00122; Bsel_2622. DR KEGG; bse:Bsel_2622; -. DR PATRIC; 38124670; VBIBacSel78655_2773. DR HOGENOM; HOG000231636; -. DR KO; K00544; -. DR OMA; KAHYMSQ; -. DR BioCyc; BSEL439292:GHLG-2694-MONOMER; -. DR Proteomes; UP000000271; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000271}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ADI00122.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000271}; KW Transferase {ECO:0000313|EMBL:ADI00122.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 213 213 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 301 301 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 302 302 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 352 AA; 39553 MW; F34159631306F4B7 CRC64; MATSKRTLEE RLQAGTVICA EGYLFEMERR GYLQAGSFVP EVALDNPDVL KQTYRDFMLA GSDVVLAFTY NAHREKMRII GKEDLLEPLN RSAIRLAKEV AKEHPEEEAL VAGNISNTNI FDPEDPASKE QVRQMFREMV QWSKEEGVDF VNAETFYYHE EAVIALEEIL RQDLPAVVTL GVMGENKMRD GLSPEESCRL LSEKGALVVG MNCFRGPDTM QPFLERIRHH VDGYVAGLPV PYRTKDDHPT FFNLPDSGCS CHLPTETTFP TSLDPLYHNR YELAEWAKEA KAIGINYIGL CCGASPAMIR AVAEATGKEA VNSTYSPDMT KHFLFGKDDS LKGHNQDYRS KA // ID D6Y9B4_THEBD Unreviewed; 288 AA. AC D6Y9B4; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADG88034.1}; GN OrderedLocusNames=Tbis_1315 {ECO:0000313|EMBL:ADG88034.1}; 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 {ECO:0000313|EMBL:ADG88034.1, ECO:0000313|Proteomes:UP000006640}; RN [1] {ECO:0000313|EMBL:ADG88034.1, ECO:0000313|Proteomes:UP000006640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19993 / DSM 43833 / CBS 139.67 / JCM 10125 / NBRC 14880 / RC R51 {ECO:0000313|Proteomes:UP000006640}; 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 ----------------------------------------------------------------------- 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; ADG88034.1; -; Genomic_DNA. DR RefSeq; WP_013131567.1; NC_014165.1. DR RefSeq; YP_003651927.1; NC_014165.1. DR EnsemblBacteria; ADG88034; ADG88034; Tbis_1315. DR KEGG; tbi:Tbis_1315; -. DR PATRIC; 38285564; VBITheBis80272_1324. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR BioCyc; TBIS469371:GHSI-1338-MONOMER; -. DR Proteomes; UP000006640; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006640}; KW Methyltransferase {ECO:0000313|EMBL:ADG88034.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006640}; KW Transferase {ECO:0000313|EMBL:ADG88034.1}. SQ SEQUENCE 288 AA; 30876 MW; CAFB43E69AC8A818 CRC64; MSYLVLDGGL ATHLEALGCD LRDELWSARL LIENPGIIRK AHLDYFAAGA DVATTASYQA SIPGFVRRGL TPGEARDLLR LAVRLAVEAR DEAGHGLVAA SVGPYGAYLA NGAEYTGAYD LGEDGLFAWH RERFEILASA GADLVAFETI PSFPEACAVA RLLRLAPEVR AWVSFSCRDD RHINDGTPFA ECVALFSGMP QVVAVGVNCT PPRHIPGLIR AGARIVYPNS GEAWDPVGRR WTGTSDPVSF GRAAVEWRAL GATHIGGCCR TTPAHIREIR ARLAESPA // ID D6YBK6_THEBD Unreviewed; 1154 AA. AC D6YBK6; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 01-APR-2015, entry version 33. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADG88566.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADG88566.1}; GN OrderedLocusNames=Tbis_1854 {ECO:0000313|EMBL:ADG88566.1}; 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 {ECO:0000313|EMBL:ADG88566.1, ECO:0000313|Proteomes:UP000006640}; RN [1] {ECO:0000313|EMBL:ADG88566.1, ECO:0000313|Proteomes:UP000006640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19993 / DSM 43833 / CBS 139.67 / JCM 10125 / NBRC 14880 / RC R51 {ECO:0000313|Proteomes:UP000006640}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001874; ADG88566.1; -; Genomic_DNA. DR RefSeq; WP_013132099.1; NC_014165.1. DR RefSeq; YP_003652459.1; NC_014165.1. DR EnsemblBacteria; ADG88566; ADG88566; Tbis_1854. DR KEGG; tbi:Tbis_1854; -. DR PATRIC; 38286765; VBITheBis80272_1923. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; TBIS469371:GHSI-1879-MONOMER; -. DR Proteomes; UP000006640; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006640}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADG88566.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006640}; KW Transferase {ECO:0000313|EMBL:ADG88566.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 225 225 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 292 292 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 735 735 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1154 AA; 126832 MW; A7763A88A5DBAEDC CRC64; MTGRPSFREA LSERILVADG AMGTMLQSYH PTIEDFQGHE GCNDVLNVSR PDIVRSVHDA YLAAGVDCIE TNTFNSNQAA LGEYGIADRI YELSEAGARL ARERADHWST PDHPRYVLGS MGPGTKLPTL GHLPYALLRD AYEQNAAGLI AGGVDALIIE TCQDLLQAKA AIVGAKRAIA KAGRDVPIIA QVTIETNGTM LLGTEIGAAL TSLEPLGIDL IGLNCATGPA EMSEHLRYLA KHARVPLSCM PNAGLPELTA EGARYPLQPE ELAEAHVTFI REFGLSLVGG CCGTTPEHMR TVVERVAGMT RSARRPRPEA GAASLYQHVP FRQDTSCLMI GERTNANGSK AFREAMLAGQ YDECVEIARA QARDGAHMLD LCVDYVGRDG VADMKELAFR FATASTLPIV LDSTEPAVLE AGLEMLGGRA VVNSVNFEDG DGPDSRFTKV MRLVKEHGAA VVALTIDEEG QARTAEWKVR VATRLIEKLV NEWGMRPEDI LVDCLTFPIA TGQEDSRRDA LETIEAIREV KRRYPDVQTT LGISNVSFGL NPAARVVLNS VFLNECVNAG LDSAIVHASK ILPMNRIPDE QRQVALDLIY DRRREGYDPL QRFMELFADA DAASMTAGKA AELAALPLWE RLKRRIIDGE RKGLEDDLDE ALTQRPALEI INDVLLDGMK TVGDLFGSGQ MQLPFVLQSA EVMKSAVAYL EPHMERVEGV SKGRIVLATV KGDVHDIGKN LVDIILSNNG YEVINLGIKQ PISAIIQAAE EKQADVIGMS GLLVKSTVVM KENLEELNAR KLAAKYPVIL GGAALTRAYV EQDLADIYEG EVRYARDAFE GLRLMDAIMA VKRGEKGASL PPLRTRRVKP GAVLRRTPAD ELPRRSDVAT DNPIPRPPFY GDRVVKGIPL ADYAAFIDER ALFMGQWGLR PSRAEGGPSY EELVETEGRP RLRMWLERLH TENLLEAAVV YGYFPCVSEG DSLIILDEDG GERLRFTFPR QRRDRHLCLA DFFRPRESGE VDVVAFQVVT VGHRIGRATA ELFGKDAYRE YLELHGLSVQ LTEALAEYWH ARVRSELGIG GDESLEDMLK VNITGCRYSF GYPACPNLED QVHLMTLLDP ARIGVTLSEE YQLHPEQSTS ALIAHHPEAK YFKV // ID D6Z0B2_DESAT Unreviewed; 631 AA. AC D6Z0B2; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 27-MAY-2015, entry version 36. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=DaAHT2_2481 {ECO:0000313|EMBL:ADH87145.1}; OS Desulfurivibrio alkaliphilus (strain DSM 19089 / UNIQEM U267 / AHT2). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales; OC Desulfobulbaceae; Desulfurivibrio. OX NCBI_TaxID=589865 {ECO:0000313|EMBL:ADH87145.1, ECO:0000313|Proteomes:UP000001508}; RN [1] {ECO:0000313|Proteomes:UP000001508} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19089 / UNIQEM U267 / AHT2 RC {ECO:0000313|Proteomes:UP000001508}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {ECO:0000256|RuleBase:RU004255}. CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ADH87145.1; -; Genomic_DNA. DR RefSeq; WP_013164655.1; NC_014216.1. DR RefSeq; YP_003691764.1; NC_014216.1. DR ProteinModelPortal; D6Z0B2; -. DR EnsemblBacteria; ADH87145; ADH87145; DaAHT2_2481. DR KEGG; dak:DaAHT2_2481; -. DR PATRIC; 38166152; VBIDesAlk70802_2513. DR HOGENOM; HOG000028409; -. DR OMA; NEVPGIQ; -. DR BioCyc; DALK589865:GHTX-2532-MONOMER; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000001508; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004255}; KW Complete proteome {ECO:0000313|Proteomes:UP000001508}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ADH87145.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000001508}; KW Transferase {ECO:0000313|EMBL:ADH87145.1}. SQ SEQUENCE 631 AA; 67799 MW; 36408261AC787161 CRC64; MSANKPDFLE YIRERVLLAD GALGSYLYAK GIELGKNIER LNLADPDLVY SVHEEYIRAG SRLIETNTFG ANRLKLENAG LEDKARQINL AGAELAVRAG SGEVYVAGSV GPSGADFPLG ETEGPEREAV EAAFKEQIEA LLEGGVDLLI LETFSHLDEL LLALKVARRL AGKMPIVANM VYPKQGCTAA GLDALECGRA ALAAGADVVG SNCGRGARAM LTAMERLAAL GEEVPLAAFP NAGFPEIVNH RLIYPAEPPY MAQLVREMVK TGARLVGGCC GTTPAHIQEF GKHLRLKRRP LTQVASDKQA TGPDSQAPTA AKAGSLLKRL PTDKLPVLVE VDPPTHLDIS GVLGGAKELA AAGADAITLG ENPLAVLRAD NISLAHKIRS EVGIATVAHV TCRDRNALGL QSQIMGAHLL EIDSILAVTG DPATTGDQPA ATGVFDVQSF GLIRMLNQFN QGRNPAGKAM KGQCDFSIGA AFSYRPNNPD LQIRRLERKA ALGAVYAMTQ PFFSAGAVED MLERTRHLEM LIFPGIFPLI SARNAEFLHH EVPGINIPED LRRKLGRYEA VEDQRRVADE FTRELIAEIC PIIDGLYLIS PLNKWEVTAE LTREVRQAGW KGSGRLAALV Q // ID D7A2F2_STAND Unreviewed; 1244 AA. AC D7A2F2; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 29-APR-2015, entry version 35. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADH89615.1}; GN OrderedLocusNames=Snov_2320 {ECO:0000313|EMBL:ADH89615.1}; 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 {ECO:0000313|EMBL:ADH89615.1, ECO:0000313|Proteomes:UP000006633}; RN [1] {ECO:0000313|Proteomes:UP000006633} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB RC 9113 {ECO:0000313|Proteomes:UP000006633}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002026; ADH89615.1; -; Genomic_DNA. DR RefSeq; WP_013167119.1; NC_014217.1. DR RefSeq; YP_003694234.1; NC_014217.1. DR EnsemblBacteria; ADH89615; ADH89615; Snov_2320. DR KEGG; sno:Snov_2320; -. DR PATRIC; 38257215; VBIStaNov45716_2319. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; SNOV639283:GCS4-2350-MONOMER; -. DR Proteomes; UP000006633; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006633}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006633}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 765 765 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1244 AA; 136517 MW; E1C0141F2F5A22F3 CRC64; MTAQPTDTLK ALRAAASERI LVLDGAMGTM IQQLKLDEAG YRGERFKTWN RDLKGNNDLL NLTKPDAVRD IHLAYFTAGA DIVETNTFSG TTIAMADYGM ESLVYEINFE GARLAKEAAK LAEAKDGRRR FVAGAIGPTN RTASISPDVN DPGFRATSFD ELATAYGEQA AALIDGGSDL LLIETIFDTL NAKAAIFAIE RLFEERGIRL PVMISGTITD LSGRTLSGQT PEAFWNSVRH AQPFSIGLNC ALGAKEMRAH IDELSRISDT FVCAYPNAGL PNEFGLYDES PAAMAKLVGE FAASGLVNVV GGCCGTTPDH IRAIAEAVAP HAPREIPEIE PRLRLSGLEP FELTPNIPFV NVGERTNVTG SARFRKLITN GDYTAALAVA RDQVENGAQV IDVNMDEGLL DSEKAMVTFL NLLAAEPDIA RVPIMVDSSK WSVIEAGLKC IQGKGIVNSI SMKEGEEAFK HHARLVRAYG AAVVVMAFDE KGQADTYERK VEICARAYRI LVEEVGFPPE DIIFDPNIFA VATGIEEHAG YGVAFIEATR AIRQQLPHAH ISGGVSNLSF SFRGNEPVRE AMHAVFLYHA IAAGMDMGIV NAGQLAPYSE IEPELREACE DVVLNRRDDS TERLLALAER FKGGGREKKE ADLTWRTWTV EKRLEHALIN GITDYVEADT EEARQAAARP LHVIEGPLMA GMNVVGDLFG AGKMFLPQVV KSARVMKQAV AYLMPFMEIE KQELGLTDAA SAGKILMATV KGDVHDIGKN IVGVVLQCNN YEVIDLGVMV PTAKILEVAK TEKVDVIGLS GLITPSLDEM VHVASEMERE GFDLPLLIGG ATTSRVHTAV KIAPQYVRGQ AVYVTDASRA VGVVSSLLND NTRADYMANV RAEYAKLADA HAKSDRNKVR VKLEEARANR LAIDFEDYRA PVPAFFGTRV FEEYDLAELV RYIDWTPFFQ SWELTGQYPR ILDDEKVGPA ARALYDDARK MLKQIVDEKW LTARAVVGFW PANTVVDDIV LYEDESRSTE LATLHTLRQQ MGKREGRHNL ALADFVAPAI TGVPDYVGGF CVSTGFGEHE RAEAFKAAHD DYSAILLKAL ADRLAEAFAE RMHERVRREF WAYAPNEVLD NENLIQENYR GIRPAPGYPA QPDHTEKAIL FKLLDATSKI GVELTESFAM WPGAAVSGLY FAHPDSSYFG VGRIERDQVE DYAARKGMSV EEAERWLAPV LNYDPLSYKS VAAE // ID D7A3B8_STAND Unreviewed; 313 AA. AC D7A3B8; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 29-APR-2015, entry version 22. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADH89677.1}; GN OrderedLocusNames=Snov_2382 {ECO:0000313|EMBL:ADH89677.1}; 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 {ECO:0000313|EMBL:ADH89677.1, ECO:0000313|Proteomes:UP000006633}; RN [1] {ECO:0000313|Proteomes:UP000006633} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB RC 9113 {ECO:0000313|Proteomes:UP000006633}; 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; ADH89677.1; -; Genomic_DNA. DR RefSeq; WP_013167181.1; NC_014217.1. DR RefSeq; YP_003694296.1; NC_014217.1. DR EnsemblBacteria; ADH89677; ADH89677; Snov_2382. DR KEGG; sno:Snov_2382; -. DR PATRIC; 38257347; VBIStaNov45716_2384. DR HOGENOM; HOG000179103; -. DR OMA; CGLMSCR; -. DR BioCyc; SNOV639283:GCS4-2413-MONOMER; -. DR Proteomes; UP000006633; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006633}; KW Methyltransferase {ECO:0000313|EMBL:ADH89677.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006633}; KW Transferase {ECO:0000313|EMBL:ADH89677.1}. SQ SEQUENCE 313 AA; 33068 MW; 2BFDC6DBC368468F CRC64; MPSTAAILEG APVILADGAI ETRLIYEFGL PTPDFSSFVH LFTREGRAAL DAIYRGYMQV AGESRLPMQV GTPTWRAHPE GLVRQGFSAP DDLRRVNEEA FRFLAGMRDA LGVGDLVMIA GVLGPRRDGY DPAVAPDAAE AQAYHRPQAR VLADLGVDLL YAPTFASAQE LLGVARAMAA TGLPYALAPV IDDDARLIDG TPLDAAVAAI DEAASPPPGN YLIGCTHAIH VTRAQGSVHW PANGRVTGLK ANASPLPPSE LDKLDHLKQD DPETFAAGLA RLHAGGMRVL GGCCGTSEAH IRALARRFVA EPA // ID D7A8X6_STAND Unreviewed; 325 AA. AC D7A8X6; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 29-APR-2015, entry version 22. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADH88681.1}; GN OrderedLocusNames=Snov_1371 {ECO:0000313|EMBL:ADH88681.1}; 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 {ECO:0000313|EMBL:ADH88681.1, ECO:0000313|Proteomes:UP000006633}; RN [1] {ECO:0000313|Proteomes:UP000006633} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB RC 9113 {ECO:0000313|Proteomes:UP000006633}; 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; ADH88681.1; -; Genomic_DNA. DR RefSeq; WP_013166186.1; NC_014217.1. DR RefSeq; YP_003693300.1; NC_014217.1. DR EnsemblBacteria; ADH88681; ADH88681; Snov_1371. DR KEGG; sno:Snov_1371; -. DR PATRIC; 38255277; VBIStaNov45716_1369. DR HOGENOM; HOG000179103; -. DR OMA; NTEDGRQ; -. DR BioCyc; SNOV639283:GCS4-1382-MONOMER; -. DR Proteomes; UP000006633; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006633}; KW Methyltransferase {ECO:0000313|EMBL:ADH88681.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006633}; KW Transferase {ECO:0000313|EMBL:ADH88681.1}. SQ SEQUENCE 325 AA; 35238 MW; 65B14A4056A9DB2F CRC64; MTDANPYGAK YRHALPLLSD RLFLMDGGME TTFIFHEGID LPCFASIDLM KDAAGREALR AYYARFAELA RAHGTGFVLD APTWRASPDW ADKLGFTQEA LAGFNRASID LLVALRERHE TPATPVVVSG VVGPRGDGYR PDGAMAIDEA ADYHATQIGI FADGPADMVS AYTMNYVEEA LGVAIAAQEL RLPSVISFTL ETDGRLPTGQ PLREAIEQVD AETGNTPAYY MINCAHPTHF DHVVAEGGAW LERIRGLRAN ASHRSHAELD SSPNLDAGDP AELGRQYRDL RGRMKNLHIL GGCCGTDLRH VEQICLACAP AQATA // ID D7AQ58_THEM3 Unreviewed; 807 AA. AC D7AQ58; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 27-MAY-2015, entry version 32. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADH61299.1}; GN OrderedLocusNames=Tmath_1591 {ECO:0000313|EMBL:ADH61299.1}; OS Thermoanaerobacter mathranii (strain DSM 11426 / CIP 108742 / A3). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Thermoanaerobacter. OX NCBI_TaxID=583358 {ECO:0000313|EMBL:ADH61299.1, ECO:0000313|Proteomes:UP000002064}; RN [1] {ECO:0000313|EMBL:ADH61299.1, ECO:0000313|Proteomes:UP000002064} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11426 / CIP 108742 / A3 RC {ECO:0000313|Proteomes:UP000002064}; 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 ----------------------------------------------------------------------- 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; ADH61299.1; -; Genomic_DNA. DR RefSeq; WP_013150563.1; NC_014209.1. DR RefSeq; YP_003677310.1; NC_014209.1. DR ProteinModelPortal; D7AQ58; -. DR EnsemblBacteria; ADH61299; ADH61299; Tmath_1591. DR KEGG; tmt:Tmath_1591; -. DR PATRIC; 38281404; VBITheMat18_1648. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR BioCyc; TMAT583358:GHOX-1647-MONOMER; -. DR Proteomes; UP000002064; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002064}; KW Methyltransferase {ECO:0000313|EMBL:ADH61299.1}; KW Transferase {ECO:0000313|EMBL:ADH61299.1}. SQ SEQUENCE 807 AA; 88194 MW; 0492AACA565A164A CRC64; MLDIFKELSN RVIVFDGAMG TQLQERGLKS GECPEYMNIT HPEVVFDIHR SYIEAGADVI ETNTFGANRI KLAKYGLENE VFNIVTQAVK IAKEASKDKP VALSIGPIGE LLTPYGDMTF DEAYDVFKEV VIAAERAGAD IVLIETMSDM LEAKAAILAA KENSNMKVIC TMTFQEDGRT LMGSDPITVV VSLQGLGLDA IGVNCSTGPD KMINVVEKMS QVSRIPIIAQ PNAGMPVIRD GKTVYDLKPE EFASFFPSLV EKGASIVGGC CGTTPHYIKL VKEAVKDLKP KVKVNKFTAV ASNTKTVFIG DDYPLRIIGE RINPTGKKKL SEAFLAGDVS LAVEEAIKQQ KCGAEILDIN VGVPGVNEEE LLPKVVSEIQ NVVDIPLQID STNIKAVEKA IRILRGRPII NSVSSKEESL KEVLPIVKKY GACVVGLTVG DKGLPKDRHE RIENAKKIIK KAEEYGIPKE DILIDCIVLT VSSEQEAAIE TLEAIKLAKE ELGVNTVVGL SNVSFGLPER KLINSAFLAM AASYGLTTAI INPCDETMMD TLRATMVLLN KDKGSVNYLN IYGKKQKEEL REKEQHKIQE EDLKSKFYIQ ILEGKKSGVE DIVKNILEEE VQPLSIVDNI IIPALKEVGD RYEKGVYFLP QLLSSAEVVQ SAFKIIKEKL PKGAVSKGKI ILATVEGDVH DIGKNIVKVL LENYGYDVID LGKDVKGEVI LEEVKRTGAP LVGLSALMTT TLFNMEKIIK LLKANTDVKI MVGGAVLTEE YAYKIGADYY GKTAQDAVKI ADKFFLKNAL LCKTCGI // ID D7B0C8_NOCDD Unreviewed; 303 AA. AC D7B0C8; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADH66335.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ADH66335.1}; GN OrderedLocusNames=Ndas_0891 {ECO:0000313|EMBL:ADH66335.1}; 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 {ECO:0000313|EMBL:ADH66335.1, ECO:0000313|Proteomes:UP000002219}; RN [1] {ECO:0000313|EMBL:ADH66335.1, ECO:0000313|Proteomes:UP000002219} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23218 / DSM 43111 / IMRU 509 / JCM 7437 / NCTC 10488 RC {ECO:0000313|Proteomes:UP000002219}; 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 ----------------------------------------------------------------------- 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; ADH66335.1; -; Genomic_DNA. DR RefSeq; WP_013151942.1; NC_014210.1. DR RefSeq; YP_003678841.1; NC_014210.1. DR EnsemblBacteria; ADH66335; ADH66335; Ndas_0891. DR KEGG; nda:Ndas_0891; -. DR PATRIC; 38211590; VBINocDas52663_0924. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR BioCyc; NDAS446468:GHUM-910-MONOMER; -. DR Proteomes; UP000002219; Chromosome 1. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002219}; KW Methyltransferase {ECO:0000313|EMBL:ADH66335.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002219}; KW Transferase {ECO:0000313|EMBL:ADH66335.1}. SQ SEQUENCE 303 AA; 31694 MW; 1090D17D902E17EF CRC64; MAGTAPSRRP LVLDGGLATR LEAYGRDLGG GLWSARLLAE EPDLVRRVHR DYFEAGADVA IAAGYQASVP ALTARGATES EALALIARSV ELARAERDAF GSGLVAAGVG PYGAARADGS EYTGDYDLDE EGLYAWHRER WRVLADSGAD LLACETVPSA AEARALARLL AETPGARAWI SFSCRDGERV SDGTPLREAA AGLAPLHADG RLVAVGVNCT APRHVPALVR AVAACGLPAV AYPNSGEEWD AARGRWTGTA EPEEFGRAAV GWYEAGAVLV GGCCRTGPEH VRSVRAHLDR AAP // ID D7B417_NOCDD Unreviewed; 1156 AA. AC D7B417; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 27-MAY-2015, entry version 38. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADH66978.1}; GN OrderedLocusNames=Ndas_1549 {ECO:0000313|EMBL:ADH66978.1}; 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 {ECO:0000313|EMBL:ADH66978.1, ECO:0000313|Proteomes:UP000002219}; RN [1] {ECO:0000313|EMBL:ADH66978.1, ECO:0000313|Proteomes:UP000002219} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23218 / DSM 43111 / IMRU 509 / JCM 7437 / NCTC 10488 RC {ECO:0000313|Proteomes:UP000002219}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002040; ADH66978.1; -; Genomic_DNA. DR RefSeq; WP_013152585.1; NC_014210.1. DR RefSeq; YP_003679484.1; NC_014210.1. DR EnsemblBacteria; ADH66978; ADH66978; Ndas_1549. DR KEGG; nda:Ndas_1549; -. DR PATRIC; 38213030; VBINocDas52663_1638. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; NDAS446468:GHUM-1573-MONOMER; -. DR Proteomes; UP000002219; Chromosome 1. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002219}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002219}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 225 225 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 292 292 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 735 735 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1156 AA; 126490 MW; 3FFF29C3997FA075 CRC64; MRASPTFRET LSRRVVVADG AMGTMLQAHD LDLDQFEGHE GCNDILNLTR PDIVRDTHAA FLAVGSDAIE TNTFSANLGG LAEYGIEDRT YEIAHAGAQV AREAADAYST PDQPRYVLGS VGPGNRLPTL GHAPYTQLRD YYEQCARGLI DGGSDAILIE TCQDLLQVKA AVVAAQRARR AAGRDVPIIA QVSIETNGTM LLGSEIGAAL TSLEPLGVDV IGLNCSTGPA EMSEHLRYLS HHSPIPISCM PNAGLPQLGP DGAFYDLSPA ELADAHDSFT SEFGLSLAGG CCGTTPEHLR HVVERVQGRG IKNRKPLVEA ASSSLYQSVP FRQDASYLAV GERTNANGSK KFREAMLEGR WDDCVEIARD QIRDGAHLLD LNIDYVGRDG VSDMRELASR LATSSTLPIM LDSTEPPVLE AGLEALGGRS VVNSVNYEDG DGPDSRFTRI MGLVKEHGAA VVGLCIDEEG QARTAEWKVR VATRLIEQIT GEWGLNTSDI MIDCLTFPIT TGQEETRRDG LETINAIREL KRLYPDVQTT LGLSNLSFGL NPAARIVLNS VFLHEAVQAG LDSAIVHASK IVPINQIPEE QREVALDMVY DRREGDYDPL SRFMEMFEGV DAKSMKASRA EELAALPLWE RLERRIIDGE MTGIEADLDE ALESKPALAI VNDTLLSGMK TVGELFGSGQ MQLPFVLKSA EVMKGAVAYL EPHMEKSDDD GKGRIVLATV KGDVHDIGKN LVDIILSNNG YDVVNIGIKQ PVSAILEAAE EQRADVIGMS GLLVKSTVIM KENLEEMNSR GLSERFPVLL GGAALTRSYV EQDLAEVFDG HVRYAKDAFE GLRLMDAFMA VKRGDEGAEL PALRQRRVKT GAKLKVSEPE EVPARSDVST TNRVPKPPFL GDRISKGIPL ADYAAFLDER ATFMGQWGLK AARGGEGPSY EELVETEGRP RMRMWLDRIQ TDGLLEAAVV HGHFPCYSEG DDLVVLDEEG AERTRFTFPR QRRDRHLCLS DFFRPKESGE LDVVSFQVVT VGSAISRATA ELFAKNAYRD YLELHGLSVQ LTEALAEYWH TRVRAELGFA GEDPAELDAF FKLGYRGARF SLGYGACPDL EDRAKIMRLL EPERVGVTLS EEFQLVPEQA TDAIVVHHPE ATYFNV // ID D7BGK6_MEISD Unreviewed; 1223 AA. AC D7BGK6; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 29-APR-2015, entry version 35. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADH63822.1}; GN OrderedLocusNames=Mesil_1947 {ECO:0000313|EMBL:ADH63822.1}; 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 {ECO:0000313|EMBL:ADH63822.1, ECO:0000313|Proteomes:UP000001916}; RN [1] {ECO:0000313|EMBL:ADH63822.1, ECO:0000313|Proteomes:UP000001916} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700542 / DSM 9946 / VI-R2 RC {ECO:0000313|Proteomes:UP000001916}; RX PubMed=21304690; RA Sikorski J., Tindall B.J., Lowry S., Lucas S., Nolan M., Copeland A., RA Glavina Del Rio T., Tice H., Cheng J.F., Han C., Pitluck S., RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., RA Goodwin L., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., RA Jeffries C.D., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.; RT "Complete genome sequence of Meiothermus silvanus type strain (VI- RT R2)."; RL Stand. Genomic Sci. 3:37-46(2010). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002042; ADH63822.1; -; Genomic_DNA. DR RefSeq; WP_013158375.1; NC_014212.1. DR RefSeq; YP_003685330.1; NC_014212.1. DR EnsemblBacteria; ADH63822; ADH63822; Mesil_1947. DR KEGG; msv:Mesil_1947; -. DR PATRIC; 38192691; VBIMeiSil18825_1985. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; MSIL526227:GJ9Q-1984-MONOMER; -. DR Proteomes; UP000001916; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001916}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001916}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 237 237 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 753 753 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1223 AA; 136111 MW; 8443312A97D751AA CRC64; MTHLGYQREA RAEAFPYLRA LSERVLIYDG AMGTEIFKYD LSAADYGAEQ YNGCPEMLNR TRPDVIEAIH KSYLEAGADV IETNTFGAFP HVLVEYGLEA EAYELAFAGA HLARRVADEH STPDQPRFVA GSMGPGTKLI SLGQISWEGL FESYRVCAQG LLDGGVDLIL IETCQDILQV RCAVLAARRA MKDVGREVPI QVQVTMETTG TMLVGTDDAA ALTVLEALPI DVVGFNCATG PDLMDTHVRF FCENATRWVS CLPNAGLPRN EGGRVVYDLT PAELARWQQK FVNEYGLNVV GGCCGTGPEH IRALAQALRR QPQKANRQGQ FPAQVASLYQ AIPLKQDTGI LIVGERTNAT GSKKFRELLF AEDWEGMLEL AQEQVAEGAH VLDVSVAWTG RDEVRDMREV VKRFATSVQI PIMIDSTQTD VMQAALEHLG GRAILNSVNL EDGLEKFDRV ASLARQHGAA LVALTIDEDK EAGMAKTPER KVEIALRMYE RLTQVHGIPG SSILFDLLTF PITQGDEDTR KLAMWTIEGI RRVRELLPEV GFILGISNVS FGLSPQARVV LNSVFLDECI KAGLTAAILN AGKIRPINQI PEEQYQLALD LIYDRRTFNP DGSVAHDPLF AFVDYFAKNK VERSSAADPF TGLSVEERLK KRIIEGRKVG LEADLESALQ AGYTPVSLIN EVLLEGMKVV GDLFGAGKMQ LPFVLQAAET MKAAVRYLEP KMDRLEGVHK GTMVLATVKG DVHDIGKNLV DIILSNNGYK VVNLGIKKPI EEILAAVEEH RPQAVGMSGL LVKSTVVMKE NLEYMRERGY RIPVILGGAA LNRHYVENDL RQTYTTGTVY YASDAFDGLQ LMDELCGHAP PKLTSRFQSG HKYKTAYEIL MEKLEAGSEY VPSNIPPAAR IPRPPFWGRQ VVRSGVGKTL PQRAGRLETQ GRFPSGRRSR TPGGELDLGV IAQYVNKNAL FRGQWGFRRG EMDKAEYAHK LEREAEPIFR ELLDQAMREG TLEPAVAYGF WPVASDKNKL VVFDPESGAE LFAFDFPRQM GQNSRHLCIA DFFRPRYADA VGDEESWIPR AAWENGARDV LGCQVVTMGR TASEYAAKLF SSDRYQDYLY WHGFSVEMAE ALAEYWHKRV RQQLGIAQDD ATDLQALFQQ GYQGSRYSFG YPACPRLEDQ RYLQDLLQWQ EIGVELSEEF QLHPEQSTSA IVVHHPSAKY FNL // ID D7BST9_STRBB Unreviewed; 1174 AA. AC D7BST9; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 29-APR-2015, entry version 36. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADI11586.1}; GN OrderedLocusNames=SBI_08468 {ECO:0000313|EMBL:ADI11586.1}; OS Streptomyces bingchenggensis (strain BCW-1). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=749414 {ECO:0000313|EMBL:ADI11586.1, ECO:0000313|Proteomes:UP000000377}; RN [1] {ECO:0000313|EMBL:ADI11586.1, ECO:0000313|Proteomes:UP000000377} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BCW-1 {ECO:0000313|EMBL:ADI11586.1, RC ECO:0000313|Proteomes:UP000000377}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002047; ADI11586.1; -; Genomic_DNA. DR RefSeq; WP_014181035.1; NC_016582.1. DR RefSeq; YP_004966717.1; NC_016582.1. DR EnsemblBacteria; ADI11586; ADI11586; SBI_08468. DR KEGG; sbh:SBI_08468; -. DR PATRIC; 43275136; VBIStrBin158249_8713. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; SBIN749414:GHKA-8550-MONOMER; -. DR Proteomes; UP000000377; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000377}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000377}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 238 238 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 751 751 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1174 AA; 127746 MW; 2933EEE3815562B4 CRC64; MASHTPTSAA TDPADRVRAL REALATRVVV ADGAMGTMLQ AQDPTLEDFQ QLEGCNEILN VTRPDIVRSV HAEYFEAGVD CVETNTFGAN HAALGEYEIS DRVYELSEAG ARVAREVADG FAADGRPRWV LGSIGPGTKL PTLGHAPYTV LRDAYQANAE GLIAGGADAL LVETTQDLLQ TKAAVLGARR ALDASGSDAP VICSVTVETT GTMLLGSEIG AALTALEPLG IDMIGLNCAT GPAEMSEHLR YLARHSRIPL SCMPNAGLPV LGKDGAHYPL TPGELADAQE TFVREYGMSL VGGCCGTTPE HLRQVVERVR ELTPTERTPR PEPGAASLYQ TVPFRQDTSY LAIGERTNAN GSKKFREAML EGRWDDCVEM AREQIREGAH LLDLCVDYVG RDGVADMEEL AGRFATASTL PLVLDSTEVD VIRAGLEKLG GRAVINSVNY EDGDGPDSRF AKVTRLAQEH GAALIALTID EEGQARTPQK KVEIAERLIA DLTGNWGIHE ADILIDTLTF TICTGQEESR KDGVATIEAI RELKRRHPDV QTTLGLSNIS FGLNPAARIL LNSVFLDECV KAGLDSAIVH ASKILPIARF DEEQVTTALD LIHDRRSEGY DPLQKLMALF EGATAKSLKA GKAEELAALP LEERLKRRII DGERNGLEAD LDEALQERPA LDIVNETLLD GMKVVGDLFG SGQMQLPFVL QSAEVMKTAV AHLEPYMEKS EDSDGAGKGT IVLATVRGDV HDIGKNLVDI ILSNNGYNVV NLGIKQPVSA ILDAAQEHRA DVIGMSGLLV KSTVIMKENL EELNQRKLAA EYPVILGGAA LTRAYVEQDL HEIYEGEVRY ARDAFEGLRL MDALVAVKRG VPGATLPELK QRRVPKRAAA VAVVEPDQGP VRSDVATDNP VPTPPFWGSR VVKGIQQADY ASWLDEGALF KGQWGLKQAR TGEGPSYEEL VETEGRPRLR GWLDKLHTEN LLEAAVVYGY YRCVSKGDDL VLLNSDSSEL TRFTFPRQRR GRRLCLADFF RPEESGETDV VGLQVVTVGS KIGEATAELF AADSYRDYLE LHGLSVQLAE ALAEYWHARV RAELGFASED PADVTDMFDL KYRGARFSLG YGACPDLEDR AKIADLLRPE RIGVKLSEEF QLHPEQSTDA IVIHHPEAKY FNAR // ID D7C8F2_STRBB Unreviewed; 308 AA. AC D7C8F2; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:ADI06341.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ADI06341.1}; GN Name=mmuM {ECO:0000313|EMBL:ADI06341.1}; GN OrderedLocusNames=SBI_03220 {ECO:0000313|EMBL:ADI06341.1}; OS Streptomyces bingchenggensis (strain BCW-1). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=749414 {ECO:0000313|EMBL:ADI06341.1, ECO:0000313|Proteomes:UP000000377}; RN [1] {ECO:0000313|EMBL:ADI06341.1, ECO:0000313|Proteomes:UP000000377} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BCW-1 {ECO:0000313|EMBL:ADI06341.1, RC ECO:0000313|Proteomes:UP000000377}; 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 ----------------------------------------------------------------------- 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; ADI06341.1; -; Genomic_DNA. DR RefSeq; WP_014175818.1; NC_016582.1. DR RefSeq; YP_004961472.1; NC_016582.1. DR EnsemblBacteria; ADI06341; ADI06341; SBI_03220. DR KEGG; sbh:SBI_03220; -. DR PATRIC; 43264264; VBIStrBin158249_3338. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR BioCyc; SBIN749414:GHKA-3233-MONOMER; -. DR Proteomes; UP000000377; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000377}; KW Methyltransferase {ECO:0000313|EMBL:ADI06341.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000377}; KW Transferase {ECO:0000313|EMBL:ADI06341.1}. SQ SEQUENCE 308 AA; 32679 MW; 7919BC5047BBA6E7 CRC64; MSARRTPLAA ALERGPLVLD GGLSNQLEAQ GCDLSDELWS ARLLADDPRQ IEEAHAAYAR AGARVLITSS YQATYEGFAR RGVLEKEATA LLERSVELAR RAAEGAGGTV DRPVWVAASV GPYGAMLADG SEYRGRYGLS VGELERFHRP RIEALAAAGP DVLALETVPD ADEAEALLRA VEGCGIPVWL SYSIAGEHTR AGQPLREAFA LAAGNDQVLA VGVNCCEPGD ADRAVEVAAT TTGKPVVVYP NSGEEWDAKA RGWRGRATFD PARVKAWRDA GARLIGGCCR VGPDRIAELA AVMADERK // ID D7CLC9_SYNLT Unreviewed; 852 AA. AC D7CLC9; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 01-APR-2015, entry version 28. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADI01514.1}; GN OrderedLocusNames=Slip_0734 {ECO:0000313|EMBL:ADI01514.1}; OS Syntrophothermus lipocalidus (strain DSM 12680 / TGB-C1). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Syntrophomonadaceae; OC Syntrophothermus. OX NCBI_TaxID=643648 {ECO:0000313|EMBL:ADI01514.1, ECO:0000313|Proteomes:UP000000378}; RN [1] {ECO:0000313|Proteomes:UP000000378} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 12680 / TGB-C1 {ECO:0000313|Proteomes:UP000000378}; 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; ADI01514.1; -; Genomic_DNA. DR RefSeq; WP_013174916.1; NC_014220.1. DR RefSeq; YP_003702079.1; NC_014220.1. DR EnsemblBacteria; ADI01514; ADI01514; Slip_0734. DR KEGG; slp:Slip_0734; -. DR PATRIC; 38267870; VBISynLip21176_0758. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR BioCyc; SLIP643648:GHUR-752-MONOMER; -. DR Proteomes; UP000000378; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000378}; KW Methyltransferase {ECO:0000313|EMBL:ADI01514.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000378}; KW Transferase {ECO:0000313|EMBL:ADI01514.1}. SQ SEQUENCE 852 AA; 91419 MW; 33FC07F91C7F848B CRC64; MFWVKGVKHL IKDLASLLRE RIIILDGAMG TMLQERGLRP GDCPELFGLE HPEVLEEIHG QYIEAGADII QTNTFGANRF KLTEYGLQDR VAEINKAAVK AAKKVAGSGA LVAIDIGPTG RLLQPAGDAT FDQLYEAFRE QVVAGAEAGA DLVSIETMTD IGELRAAVIA ARENTDLPIL AHLTFEPNGR TMMGTSPAGA ALVLEALGVT AIGANCSGGA KELLPVIEEM ARVTGIFLSV EPNAGLPKLE NGRTIFPETP ESMAVYALSL REAGANLIGG CCGTTPAHIR AMAEILRGLP PVTRRPKRVR ALASRSRYVV LSEDSPLHFI GERINPTARK KLGQDIAQGS MAMVAEEARK QVEAGAPLID VNVGVPGIDE PSAMEKAVIA VQSSVDVPIS IDSANSAAVE AALKAFVGRP LINSTTGEQK VLERILPLAK KYGAAVLGLC LDEKGIPSTA GERFEIAVRI LEQARLYGLR EEDIYIDCLV KTAGAEQAQV METIKCVRMV RERLGLATVL GISNVSHGLP AREILNSTYL AMALGSGLDL PIINPFDQRI REVILASGVL LNRDISARKF VGEFKDRTSL PSEAARPRSW VCEKCNIPLL VAGKPPGGVD DASRLPVVAG DEKIKQEEGS KGADIAARIE EAVVKGEEHL IVGLVKEALA AGIAALEVVN KSLIPGIEKV GELYEKQEYF LPQLMLSAET MKKGFATVRP FLTQQAQQQF GTIIMATVEG DIHDIGKNIV SLMLENYGFK VIDLGKNVPA QRIVEEAVRS RADIVGLSAL MTTTMPRMGE VIERLREKGL GCRVMVGGAV LTQEYAERIG ADAYARDARE AVIKARKLCN LD // ID D7CTS8_TRURR Unreviewed; 1235 AA. AC D7CTS8; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 27-MAY-2015, entry version 36. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADI15625.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADI15625.1}; GN OrderedLocusNames=Trad_2519 {ECO:0000313|EMBL:ADI15625.1}; OS Truepera radiovictrix (strain DSM 17093 / CIP 108686 / LMG 22925 / OS RQ-24). OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; OC Trueperaceae; Truepera. OX NCBI_TaxID=649638 {ECO:0000313|EMBL:ADI15625.1, ECO:0000313|Proteomes:UP000000379}; RN [1] {ECO:0000313|Proteomes:UP000000379} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17093 / CIP 108686 / LMG 22925 / RQ-24 RC {ECO:0000313|Proteomes:UP000000379}; 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 Ovchinnikova G., Munk A.C., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., RA Tindall B., Pomrenke H.G., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Truepera radiovictris DSM 17093."; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002049; ADI15625.1; -; Genomic_DNA. DR RefSeq; WP_013178986.1; NC_014221.1. DR RefSeq; YP_003706168.1; NC_014221.1. DR EnsemblBacteria; ADI15625; ADI15625; Trad_2519. DR KEGG; tra:Trad_2519; -. DR PATRIC; 38302294; VBITruRad72214_2530. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; TRAD649638:GH4M-2564-MONOMER; -. DR Proteomes; UP000000379; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000379}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADI15625.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000379}; KW Transferase {ECO:0000313|EMBL:ADI15625.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 757 757 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1235 AA; 134716 MW; 2E377695C65D912B CRC64; MKRKASAAAL QEALKRRVLV LDGAMGTMIQ RHNLTEADFR GARFRNHDRP LRGANDLLTL TQPELIEGIH RAYLEAGADI IETNTFSATR VGMSEYGVDE VLYELNVQAA RLARRAADAL STPDKPRFVA GALGPTNRTA SMSPDVNNPG FRAVDFDTLV ASYYEQVRGL LEGGADIILI ETVFDTLNCK AALFAAESVF EDVGVQLPLM VSGTITDASG RTLSGQTLEA FLISVSHAPL LSVGLNCALG PKELGPYVAE LSRLTGLYTS VYPNAGLPNA FGGYDETPAS MQRTMAAWLN EGWVNLIGGC CGTTPEHIAA FAEAAAGVPP RVPPELPPLS AFAGLEPLVL RSDSNFVNVG ERTNVTGSKK FLRLIREERF DEALSVAREQ VEGGAQIIDV NMDEAMLDAE RAMVRFLNLV AAEPDIARVP VMLDASKFEV LESGLKRLQG KGIVNSLSLK EGEAVFREQA ARVRRYGAAV VVMAFDERGQ ADTFERRIEI CARAYRILVH EVGFPPQDII FDPNIFPVAT GIEGHNRYAL DFFRATRWIK EHLPGALVSG GVSNVSFSFR GNTRVREAMH AAFLYHARQA GMDMGIVNPA MLEVYEQIPK DLLEHVEDVL LDRRPDATER LLAFAASVKG GDQKGAKDEA WRAQGVEKRL EHALVKGVTD FIEADTEEAR QRLGSPLAVI EGPLMAGMNV VGDLFGSGKM FLPQVVKSAR VMKRAVAYLT PYLEAEKAGE RTSAGKVLLA TVKGDVHDIG KNIVGVVLAC NGFEVLDLGV MVPTEKILET AERENVDVIG LSGLITPSLD EMVEVARALE RRGSRTPLLI GGATTSRVHT AVKIAPQYSG LTVHVLDASR SVGVAARAAS ATERPKLHAE VRAQYAELRR QHERRQLGRQ LIPLAQARAN APRLTYAPTP PSFLGVRAFD DYPLSELVAY IDWTPFFLAW ELSGRYPHIL DDPVVGEAAR RLFEDAQTTL GELVAGEKLR ARGVVGFFPA ARVGDDIELY MDERRTEVRA VLHTLRQQGG KREGQPNLAL ADFVAPKGER DYVGGFAVAI HGAEALAAAY ERQHDDYSAI LVKALADRLA EAFAERLHER VRRELWGYAP DEALTNDDLI RERYRGIRPA PGYPAQPDHT EKATLFGLLD AETLAGVRLT ESFAMHPGAA VSGLYFAHPE ARYFGVGKLG RDQVADYAAR KGAALREVER WLAPNLAYDP SAPQEAEPEV LAPTP // ID D7DNI8_METV0 Unreviewed; 1265 AA. AC D7DNI8; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 27-MAY-2015, entry version 34. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADI30989.1}; GN OrderedLocusNames=M301_2632 {ECO:0000313|EMBL:ADI30989.1}; OS Methylotenera versatilis (strain 301). OC Bacteria; Proteobacteria; Betaproteobacteria; Methylophilales; OC Methylophilaceae; Methylotenera. OX NCBI_TaxID=666681 {ECO:0000313|EMBL:ADI30989.1, ECO:0000313|Proteomes:UP000000383}; RN [1] {ECO:0000313|Proteomes:UP000000383} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=301 {ECO:0000313|Proteomes:UP000000383}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002056; ADI30989.1; -; Genomic_DNA. DR RefSeq; WP_013149296.1; NC_014207.1. DR RefSeq; YP_003675566.1; NC_014207.1. DR EnsemblBacteria; ADI30989; ADI30989; M301_2632. DR KEGG; meh:M301_2632; -. DR PATRIC; 38201671; VBIMetSp140979_2650. DR KO; K00548; -. DR BioCyc; MVER666681:GHRP-2685-MONOMER; -. DR Proteomes; UP000000383; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000383}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000383}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 260 260 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 325 325 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 326 326 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 793 793 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1265 AA; 138881 MW; 64C8573CA423487C CRC64; MPATSLKEQS LTEQTLRSLL QQRILILDGA MGTMIQQYKL TEADYRGSEF ADFKAPAGER ELFVKGNNEL LTLTQPHIIQ EIHEKYLAAG ADIIETNTFG ATSVAQDDYH MAHLVYEMNV QAAKLAKASC EKYSTPDKPR FVAGTLGPTP KTASISPDVN DPAARNVNFD QLVNAYLEQA RALVEGGSDI LMVETIFDTL NCKAALFAID AFFEEVGYTM PVMISGTVTD ASGRILSGQT VTAFWNSVRH AKPITIGLNC ALGATLMRPY VEELSKIADT FVCIYPNAGL PNPMSDTGFD ETPDVTSSLV KEFATSGFLN IAGGCCGTTP AHINAIYNEI KDIAPRQVPT IPEYTRLAGL EPFVIDENSL FVNVGERTNV TGSKAFARMI INEQYDEALS VARQQVENGA QVIDINMDEG MLDAVKAMTH FLNLIASEPD IARVPIMIDS SKWSVIEAGL KCVQGKSIVN SISMKEGEAE FLRQAKLCRR YGAAVIVMAF DEKGQADTYA RKIEICKRAY DLLVGMDFPP EDIIFDPNIF AIATGIEEHN NYAVDFIEAT RWIKQNLPHA KISGGVSNVS FSFRGNDPAR EAIHTVFLYH AIKAGMTMGI VNAGMMGVYD DLAPELKERV EDVVLNRITD PDNLLAPTER LIEIAGSLVA GGKKEAATLE WRGTPEAPVP VEKRLSYAMV HGITEFIVED TEEARAAVEA NGGRPIHVIE GPLMSGMNVV GDLFGQGKMF LPQVVKSARV MKQAVAHLIP YIEAEKAADE KRTGIVAKPK GKMVIATVKG DVHDIGKNIV SVVLQCNNFE VVNMGVMVPA AEILAMAKAE NADIIGLSGL ITPSLEEMTH IAKEMQRDPY FKDMKMPLLI GGATTSRAHT AVKIAPHYDG PIVYVPDASR SVSVMQNLLT PETRGAYLAE IQADYEKART QHANKKGVPL LTLADARKNK MALSFAGEFA PVKPKFIGRR VFKNIDLSLI AKYIDWAPFF QTWDLAGAYP AILSDHVVGE AASKVFAEAQ DMLKKIIDGR WLSANGVIAL QPANTVNDDD IEIYTDETRS QVAFTYYGMR QQSVKPVIDG VPRPNQCLSD FVAPKGVADY VGLFAVTAGL GIEKIEKRFI DAQDDYSGIM FKSLADRLAE AFAEYMHERI RTDFWGYAAD EKLSVDALIK EQYQGIRPAP GYPACPDHTV KPDMFNLLQC DEISMKLTES FAMQPAAAVS GFYFAHKEAK YFSVDKIGTD QLEDMAKRRN LPKDYLERWL APNLS // ID D7E529_NOSA0 Unreviewed; 1176 AA. AC D7E529; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 29-APR-2015, entry version 38. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADI63826.1}; GN OrderedLocusNames=Aazo_1661 {ECO:0000313|EMBL:ADI63826.1}; OS Nostoc azollae (strain 0708) (Anabaena azollae (strain 0708)). OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus. OX NCBI_TaxID=551115 {ECO:0000313|EMBL:ADI63826.1, ECO:0000313|Proteomes:UP000001511}; RN [1] {ECO:0000313|EMBL:ADI63826.1, ECO:0000313|Proteomes:UP000001511} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=0708 {ECO:0000313|EMBL:ADI63826.1, RC ECO:0000313|Proteomes:UP000001511}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002059; ADI63826.1; -; Genomic_DNA. DR RefSeq; WP_013190844.1; NC_014248.1. DR RefSeq; YP_003720949.1; NC_014248.1. DR ProteinModelPortal; D7E529; -. DR EnsemblBacteria; ADI63826; ADI63826; Aazo_1661. DR KEGG; naz:Aazo_1661; -. DR PATRIC; 38225829; VBINosAzo102301_2227. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; TAZO551115:GH0O-1669-MONOMER; -. DR Proteomes; UP000001511; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001511}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001511}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 228 228 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 737 737 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1176 AA; 131183 MW; 782362FFF81DC255 CRC64; MTHPFLKRLH SPERPVIVFD GAMGTNLQTQ NLTAEDFGGA QYEGCNEYLV HSKPEAVAQV HRDFLTAGAD VIETDTFGAM SIVLAEYDLA DQAYYLSKKA AELAKSITSE FSTTEKPRFV AGSIGPTTKL PTLGHIDFDT MKASFAEQAE ALFDGGVDLF LVETCQDVLQ IKAALNAIEE VFGKKGERRP LMVSVTMETM GTMLVGTEIA AVMTILEPYP IDILGLNCAT GPDLMKPHIK YLSEHSPFVV SCIPNAGLPE NVGGQAHYKL TPVELRMALM HFIEDLGVQV IGGCCGTRPE HIQQLAEIAQ DLKPKVRQPS LEPAAASIYT TQPYQQDNSF LIVGERLNAS GSKKCRDLLN AEDWDGLVSM ARSQVKEGSH ILDINVDYVG RDGVRDMHEL VSRIVNNVTL PLMLDSTEWE KMEAGLKVAG GKCLLNSTNY EDGEPRFLKV LELAKKYGAG VIIGTIDEDG MARTAEKKFL IAQRAYRQAV EYGIGPTEIF FDTLALPIST GIEEDRKNGK ATIESIRRIR QELPGCHIIL GVSNISFGLN PASRIVLNSM FLHEAMTAGM DAAIVSASKI LPLAKIESQH QEVCRQLIYD ERKFDGDVCI YDPLGELTSI FAGVKTKPKT SFDETLPIEE RLKLHIIDGE RIGLEAQLTK ALEQYPPLEI INTFLLDGMK VVGELFGSGQ MQLPFVLQSA ETMKTAVAYL EPFMEKSESG NNAKGTFVIA TVKGDVHDIG KNLVDIILSN NGYKVINLGI KQSVENIIQA YEQHKPDCIA MSGLLVKSTS FMKENLQVFN EQGITIPVIL GGAALTPKFV NQDCQGTYKG KVVYGKDAFC DLHFMDKLMP AKNAGNWDDL KGFLDELGGS EESTHRHQEI VENTFKYQVA AEPKEIDTHR SEAVAIDIER PQPPFWGTQF LQPDDISLEE LLWYLDWQAL VAGQWQFRKL KEQSKEEYQA FLAEKVYPIL EGWKQRIIEE NLLHPQVIYG YFPCQSEGNS LHIYDVENQS QQIAIFEFPR QRSGRRYCIA DFFAPKESGI IDVFPMQAVT VGEVATEFAQ KLFADNQYTD YLYFHGVAVQ VAEALAEWTH ARIRRELGFG DAEPDNIRDM LAQRYQGSRY SFGYPACPNI QDQFKQLELL GTDRMKMFMD ESEQLYPEQS TTAIITYHPV AKYFTA // ID D7FUT0_ECTSI Unreviewed; 1224 AA. AC D7FUT0; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:CBJ31736.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CBJ31736.1}; GN Name=MTR {ECO:0000313|EMBL:CBJ31736.1}; GN ORFNames=Esi_0279_0006 {ECO:0000313|EMBL:CBJ31736.1}; OS Ectocarpus siliculosus (Brown alga). OC Eukaryota; Stramenopiles; PX clade; Phaeophyceae; Ectocarpales; OC Ectocarpaceae; Ectocarpus. OX NCBI_TaxID=2880 {ECO:0000313|Proteomes:UP000002630}; RN [1] {ECO:0000313|EMBL:CBJ31736.1, ECO:0000313|Proteomes:UP000002630} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ec32 / CCAP1310/4 {ECO:0000313|Proteomes:UP000002630}; RX PubMed=20520714; DOI=10.1038/nature09016; RA Cock J.M., Sterck L., Rouz 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.F., Bowler C., Boyen C., RA Brownlee C., Carrano C.J., Charrier B., Cho G.Y., Coelho S.M., RA Collon J., Corre E., Da Silva C., Delage L., Delaroque N., RA Dittami S.M., Doulbeau S., Elias M., Farnham G., Gachon C.M.M., RA Gschloessl B., Heesch S., Jabbari K., Jubin C., Kawai H., Kimura K., RA Kloareg B., Koepper 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-Collin 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., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; FN648463; CBJ31736.1; -; Genomic_DNA. DR InParanoid; D7FUT0; -. DR Proteomes; UP000002630; Chromosome LG16. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002630}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CBJ31736.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002630}; KW Transferase {ECO:0000313|EMBL:CBJ31736.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 208 208 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 271 271 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 272 272 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 745 745 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1224 AA; 135669 MW; CEA7543FDA44A647 CRC64; MLQDYHILVK GNNDMLSITQ PHIIKEIHTK YVDSGSDIIA TNTFSATTIA MADYEMEKDV YELNFESARL AREACEEATA KDPTKPRFVM GALGPTNRTG SISPDVEDPS FRNVTFDELV VAYKDQTKGL IDGGADIIIV ETIFDTLNAK AGVFAVREYF DEQGITDVPL FVSGTLVDQS GRTLSGQTTE GFYVSMRHCK PFCIGLNCAL GASQMRPFLQ RLAKVAECFV HVYSNAGLPN AMGGYDETPE DMARDNLLFA EEGLINMLGG CCGSTPAHIK AMKDAVEPCS TRALPPPREP FMWLSGLEDL IVTKERFQFL NVGERCNVSG SIRFKKLILK GDYQTAMDVA KQQVEDGAMV IDINLDDGLL DGMAAMQKFC KIAVTEPDVS KVPFMIDSSK FPIVEAGLKW VQGKSIVNSI SLKVGEEEFK RHARIVKAHG AAVVVMAFDE EGQAADCDNK VRICKRSYDM LVDEVGFPPE DIIFDPNILT IATGIDEHNN YAVDFIQATE RIKEICPYCK ISGGVSNLSF GFRGVNVIRE SMHSVFLFHA VKAGMDMGIV NAGMLEVYDD IEPGLLKIVE DAVNNRHSGA TEALLDAAEI EKEKALKNKG KGTVEASGWR TQGVQERLTH SLIKGIDQWV IEDVEECRLM LDDQGKRPLD VIEGPLMSGM NVVGDLFGAG KMFLPQVIKS ARVMKKAVAH LLPFMEAEKL AKMIADGIDP DSIDDEDDSQ YAGKVLIATV KGDVHDIGKN IVAVVLGCNN YKVYDMGVMQ PCDLILAKAK QLKVDVIGLS GLITPSLDEM VFVAKEMAKG GFKLPLLIGG ATTSKMHTAV KISPQYASPE TPVIHVLDAS RSVTVVGALL SDRKPDYVEE IMEEYEELRE EHYAGQEERH YLPFEKASSK RKNIDFEKRP PVPPPNKPGI TVVTGSYELD DVLDYIDWNP FFQTWELRGR YPNRGYPKIF NDESVGEEAK KLFEEAQVML KKIVKEKSLN LVGLVAIFPA ATVDGEDVEV YANDSREEVL ARFCMLRQQA EKESDDPYLS QADFIAPKES GVADYMGMFA IACMGCEKMV KEFEDLNDDY SKIMVQALTD RFVEAFAEKL HEDMRKDIWG YAPDEKVEGQ DLFKLKYQGI RPAPGYPSQP DHTEKRTMWD LLNAAELTGI ELSESLSMMP ASSVSALVFA HPDSEYFAVG TIAKDQVSSY AERKGMDLET CEKWLSPILS YDRD // ID D7G637_ECTSI Unreviewed; 436 AA. AC D7G637; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:CBJ27446.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:CBJ27446.1}; GN Name=HMT {ECO:0000313|EMBL:CBJ27446.1}; GN ORFNames=Esi_0071_0065 {ECO:0000313|EMBL:CBJ27446.1}; OS Ectocarpus siliculosus (Brown alga). OC Eukaryota; Stramenopiles; PX clade; Phaeophyceae; Ectocarpales; OC Ectocarpaceae; Ectocarpus. OX NCBI_TaxID=2880 {ECO:0000313|Proteomes:UP000002630}; RN [1] {ECO:0000313|EMBL:CBJ27446.1, ECO:0000313|Proteomes:UP000002630} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ec32 / CCAP1310/4 {ECO:0000313|Proteomes:UP000002630}; RX PubMed=20520714; DOI=10.1038/nature09016; RA Cock J.M., Sterck L., Rouz 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.F., Bowler C., Boyen C., RA Brownlee C., Carrano C.J., Charrier B., Cho G.Y., Coelho S.M., RA Collon J., Corre E., Da Silva C., Delage L., Delaroque N., RA Dittami S.M., Doulbeau S., Elias M., Farnham G., Gachon C.M.M., RA Gschloessl B., Heesch S., Jabbari K., Jubin C., Kawai H., Kimura K., RA Kloareg B., Koepper 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-Collin 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., 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; FN648938; CBJ27446.1; -; Genomic_DNA. DR InParanoid; D7G637; -. DR Proteomes; UP000002630; Unassigned sequences LGUn. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 2. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002630}; KW Methyltransferase {ECO:0000313|EMBL:CBJ27446.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002630}; KW Transferase {ECO:0000313|EMBL:CBJ27446.1}. SQ SEQUENCE 436 AA; 46996 MW; 0FCC0EF0406AC892 CRC64; MASSPLDPFL LENGFVVLDG GLATELEAQG ADLTGDLWSA ALLADNPSII RNTHLAYFRA GADVATSASY QASFEGFLRK GIGPERAEEL LLLSVRLAVE ARDQFWAEYQ EERPASRPAP TKPQTLRQPS QPTATAIEEE ENAKQHQQPV RGSDGRRHRR RLRPLVAASL GCYGAVLADG SEYRGDYVDT PAGSLKEFHA RRLEILARAD GVDMVVFETV PCLAEVRAIL SLLQDFRPRV SAVISVSCKD DQHLRSGERL HDFADLIWRH AEEQDAAEGP PAVVATTTTT TTRPACVAAV GVNCTSPSHA AGTLRALAAA RARPDARHGA PRETPPSRVA LVAYPNSGEE WDASVRDWVE GTGLRDREAG GGGGAEEFGR MARDEWFAAG ATVVGGCCRT RPAHVAEIRR ALASAAEEGV QEGEGQQRTG WHQEPS // ID D7GDP5_PROFC Unreviewed; 1163 AA. AC D7GDP5; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 29-APR-2015, entry version 32. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CBL56656.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CBL56656.1}; GN Name=metH {ECO:0000313|EMBL:CBL56656.1}; GN OrderedLocusNames=PFREUD_11340 {ECO:0000313|EMBL:CBL56656.1}; 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 {ECO:0000313|EMBL:CBL56656.1, ECO:0000313|Proteomes:UP000000936}; RN [1] {ECO:0000313|EMBL:CBL56656.1, ECO:0000313|Proteomes:UP000000936} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 9614 / CIP 103027 / CIRM-BIA1 RC {ECO:0000313|Proteomes:UP000000936}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; FN806773; CBL56656.1; -; Genomic_DNA. DR RefSeq; WP_013161030.1; NC_014215.1. DR RefSeq; YP_003688086.1; NC_014215.1. DR EnsemblBacteria; CBL56656; CBL56656; PFREUD_11340. DR KEGG; pfr:PFREUD_11340; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR BioCyc; PFRE754252:GI1A-1182-MONOMER; -. DR Proteomes; UP000000936; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000936}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CBL56656.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000936}; KW Transferase {ECO:0000313|EMBL:CBL56656.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 221 221 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 287 287 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 732 732 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1163 AA; 125930 MW; BEB59283D971A2E2 CRC64; MQNRDLREVL GHEVILGDGA MGTMLQAAVL GPDDFEGHDG CNEILNVTRP DVILDIHRAY LAAGSDVIET NTFGANAAAL GEYGITDRLA ELAGAGARLA RQAADEAGPG HWVFGSIGPG TKLPTLGHID FVTLRDAYYT QVSAMIDGGV DAVQIETCQD LLQAKAAVIG ARRAARDAHV DLPIIVDITV ETTGTMLLGS ETGAALTSLA PLGVDVIGLN CATGPTEMSE HLRYLSAHAD CAVMAMPNAG LPELTADGAV YPLGPDEFAR AQLDYVERYG LAIVAGCCGT TPEHIARLRA ALGAHRPVEH RDPELVNTVS SLYSEVELRQ ETSYLAVGER TNANGSKAFR EAMLAGDLET CIDLAKAQSR EGAHCLDLCV DYVGRDGVDD MAELSQRFST AVTLPVMLDS TEPEVIRSGL EHLAGRCIIN SVNFEDGDQP GSRFARLMPI IAEHGAAVVA LTIDEEGQAR TAERKVAIAE RLVDQLVGTW GMDEGDILVD CLTFPIATGQ EETRRDGLET LNAISEFKRR HPRAGTTLGV SNISFGLNAA ARVVLNSVFL HEAVEAGLDS AIVRAAKIMP MERIDPEQRQ VALDLIYDRR TPDYDPLTRM LDMFAGVSSA DVRAEHAAEL AALPLNERLR QRIIDGDTNG LTDDLDEALR TRGALDILNS DLLEGMKTVG ELFGSGQMQL PFVLQSAETM KRAVAHLEPH MDSTDEAGKG TLVLATVKGD VHDIGKNLVD IIVSNNGYTV VNLGIKQPIS AIVEAVKQNH ADAIGMSGLL VKSTMVMKDN LAELDRLGVG KDFPVMLGGA ALTRTFVEDD LQRDFSGQVR YAKDAFEGLS LMDSVMAIKH GDPDAALPEP RKHRVVARPR ATVEPADGGP VRSDVARPVP GSLDVPRAPW FGNRMAKGIG LAEITEWLDE RALFTGRWGL RGPRKTDGTR DLIEQEGRPR LRGWLDRIAA EGLAVPGVVY GYFPCYSQGN TLILLDPTTP EALDSEASRF DFPRQAAGRR LCIADFFRDR REAEEFGPDT VALQLVTMGE RFSQVTAELF AANAYRDYLE LHGLSVQLAE ALAELWHHRI RTELGIAGED GEMTAMLQKQ AYRGGRYSFG YGACPDLDQR SLIEDLLQPD RIGVHLSEEF QLHPEQSTDA IVVTHPEAKY FNT // ID D7GQF4_9FIRM Unreviewed; 590 AA. AC D7GQF4; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 27-MAY-2015, entry version 27. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=CK3_01590 {ECO:0000313|EMBL:CBL40029.1}; OS butyrate-producing bacterium SS3/4. OC Bacteria; Firmicutes; Clostridia; Clostridiales. OX NCBI_TaxID=245014 {ECO:0000313|EMBL:CBL40029.1, ECO:0000313|Proteomes:UP000008961}; RN [1] {ECO:0000313|EMBL:CBL40029.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SS3/4 {ECO:0000313|EMBL:CBL40029.1}; 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. SS3/4."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CBL40029.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SS3/4 {ECO:0000313|EMBL:CBL40029.1}; RA Pajon A.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; CBL40029.1; -; Genomic_DNA. DR RefSeq; WP_015552349.1; NC_021035.1. DR ProteinModelPortal; D7GQF4; -. DR EnsemblBacteria; CBL40029; CBL40029; CK3_01590. DR KEGG; bprs:CK3_01590; -. DR PATRIC; 42787459; VBIButBac106850_0229. DR KO; K00547; -. DR BioCyc; BBAC245014-WGS:GSHP-128-MONOMER; -. DR Proteomes; UP000008961; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008961}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:CBL40029.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000008961}; KW Transferase {ECO:0000313|EMBL:CBL40029.1}. SQ SEQUENCE 590 AA; 64776 MW; E67977D3AB9F08AF CRC64; MNLREYLKTT NLITDGAFGT YFAAKYQTQD IPELTNITAP EKVKKIHEEY LNAGAKFIRT NTFASNTETL QEDFAEVEKN IQAAVEIARD AVNGRDAWIA GDIGPIPVNG TEDAAAAADE YYQIAKTFAE CGVTVLDFET FADLDGILPA IKKICAEYEM FIMVSFSVNQ FGYSAAGLSA KRLLADAAAV PEIDAVGLNC GVGPAHMRQI LEKAGRPGDK FLLAIPNAGY PTLTRNKLQF GNTPAYFAEK MKELQALGAD ILGGCCGTTP EFIGELSSWD GILNKIVLDT ETDNGEQTGH VQRHGFLYDE NGERKQKKLI AVELAPPFDA DDEKLLESAH LLKNAGVDVL TFPDSPSGRT RVDSVLMASK VRQATGLNVM PHICCRDRNA IAMRSLFLGA AINDIHNFLI ITGDPIPSTA RQTVKAVFNS DSTGLMKIAK EMNEDVFAKN PLCYGGAINQ GRKNLDVEIG RVKKKMEEGA EFFLTQPVFT KEDAARLRRI KEETGATILC GIMPLISRKN AMFMKNEIAG VNVTDEIVAR YPEKANRKEG EAAGIQLAKE VMKMVEDFAD GYYFSFPFNR VYMLQDIMGK // ID D7GVK6_9FIRM Unreviewed; 830 AA. AC D7GVK6; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Clostridiales sp. SS3/4 draft genome {ECO:0000313|EMBL:CBL41848.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CBL41848.1}; GN ORFNames=CK3_22670 {ECO:0000313|EMBL:CBL41848.1}; OS butyrate-producing bacterium SS3/4. OC Bacteria; Firmicutes; Clostridia; Clostridiales. OX NCBI_TaxID=245014 {ECO:0000313|EMBL:CBL41848.1, ECO:0000313|Proteomes:UP000008961}; RN [1] {ECO:0000313|EMBL:CBL41848.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SS3/4 {ECO:0000313|EMBL:CBL41848.1}; 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. SS3/4."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CBL41848.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SS3/4 {ECO:0000313|EMBL:CBL41848.1}; RA Pajon A.; 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; FP929062; CBL41848.1; -; Genomic_DNA. DR RefSeq; WP_015554104.1; NC_021035.1. DR EnsemblBacteria; CBL41848; CBL41848; CK3_22670. DR KEGG; bprs:CK3_22670; -. DR PATRIC; 42791479; VBIButBac106850_0822. DR KO; K00548; -. DR BioCyc; BBAC245014-WGS:GSHP-1954-MONOMER; -. DR Proteomes; UP000008961; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008961}; KW Methyltransferase {ECO:0000313|EMBL:CBL41848.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008961}; KW Transferase {ECO:0000313|EMBL:CBL41848.1}. SQ SEQUENCE 830 AA; 87846 MW; D8AE2D4951C257F6 CRC64; MGILELMKER RIYFDGGMGS LLQARGLKPG ELPETWNLSR PEIITEIHRE YLDAGSDVVT TNTFGANHFK FKAEDGYSVK EIVTAAVRNA KNAIAAAGHG YAALDMGPTG KLLKPYGDLE FEDAYEAYKE VVLIGKAAGA DLVIIETMGD GYELKAAVLA AKENSDLPVF ATVTLDEKGK MLTGGNVESV TALLEGLGAD VIGLNCGLGP IQLLPFMRDM AKVSSTPILV NPNAGLPRSE GGKTVYDIDA DEFATAMQEM ARNGATVLGG CCGTTPEHIH KTKLVCDDIP VCEITDKNRT VISSYSHAVT FGGRPILIGE RINPTGKPKF KQALKDKDLT YILSMGVAQQ ESRADVLDVN VGLPGIDEPQ MMVDVVKELQ GVLDLPLQID TSDPVAMERA LRIYNGKPLI NSVNGKKEVM EQIFPLVKHY GGVVVALALD ENGIPETADG RLAVARKIYE TAASYGIPKK DILVDCLCMA VSSDKNGALT TLETVRRVRD ELGGKTVLGV SNVSFGLPMR ENINSSFFLL AMQNGLSAGI VNPNLEAMMQ AYDSFLVLSA QDENCAGYVG IYGPKEAEKK RQKEILKAAA VNQAAGVSGA AGAGNSNGAG NTSGTGTGAA DTGSALKKSI VKGMSQAAAD AAKLALKDTD ALELINTDMI PALDEVGKGF EAGTVFLPQL LMSAEAAKAA FAVVKESMEA SGEVQEKKGK VILATVKGDI HDIGKNIVKV LLENYSFDVM DLGRDVPPET IVEAAVKEHV PVVGLSALMT TTVPAMEDTI KALRKDAPWV KVMVGGAVLT QEYADAIGAD TYCKDAMASV NFATSVIGEA // ID D7H1A2_BRUAO Unreviewed; 139 AA. AC D7H1A2; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Dihydropteroate synthase {ECO:0000313|EMBL:EFH34095.1}; DE Flags: Fragment; GN ORFNames=BAYG_00491 {ECO:0000313|EMBL:EFH34095.1}; OS Brucella abortus bv. 5 str. B3196. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520453 {ECO:0000313|EMBL:EFH34095.1}; RN [1] {ECO:0000313|EMBL:EFH34095.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=B3196 {ECO:0000313|EMBL:EFH34095.1}; 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; GG774511; EFH34095.1; -; Genomic_DNA. DR RefSeq; WP_002970934.1; NZ_GG774511.1. DR EnsemblBacteria; EFH34095; EFH34095; BAYG_00491. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; FT NON_TER 139 139 {ECO:0000313|EMBL:EFH34095.1}. SQ SEQUENCE 139 AA; 15072 MW; E51CCE68A741EB77 CRC64; MASSLDDLFG ATAAKPDGSE VLAALTQAAR ERILILDGAM GTQIQGLGFH EEHFRGDRFA TCDCQLQGNN DLLTLTQPKA IEEIHYAYAM AGADILETNT FSSTSIAQAD YGMEAMVYDL NRDGARLARR AALRAEQKD // ID D7H1A3_BRUAO Unreviewed; 1113 AA. AC D7H1A3; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 01-APR-2015, entry version 27. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFH34096.1}; GN ORFNames=BAYG_00492 {ECO:0000313|EMBL:EFH34096.1}; OS Brucella abortus bv. 5 str. B3196. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=520453 {ECO:0000313|EMBL:EFH34096.1}; RN [1] {ECO:0000313|EMBL:EFH34096.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=B3196 {ECO:0000313|EMBL:EFH34096.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG774511; EFH34096.1; -; Genomic_DNA. DR EnsemblBacteria; EFH34096; EFH34096; BAYG_00492. DR PATRIC; 37826540; VBIBruAbo58081_0206. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 115 115 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 178 178 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 179 179 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 635 635 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1113 AA; 122645 MW; BA5FA2B070608CFF CRC64; MGPTNRTASL SPDVNNPGFR AVTFDDLRIA YSEQIRGLID GGSDIILIET IFDTLNAKAA VFATEEVFAE KGVRLPVMIS GTITDLSGRT LSGQTPTAFW YSLRHARPFT IGLNCALGAN AMRAHLDELS GIADTFICAY PNAGLPNEFG QYDETPEAMA AQIEGFARDG LVNVVGGCCG STPDHIRAIA QAVAKYEPRK PAKVPPLMRL SGLEPFTLTK DIPFVNIGER TNVTGSARFR KLVKAGDFAA ALDVARDQVA NGAQIIDINM DEGLIDSEKA MVEFLNLIAA EPDIARVPIM LDSSKWEVIE AGLKCVQGKA VVNSISLKEG EEAFLHHARL VRAYGAAVVI MAFDETGQAD TQARKIEICT RAYKILTEQV GFPPEDIIFD PNIFAVATGI EEHNNYGVDF IEATREIVRT LPHVHISGGV SNLSFSFRGN EPVREAMHAV FLYHAIQAGM DMGIVNAGQL AVYDTIDAEL REACEDVVLN RPTKTGESAT ERLLEIAERF RDSGSREART QDLSWREWPV EKRLEHALVN GITEYIEADT EEARLAAERP LHVIEGPLMA GMNVVGDLFG SGKMFLPQVV KSARVMKQAV AVLLPFMEEE KRLNGGEGRQ SAGKVLMATV KGDVHDIGKN IVGVVLACNN YEIIDLGVMV PSQKILQVAR DEKVDIIGLS GLITPSLDEM AHVAAEMERE GFDIPLLIGG ATTSRVHTAV KIHSRYERGQ AVYVVDASRA VGVVSNLLSP EGKQAYIDGL RNEYAKVAAA HARNEAEKQR LPIARARANP HQLDWENYEP VKPAFTGTKV FETYDLAEIA RYIDWTPFFQ TWELRGRYPA ILEDEKQGEA ARQLWADAQA MLRKIIDEKW FTPRAVVGFW PANAVGDDIR LFTDESRKEE LATLFTLRQQ LTKRDGRPNV AMADFVAPVE SGKQDYVGGF VVTAGIGEIA IAERFERAND DYSAILVKAL ADRFAEAFAE LMHERVRKEF WAYAPDEAFT PEELISEPYK GIRPAPGYPA QPDHTEKTTL FRLLDATANT GVELTESYAM WPGSSVSGLY IGHPESYYFG VAKVERDQVE DYARRKDMDV EAVERWLTPI LNYVPGASKD EAA // ID D7HD92_VIBCL Unreviewed; 1226 AA. AC D7HD92; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|EMBL:EFH73779.1}; GN ORFNames=VCRC385_00259 {ECO:0000313|EMBL:EFH73779.1}; OS Vibrio cholerae RC385. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=345074 {ECO:0000313|EMBL:EFH73779.1}; RN [1] {ECO:0000313|EMBL:EFH73779.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=RC385 {ECO:0000313|EMBL:EFH73779.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG774557; EFH73779.1; -; Genomic_DNA. DR RefSeq; WP_000514267.1; NZ_GG774557.1. DR ProteinModelPortal; D7HD92; -. DR SMR; D7HD92; 654-1224. DR EnsemblBacteria; EFH73779; EFH73779; VCRC385_00259. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFH73779.1}; KW Transferase {ECO:0000313|EMBL:EFH73779.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1226 AA; 135837 MW; 53C6B420D31D23C5 CRC64; MGKEVRQQLE QQLKQRILLI DGGMGTMIQS YKLQEEDYRG ARFVDWHCDL KGNNDLLVLT QPQIIKEIHS AYLEAGADIL ETNTFNSTTI AMADYDMQSL SAEINFAAAK LAREVADEWT AKDPSRPRYV AGVLGPTNRT CSISPDVNDP GFRNVTFDGL VEAYSESTRA LIKGGSDLIL IETIFDTLNA KACAFAVDSV FEELGISLPV MISGTITDAS GRTLSGQTTE AFYNALRHVR PISFGLNCAL GPDELRQYVE ELSRISECYV SAHPNAGLPN AFGEYDLSAE EMAEHIAEWA QAGFLNLVGG CCGTTPEHIA AIAKAVEGVK PRALPDLKVE CRLSGLEPLN IGPETLFVNV GERTNVTGSA RFKRLIKEEQ YDEALDVARE QVENGAQIID INMDEGMLDA EACMVRFLNL CASEPEISKV PVMVDSSKWE VIEAGLKCIQ GKGIVNSISL KEGKEKFIAQ AKLVRRYGAA VIVMAFDEVG QADTRERKLE ICRRAYHILV DEVGFPPEDI IFDPNIFAVA TGIEEHNNYA LDFINAVADI KRELPHAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK HGMDMGIVNA GQLEIYDNVP LKLREAVEDV ILNRRSDGTE RLLEIAEAYR ENSVGKEEDA SALEWRAWPV AKRLEHALVK GITEFIVQDT EEARQQASKP LEVIEGPLMD GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AYLEPFINAQ KSGSTSNGKI LLATVKGDVH DIGKNIVGVV LQCNNFEIID LGVMVPCEQI LKVAREQNVD IIGLSGLITP SLDEMVHVAK EMERQGFELP LLIGGATTSK AHTAVKIEQN YHAPVVYVNN ASRAVGVCTS LLSDELRPGF IERLDLDYER TRDQHARKTP KSRPVTLEQA RANKAALDWA NYTPPAPAKP GVHVFENIAL ATLRPYIDWT PFFMTWSLMG KYPAILEHEE VGEEAKRLFH DANALLDKVE REGLLKASGM CALFPAASVG DDIEVYSDES RTQVAHVLYN LRQQTEKPKG ANYCLSDYVA PKESGKRDWI GAFAVTGGIG ERALADAYKA QGDDYNAIMI QAVADRLAEA FAEYLHEKVR KEIWGYASDE NLSNDELIRE RYQGIRPAPG YPACPEHTEK ATLWQMLNVE ETIGMSLTTS YAMWPGASVS GWYFSHPDSR YFAVAQIQQD QLHSYAERKG WRLEEAEKWL APNLDA // ID D7HWC6_PSESS Unreviewed; 298 AA. AC D7HWC6; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFI00775.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EFI00775.1}; GN ORFNames=PSA3335_1123 {ECO:0000313|EMBL:EFI00775.1}; OS Pseudomonas savastanoi pv. savastanoi NCPPB 3335. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=693985 {ECO:0000313|EMBL:EFI00775.1, ECO:0000313|Proteomes:UP000005729}; RN [1] {ECO:0000313|EMBL:EFI00775.1, ECO:0000313|Proteomes:UP000005729} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCPPB 3335 {ECO:0000313|EMBL:EFI00775.1}; 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). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KB644113; EFI00775.1; -; Genomic_DNA. DR EnsemblBacteria; EFI00775; EFI00775; PSA3335_1123. DR PATRIC; 37948366; VBIPseSav158853_1190. DR Proteomes; UP000005729; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005729}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EFI00775.1}; KW Transferase {ECO:0000313|EMBL:EFI00775.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 207 207 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 298 AA; 31543 MW; 5D0F46ED7956B1BB CRC64; MTQGTTVILD GGMGRELQRR GAPFRQPEWS ALALSEAPEA VSAVHAAYIE SGAQVITSNS YAVVPFHIGE ERFAREGQAL AALAGRLARE TADASGGRAQ VAGSIPPLFG SYRPDLYKPE LAADVLRPLV AGLSPYVDLW LAETQSCILE AQTIRAGLLN DGKPFWLSFT LQDEDTDEVP RLRSGESVAD AAKAAAGMGV ATLLFNCSQP EVIGGAIDAA REVFKALNVD IAIGAYANAF PPQPKDAKAN DGLDELREDL DPQGYQQWAA DWVTRGATHI GGCCGIGPEH IAVLSKSL // ID D7I0E1_PSESS Unreviewed; 353 AA. AC D7I0E1; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFH99282.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EFH99282.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFH99282.1}; GN ORFNames=PSA3335_2642 {ECO:0000313|EMBL:EFH99282.1}; OS Pseudomonas savastanoi pv. savastanoi NCPPB 3335. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=693985 {ECO:0000313|EMBL:EFH99282.1, ECO:0000313|Proteomes:UP000005729}; RN [1] {ECO:0000313|EMBL:EFH99282.1, ECO:0000313|Proteomes:UP000005729} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCPPB 3335 {ECO:0000313|EMBL:EFH99282.1}; 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). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KB644141; EFH99282.1; -; Genomic_DNA. DR EnsemblBacteria; EFH99282; EFH99282; PSA3335_2642. DR PATRIC; 37951679; VBIPseSav158853_2808. DR Proteomes; UP000005729; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005729}; KW Methyltransferase {ECO:0000313|EMBL:EFH99282.1}; KW Transferase {ECO:0000313|EMBL:EFH99282.1}. SQ SEQUENCE 353 AA; 37882 MW; D3A34F9C556C10BD CRC64; MSDRSARHQA FLTALKQRIL ILDGGMGTMI QSYRLEEHGY RGKRFADWPS DVKGNNDLLI LTRPDVIGAI EKAYLDAGAD ILETNTFNAT QVSQADYGME SIVYELNVEG ARLARKVADA KTLETPDKPR FVAGVLGPTS RTCSLSPDVN NPGFRNVTFD ELVENYSEAT KGLIEGGADL ILIETIFDTL NAKAAIFAVQ GVFEEVGFEL PIMISGTITD ASGRTLSGQT TEAFWNSISH AKPISVGLNC ALGASELRPY LQELANKANT HVSAHPNAGL PNAFGEYDEL PSQTAKIIEE FAQSGFLNIV GGCCGTTPAH IKANCRGCFG LRATRNSGHS KSLPPVGPGA VHH // ID D7IAH5_9BACE Unreviewed; 241 AA. AC D7IAH5; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 29-OCT-2014, entry version 19. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFI05654.1}; DE Flags: Fragment; GN ORFNames=HMPREF9007_01127 {ECO:0000313|EMBL:EFI05654.1}; OS Bacteroides sp. 1_1_14. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=469585 {ECO:0000313|EMBL:EFI05654.1}; RN [1] {ECO:0000313|EMBL:EFI05654.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_1_14 {ECO:0000313|EMBL:EFI05654.1}; 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; GG774703; EFI05654.1; -; Genomic_DNA. DR RefSeq; WP_008760496.1; NZ_GG774703.1. DR EnsemblBacteria; EFI05654; EFI05654; HMPREF9007_01127. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; FT NON_TER 241 241 {ECO:0000313|EMBL:EFI05654.1}. SQ SEQUENCE 241 AA; 26313 MW; 06A37C511832D4ED CRC64; MKKTISQIVS ERILILDGAM GTMIQQYNLK EEDFRGERFA HIPGQLKGNN DLLCLTRPDV IQDIHRKYLE AGADIIETNT FSSTTVSMAD YHVEEYVREI NLAATRLARE LADEYTAKSP DKPRFVAGSV GPTNKTCSMS PDVNNPAFRA LSYDELAASY QQQMEAMLEG GVDAILIETI FDTLNAKAAI FAAGQAMKVT GIEVPVMLSV TVSDIGGRTL SGQTLEAFLA SVQHANIFSV G // ID D7IW56_9BACE Unreviewed; 1230 AA. AC D7IW56; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFI07173.1}; GN ORFNames=HMPREF0104_03682 {ECO:0000313|EMBL:EFI07173.1}; OS Bacteroides sp. 3_1_19. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=469592 {ECO:0000313|EMBL:EFI07173.1}; RN [1] {ECO:0000313|EMBL:EFI07173.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_19 {ECO:0000313|EMBL:EFI07173.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG774765; EFI07173.1; -; Genomic_DNA. DR RefSeq; WP_008780887.1; NZ_GG774765.1. DR ProteinModelPortal; D7IW56; -. DR SMR; D7IW56; 650-895. DR EnsemblBacteria; EFI07173; EFI07173; HMPREF0104_03682. DR GeneID; 5305570; -. DR PATRIC; 37879733; VBIBacSp40580_3686. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1230 AA; 136496 MW; 29C6AB3EDEF7E578 CRC64; MNKERFLRLL NERILILDGG MGTMIQSFKL NEQDYRGERF ADFPGQLKGN NDLLCITRPD VIQSIHRQYL DAGADIFATN TFNANAISMA DYAMEAYVRE INLAAGRLSR EVADTYMAEH PDRTIFVAGS IGPTNKTASM SPDVSDPAYR AVTYKDLYNA YKEQVEGLVD GGVDIILFET TFDTLNVKAG LEAAEVVLKE KEKDLPIMLS LTLSAQGGRT FSGQTLLAFL ASIQHTHIVS VGLNCSFGAA DMKPYLQELA KYAPYYISAY PNAGLPNSFG TYDETPDKMA QHVKPFVEEG LVNIIGGCCG TTPAHISRYP ELVKGAKPHI PALKPDCLWL SGLELLEVKP ENNFVNVGER CNVAGSRKFL RLIKEGSYEE ALTIARKQVE DGAQVIDINM DDGMLDAVKE MKTFLNLIAS EPDIARVPVM IDSSKWEVIE EGLMCVQGKS IVNSISLKEG EEVFLKHAAR IKQLGAAAVV MAFDEKGQAD TYERKIEICE RAYRLLIEKI DFNPQDIIFD PNVLAIATGM EEHNGYGLAF IRAVEWIKKN LPGAKVSGGV SNLSFSFRGN NHVREAMHSV FLYHAIGKGM DMGIVNPSTS VLYEDIEPEF RTLLEDVILA RRPEAAEELI TYAQNLHVQA SGETPEKHEA WRELSLKERL EHALIKGIGD YLEDDLQEAL RTYSHAVDII DGPLMSGMNK VGELFGAGKM FLPQVVKTAR TMKKAVAILQ PAIESEKKAS GSAKAGKVIF ATVKGDVHDI GKNIVSIVLS CNNYEVIDLG VMVPADVIIK KAIEEKPDLV CLSGLITPSL EEMAHVADEM QKAGLTIPMM VGGATTSKLH TAVKIAPHYD YPVIHVLDAS QNPLIAAKLL NPDTRDAYIR ELEQEQEALR ASLGQKKETL ASLSEARKHP IEIDWTGYTP VVPARMGVHV IPYIPLEEVI PYIHWTFFFS AWKLNGRFSE ISQIHGCDSC RASWLAGFPE KDRAKATEAM QLYKDAVRLL DRLVNMKVEY CKAIYGFFSA NSEGDTIRMG DIALPLLRQQ VKKEENIYKC LSDYVIPVSE ERTDYVGAFV VTAGAGADCL KDKFEEEGDT YNSMLLQTLT DRLAEATAEY LHEKVRKEYW GYAKDESLSI PDLYKVKYQG IRPAIGYPSL PDQLLNFTLD GLLDMSRIGV SLTENGAMYP TASVSGIYIA HPSSQYFMIG SIDEEQMRDY ASRRNLTEEQ ARKLLSKNIG // ID D7JBS5_9BACE Unreviewed; 915 AA. AC D7JBS5; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 01-APR-2015, entry version 23. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFI10977.1}; GN ORFNames=HMPREF0106_04935 {ECO:0000313|EMBL:EFI10977.1}; OS Bacteroides sp. D22. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=585544 {ECO:0000313|EMBL:EFI10977.1}; RN [1] {ECO:0000313|EMBL:EFI10977.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=D22 {ECO:0000313|EMBL:EFI10977.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG774842; EFI10977.1; -; Genomic_DNA. DR EnsemblBacteria; EFI10977; EFI10977; HMPREF0106_04935. DR PATRIC; 37891213; VBIBacSp99518_4992. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 915 AA; 99870 MW; 4DCAF73453910D52 CRC64; MKKTISQVVS ERILILDGAM GTMIQQYNLK EEDFRGERFA HIPGQLKGNN DLLCLTRPDV IQDIHRKYLE AGADIIETNT FSSTTVSMAD YHVEEYVREM NLAAVKLARD LADEYTAKNP DKPRFVAGSV GPTNKTCSMS PDVNNPAYRA LSYDELAASY QQQMEAMLEG GVDAILIETI FDTLNAKAAV FAAEQAMKAT GVEVPVMLSL TVSDIGGRTL SGQTLDAFLA SVQHANIFSV GLNCSFGARQ LKPFLEQLAA RAPYYISAYP NAGLPNSLGK YDQTPADMAH EVREYIEEGL INIIGGCCGT TDAYIAEYPA LVKGAKPHVP ALAPDCMWLS GLELLEVKPE INFVNVGERC NVAGSRKFLR LVNEKKYDEA LSIARQQVED GALVIDVNMD DGLLDAKEEM TTFLNLIMSE PEIARVPVMI DSSKWEVIEA GLKCLQGKSI VNSISLKEGE EVFLEHARII RQYGAAAVVM AFDEKGQADT AARKIEVCER AYRLLVDKVG FNPHDIIFDP NVLAVATGIE EHNNYAVDFI EATAWIKKNL PGAHISGGVS NLSFSFRGNN YIREAMHAVF LYHAIQQGMD MGIVNPGTSV LYSDIPTDVL EKIEDVVLNR RPDAAERLIE LAESLKATMS GTAGQPAAKQ DAWREESVQE RLKYALMKGI GDFLEQDLAE ALPLYDKAVD VIEGPLMDGM NYVGELFGAG KMFLPQVVKT ARTMKKAVAI LQPIIESEKV EGSAAAGKVL LATVKGDVHD IGKNIVAVVM ACNGYDIVDL GVMVPAETIV QRAIEEKVDM IGLSGLITPS LEEMAHVALE LEKAGLDIPL LIGGATTSKM HTALKIAPVY HAPVVHLKDA SQNASVASKL LNPQLKAELV NELNSEYEAL REKSGLLKRE TVSLEEAQKN KLNLF // ID D7K1Z1_9BACE Unreviewed; 915 AA. AC D7K1Z1; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 01-APR-2015, entry version 24. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFI40740.1}; GN ORFNames=HMPREF9010_01836 {ECO:0000313|EMBL:EFI40740.1}; OS Bacteroides sp. 3_1_23. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=457390 {ECO:0000313|EMBL:EFI40740.1}; RN [1] {ECO:0000313|EMBL:EFI40740.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_23 {ECO:0000313|EMBL:EFI40740.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG774949; EFI40740.1; -; Genomic_DNA. DR EnsemblBacteria; EFI40740; EFI40740; HMPREF9010_01836. DR PATRIC; 37818949; VBIBacSp56772_1022. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 915 AA; 99981 MW; 82D703EE70F4451E CRC64; MKKTISQVVS ERILILDGAM GTMIQQYNLK EEDFRGERFA HIPGQLKGNN DLLCLTRPDV IQDIHRKYLE AGADIIETNT FSSTTVSMAD YHVEEYVREM NLAAVKLARD LADEYTVKNP DKPRFVAGSV GPTNKTCSMS PDVNNPAYRA LSYDELAASY QQQMEAMLEG GVDAILIETI FDTLNAKAAI FAAEQAMKMT GIEVPIMLSV TVSDIGGRTL SGQTLDAFLA SVQHANIFSV GLNCSFGARQ LKPFLEQLAS RAPYYISAYP NAGLPNSLGK YDQTPADMAH EVREYIEEGL INIIGGCCGT TDAYIAEYPA LVEGAKPHVP ASAPDCMWLS GLELLEVKPE INFVNVGERC NVAGSRKFLR LINEKKYDEA LSIARQQVED GALVIDVNMD DGLLEAKTEM TTFLNLIMSE PEIARVPIMI DSSKWEVIEA GLKCLQGKSI VNSISLKEGE EAFLEHARII RQYGAAAVVM AFDEKGQADT AARKIEVCQR AYRLLVDKIG FNPHDIIFDP NVLAVATGIE EHNNYAVDFI EATAWIKKNL PGAHISGGVS NLSFSFRGNN YIREAMHAVF LYHAIQQGMD MGIVNPGTSV LYTDIPADVL EKIEDVVLNR RLDAAERLIE LAESLKANMS ETAGQPAVKQ DAWREGTVQE RLKYALMKGI GDFLEQDLAE ALPLYDKAVD VIEGPLMDGM NHVGELFGAG KMFLPQVVKT ARTMKKAVAI LQPIIESEKV EGSASAGKVL LATVKGDVHD IGKNIVAVVM ACNGYDIVDL GVMVPAETIV QRAIEEKVDM IGLSGLITPS LEEMAHVAVE LEKAGLDIPL LIGGATTSKM HTALKIAPVY HAPVVHLKDA SQNASVASKL LNPQAKAELV NELEAEYQAL REKSGLMKRE TVSLEEAQKN KLNLF // ID D7L2F0_ARALL Unreviewed; 347 AA. AC D7L2F0; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Homocysteine S-methyltransferase 3 {ECO:0000313|EMBL:EFH61781.1}; GN Name=HMT3 {ECO:0000313|EMBL:EFH61781.1}; GN ORFNames=ARALYDRAFT_479786 {ECO:0000313|EMBL:EFH61781.1}; 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 {ECO:0000313|Proteomes:UP000008694}; RN [1] {ECO:0000313|Proteomes:UP000008694} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694}; 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; GL348715; EFH61781.1; -; Genomic_DNA. DR RefSeq; XP_002885522.1; XM_002885476.1. DR EnsemblPlants; fgenesh2_kg.3__2487__AT3G22740.1; fgenesh2_kg.3__2487__AT3G22740.1; fgenesh2_kg.3__2487__AT3G22740.1. DR GeneID; 9321588; -. DR KEGG; aly:ARALYDRAFT_479786; -. DR KO; K00547; -. DR Proteomes; UP000008694; Unassembled WGS sequence. DR GO; GO:0005886; C:plasma membrane; IEA:EnsemblPlants/Gramene. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008694}; KW Methyltransferase {ECO:0000313|EMBL:EFH61781.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008694}; KW Transferase {ECO:0000313|EMBL:EFH61781.1}. SQ SEQUENCE 347 AA; 38154 MW; 18877FC8536519E3 CRC64; MGSFVKEETS SLMTDFLENC GGYAVVDGGF ATELQRHGAD INDPLWSAKC LITSPHLVTK VHLDYLESGA NIIITASYQA TIQGFVAKGL SVEEAENLLR RSVEITYEAR EIFYNRCTKG SWDFAYAGKA SRRPILVAAS VGSYGAYLAD GSEYSGIYGD SVSKETLKDF HRRRVQILAN SGADFIAFET IPNKLEAEAY ADLLEEEDIN IPAWFSFTSK DGVTVPRGDS VVECAKVADS CKKVVAIGIN CTAPRYIHDL IISLRQVTRK PIVVYPNSGE IYDGLNKKWI RSEGESEEDF VSYVSKWRDA GASLFGGCCR TTPNTIRAIA KVLSDESPAT AKPKFRQ // ID D7LQW5_ARALL Unreviewed; 326 AA. AC D7LQW5; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=ATHMT-1/HMT-1 {ECO:0000313|EMBL:EFH51549.1}; GN ORFNames=ARALYDRAFT_484356 {ECO:0000313|EMBL:EFH51549.1}; 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 {ECO:0000313|Proteomes:UP000008694}; RN [1] {ECO:0000313|Proteomes:UP000008694} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL348717; EFH51549.1; -; Genomic_DNA. DR RefSeq; XP_002875290.1; XM_002875244.1. DR EnsemblPlants; fgenesh2_kg.5__348__AT3G25900.1; fgenesh2_kg.5__348__AT3G25900.1; fgenesh2_kg.5__348__AT3G25900.1. DR GeneID; 9313006; -. DR KEGG; aly:ARALYDRAFT_484356; -. DR KO; K00547; -. DR Proteomes; UP000008694; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008694}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000008694}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 241 241 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 326 AA; 35841 MW; FCBC4030A85BFEE5 CRC64; MGLEKKSALL EDLIKKCGGC AVVDGGFATQ LENHGAAIND PLWSAVSLIK NPELIKRVHM EYLEAGADIV VTSSYQATIP GFLSRGLAIE ESESLLQKSV QLAVEARDRF WDKVSKVSGH SYNRALVAAS IGSYGAYLAD GSEYSGYYGE NVSLDKLKDF HRRRLQVLVE AGPDLLAFET IPNKLEAQAC VELLEEEKVQ IPAWICFTSV DGEKAPSGES FEECLEALNK SNNIYAVGIN CAPPQFIENL ICKFAKLTKK AIVVYPNSGE VWDGKAKQWL PSQCFGDDEF EMFATKWRDL GAKLIGGCCR TTPSTIKAIS KDLKRR // ID D7LTP3_ARALL Unreviewed; 333 AA. AC D7LTP3; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Homocysteine S-methyltransferase AtHMT-2 {ECO:0000313|EMBL:EFH54766.1}; GN ORFNames=ARALYDRAFT_486829 {ECO:0000313|EMBL:EFH54766.1}; 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 {ECO:0000313|Proteomes:UP000008694}; RN [1] {ECO:0000313|Proteomes:UP000008694} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694}; 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; GL348717; EFH54766.1; -; Genomic_DNA. DR RefSeq; XP_002878507.1; XM_002878461.1. DR EnsemblPlants; fgenesh2_kg.5__2821__AT3G63250.1; fgenesh2_kg.5__2821__AT3G63250.1; fgenesh2_kg.5__2821__AT3G63250.1. DR GeneID; 9314575; -. DR KEGG; aly:ARALYDRAFT_486829; -. DR KO; K00547; -. DR Proteomes; UP000008694; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008283; P:cell proliferation; IEA:EnsemblPlants/Gramene. DR GO; GO:0006306; P:DNA methylation; IEA:EnsemblPlants/Gramene. DR GO; GO:0006260; P:DNA replication; IEA:EnsemblPlants/Gramene. DR GO; GO:0051567; P:histone H3-K9 methylation; IEA:EnsemblPlants/Gramene. DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:EnsemblPlants/Gramene. DR GO; GO:0043687; P:post-translational protein modification; IEA:EnsemblPlants/Gramene. DR GO; GO:0000394; P:RNA splicing, via endonucleolytic cleavage and ligation; IEA:EnsemblPlants/Gramene. DR GO; GO:0033528; P:S-methylmethionine cycle; IEA:EnsemblPlants/Gramene. DR GO; GO:0010050; P:vegetative phase change; IEA:EnsemblPlants/Gramene. DR GO; GO:0009616; P:virus induced gene silencing; IEA:EnsemblPlants/Gramene. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008694}; KW Methyltransferase {ECO:0000313|EMBL:EFH54766.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008694}; KW Transferase {ECO:0000313|EMBL:EFH54766.1}. SQ SEQUENCE 333 AA; 36505 MW; 01BBC3C73776CBDC CRC64; MTGSSFCSMK DYLKQTGGFA VIDGGLATEF ERHGADLNDP LWSAKCLLTS PHLIHTVHLD YLEAGADIIS SASYQATIQG FEAKGFSREI SESLLRKSVE IACEARNTYY DKCGTSSSMD DKILKKRPIL VAASVGSYGA YLADGSEYSG VYGDLITLEK LKDFHRRRLQ VLAESGADLI AFETIPNKIE AQAFAELLEE GDVKIPGWFS FNSKDGVNVV SGDSIKECIS IAENCEKVVA VGINCTPPRF IEGLVLEIEK VTSKPILVYP NSGESYDADR KEWVENTGVG DEDFVSYVEK WMDAGVSLLG GCCRTTPTTI RAIHKRLVNR RSH // ID D7T951_VITVI Unreviewed; 325 AA. AC D7T951; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 27-MAY-2015, entry version 30. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:CBI27022.3}; GN OrderedLocusNames=VIT_01s0011g03500 {ECO:0000313|EMBL:CBI27022.3}; 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 {ECO:0000313|Proteomes:UP000009183}; RN [1] {ECO:0000313|Proteomes:UP000009183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183}; 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; FN595752; CBI27022.3; -; Genomic_DNA. DR RefSeq; XP_002282549.1; XM_002282513.2. DR EnsemblPlants; VIT_01s0011g03500.t01; VIT_01s0011g03500.t01; VIT_01s0011g03500. DR GeneID; 100247323; -. DR KEGG; vvi:100247323; -. DR HOGENOM; HOG000265278; -. DR InParanoid; D7T951; -. DR KO; K00547; -. DR OMA; AINDPLW; -. DR Proteomes; UP000009183; Chromosome 1. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009183}; KW Reference proteome {ECO:0000313|Proteomes:UP000009183}. SQ SEQUENCE 325 AA; 35824 MW; 40C86AAFBCDB4FBE CRC64; MGKTSSLLED LIEKAGGCAV VDGGFATQLE IHGATINDPL WSALCLIKDP DLIKRVHLEY LEAGADILVT SSYQATIPGF LSKGLSIEEG ELLLERSVRL AVEARDKFWD VTKRVPGHGY NRALVAASIG SYGAYLADGS EYSGCYGPDM NLDKLKDFHR RRLQVLVRSC PDLLAFETIP NKLEAQACVE LLEEENVQIP SWICFSSVDG ENAPSGESFK ECLDIINKSK KVNAVGINCA PPHFLESLIC KFKELTEKPI VVYPNSGEVW DGRAKRWLPS KCFGDDKFEL YATKWRDLGA KLIGGCCRTT PSTIRAISKV LKEMS // ID D7V0J1_LISGR Unreviewed; 617 AA. AC D7V0J1; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 23. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HMPREF0556_12538 {ECO:0000313|EMBL:EFI83853.1}; OS Listeria grayi DSM 20601. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=525367 {ECO:0000313|EMBL:EFI83853.1}; RN [1] {ECO:0000313|EMBL:EFI83853.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 20601 {ECO:0000313|EMBL:EFI83853.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFI83853.1}. 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; ACCR02000005; EFI83853.1; -; Genomic_DNA. DR RefSeq; WP_003756191.1; NZ_GL538352.1. DR ProteinModelPortal; D7V0J1; -. DR EnsemblBacteria; EFI83853; EFI83853; HMPREF0556_12538. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EFI83853.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EFI83853.1}. SQ SEQUENCE 617 AA; 68895 MW; 91F5C34FBE0216F1 CRC64; MNLRRDLNEK VLIADGAMGT LLYSYGIDRS FEELNLSHPD DVSGIHRAYI EAGADIIQTN TYGANYIKLS RYGLEDEVKK INQAAIRLAK EAARGTGTYI LGTMGGINGS SDTKLPLASE EEVKRSFREQ LYCFLLEGVD GLLLETFYDV DELKTVLKIV RETTDLPVIA NVSMHEPGLL QNGQQLPEVL KELEALGADC VGMNCRLGPY HMARALETVP ILQKSHLAVY PNASLPEVRG GKVVYHTETE YFQNYGEIFR QEGARIIGGC CGTTPEHIRA LREGLKSFEP VTSKKVRPII ELVPAEKLED DGEERLLDKV KREHTILVEL DPPRTFDTDK FFEGAEALHE NGVDAITISD NSLASPRISN MALASILKHQ YGIKPLVHLT TRDHNLVGMH SHIMGFHKLG LHDVLAITGD PTKVGDFPGA SSVFDLRSVE LVQLIKKYNA GISYTGKSLK EKGRFHVAAA FNPNVLNVEK AVKLIQRKVE YGADYIITQP VYDKEKIAIL KDALQKADIK VPLFIGVMPL LSGRNAEFLH NEVPGIRLPN EVRERMREAE AADRSKEEGM KIAKEIIDSI YTEFNGIYII TPFLRYDLSV ELATYIQNKK ETHVLEK // ID D7VEJ1_LACPN Unreviewed; 618 AA. AC D7VEJ1; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 24. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN Name=metH {ECO:0000313|EMBL:EFK28400.1}; GN ORFNames=HMPREF0531_12564 {ECO:0000313|EMBL:EFK28400.1}; OS Lactobacillus plantarum subsp. plantarum ATCC 14917 = JCM 1149 = CGMCC OS 1.2437. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=525338 {ECO:0000313|EMBL:EFK28400.1, ECO:0000313|Proteomes:UP000005567}; RN [1] {ECO:0000313|EMBL:EFK28400.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 14917 {ECO:0000313|EMBL:EFK28400.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFK28400.1}. 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; ACGZ02000030; EFK28400.1; -; Genomic_DNA. DR RefSeq; WP_003643140.1; NZ_GL379767.1. DR ProteinModelPortal; D7VEJ1; -. DR EnsemblBacteria; EFK28400; EFK28400; HMPREF0531_12564. DR OrthoDB; EOG6SNDP1; -. DR Proteomes; UP000005567; Unassembled WGS sequence. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005567}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EFK28400.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EFK28400.1}. SQ SEQUENCE 618 AA; 66836 MW; 7EA66927CB801033 CRC64; MKFKQALQQR VLVADGAMGT LLYGNYGINS AFENLNLTHP DTILRVHRSY IRAGADIIQT NTYAANRLKL TRYDLQDQVT TINQAAVKIA ATAREHVDHP VYILGTIGGL AGDTDATVQR ATPATIAANV TEQLTALLAT NQLDGILLET YYDLPELLAA LKIVKAHTDL PVITNVSMLA PGVLRNGTSF TDAIVQLNAA GADVIGTNCR LGPYYLAQSF ENLAIPANVK LAVYPNAGLP GTDQDGAVVY DGEPSYFEEY AERFRQLGLN IIGGCCGTTP LHTSASVRGL SNRSIVAHDQ PATKPQPPTL VTTKSQHRFL QKVATQKTAL VELDPPRDFD TTKFFRGAER LKAAGVDGIT LSDNSLATVR IANTTIAAQL KLNYGITPIV HLTTRDHNLI GLQSEIMGLH SLGIEDILAI TGDPAKLGDF PGATSVSDVR SVELMKLIKQ FNSGIGPTGK SLKEASDFRV AGAFNPNAYR TSISTKSISR KLSYGCDYII TQPVYDLANV DALADALAAN HVNVPVFIGV MPLVSRRNAE FLHHEVHGIR IPEPILTRMA EAEQTGNERA VGIAIAKELI DGICARFNGV HIVTPFNRFK TVIELVDYIQ QKNLIKVQ // ID D7VEP4_LACPN Unreviewed; 309 AA. AC D7VEP4; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFK28453.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EFK28453.1}; GN Name=mmuM {ECO:0000313|EMBL:EFK28453.1}; GN ORFNames=HMPREF0531_12617 {ECO:0000313|EMBL:EFK28453.1}; OS Lactobacillus plantarum subsp. plantarum ATCC 14917 = JCM 1149 = CGMCC OS 1.2437. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=525338 {ECO:0000313|EMBL:EFK28453.1, ECO:0000313|Proteomes:UP000005567}; RN [1] {ECO:0000313|EMBL:EFK28453.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 14917 {ECO:0000313|EMBL:EFK28453.1}; 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. {ECO:0000313|EMBL:EFK28453.1}. 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; ACGZ02000030; EFK28453.1; -; Genomic_DNA. DR RefSeq; WP_003643193.1; NZ_GL379767.1. DR EnsemblBacteria; EFK28453; EFK28453; HMPREF0531_12617. DR OrthoDB; EOG6C019S; -. DR Proteomes; UP000005567; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005567}; KW Methyltransferase {ECO:0000313|EMBL:EFK28453.1}; KW Transferase {ECO:0000313|EMBL:EFK28453.1}. SQ SEQUENCE 309 AA; 32867 MW; 26D06A82022E87E8 CRC64; MLSLTEQLNR GPVVSDGAMA TELEKRGVAT NSALWSATAM LDHPDAIQAV HQSYLDAGAK IMTTNTYQAN VPAFEQAGIA AAQARQLIQQ AVTIAHTARD ASHVTDAVIA GSIGPYGAYL ADGSEYTGAY QLTPSAYQDF HRERLALIMA AGVDVLALET MPRLDEVQAL VQLITTTWTQ QPYWVSFSIK DPQTLCDGTS LAVAAKWVAA QPNVVAVGVN CTTLENIAPA LTTLKAAVAV PLIVYPNSGD QYDPVTKTWQ ETHLSHQFAS FVPQWLAAGA RIIGGCCRTT PKDIATVARA LSVSDSAKL // ID D7VWC0_9FLAO Unreviewed; 336 AA. AC D7VWC0; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFK38045.1}; GN ORFNames=HMPREF0204_10818 {ECO:0000313|EMBL:EFK38045.1}; OS Chryseobacterium gleum ATCC 35910. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Chryseobacterium. OX NCBI_TaxID=525257 {ECO:0000313|EMBL:EFK38045.1}; RN [1] {ECO:0000313|EMBL:EFK38045.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35910 {ECO:0000313|EMBL:EFK38045.1}; 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. {ECO:0000313|EMBL:EFK38045.1}. 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; ACKQ02000002; EFK38045.1; -; Genomic_DNA. DR RefSeq; WP_002983383.1; NZ_GL379783.1. DR EnsemblBacteria; EFK38045; EFK38045; HMPREF0204_10818. DR GeneID; 23025641; -. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFK38045.1}; KW Transferase {ECO:0000313|EMBL:EFK38045.1}. SQ SEQUENCE 336 AA; 37371 MW; D38AD60E0797CAF4 CRC64; MKNSEQLYKA LSERILILDG AMGTMLQRYK FEEEDYRGER FKDWEHPVKG NNDLLSLTQP QAIEEVHKKY LEAGADIIET NTFSGTTIAM ADYHMEDLVY ELNYESAKIA RKACDEYTAK NPDKPRFVAG SIGPTNRTAS LSPDVNDPGY RAITFEELRV AYKQQCEALL DGGSDILLVE TIFDTLNAKA ALFAIDELQD ERGIKIPIMV SGTITDASGR TLSGQTAEAF LISVSHLNLL SVGFNCALGA DQLTPYLETL AHNSEFYVSA YPNAGLPNAF GKYDETPKDM ARQIREYVEK GLINIIGGCC GTTPEHIKAI AELVKDYPPR KLKEFV // ID D7WLV3_9BACI Unreviewed; 1143 AA. AC D7WLV3; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFI70663.1}; GN ORFNames=BFZC1_00635 {ECO:0000313|EMBL:EFI70663.1}; OS Lysinibacillus fusiformis ZC1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; OC Lysinibacillus. OX NCBI_TaxID=714961 {ECO:0000313|EMBL:EFI70663.1, ECO:0000313|Proteomes:UP000004048}; RN [1] {ECO:0000313|EMBL:EFI70663.1, ECO:0000313|Proteomes:UP000004048} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ZC1 {ECO:0000313|EMBL:EFI70663.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFI70663.1}. 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; ADJR01000005; EFI70663.1; -; Genomic_DNA. DR RefSeq; WP_004224449.1; NZ_ADJR01000005.1. DR EnsemblBacteria; EFI70663; EFI70663; BFZC1_00635. DR Proteomes; UP000004048; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000004048}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 725 725 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1143 AA; 126293 MW; 8AD2F7BAF3FCE1A6 CRC64; MAKHSIEEQL EKRILILDGA MGTMLQNENL AAEDFGGEEL DGCNENLVLT RPDVIEKIHH KYLEAGADII CTNTFGGTPL VLNEYDLGTK AEEINKRAVE IARQAVDRYS TSDWPRFVAG AMGPTTKTLS VTGGITFDEL EENFYVQAKA LIEAGADVLL LETSQDMLNV KAGTLGVKRA FASTGKELPV MISGTIEPMG TTLAGQTIDA FYISIEHIKP LSVGLNCATG PEFMTDHIRS LAELSTGYIS CYPNAGLPDE EGCYHESPES LSQKLKGFAE KGWLNIVGGC CGTTPAHIAA IREVLKDEKP RQLPEKTHGH AVSGIEPLLY DDSMRPLFIG ERTNVIGSRK FKNLIIDGKF EEAAEIARAQ VKNGAHVIDI CLANPDRDEL ADMRGFMQEV VKKVKVPLVI DSTDEKVIEE ALKFSQGKAI INSINLEDGE ERFDAVLPLV KKYGASLVVG TIDEKGMAVD RHRKLEIAER SYQLLTEKWG IAPEDIIFDP LMFPVGTGDE QYIGSALETI EGIRLIKEKL PQTLTVLGVS NISFGLPPVG REVLNAVYLY HCTQAGLDYA IVNTEKLERY ASIPEEEIKL ANDLLFNTND ETLAVFTDFY RDKKKEKTEA DIPKTVEGRL AYYILEGTKE GLIEDLDAAR EIFEAPLDII NGPLMEGMAE VGRLFNDNQL IVAEVLQSAG VMKAAVAHLE QFMEKDEESA GKGKMVLATV KGDVHDIGKN LVDIILSNNG YKVVDLGIKV TPAQLIEAIR KEKPDFIGLS GLLVKSAQQM VITAQDFKEA GIDVPILVGG AALSRRFTET KIADEYGGPV IYSKDAMQGL EQANLLMGEG TRENFLAEIE ESRQKRLEAD EKRAARPAKE VTIKPARTVK DAPVFLPADL RRHVKKEYSV SHLYPYVNMR TLLGHHLGLK GQVQQLLDAG DSRATELKDL VDDYLKSDLL KPSGLYQFFP AQADGDDVVV YDPADSKTEI ERFTFPRQQV EPFLCLADFL KTVESGEMDY IALMVVTAGQ GVMAKARQLK EDGKFLESHA LQSTALELAE GFAERMHQEI RDQWGFPDAT DFTMRDRFAA KYQGQRFSFG YPACPNLEDQ EKLFGLLKPE DIGVHLTEGF MMEPEASVSA IVFAHPDARY FNV // ID D7WM37_9BACI Unreviewed; 615 AA. AC D7WM37; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 23. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=BFZC1_00630 {ECO:0000313|EMBL:EFI70662.1}; OS Lysinibacillus fusiformis ZC1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; OC Lysinibacillus. OX NCBI_TaxID=714961 {ECO:0000313|EMBL:EFI70662.1, ECO:0000313|Proteomes:UP000004048}; RN [1] {ECO:0000313|EMBL:EFI70662.1, ECO:0000313|Proteomes:UP000004048} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ZC1 {ECO:0000313|EMBL:EFI70662.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFI70662.1}. 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; ADJR01000005; EFI70662.1; -; Genomic_DNA. DR RefSeq; WP_004224447.1; NZ_ADJR01000005.1. DR ProteinModelPortal; D7WM37; -. DR EnsemblBacteria; EFI70662; EFI70662; BFZC1_00630. DR Proteomes; UP000004048; Unassembled WGS sequence. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004048}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EFI70662.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EFI70662.1}. SQ SEQUENCE 615 AA; 67850 MW; FBC476C2F9713633 CRC64; MGLLERLKTH VLTADGAIGT VLYGYGLEYC HEEMNVQRPE LIEKIHREYI AAGADIIQTN TYGANAIKLA RYGLESRVQQ FNEAAITIAK RAAADGGQFV LGTIGGIRGI RKSDATLDEI LATIEEQARV LLAGNPDGLL LETYYDLEEL TATLKMLREK TKLPIIAQVS MHEPGVLQNG VSLNNALHEL EVLGADIVGV NCRLGPHHTI QAFEGVELPH KAFMSAYPNA SLLDLEDGRV VYESEADYFG RAAVELRDQG VRLIGGCCGT TPKHIAAAKK YLEELSPVQE KHAKPKKIEI VREAEPTKYE PLHEKVKRER SVIVELDTPR HLEIDGFLEG AKQLYDAGAD VVMMADNSLA SPRISNIAMG ALLKSSHGVR PLTHITCRDR NLIGLQSHLM GLNALGIHDV LAVTGDPTKV GDFPGATSVY DVSSMELIQL IKQLNEGVSF SGKPLRKKAN FSVAAAFNPN VRVLERAVKR LENKIEHGAD YFISQPVYTK EKIVEIYEAT KHLQAPIYIG IMPVTSYKSA EFLHHEVPGI KLSEDALTRM KACGEDKERA TLEGISIAKE LVEVATQYFN GIYLITPFLR YDVTLELMKY IEQLDEQKKG VSIHG // ID D7XBA7_ECOLX Unreviewed; 1227 AA. AC D7XBA7; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFJ72450.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFJ72450.1}; GN Name=metH {ECO:0000313|EMBL:EFJ72450.1}; GN ORFNames=HMPREF9552_03950 {ECO:0000313|EMBL:EFJ72450.1}; OS Escherichia coli MS 198-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=749549 {ECO:0000313|EMBL:EFJ72450.1}; RN [1] {ECO:0000313|EMBL:EFJ72450.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 198-1 {ECO:0000313|EMBL:EFJ72450.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFJ72450.1}. 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; ADTJ01000396; EFJ72450.1; -; Genomic_DNA. DR RefSeq; WP_000096036.1; NZ_GG771478.1. DR EnsemblBacteria; EFJ72450; EFJ72450; HMPREF9552_03950. DR PATRIC; 41749265; VBIEscCol153048_3721. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFJ72450.1}; KW Transferase {ECO:0000313|EMBL:EFJ72450.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136053 MW; 84615BFEF095AB25 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARLQAERPI QVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID D7XT73_ECOLX Unreviewed; 1227 AA. AC D7XT73; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFJ85418.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFJ85418.1}; GN Name=metH {ECO:0000313|EMBL:EFJ85418.1}; GN ORFNames=HMPREF9536_04272 {ECO:0000313|EMBL:EFJ85418.1}; OS Escherichia coli MS 84-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=749533 {ECO:0000313|EMBL:EFJ85418.1}; RN [1] {ECO:0000313|EMBL:EFJ85418.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 84-1 {ECO:0000313|EMBL:EFJ85418.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFJ85418.1}. 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; ADTK01000334; EFJ85418.1; -; Genomic_DNA. DR RefSeq; WP_000096053.1; NZ_GG771687.1. DR EnsemblBacteria; EFJ85418; EFJ85418; HMPREF9536_04272. DR PATRIC; 41761038; VBIEscCol149365_4034. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFJ85418.1}; KW Transferase {ECO:0000313|EMBL:EFJ85418.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136040 MW; D1A76336C7330E3D CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID D7XXU6_ECOLX Unreviewed; 1227 AA. AC D7XXU6; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFJ99791.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFJ99791.1}; GN Name=metH {ECO:0000313|EMBL:EFJ99791.1}; GN ORFNames=HMPREF9540_00104 {ECO:0000313|EMBL:EFJ99791.1}; OS Escherichia coli MS 115-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=749537 {ECO:0000313|EMBL:EFJ99791.1}; RN [1] {ECO:0000313|EMBL:EFJ99791.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 115-1 {ECO:0000313|EMBL:EFJ99791.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFJ99791.1}. 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; ADTL01000021; EFJ99791.1; -; Genomic_DNA. DR RefSeq; WP_000096013.1; NZ_GG771728.1. DR EnsemblBacteria; EFJ99791; EFJ99791; HMPREF9540_00104. DR PATRIC; 41764233; VBIEscCol148838_0081. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFJ99791.1}; KW Transferase {ECO:0000313|EMBL:EFJ99791.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135953 MW; AC23B6627EC380AA CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDGFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASISGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAD // ID D7Y0B9_ECOLX Unreviewed; 291 AA. AC D7Y0B9; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 12. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFJ98924.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EFJ98924.1}; DE Flags: Fragment; GN Name=mmuM {ECO:0000313|EMBL:EFJ98924.1}; GN ORFNames=HMPREF9540_00988 {ECO:0000313|EMBL:EFJ98924.1}; OS Escherichia coli MS 115-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=749537 {ECO:0000313|EMBL:EFJ98924.1}; RN [1] {ECO:0000313|EMBL:EFJ98924.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 115-1 {ECO:0000313|EMBL:EFJ98924.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFJ98924.1}. 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; ADTL01000083; EFJ98924.1; -; Genomic_DNA. DR RefSeq; WP_000081353.1; NZ_GG771766.1. DR EnsemblBacteria; EFJ98924; EFJ98924; HMPREF9540_00988. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFJ98924.1}; KW Transferase {ECO:0000313|EMBL:EFJ98924.1}. FT NON_TER 291 291 {ECO:0000313|EMBL:EFJ98924.1}. SQ SEQUENCE 291 AA; 31528 MW; 26B21556EA4E3D3A CRC64; MSQNNPLRAL LDKQDILLLD GAMATELEAR GCNLADSLWS AKVLVENPEL IRKVHLDYYR AGAQCAITAS YQATPAGFAA RGLDEAQSKA LIGKSVELAR KAREAYLAEN PQAGTLLVAG SVGPYGAYLA DGSEYRGDYH CSVEAFQAFH RPRVEALLDA GADLLACETL PNFSEIEALA ELLTAYPRAR AWFSFTLRDS EHLSDGTPLR DVVAFLAGYP QVVALGINCI ALENTTAALQ HLHGLTVLPL VVYPNSGEHY DAVSKTWHHH GEHCAQLADY LPQWQGAGGR V // ID D7YIP5_ECOLX Unreviewed; 1227 AA. AC D7YIP5; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 32. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFK02811.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFK02811.1}; GN Name=metH {ECO:0000313|EMBL:EFK02811.1}; GN ORFNames=HMPREF9548_02428 {ECO:0000313|EMBL:EFK02811.1}; OS Escherichia coli MS 182-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=749545 {ECO:0000313|EMBL:EFK02811.1}; RN [1] {ECO:0000313|EMBL:EFK02811.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 182-1 {ECO:0000313|EMBL:EFK02811.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFK02811.1}. 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; ADTM01000189; EFK02811.1; -; Genomic_DNA. DR RefSeq; WP_000096011.1; NZ_GG771962.1. DR ProteinModelPortal; D7YIP5; -. DR SMR; D7YIP5; 6-639, 651-1227. DR PRIDE; D7YIP5; -. DR EnsemblBacteria; EFK02811; EFK02811; HMPREF9548_02428. DR PATRIC; 41778879; VBIEscCol159572_2310. DR OMA; DYNSIMV; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFK02811.1}; KW Transferase {ECO:0000313|EMBL:EFK02811.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135997 MW; 91F0CAA1E9127D9A CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAD // ID D7ZDT0_ECOLX Unreviewed; 1227 AA. AC D7ZDT0; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFJ81544.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFJ81544.1}; GN Name=metH {ECO:0000313|EMBL:EFJ81544.1}; GN ORFNames=HMPREF9534_02398 {ECO:0000313|EMBL:EFJ81544.1}; OS Escherichia coli MS 69-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=749531 {ECO:0000313|EMBL:EFJ81544.1}; RN [1] {ECO:0000313|EMBL:EFJ81544.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 69-1 {ECO:0000313|EMBL:EFJ81544.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFJ81544.1}. 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; ADTP01000152; EFJ81544.1; -; Genomic_DNA. DR RefSeq; WP_000095986.1; NZ_GG772400.1. DR EnsemblBacteria; EFJ81544; EFJ81544; HMPREF9534_02398. DR PATRIC; 41809611; VBIEscCol149851_2269. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFJ81544.1}; KW Transferase {ECO:0000313|EMBL:EFJ81544.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135994 MW; 59851440E485FE09 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PAVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARLQAERPI QVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID D7ZTG7_ECOLX Unreviewed; 1232 AA. AC D7ZTG7; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 01-APR-2015, entry version 23. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFK25816.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFK25816.1}; GN Name=metH {ECO:0000313|EMBL:EFK25816.1}; GN ORFNames=HMPREF9550_02061 {ECO:0000313|EMBL:EFK25816.1}; OS Escherichia coli MS 187-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=749547 {ECO:0000313|EMBL:EFK25816.1}; RN [1] {ECO:0000313|EMBL:EFK25816.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 187-1 {ECO:0000313|EMBL:EFK25816.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFK25816.1}. 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; ADTQ01000117; EFK25816.1; -; Genomic_DNA. DR EnsemblBacteria; EFK25816; EFK25816; HMPREF9550_02061. DR PATRIC; 41819832; VBIEscCol152054_2007. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFK25816.1}; KW Transferase {ECO:0000313|EMBL:EFK25816.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 252 252 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 315 315 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 316 316 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 764 764 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1232 AA; 136411 MW; 1AD1208718300DF1 CRC64; MLGASVSSKV EQLRAQLNER ILVLDGGMGT MIQSYRLNEA DFRGERFADW PCDLKGNNDL LVLSKPEVIA AIHNAYFEAG ADIIETNTFN STTIAMADYQ MESLSAEINF AAAKLARACA DEWTARTPEK PRYVAGVLGP TNRTASISPD VNDPAFRNIT FDGLVAAYRE STKALVEGGA DLILIETVFD TLNAKAAVFA VKTEFEALGV ELPIMISGTI TDASGRTLSG QTTEAFYNSL RHAEALSFGL NCALGPDELR QYVQELSRIA ECYVTAHPNA GLPNAFGEYD LDADTMAKQI REWAQAGFLN IVGGCCGTTP QHIAAMSRAV EGLAPRKLPE IPVACRLSGL EPLNIGEDSL FVNVGERTNV TGSAKFKRLI KEEKYSEALD VARQQVENGA QIIDINMDEG MLDAEAAMVR FLNLIAGEPD IARVPIMIDS SKWDVIEKGL KCIQGKGIVN SISMKEGVDA FIHHAKLLRR YGAAVVVMAF DEQGQADTRA RKIEICRRAY KILTEEVGFP PEDIIFDPNI FAVATGIEEH NNYAQDFIGA CEDIKRELPH ALISGGVSNV SFSFRGNDPV REAIHAVFLY YAIRNGMDMG IVNAGQLAIY DDLPAELRDA VEDVILNRRD DGTERLLELA EKYRGSKTDD TANAQQAEWR SWEVNKRLEY SLVKGITEFI EQDTEEARQQ ATRPIEVIEG PLMDGMNVVG DLFGEGKMFL PQVVKSARVM KQAVAYLEPF IEASKEQGKT NGKMVIATVK GDVHDIGKNI VGVVLQCNNY EIVDLGVMVP AEKILRTAKE VNADLIGLSG LITPSLDEMV NVAKEMERQG FTIPLLIGGA TTSKAHTAVK IEQNYSGPTV YVQNASRTVG VVAALLSDTQ RDDFVARTRK EYETVRIQHG RKKPRTPPVT LEAARDNDFA FDWQAYTPPV AHRLGVQEVE ASIETLRNYI DWTPFFMTWS LAGKYPRILE DEVVGVEAQR LFKDANDMLD KLSAEKTLNP RGVVGLFPAN RVGDDIEIYR DETRTHVINV SHHLRQQTEK TGFANYCLAD FVAPKLSGKA DYIGAFAVTG GLEEDALADA FEAQHDDYNK IMVKALADRL AEAFAEYLHE RVRKVYWGYA PNENLSNEEL IRENYQGIRP APGYPACPEH TEKATIWELL EVEKHTGMKL TESFAMWPGA SVSGWYFSHP DSKYYAVAQI QRDQVEDYAR RKGMSVTEVE RWLAPNLGYD AD // ID D8AD73_ECOMS Unreviewed; 1227 AA. AC D8AD73; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFK18915.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFK18915.1}; GN Name=metH {ECO:0000313|EMBL:EFK18915.1}; GN ORFNames=HMPREF9530_04517 {ECO:0000313|EMBL:EFK18915.1}; OS Escherichia coli (strain MS 21-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=749527 {ECO:0000313|EMBL:EFK18915.1}; RN [1] {ECO:0000313|EMBL:EFK18915.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 21-1 {ECO:0000313|EMBL:EFK18915.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFK18915.1}. 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; ADTR01000406; EFK18915.1; -; Genomic_DNA. DR RefSeq; WP_000096061.1; NZ_GG772756.1. DR EnsemblBacteria; EFK18915; EFK18915; HMPREF9530_04517. DR PATRIC; 41833564; VBIEscCol155740_4268. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFK18915.1}; KW Transferase {ECO:0000313|EMBL:EFK18915.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136122 MW; 213B891A6EECD254 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPMNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPAEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPT ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANTQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KMLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID D8AHL2_ECOLX Unreviewed; 1227 AA. AC D8AHL2; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 32. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFK17358.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFK17358.1}; GN Name=metH {ECO:0000313|EMBL:EFK17358.1}; GN ORFNames=HMPREF9541_00226 {ECO:0000313|EMBL:EFK17358.1}; OS Escherichia coli MS 116-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=749538 {ECO:0000313|EMBL:EFK17358.1}; RN [1] {ECO:0000313|EMBL:EFK17358.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 116-1 {ECO:0000313|EMBL:EFK17358.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFK17358.1}. 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; ADTZ01000024; EFK17358.1; -; Genomic_DNA. DR RefSeq; WP_000096011.1; NZ_GG773362.1. DR ProteinModelPortal; D8AHL2; -. DR SMR; D8AHL2; 6-639, 651-1227. DR PRIDE; D8AHL2; -. DR EnsemblBacteria; EFK17358; EFK17358; HMPREF9541_00226. DR PATRIC; 41846529; VBIEscCol149313_0206. DR OMA; DYNSIMV; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFK17358.1}; KW Transferase {ECO:0000313|EMBL:EFK17358.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135997 MW; 91F0CAA1E9127D9A CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAD // ID D8B611_ECOLX Unreviewed; 1227 AA. AC D8B611; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 32. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFJ65476.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFJ65476.1}; GN Name=metH {ECO:0000313|EMBL:EFJ65476.1}; GN ORFNames=HMPREF9547_03332 {ECO:0000313|EMBL:EFJ65476.1}; OS Escherichia coli MS 175-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=749544 {ECO:0000313|EMBL:EFJ65476.1}; RN [1] {ECO:0000313|EMBL:EFJ65476.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 175-1 {ECO:0000313|EMBL:EFJ65476.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFJ65476.1}. 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; ADUB01000277; EFJ65476.1; -; Genomic_DNA. DR RefSeq; WP_000096011.1; NZ_GG773700.1. DR ProteinModelPortal; D8B611; -. DR SMR; D8B611; 6-639, 651-1227. DR PRIDE; D8B611; -. DR EnsemblBacteria; EFJ65476; EFJ65476; HMPREF9547_03332. DR PATRIC; 41862913; VBIEscCol149395_3204. DR OMA; DYNSIMV; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFJ65476.1}; KW Transferase {ECO:0000313|EMBL:EFJ65476.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135997 MW; 91F0CAA1E9127D9A CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAD // ID D8BRV4_ECOLX Unreviewed; 1227 AA. AC D8BRV4; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 32. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFI90607.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFI90607.1}; GN Name=metH {ECO:0000313|EMBL:EFI90607.1}; GN ORFNames=HMPREF9551_00347 {ECO:0000313|EMBL:EFI90607.1}; OS Escherichia coli MS 196-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=749548 {ECO:0000313|EMBL:EFI90607.1}; RN [1] {ECO:0000313|EMBL:EFI90607.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 196-1 {ECO:0000313|EMBL:EFI90607.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFI90607.1}. 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; ADUD01000058; EFI90607.1; -; Genomic_DNA. DR RefSeq; WP_000096011.1; NZ_GG773917.1. DR ProteinModelPortal; D8BRV4; -. DR SMR; D8BRV4; 6-639, 651-1227. DR PRIDE; D8BRV4; -. DR EnsemblBacteria; EFI90607; EFI90607; HMPREF9551_00347. DR PATRIC; 41874748; VBIEscCol147078_0320. DR OMA; DYNSIMV; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFI90607.1}; KW Transferase {ECO:0000313|EMBL:EFI90607.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135997 MW; 91F0CAA1E9127D9A CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAD // ID D8DD02_COMTE Unreviewed; 358 AA. AC D8DD02; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFI59228.1}; GN ORFNames=CTS44_23536 {ECO:0000313|EMBL:EFI59228.1}; OS Comamonas testosteroni S44. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Comamonas. OX NCBI_TaxID=563045 {ECO:0000313|EMBL:EFI59228.1}; RN [1] {ECO:0000313|EMBL:EFI59228.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=S44 {ECO:0000313|EMBL:EFI59228.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFI59228.1}. 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; ADVQ01000080; EFI59228.1; -; Genomic_DNA. DR RefSeq; WP_003070538.1; NZ_ADVQ01000080.1. DR EnsemblBacteria; EFI59228; EFI59228; CTS44_23536. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFI59228.1}; KW Transferase {ECO:0000313|EMBL:EFI59228.1}. SQ SEQUENCE 358 AA; 38439 MW; F278499E23B21B7C CRC64; MSQSHPTPAY TRAQELPATL AKRLVILDGA MGTMIQRFKL GEAQYRGEGY AGADGAGERF KDFAHDVKGN NELLSLTRPD VIRDIHEKYL AAGADLIETN TFGATTIAQE DYHMADLAYE MNLKSAQLAR AACDKYSTPD HKRYVAGALG PTPKTASISP DVNDPAARNI TFEQLRQAYL EQTLALIEGG ADVILVETIF DTLNAKAALF AVDEAFEQTG ERLPIMISGT VTDASGRILS GQTVTAFWHS VRHSNPLSVG LNCALGATLM RPYVQELAKA APDTFISCYP NAGLPNPMSD TGFDETPEIT SRLVHEFAAE GLVNIVGGCC GTTPDHIGAI AKAVQATATR KLFYPAEA // ID D8DWP8_PREBR Unreviewed; 622 AA. AC D8DWP8; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFI72116.1}; DE Flags: Fragment; GN ORFNames=PBR_1304 {ECO:0000313|EMBL:EFI72116.1}; OS Prevotella bryantii B14. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=752555 {ECO:0000313|EMBL:EFI72116.1}; RN [1] {ECO:0000313|EMBL:EFI72116.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=B14 {ECO:0000313|EMBL:EFI72116.1}; 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. {ECO:0000313|EMBL:EFI72116.1}. 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; ADWO01000055; EFI72116.1; -; Genomic_DNA. DR RefSeq; WP_006282440.1; NZ_ADWO01000055.1. DR EnsemblBacteria; EFI72116; EFI72116; PBR_1304. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; FT NON_TER 622 622 {ECO:0000313|EMBL:EFI72116.1}. SQ SEQUENCE 622 AA; 68642 MW; 5184903CE5EBC580 CRC64; MKRLEDVVKE RVLVLDGAMG TMIQNYHLTE EDFRGHLFQD IKGQMKGNND MLNLTCPDVI ADIHNRYLEA GADLISTNTF SSQCISQADY SLEKYGREMA LRGAQIARKC ADAFSTEDKP RFVCGDIGPT NKTCSMSPDV SDPSAREITY DQLFGAYSEQ IEGLIDGGVD ALLVETIFDS LNAKVAIDAC VQTMQRYNVS LPIMVSATVS DLAGRTLSGQ TLDAFLASID NYPIFSVGLN CGFGADQMKP FIQELAAKAP YYISCHPNAG LPNAMGLYDE SAESMAPKMG EMVSEGLVNI IGGCCGTTEK FIEAYQPFVQ DKKPHMPVAA PRTMWLSGLE LLNVTPEVQF VNVGERCNVA GSRKFLRLIK EKNYEEATSI ARKQVEDGAL VIDVNMDDAL LDAKEEMVKF LNLIASEPEI AKVPVMIDSS KWDVILAGLK CVQGKSIVNS ISLKNGEEEF LSHARDIKRY GAAVVVMCFD EKGQATSYER RIEIAERAYK LLTEKVGMNP LDIIFDPNVL SIATGMEEHD NYALDFINAT GWIKKNLPGA HISGGVSNLS FSFRGINYIR EAMHAVFLYH AIRQGMDFGI VNPSTRITYE DIPQEHLKVI EDVVLNRRKG AA // ID D8EA71_ECOLX Unreviewed; 1227 AA. AC D8EA71; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 32. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFK44949.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFK44949.1}; GN Name=metH {ECO:0000313|EMBL:EFK44949.1}; GN ORFNames=HMPREF9346_03415 {ECO:0000313|EMBL:EFK44949.1}; OS Escherichia coli MS 119-7. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=679206 {ECO:0000313|EMBL:EFK44949.1}; RN [1] {ECO:0000313|EMBL:EFK44949.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 119-7 {ECO:0000313|EMBL:EFK44949.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFK44949.1}. 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; ADWU01000025; EFK44949.1; -; Genomic_DNA. DR RefSeq; WP_000096011.1; NZ_ADWU01000025.1. DR ProteinModelPortal; D8EA71; -. DR SMR; D8EA71; 6-639, 651-1227. DR PRIDE; D8EA71; -. DR EnsemblBacteria; EFK44949; EFK44949; HMPREF9346_03415. DR PATRIC; 41105666; VBIEscCol144184_3323. DR OMA; DYNSIMV; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFK44949.1}; KW Transferase {ECO:0000313|EMBL:EFK44949.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135997 MW; 91F0CAA1E9127D9A CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAD // ID D8EVA5_ECOLX Unreviewed; 1227 AA. AC D8EVA5; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFK48450.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFK48450.1}; GN Name=metH {ECO:0000313|EMBL:EFK48450.1}; GN ORFNames=HMPREF9345_05157 {ECO:0000313|EMBL:EFK48450.1}; OS Escherichia coli MS 107-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=679207 {ECO:0000313|EMBL:EFK48450.1}; RN [1] {ECO:0000313|EMBL:EFK48450.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 107-1 {ECO:0000313|EMBL:EFK48450.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFK48450.1}. 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; ADWV01000049; EFK48450.1; -; Genomic_DNA. DR RefSeq; WP_000096053.1; NZ_ADWV01000049.1. DR EnsemblBacteria; EFK48450; EFK48450; HMPREF9345_05157. DR PATRIC; 41119800; VBIEscCol145094_4961. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFK48450.1}; KW Transferase {ECO:0000313|EMBL:EFK48450.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136040 MW; D1A76336C7330E3D CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID D8FQE4_LACDE Unreviewed; 310 AA. AC D8FQE4; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFK31411.1}; GN ORFNames=HMPREF9264_1050 {ECO:0000313|EMBL:EFK31411.1}; OS Lactobacillus delbrueckii subsp. bulgaricus PB2003/044-T3-4. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=784613 {ECO:0000313|EMBL:EFK31411.1, ECO:0000313|Proteomes:UP000005537}; RN [1] {ECO:0000313|EMBL:EFK31411.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PB2003/044-T3-4 {ECO:0000313|EMBL:EFK31411.1}; RA Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., Nelson K.E.; RT "Genome Sequence of Lactobacillus delbrueckii subsp. bulgaricus RT PB2003/044-T3-4."; 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. {ECO:0000313|EMBL:EFK31411.1}. 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; AEAT01000105; EFK31411.1; -; Genomic_DNA. DR RefSeq; WP_003614024.1; NZ_AEAT01000105.1. DR EnsemblBacteria; EFK31411; EFK31411; HMPREF9264_1050. DR PATRIC; 41146219; VBILacDel160329_1447. DR OrthoDB; EOG6C019S; -. DR Proteomes; UP000005537; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005537}; KW Methyltransferase {ECO:0000313|EMBL:EFK31411.1}; KW Transferase {ECO:0000313|EMBL:EFK31411.1}. SQ SEQUENCE 310 AA; 33140 MW; 3983366F412F21F4 CRC64; MADLPTLLAQ GPVTLDGSMS TPLEAWGEDT NSDLWTAKAL ADNPDLVYRV HQEYFKAGAR VTITDSYQAS LPAFMKHGLS EDAARALIRE SAAVAIKARD DFEKATGIHN FVAGSVGPYG AYLADGSEYR GDYALSHEEY VDFHAPRIKE LVAGGVDCLA VETQPKLSEV RAILDYLKAK YPDLPVYVSF SLKDPASISE GLPLTEAVEE VSAYAQVFAA GANCFKLAWT VDVVKNLRAS KLPIVVYPNS GAEYDPSVKK WVYPPEAADF GQAGAAWLAA GAKLVGGCCT TMPEDIAGLA AAVKKGYTAF // ID D8FYY1_9CYAN Unreviewed; 1244 AA. AC D8FYY1; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:CBN55571.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CBN55571.1}; GN ORFNames=OSCI_2110007 {ECO:0000313|EMBL:CBN55571.1}; OS [Oscillatoria] sp. PCC 6506. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Kamptonema. OX NCBI_TaxID=272129 {ECO:0000313|EMBL:CBN55571.1}; RN [1] {ECO:0000313|EMBL:CBN55571.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PCC 6506 {ECO:0000313|EMBL:CBN55571.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CACA01000183; CBN55571.1; -; Genomic_DNA. DR RefSeq; WP_007354794.1; NZ_CACA01000183.1. DR EnsemblBacteria; CBN55571; CBN55571; OSCI_2110007. DR PATRIC; 41248651; VBIOscSp14852_2232. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 2. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 2. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CBN55571.1}; KW Transferase {ECO:0000313|EMBL:CBN55571.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 229 229 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 296 296 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 738 738 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1244 AA; 137371 MW; B5A61606080609F0 CRC64; MTNSTFLQRL HHPSRPVIVF DGAMGTNLQF QNLTAEDFGG PQYEGCNEYL IYTNPEAVAK VHRGFLEAGA DVIETDTFGA SSFVLAEYNL AQEAYNLNKA AATLAKGLAI EYSTPEKPRF VAGSIGPGTK LPTLGHIDFD TLKIAFAEQA EGLFDGGVDL LIVETCQDVL QIKAALSAIE EVFAKKGTRL PIMVSVTMET TGTMLVGSDI SAVLTILQPF PIDILGLNCA TGPDRMAEHI KYLSQYSPFV VSCIPNAGLP ENVGGHAHYK LTPMELRMAL MHFVEDLGVQ VIGGCCGTRY DHIQQLAEIS TTLTPKVRET TWQPAAASIY SAQPYDQDNS FLIVGERLNA SGSKKCRDLL NAEDWDGLIS MGREQVREGA HILDVNVDYV GRDGVRDMRE VVSRLVTNAT LPLMLDSTEW EKMEAGLKAA GGKCLLNSTN YEDGEPRFYK VLELAKTYGA GIVIGTIDED GMARSANKKF EIASRAYHAA IEYGIPAYDI FFDPLALPIS TGIEEDRANG KSTIEAIRRI RQELPGCHVI LGVSNISFGL NPAARQVLNS MFLHEAMQAG MDSAIVSPNK ILPLAKIEEK YQELCRKLIY DRREFDGNVC IYDPLGELTN AFEGATTKRD RSADKLLPLE ERLKRHIIDG ERIGLEEVLT TALEQYPPLE IINTFLLDGM KVVGELFGSG QMQLPFVLQS AETMKAAVAF LQPYMEKSES GDNAKGTFII ATVKGDVHDI GKNLVDIILS NNGYRVINLG IKQPVDNIIE AYEQHKADCI AMSGLLVKST AFMKENLETF NQRGITVPVI LGGAALTPKF VHEDCQNTYK GKVIYGKDAF SDLHFMDKLM PAKSGGKWDD LNGFADEENG NGNGVAKIEV AHKKEVETAE SATPLVIDTR RSEAVAVDIE RPIPPFWGTQ LLEGEDIPFE EIFWHLDLQA LIAGQWQYRK PKDQSREEYD GFLAEKVYPI LEGWKQRIVN EKLLHPQVVY GYFPCQSEGN SLHLYDPANP PNPPLVRGGN DVNNPLLTEG ADLTNSPLLT GGNDVNNPLL MGGDDLTNSP LSTGGNVTNP PLPRRGEEGV ITTFTFPRQK SGRRLCIADF FAPKESGKID VFPMQAVTVG HIATEFAQKL FADNQYTDYL YFHGLAVQTA EAIAEWTHAR IRRELGFGSE EPENIRDMLA QRYRGSRYSF GYPACPDMSD QYKQLELLGS DRINLYMDES EQLYPEQSTT AIITYHPAAK YFTA // ID D8GNB1_CLOLD Unreviewed; 799 AA. AC D8GNB1; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 29-APR-2015, entry version 28. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADK13735.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADK13735.1}; GN Name=metH1 {ECO:0000313|EMBL:ADK13735.1}; GN OrderedLocusNames=CLJU_c06650 {ECO:0000313|EMBL:ADK13735.1}; OS Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=748727 {ECO:0000313|EMBL:ADK13735.1, ECO:0000313|Proteomes:UP000001656}; RN [1] {ECO:0000313|EMBL:ADK13735.1, ECO:0000313|Proteomes:UP000001656} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 55383 / DSM 13528 / PETC RC {ECO:0000313|Proteomes:UP000001656}; 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 ----------------------------------------------------------------------- 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; ADK13735.1; -; Genomic_DNA. DR RefSeq; WP_013237335.1; NC_014328.1. DR RefSeq; YP_003778837.1; NC_014328.1. DR EnsemblBacteria; ADK13735; ADK13735; CLJU_c06650. DR KEGG; clj:CLJU_c06650; -. DR PATRIC; 42482524; VBICloLju82977_0631. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR BioCyc; CLJU748727:GHMO-665-MONOMER; -. DR Proteomes; UP000001656; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001656}; KW Methyltransferase {ECO:0000313|EMBL:ADK13735.1}; KW Transferase {ECO:0000313|EMBL:ADK13735.1}. SQ SEQUENCE 799 AA; 87726 MW; B6725FC51CBB350D CRC64; MLFKDLLNKF SNKFVFFDGA MGTMLQRAGL KVGELPETLN ITNSEIIRKV HREYLNAGSD IIITNTFGAN ELKYSSSDYT IKDVITAGVK IAKEEAKDKL VALDIGPTGQ VMEPTGSLSF ESAYELFKSQ VIIGEKAGAD IILIETMSDL YEAKAAILAA KENSSLPIFC TMTFQQDGRT LMGTDPKTMV FVLESLGVDA LGVNCSLGPG ELQDIVDEIL KYSSIPVIVQ PNAGLPKYDG ENTIYDITSD EFAENVVIMA KKGVRFFGGC CGTSPEFIKT MVKSLKNIVP LDIKEKNYTT VCSARDTVFL GNRIKFIGER INPTGRDIYK KELKEGKVNF IQKEAVKQKE EGAHILGLNV GLPEINEVQT MKEAVKAIQK VVQLPIDIDS PNPKVLEAGV RVYNGKPIIN SVNGRKKCME EVFPIVKKYG GCVIALTIDE NGIPDTAEGR VKIAEKIIKT AENYGIKRKD IIVDCLTLTA SAQQKEVLET IKAIKILKEQ FGVKTTLGVS NISYGLPRRC ILNRTFLALA LQAGLDLPII NTADKGVKDI ISAFEVLTNI DKEGKEYVKK YSGKSEGEKA KWGSDIPNSG ENDKNLKQTI IDGMEEEAVE LTCKLLKSKK AVDIVNSYII PALDEVGVQY ENKDIFLPQL IQSAETVKQA FEIIKKDMLK SGENKISRGK IILATVKGDI HDIGKNIVKV LLENYGFEVI DLGRDVDISE VVDAIIKNNV KLVGLSALMT TTVSNMKKTI DAIRDKGLQC KVVVGGAVLN QNYADMIGAD YYAKDARETV KIAEELFSV // ID D8GVK5_BACAI Unreviewed; 856 AA. AC D8GVK5; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 01-APR-2015, entry version 28. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase N-terminal part {ECO:0000313|EMBL:ADK06818.1}; GN OrderedLocusNames=BACI_c42190 {ECO:0000313|EMBL:ADK06818.1}; OS Bacillus cereus var. anthracis (strain CI). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=637380 {ECO:0000313|EMBL:ADK06818.1, ECO:0000313|Proteomes:UP000001657}; RN [1] {ECO:0000313|EMBL:ADK06818.1, ECO:0000313|Proteomes:UP000001657} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CI {ECO:0000313|EMBL:ADK06818.1, RC ECO:0000313|Proteomes:UP000001657}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001746; ADK06818.1; -; Genomic_DNA. DR RefSeq; WP_013246546.1; NC_014335.1. DR RefSeq; YP_003793956.1; NC_014335.1. DR EnsemblBacteria; ADK06818; ADK06818; BACI_c42190. DR KEGG; bal:BACI_c42190; -. DR PATRIC; 42183271; VBIBacCer111781_4603. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; ILESWIT; -. DR BioCyc; BCER637380:GHO7-4137-MONOMER; -. DR Proteomes; UP000001657; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001657}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADK06818.1}; KW Transferase {ECO:0000313|EMBL:ADK06818.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 856 AA; 94410 MW; 09EA75B784F6F99B CRC64; MKCIEGKLQN SILLLDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYELSHLDE ELNEKAARLA KQAVKESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGE VDVLLVETSQ DMRNVKAAYI GIQAAFDELK KIVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWVN IIGGCCGTTP EHIKAMKEAL ASLKPREHHE REGHGVSGLE ALQYDDSMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMENF LAEVTKVLKV PIMIDSTDEH VMERALTYIQ GKAVINSINL EDGEERFIKV TPLLQKYGAA IVVGTIDEDG MAVSAERKLE IAKRSYELLT TKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPDE EKRLADALLF ETTQETLEEF TNFYRVAKKK DVVVQETLTL DERLANYIVE GTKQGLHEDL SLALTEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILA NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAADIDIPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV TKEEKK // ID D8GVK6_BACAI Unreviewed; 610 AA. AC D8GVK6; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 29-APR-2015, entry version 33. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN Name=metE2 {ECO:0000313|EMBL:ADK06819.1}; GN OrderedLocusNames=BACI_c42200 {ECO:0000313|EMBL:ADK06819.1}; OS Bacillus cereus var. anthracis (strain CI). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=637380 {ECO:0000313|EMBL:ADK06819.1, ECO:0000313|Proteomes:UP000001657}; RN [1] {ECO:0000313|EMBL:ADK06819.1, ECO:0000313|Proteomes:UP000001657} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CI {ECO:0000313|EMBL:ADK06819.1, RC ECO:0000313|Proteomes:UP000001657}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ADK06819.1; -; Genomic_DNA. DR RefSeq; WP_000770326.1; NC_014335.1. DR RefSeq; YP_003793957.1; NC_014335.1. DR EnsemblBacteria; ADK06819; ADK06819; BACI_c42200. DR KEGG; bal:BACI_c42200; -. DR PATRIC; 42183273; VBIBacCer111781_4604. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR BioCyc; BCER637380:GHO7-4138-MONOMER; -. DR Proteomes; UP000001657; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001657}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ADK06819.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:ADK06819.1}. SQ SEQUENCE 610 AA; 67285 MW; C293FA7BD766EE93 CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNISDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTE INRAAVKLAK ASVTDRNAIL GTIGGMKHIG AVTTTDMERE FMLLEQASAL LEEQVDGLLL ETFYDEFELL HAVQVLRKET NIPIVAQLAL HDAGTTQNGN DVNEILEQLL DYGANVVGLN CQLGPLHMTE AFKMISIPKN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPKFIEQGI RLLGGCCGTT PEHIESMKRA TLNVTPVIEK DTIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRISNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIA LIEEVYEATK HLEQPIFIGI MPLISKRNAD FLHFEVPGIT LPEAVRERMD GHETKEAAIE EGIRISQELI DETMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID D8IB62_BRAP9 Unreviewed; 872 AA. AC D8IB62; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 01-APR-2015, entry version 29. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|EMBL:ADK30385.1}; GN Name=metH {ECO:0000313|EMBL:ADK30385.1}; GN OrderedLocusNames=BP951000_0380 {ECO:0000313|EMBL:ADK30385.1}; OS Brachyspira pilosicoli (strain ATCC BAA-1826 / 95/1000). OC Bacteria; Spirochaetes; Spirochaetales; Brachyspiraceae; Brachyspira. OX NCBI_TaxID=759914 {ECO:0000313|EMBL:ADK30385.1, ECO:0000313|Proteomes:UP000000332}; RN [1] {ECO:0000313|EMBL:ADK30385.1, ECO:0000313|Proteomes:UP000000332} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1826 / 95/1000 {ECO:0000313|Proteomes:UP000000332}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002025; ADK30385.1; -; Genomic_DNA. DR RefSeq; WP_013243340.1; NC_014330.1. DR RefSeq; YP_003784886.1; NC_014330.1. DR EnsemblBacteria; ADK30385; ADK30385; BP951000_0380. DR KEGG; bpo:BP951000_0380; -. DR PATRIC; 42195199; VBIBraPil164347_0374. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; TWTFPRQ; -. DR BioCyc; BPIL759914:GHZ5-379-MONOMER; -. DR Proteomes; UP000000332; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000332}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADK30385.1}; KW Transferase {ECO:0000313|EMBL:ADK30385.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 238 238 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 751 751 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 872 AA; 96316 MW; 291F154D2C237C6B CRC64; MFNSVKDRLK ELIREQYLII DGATGTELQK KEIKKEYWTF NGNNIEGCNE ILNITAPHIM KEIHIDYLNA NANITKTNSF GAIPWVLSEY DIADKAYELA KQAAVIANEA RDEYLKNPNS KGDLDRDIFI AGSLGPGVKL PSLGQIGFDE MYSGYTLAAR GLIEGGVDII LLETAQDVLQ LKAAILAVND TAKKLNKDIP IMVSVTIEKE GTMLLGTDIE TAYTILSNLD IFSIGMNCGT GPDMAMQHIK KLSEISCLPI SIHSNAGLPE NRDGKAYYSM TPEEFAEINS EFFNLSGLAF IGGCCGTTPK HIEALAKKVK GVKPKKPALE KQRAYIASLF NSVSIKQEPA PLMIGERSNA TGSKIFRELM IAGDMDGMLD VGIKQVKSGS HAIDVNAAWA GRNEIEDITK IISAYVKQIS LPLVIDAIKP DVIEAALKVY GGKPIINSAN MEQGEEKFDA ICSLAKRYGA SIMLLTIDEK AMALTCEDKL RMCERMYDRA FNVHKILPHD IIFDPLTFTL ASGDENSFLA GVETLNAIKE LSKRYPESSI SLGVSNISFG LKEEARKVMN SVFLYEAINH GLSAAIVNVA QIFPISKIGE KEIELARELI YNKNKTKEPL INYINYFSDK KEKKELTGEE KIKKPIREAI RDAMLDGEWK DMQNLLNEVK ENSEEFGGEK KFAQAIIDEI LLPTMADIGV KFGEGSIQLP FVLGSAEVMK KSVDFLSEFL EKKKQEKTAK IILGTVAGDV HDVGKNLVEI IIKNNGFETV NLGTKVPIEK FIEAYHEHNA DCIGMSGLLV KSTEVMKDNL AYIRDKGLKI PILLGGAALT KDFVENTCKK VYGDSGKIFY CKDGFDDIVA IKEIIADRDK EK // ID D8IHM9_LACFC Unreviewed; 310 AA. AC D8IHM9; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 29-APR-2015, entry version 22. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADJ41158.1}; GN OrderedLocusNames=LC40_0544 {ECO:0000313|EMBL:ADJ41158.1}; OS Lactobacillus fermentum (strain CECT 5716). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=712938 {ECO:0000313|EMBL:ADJ41158.1, ECO:0000313|Proteomes:UP000006910}; RN [1] {ECO:0000313|EMBL:ADJ41158.1, ECO:0000313|Proteomes:UP000006910} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CECT 5716 {ECO:0000313|EMBL:ADJ41158.1, RC ECO:0000313|Proteomes:UP000006910}; RX PubMed=20639335; DOI=10.1128/JB.00702-10; RA Jimenez E., Langa S., Martin V., Arroyo R., Martin R., Fernandez L., RA Rodriguez J.M.; RT "Complete genome sequence of Lactobacillus fermentum CECT 5716, a RT probiotic strain isolated from human milk."; RL J. Bacteriol. 192:4800-4800(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; CP002033; ADJ41158.1; -; Genomic_DNA. DR RefSeq; WP_003681749.1; NC_017465.1. DR RefSeq; YP_005848654.1; NC_017465.1. DR EnsemblBacteria; ADJ41158; ADJ41158; LC40_0544. DR GeneID; 6232276; -. DR KEGG; lfr:LC40_0544; -. DR PATRIC; 43086021; VBILacFer149467_0970. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR BioCyc; LFER712938:GLF8-535-MONOMER; -. DR Proteomes; UP000006910; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006910}; KW Methyltransferase {ECO:0000313|EMBL:ADJ41158.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006910}; KW Transferase {ECO:0000313|EMBL:ADJ41158.1}. SQ SEQUENCE 310 AA; 33675 MW; 7DA01ED5B30D73D5 CRC64; MKLLERLAQG PLVLDGSMST PLEVAGAKTN SDLWTSQTLI DNPDLVYQVH LDYFKAGADL TITDTYQTNV DALVRHGLSE EEARNLIKRA VQLANQARDD YEKETGKHNY VAGSIGPYGA YLADGSEYRG DYDLTAIQLQ NFHLPRLAAI LATGVDCLAL ETQPKLTEVV AILALLKTLE PTMPVYVSFS LRDAEHLSDG TSLKEAVQVV TKDPQVFAVG VNCVGLDLVT PAIKAIKEVT DKPVIVYPNS GATYDPTVKQ WRFEEGTPRF VNAIDDWITA GAAIIGGCCT TLPQDIAVVA EKLRGVGNNR // ID D8IVK9_HERSS Unreviewed; 1247 AA. AC D8IVK9; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 32. DE SubName: Full=Methionine synthase I, cobalamin-binding domain protein {ECO:0000313|EMBL:ADJ65817.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADJ65817.1}; GN Name=metH {ECO:0000313|EMBL:ADJ65817.1}; GN OrderedLocusNames=Hsero_4349 {ECO:0000313|EMBL:ADJ65817.1}; OS Herbaspirillum seropedicae (strain SmR1). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae; Herbaspirillum. OX NCBI_TaxID=757424 {ECO:0000313|EMBL:ADJ65817.1, ECO:0000313|Proteomes:UP000000329}; RN [1] {ECO:0000313|EMBL:ADJ65817.1, ECO:0000313|Proteomes:UP000000329} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SmR1 {ECO:0000313|EMBL:ADJ65817.1, RC ECO:0000313|Proteomes:UP000000329}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002039; ADJ65817.1; -; Genomic_DNA. DR RefSeq; WP_013236272.1; NC_014323.1. DR RefSeq; YP_003777725.1; NC_014323.1. DR EnsemblBacteria; ADJ65817; ADJ65817; Hsero_4349. DR KEGG; hse:Hsero_4349; -. DR PATRIC; 42367531; VBIHerSer153339_4387. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR BioCyc; HSER757424:GCTT-4349-MONOMER; -. DR Proteomes; UP000000329; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000329}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADJ65817.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000329}; KW Transferase {ECO:0000313|EMBL:ADJ65817.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 255 255 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 320 320 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 778 778 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1247 AA; 137677 MW; 5A16BB60E9B95C0F CRC64; MKPNELCQTE LLLRDLMSQR ILILDGAMGT MIQRYKLTEE DYRGQRFADF SVPGKDLFVK GNNELLSLTQ PHIIQEIHEQ YLAAGADLIE TNTFGATSVA QDDYHMAHLV YEMNVESARL ARAACDKYAT PDKPRFVAGA LGPTPKTASI SPDVNDPAAR NVTFDQLVAA YLEQTRALVE GGADVLLVET IFDTLNCKAA LFAIDTFFEE SGQRLPIMIS GTVTDASGRI LSGQTVTAFW NSIRHARPLT VGLNCALGAA LMRPYAEELS KIADTFVCIY PNAGLPNPMS DTGFDETPDV TSALLKEFAE SGFVNVAGGC CGTTPPHIKA IAETVAKIAP RKVPEPTHEM RLSGLEPFTI NDDSLYVNVG ERTNVTGSKA FARLILNEQY DEALAVARQQ VENGAQIIDI NMDEAMLDSV AAMTRFLNLI ASEPDIARVP IMIDSSKWEV IEAGLKCVQG KSIVNSISMK EGEEKFLREA KLCRRYGAAV IVMAFDEVGQ ADTFARKIEI CERAYRLLVD KLDFPPEDII FDPNIFAVAT GIEEHNNYAV DFIEATRWIH QNLPYAKISG GVSNVSFSFR GNDPAREAIH TVFLYHAIKA GMTMGIVNAG MIGVYDDLPA ELRERVEDVV LNRREDATER MIEYAATLKA GDKKEEATLE WRNLPVAKRL SHALVHGITQ WIVEDTEEVR QQIAADGGRP IHVIEGPLMD GMNVVGDLFG QGKMFLPQVV KSARVMKQAV AHLIPFIEEE KRQLEIATGE VAKPKGKIVI ATVKGDVHDI GKNIVTVVLQ CNNFEVVNMG VMVPCAEILA KAKEEKADII GLSGLITPSL EEMAYVAKEM QRDPYFAGLK MPLMIGGATT SRAHTAVKIA PNYEGPVVYV PDASRAVSVA QSLLADEQKT QYVAELNADY ERIREQHASK KAAPMLSLAA ARANKTKLDF APVKPKFIGR RLFKNVDLGL LANYIDWGPF FQTWDLAGPY PAILTDEVVG EAATKVFQEA QAMLKKIIDG RWLTANGVIS LLPANTVNDD DIEIYTDDSR SQVAFTYYGL RQQTEKPVVD GVARPNQCLS DFIAPKESGV QDYIGMFAVT AGLGIEKYEK RFEDAHDDYS SIMLKALADR LAEAFAEYLH ERVRKDLWGY AADENLSSTD LIKEKYLGIR PAPGYPACPE HTVKADVFRT MQCDEIGMQL TESYAMFPGA SVSGFYFAHP QSKYFVVGKI GEDQVVDMAE RRHVPKEELE RWLAPNL // ID D8JDW7_ACISD Unreviewed; 1228 AA. AC D8JDW7; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 32. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:ADI91783.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADI91783.1}; GN Name=metH {ECO:0000313|EMBL:ADI91783.1}; GN OrderedLocusNames=AOLE_14480 {ECO:0000313|EMBL:ADI91783.1}; OS Acinetobacter oleivorans (strain JCM 16667 / KCTC 23045 / DR1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=436717 {ECO:0000313|EMBL:ADI91783.1, ECO:0000313|Proteomes:UP000000392}; RN [1] {ECO:0000313|EMBL:ADI91783.1, ECO:0000313|Proteomes:UP000000392} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 1667 / KCTC 23045 / DR1 RC {ECO:0000313|Proteomes:UP000000392}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002080; ADI91783.1; -; Genomic_DNA. DR RefSeq; WP_013198632.1; NC_014259.1. DR RefSeq; YP_003733156.1; NC_014259.1. DR EnsemblBacteria; ADI91783; ADI91783; AOLE_14480. DR GeneID; 9383321; -. DR KEGG; acd:AOLE_14480; -. DR PATRIC; 42144802; VBIAciSp20010_2868. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR BioCyc; AOLE436717:GHCD-2934-MONOMER; -. DR Proteomes; UP000000392; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000392}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADI91783.1}; KW Transferase {ECO:0000313|EMBL:ADI91783.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1228 AA; 135738 MW; 484AD610F395ED3F CRC64; MSTLATLKAL LAKRILIIDG AMGTMIQRHK LEEADYRGER FADWAQDLKG NNDLLVLTQP EIIQGIHEAY LDAGADIIET NSFNGTRVSM SDYHMEDLVP EINREAARLA KAACEKYSTP DKPRFVAGVL GPTSRTCSIS PNVNDPAFRN ITFDELKENY IEATHALIEG GADIILIETV FDTLNCKAAI FAVKEVFKQI GHELPLMISG TITDASGRTL TGQTAEAFWN SVRHGDLLSI GFNCALGADA MRPHVKTVSD VADTFISAHP NAGLPNAFGE YDETPEQTAA FLKEFAESGL INITGGCCGT TPDHIRAIAN AVKDIAPRQI PETKPACRLS GLEPFNIYDD SLFVNVGERT NVTGSKKFLR LIREENFAEA LEVAQQQVEA GAQIIDINMD EGMLDSQNAM VHFLNLVASE PDISRVPIMI DSSKWEIIEA GLKCVQGKPV VNSISLKEGY DEFVEKARLC RQYGAAIIVM AFDETGQADT AERKREICKR SYDVLVNDVG FPAEDIIFDP NVFAVATGIE EHNNYGVDFI EATGWIKQNL PHAMISGGVS NVSFSFRGNE PVREAIHSVF LYHAIKQGMT MGIVNAGQMA IYDDIPKELK DAVEDVVLNQ NQGESGQLAT EKLLEVAEKF RGHSGAQREA ENLEWRNEPV EKRLEYALVK GITTYIDEDT EEARLKAKRP LDVIEGALMD GMNVVGDLFG SGKMFLPQVV KSARVMKQAV AWLNPYIEAE KTGSQSKGKV LMATVKGDVH DIGKNIVGVV LGCNGYDIVD LGVMVPCEKI LQTAIDEKCD IIGLSGLITP SLDEMVFVAK EMQRKGFNIP LLIGGATTSK AHTAVKIDPQ YQNDAVIYVA DASRAVGVAT TLLSKEMRGN FIAEHRAEYA KIRERLANKQ PKAAKLTYKE SVENGFKIDE SYVPPKPNLL GTQVLTNYPL ATLVDYFDWT PFFISWSLAG KFPKILEDEV VGEAATDLYN QAQAMLKDII DNNLFDARAV FGMFPAQRTD ADTVSVFDEA GQKVTHTFEH LRQQSDKVTG KPNLSLADYI RADREQQDYL GGFTVSIFGA EELANEYKAK GDDYSAILVQ SLADRFAEAF AEHLHERIRK EFWGYKADEQ LSNEELIKEK YVGIRPAPGY PACPEHSEKA VLFDWLGSTD KIGTKLTEHF AMMPPSSVSG FYYSHPQSEY FNVGKISQDQ LEDYAKRKGW TLDEAKRWLG PNLDDSIV // ID D8JE19_ACISD Unreviewed; 292 AA. AC D8JE19; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Homocysteine S-methyltransferase(S-methylmethionine:homocysteine methyltransferase) {ECO:0000313|EMBL:ADI91835.1}; GN OrderedLocusNames=AOLE_14740 {ECO:0000313|EMBL:ADI91835.1}; OS Acinetobacter oleivorans (strain JCM 16667 / KCTC 23045 / DR1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=436717 {ECO:0000313|EMBL:ADI91835.1, ECO:0000313|Proteomes:UP000000392}; RN [1] {ECO:0000313|EMBL:ADI91835.1, ECO:0000313|Proteomes:UP000000392} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 1667 / KCTC 23045 / DR1 RC {ECO:0000313|Proteomes:UP000000392}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; ADI91835.1; -; Genomic_DNA. DR RefSeq; WP_013198667.1; NC_014259.1. DR RefSeq; YP_003733208.1; NC_014259.1. DR EnsemblBacteria; ADI91835; ADI91835; AOLE_14740. DR GeneID; 9383373; -. DR KEGG; acd:AOLE_14740; -. DR PATRIC; 42144908; VBIAciSp20010_2921. DR HOGENOM; HOG000265278; -. DR BioCyc; AOLE436717:GHCD-2986-MONOMER; -. DR Proteomes; UP000000392; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000392}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ADI91835.1}; KW Transferase {ECO:0000313|EMBL:ADI91835.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 202 202 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 275 275 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 276 276 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 292 AA; 32094 MW; AFC2A5E1FA09685B CRC64; MKILDGGLGR ELARRGAPFR QPEWSALALI EAPETVKEVH LDFINAGSEV ITTNNYAVVP FHIGQERFET DGVRLIQVAI EQAKNAVKES GKNVKIAGCL PPLFGSYRAD LFQPEQAKNL AEPIINTLAP EVDFWLAETQ SCLKEVETVH ALLPQDGKDY WVSFTLQDEI KQEQALLRSG ENMQQVADFI KQSNAKAVLF NCCQPEVILQ AIKEIKGLIP ESVQIGAYAN AFPPQDESAT ANDGLDEIRK DLDAPAYLGF AKQWQKAGAS LVGGCCGIGP EHIAELSQFF KE // ID D8JZ02_HYPDA Unreviewed; 353 AA. AC D8JZ02; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADJ23604.1}; GN OrderedLocusNames=Hden_1801 {ECO:0000313|EMBL:ADJ23604.1}; 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 {ECO:0000313|EMBL:ADJ23604.1, ECO:0000313|Proteomes:UP000002033}; RN [1] {ECO:0000313|Proteomes:UP000002033} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51888 / DSM 1869 / NCIB 11706 / TK 0415 RC {ECO:0000313|Proteomes:UP000002033}; 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; ADJ23604.1; -; Genomic_DNA. DR RefSeq; WP_013215763.1; NC_014313.1. DR RefSeq; YP_003755925.1; NC_014313.1. DR EnsemblBacteria; ADJ23604; ADJ23604; Hden_1801. DR KEGG; hdn:Hden_1801; -. DR PATRIC; 42372237; VBIHypDen91677_1853. DR HOGENOM; HOG000265279; -. DR OMA; AQEDYKM; -. DR BioCyc; HDEN582899:GIWL-1821-MONOMER; -. DR Proteomes; UP000002033; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002033}; KW Methyltransferase {ECO:0000313|EMBL:ADJ23604.1}; KW Transferase {ECO:0000313|EMBL:ADJ23604.1}. SQ SEQUENCE 353 AA; 38698 MW; D5AD5674E786A25D CRC64; MRRKPSWAAL EKAASERILI IDGAMGTMIQ RHKLGEEHYR GERFADHSKD VKGNNDLLVL TQPKVIEGIH AEYLDAGADI IETNTFNAQR ISLADYHMDE LGYEINVAAA KLARSAADAA TARTPEKPRF VAGAVGPTNR TASISPQVND PGFRNVNFDE LRDAYKEQVR GLIDGGADII LIETIFDTLN AKAAGFATLE VFEEKDLELP IMISGTITDR SGRTLSGQTA EAFWYSMRHL KPFSIGLNCA LGAELMRPYI AELCHVADVR ISAYPNAGLP NAMGEYDETP DEMACKVEPW LADGLINVIG GCCGSTPDHI SHIANHAKNY KPRTPTKLEP RLRLSGLEPF VHG // ID D8K547_NITWC Unreviewed; 1232 AA. AC D8K547; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 33. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADJ28024.1}; GN OrderedLocusNames=Nwat_1090 {ECO:0000313|EMBL:ADJ28024.1}; OS Nitrosococcus watsoni (strain C-113). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Nitrosococcus. OX NCBI_TaxID=105559 {ECO:0000313|EMBL:ADJ28024.1, ECO:0000313|Proteomes:UP000000393}; RN [1] {ECO:0000313|EMBL:ADJ28024.1, ECO:0000313|Proteomes:UP000000393} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C-113 {ECO:0000313|EMBL:ADJ28024.1, RC ECO:0000313|Proteomes:UP000000393}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002086; ADJ28024.1; -; Genomic_DNA. DR RefSeq; WP_013220124.1; NC_014315.1. DR RefSeq; YP_003760345.1; NC_014315.1. DR EnsemblBacteria; ADJ28024; ADJ28024; Nwat_1090. DR KEGG; nwa:Nwat_1090; -. DR PATRIC; 42234607; VBINitWat28885_1181. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; NWAT105559:GHXU-1114-MONOMER; -. DR Proteomes; UP000000393; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000393}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 762 762 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1232 AA; 137263 MW; 91A54C632FCD564F CRC64; MSVTSPRITP LKEQLAKRIL ILDGALGTMI QSYGLTEAEF RGDRFADWPC DLKGNNDLLA LTQPQILREI HGHYLEAGAD IIETNTFNAT RIAMADYRME ELAVEINQTA AQLAREMADE MTAKNPDRPR FVAGVLGPTN RTASISPDVN DPGFRNTSFD ELVAAYTESI QGLIQGGADI LLVETIFDTL NAKAAVYAIE KYFEDHQSRF PVMISGTITD ASGRTLSGQT TEAFWNSLRH AEPLAFGLNC ALGPKQLRQY VEELATLADT HVAAHPNAGL PNEFGGYDET PEEMAQEIGE WAQAGFLNIV GGCCGTTPEH IRAIREAVEK YPPRKIPQRP VACRLSGLEP SNIESDSLFV NVGERTNITG SAKFRRLIKE EDYDTALEVA RQQVENGAQI IDINMDEGLL DSQKAMVRFL NLIAAEPDIS RVPVMIDSSK WEVIEAGLKC IQGKGIVNSI SLKEGEEPFL QQAKQVRRYG AAAVIMAFDE QGQAETTERK VGICARAYQL LTEKIGFPAE DIIFDPNIFA VATGIEEHNN YGVTYIEATR EIKRTLPPAL VSGGVSNVSF SFRGNEKVRE AIHAVFLYHA IQAGMDMGIV NAGQLAVYDE IDPDLRERVE DVILNRHPEA TERLLEIAEK YRGAGGEAAE RKEDLAWREL PVNERLAHAL VKGITDFVEA DTEEARLAAK RPLDVIEGPL MDGMNVVGDL FGSGKMFLPQ VVKSARVMKK AVAYLLPFME KEKESYKSHG KVVLATVKGD VHDIGKNIVA VVLQCNSFEV IDLGVMVPAE KILQTAKEES CDFVGLSGLI TPSLDEMVHV AKEMERQNFD LPLLIGGATT SKMHTAVRIE PQYSQPVVYV PDASRVVGVA QRLLNPSLKA EYAAEITEEY GQMRRRRAEQ QTERSHTPLP QARANKLKTD WTAYVPPRPT FLGLKSFADY PLEELSARID WTPFFHAWEL AGKYPKILQD EVVGEEARKL LKDAQALLKQ VLEEKWLEAR AVIGFFPANT VNEDDIELYT DESRQEVLTT LHHIRQQMVR RSGQPNYCLA DYVAPKETGV ADYIGAFAVT AGLGIDEHLA AFAQHHDDYN SILLKAIADR LAEAFAERMH ERVRKEFWRY APDEALTNEE LISENYRGVR PAPGYPACPD HTEKATLWQL IEPDKNAGII LTESYAMVPT AAVSGWYFPH PESRYFGTGK IQKDQVKDYA RRKEISVEQV ERWLRSILGY EI // ID D8MGD8_LEUGG Unreviewed; 306 AA. AC D8MGD8; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=MmuM protein {ECO:0000313|EMBL:CBL91906.1}; GN Name=mmuM {ECO:0000313|EMBL:CBL91906.1}; GN OrderedLocusNames=LEGAS_1258 {ECO:0000313|EMBL:CBL91906.1}; OS Leuconostoc gelidum subsp. gasicomitatum (strain DSM 15947 / CECT 5767 OS / JCM 12535 / LMG 18811 / TB1-10). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostocaceae; OC Leuconostoc. OX NCBI_TaxID=762550 {ECO:0000313|EMBL:CBL91906.1, ECO:0000313|Proteomes:UP000008706}; RN [1] {ECO:0000313|Proteomes:UP000008706} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15947 / CECT 5767 / JCM 12535 / LMG 18811 / TB1-10 RC {ECO:0000313|Proteomes:UP000008706}; 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 ----------------------------------------------------------------------- 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; CBL91906.1; -; Genomic_DNA. DR RefSeq; WP_010388425.1; NC_014319.1. DR RefSeq; YP_003772725.1; NC_014319.1. DR EnsemblBacteria; CBL91906; CBL91906; LEGAS_1258. DR KEGG; lgs:LEGAS_1258; -. DR PATRIC; 42384196; VBILeuGas160647_1273. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR BioCyc; LGAS762550:GHH1-1489-MONOMER; -. DR Proteomes; UP000008706; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008706}. SQ SEQUENCE 306 AA; 33393 MW; BB9B385E96A4B6A2 CRC64; MTKFESYIES GVVILDGGMG SELEKRQIDV NNSWWSASAL VQSPENICEI HKNYFNAGAS LAITDTYQAH VKSFTDQGLS DKKAYELIDS AVNLAKRGLE NSNRSDGLIA GSVGPYGAYL ANGAEYTGDY HLSESEYQTF HRPRIARLIA DGVNVLALET MPNFDETKAL GHLLQQEFPS VDAYLSFATE NGDHLWDGTP LSEAVAYFES ISQIKAIGVN CTSPQNILPA LKNITPNTSK KIVVYPNAGD DYDPATKRWV SQHGPINWDE LVPVWLAAGA SLIGGCCRTS PEDINEIALA IISTKR // ID D8MLT5_ERWBE Unreviewed; 1227 AA. AC D8MLT5; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 29-APR-2015, entry version 33. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CAX57819.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAX57819.1}; GN Name=metH {ECO:0000313|EMBL:CAX57819.1}; GN OrderedLocusNames=EbC_02880 {ECO:0000313|EMBL:CAX57819.1}; OS Erwinia billingiae (strain Eb661). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Erwinia. OX NCBI_TaxID=634500 {ECO:0000313|Proteomes:UP000008793}; RN [1] {ECO:0000313|EMBL:CAX57819.1, ECO:0000313|Proteomes:UP000008793} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Eb661 {ECO:0000313|EMBL:CAX57819.1, RC ECO:0000313|Proteomes:UP000008793}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; FP236843; CAX57819.1; -; Genomic_DNA. DR RefSeq; WP_013200326.1; NC_014306.1. DR RefSeq; YP_003739679.1; NC_014306.1. DR EnsemblBacteria; CAX57819; CAX57819; EbC_02880. DR KEGG; ebi:EbC_02880; -. DR PATRIC; 42303392; VBIErwBil95213_0558. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; EBIL634500:GHYX-316-MONOMER; -. DR Proteomes; UP000008793; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008793}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAX57819.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008793}; KW Transferase {ECO:0000313|EMBL:CAX57819.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135704 MW; 210D1D9D0C6F4A8B CRC64; MSNRIEALQQ QLAKRIMLLD GGMGTMIQSY KLDEADFRGQ RFADWQSDLK GNNDLLVLTR PDIISEIHHA YLEAGADILE TNTFNSTTIA MADYHMASLS AEINFAAAKL ARAAADEWTA RTPDRPRYVA GVLGPTNRTC SISPDVNDPA FRNVTFIQLV DAYRESTRAL VEGGCDIIMI ETVFDTLNAK AAIFAVESEF EALGITLPLM ISGTITDASG RTLSGQTTEA FYNSLRHARP LSFGLNCALG PDELRQYVAE LSRIAEGYVT AHPNAGLPNA FGEYDLDAKI MAEQIGEWAQ SGFLNIVGGC CGTTPEHIAA MAKVIEGVAP RALPELPVAC RLAGLEPLTI SADSLFVNVG ERTNVTGSAK FKRLIKEDKY NEALEVALQQ VQSGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWEV IEKGLQCIQG KGIVNSISMK EGVDAFKHHA RLVRRYGAAM VVMAFDEIGQ ADTRERKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAM DFIGACEDIK RELPHAMISG GVSNVSFSFR GNEPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLDE DLRHAVEDVV LNRTDQGTER LLEIAEKYRG TKSDEGSTKP QAEWRNWEVE KRLEYSLVKG ITEFIEEDTE AARQNASRPI EVIEGPLMAG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPYIEASK EKGSTNGKIV LATVKGDVHD IGKNIVGVVL QCNNYEIIDL GVMVPSDKIL KTAREHNADI IGLSGLITPS LDEMVNVAKE MERQGFTLPL LIGGATTSKA HTAVKIEQNY SGPVVYVQNA SRTVGVVSAL LSAAQRDDFV ARTRKEYDTV RIQHGRKKPR TPPVSLQVAR DNDLPFDWAT YTPPVAHRLG VSEVSANIET LRHYIDWTPF FMTWSLAGKY PRILEDEVVG EEARRLLADA NAMLDDLSAN KSLNPRGVVG IFPANRVDDD IEIYEDESRS HVLQVSHHLR QQTEKTGFPN YCLADFVAPK SSGKADYLGA FAVTGGLEED ALADAFDAQH DDYNKIMVKA LSDRLAEGFA EYLHERVRKV IWGFAATENL SNEELIRENY QGIRPAPGYP ACPEHTEKET IWKLLDVEKH TGMKLTESFA MWPGAAVSGW YFSHPDSKYF AVAQLQRDQI EDYARRKGMA VSEVERWLAP NLGYDAD // ID D8MVW0_ERWBE Unreviewed; 300 AA. AC D8MVW0; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=MmuM protein {ECO:0000313|EMBL:CAX60967.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:CAX60967.1}; GN Name=mmuM {ECO:0000313|EMBL:CAX60967.1}; GN OrderedLocusNames=EbC_34360 {ECO:0000313|EMBL:CAX60967.1}; OS Erwinia billingiae (strain Eb661). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Erwinia. OX NCBI_TaxID=634500 {ECO:0000313|Proteomes:UP000008793}; RN [1] {ECO:0000313|EMBL:CAX60967.1, ECO:0000313|Proteomes:UP000008793} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Eb661 {ECO:0000313|EMBL:CAX60967.1, RC ECO:0000313|Proteomes:UP000008793}; 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 ----------------------------------------------------------------------- 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; CAX60967.1; -; Genomic_DNA. DR RefSeq; WP_013203452.1; NC_014306.1. DR RefSeq; YP_003742814.1; NC_014306.1. DR EnsemblBacteria; CAX60967; CAX60967; EbC_34360. DR KEGG; ebi:EbC_34360; -. DR PATRIC; 42309896; VBIErwBil95213_3774. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR BioCyc; EBIL634500:GHYX-3512-MONOMER; -. DR Proteomes; UP000008793; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008793}; KW Methyltransferase {ECO:0000313|EMBL:CAX60967.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008793}; KW Transferase {ECO:0000313|EMBL:CAX60967.1}. SQ SEQUENCE 300 AA; 31806 MW; 0F9992F0B8BEB889 CRC64; MAAGLVLDGA MATELEARGC DLTDALWSAK VLIENPELIY QVHYDYFNAG AQVAITASYQ ATPLGFAKRG LSEEQSLTLI ARSVELASRA RADYKAAEPQ AGNLLIAGSV GPYGAYLADG SEYRGDYSLP QAEMMAFHRP RIQALVAAGA DILACETMPS FAEIQALVAL LAEFPGTPAW FSFTLRDGEH LSDGTPLSQV VSVLESCPQA VALGLNCIAL DKVTAALQTL SSLTKKPLVV YPNSGEQYDA ISKTWHSDAS TCTLIDNLSA WQSAGAKLIG GCCRTTPADI AAIAQRCHSR // ID D8N9E6_RALSL Unreviewed; 346 AA. AC D8N9E6; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=MetHa protein {ECO:0000313|EMBL:CBJ39398.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CBJ39398.1}; GN Name=metHa {ECO:0000313|EMBL:CBJ39398.1}; GN ORFNames=CMR15_30651 {ECO:0000313|EMBL:CBJ39398.1}; OS Ralstonia solanacearum CMR15. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=859655 {ECO:0000313|EMBL:CBJ39398.1, ECO:0000313|Proteomes:UP000013571}; RN [1] {ECO:0000313|EMBL:CBJ39398.1, ECO:0000313|Proteomes:UP000013571} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CMR15 {ECO:0000313|EMBL:CBJ39398.1}; 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; CBJ39398.1; -; Genomic_DNA. DR RefSeq; WP_020749872.1; NC_017559.1. DR RefSeq; YP_005998155.1; NC_017559.1. DR EnsemblBacteria; CBJ39398; CBJ39398; CMR15_30651. DR KEGG; rsm:CMR15_30651; -. DR KO; K00548; -. DR BioCyc; RSOL859655-WGS:GSTC-3255-MONOMER; -. DR Proteomes; UP000013571; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000013571}; KW Methyltransferase {ECO:0000313|EMBL:CBJ39398.1}; KW Transferase {ECO:0000313|EMBL:CBJ39398.1}. SQ SEQUENCE 346 AA; 37527 MW; FA8C19C11A4D15EE CRC64; MTAPLPYTRA ANLPALLRER ILILDGAMGT MIQRYKLTEA QYRGERFASH PVDVKGNNEL LLLTRPEVIR EIHEQYLAAG ADLIETNTFG ATTVAQEDYK MAELAYEMNV VAARLAREAC DKYSTPDKPR FVAGAFGPTP KTASISPDVN DPGARNISFD QLRDAYYEQG KALLEGGADV FLVETIFDTL NAKAALFAID QLFEDTGERV PVMISGTVTD ASGRILSGQT VEAFWNSLRH AKPITFGLNC ALGAALMRPY IAELAKICDT AVSCYPNAGL PNPMSDTGFD ETPDVTSSLV DEFAAAGLVN LVGGCCGTTP EHIQAIAERV AQRKPRAWPG QYREAA // ID D8NQP5_RALSL Unreviewed; 346 AA. AC D8NQP5; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=MetHa protein {ECO:0000313|EMBL:CBJ44373.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CBJ44373.1}; GN Name=metHa {ECO:0000313|EMBL:CBJ44373.1}; GN ORFNames=RCFBP_21197 {ECO:0000313|EMBL:CBJ44373.1}; OS Ralstonia solanacearum CFBP2957. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=859656 {ECO:0000313|EMBL:CBJ44373.1, ECO:0000313|Proteomes:UP000008677}; RN [1] {ECO:0000313|EMBL:CBJ44373.1, ECO:0000313|Proteomes:UP000008677} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CFBP2957 {ECO:0000313|EMBL:CBJ44373.1}; 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; CBJ44373.1; -; Genomic_DNA. DR RefSeq; WP_013207130.1; NC_014307.1. DR RefSeq; YP_003746955.1; NC_014307.1. DR EnsemblBacteria; CBJ44373; CBJ44373; RCFBP_21197. DR KEGG; rsc:RCFBP_21197; -. DR PATRIC; 42548989; VBIRalSol166517_2996. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR BioCyc; RSOL859656-WGS:GST9-3123-MONOMER; -. DR Proteomes; UP000008677; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008677}; KW Methyltransferase {ECO:0000313|EMBL:CBJ44373.1}; KW Transferase {ECO:0000313|EMBL:CBJ44373.1}. SQ SEQUENCE 346 AA; 37436 MW; 4BE9F982DE9CB24F CRC64; MTAPLPYTRA ANLPALLRQR ILILDGAMGT MIQRYKLTEA QYRGERFAGH PVDVKGNNEL LLLTAPEVIR EIHEQYLAAG ADLIETNTFG ATTVAQEDYK MAELAYEMNV VAARLAREAC DKYSTPDKPR FVAGAFGPTP KTASISPDVN DPGARNINFD QLRDAYYEQG KALLEGGADV FLVETIFDTL NAKAALFAID QLFEDIGERV PVMISGTVTD ASGRILSGQT VEAFWNSLRH AKPITFGLNC ALGAALMRPY IAELAKVCDT AVSCYPNAGL PNPMSDTGFD ETPDVTSSLV DEFAAAGLVN LVGGCCGTTP EHIKAIAERV AQRKPRAWPG QYREAA // ID D8NZW6_RALSL Unreviewed; 346 AA. AC D8NZW6; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=MetHa protein {ECO:0000313|EMBL:CBJ52471.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CBJ52471.1}; GN Name=metHa {ECO:0000313|EMBL:CBJ52471.1}; GN ORFNames=RPSI07_3118 {ECO:0000313|EMBL:CBJ52471.1}; OS Ralstonia solanacearum (Pseudomonas solanacearum). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=305 {ECO:0000313|EMBL:CBJ52471.1, ECO:0000313|Proteomes:UP000006858}; RN [1] {ECO:0000313|EMBL:CBJ52471.1, ECO:0000313|Proteomes:UP000006858} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PSI07 {ECO:0000313|EMBL:CBJ52471.1}; 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; CBJ52471.1; -; Genomic_DNA. DR EnsemblBacteria; CBJ52471; CBJ52471; RPSI07_3118. DR PATRIC; 42542362; VBIRalSol167236_4749. DR HOGENOM; HOG000265279; -. DR BioCyc; RSOL859657:GJJ9-3157-MONOMER; -. DR Proteomes; UP000006858; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006858}; KW Methyltransferase {ECO:0000313|EMBL:CBJ52471.1}; KW Transferase {ECO:0000313|EMBL:CBJ52471.1}. SQ SEQUENCE 346 AA; 37612 MW; 59D80E465AFD821F CRC64; MTAPLPYTRA ANLPALLRER ILILDGAMGT MIQRYKLTEA QYRGERFTDH PVDVKGNNEL LLLTRPEVIR EIHEQYLAAG ADLIETNTFG ATTVAQEDYK MADLAYEMNV VAARLAREAC DKYSTPDKPR FVAGAFGPTP KTASISPDVN DPGARNINFD QLRDAYYDQG KALLEGGADV FLVETIFDTL NAKAALFAID QLFEDTGERV PVMISGTVTD ASGRILSGQT VEAFWNSLRH ARPITFGLNC ALGAALMRPY IAELAKICDT AVSCYPNAGL PNPMSDTGFD ETPDVTSSLV DEFAAAGLVN LVGGCCGTTP EHIKAIAERV AQRKPRAWPG QYREAA // ID D8PED6_9BACT Unreviewed; 1227 AA. AC D8PED6; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 29-APR-2015, entry version 31. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CBK41595.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CBK41595.1}; GN Name=metH {ECO:0000313|EMBL:CBK41595.1}; GN ORFNames=NIDE1868 {ECO:0000313|EMBL:CBK41595.1}; OS Candidatus Nitrospira defluvii. OC Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; Nitrospira. OX NCBI_TaxID=330214 {ECO:0000313|EMBL:CBK41595.1, ECO:0000313|Proteomes:UP000001660}; RN [1] {ECO:0000313|EMBL:CBK41595.1, ECO:0000313|Proteomes:UP000001660} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; FP929003; CBK41595.1; -; Genomic_DNA. DR RefSeq; WP_013248419.1; NC_014355.1. DR RefSeq; YP_003797520.1; NC_014355.1. DR EnsemblBacteria; CBK41595; CBK41595; NIDE1868. DR KEGG; nde:NIDE1868; -. DR PATRIC; 42242749; VBICanNit28252_1762. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR BioCyc; NDEF330214:GI4U-1834-MONOMER; -. DR Proteomes; UP000001660; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001660}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CBK41595.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001660}; KW Transferase {ECO:0000313|EMBL:CBK41595.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 246 246 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135080 MW; BBAFF68C87C9C218 CRC64; MPVHEVRDLL RERILILDGA MGTMIQRYKL DEAAFRGERF RNWSKDLKGH NDLLNVTRPD VIEAIHRQYL EAGADIIETN TFNSQSVSLA DYGMDDLGYE LSKAGAECAK RAVAQVVAAH PARRCFVAGA IGPTTKTSSV STDSNDAAAR GTTYPELVRA YGEQVRGLLD GGVDLLLVET IFDTLNAKAA FFAIQQLFAE GARQVPIMAS VTFIQAGSNR GFSGQTVEGF WNSISHVPLL SVGMNCALGP KEMRPLIEEL SQIAPIFVSS HPNAGLPNPL LPTGFPETPD SLAPQLREWA QNGWLNIVGG CCGTTPDHIR SIATAVNGVT PRQPSKVEPY LRLSGLEALT VRPESNFVNV GERTNITGSP AFSKLILTGD YDKALTVARQ QVEGGAQVID INMDEGMLDS KAAMQKFLRL LAAESDIARV PIMVDSSKWE VIEEGLRNMQ GKGIVNSISL KEGEAKFLEQ ARLIRRYGAA IVVMAFDERG QADSVARRIE ICERSYRLLT EQVGVPPQDI IFDPNILTVA TGLEEHNNYA VDFIEATRWI KQHLPLAKVS GGVSNISFSF RGNNVVREAM HAAFLYHAIQ AGLDMGIVNA GQLAVYEEIP KDLLLLVEDV LLNRRPDATE RLVTFADTVK QKGKAAVKDD EWRTRPVEER LAHALVKGLT DYIDQDVEEA RQKSVRPLDV IEGPLMAGMN IVGDLFGSGK MFLPQVVKSA RVMKKAVAYL MPFMEAEKLR LGTSRANGKV LLATVKGDVH DIGKNIVGVV LGCNNYEVID LGVMVSCETI LATAREQQVD MVGLSGLITP SLDEMVHVAK EMTRQGFTVP LLIGGATTSK AHTAVKIAPS YGHATVHVLD ASRAVGVVGS LINDEQRESF SAGVRADYDR IRQAHQDRGQ KVLRSLDEAR QHKLPTDWAA ADIPVPSFTG VRQIDRMPLR ELVPYIDWSP FFHTWELRGR YPSILDDATV GPKAKELLAD AQALLEEIIR GELLTARGVY GFFPANSAGD DIHLYRDQDR REPLATFHTL RQQMEKPADQ FNLALADYVA SKESGRADYV GAFVVTAGIG VPALCAKYEK DHDDYNSIMV KALADRLAEA FAEWLHQQVR LEWGYGKTEN LTNEDMIRER YRGIRPAPGY PACPDHTEKR TLFDLLNAEA QAGVTLTESY AMLPAAAVSG LYFAHPEAKY FAVGKINRDQ VEDYATRKKL PVSEVERWLA PNLNYDA // ID D8QBK0_SCHCM Unreviewed; 370 AA. AC D8QBK0; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 07-JAN-2015, entry version 20. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EFI94769.1}; DE Flags: Fragment; GN ORFNames=SCHCODRAFT_58848 {ECO:0000313|EMBL:EFI94769.1}; 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 {ECO:0000313|Proteomes:UP000007431}; RN [1] {ECO:0000313|EMBL:EFI94769.1, ECO:0000313|Proteomes:UP000007431} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H4-8 / FGSC 9210 {ECO:0000313|Proteomes:UP000007431}; 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; GL377309; EFI94769.1; -; Genomic_DNA. DR RefSeq; XP_003029672.1; XM_003029626.1. DR GeneID; 9592228; -. DR KEGG; scm:SCHCODRAFT_58848; -. DR InParanoid; D8QBK0; -. DR KO; K00547; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000007431; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 2. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007431}; KW Reference proteome {ECO:0000313|Proteomes:UP000007431}. FT NON_TER 1 1 {ECO:0000313|EMBL:EFI94769.1}. SQ SEQUENCE 370 AA; 40210 MW; 6956708612BF83F3 CRC64; GTTLEDIFHV DVSHTALWSA KPILEQPQVI IDAHLAFLRA GADLLSTATY QCSYRTFERA GYSDADARTA MTRAVRLADE ARRKYCEESG KALSDIKLVL SLGPFGATLS PAQEYDGCYP PPFGPQAYCT SGENINAFPA GPEGDEAESR AVQALVDFHL ERLHVFAADE EVWHAIDIIA FETIPLLREI TAVRVAMAKL VAGVADGRKA WWLSVLFPDG KFPEKRRGEP SVSREVGDIV RSAFAGRTSV GDEMAVPDGV GVNCTDVSHY SGLVEALEDA LPSYIGDSVR PWLVLYPNGG DVYDPVSRTW KEGSGKEETW ADKLVDLATR AHKATVWGGV VLGGCCRCGP DKIRMLAEKR LSLVSCASLF // ID D8R6S2_SELML Unreviewed; 327 AA. AC D8R6S2; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 07-JAN-2015, entry version 20. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EFJ32723.1}; GN ORFNames=SELMODRAFT_168384 {ECO:0000313|EMBL:EFJ32723.1}; OS Selaginella moellendorffii (Spikemoss). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Lycopodiidae; Selaginellales; Selaginellaceae; Selaginella. OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514}; RN [1] {ECO:0000313|EMBL:EFJ32723.1, ECO:0000313|Proteomes:UP000001514} 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., Soerensen 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; GL377572; EFJ32723.1; -; Genomic_DNA. DR RefSeq; XP_002966696.1; XM_002966650.1. DR EnsemblPlants; EFJ32723; EFJ32723; SELMODRAFT_168384. DR GeneID; 9652519; -. DR KEGG; smo:SELMODRAFT_168384; -. DR InParanoid; D8R6S2; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR Proteomes; UP000001514; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001514}; KW Reference proteome {ECO:0000313|Proteomes:UP000001514}. SQ SEQUENCE 327 AA; 35087 MW; 27F3E8E9F1B8A08B CRC64; MGAGKNKLEE LLESSGGCAV LDGGLATQLE HCGADLNDPL WSALCLITRP QLIQKVHWDY LEAGADILVS SSYQATVQGF VSKGLSEKEG EEMLKKSVAI ACQVRDKFWD KVKQNNSSGE IRYNRALVAA SIGSYGAYLA DGSEYSGQYG PEMMNVAKLK GFHRRRLQIL ASSGADLLAI ETIPCQVEAQ ALVELLEEED IQIPSWISFN SKDGANVVSG DPLSECVALA AKSAKVAAVG INCTPPRFIH GLVSTARKVT DKPIVVYPNS GETFDPDAKQ WIPSTGVSDV DFVSYVGEWK KAGASLIGGC CRTTPATIRA IKKSLQK // ID D8R9I7_SELML Unreviewed; 326 AA. AC D8R9I7; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 07-JAN-2015, entry version 21. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EFJ31162.1}; GN ORFNames=SELMODRAFT_88753 {ECO:0000313|EMBL:EFJ31162.1}; OS Selaginella moellendorffii (Spikemoss). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Lycopodiidae; Selaginellales; Selaginellaceae; Selaginella. OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514}; RN [1] {ECO:0000313|EMBL:EFJ31162.1, ECO:0000313|Proteomes:UP000001514} 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., Soerensen 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; GL377574; EFJ31162.1; -; Genomic_DNA. DR RefSeq; XP_002967815.1; XM_002967769.1. DR EnsemblPlants; EFJ31162; EFJ31162; SELMODRAFT_88753. DR GeneID; 9630845; -. DR KEGG; smo:SELMODRAFT_88753; -. DR InParanoid; D8R9I7; -. DR KO; K00547; -. DR OMA; SYIGKWR; -. DR Proteomes; UP000001514; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001514}; KW Reference proteome {ECO:0000313|Proteomes:UP000001514}. SQ SEQUENCE 326 AA; 35774 MW; 319FBA098DB6D6BE CRC64; MGSDARPGGF DCLEELVRHK GCVVKDGGFA TQLEKHGALL NDPLWSALCL ITNPGLIAKV HWEYLESGAE VLVTSSYQAT LQGFQSRGIS LEESEALLRK SVTLACEARD RFWRTKRAQG AERFNRPLVA ASIGSYGAFL ADGSEYSGDY GPGMTLKKLK DFHRRRLQIL SSCGPDLLAI ETIPSKLEAQ AFIELLGEED IDVPAWIAFS SKDGKNVVSG DNFSESIAML DKCDKVVAVG INCCPPHFVE GLIHEARKAT SKTIVVYPNS GEQYDPKTKL WKVQERNCEK DFMAFVKNWK RAGANVIGGC CRTTPDTVRG ICSAIF // ID D8S467_SELML Unreviewed; 330 AA. AC D8S467; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 07-JAN-2015, entry version 19. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EFJ20702.1}; GN ORFNames=SELMODRAFT_108383 {ECO:0000313|EMBL:EFJ20702.1}; OS Selaginella moellendorffii (Spikemoss). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Lycopodiidae; Selaginellales; Selaginellaceae; Selaginella. OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514}; RN [1] {ECO:0000313|EMBL:EFJ20702.1, ECO:0000313|Proteomes:UP000001514} 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., Soerensen 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; GL377601; EFJ20702.1; -; Genomic_DNA. DR RefSeq; XP_002978045.1; XM_002977999.1. DR EnsemblPlants; EFJ20702; EFJ20702; SELMODRAFT_108383. DR GeneID; 9658158; -. DR KEGG; smo:SELMODRAFT_108383; -. DR InParanoid; D8S467; -. DR KO; K00547; -. DR OMA; SEWCKDG; -. DR Proteomes; UP000001514; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001514}; KW Reference proteome {ECO:0000313|Proteomes:UP000001514}. SQ SEQUENCE 330 AA; 35355 MW; 382602B603E8FE47 CRC64; MGAGKNKLEE LLESSGGCAV LDGGLATQLE HCGADLNDPL WSALCLITRP QLIQKVHWDY LEAGADILVS SSYQATVQGF VSKGLSEKEG EEMLKKSVAI ACQVRDKFWD KVKQNNSSGE IRYNRALVAA SIGSYGAYLA DGSEYSGQYG PEMMNVAKLK GFHRRRLQIL ASSGADLLAI ETIPCQVEAQ ALVELLEEED IQIPSWISFN SKDGANVVSG DPLSECVALA AKSAKVAAVG INCTPPRFIH GLVSTARKVT DKPIVVYPNS GETFDPDAKQ WIPATGVSDV DFVSYVGEWK KAGASLIGGC CRTTPATIRA IKKSLQVSLI // ID D8SED5_SELML Unreviewed; 326 AA. AC D8SED5; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 07-JAN-2015, entry version 20. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EFJ17183.1}; GN ORFNames=SELMODRAFT_179106 {ECO:0000313|EMBL:EFJ17183.1}; OS Selaginella moellendorffii (Spikemoss). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Lycopodiidae; Selaginellales; Selaginellaceae; Selaginella. OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514}; RN [1] {ECO:0000313|EMBL:EFJ17183.1, ECO:0000313|Proteomes:UP000001514} 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., Soerensen 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; GL377615; EFJ17183.1; -; Genomic_DNA. DR RefSeq; XP_002981701.1; XM_002981655.1. DR UniGene; Smo.13832; -. DR EnsemblPlants; EFJ17183; EFJ17183; SELMODRAFT_179106. DR GeneID; 9648274; -. DR KEGG; smo:SELMODRAFT_179106; -. DR InParanoid; D8SED5; -. DR KO; K00547; -. DR OMA; GEAIRNW; -. DR Proteomes; UP000001514; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001514}; KW Reference proteome {ECO:0000313|Proteomes:UP000001514}. SQ SEQUENCE 326 AA; 35845 MW; 7EA5F3BAB7FF667B CRC64; MGSDARPGGF DCLEELVRHK GCVVKDGGFA TQLEKHGALL NDPLWSALCL ITNPGLIAKV HWEYLESGAE VLVTSSYQAT LQGFQSRGIS LEESEALLRK SVTLACEARD RFWRTKRAQK AERFNRPLVA ASIGSYGAFL ADGSEYSGDY GPGMTLKKLK DFHRRRLQIL SSCGPDLLAI ETIPSKLEAQ AFIELLGEED IDVPAWIAFS SKDGKNVVSG DNFSESIAML DKCDKVVAVG INCCPPHFVE GLIHEARKAT SKTIVVYPNS GEQYDPKTKL WKVQERNCEK DFMAFVKNWK RAGANVIGGC CRTTPDTVRG ICSAIF // ID D8TLD6_VOLCA Unreviewed; 2783 AA. AC D8TLD6; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 07-JAN-2015, entry version 24. DE SubName: Full=Vitamin B12 dependent methionine synthase {ECO:0000313|EMBL:EFJ51715.1}; GN Name=metH {ECO:0000313|EMBL:EFJ51715.1}; GN ORFNames=VOLCADRAFT_87452 {ECO:0000313|EMBL:EFJ51715.1}; OS Volvox carteri (Green alga). OC Eukaryota; Viridiplantae; Chlorophyta; Chlorophyceae; OC Chlamydomonadales; Volvocaceae; Volvox. OX NCBI_TaxID=3067 {ECO:0000313|Proteomes:UP000001058}; RN [1] {ECO:0000313|EMBL:EFJ51715.1, ECO:0000313|Proteomes:UP000001058} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=f. Nagariensis / Eve {ECO:0000313|Proteomes:UP000001058}; 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; GL378326; EFJ51715.1; -; Genomic_DNA. DR RefSeq; XP_002947125.1; XM_002947079.1. DR GeneID; 9620230; -. DR KEGG; vcn:VOLCADRAFT_87452; -. DR InParanoid; D8TLD6; -. DR KO; K00548; -. DR Proteomes; UP000001058; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 3. DR Gene3D; 3.20.20.330; -; 3. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 3. DR Pfam; PF02574; S-methyl_trans; 3. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 3. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 3. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 3. DR PROSITE; PS50972; PTERIN_BINDING; 3. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001058}; KW Reference proteome {ECO:0000313|Proteomes:UP000001058}. SQ SEQUENCE 2783 AA; 303405 MW; B836245B39F0F9BF CRC64; MKLGQAFDTL WRYPIHVILA VVASAACGAA AWPVLLPLIA SLSVIAIPAF ALAAQRAIKQ PIAEPAEEVA VSVGTAEARI CGHDAGAEEP EAATAASAGA SEAPVVQQPA VHAQLDKLLR ERIIFIDGAM GTQVQKYKLQ EEDFRGERYA NHSHELKGNN DVLVITRPDV IGEIHTAYLE AGADIIETNT FNGTCISQAD YELQADEEVA LINRTAAQLA KKCVKDFLAA HPESGPRFVA GAIGPTNKTL SVSPSVENPA FRGITYDEVV DAYYKQIEAL YEGGVDMFLV ETIFDTLNAK AAVFALEQFF TDRGVRVPVF ISGTIVDNSG RTLSGQTNEA FWNSINHAKP MAVGLNCALG ASDMLKYIAN LSACADCYVL CYPNAGLPNA MGGYDQKGGE MAEEIRPFCE AGLVNAIGGC CGTGPEHIAA IKAMASAYPP RKPPATEPLM RISGLEPLNY NPDPANMRRT FLNIGERCNV AGSILFKKAI INNDYEKAVA IALQQVQQGA DVLDINMDDG LIDGVAAMTR FVNLLVSDPE ISRVPFMIDS SKFHIVEAGL KCSQGKCIVN SISLKEGEEA FCKQAEIVKR HGAAVVVMAF DEQGQAAGYA DKVRICCRAY KLLVEQVGFN PQDIIFDPNI LTIGTGLPEH NNYAVDFIRA TREIKRLCPG AKISGGVSNI AFSFRGNEAV RRAFHSAFLL HACAAGMDMG IVNAAQVKED AYDKIDKELL EFVEDVLLNR RDDATERMLE FAATLDPKSP PTNVRRLNSQ QPSGPKITPR LNPIPKGFDP LAPDSDLPPV PSYKACIEKR QESPVFGQLD KLLRERIIFI DGAMGTQVQK YKLEEEDFRG ERYANHSHEL KGNNDVLVIT RPDVIGQIHT AYLEAGADII ETNTFNGTCI SQADYELQAD EEVALINRTA AQLAKKCVKD FLAAHPESGP RFVAGAIGPT NKTLSVSPSV ENPAFRGITY DEVVDAYYKQ IEALYEGGID MFLVETIFDT LNAKAAVFAL EQFFTDRGVR VPVFISGTIV DNSGRTLSGQ TNEAFWNSIN HAKPMAVGLN CALGASDMLK YIANLSACAD CYVLCYPNAG LPNAMGGYDQ KGEEMAEEIR PFCEAGLVNA IGGCCGTGPE HIAAIKAMAS AYPPRKPPAT EPLMRISGLE PLNYNPDPAN MRRTFLNIGE RCNVAGSILF KKAIINNDYE KAVAIALQQV QQGADVLDIN MDDGLIDGVA AMTRFVNLLV SDPEISRVPF MIDSSKFHIV EAGLKCSQGK CIVNSISLKE GEEAFCKQAE IVKRHGAAVV IMAFDEQGQA AGYADKVRIC CRAYKLLVEQ VGFNPQDIIF DPNILTVGTG LPEHNNYAVD FIRATREIKR LCPGAKISGG VSNIAFSFRG NEAVRRAFHS AFLQHACAAG MDMGIVNAAQ VKEDAYDKID KELLEFVEDV LLNRCENATE RMLEFAATLD PKSPPTNVRR LNSQQPSGPK ITPRLNPIPK GFDPLAPDSD LPPVPSYKAC IEKRQESPVF GQLDKLLRER IIFIDGAMGT QVQKYKLEEE DFRGERYANH SHELKGNNDV LVITRPDVIG QIHTAYLEAG ADIIETNTFN GTCISQADYE LQADEEVALI NRTAAQLAKK CVKDFLAAHP ESGPRFVAGA IGPTNKTLSV SPSVENPAFR GITYDEVVDA YYKQIEALYE GGIDMFLVET IFDTLNAKAA VFALEQFFTD RGVRVPVFIS GTIVDNSGRT LSGQTNEAFW NSINHAKPMA VGLNCALGAS DMLKYIANLS ACADCYVLCY PNAGLPNAMG GYDQKGGEMA EEIRPFCEAG LVNAIGGCCG TGPEHIAAIK AMASAYPPRK PPATEPLMRI SGLEPLNYNP DPANMRRTFL NIGERCNVAG SILFKKAIIN NDYEKAVAIA LQQVQQGADV LDINMDDGLI DGVAAMTRFV NLLVSDPEIS RVPFMIDSSK FHIVEAGLKC SQGKCIVNSI SLKEGEEAFC KQAEIVKRHG AAVVVMAFDE QGQAAGYADK VRICCRAYKL LVEQVGFNPQ DIIFDPNILT VGTGLPEHNN YAVDFIRATR EIKRLCPGAK ISGGVSNIAF SFRGNEAVRR AFHSAFLQHA CAAGMDMGIV NAAQVKEDAY DKIDKELLEF VEDVLLNKCE NATERMLEFA ALLEPKCKPT AVVKKGATQG AAGAGAKKEE SWRDLPVEKR IEYALVKGID EFAVVDTEEA RTCGRYTKPL HVIEGPLMDG MNVVGDLFGA GKMFLPQVIK SARVMKKAVG HLVPFIEEEK RLSGTVGEDS NAGVFVLATV KGDVHDIGKN IVGVVLGCNN FKVIDLGVMT PWDVILDAAE KHKANIIGLS GLITPSLDEM VTVAKKMEER GLKTPLLIGG ATTSKMHTAV KIAPVYSGPV VHVLDASRSV PVCQAFVDKN LTQRQEFISE VAEQYAELRE EFYASLEDRK YLSLAEARKR AFAVDWKDPI NTPFKPKVLG NTVFTEYPIE DVLPYIDWNP FFQVWQLRGR YPNRGFPRIF NDATVGAEAK KLYEEAQVML NDFVKNKRVT LKAVVGLYPA AAVGDDIEVY TDESRSSVKA RLAGLRQQAE KDGVEPYYCI SDFVAPKGSG LEDYVGMFAC SAGHGLEEVI AGFKAAGDDY SYIMAEALAD RLAEALAERL HELVRRDYWG YAADEQMSVD DMLKVKYQGI RPAPGYPSQP DHTEKLTMWG LLDAEATTDI KLTESLAMWP AASVSGLYFG GRCSSYFAVG KITREQVEDY AVRKNMDIKD AERWLATMLN YEP // ID D8TYQ9_VOLCA Unreviewed; 327 AA. AC D8TYQ9; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 07-JAN-2015, entry version 17. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EFJ47356.1}; GN ORFNames=VOLCADRAFT_92147 {ECO:0000313|EMBL:EFJ47356.1}; OS Volvox carteri (Green alga). OC Eukaryota; Viridiplantae; Chlorophyta; Chlorophyceae; OC Chlamydomonadales; Volvocaceae; Volvox. OX NCBI_TaxID=3067 {ECO:0000313|Proteomes:UP000001058}; RN [1] {ECO:0000313|EMBL:EFJ47356.1, ECO:0000313|Proteomes:UP000001058} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=f. Nagariensis / Eve {ECO:0000313|Proteomes:UP000001058}; 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; GL378345; EFJ47356.1; -; Genomic_DNA. DR RefSeq; XP_002951545.1; XM_002951499.1. DR GeneID; 9615709; -. DR KEGG; vcn:VOLCADRAFT_92147; -. DR InParanoid; D8TYQ9; -. DR KO; K00547; -. DR Proteomes; UP000001058; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001058}; KW Reference proteome {ECO:0000313|Proteomes:UP000001058}. SQ SEQUENCE 327 AA; 36357 MW; 59B2DDC4C77E4C6B CRC64; MLSSLLTNTG GVLILDGAQG TELERRGVHL GGSKLWSAQL LIDDPDLIRT IHLDYLRAGS DVITTFTYQA SIQGFADAGM DARMGATLLN RAVDLAESAR TAFLDEQRQQ HEQPPPHHQQ RVRPLIAFSS GSYGAYLADG SEFRGDYADS MTLQQLANFH RDRLEPVRHR TEIDLLAFET VPCLREAEAI LELLRQERYG KPAWISFSCR DAVHTSHGER FAEQCVPLLA AAAAEGLEVV ATGVNCTAPR HLLLVCYPNS GEEWDGEHRC WRHLPDDIAE PECFAEAAAE CVYGDPRVSL MGGCCRTGPE HIRALRRWLQ AQQHCQQ // ID D9P794_ACTPL Unreviewed; 297 AA. AC D9P794; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=Homocysteine/selenocysteine methylase(S-methylmethionine-dependent) {ECO:0000313|EMBL:EFL78232.1}; GN ORFNames=APP2_0654 {ECO:0000313|EMBL:EFL78232.1}; OS Actinobacillus pleuropneumoniae serovar 2 str. 4226. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=754254 {ECO:0000313|EMBL:EFL78232.1, ECO:0000313|Proteomes:UP000005925}; RN [1] {ECO:0000313|EMBL:EFL78232.1, ECO:0000313|Proteomes:UP000005925} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4226 {ECO:0000313|EMBL:EFL78232.1}; 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. {ECO:0000313|EMBL:EFL78232.1}. 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; ADXN01000023; EFL78232.1; -; Genomic_DNA. DR RefSeq; WP_005597940.1; NZ_ADXN01000023.1. DR ProteinModelPortal; D9P794; -. DR EnsemblBacteria; EFL78232; EFL78232; APP2_0654. DR PATRIC; 41123694; VBIActPle155200_1735. DR Proteomes; UP000005925; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005925}; KW Methyltransferase {ECO:0000313|EMBL:EFL78232.1}; KW Transferase {ECO:0000313|EMBL:EFL78232.1}. SQ SEQUENCE 297 AA; 32341 MW; E74F7F51335D3F4A CRC64; MTITILDGGM SRELMRLNAP FKQPEWSALS LYEKPSAVQQ VHEDFIANGA EVITTNSYAV VPFHIGEQRF SADGKMLADL AGRLAKQAVK NSGKSAKIAG SLPPMFGSYR ADLIQADRFA EIAQPIIDGL APYVDIWLCE TQSAIIEPTS IKPLLPKDDR PLWVSFTLTD DEPTPEPQLR SGEPVALAIE KMVELGVDAI LFNCCQPEVI EQALAITQSI LKEKNVTHIQ TGAYANAFAP QPKDATANDG LDEVRKDLDP EAYLAWAQKW TAQGATIIGG CCGIGIEYIN TLAKNLK // ID D9PAC2_ACTPL Unreviewed; 297 AA. AC D9PAC2; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=Homocysteine/selenocysteine methylase(S-methylmethionine-dependent) {ECO:0000313|EMBL:EFL81388.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFM91771.1}; GN ORFNames=APP6_1587 {ECO:0000313|EMBL:EFL81388.1}, GN appser6_12310 {ECO:0000313|EMBL:EFM91771.1}; OS Actinobacillus pleuropneumoniae serovar 6 str. Femo. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=754256 {ECO:0000313|EMBL:EFL81388.1, ECO:0000313|Proteomes:UP000005341}; RN [1] {ECO:0000313|EMBL:EFM91771.1, ECO:0000313|Proteomes:UP000005341} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Femo {ECO:0000313|EMBL:EFM91771.1}; 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). RN [2] {ECO:0000313|EMBL:EFL81388.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Femo {ECO:0000313|EMBL:EFL81388.1}; 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. {ECO:0000313|EMBL:EFL81388.1}. 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; ADXO01000007; EFL81388.1; -; Genomic_DNA. DR EMBL; ADOG01000017; EFM91771.1; -; Genomic_DNA. DR RefSeq; WP_005608290.1; NZ_ADXO01000007.1. DR EnsemblBacteria; EFL81388; EFL81388; APP6_1587. DR EnsemblBacteria; EFM91771; EFM91771; appser6_12310. DR PATRIC; 40898590; VBIActPle158270_0724. DR Proteomes; UP000005341; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005341}; KW Methyltransferase {ECO:0000313|EMBL:EFL81388.1}; KW Transferase {ECO:0000313|EMBL:EFL81388.1}. SQ SEQUENCE 297 AA; 32326 MW; 3CB4460C53513841 CRC64; MTITILDGGM SRELMRLNAP FKQPEWSALS LYEKPSAVQQ VHEDFIANGA EVITTNSYAV VPFHIGEQRF SADGKMLADL AGRLAKQAVK NSGKSAKIAG SLPPMFGSYR ADLIQADRFA EIAQPIIDGL SPYVDIWLCE TQSAIIEPTS IKPLLPKDNR PLWVSFTLTD DEPTPEPQLR SGESVALAIE KMVELDVDAI LFNCCQPEVI EQALAITQSI LKAKNATHIQ TGAYANAFAP QPKDATANDG LDEVRKDLDP KAYLAWAQKW TAQGATIVGG CCGIGIEYIN TLAKHLK // ID D9Q8D7_CORP1 Unreviewed; 1199 AA. AC D9Q8D7; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 34. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADL20932.1}; GN Name=metH {ECO:0000313|EMBL:ADL20932.1}; GN OrderedLocusNames=Cp1002_1047 {ECO:0000313|EMBL:ADL20932.1}; OS Corynebacterium pseudotuberculosis (strain 1002). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=679896 {ECO:0000313|EMBL:ADL20932.1, ECO:0000313|Proteomes:UP000008684}; RN [1] {ECO:0000313|EMBL:ADL20932.1, ECO:0000313|Proteomes:UP000008684} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1002 {ECO:0000313|EMBL:ADL20932.1, RC ECO:0000313|Proteomes:UP000008684}; RX PubMed=21037006; DOI=10.1128/JB.01211-10; RG Consortium: Rede Paraense de Genomica e Proteomica (RPGP); RA Silva A., Schneider M.P., Cerdeira L., Barbosa M.S., Ramos R.T., RA Carneiro A.R., Santos R., Lima M., D'Afonseca V., Almeida S.S., RA Santos A.R., Soares S.C., Pinto A.C., Ali A., Dorella F.A., Rocha F., RA de Abreu V.A., Trost E., Tauch A., Shpigel N., Miyoshi A., Azevedo V.; RT "Complete genome sequence of Corynebacterium pseudotuberculosis I19, a RT strain isolated from a cow in Israel with bovine mastitis."; RL J. Bacteriol. 193:323-324(2011). RN [2] {ECO:0000313|EMBL:ADL20932.1, ECO:0000313|Proteomes:UP000008684} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1002 {ECO:0000313|EMBL:ADL20932.1, RC ECO:0000313|Proteomes:UP000008684}; RX PubMed=21533164; DOI=10.1371/journal.pone.0018551; RA Ruiz J.C., D'Afonseca V., Silva A., Ali A., Pinto A.C., Santos A.R., RA Rocha A.A., Lopes D.O., Dorella F.A., Pacheco L.G., Costa M.P., RA Turk M.Z., Seyffert N., Moraes P.M., Soares S.C., Almeida S.S., RA Castro T.L., Abreu V.A., Trost E., Baumbach J., Tauch A., RA Schneider M.P., McCulloch J., Cerdeira L.T., Ramos R.T., Zerlotini A., RA Dominitini A., Resende D.M., Coser E.M., Oliveira L.M., Pedrosa A.L., RA Vieira C.U., Guimaraes C.T., Bartholomeu D.C., Oliveira D.M., RA Santos F.R., Rabelo E.M., Lobo F.P., Franco G.R., Costa A.F., RA Castro I.M., Dias S.R., Ferro J.A., Ortega J.M., Paiva L.V., RA Goulart L.R., Almeida J.F., Ferro M.I., Carneiro N.P., Falcao P.R., RA Grynberg P., Teixeira S.M., Brommonschenkel S., Oliveira S.C., RA Meyer R., Moore R.J., Miyoshi A., Oliveira G.C., Azevedo V.; RT "Evidence for reductive genome evolution and lateral acquisition of RT virulence functions in two Corynebacterium pseudotuberculosis RT strains."; RL PLoS ONE 6:E18551-E18551(2011). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001809; ADL20932.1; -; Genomic_DNA. DR RefSeq; WP_013241907.1; NC_017300.1. DR RefSeq; YP_005681320.1; NC_017300.1. DR EnsemblBacteria; ADL20932; ADL20932; Cp1002_1047. DR KEGG; cpk:Cp1002_1047; -. DR PATRIC; 42895898; VBICorPse156913_1093. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR BioCyc; CPSE679896:GLBP-1100-MONOMER; -. DR Proteomes; UP000008684; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008684}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 233 233 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 750 750 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1199 AA; 130892 MW; 75A2CDC61D5CF704 CRC64; MTTANITFQT DFLDAMKDRV LIGDGAMGTQ LQAFDLDVDK DFLGLEGCNE ILNITRPDVV AQIHRSYFEA GADLVETNTF GCNLPNLADY GIAERCRELA YQGVHIARTV ADELGPGRDG LRRFVLGSMG PGTKLPSLGH ASFEELREYY SEAAVGMIEG GADAILIETA QDLLQVKAAI HGCQHAFEIV GIKLPLVCHV TVETTGTMLL GSEIGAALTA LEPLGIDMIG LNCATGPDEM SEHLRFLSQN AGIPVSVMPN AGLPVLGKNG AEYPLSAHEL AAALRGFVND YGLSMVGGCC GTTPSHISAV RDAIVGTSNA TAAHQARRSP TVGDAVSSLY TSVNLTQDTG ITMIGERTNA NGSKAFREAM LAEDWETCID IAKQQTRDGA HMLDLCVDYV GRDGRQDMAQ LASLLSTSST LPIMIDSTEP DVIQVGLEHL GGRCAVNSVN FEDGDGPKSR YQRIMRLVKQ HGAAVVALTI DEDGQARTAA KKIAIAERLI TDITQTWGLE EDDIIVDCLT FPISTGQEET RRDGIETIEV IRELKKRYPR IHTTLGLSNI SFGLNPAARQ VLNSVFLNEC IGAGLDSAIA HSSKILPMNK IDEEQRRVAL DMVYDKRTAD YDPLQAFMRL FEGVSASTAK DARAEALAAM PLFERIAQRV IDGEKTGIEA DLDQAMAEKE PLQIINEDLL EGMKTVGELF GSGQMQLPFV LQSAETMKHA VAYLEQFMEA EDDTGGNGTI VIATVKGDVH DIGKNLVDII LSNNGFNVVN IGIKQPISNI LDAAKKHNAD AIGMSGLLVK STVIMKENLQ EMNAVKASHF PVILGGAALT RAYVEDDLTE VYDGNVYYAK DAFESLRLMQ EFMASIRGEG LDPNSPDAIK AAQKKAERKA RKERSKKIAA ERKAKAEPVA VPARSQVSET SPIATPPFWG TRIVKGLNLS EYLPLLDERA LFMGRWGLKA TRGAAGPSYE ELVETEGRPR LRYWIDRLKA EKVLDHAAVI YGYFPAVSEG NDVILLESPD PEATEIARFT FPRQQRSKFL CIADFIQSRT RSLEQGSVDV FPLQLVTMGQ PIADFANELF AADNYRDYLE VHGIGVQLTE AMAEYWHARV RGELTFIDGS SAGDKDAKNL QRFFDLDYLG ARYSFGYGSC PNLEDRKTLV QLLDAQRIGV ELSEELQLHP EQSTDAFVLY HPEAKYFNV // ID D9QAE5_CORP2 Unreviewed; 1199 AA. AC D9QAE5; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 35. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADL10521.1}; GN Name=metH {ECO:0000313|EMBL:ADL10521.1}; GN OrderedLocusNames=CpC231_1045 {ECO:0000313|EMBL:ADL10521.1}; OS Corynebacterium pseudotuberculosis (strain C231). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=681645 {ECO:0000313|EMBL:ADL10521.1, ECO:0000313|Proteomes:UP000000276}; RN [1] {ECO:0000313|EMBL:ADL10521.1, ECO:0000313|Proteomes:UP000000276} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C231 {ECO:0000313|EMBL:ADL10521.1, RC ECO:0000313|Proteomes:UP000000276}; RX PubMed=21037006; DOI=10.1128/JB.01211-10; RG Consortium: Rede Paraense de Genomica e Proteomica (RPGP); RA Silva A., Schneider M.P., Cerdeira L., Barbosa M.S., Ramos R.T., RA Carneiro A.R., Santos R., Lima M., D'Afonseca V., Almeida S.S., RA Santos A.R., Soares S.C., Pinto A.C., Ali A., Dorella F.A., Rocha F., RA de Abreu V.A., Trost E., Tauch A., Shpigel N., Miyoshi A., Azevedo V.; RT "Complete genome sequence of Corynebacterium pseudotuberculosis I19, a RT strain isolated from a cow in Israel with bovine mastitis."; RL J. Bacteriol. 193:323-324(2011). RN [2] {ECO:0000313|EMBL:ADL10521.1, ECO:0000313|Proteomes:UP000000276} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C231 {ECO:0000313|EMBL:ADL10521.1, RC ECO:0000313|Proteomes:UP000000276}; RX PubMed=21533164; DOI=10.1371/journal.pone.0018551; RA Ruiz J.C., D'Afonseca V., Silva A., Ali A., Pinto A.C., Santos A.R., RA Rocha A.A., Lopes D.O., Dorella F.A., Pacheco L.G., Costa M.P., RA Turk M.Z., Seyffert N., Moraes P.M., Soares S.C., Almeida S.S., RA Castro T.L., Abreu V.A., Trost E., Baumbach J., Tauch A., RA Schneider M.P., McCulloch J., Cerdeira L.T., Ramos R.T., Zerlotini A., RA Dominitini A., Resende D.M., Coser E.M., Oliveira L.M., Pedrosa A.L., RA Vieira C.U., Guimaraes C.T., Bartholomeu D.C., Oliveira D.M., RA Santos F.R., Rabelo E.M., Lobo F.P., Franco G.R., Costa A.F., RA Castro I.M., Dias S.R., Ferro J.A., Ortega J.M., Paiva L.V., RA Goulart L.R., Almeida J.F., Ferro M.I., Carneiro N.P., Falcao P.R., RA Grynberg P., Teixeira S.M., Brommonschenkel S., Oliveira S.C., RA Meyer R., Moore R.J., Miyoshi A., Oliveira G.C., Azevedo V.; RT "Evidence for reductive genome evolution and lateral acquisition of RT virulence functions in two Corynebacterium pseudotuberculosis RT strains."; RL PLoS ONE 6:E18551-E18551(2011). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001829; ADL10521.1; -; Genomic_DNA. DR RefSeq; WP_014522409.1; NC_017301.1. DR RefSeq; YP_005683411.1; NC_017301.1. DR EnsemblBacteria; ADL10521; ADL10521; CpC231_1045. DR GeneID; 12299473; -. DR KEGG; cpq:CpC231_1045; -. DR PATRIC; 42900469; VBICorPse140234_1098. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; CPSE681645:GLBW-1104-MONOMER; -. DR Proteomes; UP000000276; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000276}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000276}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 233 233 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 750 750 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1199 AA; 130922 MW; 023CBDC0AA37870B CRC64; MTTANITFQT DFLDAMKDRV LIGDGAMGTQ LQAFDLDVDK DFLGLEGCNE ILNITRPDVV AQIHRSYFEA GADLVETNTF GCNLPNLADY GIAERCRELA YQGVHIARTV ADELGPGRDG LRRFVLGSMG PGTKLPSLGH ASFEELREYY SEAAVGMIEG GADAILIETA QDLLQVKAAI HGCQHAFEIV GIKLPLVCHV TVETTGTMLL GSEIGAALTA LEPLGIDMIG LNCATGPDEM SEHLRFLSQN AGIPVSVMPN AGLPVLGKNG AEYPLSAHEL AAALRGFVND YGLSMVGGCC GTTPSHISAV RDAIVGTSNA TAAHQARRSP TVGDAVSSLY TSVNLTQDTG ITMIGERTNA NGSKAFREAM LAEDWETCID IAKQQTRDGA HMLDLCVDYV GRDGRQDMAQ LASLLSTSST LPIMIDSTEP DVIQVGLEHL GGRCAVNSVN FEDGDGPKSR YQRIMRLVKQ HGAAVVALTI DEDGQARTAA KKIAIAERLI TDITQTWGLE EDDIIVDCLT FPISTGQEET RRDGIETIEV IRELKKRYPR IHTTLGLSNI SFGLNPAARQ VLNSVFLNEC IGAGLDSAIA HSSKILPMNK IDEEQRRVAL DMVYDKRTAD YDPLQAFMRL FEGVSASTAK DARAEALAAM PLFERIAQRV IDGEKTGIEA DLDQAMAEKE PLQIINEDLL EGMKTVGELF GSGQMQLPFV LQSAETMKHA VAYLEQFMEA EDDTGGNGTI VIATVKGDVH DIGKNLVDII LSNNGFNVVN IGIKQPISNI LDAAKKHNAD AIGMSGLLVK STVIMKENLQ EMNAVKASHF PVILGGAALT RAYVEDDLTE VYDGNVYYAK DAFESLRLMQ EFMASIRGEG LDPNSPDAIK AAQKKAERKA RKERSKKIAA ERKAKAEPVA VPARSQVSET SPITTPPFWG TRIVKGLNLS EYLPLLDERA LFMGRWGLKA TRGAAGPSYE ELVETEGRPR LRYWIDRLKA EKVLDHAAVI YGYFPAVSEG NDVILLESPD PEATEIARFT FPRQQRSKFL CIADFIQSRT RSLEQGSVDV FPLQLVTMGQ PIADFANELF AADNYRDYLE VHGIGVQLTE AMAEYWHARV RGELTFIDGS SAGDKDAKNL QRFFDLDYLG ARYSFGYGSC PNLEDRKTLV QLLDAQRIGV ELSEELQLHP EQSTDAFVLY HPEAKYFNV // ID D9QK44_BRESC Unreviewed; 356 AA. AC D9QK44; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 30. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADL01629.1}; GN OrderedLocusNames=Bresu_2319 {ECO:0000313|EMBL:ADL01629.1}; 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 {ECO:0000313|EMBL:ADL01629.1, ECO:0000313|Proteomes:UP000002696}; RN [1] {ECO:0000313|Proteomes:UP000002696} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15264 / DSM 4735 / LMG 14903 / NBRC 16000 / CB 81 RC {ECO:0000313|Proteomes:UP000002696}; 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; ADL01629.1; -; Genomic_DNA. DR RefSeq; WP_013269730.1; NC_014375.1. DR RefSeq; YP_003819252.1; NC_014375.1. DR EnsemblBacteria; ADL01629; ADL01629; Bresu_2319. DR KEGG; bsb:Bresu_2319; -. DR PATRIC; 42203847; VBIBreSub37974_2336. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR BioCyc; BSUB633149:GHJJ-2352-MONOMER; -. DR Proteomes; UP000002696; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002696}; KW Methyltransferase {ECO:0000313|EMBL:ADL01629.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002696}; KW Transferase {ECO:0000313|EMBL:ADL01629.1}. SQ SEQUENCE 356 AA; 38879 MW; B06F47AD15B4A3A8 CRC64; MTARAQRIAA LHAAARERIL VLDGSWGVMI QRAELSEEDF RGDRFTAHEG QMKGNNDILC ITRPDVIGDL HDQYFAAGAD ISETNTFSAT VIAQDDYKLE ADAVWDINLE GAKLARASAD RWTEKEPHKP RFAAGSIGPL NKMLSMSSDV NDPGARLVTF DQVYDAYRHQ VKALNEGGVD LYLIETITDT LNCKAAIKAI KDLEDEGMEA LPIWISGTIT DRSGRTLSGQ TAEAFWNSVR HAKPFAVGFN CALGADLMRP FIAELSRVAD TLVAAYPNAG LPNAMGQYDE EPHQTAHFIE EWAASGLVNI VGGCCGTTPD HIKHTAEAVS KLPTREIPER PVAMRLSGLE PFELVA // ID D9QQ07_ACEAZ Unreviewed; 562 AA. AC D9QQ07; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 29-APR-2015, entry version 26. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADL12598.1}; GN OrderedLocusNames=Acear_1072 {ECO:0000313|EMBL:ADL12598.1}; OS Acetohalobium arabaticum (strain ATCC 49924 / DSM 5501 / Z-7288). OC Bacteria; Firmicutes; Clostridia; Halanaerobiales; Halobacteroidaceae; OC Acetohalobium. OX NCBI_TaxID=574087 {ECO:0000313|EMBL:ADL12598.1, ECO:0000313|Proteomes:UP000001661}; RN [1] {ECO:0000313|EMBL:ADL12598.1, ECO:0000313|Proteomes:UP000001661} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49924 / DSM 5501 / Z-7288 RC {ECO:0000313|Proteomes:UP000001661}; RX PubMed=21304692; RA Sikorski J., Lapidus A., Chertkov O., Lucas S., Copeland A., RA Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Han C., RA Brambilla E., Pitluck S., Liolios K., Ivanova N., Mavromatis K., RA Mikhailova N., Pati A., Bruce D., Detter C., Tapia R., Goodwin L., RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., RA Jeffries C.D., Rohde M., Goker M., Spring S., Woyke T., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Acetohalobium arabaticum type strain (Z- RT 7288)."; RL Stand. Genomic Sci. 3:57-65(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; CP002105; ADL12598.1; -; Genomic_DNA. DR RefSeq; WP_013278044.1; NC_014378.1. DR RefSeq; YP_003827663.1; NC_014378.1. DR EnsemblBacteria; ADL12598; ADL12598; Acear_1072. DR KEGG; aar:Acear_1072; -. DR PATRIC; 42136357; VBIAceAra30843_1103. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EINIESA; -. DR BioCyc; AARA574087:GHPK-1139-MONOMER; -. DR Proteomes; UP000001661; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001661}; KW Methyltransferase {ECO:0000313|EMBL:ADL12598.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001661}; KW Transferase {ECO:0000313|EMBL:ADL12598.1}. SQ SEQUENCE 562 AA; 61100 MW; BAD31513722D9E0A CRC64; MKSDFLTELE SEVLLFDGAM GTQLQQAGLG TDTAPEAWNL ENPKAIKKIH KSYLAAGSRV IQTNTFGANC IKLGKYDLED KVTEINQAAV EIAKEVQKDG YVAGSIGPLG KLFAPMGTLT FREGVDVFAE QIRALVNAGV DVISFETMND LQELRAAVVA AKEVTSEVPI IAQMTFDENL RSLSGTNPQI AATVLDSLGA DIIGANCSLG PQGLLEVLKA LNRTTDKPII IQPNAGLPEI VDGETVYQQS PEEMAEYIKR FVQEGANIIG GCCGTSPEHI KAFAEKLSRL EPKRSAADKK FRLASGMELV ELSEDSRSLM IGEQINTDSD KRLTEEIKDQ VEAGAQVLNI NVDGTDIDGV EIQQVVERVQ KTSRASMAID TADIEVLEAG LEAFVGKALI NSVTGREEDL NRILPLAKKY GAGLICSTVD DDGIPGTAEK RVEIAKRIKQ QTGEYGIAPE DLLINPVAVT VSSQQEAAIE TLQAIKLIKE HLDLKTVLQV DNISDKLPKR LLLDRTFISM ALGYGLDAYI IDPLNEEIRE TILAAEVLVN RDRDAERYIT EF // ID D9R4F1_CLOSW Unreviewed; 812 AA. AC D9R4F1; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 29-APR-2015, entry version 26. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADL05021.1}; GN OrderedLocusNames=Closa_2452 {ECO:0000313|EMBL:ADL05021.1}; OS Clostridium saccharolyticum (strain ATCC 35040 / DSM 2544 / NRCC 2533 OS / WM1). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=610130 {ECO:0000313|EMBL:ADL05021.1, ECO:0000313|Proteomes:UP000001662}; RN [1] {ECO:0000313|EMBL:ADL05021.1, ECO:0000313|Proteomes:UP000001662} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35040 / DSM 2544 / NRCC 2533 / WM1 RC {ECO:0000313|Proteomes:UP000001662}; 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 ----------------------------------------------------------------------- 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; ADL05021.1; -; Genomic_DNA. DR RefSeq; WP_013273107.1; NC_014376.1. DR RefSeq; YP_003822644.1; NC_014376.1. DR EnsemblBacteria; ADL05021; ADL05021; Closa_2452. DR KEGG; csh:Closa_2452; -. DR PATRIC; 42266570; VBICloSac91065_2655. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR BioCyc; CSAC610130:GHTP-2516-MONOMER; -. DR Proteomes; UP000001662; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001662}; KW Methyltransferase {ECO:0000313|EMBL:ADL05021.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001662}; KW Transferase {ECO:0000313|EMBL:ADL05021.1}. SQ SEQUENCE 812 AA; 87353 MW; 95EA87D86ECEE6FA CRC64; MAGILEEIKK RMVFFDGGTG SLLQACGLEP GELPETWNVK HPDIIAKLHR DYLEAGADII KTNTFGANGL KFHKGAEFDL EEVVTAAFRN ARNAVDTASY PEGKGKGYIA LDLGPTGKLL KPLGDLDFED AYQMFSKVVK IGEREGADLV LIETMSDSYE AKAAVLAAKE NSSLPVFVTM IFDEKGKLLT GGNVESTVAL LEGLGVDALG INCGLGPVQM KSILADIMKV VSIPVIVNPN AGLPRSEGGK TVYDIDAGEF ADAMKEIAEE GACVIGGCCG TTPEHIKKTV ALCKDFPVRL PDRKNRTVIS SYSQAVLIGD DPVIIGERIN PTGKSKFKQA LRDHNLEYIL REGVTQQDNG AHVLDVNVGL PEIDEPSMMV EVIRELQSII DLPLQIDTSN TEAMEWAMRV YNGKPLINSV NGKKEVMETI FPLVKRYGGV VVALALDEDG IPETADGRIA VANKIYEKAG EYGIEKKDII IDALCMTVSS DSKGALTTLE TLRRIRDELG GRTILGVSNI SFGLPQREII NSTFFAMALQ NGLSAAIINP NSEAMMRSYY SFRTLAGLDP QCSGYISVYS GQVATLGETV KQGTASSSGS TSGKDMPLSE SIAKGLKDRA HAAVTELLKE LEPLTIINEE MIPALDRVGK GFENGTVFLP QLLMSAEAAK AAFEVIKEKM AEGGMAQEKK GKIILATVKG DIHDIGKNIV KVLLENYSYD VIDLGKDVPP EKIVETAVRE GVKLVGLSAL MTTTVPSMEE TIRQLRETAP AVKVMVGGAV LTEGYAKTIG ADQYCRDAMA SVNYAEGIFH GK // ID D9RVU8_PREMB Unreviewed; 915 AA. AC D9RVU8; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 36. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:ADK96944.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADK96944.1}; GN Name=metH {ECO:0000313|EMBL:ADK96944.1}; GN OrderedLocusNames=HMPREF0659_A6783 {ECO:0000313|EMBL:ADK96944.1}; 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 {ECO:0000313|EMBL:ADK96944.1, ECO:0000313|Proteomes:UP000001498}; RN [1] {ECO:0000313|Proteomes:UP000001498} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25845 / DSM 7089 / JCM 6325 / VPI 2381 / B282 RC {ECO:0000313|Proteomes:UP000001498}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002123; ADK96944.1; -; Genomic_DNA. DR RefSeq; WP_013265413.1; NC_014371.1. DR RefSeq; YP_003814824.1; NC_014371.1. DR EnsemblBacteria; ADK96944; ADK96944; HMPREF0659_A6783. DR KEGG; pmz:HMPREF0659_A6783; -. DR PATRIC; 42433368; VBIPreMel47739_1765. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PMEL553174:GH7V-1776-MONOMER; -. DR Proteomes; UP000001498; Chromosome II. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001498}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADK96944.1}; KW Transferase {ECO:0000313|EMBL:ADK96944.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 240 240 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 915 AA; 100852 MW; 21735773C9BF28A7 CRC64; MKLRDNIKDR ILILDGAMGT MIQGYNLTEK DFRGNLELLQ MLNYQGNNDM LNLSRPDIIE DIHRRYLEVG ADIISTNTFS AQRISQADYH MESFSRDIAF AGAKLARKCA DEYSTADKPR FVAGSIGPTN KTCSMSPDVS DPAKRDLTYD ALFDAYSEQV AAMIEGGIDA VLIETIFDTL NAKVAIDASL SEMKKAGIDL PIMLSVTITD LSGRTLSGQT LDAFLASVSS YPIFSVGLNC SFGAEQMRPY LKELAAKAPY YISIHPNAGL PNSMGEYDET AEIMVPQMAS FVDEGLVNII GGCCGTTEEF IAGYVKVVEG KKPHIPVDAP KEMILSGLEQ FRLTPEISFV NVGERCNVAG SRKFLRLVKE KNYEEALTIA RKQVDDGALV LDINMDDGLL EAKDEMAHFV NMISSEPEIA RVPLMIDSSD WEVVVSALKC VQGKAIVNSI SLKEGEEVFI RHAKDVLRFG AAVVVMCFDE EGQATSYERR IEIAERAYKI LTEKVGFPPQ NIIFDPNILA ICTGMKEHNS YAVDFIRATK WIKKNLPGAH VSGGVSNLSF SFRGNNYIRE AMHAVFLYHA IQVGMDFGIV NPATKVTYAD IPEDHLKIIE DVVLDRVEGA DELLIELANK ILEEKEAQKN GGATQKVAQE AWRNDILEDR LKYALRKGIS TYLNEDIHEA LEKYPHAVNI IEGPLMQGMN EVGDLFGAGK MFLPQVVKTA RTMKDAVAIL QPYIEKEKVD GKAIAGKVLL ATVKGDVHDI GKNIVGVVMA CNNYEVIDLG VMVPADQIIK KAKEENVDLI GLSGLITPSL QEMVNSVVAF KEAGLNIPVM IGGATTSQLH VALKIAPLYD APVVWVKDAS VNPSIAAALL NEKERERFCK ELDATYEKLR AGYKEEQQKV LSLSKARENK LNLFD // ID D9SI53_GALCS Unreviewed; 1224 AA. AC D9SI53; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 33. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADL54110.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADL54110.1}; GN OrderedLocusNames=Galf_0065 {ECO:0000313|EMBL:ADL54110.1}; 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 {ECO:0000313|EMBL:ADL54110.1, ECO:0000313|Proteomes:UP000001235}; RN [1] {ECO:0000313|EMBL:ADL54110.1, ECO:0000313|Proteomes:UP000001235} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ES-2 {ECO:0000313|EMBL:ADL54110.1, RC ECO:0000313|Proteomes:UP000001235}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002159; ADL54110.1; -; Genomic_DNA. DR RefSeq; WP_013292053.1; NC_014394.1. DR RefSeq; YP_003845874.1; NC_014394.1. DR EnsemblBacteria; ADL54110; ADL54110; Galf_0065. DR KEGG; gca:Galf_0065; -. DR PATRIC; 42336673; VBIGalCap53152_0068. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR BioCyc; GCAP395494:GHXI-65-MONOMER; -. DR Proteomes; UP000001235; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001235}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADL54110.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001235}; KW Transferase {ECO:0000313|EMBL:ADL54110.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 243 243 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 757 757 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1224 AA; 134068 MW; 5E35FD1015E5BEBD CRC64; MTRHLIEDII QQRILILDGA MGTMIQRYKL NEADYRGERF AQWPQDLKGN NDLLVLTKPE VIRAIHSEYL AAGADIVETN TFGANATTLK AYGMAELNYE LNVAGARLAR EACDAYSTPD KPRFVAGVLG PTDKTATISP DVNDPAARNI SFDQLVADYS DATRGLMDGG ADTILIETIF DTLNAKAAIF AVQSVFTERG TRLPIMISGT ITDASGRTLT GQVTEAFYNS LAHAQPLSIG LNCALGAEEL RQYVAELSRV ANCYVSAHPN AGLPNPLAET GYDDTPENMA GHIKEWAASG FLNIIGGCCG TSPAFIKAIA ETVQGIAPRK IPENPVECRL SGLEPFNISD SSLFVNVGER ANVTGSAKFK RLILEGKYDE ALEVAKQQVE TGAQVIDVNM DEAMLDGEAA MVRFLNLIAS EPDISKVPLM IDSSKWSIIE AGLKCVQGKS IVNSISLKEG EENFIKYATL VRKYGAAAVV MAFDEAGQAD TYARKIEICK RSYDILVNKV GFPPEDIIFD PNIFAIATGI EEHNNYAVDF IEACKWIRAN LPYAKISGGV SNVSFSFRGN EPVREAIHTV FLYHAIGAGM NMGIVNAGQL GVYEEIPREL RDAVEDVVLN RHPDAGEKLV KIAESVKGGG KEIIEDLEWR KGTVQERLTH ALVRGITTFI VEDTEEARLA AKFPVEVIED SLMSGMNVVG DLFGAGKMFL PQVVKSARVM KQAVAHLIPY IEAEKLRSGD TSTKGKILMA TVKGDVHDIG KNIVTVVLQC NNFEVVNMGV MVPCQQILDA AREHKVDVIG LSGLITPSLE EMAHVAKEME RQGFKIPLLI GGATTSRVHT AVKIEPNYPS GTVIYVTDAS RAVGVCSNLL SDTLRDDYVA SIKADYIEAR ETHEARQSKA VYVTLEAARA HGMKTDWNAY TPPKPKFTGV KELRDYSLSE IAEYIDWTPF FQAWELAGRY PKILQDEVVG EESRKLFADA QAMLKQIIDG KWLTANAVYG LFPANTINGD DIEIYTDETR SECAMTWHNL RQQTKKPASI PNYCLADYIA PKGVADYIGG FAVTTGIGID ARVAEFEAQN DDYNAIMLKA LADRLAEAFA ELLHARVRRE FWGYASDEGL DNDALIAEKY RGIRPAPGYP ACPEHSEKGP LFAMLDATRR AGISITDSFA MLPTAAVSGF YFSHPEAKYF ATGKIDRDQV ASYAERKGWD IETAERWLAP VLSY // ID D9SQZ1_CLOC7 Unreviewed; 609 AA. AC D9SQZ1; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 28. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=Clocel_0504 {ECO:0000313|EMBL:ADL50279.1}; OS Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / OS 743B). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=573061 {ECO:0000313|EMBL:ADL50279.1, ECO:0000313|Proteomes:UP000002730}; RN [1] {ECO:0000313|EMBL:ADL50279.1, ECO:0000313|Proteomes:UP000002730} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35296 / DSM 3052 / OCM 3 / 743B RC {ECO:0000313|Proteomes:UP000002730}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ADL50279.1; -; Genomic_DNA. DR RefSeq; WP_010074950.1; NZ_BABR01000250.1. DR RefSeq; YP_003842043.1; NC_014393.1. DR ProteinModelPortal; D9SQZ1; -. DR EnsemblBacteria; ADL50279; ADL50279; Clocel_0504. DR KEGG; ccb:Clocel_0504; -. DR PATRIC; 41735969; VBICloCel81632203721_1787. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR BioCyc; CCEL573061:GIXD-541-MONOMER; -. DR Proteomes; UP000002730; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002730}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ADL50279.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000002730}; KW Transferase {ECO:0000313|EMBL:ADL50279.1}. SQ SEQUENCE 609 AA; 67936 MW; 9786ED5AC44E7520 CRC64; MNLNERLLIF DGAMGTYYAS SCNNPLPKCE LANIHDKKTI LNIHKEYIKA GAGAIKTNTF GANKISLECD FDVMKEAIVS GYEIAKEATE GTDVLVFADI GPIPFLEKVD LWVGYKEIID IFLSLGASNF IFETFSSDEY LIEISEYIKE KNSKAFILTE FAVSPEGVTR LGKSGKKLLN TMLKAKTIDA CGFNCFSGPY HLLQYSKTLD IKDKTISMMP NSGYPSMINN RVFFDNTKEY FAEQMLEIAR QGVTILGGCC GTTPEYIKEM VDKLKGLEVH NILNDGRQIE TTEGLKQEKL QEKKALTEEV KDEKRVNKNP LLEKLERGEK IIAVELDPPI NTEIDFFISG AKRLKGQGID AITIADCPIA RARVDSSLLA CKLKRELDIT AIPHMTCRDR NINATKALLL GLNVEGINNV LVVTGDPIPS ADREEIKGVF SFNSSILSSY IRELNETTFS SPFNVCGALN LNVRNFSNEL EKAQKKIDNG ITMFLTQPVL TEEAMENLKL ARKKLNAKIL GGIIPVVSYR NACFMNNEIS GINVSEEIIE RYKDVSKEEA TRLAVEISTG IATEMSSYVD GFYIITPFKR IDIVSEIVSN IKNNIFTYN // ID D9SSS9_CLOC7 Unreviewed; 1220 AA. AC D9SSS9; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 29-APR-2015, entry version 35. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADL52591.1}; GN OrderedLocusNames=Clocel_2896 {ECO:0000313|EMBL:ADL52591.1}; OS Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / OS 743B). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=573061 {ECO:0000313|EMBL:ADL52591.1, ECO:0000313|Proteomes:UP000002730}; RN [1] {ECO:0000313|EMBL:ADL52591.1, ECO:0000313|Proteomes:UP000002730} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35296 / DSM 3052 / OCM 3 / 743B RC {ECO:0000313|Proteomes:UP000002730}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002160; ADL52591.1; -; Genomic_DNA. DR RefSeq; WP_010075684.1; NZ_BABR01000305.1. DR RefSeq; YP_003844355.1; NC_014393.1. DR EnsemblBacteria; ADL52591; ADL52591; Clocel_2896. DR KEGG; ccb:Clocel_2896; -. DR PATRIC; 41737468; VBICloCel81632203721_2507. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; CCEL573061:GIXD-2977-MONOMER; -. DR Proteomes; UP000002730; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002730}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002730}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 242 242 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 754 754 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1220 AA; 136606 MW; E634633B232F4012 CRC64; MKYSIEKYLQ EKILVLDGAM GTAIQGFGLV EEDFSCGCGC NHKQKGNNDI LNITNPDIVK KVHQMYLDAE ADIIETNTFN ANRISQGDYG LEDKIYELNF KGAQIAKAIA EEYTKENPDK PRFVAGSMGP TNRAASMSPD IENPGARNIT FDKLVEAYKE QAEGLIDGGC DLLLIETIID ALNARAAIFA VNTVLEEKNL KLPIMISGTI IDKSGRLLSG QTLKAFYETV RNENLLSIGL NCAFGAEDMI PFIREAAKTQ NKYISFYPNA GLPNALGQYD ELPEKTASFI EILAKEGCLN IVGGCCGTTP AHIAAIAKTV ANYKPRIVPE IERETIYCGL EEVKVNSQSN FVNIGERTNV AGSAKFARLI REKQYEEAID IAKNQVENGA QIIDINFDDG LLDAKEEMDK FLKLVASEPE IAKVPVMIDS SKWEVLETGL KAIQGKAIVN SISLKNGEEE FIKEATYINK FNAGVVVMAF DEKGQADTYE RKIEICKRAY DILVNKVNFP PENIIFDPNI LAIATGIEEH DNYGVDYINA VRWIKENLPY AKVSGGVSNL SFSFRGNNPI REAIHSVFLY HAIKAGMDMG IVNPGMIQIY DEIDKELLER VEDVVLNKRN DAAERLLEFA QSYNNSETSS SENKLKWREN PVEERLKYSL VKGITEYLEE DLEEVRKNYD KSLQVIEGPL MAGMSAVGEL FGEGKMFLPQ VVKTARVMKK AVSILLPYIE AEKEAGENSK AGTVVFATVK GDVHDIGKNI VGIVLGCNNF EVIDLGVMVP CETILQVAKE KKADIIALSG LITPSLEEMC NVAREMEAQG FDIPLMIGGA TTSRTHTAVK IEKEYSKGVV YTSDASKAVE AAKKLVDKEK KQVYLDEIKA EYNEIRRKYE EGEKKLLTLD ESRERTLKID WSKAEIVKPS FLGTKVLKNY SLSDIRKYID WTFFFLAWDM KMTYPAIMEH PKYKDEAKKL FDDANAILDV IEKEKLFTAN GVLGFFEANS VGEDIEVYTS DKRERVTIFN MLRDQELRPD NIARNLSDYI APKESNIKDY IGGFIVTAGI GAEEYSLKFK GMGDDYSAIM VKVLADRLAE AFAELLHIEV RKNYWGYAKD EELTMKEILK GEYQGIRPAF GYPCLRDHSE KTKLFDLLEG EKNTGVSLTE DGYMMTPGAS VCGLYFANKE AKYFDVNKIS KDQVEDYTAR SGKKIEETER LFNNIIVYKK // ID D9TAE2_MICAI Unreviewed; 1171 AA. AC D9TAE2; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 29-APR-2015, entry version 35. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADL46455.1}; GN OrderedLocusNames=Micau_2921 {ECO:0000313|EMBL:ADL46455.1}; 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 {ECO:0000313|EMBL:ADL46455.1, ECO:0000313|Proteomes:UP000001908}; RN [1] {ECO:0000313|EMBL:ADL46455.1, ECO:0000313|Proteomes:UP000001908} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27029 / DSM 43813 / JCM 10878 / NBRC 16125 / INA 9442 RC {ECO:0000313|Proteomes:UP000001908}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002162; ADL46455.1; -; Genomic_DNA. DR RefSeq; WP_013286082.1; NC_014391.1. DR RefSeq; YP_003836031.1; NC_014391.1. DR EnsemblBacteria; ADL46455; ADL46455; Micau_2921. DR KEGG; mau:Micau_2921; -. DR PATRIC; 42391551; VBIMicAur74833_2927. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; MAUR644283:GHOD-2953-MONOMER; -. DR Proteomes; UP000001908; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001908}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001908}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 223 223 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 734 734 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1171 AA; 127293 MW; A57FA87652A8A3AD CRC64; MPISLRDLLA DRILIADGAM GTMLQAADLT LDDFDGLEGC NEILNVTRPD VVRGVHDAYL AAGADCVETN TFGANLPNLA EYGIPGRIRE LSEAGARIAR EAADAYATEE HPRFVLGSMG PGTKLPTLGH ASYASLRDAY QENAAGLIAG GADALIIETC QDLLQVKAAV VGSKRARAEA GRDVPIICQV AVETTGTMLL GSEIGAALTA IEPLGVDLIG LNCSTGPAEM GEHLRYLAQH SRIPISVMPN AGLPVLTADG AYFPLSPDEL ADALEQFVTD YGVALIGGCC GTTPEHIRVL VERLGGRAPV AREPKPEAGV SSIYHHVPFV QDASILMVGE RTNANGSKAF RESMLAGDWQ ACVEVARSQA RDGSHLLDLC VDYVGRDGTQ DMRELAGRFA TASTLPIVLD STEPAVIEAG LEMLGGRCVV NSVNFEDGDG PDSRYARIMP VVREHGAAVV ALLIDEEGQA RTREWKVRVA CRLIDDLTGR WGMRREDILI DALTFPIATG QEETRRDGIE TIEAIREIAA RYPGVNFTAG ISNVSFGLNP AARQVLNSVF LHECAQAGLT SAIVHASKIL PMARIPDEQR EVALDLVYDR RREGYDPVQR FIEAFEGVDA ASARATRAEE LAALPLDERL KRRIIDGERN GLEADLDTAM AQGRTPLSII NDLLLDGMKV VGELFGSGQM QLPFVLQSAE VMKTAVAYLE PHMEKTDDDG KGRIVLATVK GDVHDIGKNL VDIILSNNGY DVVNIGIKQP INAILDAAEE HRADAIGMSG LLVKSTVIMK ENLAEMASRG VAERWPVLLG GAALTRAYVE DDLRSIYPGQ VHYARDAFEG LSLMDRVMAA KRGGAPMVDP EREAALAARR ERRERQRAQV REALPELDDA SVRSDVAVDV TVPKPPFFGT RVVKGVPLAD YAALLDERAT FLGQWGLRGA RGGKGPSYEE LVETEGRPRL RYWLDRLISD QVLEAAVVYG YFPAYSEGND LVVLDENGHS ERARFSFPRQ RQERRLCLAD FFRPKGDQLD VVALQLVTVG QPISEYTAKM FAGNEYRDYL EVHGLSVQLT EALAEYWHRR IRAELVLPGG GTVADEDPAD LAGLLRTDYR GCRYAFGYPA CPDLEDRAKI VELLGAERIG VQLSEEFQLV PEQATDAIVV HHPEANYFNA K // ID D9TI04_CALOO Unreviewed; 413 AA. AC D9TI04; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADL41636.1}; GN OrderedLocusNames=COB47_0289 {ECO:0000313|EMBL:ADL41636.1}; 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 {ECO:0000313|EMBL:ADL41636.1, ECO:0000313|Proteomes:UP000000347}; RN [1] {ECO:0000313|EMBL:ADL41636.1, ECO:0000313|Proteomes:UP000000347} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-2073 / strain OB47 RC {ECO:0000313|Proteomes:UP000000347}; 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 ----------------------------------------------------------------------- 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; ADL41636.1; -; Genomic_DNA. DR RefSeq; WP_013289642.1; NC_014392.1. DR RefSeq; YP_003839622.1; NC_014392.1. DR EnsemblBacteria; ADL41636; ADL41636; COB47_0289. DR KEGG; cob:COB47_0289; -. DR PATRIC; 42227670; VBICalObs143161_0315. DR HOGENOM; HOG000269747; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR BioCyc; COBS608506:GH1S-290-MONOMER; -. DR Proteomes; UP000000347; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000347}; KW Methyltransferase {ECO:0000313|EMBL:ADL41636.1}; KW Transferase {ECO:0000313|EMBL:ADL41636.1}. SQ SEQUENCE 413 AA; 45955 MW; F435AA3E6413D42D CRC64; MALLKDELYR RVLIFDGAMG TQLIQNGLKE DECPDLWSVT RQDVVSSIHR QYFEAGSDCV ETNTFGANRE KLKKYGLENE VENINKWAVC LAKEVAKEYG GYVGLSVGPT GRLFVPSGDL SFDEAERIFY EQILSGIQAG ADFVSIETMS DIKEAKAAFF AYKKVKEVLK KDIPCLVSFT FEQNKRLLMG TPPEVAAYYF SLIGCDIVGA NCSGGAIQLL EVIKQMQGFS SVPLSVKPNA GLPKVVDGKT VYESCIPEFV NLADEFIENG VRLYGGCCGT NPEYISAISK VLKGKEVSFE SGIQKKFITS IYSLLDISQK FSFYEFKLTN DFSSEAVFEL AGLEEDAIFV DIDENVEPEV LKEFLIESQD FSKKPYVFDI KTKSHADVIE RYYFGVYGTV SSIHGKSAVK VQI // ID D9TI05_CALOO Unreviewed; 605 AA. AC D9TI05; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 27. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=COB47_0290 {ECO:0000313|EMBL:ADL41637.1}; 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 {ECO:0000313|EMBL:ADL41637.1, ECO:0000313|Proteomes:UP000000347}; RN [1] {ECO:0000313|EMBL:ADL41637.1, ECO:0000313|Proteomes:UP000000347} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-2073 / strain OB47 RC {ECO:0000313|Proteomes:UP000000347}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ADL41637.1; -; Genomic_DNA. DR RefSeq; WP_013289643.1; NC_014392.1. DR RefSeq; YP_003839623.1; NC_014392.1. DR ProteinModelPortal; D9TI05; -. DR EnsemblBacteria; ADL41637; ADL41637; COB47_0290. DR KEGG; cob:COB47_0290; -. DR PATRIC; 42227672; VBICalObs143161_0316. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR BioCyc; COBS608506:GH1S-291-MONOMER; -. DR Proteomes; UP000000347; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000347}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ADL41637.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:ADL41637.1}. SQ SEQUENCE 605 AA; 67246 MW; 2578207FAC2019EC CRC64; MKKSFREFLK EQSTVIFDGA MGTELLNRGF SLDFPLEWAN IANPELVKEI HTDYILAGAQ CIETNTFGAN ECKLKIFGFE NEVERINRSA VKIAKEVADD KVFVIGSVGP LGKPVGSGFE IDTRRAREVY KRQLYFLLDE GVDAIIFETA ASTHEVQIAI EALKELNDKI PYIIQFSFTK ELSTIYGEDI YMVTEFLKVT DADVVGLNCG NGPQKTLEAL KVFSQHLKGP FSVQPNAGYP QLVQGRLIYS TSAKYFASFV PEYIKLGAKV VGGCCGTTPE HIKAIKEKVK EFLPSIEVEV VERKEEQKTV LKDTPSELSQ KLGKKFIFTV EISPPKGIEL EKTKEGVKLL KDAGADTVNI ADSPMARVRI SPIALAHILK EELGMESILH FTCRDRNLIS LQSELLGAAA LGVKNVLALT GDPPSIGDHP QAKPVFDVNS EGLVLILSRL NSGTDYMGNP IGKATNFTIG VALNLNADDL EKEIEKLKHK IENGAHFIET QPIYKPETLE RFLEKVNFSL PPILGGILPL RSSRHAEFLH NEVPGITIPD KIRERMRSSK EPAKEGVEIA CEIVEKIKHM VSGIYIMPPF EKYEMAVEII KNFKH // ID D9TM15_THETC Unreviewed; 801 AA. AC D9TM15; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 01-APR-2015, entry version 26. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADL68395.1}; GN OrderedLocusNames=Tthe_0849 {ECO:0000313|EMBL:ADL68395.1}; 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 {ECO:0000313|EMBL:ADL68395.1, ECO:0000313|Proteomes:UP000001626}; RN [1] {ECO:0000313|EMBL:ADL68395.1, ECO:0000313|Proteomes:UP000001626} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 7956 / DSM 571 / NCIB 9385 / NCA 3814 RC {ECO:0000313|Proteomes:UP000001626}; 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 ----------------------------------------------------------------------- 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; ADL68395.1; -; Genomic_DNA. DR RefSeq; WP_013297364.1; NC_014410.1. DR RefSeq; YP_003851479.1; NC_014410.1. DR PRIDE; D9TM15; -. DR EnsemblBacteria; ADL68395; ADL68395; Tthe_0849. DR KEGG; ttm:Tthe_0849; -. DR PATRIC; 42451008; VBITheThe89703_0855. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR BioCyc; TTHE580327:GHGH-884-MONOMER; -. DR Proteomes; UP000001626; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001626}; KW Methyltransferase {ECO:0000313|EMBL:ADL68395.1}; KW Transferase {ECO:0000313|EMBL:ADL68395.1}. SQ SEQUENCE 801 AA; 87179 MW; D9315247FA7987EC CRC64; MDILKNLKNS VIVFDGAMGT MLQMKGLKTG ECPEYYNITH PDIVYEIHKS YIDAGADVIE TNTFGANRIK LKAYNLSGDV PLIVRSAVKI AKKAAGDKAV ALSMGPIGEL MEPFGKLTFD EAYNAFSEVA VEGEKAGADL ALIETMSDIL EAKAAILAVK ENTNLKVICT MTFQEDGRTL MGTDPVTAVV SLQGLGLDAI GVNCSTGPDM MADIVKKMSE VARIPILAQP NAGMPHLKDG KTFYNVSPEQ FVHQSKKLLE CGASIVGGCC GTTPEFIKLL KNDVYNVEHK STMRKVTAVS SNTKTVFIGE NNPICIIGER INPTGKKRLS AAIKEGKFNI LFDEASSQEN LGADMLDINI GVPGIDEEKL MPYVVSQIQN IVNLPLQIDS SNVKAIENAV RIVRGKPIIN SVSAKEKSLQ EVLPIVKKYG TNVIGLTISD EGLPRNAEER LKNAEKIVKT AFDYGIPKED IIIDCIALTV SSEQTAAIET LKAIKLVKSE LGVSTIIGLS NISYGLPERQ LINTAFLAMA ASYGLDAVIV NPNDKITMDI LNASMVLTSR DARCEKYIQT YKKDDKISNI SDATIEEKLK KDASQMLYKN ILEGKKADID RLVLEILNEG VEPLSIVDNT IIPALKDVGD KYDKGIYFLP QLLNSAEVVE SAFKVLKEKM PKGMGSKGKI ILATVEGDIH DIGKNIVKVL LENYGYEVID LGKDVKPSTI VDELKRTKAP LVGLSALMTT TLNNMEKTIK ILRKEHDVKI MVGGAVLTKD YAMKIGADYY GANAQEAVRI ADKVFSELNK E // ID D9U8K5_PLEAT Unreviewed; 209 AA. AC D9U8K5; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Betaine-homocysteine methyltransferase {ECO:0000313|EMBL:CBH29412.1}; DE Flags: Fragment; GN Name=bhmt {ECO:0000313|EMBL:CBH29412.1}; OS Plecoglossus altivelis (Ayu). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Stomiatii; Osmeriformes; OC Plecoglossus. OX NCBI_TaxID=61084 {ECO:0000313|EMBL:CBH29412.1}; RN [1] {ECO:0000313|EMBL:CBH29412.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Gill {ECO:0000313|EMBL:CBH29412.1}; RA Lu X.J., Chen J., Huang Z.A., Shi Y.H., Wang F.; RT "Proteomic analysis on the alteration of protein expression in gills RT of ayu (Plecoglossus altivelis) associated with salinity change."; RL Comp. Biochem. Physiol. Part D Genomics Proteomics 5:185-189(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; FN561754; CBH29412.1; -; mRNA. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Methyltransferase {ECO:0000313|EMBL:CBH29412.1}; KW Transferase {ECO:0000313|EMBL:CBH29412.1}. FT NON_TER 1 1 {ECO:0000313|EMBL:CBH29412.1}. FT NON_TER 209 209 {ECO:0000313|EMBL:CBH29412.1}. SQ SEQUENCE 209 AA; 22549 MW; 87232599A474156E CRC64; IGDGGFVFAL EKRGYVKAGP WTPEAAAEHP EAVRQLHKEF LRAGANVMQT FTFYASDDKL ENRGNSLSFT GAQINEAACH LAREVANEGD ALVAGGVSQT PSYLSCKSET EVKAIFQKQL DVFIKNKVDF LIAEYFEHVE EAEWAVQVLK STGKPVAANL CIGPEGDMHG VSPGDCAVRL VKAGADIVGV NCHFDPMTCV EAVKKMKEG // ID D9UDH2_STRS3 Unreviewed; 1171 AA. AC D9UDH2; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 01-APR-2015, entry version 26. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFK98837.1}; GN ORFNames=SSLG_00896 {ECO:0000313|EMBL:EFK98837.1}; OS Streptomyces sp. (strain SPB78). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=591157 {ECO:0000313|EMBL:EFK98837.1}; RN [1] {ECO:0000313|EMBL:EFK98837.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SPB78 {ECO:0000313|EMBL:EFK98837.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG657742; EFK98837.1; -; Genomic_DNA. DR RefSeq; WP_009063690.1; NZ_GG657742.1. DR EnsemblBacteria; EFK98837; EFK98837; SSLG_00896. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 237 237 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 747 747 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1171 AA; 127386 MW; 252BF498AAE50C70 CRC64; MAHPSPHAAD DATRVTALRE ALASRVVVAD GAMGTMLQAQ NPTLEDFQDL EGCNEVLNVT RPDIVRSVHE AYFDVGVDCV ETNTFGANHS AFGEYEIADR IHELSEAGAR LARETADSYT ARDGRTRWVL GSIGPGTKLP TLGHLPYGVL RDGFQQNAEG LLAGGADALI VETTQDLLQT KASVLGARRA LDALGADVPL IVSLAFETTG TMLLGSEIGA ALTALEPLGI DLIGLNCSTG PAEMSEHLRY LAKHSRIPLT CMPNAGLPVL TKDGAHFPLT APEMADWQES FVNDYRLSLV GGCCGSTPEH LRQVVERVRG MAPGTREPQP EPGAASLYQT VPFRQDTSYL AIGERTNANG SKKFREAMLE ARWDDCVEMA REQIREGAHM LDLCVDYVGR DGVADMRELA GRFATASTLP LVLDSTEVDV LEAGLEMLGG RAVINSVNYE DGDGPESRFA KVTSLAREHG AALIALTIDE EGQARTVETK VAVAERLIAD LTGNWGIHES DILVDCLTFT ICTGQEESRK DGIATIEAIR ELKRRHPDVQ TTLGLSNISF GLNPAARILL NSVFLDECVK AGLDSAIVHA SKILPIARFS EEEVATALDL VYDRRAEGYD PLQKLMRLFE GATAKSLKAG KAEELAALPL DERLKRRIID GERNGLEADL DEALQTRPAL DIVNATLLDG MKVVGELFGS GQMQLPFVLQ SAEVMKTAVA HLEPHMEKSD AEGKGTIVLA TVRGDVHDIG KNLVDIILSN NGYNVVNLGI KQPVSAILEA AEEHRADVIG MSGLLVKSTV IMKENLQELN QRGMAADYPV ILGGAALTRA YVEQDLHEIY EGEVRYARDA FEGLRLMDAL IGVKRGVPGA TLPELKQRRV RPTASAVVTE LAEEEGQVRS DVATDNPVPA PPFWGSRVVK GIPLKDYASW LDEGALFKGQ WGLKQNRTGE GPGYEELAET EGRPRLRGWL DHLQTENLLE AAVVYGYFPC VSKGDDVILL GEDGSERTRF TFPRQRRGRR LCLADFFRPE ESGETDVIGL QVVTVGSRIG EATGKLFAAD AYRDYLELHG LSVQLAEALA EYWHARVRAE LGFGGEDPAD VEDMFALKYR GARFSLGYGA CPNLEDRAKI AALLEPERIG VQLSEEFQLH PEQSTDALVI HHPEAKYFNA R // ID D9UP69_STRS3 Unreviewed; 304 AA. AC D9UP69; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 01-OCT-2014, entry version 13. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:EFL04141.1}; GN ORFNames=SSLG_06199 {ECO:0000313|EMBL:EFL04141.1}; OS Streptomyces sp. (strain SPB78). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=591157 {ECO:0000313|EMBL:EFL04141.1}; RN [1] {ECO:0000313|EMBL:EFL04141.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SPB78 {ECO:0000313|EMBL:EFL04141.1}; 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 ----------------------------------------------------------------------- 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; EFL04141.1; -; Genomic_DNA. DR RefSeq; WP_009070904.1; NZ_GG657742.1. DR EnsemblBacteria; EFL04141; EFL04141; SSLG_06199. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFL04141.1}; KW Transferase {ECO:0000313|EMBL:EFL04141.1}. SQ SEQUENCE 304 AA; 31286 MW; EF53DAD94DDC75BD CRC64; MDGTGAHGTG SAGFVRALGE RAVVLDGGLS NELEAAGHGL ADALWSARLL RDEPAALTEA HRAYAEAGAE VATTASYQAS FEGFARHGID AARTRELLAL SVTAARAAGS RWVAASVGPY GAMLADGSEY RGRYGVGRAA LERFHGPRVE ALLAAGPDVL ALETVPDAEE ARALLAVVRG CGVPVWLSYS VADGRTWAGQ PLDAAFGLAA EAEEVVAVGV NCCEPLEVAD AVRRAVAVSG KPGVAYPNSG ERWDAHARGW RSDPSFVPEL AARWYAAGAR LVGGCCRVGP DGIRGVADVL RAGA // ID D9V2P5_9ACTO Unreviewed; 1201 AA. AC D9V2P5; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 01-APR-2015, entry version 26. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFL06940.1}; GN ORFNames=SSMG_02611 {ECO:0000313|EMBL:EFL06940.1}; OS Streptomyces sp. AA4. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=591158 {ECO:0000313|EMBL:EFL06940.1}; RN [1] {ECO:0000313|EMBL:EFL06940.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AA4 {ECO:0000313|EMBL:EFL06940.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG657746; EFL06940.1; -; Genomic_DNA. DR RefSeq; WP_009076432.1; NZ_GG657746.1. DR EnsemblBacteria; EFL06940; EFL06940; SSMG_02611. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 234 234 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 297 297 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 298 298 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 752 752 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1201 AA; 131253 MW; BC668AB1BEF8C7E1 CRC64; MTQNLRNLLD QRVVVLDGAW GTMLQGAGLA PEDYRADWLE GHEKDVTGDP DLLNLTRPDV VLDVHRQYLA AGADITTTNT FTATSIGQAD YGLQDRVREM NLRAAELARQ AADEFENRFV AGSIGPLNVT LSLSPRVEDP AFRAVTYEEV KASYAEQTKA LADGGVDLLL IETIFDTLNC KAAITAAREV APHLPLWISV TIVDLSGRTL SGQTVEAFWT SIAHARPLIV GVNCSLGAEE MRPHVEELAK LADTYTACHP NAGLPNAFGG YDQTPEETGG MLGEFAGAGM VNIVGGCCGT SPAHIAKIAE AVKGLPPRPV PAHEPSTRFS GLEPFKIGAD TGFVMIGERT NVTGSAKFRR LIEAGDHQAA VDVALEQVRG GANLLDVNFD ADLLESEREM TTFLNLIATE PEVARIPVMI DSSRWSVLEA GLRCVQGKGV VNSISLKEGE GPFLEQARRI HDYGAGVVVM AFDEKGQADT VERKVEICSR AYDLLTTQAG FAGEDIIFDP NVLAVATGIS EHNGYAKAFI EALPLIKERC PGAHASGGIS NLSFSFRGNN VVREAMHSAF LFHAVRAGLD MGIVNAGQLA VYEDIPKDLL ELVEDVLFDR RPDATDRLVE FAETVKGSGT KRVVDLSWRE NPVAERLSHA LVHGIVDFIE DDTEEARQQF ARPLEVIEGP LMDGMKIVGD LFGSGKMFLP QVVKSARVMK RSVAYLEPYM EAEKAKMQAE GRFDTSRGNG KVVLATVKGD VHDIGKNIVG VVLGCNNYEV IDLGVMVPAA KILDTAVAEH ADVVGLSGLI TPSLDEMVSV AQEMQRRGLK LPLLIGGATT SKQHTAVKIA PAYDHTTVHV LDASRVVGVV SDLLDTDRAD ALDTANRAEQ QRLRIQHENR HSTPMLTVEQ ARANAEKVSF DEIPTPEFTG VRVVEPSIPQ LREMIDWQFL FLAWELKGKY PAILDQPVAR ELFDDANQLL DEIIENGSFS ARGAYAFWPA HSEGDDILLD GEYSDWKFPM LRQQTQKPDG RANRCLADYI APAGSGDHLG GFAVAIHGAE DLAARYEAEH DDYRAIMVKA LADRLAEAFA EYLHLEARRR WFEPDVQPDL ADLHAERFRG IRPALGYPAS PDHSEKKDLF ELLGAEELGI GLTESYAMTP AAAVSGLIFA HPESRYFTVG RLGRDQMEDY ARRRGEELSE VERWLRPNLA Y // ID D9VC32_9ACTO Unreviewed; 299 AA. AC D9VC32; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=CalE2 {ECO:0000313|EMBL:EFL07749.1}; GN ORFNames=SSMG_03420 {ECO:0000313|EMBL:EFL07749.1}; OS Streptomyces sp. AA4. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=591158 {ECO:0000313|EMBL:EFL07749.1}; RN [1] {ECO:0000313|EMBL:EFL07749.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AA4 {ECO:0000313|EMBL:EFL07749.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; EFL07749.1; -; Genomic_DNA. DR RefSeq; WP_009077881.1; NZ_GG657746.1. DR EnsemblBacteria; EFL07749; EFL07749; SSMG_03420. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 206 206 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 277 277 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 278 278 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 299 AA; 31775 MW; E57626BA4DB7F138 CRC64; MTDPILLDGG VATELQRAGL SVRDPWWATR ALLTDRNRRL LQSVHEAYLA GGARVITANT FRANLRALRK TTLDGAGQAW MVHAAVGVAG AARNAARVPD ALIAGSIGPV EDCYRPDLVP PDDELRAEHG WLALQLSRAG ADLFLIETMN TIREARIAVR EVLAVGGRAW VSFACDDDGT LLSGEPVAGA VHAVQRDGAE AVLVNCTGPE ATEVALRALC RGRYGLIGAC PNLEDRTGLA AGEHVDRALP STLEPEQFAE LLARWRAEYG LDILGGCCGT TPAHIAAARQ VLAEPQLVD // ID D9VNL9_9ACTO Unreviewed; 1170 AA. AC D9VNL9; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 01-APR-2015, entry version 26. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFL14247.1}; GN ORFNames=SSNG_01499 {ECO:0000313|EMBL:EFL14247.1}; OS Streptomyces sp. C. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=253839 {ECO:0000313|EMBL:EFL14247.1}; RN [1] {ECO:0000313|EMBL:EFL14247.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C {ECO:0000313|EMBL:EFL14247.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG657750; EFL14247.1; -; Genomic_DNA. DR RefSeq; WP_007263194.1; NZ_GG657750.1. DR EnsemblBacteria; EFL14247; EFL14247; SSNG_01499. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 237 237 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 747 747 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1170 AA; 127877 MW; B7145C06F14813BE CRC64; MASLPNPPAD TQTRADALRE ALATRVVVAD GAMGTMLQAQ DPTLEDFQQL EGCNEVLNVT RPDIVRSVHE AYFSVGVDCV ETNTFGANYA ALAEYDIPER NFELSEAGAR IARQAADAFT ASTGQQRWVL GSIGPGTKLP TLGHISYAQI RDAYQVNAEG LISGGADALL VETTQDLLQT KSSIIGARRA MEALGVTVPL ICSVTVETTG TMLLGSEIGA ALTALEPLGI DMIGLNCATG PAEMSEHLRY LARNARIPLS CMPNAGLPVL TKQGAHYPLS AAELADAQET FVREYGLSLV GGCCGTTPEH LRQVVERVRG TAVTERSPQP EPGAASLYQT VPFRQDTSYM AIGERTNANG SKKFREAMLD ARWDDCVEMA RDQIREGAHM LDLCVDYVGR DGVADMQELA GRFATASTLP IVLDSTEVPV IQAGLEKLGG RAVINSVNYE DGDGPESRFA KVTRLAQEHG AALIALTIDE EGQARTVEHK VAIAERLIED LTGNWGIRES DILIDTLTFT ICTGQEESRK DGIATIESIR ELKRRHPDVQ TTLGLSNISF GLNPAARILL NSVFLDECVK AGLDSAIVHA SKILPIARFD EEQVTTALDL IYDRREGDYD PLQKLMALFE GVNTKSMKAG KAEELLALPL EERLQRRIID GEKNGLEADL EEALQTRPAL DIVNDTLLEG MKVVGELFGS GQMQLPFVLQ SAEVMKTAVA FLEPHMEKTD ADGKGTIVLA TVRGDVHDIG KNLVDIILTN NGYNVVNIGI KQPVSAILEA AQEHKADVIG MSGLLVKSTV IMKENLEELN QRKLAADYPV ILGGAALTRA YVEQDLHEIY EGEVRYARDA FEGLRLMDAL IAVKRGVPGA TLPELKQRRV AKRDTPALQV EEPEETGGRS DVAVDNPVPT PPFWGTRVIK GIPLKDYASW LDEGALFKGQ WGLKQARAGG ATYEELVESE GRPRLRGLLE KLHTENLLEA AVVYGYFPCV SKGEDLIILD EQGNERTRFT FPRQRRGRRL CLADFFRPEE SGETDVIGLQ VVTVGSRIGE ATAKLFESDS YREYLELHGL SVQLAEALAE YWHARVRAEL GFGGEDPDKV EDMFDLKYRG ARFSLGYGAC PDLEDRAKIA DLLQPERIGV HLSEEFQLHP EQSTDALVIH HPEAKYFNAR // ID D9W2F2_9ACTO Unreviewed; 288 AA. AC D9W2F2; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 01-OCT-2014, entry version 15. DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EFL18208.1}; GN ORFNames=SSNG_05460 {ECO:0000313|EMBL:EFL18208.1}; OS Streptomyces sp. C. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=253839 {ECO:0000313|EMBL:EFL18208.1}; RN [1] {ECO:0000313|EMBL:EFL18208.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C {ECO:0000313|EMBL:EFL18208.1}; 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 ----------------------------------------------------------------------- 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; EFL18208.1; -; Genomic_DNA. DR RefSeq; WP_007267133.1; NZ_GG657750.1. DR EnsemblBacteria; EFL18208; EFL18208; SSNG_05460. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 288 AA; 29447 MW; DCEDB0034FFC7083 CRC64; MPRATGPLAD TLARRAVLLD GGLSNQLADQ GCDLSGGMWT GRVLAERPGE VQAAHTAYVR AGAEVLITAS YQVGHEPDLL ERSVRVAGAA ARAAAREVWV AASVGPYGAL LADGSEYRGR YGLTEAELVA FHRPRIGALL AAGPDLLALE TVPDVLEARA LLRVLAGTGA RAWLTYTVAG GRTRAGQPLA EAFALAAAAP EVIAVGVNCC DPAEVLPALA AAASVTAKPL VAYPNDGSVW DAATGSWNAP AAPAPWPVEA WRAAGARLVG GCCRIGPDRI AALGPRLA // ID D9W3C1_9ACTO Unreviewed; 1152 AA. AC D9W3C1; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 01-APR-2015, entry version 26. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFL18395.1}; GN ORFNames=SSNG_05647 {ECO:0000313|EMBL:EFL18395.1}; OS Streptomyces sp. C. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=253839 {ECO:0000313|EMBL:EFL18395.1}; RN [1] {ECO:0000313|EMBL:EFL18395.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C {ECO:0000313|EMBL:EFL18395.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG657750; EFL18395.1; -; Genomic_DNA. DR RefSeq; WP_007267320.1; NZ_GG657750.1. DR EnsemblBacteria; EFL18395; EFL18395; SSNG_05647. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 225 225 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 292 292 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 735 735 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1152 AA; 125787 MW; E438592C4B6E64D1 CRC64; MRRSLREELA RRVVVADGAM GTMLQAADPS LDDFLGLEGC NEVLNLTRPD VVRSVHDAYF AVGVDCVETN TFGSNLSALA EYGIEDKVYE LSETGARIAR ESADAHTARD GRPRWVLGSL GPGTKLPTLG HVGYEPLREA YQQSAEGLVR GGADALLVET TQDLLQTKAA VIGARRALDW CGMGDLPLIV QVTVEATGTM LLGSEIGAAL TALEPLGIDM IGLNCATGPA EMSEHLRYLA RNARIPLSCM PNAGLPVLTK QGAHYPLSAA ELADAQETFV REYGLSLVGG CCGTTPEHLR QVVERVRGAA VTERSPQPEP GAASLYQTVP FRQDTSYMAI GERTNANGSK KFREAMLDAR WDDCVEMARD QIREGAHMLD LCVDYVGRDG VADMQELAGR FATASTLPIV LDSTEVPVIR AGLEKLGGRA VINSVNYEDG DGPESRFAKV TRLAQEHGAA LIALTIDEEG QARTVEHKVA IAERLIEDLT GNWGIRESDI LIDTLTFTIC TGQEESRKDG IATIESIREL KRRHPDVQTT LGLSNISFGL NPAARILLNS VFLDECVKAG LDSAIVHASK ILPIARFDEE QVTTALDLIY DRREGDYDPL QKLMALFEGV NTKSMKAGKA EELLALPLEE RLQRRIIDGE KNGLEADLEE ALQTRPALDI VNDTLLEGMK VVGELFGSGQ MQLPFVLQSA EVMKTAVAFL EPHMEKTDAD GKGTIVLATV RGDVHDIGKN LVDIILTNNG YNVVNIGIKQ PVSAILEAAQ EHKADVIGMS GLLVKSTVIM KENLEELNQR KLAADYPVIL GGAALTRAYV EQDLHEIYEG EVRYARDAFE GLRLMDALIA VKRGVPGAQL PPLKQRRVPQ RAAVLDVHEP EESGGRSDVA VDNLVPEPPF LGTRVVKGIP LKEYAGWLDE QALFKGQWGL KGAATVETEG RPRLRGWLDR LHTERLLEAA VVYGYFPCVS KGDDLIVLDE DGGERTRFTF PRQGRGRRLC LSDFVRPDDS GEVDVIGFQV VTVGSRIGEA TARLFESDSY REYLELHGLS VQLAEALAEY WHARVRTELG IAGSDPAAMD GMFRTEYQGC RYSLGYPACP ELADRAKIAD LLRPERIGVH LSEEFQLHPE QSTDAIVIHH PEAGYFNAGG RR // ID D9W8H4_9ACTO Unreviewed; 306 AA. AC D9W8H4; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFL22681.1}; GN ORFNames=SSOG_02395 {ECO:0000313|EMBL:EFL22681.1}; OS Streptomyces himastatinicus ATCC 53653. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=457427 {ECO:0000313|EMBL:EFL22681.1}; RN [1] {ECO:0000313|EMBL:EFL22681.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 53653 {ECO:0000313|EMBL:EFL22681.1}; 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 ----------------------------------------------------------------------- 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; EFL22681.1; -; Genomic_DNA. DR RefSeq; WP_009714502.1; NZ_GG657754.1. DR EnsemblBacteria; EFL22681; EFL22681; SSOG_02395. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFL22681.1}; KW Transferase {ECO:0000313|EMBL:EFL22681.1}. SQ SEQUENCE 306 AA; 31855 MW; 87FA2E2EA0EC9D68 CRC64; MMSVPPTPLA TALEGGPLVL DGGLSNQLEA QGCDLSDELW SARLLADDPG QIEAAHAAYV RAGARVLITS SYQATYEGFA HRGVAREDAT ALLGRSVELA RGAARGAAAP AAPVWVAASV GPYGAMLADG SEYRGRYGLS VAELERFHRP RIEALVAAGP DVLALETVPD ADEAAAMLRA VEGSGVPVWL SYSIAGEATR AGQPLREAFA VAAGNEQVIA VGINCCEPGD ADRAVEIAAE TTGKPVVVYP NSGEEWDATA RSWRGRSTFD PARVKGWRDA GARLIGGCCR VGPDRIAELA GVVRNH // ID D9WF66_9ACTO Unreviewed; 1168 AA. AC D9WF66; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFL27376.1}; GN ORFNames=SSOG_07090 {ECO:0000313|EMBL:EFL27376.1}; OS Streptomyces himastatinicus ATCC 53653. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=457427 {ECO:0000313|EMBL:EFL27376.1}; RN [1] {ECO:0000313|EMBL:EFL27376.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 53653 {ECO:0000313|EMBL:EFL27376.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG657754; EFL27376.1; -; Genomic_DNA. DR RefSeq; WP_009719175.1; NZ_GG657754.1. DR EnsemblBacteria; EFL27376; EFL27376; SSOG_07090. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 236 236 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 302 302 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 746 746 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1168 AA; 127300 MW; 524E6E4F58D40206 CRC64; MASHTSSSAS AARIDALREA LASRVVVADG AMGTMLQAQD PSLDDFQQLE GCNEILNITR PDIVRSVHEA YFAVGVDCVE TNTFGANHAA LGEYDIPERV FELSEAGVRI AREVADEFTA STGQQRWVLG SMGPGTKLPT LGHAPYTTLR DAYQQNAEGM IAGGADALLV ETTQDLLQTK ASILGARRAL DATGANLPII CSVTVETTGT MLLGSEIGAA LTALEPLGID MIGLNCATGP AEMSEHLRYL ARHSRVPLSC MPNAGLPVLG KDGAHYPLTA TELADAQETF VREYGMSLVG GCCGTTPEHL RQVVERVRDL TPAVREPRPE PGAASLYQTV PFRQDTSYLA IGERTNANGS KKFREAMLDG RWDDCVELAR EQIREGAHLL DLCVDYVGRD GVADMRELAG RFATASTLPI VLDSTEVDVI EAGLEKLGGR AVINSVNYED GDGPESRFAK VTQLAREHGA ALIALTIDEE GQARTPEKKV EIAQRIIADL TGNWGIHESD ILIDTLTFTI CTGQEESRKD GIATIEAIRE LKRRHPDVQT TLGLSNISFG LNPAARILLN SVFLDECVKA GLDSAIVHAS KILPIARFDD EQVTTALDLI YDRRAEGYDP LQKLMALFEG ATAKSLKAGK AEELAALPLD ERLQRRIIDG ERNGLEADLD EALQERPALE IVNETLLAGM KVVGELFGSG QMQLPFVLQS AEVMKTAVAH LEPHMEKSDD EGKGTIVLAT VRGDVHDIGK NLVDIILSNN GYNVVNLGIK QPVSAILDAA QEHRADVIGM SGLLVKSTVI MKENLEELNQ RSLASDYPVI LGGAALTRAY VEQDLHEIYE GEVRYARDAF EGLRLMDALI AVKRGVPGAE LPALKQRRVP KRDTPLSDPE PEGPSRSDVA TDNPVPAPPF WGTRVVKGIQ QVDYASWLDE GALFKGQWGL KEARTGDGPS YAELVESEGR PRLRGWLDKL RTENLLEAAV VYGYFPCVSK GDDLVLLNED GSERTRFTFP RQRRGRRLCL ADFFRPEESG ETDVVGLQVV TVGSRIGEAT AELFADNSYR DYLELHGLSV QLAEALAEYW HARVRAELGY AGEDPGDIED MFALKYRGAR FSLGYGACPD LEDRAKIAEL LEPERIGVKL SEEFQLHPEQ STDAIVIHHP EAKYFNAR // ID D9WYC6_STRVR Unreviewed; 1171 AA. AC D9WYC6; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFL31020.1}; GN ORFNames=SSQG_01538 {ECO:0000313|EMBL:EFL31020.1}; OS Streptomyces viridochromogenes DSM 40736. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=591159 {ECO:0000313|EMBL:EFL31020.1}; RN [1] {ECO:0000313|EMBL:EFL31020.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 40736 {ECO:0000313|EMBL:EFL31020.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG657757; EFL31020.1; -; Genomic_DNA. DR RefSeq; WP_003989133.1; NZ_GG657757.1. DR EnsemblBacteria; EFL31020; EFL31020; SSQG_01538. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 238 238 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 748 748 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1171 AA; 127903 MW; 62BA5B8AF8F7A31E CRC64; MASLPPTPSA DSRTRVSALR EALAARVVVA DGAMGTMLQA QDPTLEDFQN LEGCNEILNL TRPDIVRSVH DAYFAVGVDC VETNTFGANH TAAAEYEIAD RVHELSEAGA RIAREVADEY AAGDGRPRWV LGSVGPGTKL PTLGHVTYST IRDGYQANAE GLLAGGADAL LVETTQDLLQ TKASVLGARR AMEATGVEVP LLCSMAFETT GTMLLGSEIG AALTALEPLG IDMIGLNCST GPAEMSEHLR YLTRHSRIPL LCMPNAGLPI LTKDGAHFPL DAEGLADAQQ TFVQDYGLSL VGGCCGTTPE HLRQLVERVR GVTPSERSPE PEPGAASLYQ SVPFRQDTSY LAIGERTNAN GSKKFREAML DARWDDCVEL AREQIREGAH MLDLCVDYVG RDGVADMEEL AGRFATASTL PIVLDSTEVD VIQAGLEKLG GRAVINSVNY EDGDGPESRF AKVTALAKEH GAALIALTID EEGQARTAEK KVEIAERLID DLTGNWGIHE EDILVDCLTF TICTGQEESR KDGIATIEGI RELKRRHPKV QTTLGLSNIS FGLNPAARIL LNSVFLDECV KAGLDSAIVH ASKILPIARF SEEEVQTALD LIYDRRAEGY DPLQKLMQLF EGATAKSLKA GKAEELAALP LEERLKRRII DGEKNGLEAD LDEALQERPA LDIVNETLLE GMKVVGELFG SGQMQLPFVL QSAEVMKTAV AHLEPHMEKS DEAGKGTIVL ATVRGDVHDI GKNLVDIILS NNGYNVVNLG IKQPVSAILE AAEEHRADVI GMSGLLVKST VIMKENLEEL NQRGLAANFP VILGGAALTR AYVEQDLHEI YQGEVRYARD AFEGLRLMDA LIGVKRGVPG AKLPELKQRR VRATAPAAVQ ERPEEGHVRS DVATDNPVPE PPFSGTRVIK GIQLKEYASW LDEGALFKGQ WGLKQSRTGE GPSYEELVES EGRPRLRGLL DRLQTENLLE AAVVYGYFPC VSKDDDLIIL DEQGNERTRF TFPRQRRGRR LCLADFFRPE ESGERDVVGL QVVTVGSRIG EETARMFEAN AYRDYLELHG LSVQLAEALA EYWHARVRSE LGYAGEDPDE MQGMFELKYR GARFSLGYGA CPNLEDRAKI ADLLQPERIG VHLSEEFQLH PEQSTDAIVI HHPEAKYFNA R // ID D9X2P8_STRVR Unreviewed; 303 AA. AC D9X2P8; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:EFL35735.1}; GN ORFNames=SSQG_06253 {ECO:0000313|EMBL:EFL35735.1}; OS Streptomyces viridochromogenes DSM 40736. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=591159 {ECO:0000313|EMBL:EFL35735.1}; RN [1] {ECO:0000313|EMBL:EFL35735.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 40736 {ECO:0000313|EMBL:EFL35735.1}; 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; EFL35735.1; -; Genomic_DNA. DR RefSeq; WP_003993870.1; NZ_GG657757.1. DR EnsemblBacteria; EFL35735; EFL35735; SSQG_06253. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFL35735.1}; KW Transferase {ECO:0000313|EMBL:EFL35735.1}. SQ SEQUENCE 303 AA; 31286 MW; F027B4D3A568C3E8 CRC64; MTSTITLAEA LAAGTVVLDG GMSNQLESAG HDLSDELWSA RLLAEQPEAV TEAHLAYFRA GADVAITASY QATFEGFGKR GINPGRAAEL MALSVESARE AAGQAGVSRP LWVAASVGPY GAMLADGSEY RGRYGLTVDE LERFHRPRME ALAAARPDVL ALETVPDAEE AAALLRAVRG LGVPAWLTYS IAGGSTRAGQ PLEEAFALAA DVDEVIAVGV NCCAPEDVDG AAATAARVTG KPVVIYPNSG ETWNAEARAW TGRSTFTPDQ VKGWQQAGAR LIGGCCRVGP EAISGIAGTL GAA // ID D9XT49_9ACTO Unreviewed; 1170 AA. AC D9XT49; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFL42248.1}; GN ORFNames=SSRG_05052 {ECO:0000313|EMBL:EFL42248.1}; OS Streptomyces griseoflavus Tu4000. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=467200 {ECO:0000313|EMBL:EFL42248.1}; RN [1] {ECO:0000313|EMBL:EFL42248.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tu4000 {ECO:0000313|EMBL:EFL42248.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG657758; EFL42248.1; -; Genomic_DNA. DR RefSeq; WP_004933410.1; NZ_GG657758.1. DR EnsemblBacteria; EFL42248; EFL42248; SSRG_05052. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 238 238 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 748 748 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1170 AA; 127960 MW; 39C6B583C4554AB9 CRC64; MASLPLTPSA DSRTRVSALR EALASRVVVA DGAMGTMLQA HDPTLADFEN LEGCNEILNL TRPDIVRSVH AEYFDAGVDC VETNTFGANL TALGEYDIAE RVVELSEAGA RIARETADEY AARDGRARWV LGSMGPGTKL PTLGHTTFGA IRDAYRQNAE GLLAGGADAL LVETTQDLLQ TKASVVAARR AMETAGFEVP LIVSVTVETT GTMLLGSEIG AALTALEPLG IDMIGLNCAT GPAEMSEHLR HLARHSRVQL SCMPNAGLPE LTKDGARYPL SPGELADAQE NFVRDYGLSL VGGCCGTTPE HLRQLVERVR GLAPVERDPR PEPGAASLYQ SVPFRQDTAY LAIGERTNAN GSKKFREAML EGRWDNCVEL AREQIREGAH MLDLCVDYVG RDGVADMEEL AGRFATASTL PIVLDSTEVD VIRAGLEKLG GRAVINSVNY EDGDGPESRF ARVTRLAQEH GAALIALTID EEGQARTAEK KVEIAERLID DLTGNWGIRE EDILVDCLTF TICTGQEESR KDGVATIEGI RELKRRHPKV QTTLGLSNIS FGLNPAARIL LNSVFLDECV KAGLDSAIVH ASKILPIARF SEEEVRTALD LIHDRRSEGY DPLQKLMALF EGATAKSLKA GKAEELAALP LEERLKRRII DGERNGLEAD LDEALQTRKA LAIVNDTLLD GMKVVGELFG SGQMQLPFVL QSAEVMKTAV AHLEPHMEKT DEAGKGTIVL ATVRGDVHDI GKNLVDIILS NNGYNVVNLG IKQPVSAILE AADEHRADVI GMSGLLVKST VIMKENLEEL NQRGLAADYP VILGGAALTR AYVEQDLHEI YQGEVRYARD AFEGLRLMDA LIGIKRGVPG AQLPELRQRR VRAAAVEIEE RPEEGHVRSD VATDNPVPTP PFRGTRVVKG IQLKEYASWL DEGALFKGQW GLKQARSGDG PSYEELAETE GRPRLRGLLD RLQTENLLEA AVVYGYFPCV SKDDDLIVLD ERGNERTRFT FPRQRRGRRL CLADFFRPEE SGETDVVGFQ VVTVGSRIGE ETARMFEANA YRDYLELHGL SVQLAEALAE YWHARVRAEL GFGGEDPAAM EDMFALKYRG ARFSLGYGAC PDLEDRAKIA DLLEPERIGV QLSEEFQLHP EQSTDAIVIH HPEAKYFNAR // ID D9XU74_9ACTO Unreviewed; 312 AA. AC D9XU74; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFL38273.1}; GN ORFNames=SSRG_01077 {ECO:0000313|EMBL:EFL38273.1}; OS Streptomyces griseoflavus Tu4000. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=467200 {ECO:0000313|EMBL:EFL38273.1}; RN [1] {ECO:0000313|EMBL:EFL38273.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tu4000 {ECO:0000313|EMBL:EFL38273.1}; 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 ----------------------------------------------------------------------- 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; EFL38273.1; -; Genomic_DNA. DR RefSeq; WP_004923345.1; NZ_GG657758.1. DR EnsemblBacteria; EFL38273; EFL38273; SSRG_01077. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFL38273.1}; KW Transferase {ECO:0000313|EMBL:EFL38273.1}. SQ SEQUENCE 312 AA; 32512 MW; DA312C043A721A37 CRC64; MTSASVTGMR TTPALADALA DGRVLVLDGG MSNQLAAAGH DLSDELWSAR LLAEDPEAVT AAHLAYFEAG ADVAITASYQ ATFEGFARRG IGREEAGRLL ALSVECARTA ARRARVSRPL WVAASVGPYG AMLADGSEYR GRYGLNVAEL ERFHRPRMEV LAAAGPDVLA LETIPDADEA EALLRALRGL GVPAWLSYSV SGDRTRAGQP LEEALALAAR ADEVIAVGVN CCTPDDADHA IALAARVTGK PVVVYPNSGE TWDAGARAWT GRATFSAGQV KGWRESGARL IGGCCRVGPG TIASVASVLR AP // ID E0DEX4_9CORY Unreviewed; 1189 AA. AC E0DEX4; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFM48794.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFM48794.1}; GN Name=metH {ECO:0000313|EMBL:EFM48794.1}; GN ORFNames=HMPREF0299_6410 {ECO:0000313|EMBL:EFM48794.1}; OS Corynebacterium matruchotii ATCC 14266. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=553207 {ECO:0000313|EMBL:EFM48794.1}; RN [1] {ECO:0000313|EMBL:EFM48794.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 14266 {ECO:0000313|EMBL:EFM48794.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFM48794.1}. 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; ACSH02000005; EFM48794.1; -; Genomic_DNA. DR RefSeq; WP_005526060.1; NZ_ACSH02000005.1. DR EnsemblBacteria; EFM48794; EFM48794; HMPREF0299_6410. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFM48794.1}; KW Transferase {ECO:0000313|EMBL:EFM48794.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 233 233 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 745 745 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1189 AA; 129898 MW; D02E913ECC9D716B CRC64; MSTVLPVKTP DFLDALHSRV LIGDGAMGTQ LQGFDLDVET DFLGLEGCNE ILNDTRPDVV AQIHRAYFTA GADLVETNTF GCNLPNLADY NIADRCQELA YKGTRIARTV ADELGPGRDG MRRFVLGSMG PGTKLPSLGH APYLDLKTYY REAALGMVDG GADGILIETA QDLLQVKAAI HGCQEAFAEV GYRLPIVCHV TVETTGTMLL GSEIGAALTA LEPLGIDMIG LNCATGPDEM SEHLRYLSRN ARIPVSVMPN AGLPILGKNG AEYPLKPAEL AASLKTFIEE YGLAMVGGCC GTTPEHITAV HTMVTGGITP AERTTPDSDA VSSLYTSVNL TQDAGVTIIG ERTNANGSKA FREAMLAGDL ETCVDIAKQQ TRDGAHMLDL CVDYVGRDGR DDMAALASLL ATSSTLPIMI DSTEPNVIQT GLEHLGGRCA VNSVNFEDGD GPGSRYQRIM QLVKTHGAAV VALTIDEEGQ ARTAEKKLAI AERLITDITE NWGLDESDII VDTLTFPIST GQEETRRDGI ETINAIRELK ARHPRVHTTL GLSNISFGLN PAARQVLNSV FLNECVAAGL DSAIAHSSKL VPMNRIEDRQ REVALDMIYD RRRDGYDPLQ TFMDLFEGVS AAEAKDARAE ALAALPLFER LSQRIIDGEK TGIETDLDAA MAEKSPINII NQDLLGGMKT VGELFGSGQM QLPFVLQSAE TMKHAVAYLE NYMEATDDSG NKGTMVIATV KGDVHDIGKN LVDIILSNNG YNVINIGIKQ PIATIISAAR EHNADVVGMS GLLVKSTVVM KENLEEMNAQ NASDIPVILG GAALTRSYVE HDLDNIYAGD VHYARDAFEG LSLMDEIMAR KRGETITEDV TKQRKKAERK ARRERSQKIA AERKAKAKPV QLPERSEVAA DFPVATPPFW GTRIIKGLSV SDYLLMLDER ALFMGQWGLK STRGDGPDYE ALVESEGRPR LRAWIDQLKS RGVLDHAAVV YGYFPAVSVK DMVLILAEPR PDAEVIRELK FPRQQRGKFL CIADYVRSRT LAEETGQVDV LPLQLVTMGD PIARYANELF AMNNYRDYLE VHGIGVQLTE ALAEYWHSRI RAELRLPDGT HVGDSDAHDT RRFFDLDYSG ARYSFGYGSC PNLTDRQAIV DLLHSERIGV TLSEEYQLHP EQSTDAFVLY HPEAKYFNV // ID E0DM73_9RHIZ Unreviewed; 1261 AA. AC E0DM73; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFM57018.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFM57018.1}; GN Name=metH {ECO:0000313|EMBL:EFM57018.1}; GN ORFNames=BIBO1_1127 {ECO:0000313|EMBL:EFM57018.1}; OS Brucella inopinata BO1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=470735 {ECO:0000313|EMBL:EFM57018.1}; RN [1] {ECO:0000313|EMBL:EFM57018.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BO1 {ECO:0000313|EMBL:EFM57018.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFM57018.1}. 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; ADEZ01000012; EFM57018.1; -; Genomic_DNA. DR RefSeq; WP_008506712.1; NZ_ADEZ01000012.1. DR EnsemblBacteria; EFM57018; EFM57018; BIBO1_1127. DR PATRIC; 41366261; VBIBruSp109945_1201. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFM57018.1}; KW Transferase {ECO:0000313|EMBL:EFM57018.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 263 263 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 326 326 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 327 327 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 783 783 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1261 AA; 138564 MW; 5F802C60A5444BD6 CRC64; MASSLDDLFG ATAAKPDGSE VLAALTQAAR ERILILDGAM GTQIQGLGFH EEHFRGDRFA TCDCQLQGNN DLLTLTQPKA IEEIHYAYAM AGADILETNT FSSTSIAQAD YGMEAMVYDL NRDGARLARR AALRAEQKDG RRRFVAGALG PTNRTASLSP DVNNPGFRAV TFDDLRIAYS EQIRGLIDGG SDIILIETIF DTLNAKAAVF ATEEVFAEKG GRLPVMISGT ITDLSGRTLS GQTPTAFWYS LRHARPFTIG LNCALGANAM RAHLDELSSI ADTFICAYPN AGLPNEFGQY DETPEAMAAQ IEGFARDGLV NVVGGCCGST PDHIRAIAQA VAKYEPRKPA KVPPLMRLSG LEPFTLTKDI PFVNIGERTN VTGSARFRKL VKAGDFAAAL DVARDQVANG AQIIDINMDE GLIDSEKAMV EFLNLIAAEP DIARVPIMLD SSKWEVIEAG LKCVQGKAVV NSISLKEGEE AFLHHARLVR AYGAAVVIMA FDETGQADTQ ARKIEICTRA YKILTEQVGF PPEDIIFDPN IFAVATGIEE HNNYGVDFIE ATREIVRTLP HVHISGGVSN LSFSFRGNEP VREAMHAVFL YHAIQAGMDM GIVNAGQLAV YDTIDAELRE ACEDVVLNRP TKTGESATER LLEIAERFRD SGSREARTQD LSWREWPVEK RLEHALVNGI TEYIEADTEE ARLAAERPLH VIEGPLMAGM NVVGDLFGSG KMFLPQVVKS ARVMKQAVAV LLPFMEEEKR LNGGEGRQSA GKVLMATVKG DVHDIGKNIV GVVLACNNYE IIDLGVMVPS QKILQVARDE KVDIIGLSGL ITPSLDEMAH VAAEMEREGF DIPLLIGGAT TSRVHTAVKI HPRYERGQAV YVVDASRAVG VVSNLLSPEG KQAYIDGLRN EYAKVAAAHA RNEAEKQRLP IARARANPHQ LDWENYEPVK PAFTGTKVFE TYDLAEIARY IDWTPFFQTW ELRGRYPAIL EDEKQGEAAR QLWADAQAML QKIIDEKWFT PRAVVGFWPA NAVGDDIRLF TDESRKEELA TLFTLRQQLT KRDGRPNVAM ADFVAPVESG KQDYVGGFVV TAGIGEIAIA ERFERANDDY SAILVKALAD RFAEAFAELM HERVRKEFWA YAPDEAFTPE ELISEPYKGI RPAPGYPAQP DHTEKTTLFR LLDATANTGV ELTESYAMWP GSSVSGLYIG HPESYYFGVA KVERDQVEDY ARRKGMDVEA VERWLTPILN YVPGASKDEA A // ID E0E8T4_ACTPL Unreviewed; 297 AA. AC E0E8T4; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFM85157.1}; GN ORFNames=appser1_12000 {ECO:0000313|EMBL:EFM85157.1}; OS Actinobacillus pleuropneumoniae serovar 1 str. 4074. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=228399 {ECO:0000313|EMBL:EFM85157.1}; RN [1] {ECO:0000313|EMBL:EFM85157.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=4074 {ECO:0000313|EMBL:EFM85157.1}; 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. {ECO:0000313|EMBL:EFM85157.1}. 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; ADOD01000018; EFM85157.1; -; Genomic_DNA. DR RefSeq; WP_005597940.1; NZ_ADOD01000018.1. DR ProteinModelPortal; E0E8T4; -. DR EnsemblBacteria; EFM85157; EFM85157; appser1_12000. DR PATRIC; 41510016; VBIActPle54414203709_1204. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 297 AA; 32341 MW; E74F7F51335D3F4A CRC64; MTITILDGGM SRELMRLNAP FKQPEWSALS LYEKPSAVQQ VHEDFIANGA EVITTNSYAV VPFHIGEQRF SADGKMLADL AGRLAKQAVK NSGKSAKIAG SLPPMFGSYR ADLIQADRFA EIAQPIIDGL APYVDIWLCE TQSAIIEPTS IKPLLPKDDR PLWVSFTLTD DEPTPEPQLR SGEPVALAIE KMVELGVDAI LFNCCQPEVI EQALAITQSI LKEKNVTHIQ TGAYANAFAP QPKDATANDG LDEVRKDLDP EAYLAWAQKW TAQGATIIGG CCGIGIEYIN TLAKNLK // ID E0EKT7_ACTPL Unreviewed; 297 AA. AC E0EKT7; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFM89717.1}; GN ORFNames=appser4_11160 {ECO:0000313|EMBL:EFM89717.1}; OS Actinobacillus pleuropneumoniae serovar 4 str. M62. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=754255 {ECO:0000313|EMBL:EFM89717.1}; RN [1] {ECO:0000313|EMBL:EFM89717.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M62 {ECO:0000313|EMBL:EFM89717.1}; 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. {ECO:0000313|EMBL:EFM89717.1}. 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; ADOF01000049; EFM89717.1; -; Genomic_DNA. DR RefSeq; WP_005597940.1; NZ_ADOF01000049.1. DR ProteinModelPortal; E0EKT7; -. DR EnsemblBacteria; EFM89717; EFM89717; appser4_11160. DR PATRIC; 41518794; VBIActPle152992_1110. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 297 AA; 32341 MW; E74F7F51335D3F4A CRC64; MTITILDGGM SRELMRLNAP FKQPEWSALS LYEKPSAVQQ VHEDFIANGA EVITTNSYAV VPFHIGEQRF SADGKMLADL AGRLAKQAVK NSGKSAKIAG SLPPMFGSYR ADLIQADRFA EIAQPIIDGL APYVDIWLCE TQSAIIEPTS IKPLLPKDDR PLWVSFTLTD DEPTPEPQLR SGEPVALAIE KMVELGVDAI LFNCCQPEVI EQALAITQSI LKEKNVTHIQ TGAYANAFAP QPKDATANDG LDEVRKDLDP EAYLAWAQKW TAQGATIIGG CCGIGIEYIN TLAKNLK // ID E0EYQ1_ACTPL Unreviewed; 297 AA. AC E0EYQ1; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFM93829.1}; GN ORFNames=appser9_12140 {ECO:0000313|EMBL:EFM93829.1}; OS Actinobacillus pleuropneumoniae serovar 9 str. CVJ13261. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=754258 {ECO:0000313|EMBL:EFM93829.1}; RN [1] {ECO:0000313|EMBL:EFM93829.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CVJ13261 {ECO:0000313|EMBL:EFM93829.1}; 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. {ECO:0000313|EMBL:EFM93829.1}. 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; ADOI01000037; EFM93829.1; -; Genomic_DNA. DR RefSeq; WP_005610408.1; NZ_ADOI01000037.1. DR EnsemblBacteria; EFM93829; EFM93829; appser9_12140. DR PATRIC; 41528181; VBIActPle147488_1208. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 297 AA; 32290 MW; E74F6EB61A8D233A CRC64; MTITILDGGM SRELMRLNAP FKQPEWSALS LYEKPSAVQQ VHEDFIANGA EVITTNSYAV VPFHIGEQRF SADGKMLADL AGRLAKQAVK NSGKSAKIAG SLPPMFGSYR ADLIQADRFA EIAQPIIDGL APYVDIWLCE TQSAIIEPTS IKPLLPKDDR PLWVSFTLTD DEPTPEPQLR SGEPVALAIE KMVELGVDAI LFNCCQPEVI EQALAITQSI LKEKNVTHIQ TGAYANAFAP QPKDATANDG LDEVRKDLDP EAYLAWAQKW AAQGATIVGG CCGIGIEYIN ALAKHLK // ID E0F4Q9_ACTPL Unreviewed; 297 AA. AC E0F4Q9; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFM96207.1}; GN ORFNames=appser10_11340 {ECO:0000313|EMBL:EFM96207.1}; OS Actinobacillus pleuropneumoniae serovar 10 str. D13039. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=754259 {ECO:0000313|EMBL:EFM96207.1}; RN [1] {ECO:0000313|EMBL:EFM96207.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=D13039 {ECO:0000313|EMBL:EFM96207.1}; 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. {ECO:0000313|EMBL:EFM96207.1}. 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; ADOJ01000017; EFM96207.1; -; Genomic_DNA. DR RefSeq; WP_005612495.1; NZ_ADOJ01000017.1. DR EnsemblBacteria; EFM96207; EFM96207; appser10_11340. DR PATRIC; 41532579; VBIActPle151137_1139. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 297 AA; 32365 MW; 96F124522099EA61 CRC64; MTITILDGGM SRELMRLNAP FKQPEWSALS LYEKPSAVQQ VHEDFIANGA EVITTNSYAV VPFHIGEQRF SADGKMLADL AGRLAKQAVK NSGKSAKIAG SLPPMFGSYR ADLIQADRFA EIAQPIIDGL SPYVDIWLCE TQSAIIEPTS IKPLLPKDNR PLWVSFTLTD DEPTPEPQLR SGEPVALAIE KMVELGVDAI LFNCCQPEVI EQALAITQSI LKEKNVTHIQ TGAYANAFAP QPKDATANDG LDEVRKDLDP EAYLAWAQKW TAQGATIVGG CCGIGIEYIN TLAKHLK // ID E0FB44_ACTPL Unreviewed; 297 AA. AC E0FB44; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFM98215.1}; GN ORFNames=appser11_12130 {ECO:0000313|EMBL:EFM98215.1}; OS Actinobacillus pleuropneumoniae serovar 11 str. 56153. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=754260 {ECO:0000313|EMBL:EFM98215.1}; RN [1] {ECO:0000313|EMBL:EFM98215.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=56153 {ECO:0000313|EMBL:EFM98215.1}; 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. {ECO:0000313|EMBL:EFM98215.1}. 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; ADOK01000019; EFM98215.1; -; Genomic_DNA. DR RefSeq; WP_005610408.1; NZ_ADOK01000019.1. DR EnsemblBacteria; EFM98215; EFM98215; appser11_12130. DR PATRIC; 41537244; VBIActPle158651_1213. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 297 AA; 32290 MW; E74F6EB61A8D233A CRC64; MTITILDGGM SRELMRLNAP FKQPEWSALS LYEKPSAVQQ VHEDFIANGA EVITTNSYAV VPFHIGEQRF SADGKMLADL AGRLAKQAVK NSGKSAKIAG SLPPMFGSYR ADLIQADRFA EIAQPIIDGL APYVDIWLCE TQSAIIEPTS IKPLLPKDDR PLWVSFTLTD DEPTPEPQLR SGEPVALAIE KMVELGVDAI LFNCCQPEVI EQALAITQSI LKEKNVTHIQ TGAYANAFAP QPKDATANDG LDEVRKDLDP EAYLAWAQKW AAQGATIVGG CCGIGIEYIN ALAKHLK // ID E0FH33_ACTPL Unreviewed; 297 AA. AC E0FH33; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFN00494.1}; GN ORFNames=appser12_11230 {ECO:0000313|EMBL:EFN00494.1}; OS Actinobacillus pleuropneumoniae serovar 12 str. 1096. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=754261 {ECO:0000313|EMBL:EFN00494.1}; RN [1] {ECO:0000313|EMBL:EFN00494.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=1096 {ECO:0000313|EMBL:EFN00494.1}; 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. {ECO:0000313|EMBL:EFN00494.1}. 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; ADOL01000028; EFN00494.1; -; Genomic_DNA. DR RefSeq; WP_005615431.1; NZ_ADOL01000028.1. DR EnsemblBacteria; EFN00494; EFN00494; appser12_11230. DR PATRIC; 41541625; VBIActPle154243_1127. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 297 AA; 32367 MW; D924563351031D6C CRC64; MTITILDGGM SRELMRLNAP FKQPEWSALS LYEKPSAVQQ VHEDFIANGA EVITTNSYAV VPFHIGEQRF SADSKMLADL AGRLAKQAVK NSGKSAKIAG SLPPMFGSYR ADLIQADRFA EIAQPIIDGL SPYVDIWLCE TQSAIIEPTS IKPLLPKDNR PLWVSFTLTD DEPTPEPQLR SGEPVALAIE KMVELDVDAI LFNCCQPEVI EQALAITQSI LKAKNATHIQ TGAYANAFAP QPKDATANDG LDEVRKDLDP EAYLAWAQKW TAQGATIVGG CCGIGIEYIN TLAKHLK // ID E0FN38_ACTPL Unreviewed; 297 AA. AC E0FN38; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFN02610.1}; GN ORFNames=appser13_11620 {ECO:0000313|EMBL:EFN02610.1}; OS Actinobacillus pleuropneumoniae serovar 13 str. N273. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=754262 {ECO:0000313|EMBL:EFN02610.1}; RN [1] {ECO:0000313|EMBL:EFN02610.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=N273 {ECO:0000313|EMBL:EFN02610.1}; 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. {ECO:0000313|EMBL:EFN02610.1}. 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; ADOM01000026; EFN02610.1; -; Genomic_DNA. DR RefSeq; WP_005597940.1; NZ_ADOM01000026.1. DR ProteinModelPortal; E0FN38; -. DR EnsemblBacteria; EFN02610; EFN02610; appser13_11620. DR PATRIC; 41546049; VBIActPle159548_1162. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 297 AA; 32341 MW; E74F7F51335D3F4A CRC64; MTITILDGGM SRELMRLNAP FKQPEWSALS LYEKPSAVQQ VHEDFIANGA EVITTNSYAV VPFHIGEQRF SADGKMLADL AGRLAKQAVK NSGKSAKIAG SLPPMFGSYR ADLIQADRFA EIAQPIIDGL APYVDIWLCE TQSAIIEPTS IKPLLPKDDR PLWVSFTLTD DEPTPEPQLR SGEPVALAIE KMVELGVDAI LFNCCQPEVI EQALAITQSI LKEKNVTHIQ TGAYANAFAP QPKDATANDG LDEVRKDLDP EAYLAWAQKW TAQGATIIGG CCGIGIEYIN TLAKNLK // ID E0I3T2_9BACL Unreviewed; 631 AA. AC E0I3T2; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 22. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=PaecuDRAFT_0457 {ECO:0000313|EMBL:EFM12946.1}; OS Paenibacillus curdlanolyticus YK9. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=717606 {ECO:0000313|EMBL:EFM12946.1}; RN [1] {ECO:0000313|EMBL:EFM12946.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=YK9 {ECO:0000313|EMBL:EFM12946.1}; 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., 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; EFM12946.1; -; Genomic_DNA. DR RefSeq; WP_006036474.1; NZ_AEDD01000001.1. DR ProteinModelPortal; E0I3T2; -. DR EnsemblBacteria; EFM12946; EFM12946; PaecuDRAFT_0457. DR PATRIC; 41185075; VBIPaeCur159330_0457. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EFM12946.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EFM12946.1}. SQ SEQUENCE 631 AA; 68234 MW; C9C207A5F10D70E1 CRC64; MKQDLREALQ HRILTGDGAM GTYLYQMGFP VGVSYEEFNV LRPEVIGGVH RRYYEAGARL IETNTFSANV EKLSKYGLES DVELINRAGV RLARASVGHD AYVVGAVGPI RAARRKGVRT ATVRTALSQQ IGFLLDEGVD GILLETFLDM EEMLLALRAV RQSSNVPVIC QFAVEDGGST QDGVRLFEAF SRLQGEGADV VGFNCRTGPN GIMRSIDALD GASQLPFSVF PNAGIPDYVD GQYTYSATPA YFAATARRFA DHGARVIGGC CGTTPEHIAA IAAALDGYVP ALQGATVLDK PAAPHDSGPS VSVSSAPVPP AAPPEAEEPS IVALVRQRHT VIVELDPPRD LDITKFMEGA AALKDAKADA LTMADNSLAV TRMSNIALAS LVKERAGIRP LIHVACRDRN LIGTQSHMMG LDALGIDHVL AVTGDPARFG DLPGSSSVYD LTSFEMIKMI RQLNEGMAFS GKPLKQKAKF VIGAAFNPNI KHLDKAVQRL ERKIASGADY IMTQPVYDPA LIERIAEATG HIQVPIFIGV MPLASGRNAE YLHNEVPGIQ LSDEVRQRMA GLEGEAGRAE GVQIATELID AIMPHFNGIY LMTPFMFYEM TVQLTEHIWL KSGRFTNEKR E // ID E0I542_9BACL Unreviewed; 1137 AA. AC E0I542; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFM12084.1}; GN ORFNames=PaecuDRAFT_0764 {ECO:0000313|EMBL:EFM12084.1}; OS Paenibacillus curdlanolyticus YK9. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=717606 {ECO:0000313|EMBL:EFM12084.1}; RN [1] {ECO:0000313|EMBL:EFM12084.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=YK9 {ECO:0000313|EMBL:EFM12084.1}; 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., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AEDD01000002; EFM12084.1; -; Genomic_DNA. DR RefSeq; WP_006036779.1; NZ_AEDD01000002.1. DR EnsemblBacteria; EFM12084; EFM12084; PaecuDRAFT_0764. DR PATRIC; 41185706; VBIPaeCur159330_0774. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 218 218 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 281 281 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 282 282 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 713 713 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1137 AA; 124628 MW; F633ABBEFF48E358 CRC64; MQERILIMDG AMGTMIQQAD LTAADFGGDD LDGCNEILVL TRPDVIQSIH EQYLEAGADI LETNTFGSTS VVLQEYDIPE KARELNLAAA KLAVDAAIKY STPEKPRYVA GAMGPTTKTL SVTGGVTFDE LVDSYYEQAV ALIEGKVDAL LLETSQDTLN VKAGSIGIKR AFETTGVELP IMISGTIEPM GTTLAGQTIE SFYLSLEHLK PVSIGLNCAT GPEFMRDHIR TLSEIAASAI SCYPNAGLPD ENGQYHETPD SLAAKMAGFA ESGWLNVAGG CCGTTPAHIR AMADVMARFE PRRKMGEHLP AVTGIDTVYI EDANRPIMVG ERTNISGSLK FKRLIKEGSF DEASEIARSQ VKNGAQVIDI NLQDTDVDEE YAVHQFIPQV VKKIKAPLML DSTYDHIIEL GLKYSQGKAI INSINLEDGE SKFEKIIPLI HQYGASVVCI LIDERGQAVS REAKVEVADR AYDLLVNKYG VTPDDIIFDP NMFPVGSGDP QYIGSAVETI EGIRLIKQKY PRVKTILGLS NISFGLPPAG REVLNSVYLY ECTKAGLDYA IVNSEKLERY ASISAEERKL AEDLIFNTND ETLALFVAAF REKKVVKKEK TSTLTLEERL ASYIVEGTKE GLIPDLDEAL KTYAPLAIIN GPLMAGMEEV GRLFNGNELI VAEVLQSAEV MKASVAHLEQ FMEKEESSVK GKIILATVKG DVHDIGKNLV EIILSNNGYK IINLGIKVPP EQLIEAYRKE KADAIGLSGL LVKSAQQMVV TAQDLRSAGI DAPILVGGAA LTRKFTKTRI SPEYDGLVLY AKDAMDGLDI ANKLVNPVHR ERLESEHEEL RAAGFGITET AKPMPELSRA VRSNVATDVP VQVPPDLERH VMRNIPIPHV VPYVNMQTLI GHHLGLRGNF DKLIVDGDAK AQQLKDTVDG IFQDAAANGS IKAHGMYRFF PAQSEGNDII VYDPADHTKV LKRFSFPRQN VEPFLCLADF LRSVESGEMD YVGFLVVTAG HGIRERAESY KDNGDYLLSH AIQATAIELA EGLAERVHHI MRDIWGISDP VDMTMAQRHG ARYRGIRVSF GYPACPNLED QGPLFELMKP EDIGVELTEE FMMEPEASVS AMVFSHPEAR YFNVDKA // ID E0J0I0_ECOLW Unreviewed; 1227 AA. AC E0J0I0; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 43. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:AFH13898.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AFH13898.1}; DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFN38452.1}; GN Name=metH {ECO:0000313|EMBL:AFH13898.1}; GN OrderedLocusNames=WFL_21285 {ECO:0000313|EMBL:AFH13898.1}; GN ORFNames=EschWDRAFT_2087 {ECO:0000313|EMBL:EFN38452.1}; 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 {ECO:0000313|EMBL:EFN38452.1}; RN [1] {ECO:0000313|EMBL:EFN38452.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=W {ECO:0000313|EMBL:EFN38452.1}; 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., 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] {ECO:0000313|EMBL:AFH13898.1, ECO:0000313|Proteomes:UP000010107} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 9637 / CCM 2024 / DSM 1116 / NCIMB 8666 / NRRL B-766 / W RC {ECO:0000313|Proteomes:UP000010107}, and RC W {ECO:0000313|EMBL:AFH13898.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002967; AFH13898.1; -; Genomic_DNA. DR EMBL; AEDF01000008; EFN38452.1; -; Genomic_DNA. DR RefSeq; WP_000096010.1; NZ_AEDF01000008.1. DR RefSeq; YP_006126909.1; NC_017635.1. DR RefSeq; YP_006175684.1; NC_017664.1. DR ProteinModelPortal; E0J0I0; -. DR SMR; E0J0I0; 651-1227. DR EnsemblBacteria; ADT77667; ADT77667; ECW_m4378. DR EnsemblBacteria; AFH13898; AFH13898; WFL_21285. DR EnsemblBacteria; EFN38452; EFN38452; EschWDRAFT_2087. DR KEGG; ell:WFL_21285; -. DR KEGG; elw:ECW_m4378; -. DR PATRIC; 41593151; VBIEscCol201000_2301. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR Proteomes; UP000010107; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000010107}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AFH13898.1}; KW Transferase {ECO:0000313|EMBL:AFH13898.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135969 MW; 31A0CAA1E9127CD9 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID E0M2D3_9ENTR Unreviewed; 1243 AA. AC E0M2D3; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 01-APR-2015, entry version 27. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFM18296.1}; GN ORFNames=PanABDRAFT_3551 {ECO:0000313|EMBL:EFM18296.1}; OS Pantoea sp. aB. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Pantoea. OX NCBI_TaxID=517433 {ECO:0000313|EMBL:EFM18296.1}; RN [1] {ECO:0000313|EMBL:EFM18296.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AB {ECO:0000313|EMBL:EFM18296.1}; 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., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AEDL01000012; EFM18296.1; -; Genomic_DNA. DR EnsemblBacteria; EFM18296; EFM18296; PanABDRAFT_3551. DR PATRIC; 41209921; VBIPanSp97966_3626. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 263 263 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 326 326 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 327 327 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 775 775 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1243 AA; 137383 MW; B5A5135C6EBBAD19 CRC64; MENRVFRQQT DVNGATVSNK IDALHQQLAQ RIMVLDGGMG TMIQSYRLEE EDYRGSRFAD WPCDLKGNND LLVLSKSDVI REIHDAYLAA GADILETNTF NATSIAMADY QMESLSAEIN YEAARLARAC ADAWTAKTPD RPRYVAGVLG PTNRTCSISP DVNDPAYRNV TFNQLVEAYR ESTRALVEGG SDIIMIETVF DTLNAKAAIY AVQTEMEALG VTLPLMISGT ITDASGRTLS GQTTEAFYNS LRHAEPLSFG LNCALGPDEL RQYVAELSRI AEGYVTAHPN AGLPNAFGEY DLDAELMAQQ IGEWATSGFL NIIGGCCGTT PKHIAAMVAA VDGVAPRPLP TIPVACRLSG LEPLNITAES LFVNVGERTN VTGSAKFKRL IKEEKYNEAL EVALQQVQSG AQIIDINMDE GMLDAEAAMV RFLNLIAGEP DIARVPIMID SSKWEVIEKG LQCIQGKGIV NSISMKEGEA AFIHHARQVR RYGAAMVVMA FDEVGQADTR ARKIEICRRA YQILTEQVGF PPEDIIFDPN IFAVATGIDE HNNYAMDFIG ACEDIKRELP HAMISGGVSN VSFSFRGNDP VREAIHAVFL YYAIRNGMDM GIVNAGQLAI YDDLPTELRE AVEDVILNRR DDGTERLLAL AEKYRGGKSD GAQEKQLAEW RSWDVVKRLE YSLVKGITEF IEQDTEEARQ QVPRPIEVIE GPLMSGMNVV GDLFGEGKMF LPQVVKSARV MKQAVAYLEP FIEASKEAGR SNGKIVLATV KGDVHDIGKN IVGVVLQCNN YEIVDLGVMV PGEKILKTAR EVNADIIGLS GLITPSLDEM VNMAKEMERQ GFTIPLLIGG ATTSKAHTAV KIEQHYSGPT VYVQNASRTV GVVSSLLSAT LKDDFVARTR KEYETVRIQH ARKKPRTPPV SLQTARDNAT SIDWESYSPP VPHRLGVSQV EASIATLRHY IDWTPFFMTW SLAGKYPRIL EDEVVGEEAQ RLFADANAML DRLSEQALLK PRGVVGIFPA NRVGDDIHLY SDERRDEVLC VSHHLRQQTE KTDFANYCLA DFVAPKTSGK ADYLGAFAVT GGLEEDALAE AYDRQHDDYN KIMVKALADR LAEAFAEYLH ERVRKVIWGF APNENLSNEE LIRENYQGIR PAPGYPACPE HTEKATIWRL LAVEAQTGMK LTESYAMWPG AAVSGWYFSH PDSRYFAVAQ IQRDQVEDYA ARKGMSVTEV ERWLAPNLGY DAD // ID E0M349_9ENTR Unreviewed; 311 AA. AC E0M349; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFM18270.1}; GN ORFNames=PanABDRAFT_3817 {ECO:0000313|EMBL:EFM18270.1}; OS Pantoea sp. aB. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Pantoea. OX NCBI_TaxID=517433 {ECO:0000313|EMBL:EFM18270.1}; RN [1] {ECO:0000313|EMBL:EFM18270.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AB {ECO:0000313|EMBL:EFM18270.1}; 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., 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEDL01000013; EFM18270.1; -; Genomic_DNA. DR RefSeq; WP_003850358.1; NZ_AEDL01000013.1. DR EnsemblBacteria; EFM18270; EFM18270; PanABDRAFT_3817. DR PATRIC; 41210460; VBIPanSp97966_3896. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFM18270.1}; KW Transferase {ECO:0000313|EMBL:EFM18270.1}. SQ SEQUENCE 311 AA; 33494 MW; 10B1359BBD49DB16 CRC64; MSHNPVAQAL TESPLLILDG ALATELEARG CHLADALWSA KVLMENPELI YQVHYDYFVA GARCAITASY QATPQGFATR GLDEAQSLAL IAQSVELARR ARQDYLAVRP DAKTLLVAGS VGPYGAFLAD GSEYRGDYAL PEAEMMAFHR PRVQALLAAG ADLLACETLP SFAEAQALVK LLAEFPEGRA WFTFTLRDAG HISDGTPLSE VVSWLNQQPQ VIALGINCVA LESVTPALQQ LQRLTDKPLV VYPNSGEQYD ASSKTWHSAP SGCTLHDKLD EWQQAGAKLI GGCCRTSPND IAAIARACQP Q // ID E0MLN9_9RHOB Unreviewed; 339 AA. AC E0MLN9; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 01-OCT-2014, entry version 19. DE SubName: Full=Methionine synthase I {ECO:0000313|EMBL:EFL90705.1}; GN ORFNames=R2A130_0789 {ECO:0000313|EMBL:EFL90705.1}; OS Ahrensia sp. R2A130. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Ahrensia. OX NCBI_TaxID=744979 {ECO:0000313|EMBL:EFL90705.1}; RN [1] {ECO:0000313|EMBL:EFL90705.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=R2A130 {ECO:0000313|EMBL:EFL90705.1}; 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. {ECO:0000313|EMBL:EFL90705.1}. 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; AEEB01000003; EFL90705.1; -; Genomic_DNA. DR RefSeq; WP_009757594.1; NZ_AEEB01000003.1. DR EnsemblBacteria; EFL90705; EFL90705; R2A130_0789. DR PATRIC; 41233844; VBIAhrSp149844_0931. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 339 AA; 35813 MW; 85E3F5829D9AF6E3 CRC64; MGRLRELLDE KGVLLADGAT GTNFFNMGLL SGDAPELWNE DEPEKVMSLH QGFVDAGADI ILTNTFGANR HRLKLHHAQE RSTELNEKAA KLARKVADAA GRPVLVAGSV GPTGELFEPL GELTREAAIA SFTEQMIGLR DGGADVMWIE TMSAREEIDA AADAAEALGL DFVFTASFDT AGRTMMGITP TQLMEIATTR PAGPIAIGAN CGVGATDLLF SILDMTAAPQ DKIAVVAKAN CGVPRVSGDK VIYTGTPELM ADYARYAIDA GAAIIGGCCG TSYEHLAAMR GAIDTHKKRK RPELVDVVAA TGPLVNEIST AEQKDSSEGG GRRRGGRRR // ID E0MMV3_9RHOB Unreviewed; 300 AA. AC E0MMV3; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFL89627.1}; GN ORFNames=R2A130_2237 {ECO:0000313|EMBL:EFL89627.1}; OS Ahrensia sp. R2A130. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Ahrensia. OX NCBI_TaxID=744979 {ECO:0000313|EMBL:EFL89627.1}; RN [1] {ECO:0000313|EMBL:EFL89627.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=R2A130 {ECO:0000313|EMBL:EFL89627.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFL89627.1}. 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; AEEB01000005; EFL89627.1; -; Genomic_DNA. DR RefSeq; WP_009464324.1; NZ_AEEB01000005.1. DR EnsemblBacteria; EFL89627; EFL89627; R2A130_2237. DR PATRIC; 41234865; VBIAhrSp149844_1438. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EFL89627.1}; KW Transferase {ECO:0000313|EMBL:EFL89627.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 202 202 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 274 274 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 275 275 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 300 AA; 31331 MW; 0AB8F7BA4EC7414D CRC64; MTNIVLLDGG MGQELIARSA NPPSPLWSAR VMLDEPEIVE AVHREYIEAG AKVLTLNSYS ATPERLARDA DASLFEPLQA KAIELAMAAK GDHDDVKIGG CLPPLFGSYH PENAPDEGTC LATYRQIVAQ QKDHVDVFIC ETLGGIRETR AAVRACAEAG VPVWCGMTAM DANGSLLRSG ESVEEAAHIA KEEGAAAVAI NCSWPEAVTQ AMPILVATGL PFGGWANGFT NAGADLALGG TVDGMGKRTD LDPVSYASHA MGWVEQGATI IGGCCEVGPA HIAELAKQLR AAGHTISGDL // ID E0NRY3_9BACT Unreviewed; 351 AA. AC E0NRY3; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFM02122.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFM02122.1}; GN Name=metH {ECO:0000313|EMBL:EFM02122.1}; GN ORFNames=HMPREF0658_0934 {ECO:0000313|EMBL:EFM02122.1}; OS Prevotella marshii DSM 16973 = JCM 13450. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=862515 {ECO:0000313|EMBL:EFM02122.1}; RN [1] {ECO:0000313|EMBL:EFM02122.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 16973 {ECO:0000313|EMBL:EFM02122.1}; 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. {ECO:0000313|EMBL:EFM02122.1}. 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; AEEI01000029; EFM02122.1; -; Genomic_DNA. DR RefSeq; WP_006948830.1; NZ_GL397214.1. DR EnsemblBacteria; EFM02122; EFM02122; HMPREF0658_0934. DR PATRIC; 41241063; VBIPreMar165560_0910. DR OrthoDB; EOG6091CH; -. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFM02122.1}; KW Transferase {ECO:0000313|EMBL:EFM02122.1}. SQ SEQUENCE 351 AA; 38634 MW; 68D7629ACBEB7A46 CRC64; MTIQELIRQR ILILDGAMGT MIQRYHLTED DFRGQRFKDI TSMLKGNYDV LNITHSDIVE EIHDKYLAAG ADLISTNTFN SQAVSQAGYQ LEDFAHEMAL EGARIARRAA DRYSTPTHPR FVCGSVGPTN KTCSISPNVN NPVLRKHHYD ELFKAYTEQM DALIAGGTDT FLIETIVDTL NAKAAIAAAM QSMERAGKTL PIMLSITINN LTGNMPSGQT LEAFLADVSP YPIFSIGLNC SFGAKQMKPY LKELAHKAPY YISAYPNAGI PNSMGFYNET AETMGADIQE FIDEGIVNIV GGCCGTDETF IAEYARRAKD KRPPLMPLRN DNSANAPTAM PLPIDNAMKR G // ID E0NYG7_9FIRM Unreviewed; 332 AA. AC E0NYG7; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFM23495.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EFM23495.1}; GN Name=mmuM {ECO:0000313|EMBL:EFM23495.1}; GN ORFNames=HMPREF9166_0884 {ECO:0000313|EMBL:EFM23495.1}; OS Selenomonas sp. oral taxon 149 str. 67H29BP. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Selenomonas. OX NCBI_TaxID=864563 {ECO:0000313|EMBL:EFM23495.1}; RN [1] {ECO:0000313|EMBL:EFM23495.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=67H29BP {ECO:0000313|EMBL:EFM23495.1}; 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. {ECO:0000313|EMBL:EFM23495.1}. 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; AEEJ01000033; EFM23495.1; -; Genomic_DNA. DR RefSeq; WP_009442830.1; NZ_GL397087.1. DR EnsemblBacteria; EFM23495; EFM23495; HMPREF9166_0884. DR PATRIC; 41910639; VBISelSp164981_0596. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFM23495.1}; KW Transferase {ECO:0000313|EMBL:EFM23495.1}. SQ SEQUENCE 332 AA; 35725 MW; 33DCACD1816B8779 CRC64; MNVLEARLAV QDVLVLDGAL ATELEARGFS VDDPLWSAKA LFERPNLVRE IHLDYLRAGA DVLTSASYQA TVAGFMRRGF TAEKAAELLR RSVRLAQEAR DLYRAECGGD AAVPLVAASV GPYGAYLADG SEYRGDYDVE EDTLTAFHAQ RLRILASAAP DLLACETLPC LHEACAIVRA LRAEGIRIPA YFSFSCRDGA HISDGTEIAE CARVLDAVPE AAAIGVNCTA PQYVSGLIRM IRQETDKPIV VYPNSGEYYD AAARVWRGAA EDFGARSREY AAAGARIIGG CCRTTPHDTA SIAAWVKAGR KRGDGDGDRV RGGSSARRTR HA // ID E0P2T0_9FIRM Unreviewed; 808 AA. AC E0P2T0; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFM22041.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFM22041.1}; GN ORFNames=HMPREF9166_2397 {ECO:0000313|EMBL:EFM22041.1}; OS Selenomonas sp. oral taxon 149 str. 67H29BP. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Selenomonas. OX NCBI_TaxID=864563 {ECO:0000313|EMBL:EFM22041.1}; RN [1] {ECO:0000313|EMBL:EFM22041.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=67H29BP {ECO:0000313|EMBL:EFM22041.1}; 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. {ECO:0000313|EMBL:EFM22041.1}. 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; AEEJ01000056; EFM22041.1; -; Genomic_DNA. DR RefSeq; WP_009754189.1; NZ_GL397087.1. DR EnsemblBacteria; EFM22041; EFM22041; HMPREF9166_2397. DR PATRIC; 41913677; VBISelSp164981_2191. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFM22041.1}; KW Transferase {ECO:0000313|EMBL:EFM22041.1}. SQ SEQUENCE 808 AA; 85992 MW; D20FA33FBCC55E70 CRC64; MGVNRKMNDI IILDGGMGTE LQARGLAPGE RPELFGMEHP DVVEEVHCNY IAAGSRVIYS NTFGANGHKL IGTGKSVAEV IAANVATARR AAEHSGVEGV RVALDVGPIG ELVEPLGTLS FEEAYELFRE MVTAGAAAGA DLVVFETLTD LYEVKAAVLA AKEHTKLPIW VTMTFEQNGR TFLGAAVSSV AVTLDALGIA ALGVNCSLGP AELRPIVAEM MEWTDLPIIV KPNAGLPDPR TGAYEMTAEM FGAEMLHFAQ SGALILGGCC GTNPDFIRCL AETVAGGAAD RPARKKRKGL ASPGRVAEYG KVNVIGERIN PTGKKRLQQA LLEEDMGYIK KLAIAQQEAG AQVLDINVGA QGVDEAAIIP QVVKAVQSVV DLPLQIDSAN PTVIEAALRV TNGRAIINSV SGERARMDAI FPLAKHYGAA VLGLAMDESG LPETAAQRVA IAERIVAEAE TYGLDREDIV IDCLTLTISA QQEQAMETLR AVREVHERLG LHCALGVSNI SFGLPARVHM TVNFLIQAMH VGLDFPIINP NTKEVMDAVV SFRAVSGEDA DCAAYIERFA AEQAEIRRRK ELGITDAAAD VKSDTPTAEG DAEIDPLMDA IMRGLSDDAE QIARRLLANT APMDIIQNKV IPALDIVGDR YEKEIIFLPQ LINAANAATS ALELIKAKLA ENGQGISKGK VILATVEGDI HDIGKNIVKV VLENYGYQII DLGRDVPVQR VVEVAIEKKV GLIGLSALMT TTVTAMKRTI DALHEAGHEC QTVVGGAVLT EDYAREIGAD YYAADARSAV EIARSVLG // ID E0P2T1_9FIRM Unreviewed; 588 AA. AC E0P2T1; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 22. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HMPREF9166_2398 {ECO:0000313|EMBL:EFM22042.1}; OS Selenomonas sp. oral taxon 149 str. 67H29BP. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Selenomonas. OX NCBI_TaxID=864563 {ECO:0000313|EMBL:EFM22042.1}; RN [1] {ECO:0000313|EMBL:EFM22042.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=67H29BP {ECO:0000313|EMBL:EFM22042.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFM22042.1}. 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; AEEJ01000056; EFM22042.1; -; Genomic_DNA. DR RefSeq; WP_009754190.1; NZ_GL397087.1. DR ProteinModelPortal; E0P2T1; -. DR EnsemblBacteria; EFM22042; EFM22042; HMPREF9166_2398. DR PATRIC; 41913679; VBISelSp164981_2192. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EFM22042.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EFM22042.1}. SQ SEQUENCE 588 AA; 63579 MW; 861D95B3FA676AC3 CRC64; MADIREHLKH EPLVFDGGMG TYYAQKTNTR GKGVELANLQ SPDVVAGIHA EYLHAGAQAI KTNTFAANRI VYQGDDELVA QIIRAGWALA ARAAEPFDAY VFADIGPVIG LPPRDIAAEY RFLADTFLSC GATHFLFETN SSAEGLTETA AYIKAACPHA FVQISFTALP GGYTRDGFFA EDLVRAVAES GQVDAVGFNC VNGVRQMKEL LHHLKSVSLP LALMPNAGHP MVVDGRTFYE SAPEYFAETL AALVQDGVSI LGGCCGTTPA HIRALCTALG TQGTVTADVQ AAAEQEPVIQ AESPFFAALR DGRKVIAVEL DPPETGHAEK FLRGARELRE AGVDAITIAD NPVARARMDA AMLASRVHRE LGIEPIPHMT CRDRNLNAIK SILLGLSAEG IHNMIAITGD PIPTAERDEV KSVYQFNSRK LSAFIKSLGE HGDVLPFHVF GALNINAKHF PSQIGLAKKK LEAGMTGFFT QPVLSERAKE NLCTAREELG DALIMGGLMP VVSERNARFM ASEIAGIHVE ERIINAYHGL DREAAEELAV RLSLEIAHDI EPYIDGYYII TPFSRTPLVA RIVAELLK // ID E0PEE0_STREI Unreviewed; 618 AA. AC E0PEE0; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 24. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HMPREF9319_1213 {ECO:0000313|EMBL:EFM27219.1}; OS Streptococcus equinus ATCC 700338. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=864569 {ECO:0000313|EMBL:EFM27219.1}; RN [1] {ECO:0000313|EMBL:EFM27219.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 700338 {ECO:0000313|EMBL:EFM27219.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFM27219.1}. 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; AEEL01000015; EFM27219.1; -; Genomic_DNA. DR RefSeq; WP_003065298.1; NZ_GL397128.1. DR ProteinModelPortal; E0PEE0; -. DR EnsemblBacteria; EFM27219; EFM27219; HMPREF9319_1213. DR PATRIC; 43441077; VBIStrBov165195_0744. DR OrthoDB; EOG6SNDP1; -. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EFM27219.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EFM27219.1}. SQ SEQUENCE 618 AA; 67984 MW; 968B6819150646D6 CRC64; MSRLLERLKT DILVADGAMG TLLYANGLDN CYEAYNLTHP DKISAIHHAY LEAGADTIQT NTYAAKRHRL KGYAYDDQVK EINQAGVKIA REAAGDDAFV LGTVGALRGL KQCNLTLDEI IEETLEQVGY LIETNQIDGL LFETYYDEEE IIEVLKAVRP ITNLPIITNI ALHEAGITEN GRPLVEILGK LVMLGADVVG LNCHLGPYHM IKSLKQVPLF AQSYLSVYPN ASLLSFVDDN GSGQYGFSQN ADYFGKSAEL LVAEGARLIG GCCGTTPDHI RAVKRAVKGL KPVERKFVTP MVEEVELIKA AKQSETLVDR VKREVTIIAE LDPPKTLDIA KFTEGVKALD KAGISAITLA DNSLAKTRIC NVSIAALLKN EISTPFLLHL SCRDHNMIGL QSRLLGMDVL GFNHVLAITG DPSKIGDFPG ATSVYDATSF KLLALIKQLN KGQGYSGASI KKEANFTAAA AFNPNVKNLS RCGRLIERKV AAGADYFITQ PVFNTEIIDG LADLTRDYEA PFFVGIMPIT SYNNAIFLHN EVPGIQLSDE FLAKLEAVKD DKETCQKLAL EESKQLIDRA LEHFKGIYLI TPFMRYDLTV ELIDYIHQKV ELKNQRIS // ID E0QLH5_9FIRM Unreviewed; 798 AA. AC E0QLH5; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFM38397.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFM38397.1}; GN ORFNames=HMPREF0379_1950 {ECO:0000313|EMBL:EFM38397.1}; OS [Eubacterium] yurii subsp. margaretiae ATCC 43715. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Peptoclostridium. OX NCBI_TaxID=864565 {ECO:0000313|EMBL:EFM38397.1}; RN [1] {ECO:0000313|EMBL:EFM38397.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43715 {ECO:0000313|EMBL:EFM38397.1}; 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. {ECO:0000313|EMBL:EFM38397.1}. 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; AEES01000066; EFM38397.1; -; Genomic_DNA. DR RefSeq; WP_005367871.1; NZ_GL405246.1. DR EnsemblBacteria; EFM38397; EFM38397; HMPREF0379_1950. DR PATRIC; 43471054; VBIEubYur165861_1878. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFM38397.1}; KW Transferase {ECO:0000313|EMBL:EFM38397.1}. SQ SEQUENCE 798 AA; 88239 MW; 573F0E145146619C CRC64; MFTIKFRELI GKKIIYLDGG MGSVLQQKGL QAGELPEILN ITNPKLIQEI HYEYYLSGSN VTYSNTFGAN KLKYEDTEHD YKELIVAAID NVRAARERFE DRDEKFIALD VGPIGKLLKP VGDLDFEEAV EIFKEVIKTG ADAGADLIAI ETMSDTYELK AAVLAAKEVC DLPIIATVAF SDDKRLLNGA DAKTVISLLE GLRVDALGMN CGLDPRNIKD IVEEFLQYSS LPLVLKPNAG IPENINGEIK FNMEPDDFGK IMREFVEMGA NIVGGCCGTT HDHIRRLYEE TCTLPLIAPT FKNHTFVSSY TKTVICNEPK IIGERINPTG KKLLKQALIN KDMSYILKEA IAQEEKGAHI LDVNTGLNEI DEQEMSLAVM RAIQEISTLP LQIDSAKTNV LETSLRYYNG KAMLNSVNGK KKVMEEIFPI VKKYGAVVVA LTIDDDGIPN DAIGRYNIAK NIVETAKTYG IDKKDIVVDP LCMTISSDKN AANQTLKALS MIKENLGVKT ILGVSNISFG LPKRELINHT FFTSALRCGL DFGIINPGSD TMMMAYDAHM VLAGFDENSS NYIAKYSNDT TVATHVAKTS DISLKEAIKK GLKEDSFNIA KNMLNDHQPL DIINSELIPA LDEVGAGFEK GVIFLPQLMM SADSASRAFD ALKEKMTAME DGSKEKQKII LATVKGDVHD IGKNIVKVLL ENYGYDVYDL GKDVDYDLIL DTIEKEKVYL VGLSALMTTT VDNMQETIRL IREKIEVEVK IMVGGAVLTK AYAEKIGADR YCKDAMESVR YAKEVFGE // ID E0RAT1_PAEP6 Unreviewed; 1146 AA. AC E0RAT1; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 29-APR-2015, entry version 34. DE SubName: Full=Methionine synthase I, cobalamin-binding domain protein {ECO:0000313|EMBL:ADM70390.1}; GN OrderedLocusNames=PPE_02562 {ECO:0000313|EMBL:ADM70390.1}; OS Paenibacillus polymyxa (strain E681). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=349520 {ECO:0000313|EMBL:ADM70390.1, ECO:0000313|Proteomes:UP000002227}; RN [1] {ECO:0000313|EMBL:ADM70390.1, ECO:0000313|Proteomes:UP000002227} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=E681 {ECO:0000313|EMBL:ADM70390.1, RC ECO:0000313|Proteomes:UP000002227}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000154; ADM70390.1; -; Genomic_DNA. DR RefSeq; WP_013310539.1; NC_014483.1. DR RefSeq; YP_003870928.1; NC_014483.1. DR EnsemblBacteria; ADM70390; ADM70390; PPE_02562. DR KEGG; ppy:PPE_02562; -. DR PATRIC; 42410882; VBIPaePol94484_2576. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; PPOL349520:GH6J-2554-MONOMER; -. DR Proteomes; UP000002227; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002227}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 722 722 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1146 AA; 126551 MW; D520CED2A7C92656 CRC64; MDKVSLQDAL QRRILLLDGA MGTMIQQEDL SPDDFGGEEL EGCNEMLVLT RPDVIQGIHE AYLKAGADLI ETNTFGATSV VLADYDIPER AREINLVAAK LARNAVDKYS TADKPRFVVG AMGPTTKTLS VTGGVTFAEL IDSYQEQALA LIEGGVDVLL LETSQDTLNV KAGSIGIRQA FEQTGIELPL MISGTIEPMG TTLAGQNIES FCISLEHLHP ISIGLNCATG PEFMRDHIRS LSEMSSAAIS CYPNAGLPDE NGQYHESPDS LARKMAAFAE KGWLNIAGGC CGTTPEHIRV MSESMAQFEP RPLVGHHPPA VSGIEPVYIE QDNRPYMVGE RTNVLGSRKF KRLIVEGKYE EASEIARAQV KSGAHVIDIC VQDPDRDEMT DMEAFLKLVV NKVKVPLVID TTDIKVIDKA LQYSQGKAII NSINLEDGEE KFEKMAPLIH KYGAAVVVGT IDERGQAISR EDKLEVARRS YDLLVNRYGL AAEDLIFDTL VFPVGTGDEQ YIGSAKETIE GIRIIKEALP GVHTILGISN VSFGLPEAGR EVLNSVYLYE CTKAGLDYAI VNTEKLERYA SIPEHERKLA EDLIYKTNDD TLSAFVAAFR NKKVEKKEKI SNLSLEERLA SYVVEGSKEG LIPDLEQALV KYSSLEIING PLMKGMEEVG RLFNNNELIV AEVLQSAEVM KASVAYLEPF MEKNESSVKG KILLATVKGD VHDIGKNLVE IILSNNGYHI VNLGIKVPPE RIIEAYREEK ADMIGLSGLL VKSAQQMVLT AQDLKNANID IPIMVGGAAL TRKFTKNRIR PEYDGLVAYA KDAMDGLDIA NKLMNPESRK KMAEDMEAER EAEAAIVVEA KPLPKLTRAV RSNIAQDLPV YIPPDTDRHV LRNYPLNYIL PYVNMQMLMG HHLGLKGNVE QLLASEDPKA IQLKETVDSI MFEAVTDGII QAHAMYRFFP AQSQGNQILI YDPSDVSKVL HTFTFPRQQV EPYLCLADFL KSVESGVMDY VGFMVVTAGH GIQQISTRWK DKGDYLRSHA LQAVALEVAE GLAERLHHII RDSWGFPDPA DMTMKQRHGA RYQGIRVSFG YPACPDLEDQ GPLFQLLKPE DIGVELTEGF MMEPEASVSA MVFSHPQAQY FNVEKV // ID E0REU4_PAEP6 Unreviewed; 628 AA. AC E0REU4; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 29-APR-2015, entry version 32. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=PPE_02925 {ECO:0000313|EMBL:ADM70750.1}; OS Paenibacillus polymyxa (strain E681). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=349520 {ECO:0000313|EMBL:ADM70750.1, ECO:0000313|Proteomes:UP000002227}; RN [1] {ECO:0000313|EMBL:ADM70750.1, ECO:0000313|Proteomes:UP000002227} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=E681 {ECO:0000313|EMBL:ADM70750.1, RC ECO:0000313|Proteomes:UP000002227}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ADM70750.1; -; Genomic_DNA. DR RefSeq; WP_013310896.1; NC_014483.1. DR RefSeq; YP_003871288.1; NC_014483.1. DR ProteinModelPortal; E0REU4; -. DR EnsemblBacteria; ADM70750; ADM70750; PPE_02925. DR KEGG; ppy:PPE_02925; -. DR PATRIC; 42411608; VBIPaePol94484_2940. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR BioCyc; PPOL349520:GH6J-2915-MONOMER; -. DR Proteomes; UP000002227; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002227}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 628 AA; 68317 MW; 858CFAC78FA18A59 CRC64; MKADLRTVLN REIIVGDGAM GTFLYQLGFP VNTSFEELNI TSPDVISDVH GQYLSAGARL LETNTFSAND YKLARFGLES KVEEINRAGV RIARAAAGPE HYVVGAVGSI CGGKRLNISK LELARNYEQQ IDALLSEGVD GILCETFYSL DEIRIALHSV RKYSDIPVIC QFAVDQVGRT QDGFLVAEAF SVLRNEGADI LGFNCHSGPQ GIMSVMEQLD GPLSVPLSVY PNAGLADYVD GHYVYGASPE YFGECAKSFV DLGTRLLGGC CGTTPDHIAA ISKALNRLQP PPLASKEALL KESFQVAEQI ADEGERGNGR HTSEPNIVDL VKERHTVIVE LDPPRDLDIT RFMQGAHALK KAGADALTLA DNSLAVTRMS NMALGHLVSI ETGLRPLIHI ACRDRNLIGT QSHMMGFDAL GIDHVLAVTG DPARFGDLPG ASSVYDMTSF EIIRMIKQLN DGVAFSGKPL KQKANFVVGA AFNPNVKHLG KAVQRLEKKI ASGADYVMTQ PVYDHELIAA IAEATRHLEV PIFIGIMPLA SGRNAEYLHN EVPGIQLSDE VRARMSGLEG PEGRAMGVSI AKELLDTAME HFNGIYFMTP FMFYEMTAEL TSYVWQKSGR AQAPLFRL // ID E0RLW9_PAEP6 Unreviewed; 315 AA. AC E0RLW9; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 29-APR-2015, entry version 22. DE SubName: Full=Homocysteine S-methyltransferase (S-methylmethionine:homocysteine methyltransferase) {ECO:0000313|EMBL:ADM72527.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ADM72527.1}; GN OrderedLocusNames=PPE_04768 {ECO:0000313|EMBL:ADM72527.1}; OS Paenibacillus polymyxa (strain E681). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=349520 {ECO:0000313|EMBL:ADM72527.1, ECO:0000313|Proteomes:UP000002227}; RN [1] {ECO:0000313|EMBL:ADM72527.1, ECO:0000313|Proteomes:UP000002227} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=E681 {ECO:0000313|EMBL:ADM72527.1, RC ECO:0000313|Proteomes:UP000002227}; 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; ADM72527.1; -; Genomic_DNA. DR RefSeq; WP_013312635.1; NC_014483.1. DR RefSeq; YP_003873065.1; NC_014483.1. DR EnsemblBacteria; ADM72527; ADM72527; PPE_04768. DR KEGG; ppy:PPE_04768; -. DR PATRIC; 42415340; VBIPaePol94484_4753. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR BioCyc; PPOL349520:GH6J-4749-MONOMER; -. DR Proteomes; UP000002227; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002227}; KW Methyltransferase {ECO:0000313|EMBL:ADM72527.1}; KW Transferase {ECO:0000313|EMBL:ADM72527.1}. SQ SEQUENCE 315 AA; 35130 MW; 1F2D6A8008EF5680 CRC64; MNPIQHILDE FQLIVLDGAM ATELERHGHD LNDSLWSAKI LHEHPESIKH VHRDYFEAGA DCAITASYQA TVEGYIKRGL NENEALELIQ SSVRIAVQAR DEFWADVTAT ASQRHRPKPL VAASVGPYGA FLADGSEYRG DYKLSEEQLM EFHRPRMKAL IEAGADILAC ETIPCLVEAK AIARLLKEFP GTYAWISFSA KDGQHISNGE SAAACAEWLN WHEQVAAIGI NCTLPKFVPS LIHEIRSHTD KPVVVYPNLG EEYDPVTKTW HGSTCTETFG QSARQWYEAG ARLIGGCCRT QPQDIEEIAS WTRDV // ID E0RNR6_SPITD Unreviewed; 1213 AA. AC E0RNR6; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 36. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADN01189.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADN01189.1}; GN Name=metH {ECO:0000313|EMBL:ADN01189.1}; GN OrderedLocusNames=STHERM_c02150 {ECO:0000313|EMBL:ADN01189.1}; OS Spirochaeta thermophila (strain ATCC 49972 / DSM 6192 / RI 19.B1). OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Spirochaeta. OX NCBI_TaxID=665571 {ECO:0000313|EMBL:ADN01189.1, ECO:0000313|Proteomes:UP000001296}; 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] {ECO:0000313|EMBL:ADN01189.1, ECO:0000313|Proteomes:UP000001296} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49972 / DSM 6192 / RI 19.B1 RC {ECO:0000313|Proteomes:UP000001296}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001698; ADN01189.1; -; Genomic_DNA. DR RefSeq; WP_013313030.1; NC_014484.1. DR RefSeq; YP_003873462.1; NC_014484.1. DR EnsemblBacteria; ADN01189; ADN01189; STHERM_c02150. DR KEGG; sta:STHERM_c02150; -. DR PATRIC; 42519631; VBISpiThe146732_0217. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; STHE665571:GI3Y-215-MONOMER; -. DR Proteomes; UP000001296; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001296}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADN01189.1}; KW Transferase {ECO:0000313|EMBL:ADN01189.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1213 AA; 133592 MW; CF34102B2D108C9C CRC64; MTHPIEELLK ERILILDGAM GTMIQRYHLS EADYRGTLFE RGPTVDGREV ALKGNHDLLV LTRPHVIEEI HRAYLEAGAD IIETNTFNAT RVSQREYGTE DLVERINREA ARLARRVADE YSARTPHRPR FVAGVVGPTS KTLSLSPRAD DPAFRELSFG ELEEDYFGAV RALVEGGADL ILIETVFDTL NAKAALAAVA RFRRESGRAV PVMLSATISD AAGRLLSGQT PRAFLHSVLH GRPLSVGFNC AFGPEMMRPH LKAIQDAPCA VSVHPNAGLP NALGEYDQGP DQMAATLALY AREGLLNIAG GCCGTTPDHI RAIAGTLEGI APRPIPSPRP VAVFTGLEVL DQEVAGFILV GERTNVAGSA RFRRLLREER WEEALEVARA QISAGAHMID VNVDDPLLDP PRLMRHFLSL AASEPTVARV PVMIDSSDWE VLRAGLECLQ GKGVVNSLSL KDGEAIFLER ARVVREMGAS VLVMCFDEEG QAETFERKIA VAQRAYRLLV EEVGIPPWDI VIDPNIFAIG TGMEEHARYG VDYLEAVRWI KEHLPHARTS GGISNVSFAF RGHEGLRDAI HAVFLHHARA AGLDMAIVNP QRMMAYEEVP EEVRALIEDL IFARRRDATE RLLEAAQGLS SAGPRGRGED RAWRELPVEE RLAYALKEGI QGYLGEDLEE AHRKAGSALG VIEGPLLTGM EEVGRLFGEG RLFLPQVVRA ARVMREAVAI LEPRLKAEQG GVGKARGVVV LATVKGDVHD IGKNIVKVVL ECNGYRVVDL GVMVPPERVV EAARQGADAV GLSGLITPSL ERMRETAEAL DRAGLAVPLL IGGAATSRLH TALRIAPAYR GPVIHVRDAS EAVQVMGRLL SEGREEFVRE VRAEQARLRE QGVKGRGGVL GLGEARRRRL RPGPASPVEP RVRGPQVVRM GVAEVRPYLD WRMFYKGWGL PARTPERMRE AERAEAVRLR EEAEGVLARM EGRVRIEGVV GFFPARDVGE DCIGVLGWGG EGVIRRLPML RQQAVKEGEP TRSLVDFLPH EGHDYLGLFV ITAGKDIEHF LAEEGPGEPY RELMVRLLAD RLAEAASEYL HMLVRTTLWG YAPEEHLSPE EVLAGTYRGI RPAPGHAACP DHSLKQDIFE LLGAEERLGI RLTESFMMVP PSSVAGFYFS HPESRYFAVG RITEEQLRDY ARRRERPVDE VRGWLDHIVV ADS // ID E0S281_BUTPB Unreviewed; 821 AA. AC E0S281; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 29-APR-2015, entry version 31. DE SubName: Full=Methionine synthase MetH {ECO:0000313|EMBL:ADL33906.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADL33906.1}; GN Name=metH {ECO:0000313|EMBL:ADL33906.1}; GN OrderedLocusNames=bpr_I1166 {ECO:0000313|EMBL:ADL33906.1}; OS Butyrivibrio proteoclasticus (strain ATCC 51982 / DSM 14932 / B316) OS (Clostridium proteoclasticum). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Butyrivibrio. OX NCBI_TaxID=515622 {ECO:0000313|EMBL:ADL33906.1, ECO:0000313|Proteomes:UP000001299}; RN [1] {ECO:0000313|EMBL:ADL33906.1, ECO:0000313|Proteomes:UP000001299} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51982 / DSM 14932 / B316 RC {ECO:0000313|Proteomes:UP000001299}; 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 ----------------------------------------------------------------------- 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; ADL33906.1; -; Genomic_DNA. DR RefSeq; WP_013280560.1; NC_014387.1. DR RefSeq; YP_003830488.1; NC_014387.1. DR PRIDE; E0S281; -. DR EnsemblBacteria; ADL33906; ADL33906; bpr_I1166. DR KEGG; bpb:bpr_I1166; -. DR PATRIC; 42221607; VBIButPro41874_1176. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR BioCyc; BPRO515622:GHKV-1189-MONOMER; -. DR Proteomes; UP000001299; Chromosome 1. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001299}; KW Methyltransferase {ECO:0000313|EMBL:ADL33906.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001299}; KW Transferase {ECO:0000313|EMBL:ADL33906.1}. SQ SEQUENCE 821 AA; 88546 MW; 524B8A95534D3DB9 CRC64; MTKEEFWGLS NNRILFLDGA TGTNLMKAGM PAGVCPENWI LEHQDVMINL QSNYAKAGAD IIYAPTFTGN RIKLADYGLG DRIEEINSSL VKLTKKAAPG VLVAGDITMT GRQLRPIGDL DFEELVDVYK QQIKILEAAG CDILVVETMM SLQECRAALI AAKEVTDLAV MVTLTFEADG RTLYGSDAAS SAITLEALGA CAIGANCSTG PDKMAAIISD MAAVTSIPII AKPNAGLPSV DENGNTEYDM DCDTFVKEME LLVSAGASII GGCCGTTPDY IKGLKDRYGN VKPNDIRDGE GNPVPRKICG RRYLASERMS LSFGLDENFM IVGERINPTG KKKLQEQLRE GNLDMVCDFA ANQEKEGASI LDINVGMSGI DEKEMMLKVM EEVMSITDLP LCIDTSSAEV MEAALRLYPG RALMNSISLE KGKAEKFLPL AKKYGAMFIL LPLAEALPKD SQEKIDNINT IYEMATKLGM NKEDIVVDGL VATVGADPNA AINTLDTIGY CHENSYATIC GLSNISFGLP QRSNVNTAFL TMAIARGLTM AIANPSQEML VNAAFASDLL RKKEGADVRY ITRMERYADQ NSANSAAQNV SSSKAVLEND NILDIIKKDV LTGNKRGIVK DTEKAVKEGN SPRQILDEIL MPAINEVGDL FDKGKYFLPQ LIAGAEAMKL SIGYLEPLLK EGADSGEKLP SIVIATVHGD IHDIGKNLVA LMLKNYGFNV IDLGKDVPRE EIIKAARKYD AKIIALSALM TTTMKEMKNV VDLAHAENLD AKIIIGGAVV TQDYADEIGA DGYSSDAADA VRVVKNILGI E // ID E0SI43_DICD3 Unreviewed; 1227 AA. AC E0SI43; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 35. DE SubName: Full=Homocysteine-N5-methyltetrahydrofolate transmethylase, B12-dependent {ECO:0000313|EMBL:ADN00252.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADN00252.1}; GN Name=metH {ECO:0000313|EMBL:ADN00252.1}; GN OrderedLocusNames=Dda3937_02131 {ECO:0000313|EMBL:ADN00252.1}; OS Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Dickeya. OX NCBI_TaxID=198628 {ECO:0000313|EMBL:ADN00252.1, ECO:0000313|Proteomes:UP000006859}; RN [1] {ECO:0000313|EMBL:ADN00252.1, ECO:0000313|Proteomes:UP000006859} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3937 {ECO:0000313|EMBL:ADN00252.1, RC ECO:0000313|Proteomes:UP000006859}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002038; ADN00252.1; -; Genomic_DNA. DR RefSeq; WP_013319670.1; NC_014500.1. DR EnsemblBacteria; ADN00252; ADN00252; Dda3937_02131. DR GeneID; 9735534; -. DR PATRIC; 42320409; VBIDicDad25310_3992. DR HOGENOM; HOG000251409; -. DR OMA; DYNSIMV; -. DR BioCyc; DDAD198628:GHFQ-4149-MONOMER; -. DR Proteomes; UP000006859; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006859}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADN00252.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006859}; KW Transferase {ECO:0000313|EMBL:ADN00252.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135281 MW; FAF8644FCB160F13 CRC64; MANRLQALQQ QLAQRIMILD GGMGTMIQSY RLQEEDYRGE RFADWHCDLK GNNDLLVLSK PEVITAIHND YLAAGADILE TNTFNATRIA MADYEMEALS AEINTAAARL ARACADEWTA RTPERPRYVA GVLGPTNRTA SISPDVNDPA YRNVSFDQLV EAYRESTRAL VEGGVDIILI ETIFDTLNAK AAIFAVETEF EALGVTLPVM LSGTITDASG RTLSGQTTEA FYNSLRHARP LSFGLNCALG PDELRQYVAE LSRIAECYVT AHPNAGLPNA FGEYDLDADE MARQIGEWAQ SGFLNIIGGC CGTTPEHIAA MVKAVDGVAP RALPTLPVAC RLSGLEPLNI GDDTLFVNVG ERTNVTGSAK FKRLIKEEKY NEALDVARQQ VESGAQVIDI NMDEGMLNAE AAMVRFLNLI AGEPDIARVP IMIDSSKWEV VEAGLKCIQG KGIVNSISMK EGVDAFVHHA RLVRRYGAAV VVMAFDEVGQ ADTRARKIEI CRRAYHILTE EVGFPPEDII FDPNIFAVAT GIDEHNNYAV DFIEACADIK AQLPHAMISG GVSNVSFSFR GNEPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER MLAIAEKYRG SKSDDDSNKA EAEWRGWPVR KRLEYALVKG ITEFIEQDTE EARAQSARPI EVIEGPLMDG MNVVGDLFGA GKMFLPQVVK SARVMKQAVA YLEPFIQASK DQGSSAGKIL LATVKGDVHD IGKNIVGVVL QCNNYEIIDL GVMVPTDKIL KTAREEKVDI IGLSGLITPS LDEMVNVAKE MERQGFTLPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRSVGVVSAL LSDTQRGDFV ARIRKEYETV RIQHGRKKPR TPPVSLSVAR DNAMPIDWES YTPPVAHRLG VQSVSASIET LRNYIDWTPF FMTWSLAGKY PNILEDEVVG EEAKRLFADA NAMLDTLSAN GTLNPRGVVG LFPANRVGDD IEIYTDERRT EVLTVSHHLR QQTEKTDFPN YCLADVVAPK ASGKPDYLGA FAVTGGLEED ELAAQWEAQH DDYNKIMLKA LADRLAEAFA EYLHERVRKV HWGYAPNENL GNDALIRENY QGIRPAPGYP ACPDHTEKAT IWQLLDVDNT VGMTLTESYA MWPGASVSGW YFSHPDSKYF AVAQIQRDQV EDYAVRKQMP VEEIERWLAP NLGYDAD // ID E0SI80_DICD3 Unreviewed; 302 AA. AC E0SI80; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADM96594.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ADM96594.1}; GN OrderedLocusNames=Dda3937_01274 {ECO:0000313|EMBL:ADM96594.1}; OS Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Dickeya. OX NCBI_TaxID=198628 {ECO:0000313|EMBL:ADM96594.1, ECO:0000313|Proteomes:UP000006859}; RN [1] {ECO:0000313|EMBL:ADM96594.1, ECO:0000313|Proteomes:UP000006859} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3937 {ECO:0000313|EMBL:ADM96594.1, RC ECO:0000313|Proteomes:UP000006859}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; ADM96594.1; -; Genomic_DNA. DR RefSeq; WP_013316077.1; NC_014500.1. DR EnsemblBacteria; ADM96594; ADM96594; Dda3937_01274. DR GeneID; 9731780; -. DR PATRIC; 42313103; VBIDicDad25310_0392. DR HOGENOM; HOG000265278; -. DR OMA; PYVDVWL; -. DR BioCyc; DDAD198628:GHFQ-394-MONOMER; -. DR Proteomes; UP000006859; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006859}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ADM96594.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006859}; KW Transferase {ECO:0000313|EMBL:ADM96594.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 302 AA; 32044 MW; 7F8E83F5605DC00F CRC64; MADNVLILDG GMGRELARIG APFRQPEWSA LALMESPQHV RQVHDSYIAA GAQVITTNSY AVVPFHISDA VFNARGQALA TLAGQLARQA ADAAAHPVRV AGSLPPVLGS YRPDLFNAAA ATPILKTLID ALNPYVDVWL AETQSSLAEV ALVRELLAND ARELWLSFTL QDELDADGHA RLRSGETVAA AAQAAIQLRA ANLLFNCSRP EVMAPAVAQA SATLKAQSAA IGVGVYANAF EPEDNQRGAN EGLSRLRTDT HPEGYLQWSQ EWVAQGASLV GGCCGIGPEH IARLAQAFHR QG // ID E0TI34_PARBH Unreviewed; 351 AA. AC E0TI34; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 32. DE SubName: Full=MetH protein {ECO:0000313|EMBL:ADM09373.1}; GN OrderedLocusNames=PB2503_06537 {ECO:0000313|EMBL:ADM09373.1}; OS Parvularcula bermudensis (strain ATCC BAA-594 / HTCC2503 / KCTC OS 12087). OC Bacteria; Proteobacteria; Alphaproteobacteria; Parvularculales; OC Parvularculaceae; Parvularcula. OX NCBI_TaxID=314260 {ECO:0000313|EMBL:ADM09373.1, ECO:0000313|Proteomes:UP000001302}; RN [1] {ECO:0000313|Proteomes:UP000001302} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-594 / HTCC2503 / KCTC 12087 RC {ECO:0000313|Proteomes:UP000001302}; 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; ADM09373.1; -; Genomic_DNA. DR RefSeq; WP_013300347.1; NC_014414.1. DR RefSeq; YP_003854515.1; NC_014414.1. DR ProteinModelPortal; E0TI34; -. DR EnsemblBacteria; ADM09373; ADM09373; PB2503_06537. DR KEGG; pbr:PB2503_06537; -. DR PATRIC; 42426593; VBIParBer119301_1235. DR HOGENOM; HOG000265279; -. DR OMA; AQEDYKM; -. DR BioCyc; PBER314260:GI0G-1215-MONOMER; -. DR Proteomes; UP000001302; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001302}; KW Reference proteome {ECO:0000313|Proteomes:UP000001302}. SQ SEQUENCE 351 AA; 37563 MW; FF81A48FC14D2B32 CRC64; MTSSRRDSLI SALEERILIL DGAGGTMIQR AKPTEEDYRG ERFADWPKDL GGNNDLLTLT KPDLIRSIHD EYLAAGADII ETNTFSSTTI AQADYDMQSL AYELNVEGAR IARQAADAAA TRDKPRFVAG AIGPTNRTAS ISPDVNDPGA RNTDFDSLAA AYAEAARGLL EGGADLLLIE TIFDTLNAKA ALFGIDQLFG ELGEKVPLML SVTITDQSGR TLSGQTTEGF WNSVRHAEPL SVGINCALGP DLMRPYIMEL SRIAETYVSA YPNAGLPNAF GEYDETPEGM AAHIGEWAES GFLNIIGGCC GTTPDHIRAF AARVSGVPPR QRPARPVVMR LSGLEPVSIA G // ID E0U0U9_BACPZ Unreviewed; 315 AA. AC E0U0U9; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:ADM36302.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ADM36302.1}; GN Name=mmuM {ECO:0000313|EMBL:ADM36302.1}; GN OrderedLocusNames=BSUW23_01225 {ECO:0000313|EMBL:ADM36302.1}; OS Bacillus subtilis subsp. spizizenii (strain ATCC 23059 / NRRL B-14472 OS / W23). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=655816 {ECO:0000313|EMBL:ADM36302.1, ECO:0000313|Proteomes:UP000002233}; RN [1] {ECO:0000313|Proteomes:UP000002233} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23059 / NRRL B-14472 / W23 RC {ECO:0000313|Proteomes:UP000002233}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; ADM36302.1; -; Genomic_DNA. DR RefSeq; WP_003223788.1; NC_014479.1. DR RefSeq; YP_003864612.1; NC_014479.1. DR EnsemblBacteria; ADM36302; ADM36302; BSUW23_01225. DR KEGG; bss:BSUW23_01225; -. DR PATRIC; 42186483; VBIBacSub57968_0249. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR BioCyc; BSUB655816:GCOR-278-MONOMER; -. DR Proteomes; UP000002233; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002233}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ADM36302.1}; KW Transferase {ECO:0000313|EMBL:ADM36302.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 229 229 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 315 AA; 34743 MW; 49FC2026530B2EEF CRC64; MNPIQHILDT YPLIVLDGAM ATELERKGCD LNDSLWSAKI LMEEPDLIKQ IHTDYFAAGA DCAITASYQS TFEGFAARGL SEAKARRLIE MSVSIAAVAR DEFWALEENR LNRPKPIIAA SVGPYGAYLA DGSEYRGHYG ITEDELVEFH RPRMKALIEA GADVLACETI PCLTEAKAIV RLLKEFPETY AWISFSAKDG LHISDGTPAA DCASWLDEHH QIAAIGINCT PLQHIPSLIE ELKKHTSKPI IVYPNSGEQY DPETKTWNGA ACAEPYGQSA RMWHEKGAKL IGGCCRTKPE DIKEIAAWAH ALKTT // ID E0U104_BACPZ Unreviewed; 612 AA. AC E0U104; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 33. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN Name=yitJ {ECO:0000313|EMBL:ADM37169.1}; GN OrderedLocusNames=BSUW23_05580 {ECO:0000313|EMBL:ADM37169.1}; OS Bacillus subtilis subsp. spizizenii (strain ATCC 23059 / NRRL B-14472 OS / W23). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=655816 {ECO:0000313|EMBL:ADM37169.1, ECO:0000313|Proteomes:UP000002233}; RN [1] {ECO:0000313|Proteomes:UP000002233} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23059 / NRRL B-14472 / W23 RC {ECO:0000313|Proteomes:UP000002233}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ADM37169.1; -; Genomic_DNA. DR RefSeq; WP_003224504.1; NC_014479.1. DR RefSeq; YP_003865478.1; NC_014479.1. DR ProteinModelPortal; E0U104; -. DR EnsemblBacteria; ADM37169; ADM37169; BSUW23_05580. DR KEGG; bss:BSUW23_05580; -. DR PATRIC; 42188327; VBIBacSub57968_1138. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR BioCyc; BSUB655816:GCOR-1177-MONOMER; -. DR Proteomes; UP000002233; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002233}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ADM37169.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:ADM37169.1}. SQ SEQUENCE 612 AA; 67830 MW; FED2D35DABF86B92 CRC64; MGLLEDLQKQ VLIGDGAMGT LLYSYGIDRC FEELNISKPE EIQRIHKAYV EAGANIIQTN TYGANYIKLS RHGLEDDIKK MNQEAVKIAR ASAGDAYVLG TMGGIRTFNK NAYSLDEIKR SFREQLYLLL HEEPDGLLLE TYYDLEEARE VLKIARKETS LPIMLNVSMH EQGVLQDGTP LSEALRSIAD LGADIVGINC RLGPYHMIEA LSEVPIFDDV FLSVYPNSSL PSLEEGRLVY ETDDTYFQNS ASEFRKQGAR IIGGCCGTTP NHIRAMAEAV GGLAPITDKE VKTRPKEFIS VQDERTEPGL NEIAAKKRSI IVELDPPKKL SFDKFLSAAA ELKEAGIDAL TLADNSLATP RISNVACGAL VKQQLDMRSL VHITCRDRNI IGLQSHLMGL DTLGLNDVLA ITGDPSKIGD FPGATSVYDL TSFDLIRLIK QFNEGLSLSG KPLGKKTNFS VAAAFNPNVR HLDKAVKRLE KKIDCGADYF VSQPVYSEQQ LVDIHNETKH LKTPVYIGIM PLTSSRNAEF IHNEIPGIKL SDSIREKMAL AGEDKEKQKA EGLAIARSLL DTACELFNGI YLITPFLRSD LTAELTSYIQ QKDEQRQNIY LH // ID E0UBI0_CYAP2 Unreviewed; 1186 AA. AC E0UBI0; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 01-APR-2015, entry version 35. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADN12812.1}; GN OrderedLocusNames=Cyan7822_0786 {ECO:0000313|EMBL:ADN12812.1}; OS Cyanothece sp. (strain PCC 7822). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Cyanothece. OX NCBI_TaxID=497965 {ECO:0000313|EMBL:ADN12812.1, ECO:0000313|Proteomes:UP000008206}; RN [1] {ECO:0000313|Proteomes:UP000008206} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7822 {ECO:0000313|Proteomes:UP000008206}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002198; ADN12812.1; -; Genomic_DNA. DR RefSeq; WP_013320922.1; NC_014501.1. DR RefSeq; YP_003886087.1; NC_014501.1. DR ProteinModelPortal; E0UBI0; -. DR EnsemblBacteria; ADN12812; ADN12812; Cyan7822_0786. DR KEGG; cyj:Cyan7822_0786; -. DR PATRIC; 42282089; VBICyaSp18455_0819. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; CSP497965:GJAC-794-MONOMER; -. DR Proteomes; UP000008206; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008206}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008206}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 228 228 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 737 737 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1186 AA; 131700 MW; 62E312C4D1A56F1C CRC64; MNSPFLNRLH SLERPVLVFD GAMGTSLQSQ NLTAEDFGGP EYEGCNEYLV HTKPEAVAKV HQGYLEAGAD VIETDTFGGT SIVLAEYDLA DQAYYLNKTA AQLAKQVAQQ YSTPEKPRFV AGSMGPGTKL PTLGHIDFDT LKNAYVEQAE GLYDGGADLF IVETCQDVLQ IKAALNAIEE VLEKKDNRIP IMVSITMEVM GTMLIGTEIG AALAILEPYN IDILGLNCAT GPEQMKEHIK YLSENSPFII SCIPNAGLPE NVGGQAHYRL TPLELRMALM HFVEDLGVQI IGGCCGTRAD HIKALAEITK DLKPKERHFH YEYSAASIYS TQPYIQDNSF LIVGEKLNAS GSKKCRELLN KEDWDGLVSM AKAQVKEGAH ILDVNVDYVG RDGVKDMKEL ASRLVNNVTL PLMLDSTEWE KMEAGLKVAG GKCILNSTNF EDGEPRFYKV LELAKKYGAG VVVGTIDEEG MARTAEKKFQ IAKRAYEAAI NYGIPPEEIF FDPLALPIST GIEEDRNNGK ATVEAIKRIR EELPGCHIML GVSNISFGLN PAARQVLNSV FLHETMAVGL DGAIVSANKI LPLAKIEPEY QEISRDLIYD RRRFEGDVCV YDPLTKLTEV FAGKTTKKTG ADKANLPIEE RLKQHIIDGE RIGLEEALAE ALKQYPPLDI INVFLLDGMK VVGELFGSGQ MQLPFVLQSA QTMKAAVAYL EPFMEKEEGN GNAKGKFIIA TVKGDVHDIG KNLVDIILSN NGYKVINLGI KQPVENIIQA YEEHKADCIA MSGLLVKSTA FMKENLAVFN ERGITVPVIL GGAALTPKFV HQDCQNTYKG QVVYGKDAFS DLHFMDKLMP AKAAGNWDDI KGFLDEFEAA QEPELTQVSV GVTDEDDGKT REPAVIDTRR SEAVEADIER PVPPFWGTKI LTPDDIFLDE IFGYLDLQAL FVGQWQFRKP REQSREEYDE FLADTVHPIL ESWKRRVKDE NLLHPTVIYG YFPCQSEGNS LLVYDPEIIG QSGGKIPENL DPIWIIDFPR QKSGRRLCIA DFFAAKGSGI VDVFPMQAVT VGEVATQFAK TLFESNQYTD YLYYHGMAVQ AAEALAEWTH ARIRQELGFG DKEPSNIRDI LQQRYQGSRY SFGYPACPNI QDQYKQLELL GCDRINMYMD ESEQIYPEQS TTAIVAYHAA AKYFST // ID E0US60_SULAO Unreviewed; 1162 AA. AC E0US60; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 34. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ADN10153.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADN10153.1}; GN OrderedLocusNames=Saut_2111 {ECO:0000313|EMBL:ADN10153.1}; 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 {ECO:0000313|EMBL:ADN10153.1, ECO:0000313|Proteomes:UP000007803}; RN [1] {ECO:0000313|Proteomes:UP000007803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-671 / DSM 16294 / JCM 11897 / OK10 RC {ECO:0000313|Proteomes:UP000007803}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002205; ADN10153.1; -; Genomic_DNA. DR RefSeq; WP_013327906.1; NC_014506.1. DR RefSeq; YP_003893165.1; NC_014506.1. DR EnsemblBacteria; ADN10153; ADN10153; Saut_2111. DR KEGG; sua:Saut_2111; -. DR PATRIC; 42443876; VBISulAut92361_2125. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; SAUT563040:GH0V-2163-MONOMER; -. DR Proteomes; UP000007803; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007803}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADN10153.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007803}; KW Transferase {ECO:0000313|EMBL:ADN10153.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 732 732 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1162 AA; 129858 MW; B39FCF68A00C33EB CRC64; MTTKQYILET IKKRPLIIDG AMGTQLQQRD DKIPKEAWEG NEGCNELLNV TAPEIMNEIF HAYLNAGADF ITTNTFGSFS WVLDEYNIAD RAYELTRAGA ELVKKQCEAF STPEHPRFCL GSIGPGTKLP SLGHITYDEM YAGYTEFCLA LIDGGVDVFL IETAQDPLQI KAALHAIQEA CRQKEVEIPI MVSVTIELSG TMLIGTDAET IATIMEPFDI LSLGFNCGTG PEQVLKHVKT LSELWGKPIS VHANAGLPQN RGGYTYYPMG PDEFVVQQEK FLAYDGVSFL GGCCGTTPQH IRALVDKVTA IAPKIPSGSQ QNSIASLFNT VPLMQQPAPL LVGERSNATG SKAFRELLLA ENYEGTLSVA QQQVRAGAHV LDVNVGFAGR DETKDMTEVM AMYAQKIALP LMPDSTQTKG LETALKHIGG KPILNSVNLE DGEPKFDAVC QLAKKYGASL VCLTIDEKGM AKTVEDKIKV AERIIDLATN RHGIKKEDLV FDVLTFTLGS GDEEYFNAGI NTIEAIRQLR QKHPEVGAIL GLSNISFGLD KDARPYLNSM FLHHCVEAGL TSVIINVKHI IPLNKIPKKD QKICDDLIFN RKPNGEALFT FIEHFSSKEA VDNNAVDEEY LKMSNEEKIA KLLMDGDKDR MIPLVEEARH KIAPQKIVNE ILIDAMKVVG ELFGSGQMQL PFVLQSAETM KKAVDHLNPY LPKVEKETDT TLVLGTVKGD VHDVGKNLVD IILSNNGYKV INLGIKVELD SFLETLEKSN AQALGMSGLL VKSTQVMLEN LNILQEKGIK IPVLLGGAAL TKAFIDDFCR PAYDGPIFYC KDAFDGVTAM SRIEAGNFDT NLHPDAPEIQ RKEVKEYTIP PLSEIKMPSR DVPVPTPPFW GRREIKLTQQ QIEMAFKWIN HKLLFKSRWG YSSKGMSKEA YQKQLDEVVW PAYEKLKKRF IEEKLFEPTI LYGYWPCRSD NTSLLVFPEN EGWFTEEDVN REPLEHIIGR AEEVFTFPRQ RKKPHRALSD FFHNDRHDVV ALTCVSAGNK ISDAEREIYE RGDYTEYYQF HGLGVELAEA LAEIAHKQIR LDLNIAKDEG NTLGDVRMNR YQGSRYSFGY AACPDLELNR PLFDLLKPEE FGIELSETFQ IHPEQSTSAL VVYHPEATYY NV // ID E0VF06_PEDHC Unreviewed; 312 AA. AC E0VF06; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 07-JAN-2015, entry version 24. DE SubName: Full=Homocysteine S-methyltransferase, putative {ECO:0000313|EMBL:EEB11980.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EEB11980.1}; GN ORFNames=Phum_PHUM148250 {ECO:0000313|EMBL:EEB11980.1}; OS Pediculus humanus subsp. corporis (Body louse). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Paraneoptera; Phthiraptera; Anoplura; OC Pediculidae; Pediculus. OX NCBI_TaxID=121224 {ECO:0000313|Proteomes:UP000009046}; RN [1] {ECO:0000313|Proteomes:UP000009046} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=USDA {ECO:0000313|Proteomes:UP000009046}; RX PubMed=20566863; DOI=10.1073/pnas.1003379107; RA Kirkness E.F., Haas B.J., Sun W., Braig H.R., Perotti M.A., RA Clark J.M., Lee S.H., Robertson H.M., Kennedy R.C., Elhaik E., RA Gerlach D., Kriventseva E.V., Elsik C.G., Graur D., Hill C.A., RA Veenstra J.A., Walenz B., Tubio J.M., Ribeiro J.M., Rozas J., RA Johnston J.S., Reese J.T., Popadic A., Tojo M., Raoult D., Reed D.L., RA Tomoyasu Y., Krause E., Mittapalli O., Margam V.M., Li H.M., RA Meyer J.M., Johnson R.M., Romero-Severson J., Vanzee J.P., RA Alvarez-Ponce D., Vieira F.G., Aguade M., Guirao-Rico S., Anzola J.M., RA Yoon K.S., Strycharz J.P., Unger M.F., Christley S., Lobo N.F., RA Seufferheld M.J., Wang N., Dasch G.A., Struchiner C.J., Madey G., RA Hannick L.I., Bidwell S., Joardar V., Caler E., Shao R., Barker S.C., RA Cameron S., Bruggner R.V., Regier A., Johnson J., Viswanathan L., RA Utterback T.R., Sutton G.G., Lawson D., Waterhouse R.M., Venter J.C., RA Strausberg R.L., Berenbaum M.R., Collins F.H., Zdobnov E.M., RA Pittendrigh B.R.; RT "Genome sequences of the human body louse and its primary endosymbiont RT provide insights into the permanent parasitic lifestyle."; RL Proc. Natl. Acad. Sci. U.S.A. 107:12168-12173(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; DS235100; EEB11980.1; -; Genomic_DNA. DR RefSeq; XP_002424718.1; XM_002424673.1. DR EnsemblMetazoa; PHUM148250-RA; PHUM148250-PA; PHUM148250. DR GeneID; 8239508; -. DR KEGG; phu:Phum_PHUM148250; -. DR VectorBase; PHUM148250; Pediculus humanus. DR CTD; 8239508; -. DR InParanoid; E0VF06; -. DR KO; K00547; -. DR OMA; QCKDENT; -. DR OrthoDB; EOG7GQXW0; -. DR PhylomeDB; E0VF06; -. DR Proteomes; UP000009046; Partially assembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009046}; KW Methyltransferase {ECO:0000313|EMBL:EEB11980.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000009046}; KW Transferase {ECO:0000313|EMBL:EEB11980.1}. SQ SEQUENCE 312 AA; 35270 MW; 75892EF9069882CB CRC64; MEKIKVLDGG FSTQLARYVG DIIDGDPLWS ARFLYTNPEA VINSHLDFLK AGAEIIITNS YQASISGFKE YLGCDETEGY DLIKSSVRFA KRARDLYLET NPGARPLIAG SVGPYGASLH DGSEYTGEYM DKVDKDAIMS WHRPRITGLI EEGVDLLAFE TIPAFKEGEF LLELLKEFPK QKAWLSFQCK NSEHTAKGEN FQEVIKKCWS MNKEQLVAVG CNCLSPKYVS KLFKGINENR TDKIPLIVYP NSGEEYIPNI GWFGNEKLFN MNKLFGEWFD YGVKYIGGCC RTNADDVKNI SNAVKQWNLK KK // ID E0XVY3_9GAMM Unreviewed; 300 AA. AC E0XVY3; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 29-OCT-2014, entry version 12. DE SubName: Full=Homocysteine/selenocysteine methylase (S-methylmethionine-dependent) {ECO:0000313|EMBL:ADI18574.1}; OS uncultured gamma proteobacterium HF4000_23L14. OC Bacteria; Proteobacteria; Gammaproteobacteria; environmental samples. OX NCBI_TaxID=710988 {ECO:0000313|EMBL:ADI18574.1}; RN [1] {ECO:0000313|EMBL:ADI18574.1} 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; GU474893; ADI18574.1; -; Genomic_DNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:ADI18574.1}; KW Transferase {ECO:0000313|EMBL:ADI18574.1}. SQ SEQUENCE 300 AA; 33522 MW; 3129923A6EFC7DDB CRC64; MDRYSSLMKR VKDGECILID GATGTEVERR GVPQLKNAWN GGAALSHPDI VRQVHQEYIN LGAEIVISNT FSTNKHALSD AELDHNFKAL NERGVKLAVE AREHLNKDNV LVAGGISYWT WTDNKPSLGE LNSSITQQAK IMADAGADLI MLEMMVDIEQ MMTTLKAAQA SGLPIWVGLS CEPDQSQKMC LLDKDSLEDT IHELKSYNPD VINIMHTEVE YVDQCLDILQ NKWDGHIGVY AHSGTSIDGD WTFNNVISAD EYCAYSSNWK KRGINFIGGC CGVHTDHIDM MRRELFTNTR // ID E0Y189_9PROT Unreviewed; 289 AA. AC E0Y189; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine/selenocysteine methylase (S-methylmethionine-dependent) {ECO:0000313|EMBL:ADI20430.1}; OS uncultured alpha proteobacterium EB080_L43F08. OC Bacteria; Proteobacteria; Alphaproteobacteria; environmental samples. OX NCBI_TaxID=710797 {ECO:0000313|EMBL:ADI20430.1}; RN [1] {ECO:0000313|EMBL:ADI20430.1} 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GU474941; ADI20430.1; -; Genomic_DNA. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ADI20430.1}; KW Transferase {ECO:0000313|EMBL:ADI20430.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 200 200 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 273 273 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 274 274 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 289 AA; 30801 MW; 3B2F8027D8483CE4 CRC64; MTITFLDGGM GQELVARAGK ATSLWSVQAL LDNPEMVTAV HNEYFMVGAD VATTNTYSIL PDRLEKHGLA DQLEKLQNLA CQLATEARDL NGKGIVAGSL GPQGFSYQPE LSPPADMAAE IYSRICKIQA NHVDVFIAET MSSVDQAKGA LMGASGFNKP IWLALSVGDR DGTKLRSGED LKDILPLLNE YKPAAVMINC SAPEAVSIAL PLLSEANIPT GGYANGFVEI AKNFNKIGAT VDLLKARTDL NPEAYANIAD DWIKSGATFI GGCCEVGPAH IAELKRRFG // ID E0Y1G8_9PROT Unreviewed; 330 AA. AC E0Y1G8; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 01-OCT-2014, entry version 16. DE SubName: Full=Methionine synthase I (Cobalamin-dependent), methyltransferase domain-protein {ECO:0000313|EMBL:ADI20509.1}; OS uncultured alpha proteobacterium EB080_L58F04. OC Bacteria; Proteobacteria; Alphaproteobacteria; environmental samples. OX NCBI_TaxID=710798 {ECO:0000313|EMBL:ADI20509.1}; RN [1] {ECO:0000313|EMBL:ADI20509.1} 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; GU474942; ADI20509.1; -; Genomic_DNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:ADI20509.1}; KW Transferase {ECO:0000313|EMBL:ADI20509.1}. SQ SEQUENCE 330 AA; 34937 MW; BE132E852E15746F CRC64; MLSERPWILA DGATGTNLFN MGLLSGDAPE LWNEQHPERI RELYQMAVDA GSDLFLTNSF GGNASRLKLH DQAHRAFHLS KISAEIGRDV ADKTERDIIV AGSVGPTGDI MQPVGPLSHS DAVEIFHEQA EGLKEGGADV LWLETISAPE EYRAAAEAFA RADMAWCGTM SFDTAGRTMM GVTSSAFVEL ASGLPNPPLG FGANCGTGAA DLLRTLQGLA AHTPAQALIA KGNAGIPKYV DGHIHYDGTP ELMADYAVMA RNSGATIIGG CCGTMPDHLS AMRKALETRP SADKPSHQDI TKALGAFSSE TDGTEPGGAP PTRVRRGRRK // ID E1ARJ6_STRAU Unreviewed; 1163 AA. AC E1ARJ6; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 01-APR-2015, entry version 24. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADM72815.1}; OS Streptomyces aureofaciens. OG Plasmid pSA3239 {ECO:0000313|EMBL:ADM72815.1}. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1894 {ECO:0000313|EMBL:ADM72815.1}; RN [1] {ECO:0000313|EMBL:ADM72815.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCM3239 {ECO:0000313|EMBL:ADM72815.1}; RC PLASMID=pSA3239 {ECO:0000313|EMBL:ADM72815.1}; RX PubMed=12384301; DOI=10.1016/S0378-1119(02)00889-2; RA Novakova R., Bistakova J., Homerova D., Rezuchova B., Kormanec J.; RT "Cloning and characterization of a polyketide synthase gene cluster RT involved in biosynthesis of a proposed angucycline-like polyketide RT auricin in Streptomyces aureofaciens CCM 3239."; RL Gene 297:197-208(2002). RN [2] {ECO:0000313|EMBL:ADM72815.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCM3239 {ECO:0000313|EMBL:ADM72815.1}; RC PLASMID=pSA3239 {ECO:0000313|EMBL:ADM72815.1}; RX PubMed=16079347; DOI=10.1099/mic.0.28019-0; RA Novakova R., Homerova D., Feckova L., Kormanec J.; RT "Characterization of a regulatory gene essential for the production of RT the angucycline-like polyketide antibiotic auricin in Streptomyces RT aureofaciens CCM 3239."; RL Microbiology 151:2693-2706(2005). RN [3] {ECO:0000313|EMBL:ADM72815.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCM3239 {ECO:0000313|EMBL:ADM72815.1}; RC PLASMID=pSA3239 {ECO:0000313|EMBL:ADM72815.1}; RX PubMed=20490753; DOI=10.1007/s12223-010-0018-5; RA Novakova R., Odnogova Z., Kutas P., Feckova L., Kormanec J.; RT "Identification and characterization of an indigoidine-like gene for a RT blue pigment biosynthesis in Streptomyces aureofaciens CCM 3239."; RL Folia Microbiol. (Praha) 55:119-125(2010). RN [4] {ECO:0000313|EMBL:ADM72815.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCM3239 {ECO:0000313|EMBL:ADM72815.1}; RC PLASMID=pSA3239 {ECO:0000313|EMBL:ADM72815.1}; RX PubMed=20466770; DOI=10.1099/mic.0.037895-0; RA Novakova R., Kutas P., Feckova L., Kormanec J.; RT "The role of the TetR-family transcriptional regulator Aur1R in RT negative regulation of the auricin gene cluster in Streptomyces RT aureofaciens CCM 3239."; RL Microbiology 156:2374-2383(2010). RN [5] {ECO:0000313|EMBL:ADM72815.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCM3239 {ECO:0000313|EMBL:ADM72815.1}; RC PLASMID=pSA3239 {ECO:0000313|EMBL:ADM72815.1}; RX PubMed=21393365; DOI=10.1099/mic.0.047795-0; RA Novakova R., Rehakova A., Kutas P., Feckova L., Kormanec J.; RT "The role of two SARP family transcriptional regulators in regulation RT of the auricin gene cluster in Streptomyces aureofaciens CCM 3239."; RL Microbiology 157:1629-1639(2011). RN [6] {ECO:0000313|EMBL:ADM72815.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCM3239 {ECO:0000313|EMBL:ADM72815.1}; RC PLASMID=pSA3239 {ECO:0000313|EMBL:ADM72815.1}; RX PubMed=23373695; DOI=10.1111/1574-6968.12095; RA Novakova R., Knirschova R., Farkasovsky M., Feckova L., Rehakova A., RA Mingyar E., Kormanec J.; RT "The gene cluster aur1 for the angucycline antibiotic auricin is RT located on a large linear plasmid pSA3239 in Streptomyces aureofaciens RT CCM 3239."; RL FEMS Microbiol. Lett. 342:130-137(2013). RN [7] {ECO:0000313|EMBL:ADM72815.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCM3239 {ECO:0000313|EMBL:ADM72815.1}; RC PLASMID=pSA3239 {ECO:0000313|EMBL:ADM72815.1}; RX PubMed=24265028; DOI=10.1007/s00253-013-5373-0; RA Kormanec J., Novakova R., Mingyar E., Feckova L.; RT "Intriguing properties of the angucycline antibiotic auricin and RT complex regulation of its biosynthesis."; RL Appl. Microbiol. Biotechnol. 98:45-60(2014). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; KJ396772; ADM72815.1; -; Genomic_DNA. DR RefSeq; WP_031943712.1; NC_024970.1. DR RefSeq; YP_009060645.1; NC_024970.1. DR GeneID; 20473424; -. DR KEGG; pg:20473424; -. DR KO; K00548; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Plasmid {ECO:0000313|EMBL:ADM72815.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 230 230 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 296 296 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 297 297 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 740 740 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1163 AA; 126769 MW; 92363675A9AB8983 CRC64; MTTHQTRADA LREALATRVV VADGAMGTML QAQDPTMEDF QQLEGCNEVL NVTRPDIVRS VHEAYYSVGV DCVETNTFGA NFAALAEYDI PERNFELSEA GARIAREVAD EFTASTGQQR WVLGSIGPGT KLPTLGHITY AQIRDAYQIN AEGLISGGAD ALLVETTQDL LQTKSSIIGA RRAMEALGVS VPLICSVTVE TTGTMLLGSE IGAALTALEP LGIDMIGLNC ATGPAEMSEH LRYLARNARI PLSCMPNAGL PVLTKQGAHY PLSAPELADA QETFVREYGL SLVGGCCGTT PEHLRQVVER VRGTAVTARS PQPEPGAASL YQTVPFRQDT SYMAIGERTN ANGSKKFREA MLEARWDDCV EMARDQIREG AHMLDLCVDY VGRDGVADMQ ELAGRFATAS TLPIVLDSTE VPVIQAGLEK LGGRAVINSV NYEDGDGPES RFAKVTQLAR EHGAALIALT IDEEGQARTV GHKVAIAERL IADLTGNWGI RESDILIDTL TFTICTGQEE SRKDGIATIE SIRELKRRHP DVQTTLGLSN ISFGLNPAAR VLLNSVFLDE CVKAGLDSAI VHASKILPIA RFDEEQVTTA LDLIYDRREG DYDPLQKLMA LFEGVNTKSL KAGRAEELLA LPLDERLQRR IIDGEKNGLE ADLDEALRTR PALDIVNDTL LEGMKVVGEL FGSGQMQLPF VLQSAEVMKT AVAYLEPHME KTDDEGKGTI VLATVRGDVH DIGKNLVDII LTNNGYNVVN IGIKQPVSAI LEAAQEHKAD VIGMSGLLVK STVIMKENLE ELNARGLGSR FPVILGGAAL TRAYVEQDLH EIYEGEVRYA RDAFEGLRLM DALIAVKRGV PGATLPPLKQ RRVPPTGLVL EERPEEPPAR SDVAADNPVP APPFLGTRVV KGIPLKDYAS WLDEQALFKG QWGLKQARGG PSYEELVETE GRPRLRGWLD RLHTDNLLEA AVVHGYFPCV SKGDDLIILD EDGSERTRFT FPRQSRGRHL CLSDYVRPED SGETDVVALQ VVTMGSKIGE ATAKLFEADA YRDYMELHGL SVQLAEALAE YWHARVRAEL GIDGSDPASV DGMFRTEYQG CRYSLGYPAC PELADRAKIA DLLRPERIGV HLSEEFQLHP EQSTDAIVIH HPEATYFNAG GRS // ID E1AW41_LATJA Unreviewed; 401 AA. AC E1AW41; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 04-MAR-2015, entry version 16. DE SubName: Full=Betaine homocysteine methyltransferase {ECO:0000313|EMBL:ADM32900.1}; OS Lateolabrax japonicus (Japanese sea perch) (Japanese sea bass). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Pempheriformes; Lateolabracidae; Lateolabrax. OX NCBI_TaxID=8164 {ECO:0000313|EMBL:ADM32900.1}; RN [1] {ECO:0000313|EMBL:ADM32900.1} RP NUCLEOTIDE SEQUENCE. RA Qian X.Y., Song J.J., Qian L.; RT "Cloning of betaine homocysteine methyltransferase mRNA from RT Lateolabrax japonicus."; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HQ008859; ADM32900.1; -; mRNA. DR UniPathway; UPA00051; UER00083. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000313|EMBL:ADM32900.1}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000313|EMBL:ADM32900.1}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 210 210 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 292 292 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 401 AA; 44326 MW; 8F7213FE73479E04 CRC64; MAPVKKGILE RLNAGEVVIG DGGFVFALEK RGYVKAGPWT PEATVTHPEA VRQLHREFLR AGSNIMQTFT FYASDDKLEN WGQTLKISGA QINEAACDLA REVASEGDAL VAGGVSQTPS YLSCKSETEV KAIFKKQLEV FMKKNVDFLI AEYFEHVEEA EWAVQVLKTS GKPVAASMCI GPEGDMHGVS PGECAVRLVK AGAQIVGVNC HFDPMTCVKT VKMMKEGVEK AGLKAHYMVQ PLAFHTPDCN CQGFIDLPEF PFALEPRILT RWDMHTYARE AYKVGIRYIG GCCGFEPYHI RALTEELAPE RGIMPPGSEK HGMWGAGLEM HTKPWVRARA RRDYWEQLLP ASGRPKCASM STPEGWGVTK GHADLLQHKE ATTTQEMKHV LEKQKKAKSS A // ID E1BSH9_CHICK Unreviewed; 405 AA. AC E1BSH9; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 35. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGALP00000007182}; GN Name=BHMT {ECO:0000313|Ensembl:ENSGALP00000007182}; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; OC Phasianidae; Phasianinae; Gallus. OX NCBI_TaxID=9031 {ECO:0000313|Ensembl:ENSGALP00000007182, ECO:0000313|Proteomes:UP000000539}; RN [1] {ECO:0000313|Ensembl:ENSGALP00000007182, ECO:0000313|Proteomes:UP000000539} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Red jungle fowl {ECO:0000313|Ensembl:ENSGALP00000007182, RC ECO:0000313|Proteomes:UP000000539}; RX PubMed=15592404; DOI=10.1038/nature03154; RG International Chicken Genome Sequencing Consortium; RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., RA Ponting C.P., Bork P., Burt D.W., Groenen M.A.M., Delany M.E., RA Dodgson J.B., Chinwalla A.T., Cliften P.F., Clifton S.W., RA Delehaunty K.D., Fronick C., Fulton R.S., Graves T.A., Kremitzki C., RA Layman D., Magrini V., McPherson J.D., Miner T.L., Minx P., Nash W.E., RA Nhan M.N., Nelson J.O., Oddy L.G., Pohl C.S., Randall-Maher J., RA Smith S.M., Wallis J.W., Yang S.-P., Romanov M.N., Rondelli C.M., RA Paton B., Smith J., Morrice D., Daniels L., Tempest H.G., RA Robertson L., Masabanda J.S., Griffin D.K., Vignal A., Fillon V., RA Jacobbson L., Kerje S., Andersson L., Crooijmans R.P., Aerts J., RA van der Poel J.J., Ellegren H., Caldwell R.B., Hubbard S.J., RA Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M., Arakawa H., RA Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K., RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E., RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M., RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., RA Miller M.M., Inoko H., Shiina T., Kaufman J., Salomonsen J., RA Skjoedt K., Wong G.K.-S., Wang J., Liu B., Wang J., Yu J., Yang H., RA Nefedov M., Koriabine M., Dejong P.J., Goodstadt L., Webber C., RA Dickens N.J., Letunic I., Suyama M., Torrents D., von Mering C., RA Zdobnov E.M., Makova K., Nekrutenko A., Elnitski L., Eswara P., RA King D.C., Yang S.-P., Tyekucheva S., Radakrishnan A., Harris R.S., RA Chiaromonte F., Taylor J., He J., Rijnkels M., Griffiths-Jones S., RA Ureta-Vidal A., Hoffman M.M., Severin J., Searle S.M.J., Law A.S., RA Speed D., Waddington D., Cheng Z., Tuzun E., Eichler E., Bao Z., RA Flicek P., Shteynberg D.D., Brent M.R., Bye J.M., Huckle E.J., RA Chatterji S., Dewey C., Pachter L., Kouranov A., Mourelatos Z., RA Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M., RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O., RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., RA Betran E., Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., RA Furey T.S., Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., RA Eyras E., Castelo R., Abril J.F., Castellano S., Camara F., Parra G., RA Guigo R., Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., RA Mardis E.R., Wilson R.K.; RT "Sequence and comparative analysis of the chicken genome provide RT unique perspectives on vertebrate evolution."; RL Nature 432:695-716(2004). RN [2] {ECO:0000313|Ensembl:ENSGALP00000007182} RP IDENTIFICATION. RC STRAIN=Red jungle fowl {ECO:0000313|Ensembl:ENSGALP00000007182}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSGALP00000007182}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AC187364; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_414685.1; XM_414685.3. DR ProteinModelPortal; E1BSH9; -. DR PRIDE; E1BSH9; -. DR Ensembl; ENSGALT00000007194; ENSGALP00000007182; ENSGALG00000004518. DR GeneID; 416371; -. DR CTD; 635; -. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; E1BSH9; -. DR OMA; WGVTKGT; -. DR OrthoDB; EOG79GT7C; -. DR PhylomeDB; E1BSH9; -. DR TreeFam; TF329202; -. DR Reactome; REACT_340922; Sulfur amino acid metabolism. DR UniPathway; UPA00051; UER00083. DR NextBio; 20819838; -. DR PRO; PR:E1BSH9; -. DR Proteomes; UP000000539; Chromosome Z. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IBA:GO_Central. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR GO; GO:0033528; P:S-methylmethionine cycle; IBA:GO_Central. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000539}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Reference proteome {ECO:0000313|Proteomes:UP000000539}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 219 219 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 301 301 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 302 302 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 405 AA; 45011 MW; C28596F734698E69 CRC64; MLPIAKSLKQ GKRGILERLD AGEIVIGDGG FVFALEKRGY VKAGPWTPEA TVEHPEAVRQ LHREFLRAGS NVLQTFTFYA SEDKLENRGN YVAEKITCQK VNEAACDIAR EVANEGDALV AGGVSQTPSY LSCKDKAEVK AVFRKQLDIF MKKNVDFLIA EYFEHVEEAV WAVEVLKESG KPVAATMCIG PEGDMHGVPP GQCAVQLVKA GASIVGVNCH FDPDTVLETV KLMKEGLQAA KLKAHLMSQP LAFHTPDCGK QGFIDLPEFP FGLEPRIITR WDVQKYARKA YDLGIRYIGG CCGFEPYHVR AIAEELAPER GFLPEASEKH GSWGNSLSMH TKPWVRARAR KEYWENLKPA SGRPYCPSMS KPDGWGVTKG ARELMQQKEA TTEQQLKELF QKQKV // ID E1FVW1_LOALO Unreviewed; 316 AA. AC E1FVW1; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 07-JAN-2015, entry version 21. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFO23447.1}; GN ORFNames=LOAG_05038 {ECO:0000313|EMBL:EFO23447.1}; OS Loa loa (Eye worm) (Filaria loa). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Spirurida; OC Filarioidea; Onchocercidae; Loa. OX NCBI_TaxID=7209 {ECO:0000313|EMBL:EFO23447.1, ECO:0000313|Proteomes:UP000007040}; RN [1] {ECO:0000313|Proteomes:UP000007040} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG The Broad Institute Genome Sequencing Platform; RA Nutman T.B., Fink D.L., Russ C., Young S., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., 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., 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 Loa loa."; 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; JH712222; EFO23447.1; -; Genomic_DNA. DR RefSeq; XP_003140623.1; XM_003140575.1. DR EnsemblMetazoa; EFO23447.1; EFO23447.1; LOAG_05038. DR GeneID; 9942443; -. DR KEGG; loa:LOAG_05038; -. DR CTD; 9942443; -. DR InParanoid; E1FVW1; -. DR KO; K00547; -. DR Proteomes; UP000007040; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007040}; KW Reference proteome {ECO:0000313|Proteomes:UP000007040}. SQ SEQUENCE 316 AA; 34903 MW; B10C4E7383CB8DB2 CRC64; MDACFTWEKV QLLDGGFGTE LEAAGYNVKN HSLWSCAALF DNPNLILQVH KRFIEAGSDI ILTNTYQACI STMMNSRGMT KIAAESSLKK LVSLAQQAVD ECSAREKVKV VGSVGPYGVI FNDGSEYSGH YVDELEEQVL VDYHIQQTIP LLQAGLKVIA YETVPSYKEA VAILKAVNAI NHSYNFWISF SCKNGEQTNH NESFCKSVEK ISHHPNILGI GINCTSPNYI TQLLQSASIS VNSLPFIVYP NSGEEYECGT KKWRNGKCIF PDMGQLMEWK NLGMKVVGGC CRVGAEKIKE LSTLVAKLNS EYNSVS // ID E1HKQ0_ECOLX Unreviewed; 1227 AA. AC E1HKQ0; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFK91492.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFK91492.1}; GN Name=metH {ECO:0000313|EMBL:EFK91492.1}; GN ORFNames=HMPREF9543_01628 {ECO:0000313|EMBL:EFK91492.1}; OS Escherichia coli MS 146-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=749540 {ECO:0000313|EMBL:EFK91492.1}; RN [1] {ECO:0000313|EMBL:EFK91492.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 146-1 {ECO:0000313|EMBL:EFK91492.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFK91492.1}. 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; ADTN01000099; EFK91492.1; -; Genomic_DNA. DR RefSeq; WP_000096006.1; NZ_GG772091.1. DR EnsemblBacteria; EFK91492; EFK91492; HMPREF9543_01628. DR PATRIC; 41787859; VBIEscCol151630_1567. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFK91492.1}; KW Transferase {ECO:0000313|EMBL:EFK91492.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135967 MW; 4F820DCAF3A4B1D6 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEAGIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAD // ID E1I911_ECOLX Unreviewed; 1227 AA. AC E1I911; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 32. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFK71193.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFK71193.1}; GN Name=metH {ECO:0000313|EMBL:EFK71193.1}; GN ORFNames=HMPREF9535_04915 {ECO:0000313|EMBL:EFK71193.1}; OS Escherichia coli MS 78-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=749532 {ECO:0000313|EMBL:EFK71193.1}; RN [1] {ECO:0000313|EMBL:EFK71193.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 78-1 {ECO:0000313|EMBL:EFK71193.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFK71193.1}. 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; ADTY01000396; EFK71193.1; -; Genomic_DNA. DR RefSeq; WP_000096011.1; NZ_GG773337.1. DR ProteinModelPortal; E1I911; -. DR SMR; E1I911; 6-639, 651-1227. DR PRIDE; E1I911; -. DR EnsemblBacteria; EFK71193; EFK71193; HMPREF9535_04915. DR PATRIC; 41845720; VBIEscCol151935_4564. DR OMA; DYNSIMV; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFK71193.1}; KW Transferase {ECO:0000313|EMBL:EFK71193.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135997 MW; 91F0CAA1E9127D9A CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAD // ID E1ICX9_9CHLR Unreviewed; 318 AA. AC E1ICX9; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFO80949.1}; GN ORFNames=OSCT_1180 {ECO:0000313|EMBL:EFO80949.1}; OS Oscillochloris trichoides DG-6. OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae; OC Oscillochloridaceae; Oscillochloris. OX NCBI_TaxID=765420 {ECO:0000313|EMBL:EFO80949.1}; RN [1] {ECO:0000313|EMBL:EFO80949.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DG-6 {ECO:0000313|EMBL:EFO80949.1}; RX PubMed=21037015; DOI=10.1128/JB.00931-10; RA Kuznetsov B.B., Ivanovsky R.N., Keppen O.I., Sukhacheva M.V., RA Bumazhkin B.K., Patutina E.O., Beletsky A.V., Mardanov A.V., RA Baslerov R.V., Panteleeva A.N., Kolganova T.V., Ravin N.V., RA Skryabin K.G.; RT "Draft genome sequence of the anoxygenic filamentous phototrophic RT bacterium Oscillochloris trichoides subsp. DG-6."; RL J. Bacteriol. 193:321-322(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. {ECO:0000313|EMBL:EFO80949.1}. 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; ADVR01000033; EFO80949.1; -; Genomic_DNA. DR RefSeq; WP_006561740.1; NZ_GL501403.1. DR EnsemblBacteria; EFO80949; EFO80949; OSCT_1180. DR PATRIC; 42087640; VBIOscTri160367_1336. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFO80949.1}; KW Transferase {ECO:0000313|EMBL:EFO80949.1}. SQ SEQUENCE 318 AA; 34608 MW; 40AC6A7BAD327DBC CRC64; MNPIDTILQN FGLVILDGAL ATELERRGAD LNDPLWSARL LLEEPDLIRE VHADYFRAGA DCAITASYQA TFPGFARRGL GHQAASELMR RSVRLACDAR DAVWATLDHT RRPHPLVAAS IGPYGAFLHD GSEYRGDYTI SDADLLAFHR PRMAVLSDAG ADLLALETIP SFREAQLLLR LLEEFPQTWA WMSFSARDGQ HISDGTPFAT CVAEIAQHPQ VAAVGVNCTA PGYVAELLRV ARDLTTKPLL AYPNSGEIYD PATHAWCGIA SVGDYAAEAQ KWYAEGASIL GGCCRTTPDH IRAIAAWARA AHQGAERV // ID E1IGB4_9CHLR Unreviewed; 1168 AA. AC E1IGB4; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFO79767.1}; GN ORFNames=OSCT_2365 {ECO:0000313|EMBL:EFO79767.1}; OS Oscillochloris trichoides DG-6. OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae; OC Oscillochloridaceae; Oscillochloris. OX NCBI_TaxID=765420 {ECO:0000313|EMBL:EFO79767.1}; RN [1] {ECO:0000313|EMBL:EFO79767.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DG-6 {ECO:0000313|EMBL:EFO79767.1}; RX PubMed=21037015; DOI=10.1128/JB.00931-10; RA Kuznetsov B.B., Ivanovsky R.N., Keppen O.I., Sukhacheva M.V., RA Bumazhkin B.K., Patutina E.O., Beletsky A.V., Mardanov A.V., RA Baslerov R.V., Panteleeva A.N., Kolganova T.V., Ravin N.V., RA Skryabin K.G.; RT "Draft genome sequence of the anoxygenic filamentous phototrophic RT bacterium Oscillochloris trichoides subsp. DG-6."; RL J. Bacteriol. 193:321-322(2011). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFO79767.1}. 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; ADVR01000103; EFO79767.1; -; Genomic_DNA. DR RefSeq; WP_006562928.1; NZ_GL501404.1. DR EnsemblBacteria; EFO79767; EFO79767; OSCT_2365. DR PATRIC; 42090255; VBIOscTri160367_2614. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 233 233 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 749 749 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1168 AA; 126564 MW; 9FBA93477E06070C CRC64; MTKPTYLQAL AERVLIFDGA MGTSIDTFNL TVEDYGGEAT NGNRDYLVMT RPDVIGQIHA SYLEAGADVI ETCTFQSTRL RLEEWGLGER TVELNQAAAT LARSVADRFA AQDGRPRFVA GSMGPTGKLP SSDDPALSDI TFQQLSDIYR EQATGLIQGG VDLLLVETSV DVLEVKAALD GIRRAKADLN RPDVAVQAQV FLDLSGRMLL GTDVPALIAT LEAMPVDVIG LNCSTGPEHM REAIQYLTAH SRKPISCIPN AGLPLEVDGE TVYPMQPDEF SRILGEFVRD YGVAVVGGCC GTRPSHIAAV RETLGLNCPP KQREVDYIPS VSSGIRAAAL RQEGTLTLIG ERVNTLGSRK VKRLLLSDNY DGVVEVAREQ VDNGAHLLDV CVAMTERSDE SVQMNALLKK LTMNIELPLV IDTTETDVLE QALAMYPGRA VVNSLSLEGG RGGKIDKVLP LVARYGAATM AMTIDEEGMC HTRERKLAVA ERIAQIARDE YGVPAEALIF DVLTFPITTG QEELRNAAVE TIEGIRLVKE RIPGCFTTLG VSNLSFGVAA HARAALNSVF LFHAMAAGLD TAIINPAHIT PYTEIPAEQR EICEDLIFNR REDALARFIG YFEQHQASPE QEGANDPTAG LSVDERLHWK ILHRKKEGVE ADIEEAVANR EAAGMARGVA AVEVLNNVLL PAMKQVGDLF GAGQLILPFV LQSAEVMKKA VARLEHYLEK MEGSTKGKVL LATVLGDVHD IGKNLVNTIL ANNGYTVYDL GKQVPVNTII EQAIELQVDA IGLSALLVST SKQMPLVVQE LHQRGMNLPV LVGGAAINKQ FGQRTSFVAE NTAYAGGVFY CKDAFEGLEA MDRLSDPNGR AAYIAASLEA AAAGLGKRTV GAAALNSVGA SGPRSQVRSD VPVPTPPFWG AKATKRIRLE DVAAHLDHNA LFRLQWGAKN AKGAEWEALK AEFETRLRDL LRSAERDGWL EPQVAYGYFP VQSAGQELVV YDPASVQSGA PRELTRFSFP RQIDREHLCL ADYFRSVESG TYDLGVFQLV TVGPRADALS QQLQADGDYS QSYYVHGLAV SMAEALAEYT NQIVRQGLGL GEGRGKRYSW GYPSCPDLAE HTKLFAILPA EQIGLSLTEA YQLVPEQSTA ALVVHHPEAK YFSIGSAE // ID E1IS99_ECOLX Unreviewed; 1227 AA. AC E1IS99; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 32. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFO57739.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFO57739.1}; GN Name=metH {ECO:0000313|EMBL:EFO57739.1}; GN ORFNames=HMPREF9348_03031 {ECO:0000313|EMBL:EFO57739.1}; OS Escherichia coli MS 145-7. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=679204 {ECO:0000313|EMBL:EFO57739.1}; RN [1] {ECO:0000313|EMBL:EFO57739.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 145-7 {ECO:0000313|EMBL:EFO57739.1}; 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 (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFO57739.1}. 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; ADWS01000015; EFO57739.1; -; Genomic_DNA. DR RefSeq; WP_000096011.1; NZ_ADWS01000015.1. DR ProteinModelPortal; E1IS99; -. DR SMR; E1IS99; 6-639, 651-1227. DR PRIDE; E1IS99; -. DR EnsemblBacteria; EFO57739; EFO57739; HMPREF9348_03031. DR PATRIC; 42098121; VBIEscCol143813_2945. DR OMA; DYNSIMV; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFO57739.1}; KW Transferase {ECO:0000313|EMBL:EFO57739.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135997 MW; 91F0CAA1E9127D9A CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAD // ID E1J2Z9_ECOLX Unreviewed; 1227 AA. AC E1J2Z9; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFK69656.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFK69656.1}; GN Name=metH {ECO:0000313|EMBL:EFK69656.1}; GN ORFNames=HMPREF9347_01255 {ECO:0000313|EMBL:EFK69656.1}; OS Escherichia coli MS 124-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=679205 {ECO:0000313|EMBL:EFK69656.1}; RN [1] {ECO:0000313|EMBL:EFK69656.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 124-1 {ECO:0000313|EMBL:EFK69656.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFK69656.1}. 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; ADWT01000007; EFK69656.1; -; Genomic_DNA. DR RefSeq; WP_000096053.1; NZ_ADWT01000007.1. DR EnsemblBacteria; EFK69656; EFK69656; HMPREF9347_01255. DR PATRIC; 41089309; VBIEscCol139996_1196. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFK69656.1}; KW Transferase {ECO:0000313|EMBL:EFK69656.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136040 MW; D1A76336C7330E3D CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID E1JLQ5_9LACO Unreviewed; 307 AA. AC E1JLQ5; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFK80144.1}; GN ORFNames=HMPREF9269_1771 {ECO:0000313|EMBL:EFK80144.1}; OS Lactobacillus salivarius ACS-116-V-Col5a. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=768728 {ECO:0000313|EMBL:EFK80144.1}; RN [1] {ECO:0000313|EMBL:EFK80144.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ACS-116-V-Col5a {ECO:0000313|EMBL:EFK80144.1}; RA Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., Nelson K.E.; RT "Genome Sequence of Lactobacillus salivarius ACS-116-V-Col5a."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFK80144.1}. 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; AEBA01000058; EFK80144.1; -; Genomic_DNA. DR RefSeq; WP_003702665.1; NZ_AEBA01000058.1. DR EnsemblBacteria; EFK80144; EFK80144; HMPREF9269_1771. DR PATRIC; 41148550; VBILacSal164140_0653. DR OrthoDB; EOG6C019S; -. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EFK80144.1}; KW Transferase {ECO:0000313|EMBL:EFK80144.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 223 223 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 307 AA; 34542 MW; E3A5A3D7ECCC4C81 CRC64; MDFTEFLTNN PVVLDGAMST PLEKLGADTN NDLWTAKALI DNEELVYEVH KMYFEAGADL IITDTYQANV QAFEKVGYSE KEARNLIKKA VKIAQKARDD YENRTGKHNY IAGTIGPYGA YLANGSEYRG DYELSVEEYQ QFHLPRIEEL VNAEVDILAI ETQPKLDEVL AILELLKEKY PQQKVYVSYT LSDDDTISDG TPLPRAIHAL EDYSQVIAVG INCVKLELVE PALKNMKEIT DKHLIVYPNS SAVYDPKSKT WSQPKTSATF EELIPNWYEA GARIIGGCCT TGPKEIKAVA DFIKRNR // ID E1K0Y3_DESFR Unreviewed; 802 AA. AC E1K0Y3; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFL49748.1}; GN ORFNames=DesfrDRAFT_3533 {ECO:0000313|EMBL:EFL49748.1}; OS Desulfovibrio fructosivorans JJ. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=596151 {ECO:0000313|EMBL:EFL49748.1}; RN [1] {ECO:0000313|EMBL:EFL49748.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=JJ {ECO:0000313|EMBL:EFL49748.1}; 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., 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFL49748.1}. 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; AECZ01000034; EFL49748.1; -; Genomic_DNA. DR RefSeq; WP_005996130.1; NZ_AECZ01000034.1. DR EnsemblBacteria; EFL49748; EFL49748; DesfrDRAFT_3533. DR PATRIC; 41171831; VBIDesFru57976_3631. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFL49748.1}; KW Transferase {ECO:0000313|EMBL:EFL49748.1}. SQ SEQUENCE 802 AA; 83766 MW; 38F3B2D6567708D5 CRC64; MGDFRKALTD AGLLVFDGAM GTLLQGRGLA PGQSPELFGL SHPEAIVATH REYIEAGSRV ITANTFGGSR YKLPAGTDVV ALNREMAHLA RQAAGSTAFV AGSVGPTGQF VAPLGKVTLR ELVAAFVEQI RGLAAGGCDL IVGETHFDVA EAKALVLACR EVCDLPVAVC MTYEGAASLT GSAPEVFVDV MENLGVDLIG VNCGAGPDDM RHVGEVYSRR LSTPFFVKPN AGMPRLENGQ TVFPMGPEEF AEKTARFADL GAKALSGCCG TTPAHIAALA KALSGRSWTR PEAPDRPVLA VASRALTVAL GGKSPCAVIG ERINPTGKAE LAAELVAGEY AKALAFAEEQ AAAGASILDV NVGAPMVDET KTLPGLALEL TKRQRLPLCL DSNNAEALTN ALWASPATPL VNSISGEPGR MELLGPLCRD HGAPFILLPL KGRKLPVTAA ERLAIIEELL AQAESLRIPR RLILVDALAL TVSSKAEAGL ACLETIRHCR EAWGLPTVLG LSNISFGLPA RELVNAAFFA MCLGAGLAAA IANPNVARLM ETGAACEVLL DRDPQAGRFI ERYAGWKSSS SGGGSAPAAA AKSEEGGSPL RQAVIKGRRA ELDGLIDAAL AEGRSPASIL SEELIPGIME VGERYERKEF FLPQLLVAAE TMRAGFTRLE PLLAETSGAE KARIVMATVE GDIHDIGKNI VCLMLKNHGF EVIDLGKDVP AARIVDEAQQ RKADIIGLSA LMTTTMVRME DTVRLVKERG LTAKVMVGGA VVTAAFAKSI GADAHAADAV DAVRQAKALI GG // ID E1K2N6_DESFR Unreviewed; 610 AA. AC E1K2N6; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 25. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=DesfrDRAFT_4136 {ECO:0000313|EMBL:EFL49125.1}; OS Desulfovibrio fructosivorans JJ. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=596151 {ECO:0000313|EMBL:EFL49125.1}; RN [1] {ECO:0000313|EMBL:EFL49125.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=JJ {ECO:0000313|EMBL:EFL49125.1}; 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., 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Note=FAD.; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {ECO:0000256|RuleBase:RU004255}. CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFL49125.1}. 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; AECZ01000066; EFL49125.1; -; Genomic_DNA. DR RefSeq; WP_005997217.1; NZ_AECZ01000066.1. DR ProteinModelPortal; E1K2N6; -. DR EnsemblBacteria; EFL49125; EFL49125; DesfrDRAFT_4136. DR PATRIC; 41173133; VBIDesFru57976_4263. DR UniPathway; UPA00193; -. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004255}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EFL49125.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EFL49125.1}. SQ SEQUENCE 610 AA; 65172 MW; 00448E7F65D6E6BF CRC64; MRHDLLTTLA KRPVLADGAM GTQLLARGAA PTACLDALNL DAPEMVRSIH LDYLAAGAEV IETNTFGANR KKLERFELAD KVLEINRQGA ALARACAGDD AWVAGAMGPL GRMREEAPDP AEIAALYAEQ ARALAEGGAD LLLLETFFDF ELLRLALHAA KSATSLPVAA QFVFGGTGLS LSGHTMAECL RLLRREGADI VGLNCGSGPQ GALDILRAAG PLEGPLSVFP NAGFPERRGD RLVYPSSPEY FASVLVQCAD HGARLLGGCC GTGPEHIRAL GQALAHRAGT APRQAAVAPG PDTAATGRQP GKPRPCFLDR VGKGPLFLVE LDPPKHLDVS GTLEGAASLA SGGADAITIA ENPLASPRLS NIALANLIRA RTDVEVIVHL TGRDRNLIGM QSTIMGLACL GLENVLAITG DPPSSGGEER LSGVYDVRSY ELIGMLDCFN KGQDPQGRDM RLRTNFRIGA AFNPNTRNMA MQVRRMRRKA ELGAAYFLTQ PVYSREKVDA ILEETRDFPC PIFLGIMPLA SLRNAEFLHN EFPGISIPED VRDRLRAAGD GEAREGLEIA WELMAYALPH FAGIYLIPPF NRHAVALELI RRARGDVPAS // ID E1L4R0_9FIRM Unreviewed; 810 AA. AC E1L4R0; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFL56683.1}; GN ORFNames=HMPREF9321_0823 {ECO:0000313|EMBL:EFL56683.1}; OS Veillonella atypica ACS-049-V-Sch6. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Veillonella. OX NCBI_TaxID=866776 {ECO:0000313|EMBL:EFL56683.1}; RN [1] {ECO:0000313|EMBL:EFL56683.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ACS-049-V-Sch6 {ECO:0000313|EMBL:EFL56683.1}; 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. {ECO:0000313|EMBL:EFL56683.1}. 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; AEDR01000016; EFL56683.1; -; Genomic_DNA. DR RefSeq; WP_005375882.1; NZ_AEDR01000016.1. DR EnsemblBacteria; EFL56683; EFL56683; HMPREF9321_0823. DR PATRIC; 41224895; VBIVeiAty166341_0330. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFL56683.1}; KW Transferase {ECO:0000313|EMBL:EFL56683.1}. SQ SEQUENCE 810 AA; 86774 MW; D8A7A0F44E0FB443 CRC64; MYIFDGAMGT MLQAAGLEEG YCPELFNVEK PEVVKNIHAQ YLQHGSDVIT TNTFGACSLK LEDYDLQDRV REINIAAVKV AKEAIAEVKP SARVAGSMGP TGRFLQPLGN MSFDDIYDTY KEQADALIEG GVDFIIIETI IDVQEMRAAL LASLDAREAA GKTKEDIQII CQFSFSEDGR TITGTPPEVA TTIVEAMGAD IIGINCSLGP EQIKPLIEEI ASVTNLPISC QPNAGMPQLI NKQTVFPLSA EDMGPLMIPI VDAGASYVGG CCGTTPAHIQ SISDAVKAHT PKERAHIEPK TVITSRTKLI ELGHNVKPLI IGERINPTGR KVLAQELRDG SFIRVKRDAL DQVEAGADIL DVNMGVAGMD QTPLMEKAIF ELSMLVETPL SIDTLDPAAM EVALKNYPGR ALINSVNGEE ESITHVMPLA KRYGAALLCL PLSSGDLPEK AEDRVALAES IVNRAYNYDL QPHDLLLDPL VLTLASGEDS ARQTLKTLRL YKEKFGFPTV MGLSNISFGM PQRPYLNGQF LTMALASGLT TPIMNPLNYA AKKAFVSSST LLGWDPGSAE FIKEYGYEDE ATAPGNAAPK GPDKASFDSN DPLANIRACV EQGEKEAIVD LVKKALADGM DPLDITKKGL SEAMNVVGDK FGSGKLFLPQ VMLAAETMQA AFNTIKEIIP ASDSLDKGTV VVATVKGDIH DLGKNIVAAL LENNGYKIVD LGKDVDPEVI VQAIKDNKAA LVGICSLMTT TMPQIDNTIA AIRAAGLKTK VMVGGAVVSQ DYADQAGADI YAKDGIAAVN HANDFFETLK // ID E1L768_9FIRM Unreviewed; 339 AA. AC E1L768; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFL55777.1}; GN ORFNames=HMPREF9321_0879 {ECO:0000313|EMBL:EFL55777.1}; OS Veillonella atypica ACS-049-V-Sch6. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Veillonella. OX NCBI_TaxID=866776 {ECO:0000313|EMBL:EFL55777.1}; RN [1] {ECO:0000313|EMBL:EFL55777.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ACS-049-V-Sch6 {ECO:0000313|EMBL:EFL55777.1}; 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. {ECO:0000313|EMBL:EFL55777.1}. 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; AEDR01000037; EFL55777.1; -; Genomic_DNA. DR RefSeq; WP_005377633.1; NZ_AEDR01000037.1. DR EnsemblBacteria; EFL55777; EFL55777; HMPREF9321_0879. DR PATRIC; 41226674; VBIVeiAty166341_1181. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFL55777.1}; KW Transferase {ECO:0000313|EMBL:EFL55777.1}. SQ SEQUENCE 339 AA; 36953 MW; 05F89D4F6D114E97 CRC64; MAKRKAFLKI VKGNGPLVLD GAFGTELERH GCNIHDELWS SKMLIENPEI IKKVHISYLA AGADIIESSG YQATVAGFKA HGYGTEEALD LVKLSVRLAV QARNEFLEAK ANDALTLRGI TLGEQLPDGS VRYFSEGALP KPLVAASVGP YGAFLADGSE YRGDYGVQTE YLEVFHIPRI ALFCEENPDV LACETVPCYD EAIAIARALC DPLTTKGIPA WISFSCKDEH HISSGETIIK CAEMIDKVRQ VTGIGINCTA PEYVESLIKD IRSVTNKPIA VYPNLGETYD GEAKTWSGGQ QSFIDYVDVW RKAGANIIGG CCRTNPDIIQ EVAKQIHVK // ID E1L9Q3_9FIRM Unreviewed; 810 AA. AC E1L9Q3; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFL58666.1}; GN ORFNames=HMPREF9684_1516 {ECO:0000313|EMBL:EFL58666.1}; OS Veillonella atypica ACS-134-V-Col7a. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Veillonella. OX NCBI_TaxID=866778 {ECO:0000313|EMBL:EFL58666.1}; RN [1] {ECO:0000313|EMBL:EFL58666.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ACS-134-V-Col7a {ECO:0000313|EMBL:EFL58666.1}; 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. {ECO:0000313|EMBL:EFL58666.1}. 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; AEDS01000010; EFL58666.1; -; Genomic_DNA. DR RefSeq; WP_005379444.1; NZ_AEDS01000010.1. DR EnsemblBacteria; EFL58666; EFL58666; HMPREF9684_1516. DR PATRIC; 41228498; VBIVeiAty168093_0236. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFL58666.1}; KW Transferase {ECO:0000313|EMBL:EFL58666.1}. SQ SEQUENCE 810 AA; 86743 MW; 0A737A86D98B0D0C CRC64; MYIFDGAMGT MLQAAGLEEG YCPELFNVEK PEVVKNIHAQ YLQHGSDVIT TNTFGACSLK LEDYDLQDRV KEINIAAVKV AKEAISEFKP SARVAGSMGP TGRFLQPLGN MSFDSIYDTY REQAEALIEG GVDFIIIETI IDVQEMRAAL LASLDAREAA GKTKEDVQII CQFSFSEDGR TITGTPPEVA TTIVEAMGAD IIGINCSLGP EQITPLIEKI ASVTNLPISC QPNAGMPQLI NKQTVFPLSA EDMGPLMIPI VDAGASYVGG CCGTTPAHIQ SISDAVKAHT PKERAHIEPK TVITSRTKLL ELGHNVKPLI IGERINPTGR KVLAQELRDG SFIRVKRDAL DQVEAGADIL DVNMGVAGMD QTPLMEKAIF ELSMLVETPL SIDTLDPKAM EVALKNYPGR ALINSVNGEE ESITHVMPLA KRYGAALLCL PICSGDLPEK AEDRVALAES IVNRAYGYGL QPHDLLLDPL VLTLASGEDS ARQTLSTLRL YKEKFGFPTV MGLSNISFGM PQRPYLNGQF LTMALASGLT TPIMNPLNYA AKKAFVSSTT LLGWDPGSAE FIKEYGYEDE TTAPGNAAPK GPDKASFDSN DPLANIRACV EQGEKEAIVD LVKKALADGM DPLDITKKGL SEAMNVVGDK FGSGKLFLPQ VMLAAETMQA AFNTIKEIIP ASDSLDKGTV VVATVKGDIH DLGKNIVAAL LENNGYKIVD LGKDVDPEVI VQAIKDNKAA LVGICSLMTT TMPQIDNTIA AIRAAGLKTK VMVGGAVVSQ DYADQAGADI YAKDGIAAVN HANDFFETLK // ID E1LBD8_9FIRM Unreviewed; 339 AA. AC E1LBD8; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFL58144.1}; GN ORFNames=HMPREF9684_1409 {ECO:0000313|EMBL:EFL58144.1}; OS Veillonella atypica ACS-134-V-Col7a. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Veillonella. OX NCBI_TaxID=866778 {ECO:0000313|EMBL:EFL58144.1}; RN [1] {ECO:0000313|EMBL:EFL58144.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ACS-134-V-Col7a {ECO:0000313|EMBL:EFL58144.1}; 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. {ECO:0000313|EMBL:EFL58144.1}. 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; AEDS01000036; EFL58144.1; -; Genomic_DNA. DR RefSeq; WP_005380266.1; NZ_AEDS01000036.1. DR EnsemblBacteria; EFL58144; EFL58144; HMPREF9684_1409. DR PATRIC; 41229579; VBIVeiAty168093_0754. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFL58144.1}; KW Transferase {ECO:0000313|EMBL:EFL58144.1}. SQ SEQUENCE 339 AA; 37112 MW; 56FB165468C4B00C CRC64; MAKRKAFLKI VKENGPLVLD GAFGTELERH GCNIHDELWS SKMLIENPEI IKKVHISYLA AGADIIESSG YQATVAGFKA HGYGTEEALD LVKLSVRLAV QARNEFLEAK ANDALTLRGI TLGEQLPDGS VRYFSEGALP KPLVAASVGP YGAFLADGSE YRGDYGVQTE YLEVFHIPRI ALFCEENPDV LACETVPCYD EAIAIARTLC DPLTTKGIPA WISFSCKDEH HISNGETIIK CAEMIDKVRQ VTGIGINCTA PEYVESLIKD IRSVTNKPIA VYPNLGETYD GETKTWSGGQ QSFIDYVDVW RKAGANIIGG CCRTNPDIIQ EVAKQIHVK // ID E1NZ03_ARTGO Unreviewed; 1215 AA. AC E1NZ03; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 01-APR-2015, entry version 23. DE SubName: Full=Putative methionine synthase {ECO:0000313|EMBL:ADN91858.1}; GN Name=metH {ECO:0000313|EMBL:ADN91858.1}; OS Arthrobacter globiformis. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Micrococcaceae; Arthrobacter. OX NCBI_TaxID=1665 {ECO:0000313|EMBL:ADN91858.1}; RN [1] {ECO:0000313|EMBL:ADN91858.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NRRL B-2979 {ECO:0000313|EMBL:ADN91858.1}; RX PubMed=11422368; DOI=10.1046/j.1432-1327.2001.02239.x; RA Meskys R., Harris R.J., Casaite V., Basran J., Scrutton N.S.; RT "Organization of the genes involved in dimethylglycine and sarcosine RT degradation in Arthrobacter spp.: implications for glycine betaine RT catabolism."; RL Eur. J. Biochem. 268:3390-3398(2001). RN [2] {ECO:0000313|EMBL:ADN91858.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NRRL B-2979 {ECO:0000313|EMBL:ADN91858.1}; RA Casaite V., Bruzyte S., Meskys R.; RT "Arthrobacter globiformis N,N-dimethylglycine oxidase operon."; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AF329477; ADN91858.1; -; Genomic_DNA. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 239 239 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 769 769 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1215 AA; 131550 MW; C8C07893E4A184F0 CRC64; MPRFALDIES VPRPVRAQAL LDAVNHRVVI ADGAMGTMLQ GGLSLEKDFL GLEGCNEILN DTRPDVLADI HDAYFATGID AVETNTFGAN WSNLSDYGID DRIEELARKG AEIARERAEA AEKTDERMRW VLGSMGPGTK LPSLGHTSYD YLKQTFALQA EGLIDGGADA FLIETSQDLL QTKAAVNGCK QAIVSRGVRL PIFVEVTVET TGTMLMGSEI GAALTALEPL GVDAIGLNCA TGPDEMSEHL RHLSKQSSVA IACMPNAGLP VLGANGAHYP LSPSELATAH EQFVREFGLG LVGGCCGTTP EHMAAVVERL APFRASAAVT GGGRGTDGAR VPTEREAGIA SLYHHVPFDQ ESSYLAIGER TNANGSKAFR QAMLEERWDD CVDIAREQVR VGAHLLDVCI DYVGRDGVAD IKEVVSRFAS ASTLPLVIDS TEPPVLQAGL EHIGGRPVVN SVNYEDGDGP DSRFARIMPL VKEHGTAVIA LTIDEHGQAR TTEGKVAIAS RLIDSLVGEW GMRVEDIIVD ALTFPIATGQ EETRRDAIET IEAIRQITAK YPGIHTTLGV SNVSFGLNPA ARIVLNSVFL HEAVQAGLSS GIIDAAKIVP LASLPEEQRQ VALDLVWDRR EYDADGNVTY DPLARILDLY AGVDSAALKD QRAAELAALP TGERLQRRII DGEGKGLEED LDLARSEGMT PLGIINDQLL EGMKVVGERF GAGEMQLPFV LQSAEVMKNA VALLEPHMEK SDASGKGTMV IATVRGDVHD IGKNLVDIIL TNNGYKVINI GIKQPIADII AAAEEHDADV IGMSGLLVKS TVVMKENLAE LQSRGLAKKW PIILGGAALT RAYVEQDLAE QFEGTVRYAK DAFEGLALME PLVQVARGAA PDAVGLPPLK KRIHKGGAKL TVTEPEAMPG RSDVAADNPV PSPPFWGTRI VRGVALHDYA ALLDERATFM GQWGLKPGRG DDGDSYEELV EREGRPRLRY WLDRILAEGM LDASVAYGYF PVVSEGEQVV VLHHGEDHDG VLGTAGLLAP DGGSGGPIGT DRLRFDFPRQ RRDRHLCLAD FVRSRESGQI DVLPIQLVTA GSKIEEVTSE LFAGNHYRDY YELNGLVMQL TEALAEFWHA RIRSELGFAA EEPKDKAGYF KLDYRGARFS LGYPACPDME DRRKVTELLR PERMGVILSD ELMLHPEQST DAFVFHHPEA KYFKV // ID E1RA39_SPISS Unreviewed; 615 AA. AC E1RA39; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 31. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=Spirs_4285 {ECO:0000313|EMBL:ADK83358.1}; OS Spirochaeta smaragdinae (strain DSM 11293 / JCM 15392 / SEBR 4228). OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Spirochaeta. OX NCBI_TaxID=573413 {ECO:0000313|EMBL:ADK83358.1, ECO:0000313|Proteomes:UP000002318}; RN [1] {ECO:0000313|EMBL:ADK83358.1, ECO:0000313|Proteomes:UP000002318} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11293 / JCM 15392 / SEBR 4228 RC {ECO:0000313|Proteomes:UP000002318}; RX PubMed=21304743; RA Mavromatis K., Yasawong M., Chertkov O., Lapidus A., Lucas S., RA Nolan M., Del Rio T.G., Tice H., Cheng J.F., Pitluck S., Liolios K., RA Ivanova N., Tapia R., Han C., Bruce D., Goodwin L., Pati A., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., RA Detter J.C., Rohde M., Brambilla E., Spring S., Goker M., Sikorski J., RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Klenk H.P., Kyrpides N.C.; RT "Complete genome sequence of Spirochaeta smaragdinae type strain (SEBR RT 4228)."; RL Stand. Genomic Sci. 3:136-144(2010). CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ADK83358.1; -; Genomic_DNA. DR RefSeq; WP_013256814.1; NC_014364.1. DR RefSeq; YP_003805952.1; NC_014364.1. DR ProteinModelPortal; E1RA39; -. DR EnsemblBacteria; ADK83358; ADK83358; Spirs_4285. DR KEGG; ssm:Spirs_4285; -. DR PATRIC; 42532708; VBISpiSma89994_4385. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR BioCyc; SSMA573413:GI0C-4340-MONOMER; -. DR Proteomes; UP000002318; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002318}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ADK83358.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000002318}; KW Transferase {ECO:0000313|EMBL:ADK83358.1}. SQ SEQUENCE 615 AA; 66359 MW; 7B608FF1EFF5BE25 CRC64; MLKPYLERLA DGVLLFDGAV GTMLYEKGVF LNQCFEHVTL TSPEKVSELH REMIAAGAQA VTTNTFGANR LRLDGYGLSE LTGKINREAV RLAREAAGKE VYVAGSVGPL GKRVGPVGKI DSEEARSVFR EQMEALAEAG IDLFVLETFR NIDELLLAAE TAKATAPEIP VQAQYSFRPL RSEQYNNDLT PVFARLQESE HVDVLGINCS TGPAHMLDVI LASGGVVSKP ISVMPNAGYP RDYEGRQLYM ASPDYFAEYA LKFLDAGVHV IGGCCGTTPL HIQKMAQAIL HLDSSRHKGL SIEVSSKEIE RLEPVALEKR SAFGAALAKG EWITTVELVP PMGIDLSKAI AKAKTLGDAG ITCVNVPDGP RASSRISTLV TCMEIQRNSG VETIQHICCR DKNLIGIQSE LLGAQTAGVH NLLLLTGDPP KVGNFPDATG VFDTDSIGLL SLADSLNQGI DLAGNRLHGQ TSFVAGAGAN PAAQVLEREV ERAWKKAEAG AEYFITQPVF DVELLSTFLD KIKGTGKPVI AGIWPLASYR NALFLHYEVP GISIPADLQE RMKKHDTKEG AMEEGILIAR EIIAKIRGRV AGVQVSPPFG RLEAALQVIK NQEDI // ID E1RBM2_SPISS Unreviewed; 1156 AA. AC E1RBM2; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 31. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADK79752.1}; GN OrderedLocusNames=Spirs_0608 {ECO:0000313|EMBL:ADK79752.1}; OS Spirochaeta smaragdinae (strain DSM 11293 / JCM 15392 / SEBR 4228). OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Spirochaeta. OX NCBI_TaxID=573413 {ECO:0000313|EMBL:ADK79752.1, ECO:0000313|Proteomes:UP000002318}; RN [1] {ECO:0000313|EMBL:ADK79752.1, ECO:0000313|Proteomes:UP000002318} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11293 / JCM 15392 / SEBR 4228 RC {ECO:0000313|Proteomes:UP000002318}; RX PubMed=21304743; RA Mavromatis K., Yasawong M., Chertkov O., Lapidus A., Lucas S., RA Nolan M., Del Rio T.G., Tice H., Cheng J.F., Pitluck S., Liolios K., RA Ivanova N., Tapia R., Han C., Bruce D., Goodwin L., Pati A., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., RA Detter J.C., Rohde M., Brambilla E., Spring S., Goker M., Sikorski J., RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Klenk H.P., Kyrpides N.C.; RT "Complete genome sequence of Spirochaeta smaragdinae type strain (SEBR RT 4228)."; RL Stand. Genomic Sci. 3:136-144(2010). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002116; ADK79752.1; -; Genomic_DNA. DR RefSeq; WP_013253216.1; NC_014364.1. DR RefSeq; YP_003802346.1; NC_014364.1. DR EnsemblBacteria; ADK79752; ADK79752; Spirs_0608. DR KEGG; ssm:Spirs_0608; -. DR PATRIC; 42525096; VBISpiSma89994_0625. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR BioCyc; SSMA573413:GI0C-616-MONOMER; -. DR Proteomes; UP000002318; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002318}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADK79752.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002318}; KW Transferase {ECO:0000313|EMBL:ADK79752.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 224 224 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 729 729 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1156 AA; 123657 MW; 1419FA98A0A186F5 CRC64; MAQADFRSLL GKRIIIFDGA MGTSIQALEI PDAAWEGKAG CNEILNKTAP EYIDAIHDSF LAAGADVVET NSFGATSIVL DDYDLASQSA DLNRRAAEIA RKAAGRHTSA DRPRFVAGSM GPGTKLPTLG HITFDELYTA FRKQADALLE GGADLLVVET SQDLLQTKAA VIAAGDSAAQ SGRDIPIIAS VTVEQSGTML MGSDLSAVVA TLHPLRTDLI GINCAVGPDL MGPNLEQLAS IYNGPIFCMP NAGLPEMKDG KTVYSLGPVQ FAEIMAGYLA RFHIAVAGGC CGTTPEYIRQ LALRAEKMRP VPAPTSPMRP VLSSLFSAQP MIQEPAPFLI AEQANSNGSK VFRGMIDQED WDAAADFLLD QTGYGAHAAD LCVAVPGRNE RSDMLNILNG AAARNRLPFV IDSTDPQVIE TALKAIGGRP LINSINLEAG EEHAQKVFAL AARYGAAIIC LTIDEEGMAK TVEKKVAIAR RLAAIARHAG LRNEDLVFDP LTFTLGSGDE SLRSAGTESI RALSAIKEAV PGCLTVMGVS NISFGLAAPA RRVLNSLFLS EAVSAGLDMA IVNPKKIRPV AALDPEARKA ALDLIYHNED GSALLRYLEL FEKGKGISEE ENKEKEQSLP PQELLRSRVI AGSKDRLEEI INRCLETTAA GDIINEILIP AMGIVGERFG KGEMQLPFVL QSAEVMKRSV SILEPHMEKG DSVSKRGTVI LATVAGDVHD IGKNLVDIIL SNNGYLVKNL GIKIGIDTII KAAEEEKATA VGMSGLLVKS TAIMKSNLEE MKRRKLRLPV LLGGAALTPA FVEGQCRPAA PAEVYYCKDA FDALKALDSL KKAKGSAGSG QEADRGVVPA APITPASNTP APASTDTRKN TRPAPSPAQT ARSAHGSHAP QAAEVCTCTE CRPAGSPGPL PPPFFGARYG EGFDLHEIFE TIDRRTLFRG RWGYKRGKME QSAYEALIET EVLPKFEALK KLIIEEGLFV PHVRYGFFRC SREGDRLTVE QTGKKPCYLP FARLPQEKGG CLADRFPEEG GILPLQIVTL GEGPAQKSHL IYSEDRYGDY LRFHGLAAEA TDALAALVHK SIDTLLFPSG TRTKRYSFGY PCCPDLEANR TIGALLDAAS IGIGFTESGQ MLPELSTSAV IVPYGL // ID E1SAU7_PANVC Unreviewed; 1264 AA. AC E1SAU7; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 35. DE SubName: Full=B12-dependent homocysteine-N5-methyltetrahydrofolate transmethylase, repressor of MetE and MetF {ECO:0000313|EMBL:ADO11611.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADO11611.1}; GN Name=metH {ECO:0000313|EMBL:ADO11611.1}; GN OrderedLocusNames=Pvag_3492 {ECO:0000313|EMBL:ADO11611.1}; OS Pantoea vagans (strain C9-1) (Pantoea agglomerans (strain C9-1)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Pantoea. OX NCBI_TaxID=712898 {ECO:0000313|EMBL:ADO11611.1, ECO:0000313|Proteomes:UP000006631}; RN [1] {ECO:0000313|EMBL:ADO11611.1, ECO:0000313|Proteomes:UP000006631} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C9-1 {ECO:0000313|EMBL:ADO11611.1, RC ECO:0000313|Proteomes:UP000006631}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002206; ADO11611.1; -; Genomic_DNA. DR RefSeq; WP_013359753.1; NC_014562.1. DR RefSeq; YP_003933060.1; NC_014562.1. DR EnsemblBacteria; ADO11611; ADO11611; Pvag_3492. DR KEGG; pva:Pvag_3492; -. DR PATRIC; 42423167; VBIPanVag152020_3637. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; PVAG712898:GHQ2-3484-MONOMER; -. DR Proteomes; UP000006631; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006631}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADO11611.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006631}; KW Transferase {ECO:0000313|EMBL:ADO11611.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 347 347 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 348 348 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 796 796 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1264 AA; 139682 MW; 38B68EA0284ADE53 CRC64; MTMDGTCRRR GYFVARQACA RMKNRVFRQQ TDVNGATVST KIDALHQQLA QRIMVLDGGM GTMIQSYRLA EEDYRGSRFA DWPCDLKGNN DLLVLSKPSV IREIHDAYLA AGADILETNT FNATSIAMAD YQMESLSAEI NFEAARLARA CADAWTAKTP DRPRYVAGVL GPTNRTCSIS PDVNDPAYRN VTFTQLVEAY RESTRALVEG GADLIMIETV FDTLNAKAAV YAVKTEMDAL GVKLPLMISG TITDASGRTL SGQTTEAFYN SLRHAEPLSF GLNCALGPDE LRQYVAELSR IAEGYVTAHP NAGLPNAFGE YDLDAELMAE QIGEWATSGF LNIIGGCCGT TPQHIAAMVA AVDGIAPRRL PVIPVACRLS GLEPLNVTAE SLFVNVGERT NVTGSAKFKR LIKEEKYNDA LEVALQQVQS GAQIIDINMD EGMLDAEAAM VRFLNLIAGE PDIARVPIMI DSSKWEVIEK GLQCIQGKGI VNSISMKEGE AAFIHHARQV RRYGAAMVVM AFDEVGQADT RARKIEICRR AYRILTKQVG FPPEDIIFDP NIFAVATGID EHNNYAMDFI GACEDIKREL PHALISGGVS NVSFSFRGND PVREAIHAVF LYYAIRNGMD MGIVNAGQLA IYDDLPAELR EAVEDVILNR RDDGTERLLA LAEKYRGGKS DGAQDKQLAE WRSWDVVKRL EYSLVKGITE FIEQDTEEAR QQVPRPIEVI EGPLMSGMNV VGDLFGEGKM FLPQVVKSAR VMKQAVAYLE PFIEASKEAG RSNGKIVLAT VKGDVHDIGK NIVGVVLQCN NYEIIDLGVM VPGEKILKTA REVKADIIGL SGLITPSLDE MVNMAKEMER QGFTLPLLIG GATTSKAHTA VKIEQHYSGP TVYVQNASRT VGVVSSLLSA TLKDDFVART RKEYETVRIQ HARKKPRTPP VPLQAARHNA TSIDWESYTP PVPHRAGVSQ VEASIATLRN YIDWTPFFMT WSLAGKYPRI LEDEVVGEEA QRLFADASAM LDKLSEESLL KPRGVVGIFP ANRVGDDIHV YRDERRDEIL CVSHHLRQQT EKTDFANYCL ADFVAPKSAG KADYLGAFAV TGGLEEDALA EAYDRQHDDY NKIMVKALAD RLAEAFAEYL HERVRKVIWG FAPNENLSNE ELIRENYQGI RPAPGYPACP DHTEKAAIWR LLAVEEQTGM KLTESFAMWP GAAVSGWYFS HPDSRYFAVA QIQRDQVEDY ATRKGMSVSE VERWLAPNLG YDAD // ID E1SBC6_PANVC Unreviewed; 311 AA. AC E1SBC6; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 01-APR-2015, entry version 24. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADO10526.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ADO10526.1}; GN Name=mmuM {ECO:0000313|EMBL:ADO10526.1}; GN OrderedLocusNames=Pvag_2353 {ECO:0000313|EMBL:ADO10526.1}; OS Pantoea vagans (strain C9-1) (Pantoea agglomerans (strain C9-1)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Pantoea. OX NCBI_TaxID=712898 {ECO:0000313|EMBL:ADO10526.1, ECO:0000313|Proteomes:UP000006631}; RN [1] {ECO:0000313|EMBL:ADO10526.1, ECO:0000313|Proteomes:UP000006631} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C9-1 {ECO:0000313|EMBL:ADO10526.1, RC ECO:0000313|Proteomes:UP000006631}; 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 ----------------------------------------------------------------------- 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; ADO10526.1; -; Genomic_DNA. DR RefSeq; WP_013358791.1; NC_014562.1. DR RefSeq; YP_003931975.1; NC_014562.1. DR EnsemblBacteria; ADO10526; ADO10526; Pvag_2353. DR KEGG; pva:Pvag_2353; -. DR PATRIC; 42420835; VBIPanVag152020_2522. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR BioCyc; PVAG712898:GHQ2-2346-MONOMER; -. DR Proteomes; UP000006631; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006631}; KW Methyltransferase {ECO:0000313|EMBL:ADO10526.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006631}; KW Transferase {ECO:0000313|EMBL:ADO10526.1}. SQ SEQUENCE 311 AA; 33511 MW; 56651806A918056B CRC64; MSHNPVAQAL TESSPLILDG ALATELEARG CHLADALWSA KVLMENPELI YQVHYDYFVA GARCAITASY QATPQGFATR GLDEAQSLAL IAQSVELARR ARHDYLAVRP DAKTLLVAGS VGPYGAFLAD GSEYRGDYAL PEAEMMAFHR PRVQALLAAG ADLLACETLP SFAEAQALVK LLAEFPESRA WFTFTLHDAG HISDGTPLSE VVSWLNQQPQ VVAIGINCVA LESVTPALHQ LQRLTDKPLV VYPNSGEQYD ADSKTWHSAP SGCTLHDKLD EWQQAGAKLI GGCCRTSPND IAAIARACQP Q // ID E1STX6_FERBD Unreviewed; 1230 AA. AC E1STX6; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 01-APR-2015, entry version 33. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ADN77220.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADN77220.1}; GN OrderedLocusNames=Fbal_3020 {ECO:0000313|EMBL:ADN77220.1}; OS Ferrimonas balearica (strain DSM 9799 / CCM 4581 / PAT). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Ferrimonadaceae; Ferrimonas. OX NCBI_TaxID=550540 {ECO:0000313|EMBL:ADN77220.1, ECO:0000313|Proteomes:UP000006683}; RN [1] {ECO:0000313|EMBL:ADN77220.1, ECO:0000313|Proteomes:UP000006683} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 9799 / CCM 4581 / PAT {ECO:0000313|Proteomes:UP000006683}; RX PubMed=21304747; RA Nolan M., Sikorski J., Davenport K., Lucas S., Del Rio T.G., Tice H., RA Cheng J.F., 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.J., Jeffries C.D., Tapia R., Brettin T., RA Detter J.C., Han C., Yasawong M., Rohde M., Tindall B.J., Goker M., RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Kyrpides N.C., Klenk H.P., Lapidus A.; RT "Complete genome sequence of Ferrimonas balearica type strain (PAT)."; RL Stand. Genomic Sci. 3:174-182(2010). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002209; ADN77220.1; -; Genomic_DNA. DR RefSeq; WP_013346526.1; NC_014541.1. DR RefSeq; YP_003914294.1; NC_014541.1. DR EnsemblBacteria; ADN77220; ADN77220; Fbal_3020. DR KEGG; fbl:Fbal_3020; -. DR PATRIC; 42327844; VBIFerBal3052_3044. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; FBAL550540:GHY2-3153-MONOMER; -. DR Proteomes; UP000006683; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006683}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADN77220.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006683}; KW Transferase {ECO:0000313|EMBL:ADN77220.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1230 AA; 135904 MW; 8DAD83B231939D77 CRC64; MSDQHALEQQ LAQRILILDG AMGTMIQGYK LDEDDYRGER FADWPSPLKG NNDLLSLTQP DIIRAIHTAY LEAGADIIET NTFNSTTIAM ADYDMQSLSK EINFESARLA RAAADDVAAK TGIPRYVAGV LGPTNRTCSI SPDVNDPGFR NVHFDDLVAA YTESTEALLD GGADLILVET VFDTLNAKAA LFAIDSVFEA RGQRWPVMIS GTITDASGRT LTGQTTEAFY NSLRHIKPIA IGLNCALGPK ELVPYISELN RISECAVSAH PNAGLPNEMG GYDETPAQMA AIIGQWAADG WLNIVGGCCG TTPEHIRAIA EAVRPHAPRT PPAHLLSNDN VSTRLSGLEP CNFDADALFI NVGERTNVTG SARFLRLIKE NDYETALEVA RQQVENGAQI IDINMDEGML DAEAAMVKFL NLIASEPEIS KVPIMIDSSK WEVIEAGLKC IQGKGVVNSI SLKEGEAAFL HQAKLIRRYG AAAVVMAFDE TGQADTYQRK VEICTRAYQV LTEKAGFAPE DIIFDPNIFA IATGIEEHDN YAVDFIEACR TIRDTLPHAR LSGGVSNVSF SFRGNNPVRE AIHAVFLYHA IRNGLSMGIV NAGQLAIYDD IPKPLLERVE DVVLNRRSDG TERLLEIAEE YRGDGQQAED PKDAEWRSWP VNKRLEHALV KGITEFIDED TEAARQAATR PLDVIEGPLM DGMNVVGDLF GAGKMFLPQV VKSARVMKKA VAYLNPYIEA EKVEGQSNGK VLMATVKGDV HDIGKNIVAV VLQCNGYEVI DLGVMVPVEK IIEVAKAEKV DVIGMSGLIT PSLDEMIHNV KEFKKAGLTC PAIIGGATTS KIHTAVKIFE HYEHGAIYVP DASRTVPVVA KLIGPERHAF IEQHYREYAD LKAKREAQGN RKTLIPLEQA RANRNQIDWD NYTPAVPKQL GVQVFNDYPL TDLIDRIDWT PFFRSWGLHG KYPQIFKNPT VGAEAQELYD NAQIMLKQII EGKWLTAAAV IGLFPANTCD NHDDVALYTD ESRSEELLRL HMLRQQIERV DNDNFALSDF VAPKASGKGD YMGAFAVTAG IGIEEHVERF EKAHDDYHAI MIKALADRLA EAFAERMHER VRKEFWGYAA DENLDNEALI REKYKGIRPA PGYPACPDHT EKGLLWQLLQ PEQNIGLKIT ENFAMYPTAA VSGWYFAHPE SRYFGVTDID RDQVEDYARR IGLSVAETEK WLSPILGYSA // ID E1T5U3_BURSG Unreviewed; 356 AA. AC E1T5U3; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 30. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADN56220.1}; GN OrderedLocusNames=BC1003_0216 {ECO:0000313|EMBL:ADN56220.1}; OS Burkholderia sp. (strain CCGE1003). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=640512 {ECO:0000313|EMBL:ADN56220.1, ECO:0000313|Proteomes:UP000001550}; RN [1] {ECO:0000313|Proteomes:UP000001550} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCGE1003 {ECO:0000313|Proteomes:UP000001550}; 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 ----------------------------------------------------------------------- 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; ADN56220.1; -; Genomic_DNA. DR RefSeq; WP_013337858.1; NC_014539.1. DR RefSeq; YP_003905511.1; NC_014539.1. DR EnsemblBacteria; ADN56220; ADN56220; BC1003_0216. DR KEGG; bgf:BC1003_0216; -. DR PATRIC; 42206410; VBIBurSp98639_0224. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR BioCyc; BSP640512:GBXV-219-MONOMER; -. DR Proteomes; UP000001550; Chromosome 1. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001550}; KW Methyltransferase {ECO:0000313|EMBL:ADN56220.1}; KW Transferase {ECO:0000313|EMBL:ADN56220.1}. SQ SEQUENCE 356 AA; 38487 MW; B248205FAC6EB2E4 CRC64; MNQPAQTVKS VRPEPEYTRG KELPALLKSR ILILDGAMGT MIQRYKLDEA RYRGERFKDY GRDIKGNNEL LSITQPQIIS EIHEQYLAAG ADIIETNTFG ATTVAQADYG MEALAVEMNL ESAKLARAAC DKFSTPDKPR FVAGAIGPTP KTASISPDVN DPGARNVTFD ELHAAYYEQA KALLDGGADL FLVETIFDTL NAKAALFALD ELFENTGERL PIMISGTVTD ASGRILSGQT VEAFWNSLRH AKPLTFGLNC ALGAALMRPY IAELAKLCDT YVSCYPNAGL PNPMSDTGFD ELPADTSGLL KEFAEAGLVN IAGGCCGTTP EHIAAIAKAL AEVKPRKWPT QYRDAA // ID E1U3N9_9CYAN Unreviewed; 327 AA. AC E1U3N9; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 01-OCT-2014, entry version 9. DE SubName: Full=Putative homocysteine S-methyltransferase {ECO:0000313|EMBL:ACN96046.1}; OS Fischerella sp. MV11. OC Bacteria; Cyanobacteria; Stigonematales; Fischerella. OX NCBI_TaxID=397321 {ECO:0000313|EMBL:ACN96046.1}; RN [1] {ECO:0000313|EMBL:ACN96046.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MV11 {ECO:0000313|EMBL:ACN96046.1}; RA Hess W.R., Scholz I.D.; RT "High diversity of cyanobacterial nonribosomal peptide synthetase RT genes in isolates from geothermal sites and hot springs of Costa RT Rica."; 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; FJ211387; ACN96046.1; -; Genomic_DNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:ACN96046.1}; KW Transferase {ECO:0000313|EMBL:ACN96046.1}. SQ SEQUENCE 327 AA; 36126 MW; A52ABA8E4AD244E4 CRC64; MSKYRQNLPQ LSGDLFLTDG GLETTLIFHE GLNLPNFAAF DLFRYSDGQK SLEKYFCTYA ALATEYRVGL VLESATWRAN PDWATKLGYS REDLICIDHQ SIQLLQGIRK NYETEQSPIV ISGCVGPRGD GYHPEHCMTA DEAATYHQEQ IAAFQDADAD LVTAMTMNYT EEALGITFAA QAIGMPVVIS FTVETNGDLP TGQTLKDAIA QIDAATHNGP AYYMINCAHP THFAHILPTD EPWLGRIRGL RANASTKSHA ELDEAEELDA GNPAALGSQY RELKQKLQSL NVLGGCCGTD HRHVRAIYQA CASLWWHHMS GTVQLQI // ID E1UKL1_BACAS Unreviewed; 316 AA. AC E1UKL1; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=YbgG protein {ECO:0000313|EMBL:CBI41346.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:CBI41346.1}; GN Name=ybgG {ECO:0000313|EMBL:CBI41346.1}; GN OrderedLocusNames=BAMF_0220 {ECO:0000313|EMBL:CBI41346.1}; 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 {ECO:0000313|EMBL:CBI41346.1, ECO:0000313|Proteomes:UP000006562}; 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] {ECO:0000313|Proteomes:UP000006562} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23350 / DSM 7 / BCRC 11601 / NBRC 15535 / NRRL B-14393 RC {ECO:0000313|Proteomes:UP000006562}; 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; CBI41346.1; -; Genomic_DNA. DR RefSeq; WP_013350893.1; NC_014551.1. DR RefSeq; YP_003918816.1; NC_014551.1. DR EnsemblBacteria; CBI41346; CBI41346; BAMF_0220. DR GeneID; 9780495; -. DR KEGG; bao:BAMF_0220; -. DR PATRIC; 42469236; VBIBacAmy172706_0236. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR BioCyc; BAMY692420:GHU2-269-MONOMER; -. DR Proteomes; UP000006562; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006562}; KW Methyltransferase {ECO:0000313|EMBL:CBI41346.1}; KW Transferase {ECO:0000313|EMBL:CBI41346.1}. SQ SEQUENCE 316 AA; 34493 MW; 0CE49FDE7D8AB5AB CRC64; MNPITQILDE YPVMIIDGAM ATELERMGCD LNDDLWSAKI LLERPELIKQ VHAEYFAAGA DCAITASYQS TIEGFAARGI PETDAIRLIQ TSVELAVQAR DEFWAHEENR IHRPKPLIAA SIGPYGASLA DGSEYRGHYG LTEDELISFH RPRMKALIES GADLLACETI PCLSEAKAIT KLLEEFPGTY AWISFSAKDG RHISEGTPIS ECAALLDSCS QIAAIGINCT PIEHIPTLIE EIKRAASKPI IAYPNSGEQY DPVTKTWIGA ACENNFGKSA QSSWYEKGVS LIGGCCRTKP ADIQAIADWA KTLKTT // ID E1UQZ1_BACAS Unreviewed; 613 AA. AC E1UQZ1; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 34. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN Name=yitJ {ECO:0000313|EMBL:CBI42301.1}; GN OrderedLocusNames=BAMF_1175 {ECO:0000313|EMBL:CBI42301.1}; 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 {ECO:0000313|EMBL:CBI42301.1, ECO:0000313|Proteomes:UP000006562}; 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] {ECO:0000313|Proteomes:UP000006562} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23350 / DSM 7 / BCRC 11601 / NBRC 15535 / NRRL B-14393 RC {ECO:0000313|Proteomes:UP000006562}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; CBI42301.1; -; Genomic_DNA. DR RefSeq; WP_013351786.1; NC_014551.1. DR RefSeq; YP_003919771.1; NC_014551.1. DR ProteinModelPortal; E1UQZ1; -. DR EnsemblBacteria; CBI42301; CBI42301; BAMF_1175. DR GeneID; 9780889; -. DR KEGG; bao:BAMF_1175; -. DR PATRIC; 42471374; VBIBacAmy172706_1263. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR BioCyc; BAMY692420:GHU2-1262-MONOMER; -. DR Proteomes; UP000006562; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006562}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 613 AA; 68199 MW; 027964644E171276 CRC64; MGLLQDLEER ILIGDGAMGT LLYSYGIDRC FEELNVSKPE EIKRIHKAYV EAGADIVQTN TYGANFIKLS RYGLEDDTKR INQEAVRIAR ASSDGAYVLG TMGGIRTFNK NAYSLEEIKR SFREQLYLLL HEEPDGLLLE TYYDLEEARE VLKIARKETE LPIMLNVSMH EQGVLQDGTP LREALRSIAG LGADITGINC RLGPYHMIEA LTEVPIFRDA YLSVYPNSSL PSLEGGRLVY DTDDAYFRES AIQFRTQGAR IIGGCCGTTP NHIRAMADAV HGLSPVTDKE VKIRREEEVI SVRDERTDPG LDEIAAQKRS IIVELDPPKK LNFGKFLQAA AELKETGIEA LTLADNSLAT PRISNAACGS LLKERLDIRS LVHITCRDRN IIGLQSHLMG LDTLGLTDIL AITGDPSKIG DFPGATSVYD LTSFDLIRLI KQFNEGISLS GKPLGKKTNF SVAGAFNPNV RHLDKAVKRL EKKIECGADY FVSQPVYSEQ QLIDIHHETK HLKTPVYIGI MPLTSSRNAE FIHHEIPGIK LSDSIREKMA QGGEDKRKQK AEGLAIAKSL LDTACELFNG IYLITPFLRS DLTSELAAYI KQKDEKRADV YLH // ID E1V310_HALED Unreviewed; 1236 AA. AC E1V310; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 34. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CBV42489.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CBV42489.1}; GN Name=metH {ECO:0000313|EMBL:CBV42489.1}; GN OrderedLocusNames=HELO_2605 {ECO:0000313|EMBL:CBV42489.1}; 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 {ECO:0000313|EMBL:CBV42489.1, ECO:0000313|Proteomes:UP000008707}; RN [1] {ECO:0000313|Proteomes:UP000008707} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9 RC {ECO:0000313|Proteomes:UP000008707}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; FN869568; CBV42489.1; -; Genomic_DNA. DR RefSeq; WP_013332361.1; NC_014532.1. DR RefSeq; YP_003897674.1; NC_014532.1. DR EnsemblBacteria; CBV42489; CBV42489; HELO_2605. DR KEGG; hel:HELO_2605; -. DR PATRIC; 42354572; VBIHalElo161731_1718. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; HELO768066:GJEE-1655-MONOMER; -. DR Proteomes; UP000008707; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008707}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CBV42489.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008707}; KW Transferase {ECO:0000313|EMBL:CBV42489.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 766 766 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1236 AA; 137052 MW; 749D6592C13B4755 CRC64; MADVPVSSLA TLTDSLAERI LMLDGGMGTM LQNAGLSEEE FRGERFVDWP TDLKGNNDLL ALTCPDLVTR IHRDYLEAGA DIVETNTFNS TRLSQADYGM EALVPELNRE SARLARAICD AVARETGVPR YVAGVLGPTS RTASLSPDVN DPAMRNVTFD ELRDNYREAA EALIEGGSDL ILIETIFDTL NAKAAIYALE ELFEARGERL PVMISGTITD ASGRTLSGQT TEAFWNSVRH TRPLSVGLNC ALGAEELRPY VEELAKKADT FVSAHPNAGL PNEFGEYDQT PEEMAAIVAE FAESGLVNII GGCCGSTPEH IAAIHRAIRD TAPRRIPERA LACRLSGLEP FNIEHDSLFV NVGERTNVTG SARFKRLIKE EDYTTALEVA LEQVENGAQV IDINMDEGML ESQDAMVRFL NLIAGEPDIA RVPIMVDSSK WEIIEAGLKC IQGKAVVNSI SLKEGEDAFR EQATKCRRYG AAIVVMAFDE QGQADTFARK AEICQRAYRL LVDEIDFPAE DIIFDPNIFA IATGIEEHNN YAVDFIEATR WIREHLPHAM VSGGVSNVSF SFRGNNAVRE AIHSVFLYHA IRAGMTMGIV NAGQLAVYDD LPEELREGVE DVVLNRRDDA TERLLDLADK YKDDGSGASR KEDLEWRSWE VEKRIEHALV KGITAYIEDD TELARQRATR PIEVIEGPLM DGMNVVGDLF GAGKMFLPQV VKSARVMKQA VAYLIPYIEA EKSELSTEDQ QAKGKIVMAT VKGDVHDIGK NIVGVVLQCN NYEVIDLGVM VPAEKILQTA REENADIIGL SGLITPSLDE MVHVAKEMQR QNFDIPLLIG GATTSKAHTA VKIEPGYEHP VIYVTDASRA VGVAGKLLSP GLKEAYVTEI REEYEKVRER NAKRRPKAAE ISYAEACRHK PAIDWQDYTP PRPALAGLEV FENQDLAPLV ERIDWTPFFM SWQLAGKYPR ILDDEKVGEA ARNLFDDAQA MLKRLIDERL IQARGVIGMW PANTVDDDII EVYADESRSE VIERLHHIRQ QTTKNREGAC YSLADFVAPK ESGKPDWIGG FAVTTGHGVE ALTERYKAAG DDYNAIMVQA LADRLAEAFA EYMHERVRKQ YWGYAPDEAL DNEALIAEKY RGIRPAPGYP ACPDHTEKAT LFRLLEAETH SGLSLTESFA MWPAAAVAGW YFAHPQSKYF STGKITRDQV EMLAERKGMS LAELERWLMP VLSYDS // ID E1VKB4_9GAMM Unreviewed; 1230 AA. AC E1VKB4; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 29-APR-2015, entry version 31. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CBL45256.1}; GN Name=metH {ECO:0000313|EMBL:CBL45256.1}; GN ORFNames=HDN1F_16730 {ECO:0000313|EMBL:CBL45256.1}; OS gamma proteobacterium HdN1. OC Bacteria; Proteobacteria; Gammaproteobacteria. OX NCBI_TaxID=83406 {ECO:0000313|EMBL:CBL45256.1, ECO:0000313|Proteomes:UP000002677}; RN [1] {ECO:0000313|EMBL:CBL45256.1, ECO:0000313|Proteomes:UP000002677} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; FP929140; CBL45256.1; -; Genomic_DNA. DR RefSeq; WP_013261750.1; NC_014366.1. DR RefSeq; YP_003810908.1; NC_014366.1. DR EnsemblBacteria; CBL45256; CBL45256; HDN1F_16730. DR KEGG; gpb:HDN1F_16730; -. DR PATRIC; 42346333; VBIGamPro61291_1813. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR BioCyc; GPRO83406:GIWA-1716-MONOMER; -. DR Proteomes; UP000002677; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002677}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002677}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1230 AA; 136949 MW; 0AAC678FA82DAAC6 CRC64; MNTSRTSAIH QAIQERILIL DGAMGTMIQQ RKLSEADFCG ERFQAHPHDL KGNNDLLCLT RPDVIRQIHL DYLEAGADIL ETNTFNAQRI SQADYHLEEI VYELNREGAR LAREAADAYT AKTPEKPRFV AGVLGPTNRT ASMSRDVNDP AARSVTFDDL VENYTEATHG LMDGGADIIL IETIFDTLNA KAAVFAVRRV FAARGITLPI MISGTIVDQA GRTLSGQTVE AFYNSLRHAK PLSMGFNCAL GAEQLRPYVD ELSTKAECFV SAHPNAGLPN EFGEYDQSAE QMAAIVRDFA ASGFLNIVGG CCGTTPEHIR AIAEAVASYP PRPRPELPKA MRLAGMEAFN IDEHSLFVNV GERTNVTGSA RFRRLIREEK YEEALEVARE QVENGAQVID INMDEGMLDS QAAMMRFLNM LSMETTISRV PIMVDSSRWE IIEEGLKRIQ GKPIVNSISL KEGEAEFIER ARLCMEYGAA AVVMAFDETG QADTLERKQQ ITKRSYDCLV SIGFPPEDII FDPNAFAIAT GIEEHNNYGV DFINACAYIK QNLPYAKSSG GISNVSFSFR GNETVREAIH AVLLYHAIKA GLTMGIVNAG QLAIYEDIPA ELKERVEDVV LNRREDATDR MLEIAEQYRG GGTQKSKEDL SWRELPVEKR LEYALVKGIT TYAVEDTEIA RQKANRPIEV IEGPLMDAMN VVGDLFGSGK MFLPQVVKSA RVMKTAVAHL IPFIEAEKGG NTESKGKILL ATVKGDVHDI GKNIVGVVLQ CNNYEVIDLG VMVPSEKILE TAKNEKVDMI GLSGLITPSL DEMVHVAKEM QRTGSDLPLL IGGATTSKAH TAVKIEPQYK NEAVVYVPDA SRAVGVVSQL LNPELRNAYI EARREEYATI RQRNANRKTN TPMPFEQAQA MAPKIDFTHF KPTRPSFLGV KVFDHYPLEE VVERIDWGPF FNAWELTGKY PAILKDEVVG EAASQLFAEA QVMLKRIIDE KWINARAVVG FWRAHRKHDT NDIELFDESG AQVATLHQLR QQVDKAKQGI CRSLADFVAD SESGIEDYVG GFAVNAGDAV QERVKQYEAK NDDYNAILLK SLADRLAEAM AERMHERVRK EFWGYVHDES LNNEELINEA YQGIRPAPGY PACPDHSEKA TLFRLLDPQT RIGLQLTDHF AMFPTAAVSG WYFAHPESKY FNVGKIGKDQ VEDYARRKQV TLEQAERWLS PTLAYDPDEK // ID E1W3Y6_HAEP3 Unreviewed; 1230 AA. AC E1W3Y6; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 29-APR-2015, entry version 31. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CBW15078.1}; GN OrderedLocusNames=PARA_09720 {ECO:0000313|EMBL:CBW15078.1}; OS Haemophilus parainfluenzae (strain T3T1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=862965 {ECO:0000313|EMBL:CBW15078.1, ECO:0000313|Proteomes:UP000007052}; RN [1] {ECO:0000313|Proteomes:UP000007052} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T3T1 {ECO:0000313|Proteomes:UP000007052}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; FQ312002; CBW15078.1; -; Genomic_DNA. DR RefSeq; WP_014064802.1; NC_015964.1. DR RefSeq; YP_004822667.1; NC_015964.1. DR EnsemblBacteria; CBW15078; CBW15078; PARA_09720. DR KEGG; hpr:PARA_09720; -. DR PATRIC; 43051074; VBIHaePar168133_0972. DR KO; K00548; -. DR BioCyc; HPAR862965:GH07-995-MONOMER; -. DR Proteomes; UP000007052; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007052}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007052}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 246 246 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1230 AA; 136523 MW; EDAA603C366EB997 CRC64; MSHNQTELLK KSLAERILIL DGAMGTMIQK YKLTEADFRG ERFKESAVDL RGNNDLLTLT QPLLISAIHE KYLQAGADII ETNTFSSTTI AQADYDLQSI AYELNFAGAK LARLAADKYS TPEKPRFVAG VLGPTNRTAS ISPDVNDPGF RNITFMELVD AYAEATKGLI EGGADLIMIE TIFDTLNAKA AIFAIETVFE ELGVELPIMI SGTITDASGR TLSGQTTEAF YNSLRHAKPL TFGLNCALGP KELRQYVEQL SKISETYISV HPNAGLPNAF GGYDLGAEEM AAHLKEWAES GFVNIVGGCC GTTPEHIKAF ADAMQGIAPR KLPEIKTAMR LSGLEPLNID DESLFVNVGE RNNVTGSAKF KRLIKEDKFA EAIEIAIDQV ENGAQVIDIN MDEALLDSKK CMTRFLNIMA TEPDAAKVPV MIDSSKWEVI EAGLQSVQGK PIVNSISLKE GEEIFIDHAK LVRKYGAAVV VMAFDEVGQA DTEDRKVEIC SRAYDILVNQ VGFPPEDIIF DPNIFAIGTG IEEHNNYGVD FINATGRIKR ALPHAKISGG VSNVSFSFRG NNVMREAIHA VFLYHAIKQG MDMGIVNAGQ LAIYDDLDPE LREIVEDAVL NRSPDATEKL LDIAEKYRNQ GNDESAVDSV AEWRTWPVEE RLKHALVKGI TTYIVEDTEE ARQQLPSPLD VIEGPLMEGM DVVGDLFGDG KMFLPQVVKS ARVMKQSVAY LEPFINATKQ KGSSNGKVVI ATVKGDVHDI GKNIVSVVMQ CNNFEVIDLG VMVPADKIIQ TAIDEKADII ALSGLITPSL DEMEYFLGEM TRLGLNLPVM IGGATTSKEH TAIKLYPKYK EHGVFYTSNA SRAVTVCATL MNPESRAELW EQFKKDYEKI QQSFSNRKPL RKQLSIEEAR ANRFDGFSGE WADYVPPTPN QTGIVEFKNV PIATLRKFID WSPFFRIWGL MGGYPDAFDY PEGGEEARKV WNDAQVVLDE LEQNHKLNPS GILGIFPAER VGDDVVLFAD EERTQQIGTA YGLRQQTERG KNSKSPFNFA LSDFIADRES GKKDWMGMFA VCAGIEEMEL VEGYKAAGDD YNAILLQAVG DRLAEAMAEY LHFELRTRIW GYTQEEFDNQ GLINENYVGI RPAPGYPSCP EHTEKALIWD LLEVEQRIGM KLTESYAMWP AASVCGWYFT HPASNYFTLG RIDEDQAQDY AKRKGWDERE MMKWLGVAMK // ID E1WT23_BACF6 Unreviewed; 916 AA. AC E1WT23; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 37. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CBW23523.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CBW23523.1}; GN Name=metH {ECO:0000313|EMBL:CBW23523.1}; GN OrderedLocusNames=BF638R_3046 {ECO:0000313|EMBL:CBW23523.1}; OS Bacteroides fragilis (strain 638R). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=862962 {ECO:0000313|EMBL:CBW23523.1, ECO:0000313|Proteomes:UP000008560}; RN [1] {ECO:0000313|EMBL:CBW23523.1, ECO:0000313|Proteomes:UP000008560} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=638R {ECO:0000313|EMBL:CBW23523.1, RC ECO:0000313|Proteomes:UP000008560}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; FQ312004; CBW23523.1; -; Genomic_DNA. DR RefSeq; WP_010993239.1; NC_016776.1. DR RefSeq; YP_005112059.1; NC_016776.1. DR ProteinModelPortal; E1WT23; -. DR SMR; E1WT23; 652-896. DR EnsemblBacteria; CBW23523; CBW23523; BF638R_3046. DR KEGG; bfg:BF638R_3046; -. DR PATRIC; 42749170; VBIBacFra167533_3132. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR BioCyc; BFRA862962:GHND-2950-MONOMER; -. DR Proteomes; UP000008560; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008560}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CBW23523.1}; KW Transferase {ECO:0000313|EMBL:CBW23523.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 916 AA; 100293 MW; 2A4F401F3D578B68 CRC64; MKKTIQQLVL ERILILDGAM GTMIQQYNLR EEDFRNERFA HIPGQLKGNN DLLCLTRPDV IRDIHRKYLE AGADIIETNT FSSTTISMAD YHVQEYVREM NQAAVKLARE VADEYTALNP DKPRFVAGSV GPTNKTCSMS PDVNNPAYRA VTYDEMADAY QQQMEAMLES GVDALLIETI FDTLNAKAAI LAAERAMKAT GVKVPVMLSV TVSDTGGRTL SGQTLEAFLA SVQHADIFSV GLNCSFGARQ LKPFLEQLAA RAPYYISAYP NAGLPNSLGK YDQTPADMAH EVKEYVHEGL INIIGGCCGT TDAYIAEYPA LIAGAKPHIP VCKPDCMWLS GLELLEVKPE INFVNVGERC NVAGSRKFLR LINEKKYDEA LSIARKQVED GALIIDVNMD DGLLDAKEEM TTFLNLVASE PEIARVPVMI DSSKWEVIEA GLKCLQGKSI VNSISLKEGE EKFLEHARTV RQYGAAVVVM AFDEKGQADT ATRKIEVCER AYHLLVDKIG FNPHDIIFDP NVLAVATGIE EHNNYAVDFI EATAWIKKNL PGAHISGGVS NLSFSFRGNN YIREAMHAVF LYHAIQKGMD MGIVNPGTSV LYTDIPADVL ERIEDVVLNR RSDAAERLIE LADRLKEASA GNTSAGQPVK HDAWRDGTVE ERLQYALVKG IGDFLEEDLA EALPKYDKAV DVIEGPLMNG MNHVGELFGA GKMFLPQVVK TARTMKKAVA ILQPIIESEK VEGTASAGKV LLATVKGDVH DIGKNIVSVV MACNGYDIID LGVMVPAESI VQKAIEEKVD MIGLSGLITP SLEEMVHVAM ELEKAGLDIP LLIGGATTSK LHTALKIAPV YHAPVVHLKD ASQNAGVAAR LMSPKSKEEL AKELSGEYEA LRDKSGMMKR ETVSLKEAQE NRLKLF // ID E1WV41_BACF6 Unreviewed; 318 AA. AC E1WV41; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=Genome {ECO:0000313|EMBL:CBW23845.1}; GN OrderedLocusNames=BF638R_3380 {ECO:0000313|EMBL:CBW23845.1}; OS Bacteroides fragilis (strain 638R). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=862962 {ECO:0000313|EMBL:CBW23845.1, ECO:0000313|Proteomes:UP000008560}; RN [1] {ECO:0000313|EMBL:CBW23845.1, ECO:0000313|Proteomes:UP000008560} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=638R {ECO:0000313|EMBL:CBW23845.1, RC ECO:0000313|Proteomes:UP000008560}; 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; CBW23845.1; -; Genomic_DNA. DR RefSeq; WP_005790322.1; NC_016776.1. DR RefSeq; YP_005112378.1; NC_016776.1. DR ProteinModelPortal; E1WV41; -. DR EnsemblBacteria; CBW23845; CBW23845; BF638R_3380. DR KEGG; bfg:BF638R_3380; -. DR PATRIC; 42749905; VBIBacFra167533_3495. DR OMA; CCGTDHR; -. DR BioCyc; BFRA862962:GHND-3278-MONOMER; -. DR Proteomes; UP000008560; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008560}. SQ SEQUENCE 318 AA; 36016 MW; 08196E3D987D0044 CRC64; MEQLSFIESF RTSPFILTEG AIVERLRHEF HISPDKHIAH AALIYDDSHR EILASIYRQY LQIATEFRLP LMLMTPTRRA NIEQIAASDY RHKNVLADTM AFLSRFRDEA STPVYIGGLA GCRGNAYDGR YYLSVEEAME FHFPTVRTLA QSGADYLFAG IMPQLTEAIG MANAMAATGL PYIISFMICR DGRLIDGTFI HDAIDAIEKE TSTRPLCYMA NCVHPDVLHQ ALLHPRNDTP LVRQRFQGIQ ANAANLSPEE LDGCDHLISS SPEELADRLM TLLWDFPLKI CGGCCGTNQQ HMHRFAEMLA YRRDNKAW // ID E1X3E1_BACMS Unreviewed; 1239 AA. AC E1X3E1; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 33. DE SubName: Full=B12-dependent homocysteine-N5-methyltetrahydrofolate transmethylase {ECO:0000313|EMBL:CBW25236.1}; GN Name=metH {ECO:0000313|EMBL:CBW25236.1}; GN OrderedLocusNames=BMS_0311 {ECO:0000313|EMBL:CBW25236.1}; OS Bacteriovorax marinus (strain ATCC BAA-682 / DSM 15412 / SJ). OC Bacteria; Proteobacteria; Deltaproteobacteria; Bdellovibrionales; OC Bacteriovoracaceae; Bacteriovorax. OX NCBI_TaxID=862908 {ECO:0000313|EMBL:CBW25236.1, ECO:0000313|Proteomes:UP000008963}; RN [1] {ECO:0000313|Proteomes:UP000008963} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-682 / DSM 15412 / SJ RC {ECO:0000313|Proteomes:UP000008963}; RX PubMed=22955231; DOI=10.1038/ismej.2012.90; RA Crossman L.C., Chen H., Cerdeno-Tarraga A.M., Brooks K., Quail M.A., RA Pineiro S.A., Hobley L., Sockett R.E., Bentley S.D., Parkhill J., RA Williams H.N., Stine O.C.; RT "A small predatory core genome in the divergent marine Bacteriovorax RT marinus SJ and the terrestrial Bdellovibrio bacteriovorus."; RL ISME J. 7:148-160(2013). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; FQ312005; CBW25236.1; -; Genomic_DNA. DR RefSeq; WP_014243025.1; NC_016620.1. DR RefSeq; YP_005034209.1; NC_016620.1. DR EnsemblBacteria; CBW25236; CBW25236; BMS_0311. DR KEGG; bmx:BMS_0311; -. DR PATRIC; 42736771; VBIBacMar168520_0299. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; BMAR862908:GJBX-303-MONOMER; -. DR Proteomes; UP000008963; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008963}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CBW25236.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008963}; KW Transferase {ECO:0000313|EMBL:CBW25236.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 253 253 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 318 318 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 319 319 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 771 771 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1239 AA; 138912 MW; 3A5A6165469AC08C CRC64; MSELKPYTTM GNELLELLNK RIVFMDGAMG TMIQQYKLEE EDFRGERFKD HASPLKGNND LLSLTRADII EEVHFKYLEA GSDIIETNTF SATRIGQADY HLEDLAYEIN VESARIAKRA CEKMMQKDPT RKCFVAGALG PTNKTASMSP DVNNPAYRAV TFDELVENYY QQAKALLEGG ADILLPETTF DTLNIKCAIF AIDKLFNELD YRVPVMLSVT ITDASGRTLS GQTIEAFWNS VRHANPLSVG INCALGAKEM RPYMDRLSQI ADCYTSCYPN AGLPNPLSDT GYDELPIDTA TFLEDYADSG FLNLVGGCCG TTPSHIKAIR EKLEEKKPRV KPTLKEVMNL SGLEPLYIDR EDQSRPFYMV GERTNVTGSP RFAKLIKNGD FDTALEVARQ QVENGANIID INFDEGLLDS KACMIKFMNL VASEPEICKV PIMIDSSKWE VIEEGLKCMQ GKGIVNSISL KEGEEKFIEQ AKLIKSYGAA TVVMAFDEEG QAADKADKVR ICQRAYKILV EKVNFDPRDI IFDPNILTVA TGIEEHNNYA LDFIEAVKEI KETCPGVLTS GGVSNVSFSF RGNNVVREAI HSSFLYHAIK AGLDMGIVNA GMLGVYEDIE PNLLQLVEDV LLNRHPDATE KLVDFAEKIK GSGKKKEVKD DKWRHGTLQE RMTHALVKGI STHIEEDTEE ARQELGIPLN VIEGPLMEGM KVVGELFGSG KMFLPQVVKS ARVMKAAVAY LEPFMEEERK KNANARKQGT FVIATVKGDV HDIGKNIVAV VLACNGYEVI DLGVMVSCEE IIKKAKEHDA CIIGMSGLIT PSLDEMIYNV KEFERLGFSC PIMIGGATTS KAHNAIKIAP HYSGPVAQVG DASLVVEVCS KLLNPTTAPA YTKELKEHQA KLKERFDLGK QDQSKLVSLE QSREWKFICD WEKQEIATPS FTGIKKYLDV SLEEIVPYID WSPLFWTWQL KGTYPKILNN EKYGEQAKSL FKDANIILEK VIAEKRFSPK AIVSIHKANS IGDDVEVYDD NGKKIETFHY LRQQKEKSEH KPHLCLSDYI APKESGREDY LGNFVVTMGH EVEEFAKIYE QRNDDYNAIM VKAIGDRLAE AFAEYMHKVI RDEFGYGKEE NFSNEDLIKE KYRGIRPAPG YPSCPDHTEK PIMWDLLNVE SEIGVSLTEN CAMNPPSSVS GQYFCHPGAK YFTLGPIARD QVENYSKRKD MEIKRVERWL APNLGYNPE // ID E1YYC6_9PORP Unreviewed; 1230 AA. AC E1YYC6; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFK61481.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFK61481.1}; GN Name=metH {ECO:0000313|EMBL:EFK61481.1}; GN ORFNames=HMPREF9008_03951 {ECO:0000313|EMBL:EFK61481.1}; OS Parabacteroides sp. 20_3. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Parabacteroides. OX NCBI_TaxID=469591 {ECO:0000313|EMBL:EFK61481.1}; RN [1] {ECO:0000313|EMBL:EFK61481.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=20_3 {ECO:0000313|EMBL:EFK61481.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG774998; EFK61481.1; -; Genomic_DNA. DR RefSeq; WP_005865197.1; NZ_GG774998.1. DR EnsemblBacteria; EFK61481; EFK61481; HMPREF9008_03951. DR PATRIC; 40938600; VBIBacSp9858_3703. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFK61481.1}; KW Transferase {ECO:0000313|EMBL:EFK61481.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1230 AA; 136569 MW; 0E29177212EA65FA CRC64; MNKERFLRLL NERILILDGG MGTMIQSFKL NEQDYRGERF ADFPGQLKGN NDLLCITRPD VIQSIHRQYL DAGADIFATN TFNANAISMA DYAMEAYVRE INLAAGRLSR EVADTYMAEH PDRTIFVAGS IGPTNKTASM SPDVSDPAYR AVTYKDLYNA YKEQVEGLVD GGVDIILFET TFDTLNVKAG LEAAEVVLKE KEKDLPIMLS LTLSAQGGRT FSGQTLLAFL ASIQHTHIVS VGLNCSFGAA DMKPYLQELA KYAPYYISAY PNAGLPNSFG TYDETPDKMA QHVKPFVEEG LVNIIGGCCG TTPAHISRYP ELVKGAKPHI PALKPDCLWL SGLELLEVKP ENNFVNVGER CNVAGSRKFL RLIKEGSYEE ALTIARKQVE DGAQVIDINM DDGMLDAVKE MKTFLNLIAS EPDIARVPVM IDSSKWEVIE EGLMCVQGKS IVNSISLKEG EEVFLKHAAR IKQLGAAAVV MAFDEKGQAD TYERKIEICE RAYRLLIEKI DFNLQDIIFD PNVLAIATGM EEHNGYGLAF IRAVEWIKKN LPGAKVSGGV SNLSFSFRGN NHVREAMHSV FLYHAIGKGM DMGIVNPSTS VLYEDIEPEF RTLLEDVILA RRPEAAEELI TYAQNLHVQA SGETPEKHEA WRELSLKERL EHALIKGIGD YLEDDLQEAL RTYSHAVDII DGPLMSGMNK VGELFGAGKM FLPQVVKTAR TMKKAVAILQ PAIESEKKAS GSAKAGKVIF ATVKGDVHDI GKNIVSIVLS CNNYEVIDLG VMVPADVIIK KAIEEKPDLV CLSGLITPSL EEMAHVADEM QKAGLTIPMM VGGATTSKLH TAVKIAPHYD YPVIHVLDAS QNPLIAAKLL NPDTRDAYIR ELEQEQEALR ASLGQKKETL ASLSEARKHP IEIDWTGYTP VVPARMGVHV IPYIPLEEVI PYIHWTFFFS AWKLNGRFSE ISQIHGCDSC RASWLAGFPE KDRAKATEAM QLYKDAVRLL DRLVNMKVEY CKAIYGFFSA NSEGDTIRMG DIALPLLRQQ VKKEENIYKC LSDYVIPVSE ERTDYVGAFV VTAGAGADCL KDKFEEEGDT YNSMLLQTLT DRLAEATAEY LHEKVRKEYW GYAKDESLSI PDLYKVKYQG IRPAIGYPSL PDQLLNFTLD GLLDMSRIGV SLTENGAMYP TASVSGIYIA HPSSQYFMIG SIDEEQMRDY ASRRNLTEEQ VRKLLSRNIG // ID E1Z1X5_CHLVA Unreviewed; 263 AA. AC E1Z1X5; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 07-JAN-2015, entry version 15. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EFN59570.1}; GN ORFNames=CHLNCDRAFT_132909 {ECO:0000313|EMBL:EFN59570.1}; OS Chlorella variabilis (Green alga). OC Eukaryota; Viridiplantae; Chlorophyta; Trebouxiophyceae; Chlorellales; OC Chlorellaceae; Chlorella. OX NCBI_TaxID=554065 {ECO:0000313|Proteomes:UP000008141}; RN [1] {ECO:0000313|EMBL:EFN59570.1, ECO:0000313|Proteomes:UP000008141} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NC64A {ECO:0000313|EMBL:EFN59570.1, RC ECO:0000313|Proteomes:UP000008141}; 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; GL433835; EFN59570.1; -; Genomic_DNA. DR RefSeq; XP_005851672.1; XM_005851610.1. DR GeneID; 17359258; -. DR KEGG; cvr:CHLNCDRAFT_132909; -. DR InParanoid; E1Z1X5; -. DR Proteomes; UP000008141; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008141}; KW Reference proteome {ECO:0000313|Proteomes:UP000008141}. SQ SEQUENCE 263 AA; 27474 MW; CEC79C0655F9DF30 CRC64; MGAVTLLDGG IGHLLKAKGV ERLVPGLEYE QLFLAGADVI TVNSFACTEW SLGRIGKAGL QQELLEAAAR LARAAATEAA SSGSGRQVLV AGCLPPLRES YQAQASGLRA FEEMQPEYNL LAGKRDAAVH HCDLLLCETL STCTEGLAAG TAAAASGLPW WASWTIEDRD DDAVVAVAEL PGLEAVLVNC CSPQAVAAAL PVLKAAAPPG KTTMQAWRGK LDGIILAEAY ARHAARWVDL GASIVGGCCG VGPRHIELIR RRL // ID E1ZPJ8_CHLVA Unreviewed; 1276 AA. AC E1ZPJ8; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 01-APR-2015, entry version 27. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EFN52253.1}; GN ORFNames=CHLNCDRAFT_36916 {ECO:0000313|EMBL:EFN52253.1}; OS Chlorella variabilis (Green alga). OC Eukaryota; Viridiplantae; Chlorophyta; Trebouxiophyceae; Chlorellales; OC Chlorellaceae; Chlorella. OX NCBI_TaxID=554065 {ECO:0000313|Proteomes:UP000008141}; RN [1] {ECO:0000313|EMBL:EFN52253.1, ECO:0000313|Proteomes:UP000008141} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NC64A {ECO:0000313|EMBL:EFN52253.1, RC ECO:0000313|Proteomes:UP000008141}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GL433857; EFN52253.1; -; Genomic_DNA. DR RefSeq; XP_005844355.1; XM_005844293.1. DR GeneID; 17351717; -. DR KEGG; cvr:CHLNCDRAFT_36916; -. DR InParanoid; E1ZPJ8; -. DR KO; K00548; -. DR Proteomes; UP000008141; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008141}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008141}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 264 264 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 327 327 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 328 328 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 801 801 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1276 AA; 141222 MW; DE3ACBC155C9E1BF CRC64; MTDVPAYQPW RDPLAKSEAF GQLEAMMQER IIFIDGAMGT MIQRYKLQEE DFRGERYKSH EHELKGNNDL LVLTRPDVIE EIHTAYLTGG ADIIETNTFN GTTISQADYQ LDQVEEVALI NRTAAQLAKK ATAAYMAANP GSRKFVAGAI GPTNKTLSVS PSVENPALRG VTYDEIEQAY YEQARALYEG GVDMYLVETI FDTGNAKAAI YALERFFEEQ GVRIPVFISG TIVDNSGRTL SGQTNEAFWN SVSHAKPLAI GLNCALGASD MKQYIANLSA CADCYVFCYP NAGLPNAMGG YDQRGPDMAE DIRPFCEEGL VNAIGGCCGT TPEHIAAIRE MASAYPPRQL HDVPQLLRLS GLEPLNYQPN PDNMRETFLM IGERCNVAGS IIYKKAIVDG DYDKAVSIAL SQVNAGAHVL DINMDDGLID GVPAMTRFVN LLVSDPEASR VPFMVDSSKF FIIEAGLKCC QGKCIVNSIS LKEGEDKFRE QARIVKRHGA AVVVMAFDEE GQAADCANKV RICQRAYRIL VEEVGFNPQD IIFDPNILTV GTGMAEHNNY AVDFIRGTRE IKRLCPGAKI SGGVSNIAFS FRGNEPVRRA FHSAFLHHAC KAGMDMGIVN ATQVQADVYE KIDKELLEFV EDVLLNRCEN ATERMLEYAA TLEPKCKPTD VKRKGQGVAQ NGGPKQDEWR EASVEKRLEY ALIKGIDKFV VADTEEARVS GRYPRPLNVI EGPLMDGMNV VGDLFGAGKM FLPQVIKSAR VMKRAVGHLI PYIEEEKARN GQTGDDNAGV IIMATVKGDV HDIGKNIVGV VLGCNNFKVI DMGVMCPWEK ILDAAVEHNA DIIGLSGLIT PSLDEMVTVA KRMEERGLRL PLLIGGATTS KMHTAVKIEP QYSGPVVYVL DASRSVPVAQ SLLDARQKEE FVEDIREQYS EMREEFYAGL EDRKYVTLQE AQRKGLQVDW SAPENAPVRP RQLGTQAYLD MPIEELLPYI DWNPFFQVWQ LRGRYPNRGY PKIFNDEAVG GEARKLFDEA QAMLQDIIAG KKLRIVGIVG IFPANSVGDD IEVYTDESRA QVAARFHGLR QQAEKDGDEP YYCLSDFVAP RSTGTVDYLG MFANSAMGVE AMTEVFKAEG DDYSYIMAEA LADRLAEAAA ERLHELVRRE VWGYAADEAL SVDDMLKVKY RGIRPAAGYP SQPDHTEKRT MWELMRVEQQ VGSSLTESMA MLPAASVSGL YFASPAAQYF AVGKITQDQV ADYAARKKMD LAEAQRWLRP MLNYEP // ID E1ZUA0_CHLVA Unreviewed; 861 AA. AC E1ZUA0; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EFN50595.1}; DE Flags: Fragment; GN ORFNames=CHLNCDRAFT_55718 {ECO:0000313|EMBL:EFN50595.1}; OS Chlorella variabilis (Green alga). OC Eukaryota; Viridiplantae; Chlorophyta; Trebouxiophyceae; Chlorellales; OC Chlorellaceae; Chlorella. OX NCBI_TaxID=554065 {ECO:0000313|Proteomes:UP000008141}; RN [1] {ECO:0000313|EMBL:EFN50595.1, ECO:0000313|Proteomes:UP000008141} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NC64A {ECO:0000313|EMBL:EFN50595.1, RC ECO:0000313|Proteomes:UP000008141}; 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; GL433938; EFN50595.1; -; Genomic_DNA. DR RefSeq; XP_005842720.1; XM_005842663.1. DR GeneID; 17350028; -. DR KEGG; cvr:CHLNCDRAFT_55718; -. DR InParanoid; E1ZUA0; -. DR KO; K00548; -. DR Proteomes; UP000008141; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008141}; KW Reference proteome {ECO:0000313|Proteomes:UP000008141}. FT NON_TER 1 1 {ECO:0000313|EMBL:EFN50595.1}. FT NON_TER 861 861 {ECO:0000313|EMBL:EFN50595.1}. SQ SEQUENCE 861 AA; 95907 MW; E48F0BE8F2AD02F0 CRC64; GKCIVNSISL KEGEDKFREQ ARIVKRHGAA VVVMAFDEEG QAADCANKVR ICQRAYRILV EEVGFNPQDI IFDPNILTVG TGMAEHNNYA VDFIRGTREI KRLCPGAKIS GGVSNIAFSF RGNEPVRRAF HSAFLHHACK AGMDMGIVNA TQVQADLYEK IDKELLEYVE DVLLNRREDS TERLLDYAGT LDPKSKPTAP RKLNGEPSTP AFTPKLNPIP AGVDPLAPDT DLPPVPAYQP WRDPLAKSEA FGQLEAMMQE RIIFIDGAMG TMIQRYKLQE EDFRGERYKS HEHELKGNND LLVLTRPDVI EEIHTAYLTG GADIIETNTF NGTTISQADY QLDQVEEVAL INRTAAQLAK KATAAYMAAN PGSRKFVAGA IGPTNKTLSV SPSVIKSARV MKRAVGHLIP YIEEEKARNG QTGDDNAGVI IMATVKGDVH DIGKNIVGVV LGCNNFKVQQ GVRRKVLRWV IDMGVMCPWE KILDAAVEHN ADIIGLSGLI TPSLDEMVTV AKRMEERGLR LPLLIGGATT SKMHTAVKIE PQYSGPVVYV LDASRSVPVA QSLLDARQKE EFVEDIREQY SEMREEFYAG LEDRKYVTLQ EAQRKGLQVD WSAPENAPVR PRQLGTQAYL DMPIEELLPY IDWNPFFQVW QLRGRYPNRG YPKIFNDEAV GGEARKLFDE AQAMLQDIIA GKKLRIVGIV GIFPANSVGD DIEVYTDESR AQVAARFHGL RQQAEKDGDE PYYCLSDFVA PRSTGTVDYL GMFANSAMGV EAMTEVFKAE GDDYSYIMAE ALADRLAEAA AERLHELVRR EVWGYAADEA LSVDDMLKVK YRGIRPAAGY PSQPDHTEKR TMWELMRVEQ Q // ID E1ZUG2_CHLVA Unreviewed; 561 AA. AC E1ZUG2; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EFN50533.1}; GN ORFNames=CHLNCDRAFT_37749 {ECO:0000313|EMBL:EFN50533.1}; OS Chlorella variabilis (Green alga). OC Eukaryota; Viridiplantae; Chlorophyta; Trebouxiophyceae; Chlorellales; OC Chlorellaceae; Chlorella. OX NCBI_TaxID=554065 {ECO:0000313|Proteomes:UP000008141}; RN [1] {ECO:0000313|EMBL:EFN50533.1, ECO:0000313|Proteomes:UP000008141} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NC64A {ECO:0000313|EMBL:EFN50533.1, RC ECO:0000313|Proteomes:UP000008141}; 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; GL434002; EFN50533.1; -; Genomic_DNA. DR RefSeq; XP_005842665.1; XM_005842608.1. DR GeneID; 17349966; -. DR KEGG; cvr:CHLNCDRAFT_37749; -. DR InParanoid; E1ZUG2; -. DR KO; K00548; -. DR Proteomes; UP000008141; Unassembled WGS sequence. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008141}; KW Reference proteome {ECO:0000313|Proteomes:UP000008141}. SQ SEQUENCE 561 AA; 61480 MW; 9FAC14230F3E51E9 CRC64; MLLVTCLQVQ ADLYEKIDKE LLEYVEDVLL NRREDSTERL LDYAGTLDPK SKPTAPRKLN GEPSTPAFTP KLNPIPAGVD PLAPDTDLPP VPAYQPWRDP LAKSEAFGQL EAMMQERIIF IDGAMGTMIQ RYKLQEEDFR GERYKSHEHE LKGNNDLLVL TRPDVIEEIH TAYLTGGADI IETNTFNGTT ISQADYQLDQ VEEVALINRT AAQLAKKATA AYMAANPGSR KFVAGAIGPT NKTLSVSPSV ENPALRGVTY DEIEQAYYEQ ARALYEGGVD MYLVETIFDT GNAKAAIYAL ERFFEEQGVR IPVFISGTIV DNSGRTLSGQ TNEAFWNSVS HAKPLAIGLN CALGASDMKQ YIANLSACAD CYVFCYPNAG LPNAMGGYDQ RGPDMAEDIR PFCEEGLVNA IGGCCGTTPE HIAAIREMAS AYPPRQLHDV PQLLRLSGLE PLNYQPNPDN MRETFLMIGE RCNVAGSIIY KKAIVDGDYD KAVSIALSQV NAGAHVLDIN MDDGLIDGVP AMTRFVNLLV SDPEASRVPF MVDSSKFFII EAGLKCCQVC T // ID E2AY57_CAMFO Unreviewed; 324 AA. AC E2AY57; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 07-JAN-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase 1 {ECO:0000313|EMBL:EFN61653.1}; GN ORFNames=EAG_05957 {ECO:0000313|EMBL:EFN61653.1}; OS Camponotus floridanus (Florida carpenter ant). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; OC Vespoidea; Formicidae; Formicinae; Camponotus. OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311}; RN [1] {ECO:0000313|EMBL:EFN61653.1, ECO:0000313|Proteomes:UP000000311} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20798317; DOI=10.1126/science.1192428; RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G., RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D., RA Wang J., Liebig J.; RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos RT saltator."; RL Science 329:1068-1071(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; GL443762; EFN61653.1; -; Genomic_DNA. DR InParanoid; E2AY57; -. DR Proteomes; UP000000311; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000311}; KW Methyltransferase {ECO:0000313|EMBL:EFN61653.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000311}; KW Transferase {ECO:0000313|EMBL:EFN61653.1}. SQ SEQUENCE 324 AA; 35700 MW; ABEA3F514535F37A CRC64; MTTTVKILDG GFSGQLSRHV GAKIDGDPLW TARFLATDPD AVYATHLDFL RAGVDIIETN TYQASVPGLM RYLNVNEHES LNLLAKAVGL AKKAVDIHIQ ETDNLRKPHT RPMIAGSCGP YGAYLHDSSE YTGFYGKSVS RQELIDWHRP RVQALLDAGV DLLALETIPC IEEAEALLEL LREFPHARAW LSFSCRDGQL LADGSIFQEV AVRCYRALPS QIVAVGINCI DSRYVTPLLK GINVNGKSSS QDFIPLIVYP NRGGSYSSID GWTAVPDDHS LKLPISEWVD MGVRYIGGCC KIFAEDIKVI RSEVDQYCAK ITAV // ID E2AY58_CAMFO Unreviewed; 321 AA. AC E2AY58; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 07-JAN-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase 3 {ECO:0000313|EMBL:EFN61654.1}; GN ORFNames=EAG_05958 {ECO:0000313|EMBL:EFN61654.1}; OS Camponotus floridanus (Florida carpenter ant). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; OC Vespoidea; Formicidae; Formicinae; Camponotus. OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311}; RN [1] {ECO:0000313|EMBL:EFN61654.1, ECO:0000313|Proteomes:UP000000311} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20798317; DOI=10.1126/science.1192428; RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G., RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D., RA Wang J., Liebig J.; RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos RT saltator."; RL Science 329:1068-1071(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; GL443762; EFN61654.1; -; Genomic_DNA. DR InParanoid; E2AY58; -. DR Proteomes; UP000000311; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000311}; KW Methyltransferase {ECO:0000313|EMBL:EFN61654.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000311}; KW Transferase {ECO:0000313|EMBL:EFN61654.1}. SQ SEQUENCE 321 AA; 35847 MW; 4F741CF9F5D73266 CRC64; MKIKVLDAGF STQLSTHVGD KIDGDPLWTA RFLVTDPNAV FATHLDFLRA GADIILTNTY QATIDGFVKY LNMTEEESLQ IIGNAVDYAK DAVNVYSKEI EDNANIVTNR KPLIAGSCGP YGACLHDGSE YTGSYCPNVS RQFLIDWHRP RIRTLIEKGV DLLAIETIPC VREAEAIIDL LKEFPDTYAW LTFSCRDDGK SIADGSNFQK IAMRCYKKAL PGQLLAIGIN CISPQYVTAL LKGINQNSDD FIPLVVYPNS GEKYIVSEGW KKEGEAPSLH EFIDEWLDLG VCYIGGCCRT YATDIKKIRS KVDQRQEQHI E // ID E2C779_HARSA Unreviewed; 346 AA. AC E2C779; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 07-JAN-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFN76192.1}; GN ORFNames=EAI_05587 {ECO:0000313|EMBL:EFN76192.1}; OS Harpegnathos saltator (Jerdon's jumping ant). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; OC Vespoidea; Formicidae; Ponerinae; Ponerini; Harpegnathos. OX NCBI_TaxID=610380 {ECO:0000313|Proteomes:UP000008237}; RN [1] {ECO:0000313|EMBL:EFN76192.1, ECO:0000313|Proteomes:UP000008237} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R22 G/1 {ECO:0000313|EMBL:EFN76192.1, RC ECO:0000313|Proteomes:UP000008237}; RX PubMed=20798317; DOI=10.1126/science.1192428; RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G., RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D., RA Wang J., Liebig J.; RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos RT saltator."; RL Science 329:1068-1071(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; GL453340; EFN76192.1; -; Genomic_DNA. DR InParanoid; E2C779; -. DR Proteomes; UP000008237; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008237}; KW Methyltransferase {ECO:0000313|EMBL:EFN76192.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008237}; KW Transferase {ECO:0000313|EMBL:EFN76192.1}. SQ SEQUENCE 346 AA; 39155 MW; F38A133E29779AE3 CRC64; MNQLLVLDGD FEAQLLRRSK HANEVGKSFM LQVITSEPYS VLQTHMDFLR AGAQLIRTNT HRISTGSIGT HMNLDSTEVK PMVDMAVNLA KKAIMKYLHE VHDQKTSVEQ YNFSSRPILA GCCGSYNATL FDNVFDTWKL TESLSLNYLS WFHQQRMQVL LNANVDLLTF ESIPTLREVD AIITVLKLHP TARALITFLC TENGKLLDGS NFADVAVHCY NSLTNQIFAI GTEANNAIAD WTLQVMKNIN YNREDKIPFV LYVSQSQLHT MWGEDKFSLS QQHNYVQDWL DAGICCIGGG SNTVAQDIRM ICKEVNNYCI YTNRAFASDK GSCPVYTRIQ KNLSRL // ID E2C780_HARSA Unreviewed; 343 AA. AC E2C780; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 07-JAN-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase 2 {ECO:0000313|EMBL:EFN76193.1}; GN ORFNames=EAI_05588 {ECO:0000313|EMBL:EFN76193.1}; OS Harpegnathos saltator (Jerdon's jumping ant). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; OC Vespoidea; Formicidae; Ponerinae; Ponerini; Harpegnathos. OX NCBI_TaxID=610380 {ECO:0000313|Proteomes:UP000008237}; RN [1] {ECO:0000313|EMBL:EFN76193.1, ECO:0000313|Proteomes:UP000008237} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R22 G/1 {ECO:0000313|EMBL:EFN76193.1, RC ECO:0000313|Proteomes:UP000008237}; RX PubMed=20798317; DOI=10.1126/science.1192428; RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G., RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D., RA Wang J., Liebig J.; RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos RT saltator."; RL Science 329:1068-1071(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; GL453340; EFN76193.1; -; Genomic_DNA. DR InParanoid; E2C780; -. DR Proteomes; UP000008237; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008237}; KW Methyltransferase {ECO:0000313|EMBL:EFN76193.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008237}; KW Transferase {ECO:0000313|EMBL:EFN76193.1}. SQ SEQUENCE 343 AA; 39436 MW; 6D07698751378383 CRC64; MENLMVLDGD SEAQLYQRLK PSKELEKIIA LYAVEYHKEE VIETYLDFLR AGAQIIRTNT YRLSDYTIEK YFKPESSQFY TELMEKSVKL ARAAVTKYLE EKRKDPKYSE LFDRCEILVA GCCGSSVVSE CVDKYELTLK DTQIAAQLIY FHHNDRVIEL VKYGVDILTF ESIPSLVETD IIISIMKRHH PIRGWITFLC RADGKLLDGN TLETVAMRCY DALGHQIIAI GAECPVPDVM KSIVLDIGIL KLSHEVQVPF VLYIDKVHLP ITENKEASNS LMSDYVDEWL DHGIRYIGGG INTRPEDVAL IRKQVDDYRI FSQRPFTTLR PSSYKTTKKQ SKL // ID E2C781_HARSA Unreviewed; 342 AA. AC E2C781; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 07-JAN-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFN76194.1}; GN ORFNames=EAI_05589 {ECO:0000313|EMBL:EFN76194.1}; OS Harpegnathos saltator (Jerdon's jumping ant). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; OC Vespoidea; Formicidae; Ponerinae; Ponerini; Harpegnathos. OX NCBI_TaxID=610380 {ECO:0000313|Proteomes:UP000008237}; RN [1] {ECO:0000313|EMBL:EFN76194.1, ECO:0000313|Proteomes:UP000008237} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R22 G/1 {ECO:0000313|EMBL:EFN76194.1, RC ECO:0000313|Proteomes:UP000008237}; RX PubMed=20798317; DOI=10.1126/science.1192428; RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G., RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D., RA Wang J., Liebig J.; RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos RT saltator."; RL Science 329:1068-1071(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; GL453340; EFN76194.1; -; Genomic_DNA. DR InParanoid; E2C781; -. DR Proteomes; UP000008237; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008237}; KW Methyltransferase {ECO:0000313|EMBL:EFN76194.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008237}; KW Transferase {ECO:0000313|EMBL:EFN76194.1}. SQ SEQUENCE 342 AA; 38583 MW; 5D076B5C508A85BA CRC64; MDKVIVLDGA LDKQLSRNMP HISETDEVLA MRALMYDQDA VYKAHLDFLR AGAQIIRTNT YRTTISLFPS AFGLPICICD QTRVITAVAL AKKAVRKYFE EIGGDSNNIE DYNQRRPLIA GCCDGYNFLP FYDVGKITKE LPISQLLSFH EERIDILVRS GVDILAFESI SCLIEVIAIS QALRKYPTIR VWITFLCKMN GDLLDDNLLI TAIMLCKETL PGQLMAVGVE CQYIASSLEP IRTLMRNINN FKDWVFPFLF YIDKNHLSTM TVPVDAAGPS RPVQPVAQWL DIGVRYVGGG FGTNAEDIKE ICREVDYYRI SRGEMFATLM TCSAQNKNLS KM // ID E2C782_HARSA Unreviewed; 339 AA. AC E2C782; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 07-JAN-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFN76195.1}; GN ORFNames=EAI_05590 {ECO:0000313|EMBL:EFN76195.1}; OS Harpegnathos saltator (Jerdon's jumping ant). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; OC Vespoidea; Formicidae; Ponerinae; Ponerini; Harpegnathos. OX NCBI_TaxID=610380 {ECO:0000313|Proteomes:UP000008237}; RN [1] {ECO:0000313|EMBL:EFN76195.1, ECO:0000313|Proteomes:UP000008237} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R22 G/1 {ECO:0000313|EMBL:EFN76195.1, RC ECO:0000313|Proteomes:UP000008237}; RX PubMed=20798317; DOI=10.1126/science.1192428; RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G., RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D., RA Wang J., Liebig J.; RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos RT saltator."; RL Science 329:1068-1071(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; GL453340; EFN76195.1; -; Genomic_DNA. DR InParanoid; E2C782; -. DR Proteomes; UP000008237; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008237}; KW Methyltransferase {ECO:0000313|EMBL:EFN76195.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008237}; KW Transferase {ECO:0000313|EMBL:EFN76195.1}. SQ SEQUENCE 339 AA; 38953 MW; 3FEEFB4DA5386DD2 CRC64; MMDARKEIKT IDGDFVAQLC CNLKKQANFE AVDPLVDIRI IQTNRYAIYR VHLDFLHAGA TIIRTNTARI SEAALSKINS NKSVRYFIKN AVLLARKAVC KYYKETRGDM QSPEIYDRNR PQIAGYCTNF LKSCFRKGLP FDYWNEVSRE EMLKLHRLRI RELLKAGVDM LAIEDIHNMV ELKIIVEVLR RYKSAKVWIS FTCLNDVELF DGSLLLDAIK HCRRSLHSGQ IIAIGAKCWM DGKELSLLKD IYNATRKDRI PLIAYINEEV LKFYQPDIMY YVKEAVKYGA KYFSGDNGGN LNEIKMISSL AHTYNIIHFT YFPDLSTSSS SSSSSSDSS // ID E2C783_HARSA Unreviewed; 346 AA. AC E2C783; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 07-JAN-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFN76196.1}; GN ORFNames=EAI_05591 {ECO:0000313|EMBL:EFN76196.1}; OS Harpegnathos saltator (Jerdon's jumping ant). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; OC Vespoidea; Formicidae; Ponerinae; Ponerini; Harpegnathos. OX NCBI_TaxID=610380 {ECO:0000313|Proteomes:UP000008237}; RN [1] {ECO:0000313|EMBL:EFN76196.1, ECO:0000313|Proteomes:UP000008237} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R22 G/1 {ECO:0000313|EMBL:EFN76196.1, RC ECO:0000313|Proteomes:UP000008237}; RX PubMed=20798317; DOI=10.1126/science.1192428; RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G., RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D., RA Wang J., Liebig J.; RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos RT saltator."; RL Science 329:1068-1071(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; GL453340; EFN76196.1; -; Genomic_DNA. DR InParanoid; E2C783; -. DR Proteomes; UP000008237; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008237}; KW Methyltransferase {ECO:0000313|EMBL:EFN76196.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008237}; KW Transferase {ECO:0000313|EMBL:EFN76196.1}. SQ SEQUENCE 346 AA; 38451 MW; CC77676E2AD7BD67 CRC64; MLRLPTVLDG DFISQTAANM GKTSIDDLPS ILATVTNEST MFDTHLAFLR AGANMIRTNT YRTSVYNLNH FLGINVNNSA SVITKAAMAA RKAVLTHHSE TSNDPTNQEV FHKTRPWIVG SCGPYGASLG DGTEYTGAYA KHLSLEDLID WHEPRVRALL DAGVDMLSLG SVPCAKEAAA FVELMRNFPS TRVWISFYCY NDRILADGSN FRKIVKHCYN RLGDQMIAIG VSCVESSLVK PLFNIINREI FPRKIPLLVC PDKTTYRFKE DFTMETTGTT RSFFELPISD WLNDGAGIIG GCCGTLTDDI KYIRSEVDKY QDNVTIKQCP VNKNCSFNPS VDKAKL // ID E2C786_HARSA Unreviewed; 323 AA. AC E2C786; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 07-JAN-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase 2 {ECO:0000313|EMBL:EFN76199.1}; GN ORFNames=EAI_05594 {ECO:0000313|EMBL:EFN76199.1}; OS Harpegnathos saltator (Jerdon's jumping ant). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; OC Vespoidea; Formicidae; Ponerinae; Ponerini; Harpegnathos. OX NCBI_TaxID=610380 {ECO:0000313|Proteomes:UP000008237}; RN [1] {ECO:0000313|EMBL:EFN76199.1, ECO:0000313|Proteomes:UP000008237} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R22 G/1 {ECO:0000313|EMBL:EFN76199.1, RC ECO:0000313|Proteomes:UP000008237}; RX PubMed=20798317; DOI=10.1126/science.1192428; RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G., RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D., RA Wang J., Liebig J.; RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos RT saltator."; RL Science 329:1068-1071(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; GL453340; EFN76199.1; -; Genomic_DNA. DR InParanoid; E2C786; -. DR Proteomes; UP000008237; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008237}; KW Methyltransferase {ECO:0000313|EMBL:EFN76199.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008237}; KW Transferase {ECO:0000313|EMBL:EFN76199.1}. SQ SEQUENCE 323 AA; 36060 MW; 44785048173EA996 CRC64; MTQCAKVLDG GFSSQLSRHV GAKFDDDPLW TARFLQTNPS AVYNTHLDYL RAGAEIIETN TYQASVPGLM KYLNISMDES LALLAKAVEL AKQAVVTYMK ENTTNDKQGG EKPLVAGSCG PYGACLHDKS EYTGAYGKSM SRQELMDWHR PRIQALLDAG VDLLALETIP YAEEADALVE LLREFPRARA WLSFSCRDDR HIADGSDFRE VAVRCYRALP EQVVAVGVNC VPPNYVKTLL QGINKEERSQ DFIPLIVYPN RGGCYSETDE WIPVPDDQRI NLPVLDWLDL GVRYIGGCCK VFAEDIGAIR SLVNRCHPAE QRH // ID E2C787_HARSA Unreviewed; 321 AA. AC E2C787; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFN76200.1}; GN ORFNames=EAI_05595 {ECO:0000313|EMBL:EFN76200.1}; OS Harpegnathos saltator (Jerdon's jumping ant). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; OC Vespoidea; Formicidae; Ponerinae; Ponerini; Harpegnathos. OX NCBI_TaxID=610380 {ECO:0000313|Proteomes:UP000008237}; RN [1] {ECO:0000313|EMBL:EFN76200.1, ECO:0000313|Proteomes:UP000008237} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R22 G/1 {ECO:0000313|EMBL:EFN76200.1, RC ECO:0000313|Proteomes:UP000008237}; RX PubMed=20798317; DOI=10.1126/science.1192428; RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G., RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D., RA Wang J., Liebig J.; RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos RT saltator."; RL Science 329:1068-1071(2010). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL453340; EFN76200.1; -; Genomic_DNA. DR InParanoid; E2C787; -. DR Proteomes; UP000008237; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008237}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EFN76200.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008237}; KW Transferase {ECO:0000313|EMBL:EFN76200.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 232 232 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 301 301 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 321 AA; 35465 MW; 455B79E30F7EC7B0 CRC64; MSKIKVLDGG FSTQLSTHVG DRIDGDPLWT ARFLITDPNA VFATHLDFLR AGADIIQTNT YQATIDGFVK YVGISEEESL EIIRRAVDYA KNAVNAYTKE IADDESIMSR NKPLIAGSCG PYGACQHDGS EYTGSYGTRV SKEFLINWHR PRVRALLEEG VSLLAIETIP CEREADAVVE LLKEFPDARA WLSFSCRDDG KNLADGTSFR ETAVRCYKNA LPGQIIAVGV NCIAPQHVTS LLKGVNKGNT DDNLIPLVVY PNSGEKYLVT EGWKKCGEAP SLHEFIDEWL DLGVRYIGGC CRTCAVDVKR IKSKVDHRRA T // ID E2CKI5_9RHOB Unreviewed; 1242 AA. AC E2CKI5; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 01-APR-2015, entry version 24. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFO31083.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFO31083.1}; GN Name=metH {ECO:0000313|EMBL:EFO31083.1}; GN ORFNames=TRICHSKD4_3607 {ECO:0000313|EMBL:EFO31083.1}; OS Roseibium sp. TrichSKD4. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseibium. OX NCBI_TaxID=744980 {ECO:0000313|EMBL:EFO31083.1}; RN [1] {ECO:0000313|EMBL:EFO31083.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TrichSKD4 {ECO:0000313|EMBL:EFO31083.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GL476318; EFO31083.1; -; Genomic_DNA. DR RefSeq; WP_009467906.1; NZ_GL476318.1. DR EnsemblBacteria; EFO31083; EFO31083; TRICHSKD4_3607. DR PATRIC; 41703735; VBIRosSp158592_3442. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFO31083.1}; KW Transferase {ECO:0000313|EMBL:EFO31083.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 249 249 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 764 764 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1242 AA; 136333 MW; 3C17109A4B2F19F1 CRC64; MLKSEAFERI QEAAQSRILV LDGAMGTELQ LLKLKEDDFR GDRFKDWPSD LAGNNDILSL SQPDAIRKIH VDYLEAGADI VETNTFSSTT IAQADYGMEE LAFELNVESA KLARQACDIV EAKDTSRPRF VAGALGPTNR TASISPDVNN PGYRAVSFDD LRIAYAEAVR GLLEGGADIL LVETIFDTLN AKAALFAIDE VFEERDKAVP VMISGTITDL SGRTLSGQTP EAFWNSVRHS NPLTIGLNCA LGAKEMRAHL AEISRVADTL VCAYPNAGLP NEFGEYDESP EYMASLIEEF AEAGLVNVVG GCCGSTPAHI RAIAEAVKDK APRKIAEPPV HMRLSGLEPF TLTPEVNFVN VGERTNVTGS ARFRKLIKTG DYTTALDVAR DQVENGAQII DVNMDEGLLD SEEAMVTFLN LMAAEPDISK VPVMVDSSKW SVIEAGLKCL QGKGVVNSIS LKEGEENFIE QANLIRRYGA AVVIMAFDEQ GQADTFERKI EICKRSYDVL VEKVGFPPED IIFDPNIFAV ATGIEEHNNY GVDFIEATGW IRENLPHAHV SGGVSNLSFS FRGNEGVREA MHSVFLYHAI KKGMDMGIVN AGQLAVYDKL DKELRDLCED VVLNRTPDAT DNMLEAAERW KGEGGKKREV DLSWRELPVA KRLEHALVNG IDEYVVEDTE EARTQFDRPL HVIEGPLMDG MNVVGDLFGS GQMFLPQVVK SARVMKKAVA YLMPFMEKEK EEQGLEGASS NGKILMATVK GDVHDIGKNI VGVVLQCNNF EVIDLGVMVP AAKILEVAKE EKVDIIGLSG LITPSLDEMC HVAGELEREG LDVPLLIGGA TTSEVHTAVK IHPNYARGQA IYVTDAGRAV GVASRLMSDG QRTPYFEEVR GKYATIAEKH AASRGTSQRV SIEAARENAF KPDFKTHRPV KPKQLGSKVY DDFPLEDLVP LIDWTPFFAT WEIKGRYPDV LTDNRYGPAA KGLYDDARRM LDEIVEKKLL TARGMAALWP AAGRGDDIVL FKDDSRSEEL ATFYTLRQQM ARTAGGRANV ALSDFVAPEA SGLADYVGGF AVTAGHGEDE LAGRYAKAGD DYNKILSQAL ADRLAEAFAE KLHQIVRTEL WGYAANETLS NEEIIAEKYQ GIRPAPGYPA QPDHTEKETL FRLLDAERLT GIQLTESYAM APGSSVSGLY FGHPDSHYFG VGKIEKDQVE DYAMRKGWDL AYAERWLAPI LNYDPARLIA AE // ID E2CPW9_9RHOB Unreviewed; 346 AA. AC E2CPW9; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 01-OCT-2014, entry version 19. DE SubName: Full=Chain B, Cobalamin-Dependent Methionine Synthase {ECO:0000313|EMBL:EFO29512.1}; GN ORFNames=TRICHSKD4_5341 {ECO:0000313|EMBL:EFO29512.1}; OS Roseibium sp. TrichSKD4. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseibium. OX NCBI_TaxID=744980 {ECO:0000313|EMBL:EFO29512.1}; RN [1] {ECO:0000313|EMBL:EFO29512.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TrichSKD4 {ECO:0000313|EMBL:EFO29512.1}; 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; GL476320; EFO29512.1; -; Genomic_DNA. DR RefSeq; WP_009759760.1; NZ_GL476320.1. DR EnsemblBacteria; EFO29512; EFO29512; TRICHSKD4_5341. DR PATRIC; 41707089; VBIRosSp158592_5540. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 346 AA; 35972 MW; 8E2AAD870EAA54F0 CRC64; MGKKIMSKFE DLLANKGALL ADGATGTTLF DMGLTSGDAP ELWNVDEPEK IKELHRGFAE AGSDIILTNT FGANRHRLKL HNAEGRVKEL NAAGVRLARE VGEALGRDVL VAGSIGPTGE LFQPLGALSF EEAVEAFVEQ IDGLIEGGTD ILWVETMSAP EEMKAAAEAA KGKGVPLVIT ASFDTAGKTM MGLSPKGMAQ LKSEFSCEPV AIGSNCGVGA SDLLAAISEI TEADPSAIVV AKANCGIPEV RGDEVVYTGT PELMGKYTHM ALDAGARIIG GCCGTSAGHL AAMRSAMDTH TKGERPTLEA ILSEIGPLVS PPNLEADAAR ESDGGGSGRR RGRRRG // ID E2MWQ9_CORAY Unreviewed; 1219 AA. AC E2MWQ9; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEB63149.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EEB63149.1}; GN Name=metH {ECO:0000313|EMBL:EEB63149.1}; GN ORFNames=CORAM0001_0986 {ECO:0000313|EMBL:EEB63149.1}; OS Corynebacterium amycolatum SK46. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=553204 {ECO:0000313|EMBL:EEB63149.1}; RN [1] {ECO:0000313|EMBL:EEB63149.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK46 {ECO:0000313|EMBL:EEB63149.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EEB63149.1}. 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; ABZU01000007; EEB63149.1; -; Genomic_DNA. DR RefSeq; WP_005510794.1; NZ_ABZU01000007.1. DR EnsemblBacteria; EEB63149; EEB63149; CORAM0001_0986. DR PATRIC; 29089493; VBICorAmy112151_1249. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EEB63149.1}; KW Transferase {ECO:0000313|EMBL:EEB63149.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 230 230 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 296 296 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 297 297 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1219 AA; 132701 MW; AAA31AE420DF259A CRC64; MTERHSSEFL TALHSRVLIG DGAMGTQLQS FDLDVDADFL GYEGCNEILN DTRPDIIETI HRRYFEAGAD LVETNTFGCN FPNLADYDIE DRIQELAHKG TAIARKVADE MGPGREGMRR FVLGSLGPGT KLPSLGHAPY AQLRDAYTEA GLGMISGGAD AFLIETCQDL LQVKAAVNGV KAAMRQADKK IPIVVHVTVE TTGTMLMGSE IGAALAALQP LGIDMIGLNC ATGPDEMSEH LRYLSSFASI PVSVMPNAGL PVLGKNGATY PLTAPELATA LRGFVEEFGL SMVGGCCGTT PEHVSAVRDA ITGTGAYAEQ GPAVQAARPS TDPNAKPIDE VASLYSATPL TQTTGITMIG ERTNANGSKA FREAMLAGDW EKCLNTARGQ VTDGAHMIDL CVDYVGRDGR DDMATLASQI ATSVTLPVML DSTEPEVLKT GLEHLGGRCA VNSVNFEDGD GPDSRYQRIM RQVVEHGAAV VALTIDEEGQ ARTKDKKIEI AERLIADITG TWGLREQDII VDCLTFPIST GQEETRRDGI ETIEAIRELK RRHPNVHTTL GLSNISFGLN PAARQVLNSV FLNECIEAGL DSAIAHSSKI LPMNKIDDKQ REVALDMVYD RRREAGHPDG EYDPLQVFME LFEGVSAADA KDARAEQLAA MPLFDRLAQR IIDGERTGIE ADLDESMKEK EPLAIVNEDL LRGMQTVGDL FGSGQMQLPF VLQSAETMKA AVGYLEGFMD AEDATGSKGS IVLATVKGDV HDIGKNLVEI ILSNNGYTVH NLGIKQPIAT ILSAAKELDV DAIGMSGLLV KSTVVMKDNL LEINSAGDAA RFPVLLGGAA LTRSYVEDDL SELYHGDVYY GRDAFEGLRI MDELMAAKKG LGPDENSPEA IAAREKKEAR RARRERSKRI AAQRAAKAAA EAPEVPERSD VAADVPVATP PFWGTRIVKG LPLDDYLTTL DERALFMGQW GLRGTRGDEG PSYEELVESD GRPRLRAWLQ RLRAENILQH AAVVYGYFPA VSEGDTVHVL PLPAEGEQPD PTAEPVVSWT FPRQQRGRFL CIADFIRSRE DAIAAGQTDV MPFQLVTMGQ PIADFANDIY AKNEYRDYLE VHGIGVQLTE ALAEYWHQRI RSELAFSDGT SVGAEDSDDT QDFFDLKYRG ARYSFGYGSC PDLTFRQGMI DLLQPERIGV ELSEELQLHP EQSTDAFVLY HPEAKYFNV // ID E2N876_9BACE Unreviewed; 297 AA. AC E2N876; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Homocysteine S-methyltransferase domain protein {ECO:0000313|EMBL:EEF91874.1}; GN ORFNames=BACCELL_00471 {ECO:0000313|EMBL:EEF91874.1}; OS Bacteroides cellulosilyticus DSM 14838. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=537012 {ECO:0000313|EMBL:EEF91874.1}; RN [1] {ECO:0000313|EMBL:EEF91874.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 14838 {ECO:0000313|EMBL:EEF91874.1}; 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] {ECO:0000313|EMBL:EEF91874.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 14838 {ECO:0000313|EMBL:EEF91874.1}; 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. {ECO:0000313|EMBL:EEF91874.1}. 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; ACCH01000041; EEF91874.1; -; Genomic_DNA. DR RefSeq; WP_007209861.1; NZ_EQ973488.1. DR EnsemblBacteria; EEF91874; EEF91874; BACCELL_00471. DR PATRIC; 26969580; VBIBacCel136693_0315. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEF91874.1}; KW Transferase {ECO:0000313|EMBL:EEF91874.1}. SQ SEQUENCE 297 AA; 32738 MW; CC626EB2253FC1D6 CRC64; MEGALGERLK REYGLTINGS VAMADLIYSQ QGRLALDTLW RGYMGIAEKY NLPFLATTPT RRANKQQVIQ AGYDEAIIED NVRFLRKIKE TSNIEMYIGG LMGCKGDAYT GAGALNIEEA HDFHHWQAQL FKLAKADFLY AGIMPVLAEA MGMARAMSDT GIPYIISFTI QKDGKLIDGH TIDYAIRFID DNVSRKPVCY MTNCVHPCIV YEALAHNFNQ TEAVRTRFIG IQANTSALSY SELDGSADLQ SSSPADLAEG MMKLKSEYDF RIFGGCCGTD DTHMGEIAKS ISCGALS // ID E2NLR3_9BACE Unreviewed; 297 AA. AC E2NLR3; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEF87140.1}; GN ORFNames=BACCELL_05257 {ECO:0000313|EMBL:EEF87140.1}; OS Bacteroides cellulosilyticus DSM 14838. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=537012 {ECO:0000313|EMBL:EEF87140.1}; RN [1] {ECO:0000313|EMBL:EEF87140.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 14838 {ECO:0000313|EMBL:EEF87140.1}; 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] {ECO:0000313|EMBL:EEF87140.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 14838 {ECO:0000313|EMBL:EEF87140.1}; 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. {ECO:0000313|EMBL:EEF87140.1}. 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; ACCH01000432; EEF87140.1; -; Genomic_DNA. DR RefSeq; WP_007214590.1; NZ_EQ973495.1. DR EnsemblBacteria; EEF87140; EEF87140; BACCELL_05257. DR PATRIC; 26978142; VBIBacCel136693_4565. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEF87140.1}; KW Transferase {ECO:0000313|EMBL:EEF87140.1}. SQ SEQUENCE 297 AA; 32621 MW; DABC14438793821B CRC64; MVSIEKLVRE RILILDGAMG TMIQRYNLTE EDFRGERFAD IPGQMKGNND LLCLTRPDVI QDIHRKYLMA GADIIETNTF SSTSVSMADY HVQEYVREMN LAAVKLAREV ADEFSTPDKP RFVAGSIGPT NKTCSMSPDV NNPAMRALTY DELADAYREQ MEALLEGGVD ALLIETIFDT LNAKAAIFAA EKAMEATGIQ VPVMLSVTVS DTGGRTLSGQ TLEAFLASVQ HANIFSVGLN CSFGARQLKP FLEQLAARAP YYISAYPNAG LPNSLGQYDQ TPADMAHEVK EYIQEGL // ID E2NUH8_9FIRM Unreviewed; 791 AA. AC E2NUH8; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EEF93104.1}; GN ORFNames=CATMIT_02259 {ECO:0000313|EMBL:EEF93104.1}; OS Catenibacterium mitsuokai DSM 15897. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae; Catenibacterium. OX NCBI_TaxID=451640 {ECO:0000313|EMBL:EEF93104.1}; RN [1] {ECO:0000313|EMBL:EEF93104.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 15897 {ECO:0000313|EMBL:EEF93104.1}; 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. {ECO:0000313|EMBL:EEF93104.1}. 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; ACCK01000410; EEF93104.1; -; Genomic_DNA. DR RefSeq; WP_006506443.1; NZ_ACCK01000410.1. DR EnsemblBacteria; EEF93104; EEF93104; CATMIT_02259. DR PATRIC; 30396110; VBICatMit90418_1631. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EEF93104.1}; KW Transferase {ECO:0000313|EMBL:EEF93104.1}. SQ SEQUENCE 791 AA; 85659 MW; 03D4CD38AF943B2A CRC64; MGFKERLTKE WLFWDGGTGS VLQSWGLQAG ELPETWNIIH PEKIVELNKG YLEAGCDIIN TNTFGANRLK YPDNLEEIVT KAVEHAKKAR ELTGRADALI ALDLGPTGKL LEPLGDLSFD DAVDIYAEVI EYGTKAGADV ILIETMQDSY ELKAAVLAAK EHSDLPVCAT VVFDEKGKML TGGTPESVVA LLEGLHIDAL GINCSLGPRQ IKPFVERMIQ VSSTPIIVTP NAGLPQTDDE GHTYYDMSAD DFALEMKEIA SLNVHVLGGC CGTTPEYLSK TIELVKDLPI EPPVKKNMSV VTSFSQSVEI GPKPVIIGER INPTGKKKFK QALRDGDINY ILSEGLKQED AGAHILDVNV GLPEIDEPKM MVEVMKKLQS VIALPLQIDT SDPIALEAAL RHYNGKAMIN SVNGKQESMD AVFPLVQKYG GVVVGLALDE DGIPDNAADR IRIAKKIYKE AGKYGIEPKD IVIDGLAMTI SSDPTSAIAT LETLRIIRDE LHGHSILGVS NISFGLPQRP IVNANFFTMA MQSGLSCAII NPSSEAMMKS YRAYLALSGL DTNFTEYISA YGNSAPATPI KSEAVDMSLY ESIKRGMSEN AGKATKKQLE SKEGLEIINE ELIPALDEVG KGFEKGTIFL PQLLMSAEAA KAAFAVIKDS MAGKPRKMKG KIIIATVKGD IHDIGKNIVK VMLENYGYDV IDLGKDVPPE QIVDTAIQED VKLVGLSALM TTTVVSMEDT IKLLKEKKPD TLTVVGGAVM TQEYAGRIGA DCYAKDAMET VRFADKVFGG E // ID E2P8W1_PASHA Unreviewed; 298 AA. AC E2P8W1; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EEY12318.1}; GN ORFNames=COK_1601 {ECO:0000313|EMBL:EEY12318.1}; OS Mannheimia haemolytica serotype A2 str. BOVINE. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Mannheimia. OX NCBI_TaxID=669262 {ECO:0000313|EMBL:EEY12318.1, ECO:0000313|Proteomes:UP000004125}; RN [1] {ECO:0000313|EMBL:EEY12318.1, ECO:0000313|Proteomes:UP000004125} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BOVINE {ECO:0000313|EMBL:EEY12318.1}; 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. {ECO:0000313|EMBL:EEY12318.1}. 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; ACZY01000058; EEY12318.1; -; Genomic_DNA. DR RefSeq; WP_006251729.1; NZ_ACZY01000058.1. DR EnsemblBacteria; EEY12318; EEY12318; COK_1601. DR PATRIC; 36009977; VBIManHae138272_1541. DR Proteomes; UP000004125; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000004125}; KW Methyltransferase {ECO:0000313|EMBL:EEY12318.1}; KW Transferase {ECO:0000313|EMBL:EEY12318.1}. SQ SEQUENCE 298 AA; 32644 MW; 330F4B23BA00B957 CRC64; MQITILDGGI SRELMRRNAP FHQPEWSAAA LYEGPHFVQA VHEDFIAHGA EVITTDSYAV VPFHIGEKRF AADGKMLADL AGRLAKQAVK NSENFATQIA GSLPPMFGSY RADLIQMERF AEVAQPLIDG LSPYVDIWLC ETQSAIIEPI SIKALLPKDN RPLWVSFTLT DDEPTTEPQL RSGESVKQAV EEMVKLGVQA ILFNCCQPEV IGEALSVTQK TLAELKATHI RTGAYANAFA PQPKDATAND GLDEVRQDLT LEAYLGWAKK WTEQGATIIG GCCGIGVEYI ETLAKNLK // ID E2PBA1_PASHA Unreviewed; 589 AA. AC E2PBA1; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EEY11426.1}; GN ORFNames=COK_2458 {ECO:0000313|EMBL:EEY11426.1}; OS Mannheimia haemolytica serotype A2 str. BOVINE. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Mannheimia. OX NCBI_TaxID=669262 {ECO:0000313|EMBL:EEY11426.1, ECO:0000313|Proteomes:UP000004125}; RN [1] {ECO:0000313|EMBL:EEY11426.1, ECO:0000313|Proteomes:UP000004125} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BOVINE {ECO:0000313|EMBL:EEY11426.1}; 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. {ECO:0000313|EMBL:EEY11426.1}. 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; ACZY01000083; EEY11426.1; -; Genomic_DNA. DR EnsemblBacteria; EEY11426; EEY11426; COK_2458. DR PATRIC; 36011653; VBIManHae138272_2349. DR Proteomes; UP000004125; Unassembled WGS sequence. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000004125}. SQ SEQUENCE 589 AA; 64432 MW; 3E14DE96E6CC96E6 CRC64; MNTQHRTELL QNALTERILI LDGAMGTMIQ KYKLTESDFR GERFKNSTID LKGNNDLLTL TQPLLISAIH EKYLAAGADI IETNTFSATT IAQADYELES IAYGLNLVGA KLARLAADKF STPEKPRFVA GILGPTNRTC SISPDVNDPG FRNITFMQLV EAYAEATRGL IEGGADLIMI ETIFDTLNAK AAVFAIETVF DELGVKLPIM ISGTITDASG RTLSGQTTEA FYNSLRHAKP LTFGLNCALG PKELRPYVEM MSKISETFVS VHPNAGLPNA FGGYDLGAEE MATYIKEWAE LGWLNIVGGC CGTTPEHIQA FAEATKGVAP RKLPEIPTAM RLSGLEPLTI DDNSLFVNVG ERNNVTGSAK FKKLIKEEKF AEAIEIAISQ VENGAQVIDV NMDEALLDSK KCMTRFLNIL ATEPEAAKVP IMIDSSKWEV IEAGLQTVQG KPIVNSISLK EGEEKFIHQA KLCRRYGAAV VVMAFDEVGQ ADTEERKVEI CTRAYRILVD QLGFPPEDII FDPNIFAIAT GIEEHNNYGV DFIQACERIK RDLPHAKISG GVSNVSFSYQ GLRVSGNLAI NGKLLKYAQ // ID E2PQ50_9RHIZ Unreviewed; 1261 AA. AC E2PQ50; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 01-APR-2015, entry version 24. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFM58865.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFM58865.1}; GN Name=metH {ECO:0000313|EMBL:EFM58865.1}; GN ORFNames=BIBO2_2308 {ECO:0000313|EMBL:EFM58865.1}; OS Brucella sp. BO2. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=693750 {ECO:0000313|EMBL:EFM58865.1}; RN [1] {ECO:0000313|EMBL:EFM58865.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BO2 {ECO:0000313|EMBL:EFM58865.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFM58865.1}. 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; ADFA01000126; EFM58865.1; -; Genomic_DNA. DR RefSeq; WP_009364807.1; NZ_ADFA01000126.1. DR EnsemblBacteria; EFM58865; EFM58865; BIBO2_2308. DR PATRIC; 41376022; VBIBruSp146994_2492. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFM58865.1}; KW Transferase {ECO:0000313|EMBL:EFM58865.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 263 263 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 326 326 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 327 327 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 783 783 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1261 AA; 138574 MW; 409D5003A4548A1C CRC64; MASSLDDLFG ATAAKPDGSE VLAALTQAAR ERILILDGAM GTQIQGLGFH EEHFRGDRFA TCDCQLQGNN DLLTLTQPKA IEEIHYAYAM AGADILETNT FSSTSIAQAD YGMEAMVYDL NRDGARLARR AALRAEQKDG RRRFVAGALG PTNRTASLSP DVNNPGFRAV TFDDLRIAYS EQIRGLIDGG SDIILIETIF DTLNAKAAVF ATEEVFAEKG VRLPVMISGT ITDLSGRTLS GQTPTAFWYS LRHARPFTIG LNCALGANAM RAHLDELSGI ADAFICAYPN AGLPNEFGQY DETPEAMAAQ IEGFARDGLV NVVGGCCGST PDHIRAIAQA VAKYEPRKPA KVPPLMRLSG LEPFTLTKDI PFVNIGERTN VTGSARFRKL VKAGDFAAAL DVARDQVANG AQIIDINMDE GLIDSEKAMV EFLNLIAAEP DIARVPIMLD SSKWEVIEAG LKCVQGKAVV NSISLKEGEE AFLHHARLVR AYGAAVVIMA FDETGQADTQ ARKIEICTRA YKILTEQVGF PPEDIIFDPN IFAVATGIEE HNNYGVDFIE ATREIVRTLP HVHISGGVSN LSFSFRGNEP VREAMHAVFL YHAIQAGMDM GIVNAGQLAV YDTIDAELRE ACEDVVLNRP TKTGESATER LLEIAERFRD SGSREARTQD LSWREWPVEK RLEHALVNGI TEYIEADTEE ARLAAERPLH VIEGPLMAGM NVVGDLFGSG KMFLPQVVKS ARVMKQAVAV LLPFMEEEKR LNGGEGRQSA GKVLMATVKG DVHDIGKNIV GVVLACNNYE IIDLGVMVPS QKILQVARDE KVDIIGLSGL ITPSLDEMAH VAAEMEREGF DIPLLIGGAT TSRVHTAVKI HPRYERGQAV YVVDASRAVG VVSNLLSPEG KQAYIDGLRN EYAKVAAAHA RNEAEKQRLP IARARANPHQ LDWENYEPVK PAFTGTKVFE TYDLAEIARY IDWTPFFQTW ELRGRYPAIL EDEKQGEAAR QLWADAQAML RKIIDEKWFT PRAVVGFWPA NAVGDDIRLF TDESRKEELA TLFTLRQQLT KRDGRPNVAM ADFVAPVESG KQDYVGGFVV TAGIGEIAIA ERFERANDDY SAILVKALAD RFAEAFAELM HERVRKEFWA YAPDEAFTPE ELISEPYKGI RPAPGYPAQP DHTEKTTLFR LLDATANTGV ELTESYAMWP GSSVSGLYIG HPESYYFGVA KVERDQVEDY ARRKGMDVEA VERWLTPILN YVPGASKDEA A // ID E2R716_CANFA Unreviewed; 1268 AA. AC E2R716; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 37. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCAFP00000015601}; GN Name=MTR {ECO:0000313|Ensembl:ENSCAFP00000015601}; OS Canis familiaris (Dog) (Canis lupus familiaris). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; OC Canis. OX NCBI_TaxID=9615 {ECO:0000313|Ensembl:ENSCAFP00000015601, ECO:0000313|Proteomes:UP000002254}; RN [1] {ECO:0000313|Ensembl:ENSCAFP00000015601, ECO:0000313|Proteomes:UP000002254} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000015601, RC ECO:0000313|Proteomes:UP000002254}; RX PubMed=16341006; DOI=10.1038/nature04338; RG Broad Sequencing Platform; RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B., RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., RA Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A., RA Ponting C.P., Galibert F., Smith D.R., deJong P.J., Kirkness E.F., RA Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A., RA Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M., RA Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L., RA Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J., RA Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A., RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P., RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., RA Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A., RA Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L., RA Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N., RA Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A., RA Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N., RA Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., RA Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S., RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., RA Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G., RA Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E., RA Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C., RA Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L., RA Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C., RA Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T., RA Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J., RA Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J., RA Marabella R., Maru K., Matthews C., McDonough S., Mehta T., RA Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K., RA Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J., RA Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N., RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., RA Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., RA Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., RA Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., RA Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., RA Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., RA Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., RA Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T., RA Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T., RA Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X., RA Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.; RT "Genome sequence, comparative analysis and haplotype structure of the RT domestic dog."; RL Nature 438:803-819(2005). RN [2] {ECO:0000313|Ensembl:ENSCAFP00000015601} RP IDENTIFICATION. RG Ensembl; RL Submitted (APR-2011) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 1}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSCAFP00000015601}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSCAFT00000016858; ENSCAFP00000015601; ENSCAFG00000010464. DR GeneTree; ENSGT00420000029824; -. DR InParanoid; E2R716; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG7TF786; -. DR TreeFam; TF312829; -. DR Reactome; REACT_300587; Cobalamin (Cbl, vitamin B12) transport and metabolism. DR Reactome; REACT_308293; Sulfur amino acid metabolism. DR Reactome; REACT_308831; Methylation. DR Proteomes; UP000002254; Chromosome 4. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IBA:GO_Central. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002254}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002254}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 260 260 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 785 785 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1268 AA; 140854 MW; 36292295D0B63522 CRC64; MSPALPALTP SASVKKSLQD EIEAILRERI MVLDGGMGTM IQRHKLSEED FRGHEFQDHA RSLKGNNDIL SITQPNVIYQ IHKDYLLAGA DIIETNTFSS TNVAQADYGL EHLAYQMNKC SAGVARKAAE EVSFQTGIKR FVAGALGPTN KTLSVSPSVE KPDYRNITFD ELVEAYKEQA KGLLDGGVDI LLIETIFDTA NAKAALFALQ TLFEEEYSPR PIFISGTIID KSGRTLSGQT GEAFVISVSH ASPLCIGLNC ALGAAEMRPF IETIGKCTTA YVLCYPNAGL PNTFGDYDET PQMMAMQLKD FAMDGLVNIV GGCCGTSPDH IREIAKAVKN CKPRVPPATV FEEHMLLSGL EPFRIGPYTN FVNIGERCNV AGSRKFAKLV MAGNYEEALS VAKAQVEMGA QVLDINMDDG MLDGPSAMTK FCNFIASEPD IAKVPLCIDS SNFAVIEAGL KCCQGKCIVN SISLKEGEDD FLEKARKIKK FGAAVVVMAF DEEGQATETD TKIRVCIRAY HLLVNKLGFN PNDIIFDPNI LTIGTGMEEH NLYAVNFIHA TKIIKETLPG VRVSGGLSNL SFSFRGMEAI REAMHGVFLY HAIKFGMDMG IVNAGSLPVY DDIHKELLQL CEDLIWNKDP EATEKLLRYA QTHGKGGKKV IQTDEWRNGP IEERLEYALV KGIEKHIIED TEEARLNQEK YPRPLNIIEG PLMNGMKVVG DLFGAGKMFL PQVIKSARVM KKAVGHLIPF MEEEREKNKT HAGTMEEEDP YQGTIVLATV KGDVHDIGKN IVGVVLGCNN FRVIDLGVMT PCDKILKAAL DHKAEIIDII GLSGLITPSL DEMIFVAKEM ERLAIKIPLL IGGATTSRTH TAVKIAPRYS APVIHVLDAS KSVVVCSQLL DENLKDEYFE EIMEEYEDIR QDHYESLKER RYLTLSQARK NGFHIDWLSE PPPVKPTFLG TRVFEDYDLQ KLVAYIDWKP FFDVWQLRGK YPNRSFPKIF KDKAVGEEAK KVYDDAQNML KVLISQKKLQ ARGVVGFWPA QSVQDDIHLY AEDAAPQAAE PIATFHGLRQ QAEKDSASTD PYHCLSDFIA PLHSGVRDYL GLFAVACFGV EELSKAYEQE CDDYSSIMVK ALGDRLAEAF AEELHERVRR ELWAYCSCEQ LDVVDLRRLR YEGIRPAPGY PSQPDHSEKL TMWKLANVEQ CTGIRLTESL AMAPASAVSG LYFSNLKSKY FAVGKISKDQ IEDYALRKNM SVAEVEKWLG PILGYDTE // ID E2RSV3_CANFA Unreviewed; 363 AA. AC E2RSV3; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 2. DT 27-MAY-2015, entry version 35. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCAFP00000013388}; GN Name=BHMT2 {ECO:0000313|Ensembl:ENSCAFP00000013388}; OS Canis familiaris (Dog) (Canis lupus familiaris). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; OC Canis. OX NCBI_TaxID=9615 {ECO:0000313|Ensembl:ENSCAFP00000013388, ECO:0000313|Proteomes:UP000002254}; RN [1] {ECO:0000313|Ensembl:ENSCAFP00000013388, ECO:0000313|Proteomes:UP000002254} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000013388, RC ECO:0000313|Proteomes:UP000002254}; RX PubMed=16341006; DOI=10.1038/nature04338; RG Broad Sequencing Platform; RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B., RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., RA Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A., RA Ponting C.P., Galibert F., Smith D.R., deJong P.J., Kirkness E.F., RA Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A., RA Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M., RA Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L., RA Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J., RA Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A., RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P., RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., RA Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A., RA Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L., RA Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N., RA Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A., RA Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N., RA Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., RA Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S., RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., RA Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G., RA Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E., RA Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C., RA Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L., RA Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C., RA Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T., RA Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J., RA Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J., RA Marabella R., Maru K., Matthews C., McDonough S., Mehta T., RA Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K., RA Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J., RA Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N., RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., RA Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., RA Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., RA Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., RA Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., RA Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., RA Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., RA Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T., RA Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T., RA Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X., RA Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.; RT "Genome sequence, comparative analysis and haplotype structure of the RT domestic dog."; RL Nature 438:803-819(2005). RN [2] {ECO:0000313|Ensembl:ENSCAFP00000013388} RP IDENTIFICATION. RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000013388}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSCAFP00000013388}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAEX03002116; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_546051.2; XM_546051.3. DR Ensembl; ENSCAFT00000014475; ENSCAFP00000013388; ENSCAFG00000009102. DR GeneID; 488934; -. DR KEGG; cfa:488934; -. DR CTD; 23743; -. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; E2RSV3; -. DR OMA; PEGDMHD; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000002254; Chromosome 3. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IBA:GO_Central. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IBA:GO_Central. DR GO; GO:0061627; F:S-methylmethionine-homocysteine S-methyltransferase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl. DR GO; GO:0046500; P:S-adenosylmethionine metabolic process; IEA:Ensembl. DR GO; GO:0033528; P:S-methylmethionine cycle; IBA:GO_Central. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002254}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Reference proteome {ECO:0000313|Proteomes:UP000002254}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 208 208 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 363 AA; 39523 MW; 49B300D718DC6AAA CRC64; MAPVGGPGAK KGILERLDSG EVVVGDGSFL ITLEKRGYVK AGLWTPEAIV DHPDAVRQLH MEFLRAGSNV MQTFTFSASE DNMGSKWEDV NAAACDLARE VAGKGDALVA GGISQTSVYR HHKDEARVKK LFQLQLEVFI RKNVDFLIAE YFEHAEEAVW AVEVLKESGK PVAVTMCIGP DGDMCGVKPG ECAVKLVKAG AAIVGVNCRF GPSTSLKTMK LMKEGLQAAG LQAHLIVQSL GFHTPDCGKG GVVDLPEYPF GLEPRVATRW DIQKYAREAY NLGVRYIGGC CGFEPYHIRA IAEELAPERG FLPPASEKHG SWGSGLNMHT KPWIRARARR EYWENLLPAS GRPFCPSLSQ PDA // ID E2RSW1_CANFA Unreviewed; 407 AA. AC E2RSW1; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAY-2015, entry version 39. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCAFP00000013380}; GN Name=BHMT {ECO:0000313|Ensembl:ENSCAFP00000013380}; OS Canis familiaris (Dog) (Canis lupus familiaris). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; OC Canis. OX NCBI_TaxID=9615 {ECO:0000313|Ensembl:ENSCAFP00000013380, ECO:0000313|Proteomes:UP000002254}; RN [1] {ECO:0000313|Ensembl:ENSCAFP00000013380, ECO:0000313|Proteomes:UP000002254} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000013380, RC ECO:0000313|Proteomes:UP000002254}; RX PubMed=16341006; DOI=10.1038/nature04338; RG Broad Sequencing Platform; RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B., RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., RA Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A., RA Ponting C.P., Galibert F., Smith D.R., deJong P.J., Kirkness E.F., RA Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A., RA Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M., RA Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L., RA Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J., RA Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A., RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P., RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., RA Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A., RA Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L., RA Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N., RA Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A., RA Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N., RA Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., RA Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S., RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., RA Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G., RA Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E., RA Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C., RA Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L., RA Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C., RA Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T., RA Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J., RA Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J., RA Marabella R., Maru K., Matthews C., McDonough S., Mehta T., RA Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K., RA Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J., RA Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N., RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., RA Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., RA Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., RA Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., RA Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., RA Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., RA Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., RA Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T., RA Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T., RA Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X., RA Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.; RT "Genome sequence, comparative analysis and haplotype structure of the RT domestic dog."; RL Nature 438:803-819(2005). RN [2] {ECO:0000313|Ensembl:ENSCAFP00000013380} RP IDENTIFICATION. RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000013380}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSCAFP00000013380}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAEX03002116; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_536313.2; XM_536313.4. DR ProteinModelPortal; E2RSW1; -. DR Ensembl; ENSCAFT00000014467; ENSCAFP00000013380; ENSCAFG00000009093. DR GeneID; 479171; -. DR KEGG; cfa:479171; -. DR CTD; 635; -. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; E2RSW1; -. DR KO; K00544; -. DR OMA; WGVTKGT; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR Reactome; REACT_308293; Sulfur amino acid metabolism. DR UniPathway; UPA00051; UER00083. DR NextBio; 20854390; -. DR Proteomes; UP000002254; Chromosome 3. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IBA:GO_Central. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006577; P:amino-acid betaine metabolic process; IEA:Ensembl. DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl. DR GO; GO:0033528; P:S-methylmethionine cycle; IBA:GO_Central. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR000082; SEA_dom. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50024; SEA; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002254}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Reference proteome {ECO:0000313|Proteomes:UP000002254}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 217 217 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 407 AA; 45102 MW; FCC8EA505EB80B94 CRC64; MAPVGGRKAR RGILERLNSG EVVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAVRQLH REFLRAGSNV MQTFTFYASE DKLENRGNYV AEKISGQKVN EAACDIARQV ADEGDALVAG GVSQTPSYLS CKSETEVKKV FQQQLEVFVK KNVDFLIAEY FEHVEEAVWA VEALKASGKP VAATMCIGPE GDLHGVSPGE CAVRLVKAGA SIVGVNCHFD PTISLQTVKL MKEGLDAARL KAHLMSQPLA YHTPDCNKQG FIDLPEFPFG LEPRVATRWD IQKYAREAYN LGVRYIGGCC GFEPYHIRAI AEELAPERGF LPPASEKHGS WGSGLDMHTK PWIRARARKE YWENLRIASG RPYNPSMSKP DAWGVTKGTT ELMQQKEATT EQQLKELFEK QRFKSAQ // ID E2S9W9_9ACTO Unreviewed; 1266 AA. AC E2S9W9; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFQ84043.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFQ84043.1}; GN Name=metH {ECO:0000313|EMBL:EFQ84043.1}; GN ORFNames=HMPREF0063_10759 {ECO:0000313|EMBL:EFQ84043.1}; OS Aeromicrobium marinum DSM 15272. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Nocardioidaceae; Aeromicrobium. OX NCBI_TaxID=585531 {ECO:0000313|EMBL:EFQ84043.1, ECO:0000313|Proteomes:UP000003111}; RN [1] {ECO:0000313|EMBL:EFQ84043.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 15272 {ECO:0000313|EMBL:EFQ84043.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFQ84043.1}. 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; ACLF03000003; EFQ84043.1; -; Genomic_DNA. DR RefSeq; WP_007077781.1; NZ_CM001024.1. DR EnsemblBacteria; EFQ84043; EFQ84043; HMPREF0063_10759. DR Proteomes; UP000003111; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000003111}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFQ84043.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000003111}; KW Transferase {ECO:0000313|EMBL:EFQ84043.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 254 254 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 318 318 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 771 771 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1266 AA; 139551 MW; 519DF6E4B0C1917D CRC64; MNHEQQWRPD ATDDLTRMLR ERILVLDGAM GTAIQRDRPD EAGYRGERFA DWPSDVQGNN DLLTLTQPEI IAGIHREYLE AGADMIETNT FNANCISLSD YGMQDLAYEF NLESARLARR ECDAMTQRTP DRPRYVAGAL GPTSRTASIS PDVNDPGARN VTYDELVDAY KEATRGLLDG GSDVIIIETI FDTLNAKAAI FAVETVYEEL GRRWPVIISG TITDASGRTL SGQVTEAFWH SIRHAKPLLV GLNCALGAQE MRPYIAEMAR VADTFVSCYP NAGLPNAFGE YDEEPDQTAA IVSEFADAGF VNMVGGCCGT TPAHIASIAR EVDGSTPRPV PDTTPALRLS GLEPVTVVED TLFVNVGERT NITGSARFRN LIKAGDYTTA LAVARQQVEA GAQVIDVNMD EGMIDGVEAM DRFMKLVATE PDICRVPTMI DSSKWEVIEA GLKCVQGKSI VNSISMKEGE EKFVREARLC RKYGAAVVVM AFDEEGQADN LERRRQICER AYRILVDEVG FPAEDIIFDP NVFAVATGIE EHANYGVDFI EATRWIKQNL PGALVSGGVS NVSFSFRGNN PVREAIHAVF LYHAIGAGMD MGIVNAGALE VYDEVPELLR ERIEDVILNR REDSTERLLD IAADFAGDGS VKEVATEEWR SLPVGERITH ALVKGIDEFA ESDTEELRAE ISARGGRPIE VIEGPLMAGM NVVGDLFGEG KMFLPQVVKS ARVMKKAVAY LIPFIEAEKQ PGDAERSNGK VIMATVKGDV HDIGKNIVGV VLQCNNYDVV DLGVMVPAQK ILDAAKAEGA DVIGLSGLIT PSLDEMVNFA VEMERQGFEI PLMIGGATTS RAHTAVKVAE KYHGPVIWVK DASRSVPVVA ALLSDEQRPK LLAETTADYV TLRERHAARQ DTRKLLPIAV AREKATPIDW TGYQPPRPRL LLQQARDLCS GPGCDHRHGD ATQFVKTLTD YSLAELRPYI DWQPFFNAWE MRGRFPDILN NPSTGEAARK LYEDAQQMLD QVVEEKWIRA NGVFGLFPAS QVPGDDIEVY TDESRSAVLT TLHQLRQQGE GREGSARKSL ADFVAPKDTG LRDYVGAFAV TAGVGIGEKI EEFKKNLDDY NAILLESLAD RLAEAFAERL HERVRKEFWA HSPHEALSNE DLIGEKYDGI RPAPGYPACP EHTEKQTIWE LLDVEANTGI ELTESMAMWP GASVSGLYFS HPESQYFVLG RIGRDQVEDY AGRKGWTVTE AERWLSPNLG YRTEDE // ID E2SNE3_9FIRM Unreviewed; 596 AA. AC E2SNE3; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 07-JAN-2015, entry version 20. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HMPREF0983_02659 {ECO:0000313|EMBL:EFP60952.1}; OS Erysipelotrichaceae bacterium 3_1_53. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae. OX NCBI_TaxID=658659 {ECO:0000313|EMBL:EFP60952.1}; RN [1] {ECO:0000313|EMBL:EFP60952.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_53 {ECO:0000313|EMBL:EFP60952.1}; 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., Sibley C., Daigneault M., Haas B., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Erysipelotrichaceae bacterium strain 3_1_53."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFP60952.1}. 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; ACTJ01000060; EFP60952.1; -; Genomic_DNA. DR RefSeq; WP_009273473.1; NZ_GL520141.1. DR EnsemblBacteria; EFP60952; EFP60952; HMPREF0983_02659. DR PATRIC; 42052322; VBIEryBac143843_3086. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EFP60952.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EFP60952.1}. SQ SEQUENCE 596 AA; 67328 MW; EBBC13591D41A321 CRC64; MITEYIKKQG YFLFDGAFGT YYAQKYEDDQ EPCELANLYH PQRVANIHRE YIEAGADAVK TNTFSANEQH LECSWDIIRR LLQEGYRIAK NAAQDQALVF ADIGPIMEQK NVSLFTQYKR IIDVFLEEGA DCFLFETLLN THALHEVSAY IKKRCPNATI VVSFAVTADG YSRQGIAMSK LLQDCFADDD VDACGLNCVC GPMHMKRLLD TIDKTKKPIL IMPNAGYPTI LANRTYFRDS STYFAKEMKQ ILEKGAALLG GCCGTTPVYI RKLKDALQER KEQMEAVIQS VPAQKKVNRR DCNPLRRKLQ KKQPVIAVEF DPPANCEIER FLNNAEFLKE AGVDAITIAD CPIARARVDS SLLACKLHRE LDLEVIPHMT CRDRNINATK ALLFGLQIEG IRNVLVVTGD PIPSEDRQEV KGVFNFNSQI LAGYIRDLNK TMFSEPFMIF AALNLNAVNF EAELMKAKRK VEQGVEGFLT QPIHSHQALA NLRRANAELD AYLLGGVLPI VSHRNAVYMN NEISGIEVDE EIVSLYEGTT REEAQRLAVT ISCQSVDEMR PYVDGYYLIT PFNRVEIIAD IVAHLHRQEE DASKKQ // ID E2X3U3_SHIDY Unreviewed; 1232 AA. AC E2X3U3; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFP73518.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFP73518.1}; GN Name=metH {ECO:0000313|EMBL:EFP73518.1}; GN ORFNames=SD1617_0518 {ECO:0000313|EMBL:EFP73518.1}; OS Shigella dysenteriae 1617. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=754093 {ECO:0000313|EMBL:EFP73518.1}; RN [1] {ECO:0000313|EMBL:EFP73518.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=1617 {ECO:0000313|EMBL:EFP73518.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFP73518.1}. 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; ADUT01000010; EFP73518.1; -; Genomic_DNA. DR RefSeq; WP_000095944.1; NZ_ADUT01000010.1. DR ProteinModelPortal; E2X3U3; -. DR SMR; E2X3U3; 651-1224. DR EnsemblBacteria; EFP73518; EFP73518; SD1617_0518. DR PATRIC; 42072635; VBIShiDys151583_0558. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFP73518.1}; KW Transferase {ECO:0000313|EMBL:EFP73518.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1232 AA; 136502 MW; 956C0DFD196C270E CRC64; MSSKVEQLRA QLNEHILVLD SGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVNTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSQIAECYVT AHPNAGLPNA FGEYALDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRAWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVVVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPSASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYGDAANL LI // ID E2XR39_PSEFL Unreviewed; 1243 AA. AC E2XR39; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFQ63669.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFQ63669.1}; GN Name=metH {ECO:0000313|EMBL:EFQ63669.1}; GN ORFNames=PFWH6_2475 {ECO:0000313|EMBL:EFQ63669.1}; OS Pseudomonas fluorescens WH6. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=746360 {ECO:0000313|EMBL:EFQ63669.1, ECO:0000313|Proteomes:UP000004576}; RN [1] {ECO:0000313|EMBL:EFQ63669.1, ECO:0000313|Proteomes:UP000004576} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WH6 {ECO:0000313|EMBL:EFQ63669.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFQ63669.1}. 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; AEAZ01000018; EFQ63669.1; -; Genomic_DNA. DR RefSeq; WP_003173591.1; NZ_CM001025.1. DR EnsemblBacteria; EFQ63669; EFQ63669; PFWH6_2475. DR PATRIC; 44835449; VBIPseFlu158595_2654. DR Proteomes; UP000004576; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000004576}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFQ63669.1}; KW Transferase {ECO:0000313|EMBL:EFQ63669.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 257 257 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 320 320 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 768 768 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1243 AA; 136219 MW; 49CF893A1FC9515B CRC64; MPDQSSPMSD RSARLHALHH ALKDRILILD GGMGTMIQSY KLEEHDYRGK RFADWPSDVK GNNDLLVLTR PDVIGGIEKA YLDAGADILE TNTFNATRIS MADYGMEELA YELNVEGARL ARKIADAKTA ENPAKPRFVA GVLGPTSRTC SLSPDVNNPG YRNVTFDELV ENYTEATQGL IEGGADLILI ETIFDTLNAK AAIFAVQGVF EALGIELPIM ISGTITDASG RTLSGQTTEA FWNSVAHAKP ISVGLNCALG ASELRPYLEE LSNKANTHVS AHPNAGLPNE FGEYDELPSE TAKVIEEFAQ SGFLNIVGGC CGTTPGHIEA IAKAVAGYAP RPIPDIPKAC RLSGLEPFTI DRSSLFVNVG ERTNITGSAR FARLIREDNY TEALEVALQQ VEAGAQVIDI NMDEGMLDSK KAMVTFLNLI AGEPDISRVP IMIDSSKWEV IEAGLKCIQG KGIVNSISMK EGVEQFIHHA RLCKRYGAAV VVMAFDEAGQ ADTEARKKEI CKRSYDILVN EVGFPPEDII FDPNIFAVAT GIEEHNNYAV DFINACAYIR DELPYALTSG GVSNVSFSFR GNNPVREAIH SVFLLYAIRN GLTMGIVNAG QLEIYDQIPA ELRDAVEDVV LNRTPDGTDA LLAIADKYKG EGSVKEAETE EWRGWPVNKR LEHALVKGIT THIVEDTEES RLSFARPIEV IEGPLMSGMN IVGDLFGAGK MFLPQVVKSA RVMKQAVAHL IPFIELEKGD KPEAKGKILM ATVKGDVHDI GKNIVGVVLG CNGYDIVDLG VMVPAEKILQ VAREQKCDII GLSGLITPSL DEMVHVAREM QRQDFHLPLM IGGATTSKAH TAVKIEPKYS NDAVIYVTDA SRAVGVATQL LSKELKAGFV EKTRLEYIDV RERTSNRSAR TERLSYPAAI AKKPQFDWSS YTPVVPTFTG AKVLDNIDLN VLAEYIDWTP FFISWDLAGK FPRILTDEVV GEAATALYAD AREMLRKLID EKLISARAVF GFWPTNQVQD DDLEVYGADG QPIARLHHLR QQIIKTDGKP NFSLADFVAP KDSGVTDYIG GFITTAGIGA EEVAKAYQDA GDDYNSIMVK ALADRLAEAC AEWLHQQVRK DYWGYAKDEQ LDNEALIKEQ YSGIRPAPGY PACPDHTEKA QLFQLLDPEA REMQAGRSGV FLTEHYAMFP AAAVSGWYFA HPQAQYFAVG KVDKDQVTSY TARKGQDLAV TERWLAPNLG YDN // ID E2Y059_PSEFL Unreviewed; 311 AA. AC E2Y059; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EFQ60581.1}; GN ORFNames=PFWH6_5855 {ECO:0000313|EMBL:EFQ60581.1}; OS Pseudomonas fluorescens WH6. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=746360 {ECO:0000313|EMBL:EFQ60581.1, ECO:0000313|Proteomes:UP000004576}; RN [1] {ECO:0000313|EMBL:EFQ60581.1, ECO:0000313|Proteomes:UP000004576} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WH6 {ECO:0000313|EMBL:EFQ60581.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFQ60581.1}. 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; AEAZ01000053; EFQ60581.1; -; Genomic_DNA. DR RefSeq; WP_003176996.1; NZ_CM001025.1. DR EnsemblBacteria; EFQ60581; EFQ60581; PFWH6_5855. DR PATRIC; 44842292; VBIPseFlu158595_0687. DR Proteomes; UP000004576; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000004576}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EFQ60581.1}; KW Transferase {ECO:0000313|EMBL:EFQ60581.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 218 218 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 311 AA; 32989 MW; B431F00D362F383F CRC64; MSYFHKLMSK KNMAAETVIL DGGMGRELQR RGAPFRQPEW SALALSEAPQ AVEAVHAAYI DSGANVITSN SYAVVPFHIG EARFAAEGQA LAALAGELAR RAVDACGKAV RVAGSLPPLF GSYRPDLFEA ERVTELLTPL VRGLAPHVDL WLAETQSSIA EARAIQAGLP ADGKPFWLSF TLKDEDTDDV PRLRSGEPVA QAAEAAAQLG VQVLLFNCSQ PEVIGAAIDA ARDTFARLGV AIQIGAYANA FPPQPKEATA NDGLDPLRDD LDPPGYLHWA ADWKARGASH LGGCCGIGPE HIAVLAQHLA N // ID E2ZDC4_9FIRM Unreviewed; 839 AA. AC E2ZDC4; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFQ03683.1}; GN ORFNames=HMPREF9429_01633 {ECO:0000313|EMBL:EFQ03683.1}; OS Megasphaera micronuciformis F0359. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Megasphaera. OX NCBI_TaxID=706434 {ECO:0000313|EMBL:EFQ03683.1}; RN [1] {ECO:0000313|EMBL:EFQ03683.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0359 {ECO:0000313|EMBL:EFQ03683.1}; 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 (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. {ECO:0000313|EMBL:EFQ03683.1}. 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; AECS01000039; EFQ03683.1; -; Genomic_DNA. DR RefSeq; WP_006942939.1; NZ_GL538208.1. DR EnsemblBacteria; EFQ03683; EFQ03683; HMPREF9429_01633. DR PATRIC; 44912738; VBIMegMic155926_1507. DR OrthoDB; EOG6091CH; -. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFQ03683.1}; KW Transferase {ECO:0000313|EMBL:EFQ03683.1}. SQ SEQUENCE 839 AA; 90593 MW; 6D09254520792B00 CRC64; MRQDLRKRLG KERLFFDGGT GSLLQAAGLK PGELPETWNL TRADVIIDLH KQYLDSGCHI FNTNTFGANR LKYPDNLDDI VTASIRLAKE ARRLANREDD AYVALDIGPT GKLLEPMGDL PFEEAVDIFA DLVKIGVREE ADLILIETMN DSYEAKAALL AAKENSDLPV LLTCVFDEGG KMLTGGTPES MVAMAEGLGV DGIGTNCSLG PAAMLSTVKR FVAAASVPVL VNPNAGLPES IDGQTVYNVD AHEFAKEMKD IVEAGAHAVG GCCGTTPEYI QALIAEVEDI PFIPPTPKHK TVISSFSRTS LIGDEAQPLI IGERINPTGK KRFKQALIDH DIDYIISQGL EQEKAGAHAL DVNVGSPEVD EVELIQEVVG KLQSILPLPL QIDTSNVEAM EKALRMYNGK ALINSVNGKE ETMEAVFPLV KKYGGVVIGL ALDEDGIADT ADGRVAVARK IYERAADYGI AKENVIIDGL CMTVSADPES ALVTLETIRR IHDELGGNTI LGVSNISFGL PARELINSYF FAMALQAGLS SAIINPNNKA MMQAYRTYCA LSGKDTNFTN FITAYQNYET PDKRVQKAVD DYKRKVLSAL DLDGADLSHI RNVKKETDTP SAPDATKDET YGNKLMEAVE RGMAGPAAEA THNALLTRNA LDIINEDLVP ALDNVGQGFE KGTLFLPQLL MAAEAAKAAF AVVKEALTDA PQETKGKVIL ATVKGDIHDI GKNIVKVLLE NYGYQAVDLG RDVAPETIVE TAVKEDIRLV GLSALMTTTV VNMEETIRLL REKKPDCKVI VGGAVMTKQY ADSIGADCYG KDAMSTVRYA DELLEQGLM // ID E2ZJF6_9FIRM Unreviewed; 812 AA. AC E2ZJF6; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFQ06675.1}; GN ORFNames=HMPREF9436_01804 {ECO:0000313|EMBL:EFQ06675.1}; OS Faecalibacterium cf. prausnitzii KLE1255. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Faecalibacterium. OX NCBI_TaxID=748224 {ECO:0000313|EMBL:EFQ06675.1}; RN [1] {ECO:0000313|EMBL:EFQ06675.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=KLE1255 {ECO:0000313|EMBL:EFQ06675.1}; 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 (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. {ECO:0000313|EMBL:EFQ06675.1}. 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; AECU01000146; EFQ06675.1; -; Genomic_DNA. DR RefSeq; WP_005942888.1; NZ_GL538328.1. DR EnsemblBacteria; EFQ06675; EFQ06675; HMPREF9436_01804. DR PATRIC; 44920265; VBIFaeCf154181_1414. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFQ06675.1}; KW Transferase {ECO:0000313|EMBL:EFQ06675.1}. SQ SEQUENCE 812 AA; 85711 MW; D6AFADDCE998A027 CRC64; MQASELFKQS NTILLDGGMG TMLQASGLKL GAKPEELNIT NPELIESIHA KYAAAGSRIV NANTFGASAH KLAGSAYSLE EIIAAGIANC KRACAPYGAL TALDVGPLGE LLEPSGTLAF EDAVSEYARI VRAGAAAGAD LIFFETFTDL YELKAALLAA KENSGLPILA SMSFEAGGRT FTGCTVESFG VTARGLGANA VGINCSLGPK EIFPMAKRLA EAVPGDFPVF VKPNAGLPRA DGSGYDITPQ LFAMEMKPYR DLHLFAAGGC CGTTPEFIKL LNSVFAGCVP GRSAHKMPSV LCTPVNFVNV DGITVVGERI NPTGKKRFQQ ALREEDMNYV LEQAVSQVEA GAQVLDVNVG APGVDEPALM PKVVKALQSV TSLPLQLDSS NVEALENGLR VYNGKPIVNS TNGEQEKLDA ILPLCKKYGA AIVGLAIDER GILPAAEDRV AIARRITEAA LAVGIPREDI YIDCLTLTAS AQQKDVLATV QALEACKKEL GVRTILGVSN ISFGLPCRPY LNTTFLTMAM YAGLDLAIMN PSSEEMMAAV YAYNVLTNRD PQSTKYIERY ADRVPASAAL KQAAQTVPAA SASASGESAE LTGPYALLMK AVEKGLKGDA AAQTKALLAE KQPLEVVDEA LIPALDIVGA KYEKGTLFLP QLLQAASAAQ SAFEEIKNVI AQKGEGSASK GRIVLATVKG DVHDIGKNIV KVILENYGFE VIDLGRDVPV ETVVNTVREK NVHLVGLSAL MTTTLKSMEE TIAALHEAGL DCKIMVGGAV LTPEYAEKIG ADWYAKDAKR SADIAKEFFG AQ // ID E2ZMC3_9FIRM Unreviewed; 595 AA. AC E2ZMC3; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 27-MAY-2015, entry version 18. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HMPREF9436_02839 {ECO:0000313|EMBL:EFQ05697.1}; OS Faecalibacterium cf. prausnitzii KLE1255. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Faecalibacterium. OX NCBI_TaxID=748224 {ECO:0000313|EMBL:EFQ05697.1}; RN [1] {ECO:0000313|EMBL:EFQ05697.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=KLE1255 {ECO:0000313|EMBL:EFQ05697.1}; 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 (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFQ05697.1}. 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; AECU01000207; EFQ05697.1; -; Genomic_DNA. DR RefSeq; WP_005945467.1; NZ_GL538344.1. DR EnsemblBacteria; EFQ05697; EFQ05697; HMPREF9436_02839. DR PATRIC; 44922010; VBIFaeCf154181_2336. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EFQ05697.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EFQ05697.1}. SQ SEQUENCE 595 AA; 63782 MW; CE6E742698FAE49C CRC64; MKDVREILKK RPLLFDGGMG TYYKAKPGQE CEQANLLDPD GILTVHRAYL EAGADAIKTN TFGLPRMAAA QNPMWEAMAD EGWKLAAQAA AKTSAAVFAD LGPAPDTEAL PAAQIYTALA ERFAALGAKN FLFETLSSDA GVAEAARQIK EAVPDAFVLV SFAVLPDGYT REGRHCAELV RSMTACGAVD AVGLNCVSAP GAMRALVQQL GETKLPLAVM PNAGYPVVTR TRVQYQGKPE YFARELARLA AEGVRILGGC CGTTPAHIAA LRAALDALPE TLPAAPAAAV STAAKPEVEK DDAFLRKLNA GKKVIAIELD SPKDADMTGY LDGARRLQAA GADLLTIADC PIARARMDSS LVACRVHREL GLNVLPHMTC RDRNLNATKA LLLGLYAEGV REVLAITGDP IPTAERDEVK NVYQFNSRKL AQYIVSLAGE GREMPSPLTV FGALNLNARN FDVELRRAQE KLQNGMSGFL TQPVLSAQAV VNLKKTRETL GEKAKILAGI MPVVSQRNAI FMENEVNGIH VDAEIIERFA GLDRAQGEEL GLEVSVKAAQ AAAPYADGFY LMTPFNRIAL MERLIARLKD EGIAD // ID E3BDN0_9MICO Unreviewed; 1262 AA. AC E3BDN0; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 01-APR-2015, entry version 23. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFP56853.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFP56853.1}; GN Name=metH {ECO:0000313|EMBL:EFP56853.1}; GN ORFNames=HMPREF0321_0488 {ECO:0000313|EMBL:EFP56853.1}; OS Dermacoccus sp. Ellin185. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Dermacoccaceae; Dermacoccus. OX NCBI_TaxID=188626 {ECO:0000313|EMBL:EFP56853.1}; RN [1] {ECO:0000313|EMBL:EFP56853.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Ellin185 {ECO:0000313|EMBL:EFP56853.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFP56853.1}. 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; AEIQ01000119; EFP56853.1; -; Genomic_DNA. DR RefSeq; WP_006947305.1; NZ_AEIQ01000119.1. DR EnsemblBacteria; EFP56853; EFP56853; HMPREF0321_0488. DR PATRIC; 42133646; VBIDerSp75128_2727. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFP56853.1}; KW Transferase {ECO:0000313|EMBL:EFP56853.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 266 266 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 329 329 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 330 330 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 786 786 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1262 AA; 137568 MW; ABC92590C03265A9 CRC64; MSSRSKATDP TTTDHDARRD AGGDRSEELA ALMRERILVM DGAMGTMIQR HGLSEDDYRG ERFADWPSDL KGNNDLLSLT QPDIIEGIHR EYLEAGADIV ETNTFNAQRI SLADYDMSEF AYEFNVESAK LARTAADSVT TGARPRFVAG AIGPTNRTAS ISPDVNDPGA RNVSFDDLVG AYLEQARGLA DGGVDLMLIE TIFDTLNAKA AIFALEQLFE ERGRRWPVII SGTITDASGR TLSGQTGEAF WNSVRHARPL AVGLNCALGA DEMRPYVADL SRIADCFVSC YPNAGLPNAF GEYDETPEAM TQTVAAFAGD GLVNLVGGCC GTSPDHIGAI ADAVAATAPR SVPDVAPALR LSGLEPFTVD EDSLFVNVGE RTNITGSARF RKLIKDGDYA TALSVARQQV ENGAQIIDVN MDEGMIDGVA AMDRFCKLIA SEPDICRVPV MVDSSKWEVI EAGLKCIQGK SIVNSISMKE GVEPFIEHAR LCKRYGAAIV VMAFDEDGQA DTLERRKTIT KRAYDILTGP DVDFPAEDII FDPNIFAIGT GIEEHANYGV DFIEGTRWIK ANLPGALVSG GVSNVSFSFR GNNPVREAIH AVFLYHAVAA GMDMGIVNAG ALVVYDEIDP ELRELIEDVV LNRRADATER LLEAAEQYNS SGEQAEAKTE QWRELPVRER ITHALVKGID DHVEADTEQM RAELEAEGKR PLEVIEGPLM DGMGVVGDLF GAGKMFLPQV VKSARVMKKA VAYLIPFIEA EKEASGVTSK QTNGTVVLAT VKGDVHDIGK NIVGVVLQCN NYEVIDLGVM VAPQKILDAA REHDADIIGL SGLITPSLDE MVHLASEMQR QGFTQPLLIG GATTSRAHTA VKIDGRYDEP VVWVKDASRS VPVVAALLST GERREALLAD VVADYDALRA RHAAKRDERP LLTLDEARAN VTEMDWAAGV PDAPALAVDG APVTRVFTDY PVSELREYID WQPFFAAWEM KGRFPDILSN PAQGEAARKL YDDAQTMLDR ISDEGWLHPA GVIGFWPAQA DGDDTVLFGD ASRSAEVARL HHLRQQGTHR DGVPNRSLAD FVAPTGAADD WVGAFAVTAG TELPERIRAF KDDLDDYSAI LLEALADRLA EAFAERLHER VRREFWGYEA GEKLSNDELI RERYQGIRPA PGYPACPEHT EKDTLFDLLD VTASIGVELT ESRAMWPGAS VSGWYFAHPQ AQYFVVGRIG RDQVADYAER KGWTMAEAER HLAPNLGYDP ED // ID E3BFI2_9VIBR Unreviewed; 298 AA. AC E3BFI2; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EFP98160.1}; GN ORFNames=VIBC2010_10237 {ECO:0000313|EMBL:EFP98160.1}; OS Vibrio caribbeanicus ATCC BAA-2122. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=796620 {ECO:0000313|EMBL:EFP98160.1}; RN [1] {ECO:0000313|EMBL:EFP98160.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-2122 {ECO:0000313|EMBL:EFP98160.1}; 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. {ECO:0000313|EMBL:EFP98160.1}. 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; AEIU01000022; EFP98160.1; -; Genomic_DNA. DR RefSeq; WP_009599669.1; NZ_AEIU01000022.1. DR EnsemblBacteria; EFP98160; EFP98160; VIBC2010_10237. DR PATRIC; 44962401; VBIVibCar171609_0453. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFP98160.1}; KW Transferase {ECO:0000313|EMBL:EFP98160.1}. SQ SEQUENCE 298 AA; 32624 MW; 4A6EFBF96CEC1DF9 CRC64; MRTPVSLVIL DGGMGRELQR IGAPFSQPLW SAQALIEAPE YVKQAHCNFI QAGADIITIN SYACVPFHLG AALYKQKGPE LAIQAAILAR EAVQNSEKKT ALIAGSLPPV LGSYRPDLFK PKIAFDVTEQ LYTAQDPYCD LWIAETVASI AELKVMLTFA AQSSKPFYIA FTLNDDVNAK TPTLRSGEQL SEAIEYLRET DVRGVLLNCS IPEVIGPALL LIKALRKHLT IGAYANSFIP IDENHKANST FQSLRSVSEQ AYLHHAQNWY EAGARIIGGC CGIGPSHIAE IAQWKEKL // ID E3CHB4_STRDO Unreviewed; 611 AA. AC E3CHB4; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 27-MAY-2015, entry version 17. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HMPREF9176_1992 {ECO:0000313|EMBL:EFQ58053.1}; OS Streptococcus downei F0415. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=904293 {ECO:0000313|EMBL:EFQ58053.1}; RN [1] {ECO:0000313|EMBL:EFQ58053.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0415 {ECO:0000313|EMBL:EFQ58053.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFQ58053.1}. 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; AEKN01000003; EFQ58053.1; -; Genomic_DNA. DR RefSeq; WP_002997040.1; NZ_AEKN01000003.1. DR EnsemblBacteria; EFQ58053; EFQ58053; HMPREF9176_1992. DR PATRIC; 45000958; VBIStrDow169691_0285. DR OrthoDB; EOG6SNDP1; -. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EFQ58053.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EFQ58053.1}. SQ SEQUENCE 611 AA; 67956 MW; 9062E2D0D89FA446 CRC64; MSKLLDKLKT DILVADGAMG TLLYAEGLES CHAYYNISHP ERILAIHKAY IDAGADIIQT NTYDAKRHRL KSFGYDNDVK QINQKAAEIA RQAAGRNVFV LGTIGASRGL RQCDLSLEDI VKETVEQAQA LLETEQLDGL LFETYYDREE LEAVIKAIRP LTDLPLITNM ALHEAGITED GRPLVEALSH LVMLGADIVG LNCHLGPYHM IQSFKQVPLF AQSYLSAYPN ASLLSFAGDD EKGQYRFSQN ADYFEYCAQL FVEEGVRLIG GCCGTTPDHI RAIKRGIKNL KPVERKTITP LITEEELIDE IAKKETLADK AKKEVTIIAE IDPPKTLAIE KFIEGIKALD KKNIAAITLA DNSLAKTRIC NLSLASLLKN EIATPFLLHI ACRDHNMIGL QSRLLGMDVL GFNQLLAITG DPTKIGDFPG ATSVYDATSF KLLSLIKQLN HGKGYSGASL KRATHFTTAA AFNPNVRQLE KSNRLIERKI KAGADYFITQ PIFSEEIIHQ LGSLTKTYEQ PFFIGIMPIT SYNNAVFLHN EVPGIHLSEA FLEKLETVKD DKEACQAIAL AESKKLIDCA LEYFNGIYLI TPFLRYDLTL DLIDYIQKRK P // ID E3CII1_STRDO Unreviewed; 315 AA. AC E3CII1; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 27-MAY-2015, entry version 12. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFQ57564.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EFQ57564.1}; GN Name=mmuM {ECO:0000313|EMBL:EFQ57564.1}; GN ORFNames=HMPREF9176_1498 {ECO:0000313|EMBL:EFQ57564.1}; OS Streptococcus downei F0415. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=904293 {ECO:0000313|EMBL:EFQ57564.1}; RN [1] {ECO:0000313|EMBL:EFQ57564.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0415 {ECO:0000313|EMBL:EFQ57564.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFQ57564.1}. 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; AEKN01000006; EFQ57564.1; -; Genomic_DNA. DR RefSeq; WP_002998254.1; NZ_AEKN01000006.1. DR EnsemblBacteria; EFQ57564; EFQ57564; HMPREF9176_1498. DR PATRIC; 45001905; VBIStrDow169691_0750. DR OrthoDB; EOG6C019S; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFQ57564.1}; KW Transferase {ECO:0000313|EMBL:EFQ57564.1}. SQ SEQUENCE 315 AA; 34564 MW; C87FA8769132230A CRC64; MGRFKDLLAS QDYLILHGAL GTELEYRGYD VSGKLWSAKY LLEDPKAIQD IHETYLRAGS DIVTTASYQA TLPGLESYGL TEAQAKKIIA STVDIAKSAR DQVWSSLSEI EKESRPYPLI SGDVGPYAAY LADGSEYTGD YGAITKQELK DFHRPRLAIL KEQGVDLLAL ETMPNFLEAQ ALVELLSEDF PQVEAYISFT SQDGQSISDG TALSEVAKLV EASSQILAVG LNCSSPKVYP DFLHQLRQYT AKPLVTYPNS GEVYDGATQT WTKDPDHSHS LLENTLTWQK LGAKVVGGCC RTRPSDIQVL AQGLK // ID E3CQ62_STRVE Unreviewed; 316 AA. AC E3CQ62; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 27-MAY-2015, entry version 12. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFQ59660.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EFQ59660.1}; GN Name=mmuM {ECO:0000313|EMBL:EFQ59660.1}; GN ORFNames=HMPREF9192_1314 {ECO:0000313|EMBL:EFQ59660.1}; OS Streptococcus vestibularis F0396. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=904306 {ECO:0000313|EMBL:EFQ59660.1}; RN [1] {ECO:0000313|EMBL:EFQ59660.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0396 {ECO:0000313|EMBL:EFQ59660.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFQ59660.1}. 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; AEKO01000007; EFQ59660.1; -; Genomic_DNA. DR RefSeq; WP_003094879.1; NZ_AEKO01000007.1. DR EnsemblBacteria; EFQ59660; EFQ59660; HMPREF9192_1314. DR PATRIC; 45007909; VBIStrVes173029_1422. DR OrthoDB; EOG6C019S; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFQ59660.1}; KW Transferase {ECO:0000313|EMBL:EFQ59660.1}. SQ SEQUENCE 316 AA; 34776 MW; AE33667FE184C3BA CRC64; MATFKDYLEN NSPLILHGAL GTEMEALGYD ISGKLWSAKY LLEKPEIIQE IHETYIAAGA DLITTSSYQA TLPGLVEAGL TEKAAEQIIA LTVRLAKAAR DKVWVVLDET EKAKRPYPLI SGDVGPYAAY LANGSEYSGD YGQITIEELK DFHRPRIQIL LDQGVDLLAL ETIPNRLEAQ ALIELLAEEF PEAEAYISFT VQEPGTISDG TSLDEIAKLV SQSNQILAVG INCSSPLLYN QALAILKNAG KVLITYPNSG EVYDGNSQTW KTKDKDALTL VEHSKDWHAH FGVKILGGCC RTRPNDIKAL YQEFRT // ID E3CXR8_9BACT Unreviewed; 801 AA. AC E3CXR8; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:EFQ22661.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFQ22661.1}; GN ORFNames=Apau_0225 {ECO:0000313|EMBL:EFQ22661.1}; OS Aminomonas paucivorans DSM 12260. OC Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae; OC Aminomonas. OX NCBI_TaxID=584708 {ECO:0000313|EMBL:EFQ22661.1, ECO:0000313|Proteomes:UP000005096}; RN [1] {ECO:0000313|EMBL:EFQ22661.1, ECO:0000313|Proteomes:UP000005096} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 12260 {ECO:0000313|EMBL:EFQ22661.1}; 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 ----------------------------------------------------------------------- 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; EFQ22661.1; -; Genomic_DNA. DR RefSeq; WP_006299805.1; NZ_CM001022.1. DR EnsemblBacteria; EFQ22661; EFQ22661; Apau_0225. DR PATRIC; 44970421; VBIAmiPau86579_0234. DR Proteomes; UP000005096; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005096}; KW Methyltransferase {ECO:0000313|EMBL:EFQ22661.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005096}; KW Transferase {ECO:0000313|EMBL:EFQ22661.1}. SQ SEQUENCE 801 AA; 83808 MW; A244249C6182DC95 CRC64; MKRLFAGQVS PVILDGGMGT QLALAGWRPP LLPEEMVLEN PDSVTAIHRA YVEAGARIVE TDTFGGSALK LAHRGLEGRT EEINRRAAEL ARQAVGDRAF VAGSMGPIGR LVDPLGDLTF DEAVEAFRPQ AAGLARGGAD FLLVETMLDL KEAQAAAVAC REAAPGLPFA VSFTFDKDGS TVTGTPPEAA AVWAEAVGAF AVGANCGVGP EEYVDTVHRL AASTDLPVFV YPNAGVPSSR DYLGPEAFAG ACEALVRAGA AVVGGCCGTT PEHTAALVRR LGGMAIPPSL RRERGVLRFA SRSRVVEAGQ GRPLLLIGER INVSRKSPLR EELRVQDYTT VRAEARDQTA AGAGLLDVNV GLPEIDRIRA MGKAIHVAEA ASSLPLSVDS DDPTVLERGL REAVGVPLLN SVTAKAEALE RGIDLAWKYG AVLAVLTIDE SGIPERAYDR VAIAQRVLLR ASERGLGPER ILLDPLTLAL GADPRNALAT CEALRCIREL GGHTMLGISN ISHGLPARGL LNRTFLVMAM EAGLDAVLCN PLDERLLATV AAADALRGRD EGLRRYLAFA PGWSEGVPAS GGASRGEPAK GGEQPLTRCI LEGDPAGAEA SARALVDRGT SPLDLVSSWV VPALEEVGRL YECGDTFLPQ LLASAQAAGG VCRLAEELLA RQGVKQEPKG TVVLATVEGD LHDLGKNVVG MVLASHGYRV VDLGKDVPAE RILEAAEAER ADVVGLSALM TSTVPQMEAV IRGARERGAA YRIIVGGAAV SPQYAESIGA DGTSSDAVGA ARLVEQLLAR R // ID E3DK37_ERWSE Unreviewed; 300 AA. AC E3DK37; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:ADP11879.1}; GN OrderedLocusNames=EJP617_21980 {ECO:0000313|EMBL:ADP11879.1}; OS Erwinia sp. (strain Ejp617). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Erwinia. OX NCBI_TaxID=215689 {ECO:0000313|EMBL:ADP11879.1, ECO:0000313|Proteomes:UP000006865}; RN [1] {ECO:0000313|EMBL:ADP11879.1, ECO:0000313|Proteomes:UP000006865} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ejp617 {ECO:0000313|EMBL:ADP11879.1, RC ECO:0000313|Proteomes:UP000006865}; 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(2011). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; ADP11879.1; -; Genomic_DNA. DR RefSeq; WP_014543686.1; NC_017445.1. DR RefSeq; YP_005818766.1; NC_017445.1. DR EnsemblBacteria; ADP11879; ADP11879; EJP617_21980. DR KEGG; erj:EJP617_21980; -. DR PATRIC; 42941356; VBIErwSp41759_2342. DR OMA; PYVDVWL; -. DR BioCyc; ESP215689:GLCY-2265-MONOMER; -. DR Proteomes; UP000006865; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006865}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ADP11879.1}; KW Transferase {ECO:0000313|EMBL:ADP11879.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 208 208 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 300 AA; 31780 MW; 67E261A70F566001 CRC64; MTQQIQILDG GMGRELARVG APFRQPEWSA LALYEAPQRV REVHDSFISA GAGTITTNSY AVVPFHIGEA RFNADGEHLA ALAGQLARQA ANAATHPVQV AGSLPPALGS YRPDLFDAQQ ALKIYRVLVA AQAPYVDIWL GETISSLAEA VAIHQAVAEQ PQPLWLSFSL QDGPDKTRRD STLRSGESVS AAVELAVESG ATHILFNCSN PEVMLSAVQQ AAATLRRLGS GAGIGVYANA FEHGSNESGA NEGLSDLRQD THPEGYLRWA REWVAAGATL VGGCCGIGPE HIQCLASAFK // ID E3DMZ0_HALPG Unreviewed; 796 AA. AC E3DMZ0; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ADO77479.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADO77479.1}; GN OrderedLocusNames=Hprae_1346 {ECO:0000313|EMBL:ADO77479.1}; OS Halanaerobium praevalens (strain ATCC 33744 / DSM 2228 / GSL). OC Bacteria; Firmicutes; Clostridia; Halanaerobiales; Halanaerobiaceae; OC Halanaerobium. OX NCBI_TaxID=572479 {ECO:0000313|EMBL:ADO77479.1, ECO:0000313|Proteomes:UP000006866}; RN [1] {ECO:0000313|Proteomes:UP000006866} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33744 / DSM 2228 / GSL RC {ECO:0000313|Proteomes:UP000006866}; 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 ----------------------------------------------------------------------- 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; ADO77479.1; -; Genomic_DNA. DR RefSeq; WP_014553506.1; NC_017455.1. DR RefSeq; YP_005836639.1; NC_017455.1. DR EnsemblBacteria; ADO77479; ADO77479; Hprae_1346. DR KEGG; hpk:Hprae_1346; -. DR PATRIC; 43055999; VBIHalPra106773_1362. DR KO; K00548; -. DR BioCyc; HPRA572479:GLDS-1389-MONOMER; -. DR Proteomes; UP000006866; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006866}; KW Methyltransferase {ECO:0000313|EMBL:ADO77479.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006866}; KW Transferase {ECO:0000313|EMBL:ADO77479.1}. SQ SEQUENCE 796 AA; 86921 MW; B7AA208FC44753EF CRC64; MNLKSKLGKE VIIFDGAMGT VLQKQGLEIG KFPEKLNLEA PRRIIEIHKS YLKAGADIIT TNTFGANSLK LKGSQYSVEQ IISAAVKNAK VAVAESGFAA NIALSLGPLG ELIEPNGKLS FKKAYKLYQK QVLLGVENGI DLIQIETISQ LAAARAAVLA AKENSDLAIF CTLTFTESGR TFTGCNLRSM ISVLEGLGVD ALGLNCSLGP KKAEVLVEKI LKYSKLPVIL QANAGLPVIE AGKTNYKISP ATYYTPLARL YQQGLAIIGG CCGTTPEYIS LIADKLKGKK IKKRKIIKKD LVCSAVEYSD LSGINVVGER INPTGKAEFK ENLKKGNLDY LLKIALAEIE AGADILDINL GLPEIDEKKM MLKFIQELQQ NITKPLQIDS TNLEVIETAL RNYNGIAIIN SVTGKKDSLE KVLTVAKKYG AFVIGLTIDE NGIPETAAGR LKIAEKIVNK AVELKISKDK IIIDCLALTV SAQPKSIEKT LTALKLVQEK LEVKTILGIS NISFGLPARS ILNRSFLTMA LAQGLNLAIM DPNDPEMMAT VKAVSVLKNL DQGAEKYIDF ISHFKNQSKT IKTKKQKSEK KDLKELIISG LKDETKKLTK ELLLEKEPLE IIDQHLIPAL NLVGEKYEKG ELFLPKLLKT AATVKESFSV LKMQMKQENN QKLAKGKILL ATVEGNVHDI GKNIVKVLLE NYNYQVIDLG KNIETEKIVN TVLKNEIKLL GLSALMTTTV KNMQKVIKAV KKAAPNCKIM VGGAVLTADY AKMIKANFYA QDAQTAVEIA NNLFLD // ID E3E4I7_PAEPS Unreviewed; 1146 AA. AC E3E4I7; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 2. DT 27-MAY-2015, entry version 37. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADO56886.2}; GN Name=metH {ECO:0000313|EMBL:ADO56886.2}; GN ORFNames=PPSC2_13700 {ECO:0000313|EMBL:ADO56886.2}; OS Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=886882 {ECO:0000313|EMBL:ADO56886.2, ECO:0000313|Proteomes:UP000006868}; RN [1] {ECO:0000313|EMBL:ADO56886.2, ECO:0000313|Proteomes:UP000006868} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SC2 {ECO:0000313|EMBL:ADO56886.2, RC ECO:0000313|Proteomes:UP000006868}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002213; ADO56886.2; -; Genomic_DNA. DR RefSeq; WP_013371489.1; NC_014622.1. DR RefSeq; YP_003947127.1; NC_014622.1. DR EnsemblBacteria; ADO56886; ADO56886; PPSC2_c2921. DR KEGG; ppm:PPSC2_c2921; -. DR PATRIC; 42509034; VBIPaePol172748_2793. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; PPOL886882:GBY1-3014-MONOMER; -. DR Proteomes; UP000006868; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006868}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006868}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1146 AA; 126280 MW; 504391B54E71145D CRC64; MDKVSLQDAL QRRILLLDGA MGTMIQQEDL SPADFGGEEL EGCNEMLVLT RPDVIQGIHE AYLEAGADLI ETNTFGATSV VLADYDIPER AREINLVAAK LARNAVDKYS TADKPRFVVG AMGPTTKTLS VTGGVTFVEL IESYQEQALA LIEGGVDVLL LETSQDTLNV KAGSIGIRQA FEQTGIELPL MISGTIEPMG TTLAGQNIES FCISLEHLNP ISIGLNCATG PEFMRDHIRS LSEMSSAAIS CYPNAGLPDE NGQYHESPDS LARKMAAFAE KGWLNIAGGC CGTTPEHIRV MSESMAQFEP RQLVGHHPPA VSGIEPVYIE QDNRPYMVGE RTNVLGSRKF KRLIVEGKYE EASEIARAQV KSGAHVIDIC VQDPDRDEMI DMEAFLKLVV NKVKVPLVID TTDIKVIDKA LQYSQGKAII NSINLEDGEE KFEKMAPIIH KYGAAVVVGT IDERGQAIAR EDKLEVAKRS YDLLVNRYGL AAEDIIFDTL VFPVGTGDEQ YIGSAKETIE GIRIIKEALP GVHTILGISN VSFGLPEAGR EVLNSVYLYE CTKAGLDYAI VNTEKLERYA SIPEHERKLA EDLIYNTNDD TLSAFVAAFR NKKVEKKEKI SNLSLEERLA SYVVEGSKEG LIPDLEQALA KYSSLEIING PLMKGMEEVG RLFNNNELIV AEVLQSAEVM KASVAYLEPF MEKNESSVKG KILLATVKGD VHDIGKNLVE IILSNNGYHI VNLGIKVPPE RIIEAYREEK ADMIGLSGLL VKSAQQMVLT AQDLKNANID IPIMVGGAAL TRKFTKNRIR PEYDGLVAYA KDAMDGLDIA NKLMDPESRK KMAEDMKAEQ EAEAATVVEA KPLPKLTRAV RSNIAQDLPV YIPPDTDRHV LRNYPLNYIL PYVNMQMLMG HHLGLKGNVE QLLASGDPKA IQLKETVDSI MFEAVTDGII QASAMYRFFP AQSQGNQILI YDPSDVSKVL HTFTFPRQQV EPYLCLADFL KSVESGVMDY VGFMVVTAGH GIQKLSTQWK DNGDYLRSHA LQAVALEVAE GLAERLHHII RDSWGFPDPA DMTMKQRHGA RYQGIRVSFG YPACPDLEDQ GPLFQLLKPE DIGVELTEGF MMEPEASVSA MVFSHPQAQY FNVEKV // ID E3E872_PAEPS Unreviewed; 628 AA. AC E3E872; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 27-MAY-2015, entry version 31. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN Name=yitJ {ECO:0000313|EMBL:ADO57264.1}; GN ORFNames=PPSC2_15475 {ECO:0000313|EMBL:ADO57264.1}; OS Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=886882 {ECO:0000313|EMBL:ADO57264.1, ECO:0000313|Proteomes:UP000006868}; RN [1] {ECO:0000313|EMBL:ADO57264.1, ECO:0000313|Proteomes:UP000006868} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SC2 {ECO:0000313|EMBL:ADO57264.1, RC ECO:0000313|Proteomes:UP000006868}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ADO57264.1; -; Genomic_DNA. DR RefSeq; WP_013371853.1; NC_014622.1. DR RefSeq; YP_003947505.1; NC_014622.1. DR EnsemblBacteria; ADO57264; ADO57264; PPSC2_c3307. DR GeneID; 9851603; -. DR KEGG; ppm:PPSC2_c3307; -. DR PATRIC; 42509778; VBIPaePol172748_3166. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR BioCyc; PPOL886882:GBY1-3400-MONOMER; -. DR Proteomes; UP000006868; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006868}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ADO57264.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000006868}; KW Transferase {ECO:0000313|EMBL:ADO57264.1}. SQ SEQUENCE 628 AA; 68291 MW; 7A060556663DC3BF CRC64; MKPDLRTVLN REIIVGDGAM GTFLSQLGFP VNTSYEELNI TSPGVISDVH GQYLNAGARL LETNTFSAND YKLARFGLES KVEEINRAGV RIARAAAGPE HYVVGAVGSI CGGKRLNISK LELSRNYEQQ IDALLSEGVD GILCETFYSL DEMRIALHSV RKYSDIPVIC QFAVDQIGRT QDGFLMAQAF STLRSEGADI LGFNCHSGPQ GIMSVMEQLD GPLSVPLSVY PNAGLADYVD GHYVYGASPE YFGECATSFV DLGTRLIGGC CGTTPDHIAA ISKALNNLQP PPLAPKETFS TEVIHVVEQT ADEGGRGNGR HTSEPNIVDL VKERHTVIVE LDPPRDLDIT RFMQGAHALK KAGADALTLA DNSLAVTRMS NMALGHLVSI ETGLRPLIHI ACRDRNLIGT QSHMMGFDAL GIDHVLAVTG DPARFGDLPG ASSVYDMTSF EIIRMIKQLN DGVAFSGKPL KQKANFVVGA AFNPNVKHLG KAVQRLEKKI ASGADYIMTQ PVYDPELIKA IAEQTRHLEI PIFIGIMPLA SGRNAEYLHN EVPGIQLSDE VRARMSGLEG PEGRAMGVSI AKELLDTAME HFNGIYFMTP FMFYEMTAEL TSYVWQKSGR AQAPLFRL // ID E3E918_PAEPS Unreviewed; 315 AA. AC E3E918; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:ADO59225.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ADO59225.1}; GN Name=mmuM {ECO:0000313|EMBL:ADO59225.1}; GN ORFNames=PPSC2_24755 {ECO:0000313|EMBL:ADO59225.1}; OS Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=886882 {ECO:0000313|EMBL:ADO59225.1, ECO:0000313|Proteomes:UP000006868}; RN [1] {ECO:0000313|EMBL:ADO59225.1, ECO:0000313|Proteomes:UP000006868} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SC2 {ECO:0000313|EMBL:ADO59225.1, RC ECO:0000313|Proteomes:UP000006868}; 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; ADO59225.1; -; Genomic_DNA. DR RefSeq; WP_013373758.1; NC_014622.1. DR RefSeq; YP_003949466.1; NC_014622.1. DR EnsemblBacteria; ADO59225; ADO59225; PPSC2_c5288. DR GeneID; 9853563; -. DR KEGG; ppm:PPSC2_c5288; -. DR PATRIC; 42513670; VBIPaePol172748_5058. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR BioCyc; PPOL886882:GBY1-5438-MONOMER; -. DR Proteomes; UP000006868; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006868}; KW Methyltransferase {ECO:0000313|EMBL:ADO59225.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006868}; KW Transferase {ECO:0000313|EMBL:ADO59225.1}. SQ SEQUENCE 315 AA; 35212 MW; FB3F29A244F213A7 CRC64; MNPIQRIVNK FQLIVLDGAM ATELERHGHD LNDSLWSAKI LYEYPDSIKR VHRDYFEAGA DCAITASYQA TVEGYVQRGL SENEALKLIQ SSVQIALQAR DEFWADVTAT ASQQHRPKPL VAASVGPYGA FLADGSEYRG DYKLSEEQLM EFHRPRMKAL IEAGADILAC ETIPCLVEAK AIARLLKEFP GTYAWISFSA KDEQHISNGE SVAACAKWLN EHEQVAAVGI NCTLPKFIPS LIHEIHSHTD KPVVVYPNLG EEYDPVTKTW QGHTCTETFG QSARQWYKAG ARMIGGCCRT QPQDIKEIVA WSREI // ID E3EX22_KETVY Unreviewed; 1248 AA. AC E3EX22; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 27-MAY-2015, entry version 34. DE SubName: Full=Probable 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:ADO41266.1}; GN Name=metH {ECO:0000313|EMBL:ADO41266.1}; GN OrderedLocusNames=EIO_0075 {ECO:0000313|EMBL:ADO41266.1}; OS Ketogulonicigenium vulgare (strain Y25). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Ketogulonicigenium. OX NCBI_TaxID=880591 {ECO:0000313|EMBL:ADO41266.1, ECO:0000313|Proteomes:UP000006871}; RN [1] {ECO:0000313|EMBL:ADO41266.1, ECO:0000313|Proteomes:UP000006871} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Y25 {ECO:0000313|EMBL:ADO41266.1, RC ECO:0000313|Proteomes:UP000006871}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002224; ADO41266.1; -; Genomic_DNA. DR RefSeq; WP_013382919.1; NC_014625.1. DR RefSeq; YP_003962566.1; NC_014625.1. DR EnsemblBacteria; ADO41266; ADO41266; EIO_0075. DR KEGG; kvu:EIO_0075; -. DR PATRIC; 43492402; VBIKetVul170732_0320. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; KVUL880591:GHQW-75-MONOMER; -. DR Proteomes; UP000006871; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006871}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADO41266.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006871}; KW Transferase {ECO:0000313|EMBL:ADO41266.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 263 263 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 326 326 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 327 327 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 779 779 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1248 AA; 136405 MW; 6D1750B6A27C9422 CRC64; MPPEDAMTAL PKSASFARIV DAARQRILVL DGAMGTQIQL LKMGEDEYLG HGSAGCQCHI HSDHPQKGNN DLLNLTQPEA IEEIHFRYAM AGADIVETNT FSSTTIAQAD YALEDQVHAL NVQGARLARS GVDRATAIDG RMRFVAGAVG PTNRTASISP DVNDPGFRAV SFDDLRIAYA QQIRGLIEGG VDLILIETIF DTLNAKAAIF AAEEVFIEIG ERLPVMISGT ITDLSGRTLS GQTPTAFWHS VRHAGPFTIG LNCALGANAM RAHLAEISAI ADTFVCVYPN AGLPNAMGDY DETPAFTAQQ IEGFARDGLV NIVGGCCGTS PEHIRAMAEA VAKYRPRAIP EHAPLMRLSG LEPFILTPEI PFVNVGERTN VTGSAKFRKM ITAGDFASAL QVARDQVENG AQIIDINMDE GLIDSQAAMV KFLNLVASEP DIARVPVMID SSKWDVIEAG LKCVQGKAIV NSISMKEGEA AFLHHARLCR AYGAAVVVMA FDETGQADTE DRKVEICSRA YKLLTEEVGF PPEDIIFDPN VFAVATGIEE HNNYGVDFIN ATRRIMEACP HVHISGGISN LSFSFRGNEP VREAMHAVFL YHAIQVGMDM GIVNAGQLAV YDQIDPELRE ACEDVVLNRR DDATERLLDL AERYRGQGGA EKKERDLAWR DWDVAKRLEH ALVNGITEFI EGDTEEARLA AQRPLHVIEG PLMDGMNVVG DLFGAGKMFL PQVVKSARVM KQAVAVLLPY LEEEKAAGGG VGRQSAGKIL MATVKGDVHD IGKNIVGVVL ACNNYDIIDL GVMVSSEKIL AAAREHDVDA IGLSGLITPS LDEMVHVAAE MERQGFDIPL LIGGATTSRV HTAVKIAPAY QRGQVVYSVD ASRAVGVAQN LLGSRSLAYQ AEVRAEYEKV AEGYLRGERE KQRLPLADAR ANPVKIDWAA YQAKVPSFLG TKVYDDWDLA DLAQYIDWTP FFQSWELKGV YPRILQDEKY GETARSLFAD AQAMLQQIID EKWFDPRAVV GFWPANAVGD DIVLFADETR SHILATMHTL RQQLPRRDGR PNIAMSDFVA PMGQAEYIGG FVVTAGFKEL EIAARFEAAN DDYNAIMVKA LADRFAEAFA ERMHQHVRRE LWAYAADEVL PNDALIREEY AGIRPAPGYP AQPDHTEKLT LFRLLDAEAA TGVKLTESMA MWPGSTVSGL YIAHPESYYF GVAKVEEDQV ADYAARKGMD KAEAERWLAP ILNYIPKA // ID E3G2G3_ENTLS Unreviewed; 1227 AA. AC E3G2G3; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 27-MAY-2015, entry version 35. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADO50380.1}; GN OrderedLocusNames=Entcl_4147 {ECO:0000313|EMBL:ADO50380.1}; OS Enterobacter lignolyticus (strain SCF1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex. OX NCBI_TaxID=701347 {ECO:0000313|EMBL:ADO50380.1, ECO:0000313|Proteomes:UP000006872}; RN [1] {ECO:0000313|Proteomes:UP000006872} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SCF1 {ECO:0000313|Proteomes:UP000006872}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002272; ADO50380.1; -; Genomic_DNA. DR RefSeq; WP_013368096.1; NC_014618.1. DR RefSeq; YP_003943664.1; NC_014618.1. DR EnsemblBacteria; ADO50380; ADO50380; Entcl_4147. DR KEGG; esc:Entcl_4147; -. DR PATRIC; 42602560; VBIEntClo171306_4225. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; ECLO701347:GH9V-4228-MONOMER; -. DR Proteomes; UP000006872; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006872}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006872}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135630 MW; F0733C41FEEADAF4 CRC64; MSSKTEQLHA QLKERILVLD GGMGTMIQSY RLTEEDFRGA RFADWPCDLK GNNDLLVLSK PEVISAIHNA YFEAGADIIE TNTFNSTPIA MADYQMESLS AEINFAAATL ARACADEWTA RTPDKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGSDLILI ETVFDTLNAK AAIFAVKAEF DALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHADA LTFGLNCALG PDELRQYVQE LSRIADCYVT AHPNAGLPNA FGEYDLDADT MAAQIREWAE AGFLNIVGGC CGTTPEHIAA MSRVVTGLTP RKLPEIPVAC RLAGLEPLTI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VESGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVEPFIHHA KLVRRYGAAV VVMAFDEVGQ ADTRERKIEI CRRAYQILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAV DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDGVEDVI LNRRDDATER MLDLAEKYRG SKSDDGANAQ QAEWRSWEVK KRLEYSLVKG ITEFIEQDTE EARQQAARPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EKGKSNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPTEKIL KTAREVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDSQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLQAAR DNDLAFDWAS YTPPVAHRLG VQEVSASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG EEAQRLFRDA NEMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVLAVSRHLR QQTEKVGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFDARH DDYNKIMVKA IADRLAEAFA EYLHERVRKV QWGYAANENL SNDELIRENY QGIRPAPGYP ACPEHTEKGT IWQLLDVETH TGMKLTESFA MWPGASVSGW YFSHPDSKYF AVAQLQRDQV EDYAFRKGMS VSEVERWLAP NLGYDAD // ID E3GG57_EUBLK Unreviewed; 791 AA. AC E3GG57; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 29-APR-2015, entry version 28. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADO38597.1}; GN OrderedLocusNames=ELI_3641 {ECO:0000313|EMBL:ADO38597.1}; OS Eubacterium limosum (strain KIST612). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium. OX NCBI_TaxID=903814 {ECO:0000313|EMBL:ADO38597.1, ECO:0000313|Proteomes:UP000006873}; RN [1] {ECO:0000313|Proteomes:UP000006873} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KIST612 {ECO:0000313|Proteomes:UP000006873}; 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; ADO38597.1; -; Genomic_DNA. DR RefSeq; WP_013381904.1; NC_014624.2. DR RefSeq; YP_003961560.1; NC_014624.2. DR EnsemblBacteria; ADO38597; ADO38597; ELI_3641. DR KEGG; elm:ELI_3641; -. DR PATRIC; 42610069; VBIEubLim172772_3373. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR BioCyc; ELIM903814:GH0C-3704-MONOMER; -. DR Proteomes; UP000006873; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006873}; KW Methyltransferase {ECO:0000313|EMBL:ADO38597.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006873}; KW Transferase {ECO:0000313|EMBL:ADO38597.1}. SQ SEQUENCE 791 AA; 85545 MW; 21D244E53B08F0BF CRC64; MKFTEALKTK RLYLDGAMGS LLQAKLENIG PVPEALTLTH PEIIQDIHRA YIEAGADIIT TCTFGANGYK LNDTEYDQGA IITAAVKLAK ELKPGYVALD IGPLGALIGS LGEISFDEAY HYFAQMVEIG AAAGADVLLI ETVTDIYEMK AAVLAAKEHS NLPVIASMTF EENGRTLTGS DPQTVVTVLE ALGVDAIGIN CSTGPDKMMP VIDTLLKYAS VPVVVQPNAG LPRVVDEKTF YDITSDEFAA YMAEIAQNGA SVLGGCCGTT PEYIQKTIDA TKVSPLPDLG NLRPEKQQTL VATGTRTVAL GQDIRIIGEC INPTTNVALK EELRRGELSL VKKLAIEQKK EGAHILDINL GLPDIDEKEM MLKAVEAVSN LVDLPLQIDS SDPEVIEAVL RQYNGKPIIN SVNGEQSSME RILPIARKYG ACVLGLTMDE KGIPEKAKDR LAIGKRIIHK AASMGIPKKN MLLDCLVLTA SAQQEMVKET IKALELIHSE LQVPTVLGIS NISFGLPNRE LMNRTFLTMA FTAGLNTPIM NPSDQGMMDV VTSFRGLWGY DERCIQYVTK YNSKSAAPVA KDKGEALPDL KKMVVKGMKE EAAAATEELL KTLDPMALVN DYLIPGLDIV GEEFETGEAF LPNLIFAAEA VQKSFEIIKS HLSAEEQIIK GRIVLATVSG DVHDIGKNIL KVILENYGYE ILDLGKDVET ERIVATVKKE NIRLVGLSAL MTTTVKNMAE TVSQLHERCP ETAVMVGGAV LNAEYAADIG ADYYGKDAKA GVNIAQSIFE K // ID E3HDK0_ILYPC Unreviewed; 1141 AA. AC E3HDK0; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 27-MAY-2015, entry version 34. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ADO84186.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADO84186.1}; GN OrderedLocusNames=Ilyop_2427 {ECO:0000313|EMBL:ADO84186.1}; OS Ilyobacter polytropus (strain DSM 2926 / CuHBu1). OG Plasmid pILYOP01 {ECO:0000313|EMBL:ADO84186.1, OG ECO:0000313|Proteomes:UP000006875}. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Ilyobacter. OX NCBI_TaxID=572544 {ECO:0000313|EMBL:ADO84186.1, ECO:0000313|Proteomes:UP000006875}; RN [1] {ECO:0000313|EMBL:ADO84186.1, ECO:0000313|Proteomes:UP000006875} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2926 / CuHBu1 {ECO:0000313|Proteomes:UP000006875}, and RC Plasmid pILYOP01 {ECO:0000313|Proteomes:UP000006875}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002282; ADO84186.1; -; Genomic_DNA. DR RefSeq; WP_013388845.1; NC_014633.1. DR RefSeq; YP_003968534.1; NC_014633.1. DR EnsemblBacteria; ADO84186; ADO84186; Ilyop_2427. DR KEGG; ipo:Ilyop_2427; -. DR PATRIC; 42648783; VBIIlyPol34265_2514. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; IPOL572544:GJ9I-2516-MONOMER; -. DR Proteomes; UP000006875; Plasmid pILYOP01. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006875}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADO84186.1}; KW Plasmid {ECO:0000313|EMBL:ADO84186.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006875}; KW Transferase {ECO:0000313|EMBL:ADO84186.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 237 237 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 301 301 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 734 734 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1141 AA; 125954 MW; C0EDEC09DBAC7DA3 CRC64; MRELLKEKIL ILDGAMGTAI QNYSLEESDF RGELFSHIKG SLRGCNELLN LTKPEVLEEI HLSYLEAGAD IIETNTFNSN RISMREYGLE EKSYDLSKAG AELAVKAARK YEYDNKKRIF VAGSMGPTSK SASIPTGGDP FGREVSYSEL KAAYKEQALG LFDGGVDAFL IETIFDGLNA KAAVIAIEEV LEEKGEKLPI MISGTVDVNG KLLSGQSIES LIVAIDRDSI ISYGLNCSFG AKELIPLIKK LGKLTKKNIS LYPNAGLPNE KGEYDETPHM TGSYVKELIE NKDINILGGC CGTTPEHIKV MAELAQGKSP RKTSMENLAG IVSGNDTVSL HEEFLVVGER NNVSGSRKFA RLIREESYDE ALDIARTQVE KGAKILDINL DDALLDSVEE MEKFIRLLQN DMILSKLPIM IDSSNFDVIE KGLENLAGKG IVNSISLKDG EHEFLRKAAV VRKFGAALVV MAFDEKGQAV SSERKKEICK RAYELLTSNN FPAEDIIFDP NVLTVGTGTE EDRMHGVDFI DSVKWIKENL PGAGVSGGVS NLSFAFRGNN ILRHTIHKIF LEEGEKAGMT MAIVNPGEDP GNITPEVRKA VENLLAGDKN AVDEILNLSF EKSAKKTAEI KPVTVEERLK DYLLKGRSQG IEDDIKTALE KYSPLQVIQE VLMEGMEEVG ALFEKGELFL PQILRSAAVM EKAVEFLTPL IEAGGKEKNV KGKVLMATVE GDVHDIGKNI VGTVLKCNGF DVVDLGVMVP KDQILEAILR HDVDMVTLSG LITPSLMEME KVAEMMAEQN MDIPLLIGGA AASELSTAVR IEPKYSGRVI HVTDASGTLP VVSSLMSEKK SDFLDERKKK AEYLRDAYLK NKNKKEMHSL EEARKRRKKL DNAIEYPKEI GKQFIEIALE DLEPLIDWDM LLHALKSKGN TQEKKVLDES KEILSKMKDM NIKAKCAFGI FNLFKDEDTL IVSGEKDYEL PMVRSQIGNE TISMADFFSK EDHIGAFVIS VPEIAGSDDY ESIIYQLLGT RLAEAASEWM EKYVNDNIWR VNIRPAIGYP SVPDHSMKKE IFKLVDGAET GAKLSSNYAM TPLSSVCGLY VSNPNSFYFD PGKISYDQLK ELANLRGLSV DDMNALLGGI V // ID E3HVK2_ACHXA Unreviewed; 1257 AA. AC E3HVK2; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 29-APR-2015, entry version 32. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADP13867.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADP13867.1}; GN Name=metH {ECO:0000313|EMBL:ADP13867.1}; GN OrderedLocusNames=AXYL_00509 {ECO:0000313|EMBL:ADP13867.1}; OS Achromobacter xylosoxidans (strain A8). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Achromobacter. OX NCBI_TaxID=762376 {ECO:0000313|EMBL:ADP13867.1, ECO:0000313|Proteomes:UP000006876}; RN [1] {ECO:0000313|EMBL:ADP13867.1, ECO:0000313|Proteomes:UP000006876} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A8 {ECO:0000313|EMBL:ADP13867.1, RC ECO:0000313|Proteomes:UP000006876}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002287; ADP13867.1; -; Genomic_DNA. DR RefSeq; WP_013391263.1; NC_014640.1. DR RefSeq; YP_003976582.1; NC_014640.1. DR EnsemblBacteria; ADP13867; ADP13867; AXYL_00509. DR GeneID; 9894841; -. DR KEGG; axy:AXYL_00509; -. DR PATRIC; 42553998; VBIAchXyl160325_0511. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; AXYL762376:GJUB-509-MONOMER; -. DR Proteomes; UP000006876; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006876}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADP13867.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006876}; KW Transferase {ECO:0000313|EMBL:ADP13867.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 256 256 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 789 789 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1257 AA; 138840 MW; F504FF4CD4B41593 CRC64; MSYPRLPYPP EAYTHGGEFA RLLGKRILIL DGAMGTMIQR YKLGEADFRG ERFAAHGKDV KGNNELLSLV RPDVISEIHR QYLEAGADVI ETNTFGATTI AQGDYELPAL AYELNLVSAR LAREACDAYS TPDRPRFVAG ALGPQPKTAS ISPDVNDPGA RNVTFEELRV AYVEQLNGLL DGGIDIVLIE TIFDTLNAKA AIFATEEVFE ARGVRLPVMI SGTVTDASGR ILSGQTVEAF WNSVRHARPI TIGLNCALGA ALMRPYVAEL ARICDTYVCV YPNAGLPNPM AETGFDETPA DTSALLEEFA RAGLVNMSGG CCGTTPDHIR EIAAKVMSLT PRAVPDIPVK TRLSGLEPLN IDEDTLYVNV GERTNVTGSK MFARLIREEK YDEALAVARQ QVENGAQIID INMDEAMLDS VACMRRFLNL IASEPDIARV PIMIDSSKWE VIEEGLKCVQ GKPVVNSISM KEGLEPFRHH ARLCRRYGAA VVVMAFDELG QADTLERRKE ICGRAYKILV EEEGFPPEDI IFDPNVFAVA TGIDEHNHYA VDFIEGTRWI RENLPHARIS GGVSNVSFSF RGNEPMREAI HTVFLYYAVK EGMTMGIVNA GQLGVYADLD PKLRDLVEDV VLDRAEPVGK TEADDERTPT ERLVQFADSV KGSGAKKEED LAWRDAEVEK RLSHALVHGI TTFIVEDTEE VRQKIFDRGG RPIEVIEGPL MDGMNVVGDL FGEGKMFLPQ VVKSARVMKQ AVAHLIPFIE EEKRQIAAAG GDVRAKGKIV IATVKGDVHD IGKNIVSVVL QCNNFEVVNM GVMVPCAQIL EKAKEENADI VGLSGLITPS LEEMAYVASE MQRDEYFRSR KLPLMIGGAT TSRVHTAVKI APNYEGPVIY VPDASRSVGV ATNLMSDQSE TYLAELAEEY EEVRRRHANR KATPILPLAE ARASRPAIDW DNYTPPRPKF IGRRTFKSYD LAEIAKYVDW GPFFQTWSLF GPFPAILDDK VVGEQARKVY ADGLAMMKRI IEGRWLTANG VVGFYPANSI NDEDIEVYKD ETRSEVLFTY RNLRQQGAKR EGVSNKSLSD FIAPKSSGKL DYIGMFAVTA GLGIEKKEAE FEKALDDYSS IMLKSLADRL AEGFAECLHA RVRQDLWGYA PDEALSNEDM IAEKYVGIRP APGYPACPEH VIKTDMFRVL DGADIGMMLT DSYAMYPASS VSGFYFSHPQ SQYFNVGVIG EDQLQDYAAR SGRSIEDLKR TLAPNLG // ID E3I491_RHOVT Unreviewed; 353 AA. AC E3I491; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADP69310.1}; GN OrderedLocusNames=Rvan_0019 {ECO:0000313|EMBL:ADP69310.1}; 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 {ECO:0000313|EMBL:ADP69310.1, ECO:0000313|Proteomes:UP000001399}; RN [1] {ECO:0000313|Proteomes:UP000001399} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG 4299 RC {ECO:0000313|Proteomes:UP000001399}; 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; ADP69310.1; -; Genomic_DNA. DR RefSeq; WP_013417717.1; NC_014664.1. DR RefSeq; YP_004010409.1; NC_014664.1. DR EnsemblBacteria; ADP69310; ADP69310; Rvan_0019. DR KEGG; rva:Rvan_0019; -. DR PATRIC; 42667024; VBIRhoVan113057_0019. DR HOGENOM; HOG000265279; -. DR OMA; AQEDYKM; -. DR BioCyc; RVAN648757:GHZT-19-MONOMER; -. DR Proteomes; UP000001399; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001399}; KW Methyltransferase {ECO:0000313|EMBL:ADP69310.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001399}; KW Transferase {ECO:0000313|EMBL:ADP69310.1}. SQ SEQUENCE 353 AA; 38057 MW; CEA6B6D8FF99625B CRC64; MNRTDRIAAL KAAAKERILI LDGGMGTMIQ RHKPTEADYR GERFKDWPSD LKGNNDLLVL TQPAIIKGVH EAYFEAGADI IETNSFNAQR ISMADYGMEA LSAEINLAAA KLAREAADAY TAKTPEKPRF VAGSIGPTNR TASLSPDVNN PGFRNISFDE LVDAYGEQTR ALIEGGVDAI LIETIFDTLN AKAAGFAVKK AFDETGVELP LMLSGTVTDL SGRNLSGQTP EAFWYSLRHL KPFSVGMNCA FGAEQLRPPV ALLSKVADTY MSVYANAGLP NEMGEYDETP EDMARAMASW AADGLLNIVG GCCGTTPDHI AAIAKAVAPY PPRRIPELEP RLRLSGLEAF VQG // ID E3JAH3_FRASU Unreviewed; 1236 AA. AC E3JAH3; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 01-APR-2015, entry version 31. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADP81024.1}; GN OrderedLocusNames=FraEuI1c_2999 {ECO:0000313|EMBL:ADP81024.1}; OS Frankia sp. (strain EuI1c). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Frankineae; Frankiaceae; Frankia. OX NCBI_TaxID=298654 {ECO:0000313|EMBL:ADP81024.1, ECO:0000313|Proteomes:UP000002484}; RN [1] {ECO:0000313|EMBL:ADP81024.1, ECO:0000313|Proteomes:UP000002484} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EuI1c {ECO:0000313|EMBL:ADP81024.1, RC ECO:0000313|Proteomes:UP000002484}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002299; ADP81024.1; -; Genomic_DNA. DR RefSeq; WP_013424142.1; NC_014666.1. DR RefSeq; YP_004016894.1; NC_014666.1. DR EnsemblBacteria; ADP81024; ADP81024; FraEuI1c_2999. DR KEGG; fri:FraEuI1c_2999; -. DR PATRIC; 42618098; VBIFraSp2231_3085. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; QPFFNAW; -. DR BioCyc; FSP298654:GHN6-3031-MONOMER; -. DR Proteomes; UP000002484; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002484}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002484}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 261 261 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 325 325 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 784 784 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1236 AA; 131966 MW; D45FDAA87CCDC299 CRC64; MGTGVNQSLT AGHDVAARGR RIQELRDLLA QRVVVVDGAY GTMLQSVGLT PADYRVGGVV PEDHPRDVTG DPDLLNLTRP DVIRDVHHQY LVAGADVITT NTFTATSIGQ GDYALQPLVR EMNLAGAALA RKVADEVAAE TGTTRFVAGS IGPLNVTLSL SPRVDEPAYR AVTFDEVKAS YAEQISALAD GGVDLLLIET IFDTLNAKAA IAAAKEAAPE LPLWISVTIV DMSGRTLSGQ TVEAFWASIA HADPLVVGLN CSLGAAEMRP YVAELSALAG THIASYPNAG LPNAFGGYDQ TPAEAGQLLG EFATSGIVNI VGGCCGTTPA HIASVAGAVK GVTPRALPDR PARTRFSGLE PFEIAPSTGF VMIGERTNVT GSARFRRLIE ADDYQAAVDV ALEQVRGGAN LLDVNMDADL LDGEQAMTTF LNLIATEPEV ARIPIMIDSS KWSVLEAGLR CVQGKGVVNS ISLKEGEEPF LDHARLIRSY GAGVVVMAFD EQGQADTTER KVAICGRAYD LLTQKIGFPA EDIIFDPNVL AVATGIAEHN GYAKAFIDAL PLIKERCPGV HLSGGISNLS FSFRGNDVVR EAMHSAFLYY AVTAGLDMGI VNAGQLAVYS DIPAELLELV EDVLFDRRED ATDRLVTYAE ELRASGGGAT GPRKGADLSW RAGTVEERLS HALVRGIVDF IEEDTEEARA KSARPLDVIE GPLMDGMKIV GDLFGAGKMF LPQVVKSARV MKRSVAYLEP YMEAEKAQAL AEGRIAPGRG AGKVVLATVK GDVHDIGKNI VGVVLGCNNY EVIDLGVMVP TAKILDTAVA EGADAVGLSG LITPSLDEMV SVAAEMDRRG LKLPLLIGGA TTSRQHTAVR IAPAYQGTTV HVLDASRVVG VVSDLLDADR AAALDVRNRA DQATLREQHE NRQVRPLLSL AAARANREQI SFDNLPTPSF TGLRTLTPSI AELREFIDWR FFFLAWELKG SYPAILDEPV ARELFDDATA LLDQVIADGT LTAHGVHGVW PAHADGDDLV VASSDGDVRF PMLRQQTEKP AGRANRSLAD YVAPAGGGDH LGAFAVCIQG ADALAAGFEA DQDDYRSIMI KALADRLAEA FAEFIHLEAR RAWFEPDASP AMADLHAERF RGIRPALGYP ACPDHTEKRE LFDLLGAETL GMQLTSSFAM TPAAAVSGLI FANPEARYFT VGRISREQVE DYAARQGKPV TEVERWLRPN LAYDPA // ID E3K086_PUCGT Unreviewed; 370 AA. AC E3K086; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 2. DT 29-APR-2015, entry version 24. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EFP77711.2}; GN ORFNames=PGTG_03667 {ECO:0000313|EMBL:EFP77711.2}; 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 {ECO:0000313|EMBL:EFP77711.2, ECO:0000313|Proteomes:UP000008783}; 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] {ECO:0000313|Proteomes:UP000008783} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CRL 75-36-700-3 / race SCCL RC {ECO:0000313|Proteomes:UP000008783}; 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; DS178268; EFP77711.2; -; Genomic_DNA. DR RefSeq; XP_003322130.2; XM_003322082.2. DR EnsemblFungi; EFP77711; EFP77711; PGTG_03667. DR GeneID; 10539083; -. DR KEGG; pgr:PGTG_03667; -. DR EuPathDB; FungiDB:PGTG_03667; -. DR InParanoid; E3K086; -. DR KO; K00547; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000008783; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008783}; KW Reference proteome {ECO:0000313|Proteomes:UP000008783}. SQ SEQUENCE 370 AA; 40616 MW; DA0D90D79339118C CRC64; MERLFPNHAG HPKIVLMDGG SGTTLEDEFG CRLKSQLWSS ELLLNRPEIL SSLHHAWEQA GAQIISTASY QATLEGFRSL LSQSSRGETE EKDVGSDVSL QLLRRSVALA RDSLSGSNAR VALSLGPYGA TLTPGQEYSG CYPAPYDSEE KLVNFHFDRL MDYAEDYSTW EKVDIVLFET VPNLTEARAI RRAWKKFERT LHALIRRSAT GANPDSSSKP WVISFVFPTS TGQFPTGENP SQVLQAALIT DADAELAEPS GVGVNCTKLG NLQPILEAWR TSAVDHSKTW LWLYPDGGPT YDSVNRSWTG SPITHQEWAN QLFTIASNFS ASWAGIVLGG CCKAGTPHIR ALHQLLSSTA RNEDSLNNSD // ID E3M453_CAERE Unreviewed; 1288 AA. AC E3M453; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 01-APR-2015, entry version 30. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EFO91498.1}; GN ORFNames=CRE_11691 {ECO:0000313|EMBL:EFO91498.1}; OS Caenorhabditis remanei (Caenorhabditis vulgaris). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281}; RN [1] {ECO:0000313|Proteomes:UP000008281} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281}; RG Caenorhabditis remanei Sequencing Consortium; RA Wilson R.K.; RT "PCAP assembly of the Caenorhabditis remanei genome."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; DS268424; EFO91498.1; -; Genomic_DNA. DR RefSeq; XP_003108989.1; XM_003108941.1. DR EnsemblMetazoa; CRE11691; CRE11691; CRE11691. DR GeneID; 9820934; -. DR CTD; 9820934; -. DR InParanoid; E3M453; -. DR OMA; DYNSIMV; -. DR Proteomes; UP000008281; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 2. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008281}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008281}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 287 287 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 350 350 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 351 351 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 813 813 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1288 AA; 143367 MW; F551137A9A88A66B CRC64; MTRSSLFKEL ADIAKERIMI IDGAMGTMIQ REYMEENDFR GEMIEAQKCS SDDVLIELKQ LCFQILKDHD KPLKGNNDLL SITRPDIIYK IHKLYLEAGA DFVETNTFSG TTIAQADYRC EHLVHEINYQ SALVARKACD DVGAATGKLE NLIEDVELFL NLGRRRYVCG AIGPTNRTLS ISPSVEKPDF RNVTFQELVK AYGDQARSLI QGGVDVLLVE TVFDSANAKA ALFAIRTLFE DEGVPEIPVF LSGTIVDMSG RTLSGQTGEA FLVSTKQGSP MAVGLNCALG AKDMRQFVAN MSKWSDTLIL CYPNAGLPNA LGGYDETPQE MADVLREFAR DGLVNIIGGC CGTTPDHINA MYKAVQGISP RIPPSDPHAG KMLLSGLEPS IVGPETNFVN IGERCNVAGS RRFCNLIKNE NYDTAIDVAR VQVDSGAQIL DVNMDDGLLD GPYAMAKFLR LISSEPDVAK IPVCIDSSDF DVIIAGLEST QGKCVVNSIS LKEGEEKFKE RARIVKRYGA AVVVMAFDEE GQAAETERKF EICERSYRIL TEEVGFNPND IIFDANILTI ATGMEEHSNY GMYFIEATRM IRENLPGAHV SGGVSNISFS FRGMEAIREA MHSVFLFYAI KAGMDMGIVN AGALPVYEDI DKPLLQLLED LLFNRDPEAT EKLLVAAQEM KKDGKKSDTK TDEWRTTTVE ERLKFALVKG IDQFVVADTE EARQNTEKYP RPLNVIERPL MDGMAVVGEL FGAGKMFLPQ VIKSARVMKK AVAHLLPFMD AERQANIEKL GLTEEESPYQ GTVVIATVKG DVHDIGKNIV AVVLGCNNFK VVDLGVMTPC ENIIKAAIEE KADFIGLSGL ITPSLDEMVH VAKEMSRVGL KIPLLIGGAT TSKTHTAVKI APRYPHPVVH CLDASKSVVV CSSLSDMTVR DAFLQDLNED YEDVRQEHYE SLKDRRFTAL GKTREKKFNI DWNKFTAVKP SFVGRREYQN FDLNELIPYI DWKPFFDVWQ LRGKYPNRSY PKIFHDADVG AEAKKVFDDA QKWLKKLIDE KVLTANAVVS FLPAASEGDD IHVYDPENGN KLDTFFGLRQ QSGREHDQSH FCLSDFIKPL KSGKSFFLHT WQFFLIFTIS GVPDDYLGLF ACTAGLGAEE YCKVLEENHD DYASIMVKAL ADRLAEAYAE YLHKEVRTNL WGYSTNEQLT ETDLLSIKYE GIRPACGYPS QPDHTEKRTL WKLLEAENNG IILTEHLAML PAASVSGLYF ANPQSQYFAV GKIDEDQVCF IEENKSIL // ID E3M9Z8_CAERE Unreviewed; 302 AA. AC E3M9Z8; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 07-JAN-2015, entry version 21. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EFO96913.1}; GN ORFNames=CRE_17193 {ECO:0000313|EMBL:EFO96913.1}; OS Caenorhabditis remanei (Caenorhabditis vulgaris). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281}; RN [1] {ECO:0000313|Proteomes:UP000008281} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281}; RG Caenorhabditis remanei Sequencing Consortium; RA Wilson R.K.; RT "PCAP assembly of the Caenorhabditis remanei genome."; 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; DS268431; EFO96913.1; -; Genomic_DNA. DR RefSeq; XP_003107073.1; XM_003107025.1. DR EnsemblMetazoa; CRE17193; CRE17193; CRE17193. DR GeneID; 9809869; -. DR CTD; 9809869; -. DR InParanoid; E3M9Z8; -. DR OMA; HWTFPAN; -. DR Proteomes; UP000008281; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008281}; KW Reference proteome {ECO:0000313|Proteomes:UP000008281}. SQ SEQUENCE 302 AA; 33858 MW; 5FA5F0DC58E9C680 CRC64; MVRLLDGSMS AQLKHFGYDC NSAENIPHWT FPANSDESLV ANAYKSFLDL GVTDITTNTY HFGSTLDKRI PENDSKKKIY EKYFKIACSS LVKLTEMKDG VRVWGSVGTL ATLYHDMSEY NGKYMDNEDA ENTARNYYQT ILTLFQTKTK VRNLVFETIP LAVEGLMALE ALKRFPEMRA VMSFTFKENA CLRHGEEIDT LAGELRKCSQ IVGMGINCTD PENVLPALKV IKKHNFPEVF VYPNMGDSKF LNEGSDESDV FNIDMVTGWV ENGATAIGGC CGVTEAQMKI LKKIVDNLNN AK // ID E3PBY4_ECOH1 Unreviewed; 1227 AA. AC E3PBY4; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 27-MAY-2015, entry version 32. DE SubName: Full=Escherichia coli ETEC H10407, complete genome {ECO:0000313|EMBL:CBJ03780.1}; GN OrderedLocusNames=ETEC_4274 {ECO:0000313|EMBL:CBJ03780.1}; OS Escherichia coli O78:H11 (strain H10407 / ETEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=316401 {ECO:0000313|EMBL:CBJ03780.1, ECO:0000313|Proteomes:UP000006877}; RN [1] {ECO:0000313|EMBL:CBJ03780.1, ECO:0000313|Proteomes:UP000006877} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H10407 / ETEC {ECO:0000313|Proteomes:UP000006877}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; FN649414; CBJ03780.1; -; Genomic_DNA. DR RefSeq; WP_000096005.1; NC_017633.1. DR RefSeq; YP_006117811.1; NC_017633.1. DR EnsemblBacteria; CBJ03780; CBJ03780; ETEC_4274. DR KEGG; elh:ETEC_4274; -. DR PATRIC; 42965084; VBIEscCol136115_4854. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; ECOL316401:GLD0-4370-MONOMER; -. DR Proteomes; UP000006877; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006877}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136011 MW; 7B2186DA075BD743 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETI RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAD // ID E3PU13_CLOSD Unreviewed; 770 AA. AC E3PU13; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 29-APR-2015, entry version 23. DE SubName: Full=Str. DSM 519 chromosome, complete genome {ECO:0000313|EMBL:CBH20274.1}; GN OrderedLocusNames=CLOST_0144 {ECO:0000313|EMBL:CBH20274.1}; OS Clostridium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / NCIB OS 10654). OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Peptoclostridium. OX NCBI_TaxID=499177 {ECO:0000313|Proteomes:UP000007041}; RN [1] {ECO:0000313|Proteomes:UP000007041} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / NCIB 10654 RC {ECO:0000313|Proteomes:UP000007041}; 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 ----------------------------------------------------------------------- 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; CBH20274.1; -; Genomic_DNA. DR RefSeq; YP_003935179.1; NC_014614.1. DR EnsemblBacteria; CBH20274; CBH20274; CLOST_0144. DR KEGG; cst:CLOST_0144; -. DR PATRIC; 42270870; VBICloSti32817_0141. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR BioCyc; CSTI499177:GJE9-152-MONOMER; -. DR Proteomes; UP000007041; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007041}; KW Reference proteome {ECO:0000313|Proteomes:UP000007041}. SQ SEQUENCE 770 AA; 84199 MW; EAC32FD0AA9B4C05 CRC64; MIKIFDGGFG SQLISKSICF ECPEELNLTQ GEVIKQIHKE YADNGADIIT TNTFGANPLK LKSYDLEDKV MEINVAGINL AKTTGKEIAF SVGPTGEFVK PVGDVSFEEM YEIFYRQLEA ITISQPDYVI FETFSDIGEL RAGIIALKDI FKKHNIKIPI LASMTYDSIY TLTGVSPAAQ GVILDALGVD AIGINCSKGP KDILELLVEI EKYTSVKLIA QPNAGMPEIV GEDVVYSMSA SEFANQMKPY FELNMGYIGS CCGSTPEFTK ELRRLVDSIE VKNIKENKAS SHGYLASKGK VVSSEAFILI GEAINPHARK AVKLYMEEFD IKGLTSVISE QCLKGADVID INVNAEGADK KALARELVIS GQLNSDFVLC IDSKEPEIIE EALKNYAGKA LINSVALDEK ELSEILPLAK KYGASVIGLC IENEILPTTI AETVEIAEKL QSRLLSEGIR AEDIYIDPLL FTNKTYSISP LDTVEIVRQL SNKGIKTSLG LSNVSYGMKN RDRLNQTLLS MLIGSGLSMA IASASSKGIV ETIESAQILM GKEKISNKTY IELEDIDKLT IEGELIYQLI NKEEPSAFDS LLAEKTEQEV INTMLIALDQ AGKLYDEKTI FLPDMMQVVE KVQGLFDRLE NKAKSSHTLV FGTVYGDIHD IGKNIVKSVL KPFGYNIIDL GKSVTKEAFV AKAKEVNADI IGISALMTTT MVNLEPTIEY IKSELPNVKI IVGGAVVTED YARKVGADGY SKDAIKAIGL VKSLTEVDEK // ID E3QXE4_COLGM Unreviewed; 355 AA. AC E3QXE4; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 04-MAR-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFQ35532.1}; GN ORFNames=GLRG_10676 {ECO:0000313|EMBL:EFQ35532.1}; 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 Colletotrichum. OX NCBI_TaxID=645133 {ECO:0000313|Proteomes:UP000008782}; RN [1] {ECO:0000313|Proteomes:UP000008782} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M1.001 / M2 / FGSC 10212 {ECO:0000313|Proteomes:UP000008782}; 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; GG697395; EFQ35532.1; -; Genomic_DNA. DR EnsemblFungi; EFQ35532; EFQ35532; GLRG_10676. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000008782; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008782}; KW Methyltransferase {ECO:0000313|EMBL:EFQ35532.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008782}; KW Transferase {ECO:0000313|EMBL:EFQ35532.1}. SQ SEQUENCE 355 AA; 38428 MW; F409D5A9DD0CE32A CRC64; MDDAEKQSPR ILVLDGGLGT SLEDKYGIGF ESATTPLWST HLLVDGQDTL LACQKDFGNV PVDIILTATY QLSIDGFANT RTAKYPNGID CAAIRNFIQD AIRIAHEAGR AHGTKTALSI GPYGACMIPG QEYSGAYDSD HDSLEKLRDW HLERLQLFKD AGAFSSPVAY VAVETIPRSD EIKAVRQALD RIGLFATENP LPFWIATLFP RQDNCLPDGS SVKEAVTAML GPDVAMSRPW GIGINCTKVW KLESLIKSYE SAVQELIQEG AIAEAPALVL YPDGTNGEVY NTATQKWELP GGSHHPVTSW EAQLSQVVAG AQSRGLWNQI VVGGCCKASH SDIARLRAAV EGLSR // ID E3R3B5_9LACO Unreviewed; 329 AA. AC E3R3B5; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Putative homocysteine S-methyltransferase {ECO:0000313|EMBL:EFQ44904.1}; GN ORFNames=LBKG_00782 {ECO:0000313|EMBL:EFQ44904.1}; OS Lactobacillus crispatus CTV-05. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=440496 {ECO:0000313|EMBL:EFQ44904.1}; RN [1] {ECO:0000313|EMBL:EFQ44904.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CTV-05 {ECO:0000313|EMBL:EFQ44904.1}; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease.; RA Ward D., Xu Q., Earl A., Liu Y., Feldgarden M., Gevers D., Young S.K., RA Zeng Q., Koehrsen M., Alvarado L., Berlin A., 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., Howarth C., RA Jen D., Larson L., Mehta T., Neiman D., Park D., Pearson M., RA Richards J., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Haas B., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Lactobacillus crispatus strain CTV-05."; 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; GL531737; EFQ44904.1; -; Genomic_DNA. DR RefSeq; WP_005719570.1; NZ_GL531737.1. DR EnsemblBacteria; EFQ44904; EFQ44904; LBKG_00782. DR GeneID; 9107864; -. DR PATRIC; 44747606; VBILacCri70875_0775. DR OrthoDB; EOG6C019S; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFQ44904.1}; KW Transferase {ECO:0000313|EMBL:EFQ44904.1}. SQ SEQUENCE 329 AA; 37079 MW; AC5A97247149A998 CRC64; MNLLKQIRDR GLILDGAMST ALEKLGIDTN NELWTAIALE HNLAQIYQVH MNYFKAGAQM AITDTYQANI PAFEKHGFTQ DQATKLITNA VQIAKKARDD FAKTTGIHNY VAASVGPYGA YLAQGDEFRG DYSLTTEEYL NFHLPRLKIL LANKPDCLAL ETQPKLDEVV AILDWLKENA PEIPVYVSFT LHDTTKISDG TPLKRVVQKL NEYDQVFAIG ANCFKPFLAT AVIDKIHDFT DKQIVIYPNL GGVYNEFERN WIPFNAKFDF KKLSQEWYEH GARIIGGCCS TTEKEIGQIS AFFKTINNAK SKSVKSELKK VKNDSNIQI // ID E3RMW9_PYRTT Unreviewed; 319 AA. AC E3RMW9; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 07-JAN-2015, entry version 16. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EFQ92923.1}; GN ORFNames=PTT_09865 {ECO:0000313|EMBL:EFQ92923.1}; 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 {ECO:0000313|Proteomes:UP000001067}; RN [1] {ECO:0000313|EMBL:EFQ92923.1, ECO:0000313|Proteomes:UP000001067} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ92923.1, RC ECO:0000313|Proteomes:UP000001067}; 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; GL534109; EFQ92923.1; -; Genomic_DNA. DR RefSeq; XP_003298974.1; XM_003298926.1. DR EnsemblFungi; EFQ92923; EFQ92923; PTT_09865. DR GeneID; 10523434; -. DR KEGG; pte:PTT_09865; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000001067; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001067}; KW Reference proteome {ECO:0000313|Proteomes:UP000001067}. SQ SEQUENCE 319 AA; 34383 MW; 88314F80BA7EB962 CRC64; MAFTAPPNRL SAHIAKGSPL ILDGALATYL ETLGADISGA LWSASILLDQ PSLIKQTHLD YFRAGANVAI TASYQASIPG LVKHLQLSER EAKDVVKKSV ELAQEARDHY ITESTAEVGN QLFIAGSVGP YGAFLADGSE YRGDYSIPRE EMKDFHRGRI QALVEAGVDI LACETIPSKA ETEALLDLLI TEFASTEAWF GFTLRDSAHI SDGTSLADIA ALFENVQQVV ALGFNCVPDD LSVAALKTLK PLVKRGTLVV YPNSGEQWNA QAREWEGKRT EGSSLAEKTR EWRDAGAGLI GGCCRTTPED IGVMEKALN // ID E3XJI1_ECOLX Unreviewed; 1227 AA. AC E3XJI1; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFR17892.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFR17892.1}; GN Name=metH {ECO:0000313|EMBL:EFR17892.1}; GN ORFNames=EC236275_1115 {ECO:0000313|EMBL:EFR17892.1}; OS Escherichia coli 2362-75. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=670897 {ECO:0000313|EMBL:EFR17892.1}; RN [1] {ECO:0000313|EMBL:EFR17892.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=2362-75 {ECO:0000313|EMBL:EFR17892.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; ADUL01000050; EFR17892.1; -; Genomic_DNA. DR RefSeq; WP_000095940.1; NZ_ADUL01000050.1. DR EnsemblBacteria; EFR17892; EFR17892; EC236275_1115. DR PATRIC; 44763445; VBIEscCol143135_1041. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFR17892.1}; KW Transferase {ECO:0000313|EMBL:EFR17892.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136052 MW; 0CD8269975292F72 CRC64; MSSKVEQLCA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVISAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPAEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPT ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANTQ QAEWRSWVVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KMLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK VSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAE // ID E3Y448_SHIFL Unreviewed; 1227 AA. AC E3Y448; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFS13108.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFS13108.1}; GN Name=metH {ECO:0000313|EMBL:EFS13108.1}; GN ORFNames=SF2457T_2815 {ECO:0000313|EMBL:EFS13108.1}; OS Shigella flexneri 2a str. 2457T. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=198215 {ECO:0000313|EMBL:EFS13108.1}; RN [1] {ECO:0000313|EMBL:EFS13108.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=2457T {ECO:0000313|EMBL:EFS13108.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; ADUV01000046; EFS13108.1; -; Genomic_DNA. DR RefSeq; WP_000096021.1; NZ_ADUV01000046.1. DR ProteinModelPortal; E3Y448; -. DR SMR; E3Y448; 651-1227. DR EnsemblBacteria; EFS13108; EFS13108; SF2457T_2815. DR KEGG; sfx:S3645; -. DR PATRIC; 18709098; VBIShiFle31049_3987. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFS13108.1}; KW Transferase {ECO:0000313|EMBL:EFS13108.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135857 MW; DA24CC6AD801C059 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLA AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKADDTANAQ QAEWRSWDVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RIAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFAIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTCKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDHARRKGMS VSDVERWLAP NLGYDAD // ID E3YQX3_9LIST Unreviewed; 617 AA. AC E3YQX3; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 07-JAN-2015, entry version 20. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=NT05LM_1970 {ECO:0000313|EMBL:EFR87493.1}; OS Listeria marthii FSL S4-120. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=702457 {ECO:0000313|EMBL:EFR87493.1, ECO:0000313|Proteomes:UP000003412}; RN [1] {ECO:0000313|EMBL:EFR87493.1, ECO:0000313|Proteomes:UP000003412} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FSL S4-120 {ECO:0000313|EMBL:EFR87493.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFR87493.1}. 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; ADXF01000703; EFR87493.1; -; Genomic_DNA. DR EnsemblBacteria; EFR87493; EFR87493; NT05LM_1970. DR PATRIC; 44804919; VBILisMar157200_1874. DR Proteomes; UP000003412; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003412}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EFR87493.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EFR87493.1}. SQ SEQUENCE 617 AA; 68435 MW; 3BCDF47CCD2E4A55 CRC64; MNLRKDLSEK VLIADGAMGT LLYSYGVDRS FEELNLSHPE DIVAIHKAYI GAGADIIQTN TYGANYIKLA RYGLEDEVKR INQAAIRLAK EAARGTGTYI FGTIGGINGA VDARLPAAPL EEIKRSFREQ LYCFLLDGVD AILLETYYDL DELKTVLKIL RETTDLPVVA NVSMHEPGIL QNGQKLPDAL EELIALGADV VGINCRLGPY HMARALETVP LYDKAYLAVY PNASLPEMQE GKVVYQSDTD YFAQYGEVFR QEGARIIGGC CGTTPDHIRA LRAGLQSTKP ILEKEVRPIL ELVPEEVEDA ESGERLLDKV KERLTILVEL DPPRTFDTTK FFEGAKALDA AGVDAITISD NSLATPRISN MALASILKHE YGIKPLIHLT TRDHNLVGMH SHVMGFHKLG LHDVLAITGD PTKVGDFPGA SSVFDLRSVE LVQLIKKFNA GISYTGKSLK EKARFHVGAA FNPNVLNLEK AVRLIERKVD YGADYIITQP IYDVNKAVLL KEALQKAKID VPLFIGVMPL LSSRNAEFLH NEVPGIRLTD EVRERMREAE EHGHANEEGM AIARELVDAI CEHFQGIYII TPFLRYDLSI ELAKYVQNKQ QVQIVSK // ID E3ZR79_LISSE Unreviewed; 617 AA. AC E3ZR79; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAY-2015, entry version 20. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=NT03LS_1996 {ECO:0000313|EMBL:EFR99872.1}; OS Listeria seeligeri FSL N1-067. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=702453 {ECO:0000313|EMBL:EFR99872.1, ECO:0000313|Proteomes:UP000004302}; RN [1] {ECO:0000313|EMBL:EFR99872.1, ECO:0000313|Proteomes:UP000004302} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FSL N1-067 {ECO:0000313|EMBL:EFR99872.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFR99872.1}. 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; ADXJ01000726; EFR99872.1; -; Genomic_DNA. DR RefSeq; WP_003748159.1; NZ_CM001051.1. DR EnsemblBacteria; EFR99872; EFR99872; NT03LS_1996. DR Proteomes; UP000004302; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004302}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EFR99872.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EFR99872.1}. SQ SEQUENCE 617 AA; 68619 MW; 1F8F609F8E0D2952 CRC64; MNLRKDLSEK VLIADGAMGT LLYSYGVDRS FEELNLSHPE DIIAIHKAYI GAGADIIQTN TYGANYIKLS RYGLEDQVKR INQAAIRLAK EAARGTGTYI FGTIGGINGA VDAKLPAAPL EEIKRSFREQ LYCFLLEGVD AILLETYYDL DELKTVLKII RETTDLPVVA NVSMHEPGLL QNGQKLSDAL EELIALGADV VGVNCRLGPY HMARALETVP LYDHAYLAVY PNASLPEMQE GKVIYQSDTD YFEHYGEVFR QGGARIIGGC CGTTPDHIRA LRKGLKSIKP VLAKEVRPIL ELVPEEIVDE DSGERLLDKV KERLTILVEL DPPRTFDTTK FFEGAKALNE AGVDAITISD NSLATPRISN MALASILKHE YGIKPLIHLT TRDHNLVGMH SHVMGFHKLG LHDVLAITGD PTKVGDFPGA SSVFDLRSVE LVQLIKKFND GISYTGKSLK EKARFHVGAA FNPNVLNLEK AIRLIERKVE YGADYIITQP IYDVNKAILL KEALQKANIK VPLFIGVMPL LSSRNAEFLH NEVPGIRLTD EVRERMREAE EQGRANEEGM QIARELIDSI CTCFQGIYII TPFLRYDLSI ELAKYVQSKQ QVQIVSK // ID E4HP07_9ACTO Unreviewed; 394 AA. AC E4HP07; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFS91221.1}; GN ORFNames=HMPREF9607_02511 {ECO:0000313|EMBL:EFS91221.1}; OS Propionibacterium humerusii HL044PA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=765109 {ECO:0000313|EMBL:EFS91221.1, ECO:0000313|Proteomes:UP000003179}; RN [1] {ECO:0000313|EMBL:EFS91221.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HL044PA1 {ECO:0000313|EMBL:EFS91221.1}; 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 (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. {ECO:0000313|EMBL:EFS91221.1}. 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; ADZU01000041; EFS91221.1; -; Genomic_DNA. DR RefSeq; WP_002526794.1; NZ_GL383193.1. DR EnsemblBacteria; EFS91221; EFS91221; HMPREF9607_02511. DR PATRIC; 52241830; VBIProAcn160378_2363. DR Proteomes; UP000003179; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000003179}; KW Methyltransferase {ECO:0000313|EMBL:EFS91221.1}; KW Transferase {ECO:0000313|EMBL:EFS91221.1}. SQ SEQUENCE 394 AA; 41646 MW; 8C0EA9A7EE075D04 CRC64; MTLRTALSQN VLIIDGAMGT MLQSSDVTMD AFQGLEGCNE ILNVTRPDVI SGIHDAYLDA GADIIETNTF GANLPALTDY GIASRASELA SAATKLAREA ADKRTDKPRY VVGSIGPGTK LPTLRQIGFA AIRDVYQQVI EAMIDAGIDG VQIETCQDLL QARAAIIGAH RAAAAHKVDL PVLVDFTVET TGTMLMGSET GAALTVLESL GVDAIGLNCA TGPAEMAEHL RTLSRGARVP IMCMPNAGLP EITGEGRVTR WAPMTWPQFL TNTSIATGWP SSVAAVVPLP IIPGPLRSGC PVDRFLSETF TTSMPLLLYT ATSRSVRIPL IWPSANALMP TVPGRSVRPC WLRSGTSAST LPKPKPAMVP IYLICALTTS GATAFRTCQS CRPV // ID E4L9H9_9FIRM Unreviewed; 306 AA. AC E4L9H9; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAY-2015, entry version 12. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFR42475.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EFR42475.1}; GN Name=mmuM {ECO:0000313|EMBL:EFR42475.1}; GN ORFNames=HMPREF9220_0405 {ECO:0000313|EMBL:EFR42475.1}; OS Dialister microaerophilus UPII 345-E. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Dialister. OX NCBI_TaxID=910314 {ECO:0000313|EMBL:EFR42475.1}; RN [1] {ECO:0000313|EMBL:EFR42475.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UPII 345-E {ECO:0000313|EMBL:EFR42475.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFR42475.1}. 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; AENT01000024; EFR42475.1; -; Genomic_DNA. DR RefSeq; WP_007554746.1; NZ_AENT01000024.1. DR EnsemblBacteria; EFR42475; EFR42475; HMPREF9220_0405. DR PATRIC; 45033929; VBIDiaMic169777_0877. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFR42475.1}; KW Transferase {ECO:0000313|EMBL:EFR42475.1}. SQ SEQUENCE 306 AA; 34167 MW; B069366042EEADE2 CRC64; MSTIIELLKE KKLLVIDGSF ASELEKAGLN LCDSLWSAKA LYENPELVTK VHESYFESGA GIAITGSYQA HVQGLLKKGF THEKAIELIK LSVKLAKKAR ENCLKKHPER KLAIAAAVGP YGAYLADGSE YVGNYGLSVK ELEEFHEEKI EALASENPDF FAFETIPSFD EVRAYVNILK RHENITGWFT FSCKDEKHIS EGVEISEVAK FLDKENQVHA IGVNCTKPEY IEPLICEIKK ATDKPVAVYP NTGEKYDPVT KTWSGEPVDF IKYAKRWYES GARLIGGCCR TSPDEIKAVC KFAKSI // ID E4LD30_9FIRM Unreviewed; 811 AA. AC E4LD30; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFR60352.1}; GN ORFNames=HMPREF9199_2008 {ECO:0000313|EMBL:EFR60352.1}; OS Veillonella sp. oral taxon 158 str. F0412. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Veillonella. OX NCBI_TaxID=879309 {ECO:0000313|EMBL:EFR60352.1}; RN [1] {ECO:0000313|EMBL:EFR60352.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0412 {ECO:0000313|EMBL:EFR60352.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFR60352.1}. 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; AENU01000014; EFR60352.1; -; Genomic_DNA. DR RefSeq; WP_009351552.1; NZ_AENU01000014.1. DR EnsemblBacteria; EFR60352; EFR60352; HMPREF9199_2008. DR PATRIC; 45036577; VBIVeiSp174732_0795. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFR60352.1}; KW Transferase {ECO:0000313|EMBL:EFR60352.1}. SQ SEQUENCE 811 AA; 86918 MW; 0074A723BCFFE8D3 CRC64; MYIFDGAMGT MLQAAGLEEG YCPELFNIER PEVVKNIHAQ YLQHGSDVIT TNTFGACGLK LEDYDLQDRV REINIAAVKV AKEAIAEVKP SARVAGSMGP TGRFLQPLGN MSFDDIYDTY REQADALIEG GADFIIIETI IDVQEMRAAL LASLDAREAA GKTKEDVQII CQFSFSEDGR TITGTPPAVA TAIVEAIGAD IIGINCSLGP EQITPLIEEI ASVTNLPISC QPNAGMPQLI NKQTVFPLTA EEMGPLMLPI VDAGASYVGG CCGTTPAHIQ SISDAVKAHT PKERAHVEPK TIITSRTRLL ELGHNTKPLI IGERINPTGR KVLAQELRDG SFIRVKRDAL DQVEAGADIL DVNMGVAGMD QTPLMERAIF ELSMLVETPL SIDTLDPSAM EVALKNYPGR ALINSVNGEE ESITQVMPLA KRYGAALLCL PISSGDLPEK AEDRVALAES IVNRAYGYGL QPHDLLLDPL VLTLASGEDS ARQTLRTLQL YKEKFGFPTV MGLSNISFGM PQRPYLNGQF LTMALACGLT TPIMNPLNYP AKKAFVSSTT LLGWDPGSAQ FIKEYGYEDE SSAPGNSAPK GPEKKSFDSN DPLANIRACV EQGEKEAIVE LVKKALADGM DPLDITKKGL SEAMNVVGDK FGSGKLFLPQ VMLAAETMQA AFNTIKEIIP ASESLDKGTV VVATVKGDIH DLGKNIVAAL LENNGYKIVD LGKDVDPEVI VQAIKDNKAA LVGICSLMTT TMPQIDNTVA AIRAAGLKTK IMVGGAVVSQ DYADQAGADI YAKDGIAAVN HANDFFETLE K // ID E4LE21_9FIRM Unreviewed; 341 AA. AC E4LE21; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFR59881.1}; GN ORFNames=HMPREF9199_0127 {ECO:0000313|EMBL:EFR59881.1}; OS Veillonella sp. oral taxon 158 str. F0412. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Veillonella. OX NCBI_TaxID=879309 {ECO:0000313|EMBL:EFR59881.1}; RN [1] {ECO:0000313|EMBL:EFR59881.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0412 {ECO:0000313|EMBL:EFR59881.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFR59881.1}. 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; AENU01000018; EFR59881.1; -; Genomic_DNA. DR RefSeq; WP_009351960.1; NZ_AENU01000018.1. DR EnsemblBacteria; EFR59881; EFR59881; HMPREF9199_0127. DR PATRIC; 45037299; VBIVeiSp174732_1135. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFR59881.1}; KW Transferase {ECO:0000313|EMBL:EFR59881.1}. SQ SEQUENCE 341 AA; 37241 MW; CBAAC8C45F7E8755 CRC64; MGDMMAKRSA FLDIIKDKGA LVLDGALGTE LERYGCNIQH KLWSAKVLME QPDVIKKIHI TYLAVGADII QSSGYQATVA GFKGLGYGTE EAIELVKLSV RLAVQARNEF LEAKASGALM LRGITLGEET SNGVKYFSEG ALPKPLVAAS VGPYGAFLAD GSEYRGYPDV QTEYLEVFHI PRLALFAEEN PDILSFETIP SYDETIAIAR AMSDPFTSRG IPAWIAFACK DEHHVASGET IIKCAEMIDK VRPVTGIGIN CTKPEYVESL IKDIRTVTDK PIAVYPNLGE SYDSKTKTWY GDPASFVDYV DVWRKAGAEI IGGCCRTTPE IIGDIAKKIH N // ID E4LGN5_9FIRM Unreviewed; 332 AA. AC E4LGN5; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAY-2015, entry version 12. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFR42051.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EFR42051.1}; GN Name=mmuM {ECO:0000313|EMBL:EFR42051.1}; GN ORFNames=HMPREF9162_1283 {ECO:0000313|EMBL:EFR42051.1}; OS Selenomonas sp. oral taxon 137 str. F0430. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Selenomonas. OX NCBI_TaxID=879310 {ECO:0000313|EMBL:EFR42051.1}; RN [1] {ECO:0000313|EMBL:EFR42051.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0430 {ECO:0000313|EMBL:EFR42051.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFR42051.1}. 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; AENV01000002; EFR42051.1; -; Genomic_DNA. DR RefSeq; WP_009438145.1; NZ_AENV01000002.1. DR EnsemblBacteria; EFR42051; EFR42051; HMPREF9162_1283. DR PATRIC; 45039167; VBISelSp169704_0067. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFR42051.1}; KW Transferase {ECO:0000313|EMBL:EFR42051.1}. SQ SEQUENCE 332 AA; 36158 MW; 5E4FDBC91132C875 CRC64; MNIIEERLAV SNILVLDGAF ATELEARGFS VNDALWSAKA IFERPDLVRD VHLDYLRAGA DIVTSASYQA TVEGFVKKGF TEEQAAALIV RSVELAREAR DIYCLESLAD EYHAQEESTR EEQTSCSSDR REKSGGAPLV AASVGPYGAY LADGSEYRGD YGVNEETLSA FHAERLVLLA EGQPDLLACE TLPCLTEAQA IVRALREKEI RIPAWFSFSC RDGAHISDGT PITDCARFLD TVPEAAAVGV NCTAPQYVED LIHAIRRETD KPVVVYPNSG EDYSVSDKSW HGTAEDFAAG ARRWRTAGAR IIGGCCRTSP RDIAGITAWA KA // ID E4LH19_9FIRM Unreviewed; 806 AA. AC E4LH19; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFR41914.1}; GN ORFNames=HMPREF9162_1418 {ECO:0000313|EMBL:EFR41914.1}; OS Selenomonas sp. oral taxon 137 str. F0430. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Selenomonas. OX NCBI_TaxID=879310 {ECO:0000313|EMBL:EFR41914.1}; RN [1] {ECO:0000313|EMBL:EFR41914.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0430 {ECO:0000313|EMBL:EFR41914.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFR41914.1}. 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; AENV01000002; EFR41914.1; -; Genomic_DNA. DR RefSeq; WP_009438018.1; NZ_AENV01000002.1. DR EnsemblBacteria; EFR41914; EFR41914; HMPREF9162_1418. DR PATRIC; 45039439; VBISelSp169704_0201. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFR41914.1}; KW Transferase {ECO:0000313|EMBL:EFR41914.1}. SQ SEQUENCE 806 AA; 86533 MW; B05C67427B9FA7BC CRC64; MQDIIILDGG MGTELQARGL APGERPELFG MEHPEVIEEV HRNYIAAGSR VIYSNTFGAN GHKLVGTGKT VAEVIGANVA IARRAAENSG VPGVRVALDI GPIGELVEPL GTLSFEDAYE LFREMVTAGE AAGADLVIFE TLTDLYEVKA AVLAAKEHTK LPIWVTMTFE QNGRTFLGAA VPSVAVTLDA LGVAALGVNC SLGPVELLPI VAQMMEWTDL PIIVKPNAGL PDPRTGAYEM TAEEFGREMA EFARRGAVIM GGCCGTNPDF IRALAAAVAG GAEDRPKRKK RKGVASPGCV AEYGKLNVIG ERINPTGKKR LQQALLDEDM GYIKKLAISQ QEAGANVLDI NVGAQGVDEE AIIPRVVKAV QSVVDLPLQI DSANPKVIEA ALRVTNGRVI INSVSGERER MNDIFPLAKH YGAAVLGLAL DEAGLPQTAA ERVAIAERII EEAERYGIDR EDIIIDCLTL TVSAQQEQAM ETLRAVREVH DRLGLHCALG VSNISFGLPA RVHMTENFLI QAMHVGLDFP IVNPNTKEIM DAVVSYRAVS GEDVDCAAYI TRFAPEQAEM RRRKELGLTG DTGVDAAVQT AVEQAGDVDP LMDAIMRGLS DDAERITRKL LTEMAPMDII QEKVIPALDI VGDRYEKEII FLPQLINAAN AATAGLELIK VKLAESGQGV SKGKIILATV EGDIHDIGKN IVKVVLENYG YQIIDLGRDV PVTRVVEVAI EKQVGLIGLS ALMTTTVTAM KRTIEALHEA GHDCQTIVGG AVLTEDYARE IGADYYAGDA RSIVEIARRV LDEQED // ID E4LH20_9FIRM Unreviewed; 592 AA. AC E4LH20; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAY-2015, entry version 18. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HMPREF9162_1419 {ECO:0000313|EMBL:EFR42028.1}; OS Selenomonas sp. oral taxon 137 str. F0430. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Selenomonas. OX NCBI_TaxID=879310 {ECO:0000313|EMBL:EFR42028.1}; RN [1] {ECO:0000313|EMBL:EFR42028.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0430 {ECO:0000313|EMBL:EFR42028.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFR42028.1}. 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; AENV01000002; EFR42028.1; -; Genomic_DNA. DR RefSeq; WP_009438122.1; NZ_AENV01000002.1. DR EnsemblBacteria; EFR42028; EFR42028; HMPREF9162_1419. DR PATRIC; 45039441; VBISelSp169704_0202. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EFR42028.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EFR42028.1}. SQ SEQUENCE 592 AA; 64707 MW; E9555798552C88A4 CRC64; MAQGRAELRD YLKTAPLIFD GGMGTYYAQK LHTRGKGVEL ANIETPIVVS DIHTEYLRAG AQAIKTNTFA ANRIVYQGDE ELVRRIVTAG WEIAARAAAP FDAYVFADIG PVMGLPHADI IDEYRFLADI FLALGARHFI FETNSSDEGL IETAAHIKQK CPEAFVLNSF SAYPGGYTRD GRFVEDLVRA VAGSGYVDAV GFNCVNGTKQ MKELIRHLGK QILPLSLMPN AGHPVVVDGR TFYESAPDYF GSSLAAIRRE GVSILGGCCG TTPAHIKALC DALAAQGDIM PEEDEETPPQ VALLPKSPFY EALKSGAKPI AVELDPPETG SADKFMAGAR ELMAAGINAI TIADNPIARA RMDAAMLAGR VHRELGIEPI PHMTCRDRNL NAIKSLLLGL SAEGVHNIIT ITGDPIPTAE RDEVKSVYQF NSRKLASFIT SLGSRGDVVP FHIFGALNVN AKFFGTQINL AKKKVEEGMM GFFTQPVLSE RAKENMRAVR ETFPEALILG GIMPVVSERN ARYMESEITG IHVEERIIDM YRGLDRTQAE ELAVRLSLEI ARDIEPYIDG YYIITPFSRT ALVARIVKAL KK // ID E4LRC4_9CLOT Unreviewed; 587 AA. AC E4LRC4; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 04-FEB-2015, entry version 18. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HMPREF9406_0214 {ECO:0000313|EMBL:EFR38659.1}; OS Clostridium sp. HGF2. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=908340 {ECO:0000313|EMBL:EFR38659.1}; RN [1] {ECO:0000313|EMBL:EFR38659.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HGF2 {ECO:0000313|EMBL:EFR38659.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFR38659.1}. 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; AENW01000007; EFR38659.1; -; Genomic_DNA. DR RefSeq; WP_008818813.1; NZ_AENW01000007.1. DR EnsemblBacteria; EFR38659; EFR38659; HMPREF9406_0214. DR PATRIC; 45046058; VBICloSp171430_0990. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EFR38659.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EFR38659.1}. SQ SEQUENCE 587 AA; 66542 MW; F3951C2FB5ACA13A CRC64; MIENYLNTQG YMLFDGAFGT YYAQRYAEDQ KPCEMANLNH PKRVAAIHQE YIEAGADAIK TNTFSANEQH LECSWEMIRR ILQEGYRIAK EAAKDKVKVF ADIGPIMEQK NVSLAQQYQQ IVDVFLAEGA DCFLFETLLN TQELHAVTSY IKEQCPQACI IVSFAVTADG YSRQGIAMSR LLQDCLADEH VDACGLNCVC GPMHMKRLLD SIDRTQKPIL IMPNAGYPTI LANRTYFRDS STYFAKEMRE IWQKGARLLG GCCGTTPVYI QKTREALQEH KIIQKVQQPV QETERIPQED HNPLRRKLQR KQPVIAVEFD PPANCEIERF MNHVEFLKEA GVDAVTIADC PIARARVDSS LIACKLHREL GLDVIPHMTC RDRNINATKA LLFGLQIEGI RNVLVVTGDP IPSEDRQEVK GVFNFNSQIL AGYIRDLNAT MFTSPFMVFG ALNLNAVNFE AELAKAKRKV TQGMEGFLTQ PVHSRQALFN LKRARKELQA YILGGVLPIV SHRNAVYMNN EISGIEVDEE IVAMYEGTTR KEAQKLAVDI SCKTMDEMRP YIDGYYLITP FNRVEIIADM ITYIHKQ // ID E4LRC5_9CLOT Unreviewed; 786 AA. AC E4LRC5; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFR38756.1}; GN ORFNames=HMPREF9406_0215 {ECO:0000313|EMBL:EFR38756.1}; OS Clostridium sp. HGF2. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=908340 {ECO:0000313|EMBL:EFR38756.1}; RN [1] {ECO:0000313|EMBL:EFR38756.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HGF2 {ECO:0000313|EMBL:EFR38756.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFR38756.1}. 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; AENW01000007; EFR38756.1; -; Genomic_DNA. DR RefSeq; WP_008818812.1; NZ_AENW01000007.1. DR EnsemblBacteria; EFR38756; EFR38756; HMPREF9406_0215. DR PATRIC; 45046060; VBICloSp171430_0991. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFR38756.1}; KW Transferase {ECO:0000313|EMBL:EFR38756.1}. SQ SEQUENCE 786 AA; 85411 MW; FE4576F3F7004FE8 CRC64; MEIENKIQFL DGAMGTQLQD KGLPAGASPE LFMMEHGEII EDVHAAYIDS GSDIIYTNTF GANAKKLCKS QYTVEEVITR AVQLAKSAAK RRNGVQVALD IGPIGELLEP NGYLPFEEAY ELYRQQVVAG EQAGADLVIF ETMSDLYEVK AAILAAKEHT QLPVFVTMSF EADHRTFTGC TTASFALCAE GLGADAIGIN CSLGPDQILP IAEELAAMTN LPLIIKANAG LPDPLTNTYS IDAAAYARML LPYTKLPLAY VGGCCGTTPQ FIQELKNTLP TTIAVEKRKR RIGSYACTPT KCLHIQDVHV IGERINPTGN KRMKAALQEH RMDEILAIAM EEVEGGADIL DVNVGLPGID EKEMMVEVIK ELQSVIDLPL QIDSTDPAVI RAALRAVNGV AIVNSVNGEA AVMESILPAV KKYGANVVGL TMDEDGIPAC AQKRLEIGTR IVETAQRYGI AKERVFLDCL TLTVSAQQSG AKETLQALTA IREQLGVHTV LGVSNISFGL PSRILLNQSF LTMAMQAGLS MPIMNPNQAA MMDAVRSYRV LQGIDVDSQE YIRIYAQQKR EGGKPHIESV HINIEESIMR GLKEETRQLC TKLLSEKEPL QIVNEHLIPA LDAVGARYEK KEIYLPQLIN AATASQCAFE EIRRSVQAGG LESISKGKII LATVKGDVHD IGKNIVKVVL ENYGYQVFDL GKDVPVETVV ETAIKEQVRL IGLSALMTTT LKSMEETIQA LHESGHECKI MVGGAVVSAD YAKQIHADYY ARDAKESADI AKEVLG // ID E4MC87_9BACT Unreviewed; 1203 AA. AC E4MC87; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 01-APR-2015, entry version 23. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFR57455.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFR57455.1}; GN Name=metH {ECO:0000313|EMBL:EFR57455.1}; GN ORFNames=HMPREF9720_0144 {ECO:0000313|EMBL:EFR57455.1}; OS Alistipes sp. HGB5. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Rikenellaceae; OC Alistipes. OX NCBI_TaxID=908612 {ECO:0000313|EMBL:EFR57455.1}; RN [1] {ECO:0000313|EMBL:EFR57455.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HGB5 {ECO:0000313|EMBL:EFR57455.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFR57455.1}. 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; AENZ01000051; EFR57455.1; -; Genomic_DNA. DR RefSeq; WP_009597740.1; NZ_AENZ01000051.1. DR EnsemblBacteria; EFR57455; EFR57455; HMPREF9720_0144. DR PATRIC; 52765305; VBIAliSp174513_1774. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFR57455.1}; KW Transferase {ECO:0000313|EMBL:EFR57455.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 243 243 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 753 753 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1203 AA; 131819 MW; 0B79BE12C1FC300D CRC64; MADIYEQLES RILLLDGGFG TMVQQYGLTE EDYRGERFRE WPALLKGCND LLALTRPEAV REIHVKYLQA GADIIETDSF NANAVSLADY GLEAYAYEMS RAAAAVARSA ADEFTARNPQ KPRFVAGSMG PTNRTASMSA DVANPAAREV TFAQLVEAYT DQARGLLDGG ADILLVETIF DTLNAKAALY AIDALAEKLG RTIRVMASGT LADASGRTLS GQTVEAFCTS LSHAQLLSLG LNCAYGAKQL LPYLERLAET APLRISAHPN AGLPNVMGGY DETPEMFAED VGEYMRRGLV NIVGGCCGTT PAHIFELSKI ACNYAPRPVP APRRVTTLSG LEPLRIAPET NFVNVGERTN VAGSAKFARL IREGNYEEAL SVARAQVDAG AQIVDVCMDD GMIDGVEAMR TFLNLMASEP EIARVPTMID SSKWEVLAAG LEVTQGKAVV NSISLKEGEA EFLRRAREIH RYGAAAVVML FDEQGQADTC ERKIEVASRA YRLLTDAGFP AEDIIFDPNI LAVATGIPEH DGYAKAFIDA TRWIKENLPY AKVSGGVSNL SFAFRGNNAV REAMHSAFLY HAIRAGMDMG IVNPQMVKIY SEIEPELLQR VEDVILCRRA DAAERLTEYA QQVRTTAETQ PQAPDAWRAG TLAERIGHAM LKGVADYIEQ DALEGYEALG TPMAVIDTLL MPAMERVGTL FGEGKMFLPQ VVKTARVMKR AVAALTPYIE QGGAQTPHNA GKVLIATVKG DVHDIGKNIV AVVMACNGYE IKDLGVMVES QRIVEEAVAW GADCICLSGL ITPSLDEMAH VCEELERRAL RLPVIIGGAT TSNLHTAVKI APVYSGLVIH SPNASRNSQI LAQLLGPDGQ LYADKVRADQ QALRSDYLRA ERTRNLIPIV EVRKTRKGAA PHLPVEPLHP GRMVFPDFDV ADAEPYIDWS FFFAAWGLKG RYPEILDHPE KGAEARKVFA DAEALLARIR DERLLTLQAA VGIFPARAEG DDIWITDQKG RERRLAMLRN QTRGEENRSL ADCIAPHSDW IGCFAVTAGI GLRELCEKFR AEGDDYGAIM AKLLADRLTE AFAEAVHTFV RRQMWGYETG EPLTPQQTVR GQYRGRRMAF GYPASPDHSL KREVFDLLSV EMTTGMKLTE NYMIDPGEAL CGLMFADADY FSVGTIDTKQ LLDYARRRGM EVEEIKKLIP NNI // ID E4N2M6_KITSK Unreviewed; 1167 AA. AC E4N2M6; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=Putative methionine synthase {ECO:0000313|EMBL:BAJ32410.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:BAJ32410.1}; GN Name=metH {ECO:0000313|EMBL:BAJ32410.1}; GN OrderedLocusNames=KSE_66510 {ECO:0000313|EMBL:BAJ32410.1}; 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 {ECO:0000313|EMBL:BAJ32410.1, ECO:0000313|Proteomes:UP000007076}; RN [1] {ECO:0000313|EMBL:BAJ32410.1, ECO:0000313|Proteomes:UP000007076} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33774 / DSM 43861 / JCM 3304 / KCC A-0304 / NBRC 14216 / RC KM-6054 {ECO:0000313|Proteomes:UP000007076}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP010968; BAJ32410.1; -; Genomic_DNA. DR RefSeq; WP_014139706.1; NC_016109.1. DR RefSeq; YP_004908366.1; NC_016109.1. DR EnsemblBacteria; BAJ32410; BAJ32410; KSE_66510. DR KEGG; ksk:KSE_66510; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; KSET452652:GJFD-6657-MONOMER; -. DR Proteomes; UP000007076; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007076}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAJ32410.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007076}; KW Transferase {ECO:0000313|EMBL:BAJ32410.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 236 236 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 302 302 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 746 746 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1167 AA; 127552 MW; FA4A747645B900F5 CRC64; MATVVPPSAQ QVRADALREA LATRVVVADG AMGTMLQAQD PSMEDFQQLE GCNEVLNVTR PDIVRSVHEA YFGVGVDCVE TNTFGANHWA LGEYEISERI FELSEAGARI AREVADEFTA GDGRTRWVLG SMGPGTKLPT LGHTTFEVVR EGFRQNAAGL IAGGVDALLI ETSQDLLQTK ASVLGCKAAL AEAGVELPIL AQITVETTGT MLLGSETGAA LTALEPLGID FIGLNCATGP EQYSEHLRYL AKNARIGLSA MPNAGLPILT KDGSHYPLSP VELADAQESF VRDYGLALVG GCCGTTPEHL RHLVERVQGR PLTPRDPRPE ASAASLYQSV PFRQDTSYLA IGERTNANGS KKFRESMIAG DWQACVEIAR EQIREGAHLL DLCVDYVGRD GVADMREIAG RLATASTLPI VLDSTEPPVL KAGLEMLGGR AVLNSVNYED GDGPDTRFGK IASLAREHGA GLIALTIDEQ GQARTAEHKV AIAERLIEQL GREYGIEESS ILVDCLAFTL ATGQEESRRD GIETIEAIRE LKRRHPNVQT TLGLSNISFG LNPAARQVVN SVFLHECVEA GLDSAIVHAA KILPMNRIPE DRRQTALDLV YDRRSEGYDP LQKLLQLFEG VSAASSAASR AEELAALPLE ERLQRRIIDG ERNGLEADLD AALLERPALE IINGTLLSGM KTVGELFGSG EMQLPFVLQS AEVMKAAVAH LEPHMEKSDS AGKGTIVLAT VKGDVHDIGK NLVDIILSNN GYNVVNIGIK QPVSAILEAA QEHQADVIGM SGLLVKSTVI MKENLEELNQ RGLAADFPVI LGGAALTRAY VEQDLHEIYQ GEVRYARDAF EGLRLMDALI GVKRGVPGAA LPELRKRRHA RVEVEEPEEV NLGQIRSDVA VDNRVPTPPF WGDRIIKGVP FQDYASWLDE DALFKGQWGL KGGRSGGPSY EELVETEGRP RLRGWLDRLQ TEGWLEPAVV YGYYPANSKG DDLILYREDG SELTRFTFPR QRRGRRLCLA DFFRPEESGE RDVVGLQVVT MGNRISEAAN ELFATDSYRD YLELHGLSVQ LAEALAEFWH ARVRYELGFG DEDPQDVRDM FALKYRGARF SLGYGACPNL EDRAKIAELL KPERVGVVLS EEYQLHPEQS TDAIVLHHPE AKYFNAR // ID E4N857_KITSK Unreviewed; 312 AA. AC E4N857; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 29-APR-2015, entry version 21. DE SubName: Full=Putative homocysteine S-methyltransferase {ECO:0000313|EMBL:BAJ27388.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:BAJ27388.1}; GN Name=mmuM {ECO:0000313|EMBL:BAJ27388.1}; GN OrderedLocusNames=KSE_15610 {ECO:0000313|EMBL:BAJ27388.1}; 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 {ECO:0000313|EMBL:BAJ27388.1, ECO:0000313|Proteomes:UP000007076}; RN [1] {ECO:0000313|EMBL:BAJ27388.1, ECO:0000313|Proteomes:UP000007076} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33774 / DSM 43861 / JCM 3304 / KCC A-0304 / NBRC 14216 / RC KM-6054 {ECO:0000313|Proteomes:UP000007076}; 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 ----------------------------------------------------------------------- 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; BAJ27388.1; -; Genomic_DNA. DR RefSeq; WP_014134706.1; NC_016109.1. DR RefSeq; YP_004903344.1; NC_016109.1. DR EnsemblBacteria; BAJ27388; BAJ27388; KSE_15610. DR KEGG; ksk:KSE_15610; -. DR KO; K00547; -. DR OMA; PYVDVWL; -. DR BioCyc; KSET452652:GJFD-1547-MONOMER; -. DR Proteomes; UP000007076; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007076}; KW Methyltransferase {ECO:0000313|EMBL:BAJ27388.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007076}; KW Transferase {ECO:0000313|EMBL:BAJ27388.1}. SQ SEQUENCE 312 AA; 31568 MW; A49EB6E38665F591 CRC64; MTDFGASPSG AALVAAMADG PVLLDGGLSN RLAEQGCDLS DGLWSARLLL DEPGQLLAAH RAYFAAGAQV ATTASYQASR AGFAARGVDA AKTDRLLALS VEVARLAAEE VSAELGDGRP RWVAASVGPY GAVLADGSEY RGHYGLSAAE LAEFHRPRLE ALAAAGPDVL AVETVPDLLE AAVLADCVRG LGVPVWFSFG AADGLTRGGE PLSEVFALVA EVPETIAVGV NCCAPREVDA AVALAAEVTG LPAVAYPNSG EGWDAAARDW TGEAAFDPAL AADWVAAGAR LVGGCCRVGT DGIARLAAAL RA // ID E4PKP3_MARAH Unreviewed; 301 AA. AC E4PKP3; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:ADP98519.1}; GN OrderedLocusNames=HP15_2755 {ECO:0000313|EMBL:ADP98519.1}; OS Marinobacter adhaerens (strain HP15). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Marinobacter. OX NCBI_TaxID=225937 {ECO:0000313|EMBL:ADP98519.1, ECO:0000313|Proteomes:UP000007077}; RN [1] {ECO:0000313|Proteomes:UP000007077} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HP15 {ECO:0000313|Proteomes:UP000007077}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; ADP98519.1; -; Genomic_DNA. DR RefSeq; WP_014578018.1; NC_017506.1. DR RefSeq; YP_005886447.1; NC_017506.1. DR PRIDE; E4PKP3; -. DR EnsemblBacteria; ADP98519; ADP98519; HP15_2755. DR KEGG; mad:HP15_2755; -. DR PATRIC; 43117776; VBIMarBac104501_2783. DR OMA; QPEVMAA; -. DR BioCyc; MADH225937:GLG5-2811-MONOMER; -. DR Proteomes; UP000007077; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007077}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ADP98519.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007077}; KW Transferase {ECO:0000313|EMBL:ADP98519.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 200 200 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 271 271 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 272 272 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 301 AA; 32077 MW; EE3A9195CDFEE452 CRC64; MKSVALLDGG LGQEIYRRAM NVTSLLWSVA VMREQPDVVT EVHADFIRAG ARTLTLNTYA ATPTRLAREG LGDEIGTIHQ RAFEVLERAI ALTGADVDIA GCLPPLVGSY RSQPDRTFED LKSEFDILVK LQSGADVFLI ETMTNSLEAK AACAAASESG KPFGVAFRLE ADGKLRSGET LAEAVEAVRA SGPTAIMLNC CDPEVISQAM PELAGLYPCT GGYANAFKTV EPMAGGALVD ELEARQDVSP GVYGLQVKQW LDDGAGVVGG CCEITPEHIS HLADVLTGEY NLIRFSELPR G // ID E4PNR2_MARAH Unreviewed; 1232 AA. AC E4PNR2; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAY-2015, entry version 31. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:ADP97556.1}; GN OrderedLocusNames=HP15_1792 {ECO:0000313|EMBL:ADP97556.1}; OS Marinobacter adhaerens (strain HP15). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Marinobacter. OX NCBI_TaxID=225937 {ECO:0000313|EMBL:ADP97556.1, ECO:0000313|Proteomes:UP000007077}; RN [1] {ECO:0000313|Proteomes:UP000007077} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HP15 {ECO:0000313|Proteomes:UP000007077}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001978; ADP97556.1; -; Genomic_DNA. DR RefSeq; WP_014577161.1; NC_017506.1. DR RefSeq; YP_005885484.1; NC_017506.1. DR EnsemblBacteria; ADP97556; ADP97556; HP15_1792. DR KEGG; mad:HP15_1792; -. DR PATRIC; 43115785; VBIMarBac104501_1801. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; MADH225937:GLG5-1835-MONOMER; -. DR Proteomes; UP000007077; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007077}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007077}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1232 AA; 136873 MW; 40D9171EFA40A5D3 CRC64; MTDRTTRLDQ LHKALQERIV ILDGGMGTMI QNLKLDEKAF RGDRFADYER EVQGNNDLLN LTQPALLRNI HADYLDAGAD IIETNTFNST QLSQADYGLE AIARELNVAA AELARQIADE YTAKNPEKPR FVAGAVGPTS RTASISPDVN NPGYRNVDFQ TLVDNYYEAV GGLVEGGCDL ILIETIFDTL NAKAAIYATQ QYFEDSGITL PIMISGTITD ASGRTLSGQT TEAFWNSVAH AKPISVGLNC ALGADALRPY VEELSAKAET YVSAHPNAGL PNEFGEYDQT PEEMAEIIEG FARDGFLNII GGCCGSRPDH IEAIAQAVSK YPPRKIPERP KALRLSGLEP FTGDDNVLFI NVGERTNVTG SKRFLRLIKE EQYEEALSVA RDQVENGAQI IDINMDEGML ESKEVMVTFL NLVASEPDIS RVPIMIDSSK WDVIEAGLRC IQGKAVVNSI SLKEGEEEFV KRARDCMRYG AAVVVMAFDE QGQADTYERK TEICKRSYDV LTGIGFNPAD IIFDPNIFAI ATGIEEHNNY AVDFINATRW IRENLPHASI SGGVSNVSFS FRGNDVVREA IHSVFLYHAI KAGMNMGIVN PGQLVIYDEI DPELKELVED VVLNRRDDST DRLLEIAERY KGKGGKTQEE DLAWREWPVE KRLEHALVKG ITTYIVDDTE ACRQRATHPI EVIEGPLMDG MNVVGDLFGD GKMFLPQVVK SARVMKQAVA HLIPYIEAEK TEDQKAKGKI LMATVKGDVH DIGKNIVGVV LQCNNYEVID LGVMVPCDKI LAAAKEHDVD LIGLSGLITP SLDEMVHVAR EMQRLDFNIP LMIGGATTSK AHTAVKIEPQ YKNDIALYVS DASRCVNVAS QLLSKNAKPE FVEAARTEYD EIRERRKNRG DRTKLVSLKE ARDRAPDISF EGYQPPKPAF TGIRVFEEYD LNELVDYIDW TPFFMSWDIS GKYPAIFDDP KRGEAARHLF DDAQKILHRM IDEKRVSARG VIGFWPANRR GDDVVLYTDE SCTEELTTLH HLRQQDEKAP GKPMMALSDF VAPEGSGTVD YVGGFAVTTG IGAEEFSVEF KDANDDYNAI MVKALADRLA EAFAERMHER VRQEFWGYAA DEKLANDDLI KERYRGIRPA PGYPACPDHT EKATLFSLLE ATDTAGIELT EHFAMFPTAA VSGWYFAHPE SKYFAVGKIG ADQVEDYAER KGISKAEAER WLAPSLAYDP AE // ID E4Q2R7_CALOW Unreviewed; 413 AA. AC E4Q2R7; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 29-APR-2015, entry version 28. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADQ03821.1}; GN OrderedLocusNames=Calow_0216 {ECO:0000313|EMBL:ADQ03821.1}; 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 {ECO:0000313|EMBL:ADQ03821.1, ECO:0000313|Proteomes:UP000006889}; 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] {ECO:0000313|EMBL:ADQ03821.1, ECO:0000313|Proteomes:UP000006889} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700167 / DSM 13100 / OL RC {ECO:0000313|Proteomes:UP000006889}; 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 owensenis, and RT Caldicellulosiruptor lactoaceticus."; RL J. Bacteriol. 193:1483-1484(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; CP002216; ADQ03821.1; -; Genomic_DNA. DR RefSeq; WP_013411235.1; NC_014657.1. DR RefSeq; YP_004001621.1; NC_014657.1. DR EnsemblBacteria; ADQ03821; ADQ03821; Calow_0216. DR KEGG; cow:Calow_0216; -. DR PATRIC; 42589500; VBICalOwe108203_0237. DR HOGENOM; HOG000269747; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR BioCyc; COWE632518:GHVV-217-MONOMER; -. DR Proteomes; UP000006889; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006889}; KW Methyltransferase {ECO:0000313|EMBL:ADQ03821.1}; KW Transferase {ECO:0000313|EMBL:ADQ03821.1}. SQ SEQUENCE 413 AA; 46099 MW; D0BFA9552366D012 CRC64; MALLKDELYR RVLIFDGAMG TQLIRNGLRE DECPDLWSVT RQDVVSSIHR QYFEAGSDCV ETNTFGANRE KLKKYGLENE VENINKWAVR LAKEVSKEYG GYVGLSVGPT GRLFLPSGDL SFDEAERIFY EQILSGIQAG ADFVSIETMS DIKEAKAAFF AYKKAKEVLK KDIPCLVSFT FEQNKRLLMG TPPEVAAYYF SLIGCDIVGA NCSGGAMQLL EVIKQMQGFS CVPLSVKPNA GLPKVVDGKT VYESCIPEFV NLADEFVQNG VRLYGGCCGT TPEYISAISK VLKGKEVSFK SGIQNKFITS IYSLLDISQK FSFYEYKLTN DFSSEAVFEL AGLEEDAIFV DIDENVEPEV LKEFLIESQD FSKKPYVFNI KTKSHVEIIE RYYFGVYGAV SSIHGKSAVK VQI // ID E4Q2R8_CALOW Unreviewed; 605 AA. AC E4Q2R8; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAY-2015, entry version 28. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=Calow_0217 {ECO:0000313|EMBL:ADQ03822.1}; 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 {ECO:0000313|EMBL:ADQ03822.1, ECO:0000313|Proteomes:UP000006889}; 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] {ECO:0000313|EMBL:ADQ03822.1, ECO:0000313|Proteomes:UP000006889} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700167 / DSM 13100 / OL RC {ECO:0000313|Proteomes:UP000006889}; 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 owensenis, and RT Caldicellulosiruptor lactoaceticus."; RL J. Bacteriol. 193:1483-1484(2011). CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ADQ03822.1; -; Genomic_DNA. DR RefSeq; WP_013411236.1; NC_014657.1. DR RefSeq; YP_004001622.1; NC_014657.1. DR EnsemblBacteria; ADQ03822; ADQ03822; Calow_0217. DR KEGG; cow:Calow_0217; -. DR PATRIC; 42589502; VBICalOwe108203_0238. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR BioCyc; COWE632518:GHVV-218-MONOMER; -. DR Proteomes; UP000006889; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006889}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ADQ03822.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:ADQ03822.1}. SQ SEQUENCE 605 AA; 67500 MW; 0288C0A394FA657A CRC64; MKKSFREFLK EQSIIIFDGA MGTELLNRGF SVDFPLEWAN IANPELVKQI YRDYILAGAQ CIETNTFGAN ECKLKIFGFE NEVERINRSA VRIAKEMADD KVFVIGSVGP LGKPVGSGFE IDATRAKEAY KRQLYFLLDE GVDAIIFETA ASTHEVQIAI EALKELNDKI PYIIQFSFTR ELTTIYGEDI YRVIEFLKFT DADVVGLNCG NGPQKTLEAL KIFSQHLKGP FSVQPNAGYP QMIQGRPVFS TPAEYFAWFA PEYVKLGAKI VGGCCGTTPE HIKAIKDKVK EFLHGIEVEV VEREEKQEAV LKDTPSEFSQ KLGKKFIFTV EISPPKGIEL EKTKEGVKLL KEAGADTVNI ADSPMARVRI SPIALAHILK EELGMESILH FTCRDRNLIS LQSELLGAAA LGVKNVLALT GDPPSIGDHP QAKPVFDVNS EGLVLILSRL NSGTDYMGNP IGKATNFTIG VALNLNADDL EKEIERLKRK IENGAHFIET QPIYDAETLE RFLEKVDFAL PPILGGILPL RSSRHAEFLH NEVPGITIPD KIRERMRSSK EPAKEGVEIA CEIVEKIKHM VSGIYIMPPF EKYEMAVEII KNFKY // ID E4Q8M7_CALH1 Unreviewed; 605 AA. AC E4Q8M7; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 29-APR-2015, entry version 28. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=Calhy_2297 {ECO:0000313|EMBL:ADQ08001.1}; 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 {ECO:0000313|EMBL:ADQ08001.1, ECO:0000313|Proteomes:UP000006890}; 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] {ECO:0000313|EMBL:ADQ08001.1, ECO:0000313|Proteomes:UP000006890} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18901 / VKM B-2411 / 108 RC {ECO:0000313|Proteomes:UP000006890}; 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 owensenis, and RT Caldicellulosiruptor lactoaceticus."; RL J. Bacteriol. 193:1483-1484(2011). CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ADQ08001.1; -; Genomic_DNA. DR RefSeq; WP_013404143.1; NC_014652.1. DR RefSeq; YP_003993370.1; NC_014652.1. DR EnsemblBacteria; ADQ08001; ADQ08001; Calhy_2297. DR KEGG; chd:Calhy_2297; -. DR PATRIC; 42588313; VBICalHyd101559_2406. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR BioCyc; CHYD632292:GHA8-2359-MONOMER; -. DR Proteomes; UP000006890; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006890}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ADQ08001.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:ADQ08001.1}. SQ SEQUENCE 605 AA; 67184 MW; A3310558291A2D43 CRC64; MKKSFREFLK EQSTVIFDGA MGTELLNRGF SLDFPLEWAN VTRPELVKQI HTDYILAGAS SIETNTFGAN ECKLKVFGFE NEVERINRSA VRIAKEAAEN KVYVIGSVGP LGKPVGSGFE IDARRAKEVY KRQLYFLLDE GVDAIIFETA ASTHEVQIAI EALKELNDKI PYIIQFSFTK DLSTIYGEDI YRVIEFLKST DADVVGLNCG NGPQKTLEAL KIFSQHLKGP FSVQPNAGYP QLVQGRLIFS TSAKYFASFV PEYIKLGAKV VGGCCGTTPE HIKAIKEKVK EFSPSIEVEV SERKEEQKAV LKDTPSELSQ KLGKKFIFTV EISPPKGIEL EKTKEGVKLL KEAGADTVNI ADSPMARVRI SPIALAHILK EELGMESILH FTCRDRNLIS LQSELLGAAA LGVKNVLALT GDPPSIGDHP QAKPVFDVNS EGLVLILSRL NNGTDYMGNP IGKATNFTIG VALNLNADDL GKEIEKLKHK IENGAHFIET QPIYDAETLE RFLEKVDFTL PPILGGILPL RSSRHAEFLH NEVPGITIPD KIRERMRSSK EPAKEGVEIA CEIVDRIKHM VSGIYIMPPF EKYEMAVEII RNFRY // ID E4Q8M8_CALH1 Unreviewed; 413 AA. AC E4Q8M8; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAY-2015, entry version 30. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADQ08002.1}; GN OrderedLocusNames=Calhy_2298 {ECO:0000313|EMBL:ADQ08002.1}; 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 {ECO:0000313|EMBL:ADQ08002.1, ECO:0000313|Proteomes:UP000006890}; 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] {ECO:0000313|EMBL:ADQ08002.1, ECO:0000313|Proteomes:UP000006890} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18901 / VKM B-2411 / 108 RC {ECO:0000313|Proteomes:UP000006890}; 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 owensenis, and RT Caldicellulosiruptor lactoaceticus."; RL J. Bacteriol. 193:1483-1484(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; CP002219; ADQ08002.1; -; Genomic_DNA. DR RefSeq; WP_013404144.1; NC_014652.1. DR RefSeq; YP_003993371.1; NC_014652.1. DR EnsemblBacteria; ADQ08002; ADQ08002; Calhy_2298. DR KEGG; chd:Calhy_2298; -. DR PATRIC; 42588315; VBICalHyd101559_2407. DR HOGENOM; HOG000269747; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR BioCyc; CHYD632292:GHA8-2360-MONOMER; -. DR Proteomes; UP000006890; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006890}; KW Methyltransferase {ECO:0000313|EMBL:ADQ08002.1}; KW Transferase {ECO:0000313|EMBL:ADQ08002.1}. SQ SEQUENCE 413 AA; 46095 MW; 30CF2662A6942D02 CRC64; MALLKDELYR RVLIFDGAMG TQLIQNGLTE DECPDLWSVS RQDVVSSIHK QYFEAGSDCV ETNTFGANRE KLKKYGLENE VENINKWAVK LAKEVAKEYS GYVGLSVGPT GRLFIPSGDL SFDEAERIFY EQILSGIQAG ADFVSIETMS DIKEAKAAFF AYKKAKEELN KDIPCLVSFT FEQNKRLLMG TPPEVAAYYF SLIGCDIVGA NCSGGAMHLL EVIKQMQGFS FVPLSVKPNA GLPKVLDGKT VYESCIPEFV NLADEFVENG VRLYGGCCGT NPEYIRAISK VLKGKEVSFE SSIQKKFITS IYSLLDISQK FSVYEFKLTN DFSAEAVFEL AGLEEDAIFV DIDENVEPEV LKEFLIESQD FSKKPYIFNI ETKSHIDVIE RYYFGVYGAV SSMHGKSAVK VLI // ID E4RIR2_HALHG Unreviewed; 793 AA. AC E4RIR2; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 01-APR-2015, entry version 26. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADQ15132.1}; GN OrderedLocusNames=Halsa_1709 {ECO:0000313|EMBL:ADQ15132.1}; OS Halanaerobium hydrogeniformans (Halanaerobium sp. (strain OS sapolanicus)). OC Bacteria; Firmicutes; Clostridia; Halanaerobiales; Halanaerobiaceae; OC Halanaerobium. OX NCBI_TaxID=656519 {ECO:0000313|EMBL:ADQ15132.1, ECO:0000313|Proteomes:UP000007434}; RN [1] {ECO:0000313|EMBL:ADQ15132.1, ECO:0000313|Proteomes:UP000007434} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=sapolanicus {ECO:0000313|Proteomes:UP000007434}; 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 ----------------------------------------------------------------------- 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; ADQ15132.1; -; Genomic_DNA. DR RefSeq; WP_013406209.1; NC_014654.1. DR RefSeq; YP_003995486.1; NC_014654.1. DR EnsemblBacteria; ADQ15132; ADQ15132; Halsa_1709. DR KEGG; has:Halsa_1709; -. DR PATRIC; 42642133; VBIHalSp157090_1781. DR KO; K00548; -. DR BioCyc; HHYD656519:GHYV-1750-MONOMER; -. DR Proteomes; UP000007434; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007434}; KW Methyltransferase {ECO:0000313|EMBL:ADQ15132.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007434}; KW Transferase {ECO:0000313|EMBL:ADQ15132.1}. SQ SEQUENCE 793 AA; 86745 MW; AE749022F10D69A3 CRC64; MELENRLGKK VMLFDGAMGT VLQQRGLKAG SVPEILNIGK KEVIIDIHKS YLKAGSEIIT TNTFGANKLK MSEIDYTVEE IISAAVENAK RAVIESSKDA LVALGLGPLG ELLEPMGSLT FDEAYSLYQQ QILQGVKSGV DIIHIETIAD LCEAKAAVLA AKENSNLPVF CTLTFEEDGR TFTGGNIHST ISVLEGLGVD ALGLNCSLGP EKLESLAEEV LKYSNTPVIL QANAGLPVVE EGKTVFKLSP EEYYKPIARL YEKGLAVVGG CCGTNEDFIA LIADFLKDKA VKKSNNEEIS IACTPSKWKD LKKINVVGER INPTGKNEFK KALRNKDLDY ITRVAIEQVE AGADILDVNL GLPEINEEEM MVKVIKELQA ILDIPLQIDS SDENVIAKAL RYYNGTAVVN SINGETEVLE KTLPLIKKYG AAVIALTMDE DGIPETAEGR FEIAKRIVNK AEEYGIKREK IIVDCLTLTA SAQQKGVKET LKALKMVKEK LNVNTTLGVS NVSFGLPARA VLNRNFLTLA LYQGLNLAII DPNDSEMMAN IKAFKVLANL DKGAVEYIEF MANVDQEEIK KENSAIETME LEEIIVKGIK KEAAKLTKKL LAEKDALEIV NNHLIPALDI VGERYEEGKI FLPQLVQSAE TVKEAFAVLK AEMAKNGDED ISRGEIVLAT VKGDVHDIGK NIVKTVLENY GYKIIDLGRN VSENEVKKVV KDNNIKLLGL SALMTTTVKN MEKTIQIVKE ENPDCLIMVG GAVLTPDYAE MINADYYAKD AKDAVEIAKK IFG // ID E4RR14_LEAB4 Unreviewed; 1238 AA. AC E4RR14; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAY-2015, entry version 32. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ADQ16609.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADQ16609.1}; GN OrderedLocusNames=Lbys_0863 {ECO:0000313|EMBL:ADQ16609.1}; OS Leadbetterella byssophila (strain DSM 17132 / KACC 11308 / 4M15). OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae; OC Leadbetterella. OX NCBI_TaxID=649349 {ECO:0000313|EMBL:ADQ16609.1, ECO:0000313|Proteomes:UP000007435}; 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] {ECO:0000313|EMBL:ADQ16609.1, ECO:0000313|Proteomes:UP000007435} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17132 / KACC 11308 / 4M15 RC {ECO:0000313|Proteomes:UP000007435}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002305; ADQ16609.1; -; Genomic_DNA. DR RefSeq; WP_013407660.1; NC_014655.1. DR RefSeq; YP_003996962.1; NC_014655.1. DR EnsemblBacteria; ADQ16609; ADQ16609; Lbys_0863. DR KEGG; lby:Lbys_0863; -. DR PATRIC; 42651655; VBILeaBys116579_0891. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; LBYS649349:GHFA-876-MONOMER; -. DR Proteomes; UP000007435; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007435}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADQ16609.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007435}; KW Transferase {ECO:0000313|EMBL:ADQ16609.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 246 246 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1238 AA; 137980 MW; CE422904E48F24DA CRC64; MTRLRQALRD RILVLDGAMG TMIQRYKLSD ADYRGERFKD FPHDVKGNND LLSITRPDVI LAIHKEYLDA GADIIETNTF SGTWVAQDDY HMADLVYEIN YEGAKIARQA ADAYSTPEKP RFVVGSMGPT TKMASLSPDV NNPGFRAITF DQLVDAFSTQ IRALIEGGVD ALLIETVTDT LNCKAALYAA KSIIEEKKAV DPDFDRPLMV SGTITDQSGR TLTGQTSEAF YNSVSHAGLL SIGLNCALGA KAMKPYLAEL SRVANCYVSV YPNAGLPNEM GQYDETPAYM AEQVREFLEE GYVNILGGCC GTTPEHIRAF AELAKNYKPR VPSEPEPLLR LSGLEPLTLT PELGFVNVGE RTNVTGSKKF LRLIKSRKFD EALSVAQDQV EGGANVIDVN MDEGMLDGVE AMTTFLNLMA AEPEISRIPV MIDSSKWEII EAGLKCIQGK GIVNSISLKA GEEEFKRQAS TILKYGAAVV VMAFDEQGQA DTTERRIEIS KRSYDILVNQ LGFPPQDIIF DLNIFPVATG IEEHRINALS FFEATKWVRE NLPLVHVSGG VSNVSFSFRG NDRVREAIHS AFLYHGRKAG MDMGIVNPSM LEVYDDIPAD LLKAVEDVLL NRTDDATEVL LELAESLKGE GKAEDKAIQE WRTLPVNKRI EHALVKGIVE FIDEDIEEIR HQYPTPLQVI EGPLMDGMNV VGDLFGSGKM FLPQVVKSAR VMKKAVAYLL PYLEEEKLKS GNTQQNNGKV LMATVKGDVH DIGKNIVGVV LACNNYEIID LGVMVPAEKI LEEAQKHQVD AIGLSGLITP SLDEMVYVAK EMQKRDMTDM PLLIGGATTS RAHTAVKIDP VFNGPVIHVL DASKSVPVVS NLLSKDLRED FVKKTKADYA LFRDDYQKRQ GIKHYISLEE ARKNKLPLDW NNYEIKVPSL RGTKTYRNYS LREISQYIDW TPFFQSWDLH GHYPRILEDE KVGSTAQKLF ADAQVMLQQI IENRSFDARA VVGFYPTNTQ DHDVQVVYGW KEGNCDCHTH VDKETVLATL PQLRQQGKKG AGIPNLSLAD FIAPVESGKI DYFGTFAVGI FGAEDLAKKY EVSFDDYNAI MVKVLADRFA EAFTELLHEK VRKELWGYQH QESLTNEDLI KEKYVGIRPA PGYPACPDHL AKKEIFNLLD VENQIGLHLT ESLAMWPASA VSGFYYSHPD AKYFGLGKIE KDQLEFYVKA KGISLEEAEK WLSPVLNF // ID E4S7K3_CALKI Unreviewed; 411 AA. AC E4S7K3; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAY-2015, entry version 30. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADQ39848.1}; GN OrderedLocusNames=Calkr_0284 {ECO:0000313|EMBL:ADQ39848.1}; 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 {ECO:0000313|EMBL:ADQ39848.1, ECO:0000313|Proteomes:UP000009256}; 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] {ECO:0000313|EMBL:ADQ39848.1, ECO:0000313|Proteomes:UP000009256} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700853 / DSM 12137 / I77R1B RC {ECO:0000313|Proteomes:UP000009256}; 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 owensenis, and RT Caldicellulosiruptor lactoaceticus."; RL J. Bacteriol. 193:1483-1484(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; CP002326; ADQ39848.1; -; Genomic_DNA. DR RefSeq; WP_013431696.1; NC_014721.1. DR RefSeq; YP_004025461.1; NC_014721.1. DR EnsemblBacteria; ADQ39848; ADQ39848; Calkr_0284. DR KEGG; cki:Calkr_0284; -. DR HOGENOM; HOG000269747; -. DR KO; K00548; -. DR BioCyc; CKRI632335:GI3P-289-MONOMER; -. DR Proteomes; UP000009256; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009256}; KW Methyltransferase {ECO:0000313|EMBL:ADQ39848.1}; KW Transferase {ECO:0000313|EMBL:ADQ39848.1}. SQ SEQUENCE 411 AA; 45763 MW; 07CE8AEDBC2B4AA1 CRC64; MLKDELYRRV LIFDGAMGTQ LIQNGLKEDE CPDLWSVTRQ DVVASIHRQY FEAGSDCVET NTFGANREKL KKYGLENEVE NINKCAVKLA KEVAKEYSGY VGLSVGPTGR LFTPSGDLSF DEAERIFYEQ ILSGIQAGAD FVSIETMSDI KEAKAAFFAY KKAKEEAKRD IPCLVSLTFE QNKRLLMGTP PEVAAYYFSV IGCDIVGANC SGGAMQLLEV IKQMQGFSFV PLSVKPNAGL PKVVDGKTVY ESCIPEFVNL ADEFVESGVR LYGGCCGTNP EYIRAISKVL KGKEALFESS TQKRFITSIY SLLDISQKFS VYEFKLTNDF SAEAVFELAG LEEDAIFVDI DENVEPELLK EFLIESQDFS KKPYVFNIKT KSHADVIERY YFGVYGVVGN IHGKSAVKVQ I // ID E4S7K4_CALKI Unreviewed; 604 AA. AC E4S7K4; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAY-2015, entry version 33. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=Calkr_0285 {ECO:0000313|EMBL:ADQ39849.1}; 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 {ECO:0000313|EMBL:ADQ39849.1, ECO:0000313|Proteomes:UP000009256}; 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] {ECO:0000313|EMBL:ADQ39849.1, ECO:0000313|Proteomes:UP000009256} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700853 / DSM 12137 / I77R1B RC {ECO:0000313|Proteomes:UP000009256}; 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 owensenis, and RT Caldicellulosiruptor lactoaceticus."; RL J. Bacteriol. 193:1483-1484(2011). CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ADQ39849.1; -; Genomic_DNA. DR RefSeq; WP_013431697.1; NC_014721.1. DR RefSeq; YP_004025462.1; NC_014721.1. DR EnsemblBacteria; ADQ39849; ADQ39849; Calkr_0285. DR KEGG; cki:Calkr_0285; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR BioCyc; CKRI632335:GI3P-290-MONOMER; -. DR Proteomes; UP000009256; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009256}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ADQ39849.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:ADQ39849.1}. SQ SEQUENCE 604 AA; 67087 MW; 39C2F6A5BE75BC3F CRC64; MKKNFREFLK EQSTVIFDGA MGTELLNRGF SLDFPLEWAN VTRPELVKQI HTDYILAGAS SIETNTFGAN ECKLKVFGFE NEVERINRSA VRIAKETADD KVYVIGSVGP LGKPVGSGFE IDDRRAKEVY KRQLYFLLDE GVDAIIFETA ASTHEVQIAI EALKDLNDEI PYIIQFSFTK DLSTIYGEDI YRVIEFLKST DADVVGLNCG NGPQKTLEAL KIFSQNLKGP FSVQPNAGYP QLVQGRLVYS TSAKYFASFV PEYIKLGAKV VGGGCGTTPE HIKAIKEKVK EFLPSIEVEV VERKEEQKAV LKDTPSELSQ KLGKKFIFTV EISPPKGIEL EKTKEGVKLL KEAGADTVNI ADSPMARVRI SPIALAHILK EELGMESILH FTCRDRNLIS LQSELLGAAA LGVKNVLALT GDPPSIGDHP QAKPVFDVNS EGLVLILSRL NNGTDYMGNP IGKATNFTIG VALNLNADDL GKEIEKLKHK IENGAHFIET QPIYEPETLE RFFEKVDFKL PPILGGILPL RSSRHAEFLH NEVPGITIPD KIRERMRSSK EPAKEGVEIA CEIVEKIKHM VSGIYIMPPF EKYEMAAEII KMFK // ID E4SH95_CALK2 Unreviewed; 605 AA. AC E4SH95; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAY-2015, entry version 30. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=Calkro_2295 {ECO:0000313|EMBL:ADQ47120.1}; 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 {ECO:0000313|EMBL:ADQ47120.1, ECO:0000313|Proteomes:UP000006835}; 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] {ECO:0000313|EMBL:ADQ47120.1, ECO:0000313|Proteomes:UP000006835} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18902 / VKM B-2412 / 2002 RC {ECO:0000313|Proteomes:UP000006835}; 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 owensenis, and RT Caldicellulosiruptor lactoaceticus."; RL J. Bacteriol. 193:1483-1484(2011). CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ADQ47120.1; -; Genomic_DNA. DR RefSeq; WP_013431191.1; NC_014720.1. DR RefSeq; YP_004024939.1; NC_014720.1. DR EnsemblBacteria; ADQ47120; ADQ47120; Calkro_2295. DR KEGG; ckn:Calkro_2295; -. DR PATRIC; 42811681; VBICalKro6863_2416. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR BioCyc; CKRO632348:GI5C-2353-MONOMER; -. DR Proteomes; UP000006835; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006835}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ADQ47120.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:ADQ47120.1}. SQ SEQUENCE 605 AA; 67151 MW; 3C59881EED74D98E CRC64; MKKNFREFLK EQAIVIFDGA MGTQLLLRGF SVDFPLEWAN VANPELVKQI HTDYILAGAT CVETNTFGAN ECKLKVFGFE NEVERINRSA VRIAKEVAEN KVYVIGSVGP LGKPVGNGFE IDDKKAKDVY KRQLYFLLDE GVDAIIFETA ASTHEVQIAI EALKELNDEI PYIIQFSFTK ELSTVYGEDI YRVIEFLKYT DADVVGLNCG NGPQKTLEAL KIFSQHLKGP FSVQPNAGYP QLIQGRPVFS TSANYFASFV PEYLKLGAKI VGGCCGTGPE HIKAVKEKIK EVSPSLEIEV VERKEEQKAV LKDTPSELSQ KLGKKFIFTV EISPPKGIEL EKTKEGVKLL KEAGADTVNI ADSPMARVRI SPIALAHILK EELGMESILH FTCRDRNLIS LQSELLGAAA LGVKNVLALT GDPPSIGDHP QAKPVFDVNS EGLVLILSRL NNGTDYMGNP IGKATNFTIG VALNLNADDL GKEIEKLKHK IENGAHFIET QPIYEPETLE KFFEKVDFKL PPILGGILPL RSPRHAEFLH NEVPGITIPD KIRERMRSSK EPAKEGVEIA CEIVEKIKHM VSGIYIMPPF EKYEMAVEII RNFKI // ID E4SH96_CALK2 Unreviewed; 413 AA. AC E4SH96; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAY-2015, entry version 30. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADQ47121.1}; GN OrderedLocusNames=Calkro_2296 {ECO:0000313|EMBL:ADQ47121.1}; 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 {ECO:0000313|EMBL:ADQ47121.1, ECO:0000313|Proteomes:UP000006835}; 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] {ECO:0000313|EMBL:ADQ47121.1, ECO:0000313|Proteomes:UP000006835} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18902 / VKM B-2412 / 2002 RC {ECO:0000313|Proteomes:UP000006835}; 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 owensenis, and RT Caldicellulosiruptor lactoaceticus."; RL J. Bacteriol. 193:1483-1484(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; CP002330; ADQ47121.1; -; Genomic_DNA. DR RefSeq; WP_013431192.1; NC_014720.1. DR RefSeq; YP_004024940.1; NC_014720.1. DR EnsemblBacteria; ADQ47121; ADQ47121; Calkro_2296. DR KEGG; ckn:Calkro_2296; -. DR PATRIC; 42811683; VBICalKro6863_2417. DR HOGENOM; HOG000269747; -. DR KO; K00548; -. DR BioCyc; CKRO632348:GI5C-2354-MONOMER; -. DR Proteomes; UP000006835; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006835}; KW Methyltransferase {ECO:0000313|EMBL:ADQ47121.1}; KW Transferase {ECO:0000313|EMBL:ADQ47121.1}. SQ SEQUENCE 413 AA; 46023 MW; 8C67FD640CC006D9 CRC64; MALLKDELYR RVLIFDGAMG TQLIQNGLTE DECPDLWSVT RQDVVSSIHR QYFEAGSDCV ETNTFGANRE KLKKYGLENE VENINKCAVK LAKEVAKEYN GYVGLSVGPT GRLFIPSGDL SFDEAESIFY EQILSGIEAG ADFVSIETMS DIKEAKAAFY AFKKAKEDLN IDIPCLVSLT FEQNKRLLMG TPPEVAAYYF SSIGCDIVGA NCSGGAIQLL EIIKQMQVFS FVPLSVKPNA GLPKVIDGKT VYESCIPEFV NLADEFVENG VRLYGGCCGT NPEYIRSISK VLKGKEVSFE SSTQKKFITS IYSLLDISQK FSVYEFKLTN DFLSEAVFEL AGLEEDVIFV DIDENIEPEL LKEFLIESQD FSKKPYIFNI ETKSHVDVIE RYYFGVYGAV SSIHGKSAVN VQI // ID E4SIL4_LACAR Unreviewed; 331 AA. AC E4SIL4; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:ADQ59013.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ADQ59013.1}; GN Name=mmuM {ECO:0000313|EMBL:ADQ59013.1}; GN OrderedLocusNames=LA2_05260 {ECO:0000313|EMBL:ADQ59013.1}; OS Lactobacillus amylovorus (strain GRL 1112). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=695560 {ECO:0000313|EMBL:ADQ59013.1, ECO:0000313|Proteomes:UP000007033}; RN [1] {ECO:0000313|EMBL:ADQ59013.1, ECO:0000313|Proteomes:UP000007033} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GRL 1112 {ECO:0000313|EMBL:ADQ59013.1, RC ECO:0000313|Proteomes:UP000007033}; RX PubMed=21131492; DOI=10.1128/JB.01365-10; RA Kant R., Paulin L., Alatalo E., de Vos W.M., Palva A.; RT "Genome sequence of Lactobacillus amylovorus GRL1112."; RL J. Bacteriol. 193:789-790(2011). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002338; ADQ59013.1; -; Genomic_DNA. DR RefSeq; WP_013437811.1; NC_014724.1. DR RefSeq; YP_004031808.1; NC_014724.1. DR EnsemblBacteria; ADQ59013; ADQ59013; LA2_05260. DR KEGG; lam:LA2_05260; -. DR PATRIC; 43077114; VBILacAmy150400_1049. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; SEWCKDG; -. DR BioCyc; LAMY695560:GI0Z-1071-MONOMER; -. DR Proteomes; UP000007033; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007033}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ADQ59013.1}; KW Transferase {ECO:0000313|EMBL:ADQ59013.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 223 223 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 331 AA; 37444 MW; B05EEE3527F16DB9 CRC64; MDLIKQISSK GLVLDGAMST ALEKQGIDTN TDLWTAVALD KDLDKVYKVH MNYFQAGAQM AITDTYQANV QAFEKHGYSE DKAKEMIADA VKIAKKARDD FEKKTGIHNY VAASVGPYGA YLAKGDEFRG DYDLTKKQYL DFHLPRLQVL LQNKPDCLAI ETQPKLDEVV VLLDWLKENA PEMPVYVSFT LHDTTKISDG TPLKKVMEKI NEYDQVFAVG ANCFKPFLAT TAIDKMREFT KKNIIVYPNL GGVYNEFERN WIPFNAKFDF GKLSKEWYEH GACIIGGCCS TGVKEISQIA AFYKILNNQK SRQKLDLKPN INLMKSTRSK V // ID E4SW16_LACDN Unreviewed; 310 AA. AC E4SW16; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 29-APR-2015, entry version 24. DE SubName: Full=Homocysteine/selenocysteine methylase (S-methylmethionine-dependent) {ECO:0000313|EMBL:ADQ60323.1}; GN Name=mmuM {ECO:0000313|EMBL:ADQ60323.1}; GN OrderedLocusNames=LDBND_0272 {ECO:0000313|EMBL:ADQ60323.1}; OS Lactobacillus delbrueckii subsp. bulgaricus (strain ND02). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=767455 {ECO:0000313|EMBL:ADQ60323.1, ECO:0000313|Proteomes:UP000008717}; RN [1] {ECO:0000313|Proteomes:UP000008717} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ND02 {ECO:0000313|Proteomes:UP000008717}; RA Chen W., Zhang H., Sun Z., Chen X., Guo Z., Wang J., Wu L., Zhang X., RA Zhou Z., Sun T., Wang L., Meng H.; RT "Complete genome sequence of Lactobacillus delbrueckii subsp. RT bulgaricus strain ND02."; 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; CP002341; ADQ60323.1; -; Genomic_DNA. DR RefSeq; WP_013439063.1; NC_014727.1. DR RefSeq; YP_004033300.1; NC_014727.1. DR EnsemblBacteria; ADQ60323; ADQ60323; LDBND_0272. DR KEGG; lde:LDBND_0272; -. DR PATRIC; 43079834; VBILacDel160915_0268. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; YGRSVTK; -. DR BioCyc; LDEL767455:GHXE-279-MONOMER; -. DR Proteomes; UP000008717; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008717}; KW Methyltransferase {ECO:0000313|EMBL:ADQ60323.1}; KW Transferase {ECO:0000313|EMBL:ADQ60323.1}. SQ SEQUENCE 310 AA; 33265 MW; EF25ADF1AC5954BA CRC64; MADLPTLLTQ GPVTLDGSMS MPLEAWGEDT NSDLWTAKAL ADNPDLVYRV HQEYFKAGAR VTITDSYQAS LSAFMKHGLS EDAARGLIRE SAAVAIKARD DFEKATGTHN FVAGSVGPYG AYLADGSEYR GDYALSHEEY VDFHAPRIEE LVAGGVDCLA VETQPKLSEV RAILDYLKAK YPDLPVYVSF SLKDPATISE GLPLTEAVEE VSAYAQVFAA GANCFKLAWT VDVVKNLRAS KLPIVVYPNS GAEYDPSVKK WVYPPEAADF GQAGADWLAA GAKLVGGCCT TMPEDIAGLA AAVKKVYTAF // ID E4T592_PALPW Unreviewed; 910 AA. AC E4T592; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAY-2015, entry version 31. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ADQ79886.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADQ79886.1}; DE Flags: Precursor; GN OrderedLocusNames=Palpr_1747 {ECO:0000313|EMBL:ADQ79886.1}; OS Paludibacter propionicigenes (strain DSM 17365 / JCM 13257 / WB4). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Paludibacter. OX NCBI_TaxID=694427 {ECO:0000313|EMBL:ADQ79886.1, ECO:0000313|Proteomes:UP000008718}; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WB4; 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., Munk A.C., Brettin T., RA Detter J.C., Han C., Tapia R., 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 Paludibacter propionicigenes DSM 17365."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADQ79886.1, ECO:0000313|Proteomes:UP000008718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17365 / JCM 13257 / WB4 RC {ECO:0000313|Proteomes:UP000008718}; RX PubMed=21475585; DOI=10.4056/sigs.1503846; RA Gronow S., Munk C., Lapidus A., Nolan M., Lucas S., Hammon N., RA Deshpande S., Cheng J.F., Tapia R., Han C., 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., Brambilla E., Rohde M., Goker M., Detter J.C., RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Paludibacter propionicigenes type strain RT (WB4)."; RL Stand. Genomic Sci. 4:36-44(2011). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002345; ADQ79886.1; -; Genomic_DNA. DR RefSeq; WP_013445255.1; NC_014734.1. DR RefSeq; YP_004042871.1; NC_014734.1. DR EnsemblBacteria; ADQ79886; ADQ79886; Palpr_1747. DR KEGG; ppn:Palpr_1747; -. DR PATRIC; 45311560; VBIPalPro155528_1784. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR BioCyc; PPRO694427:GHIQ-1791-MONOMER; -. DR Proteomes; UP000008718; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008718}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADQ79886.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008718}; KW Signal {ECO:0000313|EMBL:ADQ79886.1}; KW Transferase {ECO:0000313|EMBL:ADQ79886.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT SIGNAL 1 19 Potential. {ECO:0000313|EMBL:ADQ79886.1}. FT CHAIN 20 910 Potential. {ECO:0000313|EMBL:ADQ79886.1}. FT /FTId=PRO_5000660873. FT METAL 242 242 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 755 755 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 910 AA; 100216 MW; 5086882AD9B69B0A CRC64; MNLRTILENR ILILDGAMGT MIQRHKLNEA DYRGTRFANC EILQKGNNDL LVLTQPDIIY GIHNQYLEAG ADIIETNTFN AQRISMEDYG MCDLVREINI EAAKLARKAA DEFTAKNLAK PRFVAGAVGP TNKTASMSPD VNNPAFRAVS FDDLVAAYKE QILALIEGGV DALLIETIFD TLNAKAAIFA AEEAMSELGK RVEIMLSATV ADTSGRTLSG QTIRAFLASI GHANILSVGL NCSFGAKDLK PYLHEINEHS PWFVSAYPNA GLPNQFGEYD ETPETMAIQV KEYFDEKLVN IIGGCCGTSP DHIATYSALI ENKEVRKPGL ASKKLELSGL EELEIEDSSL FVNIGERCNV AGSRMFLRLI NEKKYEEALS IARKQVEDGA QVIDINMDDA MLESKEEMVT FLNYVAAEPE ISRVPIMIDS SKWEVIEAGL KCVQGKCIVN SISLKEGEEE FLYKARKIRA YGAAVVVMAF DEQGQADSFD RKTQICSRAY HLLVDKIGFP PQDIIFDPNV LAIATGIEEH NNYGVDFINA TRWIKQNLPY AKISGGVSNL SFSFRGNNVV REAIHSVFLY YAIKEGMDMG IVNAGMLQIY QDIEPELLEH VEDIVLNRRP DATERMIELA EKVKNQASGE KVEKVDEWRS RTLQGRLEHA LIKGISEFLE EDLSEALTQF DTAIEIIEGP LMSGMNIVGE LFGEGKMFLP QVVKTARTMK KAVAILQPEI EKQKVPGQSS SAGKFLIATV KGDVHDIGKN IVAVVLACNN FEVIDLGVMT PTEKIIQTAI DEKVDMVGLS GLITPSLEEM AHVATEMQKA GLSIPLLIGG ATTSKVHTAV KIAPNYGGPV VYVKDASVNT HVVAQLMSKT QHVAYEAGIA AEYQALREKQ TKKADLLSLD EAKKRKPNLF // ID E4TDS6_RIEAD Unreviewed; 337 AA. AC E4TDS6; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAY-2015, entry version 33. DE SubName: Full=Homocysteine s-methyltransferase {ECO:0000313|EMBL:AFD56948.1}; GN ORFNames=RA0C_2078 {ECO:0000313|EMBL:AFD56948.1}; 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 {ECO:0000313|EMBL:AFD56948.1, ECO:0000313|Proteomes:UP000010093}; RN [1] {ECO:0000313|EMBL:AFD56948.1, ECO:0000313|Proteomes:UP000010093} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 11845 {ECO:0000313|EMBL:AFD56948.1}; 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). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003388; AFD56948.1; -; Genomic_DNA. DR RefSeq; WP_004917492.1; NC_017045.1. DR RefSeq; YP_004046441.1; NC_014738.1. DR RefSeq; YP_005395491.1; NC_017045.1. DR EnsemblBacteria; ADQ82935; ADQ82935; Riean_1780. DR EnsemblBacteria; AFD56948; AFD56948; RA0C_2078. DR KEGG; rai:RA0C_2078; -. DR KEGG; ran:Riean_1780; -. DR PATRIC; 45354362; VBIRieAna155424_1810. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR BioCyc; RANA693978:GHF6-1830-MONOMER; -. DR Proteomes; UP000010093; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000010093}; KW Methyltransferase {ECO:0000313|EMBL:AFD56948.1}; KW Transferase {ECO:0000313|EMBL:AFD56948.1}. SQ SEQUENCE 337 AA; 37386 MW; 6B83FE4268BC1D1B CRC64; METNIFNQLD ALLQKRILIL DGAMGTMIQR YNFTEEHYRG ERFKDWEHPV KGNNDLLSLT QPQAIEEIHR LYLDAGADII ETNTFSSTTI AMADYAMESL VEELNYESAR IAKKLCEVYT ENNPDKPRFV AGAMGPTNRT ASLSPDVNDP GYRAITFEDL RKAYKQQAKA LLEGGADILL VETIFDTLNA KAALFAIDEL AEERNTKIPI MVSGTITDAS GRTLSGQTAE AFLISVSHLD LLSVGLNCAL GAKQLTPYLQ ALSEHSNFYI SVYPNAGLPN AFGAYDETAE QTAEQVKEYL DKRLVNIIGG CCGTTPEHIR AIAELVQHYE PRKLNLV // ID E4TJJ8_CALNY Unreviewed; 1126 AA. AC E4TJJ8; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAY-2015, entry version 32. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ADR18160.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADR18160.1}; GN OrderedLocusNames=Calni_0247 {ECO:0000313|EMBL:ADR18160.1}; OS Calditerrivibrio nitroreducens (strain DSM 19672 / NBRC 101217 / OS Yu37-1). OC Bacteria; Deferribacteres; Deferribacterales; Deferribacteraceae. OX NCBI_TaxID=768670 {ECO:0000313|EMBL:ADR18160.1, ECO:0000313|Proteomes:UP000007039}; 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] {ECO:0000313|EMBL:ADR18160.1, ECO:0000313|Proteomes:UP000007039} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19672 / NBRC 101217 / Yu37-1 RC {ECO:0000313|Proteomes:UP000007039}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002347; ADR18160.1; -; Genomic_DNA. DR RefSeq; WP_013450377.1; NC_014758.1. DR RefSeq; YP_004050323.1; NC_014758.1. DR EnsemblBacteria; ADR18160; ADR18160; Calni_0247. DR KEGG; cni:Calni_0247; -. DR PATRIC; 45188171; VBICalNit163602_0310. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; CNIT768670:GHD1-250-MONOMER; -. DR Proteomes; UP000007039; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007039}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADR18160.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007039}; KW Transferase {ECO:0000313|EMBL:ADR18160.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 217 217 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 717 717 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1126 AA; 126051 MW; C55B3405BF74E285 CRC64; MGDFVKFAKD RVILFDGAMG TNIQKYSISD ATWQGKNGCN EYLNIVAPHI IEEIHGNFLE AGADVLETNS FGGTRLVLSE YGLEDAVYEI NLQAARIARR VADKYGRFVA GSVGPGTKLV SLGHISYDDL FYMYKEQSLA LIDGGVDLFI IETCQDMLQI KAAINGIRSG MEEKKVNLPI MVSVTVEING TMLTGSDLSA VAVTMAGYPI YSLGINCALG PDLMYEPLTT LSNSWGGRIS CIPNAGLPMN INGKFVYNME PDRMAEIIDD ILNHFPISIV GGCCGTSYEH IREMRKVCDK HKVPDPVRFQ VKGMAASIYT ATSLNQEPPP ALIGERANAN GSKAFRELLI KEDFDGMLKI VKDQEEEAAH FVDICVAYAG RDEKRDMARF ISMVNRMSLL PAVIDTTEPD VLEEALKRYS GKPIINSINF EDGGKKLHRV LNLVKDFPAA VIGLTIDEDG MAMTAAKKFE IAKRIYTVFT EEYHLDPEDL IIDPLTFSIG SGDETLRYAA LQTLEAIKMI KNELPGVKTV LGLSNVSFGL SPKSRIILNS VFLKKAVESG LDMAIVHASK ILPEASIPTE EYDLALNLIN GEEGALEKFI NFYSAKKDDD ISVDKNDISD EELLIVKLKK GDKTDIETLL DRLLKRYTPY DIINNILMSG MQEIGELFGK GKMLLPFVLQ SAEVMKKSVS YLEKFMEKTD TEPKGKIVLA TVKGDVHDIG KNLVDIILSN NGYRVYNLGI KVPVEEMIEK AIEVGADAIG MSGLLVKSTI IMKENIEEIK RRGLKVKVLL GGAALTEGYV KNECAPVYDG EVYYCKDAFD AITYLQEEKG VESDVQNDVD VKIDSKNDKD SLKPSVKNDL SSTIVPQPPF LGVRVVECIN FDDVEKFLNK RTLWTNRWGY KKLKEQSNTE YEKLLEEVVK PEYNSILEKV KLSKLVDMKL IYGYFRVVSV GDDVIILDER ENEVERLTFP RQRVEPYLCL ADYFKPLDKG IVDILPLQIV TLGDRPVEFL KKLKDSNYKE YFLYHGFFTE FTEAVAEYWH RHIRYELGIT ENEPQSVEGI LTNRYRGLRY SFGYPSCPDL EGNKKIIELL DASKIGVSIT ETFQMVPEFT TSAIIVHSDK AKYFVV // ID E4TPQ8_MARTH Unreviewed; 1372 AA. AC E4TPQ8; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAY-2015, entry version 34. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADR23595.1}; GN OrderedLocusNames=Ftrac_3625 {ECO:0000313|EMBL:ADR23595.1}; 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 {ECO:0000313|EMBL:ADR23595.1, ECO:0000313|Proteomes:UP000008720}; RN [1] {ECO:0000313|Proteomes:UP000008720} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23168 / DSM 4126 / NBRC 15989 / NCIMB 1408 / VKM B-1430 / RC H-43 {ECO:0000313|Proteomes:UP000008720}; 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; ADR23595.1; -; Genomic_DNA. DR RefSeq; WP_013455737.1; NC_014759.1. DR RefSeq; YP_004055703.1; NC_014759.1. DR EnsemblBacteria; ADR23595; ADR23595; Ftrac_3625. DR KEGG; mtt:Ftrac_3625; -. DR PATRIC; 45220734; VBIMarTra126157_3745. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; MTRA643867:GI2X-3675-MONOMER; -. DR Proteomes; UP000008720; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR007569; DUF559. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF04480; DUF559; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF52980; SSF52980; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008720}; KW Reference proteome {ECO:0000313|Proteomes:UP000008720}. SQ SEQUENCE 1372 AA; 153283 MW; A65FC0B9E7BE2EBB CRC64; MSRFSKDILK DRILVLDGAM GTMIQNYKLT EADYRGDRFA DYPSDLKGNN DLLSLTQPKI IKDIHRAYLD AGADIIETNT FSGTTIAMAD YDMQDLVWEL NEQSAKIAKE VTEEYADKPR FVAGSIGPTN KTASLSPDVN RPGFRATSFD ELKIAYKLQA EALAVGGVDI FLVETVFDTL NCKSALMAIQ ELKEEKGIEI PVMVSGTITD ASGRTLSGQT VGAFWNSIRH FPLLSVGFNC ALGADQLKTY LQQLARISDV AISCHPNAGL PNEFGEYDES PSEMSSIIKS YFDEGLVNII GGCCGTQPEH IKAIAEYAAK SQPHKIAAQK KIMRLSGLEP LSVTPEINFV NIGERTNVSG SKKFARLIRE EKFEEAVDIA IDQVEGGAQI IDINMDDGML DAVKVLPNFV NLISSEPDIA RLPFMIDSSK WEVIEAGLKC LQGKGIVNSI SLKEGEEDFI AKAKKIKSYG ASVVVMAFDE TGQADTFDRK IAVCKRCYDL LVNKAEFPPE DIIFDPNILT IGTGMEEHNN YAVDFINAVQ WIKENLPYAK TSGGVSNISF SFRGNNTVRE AMHSAFLYHA IKAGLDMGIV NPGMLEVYDE IDKELLDYVE DLLFNKRADA TERLMAYAEN IKPGEKAEKA TQEWRNLPVN KRLEHALIKG ITEYIEEDTE ESRLQAERPL DVIEGPLMDG MNVVGDLFGS GKMFLPQVVK SARVMKKAVA ILLPYIEAEK KKNSPKAPYP PKGADSAQHW QTADPILYGL MKDFAKQMRH DHPTHAELVL WDALKGKQLE GYKFRRQHII GGYITDFICL KAKLIIEIDG LIHQLPENKA NDEERTKWLE EQGYKVIRFT NSEVITQLDI VLKKILEALS TPPLGAGGPL GAEEPVQERS GKGKILMATV KGDVHDIGKN IVSVVLACNN YEIIDLGVMV PLQKILEEAE KNQVDIIGLS GLITPSLDEM IYVVEEMEKR GLKTPVMIGG ATTSRIHTAV KIKPNYSGPV IHVNDASRSV TVAGKLLGKD KEEFYKEIER EYAEAKAGHG KRGEAKNYVS IEEARANKYQ IDWNNHRPHA PQKIGSEVLL DYDLKEIAEY IDWTPFFQTW EMKGRYPKIL DDAEKGQEAR KLFADAQQML QEIIDQKLLT ANAIFGLYPA HTKNHDSIEV FGDTDKTQKL TEFHTLRQQN KKGEKNPNYA FSDFLAPSEA DYTDYMGCFA VTTGIGLDKL TAKYEADHDD YNSIMAKALA DRLAEAFAEL LHKKVRTEYW GYAKDEALDN ESLIKEQYKG IRPAPGYPGC PDHTEKITLF ELLDVEKNTG IMLTENLAML PTASVSGFYF GHPESRYFGL GKIGKDQVED IAKRKNQEYK EIERWLKPNL NY // ID E4TXB2_SULKY Unreviewed; 1166 AA. AC E4TXB2; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAY-2015, entry version 30. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ADR32809.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADR32809.1}; GN OrderedLocusNames=Sulku_0142 {ECO:0000313|EMBL:ADR32809.1}; 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 {ECO:0000313|EMBL:ADR32809.1, ECO:0000313|Proteomes:UP000008721}; RN [1] {ECO:0000313|EMBL:ADR32809.1, ECO:0000313|Proteomes:UP000008721} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-921 / DSM 16994 / JCM 11577 / YK-1 RC {ECO:0000313|Proteomes:UP000008721}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002355; ADR32809.1; -; Genomic_DNA. DR RefSeq; WP_013459006.1; NC_014762.1. DR RefSeq; YP_004059009.1; NC_014762.1. DR EnsemblBacteria; ADR32809; ADR32809; Sulku_0142. DR KEGG; sku:Sulku_0142; -. DR PATRIC; 45369042; VBISulKuj150841_0399. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR BioCyc; SKUJ709032:GHTQ-150-MONOMER; -. DR Proteomes; UP000008721; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008721}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADR32809.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008721}; KW Transferase {ECO:0000313|EMBL:ADR32809.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 729 729 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1166 AA; 129993 MW; 0CAF08DD79742234 CRC64; MSVKNTLLET ISRRPLIIDG AMGTQLQERA DKIPESAWEG LEGCNELLNV TCPEVMSDIF HAYLTAGADL ITTNTFGAFS WVLDEYGIGH RAYELSRAGA AVCKAECDKF STSDHPRYVL GSIGPGTKLP SLGHIHYDEM YEGYLECCLG LIDGGCDIFL LETCQDPLQI KAALHACEAA NKERTTALPI MVSVTIELAG SMLIGTDAAT IATIMEPFDI ISLGFNCGTG PEQYAKHVRT LSEVWGKPIS VHANAGLPQN RGGYSYYPMG PDEFANLQRD FLNYDGVSFL GGCCGTTPQH IRALVDKVSR VAPKKPSGET KPSIASLFNT VELIQTPAPL LIGERSNSTG SKAFRELIIA SDYEGTLSVG QAQVRDGAHC LDVNVEFAGR DGAVDMSHVM RLYNQKIPLP LMPDATRVNT MEEALKCIGG KPIINSVNLE DGEERLDAIC SLAKKFGTAL VCLVIDEKGM AKTTEDKMRI ADRIYDLCVN RHGIDPRNLM FDMLTFTVGS GDLEYRDAAI QTLEAIRQLH FKYPNVGSTL GLSNISFGLS TNARVFLNSV FLHHCIEAGM TSVIINVKHI IPLSKMSEED RAICEELLFH PDDQSLFKFI GHFSDKTIDN SKNDEAYEAL SDEEKIAKLL LDGDKERMIP LVERVRLTIS PDKIVNEILI DAMKVVGELF GSGKMQLPFV LQSAETMKTT VDYLNPYLSK QEKDTDTTLV IGTVKGDVHD VGKNLVDIIL SNNGFKVINI GIKTELEEYL EVMKSKDIHA IGMSGLLVKS TQVMKDNLET MAGMGITTPV LLGGAALTRS FVDDFCRPIY QGPIFYCRDA FDGVIAMSRI EKYNADPSIG LDTRLGGDMV EKSVKEVIDV VIPPFHELKM PSREVKIPTP PFWGRRVLRK EQLDFDMVCE WINKRSLFKL HWGYKRAGMP VDEYKKLLET KVYPAYERIK REIVKRGLFD PTIIYGYYPV RSSDQELLIF DESSGWNIDE NANRQPLDEV IGNAKYVFEF PRQRKVPHRA LSDFFTHTRD DVLPLTCVSV GDKFSEYEKE LYAANEYLEY NLVHGFGVEL AEALAEVAHK QIRLDLNIAS DDEGFSLRDV RMNRYAGARY SFGYPACPDL EPSRIIFDLL RPEEFGITLS ETFQIHPEQS TTALVVHHKE ATYYNI // ID E4U971_OCEP5 Unreviewed; 1187 AA. AC E4U971; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAY-2015, entry version 32. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ADR36901.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADR36901.1}; GN OrderedLocusNames=Ocepr_1445 {ECO:0000313|EMBL:ADR36901.1}; OS Oceanithermus profundus (strain DSM 14977 / NBRC 100410 / VKM B-2274 / OS 506). OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; OC Oceanithermus. OX NCBI_TaxID=670487 {ECO:0000313|EMBL:ADR36901.1, ECO:0000313|Proteomes:UP000008722}; RN [1] {ECO:0000313|Proteomes:UP000008722} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14977 / NBRC 100410 / VKM B-2274 / 506 RC {ECO:0000313|Proteomes:UP000008722}; 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., Zhang X., 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., Tindall B., RA Faehnrich R., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete sequence of chromosome of Oceanithermus profundus DSM RT 14977."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002361; ADR36901.1; -; Genomic_DNA. DR RefSeq; WP_013458071.1; NC_014761.1. DR RefSeq; YP_004058074.1; NC_014761.1. DR EnsemblBacteria; ADR36901; ADR36901; Ocepr_1445. DR KEGG; opr:Ocepr_1445; -. DR PATRIC; 45306272; VBIOcePro145519_1573. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR BioCyc; OPRO670487:GH5I-1477-MONOMER; -. DR Proteomes; UP000008722; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008722}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADR36901.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008722}; KW Transferase {ECO:0000313|EMBL:ADR36901.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 255 255 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1187 AA; 131141 MW; 77FA8B50A7F9F0C2 CRC64; MAHDHEHAPQ GTGWGELPLP RLRYDLAERA RRFPYLRALS ERVLVFDGAM GTELQKYDLK PEDYGGAEYD GCPEILNLTR PDVIREIHER YLEAGADVIE TNTFGVMPHV IGEYGLAARA RELAEAGARL ARQMADAFSS PEKSRFVAGS LGPGTKLISL GQISWDELFE SYRTAARGLI AGGVDLIVIE TAQDILQVRC AVQAVRQAMR DEGREVPLQT QVTIETTGQM LVGSDAEAAL AALESLPVDV VGMNCATGPD LMDPHIRVFA EHSSRPTVCM PNAGLPRNED GQVVYDLTPE ELARWQTKFV TEYGLNVVGG CCGTGPEHIR ALSQALAGAP QTRPRPARLE PPAVASLYQA VELRPQAGVL MIGERTNATG SKKFRELLFA GDLDGIVELA QDQVAGGAQM LDVSVAWTGR DEKADMVRVV ERLAREVDAA LMIDSTQPEV IEAALEHVPG RPVINSVNFE DGEARFDRTA ALARAHGAAV VALTIDEEGM AKTVERKLEV AQRIYRRLVE KHGFLPEDIL FDLLTFPITQ GDEDTRRLAL ATLEAMRYLK DALPGVGFVL GVSNVSFGLK PPARKVLNAV FLHEAQQAGL TAAIVHPGKI VPVNQIPEEA VWLARDLIYD RREEGYDPLF AFIDYFESHT LDEARKDEAE LPVEERLHRR IVEGRKKGLE EDLAEALEKY RAEEIINRIL LGGMQEVGDL FGSGQMQLPF VLKSAEVMKA AVAWLEPHME RQEGSHKGTL VLATVKGDVH DIGKNLVDII LSNNGYRVIN LGIKQPIDSI LEAVERYRPD AVGMSGLLVK STAVMKENLE HMAALGHRIP VILGGAALNR SYVERDLRAV YPGTVHYAPD AFAGLKLMEE IVGARGRAEP AKPAAAARPK PRTAPARAKP VAPPPRVPRP PFFGRRIVEP GELDLFTIAR YLNENALFRG QWGYKRGQLS PEEHRALIER EARPRLRRWL ERAADENLLE PRVVYGFWPA AREGDAVVLF DPETGTELER FAFPRQAGGG LALADYFRPR SAEPLGDEEE WLPPAAWAAG ARDVMALMAV TMGPRASAYS QQLFDAGEYE DYLLFHGLSV EMTEALAEFW HKRLRQQWGI AAADATDLQK LFAQGYQGAR YAPGYPACPH LEDQAKLERL LSWRDIGLSL TEDFQLVPEQ STSAFVVHHP EARYFNV // ID E4V5P1_ARTGP Unreviewed; 226 AA. AC E4V5P1; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 07-JAN-2015, entry version 18. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EFR05416.1}; GN ORFNames=MGYG_08428 {ECO:0000313|EMBL:EFR05416.1}; OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum OS gypseum). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum. OX NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669}; RN [1] {ECO:0000313|Proteomes:UP000002669} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669}; 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; DS989830; EFR05416.1; -; Genomic_DNA. DR RefSeq; XP_003169523.1; XM_003169475.1. DR GeneID; 10024753; -. DR InParanoid; E4V5P1; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000002669; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002669}; KW Reference proteome {ECO:0000313|Proteomes:UP000002669}. SQ SEQUENCE 226 AA; 25129 MW; 6F420C151EEEF3D0 CRC64; MPGYNIDPEK NMAGTLLQCQ RDFGNVPVDI ILTATYQVSI DAFAQTKTKA FPNGILSTRI PEIVNDAVRV AEEAKCKGAK VALSIGPYGA TMKPCQEYSG QYDNAHHSLD ALHHWHRERM KLLAGITDIR PRLGYLSLET IPRIDEIKAM RKFPDATPKL AEIPFWMACV YSDAAETLPS GASAEEAVDA TVNFYPCILS KSLRDVLTLV KLFNDFHWLI ELSTLT // ID E4VYL7_BACFG Unreviewed; 916 AA. AC E4VYL7; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 01-APR-2015, entry version 21. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFR54551.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFR54551.1}; GN Name=metH {ECO:0000313|EMBL:EFR54551.1}; GN ORFNames=BFAG_03249 {ECO:0000313|EMBL:EFR54551.1}; OS Bacteroides fragilis 3_1_12. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=457424 {ECO:0000313|EMBL:EFR54551.1}; RN [1] {ECO:0000313|EMBL:EFR54551.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_12 {ECO:0000313|EMBL:EFR54551.1}; 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., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; EQ973215; EFR54551.1; -; Genomic_DNA. DR EnsemblBacteria; EFR54551; EFR54551; BFAG_03249. DR PATRIC; 27024769; VBIBacFra64498_3178. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFR54551.1}; KW Transferase {ECO:0000313|EMBL:EFR54551.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 916 AA; 100383 MW; 9403E14A837871ED CRC64; MKRTIQQLVP ERILILDGAM GTMIQQYNLR EEDFRSERFA HIPGQLKGNN DLLCLTRPDV VQDIHRKYLE AGADIIETNT FSSTTISMAD YHVQEYVREI NQTAVKLARE VADEYTALNP DKPRFVAGSV GPTNKTCSMS PDVNNPAYRA VTYDEMADAY QQQMEAMLES GVDALLIETI FDTLNAKAAI LAAERAMQAT GFKVPVMLSV TVSDIGGRTL SGQTLEAFLA SVQHADIFSV GLNCSFGAKQ LKPFLEQLAA RAPYYISAYP NAGLPNSLGK YDQTPADMAH EVEEYIHEGL INIIGGCCGT TDAYIAEYPA LIAGAKPHVP ARRPDCMWLS GLELLEVKPE INFVNVGERC NVAGSRKFLR LINEKKYDEA LSIARQQVED GALIIDVNMD DGLLDAKEEM TTFLNLVASE PEIARVPVMI DSSKWEVIEA GLKCLQGKSI VNSISLKEGE EKFLEHAQTV RQYGAAVVVM AFDEKGQADT AARKIEVCER AYRLLVDKIG FNPHDIIFDP NVLAVATGIE EHNNYAVDFI EATAWIKKNL PGAHISGGVS NLSFSFRGNN YIREAMHAVF LYYAIQKGMD MGIVNPGTSV LYTDIPADVL ERIEDVVLNR RPDAAERLIE LADKLKEASA GNASAGQPVK HDAWRDGTVE ERLQYALVKG IGDFLEEDLA EALPQYDKAV DVIEGPLMDG MNHVGELFGE GKMFLPQVVK TARTMKKAVA ILQPVIESEK VEGTSSAGKV LLATVKGDVH DIGKNIVSVV MACNGYDIID LGVMVPAESI VQKAIEEKVD MIGLSGLITP SLEEMVHVAM ELEKAGLDIP LLIGGATTSK LHTALKIAPV YHAPVVHLKD ASQNAGVAAR LMSPKLKEEL AQELSGEYQV LRDKSGLMKR ETVSLKEAQE KRLKLF // ID E4W2H5_BACFG Unreviewed; 318 AA. AC E4W2H5; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFR55909.1}; GN ORFNames=BFAG_04608 {ECO:0000313|EMBL:EFR55909.1}; OS Bacteroides fragilis 3_1_12. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=457424 {ECO:0000313|EMBL:EFR55909.1}; RN [1] {ECO:0000313|EMBL:EFR55909.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_12 {ECO:0000313|EMBL:EFR55909.1}; 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., 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; EQ973219; EFR55909.1; -; Genomic_DNA. DR RefSeq; WP_005782778.1; NZ_EQ973219.1. DR EnsemblBacteria; EFR55909; EFR55909; BFAG_04608. DR PATRIC; 27027494; VBIBacFra64498_4517. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFR55909.1}; KW Transferase {ECO:0000313|EMBL:EFR55909.1}. SQ SEQUENCE 318 AA; 36023 MW; 47EBED0E6EAD3549 CRC64; MDQLSFVESF RTSPFILTEG AIVERLRHEF QIPLDKHIVH AALIYNDSYR ETLAEIYRQY LQIATDFRLP LMLMTPTRRA NMEQIAESDY RHKNVLADNV SFLSRFRIGT SIPVYIGGLA GCRGDAYDGR YCLSVEEAME FHFPAVRTMA ESGVDYLFAG IMPQLTEAIG MANAMAATGL PYIISFMVCR DGRLIDGTFI HDAIDAIEKE TSTRPLCYMA NCIHPDILHQ ALLHPRNDTP LVHQRFQGIQ ANAANLSPEE LNGCEHLISS PPEELADRLM TLLWDFPLKI CGGCCGTNQQ HMRRFAEMLA CRRDKMGR // ID E4WHF2_RHOE1 Unreviewed; 1192 AA. AC E4WHF2; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 29-APR-2015, entry version 33. DE SubName: Full=Methionine synthase MetH {ECO:0000313|EMBL:CBH48357.1}; GN Name=metH {ECO:0000313|EMBL:CBH48357.1}; GN OrderedLocusNames=REQ_23110 {ECO:0000313|EMBL:CBH48357.1}; OS Rhodococcus equi (strain 103S) (Corynebacterium equi). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Nocardiaceae; Rhodococcus. OX NCBI_TaxID=685727 {ECO:0000313|EMBL:CBH48357.1, ECO:0000313|Proteomes:UP000006892}; RN [1] {ECO:0000313|Proteomes:UP000006892} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=103S {ECO:0000313|Proteomes:UP000006892}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; FN563149; CBH48357.1; -; Genomic_DNA. DR RefSeq; WP_013416010.1; NC_014659.1. DR RefSeq; YP_004007041.1; NC_014659.1. DR EnsemblBacteria; CBH48357; CBH48357; REQ_23110. DR KEGG; req:REQ_23110; -. DR PATRIC; 42662051; VBIRhoEqu141084_2309. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; REQU685727:GHKP-2231-MONOMER; -. DR Proteomes; UP000006892; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006892}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 232 232 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 298 298 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 742 742 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1192 AA; 130531 MW; 1AB6E5A588C2C009 CRC64; MDGMSAPFHS ALLDALKQRV VIGDGAMGTM LQAADLTLDD FLGLEGCNEI LNETRPDVLR DIHRAYFEAG ADAVETNTFG CNLPNLADYD IAHRIRDLSE RGTRIAREVA DEMGPGRDGM GRFVLGSMGP GTKLPTLGHA PFAVLRDAYT ESALGMIEGG ADAILVETCQ DLLQVKAAII GSQHAMEKLG RRLPIITHVT VETTGTMLLG SEIGAALTAL EPLGIDMIGL NCATGPDEMS EHLRHLSRHS KLPVSVMPNA GLPQLGPNGA EYPLSAEELA VALSGFVSEF GLSFVGGCCG TTPEHIRQVA DAVRRVEQAK RTPEPEDGTS SLYQAVPFDQ DASILMIGER TNSNGSKAFR EAMIAEDYQK CIDIAKDQTR DGAHMLDLNV DYVGRDGAAD MAALASRFAT ASTLPIMLDS TEPEVLRAGL EHLGGRCAVN SVNYEDGDGP NSRYQRIMKL VKEHGAAVVA LTIDEEGQAR TAEHKVRIAE RLIQDITTTW GLSQSDIIID ALTFPISTGQ EEVRRDGIET IEAIREIKRR YPDVHFTLGI SNISFGLNPA ARQVLNSVFL HECTEAGLDT AIVHASKILP MARIPDEQRE TALDLVYDRR REGYDPLQKL MELFEGVSAA SARESRAEEL AALPLFERLE RRIVDGERNG LEADLDAAMV ERPPLEIINE TLLSGMKTVG ELFGSGQMQL PFVLQSAEVM KAAVAYLEPH MESTGDEGKG RIVLATVKGD VHDIGKNLVD IILSNNGYEV VNIGIKQPIA TILDVALDKK ADVIGMSGLL VKSTVVMKEN LEELNAKGVA EQFPVLLGGA ALTRSYVEND LSDVYQGEVS YARDAFEGLH LMDTIMAVKR GEGPAPDSPE AIAAAEKAAE RKARHERSKR IAEKRKAESA PVEVPERSDV AADIVVPTPP FWGTRIVKGI ALAEYSGLLD ERALFLGQWG LRGQRAGDGP TYEELVETEG RPRLRYWLDR LSTEGVLQHA AVVYGYFPAV SEGDDVIVLE SPDPDAPERF RFTFPRQQRD RFLCIADFVR SRDDARKDGQ VDVLPMNLVT MGQPIADFAN ELFAANSYRD YLEVHGIGVQ LTEALAEYWH RRVREELVLP GGHNLAEQDP SDVEDFFKLE YRGARYSFGY GACPDLEDRR KLVALLEPER IGVELSEEVQ LHPEQSTDAF VLHHPEAKYF NV // ID E4XNA3_OIKDI Unreviewed; 148 AA. AC E4XNA3; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 07-JAN-2015, entry version 15. DE SubName: Full=Whole genome shotgun assembly, reference scaffold set, scaffold scaffold_68 {ECO:0000313|EMBL:CBY11341.1}; GN ORFNames=GSOID_T00015658001 {ECO:0000313|EMBL:CBY11341.1}; OS Oikopleura dioica (Tunicate). OC Eukaryota; Metazoa; Chordata; Tunicata; Appendicularia; Oikopleuridae; OC Oikopleura. OX NCBI_TaxID=34765 {ECO:0000313|Proteomes:UP000001307}; RN [1] {ECO:0000313|EMBL:CBY11341.1, ECO:0000313|Proteomes:UP000001307} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21097902; DOI=10.1126/science.1194167; RA Denoeud F., Henriet S., Mungpakdee S., Aury J.M., Da Silva C., RA Brinkmann H., Mikhaleva J., Olsen L.C., Jubin C., Canestro C., RA Bouquet J.M., Danks G., Poulain J., Campsteijn C., Adamski M., RA Cross I., Yadetie F., Muffato M., Louis A., Butcher S., RA Tsagkogeorga G., Konrad A., Singh S., Jensen M.F., Cong E.H., RA Eikeseth-Otteraa H., Noel B., Anthouard V., Porcel B.M., RA Kachouri-Lafond R., Nishino A., Ugolini M., Chourrout P., Nishida H., RA Aasland R., Huzurbazar S., Westhof E., Delsuc F., Lehrach H., RA Reinhardt R., Weissenbach J., Roy S.W., Artiguenave F., RA Postlethwait J.H., Manak J.R., Thompson E.M., Jaillon O., RA Du Pasquier L., Boudinot P., Liberles D.A., Volff J.N., Philippe H., RA Lenhard B., Roest Crollius H., Wincker P., Chourrout D.; RT "Plasticity of animal genome architecture unmasked by rapid evolution RT of a pelagic tunicate."; RL Science 330:1381-1385(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; FN653082; CBY11341.1; -; Genomic_DNA. DR InParanoid; E4XNA3; -. DR Proteomes; UP000001307; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001307}; KW Reference proteome {ECO:0000313|Proteomes:UP000001307}. SQ SEQUENCE 148 AA; 16535 MW; F0FC825838D8A455 CRC64; MWNQVKVIDG GMGTELVRCG VQDVDKHKLW SALANVDFPD SVVQAHKNFI DAGADVIISN TYQSNQPLLM SELQISREEA DNLLLKTVDL ARKAAGSETI VAGSIGPFPD CPASEYDPQY LKRMSFEELY NWHLPRFELL AKKGLILQ // ID E5A393_LEPMJ Unreviewed; 333 AA. AC E5A393; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 07-JAN-2015, entry version 18. DE SubName: Full=Similar to homocysteine S-methyltransferase {ECO:0000313|EMBL:CBX98106.1}; GN ORFNames=LEMA_P095150.1 {ECO:0000313|EMBL:CBX98106.1}; 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 {ECO:0000313|Proteomes:UP000002668}; RN [1] {ECO:0000313|Proteomes:UP000002668} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8 RC {ECO:0000313|Proteomes:UP000002668}; 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; FP929133; CBX98106.1; -; Genomic_DNA. DR RefSeq; XP_003841585.1; XM_003841537.1. DR EnsemblFungi; CBX98106; CBX98106; LEMA_P095150.1. DR GeneID; 13285980; -. DR InParanoid; E5A393; -. DR OMA; SYIGKWR; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000002668; Whole genome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002668}; KW Methyltransferase {ECO:0000313|EMBL:CBX98106.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002668}; KW Transferase {ECO:0000313|EMBL:CBX98106.1}. SQ SEQUENCE 333 AA; 35668 MW; 0C1601628291CEA8 CRC64; MSTTTLEQAI HAQTPIILDG ALATYLETLG ADISGALWSA DILLKNPSLI KQAHLDYYRA GAQIAITASY QASLPGLVQH LGPGTVGEDE VKEVVRTSVR LAQQARDEYV AERTREGAGE TSTPPPQLWV AGSVGPYGAF LANGSEYRGD YELPIPAMQA FHRGRIAALV SAGADILALE TIPSKQETIA LLDLLRHEFP TTKAWFTFTL AGPDAIADGT PLAELVPLFR HEAQVLALGF NCVPDGVGLA AVKVLKTVLL EQGMARVGTV MYPNSGELWN ARAREWEGSR TEGGLLGEKT REWYAAGARL IGGCCRTTPG DIGVMREALE GFR // ID E5AMJ1_BURRH Unreviewed; 379 AA. AC E5AMJ1; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CBW76223.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CBW76223.1}; GN OrderedLocusNames=RBRH_02239 {ECO:0000313|EMBL:CBW76223.1}; OS Burkholderia rhizoxinica (strain DSM 19002 / CIP 109453 / HKI 454). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=882378 {ECO:0000313|EMBL:CBW76223.1, ECO:0000313|Proteomes:UP000007437}; RN [1] {ECO:0000313|EMBL:CBW76223.1, ECO:0000313|Proteomes:UP000007437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19002 / CIP 109453 / HKI 454 RC {ECO:0000313|Proteomes:UP000007437}; 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; CBW76223.1; -; Genomic_DNA. DR RefSeq; WP_013436452.1; NC_014722.1. DR RefSeq; YP_004030367.1; NC_014722.1. DR EnsemblBacteria; CBW76223; CBW76223; RBRH_02239. DR KEGG; brh:RBRH_02239; -. DR PATRIC; 45187158; VBIBurRhi170666_3338. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR BioCyc; BRHI882378:GJIB-2761-MONOMER; -. DR Proteomes; UP000007437; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007437}; KW Methyltransferase {ECO:0000313|EMBL:CBW76223.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007437}; KW Transferase {ECO:0000313|EMBL:CBW76223.1}. SQ SEQUENCE 379 AA; 40997 MW; 5CE85977E16FDACC CRC64; MSDYGALRHA PPPTVTTCRD AVSRDSCIHP MQKAHSLRYT RGSALPALLA RRILILDGAM GTMIQRYKLS EAHYRGERFA ALDHDVKGNN ELLSITQPQI IGQIHEQYLA AGADIVETNT FGATRIAQAD YRMETLAIEM NIASARLARA ACDRYSTPDK PRFVAGAIGP TPKTASISPD VNDPGARNVT FDELRDSYYE QAQALLDGGA DLFLVETIFD TLNAKAALFA LDQLFEDTGE VLPIMISGTV TDASGRILSG QTVEAFWNAL RHARPLTFGL NCALGAALMR PYIAELAKLC DTYVSCYPNA GLPNPMSETG FDETPEVTSG LLKEFADSGL VNLAGGCCGT TPEHIAAIAA RLADVKPRAW AHYQEKSES // ID E5B3D3_ERWAM Unreviewed; 300 AA. AC E5B3D3; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAY-2015, entry version 12. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:CBX79920.1}; DE EC=2.1.1.- {ECO:0000313|EMBL:CBX79920.1}; GN ORFNames=EAIL5_1100 {ECO:0000313|EMBL:CBX79920.1}; OS Erwinia amylovora ATCC BAA-2158. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Erwinia. OX NCBI_TaxID=889211 {ECO:0000313|EMBL:CBX79920.1}; RN [1] {ECO:0000313|EMBL:CBX79920.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-2158 {ECO:0000313|EMBL:CBX79920.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR719189; CBX79920.1; -; Genomic_DNA. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:CBX79920.1}; KW Transferase {ECO:0000313|EMBL:CBX79920.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 208 208 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 300 AA; 31894 MW; CE9E1293FC773545 CRC64; MTQQIKILDG GMGRELARVG APFRQPEWSA LALYEAPQRV REVHDSFISA GAGTITTNSY AVVPFHIGQA RFHADGEYLA ALAGQLARQA ANAATHPVQV AGSLPPALGS YRPDLFDAQQ ALKIYRLLVA AQAPYVDIWL GETISSLAEA VAIHQAVADQ PHPLWLSFSL EDDPDKTRRD STLRSGESVS AAVELAVESG ATHILFNCSN PEVMLSAVQQ AAATLRRLGS EAGIGVYANA FEHGSNGGGA NEGLSDLRQD THPEGYLRWA REWVAAGATL VGGCCGIGPE HIRCLASAFK // ID E5BGG0_9FUSO Unreviewed; 302 AA. AC E5BGG0; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFS21583.1}; GN ORFNames=FSBG_01080 {ECO:0000313|EMBL:EFS21583.1}; OS Fusobacterium gonidiaformans 3-1-5R. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=469605 {ECO:0000313|EMBL:EFS21583.1, ECO:0000313|Proteomes:UP000002975}; RN [1] {ECO:0000313|EMBL:EFS21583.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_5R {ECO:0000313|EMBL:EFS21583.1}; 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., 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 ----------------------------------------------------------------------- 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; EFS21583.1; -; Genomic_DNA. DR EnsemblBacteria; EFS21583; EFS21583; FSBG_01080. DR Proteomes; UP000002975; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002975}; KW Methyltransferase {ECO:0000313|EMBL:EFS21583.1}; KW Transferase {ECO:0000313|EMBL:EFS21583.1}. SQ SEQUENCE 302 AA; 34195 MW; DBC550FAD12FE13E CRC64; MREIIFFFGG RNMLLEALKR RILVLDGAMG TMLASYGEKP CYEVLNKTKE NLIQKIHEKY IEAGADIITT NSFNCNQMAL QKYHLKESVY DLTKKSVEIA KKATKNSKKA VYILGSIGPS IANLPEDMKS WKQSYFQQIL GLLDGGVDAL LLETIYDENK ANCILGNIEE IFQEKKVEVP VFCSMTINQN GKLLTGTSIT RAVEKMDRPW IVGFGLNCSY GMENIVSFLP ELIRATDKYC MVYANAGFPN EKGEYTENIE EMLELLQPFL EKHWIHIVGG CCGTNEKYTY AFAKKIALLA ER // ID E5C3P4_9BACE Unreviewed; 915 AA. AC E5C3P4; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 01-APR-2015, entry version 27. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFS30080.1}; GN ORFNames=BSGG_0780 {ECO:0000313|EMBL:EFS30080.1}; OS Bacteroides sp. D2. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=556259 {ECO:0000313|EMBL:EFS30080.1}; RN [1] {ECO:0000313|EMBL:EFS30080.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=D2 {ECO:0000313|EMBL:EFS30080.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFS30080.1}. 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; ACGA02000065; EFS30080.1; -; Genomic_DNA. DR EnsemblBacteria; EFS30080; EFS30080; BSGG_0780. DR PATRIC; 30555488; VBIBacSp21829_0682. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 915 AA; 99914 MW; 6FD848D66EE0DC22 CRC64; MKKTISQIVS ERILILDGAM GTMIQQYNLK EEDFRGERFA HIPGQLKGNN DLLCLTRPDV IQDIHRKYLE AGADIIETNT FSSTTVSMAD YHVEEYVREM NLAAVKLARD LADEYTAKNP DKPRFVAGSV GPTNKTCSMS PDVNNPAYRA LSYDELAASY QQQMEAMLEG GVDAILIETI FDTLNAKTAI FAAEQAMKAT GVEVPIMLSV TVSDIGGRTL SGQTLDAFLA SVQHANIFSV GLNCSFGARQ LKPFLEQLAS HAPYYISAYP NAGLPNSLGK YDQTPADMAH EVREYVEEGL INIIGGCCGT TDAYIAEYPA LVEGAKPHVP ASAPDCMWLS GLELLEVKPE INFVNVGERC NVAGSRKFLR LINEKKYDEA LSIARQQVED GALVIDVNMD DGLLEAKTEM TTFLNLIMSE PEIARVPIMI DSSKWEVIEA GLKCLQGKSI VNSISLKEGE EVFLEHARII RQYGAAAVVM AFDEKGQADT AARKIEVCQR AYRLLVDKIG FNPHDIIFDP NVLAVATGIE EHNNYAVDFI EATAWIKKNL PGAHISGGVS NLSFSFRGNN YIREAMHAVF LYHAIQQGMD MGIVNPGTSV LYTDIPADVL EKIEDVVLNR RPDAAERLIE LAESLKATMS GTAGQPAVKH DAWREESVQE RLKYALMKGI GDFLEQDLAE ALPLYDKAVN VIEGPLMDGM NHVGELFGAG KMFLPQVVKT ARTMKKAVAI LQPIIESEKV EGSASAGKVL LATVKGDVHD IGKNIVAVVM ACNGYDIVDL GVMVPAETIV QRAIEEKVDM IGLSGLITPS LEEMAHVAVE LEKAGLDIPL LIGGATTSKM HTALKIAPVY HAPVVHLKDA SQNASVASKL LNPQAKAELV NELETEYEAL REKSGLMKRE TVSLEEAQKN KLNLF // ID E5CI89_STAHO Unreviewed; 612 AA. AC E5CI89; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HMPREF0798_01620 {ECO:0000313|EMBL:EFS20255.1}; OS Staphylococcus hominis subsp. hominis C80. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=435837 {ECO:0000313|EMBL:EFS20255.1, ECO:0000313|Proteomes:UP000010143}; RN [1] {ECO:0000313|EMBL:EFS20255.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C80 {ECO:0000313|EMBL:EFS20255.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL545254; EFS20255.1; -; Genomic_DNA. DR RefSeq; WP_002454538.1; NZ_GL545254.1. DR EnsemblBacteria; EFS20255; EFS20255; HMPREF0798_01620. DR PATRIC; 44620346; VBIStaHom42890_0061. DR Proteomes; UP000010143; Unassembled WGS sequence. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010143}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 612 AA; 68204 MW; E213F1646774B617 CRC64; MSRLLNHLKN NVLVADGAMG TILYSEGLDT CPEAYNLTHP NKVERIHRSY IEAGADVIQT NTYGANFEKL KVFGLEHKVK EIHKAAVQIA KRAANKETFI LGTVGGFRGI KQEDLSLSTI QYHTDNQIDT LIEEGVDGLL FETYYDLDEL TSVITATRQK YDIPIIAQLT ASNTNYLVDG TEINEALKHL IECGANVVGL NCHHGPHHMQ RSFSHIELPE HAYLSCYPNA SLLDIENSEF KYSNNAKYFG DVAQELINEG VRLIGGCCGT TPEHISYIKE SVKHLKPIKT KKVIPIHRTI NTNAKRTLKQ NLTSKVKQRP TVIVELDTPK HLDTELFFEN IGKLDEANID AVTLADNSLA TVRVSNIAAA SLIKQRYEIE PLVHITCRDR NLIGLQSHLL GLSLIGVSEI LAITGDPSKV GHLPGATNVY DVNSKGLTEL ALRFNQGINV DGDALKKHTN FNIAGAFDPN VRKLDGAVKR LEKKVAAGMS YFITQPVYSK EKIKEVYEAT KHLDTPLFIG IMPIASYNNA LFLHNEVPGI KMSEDVLNQF KAVKDDKEKT KELSLRLSKE LIDTVHEYFN GLYLITPFQR IDYSLELAAY SKAITQNKEA IS // ID E5RH96_HUMAN Unreviewed; 68 AA. AC E5RH96; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=S-methylmethionine--homocysteine S-methyltransferase BHMT2 {ECO:0000313|Ensembl:ENSP00000428640}; DE Flags: Fragment; GN Name=BHMT2 {ECO:0000313|Ensembl:ENSP00000428640}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000428640, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000428640, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., RA Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [2] {ECO:0000313|Ensembl:ENSP00000428640} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSP00000428640}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AC008502; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; E5RH96; -. DR SMR; E5RH96; 2-68. DR BindingDB; E5RH96; -. DR Ensembl; ENST00000518666; ENSP00000428640; ENSG00000132840. DR HGNC; HGNC:1048; BHMT2. DR GeneTree; ENSGT00390000003122; -. DR ChiTaRS; BHMT2; human. DR NextBio; 35498294; -. DR Proteomes; UP000005640; Chromosome 5. DR Bgee; E5RH96; -. DR ExpressionAtlas; E5RH96; baseline and differential. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Proteomics identification {ECO:0000213|PeptideAtlas:E5RH96}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}. FT NON_TER 68 68 {ECO:0000313|Ensembl:ENSP00000428640}. SQ SEQUENCE 68 AA; 7440 MW; E6DFB104E346B1E2 CRC64; MEFLRAGSNV MQTFTFSASE DNMESKWEDV NAAACDLARE VAGKGDALVA GGICQTSIYK YQKDEARI // ID E5RJH0_HUMAN Unreviewed; 253 AA. AC E5RJH0; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAY-2015, entry version 33. DE SubName: Full=Betaine--homocysteine S-methyltransferase 1 {ECO:0000313|Ensembl:ENSP00000428240}; GN Name=BHMT {ECO:0000313|Ensembl:ENSP00000428240}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000428240, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000428240, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., RA Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [2] {ECO:0000313|Ensembl:ENSP00000428240} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. RN [3] {ECO:0000213|PubMed:24275569} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSP00000428240}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AC008502; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; E5RJH0; -. DR SMR; E5RJH0; 8-250. DR Ensembl; ENST00000524080; ENSP00000428240; ENSG00000145692. DR UCSC; uc011cti.2; human. DR HGNC; HGNC:1047; BHMT. DR GeneTree; ENSGT00390000003122; -. DR ChiTaRS; BHMT; human. DR NextBio; 35498964; -. DR Proteomes; UP000005640; Chromosome 5. DR Bgee; E5RJH0; -. DR ExpressionAtlas; E5RJH0; baseline and differential. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Proteomics identification {ECO:0000213|PeptideAtlas:E5RJH0}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}. SQ SEQUENCE 253 AA; 28206 MW; BD2C7BC33488D7C9 CRC64; MPPVGGKKAK KGILERLNAG EIVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAGASII GVNCHFDPTI SLKTVKLMKE GLEAARLKAH LMSQPLAYHT PDCNKQGFID LPEFPFGLEP RVATRWDIQK YAREAYNLGV RYIGGCCGFE PYHIRAIAEE LAPERGFLPP ASEKHGSWGS GLDMHTKPWV RARARKEYWE NLRIASGRPY NPSMSKPDGW GVTKGTAELM QQKEATTEQQ LKELFEKQKF KSQ // ID E5S7E5_TRISP Unreviewed; 242 AA. AC E5S7E5; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 07-JAN-2015, entry version 24. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFV59295.1}; GN ORFNames=Tsp_07637 {ECO:0000313|EMBL:EFV59295.1}; OS Trichinella spiralis (Trichina worm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichocephalida; Trichinellidae; Trichinella. OX NCBI_TaxID=6334 {ECO:0000313|EMBL:EFV59295.1, ECO:0000313|Proteomes:UP000006823}; RN [1] {ECO:0000313|EMBL:EFV59295.1, ECO:0000313|Proteomes:UP000006823} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISS 195 {ECO:0000313|EMBL:EFV59295.1, RC ECO:0000313|Proteomes:UP000006823}; RX PubMed=21336279; DOI=10.1038/ng.769; RA Mitreva M., Jasmer D.P., Zarlenga D.S., Wang Z., Abubucker S., RA Martin J., Taylor C.M., Yin Y., Fulton L., Minx P., Yang S.P., RA Warren W.C., Fulton R.S., Bhonagiri V., Zhang X., Hallsworth-Pepin K., RA Clifton S.W., McCarter J.P., Appleton J., Mardis E.R., Wilson R.K.; RT "The draft genome of the parasitic nematode Trichinella spiralis."; RL Nat. Genet. 43:228-235(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. {ECO:0000313|EMBL:EFV59295.1}. 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; ABIR02000648; EFV59295.1; -; Genomic_DNA. DR RefSeq; XP_003381089.1; XM_003381041.1. DR EnsemblMetazoa; EFV59295; EFV59295; EFV59295. DR GeneID; 10903530; -. DR KEGG; tsp:Tsp_07637; -. DR CTD; 10903530; -. DR InParanoid; E5S7E5; -. DR KO; K00548; -. DR OMA; VERPEYP; -. DR Proteomes; UP000006823; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006823}; KW Reference proteome {ECO:0000313|Proteomes:UP000006823}. SQ SEQUENCE 242 AA; 27219 MW; BE8B8F8278C3E368 CRC64; MAKKCDDMFK KFRSILEKRV MIIDGGMGTM IQRFHLDESS YRGTRFADHP VSLKGNNDLL TLTRPDIIYE IHRRYFDAGA DFIETNTFSS NRIAQADYKL ESLIYELNFE ASKIAKQAAS DTENETGQQC FVLGSIGPTN KTLSISPSVE RPEYPFTELA NAYKEQAEAL LDGEVDAFLV ETIFDTANAK AAIFAIQTLF EERQTRIPVF LSGTVVDKSG RTLSGQSIEA FLISVQHADP FW // ID E5S7E6_TRISP Unreviewed; 929 AA. AC E5S7E6; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAY-2015, entry version 31. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFV59296.1}; GN ORFNames=Tsp_07638 {ECO:0000313|EMBL:EFV59296.1}; OS Trichinella spiralis (Trichina worm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichocephalida; Trichinellidae; Trichinella. OX NCBI_TaxID=6334 {ECO:0000313|EMBL:EFV59296.1, ECO:0000313|Proteomes:UP000006823}; RN [1] {ECO:0000313|EMBL:EFV59296.1, ECO:0000313|Proteomes:UP000006823} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISS 195 {ECO:0000313|EMBL:EFV59296.1, RC ECO:0000313|Proteomes:UP000006823}; RX PubMed=21336279; DOI=10.1038/ng.769; RA Mitreva M., Jasmer D.P., Zarlenga D.S., Wang Z., Abubucker S., RA Martin J., Taylor C.M., Yin Y., Fulton L., Minx P., Yang S.P., RA Warren W.C., Fulton R.S., Bhonagiri V., Zhang X., Hallsworth-Pepin K., RA Clifton S.W., McCarter J.P., Appleton J., Mardis E.R., Wilson R.K.; RT "The draft genome of the parasitic nematode Trichinella spiralis."; RL Nat. Genet. 43:228-235(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. {ECO:0000313|EMBL:EFV59296.1}. 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; ABIR02000648; EFV59296.1; -; Genomic_DNA. DR RefSeq; XP_003381088.1; XM_003381040.1. DR EnsemblMetazoa; EFV59296; EFV59296; EFV59296. DR GeneID; 10903529; -. DR KEGG; tsp:Tsp_07638; -. DR CTD; 10903529; -. DR InParanoid; E5S7E6; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR Proteomes; UP000006823; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006823}; KW Reference proteome {ECO:0000313|Proteomes:UP000006823}. SQ SEQUENCE 929 AA; 103441 MW; 8CA10097D24D0ECD CRC64; MRPFIETVSK NTSAYVICYP NAGLPNSFGE YDESPEQTAA TIKQFAVDGL VNIVGGCCGT TPDHIAKICQ AVKGVPPRCP QKDIFKSYTL LSGLESMQIG PFTNFVNIGE RCNVAGSRRF ASMIKKGNYE MALQVAKEQV ELGAQILDVN LDEAMLDGVN SMIKFVNLIS SDPDISKVPL CIDSSNFLVI EAGLQCFQGK CIANSISLKE GEEKFLQHAK TLKKYGAAIV VMAFDETGQA TTVEHRVKVC QRSYNLLVEE AKIDPADIIF DLNVLTVGTG IEEHNTYAVS FFESAKIVKK LFPECRISGG ISNVSFAFRG RDKIREAMHS AGLDMGIVNA GCLPVYSEIE KTLLELCTNL LLNRSPGATE DLLAYAEKEG DKLTEEKNIP KVEWRDWPVD ERLKHALIKG ISDYVIDDVE QARNMTDIYP RPLNIIEGPL MTGMAAVGDL FGSGKMFLPQ VIKSARVMKK AVEYLVPFME REKESKAEDE INYRGTIILA TVKGDVHDIG KNIVSVVLGC NNFKVIDLGI MTPCDKILKA AIDNNADMIG LSGLITPSLE EMIYVAKEMQ RVDFKIPLLI GGATTSRIHT AVKIKSAYSG PVVHCSSLMD EKMRGEFLCE TEELYEEIRQ DYFDNFSELR FVPLNVAREH SLKLDWSTGK YPNRGFPKLF DDPDIGEEAK RVFDDAQQLL SKICNESLLQ ANAVIGIFPA LSDGDDILIL NPENMDKSSP IGVLHGLRQQ AVKEQSEQPY LCLSDFIVPK SMDMYDYIVG IGLEKLVSSY EQQLDDYHAI MCKALADRLS EAFAEELHER VRLNFWGYTS ESLSVDALHR IQYEGIRPAP GYPCQPDLSE MRTLWKLLDV DKNTGIHLTE SMAMHPTASV CGLYFAHSKA KYFAVGKIDK DQIMDYATRK GVSTEEVQKW LSQCLRFES // ID E5S7E8_TRISP Unreviewed; 951 AA. AC E5S7E8; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAY-2015, entry version 31. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFV59276.1}; GN ORFNames=Tsp_07640 {ECO:0000313|EMBL:EFV59276.1}; OS Trichinella spiralis (Trichina worm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichocephalida; Trichinellidae; Trichinella. OX NCBI_TaxID=6334 {ECO:0000313|EMBL:EFV59276.1, ECO:0000313|Proteomes:UP000006823}; RN [1] {ECO:0000313|EMBL:EFV59276.1, ECO:0000313|Proteomes:UP000006823} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISS 195 {ECO:0000313|EMBL:EFV59276.1, RC ECO:0000313|Proteomes:UP000006823}; RX PubMed=21336279; DOI=10.1038/ng.769; RA Mitreva M., Jasmer D.P., Zarlenga D.S., Wang Z., Abubucker S., RA Martin J., Taylor C.M., Yin Y., Fulton L., Minx P., Yang S.P., RA Warren W.C., Fulton R.S., Bhonagiri V., Zhang X., Hallsworth-Pepin K., RA Clifton S.W., McCarter J.P., Appleton J., Mardis E.R., Wilson R.K.; RT "The draft genome of the parasitic nematode Trichinella spiralis."; RL Nat. Genet. 43:228-235(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. {ECO:0000313|EMBL:EFV59276.1}. 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; ABIR02000649; EFV59276.1; -; Genomic_DNA. DR RefSeq; XP_003381108.1; XM_003381060.1. DR EnsemblMetazoa; EFV59276; EFV59276; EFV59276. DR GeneID; 10903550; -. DR KEGG; tsp:Tsp_07640; -. DR CTD; 10903550; -. DR InParanoid; E5S7E8; -. DR KO; K00548; -. DR OMA; QPFFNAW; -. DR Proteomes; UP000006823; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006823}; KW Reference proteome {ECO:0000313|Proteomes:UP000006823}. SQ SEQUENCE 951 AA; 105900 MW; 5E949AB5CC1BA9D5 CRC64; MRPFIETVSK NTSAYVICYP NAGLPNSFGE YDESPEQTAA TLKQFAVDGL VNIVGGCCGT TPDHIAKICQ AVKGVPPRCP QKDIFKSYTL LSGLESMQIG PFTNFVNIGE RCNVAGSRRF ASMIKKGNYE MALQVAKEQV ELGAQILDVN LDEAMLDGVN SMIKFVNLIS SDPDISKVPL CIDSSNFLVI EAGLQCFQGK CIANSISLKE GEEKFLQHAK TLKKYGAAIV VMAFDETGQV NADKLRERED EITKATTVEH RVKVCQRSYN LLVEEAKIDP ADIIFDLNVL TVGTGIEEHN TYAVSFFESA KIVKKLFPEC RISGGISNVS FAFRGRDKIR EAMHSAGLDM GIVNAGCLPV YSEIEKTLLE LCTNLLLNRS PGATEDLLAY AEKEGDKLTE EKNIPKVEWR DWPVDERLKH ALIKGISDYV IDDVEQARNM TDIYPRPLNI IEGPLMTGMA AVGDLFGSGK MFLPQVIKSA RVMKKAVEYL VPFMEQEKES KAEDEINYRG TIILATVKGD VHDIGKNIVS VVLGCNNFKV IDLGIMTPCD KILKAAIDNN ADMIGLSGLI TPSLEEMIYV AKEMQRVDFK IPLLIGGATT SRIHTAVKIK SAYSGPVIHV SDASKSCSSL MDEKMRGEFL CETEELYEEI RQDYFDNFSE LRFVPLNVAR EHSLKLDWST GKYPNRGFPK LFDDPDIGEE AKRVFDDAQQ LLSKICNESL LQANAVIGIF PALSDGDDIL ILNPENMDKS SPIGVLHGLR QQAVKEQSEQ PYLCLSDFIV PKSMDMYDYI VGIGLEKLVS SYEQQLDDYH AIMCKALADR LSEAFAEELH ERVRLNFWGY TSESLSVDAL HRIQYEGIRP APGYPCQPDL SEMRTLWKLL DVDKNTGIHL TESMAMHPTA SVCGLYFAHS KAKYFAVGKI DKDQIMDYAT RKGVSTEEVQ KWLSQCLRFE S // ID E5SW97_TRISP Unreviewed; 324 AA. AC E5SW97; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 07-JAN-2015, entry version 19. DE SubName: Full=Putative homocysteine S-methyltransferase {ECO:0000313|EMBL:EFV50941.1}; GN ORFNames=Tsp_04840 {ECO:0000313|EMBL:EFV50941.1}; OS Trichinella spiralis (Trichina worm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichocephalida; Trichinellidae; Trichinella. OX NCBI_TaxID=6334 {ECO:0000313|EMBL:EFV50941.1, ECO:0000313|Proteomes:UP000006823}; RN [1] {ECO:0000313|EMBL:EFV50941.1, ECO:0000313|Proteomes:UP000006823} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISS 195 {ECO:0000313|EMBL:EFV50941.1, RC ECO:0000313|Proteomes:UP000006823}; RX PubMed=21336279; DOI=10.1038/ng.769; RA Mitreva M., Jasmer D.P., Zarlenga D.S., Wang Z., Abubucker S., RA Martin J., Taylor C.M., Yin Y., Fulton L., Minx P., Yang S.P., RA Warren W.C., Fulton R.S., Bhonagiri V., Zhang X., Hallsworth-Pepin K., RA Clifton S.W., McCarter J.P., Appleton J., Mardis E.R., Wilson R.K.; RT "The draft genome of the parasitic nematode Trichinella spiralis."; RL Nat. Genet. 43:228-235(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. {ECO:0000313|EMBL:EFV50941.1}. 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; ABIR02001865; EFV50941.1; -; Genomic_DNA. DR RefSeq; XP_003369425.1; XM_003369377.1. DR EnsemblMetazoa; EFV50941; EFV50941; EFV50941. DR GeneID; 10912701; -. DR KEGG; tsp:Tsp_04840; -. DR CTD; 10912701; -. DR InParanoid; E5SW97; -. DR KO; K00547; -. DR OMA; SEWCKDG; -. DR Proteomes; UP000006823; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006823}; KW Methyltransferase {ECO:0000313|EMBL:EFV50941.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006823}; KW Transferase {ECO:0000313|EMBL:EFV50941.1}. SQ SEQUENCE 324 AA; 36567 MW; D5A854D1F6BE1294 CRC64; MPLLRGPLVL DGSMATTLIN AGCDYIEWKN LLKNYNIYFC LMNFQLEYVT EFECILFYSS FLKVGADIVQ TNTYQACISR LQDVLGISIR ESYEIVEYAA SLARRSIEHF IEDNGRNINE YYVAGSVGPY AVSLCDGSEY SGRYIQDTAV SEIRKYYHDQ FCAMTMARVD FLALETMPSL TEAKIALEVL SEYNHPPCWV SFSCKDEYRT NYGDLFSDVV YEISRCPGVT AVGINCTKPD FISGLLKQAR NVLMPFVVYP NSGRWTRATG WVEPPYYSKP IGERVQEWIE LGARIIGGCC GVSPMQLAEV SKSVKGPLVQ NCPF // ID E5U874_ALCXX Unreviewed; 1257 AA. AC E5U874; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFV84855.1}; GN ORFNames=HMPREF0005_02521 {ECO:0000313|EMBL:EFV84855.1}, GN LH59_02545 {ECO:0000313|EMBL:AIR49689.1}; OS Achromobacter xylosoxidans C54. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Achromobacter. OX NCBI_TaxID=562971 {ECO:0000313|EMBL:EFV84855.1}; RN [1] {ECO:0000313|EMBL:EFV84855.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C54 {ECO:0000313|EMBL:EFV84855.1}; 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. RN [2] {ECO:0000313|EMBL:AIR49689.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C54 {ECO:0000313|EMBL:AIR49689.1}; RA Hazbon M.H., Riojas M.A., Damon A.M., Alalade R.O., Cantwell B.J., RA Monaco A., King S., Sohrabi A.; RT "Phylogenetic analysis of bacterial species using whole genome RT sequences."; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP009448; AIR49689.1; -; Genomic_DNA. DR EMBL; ACRC01000489; EFV84855.1; -; Genomic_DNA. DR RefSeq; WP_006386874.1; NZ_GL636044.1. DR EnsemblBacteria; AIR49689; AIR49689; LH59_02545. DR EnsemblBacteria; EFV84855; EFV84855; HMPREF0005_02521. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 256 256 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 789 789 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1257 AA; 138447 MW; B1AE99797EB91680 CRC64; MSYPRLPYPP ESFTRGGEFA RQLGQRILIL DGAMGTMIQR YKLGEADFRG ERFAGHGKDL KGDNELLSLV RPDVISEIHR QYLEAGADVI ETNTFGATSI AQGDYDLPEL AYELNLVSAQ LAREACDQYS TPDKPRFVAG ALGPQPKTAS ISPDVNDPGA RNVTFDELRM AYVEQLNGLL DGGIDIVLIE TIFDTLNAKA AIFATEEVFE QRGIRLPVMI SGTVTDASGR ILSGQTVEAF WNSVRHARPV TIGLNCALGA ALMRPYVAEL SKICDTYVCV YPNAGLPNPM AETGFDETPA DTSALLEEFA RAGLVNMSGG CCGTTPDHIR AIADKVAALT PRVVPEIPVK TRLSGLEPLN IDEDTLFVNV GERTNVTGSK MFARLIREEK YDEALAVARQ QVENGAQIID INMDEAMLDS VACMHRFLNL IASEPDIARV PVMIDSSKWD VIETGLKCVQ GKPVVNSISM KEGLEPFRHH ARLCRRYGAA VVVMAFDEQG QADTLERRKE ICGRAYKILV EEEGFPPEDI IFDPNVFAVA TGIDEHNHYA VDFIEGTRWI RENLPHARIS GGVSNVSFSF RGNEPMREAI HTVFLYYAVK EGMTMGIVNA GQLGVYADLD PKLRDLVEDV VLDRAEPVGK TDPADERTPT ERLVQFADSV KGSGAKKEED LAWRNAEVEA RLSHALVHGI TAFIVEDTEE VRQKIAARGG RPIEVIEGPL MDGMNVVGDL FGAGKMFLPQ VVKSARVMKQ AVAHLIPFIE EEKRQIAAAG GDVRAKGKIV IATVKGDVHD IGKNIVSVVL QCNNFEVVNM GVMVPCAQIL EKAKEENADI VGLSGLITPS LEEMAYVASE MQRDEYFRSR KVPLMIGGAT TSRVHTAVKI APNYEGPVIY VPDASRSVGV ATSLMSDQAD AYLAELAEEY EDVRRRHANR KATPILPLAE ARASRPRIDW DSYTPPRPKF IGRRTFKSYD LAEIAKYVDW GPFFQTWSLF GPYPAILEDK VVGEQARKVY ADGQAMMKRI VEGRWLTANG VVGFYPANSV NDEDIEVYKD ESRSEVLFTY RNLRQQGAKR EGVSNKSLSD FIAPKSSGKL DYIGMFAVTA GIGIEKKEAE FEKALDDYSG IMLKSLADRL AEAFAECLHA RVRQDLWGYA PDEALSNDDM IAEKYVGIRP APGYPACPEH VVKTDMFRVL DGADIGMMLT DSYAMFPASS VSGFYFSHPQ SQYFNVGIIG EDQLQDYAAR SGRSIEDLKR TLAPNLG // ID E5UVU6_9BACE Unreviewed; 917 AA. AC E5UVU6; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|EMBL:EFV66737.1}; GN ORFNames=HMPREF9011_02818 {ECO:0000313|EMBL:EFV66737.1}; OS Bacteroides sp. 3_1_40A. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=469593 {ECO:0000313|EMBL:EFV66737.1}; RN [1] {ECO:0000313|EMBL:EFV66737.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_40A {ECO:0000313|EMBL:EFV66737.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFV66737.1}. 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; ACRT01000089; EFV66737.1; -; Genomic_DNA. DR RefSeq; WP_008669919.1; NZ_GL635658.1. DR ProteinModelPortal; E5UVU6; -. DR EnsemblBacteria; EFV66737; EFV66737; HMPREF9011_02818. DR PATRIC; 44631151; VBIBacSp86371_3108. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFV66737.1}; KW Transferase {ECO:0000313|EMBL:EFV66737.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 243 243 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 917 AA; 100896 MW; E97F0983C01F0FDB CRC64; MATLKQLIDE RVLILDGAMG TMIQRYNLSE QDFRGERFAE MPGQMKGNND LLCLTRPDVI KDIHHKYLEA GADIIETNTF NAQRVSMADY HMQDLCREIN LAAAGLAREM ADEYTAKTPH KPRFVAGSVG PTNKTCSMSP DVNNPALRAL TYDELAAAYQ EQMEALLEGG VDALLIETIF DSLNAKAAIY AAETAMKKVG REVPLMLSVT VSDIAGRTLS GQTLDAFLAS VQHAPIFSIG LNCSFGAKQL KPFLEGLAAR APYYISAYPN AGLPNSLGQY DQTPEEMASE VKEYIDEGLV NIIGGCCGTT EEYIAKYQEL IVSGSAWVSP HIPATTPERL WLSGLELLEQ TPEMNFINVG ERCNVAGSRK FLRLINEKKY EEALSIARKQ VEDGALVIDV NMDDGLLDAR EEMTTFLNLV MSEPDIARVP VMIDSSKWEV IEAGLKCLQG KSIVNSISLK EGEEIFIEHA RLIKKLGAAV VVMAFDEKGQ ADTFERKIEV CARAYKILTE QVDFNPHDII FDPNVLAVAT GIEEHDNYAV DFIKATGWIK KNLPGAHVSG GVSNLSFSFR GNNYIREAMH AVFLYHAIRQ GMDMGIVNPA ASVLYTDIPA DVLERIEDVV LNRRPDAAER LIETAEALKR TSTGTEAVKQ DVWREEPMVE KRLQYALIKG IGDHLEEDLA EAVKLYPKAV DIIEGPLMEG MNKVGELFGA GKMFLPQVVK TARTMKKAVA ILQPLIEADK QEGVRSAGKV LMATVKGDVH DIGKNIVSVV MACNNYEIID LGVMVPAEMI VRKAIEEKVD IIGLSGLITP SLEEMAHVAV ELKRAGLDIP IMIGGATTSK LHTALKIAPV YGGPVIHMKD ASQNALVAAR LLNPESSSEF VERLNKEYED LRLKNSVRQV KTVSLEEAQK NKLNLWS // ID E5V2R5_9BACL Unreviewed; 613 AA. AC E5V2R5; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAY-2015, entry version 20. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HMPREF0432_00671 {ECO:0000313|EMBL:EFV35638.1}; OS Gemella morbillorum M424. OC Bacteria; Firmicutes; Bacilli; Bacillales; OC Bacillales Family XI. Incertae Sedis; Gemella. OX NCBI_TaxID=562982 {ECO:0000313|EMBL:EFV35638.1}; RN [1] {ECO:0000313|EMBL:EFV35638.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M424 {ECO:0000313|EMBL:EFV35638.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFV35638.1}. 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; ACRX01000009; EFV35638.1; -; Genomic_DNA. DR RefSeq; WP_004632755.1; NZ_GL622607.1. DR EnsemblBacteria; EFV35638; EFV35638; HMPREF0432_00671. DR PATRIC; 44636533; VBIGemMor7618_0680. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EFV35638.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EFV35638.1}. SQ SEQUENCE 613 AA; 68072 MW; 9EE8314767BE9DFC CRC64; MRNLLERLEK DVLVADGAMG TALYGNGLES CHEYNNISNP DSVEKIHRAY IEAGADIIQT NTYAAKKCQL KTYGYEDKFE EINIKAAEIA RKAAGENTIV FGTIGAIRGL RECELTLETI VKETLDQVKV LLSTDKIDAL LFETYYDQEE IRTVLTEARK LTNLPIITNI SLLEAGITQN GEKVTDALST LVNLGADVVG LNCHLGPYHM IKSLKQVPLF AQSYLSAYPN ASLLQLTQTT HGNEYRFRKN SAYFEQSAKL LVEEGVRLIG GCCGTTPEHI RAIKRGIKNL KPIRRKIITP LPAEEELIRV ANNNPTIVDK AKKQVTIIAE LDPPKHLNID KFIEGAKAID KKNIEAITLA DNSLASTRIC NLATAALLKE HITTPTLLHL TCRDHNLIGL QSRLMGFDLL GINNILAITG DPSKLGDFPG ATSVYDVTSL KLIPFIKQLN DGLGYNGASL KKATNFTVAA AYNPNVRDLS KTKRLVEKKI KSGADYFITQ PVFESDKIVQ LAEFVADYPD TPFFLGIMPI TSYNNAIFLH NEVPGIKLSE DFLAKLEKVK DDKVLCQKVA LEESKKLLDV ALKHFNGIYL ITPFTKYDLT IELIDYIEKN KTK // ID E5VE52_9BACE Unreviewed; 921 AA. AC E5VE52; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 01-APR-2015, entry version 25. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFV24796.1}; GN ORFNames=HMPREF1007_03038 {ECO:0000313|EMBL:EFV24796.1}; OS Bacteroides sp. 4_1_36. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=457393 {ECO:0000313|EMBL:EFV24796.1}; RN [1] {ECO:0000313|EMBL:EFV24796.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=4_1_36 {ECO:0000313|EMBL:EFV24796.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFV24796.1}. 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; ACTC01000115; EFV24796.1; -; Genomic_DNA. DR EnsemblBacteria; EFV24796; EFV24796; HMPREF1007_03038. DR PATRIC; 44645057; VBIBacSp136900_3173. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 243 243 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 765 765 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 921 AA; 100909 MW; 82717613901A42F4 CRC64; MSKLGSLVRE RILILDGAMG TMIQQYNLTE EDFRGERFSQ IPGQMKGNND LLCLTRPDVI QDIHRKYLAA GADIIETNTF SSTRVSMADY HVQDYVREMN LAAVRLARKV ADEFTSLTPD KPRFVAGSVG PTNKTCSMSP DVNNPAFRAL SYDELADAYR EQMEALLEGG VDALLIETIF DTLNAKAAIF AAGQAMETVG VHVPLMLSVT VSDIGGRTLS GQTLDAFLAS VQHADIFSVG LNCSFGARQL KPFLEQLAAR APYYISAYPN AGLPNSLGTY DQTPADMAHE VKEYIHEGLV NIIGGCCGTT DAYIAEYSSL IAGATPHQPV PRPENLWLSG LELLEVKPEN NFVNVGERCN VAGSRKFLRL INEKKYDEAL SIARQQVEDG AQVIDINMDD GLLDAQVEMT TFLHLIASEP EIARVPVMID SSKWEVIVAG LKCLQGKSIV NSISLKEGED KFLEHARTIK QYGAAAVVMA FDEKGQADTY ERKIEVCERA YRLLVDKIGF NPHDIIFDPN VLAVATGMDE HNNYAVDFIR ATGWIRKNLP GAHVSGGVSN LSFSFRGNNY IREAMHAVFL YYAIREGMDM GIVNPAASVL YTDIPADILE RIEDVVLNRR PDAAERLIET AERLKAEAEA AKTSGGERQA AAHSQLAWRE GTPVEERLKY ALTKGIGDYL EEDLAEALKL YPKAVSIIEG PLMAGMNHVG DLFGAGKMFL PQVVKTARTM KRAVAILQPV IESEKEEGAT AAGKVLLATV KGDVHDIGKN XVSVVMACNG YEIIDLGVMV PAETIVQHAI EEKVDMIGLS GLITPSLDEM VHVAIELEKA GLDVPLLIGG ATTSPLHTAL KIAPVYHAPV IHLKDASQNA TVAAKLMNPK TKEELEEELH EKYRQLCEKN REKQVTTVSL EEARKNKLNL F // ID E5VHP2_9FIRM Unreviewed; 199 AA. AC E5VHP2; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 07-JAN-2015, entry version 13. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:EFV17651.1}; GN ORFNames=HMPREF0996_00551 {ECO:0000313|EMBL:EFV17651.1}; OS Lachnospiraceae bacterium 5_1_63FAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=658089 {ECO:0000313|EMBL:EFV17651.1}; RN [1] {ECO:0000313|EMBL:EFV17651.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=5_1_63FAA {ECO:0000313|EMBL:EFV17651.1}; 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. {ECO:0000313|EMBL:EFV17651.1}. 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; ACTS01000010; EFV17651.1; -; Genomic_DNA. DR RefSeq; WP_009264215.1; NZ_GL622402.1. DR EnsemblBacteria; EFV17651; EFV17651; HMPREF0996_00551. DR PATRIC; 44647704; VBILacBac124763_0569. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 2. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFV17651.1}; KW Transferase {ECO:0000313|EMBL:EFV17651.1}. SQ SEQUENCE 199 AA; 22268 MW; 85964D0D12EB083A CRC64; MTLCPHHWKI GGVSLNSKLW TAKILAEQPE LIKQVHKNYF KAGADIILFE TVPSLKEAKV EAEIAEEYGY DYWISFSCLS ENIICEGTPI AECAKTFAKG YPHLKMIGVN CTKPEYIVGL IHKIKENCDI PIGVYPNSGE EYDAVKKVWF GKQSALSFDQ YAYNYMKAGA SAVGGCCTTV AKHVEDVVRA KKQFCKEQK // ID E5VIR5_9FIRM Unreviewed; 791 AA. AC E5VIR5; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 07-JAN-2015, entry version 19. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFV17226.1}; GN ORFNames=HMPREF0996_00926 {ECO:0000313|EMBL:EFV17226.1}; OS Lachnospiraceae bacterium 5_1_63FAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=658089 {ECO:0000313|EMBL:EFV17226.1}; RN [1] {ECO:0000313|EMBL:EFV17226.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=5_1_63FAA {ECO:0000313|EMBL:EFV17226.1}; 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. {ECO:0000313|EMBL:EFV17226.1}. 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; ACTS01000018; EFV17226.1; -; Genomic_DNA. DR RefSeq; WP_009264485.1; NZ_GL622404.1. DR EnsemblBacteria; EFV17226; EFV17226; HMPREF0996_00926. DR PATRIC; 44648541; VBILacBac124763_0957. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFV17226.1}; KW Transferase {ECO:0000313|EMBL:EFV17226.1}. SQ SEQUENCE 791 AA; 86581 MW; 572E30D1200F226E CRC64; MLQNRLGKEL LIFDGAMGTQ LQNAGLSAGD IPEELNIDRP DLLRSIHKNY LKAGADFITT NTFGCNRLKM EEAKYEAKDM LLAAVENARA ARTEAGREDD SYIVLDIGPI GQLLEPMGTL TFDEAYDIIL EQVETVKDQV DLVLFETMSD LYEVKAGVLA VKEHTDLPVF VTMTFEQNGR TLSGNDPETF INVAEGLGVD ALGVNCSLGP DELKPIIDEI LEKASIPVML QPNAGLPCLE HGETHYHVTP EEYVESMKDY MARGAAIVGG CCGTTPEFIG KLAEAAPKAV AERTVEKKTR VSSQTQTVTF GDHVIVCGER LNPTGKKKMK KALLEERYDE LVVEAVKQVE AGAEVLDVNV GLPGIDEPET MKRVVRLLQE VVTLPLQIDS SEADAIENAC RYYNGKPLIN SVNGKDEVME KIFPIAKKYG GVVIGLTLED GIPLKAEERF EIAKKIVNKA AEYGIGKENI IIDCLTLTAS AQQKEVKETL RAIKMVKKEL GVHTVLGVSN VSFGLPNRPL LNRTFLALAM EAGLDLPIIN PLDAELMGTI DAFHVLFYKD VDSQTYIKNQ SKDKETKPAT AAATTNFTLK DVIIHGLKDE VEKVTKEELK DKEALTVINE VIIPALNIVG KDYETGKIFL PQLIQSAETT KKAFEVVKET FSANDGEEKG PIIIATVEGD IHDIGKNIVK VVLESYGYKI IDLGKDVKVE KVVEAYKKYK PKAIGLSALM TTTVASMERT IKALHEAGCS EPIWVGGAVV TEDIAHNIGA DYYTEDAMAA VNLLENEILI L // ID E5VRX1_9FIRM Unreviewed; 784 AA. AC E5VRX1; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFV23443.1}; GN ORFNames=HMPREF1011_00744 {ECO:0000313|EMBL:EFV23443.1}; OS Anaerostipes sp. 3_2_56FAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Anaerostipes. OX NCBI_TaxID=665937 {ECO:0000313|EMBL:EFV23443.1}; RN [1] {ECO:0000313|EMBL:EFV23443.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_2_56FAA {ECO:0000313|EMBL:EFV23443.1}; 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. {ECO:0000313|EMBL:EFV23443.1}. 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; ACWB01000021; EFV23443.1; -; Genomic_DNA. DR RefSeq; WP_009289266.1; NZ_GL629687.1. DR EnsemblBacteria; EFV23443; EFV23443; HMPREF1011_00744. DR PATRIC; 44654626; VBIAnaSp142028_0460. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFV23443.1}; KW Transferase {ECO:0000313|EMBL:EFV23443.1}. SQ SEQUENCE 784 AA; 85819 MW; 0982DFDCC8998138 CRC64; MLLDRIGKDL LIFDGAMGTQ LQEAGLRAGD IPEELNIDRP ELIVSIHEKY LGAGADFITT NTFGCNELKM QESKYEYRDM LRAAVSNANE ARKNAGREQD AYIVLDIGPI GQLLEPMGTL TFDEAYDIIL SQVETVKHDV DAVLFETMSD LYEVKAGILA VKENTSLPVF VTMTFEQNGR TLSGNDPVTF VNTVQGLGAD MLGVNCSLGP AELGPIIEEI LSVSSVPVMI QPNAGLPCLE HGETHYHVTS DEYAELMQGY LKDGISAAGG CCGTTPEFIR KLKAAAPKKA APRKIEKKTR VSSQTKTVTF GDRVIVCGER LNPTGKKKLK LALKEERYDE LVSEAIKQDE AGADVLDVNV GLPGIDEPET MKHVVKLLQE VITLPLQIDS SNARAIELAC RYYNGKPLIN SVNGKDEVME AIFPIVKKYG GVVIGLTLDE GIPLKAEERF EIAQKIIAKA AEYGIGKEDI IIDCLTLTAS AQQKEVKETL KAIEMVKKLG VHTVLGVSNV SFGLPNRPLL NRTFLALAMQ AGLDLPIINP LDKELMGTID AFHVLFYKDI DSESYIRNQS NAAETKAAVQ TEFSLHDIIL HGLKDEVEAK TREELEKKEP LVLINEVIIP ALNVVGKDYE TGKIFLPQLI QSAETTKKAF EVVKQCFTAD AGEEKGPVVM ATVEGDIHDI GKNIVKVVLE SYGYRIIDLG KDVKIEKVAE AWKKYQPKAI GLSALMTTTV ISMEKTIQRL REEDCSCPIW VGGAVLTEDI ANSIGADYYA EDAMASVALL EKLI // ID E5WMP6_9BACI Unreviewed; 430 AA. AC E5WMP6; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFV76093.1}; GN ORFNames=HMPREF1013_03731 {ECO:0000313|EMBL:EFV76093.1}; OS Bacillus sp. 2_A_57_CT2. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=665959 {ECO:0000313|EMBL:EFV76093.1}; RN [1] {ECO:0000313|EMBL:EFV76093.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=2_A_57_CT2 {ECO:0000313|EMBL:EFV76093.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFV76093.1}. 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; ACWD01000055; EFV76093.1; -; Genomic_DNA. DR EnsemblBacteria; EFV76093; EFV76093; HMPREF1013_03731. DR PATRIC; 44678737; VBIBacSp146025_4399. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; SQ SEQUENCE 430 AA; 47160 MW; C42914E90C3ECD55 CRC64; MHKPSLQEQI KKKILIMDGA MGTMLQRADL TAADFGGEEY EGCNENLNIT APSVIEHIHL EYLKAGADII ETNTFGATSI VLADYDLEEK AYELNKIAVE IAREAADRIS TPEWPRYVAG AMGPTTKTLS VTGGSTFEEM IAAYEEQARG LIDGGADLLL LETSQDMLNV KAGFIGIENA SKKTGIKLPL IVSGTIEPMG TTLAGQSIEA FYISLEHMKP LAVGLNCATG PEFMQDHIRS LSGLASTAVS CYPNAGLPDE EGQYHETPES LARKLEGFAK EGWLNIVGGC CGTTPEHIQA IAESVKDYKP RNYEGNSVHK VSGIEPLIYD DPTLRPIMVG ERTNVIGSRK FKRLIAEGKF EEAAEIGRAQ VKGGAHVIDI CLADPDREEM QDVENFIKEL VKKLRFRWSL IQLMKRLSRR PSPIHRVKPS // ID E5WMP7_9BACI Unreviewed; 616 AA. AC E5WMP7; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 07-JAN-2015, entry version 21. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HMPREF1013_03732 {ECO:0000313|EMBL:EFV76094.1}; OS Bacillus sp. 2_A_57_CT2. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=665959 {ECO:0000313|EMBL:EFV76094.1}; RN [1] {ECO:0000313|EMBL:EFV76094.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=2_A_57_CT2 {ECO:0000313|EMBL:EFV76094.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFV76094.1}. 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; ACWD01000055; EFV76094.1; -; Genomic_DNA. DR RefSeq; WP_009334538.1; NZ_GL635754.1. DR EnsemblBacteria; EFV76094; EFV76094; HMPREF1013_03732. DR PATRIC; 44678739; VBIBacSp146025_4400. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 616 AA; 67613 MW; 689D63BEC1F3216B CRC64; MSFLNKLKNE IIIADGAMGT LLYSYGTDSC FEELNLSQSE QIQHIHEAYI GAGAELIQTN TYAANYLKLQ RYGLEDSVKE INSAAARIAK KAAKERAYVA GTIGGIRGFK PNMITLEEIK RSFREQLYCL LLENVDGILL ETYYDLEELE TVLAIARKET DLPIIAQVSL QEAGVLQNQT SIADALAKLE GIGADVVGIN CRLGPHHMLK TLESVPLPKH AYLSAYPNAS IPAYTDGKFH YEGDAEYFRQ SAIEFRNQGV RLLGGCCGTT PDHIKAFSDV LKGLPPIEEK ETKAINKVMV SEKPSSSREL PPLQDIVRER PSVIVELDPP RKLDTSRFFE GAKALKEAGI DSITLADNSL ASPRVCNSAL GYLVKQQTGL RPLVHVTCRD RNIIGLQSHL MGLHALGLND ILAVTGDPAR VGDFPGASSV YDVSSFELIS MIKQLNEGLS FSGKDLGQKA AFSVAGAFNP NVRSLEKAVG RLEKKIEHGA DYFISQPVFS EEKLLEVHEA VKDLKAPVYI GLMPLTGSRN AEFLHNEVPG IKISDSIRNR MASLKDDPAQ AGAEGIAIAK SLIDAAAELF NGIYLITPFM RYEMTVELSN YARETTERLS RRKQHA // ID E5WU14_9BACE Unreviewed; 923 AA. AC E5WU14; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 29-APR-2015, entry version 25. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFV31658.1}; GN ORFNames=HMPREF1016_00165 {ECO:0000313|EMBL:EFV31658.1}; OS Bacteroides eggerthii 1_2_48FAA. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=665953 {ECO:0000313|EMBL:EFV31658.1}; RN [1] {ECO:0000313|EMBL:EFV31658.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_2_48FAA {ECO:0000313|EMBL:EFV31658.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFV31658.1}. 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; ACWG01000002; EFV31658.1; -; Genomic_DNA. DR EnsemblBacteria; EFV31658; EFV31658; HMPREF1016_00165. DR PATRIC; 44683864; VBIBacEgg142087_0178. DR GO; GO:0000786; C:nucleosome; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000558; Histone_H2B. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SMART; SM00427; H2B; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 243 243 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 767 767 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 923 AA; 100984 MW; 4F1B7E8B53271352 CRC64; MSRLEGLVRE RILILDGAMG TMIQQYNLTE EDFRGERFAQ IPGQLKGNND ILCLTRPDVI RDIHRKYLAA GADIIETNTF SSTSVSMADY HVQDYVREIN LAAVKLAREV ADEFTALTPD KPRFVAGSVG PTNKTCSMSP DVNNPAFRAL TYDELVIAYR EQMEAMLEAG VDALLIETIF DTLNAKAAIY AAKQAMNVAG IRVPLMLSVT VSDIAGRTLS GQTLDAFLAS VQHADIFSIG LNCSFGARQL KPFLEQLAAR APYYVSAYPN AGLPNSLGTY DQTPAEMAAE IKEYIHEGLV NIVGGCCGTT DEYIAAYSSL IDGVVPRIPV GKPDCLWLSG LELLEVRPEN NFVNVGERCN VAGSRKFLRL INEKKYDEAL SIARQQVEDG AQVIDINMDD GLLDAEQEMT TFLHLIASEP EIARVPVMID SSKWDVIVAG LKCVQGKSIV NSISLKEGEE TFLEHARTVK EYGAAAIVMA FDERGQADTY ERRIEVCERA YRLLVDKVGF NPHDIIFDPN VLAVATGMDE HNNYAVDFIR ATGWIRKNLP GAHVSGGVSN LSFSFRGNNY IREAMHAVFL YHAIREGMDM GIVNPATSVL YTDIPADILE RIEDVVLNRR ADAAERLIET AERLKAEADA AKVSASNGDS QLSASGSRFQ WREGAVEERL KYALTKGVGD YLEEDLAEAL NAYPKAVDII EGPLMAGMNH VGDLFGAGKM FLPQVVKTAR TMKKAVAILQ PVIESEKQAG AASAGKVLLA TVKGDVHDIG KNIVAVVMAC NGYEIIDLGV MVPAETIVQR AIEEKADMIG LSGLITPSLD EMVHVAMELE KAGLDIPLLI GGATTSPLHT ALKIAPVYHA PVVHLKDASQ NASIAARLMN PNQKEELAKN LFTEYQRLRE KNQERQVETV SLEEAKANRL KLF // ID E5XE64_9FIRM Unreviewed; 826 AA. AC E5XE64; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFV20412.1}; GN ORFNames=HMPREF1026_00417 {ECO:0000313|EMBL:EFV20412.1}; OS Lachnospiraceae bacterium 8_1_57FAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=665951 {ECO:0000313|EMBL:EFV20412.1, ECO:0000313|Proteomes:UP000003339}; RN [1] {ECO:0000313|EMBL:EFV20412.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=8_1_57FAA {ECO:0000313|EMBL:EFV20412.1}; 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 8_1_57FAA."; 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. {ECO:0000313|EMBL:EFV20412.1}. 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; ACWQ01000009; EFV20412.1; -; Genomic_DNA. DR RefSeq; WP_004844944.1; NZ_GL622449.1. DR ProteinModelPortal; E5XE64; -. DR EnsemblBacteria; EFV20412; EFV20412; HMPREF1026_00417. DR PATRIC; 44699182; VBILacBac145843_0798. DR Proteomes; UP000003339; Unassembled WGS sequence. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000003339}; KW Methyltransferase {ECO:0000313|EMBL:EFV20412.1}; KW Transferase {ECO:0000313|EMBL:EFV20412.1}. SQ SEQUENCE 826 AA; 90755 MW; A9D2C7AB0EC769C4 CRC64; MIRQRLGKDL LFFDGGMGTL LQEKGLAPGE LPETWNLTHS EEIYKIHRQY IEAGSDIILT NTFGANALKF HDDSCSLEEI IKAAVSHVKK AEREALLQTG DERKIYTALD VGPTGKLLKP MGDLEFETAY EAFKEVVILG EQAGADLIHI ETMSDTYELK AAVLAAKENT SLPVFATVIF DERKKLLTGA DVSSVVALLE GLGVDALGIN CAMGPKEMLP VLEELIKYSS VPIIVKPNAG LPKQRDGKTY YDVTEDEFAA YMEQIVRMGA CVIGGCCGTT PEHIRAMRKR CENAELVPVT EKEFTVVSSY GQSVILGEGS KIIGERINPT GKKRFKQALK EHDLDYILRE GITQQDQGAH ILDVNVGLPD IDEPALMEEV VQELQSVVNI PLQIDTVDEK AMEKALRIYN GKAMVNSVSG KKESMEKVFP LVKKYGGVVI GLTLDEDGIP ADADGRVRIA EKIIKTAEKF GIKKKDIVID ALAMTISSEP EGAKVTLETL RRLRDEIGVN TVLGVSNISF GLPCRPIVNA AFYTMAMLNG LSAGIINPSS EDMMKSWYAY HALMNLDNNC EQYIQKYANS VVSTNIMKTS ELSETKLKGE NDRSRKSSSK MTLQEAIEKG LRDDAGKITT DMIATEAPLD IINEELIPAL NHVGDGFEKG TVFLPQLLMS AEAAKSAFSV LKEKMEKSGE IREKKGRVIL ATVKGDIHDI GKNIVKVLLE NYSFDVIDLG KDVSPEKIVE TACEKQVPLV GLSALMTTTV VSMEETIKML REKKPDCKVM VGGAVLNQEY ADMIGADFYG KDAMQSVHYA EKIFKDALQK SADKKE // ID E5Y8U3_BILWA Unreviewed; 805 AA. AC E5Y8U3; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|EMBL:EFV43585.1}; GN ORFNames=HMPREF0179_02601 {ECO:0000313|EMBL:EFV43585.1}; OS Bilophila wadsworthia 3_1_6. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Bilophila. OX NCBI_TaxID=563192 {ECO:0000313|EMBL:EFV43585.1}; RN [1] {ECO:0000313|EMBL:EFV43585.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_6 {ECO:0000313|EMBL:EFV43585.1}; 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] {ECO:0000313|EMBL:EFV43585.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_6 {ECO:0000313|EMBL:EFV43585.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFV43585.1}. 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; ADCP02000001; EFV43585.1; -; Genomic_DNA. DR RefSeq; WP_005028530.1; NZ_KE150238.1. DR EnsemblBacteria; EFV43585; EFV43585; HMPREF0179_02601. DR PATRIC; 44721521; VBIBilWad76794_2832. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFV43585.1}; KW Transferase {ECO:0000313|EMBL:EFV43585.1}. SQ SEQUENCE 805 AA; 84926 MW; 7326F236CED5FEA1 CRC64; MADFRSALAS GRTLLLDGGM GTMLQARGLP AGEHPEQFCL DRPDVLRGIH ADYLAAGADI ILTCTFGGSR LKLPAGIDVT PFNRTMARIA RAAVDAAGRE AFVAGDMGPC GQFVRPLGDL HPLELYEALR EQARGLVEGG VDLFLIETQF DLAEVRIAVA AIRAESDLPI MVSMTFEQGT SLTGTTPEIF AETMQNLGVD ALGLNCGLGP EQMAPLMERF LACSSVPVLA EPNAGLPELV DGKTVFRLPP EPFAEKTAAF VGMGARLVGG CCGTTPDHIA ALRRAVDAVG PCPAPAVTPS GIVLTTRTRL VRVSPAEPFK IIGERINPTG KKDLQAELQA GEYGLAMRFA SEQVALGAPI LDVNVGAPMV DEALLLPELV QRLTGKYAEP LSLDSSHAEA IAAALPFCPG SPLVNSISGE ADRMEHLGPL CRQWGAPFIL LPIQGRKLPV KAADRIAIIE NMLDKAAMLG IPRRLVLVDV LALAVASKAE AAREGLETIR WCAAHGLATT IGLSNISFGL PARELVNTTF LSMAMGAGLS SCIANPSSGR LREAKAAGDV LMGHDRDAAA FVNGYAMWTP GNGGTADAAA FARATAQTVE EAVILGDRES VVGLVEKELE AGADPFELVR GRLIPAITEV GSKYERREYF LPQLLRSAET MQTAFARLKP LLEREANAEA QKIIVVATVE GDIHDIGKNI VSLMLGNHGF KVVDLGKDVK AEAIVEAAVA HKADLIGLSA LMTTTMVRMR DTVDLVKQRG LGVDVMVGGA VVTPAFAESI GANYSSDAVD AVRLAKSLIA ARKNQ // ID E5YJ87_9ENTR Unreviewed; 1227 AA. AC E5YJ87; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 01-APR-2015, entry version 24. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFV39693.1}; GN ORFNames=HMPREF0864_02598 {ECO:0000313|EMBL:EFV39693.1}; OS Enterobacteriaceae bacterium 9_2_54FAA. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae. OX NCBI_TaxID=469613 {ECO:0000313|EMBL:EFV39693.1}; RN [1] {ECO:0000313|EMBL:EFV39693.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=9_2_54FAA {ECO:0000313|EMBL:EFV39693.1}; 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 Sibley C., Haas B., Nusbaum C., Birren B.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EFV39693.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=9_2_54FAA {ECO:0000313|EMBL:EFV39693.1}; RG The Broad Institute Genomics Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Allen-Vercoe E., RA Ambrose C., Strauss J., Sibley C., Walker B., Young S.K., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., RA 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 Enterobacteriaceae bacterium 9_2_54FAA."; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFV39693.1}. 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; ADCU02000001; EFV39693.1; -; Genomic_DNA. DR RefSeq; WP_008814713.1; NZ_ADCU02000001.1. DR EnsemblBacteria; EFV39693; EFV39693; HMPREF0864_02598. DR PATRIC; 44729574; VBIEntBac91544_2725. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135698 MW; 7416CE2D0EA86EAB CRC64; MSTTVERLRH QLSQRILVLD GGMGTMIQGY RLTEEDFRGD RFADWQSDLK GNNDLLVLTK PDIISAIHYD YLEAGADILE TNTFNSTRIA MADYHMESLS AEINYEAARL ARACADEWTA RTPNKPRYVA GVLGPTNRTA SISPDVNDPA FRNISFDQLV EAYRESTRAL VEGGVDLIMI ETIFDTLNAK AAIYAVETEF EAMGVELPVM ISGTITDASG RTLSGQTTEA FYNSLRHVKP LTFGLNCALG PDELRQYVAE LSRIAECFVT AHPNAGLPNA FGEYDLGPKE MAEHIAEWAQ AGFLNIVGGC CGTTPAHIAA ISRAVDGVKP RALPDIPVAC RLAGLEPLTI DANTLFVNVG ERTNVTGSAK FKRLIKEDKY AEALEVALQQ VESGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGEDKFIEHA RKVRRYGAAM VVMAFDEVGQ ADTRARKIEI CRRAYKLLTE TVGFPPEDII FDPNIFAVAT GIEEHNNYAV DFIEACADIK AELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPT DLRDAVEDVI LNRREDGTER LLDLAEKYRG SKSDDDSNKP QAEWRSWPVK KRLEYSLVKG ITEFIEADTE EARLEAERPI EVIEGPLMDG MNVVGDLFGD GKMFLPQVVK SARVMKQAVA YLEPFIEASK EKGTSAGKVL LATVKGDVHD IGKNIVGVVL QCNNYEIIDL GVMVPCDKIL KTAREQNVDI IGLSGLITPS LDEMVYVAKE MERQGFDLPL LIGGATTSKA HTAVKIEQNY SGPTTYVSNA SRTVGVVAAL LSPTQKPDFV ARTRKEYETV RIQHGRKKPR TPPVSLEAAR ENATSLDWSD YTPPVPHRLG VHQVTASIDT LRNYIDWTPF FMTWSLAGKY PRILEDEVVG EEAKRVFADA NAMLDDLASS GKLNPRGVYG IFPANRVGDD VEIYSNEFRD EVLVTGHHLR QQTEKTDFAN YCLADFVAPK SSGKSDYIGA FAVTGGLEED ALADAYEAQH DDYNKIMVKA LSDRLAEAFA EYLHEKVRKV YWGYAANENL SNEELIRENY QGIRPAPGYP ACPEHTEKAA IWTLLDAENT VGMKLTESYA MWPGASVSGW YFSHPESKYF AVAQIQRDQV EDYAQRKGMP VAEVERWLAP NLGYDAD // ID E6B3R4_ECOLX Unreviewed; 1227 AA. AC E6B3R4; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFU97988.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFU97988.1}; GN Name=metH {ECO:0000313|EMBL:EFU97988.1}; GN ORFNames=EC3431_2206 {ECO:0000313|EMBL:EFU97988.1}; OS Escherichia coli 3431. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=670892 {ECO:0000313|EMBL:EFU97988.1}; RN [1] {ECO:0000313|EMBL:EFU97988.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=3431 {ECO:0000313|EMBL:EFU97988.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; ADUM01000089; EFU97988.1; -; Genomic_DNA. DR RefSeq; WP_000096006.1; NZ_ADUM01000089.1. DR EnsemblBacteria; EFU97988; EFU97988; EC3431_2206. DR PATRIC; 47867067; VBIEscCol139805_2287. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFU97988.1}; KW Transferase {ECO:0000313|EMBL:EFU97988.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135967 MW; 4F820DCAF3A4B1D6 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEAGIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAD // ID E6BLY7_ECOLX Unreviewed; 1227 AA. AC E6BLY7; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFU34638.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFU34638.1}; GN Name=metH {ECO:0000313|EMBL:EFU34638.1}; GN ORFNames=HMPREF9350_03405 {ECO:0000313|EMBL:EFU34638.1}; OS Escherichia coli MS 85-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=679202 {ECO:0000313|EMBL:EFU34638.1}; RN [1] {ECO:0000313|EMBL:EFU34638.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 85-1 {ECO:0000313|EMBL:EFU34638.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFU34638.1}. 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; ADWQ01000015; EFU34638.1; -; Genomic_DNA. DR RefSeq; WP_000096053.1; NZ_ADWQ01000015.1. DR EnsemblBacteria; EFU34638; EFU34638; HMPREF9350_03405. DR PATRIC; 47936913; VBIEscCol146587_3143. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFU34638.1}; KW Transferase {ECO:0000313|EMBL:EFU34638.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136040 MW; D1A76336C7330E3D CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID E6J8H1_9ACTO Unreviewed; 1186 AA. AC E6J8H1; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Putative 5-methyltetrahydrofolate:homocysteine S-methyltransferase {ECO:0000313|EMBL:EFV92098.1}; GN ORFNames=ES5_07599 {ECO:0000313|EMBL:EFV92098.1}; OS Dietzia cinnamea P4. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Dietziaceae; Dietzia. OX NCBI_TaxID=910954 {ECO:0000313|EMBL:EFV92098.1}; RN [1] {ECO:0000313|EMBL:EFV92098.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=P4 {ECO:0000313|EMBL:EFV92098.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFV92098.1}. 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; AEKG01000145; EFV92098.1; -; Genomic_DNA. DR RefSeq; WP_007629266.1; NZ_AEKG01000145.1. DR EnsemblBacteria; EFV92098; EFV92098; ES5_07599. DR PATRIC; 46573946; VBIDieCin172986_1408. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFV92098.1}; KW Transferase {ECO:0000313|EMBL:EFV92098.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 230 230 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 296 296 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 297 297 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 740 740 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1186 AA; 128945 MW; 744339C2ABFED8B0 CRC64; MSVDFDSPLL DAARRRVLIG DGAMGTMLQA VDLDVDEDFL GLEGCNEILN ATRPDVVEGI HRAFFEAGAD LVETNTFGCN LSNLGDYDIV DRIGELAEKG AAIARRVADE IGPSEDGTPR MVLGSLGPGT KLPSLGQTTF EDIRDAYSKA AEGLARGGAD AYLIETSQDL LQVKAAVLGC QDGMAAAGRR LPIISHVTIE TTGTMLLGSD IGAALTALQP LGIDMIGLNC ATGPAEMVEH LRYLSRHAEI PVSVMPNAGL PELGEHGAVY PLGAEEFGPQ VADFVSEFGL SMVGGCCGTT PEHITRLKEQ VSARTRAERT VEPVNAVASL YSSTPLRADA GIIMIGERTN ANGSKRFREA MLASDWDTCM DIAKEQMRDG AQMVDLCVDY VGRDGSGDMA ELAGRMATSS TLPIMLDSTE PEVIRAGLEK LGGRCAVNSV NYEDGAGPDS RFQRIMRLVS RHGAAVVGLT IDEEGQARTA DRKVEIAERL IADLTGNWGM AEEDIIIDCL TFPISTGQEE VRRDGIETIE AIRRLTEAHP RIHTTLGLSN ISFGLNPAAR QVLNSVFLHE CVQAGLDSAI AHSSKILPMS KIDDRQREVA LDLVYDRRRE GYDPLQVFME LFEGVSAAGA KNARAAELAA MPLMERLAAR IVDGERKGLE EDLDAAMVEI PPLEIINEHL LGGMKTVGEL FGSGQMQLPF VLQSAETMKA AVAHLEPHME ASDEDGKGRI VLATVKGDVH DIGKNLVDII LSNNGYDVVN IGIKQPISEI ISAAREHKAD VIGMSGLLVK STVVMKDNLA ELNSEGIAGE FPVLLGGAAL TRSYVEVDLA EMYQGDVFYA RDAFEGLRLM DEVMTAKRTG VPMAQSSEAA AKAAERRERR ARSERIAAKR AAEAEPVVIP ERSDVAADQP IATPPFWGTR IAKGIPVADY LGHLDERALY FGQWGLRGTR SGEGPDYDEL VETEGRPRMR AWIDRLTTEG ILSHSAVVYG YFPAYSVGDE IWVLAEPRPD AEVLHKIAFP RQQRSRFLAI PDFVASRERC EAEGTVDVLP FQLVTMGSPI ADFANELFAG DNYRDYLEVH GLSVQLTEAL AEFWHRRVRD ELTLPDGSVS DEDPDSIQDY FNLKYRGARY SFGYGACPDL ESRKVVVDLL EPERIGVVLS EELQLHPEQS TDAFVLYHPE AKYFNV // ID E6K7A7_9BACT Unreviewed; 932 AA. AC E6K7A7; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFU30474.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFU30474.1}; GN Name=metH {ECO:0000313|EMBL:EFU30474.1}; GN ORFNames=HMPREF6485_1753 {ECO:0000313|EMBL:EFU30474.1}; OS Prevotella buccae ATCC 33574. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=873513 {ECO:0000313|EMBL:EFU30474.1, ECO:0000313|Proteomes:UP000003112}; RN [1] {ECO:0000313|EMBL:EFU30474.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33574 {ECO:0000313|EMBL:EFU30474.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFU30474.1}. 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; AEPD01000028; EFU30474.1; -; Genomic_DNA. DR RefSeq; WP_004345847.1; NZ_GL586311.1. DR EnsemblBacteria; EFU30474; EFU30474; HMPREF6485_1753. DR PATRIC; 45074515; VBIPreBuc167547_1143. DR OrthoDB; EOG6091CH; -. DR Proteomes; UP000003112; Unassembled WGS sequence. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000003112}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFU30474.1}; KW Transferase {ECO:0000313|EMBL:EFU30474.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 241 241 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 774 774 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 932 AA; 102257 MW; AADD24BE3E906BEA CRC64; MKTIQELVKE RILILDGAMG TMIQNYHLTE EDFRGELFRR QPGVMKGNND MLNITRPDVV KDIFRQYIEA GADIITTNTF SSQRISQADY LLEDYVGEMA LQGARIAREV ADEYASEKHP CFVAGSVGPT NKTCSMSPDV SNPAARNLTY DQLFDAYCEQ IDGLVEGGVD VILIETIFDT LNAKVAIDAA LTIMARREVE LPIMLSLTIA DLAGRTLSGQ TIEAFLASVS SYPIFSVGLN CSFGAPQMKP FLEQMAKVAP YYVSVYPNAG IPNELGLYDE TAGTMAPQIG DFVNEGLVNF VGGCCGTTPE FIAAYRPFVE GKTPRRVPSP TRRMCLSGLD VLVPLDNIPG EDEQAAISGF TNIGERCNVA GSRKFLRLIK EKQYEEAVAI ARKQVDDGAL ILDINMDDGL LDAKAEMVNF LNMIASDPDI ARVPVMIDSS KWEVIVAGLK CVQGKSIVNS ISLKEGEEQF LAHARDIKRY GAACVVMCFD EQGQATTFDR RIEIAQRAYD LLTRKVGIQP QDIIFDPNVL AIATGMEEHD DYAMDFIRAT RWIKEHLPGA HVSGGVSNLS FSFRGNNYIR EAMHAVFLYH AISNGMDFGI VNPSAKITYA DIPQAELEVM EDVVLNRRRG AGEDLIALAQ RILDVKTVAT EGPQKGSDTS GTNGTPEWRS TPLDERLEYA LRKGVADFLE EDLREAMDEY SKAVDIIEGP LMHGMNVVGE LFGAGKMFLP QVVKTARTMK RAVAILQPAI EAERREGATK AGKVLLATVK GDVHDIGKNI VSVVMSCNNY EVIDMGVMVP ADQIVKKAVA EHVDIIGLSG LVTPSLDEMV NVATELHKAG LHVPIMIGGA TTSKLHVALK IAPVYSGPVI WMKDASQNPI VASKLLNKTE KKSFAQKLNA DYEKLREGYH QEQDKLASIE DARKNKLNLF DS // ID E6KY17_9PAST Unreviewed; 1229 AA. AC E6KY17; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFU67730.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFU67730.1}; GN Name=metH {ECO:0000313|EMBL:EFU67730.1}; GN ORFNames=HMPREF9064_1049 {ECO:0000313|EMBL:EFU67730.1}; OS Aggregatibacter segnis ATCC 33393. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Aggregatibacter. OX NCBI_TaxID=888057 {ECO:0000313|EMBL:EFU67730.1}; RN [1] {ECO:0000313|EMBL:EFU67730.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33393 {ECO:0000313|EMBL:EFU67730.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFU67730.1}. 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; AEPS01000005; EFU67730.1; -; Genomic_DNA. DR RefSeq; WP_006718438.1; NZ_GL622200.1. DR EnsemblBacteria; EFU67730; EFU67730; HMPREF9064_1049. DR PATRIC; 45092044; VBIAggSeg171182_1564. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFU67730.1}; KW Transferase {ECO:0000313|EMBL:EFU67730.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 757 757 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1229 AA; 136281 MW; 053B39174A850350 CRC64; MKNTTEILKN ALAQRILILD GAMGTMIQKY KLTEADFRGE RFAESAVDLR GNNDLLTLTQ PLLISAIHEK YLEAGADIIE TNTFSSTTIA QADYDLQSIA YELNFAGAKL ARLAADKYST PEKPRFVAGI LGPTNRTASI SPNVNDPGFR NVTFMELVDA YSEATRGLIE GGADLIMIET IFDTLNAKAA VFAIETVFEE LGVELPIMIS GTITDASGRT LSGQTTEAFY NSLRHAKPLT FGLNCALGPK ELRQYVEQLS KISETYVSVH PNAGLPNAFG GYDLGAEDMA AHLKEWAESG FVNIIGGCCG TTPEHIKAFA EAVENIPPRK LPQIKTAMRL SGLEPLNIDD ESLFVNVGER NNVTGSAKFK RLIKEDKFAE AIEIAIDQVE NGAQVIDVNM DEALLDGKKC MTRFLNIMAT EPDAAKVPVM IDSSKWEVIE AGLQSVQGKP IVNSISLKEG EEIFIEHAKL VRKYGAAVVV MAFDEVGQAD TEDRKVEICT RAYNILVNQL GFPPEDIIFD PNIFAIGTGI EEHNNYGVDF INATGRIKRS LPHAKISGGV SNVSFSFRGN NVMREAIHAV FLYHAIKQGM DMGIVNAGQL AIYDDLDPEL RNVIEDAVLN RTPDGTERLL DIAEKYRNQG NDESAVDSVA EWRTWPVEER LKHALVKGIT THIIEDTEEA RQKLPTPLEV IEGPLMAGMD VVGDLFGDGK MFLPQVVKSA RVMKQSVAYL EPFINATKQK GSSNGKVVIA TVKGDVHDIG KNIVSVVLQC NNFEVIDLGV MVPADKIIQT AIDEKADLIG LSGLITPSLD EMEYFLGEMT RLGLNLPVLI GGATTSKEHT AIKLYPKYKQ HGVFYTSNAS RAVTVCATLM NPEGRAALWE QFKKDYEKIQ QSFANRKPLR KQLSIEEARA NRFDGFNGEW ADYVPPTPKQ TGIVEFKNVP IAELRKFIDW SPFFRVWGLM GGYPDAFAHP ESGEEARRVW NDAQAMLDAF EQNHKLNPSG VLGIFPAERV DDDVVLFSDE DRTQSIGTAY GLRQQTERGK NSKSQFNFAL SDFIADRESG KKDWMGMFAV CAGIEEMELV EGYKAAGDDY NAILLQAVGD RLAEAMAEYL HFELRTRIWG YTQEEFDNQG LINENYVGIR PAPGYPSCPE HTEKALIWDL LEVEQRIGMK LTESYAMWPA ASVCGWYFTH PASNYFTLGR IDEDQAQDYA KRKGWDEREM MKWLGVAMK // ID E6L173_9PROT Unreviewed; 1159 AA. AC E6L173; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFU70947.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFU70947.1}; GN Name=metH {ECO:0000313|EMBL:EFU70947.1}; GN ORFNames=HMPREF9401_0199 {ECO:0000313|EMBL:EFU70947.1}; OS Arcobacter butzleri JV22. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Arcobacter. OX NCBI_TaxID=888827 {ECO:0000313|EMBL:EFU70947.1}; RN [1] {ECO:0000313|EMBL:EFU70947.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=JV22 {ECO:0000313|EMBL:EFU70947.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFU70947.1}. 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; AEPT01000006; EFU70947.1; -; Genomic_DNA. DR RefSeq; WP_004510159.1; NZ_GL622206.1. DR EnsemblBacteria; EFU70947; EFU70947; HMPREF9401_0199. DR PATRIC; 45096256; VBIArcBut170584_1391. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFU70947.1}; KW Transferase {ECO:0000313|EMBL:EFU70947.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 223 223 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 728 728 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1159 AA; 129408 MW; B2ED59FCCD57A04C CRC64; MEELIKNLID KRVLIIDGAM GTQLQIADIK KEEWFFEDLD LEGCNELLNL TAPHILETIH DNYAKAGADL ISTNTFGSMP WVLDEYNIGH MSYELSKLGA SLVKKSCEKF STPEKPRFCL ASIGPGTKLP SLGHIKYDEM YEGYKIMAKG LVDGGTDIFL LETCQDPLQI KAALHALNDV APNIPIMVSV TIELSGTMLI GTDAMTIAAI MAPFNILSLG FNCGTGPVQV HKHVKTLSQV CKFPISVHSN AGLPQNRGGK TYYPMQPEEF TALQKEFLKI NGVSFLGGCC GTTPEHIEAL AKAVENEVPL KPCGFLKASL ASLFNIVPLK QEPAPLLIGE RSNATGSKAF RELLKANDYE GTLSVAQQQV RAGAHVIDVS VGFAGRDERF DMDEVVSLYS QKIALPLMPD STQILALEAA LKQIGGRCII NSVNLEDGIE KFDAVCSLAK KFGAALVCLV IDEIGMAKSK ERKLEVAERI FDLCVNRHGF DPADLVFDML TFTIGSGDDE YRTAGIETLE AIREFEIRHP EVGTTLGLSN ISFGLATNAR IYLNSIYLDH CVKAGLTSAI VNVKHILPLN KISEEDKKAC DNLIFNIWEN GADPLFAFIE HFSNVEGQEE QSDEEYQKLE PIEKVKKLLL DGDKERLIPL ALELRHTISP EIIVNEWLID GMKVIGELFG SGQMQLPFVL QSAETMKACV DSLNPYLPKQ EKASETTLIL GTVKGDVHDV GKNLVDIILS NNGFKVVNVG IKADLGQFVE ELNKHNAHAI GMSGLLVKST AVMKENLEEL QKLGIKVPVL LGGAALTKNF VDEYCRTIYD GPIFYCRDAF DGVVSMQRIE KGDENNTALA ADLIERIDTS DRVEKEEIEI PPYEEISMPE RGKFVFPPIW DRVTKRGEKL NKELIFKWIN HRVLFRQRWG YKRGKQTPEA FMKYERDVVE PTYEALKAEL VDKDIFDPIA IYAYYPCISF DNKLYIFDKK YLFNSLEESK NIPPLSEAIK VLEFPRQKRK PFRCIPDFFA NDRLDVVAFT LASAGLKITD YERSLYDNGE FTKYYQVHGL GVELAEALAE VLHKQIRLDL DIVPNEGHTL NDVQMKQYVG CRYSPGYAAC PDLAMNRDIF DLLNPEEFGI ELSETFQMHP EQTTCAIVVT NPEANYYNV // ID E6LQ59_9FIRM Unreviewed; 590 AA. AC E6LQ59; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAY-2015, entry version 18. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HMPREF0381_2094 {ECO:0000313|EMBL:EFU75978.1}; OS Lachnoanaerobaculum saburreum DSM 3986. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Lachnoanaerobaculum. OX NCBI_TaxID=887325 {ECO:0000313|EMBL:EFU75978.1}; RN [1] {ECO:0000313|EMBL:EFU75978.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 3986 {ECO:0000313|EMBL:EFU75978.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFU75978.1}. 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; AEPW01000082; EFU75978.1; -; Genomic_DNA. DR RefSeq; WP_008751858.1; NZ_GL622296.1. DR EnsemblBacteria; EFU75978; EFU75978; HMPREF0381_2094. DR PATRIC; 45111113; VBIEubSab170007_2290. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EFU75978.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EFU75978.1}. SQ SEQUENCE 590 AA; 65636 MW; 4BC609F46E2C463C CRC64; MENIRDYLKN NILLFDGAMG TYYDELTDDG IGCELANIKN PELIKGIHNE YIEAGAKAIL TNTFAVGIDV FNGDRKLQKE VIVAGIDIAN DAAKDRAYVF ADIGPIHMSR NELVFEEYKV LIDIFLEKGI KNFLFETQSN TSGMVLSAGY IKGKCSDAFI AASFAVMPDG YSSEGYQYKA LFAEVTDSGL FDAVGLNCVS GANHMAKLLK GVDTKGLYLF AKPNAGYPVV RDDRVYYSSL ANYFANQIED ILEMGVNIVG GCCGTTPKHI ELLKKSMSGK LIKPRRAIKS EKNTTQNIRL NRFKNKLESG QKAIAVELDS PIDTNVNKFI ENAKKLKLAG ADIVTIADNP IARARMDSCL LACKVRNELD FDVLPHMTCR DRNVNASRGL LLGANAMGVD NVLVITGDPI PNAQRDEIRS VFEFNSVKFA NFIKSLNDEV FESPMNICAA LNVNSRNFSA ELKKAKRKQE NGVEVLFTQP VLTKRAIENL KEARENLDVK IMGGIIPIVS ERNARYMQSE VNGIYITDDI VEKYIGKERE EAEEIALSMS KEIANEIYDL VDGYYLITVL NRVSLMERLI KTVKEVCEKR // ID E6LQ60_9FIRM Unreviewed; 788 AA. AC E6LQ60; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFU75979.1}; GN ORFNames=HMPREF0381_2095 {ECO:0000313|EMBL:EFU75979.1}; OS Lachnoanaerobaculum saburreum DSM 3986. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Lachnoanaerobaculum. OX NCBI_TaxID=887325 {ECO:0000313|EMBL:EFU75979.1}; RN [1] {ECO:0000313|EMBL:EFU75979.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 3986 {ECO:0000313|EMBL:EFU75979.1}; 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. {ECO:0000313|EMBL:EFU75979.1}. 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; AEPW01000082; EFU75979.1; -; Genomic_DNA. DR RefSeq; WP_008751859.1; NZ_GL622296.1. DR EnsemblBacteria; EFU75979; EFU75979; HMPREF0381_2095. DR PATRIC; 45111115; VBIEubSab170007_2291. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFU75979.1}; KW Transferase {ECO:0000313|EMBL:EFU75979.1}. SQ SEQUENCE 788 AA; 85854 MW; 0DC5882C16530D7F CRC64; MHNLLILDGA MGTMLQAAGM KAGEHPEVFG FDNPEIVKNI HLKYIESGSN VIYTNTFGAN AHKLEGCKID VDTAIATAIK SAKEAVAKSK RKVKVALDIG PIGELLEPLG VLRFEDAYEI YKEMVVAGEK YGADIIIFET FTDLYDVRAG VLAAKENTNL PVWVTMTYET TGRTFTGTKI ESMAVTLEGL GVDAVGFNCS LGPKEILPLA KKLKEWTNLP IIIKPNAGLP NPSTGEYDLL ASDFAKLMAD FGEIGIEYAG GCCGTSPEFI SELKKEFENR KFSEIKPTKA KTGICSGNEM VELNGVRVVG ERLNPTGKKR FQEALLNHEM EYICKVAIEE EESGADILDI NVGVPGGDEV ALMIEAVKAV QSVVNIPLQI DSSNPEAIEA GLRVYNGRAI VNSVNAEDER LDLILPIVKK YGAAVIGLAL NEGGLPTTAQ ERFDNAKHIL DKAIEYGLKK EDVIIDCLTL TVSAQQDQAK ETLEAVRRVT RELGLHTTLG VSNISFGLPA RSHITENFLI QAMYAGLDLP IVNPNIEGIM NAVYSFKVLS GEDKDSVKYI ERFAAVKAET KIIQVSATGE VTKEVVQDAI LKGLKEETYN NAKKLLESHS ELEIINEYLI PALDKVGDLY EKQVIFLPQL INAANAASSA FELIKEEIAK KGDKNVSKGK IVVCTVKGDI HDIGKNIVKV ILENYGYRMI DLGRDVDIQR VVDTVVKENV KLVGLSALMT TTLPAMKKTI EEIRKVSDDC KVWVGGAVLT KEYADEMGAD FYAPDARSSV DIAKTVLG // ID E6MCF5_STALU Unreviewed; 612 AA. AC E6MCF5; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAY-2015, entry version 19. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HMPREF0790_2108 {ECO:0000313|EMBL:EFU83276.1}; OS Staphylococcus lugdunensis M23590. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=525377 {ECO:0000313|EMBL:EFU83276.1, ECO:0000313|Proteomes:UP000004055}; RN [1] {ECO:0000313|EMBL:EFU83276.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M23590 {ECO:0000313|EMBL:EFU83276.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFU83276.1}. 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; AEQA01000017; EFU83276.1; -; Genomic_DNA. DR RefSeq; WP_002461092.1; NZ_GL622352.1. DR EnsemblBacteria; EFU83276; EFU83276; HMPREF0790_2108. DR PATRIC; 45126993; VBIStaLug105164_2070. DR Proteomes; UP000004055; Unassembled WGS sequence. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004055}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EFU83276.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EFU83276.1}. SQ SEQUENCE 612 AA; 67924 MW; E0A74DD81818CB41 CRC64; MSQFLNQLQN NILVADGAIG TILYSEGLDT CPEAYNLTHP DKVERIHRSY IEAGADVIQT NTYGANFEKL KPFGLEHKVK EIHKAAVKIA KRAATKNTFI LGTVGGFRGI KQDDISLSTI QYHTENQIDT LIEEGVDALL FETYYDLDEL KRIVTWTKRN YDIPVVAQLT ASNTTYLVDG TEINDALAQL VTCGADVVGL NCHHGPHHME KSFSHIALPD NAYLSCYPNA SLLDIENSEF KYSDNAQYFG AVAEKLIEQG VRLIGGCCGT TPQHIHYIKS SVSHLSPVNH KKVIPIHKKS NQRRTDSIKQ SLTSKVKQGP TVIVELDTPK HLDTDLFFEN IGKLDAAHID AVTLADNSLA TVRISNIAAA SLIKQRYDIE PLVHITCRDR NLIGLQSHLL GLSLIGVNEI LAITGDPSKV GHLPGSTNVY DVNSKGLTEL ALRFNQGINT DGDALKKHTN FNIAGAFDPN VRKLDGAVKR LEKKIASGMS YFITQPVYSK EKIIQVYEAT KHLNIPIFIG IMPIASYNNA LFLHNEVPGI KMSESVLNQF KAVKDDKEKT KELSLRLSKD LIDTVHQYFN GLYIITPFQR VDYSLELAAY SRSITTNKEA IL // ID E6ME32_9FIRM Unreviewed; 805 AA. AC E6ME32; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFV02791.1}; GN ORFNames=HMP0721_0265 {ECO:0000313|EMBL:EFV02791.1}; OS Pseudoramibacter alactolyticus ATCC 23263. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Pseudoramibacter. OX NCBI_TaxID=887929 {ECO:0000313|EMBL:EFV02791.1}; RN [1] {ECO:0000313|EMBL:EFV02791.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 23263 {ECO:0000313|EMBL:EFV02791.1}; 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. {ECO:0000313|EMBL:EFV02791.1}. 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; AEQN01000005; EFV02791.1; -; Genomic_DNA. DR RefSeq; WP_006597684.1; NZ_GL622359.1. DR EnsemblBacteria; EFV02791; EFV02791; HMP0721_0265. DR PATRIC; 45128204; VBIPseAla174371_2203. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFV02791.1}; KW Transferase {ECO:0000313|EMBL:EFV02791.1}. SQ SEQUENCE 805 AA; 84340 MW; 501ED7F3CA16041C CRC64; MDIKTILGNE RLYLDGGMGS MIQKRIENPG PIPEELNLTH PEVIGEIQAA YVAAGADILV ANTFGANGHK MAGSPYSVDE VVRAAVHIAK ARHPRFVAMD IGPTGALIGD LGDLSFDAAK ACFAEAVRAG AAAGADLIFI ETMTDIYEAR AAVLAAKEHC DLPIICSMTY EDNSRTLTGS DPETVVTILE GLGVDAIGIN CSTGPDKMMP VIDRLLKAAS VPIVVEPNAG LPRVVDGETV YDIDAAAFAG SMCEIAVKGA AVLGGCCGTT PDYIAATIAR TRSVALPARG GARRPMRIAS STRTVTLGTD IRVIGEAINP TTNPELKADL RQGRMAVVKR LALEQKQQGA DILDVNVGLP EVDEAALMVQ AVHAISQVVE LPLQIDSTKP EVIEAVLKNY NGKPLVNSVN GEAASMAGIL PIVAHYGAAV LGLTLDDDGI PATAAGRVAV ADKLIAEAAK QGIGVEHIAI DCLVLTASAQ QAGVRETLDA VRAVKAKYGV PTVLGVSNIS FGLPNRRLIN KTFLTMALSA GLDTPIMKAA DAEMMNAVSA YRALAGLDDG CMAYVAAYKD DQNIEMAAAG PGQTTDAQNE ENGEAVSASG EADVIGMVVD GLKDEIVPVV QEMLTRMPPM DIVNNYLIPG LDKIGDLFET GEVFLPNLIF AAETVQNAFA EIKKAIKSDE QTVKGTVVLA TVKGDVHDIG KNILRVIMEN YGYRVVDLGK DVDPEVIVDA ARREGAGLVG LSALMTTTVK NMEITIARLK AELPEVPVMV GGAVMNETYA QSIHADFYGK DARAGVAIAD KVFGG // ID E6MLC8_9BACT Unreviewed; 922 AA. AC E6MLC8; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFV05565.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFV05565.1}; GN Name=metH {ECO:0000313|EMBL:EFV05565.1}; GN ORFNames=HMPREF9420_0295 {ECO:0000313|EMBL:EFV05565.1}; OS Prevotella salivae DSM 15606. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=888832 {ECO:0000313|EMBL:EFV05565.1}; RN [1] {ECO:0000313|EMBL:EFV05565.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 15606 {ECO:0000313|EMBL:EFV05565.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFV05565.1}. 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; AEQO01000025; EFV05565.1; -; Genomic_DNA. DR RefSeq; WP_007133588.1; NZ_GL629647.1. DR EnsemblBacteria; EFV05565; EFV05565; HMPREF9420_0295. DR PATRIC; 45133417; VBIPreSal169364_2045. DR OrthoDB; EOG6091CH; -. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFV05565.1}; KW Transferase {ECO:0000313|EMBL:EFV05565.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 765 765 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 922 AA; 101777 MW; 1CA9445E2C46A81B CRC64; MLRMKGLQDL IREKILILDG AMGTMIQSYH LTEEDFRGTR FQQVEGRQLK GNNDLLSLTR PDVILDIHRR YLAAGADIIE TNTFSSQRIS QADYGLEDIS YELAYEGARL ARQAVDELAD GTCRFVAGAI GPTNKTCSMS PDVSNPAARD LTYDELYFAY EEQIKGLLDG GVDALLIETI FDTLNAKVAI DVATNAMEAR NLELPIMLSV TVSDLAGRTL SGQTLEAFLG SICSYPIFSV GLNCSFGASQ MKPYLKELGK KAPYYISAYP NAGLPNSMGE YDETAESMSP QIGEFIDEQL VNIVGGCCGT TEEFIRRYAE MARGKAPRKP VERPKDLWLS GLELLEVSPE VRFVNVGERC NVAGSRKFLR LIKEKNYEEA LTIARKQVSD GALIIDVNMD DGLLDAQTEM VNFLNLIASE PDVARVPVMI DSSKWDVIVA GLKCMQGKCV VNSISLKNGE QEFLRHAREI KRFGAAVVVM CFDEVGQATT FERKIEIAER AYRLLVDKVG FNPLDIIFDP NILSIATGIE AHDNYAVDFI RATGWIKKHL PGAHISGGVS NLSFSFRGNN YIREAMHAVF LYHAINQGMD FGIVNPATKI TYADIPSDHL RIIEDVVLNR KEGAAEALIE LANEIKANED ARKAGGEVLG KTAEQHEEWR DFPVAKRLEY ALRKGISEHL QADLTEALAQ YPHAVDIIEG PLMDGMNEVG ELFGAGKMFL PQVVKTARTM KQAVAILQPY IEMEKADDTY KAGKIILATV KGDVHDIGKN IVGVVMACNN YEVIDLGVMV PAEQIVKRAI AENADMIGLS GLITPSLEEM VNVALEMKKA QLEIPIMIGG ATTSQLHVAL KIAPVYGGPV VWMKDASQNA LIAAKLLNKK ERAVLKHNLD EKYAELRSGY EKEQQKIISL DEARKNKLDL FS // ID E6PI36_9ZZZZ Unreviewed; 1157 AA. AC E6PI36; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 01-OCT-2014, entry version 15. DE SubName: Full=Methionine synthase (5-methyltetrahydrofolate--homocysteine methyltransferase) (Methionine synthase, vitamin-B12 dependent) (MS) {ECO:0000313|EMBL:CBH76126.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CBH76126.1}; GN Name=metH {ECO:0000313|EMBL:CBH76126.1}; GN ORFNames=CARN1_0606 {ECO:0000313|EMBL:CBH76126.1}; OS mine drainage metagenome. OC unclassified sequences; metagenomes; ecological metagenomes. OX NCBI_TaxID=410659 {ECO:0000313|EMBL:CBH76126.1}; RN [1] {ECO:0000313|EMBL:CBH76126.1} 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. {ECO:0000313|EMBL:CBH76126.1}. 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; CABL01000019; CBH76126.1; -; Genomic_DNA. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:CBH76126.1}; KW Transferase {ECO:0000313|EMBL:CBH76126.1}. SQ SEQUENCE 1157 AA; 126289 MW; 553394F0127B9150 CRC64; MTSYLDALRE RVLLFDGAMG TQLMALELTA EDFGGARQLG CNEALVLSRP DLIRSIHERY FEAGADVVET DSFTASRLKL DEFGIGEHTY AVNHDAARLA RKAADLYATP TRPRFVAGSM GPTGMLVSSS DPSLSKITFE ELAALYGEQA RALVEGGVDL LLLETMQDLL ELKAAIVGIG RAFREGVRRV PIQAQPTLIT EGRMLLGTDI SSVCAVLDAL PIDVIGLNCS TGPAQMRDSV RYLGETSRCY VSVIPNAGLP LMGPKGETIY PETPSELTSE LMEFVRSFGV RAIGGCCGTT PEHIASLRAA LDASPASRAP HRAAPPRPEF VASAMTAVSL EQEPRPLIVG ERINSQGSRR VKRLLLEDDY EVIGQLARDQ IEGGAHVLDV CTALTERTDE PEQMRAVVRR LAQSVEAPLM IDSTEAAVVR SALENYPGRA IVNSVHLESG RTKIDAILPM AIEHGAAVVA LTIDESGMAK TAQRKLDVAR RIYDIVVGEY GLAPGALIFD DLTFTLATGD AEYIDSARES IDGIRAIKAA LPGVLTSLGV SNVSFGLKPA ARAALNSVFL HHCVEAGLDL ALVHPKEITP YAELDAEARE ACDDLVFNRR PDALARFIER YENAVVRSDE DTANDEVGLP AEARIHRAIL HRKKDGIETM LDEVLLRRTP VEVLNEVLLP AMKEVGDRFG AGELILPFVL QSAEVMKRAV AHVEQFLERR EGSTKGTVVL ATVFGDVHDI GKNLVNTILS NNGYTVYDLG KQVPMNVILE KATEVNADAI GLSALLVSTS KQMPICVQEQ DARALAFPVI VGGAAINRDF GRRISLLDEG RRPFEPGVFY AKDAFEGLDI MDMLTGDPER RRGFIDRIKN DALKAQAKVR EPSHPVGELR ISSVKSVVVE PPKAPFLGPR SIDSIDVREL WDCFDLKSLY RLSWGASNQK GEAFEKTVRE EFEPRLARYR AEAERGGILH PRVAYGYFPV AGIGNDVLFF DPNDATREIA RMSFARQIGG EHLSLADYLR EPIDGRASDI VALQVVTVGA EVAEEIEALH ARGDFSESYF LHGFSVQSAE ALAEWSHRRI RHELGLAPER GKRYSWGYGA CPDLSQHEVA FALLDAVRSI GVRLTESFQI VPEQSTAALV IHHPQASYFN AAATIER // ID E6PVI9_9ZZZZ Unreviewed; 356 AA. AC E6PVI9; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 01-APR-2015, entry version 15. DE SubName: Full=Putative Homocysteine S-methyltransferase {ECO:0000313|EMBL:CBH98946.1}; GN ORFNames=CARN2_0120 {ECO:0000313|EMBL:CBH98946.1}; OS mine drainage metagenome. OC unclassified sequences; metagenomes; ecological metagenomes. OX NCBI_TaxID=410659 {ECO:0000313|EMBL:CBH98946.1}; RN [1] {ECO:0000313|EMBL:CBH98946.1} 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. {ECO:0000313|EMBL:CBH98946.1}. 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; CABM01000064; CBH98946.1; -; Genomic_DNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:CBH98946.1}; KW Transferase {ECO:0000313|EMBL:CBH98946.1}. SQ SEQUENCE 356 AA; 38248 MW; 0654431AD9E2C5D5 CRC64; MTSATPAQPQ PAYTRGAQLP ALLRQRILIL DGAMGTMIQR FKLNEAQYRS ERFKTWPKDV KGNNELLNLT QPQIIRDIHD GYFQAGADIV ETNTFGATTI AQDDYAMAGL ADEMNRAAAR IARASADAHS TPAKPRFVAG AFGPTPKTAS ISPDVNDPGA RNITFEQLRA AYYEQAKALG EEGVDLFLVE TIFDTLNAKA ALFAIDEWFE ASGERLPLVI SGTVTDASGR ILSGQTVPAF WASVRHAQPL AVGLNCALGA ALMRPYLQEL AKAAGDTFIS CYPNAGLPNP MSDTGFDETP DVTSRLLHEF AAEGLVNIVG GCCGTTPEHI AAIGRAVDHQ KPRLLAGRGP FYQRAA // ID E6PZQ3_9ZZZZ Unreviewed; 1105 AA. AC E6PZQ3; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 01-OCT-2014, entry version 15. DE SubName: Full=Methionine synthase (5-methyltetrahydrofolate--homocysteine methyltransferase) (Methionine synthase,vitamin-B12 dependent) (MS) {ECO:0000313|EMBL:CBI00412.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CBI00412.1}; GN Name=metH {ECO:0000313|EMBL:CBI00412.1}; GN ORFNames=CARN3_1437 {ECO:0000313|EMBL:CBI00412.1}; OS mine drainage metagenome. OC unclassified sequences; metagenomes; ecological metagenomes. OX NCBI_TaxID=410659 {ECO:0000313|EMBL:CBI00412.1}; RN [1] {ECO:0000313|EMBL:CBI00412.1} 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. {ECO:0000313|EMBL:CBI00412.1}. 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; CABN01000132; CBI00412.1; -; Genomic_DNA. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:CBI00412.1}; KW Transferase {ECO:0000313|EMBL:CBI00412.1}. SQ SEQUENCE 1105 AA; 120451 MW; C801335A35CA4271 CRC64; MIETDSFGST DIVLAEFELE NRTRELNLAA ARLAREVADQ YFTAEKPRFV AGSMGPTTKL PSLGHIGYDA MAASYRQQAE ALIEGGVDIL LVETSQDLLQ AKIASAACHD AIAAAVAAGG RRVALQVQVT LEATGTMLLG SEIGAALAVL EAMQPDVIGL NCATGPEEMN DAVRFLCQNS TLPICIQPNA GLPQNEGGHA VYKLTPAELA AHHRRFVTEY GVAVVGGCCG TTPEHLRAVA EAVAGLKPLD RNVRPQSVVA SAFTAVPLEV DGQPVVIAEE MNTTTRLEYF RNLVRGGDYE GILTMAKRLV GEGSQMLDLC CAIVGEDEQA YMNGVLEKIA TRVPAPILVD STEAEVIEEA LKRIPGKPVI NSINLEDGEK RTSRVLPMAR RYGAAVIALT IDEDGMALTA DKKVAIAHRI HDMAVHRYGL RAQDIIFDPL TLPISTGQED YRSAAIETLE AVRRIKLDLP GVKTVLGVSN ISFGLNAYAR RVLNSVFLKE AVDRGLDTAI VNYSRIYPLY KIPEKEVELA RRLIFQEWEV DGARVDPLQA YMGYFAGLSK GSVPEDEIAV EDLSVEDRLK QLIIRGERSI GLGEQKQTLE EAIEAALVSY SPLALINDVL LDGMKTVGEL FGARKMQLPS VLDSAAVMKA AVAYLEPKME KSDGGGKGTM VLATVKGDVH DIGKNLVDII LTNNGYRVIN LGIKQPSDVI VAAARAQATD SIGLSGLLVK STLEMKYVLQ DLERLGLEIP VICGGAALTR KYVEEDLRKE YSGPVYYAED AFAGLNIMSD LVSEDAGVRE TRVTEGKTVK IYAKGNASAM VEITSVELTA EGRSPTVEAP PNVPEPEFWG ARVFKDYSLD DLFPFINETA LFKNQWQLKT AAQGEYLRLV EEKYRPILTE MQEEVKAAGC FHPQAVIGFY PCNSVGDEVV LYDPADPERE IERMRFPRQA QGRRLSIADY FLPISAGRRD VIGCTIVTIG SQASVETQKL FDAGDFTKYL YLHGLSVETA EALAEFVHKQ ARELLGIAGG DAPKVTDLFH QKYRGSRYSF GYPACPNLED QAKIFKLLKP EESIGVHLTE GYHLEPEQST NAILVHHPQA KYFVA // ID E6Q417_9ZZZZ Unreviewed; 1157 AA. AC E6Q417; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 01-OCT-2014, entry version 15. DE SubName: Full=Methionine synthase (5-methyltetrahydrofolate--homocysteine methyltransferase) (Methionine synthase,vitamin-B12 dependent) (MS) {ECO:0000313|EMBL:CBI01976.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CBI01976.1}; GN Name=metH {ECO:0000313|EMBL:CBI01976.1}; GN ORFNames=CARN4_2171 {ECO:0000313|EMBL:CBI01976.1}; OS mine drainage metagenome. OC unclassified sequences; metagenomes; ecological metagenomes. OX NCBI_TaxID=410659 {ECO:0000313|EMBL:CBI01976.1}; RN [1] {ECO:0000313|EMBL:CBI01976.1} 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. {ECO:0000313|EMBL:CBI01976.1}. 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; CABO01000028; CBI01976.1; -; Genomic_DNA. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:CBI01976.1}; KW Transferase {ECO:0000313|EMBL:CBI01976.1}. SQ SEQUENCE 1157 AA; 126193 MW; 936D6C1A9A50F48E CRC64; MTSYLDALRE RVLLFDGAMG TQLMALELTA EDFGGARQLG CNEALVLSRP DLIRSIHERY FEAGADVVET DSFTASRLKL DEFGIGEHTY AVNHDAAQLA RKAADAYATP RRPRFVAGSM GPTGMLVSSS DPSLSKVTFQ ELAALYGEQA RALVEGGVDL LLLETMQDLL ELKAAIVGIG RAFREGVRRV PIQAQPTLIT EGRMLLGTDI SAVCAVLDAL PIDVIGLNCS TGPAQMRDSI RYLGETSRCY VSVIPNAGLP LMGPKGETIY PETPSELTSE LMEFVRSFGV RAIGGCCGTT PEHIASLRAA LDAIPESRSP HRAAPPRPQF VASAMTAVSL EQEPRPLIVG ERINSQGSRR VKRLLLEDDY EAIGQLARDQ IEGGAHVLDV CTALTERTDE PEQMRAVVRR LAQSVEAPLM IDSTEAAVVR SALENYPGRA IVNSVHLESG RAKIDAILPM AIEHGAAVVA LTIDESGMAK TAQRKLDVAR RIYDIVVGEY GLAPGALIFD DLTFTLATGD AEYIDSARES IEGIRAIKAA LPSVLTSLGV SNVSFGLKPA ARAALNSVFL HHCVEAGLDL ALVHPKEITP YAELDAEARE ACDDLVFNRR PDALARFIER YENAVVRSDE DTANDEVGLP AEARIHQAIL RRKKDGIEAM LDEVLLRRTP VEVLNEVLLP AMKEVGDRFG AGELILPFVL QSAEVMKRAV AHVEQFLERR EGSTKGTVVL ATVFGDVHDI GKNLVNTILS NNGYTVYDLG KQVPMNLILE KATEVNADAI GLSALLVSTS KQMPICVQEQ DARALQFPVI VGGAAINRDF GRRISMLDDG QRPFEPGVFY AKDAFEGLDI MDLLTGDPER RRGFIERIKN EAVKAQAKVQ QLSHPVGELR ISSVKSVVVE PPKAPFLGPR SIDSIDVREL WDCFDLKSLY RLSWGASNQK GEAFEKTVRE EFEPRLALYR AEAERGAILH PRVAYGYFPV AGIGNDVLFF DPNDATREIA RMSFARQIGG EHLSLADYLR EPIAGAASDI VALQVVTVGA EVAKEIEALH ARGDFSESYF LHGFSVQSAE ALAEWSHRRI RRELGLAPER GKRYSWGYGA CPDLSQHEIA FALLDAVRSI GVRLTESFQI VPEQSTAALV IHHPNASYFN AAATIER // ID E6QK94_9ZZZZ Unreviewed; 132 AA. AC E6QK94; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 01-OCT-2014, entry version 10. DE SubName: Full=Homocysteine methylase using (R,S)AdoMet {ECO:0000313|EMBL:CBI07661.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:CBI07661.1}; GN ORFNames=CARN6_1029 {ECO:0000313|EMBL:CBI07661.1}; OS mine drainage metagenome. OC unclassified sequences; metagenomes; ecological metagenomes. OX NCBI_TaxID=410659 {ECO:0000313|EMBL:CBI07661.1}; RN [1] {ECO:0000313|EMBL:CBI07661.1} 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. {ECO:0000313|EMBL:CBI07661.1}. 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; CABQ01000120; CBI07661.1; -; Genomic_DNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:CBI07661.1}; KW Transferase {ECO:0000313|EMBL:CBI07661.1}. SQ SEQUENCE 132 AA; 14292 MW; 8F5E07A31C938195 CRC64; MKAWLSFTCS DGTHVAHGEP LRLCAEFAAT LPQTIAIGVN CTAPQWIPAL IAELKLASDK PILVYPNSGE IWDAEARCWR GTGDPDSFAN QAQSWFKAGA QMVGGCCRTR PEHIRRVAAN SRQQTATTPL AP // ID E6QML5_9ZZZZ Unreviewed; 626 AA. AC E6QML5; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 01-OCT-2014, entry version 17. DE SubName: Full=Methylenetetrahydrofolate reductase {ECO:0000313|EMBL:CBI08486.1}; DE EC=1.5.1.20 {ECO:0000313|EMBL:CBI08486.1}; GN ORFNames=CARN6_1960 {ECO:0000313|EMBL:CBI08486.1}; OS mine drainage metagenome. OC unclassified sequences; metagenomes; ecological metagenomes. OX NCBI_TaxID=410659 {ECO:0000313|EMBL:CBI08486.1}; RN [1] {ECO:0000313|EMBL:CBI08486.1} 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. {ECO:0000313|EMBL:CBI08486.1}. 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; CABQ01000228; CBI08486.1; -; Genomic_DNA. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Oxidoreductase {ECO:0000313|EMBL:CBI08486.1}. SQ SEQUENCE 626 AA; 67110 MW; 955E4A7CAE01F8C3 CRC64; MLQKIFADQP VLCDGAMGTV LYGRGVFIHR CYDELNLSDP SLILAIHEEY LQSGAQILET NTFGANRFRL GRHGLAGKVA EINTAGVRIA REAAAHLKDK QAGEAWVAGA IGPLGVRLEP LGKTGLAEAR EAFEEQMQAL VTAGVDLLII ETMPALNEAR EALSAAKTIA PDIPVAVMIT VDEEGRCLDG ASPEQAAALL TEWGADALGC NCSTGPSTVL TAIEAMRTAT HLPLMAMPNA GMPRAVEGRN IYLCSPEYMA SFARKAIKAG AQFVGGCCGT TPNHIRAMKS ALRALDAQSH ITLNEPARVA LSEETPPLPL AQRSFVGRLI AEGQFVTLVE IVPPRGIDCD KEIEGARLLA SLGVHAINVP DSPRASARMS AQSLCIQIQQ KTGIETVLHY TCRDRNILSI QSDLLGASSL GLRNILCLTG DPPKLGNYPD ATAVFDVDAI GLVNVVRRLN HGLDIGSNAI GGSTNFTIGV AANPGVPDIE QELRRFAWKV DAGAEYAITQ PVFDMRLLEA FLKRIEQFRI PVIAGIWPLT SLRNAEFMRN DLRVSMPEAI MLRMAQAESP EAARTEGIRI AQEMLAEARP MVQGVQVSAP FSRYSLAAEI LTSVLSKTAN LSVQNS // ID E6RCB8_CRYGW Unreviewed; 382 AA. AC E6RCB8; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 29-APR-2015, entry version 19. DE SubName: Full=Homocysteine S-methyltransferase, putative {ECO:0000313|EMBL:ADV24446.1}; GN OrderedLocusNames=CGB_I3420C {ECO:0000313|EMBL:ADV24446.1}; 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 {ECO:0000313|EMBL:ADV24446.1, ECO:0000313|Proteomes:UP000007805}; RN [1] {ECO:0000313|EMBL:ADV24446.1, ECO:0000313|Proteomes:UP000007805} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WM276 / ATCC MYA-4071 {ECO:0000313|Proteomes:UP000007805}; 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., 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; CP000294; ADV24446.1; -; Genomic_DNA. DR RefSeq; XP_003196233.1; XM_003196185.1. DR GeneID; 10186436; -. DR KEGG; cgi:CGB_I3420C; -. DR EuPathDB; FungiDB:CGB_I3420C; -. DR KO; K00547; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000007805; Chromosome I. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 2. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007805}; KW Methyltransferase {ECO:0000313|EMBL:ADV24446.1}; KW Transferase {ECO:0000313|EMBL:ADV24446.1}. SQ SEQUENCE 382 AA; 42102 MW; 2D8625B5691F1F0C CRC64; MSSNILILDG GMGTTLESLG ADISSPLWGS EALRTNPDVI RKVYEGYVQA GADLVETATY QLTPQNLCDH LHCSREEAER ILCSGVKLVA SSIASCSSRN QEHKDKDKGN NGSKVVLSFG PYGSTLQPGQ EYGGIYPPPY GPSTSTNAFP PDYNDKEEEA IQALAYHHLD KLEAINHDEA AWREVGWIAF ETIPVLHEVR GIRRAMGIMR RKLPALYTGG DNGSLWWDKK FWITSPFPMG QHPQLLPDGS HASIPQVIDA LFSGPDPIPN GIGINCANPS YLRSLTSLFT SHLPFEFFGK VEMVIYPDGG QVYDTTTRTW VLAPQSPENS EKWAEVVGGM AKEIRGAERD EKRVWKGVVV GGCCKSSFDE IRALRRFVDS QQ // ID E6RMB9_PSEU9 Unreviewed; 195 AA. AC E6RMB9; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 01-APR-2015, entry version 19. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:ADT70002.1}; GN OrderedLocusNames=PSM_A3089 {ECO:0000313|EMBL:ADT70002.1}; OS Pseudoalteromonas sp. (strain SM9913). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=234831 {ECO:0000313|EMBL:ADT70002.1, ECO:0000313|Proteomes:UP000007933}; RN [1] {ECO:0000313|EMBL:ADT70002.1, ECO:0000313|Proteomes:UP000007933} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM9913 {ECO:0000313|Proteomes:UP000007933}; 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; ADT70002.1; -; Genomic_DNA. DR RefSeq; WP_013466248.1; NC_014803.1. DR RefSeq; YP_004070154.1; NC_014803.1. DR EnsemblBacteria; ADT70002; ADT70002; PSM_A3089. DR KEGG; psm:PSM_A3089; -. DR PATRIC; 45333634; VBIPseSp136886_3658. DR BioCyc; PSP234831:GH93-3138-MONOMER; -. DR Proteomes; UP000007933; Chromosome I. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007933}; KW Methyltransferase {ECO:0000313|EMBL:ADT70002.1}; KW Transferase {ECO:0000313|EMBL:ADT70002.1}. SQ SEQUENCE 195 AA; 21545 MW; E9354BE36814DE12 CRC64; MSKLIILDGG MGRELKRMGA PFSQPLWSAQ ALIEAPQCVT QAHQGFIDAG AEIITVNSYA CVPFHLEEFE WQLADGASAI SYSFSANGEH FLVLDSLGFL NVLEAHAHDD HIHWELAGQV DITQEDVTTM PEGMKFSMTV AKNGQFAYVA DPIAQHVVQV HLEDLEIEGE LELTFPPVAI TWLGIAQEEE HDHVH // ID E6RNR9_PSEU9 Unreviewed; 356 AA. AC E6RNR9; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=Putative B12-dependent homocysteine-N5-methyltetrahydrofolate transmethylase (N terminal) {ECO:0000313|EMBL:ADT67820.1}; GN OrderedLocusNames=PSM_A0872 {ECO:0000313|EMBL:ADT67820.1}; OS Pseudoalteromonas sp. (strain SM9913). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=234831 {ECO:0000313|EMBL:ADT67820.1, ECO:0000313|Proteomes:UP000007933}; RN [1] {ECO:0000313|EMBL:ADT67820.1, ECO:0000313|Proteomes:UP000007933} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM9913 {ECO:0000313|Proteomes:UP000007933}; 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; ADT67820.1; -; Genomic_DNA. DR RefSeq; WP_008465493.1; NC_014803.1. DR RefSeq; YP_004067971.1; NC_014803.1. DR EnsemblBacteria; ADT67820; ADT67820; PSM_A0872. DR KEGG; psm:PSM_A0872; -. DR PATRIC; 45329151; VBIPseSp136886_1485. DR HOGENOM; HOG000265279; -. DR OMA; AQEDYKM; -. DR BioCyc; PSP234831:GH93-889-MONOMER; -. DR Proteomes; UP000007933; Chromosome I. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007933}; KW Methyltransferase {ECO:0000313|EMBL:ADT67820.1}; KW Transferase {ECO:0000313|EMBL:ADT67820.1}. SQ SEQUENCE 356 AA; 38975 MW; FA5ACB3619B66E29 CRC64; MPNNPQNNKH QELSAALKQR ILILDGAMGT MIQAHKLEEQ DYRGERFKDW HVLIKGNNDL LSLTKPEIIT DIHRSFLAAG ADIIETNTFN STTISMEDYD MASISREVNL ESAKLARAVC DEFSAKTPEK PRYVAGVLGP TSKTCSLSPD VNDPGYRNIT FDKLVTAYVE STLALMEGGV DIILIETIFD TLNAKAASFA VEEAFEQAGR TLPVMISGTI TDASGRTLSG QTTEAFYNSI RHIKPLSIGL NCALGPDLLR QYVEELSRVC ETFVSVHPNA GLPNEFGEYD LEADDMAKEI IDWGKSGFIN IVGGCCGTTP AHIRAFAKGL EGTAPRKLPE LEVRMRLSGL EACNLN // ID E6SA58_INTC7 Unreviewed; 1263 AA. AC E6SA58; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 29-APR-2015, entry version 27. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ADU48268.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADU48268.1}; GN OrderedLocusNames=Intca_1755 {ECO:0000313|EMBL:ADU48268.1}; 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 {ECO:0000313|EMBL:ADU48268.1, ECO:0000313|Proteomes:UP000008914}; RN [1] {ECO:0000313|EMBL:ADU48268.1, ECO:0000313|Proteomes:UP000008914} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23552 / DSM 43043 / JCM 3097 / NBRC 12989 / 7 KIP RC {ECO:0000313|Proteomes:UP000008914}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002343; ADU48268.1; -; Genomic_DNA. DR RefSeq; WP_013492583.1; NC_014830.1. DR RefSeq; YP_004098995.1; NC_014830.1. DR EnsemblBacteria; ADU48268; ADU48268; Intca_1755. DR KEGG; ica:Intca_1755; -. DR PATRIC; 45245041; VBIIntCal153415_1791. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR BioCyc; ICAL710696:GH9U-1786-MONOMER; -. DR Proteomes; UP000008914; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008914}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADU48268.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008914}; KW Transferase {ECO:0000313|EMBL:ADU48268.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 254 254 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 318 318 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 775 775 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1263 AA; 138592 MW; DE16796FECA4DB9E CRC64; MTHPRVHRPD VTEILSATLR ERIMVLDGAM GTAIQRDRPD EAGYRGERFA DWPTDLQGNN DLLTLTQPEL VAQIHRDYLE AGADVIETNT FNANAISLGD YGMSELAYEI NWEAARLARR EADAMTARTP DRPRWVAGAI GPTTRTASIS PDVNDPGARN VTFDQLVDAY SEAARGLLDG GADLLLVETI FDTLNAKAAI FAVESVFEEY GRRWPVIVSG TITDASGRTL SGQVTEAFWN SVRHVRPLAI GLNCALGAKE LRPYISELAR VADCFVSCYP NAGLPNAFGE YDEAPDETAE VISEFAAAGF VNIVGGCCGT TPEHIAAIAK AVDGKPGHTV APPTTAMRLS GLEPFTINED SLFVNVGERT NITGSARFRT LIKDGDYDTA LSVAAQQVEN GAQVIDVNMD EGMIDGVAAM DRFLKLVASE PDISRVPVMI DSSKWEVIEA GLKCVQGKAI VNSISLKEGE ESFIEHARLV RKYGAAAVVM AFDEDGQADS LESRTQICAR AYRILTEEVG FPAEDIIFDP NVFAVATGIE EHASYGRDFI EATRWIKENL PGAKVSGGIS NVSFSFRGNN PVREAIHAVF LYHAIAAGLD MGIVNAGALA VYDEIDEELR DRVEDVVLNR RPDAAERLLE VAERYNRAAG PDAVTEDEWR GLPVRERITH SLVKGVDAHI EDDTELLRAE IAAAGGQPIE VIEGPLMDGM NVVGDLFGAG KMFLPQVVKS ARVMKKAVAY LIPYIEEEKA KDPALAKQKD TNGTIVMATV KGDVHDIGKN IVGVVLQCNN YEVIDLGVMV PAQKILDAAR EHEADLIGLS GLITPSLDEM VGFAAEMQRQ GFDIPLLIGG ATTSRAHTAV KVDPRYDGPV VWVKDASRSV PTAAALLSPD QRARLMVDVK ADYDALRTRH ATKHDRPLLP LERARANATP MTWEGYHPPR PHLLLQQEKD VSPVVWHEGS TQHVRVYKHY PVEELRRYID WQPFFNAWEL KGSFPDILNN PASGPAARKL YDDAQAMIDR VVSEDWLTAN AVVGLFPANS VGDDTEVYLD EHRQDPVAVL HHLRQQGEHR GGVPNRSLAD YVAPRSTGLR DYVGAFAVTA GLGSQERVAA FRAELDDYNA ILLESIADRL AEAFAERMHE KVRKELWGYA PDEHLDNAGL IKEAYQGIRP APGYPACPEH TEKETLWRLL DVETHTGIQL TEGMSMWPGA SVSGWYFSHP QSQYFVVGRL GRDQVADYAE RKGWTLAQAE RWLSSNLAYD PED // ID E6SH71_THEM7 Unreviewed; 782 AA. AC E6SH71; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAY-2015, entry version 30. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=Tmar_1626 {ECO:0000313|EMBL:ADU51735.1}; 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 {ECO:0000313|EMBL:ADU51735.1, ECO:0000313|Proteomes:UP000008915}; RN [1] {ECO:0000313|Proteomes:UP000008915} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700841 / DSM 12885 / JCM 10246 / 7p75a RC {ECO:0000313|Proteomes:UP000008915}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ADU51735.1; -; Genomic_DNA. DR RefSeq; WP_013496036.1; NC_014831.1. DR RefSeq; YP_004102462.1; NC_014831.1. DR EnsemblBacteria; ADU51735; ADU51735; Tmar_1626. DR KEGG; tmr:Tmar_1626; -. DR PATRIC; 45380539; VBITheMar50867_1676. DR KO; K00547; -. DR BioCyc; TMAR644966:GHKT-1665-MONOMER; -. DR Proteomes; UP000008915; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008915}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000008915}. SQ SEQUENCE 782 AA; 79830 MW; 8FD1A867F4248B61 CRC64; MTHSSRQRGS TAPPPGHPHP DEPAGFGPAV PAGEGAGRLF PPFPMLADGD PSWSLAAGIG EPGQTARPAA ARTAAAAAAA RAAPTPPEAG PPGEVLAEVA WWPLRRPRAV EAAHLEAIRA GARLVRTHTR WASPAWLDRV PRTRVEQINL WAAKLARSAR EVAGEPCLVA GLLGPLPAAP AGAAADGWEE ALAAYRTQVA GLLAGGVDLF WIEARTAAEA AAALAAVREA CRLPAGLVWI PGGPGSGGDG TGTGDPGELE AHTPQGFVGQ LVKVVRAAGS PDALGVAVTG GPAEAARWLG GLRRAGWAGP LWASLGTAGE AAADREGWEA LRTLGVGWIA GTGPWSPAGL AALGRRAGLV PATLGDAQDT PAHPATPVPP RPARPHTVQP VPAPPATHGA PPHPAVAGPL AGSHAPRVSG APATPPLLPG AGEPAPLREK LGRRFVISVE LDPPRGPVTT KFVADARTVA AAGADAVNVG DSPMARPRMA ALAGAYLVRA AAGIEAIMHC TTRDRNLMAL QADLLAAHAL GVRNVLALTG DHPKLGTSGA SPVYDVDSIG LLEVLAALRR GEDPQGNPLG APADFTVACA LSPNADDLDR ELDRFRRKLA VGVVDFVMTQ PLYEIEPLER VLDRLGGCPV PILMGVMPLH SGRHAHYLHH QVPGISIPAP VREALDRAGD RGLEVGLELA EAVVEAARPY IAGVYVVVSY GKAEPVAEFV RRLRTRFDQP LPGPQGAVTV AGPPSGTATA AGSSAPVAAV QAPVTSGPMP VSRQGEVRPH AG // ID E6SPW2_BACT6 Unreviewed; 921 AA. AC E6SPW2; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 29-APR-2015, entry version 29. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ADV44941.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADV44941.1}; GN OrderedLocusNames=Bache_3009 {ECO:0000313|EMBL:ADV44941.1}; 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 {ECO:0000313|EMBL:ADV44941.1, ECO:0000313|Proteomes:UP000008630}; 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] {ECO:0000313|EMBL:ADV44941.1, ECO:0000313|Proteomes:UP000008630} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35417 / DSM 20613 / JCM 6297 / P 36-108 RC {ECO:0000313|Proteomes:UP000008630}; RX PubMed=21475586; RA Pati A., Gronow S., Zeytun A., Lapidus A., Nolan M., Hammon N., RA Deshpande S., Cheng J.F., 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.J., Jeffries C.D., RA Detter J.C., Brambilla E., Rohde M., Goker M., Woyke T., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., RA Lucas S.; RT "Complete genome sequence of Bacteroides helcogenes type strain (P 36- RT 108)."; RL Stand. Genomic Sci. 4:45-53(2011). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002352; ADV44941.1; -; Genomic_DNA. DR RefSeq; WP_013548528.1; NC_014933.1. DR RefSeq; YP_004162527.1; NC_014933.1. DR EnsemblBacteria; ADV44941; ADV44941; Bache_3009. DR KEGG; bhl:Bache_3009; -. DR PATRIC; 45176757; VBIBacHel147569_3152. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR BioCyc; BHEL693979:GHID-3083-MONOMER; -. DR Proteomes; UP000008630; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008630}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADV44941.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008630}; KW Transferase {ECO:0000313|EMBL:ADV44941.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 243 243 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 765 765 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 921 AA; 101257 MW; 134927329C86B87C CRC64; MASIEKIVHE RILILDGAMG TMIQQYNLEE KDFRGERFSD IQGQLKGNND LLCLTRPDVI QDIHRKYLAA GADIIETNTF NSTRVSMADY HVQEYVREIN FAAVRLAREI ADEFTSLTPD KPRFVAGSVG PTNKTCSMSP DVNNPAFRAL TYDELAADYC EQMEALLQGG VDALLIETIF DTLNAKAAIW AAEQAMKATG KHVPLMLSVT VSDTAGRTLS GQTLEAFLAS VQHADIFSVG LNCSFGARQL KPFLEQFACR APYYISAYPN AGLPNSLGKY DQTPADMAHE IREYIREGLV NIIGGCCGTT DAYIAEYSAL VAGVVPHVPA SAPDNLWLSG LELLEVKPEN NFVNVGERCN VAGSRKFLRL INEKKYDEAL SIARQQVEDG AQVIDINMDD GLLDARAEMT TFLNLVASEP EIARVPVMID SSKWEVIVAG LKCLQGKSIV NSISLKEGEE NFLEHARTVR EYGAAAVVMA FDEKGQADTY ERKIEVCERA YRLLVDKVKF NPHDIIFDPN ILAVATGMDE HNNYAVDFIN AVGWIRKNLP GAHVSGGVSN LSFSFRGNNY IREAMHAVFL YYAIREGMDM GIVNPATSVL YTDIPADILE RLEDVVLNRR PDAAERLIET AERLKAEADA AKASGTGNVQ PVNSQLSWRE NSTVEDRLKY ALTKGIIDYL DEDLAQALEQ YPKAVDIIEG PLMAGMNHVG DLFGAGKMFL PQVVKTARTM KKAVAILQPV IESERKEDST SAGRVLLATV KGDVHDIGKN IVSVVMACNG YEIIDLGVMV PAETIVQHAI EEKVDMIGLS GLITPSLDEM VHVAIELEKA GLDIPLLIGG ATTSQLHTAL KIASVYHAPV IHLKDASQNA TVAARLMNPK QKEELVEDLS TKYRQLREKN GERQVSTVSL EEAKKNKLNL F // ID E6TH71_MYCSR Unreviewed; 1246 AA. AC E6TH71; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAY-2015, entry version 30. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ADT99011.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADT99011.1}; GN OrderedLocusNames=Mspyr1_23680 {ECO:0000313|EMBL:ADT99011.1}; OS Mycobacterium sp. (strain Spyr1). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=278137 {ECO:0000313|EMBL:ADT99011.1, ECO:0000313|Proteomes:UP000008916}; RN [1] {ECO:0000313|Proteomes:UP000008916} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Spyr1 {ECO:0000313|Proteomes:UP000008916}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002385; ADT99011.1; -; Genomic_DNA. DR RefSeq; WP_013471489.1; NC_014814.1. DR RefSeq; YP_004076846.1; NC_014814.1. DR EnsemblBacteria; ADT99011; ADT99011; Mspyr1_23680. DR KEGG; msp:Mspyr1_23680; -. DR PATRIC; 45285885; VBIMycSp109077_2603. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; QPFFNAW; -. DR BioCyc; MSP278137:GHD6-2352-MONOMER; -. DR Proteomes; UP000008916; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008916}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADT99011.1}; KW Transferase {ECO:0000313|EMBL:ADT99011.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 255 255 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 318 318 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 319 319 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 775 775 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1246 AA; 136746 MW; 379B4C121134A8C8 CRC64; MNAVEFEPNI RPDCTEELTA ALRERIMVID GAMGTAIQRD RPDEAGYRGD RFTEWPTALQ GNNDLLNLTQ PQIIEAIHRE YLDAGADILE TNTFNANAIS LSDYDMTDLA YELNYAGAAL ARKAADEYST ADKPRYVAGA IGPTTRTASI SPDVNDPGAR NVSYDQLVAA YLEAANGLVD GGSDLIMIET IFDSLNAKAA VFAVETLFEE RGRRWPVIIS GTITDASGRT LSGQVTEAFW NAIRHAKPLA VGLNCALGAP EMRPYIAEVA RIADTFVSCY PNAGLPNAFG EYDESPERQA SYIAEFAEAG LVNLVGGCCG TAPPHIAEIA KVVDGKTPRE LPQIPVATRL SGLEPLNIND ESLFVNIGER TNITGSARFR NLIKAEDYDT ALSVALQQVE VGAQVIDINM DEGMIDGVAA MDRFTKLIAS EPDISRVPVM IDSSKWEVIE AGLKNVQGKP IVNSISMKEG EEKFIREAQL CRKYGAAVVV MAFDEQGQAD NLERRKEICG RAYRILTEKV GFPAEDIIFD PNCFALATGI EEHATYGIDF IEACAWIKEN LPGVHISGGI SNVSFSFRGN NPVREAIHAV FLFHAIKAGL DMGIVNAGAL VPYDSIDPEL RDRIEDVVLN RRADAAERLL EIAERFNKAD KGEDPQAAEW RSLPVRERIT HALVKGIDAH VDDDTEELRA EIEAAGGRPI EVIEGPLMDG MNVVGDLFGS GKMFLPQVVK SARVMKKAVA YLLPYIEAEK ADAGTTGSKD TNGTIVMATV KGDVHDIGKN IVGVVLQCNN FEVIDLGVMV PPQKILDAAR EHDADIIGLS GLITPSLDEM SNFAVEMERA GLEIPLLIGG ATTSRAHTAV KISPRRSGPV VWVKDASRSV PVAAALLDDK QRPALLEATE KDYASLRERH AQKNDRPMLT LEKARANRTP IEWDGYTPPV PAQGVGVREF IDYDLAELRE YIDWQPFFNA WEMKGRFPDI LNNPATGEAA RKLYNDAQEM LDTLIKEKWL TANGVIGFFC ANAVGDDIEV YTDDTRTEVL TTLYNLRQQG EHRDGIPNRS QGDFIAPKET GLRDYIGAFA VTAGLGSQAK IMEFKAALDD YSAILLESLA DRLAEAFAER MHERVRTEFW GYQPDEQLDN NALIAERYVG IRPAPGYPSC PEHTEKATLF GLLDATERTG IELTESMAMW PGAAVSGWYF SHPQSQYFVV GRLAQDQVAD YARRKGWTLQ EAERWLAPNL GYNPED // ID E6U1T9_BACCJ Unreviewed; 1145 AA. AC E6U1T9; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAY-2015, entry version 32. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADU31586.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADU31586.1}; GN OrderedLocusNames=Bcell_3344 {ECO:0000313|EMBL:ADU31586.1}; 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 {ECO:0000313|EMBL:ADU31586.1, ECO:0000313|Proteomes:UP000001401}; RN [1] {ECO:0000313|Proteomes:UP000001401} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 21833 / DSM 2522 / FERM P-1141 / JCM 9156 / N-4 RC {ECO:0000313|Proteomes:UP000001401}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002394; ADU31586.1; -; Genomic_DNA. DR RefSeq; WP_013489917.1; NC_014829.1. DR RefSeq; YP_004096317.1; NC_014829.1. DR EnsemblBacteria; ADU31586; ADU31586; Bcell_3344. DR KEGG; bco:Bcell_3344; -. DR PATRIC; 45162752; VBIBacCel7049_3440. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; BCEL649639:GHTT-3432-MONOMER; -. DR Proteomes; UP000001401; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001401}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADU31586.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001401}; KW Transferase {ECO:0000313|EMBL:ADU31586.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 226 226 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 722 722 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1145 AA; 126473 MW; F3127FBC532DAD4F CRC64; MATLFEQQLR KKILIFDGAT GTMFQQANLT AEDFGGEEYE GCNEYLNIVS PHVVERIHHE YFKAGSDIIE TNTFGATSIV LDDYDLGHIA EEVNFKSAQL ARRAADEWST SEWPRFVAGA MGPTTKAISV TGGVTFEQLI DTYEEQARGL IRGEVDVLLL ETSQDMRNVK AAFLGIQRAS EKLGKTLPLI VSGTIEPMGT TLAGQSIEAF YLSLEHMNPV MVGLNCATGP EFMREHIRSL SNLATTAVSC YPNAGLPDEE GNYHESPESL AKKIAGFAEK GWLNMVGGCC GTTPAHIKAL ADAIKPFSPR KVPEDHPHAV SGIEPLIYDE DMRPLMVGER TNVIGSRKFK NLIADGKYEE ASEIARAQVK NGAHIIDICL ADPDREELED MEHFLQQVIN KVKVPLMIDS TDDAVIEKAL TYSQGKAIIN SINLEDGEER FEKVAPLIRQ YGAAVVVGTI DEIGMATTAD RKLEVAKRSY DLLVNKYGLN PKDIIFDPLV FPVGTGDEQY IGAAKETVDG IKLIKEALPD CLTILGVSNV SFGLPPVGRE IVNAVYLYHC TKAGLDYAIV NTEKLERFAS IAPEEIEMAE TLLFKTSSET LAKLVEFYRG KKSTVKKEVN NLPLEERLAH YVVEGTKEGL IPDLEKALEK FSDPLEIING PLMTGMAKVG ELFDKNQLIV AEVLQSAEVM KAAVAYLEDF MEVKDDSGKG KVILATVKGD VHDIGKNLVE IILSNNGFRV VDLGIKVTSQ TLIDAVRKEK PDMIGLSGLL VKSAQQMMLT AQDLKQSEVS IPILVGGAAL SRKFTDNKIS PEYEGLVMYA KDAMDGLHIA NQLQKPEERE KLVTAHKEKL ENIAISKAKE TKKAEPEVAV KVRSNVSRTA PIHTPPDLDK HILRNFSLPH LTPYLNWQTL LCSHLGVQGN IKRRLEKKDP KTLELKGLVE ELLVQGDKEG SISVNGMYQF FPAQSDGDDI IVYDPNEKGK VLERFTFPRQ TKSPYLCLAD FLRSVDSGEM DYVGFLAVTA GGGIREQARV WKEQGDYLKS HAIQALALEL AEGFAEYVHH LMRDQWGIPD PADFTMQQRF SAKYEGVRVS YGYPACPNLE DQAKLFNLIK PGEIGIELTD GFMMEPEASV TAMVFAHPEG RYFSV // ID E6U1U0_BACCJ Unreviewed; 638 AA. AC E6U1U0; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAY-2015, entry version 31. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=Bcell_3345 {ECO:0000313|EMBL:ADU31587.1}; 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 {ECO:0000313|EMBL:ADU31587.1, ECO:0000313|Proteomes:UP000001401}; RN [1] {ECO:0000313|Proteomes:UP000001401} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 21833 / DSM 2522 / FERM P-1141 / JCM 9156 / N-4 RC {ECO:0000313|Proteomes:UP000001401}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ADU31587.1; -; Genomic_DNA. DR RefSeq; WP_013489918.1; NC_014829.1. DR RefSeq; YP_004096318.1; NC_014829.1. DR ProteinModelPortal; E6U1U0; -. DR EnsemblBacteria; ADU31587; ADU31587; Bcell_3345. DR KEGG; bco:Bcell_3345; -. DR PATRIC; 45162754; VBIBacCel7049_3441. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR BioCyc; BCEL649639:GHTT-3433-MONOMER; -. DR Proteomes; UP000001401; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001401}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ADU31587.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000001401}; KW Transferase {ECO:0000313|EMBL:ADU31587.1}. SQ SEQUENCE 638 AA; 70536 MW; 1AF89717624080A9 CRC64; MGLLDDLKKQ VIVADGAMGT LLYSYGVGNC FEEMNLSHPD QIKEIHGAYL AAGSQVIQTN TYGANYEKLL RYGLEDQVKN INTKAVRLAK AALEEHRSDL SSFSSEENKY ILGTLGGVRA VPGKPISLTE IKRSFREQLY CLLMEEVDGI LLETYYDFEE LKTVLQIARK ETQLPIIAQV SLHDIGIVQG GISVDDAMKT LDDLGANIVG LNCRMGPHHM IRSLEQVSIP ENAYLSAYPN ASLPSYSNGR YHYSSNSEYF QQSANLLWEQ GVSLIGGCCG TTPEHIKAIA DAVKGKAPIT EKEITVNQKS VVHIETPEPP KVEKLNEVVK TRSSIIVELD TPKDLVTTKF LEGAKALKEA GVDAVTLADN SLANPRICNL SMSTILKEKL QVTPLAHITC RDRNLIGLQS HLMGLSTLGI DNVLAITGDP AKVGDFPGAT SVYDLSSFEL IQMIKQCNEG LSFTGKPLGK KTNFTVAAAF NPNVRHLDKA VERLQKKIDC GADYFMTQPV YSEKQIENIY EHTKHIKAPI YLGIMPLTSY RNAEFLHHEV PGIKLTDDIR QAMALHKEDK ARSQQEGIAI AKNLIDTALH YFNGIYLITP FTKYEITVEL TNYIKEKTSA ATDRQAGPIR KVYDGNII // ID E6U6U9_ETHHY Unreviewed; 792 AA. AC E6U6U9; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 29-APR-2015, entry version 29. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADU26916.1}; GN OrderedLocusNames=Ethha_1378 {ECO:0000313|EMBL:ADU26916.1}; 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 {ECO:0000313|EMBL:ADU26916.1, ECO:0000313|Proteomes:UP000001551}; RN [1] {ECO:0000313|EMBL:ADU26916.1, ECO:0000313|Proteomes:UP000001551} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18485 / JCM 12961 / CGMCC 1.5033 / YUAN-3 RC {ECO:0000313|Proteomes:UP000001551}; 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 ----------------------------------------------------------------------- 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; ADU26916.1; -; Genomic_DNA. DR RefSeq; WP_013485271.1; NC_014828.1. DR RefSeq; YP_004091647.1; NC_014828.1. DR EnsemblBacteria; ADU26916; ADU26916; Ethha_1378. DR KEGG; eha:Ethha_1378; -. DR PATRIC; 45209918; VBIEthHar145175_1503. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR BioCyc; EHAR663278:GIWT-1415-MONOMER; -. DR Proteomes; UP000001551; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001551}; KW Methyltransferase {ECO:0000313|EMBL:ADU26916.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001551}; KW Transferase {ECO:0000313|EMBL:ADU26916.1}. SQ SEQUENCE 792 AA; 84976 MW; B877983F7B5D9F1D CRC64; MRVLEDLGKR IVFFDGGMGT LLQAKGLEPG ELPELWNLTH ADVVRDIHSA YRAAGAEIIK TNTFGANRFK YPEAGLLERV ITEGVRLAKE AAGSDGLVAM DIGPTGKLLE PIGDLPFERA VEVFGEEAEI GAKAGADLIL IETMTDTYEC KAAVLAAKER TNLPVFATLV SDDKGKLLTG GDIPSAVALL EGLGVNALGL NCGFGPDLMR RLLPGLLECA SVPVIINPNA GLPKTERGRT IYTIGPDAFA GEMREIVRGG AWIVGGCCGT TPEYIAAEVR TCKNIVPVPL VPKRHTVVSS YAKAVDFAHI APVLIGERIN PTGKPRLKQA LRDGDIDYVL QEGIAQMQLG AHVLDVNVGL PELDEPNVMA KVVSALQGVV DIPLQIDTSS PEAMERALRL YSGKALINSV NGKEESMHAI FPLVKKYGGV VVALTLDESG IPATAEGRVQ IARKIMETAA TYGIAPENLL VDPLVMTISA GQENAAVTLE ALERIHRELG LHTSLGVSNV AFGLPEREKL NAAFFTMALQ RGLDAAIVNP KSQAMMDVYR AYRALSGKDE QCMEYIAAYS GQKEKTAPLS HGEIISLFDA IVTGLKTSAA EAAEQLVVTK QPLDIIEEQL IPALDQVGYD FETGVLFLPQ LLMSAEAARA AFEVLRGKLD VDGQKTRKAK VILATVKGDI HDIGKNIVKI LLQNYSYEVI DLGKNVLPAD VVKTARNEQV HLVGLSALMT TTVENMEETI RQLRKDVPAC KIMVGGAVLN AEYAARIGAD FYAKDAMGAV RYAEQLFEDT VG // ID E6UKG7_RUMA7 Unreviewed; 788 AA. AC E6UKG7; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADU24163.1}; GN OrderedLocusNames=Rumal_3726 {ECO:0000313|EMBL:ADU24163.1}; OS Ruminococcus albus (strain ATCC 27210 / DSM 20455 / JCM 14654 / NCDO OS 2250 / 7). OG Plasmid pRUMAL02 {ECO:0000313|EMBL:ADU24163.1, OG ECO:0000313|Proteomes:UP000006919}. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus. OX NCBI_TaxID=697329 {ECO:0000313|EMBL:ADU24163.1, ECO:0000313|Proteomes:UP000006919}; RN [1] {ECO:0000313|Proteomes:UP000006919} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27210 / DSM 20455 / JCM 14654 / NCDO 2250 / 7 RC {ECO:0000313|Proteomes:UP000006919}; 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; CP002405; ADU24163.1; -; Genomic_DNA. DR RefSeq; WP_013483708.1; NZ_JHYT01000016.1. DR RefSeq; YP_004090049.1; NC_014825.1. DR EnsemblBacteria; ADU24163; ADU24163; Rumal_3726. DR KEGG; ral:Rumal_3726; -. DR PATRIC; 45355680; VBIRumAlb150544_0412. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR BioCyc; RALB697329:GIWQ-3815-MONOMER; -. DR Proteomes; UP000006919; Plasmid pRUMAL02. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006919}; KW Methyltransferase {ECO:0000313|EMBL:ADU24163.1}; KW Plasmid {ECO:0000313|EMBL:ADU24163.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006919}; KW Transferase {ECO:0000313|EMBL:ADU24163.1}. SQ SEQUENCE 788 AA; 85655 MW; AB6EE1F05C0C2C93 CRC64; MGFRELLNNK EFVILDGAMG TMLQAKGLKM GETPEVMNIE KPEWLLDIHR QYIEAGSDII YANTFGGNRH KLAKCGYSVE TLIGEGIRLA RKAAEGHDTL VALDIGSIGV MLEPTGTLTF EEAYDIFKEM VIAGREADVI VFETMTDLYE LKAAILAAKE NSDLPIMCTM TFEENMRTFT GVDISAMCLT AEGLGVDALG VNCSLGPKEL YPVVEKICQW TTLPVVVKPN AGLPDPVTNE YNCSAEDFAD FAEKLIPLGI KVIGGCCGTD PSYIAALKKM LEGKKYVERE AHIPAVCCSP TETVVIDQPR IIGERINPTG KKRFKQALLE DDIDYILGQA MEQIDAGADI LDVNVGLPAI DEKAMMVKAV KALQGVCDVP LQLDSTIPEV MEAALRVYNG KPIVNSVNAE EKSLETVLPL VKKYGAAVVG LTLDENGIPK TADARFALAK KILDRAMAIG IRKEDVYIDC LTLTASAEQE NVMQTVNAVR RVKEELGLRT VLGVSNISFG LPSREIVNHN FLMMCLTSGL DLPIMNPNID SMTATVRTYK LLTNIDKNSM DFIAHYGADT SSPAPKAEKK SDMDLPYAIE HGLKGEGAEI TAKLLETTDS MVIINEMLVP ALDKAGEQFE KGKIFLPQLI QTAGVAQACF EVIKQKMLAE GGNSVSKGKI ILATVKGDIH DIGKNIVKVL LENYGYEVID LGKDVDYQTV VDAAIENDVH LVGLSALMTT TLVSMEETIK LLRANNVDCK IMVGGAVVTP DYAEQIGADF YSKDAKQSVD IARQVFGN // ID E6V0A2_VARPE Unreviewed; 349 AA. AC E6V0A2; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADU34416.1}; GN OrderedLocusNames=Varpa_0194 {ECO:0000313|EMBL:ADU34416.1}; OS Variovorax paradoxus (strain EPS). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Variovorax. OX NCBI_TaxID=595537 {ECO:0000313|EMBL:ADU34416.1, ECO:0000313|Proteomes:UP000008917}; RN [1] {ECO:0000313|Proteomes:UP000008917} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EPS {ECO:0000313|Proteomes:UP000008917}; 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 ----------------------------------------------------------------------- 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; ADU34416.1; -; Genomic_DNA. DR RefSeq; WP_013538663.1; NC_014931.1. DR RefSeq; YP_004152527.1; NC_014931.1. DR EnsemblBacteria; ADU34416; ADU34416; Varpa_0194. DR KEGG; vpe:Varpa_0194; -. DR PATRIC; 45386263; VBIVarPar156291_0196. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR BioCyc; VPAR595537:GHGJ-200-MONOMER; -. DR Proteomes; UP000008917; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008917}; KW Methyltransferase {ECO:0000313|EMBL:ADU34416.1}; KW Transferase {ECO:0000313|EMBL:ADU34416.1}. SQ SEQUENCE 349 AA; 37587 MW; D9C5B09304A7A408 CRC64; MKPLVYTRGQ ALAGILEKRI AILDGAMGTM IQRFKLTEEQ YRGERFKDFE RDVKGNNELL SLTRPDVISD IHEGYLAAGA DLIETNTFGA TTIAQEDYKM AHLAREMNLE SARIARAACD KFSTPDKPRF VAGALGPTPK TASISPDVND PGARNVDFEQ LRAAYYEQTE ALVEGGADVI LVETIFDTLN AKAALFAVDE YFDNSGERLP LIISGTVTDA SGRILSGQTV TAFWHSVRHA RPLAIGLNCA LGAALMRPYI QELARVAGDT FISCYPNAGL PNPMSDTGFD ETPDVTSRLL HEFAAEGLVN IVGGCCGTTP DHIAAIGRAV APVPGRLLNN TAGFYSEAA // ID E6VK05_RHOPX Unreviewed; 1293 AA. AC E6VK05; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAY-2015, entry version 31. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADU43267.1}; GN OrderedLocusNames=Rpdx1_1650 {ECO:0000313|EMBL:ADU43267.1}; OS Rhodopseudomonas palustris (strain DX-1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Rhodopseudomonas. OX NCBI_TaxID=652103 {ECO:0000313|EMBL:ADU43267.1, ECO:0000313|Proteomes:UP000001402}; RN [1] {ECO:0000313|Proteomes:UP000001402} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DX-1 {ECO:0000313|Proteomes:UP000001402}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002418; ADU43267.1; -; Genomic_DNA. DR RefSeq; WP_013501417.1; NC_014834.1. DR RefSeq; YP_004108000.1; NC_014834.1. DR EnsemblBacteria; ADU43267; ADU43267; Rpdx1_1650. DR KEGG; rpx:Rpdx1_1650; -. DR PATRIC; 45343569; VBIRhoPal82507_1681. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR BioCyc; RPAL652103:GHQR-1665-MONOMER; -. DR Proteomes; UP000001402; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001402}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 770 770 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1293 AA; 139603 MW; 02E02F2CBB2EB394 CRC64; MSTSKSPIAD RLHALAAQRI LVLDGAMGTM IQQLQLDEAA FRGMRFKDFH RDLRGNNDLL ILTQPQAIED IHAQYLRAGA DIVATNTFSS TSIAQADYDM SDLAYEMSRD GARLARNAAA KVEAEDGKPR FVAGAIGPTN RTASISPDVA NPGYRAVTFD DLRIAYAEQI NGLLDGGADI LLLETIFDTL NAKAALYAIA EITDARGIDV PVMISGTITD KSGRLLSGQM PEAFWNSVRH AKPLTIGFNC ALGAKDLRAH IADISRVADT LVCAYPNAGL PNEFGQYDES PEYMAGLVGE FAEAGLVNIV GGCCGTTPAH IKAIAEAVAP HQPRVIPTIE PRLRLSGLEP FELTAAIPFV NVGERTNVTG SAKFRKLITA GDYAAALQVA RDQVENGAQI IDVNMDEGLL DSEAAMVTFL NLVAAEPDIA KVPVMVDSSK FNVIEAGLKC LQGKPVVNSI SLKEGEDKFV HEAGIAKRHG AAVVVMAFDE TGQADTYARK TEICARAYDI LVNRIGFPPE DIIFDPNIFA IATGLEEHNN YGVDFIEATR WIRQNLPHAH VSGGVSNLSF SFRGNEPVRE AMHSVFLYHA IKAGMDMGIV NAGQMIVYDD IDPELRQVCE DVILNRDAGA SERLLALADK YRGQGKQQKE QDLAWRSWPV EQRLSHALVH GITEFIELDT EEARAKAERP LHVIEGPLMA GMNVVGDLFG DGKMFLPQVV KSARVMKQAV AYLMPFMETE KAANLAAGKD SGERSSAGKI VLATVKGDVH DIGKNIVGIV LQCNNFEVID LGVMVPAAKI IETAKAENAD IIGLSGLITP SLDEMSFLAG ELQRSGFDIP LLIGGATTSR VHTAVKIDPA YPAGSVVHVN DASRAVGVAS SLLSKDKGAA YAAEIRADYA KISAAHHRAQ ADKKRLTLAA ARANATKIDW AATKPVKPSF IGTRSFSSYS LAELVHYIDW TPFFQAWELA GRFPAILEDS VVGEAARSLY ADARKMLDRI VTENWFTANA TIGFWPANAQ GDDILVYADE ARTTPIATLH SLRQQLDKRE GRANAALSDF IAPVASGVAD YIGGFVVTAG IGEDVIADKF KAERDDYSSI MVKALADRLA EAFAERMHAR VRREFWGYAP DETLSADDLI LEKYQGIRPA PGYPAQPDHT EKATLFELLD AEASAGVTLT ESFAMWPGSS VSGLYFSHPQ SAYFGVGKIE RDQVEDYAAR KGWDVATAER WLAPVLNYIP SRSTGATDET GMPPLAPQAD APLSADDAAL ASHPQGCTCA LHLAWRKQKV AAK // ID E6VR40_DESAO Unreviewed; 803 AA. AC E6VR40; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 29-APR-2015, entry version 26. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADU64124.1}; GN OrderedLocusNames=Daes_3132 {ECO:0000313|EMBL:ADU64124.1}; OS Desulfovibrio aespoeensis (strain ATCC 700646 / DSM 10631 / Aspo-2). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=643562 {ECO:0000313|EMBL:ADU64124.1, ECO:0000313|Proteomes:UP000002191}; RN [1] {ECO:0000313|Proteomes:UP000002191} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700646 / DSM 10631 / Aspo-2 RC {ECO:0000313|Proteomes:UP000002191}; 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 ----------------------------------------------------------------------- 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; ADU64124.1; -; Genomic_DNA. DR RefSeq; WP_013516025.1; NC_014844.1. DR RefSeq; YP_004122870.1; NC_014844.1. DR ProteinModelPortal; E6VR40; -. DR EnsemblBacteria; ADU64124; ADU64124; Daes_3132. DR KEGG; das:Daes_3132; -. DR PATRIC; 45206396; VBIDesAes51796_3184. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR BioCyc; DAES643562:GH9Z-3191-MONOMER; -. DR Proteomes; UP000002191; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002191}; KW Methyltransferase {ECO:0000313|EMBL:ADU64124.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002191}; KW Transferase {ECO:0000313|EMBL:ADU64124.1}. SQ SEQUENCE 803 AA; 85388 MW; 4CC7D7794901FF9C CRC64; MPDFRSILRD DRIYFFDGGY GTLLQGRGLP PGLSPELWGL KAPEVIRGVH QEYLEAGADI LTTNTFGGSR PKLGLDADPY ELNRAMTRIA RQVAGDRAFV AASIGPTGHF VEPLGDLTFR ELVEIFKEQI RGCVDGGADL ILGETHFDLA EARAVVVAAR LVCSLPVAMS MTFEGPASLT GTTPLTFVDT MQNMGVELIG TNCSAGPEQM RDTLAAWAPR LTVPCFAEAN AGLPELDAEG NTAFRLGPEP FAEQAVRFVD LGAKFIGGCC GTTPEHIRAV RGKVGDTPWR RPAPTDDAQM VLTSRSVSVP VGFSHPGVII GERINPTGKP LLTSELQDGV FAEALRFAAE QIDLGAPVLD VNVGAPMADE KILLPGLIKA LSGRFTTPLS IDSNDSGAVE AGLWVYPGSP LVNSISGEPG KMEALGPLCK LFGAPFILLP IVGRKLPVTA TERLAVIEDL LVEAEGLGIP RRLIMVDALA LTVSSKPEAA RHSMEVMRRC RDDWGLPTTI GLSNISFGLP ARELLNSTFL ALSMASGLCS FIANPNSARI QETLHAAEAL LNRDPQAARY IGRFSDWTGG GGSQAAPTAR AATDTPDLPP VQAAVIKGDK GGVVPLVEAE LDRGMTAMSI VNDLLIPGIL VVGEKYERKE YFLPQLLQSA ETMQVAFARL KPLLEADGGS ADRPVVVMAT VEGDIHDIGK NIVCLMLKNY GFDVVDLGKD VAAERIVDAA QERGAAIIGL SALMTTTMVR MEDTVRLVRE RGLKTKVIIG GAVVTEKFCT AIGADGWSTD AVRAVKLAQS LVA // ID E6W3E3_DESIS Unreviewed; 1142 AA. AC E6W3E3; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAY-2015, entry version 30. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADU65736.1}; GN OrderedLocusNames=Selin_1001 {ECO:0000313|EMBL:ADU65736.1}; OS Desulfurispirillum indicum (strain ATCC BAA-1389 / S5). OC Bacteria; Chrysiogenetes; Chrysiogenales; Chrysiogenaceae; OC Desulfurispirillum. OX NCBI_TaxID=653733 {ECO:0000313|EMBL:ADU65736.1, ECO:0000313|Proteomes:UP000002572}; RN [1] {ECO:0000313|EMBL:ADU65736.1, ECO:0000313|Proteomes:UP000002572} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1389 / S5 {ECO:0000313|Proteomes:UP000002572}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002432; ADU65736.1; -; Genomic_DNA. DR RefSeq; WP_013505619.1; NC_014836.1. DR RefSeq; YP_004112292.1; NC_014836.1. DR ProteinModelPortal; E6W3E3; -. DR EnsemblBacteria; ADU65736; ADU65736; Selin_1001. DR KEGG; din:Selin_1001; -. DR PATRIC; 45166922; VBIDesInd86994_1024. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; DIND653733:GHGZ-1021-MONOMER; -. DR Proteomes; UP000002572; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002572}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002572}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 232 232 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 296 296 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 730 730 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1142 AA; 125914 MW; FC6084E5863266AC CRC64; MTTQQQRIDL LRQRAASHIL CLDGATGTAL ASFELTAADF GGAAYDGCNE YLVITRPDVV EGVHRRYLEA GADIIETNSF GSTSIVLREY ALEDQVHRLN LEAARIARTM ADRYSTADKP RFVAGCMGPT SKSICITGGV TFHELRDAFR QQALALIEGG VDYLLLETMQ DTLNLKAGLI GATEAMEQLG VDMPLAVSVT IEPMGTMLAG QAIEALYNSI EHFPLLYVGL NCATGPDFMT GHIRSLAQLA TCGVACVPNA GLPDENGRYQ QSPTDVAGKL AQFMDEGWLN FVGGCCGTTD EHIRMISAEA AKRPARTPQP ATPFALSGIE YLPIEPGELY LVGERTNVIG SRKFKRLIAE GNLDEAVEVA RKQIRGGAHI IDVCLANPDR DEHTDMQAFM AALMRSIKVP FMIDSTDAAV VEVALQYSQG KAIINSINLE QGTERLDEVV PLLKTYGAAV VVGTIDEDPE HGMAVTAQRK LEIARRSYDI LVNRYGLRPE NIVFDPLVFP VATGDEQYRT SARETIEGIA LIREEFPHCA ITIGLSNVSF GLPPAAREIL NAVFLKHCVD AGLTMPIINP EMMVRYASIE AEDLQLAENL IFARGEDPIT PFADKFRERK TQQKATSDES LPVAQRLQSN IVEGSRENLH PRLDEAMAQM PPLDVINGPL MAGMAEVGRL FNDNKLIVAE VLQSAEVMKA SVDYLSQFME ADQVTTRGTM VLATVKGDVH DIGKNLVDII MTNNGYKVIN LGIKIPSEQI IEAIEKHKPD FVGLSGLLVR SAQQMTTTAA DMKAAGIDIP LMVGGAALSE NFTSQKIQPQ YEGLAIYCRD PMECLALAGR LLDDDQRQSV VEELWNKRLK REELSQEAAS TRPAASTASQ RVQPVERVPL PPDLKRHVHM ESDLQTIFDH INPHMLYGKH LGYKGFPEAL ARGEAKAVQL QKQVQEIMDE IQRRGDIQPG AVYRYFQAHR SSENSITLLD SLEQPLRTIS FPRNPGLDLC LADYVHPERD YLCLFIVSTG PKLGQLAQQE KEKGNYQRSH IMASLALEMA ESLAEILHIR LRHMWGIGEQ SPLPKQDLFG ARYRGKRYAP GYSALPDLSV QEDLFALLHP DELGVKLTES HMMDPEASTS GFVFHHPQAR YF // ID E6WFP2_PANSA Unreviewed; 311 AA. AC E6WFP2; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 01-APR-2015, entry version 23. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADU70316.1}; GN OrderedLocusNames=Pat9b_3017 {ECO:0000313|EMBL:ADU70316.1}; OS Pantoea sp. (strain At-9b). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Pantoea. OX NCBI_TaxID=592316 {ECO:0000313|EMBL:ADU70316.1, ECO:0000313|Proteomes:UP000001624}; RN [1] {ECO:0000313|EMBL:ADU70316.1, ECO:0000313|Proteomes:UP000001624} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=At-9b {ECO:0000313|EMBL:ADU70316.1, RC ECO:0000313|Proteomes:UP000001624}; 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 ----------------------------------------------------------------------- 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; ADU70316.1; -; Genomic_DNA. DR RefSeq; WP_013510168.1; NC_014837.1. DR RefSeq; YP_004116872.1; NC_014837.1. DR EnsemblBacteria; ADU70316; ADU70316; Pat9b_3017. DR KEGG; pao:Pat9b_3017; -. DR PATRIC; 45320439; VBIPanSp129740_3016. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR BioCyc; PSP592316:GI0L-3087-MONOMER; -. DR Proteomes; UP000001624; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001624}; KW Methyltransferase {ECO:0000313|EMBL:ADU70316.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001624}; KW Transferase {ECO:0000313|EMBL:ADU70316.1}. SQ SEQUENCE 311 AA; 33057 MW; 7B5E98ABF4A94753 CRC64; MWRNPVAQAL SQTDTLILDG ALATELEARG CNLADTLWSA KVLMENPELI YQVHYDYFAA GAHCAITASY QATPQGFAQR GLDEAQSRAL IQQSAALAQR ARDDYRAASG TNAPLLVAGS IGPYGAFLAN GAEYRGDYAL PAAEMKAFHR PRVAALLEAG VDLLACETLP SFAEAQALVS LLAEFPDSSA WFSFTLRDAN HISDGTPLST VAALLNASPQ VVAVGINCVA LENVTPALRS LQALCTQPLL VYPNSGEQYD ATSKTWHSAP SGCTLHDKFP EWQQAGARLI GGCCRTTPQD IAAIAACCQP Q // ID E6WI44_PANSA Unreviewed; 1243 AA. AC E6WI44; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 01-APR-2015, entry version 33. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADU67558.1}; GN OrderedLocusNames=Pat9b_0232 {ECO:0000313|EMBL:ADU67558.1}; OS Pantoea sp. (strain At-9b). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Pantoea. OX NCBI_TaxID=592316 {ECO:0000313|EMBL:ADU67558.1, ECO:0000313|Proteomes:UP000001624}; RN [1] {ECO:0000313|EMBL:ADU67558.1, ECO:0000313|Proteomes:UP000001624} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=At-9b {ECO:0000313|EMBL:ADU67558.1, RC ECO:0000313|Proteomes:UP000001624}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002433; ADU67558.1; -; Genomic_DNA. DR RefSeq; WP_013507427.1; NC_014837.1. DR RefSeq; YP_004114114.1; NC_014837.1. DR EnsemblBacteria; ADU67558; ADU67558; Pat9b_0232. DR KEGG; pao:Pat9b_0232; -. DR PATRIC; 45314731; VBIPanSp129740_0228. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; PSP592316:GI0L-251-MONOMER; -. DR Proteomes; UP000001624; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001624}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001624}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 263 263 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 326 326 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 327 327 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 775 775 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1243 AA; 137528 MW; 4D119676EDB309B3 CRC64; MSGWHFSQRN DVDGARVSNR IEALHQQLAR RIMILDGGMG TMIQSYKLDE QDFRGSRFVD WPCDLKGNND LLVLSKPEVI REIHHAYLAA GADILETNTF NSTTIAMADY EMEALSAEIN FEAAKLARAC ADEWSAKTPE RPRYVAGVLG PTNRTCSISP DVNDPAFRNI TFNQLVDAYR ESTHALIKGG SDLIMIETVF DTLNAKAAIY AVQAEMEAMG VKLPLMISGT ITDASGRTLS GQTTEAFYNS LRHAEPLSFG LNCALGPDEL RQYVAELSRI AEGYVTAHPN AGLPNAFGEY DLDAATMAQQ IGEWARSGFL NIIGGCCGTT PEHIAAMAAV VDGVAPRQLP EIPVACRLSG LEPLNISADS LFVNVGERTN VTGSAKFKRL IKEEKYNEAL DVARQQVESG AQIIDINMDE GMLDAEAAMV RFLNLIAGEP DIARVPIMID SSKWEVIEKG LQCIQGKGIV NSISMKEGIE PFIDHARKVR RYGAAMVVMA FDEVGQADTR ARKIEICRRA YQILTEEVGF PPEDIIFDPN IFAVATGIEE HNNYAMDFIG ACEDIKRELP HAMISGGVSN VSFSFRGNEP VREAIHAVFL YYAIRNGMDM GIVNAGQLAI YDDLPAELRD AVEDVILNRR DDGTERLLEL AEKYRGAKGD GEQEKQQAEW RSWDVVKRLE YSLVKGITEF IEQDTEEARQ ASARPIEVIE GPLMSGMNVV GDLFGEGKMF LPQVVKSARV MKQAVAYLEP FIQASKEAGS SNGKIVLATV KGDVHDIGKN IVGVVLQCNN YEIIDLGVMV PSDKILKTAI EQKADIIGLS GLITPSLDEM VNVAKEMERQ GFTLPLLIGG ATTSKAHTAV KIEQNYSGPT VYVQNASRTV GVVSSLLSPT LKEDFVARTR KEYDTVRIQH ARKKPRTPPV SLQTARDNDF AFDWASYTPP VAHRLGVTAV EASIETLRNY IDWTPFFMTW SLAGKYPRIL QDEVVGEEAQ RLFHDANAML DMLGQQGTLQ PRGVVGIFPA NRVGDDIEIY TDENRNQVLC VSHHLRQQTE KTDFANYCLA DFVAPKSSGK ADYLGAFAVT GGLEEDALAE AYDQQHDDYN KIMIKAVADR LAEAFAEYLH ERVRKVIWGF AAHENLSNDE LIRENYQGIR PAPGYPACPE HTEKAQIWQL LDVETHTGMK LTESFAMWPG ASVSGWYFSH PDSRYFAVAQ IQRDQVEDYA ARKGMSISEV ERWLAPNLGY DAD // ID E6WTZ1_PSEUU Unreviewed; 364 AA. AC E6WTZ1; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAY-2015, entry version 30. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADV27640.1}; GN OrderedLocusNames=Psesu_1798 {ECO:0000313|EMBL:ADV27640.1}; OS Pseudoxanthomonas suwonensis (strain 11-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Pseudoxanthomonas. OX NCBI_TaxID=743721 {ECO:0000313|EMBL:ADV27640.1, ECO:0000313|Proteomes:UP000008632}; RN [1] {ECO:0000313|EMBL:ADV27640.1, ECO:0000313|Proteomes:UP000008632} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=11-1 {ECO:0000313|Proteomes:UP000008632}; 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 ----------------------------------------------------------------------- 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; ADV27640.1; -; Genomic_DNA. DR RefSeq; WP_013535468.1; NC_014924.1. DR RefSeq; YP_004146871.1; NC_014924.1. DR EnsemblBacteria; ADV27640; ADV27640; Psesu_1798. DR KEGG; psu:Psesu_1798; -. DR PATRIC; 45337461; VBIPseSuw172708_1827. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR BioCyc; PSUW743721:GH68-1833-MONOMER; -. DR Proteomes; UP000008632; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008632}; KW Methyltransferase {ECO:0000313|EMBL:ADV27640.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008632}; KW Transferase {ECO:0000313|EMBL:ADV27640.1}. SQ SEQUENCE 364 AA; 39153 MW; 4A1769486160319D CRC64; MPRSLPWLHP ERVALLERAL RERILVIDGA MGTMIQRHQL EEADYRGERF AEGYDRQHHA AHDGHGPGCG HDLKGNNDLL LLTRPEVIEG IHRAYLEAGA DLVETNTFNA TSVSQADYHL EHLVHELNRA GAALARKACD EVEKATDQPR FVIGVLGPTS RTASISPDVN DPGFRNTSFD ELRGAYREAV EGLIDGGADT IMVETIFDTL NAKAALFAIE EVFEARGARL PVMISGTITD ASGRTLSGQT AEAFHTSLAH ARPLSIGLNC ALGARDLRPH VEALAKVSPY YVSAHPNAGL PNAFGGYDET PEEMAATLRE FAEAGLLNLV GGCCGTTPDH IRAIAEAVRG LPPRVPAGAL EQAA // ID E6X0N2_NITSE Unreviewed; 1168 AA. AC E6X0N2; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ADV45752.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADV45752.1}; GN OrderedLocusNames=Nitsa_0482 {ECO:0000313|EMBL:ADV45752.1}; OS Nitratifractor salsuginis (strain DSM 16511 / JCM 12458 / E9I37-1). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Nitratifractor. OX NCBI_TaxID=749222 {ECO:0000313|EMBL:ADV45752.1, ECO:0000313|Proteomes:UP000008633}; RN [1] {ECO:0000313|Proteomes:UP000008633} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16511 / JCM 12458 / E9I37-1 RC {ECO:0000313|Proteomes:UP000008633}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002452; ADV45752.1; -; Genomic_DNA. DR RefSeq; WP_013553448.1; NC_014935.1. DR RefSeq; YP_004167501.1; NC_014935.1. DR EnsemblBacteria; ADV45752; ADV45752; Nitsa_0482. DR KEGG; nsa:Nitsa_0482; -. DR PATRIC; 46982488; VBINitSal150288_0481. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR BioCyc; NSAL749222:GHWN-498-MONOMER; -. DR Proteomes; UP000008633; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008633}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADV45752.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008633}; KW Transferase {ECO:0000313|EMBL:ADV45752.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 230 230 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 296 296 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 297 297 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 732 732 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1168 AA; 130995 MW; B7FFCC99A5756AD3 CRC64; MKPADRIREI IAERYLVIDG AMGTQIQDLK VPAEAWLDEK GESQEGCNEL LNATAPELIG RIHKRYAMAG ADMIKTNTFG AMPWVLDEYG LGERAYELSR KGAELVKAVC EEYSTPEKPR FVLGSIGPGT KLPSLGHIDY EAMYEGYLET ARGLIDGGCD VFLLETCQDP LQIKAALHAC EAANAEKSAS LPIMVSVTIE LSGSMLIGTD AATIVTILEP FDILSLGFNC GTGPDQVKKH LKTLSERCKF PISVHSNAGL PQNRGGHTFY PMGPDEFAKK ELEFIDFDGV AFLGGCCGTT PQHIQALAKA IEGKKPKSPT GSIPPSIASL FESVELFQDP APLLIGERSN ATGSKAFRQL ILDEDYEGTL TVAQEQVRAG AHALDVNVEF AGRDGAKDMK EVISLYNQKI PIPLMPDATN VHTMEVGLRR IGGRPIINSA NLEDGIERFD RICRLAKKYG AALVLLTIDE TGMAKEKERK VEVAERMIER AVNLHGLRKE ELIVDVLTFT VGSGDEEYRD AAVQTLEAIR ELHKRHPELG TTLGLSNISF GLAPHARVYL NSVFLHHCVE AGLSSVIINV KHIVPLSRMS EEDIAVCEEL LFHADENSLF RFIEHFSDKS LETEQTDEEY EKLSTEEKIQ KLLMDGDKER LIPLVEEARH ELGADRIVNE ILIDGMKVIG ELFGSGQMQL PFVLQSAETM KATVDYLNPY LTKQEKESDT TLVIGTVKGD VHDVGKNLVD IILSNNGFKV KNIGIKVELE QFLEAYEEVN ADAIGMSGLL VKSTQVMKEN LEELARRGIE IPIIMGGAAL TRGFVDDYCR PIYKGPIFYC RDAFDGVVAM SRIEEWKKDP SKPLDTRMAG DMNERVVKEK KEVVIPPFEE IKMPKPVEIP TPPFWGRRVM DRENLDLSMI FDWVNKRTLF KMHWGYKSKG MSKEEYQKLL DKTVYPAWER LKDTFLKEKL FEPTILYGYY PCRSDDQELF LFSPDEGWFS ESEVNREPLE EIVGRAVGVF NFPRQRRKPY RALSDFFRHE RHDVVALTCV SAGPKITEYE RALYEKGEYL EYNLVHGLGV ELAEALAEVA HKQIRLDLGI ASEDEGHTLR DVRMNRYRGA RYSFGYAACP DLEQSRVIFD LLEPEEFGIE LSETFQIHPE QSTTAIVVHH PEATYYAV // ID E6X5D2_CELAD Unreviewed; 331 AA. AC E6X5D2; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADV49468.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADV49468.1}; GN OrderedLocusNames=Celal_2173 {ECO:0000313|EMBL:ADV49468.1}; OS Cellulophaga algicola (strain DSM 14237 / IC166 / ACAM 630). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Cellulophaga. OX NCBI_TaxID=688270 {ECO:0000313|EMBL:ADV49468.1, ECO:0000313|Proteomes:UP000008634}; RN [1] {ECO:0000313|EMBL:ADV49468.1, ECO:0000313|Proteomes:UP000008634} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14237 / IC166 / ACAM 630 RC {ECO:0000313|Proteomes:UP000008634}; RX PubMed=21475589; RA Abt B., Lu M., Misra M., Han C., Nolan M., Lucas S., Hammon N., RA Deshpande S., Cheng J.F., Tapia R., Goodwin L., Pitluck S., RA Liolios K., Pagani I., Ivanova N., Mavromatis K., Ovchinikova G., RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., RA Jeffries C.D., Detter J.C., Brambilla E., Rohde M., Tindall B.J., RA Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.; RT "Complete genome sequence of Cellulophaga algicola type strain RT (IC166)."; RL Stand. Genomic Sci. 4:72-80(2010). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; ADV49468.1; -; Genomic_DNA. DR RefSeq; WP_013550944.1; NC_014934.1. DR RefSeq; YP_004164966.1; NC_014934.1. DR EnsemblBacteria; ADV49468; ADV49468; Celal_2173. DR KEGG; cao:Celal_2173; -. DR PATRIC; 46909875; VBICelAlg158510_2203. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR BioCyc; CALG688270:GHJ1-2204-MONOMER; -. DR Proteomes; UP000008634; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008634}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ADV49468.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008634}; KW Transferase {ECO:0000313|EMBL:ADV49468.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 331 AA; 36054 MW; 46FD5DE13A02D7B2 CRC64; MKNIKEILKE RILVLDGAMG TMLQRHKFTE EDFRGERFKD WEHPLQGNND LLSLTQPAAI ADVHRKYFAA GADIVETNTF SSTTIAMADY YMEDLVYELN YESAKIAKQV ADEFTAKEPH KPRFVVGSIG PTNKTASMSP DVNDPGYRAV SFDELRIAYK QQVEALIDGG SDLLMVETIF DTLNAKAALF AIEEVKDERG IDIPIMVSGT ITDASGRTLS GQTAEAFLIS ISHIPILSVG FNCALGASQL VPHLEVLSAK TGFAVSAHPN AGLPNAFGEY DETPDEMAAQ IKEYVEKNLV NIVGGCCGTT PEHISAIANV VKDIKPRIVA G // ID E6XKP6_SHEP2 Unreviewed; 1244 AA. AC E6XKP6; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 29-APR-2015, entry version 28. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase, MetH {ECO:0000313|EMBL:ADV55467.1}; GN OrderedLocusNames=Sput200_3070 {ECO:0000313|EMBL:ADV55467.1}; OS Shewanella putrefaciens (strain 200). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=399804 {ECO:0000313|EMBL:ADV55467.1, ECO:0000313|Proteomes:UP000008209}; RN [1] {ECO:0000313|EMBL:ADV55467.1, ECO:0000313|Proteomes:UP000008209} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=200 {ECO:0000313|Proteomes:UP000008209}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002457; ADV55467.1; -; Genomic_DNA. DR RefSeq; WP_014611162.1; NC_017566.1. DR RefSeq; YP_006010933.1; NC_017566.1. DR ProteinModelPortal; E6XKP6; -. DR SMR; E6XKP6; 668-1244. DR EnsemblBacteria; ADV55467; ADV55467; Sput200_3070. DR KEGG; shp:Sput200_3070; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; SPUT399804:GLK4-3177-MONOMER; -. DR Proteomes; UP000008209; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008209}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADV55467.1}; KW Transferase {ECO:0000313|EMBL:ADV55467.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 258 258 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 774 774 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1244 AA; 138068 MW; 59439297EF563087 CRC64; MTIPSTKAGQ ILADIRKQLA ERILILDGAM GTMIQGYKLE EEDYRGERFK DWHTDVKGNN DLLVLTQPHI IKQIHTDYLN AGADIIETNT FNATTIAMAD YDMQSLSAEI NREGARLARE ACDEAFAATG IPRYVAGVLG PTNRTCSISP DVNDPGYRNV SFDELVTAYK ESTKALIEGG ADIIMVETIF DTLNAKAALF AIESVFDDLF GQHSKDRLPI MISGTITDAS GRTLTGQTTE AFYNSLRHIK PLSIGLNCAL GPKELRPYVE ELSRISECYV SAHPNAGLPN EFGGYDETPE DMANVIEDWA REGMLNIIGG CCGSTPEHIR VIRQAVEKYD PRVLPDIPVA CRLAGLEPLT IDAQTLFVNV GERTNVTGSA KFLKLIKEGK FEQALDVARE QVESGAQIID INMDEGMLDG VEIMHKFLNL IASEPDISRV PIMIDSSKWE VIEAGLKCIQ GKGIVNSISL KEGEAKFIEQ ATLVKRYGAA AIIMAFDEQG QADTKARKIE ICTRAYRVLV DKVGFPPEDI IFDPNIFAIA TGIDEHDNYA VDFIDAIKAI KATLPHAMIS GGVSNVSFSF RGNNPVREAI HAVFLYHAIK VGMDMGIVNA GQLAIYDDID PELKERVENV VLNLPCPVEG SSNTEQLLEI AEKFRGDGAQ VGKKEDLEWR SWPVNQRLAH ALVKGITEFI DEDTEAARQE AKRPLDVIEG PLMDGMNVVG DLFGSGKMFL PQVVKSARVM KKAVAYLNPF IEKEKVAGQS NGKILMVTVK GDVHDIGKNI VGVVLACNGF EVFDLGVMVS VERILEAVKE HNIDIIGMSG LITPSLDEMV HNVKTFHREG LTIPAIIGGA TCSKIHTAVK IAPHYPHGAI YIADASRAVP MVSKLVNNET RQATIDETYA EYDDMRTKRL SQAKRKEIVS LEAARENRCQ HDWASYTPFK PNVLGRQVFD DYPLEDLVER IDWTPFFRSW ELHGHYPEIL SDKVVGVEAQ KLFADGQAML KKIIEEKWLT AKAVIGLFPA NTVNYDDIEL YTDESRTTVE MTTHHLRMQL ERVGNDNFCL ADFVAPKDSG VADYMGGFAV TAGHGIDEHV ARFEANHDDY NAIMLKCLAD RLAEAFAERM HERVRKEFWG YAADEQLSNE ALIREKYKGI RPAPGYPACP DHTEKGLLWD LLKPDETIDL NITESYAMFP TAAVSGWYFA HPKSRYFGVS NIGRDQVEDY AKRKGMTVAE TEKWLAPVLD YDPE // ID E6XPF2_SHEP2 Unreviewed; 300 AA. AC E6XPF2; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 01-APR-2015, entry version 21. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADV52586.1}; GN OrderedLocusNames=Sput200_0096 {ECO:0000313|EMBL:ADV52586.1}; OS Shewanella putrefaciens (strain 200). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=399804 {ECO:0000313|EMBL:ADV52586.1, ECO:0000313|Proteomes:UP000008209}; RN [1] {ECO:0000313|EMBL:ADV52586.1, ECO:0000313|Proteomes:UP000008209} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=200 {ECO:0000313|Proteomes:UP000008209}; 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 ----------------------------------------------------------------------- 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; ADV52586.1; -; Genomic_DNA. DR RefSeq; WP_014609553.1; NC_017566.1. DR RefSeq; YP_006008052.1; NC_017566.1. DR EnsemblBacteria; ADV52586; ADV52586; Sput200_0096. DR KEGG; shp:Sput200_0096; -. DR OMA; PYVDVWL; -. DR BioCyc; SPUT399804:GLK4-99-MONOMER; -. DR Proteomes; UP000008209; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008209}; KW Methyltransferase {ECO:0000313|EMBL:ADV52586.1}; KW Transferase {ECO:0000313|EMBL:ADV52586.1}. SQ SEQUENCE 300 AA; 31837 MW; 4DF8F5B3D84AE8CA CRC64; MKKQALWVLD GGMGRELARR GAPFRQPEWS ALALMEAPQT VREVHQAYVA SGARVITTNS YALVPFHIGA ERFAAEGEAL AALAGQLARE VANEQPGSVQ VAGSLPPLFG SYRADLFEAD RVGELATPLI RALTPHVDIW LAETMSLIAE PLALKALLPQ DGKPFWVSFT LQDEAPGSEP ALRSGERVAD AVTALAAVGV DAILFNCCQP EVIEAALTVA GDSLQALGRG DIRLGAYANA FPPQPKEATA NDGLDEIRAD LGPLDYLGWA ERWRAVGASL IGGCCGIGPE HIQALASRLR // ID E6ZXQ1_SPORE Unreviewed; 445 AA. AC E6ZXQ1; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 29-APR-2015, entry version 16. DE SubName: Full=Chromosome 3 complete DNA sequence {ECO:0000313|EMBL:CBQ72008.1}; GN ORFNames=sr12865 {ECO:0000313|EMBL:CBQ72008.1}; OS Sporisorium reilianum (strain SRZ2) (Maize head smut fungus). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina; OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium. OX NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ72008.1, ECO:0000313|Proteomes:UP000008867}; RN [1] {ECO:0000313|EMBL:CBQ72008.1, ECO:0000313|Proteomes:UP000008867} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867}; RX PubMed=21148393; DOI=10.1126/science.1195330; RA Schirawski J., Mannhaupt G., Munch K., Brefort T., Schipper K., RA Doehlemann G., Di Stasio M., Rossel N., Mendoza-Mendoza A., Pester D., RA Muller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T., RA Munsterkotter M., Wong P., Walter M., Stukenbrock E., Guldener U., RA 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; FQ311452; CBQ72008.1; -; Genomic_DNA. DR EnsemblFungi; CBQ72008; CBQ72008; sr12865. DR InParanoid; E6ZXQ1; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000008867; Chromosome 3. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008867}; KW Reference proteome {ECO:0000313|Proteomes:UP000008867}. SQ SEQUENCE 445 AA; 48163 MW; 0E4C6589A643B865 CRC64; MLALIDQSAL ESLLGPGRIG ILDGGLATYL EDGLNFDLSK GPLWSARLLD EKEDDVSGGK GQKGIFDAHL HYLQAGAGII GTATYQASLE SFARANYDQA SASHLMSKAV DLACQALHSH NNTSNAASTS NGRPLISLSL GPYGAMLSNG AEYTGDYRRT FLPEFDPQRE QQPSLDEMAA FHQRRIEAFV AQPSWQHVGV LAVETVPRAD EALAFRVALE NVVRSHQQQG KPLERKPVYI SMAFPDDRRL PWPPLASSST NQDGDVDMDE DDDDDTDAAE QEGAVQEEMN WLVQIVTDTQ VQGHDSLWPI SGIGINCTKP YLLPKLAERM SASLVTLNRP ASQGGMDLER RRSAMGLQKP LLFLYPDGGL VYDAVRKIWL TPSNAGELGG DNSAASWAAN LMKLAKSITA AGEANSPDVW RGVFVGGCCK SGTDEIRALC QCRSA // ID E7C3S7_9BACT Unreviewed; 1217 AA. AC E7C3S7; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 01-APR-2015, entry version 23. DE SubName: Full=Methionine synthase I, cobalamin-binding domain {ECO:0000313|EMBL:ADI22101.1}; OS uncultured Planctomycetales bacterium HF0200_11L05. OC Bacteria; Planctomycetes; Planctomycetia; Planctomycetales; OC environmental samples. OX NCBI_TaxID=723607 {ECO:0000313|EMBL:ADI22101.1}; RN [1] {ECO:0000313|EMBL:ADI22101.1} 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GU567975; ADI22101.1; -; Genomic_DNA. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 240 240 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 750 750 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1217 AA; 135552 MW; 3418841809D134E6 CRC64; MKLSDFNKKL KEKILVIDGA MGTEIQSKKL SEEDFRGELY KKYNKDLKGN NDLLNLTQPE IIKEIHKSFL DKGCDFIQTN TFNSSSISQK DYDLQEKAYD LNFMGAKIAK EAISETNSNA WVIGSIGPTN TTASISPDVT DPAKRNILFD ELVISYRECI DGLLEGGVDF LMFETIFDTL NAKAGIFAYL DKCEEVGKKI PLMISGTITD NSGRTLSGQT AEAFWTSVKH ANPCSIGFNC ALGAEQLRPH LISLNKISDI PISLHPNAGL PNEMGEYDET PSHMASIIKE MAESSLLNIV GGCCGTTPDH IEAISYAIKG IKPKKLSASK PQRSFSGLET LVLNDNSLFI NIGERSNVTG SAKFARLIKE KNYAEALEVA KEQVELGAQM IDVNMDEGML DSLKEMDHFL KLVATEPDIS KVPIVIDSSK WEVIESGLKV IQGKAIVNSI SLKEGEDNFI KVAKLCLKYG AAIIVMAFDE KGQADSLKRR KEICRRSYEV LTKVVKYPPQ DIIFDPNVFA VATGLEEHNN YAKDFIDACA YIKEEFPLTS ISGGISNVSF SFRGNDAVRE AMHSVFLYHA INKGLTMGIV NAGQLAVYED INPELKTLVE DVILNRREDA TERLVDEATK FLKDQTRKTT DEKWRNLEIN ERINHALVQG INKYIIEDVE EARCKSNSPV EVIEGPLMDG MNIVGDLFGD GKMFLPQVVK SARVMKEAVA YLVPYLEEEK EGGIQTNGKI VMATVKGDVH DIGKNIVTVV LQCNNYEVIN LGVMVPAEQI IDTAISENAD LIGLSGLITP SLDEMIGVVQ ELTRRKMNIP VLIGGATTSK AHTALKIEPN YKTGFAIHVL DASRSVGVVQ NLLNKKKSKS YTEKIREDYL ATRLRLEEKS SPKLLSLKEA NNNKLNINWE KSKPVKPSFL GVRNLESISI SSLRPYIDWT PFFKSWSLAG SYPKILDDEV VGEAATQLFK DANEMLDELG KSNSISNQSV IGFWPASQDK NNQVKVFKDE KRKDLLTTLN FPRQQRFQGK GNPNLSLSDF IAPEKKKIKD YIGAFAVTSG LGVEEACTNY ENNNDDYSSI MLKAIADRLA ESLAEYVHEK VRKEYWGYSR EEELSNEQLI REKYVGIRPA PGYPACPDHS EKIKLFSLLD AENKASISLT ENFAMLPAAS VSGWYFSHID SKYFGLGKIT EEQIKTISDN RNENINLTKK YYSTNLE // ID E7C414_9GAMM Unreviewed; 81 AA. AC E7C414; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 01-OCT-2014, entry version 11. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:ADI22188.1}; OS uncultured gamma proteobacterium HF0200_34B07. OC Bacteria; Proteobacteria; Gammaproteobacteria; environmental samples. OX NCBI_TaxID=723571 {ECO:0000313|EMBL:ADI22188.1}; RN [1] {ECO:0000313|EMBL:ADI22188.1} 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; GU567978; ADI22188.1; -; Genomic_DNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; SQ SEQUENCE 81 AA; 8771 MW; E1D8E898C12E3D44 CRC64; MHTEVSHVDS CLDVAEEMWV VPVGVYAHSS NYVGGKWIFN NVISSVDYAT AAQGWRNRGV RVIGGACGVG PTHIRALITK E // ID E7C4C4_9ACTN Unreviewed; 81 AA. AC E7C4C4; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 01-OCT-2014, entry version 11. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:ADI22298.1}; OS uncultured actinobacterium HF0200_46I24. OC Bacteria; Actinobacteria; marine Actinobacteria clade; OC environmental samples. OX NCBI_TaxID=723602 {ECO:0000313|EMBL:ADI22298.1}; RN [1] {ECO:0000313|EMBL:ADI22298.1} 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; GU567981; ADI22298.1; -; Genomic_DNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; SQ SEQUENCE 81 AA; 8771 MW; E1D8E898C12E3D44 CRC64; MHTEVSHVDS CLDVAEEMWV VPVGVYAHSS NYVGGKWIFN NVISSVDYAT AAQGWRNRGV RVIGGACGVG PTHIRALITK E // ID E7D6R2_PIG Unreviewed; 407 AA. AC E7D6R2; F1RFS0; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 01-APR-2015, entry version 33. DE SubName: Full=Betaine homocysteine methyltransferase {ECO:0000313|EMBL:ADU33182.1}; DE SubName: Full=Betaine--homocysteine S-methyltransferase 1 {ECO:0000313|Ensembl:ENSSSCP00000015001}; DE SubName: Full=Homocysteine methyltransferase splice variant 10 {ECO:0000313|EMBL:AGS56956.1}; DE SubName: Full=Homocysteine methyltransferase splice variant 2 {ECO:0000313|EMBL:AGS56948.1}; DE SubName: Full=Homocysteine methyltransferase splice variant 4 {ECO:0000313|EMBL:AGS56950.1}; DE SubName: Full=Homocysteine methyltransferase splice variant 5 {ECO:0000313|EMBL:AGS56951.1}; DE SubName: Full=Homocysteine methyltransferase splice variant 7 {ECO:0000313|EMBL:AGS56953.1}; DE SubName: Full=Homocysteine methyltransferase splice variant 8 {ECO:0000313|EMBL:AGS56954.1}; DE SubName: Full=Homocysteine methyltransferase splice variant 9 {ECO:0000313|EMBL:AGS56955.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSSSCP00000021610}; GN Name=bhmt {ECO:0000313|EMBL:ADU33182.1}; GN Synonyms=BHMT {ECO:0000313|EMBL:AGS56948.1, GN ECO:0000313|Ensembl:ENSSSCP00000015001}, GN LOC100739497 {ECO:0000313|Ensembl:ENSSSCP00000021610}; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; OC Sus. OX NCBI_TaxID=9823 {ECO:0000313|EMBL:ADU33182.1}; RN [1] {ECO:0000313|Ensembl:ENSSSCP00000015001, ECO:0000313|Proteomes:UP000008227} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG Porcine genome sequencing project; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADU33182.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=21156199; DOI=10.1016/j.gene.2010.11.015; RA Ganu R.S., Garrow T.A., Sodhi M., Rund L.A., Schook L.B.; RT "Molecular characterization and analysis of the porcine betaine RT homocysteine methyltransferase and betaine homocysteine RT methyltransferase-2 genes."; RL Gene 473:133-138(2011). RN [3] {ECO:0000313|Ensembl:ENSSSCP00000015001} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2011) to UniProtKB. RN [4] {ECO:0000313|Ensembl:ENSSSCP00000021610} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2012) to UniProtKB. RN [5] {ECO:0000313|EMBL:AGS56948.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Brain {ECO:0000313|EMBL:AGS56953.1}, RC Fetal g90 lungs {ECO:0000313|EMBL:AGS56956.1}, RC Heart {ECO:0000313|EMBL:AGS56951.1}, RC Kidney cortex {ECO:0000313|EMBL:AGS56955.1}, RC Kidney medulla {ECO:0000313|EMBL:AGS56948.1}, RC Liver {ECO:0000313|EMBL:AGS56954.1}, and RC Lungs {ECO:0000313|EMBL:AGS56950.1}; RX PubMed=23948084; RA Ganu R., Garrow T., Koutmos M., Rund L., Schook L.B.; RT "Splicing variants of the porcine betaine-homocysteine S- RT methyltransferase gene: Implications for mammalian metabolism."; RL Gene 529:228-237(2013). CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU468550; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; HQ130333; ADU33182.1; -; mRNA. DR EMBL; JX988430; AGS56948.1; -; mRNA. DR EMBL; JX988432; AGS56950.1; -; mRNA. DR EMBL; JX988433; AGS56951.1; -; mRNA. DR EMBL; JX988435; AGS56953.1; -; mRNA. DR EMBL; JX988436; AGS56954.1; -; mRNA. DR EMBL; JX988437; AGS56955.1; -; mRNA. DR EMBL; JX988438; AGS56956.1; -; mRNA. DR RefSeq; NP_001186971.1; NM_001200042.1. DR RefSeq; XP_003484245.1; XM_003484197.2. DR UniGene; Ssc.16105; -. DR UniGene; Ssc.82464; -. DR Ensembl; ENSSSCT00000015410; ENSSSCP00000015001; ENSSSCG00000014108. DR Ensembl; ENSSSCT00000025802; ENSSSCP00000021610; ENSSSCG00000024331. DR GeneID; 100739497; -. DR GeneID; 397371; -. DR KEGG; ssc:100739497; -. DR KEGG; ssc:397371; -. DR CTD; 635; -. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; E7D6R2; -. DR KO; K00544; -. DR OMA; WGVTKGT; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000008227; Chromosome 2. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IBA:GO_Central. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR GO; GO:0033528; P:S-methylmethionine cycle; IBA:GO_Central. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Complete proteome {ECO:0000313|Proteomes:UP000008227}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000313|EMBL:ADU33182.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008227}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000313|EMBL:ADU33182.1}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 217 217 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 407 AA; 44945 MW; 0AD255A6F44777E7 CRC64; MAPVGDKKAK KGILERLNSG EVVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAVRQLH REFLRAGSNV MQTFTFYASE DKLENRGNYV AEKISGQKVN EAACDIARQV ADEGDALVAG GVSQTPSYLS CKSETEVKKV FRQQLEVFMK KNVDFLIAEY FEHVEEAVWA VEALKASGKP VAATMCIGPE GDLHGVTPGQ CAVRLVKAGA SIVGVNCHFD PTISLQTVKL MKEGLQAAGL KAHLMSQPLA YHTPDCGKQG FIDLPEFPFG LEPRVATRWD IQKYAREAYN LGVRYIGGCC GFEPYHIRAI AEELAPERGF LPPASEKHGS WGSALDMHTK PWVRARARKE YWENLRIASG RPYNPSMSKP DAWGVTKGTA ELMQQKEATT EQQLRELFEK QKFPSAQ // ID E7D6R3_PIG Unreviewed; 363 AA. AC E7D6R3; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAY-2015, entry version 30. DE SubName: Full=Betaine homocysteine methyltransferase-2 {ECO:0000313|EMBL:ADU33183.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSSSCP00000015005}; GN Name=bhmt-2 {ECO:0000313|EMBL:ADU33183.1}; GN Synonyms=BHMT2 {ECO:0000313|Ensembl:ENSSSCP00000015005}; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; OC Sus. OX NCBI_TaxID=9823; RN [1] {ECO:0000313|Ensembl:ENSSSCP00000015005, ECO:0000313|Proteomes:UP000008227} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG Porcine genome sequencing project; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADU33183.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=21156199; DOI=10.1016/j.gene.2010.11.015; RA Ganu R.S., Garrow T.A., Sodhi M., Rund L.A., Schook L.B.; RT "Molecular characterization and analysis of the porcine betaine RT homocysteine methyltransferase and betaine homocysteine RT methyltransferase-2 genes."; RL Gene 473:133-138(2011). RN [3] {ECO:0000313|Ensembl:ENSSSCP00000015005} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU468550; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; HQ130334; ADU33183.1; -; mRNA. DR RefSeq; NP_001191700.1; NM_001204771.1. DR UniGene; Ssc.48149; -. DR Ensembl; ENSSSCT00000015414; ENSSSCP00000015005; ENSSSCG00000014111. DR GeneID; 100523776; -. DR KEGG; ssc:100523776; -. DR CTD; 23743; -. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; E7D6R3; -. DR OMA; PEGDMHD; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000008227; Chromosome 2. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IBA:GO_Central. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IBA:GO_Central. DR GO; GO:0061627; F:S-methylmethionine-homocysteine S-methyltransferase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl. DR GO; GO:0046500; P:S-adenosylmethionine metabolic process; IEA:Ensembl. DR GO; GO:0033528; P:S-methylmethionine cycle; IBA:GO_Central. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000008227}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000313|EMBL:ADU33183.1}; KW Proteomics identification {ECO:0000213|PeptideAtlas:E7D6R3}; KW Reference proteome {ECO:0000313|Proteomes:UP000008227}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000313|EMBL:ADU33183.1}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 208 208 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 363 AA; 40049 MW; 787332F6BCC64E0A CRC64; MAPAGSPRAK KGILERLDAG EVVVGDGGFL LTLEKRGYVK AGLWTPEAVV EHPNAVRQLH MEFLRAGSNV MQTFTFSANE DNMESQWEAV NAAACDLAQE VAGKGDALVA GGLCQTSLYK HHKDEDRIKK LFRLQLEVFV RKNVDFLIAE YFEYAEEAVW AVEVLKESGK PVAATMCIGP EGDMHGVTPG ECAVKLVKAG ASIIGVNCRF GPWTSLKTMR LMKEGLQAAG LKAHLMVQSL VFHMPDCGKG GFVDLPEYPF ALEPRVATRW DIQKYAREAY NLGIRYIGGC CGFEPYHIRA IAEELAPERG FLPPASEKHG SWGSGLNMHT KPWIRARARR EYWENLLPAS GRPFCPSLSK PDV // ID E7FB51_DANRE Unreviewed; 1202 AA. AC E7FB51; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAY-2015, entry version 33. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSDARP00000057160}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000057160, ECO:0000313|Proteomes:UP000000437}; RN [1] {ECO:0000313|Ensembl:ENSDARP00000057160} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000057160}; RG The Danio rerio Sequencing Project at the Sanger Institute; RT "The genomic sequence of Danio rerio."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSDARP00000057160} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000057160}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. RN [3] {ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Proteomes:UP000000437}; RX PubMed=23594743; DOI=10.1038/nature12111; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., RA Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., RA McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., RA Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T., RA Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., RA Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., RA Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., RA Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G., RA Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., RA Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., RA Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., RA Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., RA Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., RA Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., RA Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., RA Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., RA Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., RA Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., RA Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., RA Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., RA Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., RA Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., RA Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., RA Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., RA Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., RA Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the RT human genome."; RL Nature 496:498-503(2013). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 1}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSDARP00000057160}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CABZ01057908; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABZ01057909; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABZ01057910; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABZ01057911; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABZ01088977; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABZ01088978; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABZ01088979; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABZ01088980; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABZ01088981; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABZ01088982; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABZ01088983; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABZ01089791; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABZ01089792; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABZ01089793; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABZ01089794; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABZ01091961; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABZ01091962; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSDART00000057161; ENSDARP00000057160; ENSDARG00000039134. DR GeneTree; ENSGT00420000029824; -. DR InParanoid; E7FB51; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG7TF786; -. DR TreeFam; TF312829; -. DR Reactome; REACT_302794; Cobalamin (Cbl, vitamin B12) transport and metabolism. DR Reactome; REACT_342706; Sulfur amino acid metabolism. DR Reactome; REACT_353431; Methylation. DR PRO; PR:E7FB51; -. DR Proteomes; UP000000437; Chromosome 12. DR Bgee; E7FB51; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 2. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 1: Evidence at protein level; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000437}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Proteomics identification {ECO:0000213|PeptideAtlas:E7FB51}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 258 258 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 783 783 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1202 AA; 132676 MW; 5EBF4D9222334905 CRC64; MPPTIHQSPA GRASSLRLEL TELLQQRILV LDGGMGTMIQ QRHLEEEEFR GQEFKDHPKS LKGNNDILSI TQPDVIYSIH KEYLEAGADI IETNTFSSTS IAQADYGMED LAYRLNKASA EVARRAADDV SAQTGCKRFV AGALGPTNKT LSVSPSVERP DYRNITFDEL VEAYAEQVKG LLDGGADVLL VETIFDTANA KAALFAIDRL FEESYEARPV LISGTIVDKS GRTLSGQTGE AFVISVSHTQ PLCIGLNCAL GASEMRPFIE AIGKSTSAFV ICYPNAGLPN TFGGYDETPD VTAAHLKEFA VDGLVNIVGG CCGTTPDHIR AIAESVRHVK PRVPPTDVYS DYMLLSGLEP FRIGPYTNFV NIGERCNVAG SRKFAKLIMA GNYEPAGASP KCTLKLGSQI CDRNNTRGFL DGAAAMSRFC NLIASEPDIC KVPLCIDSSN FSVIEAGLKC CQGKCIVNSI SLKEGEQDFL RRARQVRRYG AAVVVMAFDE DGQATETDQK VQICSRAYHL LIDQAGFNPN DIIFDPNILT IGTGMEEHSM YAINFIRATR IIKESLPGAR VSGGLSNLSF SFRGMEAIRE AMHGAFLYHA IKDGMDMGIV NAGNLPVYDD IDKELLLLCE NIIWNRDPDA TEKLLLYAQN NAKGGKKVVQ TDEWRTGSVE ERLEYALVKG IEKYVVEDTE EARAQTERYP RPLHVIEGPL MNGMKTVGDL FGAGKMFLPQ VIKSARVMKK AVGHLIPFME KEREEMMATS GCVEEVDPYQ GTVLLATVKG DVHDIGKNIV GVVLGCNNFR VIDLGVMIPC DRILREAIHN KADIIGLSGL ITPSLDEMIH VAKEMERLGL KIPLLIGGAT TSKTHTAVKI APRYSSPVVH VLDASRSVVV CSQLLDEGVR DDYFEEVQEE YEDIRQDHYD SLKDRRFLSL SRAREKGLHI DWLAQPKPVR PQFLGTHVFD TYDLRKLVDF IDWKPFFDVW QLRGKYPNRG YPKIFKDKTV GQCSRSVSSS GQSLCVCVCV CVCVCVCVCV CVCVCVCVCV CVCVCVLCVC VYVCVCVCVC VSLHMDVCVC VYNMCMHVCL KRGCAPRSSG VQDYVGLFAV SVFGAEELSQ KFEKQGDDYR SIMVKALADR LAEAFAEELH VRVRRDLWGY SSEEDLPASD LHKLRYEGIR PAAGYPSQPD HSEKLTMWKL ADIQEKTGER LT // ID E7G958_9FIRM Unreviewed; 787 AA. AC E7G958; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFW05499.1}; GN ORFNames=HMPREF9488_01296 {ECO:0000313|EMBL:EFW05499.1}; OS Coprobacillus sp. 29_1. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae; Coprobacillus. OX NCBI_TaxID=469596 {ECO:0000313|EMBL:EFW05499.1}; RN [1] {ECO:0000313|EMBL:EFW05499.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=29_1 {ECO:0000313|EMBL:EFW05499.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFW05499.1}. 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; ADKX01000023; EFW05499.1; -; Genomic_DNA. DR RefSeq; WP_008788412.1; NZ_GL636578.1. DR EnsemblBacteria; EFW05499; EFW05499; HMPREF9488_01296. DR PATRIC; 46465851; VBICopSp159203_1059. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFW05499.1}; KW Transferase {ECO:0000313|EMBL:EFW05499.1}. SQ SEQUENCE 787 AA; 86589 MW; 4A4EC91E7E32859E CRC64; MLRERLGKDL LIFDGAMGTQ LQEAGLKAGE IPEVYNIEHP EIIIDIHSRY LQSGANFITT NTFGCNPLKM ADSGYCYCDL LKAAVKNARI ARDKVNPNAY IALDIGPIGQ LLEPLGTLTF DEAYEMIASQ ILIVKDQVDV VLLETMTDLY EVKAAILAVK ENSDLPVFVT MTFEQNKRTL TGTDPLTFVN VVEGLGVDAL GVNCSLGPNE LKPIIDEILE VSSIPVMIQP NAGLPCLHNG QTCYEVTSDE YALAMIDYMQ RGVSIVGGCC GTTPDFIAEL KKRAPQNVTS RDVKRLTRVS SQNQTVTFEG QVVVCGERLN PTGKKKLKAA LKEERYDECV VEGIKQQQAG ADVLDVNVGL PGIDEPATMV KVMKLLQEVI NLPLQIDSSS PEAIEKACRY YNGKPLINSV NGKDEVMEAI FPIVKKYGGV VIGLTLEDGI PLYAHERLAI AKKIIDKASE YGIAKEDIII DCLTLTASAQ QKEVQETLKA LTLVKEELGV HTVLGVSNVS FGLPNRPLLN RTFLALAMQS GLDLPIINPL DQELMGTIDA YNVLYHFDKD SSRYISKQSQ VTTLAPLTTS SFTLEDMIIH GLKDEVQAKT KELLQEREAM DVINNVIIPA LNRVGKDYET NKIFLPQLIQ SAETTKKAFE VVKSTFRVDS QSKGPIMMCT VEGDIHDIGK NIVKVVLESY GYQVIDLGKD VKVEKVVEAY HKYQPKMIGL SALMTTTVVN MKKTIEALHK VNCQCPIWVG GAVLTQEIAD EIGADYYSED AMASVTLLNH IFDERGE // ID E7GJP5_CLOSY Unreviewed; 833 AA. AC E7GJP5; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGA95019.1}; GN ORFNames=HMPREF9474_01100 {ECO:0000313|EMBL:EGA95019.1}; OS [Clostridium] symbiosum WAL-14163. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=742740 {ECO:0000313|EMBL:EGA95019.1, ECO:0000313|Proteomes:UP000002970}; RN [1] {ECO:0000313|EMBL:EGA95019.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=WAL-14163 {ECO:0000313|EMBL:EGA95019.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGA95019.1}. 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; ADLQ01000029; EGA95019.1; -; Genomic_DNA. DR RefSeq; WP_003499226.1; NZ_GL834306.1. DR EnsemblBacteria; EGA95019; EGA95019; HMPREF9474_01100. DR PATRIC; 46473739; VBICloSym155749_0982. DR Proteomes; UP000002970; Unassembled WGS sequence. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002970}. SQ SEQUENCE 833 AA; 89045 MW; CE2ACDC42325520E CRC64; MAILEELREK ILLFDGGTGS LLQEAGLKPG ELPETWNISH PDIVVKLHSD YLEAGCDIIK TNTFGANRFK YNSGTQYSLK EIVTAAMDNA KCAVKKAGRG YIALDIGPTG KLLKPMGQLD FEEAVSVFRE VAETGAEQGA DLILIETMSD TYELKAAVLA AKESSSLPVF ATVIFDEKGK MLTGGTPQTA IALLEGLGVD AVGMNCGLGP VQMKPLAAEF IKYASVPVIV NPNAGLPRSE GGRTVYDIGP DEFEQAMEEI LDMGISVAGG CCGTTPGHIR RLNRLRAGRR QKLPQEKQST VITSYAAAVE IGDDPVIIGE RINPTGKSKF KQALRDHDLE FILREGISQQ ERGAHVLDVN VGLPEIDEPS MMAEVIRELQ GITELPLQID TSNTEAMARA MRVYNGKPLL NSVNGKQEVM DAVFPLVKRY GAVVVALTLD ESGIPETADG RIAIAEKIYR EAAKYGIGKK DILIDALCMT ISSDRLGALT TLETVKRVRQ EMGGRTILGV SNISFGLPVR ENINANFFTL ALYNGLNAAI INPGSEAMMC SYHSFRALAA LDENCGSYIE AYKNAAASSA AGSGSPAGSP APGTSGNRLG SDTAGRKAEA GPGSGNGRGN NPAWDGEEER LALSVEKGLR EQAAQSAKQL LAEKEPLDVI NTCMIPALDH VGKGFEAGTV FLPQLLMSAE AAKAAFDVIK EKMAESGQAR EKKGKIILAT VKGDIHDIGK NIVRVLLENY SYDVLDLGKD VAPEQIVREA VKQHVPLVGL SALMTTTVPA MEETIQRLRQ EAPWTKIMVG GAVLTPEYAK TIGADTYCSD AMASVSYAQK IIG // ID E7H5V6_9BURK Unreviewed; 318 AA. AC E7H5V6; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 12. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFW00784.1}; GN ORFNames=HMPREF9464_02094 {ECO:0000313|EMBL:EFW00784.1}; OS Sutterella wadsworthensis 3_1_45B. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Sutterellaceae; Sutterella. OX NCBI_TaxID=742821 {ECO:0000313|EMBL:EFW00784.1}; RN [1] {ECO:0000313|EMBL:EFW00784.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_45B {ECO:0000313|EMBL:EFW00784.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFW00784.1}. 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; ADMF01000037; EFW00784.1; -; Genomic_DNA. DR RefSeq; WP_005432260.1; NZ_GL636554.1. DR EnsemblBacteria; EFW00784; EFW00784; HMPREF9464_02094. DR PATRIC; 46500003; VBISutWad150710_2275. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFW00784.1}; KW Transferase {ECO:0000313|EMBL:EFW00784.1}. SQ SEQUENCE 318 AA; 35241 MW; 4C27620AB2E8A1E8 CRC64; MALTKHPIAD LIARRGGLVI DGAMSTPLEA AGLNLNDTLW SAKALLECPD LVRKVHYDYY AAGANAVEAC SYQATEAAFA RKGIEKAEAS RLIRLSGELV REAKNDVLLE HPEWDPADLL TAGSIGPYGA YLADGSEYTG AYDLTREEYY AFHQLRLDEL LNSGMDILAI ETQPRFDEIE ALLAMIADRD ITCWVTVTLK DGDMPDGTKL EVLAKCLDAD PHVEAFGFNC VKREWVEPGL KRLSAYTDKP LVVYPNSGET YDPTTKTWHA QGVHEPDWNH YVPLWEHTGA RCIGGCCRTL PKDIVQIADL LHRAAEKH // ID E7I5Z4_ECOLX Unreviewed; 1227 AA. AC E7I5Z4; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EFZ60094.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFZ60094.1}; GN Name=metH {ECO:0000313|EMBL:EFZ60094.1}; GN ORFNames=ECLT68_0917 {ECO:0000313|EMBL:EFZ60094.1}; OS Escherichia coli LT-68. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=670890 {ECO:0000313|EMBL:EFZ60094.1}; RN [1] {ECO:0000313|EMBL:EFZ60094.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=LT-68 {ECO:0000313|EMBL:EFZ60094.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; ADUP01000028; EFZ60094.1; -; Genomic_DNA. DR RefSeq; WP_000096055.1; NZ_ADUP01000028.1. DR EnsemblBacteria; EFZ60094; EFZ60094; ECLT68_0917. DR PATRIC; 47886812; VBIEscCol138002_0897. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFZ60094.1}; KW Transferase {ECO:0000313|EMBL:EFZ60094.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136068 MW; 71F76336C7330F7E CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAD // ID E7KF95_YEASA Unreviewed; 324 AA. AC E7KF95; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 07-JAN-2015, entry version 15. DE SubName: Full=Mht1p {ECO:0000313|EMBL:EGA73985.1}; GN ORFNames=AWRI796_3052 {ECO:0000313|EMBL:EGA73985.1}; OS Saccharomyces cerevisiae (strain AWRI796) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=764097 {ECO:0000313|EMBL:EGA73985.1, ECO:0000313|Proteomes:UP000000306}; RN [1] {ECO:0000313|EMBL:EGA73985.1, ECO:0000313|Proteomes:UP000000306} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AWRI796 {ECO:0000313|EMBL:EGA73985.1, RC ECO:0000313|Proteomes:UP000000306}; 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. {ECO:0000313|EMBL:EGA73985.1}. 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; ADVS01000037; EGA73985.1; -; Genomic_DNA. DR ProteinModelPortal; E7KF95; -. DR SMR; E7KF95; 3-313. DR OrthoDB; EOG7X9GHR; -. DR Proteomes; UP000000306; Chromosome XII. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000306}; KW Reference proteome {ECO:0000313|Proteomes:UP000000306}. SQ SEQUENCE 324 AA; 36715 MW; A77194694B6E5C14 CRC64; MKRIPIKELI VEHPGKVLIL DGGQGTELEN RGININSPVW SAAPFTSESF WEPSSQERKV VEEMYRDFMI AGANILMTIT YQANFQSISE NTSIKTLAAY KRFLDKIVSF TREFIGEERY LIGSIGPWAA HVSCEYTGDY GPHPENIDYY GFFKPQLENF NQNRDIDLIG FETIPNFHEL KAILSWDEDI ISKPFYIGLS VDDNSLLRDG TTLEEISVHI KGLGNKINKN LLLMGVNCVS FNQSALILKM LHEHLPGMPL LVYPNSGEIY NPKEKTWHRP TNKLDDWETT VKKFVDNGAR IIGGCCRTSP KDIAEIASAV DKYS // ID E7KGP6_YEASA Unreviewed; 112 AA. AC E7KGP6; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Sam4p {ECO:0000313|EMBL:EGA73625.1}; GN ORFNames=AWRI796_3906 {ECO:0000313|EMBL:EGA73625.1}; OS Saccharomyces cerevisiae (strain AWRI796) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=764097 {ECO:0000313|EMBL:EGA73625.1, ECO:0000313|Proteomes:UP000000306}; RN [1] {ECO:0000313|EMBL:EGA73625.1, ECO:0000313|Proteomes:UP000000306} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AWRI796 {ECO:0000313|EMBL:EGA73625.1, RC ECO:0000313|Proteomes:UP000000306}; 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. {ECO:0000313|EMBL:EGA73625.1}. 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; ADVS01000041; EGA73625.1; -; Genomic_DNA. DR ProteinModelPortal; E7KGP6; -. DR OrthoDB; EOG7X9GHR; -. DR Proteomes; UP000000306; Chromosome XIII. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000306}; KW Reference proteome {ECO:0000313|Proteomes:UP000000306}. SQ SEQUENCE 112 AA; 12436 MW; F01DDDA7CEAF4926 CRC64; MEEIAQVIKD LGDKINPNFS FLGINCVSFN QSPDILESLH QALPNMALLA YPNSGEVYDT EKKIWLPNSD KLNSWDTVVK QYISSGARII GGCCRTSPKD IQEISAAVKK YT // ID E7KJ32_YEASA Unreviewed; 325 AA. AC E7KJ32; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 07-JAN-2015, entry version 16. DE SubName: Full=Sam4p {ECO:0000313|EMBL:EGA72516.1}; GN ORFNames=AWRI796_4745 {ECO:0000313|EMBL:EGA72516.1}; OS Saccharomyces cerevisiae (strain AWRI796) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=764097 {ECO:0000313|EMBL:EGA72516.1, ECO:0000313|Proteomes:UP000000306}; RN [1] {ECO:0000313|EMBL:EGA72516.1, ECO:0000313|Proteomes:UP000000306} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AWRI796 {ECO:0000313|EMBL:EGA72516.1, RC ECO:0000313|Proteomes:UP000000306}; 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. {ECO:0000313|EMBL:EGA72516.1}. 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; ADVS01000048; EGA72516.1; -; Genomic_DNA. DR ProteinModelPortal; E7KJ32; -. DR SMR; E7KJ32; 15-315. DR OrthoDB; EOG7X9GHR; -. DR Proteomes; UP000000306; Chromosome XVI. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000306}; KW Reference proteome {ECO:0000313|Proteomes:UP000000306}. SQ SEQUENCE 325 AA; 36669 MW; 54658C7B92A610F0 CRC64; MARLPLKQFL ADNPKKVLVL DGGQGTELEN RGIKVANPVW STIPFISESF WSDESSANRK IVKEMFNDFL NAGAEILMTT TYQTSYKSVS ENTPIRTLSE YNNLLNRIVD FSRNCIGEDK YLIGCIGPWG AHICREFTGD YGAEPENIDF YQYFKPQLEN FNKNDKLDLI GFETIPNIHE LKAILSWDES ILSRPFYIGL SVHEHGVLRD GTTMEEIAQV IKDLGDKINP NFSFLGINCV SFNQSPDILE SLHQALPNMA LLAYPNSGEV YDTEKKIWLP NSDKLNSWDT VVKQYISSGA RIIGGCCRTS PKDIQEISAA VKKYT // ID E7KRB6_YEASL Unreviewed; 324 AA. AC E7KRB6; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 07-JAN-2015, entry version 15. DE SubName: Full=Mht1p {ECO:0000313|EMBL:EGA81839.1}; GN ORFNames=QA23_3047 {ECO:0000313|EMBL:EGA81839.1}; OS Saccharomyces cerevisiae (strain Lalvin QA23) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=764098 {ECO:0000313|EMBL:EGA81839.1, ECO:0000313|Proteomes:UP000007236}; RN [1] {ECO:0000313|EMBL:EGA81839.1, ECO:0000313|Proteomes:UP000007236} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Lalvin QA23 {ECO:0000313|EMBL:EGA81839.1, RC ECO:0000313|Proteomes:UP000007236}; 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. {ECO:0000313|EMBL:EGA81839.1}. 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; ADVV01000059; EGA81839.1; -; Genomic_DNA. DR ProteinModelPortal; E7KRB6; -. DR SMR; E7KRB6; 3-313. DR OrthoDB; EOG7X9GHR; -. DR Proteomes; UP000007236; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007236}; KW Reference proteome {ECO:0000313|Proteomes:UP000007236}. SQ SEQUENCE 324 AA; 36715 MW; A77194694B6E5C14 CRC64; MKRIPIKELI VEHPGKVLIL DGGQGTELEN RGININSPVW SAAPFTSESF WEPSSQERKV VEEMYRDFMI AGANILMTIT YQANFQSISE NTSIKTLAAY KRFLDKIVSF TREFIGEERY LIGSIGPWAA HVSCEYTGDY GPHPENIDYY GFFKPQLENF NQNRDIDLIG FETIPNFHEL KAILSWDEDI ISKPFYIGLS VDDNSLLRDG TTLEEISVHI KGLGNKINKN LLLMGVNCVS FNQSALILKM LHEHLPGMPL LVYPNSGEIY NPKEKTWHRP TNKLDDWETT VKKFVDNGAR IIGGCCRTSP KDIAEIASAV DKYS // ID E7KT56_YEASL Unreviewed; 163 AA. AC E7KT56; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 07-JAN-2015, entry version 13. DE SubName: Full=Sam4p {ECO:0000313|EMBL:EGA81282.1}; GN ORFNames=QA23_3889 {ECO:0000313|EMBL:EGA81282.1}; OS Saccharomyces cerevisiae (strain Lalvin QA23) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=764098 {ECO:0000313|EMBL:EGA81282.1, ECO:0000313|Proteomes:UP000007236}; RN [1] {ECO:0000313|EMBL:EGA81282.1, ECO:0000313|Proteomes:UP000007236} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Lalvin QA23 {ECO:0000313|EMBL:EGA81282.1, RC ECO:0000313|Proteomes:UP000007236}; 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. {ECO:0000313|EMBL:EGA81282.1}. 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; ADVV01000069; EGA81282.1; -; Genomic_DNA. DR Proteomes; UP000007236; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007236}; KW Reference proteome {ECO:0000313|Proteomes:UP000007236}. SQ SEQUENCE 163 AA; 18822 MW; 444951F6C1B3BBA4 CRC64; MFNDFLNAGA EILMTTTYQT SYKSVSENTP IRTLSEYNNL LNRIVDFSRN CIGEDKYLIG CIGPWGAHIC REFTGDYGAE PENIDFYQYF KPQLENFNKN DKLDLIGFET IPNIHELKAI LSWDESILSR PFYIGLSVHE HGVLRDGTTM EKSHKLLRTW ATK // ID E7KV57_YEASL Unreviewed; 261 AA. AC E7KV57; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Sam4p {ECO:0000313|EMBL:EGA80349.1}; GN ORFNames=QA23_4709 {ECO:0000313|EMBL:EGA80349.1}; OS Saccharomyces cerevisiae (strain Lalvin QA23) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=764098 {ECO:0000313|EMBL:EGA80349.1, ECO:0000313|Proteomes:UP000007236}; RN [1] {ECO:0000313|EMBL:EGA80349.1, ECO:0000313|Proteomes:UP000007236} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Lalvin QA23 {ECO:0000313|EMBL:EGA80349.1, RC ECO:0000313|Proteomes:UP000007236}; 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. {ECO:0000313|EMBL:EGA80349.1}. 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; ADVV01000082; EGA80349.1; -; Genomic_DNA. DR ProteinModelPortal; E7KV57; -. DR OrthoDB; EOG7X9GHR; -. DR Proteomes; UP000007236; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007236}; KW Reference proteome {ECO:0000313|Proteomes:UP000007236}. SQ SEQUENCE 261 AA; 29529 MW; 033A9E74EBAE569C CRC64; MFNDFLNAGA EILMTTTYQT SYKSVSENTP IRTLSEYNNL LNRIVDFSRN CIGEDKYLIG CIGPWGAHIC REFTGDYGAE PENIDFYQYF KPQLENFNKN DKLDLIGFET IPNIHELKAI LSWDESILSR PFYIGLSVHE HGVLRDGTTM EEIAQVIKDL GDKINPNFSF LGINCVSFNQ SPDILESLHQ ALPNMALLAY PNSGEVYDTE KKIWLPNSDK LNSWDTVVKQ YISSGARIIG GCCRTSPKDI QEISAAVKKY T // ID E7KW64_YEASL Unreviewed; 304 AA. AC E7KW64; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 07-JAN-2015, entry version 14. DE SubName: Full=Sam4p {ECO:0000313|EMBL:EGA80175.1}; DE Flags: Fragment; GN ORFNames=QA23_5273 {ECO:0000313|EMBL:EGA80175.1}; OS Saccharomyces cerevisiae (strain Lalvin QA23) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=764098 {ECO:0000313|EMBL:EGA80175.1, ECO:0000313|Proteomes:UP000007236}; RN [1] {ECO:0000313|EMBL:EGA80175.1, ECO:0000313|Proteomes:UP000007236} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Lalvin QA23 {ECO:0000313|EMBL:EGA80175.1, RC ECO:0000313|Proteomes:UP000007236}; 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. {ECO:0000313|EMBL:EGA80175.1}. 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; ADVV01000158; EGA80175.1; -; Genomic_DNA. DR OrthoDB; EOG7X9GHR; -. DR Proteomes; UP000007236; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007236}; KW Reference proteome {ECO:0000313|Proteomes:UP000007236}. FT NON_TER 304 304 {ECO:0000313|EMBL:EGA80175.1}. SQ SEQUENCE 304 AA; 34388 MW; 9852C8C85BF249E4 CRC64; MARLPLKQFL ADNPKKVLVL DGGQGTELEN RGIKVANPVW STIPFISESF WSDESSANRK IVKEMFNDFL NAGAEILMTT TYQTSYKSVS ENTPIRTLSE YNNLLNRIVD FSRNCIGEDK YLIGCIGPWG AHICREFTGD YGAEPENIDF YQYFKPQLEN FNKNDKLDLI GFETIPNIHE LKAILSWDES ILSRPFYIGL SVHEHGVLRD GTTMEEIAQV IKDLGDKINP NFSFLGINCV SFNQSPDILE SLHQALPNMA LLAYPNSGEV YDTEKKIWLP NSDKLNSWDT VVKQYISSGA RIIG // ID E7LX61_YEASV Unreviewed; 185 AA. AC E7LX61; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 07-JAN-2015, entry version 14. DE SubName: Full=Mht1p {ECO:0000313|EMBL:EGA77782.1}; GN ORFNames=VIN13_3031 {ECO:0000313|EMBL:EGA77782.1}; OS Saccharomyces cerevisiae (strain VIN 13) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=764099 {ECO:0000313|EMBL:EGA77782.1, ECO:0000313|Proteomes:UP000000307}; RN [1] {ECO:0000313|EMBL:EGA77782.1, ECO:0000313|Proteomes:UP000000307} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VIN 13 {ECO:0000313|Proteomes:UP000000307}; 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. {ECO:0000313|EMBL:EGA77782.1}. 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; ADXC01000055; EGA77782.1; -; Genomic_DNA. DR OrthoDB; EOG7X9GHR; -. DR Proteomes; UP000000307; Chromosome XII. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000307}; KW Reference proteome {ECO:0000313|Proteomes:UP000000307}. SQ SEQUENCE 185 AA; 20925 MW; 73FDA81B6151121D CRC64; MVPILRILIT TAFFKPQLEN FNQNRDIDLI GFETIPNFHE LKAILSWDED IISKPFYIGL SVDDNSLLRD GTTLEEISVH IKGLGNKINK NLLLMGVNCV SFNQSALILK MLHEHLPGMP LLVYPNSGEI YNPKEKTWHR PTNKLDDWET TVKKFVDNGA RIIGGCCRTS PKDIAEIASA VDKYS // ID E7M213_YEASV Unreviewed; 112 AA. AC E7M213; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Sam4p {ECO:0000313|EMBL:EGA76238.1}; GN ORFNames=VIN13_5204 {ECO:0000313|EMBL:EGA76238.1}; OS Saccharomyces cerevisiae (strain VIN 13) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=764099 {ECO:0000313|EMBL:EGA76238.1, ECO:0000313|Proteomes:UP000000307}; RN [1] {ECO:0000313|EMBL:EGA76238.1, ECO:0000313|Proteomes:UP000000307} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VIN 13 {ECO:0000313|Proteomes:UP000000307}; 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. {ECO:0000313|EMBL:EGA76238.1}. 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; ADXC01000131; EGA76238.1; -; Genomic_DNA. DR ProteinModelPortal; E7M213; -. DR OrthoDB; EOG7X9GHR; -. DR Proteomes; UP000000307; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000307}; KW Reference proteome {ECO:0000313|Proteomes:UP000000307}. SQ SEQUENCE 112 AA; 12436 MW; F01DDDA7CEAF4926 CRC64; MEEIAQVIKD LGDKINPNFS FLGINCVSFN QSPDILESLH QALPNMALLA YPNSGEVYDT EKKIWLPNSD KLNSWDTVVK QYISSGARII GGCCRTSPKD IQEISAAVKK YT // ID E7N2Q2_9FIRM Unreviewed; 333 AA. AC E7N2Q2; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 11. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFW29463.1}; GN ORFNames=HMPREF9555_01273 {ECO:0000313|EMBL:EFW29463.1}; OS Selenomonas artemidis F0399. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Selenomonas. OX NCBI_TaxID=749551 {ECO:0000313|EMBL:EFW29463.1}; RN [1] {ECO:0000313|EMBL:EFW29463.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0399 {ECO:0000313|EMBL:EFW29463.1}; 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 (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. {ECO:0000313|EMBL:EFW29463.1}. 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; AECV01000023; EFW29463.1; -; Genomic_DNA. DR RefSeq; WP_009349931.1; NZ_GL638136.1. DR EnsemblBacteria; EFW29463; EFW29463; HMPREF9555_01273. DR PATRIC; 46558040; VBISelArt149184_0824. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFW29463.1}; KW Transferase {ECO:0000313|EMBL:EFW29463.1}. SQ SEQUENCE 333 AA; 36239 MW; 7943AF986547A432 CRC64; MLNIIEERLA VSNILVLDGA FATELEARGF SVNDALWSAK AIFERPDLVR DVHLDYLRAG ADIVTSASYQ ATVEGFVKKG FTEEQAAALI VRSVELAREA RDIYCLESLA DEYHAHEEFT RGSCERCAPA QRRSLGEEPL VAASVGPYGA YLADGSEYRG DYDVDEDALT AFHADRLALL AEGQPDLLAC ETLPCLPEAR AIVRALREKK IHIPAWFSFS CRDGAHISDG TPIADCARFL AGVPEAAAIG VNCTAPQYIE DLIRAIRRET DKPVVVYPNS GEDYSASDKS WHGTAEDFAA GARRWRDAGA RIIGGCCRTS PRDIAGIAAW AKA // ID E7N337_9FIRM Unreviewed; 811 AA. AC E7N337; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFW29598.1}; GN ORFNames=HMPREF9555_01409 {ECO:0000313|EMBL:EFW29598.1}; OS Selenomonas artemidis F0399. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Selenomonas. OX NCBI_TaxID=749551 {ECO:0000313|EMBL:EFW29598.1}; RN [1] {ECO:0000313|EMBL:EFW29598.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0399 {ECO:0000313|EMBL:EFW29598.1}; 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 (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. {ECO:0000313|EMBL:EFW29598.1}. 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; AECV01000023; EFW29598.1; -; Genomic_DNA. DR RefSeq; WP_009350069.1; NZ_GL638136.1. DR EnsemblBacteria; EFW29598; EFW29598; HMPREF9555_01409. DR PATRIC; 46558304; VBISelArt149184_0955. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFW29598.1}; KW Transferase {ECO:0000313|EMBL:EFW29598.1}. SQ SEQUENCE 811 AA; 86884 MW; B59E58C8E25698A4 CRC64; MGDIGMQDII ILDGGMGTEL QARGLAPGER PELFGMEHPE VIEEVHRNYI AAGSRVIYSN TFGANGHKLI GTGKTVAEVI GANVAIARHA AENSGVPGVR VALDIGPIGE LVEPLGTLSF EDAYELFREM VTAGEAAGAD LVIFETLTDL YEVKAAVLAA KEHTKLPIWV TMTFEQNGRT FLGAAVPSVA VTLDALGVAA LGVNCSLGPV ELLPIVAQMM EWTDLPIIVK PNAGLPDPRT GAYEMTAEEF GTEMAEFARR GAVIMGGCCG TNPDFIRALT AAIASGAEDR PKRKKRKGVA SPGCVAEYGK LNVIGERINP TGKKRLQQAL LEEDMGYIKK LAISQQEAGA NVLDINVGAQ GVDEEAIIPR VVKAVQSVVD LPLQIDSANP KVIEAALRVT NGRVIINSVS GERARMDEIF PLAKHYGAAV LGLALDEAGL PQTAAERVAI AERIIEEAER YGLDREDIII DCLTLTVSAQ QEQAMETLRA VREVHDRLGL HCALGVSNIS FGLPARVHMT ENFLIQAMHV GLDFPIVNPN TKEIMDAVVS YRAVSGEDVD CAAYITRFAP EQAEMRRRKE LGLTGDTGVD AAVQTAVEQA GDVDPLMDAI MCGLSDDAER ITRKLLTEMA PMDIIQEKVI PALDIVGDRY EKEIIFLPQL INAANAATAG LELIKVKLAE AGQGVSKGKI ILATVEGDIH DIGKNIVKVV LENYGYQIID LGRDVPVTRI VEVAIEKKVG LIGLSALMTT TVTAMKRTIE ALREAGHDCQ TVVGGAVLTE DYAREIGADY YAGDARSIVE IARRVLDEQE G // ID E7N338_9FIRM Unreviewed; 592 AA. AC E7N338; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 17. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HMPREF9555_01410 {ECO:0000313|EMBL:EFW29599.1}; OS Selenomonas artemidis F0399. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Selenomonas. OX NCBI_TaxID=749551 {ECO:0000313|EMBL:EFW29599.1}; RN [1] {ECO:0000313|EMBL:EFW29599.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0399 {ECO:0000313|EMBL:EFW29599.1}; 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 (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFW29599.1}. 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; AECV01000023; EFW29599.1; -; Genomic_DNA. DR RefSeq; WP_009350070.1; NZ_GL638136.1. DR EnsemblBacteria; EFW29599; EFW29599; HMPREF9555_01410. DR PATRIC; 46558306; VBISelArt149184_0956. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EFW29599.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EFW29599.1}. SQ SEQUENCE 592 AA; 64615 MW; 219960C464FC0226 CRC64; MAQGRAELRD YLKTAPLIFD GGMGTYYAQK LHTRGKGVEL ANIETPIVVG DIHTEYLRAG AQAIKTNTFA ANRIVYQGDE ELVRRIVTAG WEIAAHAAAP FDAYVFADIG PVMGLPHADI IDEYAFLADT FLALGARYFI FETNSSDEGL IETAAHIKQK CPEAFVLNSF SAYPGGYTRD GRFVEDLVRA VAGSGYVDAV GFNCVNGTKQ MKELIRHLGA HELPLSLMPN AGHPVVVDGR TFYESAPDYF GSSLAAVRRD GVSILGGCCG TTPAHIKALC DALAAQGDIM PEEDEEAPPQ VAELPKSPFY EALKSGAKPI AVELDPPETG SADKFMAGAR ELMAAGVNAI TIADNPIARA RMDAAMLAGR VHRELGIEPI PHMTCRDRNL NAIKSLLLGL SAEGVHNIIT ITGDPIPTAE RDEVKSVYQF NSRKLASFIT SLGSRGDVVP FHIFGALNVN AKFFGTQINL AKKKVEEGMM GFFTQPVLSE RAKENMRAVR ETFPEALILG GIMPVVSERN ARYMESEITG IHVEERIIDM YRGLDREQAE ELAVRLSLEI ARDIEPYIDG YYIITPFSRT TLVARIVKEL KK // ID E7NDU4_9ACTO Unreviewed; 325 AA. AC E7NDU4; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 12. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFW25658.1}; GN ORFNames=HMPREF9057_02987 {ECO:0000313|EMBL:EFW25658.1}; OS Actinomyces sp. oral taxon 171 str. F0337. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Actinomycineae; Actinomycetaceae; Actinomyces. OX NCBI_TaxID=706439 {ECO:0000313|EMBL:EFW25658.1}; RN [1] {ECO:0000313|EMBL:EFW25658.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0337 {ECO:0000313|EMBL:EFW25658.1}; 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 (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. {ECO:0000313|EMBL:EFW25658.1}. 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; AECW01000547; EFW25658.1; -; Genomic_DNA. DR RefSeq; WP_009398525.1; NZ_GL637946.1. DR EnsemblBacteria; EFW25658; EFW25658; HMPREF9057_02987. DR PATRIC; 46564698; VBIActSp147751_2242. DR OrthoDB; EOG6C019S; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFW25658.1}; KW Transferase {ECO:0000313|EMBL:EFW25658.1}. SQ SEQUENCE 325 AA; 34028 MW; 84CA21A63F890A72 CRC64; MRTLSVSATS FGGEPVRLSD LLARGPVVLD GAMGTELDAR GVDTRNALWS ARALTTAPDL VREVHSDYLD AGARVITTNT YQATLPALIR SGEDAAGARR VIAVGARLAK EAARRFGEEH PEESVLVAGG IGPYGAYLAD GSEYTGAYDI DIPEDPGFQE VHLPRIEVLV GEGIHLFALE TIPRLDEAQA LVAMVKGLAP RAECWVSFQV RSDGARLADG APLAEAAAWG AQEEMVVAVG INCVAPGVVA RALPVLRAAT GKPLAAYPNA GDLYDPATKT WQSTGDRAGI PALAPSWIDA GVRLVGGCCR TRPAQISELA RAVCP // ID E7NKB1_YEASO Unreviewed; 324 AA. AC E7NKB1; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 07-JAN-2015, entry version 15. DE SubName: Full=Mht1p {ECO:0000313|EMBL:EGA61411.1}; GN ORFNames=FOSTERSO_2995 {ECO:0000313|EMBL:EGA61411.1}; OS Saccharomyces cerevisiae (strain FostersO) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=764101 {ECO:0000313|EMBL:EGA61411.1, ECO:0000313|Proteomes:UP000007237}; RN [1] {ECO:0000313|EMBL:EGA61411.1, ECO:0000313|Proteomes:UP000007237} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FostersO {ECO:0000313|EMBL:EGA61411.1, RC ECO:0000313|Proteomes:UP000007237}; 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. {ECO:0000313|EMBL:EGA61411.1}. 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; AEEZ01000062; EGA61411.1; -; Genomic_DNA. DR ProteinModelPortal; E7NKB1; -. DR SMR; E7NKB1; 3-313. DR OrthoDB; EOG7X9GHR; -. DR Proteomes; UP000007237; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007237}; KW Reference proteome {ECO:0000313|Proteomes:UP000007237}. SQ SEQUENCE 324 AA; 36715 MW; A77194694B6E5C14 CRC64; MKRIPIKELI VEHPGKVLIL DGGQGTELEN RGININSPVW SAAPFTSESF WEPSSQERKV VEEMYRDFMI AGANILMTIT YQANFQSISE NTSIKTLAAY KRFLDKIVSF TREFIGEERY LIGSIGPWAA HVSCEYTGDY GPHPENIDYY GFFKPQLENF NQNRDIDLIG FETIPNFHEL KAILSWDEDI ISKPFYIGLS VDDNSLLRDG TTLEEISVHI KGLGNKINKN LLLMGVNCVS FNQSALILKM LHEHLPGMPL LVYPNSGEIY NPKEKTWHRP TNKLDDWETT VKKFVDNGAR IIGGCCRTSP KDIAEIASAV DKYS // ID E7NLX4_YEASO Unreviewed; 261 AA. AC E7NLX4; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 07-JAN-2015, entry version 14. DE SubName: Full=Sam4p {ECO:0000313|EMBL:EGA60884.1}; GN ORFNames=FOSTERSO_3826 {ECO:0000313|EMBL:EGA60884.1}; OS Saccharomyces cerevisiae (strain FostersO) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=764101 {ECO:0000313|EMBL:EGA60884.1, ECO:0000313|Proteomes:UP000007237}; RN [1] {ECO:0000313|EMBL:EGA60884.1, ECO:0000313|Proteomes:UP000007237} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FostersO {ECO:0000313|EMBL:EGA60884.1, RC ECO:0000313|Proteomes:UP000007237}; 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. {ECO:0000313|EMBL:EGA60884.1}. 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; AEEZ01000079; EGA60884.1; -; Genomic_DNA. DR OrthoDB; EOG7X9GHR; -. DR Proteomes; UP000007237; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007237}; KW Reference proteome {ECO:0000313|Proteomes:UP000007237}. SQ SEQUENCE 261 AA; 29516 MW; C21D6DB5CC4A6D24 CRC64; MFNDFLNAGA EILMTTTYQT SYKSVSENTP IRTLSEYNNL LNRIVDFSRN CIGEDKYLIG CIGPWGAHIC CEFTGDYGAE PENIDFYQYF KPQLENFNKN DKLDLIGFET IPNIHELKAI LSWDESILSR PFYIGLSVHE HGVLRDGTTM EEIAQVIKDL GDKINHNFSF LGINCVSFNQ SPDILESLHQ ALPNMALLAY PNSGEVYDTE KKIWLPNSDK LNSWDTVVKQ YISSGARIIG GCCRTSPKDI QEISAAVKKY T // ID E7NNJ3_YEASO Unreviewed; 112 AA. AC E7NNJ3; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 07-JAN-2015, entry version 14. DE SubName: Full=Sam4p {ECO:0000313|EMBL:EGA60175.1}; GN ORFNames=FOSTERSO_4613 {ECO:0000313|EMBL:EGA60175.1}; OS Saccharomyces cerevisiae (strain FostersO) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=764101 {ECO:0000313|EMBL:EGA60175.1, ECO:0000313|Proteomes:UP000007237}; RN [1] {ECO:0000313|EMBL:EGA60175.1, ECO:0000313|Proteomes:UP000007237} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FostersO {ECO:0000313|EMBL:EGA60175.1, RC ECO:0000313|Proteomes:UP000007237}; 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. {ECO:0000313|EMBL:EGA60175.1}. 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; AEEZ01000096; EGA60175.1; -; Genomic_DNA. DR OrthoDB; EOG7X9GHR; -. DR Proteomes; UP000007237; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007237}; KW Reference proteome {ECO:0000313|Proteomes:UP000007237}. SQ SEQUENCE 112 AA; 12435 MW; F01DD58F6C2D4926 CRC64; MEEIAQVIKD LGDKINPNFS FLGINCVSFN QSPDILESLH QALPNMALLA YPNSGEVYDT EKKIWLPNSN KLNSWDTVVK QYISSGARII GGCCRTSPKD IQEISAAVKK YT // ID E7NPN0_YEASO Unreviewed; 169 AA. AC E7NPN0; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 07-JAN-2015, entry version 14. DE SubName: Full=Sam4p {ECO:0000313|EMBL:EGA59902.1}; DE Flags: Fragment; GN ORFNames=FOSTERSO_5207 {ECO:0000313|EMBL:EGA59902.1}; OS Saccharomyces cerevisiae (strain FostersO) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=764101 {ECO:0000313|EMBL:EGA59902.1, ECO:0000313|Proteomes:UP000007237}; RN [1] {ECO:0000313|EMBL:EGA59902.1, ECO:0000313|Proteomes:UP000007237} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FostersO {ECO:0000313|EMBL:EGA59902.1, RC ECO:0000313|Proteomes:UP000007237}; 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. {ECO:0000313|EMBL:EGA59902.1}. 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; AEEZ01000222; EGA59902.1; -; Genomic_DNA. DR OrthoDB; EOG7NCVHW; -. DR Proteomes; UP000007237; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007237}; KW Reference proteome {ECO:0000313|Proteomes:UP000007237}. FT NON_TER 169 169 {ECO:0000313|EMBL:EGA59902.1}. SQ SEQUENCE 169 AA; 19306 MW; 9CCA4341B31CE17F CRC64; MARLPLKQFL ADNPKKVLVL DGGQGTELEN RGIKVANPVW STIPFISESF WSDESSANRK IVKEMFNDFL NAGAEILMTT TYQTSYKSVS ENTPIRTLSE YNNLLNRIVD FSRNCIGEDK YLIGCIGPWG AHICREFTGD YGAEPENIDF YQYFKPQLEN FNKNDKLDL // ID E7P1A2_PSESG Unreviewed; 298 AA. AC E7P1A2; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EFW81777.1}; GN ORFNames=PsgB076_04913 {ECO:0000313|EMBL:EFW81777.1}; OS Pseudomonas savastanoi pv. glycinea str. B076. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=875329 {ECO:0000313|EMBL:EFW81777.1, ECO:0000313|Proteomes:UP000002992}; RN [1] {ECO:0000313|EMBL:EFW81777.1, ECO:0000313|Proteomes:UP000002992} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B076 {ECO:0000313|EMBL:EFW81777.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFW81777.1}. 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; AEGG01000017; EFW81777.1; -; Genomic_DNA. DR RefSeq; WP_004663920.1; NZ_AEGG01000017.1. DR EnsemblBacteria; EFW81777; EFW81777; PsgB076_04913. DR PATRIC; 52501207; VBIPseSyr168192_0966. DR Proteomes; UP000002992; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002992}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EFW81777.1}; KW Transferase {ECO:0000313|EMBL:EFW81777.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 207 207 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 298 AA; 31537 MW; C43D9CCFA2D4F928 CRC64; MTQGTTVILD GGMGRELQRR GAPFRQPEWS ALALSEAPEA VSAVHAAYIE SGAQVITSNS YAVVPFHIGE ERFAREGQAL AALAGRLARE TADASGGRAQ VAGSIPPLFG SYRPDLYKPE LAADVLRPLV AGLSPYVDLW LAETQSCILE AQTIRAGLPN DGKPFWLSFT LQDEDTDEVP RLRSGEPVAD AAKAAAGMGV ATLLFNCSQP EVIGGAIDAA REVFKALNVD IAIGAYANAF PPQPKDAKAN DGLDELREDL DPQGYQQWAA DWVTRGATHI GGCCGIGPEH IAVLSKSL // ID E7P512_PSESG Unreviewed; 1239 AA. AC E7P512; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EFW80678.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFW80678.1}; GN Name=metH {ECO:0000313|EMBL:EFW80678.1}; GN ORFNames=PsgB076_11785 {ECO:0000313|EMBL:EFW80678.1}; OS Pseudomonas savastanoi pv. glycinea str. B076. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=875329 {ECO:0000313|EMBL:EFW80678.1, ECO:0000313|Proteomes:UP000002992}; RN [1] {ECO:0000313|EMBL:EFW80678.1, ECO:0000313|Proteomes:UP000002992} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B076 {ECO:0000313|EMBL:EFW80678.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFW80678.1}. 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; AEGG01000033; EFW80678.1; -; Genomic_DNA. DR RefSeq; WP_004665057.1; NZ_AEGG01000033.1. DR EnsemblBacteria; EFW80678; EFW80678; PsgB076_11785. DR PATRIC; 52504015; VBIPseSyr168192_2320. DR Proteomes; UP000002992; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002992}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFW80678.1}; KW Transferase {ECO:0000313|EMBL:EFW80678.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1239 AA; 135956 MW; 8C33C216367528EA CRC64; MSDRSARHQA FLTALKQRIL ILDGGMGTMI QSYRLEEQDY RGKRFADWPS DVKGNNDLLI LTRPDVIGAI EKAYLDAGAD ILETNTFNAT QVSQADYGME SIVYELNVEG ARLARKVADA KTLETPDKPR FVAGVLGPTS RTCSLSPDVN NPGYRNVTFD ELVENYSEAT KGLIEGGADL ILIETIFDTL NAKAAIFAVQ GVFEEVGFEL PIMISGTITD ASGRTLSGQT TEAFWNSISH AKPISVGLNC ALGASELRPY LQELANKANT HVSAHPNAGL PNAFGEYDEL PSQTAKIIEE FAQSGFLNIV GGCCGTTPAH IKAIAEAVSG YAPRKIPDIP KACRLSGLEP FTIDRQSLFV NVGERTNITG SARFARLIRE DNYTEALEVA LQQVEAGAQV IDINMDEGML DSKKAMVTFL NLIAGEPDIS RVPIMIDSSK WEVIEAGLKC IQGKGIVNSI SMKEGVEQFI HHARLCKRYG AAVVVMAFDE QGQADTEARK KEICKRSYDI LVNEVGFPPE DIIFDPNIFA IATGIEEHNN YAVDFINACA YIRDELPYAL TSGGVSNVSF SFRGNNPVRE AIHSVFLLHA IRNGLSMGIV NAGQLEIYDQ IPAELRDCVE DVVLNRNAEG TDALLAIADK FKGDGSVKEA ETEEWRSWPV NQRLEHALVK GITTHIVQDT EESRLAFTRP IEVIEGPLMA GMNVVGDLFG AGKMFLPQVV KSARVMKQAV AHLIPFIELE KGDKPEAKGK ILMATVKGDV HDIGKNIVGV VLGCNGYDIV DLGVMVPAEK ILQVARDEKC DIIGLSGLIT PSLDEMVHVA REMQRQDFHL PLMIGGATTS KAHTAVKIEP KYSNDAVIYV TDASRAVGVA TQLLSKELKP AFIEKTRLEY VEVRERTSAR SARTERLSYG AAVAKKPQFD WENYTPAQPT FTGTRVLQDI DLNVLAEYID WTPFFISWDL AGKYPRILTD EVVGEAATAL YADATQMLRK LIDEKLISAR AVFGFWPANQ VNDDDLEVYG DDGKPLAKLH HLRQQTIKPD GKPNFSLADF VAPKDSGLTD YIGGFITTAG IGAEEVAKAY QDKGDDYNSI MVKALADRLA EACAEWLHQQ VRKEYWGYAK DEALDNEALI KEQYMGIRPA PGYPACPDHT EKGTLFALLD PLPEGTPEHT PGKSGVFLTE HYAMFPAAAV SGWYFAHPQA QYFAVGKVDK DQVESYTARK GQDLSVTERW LAPNLGYDE // ID E7PNM1_PSESG Unreviewed; 1239 AA. AC E7PNM1; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EFW84973.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFW84973.1}; GN Name=metH {ECO:0000313|EMBL:EFW84973.1}; GN ORFNames=PsgRace4_16869 {ECO:0000313|EMBL:EFW84973.1}; OS Pseudomonas savastanoi pv. glycinea str. race 4. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=875330 {ECO:0000313|EMBL:EFW84973.1}; RN [1] {ECO:0000313|EMBL:EFW84973.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Race 4 {ECO:0000313|EMBL:EFW84973.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFW84973.1}. 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; AEGH01000064; EFW84973.1; -; Genomic_DNA. DR RefSeq; WP_004665057.1; NZ_AEGH01000064.1. DR EnsemblBacteria; EFW84973; EFW84973; PsgRace4_16869. DR PATRIC; 52518047; VBIPseSyr203741_3315. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFW84973.1}; KW Transferase {ECO:0000313|EMBL:EFW84973.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1239 AA; 135956 MW; 8C33C216367528EA CRC64; MSDRSARHQA FLTALKQRIL ILDGGMGTMI QSYRLEEQDY RGKRFADWPS DVKGNNDLLI LTRPDVIGAI EKAYLDAGAD ILETNTFNAT QVSQADYGME SIVYELNVEG ARLARKVADA KTLETPDKPR FVAGVLGPTS RTCSLSPDVN NPGYRNVTFD ELVENYSEAT KGLIEGGADL ILIETIFDTL NAKAAIFAVQ GVFEEVGFEL PIMISGTITD ASGRTLSGQT TEAFWNSISH AKPISVGLNC ALGASELRPY LQELANKANT HVSAHPNAGL PNAFGEYDEL PSQTAKIIEE FAQSGFLNIV GGCCGTTPAH IKAIAEAVSG YAPRKIPDIP KACRLSGLEP FTIDRQSLFV NVGERTNITG SARFARLIRE DNYTEALEVA LQQVEAGAQV IDINMDEGML DSKKAMVTFL NLIAGEPDIS RVPIMIDSSK WEVIEAGLKC IQGKGIVNSI SMKEGVEQFI HHARLCKRYG AAVVVMAFDE QGQADTEARK KEICKRSYDI LVNEVGFPPE DIIFDPNIFA IATGIEEHNN YAVDFINACA YIRDELPYAL TSGGVSNVSF SFRGNNPVRE AIHSVFLLHA IRNGLSMGIV NAGQLEIYDQ IPAELRDCVE DVVLNRNAEG TDALLAIADK FKGDGSVKEA ETEEWRSWPV NQRLEHALVK GITTHIVQDT EESRLAFTRP IEVIEGPLMA GMNVVGDLFG AGKMFLPQVV KSARVMKQAV AHLIPFIELE KGDKPEAKGK ILMATVKGDV HDIGKNIVGV VLGCNGYDIV DLGVMVPAEK ILQVARDEKC DIIGLSGLIT PSLDEMVHVA REMQRQDFHL PLMIGGATTS KAHTAVKIEP KYSNDAVIYV TDASRAVGVA TQLLSKELKP AFIEKTRLEY VEVRERTSAR SARTERLSYG AAVAKKPQFD WENYTPAQPT FTGTRVLQDI DLNVLAEYID WTPFFISWDL AGKYPRILTD EVVGEAATAL YADATQMLRK LIDEKLISAR AVFGFWPANQ VNDDDLEVYG DDGKPLAKLH HLRQQTIKPD GKPNFSLADF VAPKDSGLTD YIGGFITTAG IGAEEVAKAY QDKGDDYNSI MVKALADRLA EACAEWLHQQ VRKEYWGYAK DEALDNEALI KEQYMGIRPA PGYPACPDHT EKGTLFALLD PLPEGTPEHT PGKSGVFLTE HYAMFPAAAV SGWYFAHPQA QYFAVGKVDK DQVESYTARK GQDLSVTERW LAPNLGYDE // ID E7PTP0_PSESG Unreviewed; 298 AA. AC E7PTP0; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EFW83379.1}; GN ORFNames=PsgRace4_26556 {ECO:0000313|EMBL:EFW83379.1}; OS Pseudomonas savastanoi pv. glycinea str. race 4. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=875330 {ECO:0000313|EMBL:EFW83379.1}; RN [1] {ECO:0000313|EMBL:EFW83379.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Race 4 {ECO:0000313|EMBL:EFW83379.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFW83379.1}. 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; AEGH01000079; EFW83379.1; -; Genomic_DNA. DR RefSeq; WP_004663920.1; NZ_AEGH01000079.1. DR EnsemblBacteria; EFW83379; EFW83379; PsgRace4_26556. DR PATRIC; 52521987; VBIPseSyr203741_5202. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EFW83379.1}; KW Transferase {ECO:0000313|EMBL:EFW83379.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 207 207 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 298 AA; 31537 MW; C43D9CCFA2D4F928 CRC64; MTQGTTVILD GGMGRELQRR GAPFRQPEWS ALALSEAPEA VSAVHAAYIE SGAQVITSNS YAVVPFHIGE ERFAREGQAL AALAGRLARE TADASGGRAQ VAGSIPPLFG SYRPDLYKPE LAADVLRPLV AGLSPYVDLW LAETQSCILE AQTIRAGLPN DGKPFWLSFT LQDEDTDEVP RLRSGEPVAD AAKAAAGMGV ATLLFNCSQP EVIGGAIDAA REVFKALNVD IAIGAYANAF PPQPKDAKAN DGLDELREDL DPQGYQQWAA DWVTRGATHI GGCCGIGPEH IAVLSKSL // ID E7Q6M0_YEASB Unreviewed; 324 AA. AC E7Q6M0; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 07-JAN-2015, entry version 15. DE SubName: Full=Mht1p {ECO:0000313|EMBL:EGA57694.1}; GN ORFNames=FOSTERSB_3009 {ECO:0000313|EMBL:EGA57694.1}; OS Saccharomyces cerevisiae (strain FostersB) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=764102 {ECO:0000313|EMBL:EGA57694.1, ECO:0000313|Proteomes:UP000000309}; RN [1] {ECO:0000313|EMBL:EGA57694.1, ECO:0000313|Proteomes:UP000000309} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FostersB {ECO:0000313|EMBL:EGA57694.1, RC ECO:0000313|Proteomes:UP000000309}; 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. {ECO:0000313|EMBL:EGA57694.1}. 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; AEHH01000049; EGA57694.1; -; Genomic_DNA. DR ProteinModelPortal; E7Q6M0; -. DR SMR; E7Q6M0; 3-313. DR OrthoDB; EOG7X9GHR; -. DR Proteomes; UP000000309; Chromosome XII. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000309}; KW Reference proteome {ECO:0000313|Proteomes:UP000000309}. SQ SEQUENCE 324 AA; 36715 MW; A77194694B6E5C14 CRC64; MKRIPIKELI VEHPGKVLIL DGGQGTELEN RGININSPVW SAAPFTSESF WEPSSQERKV VEEMYRDFMI AGANILMTIT YQANFQSISE NTSIKTLAAY KRFLDKIVSF TREFIGEERY LIGSIGPWAA HVSCEYTGDY GPHPENIDYY GFFKPQLENF NQNRDIDLIG FETIPNFHEL KAILSWDEDI ISKPFYIGLS VDDNSLLRDG TTLEEISVHI KGLGNKINKN LLLMGVNCVS FNQSALILKM LHEHLPGMPL LVYPNSGEIY NPKEKTWHRP TNKLDDWETT VKKFVDNGAR IIGGCCRTSP KDIAEIASAV DKYS // ID E7Q803_YEASB Unreviewed; 157 AA. AC E7Q803; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 07-JAN-2015, entry version 14. DE SubName: Full=Sam4p {ECO:0000313|EMBL:EGA57298.1}; DE Flags: Fragment; GN ORFNames=FOSTERSB_3769 {ECO:0000313|EMBL:EGA57298.1}; OS Saccharomyces cerevisiae (strain FostersB) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=764102 {ECO:0000313|EMBL:EGA57298.1, ECO:0000313|Proteomes:UP000000309}; RN [1] {ECO:0000313|EMBL:EGA57298.1, ECO:0000313|Proteomes:UP000000309} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FostersB {ECO:0000313|EMBL:EGA57298.1, RC ECO:0000313|Proteomes:UP000000309}; 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. {ECO:0000313|EMBL:EGA57298.1}. 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; AEHH01000063; EGA57298.1; -; Genomic_DNA. DR OrthoDB; EOG7X9GHR; -. DR Proteomes; UP000000309; Chromosome XIII. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000309}; KW Reference proteome {ECO:0000313|Proteomes:UP000000309}. FT NON_TER 1 1 {ECO:0000313|EMBL:EGA57298.1}. SQ SEQUENCE 157 AA; 17657 MW; 67CCE2CF9ED78723 CRC64; FDWFETIPNI HELKAILSWD ESILSRPFYI GLSVHEHGVL RDGTTMEEIA QVIKDLGDKI NPNFSFLGIN CVSFNQSPDI LESLHQALPN MALLAYPNSG EVYDTKKKIW LPNSNKLNSW DTVVKQYISS GARIIGGCCR TSPKDIQEIS AAVKKYT // ID E7QHL5_YEASZ Unreviewed; 324 AA. AC E7QHL5; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Mht1p {ECO:0000313|EMBL:EGA85856.1}; GN ORFNames=VL3_3050 {ECO:0000313|EMBL:EGA85856.1}; OS Saccharomyces cerevisiae (strain Zymaflore VL3) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=764100 {ECO:0000313|EMBL:EGA85856.1, ECO:0000313|Proteomes:UP000007238}; RN [1] {ECO:0000313|EMBL:EGA85856.1, ECO:0000313|Proteomes:UP000007238} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Zymaflore VL3 {ECO:0000313|Proteomes:UP000007238}; 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. {ECO:0000313|EMBL:EGA85856.1}. 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; AEJS01000048; EGA85856.1; -; Genomic_DNA. DR ProteinModelPortal; E7QHL5; -. DR OrthoDB; EOG7X9GHR; -. DR Proteomes; UP000007238; Chromosome XII. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007238}; KW Reference proteome {ECO:0000313|Proteomes:UP000007238}. SQ SEQUENCE 324 AA; 36729 MW; AD4F03CA4CC76284 CRC64; MKRIPIKELI IEHPGKVLIL DGGQGTELEN RGININSPVW SAAPFTSESF WEPSSQERKV VEEMYRDFMI AGANILMTIT YQANFQSISE NTSIKTLAAY KRFLDKIVSF TREFIGEERY LIGSIGPWAA HVSCEYTGDY GPHPENIDYY GFFKPQLENF NQNRDIDLIG FETIPNFHEL KAILSWDEDI ISKPFYIGLS VDDNSLLRDG TTLEEISVHI KGLGNKINKN LLLMGVNCVS FNQSALILKM LHEHLPGMPL LVYPNSGEIY NPKEKTWHRP TNKLDDWETT VKKFVDNGAR IIGGCCRTSP KDIAEIASAV DKYS // ID E7QJH4_YEASZ Unreviewed; 140 AA. AC E7QJH4; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 07-JAN-2015, entry version 14. DE SubName: Full=Sam4p {ECO:0000313|EMBL:EGA85210.1}; DE Flags: Fragment; GN ORFNames=VL3_3901 {ECO:0000313|EMBL:EGA85210.1}; OS Saccharomyces cerevisiae (strain Zymaflore VL3) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=764100 {ECO:0000313|EMBL:EGA85210.1, ECO:0000313|Proteomes:UP000007238}; RN [1] {ECO:0000313|EMBL:EGA85210.1, ECO:0000313|Proteomes:UP000007238} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Zymaflore VL3 {ECO:0000313|Proteomes:UP000007238}; 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. {ECO:0000313|EMBL:EGA85210.1}. 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; AEJS01000054; EGA85210.1; -; Genomic_DNA. DR OrthoDB; EOG7X9GHR; -. DR Proteomes; UP000007238; Chromosome XIII. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007238}; KW Reference proteome {ECO:0000313|Proteomes:UP000007238}. FT NON_TER 1 1 {ECO:0000313|EMBL:EGA85210.1}. SQ SEQUENCE 140 AA; 15591 MW; 19E46DBC02A0BDDF CRC64; SWDESILSRP FYIGLSVHEH GVLRDGTTME EIAQVIKDLG DKINPNFSFL GINCVSFNQS PDILESLHQA LPNMALLAYP NSGEVYDTEK KIWLPNSDKL NSWDTVVKQY ISSGARIIGG CCRTSPKDIQ EISAAVKKYT // ID E7QLI4_YEASZ Unreviewed; 164 AA. AC E7QLI4; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 07-JAN-2015, entry version 14. DE SubName: Full=Sam4p {ECO:0000313|EMBL:EGA84434.1}; GN ORFNames=VL3_4715 {ECO:0000313|EMBL:EGA84434.1}; OS Saccharomyces cerevisiae (strain Zymaflore VL3) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=764100 {ECO:0000313|EMBL:EGA84434.1, ECO:0000313|Proteomes:UP000007238}; RN [1] {ECO:0000313|EMBL:EGA84434.1, ECO:0000313|Proteomes:UP000007238} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Zymaflore VL3 {ECO:0000313|Proteomes:UP000007238}; 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. {ECO:0000313|EMBL:EGA84434.1}. 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; AEJS01000063; EGA84434.1; -; Genomic_DNA. DR OrthoDB; EOG7NCVHW; -. DR Proteomes; UP000007238; Chromosome XVI. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007238}; KW Reference proteome {ECO:0000313|Proteomes:UP000007238}. SQ SEQUENCE 164 AA; 18735 MW; 2B917FBA00ADFC9D CRC64; MARLPLKQFL ADNPKKVLVL DGGQGTELEN RGIKVANPVW STIPFISESF WSDESSANRK IVKEMFNDFL NAGAEILMTT TYQTSYKSVS ENTPIRTLSE YNNLLNRIVD FSRNCIGEDK YLIGCIGPWG AHICREFTGD YGAEPENIDF YQYFKPQLEN FNKK // ID E7QMB1_YEASZ Unreviewed; 261 AA. AC E7QMB1; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Sam4p {ECO:0000313|EMBL:EGA84233.1}; GN ORFNames=VL3_5209 {ECO:0000313|EMBL:EGA84233.1}; OS Saccharomyces cerevisiae (strain Zymaflore VL3) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=764100 {ECO:0000313|EMBL:EGA84233.1, ECO:0000313|Proteomes:UP000007238}; RN [1] {ECO:0000313|EMBL:EGA84233.1, ECO:0000313|Proteomes:UP000007238} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Zymaflore VL3 {ECO:0000313|Proteomes:UP000007238}; 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. {ECO:0000313|EMBL:EGA84233.1}. 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; AEJS01000085; EGA84233.1; -; Genomic_DNA. DR ProteinModelPortal; E7QMB1; -. DR OrthoDB; EOG7X9GHR; -. DR Proteomes; UP000007238; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007238}; KW Reference proteome {ECO:0000313|Proteomes:UP000007238}. SQ SEQUENCE 261 AA; 29529 MW; 033A9E74EBAE569C CRC64; MFNDFLNAGA EILMTTTYQT SYKSVSENTP IRTLSEYNNL LNRIVDFSRN CIGEDKYLIG CIGPWGAHIC REFTGDYGAE PENIDFYQYF KPQLENFNKN DKLDLIGFET IPNIHELKAI LSWDESILSR PFYIGLSVHE HGVLRDGTTM EEIAQVIKDL GDKINPNFSF LGINCVSFNQ SPDILESLHQ ALPNMALLAY PNSGEVYDTE KKIWLPNSDK LNSWDTVVKQ YISSGARIIG GCCRTSPKDI QEISAAVKKY T // ID E7RFH7_9BACL Unreviewed; 619 AA. AC E7RFH7; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 20. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=GPDM_06103 {ECO:0000313|EMBL:EGA90264.1}; OS Planococcus donghaensis MPA1U2. OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; OC Planococcus. OX NCBI_TaxID=933115 {ECO:0000313|EMBL:EGA90264.1}; RN [1] {ECO:0000313|EMBL:EGA90264.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MPA1U2 {ECO:0000313|EMBL:EGA90264.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGA90264.1}. 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; AEPB01000020; EGA90264.1; -; Genomic_DNA. DR RefSeq; WP_008429916.1; NZ_AEPB01000020.1. DR EnsemblBacteria; EGA90264; EGA90264; GPDM_06103. DR PATRIC; 46586929; VBIPlaDon176822_1177. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EGA90264.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EGA90264.1}. SQ SEQUENCE 619 AA; 68050 MW; 7AFE7A048148DB6C CRC64; MGLLDELKTR ILTADGAMGT LLYSYGIEYC NEELNLQRPE IVEKIHLDYI KAGADIIQTN TYGANALKLA RYGLESQVAE INKAAIDIAN RAAAPGGQFV FGTIGGIRGI RKSDASLQEI IAMVDQQATH LLEGNPDGLL LETYYDFEEL AATVKHLKSI TNTPLIAQVS MHDPGILQNG MSLNDALHQL ETLGADIVGV NCRLGPHHTI QAFEEVTLPE KAFLSAYPNA SLLDVEDGRI VYESEADYFG RAALLLREEG VRLIGGCCGT TPKHIEAVKK HLGQLAPIVR KEVTERKPIV IREAEALEVK PLHEKAKTER TIIVELDTPR HLDVTKFLEG SVALKAAGVD AVTMADNSLA SPRISNMAMG SILKHTEDIR ALAHITCRDR NLIGLQSHLM GLDALGIHDI LAVTGDPTKV GDFPGATSVY DVSSMELIQL IKKLNEGISF SGKSLRKKAN FSVAAAFNPN VRVLDRAVAR LEKKIESGAD YFISQPVYTK EKITEIYEAT KHLETPIFIG VMPLTSIRSA EFLHNEVPGI KLSDDALARM RACGDDKDRA TEEGIQIAKE LIDTAAELFH GIYLITPFVR YDMTVELIHY IRQLDQQKES DRNHVQASY // ID E7RFH8_9BACL Unreviewed; 1145 AA. AC E7RFH8; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGA90265.1}; GN ORFNames=GPDM_06108 {ECO:0000313|EMBL:EGA90265.1}; OS Planococcus donghaensis MPA1U2. OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; OC Planococcus. OX NCBI_TaxID=933115 {ECO:0000313|EMBL:EGA90265.1}; RN [1] {ECO:0000313|EMBL:EGA90265.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MPA1U2 {ECO:0000313|EMBL:EGA90265.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGA90265.1}. 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; AEPB01000020; EGA90265.1; -; Genomic_DNA. DR RefSeq; WP_008429917.1; NZ_AEPB01000020.1. DR EnsemblBacteria; EGA90265; EGA90265; GPDM_06108. DR PATRIC; 46586931; VBIPlaDon176822_1178. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 725 725 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1145 AA; 126141 MW; 4F34E500E1FBCE51 CRC64; MSKHLIEQQL EKRILIIDGA MGTMIQNEDL SPEDFGGEEF DGCNEYLNIV RPDVIKNVHT AYLEAGADIL CTNTFGGTPI VLDEYGIGDQ AADINRRAVE IAKKAAAEFS TPEWPRFVAG AIGPTTKTLS VTGGATFDEM LENFYVQAKA LIEGGADLIL LETSQDMLNV KAATIGINQA FEETGLELPI MVSGTIEPMG TTLAGQSIEA FYISIEHVKP LSVGLNCATG PEFMTDHIRS LSELSDGYVS CYPNAGLPDE DGHYHETPES LAKKLRGFAD KGWLNVVGGC CGTTPAHIKA VREAMDGLPP RKPDPIEHGH VVSGIEPLQY DETMRPLFIG ERTNVIGSRK FKRLIIDGQF EEAAEIARAQ VKNGAHVIDI CLANPDRDEV EDMTHFMKEV VKKVKVPLVI DSTDEEVIEV ALKFSQGKAI INSINLEDGE ERFEAVMPLV KKYGAAVVVG TIDEVGMAVT RERKLEIAER SYDLLVNKWG LAPEDIIFDP LVFPVGTGDQ QYIGSAVETI EGIRLIKEKL PRTLTILGVS NVSFGLPPVG REVLNAVYLY HCTQAGLDYA IVNTEKLERY ASIPKQEIDM ANELLFTTTD DTLADFTAFY RDKKKEKTED DIPKTVPDRL AYYIIEGTKE GLIPDLEKAL DMYDEPLDVI NGPLMKGMAE VGRLFNDNQL IVAEVLQSAG VMKAAVSFLE QFMEKKEDDS GKGKIVLATV KGDVHDIGKN LVEIILSNNG FKVIDVGIKV TPATLIEVIR KEKPDMIGLS GLLVKSAKQM VITAQDFKEA GIDVPILVGG AALSRRFTET KISAEYDGPV IYAKDAMQGL DLANRLQSGA GKAELLLELD AQQEKRQASE AVRAAKPAVA VAEKPVKTVR EDVTVYVPND LRRHVLKDYS VAHLYPYVNM RTLIGHHLGL KGFSEKTLAK GDPRAVQLHE LATEFLGSGV LKPSGMYQFF PAQSDGDDVI VYDPKDGKTE IERFTFPRQS APPFLCLSDY LKSVDSGEMD YVAFMQVTAG FGVREQATRL KEQGKFLESH ALQATALELA EGFAERIHQE IRDQWGFPDA TDFSMRERFA AKYQGQRFSF GYPACPNLED QAKLFNLIKP EDIGVHLTEE YMMDPEASVS AIVFAHPDAR YFIVD // ID E7RSR1_9BACT Unreviewed; 919 AA. AC E7RSR1; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFZ36262.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFZ36262.1}; GN Name=metH {ECO:0000313|EMBL:EFZ36262.1}; GN ORFNames=HMPREF0663_12329 {ECO:0000313|EMBL:EFZ36262.1}; OS Prevotella oralis ATCC 33269. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=873533 {ECO:0000313|EMBL:EFZ36262.1, ECO:0000313|Proteomes:UP000005580}; RN [1] {ECO:0000313|EMBL:EFZ36262.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33269 {ECO:0000313|EMBL:EFZ36262.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFZ36262.1}. 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; AEPE02000006; EFZ36262.1; -; Genomic_DNA. DR RefSeq; WP_004370558.1; NZ_GL833119.1. DR EnsemblBacteria; EFZ36262; EFZ36262; HMPREF0663_12329. DR OrthoDB; EOG6091CH; -. DR Proteomes; UP000005580; Unassembled WGS sequence. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000005580}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFZ36262.1}; KW Transferase {ECO:0000313|EMBL:EFZ36262.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 240 240 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 919 AA; 101426 MW; FB61DBBE97DF868B CRC64; MTLRDAAAQR ILILDGAMGT MIQDYGLTEN DFRNEQLVDI PGQMKGNNDV LNLTRPDVIM DIHRRYLQAG ADIIETNTFS SQRISQADYR LEGYAVRLSL EGARLARQAA NEFSTPEKPR FVAGSVGPTN KTCSMSPDVS NPAARELTYD DLYQAYTEQI EALVEGGVDA LLIETIFDTL NAKVAIDAAQ SVMASHQISL PIMLSVTVSD LAGRTLSGQT LEAFLASIST YDIFSVGLNC SFGARQMKPY LKELARKAPY YISAYPNAGL PNSMGLYDET AESMTPQIGE FIDEGLVNIV GGCCGTTDEF IARYARWAQG KKPRRVVAKP KTMWLSGLEL LDETPEVQFV NVGERCNVAG SRKFLRLIKE KNYEEAMSIA RKQVEDGALV IDVNMDDGLL DAKAEMVTFL NMIAAEPDIA KVPVMIDSSK WDVIVAGLKC CQGKCVVNSI SLKEGEEKFI EHAKDVQRYG AAVVVMCFDE RGQATSFERR IEIAGRAYRI LTEKVGMNPL DIIFDPNILA IATGMEEHDN YAVDFIKSVE WIKNNLPGAH VSGGISNLSF SFRGNNYVRE AMHAVFLYYA IKAGMDFGIV NPAAKVMYTD IPEEHLQILE DVVLNRRKNA SEDLIELADR LKKEAEEASA RQNVGNSQAE NREGWRSEPV DKRLGYALRK GIGDYLDEDI REALKVYPRA VDIIEGPLMA GMNEVGELFG AGKMFLPQVV KTARTMKQAV YILQPYIEGE KKDNSSKAGK VILATVKGDV HDIGKNIVSV VMSCNNYEVI DMGVMVPAEH IVKKAIEEKA DLIGLSGLIT PSLEEMVNVA VEMRRAGLDI PIMIGGATTS QLHVALKIAP VYSGPVVWMK DASQNALAAA KLLNKAEEPS YANSLNEKYA KLREGYRQEQ QQLISIDEAR KNKLNLFES // ID E7RZQ6_9BURK Unreviewed; 1260 AA. AC E7RZQ6; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFV94055.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFV94055.1}; GN Name=metH {ECO:0000313|EMBL:EFV94055.1}; GN ORFNames=HMPREF0551_2170 {ECO:0000313|EMBL:EFV94055.1}; OS Lautropia mirabilis ATCC 51599. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Lautropia. OX NCBI_TaxID=887898 {ECO:0000313|EMBL:EFV94055.1}; RN [1] {ECO:0000313|EMBL:EFV94055.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 51599 {ECO:0000313|EMBL:EFV94055.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFV94055.1}. 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; AEQP01000022; EFV94055.1; -; Genomic_DNA. DR RefSeq; WP_005674567.1; NZ_GL636062.1. DR EnsemblBacteria; EFV94055; EFV94055; HMPREF0551_2170. DR PATRIC; 46595521; VBILauMir174490_1265. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFV94055.1}; KW Transferase {ECO:0000313|EMBL:EFV94055.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 249 249 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 315 315 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 786 786 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1260 AA; 139043 MW; 42449DC3887C696A CRC64; MGPVETRLRE LLKERILILD GAMGTMIQQY KLGEDDYRGE RFRDHAHDVK GNNELLSLTR PDIIQEIHEK YLEAGADLIE TNTFGATAVA QADYHLPELA YEMNVASARL ARAAADKYST PERPRFVAGA LGPQPKTASI SPDVNDPAAR NITFEELRAA YLEQARGLAE GGADVFLVET IFDTLNAKAA LFALDELAEE RSAQGLPRIP VMISGTVTDA SGRILSGQTV EAFWNSVRHA KPLTIGLNCA LGAALMRPYI EELARKADTF VCVYPNAGLP NPMAETGFDE TPDITSALLK EFAQANLVNI AGGCCGTTPA HIRAIAEAVR PLTPRVPPVI PVATRLSGLE PFNIDEDSLF VNVGERTNVT GSKAFARMIL NEQYDEALQV ARQQVENGAQ IIDVNMDEAM LDAMKAMPRF LNLIASEPDI ARVPIMIDSS KWEVIEAGLR CVQGKAVVNS ISLKEGEEKF LHQARLVRRY GAAAVVMAFD EQGQADTFQR KIEICKRAYD LLVNEVGFPP EDIIFDPNIF AVATGIEEHD EYGNDFIRAC QWIHDNLPHA RISGGVSNVS FSFRGNNPAR EAIHTVFLYH AIKAGLTMGI VNAGMMGVYD EVPLELRNRI EDVVLNRKPV FPDDLPVDAP ERELTATERL IEIAQTLKDD GGKKEADQAW RKGSVQERIT HAMVHGITQY IVEDTEEIRQ EIAARGGRPI EVIEGPLMAG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA HLLPFIEAEK AALAAAGGDV RSRGKIVIAT VKGDVHDIGK NIVSVVLECN NFEVVNMGVM VPCAQILEKA RETGADLIGL SGLITPSLEE MAFVAGEMER DEYFRSRKIP LLIGGATTSR VHTAVKIAPN YSGPVVYVPD ASRSVPVAQA LVSEEQREGF LADLHSEYDR VRNLHGKKKG PNFIPLADAR ANREQTDWST YVPPRPKFIG RRTFKNQDLS KLAEYIDWGP FFQTWDLAGK FPDILDDAVV GEEARKVYAD GKAMLKKIID NRWLTANGVV MFLPANTIND DDIEIYTDDS RTQVAMTWRN LRQQNAKREG IPNKSLADYI APKFIDGKPS GIQDYIGMFA VTAGIGADKK EAEYMAALDD YNAIAFKSIA DRLAEAFAEA LHERVRKDLW GYASDEKFTN DELIAEAYTG IRPAPGYPSC PEHTIKKEMF ELMDCQEIGM HVTEALAMWP AASVSGFYFS HPHSEYFGIG NIDEDQLQDF IRRSGRDEAE VRRALAPLLG // ID E7S1K5_STRAG Unreviewed; 614 AA. AC E7S1K5; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 18. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HMPREF9171_0151 {ECO:0000313|EMBL:EFV98344.1}; OS Streptococcus agalactiae ATCC 13813. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=888745 {ECO:0000313|EMBL:EFV98344.1}; RN [1] {ECO:0000313|EMBL:EFV98344.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 13813 {ECO:0000313|EMBL:EFV98344.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFV98344.1}. 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; AEQQ01000009; EFV98344.1; -; Genomic_DNA. DR RefSeq; WP_000032992.1; NZ_GL636070.1. DR EnsemblBacteria; EFV98344; EFV98344; HMPREF9171_0151. DR PATRIC; 52949840; VBIStrAga174344_0145. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EFV98344.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EFV98344.1}. SQ SEQUENCE 614 AA; 68048 MW; 09EEF756896B24FC CRC64; MSKFLEKLKT DILVADGAMG TLLYTYGLDT CHESYNVTHP EKVLAIHQAY IEAGADVIQT NTYGAQRHRL KNYGLEDQVV SINQAAVNLA HQATLGKETF ILGTVGGFRS QRQCDLTLDN IVEETLEQIE ALLATGQLDG LLFETYYDIE EITTVLKIVR EMTDLPIITN ISLHEAGVTS NGKPIVEALS QLVMLGADVI GLNCHLGPYH MIQSLKQVPL FAQSYLSVYP NASQLSLDGE NSQYQFSQNS EYFGKSAELL VAEGVRLIGG CCGTTPDHIR AVKRSIRGLK PIERKVVTPI IPVKDFVRRI RRTDTLVDKV KKEVTIIAEL DPPKHLDIVQ FQKAIRAIDQ KGIAAITLAD NSLSNTRICN LSIASLLKDE ISTPFLLHIA CRDHNLIGLQ SRLLGMELLG FNHILAITGD PTKLGDFPGA TSVYDVTSFK LLSLIKQLNQ GLSYSGASLR RPTDFTVAAA FNPNVKNLTR TVKLIEKKVA SGADYFMTQP IFDHSVLKEL ADLTKTVEQP FFIGIMPITS YNNAVFLHNE VPGIKLSESF LSALEKVKDD KEACLTLALN ESKSLIDEAL NYFNGIYLIT PFLRYDLTLE LIDYIQKKQV RKSS // ID E7S3S2_STRAG Unreviewed; 335 AA. AC E7S3S2; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 01-OCT-2014, entry version 11. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFV97620.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EFV97620.1}; GN Name=mmuM {ECO:0000313|EMBL:EFV97620.1}; GN ORFNames=HMPREF9171_0918 {ECO:0000313|EMBL:EFV97620.1}; OS Streptococcus agalactiae ATCC 13813. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=888745 {ECO:0000313|EMBL:EFV97620.1}; RN [1] {ECO:0000313|EMBL:EFV97620.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 13813 {ECO:0000313|EMBL:EFV97620.1}; 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. {ECO:0000313|EMBL:EFV97620.1}. 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; AEQQ01000050; EFV97620.1; -; Genomic_DNA. DR EnsemblBacteria; EFV97620; EFV97620; HMPREF9171_0918. DR PATRIC; 52951390; VBIStrAga174344_0889. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFV97620.1}; KW Transferase {ECO:0000313|EMBL:EFV97620.1}. SQ SEQUENCE 335 AA; 36558 MW; 38BF0648C1197B0C CRC64; MFHLLFSAIF ITNYVTRNGD LMGRFKELLE SKKTFILHGA LGTELESRGC DVSGKLWSAK YLIEDPAAIQ TIHEDYIRAG ADIVTTSTYQ ATLQGLAQVG VSESQAEDLI RLTVQLAKAA REQVWKSLTK EEKSERIYPL ISGDVGPYAA FLADGSEYTG LYDIDKEDLK NFHRHRIELL LDEDVDLLAL ETIPNAQEAE ALIELLAEDF PQVEAYMSFT SQDGKTISDG SAVAGLAKAI NASPQVVALG INCSSPSLVA DFLQAIAEQT NKPLVTYPNS GEVYDGASQS WQSSPDHSHT LLENTSDWQK LGAQVVGGCC RTRPADIADL SAHLT // ID E7SFY8_SHIDY Unreviewed; 1227 AA. AC E7SFY8; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFW51560.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFW51560.1}; GN ORFNames=SDB_00969 {ECO:0000313|EMBL:EFW51560.1}; OS Shigella dysenteriae CDC 74-1112. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=941429 {ECO:0000313|EMBL:EFW51560.1}; RN [1] {ECO:0000313|EMBL:EFW51560.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CDC 74-1112 {ECO:0000313|EMBL:EFW51560.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFW51560.1}. 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; AERM01000053; EFW51560.1; -; Genomic_DNA. DR RefSeq; WP_000096050.1; NZ_AERM01000053.1. DR EnsemblBacteria; EFW51560; EFW51560; SDB_00969. DR PATRIC; 47301407; VBIAERShi179086_0983. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFW51560.1}; KW Transferase {ECO:0000313|EMBL:EFW51560.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136085 MW; D026735AA497DBBD CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEAQDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTDNAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKSDYIGA FAVTGGPEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID E7T246_SHIBO Unreviewed; 1227 AA. AC E7T246; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFW53963.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFW53963.1}; GN ORFNames=SGB_03702 {ECO:0000313|EMBL:EFW53963.1}; OS Shigella boydii ATCC 9905. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=932676 {ECO:0000313|EMBL:EFW53963.1}; RN [1] {ECO:0000313|EMBL:EFW53963.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 9905 {ECO:0000313|EMBL:EFW53963.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFW53963.1}. 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; AERN01000077; EFW53963.1; -; Genomic_DNA. DR RefSeq; WP_000095991.1; NZ_AERN01000077.1. DR EnsemblBacteria; EFW53963; EFW53963; SGB_03702. DR PATRIC; 47317789; VBIAERShi181732_3728. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFW53963.1}; KW Transferase {ECO:0000313|EMBL:EFW53963.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136029 MW; 123D640213FF4034 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHKA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGTAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG EEAKRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID E8I2I3_ECOLX Unreviewed; 1227 AA. AC E8I2I3; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EFX17976.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EFX17976.1}; GN Name=metH {ECO:0000313|EMBL:EFX17976.1}; GN ORFNames=ECO2687_20864 {ECO:0000313|EMBL:EFX17976.1}; OS Escherichia coli O157:H- str. H 2687. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=926028 {ECO:0000313|EMBL:EFX17976.1, ECO:0000313|Proteomes:UP000004043}; RN [1] {ECO:0000313|EMBL:EFX17976.1, ECO:0000313|Proteomes:UP000004043} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H 2687 {ECO:0000313|EMBL:EFX17976.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EFX17976.1}. 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; AETZ01000110; EFX17976.1; -; Genomic_DNA. DR RefSeq; WP_000096047.1; NZ_AETZ01000110.1. DR ProteinModelPortal; E8I2I3; -. DR SMR; E8I2I3; 651-1227. DR EnsemblBacteria; EFX17976; EFX17976; ECO2687_20864. DR PATRIC; 48141014; VBIEscCol183164_2953. DR Proteomes; UP000004043; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000004043}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EFX17976.1}; KW Transferase {ECO:0000313|EMBL:EFX17976.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136040 MW; 8FB5738E12303E7E CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID E8JNP0_STREI Unreviewed; 314 AA. AC E8JNP0; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFW89164.1}; GN ORFNames=HMPREF0819_0613 {ECO:0000313|EMBL:EFW89164.1}; OS Streptococcus equinus ATCC 9812. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=525379 {ECO:0000313|EMBL:EFW89164.1}; RN [1] {ECO:0000313|EMBL:EFW89164.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 9812 {ECO:0000313|EMBL:EFW89164.1}; 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. {ECO:0000313|EMBL:EFW89164.1}. 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; AEVB01000019; EFW89164.1; -; Genomic_DNA. DR RefSeq; WP_004232040.1; NZ_GL698429.1. DR EnsemblBacteria; EFW89164; EFW89164; HMPREF0819_0613. DR PATRIC; 46642296; VBIStrEqu32851_0214. DR OrthoDB; EOG6C019S; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFW89164.1}; KW Transferase {ECO:0000313|EMBL:EFW89164.1}. SQ SEQUENCE 314 AA; 34615 MW; 52E7A45581C72A3F CRC64; MGKFKDLLDK NEYVILDGAL GTELENRGYD VSGKLWSAKY LLENPKVIQD LHEVYLRAGA DIITTSSYQA TIQGLEDYGL TEQEATDTIA LTVDLAKKAR ENVWNVLSDD EKSKRPYPLI SGDVGPYAAY LADGSEYNGN YHLSKEEFKD FHCTRIKALL SAGCDFLGIE TIPNVVEAEA LIELLADEFP ETEAYMSFTA QDDESISDGT AIETVAALCD ASKQILAFGI NCSSPAVISN LLKKIRTVSQ KPLVTYPNSG EIYDGVTQTW KSLPDHTHTL LENSQIWHQF GAKVVGGCCR TTPDDIACLT NHLR // ID E8JNU6_STREI Unreviewed; 618 AA. AC E8JNU6; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 18. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HMPREF0819_0669 {ECO:0000313|EMBL:EFW89106.1}; OS Streptococcus equinus ATCC 9812. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=525379 {ECO:0000313|EMBL:EFW89106.1}; RN [1] {ECO:0000313|EMBL:EFW89106.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 9812 {ECO:0000313|EMBL:EFW89106.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFW89106.1}. 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; AEVB01000020; EFW89106.1; -; Genomic_DNA. DR RefSeq; WP_004232158.1; NZ_GL698429.1. DR EnsemblBacteria; EFW89106; EFW89106; HMPREF0819_0669. DR PATRIC; 46642402; VBIStrEqu32851_0294. DR OrthoDB; EOG6SNDP1; -. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EFW89106.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EFW89106.1}. SQ SEQUENCE 618 AA; 68049 MW; 622EE85477D5EF09 CRC64; MSRLLERLKT DILVADGAMG TLLYANGLDN CYEAYNLIHP EKVSAIHKAY IEAGADVIQT NTYAAKRHRL KGYGYEDKVK EINQAGVRIA RQAAGKDFFV LGTVGALRGL KQCELSLDEI IQETLEQVNC LLETNQIDGL LFETYYDEEE IIAVLKAVRP LTDLPIITNI ALHEAGITEN GKPLVEIFGK LVMLGADVVG LNCHLGPYHM IQSLKQVPLF AQSYLSVYPN ASLLSFVDDN GSGQYGFSQN ADYFGKSAEL LVAEGARLIG GCCGTTPDHI RAVKRAIKGL KPVSRKFVTP MVEEAELIKA VKQSETIVDK VKRQVTVIAE IDPPKTLDIE KFTEGVKALD DAGVSAITLA DNSLAKTRIC NVSIASLLKN EISTPFLLHL SCRDHNMIGL QSRLLGMDVL GFHQVLAITG DPSKIGDFPG ATSVYDATSF KLLELIQQLN KGKGYSGASI KKETSFTAAA AFNPNVKNLS RCSRLIDKKI AAGADCFITQ PIFNKEIIEN LAELTRDYEA PFFIGIMPIT SYNNAIFLHN EVPGIQLSDD FLEKIEAVKD DKNKCQELAL QESKALIDSA LECFNGIYLI TPFMRYDLTV ELVNYIHQKV EEKKQKIS // ID E8JSS0_STRCR Unreviewed; 314 AA. AC E8JSS0; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFX53775.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EFX53775.1}; GN Name=mmuM {ECO:0000313|EMBL:EFX53775.1}; GN ORFNames=HMPREF9422_0250 {ECO:0000313|EMBL:EFX53775.1}; OS Streptococcus cristatus ATCC 51100. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=889201 {ECO:0000313|EMBL:EFX53775.1, ECO:0000313|Proteomes:UP000002829}; RN [1] {ECO:0000313|EMBL:EFX53775.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 51100 {ECO:0000313|EMBL:EFX53775.1}; 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. {ECO:0000313|EMBL:EFX53775.1}. 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; AEVC01000004; EFX53775.1; -; Genomic_DNA. DR RefSeq; WP_005589761.1; NZ_GL732518.1. DR EnsemblBacteria; EFX53775; EFX53775; HMPREF9422_0250. DR EnsemblBacteria; EGU68092; EGU68092; HMPREF9960_1761. DR PATRIC; 46645150; VBIStrCri174845_1231. DR OrthoDB; EOG6C019S; -. DR Proteomes; UP000002829; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002829}; KW Methyltransferase {ECO:0000313|EMBL:EFX53775.1}; KW Transferase {ECO:0000313|EMBL:EFX53775.1}. SQ SEQUENCE 314 AA; 34765 MW; 323C3C35DF1CF70A CRC64; MGAFKDLLEK QEIIILDGAL GTELERQGYD VSGRLWSAKY LLENPQIIQG LHEDYVRASS DIITTSSYQA SIPAFVEEGL SLDKAYELFK ETVFLAQAAV KNVWQGLSLD EQQRSYPLIA GSVGPYAAYL ADGSEYTGAY HLSEEEFKDF HRPRIQALLD AGCDLLALET IPNGAETEAL VHLLSEEFPQ VEAYLSFTAQ TVSAISDGTL IEEVGRLAQS SPQVLAVGFN CTAPHLIAPL LEKLKQVCDK PLLAYPNSGE IYNGVTNTWQ DNPEQQLCLT DYSHLWKKQG VQLFGGCCRT RPEDIRRLAG ELRT // ID E8KIN1_9PAST Unreviewed; 301 AA. AC E8KIN1; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 12. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFX91239.1}; GN ORFNames=HMPREF0027_1698 {ECO:0000313|EMBL:EFX91239.1}; OS Actinobacillus ureae ATCC 25976. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=887324 {ECO:0000313|EMBL:EFX91239.1}; RN [1] {ECO:0000313|EMBL:EFX91239.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 25976 {ECO:0000313|EMBL:EFX91239.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFX91239.1}. 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; AEVG01000116; EFX91239.1; -; Genomic_DNA. DR RefSeq; WP_005623806.1; NZ_GL831080.1. DR EnsemblBacteria; EFX91239; EFX91239; HMPREF0027_1698. DR PATRIC; 46663301; VBIActUre170509_0300. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFX91239.1}; KW Transferase {ECO:0000313|EMBL:EFX91239.1}. SQ SEQUENCE 301 AA; 32683 MW; 13CEEBFBF5A8B97E CRC64; MLSPITILDG GMSRELMRLN APFKQPEWSA LSLYEKPSAV QQVHEDFIAN GAEVITTNSY AVVPFHIGEQ RFSADGKMLA DLAGRLAKQA VKNSGKSAKI AGSLPPMFGS YRADLIQADR FAEIAQPIID GLSPYVDIWL CETQSAIIEP TSIKPLLPKD DRPLWVSFTL TDDEPTPEPQ LRSGEPVALA IEKMVGLGVD AILFNCCQPE VIEQALAITQ SILKEKNATH IQTGAYANAF APQPKDATAN DGLDEVRKDL GLKPILRGRK NGQHKAQRLS VAVAVSGSNI STHWLKSTTS K // ID E8KPQ1_STRSA Unreviewed; 315 AA. AC E8KPQ1; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFX93854.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EFX93854.1}; GN Name=mmuM {ECO:0000313|EMBL:EFX93854.1}; GN ORFNames=HMPREF9398_1344 {ECO:0000313|EMBL:EFX93854.1}; OS Streptococcus sanguinis VMC66. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=888825 {ECO:0000313|EMBL:EFX93854.1}; RN [1] {ECO:0000313|EMBL:EFX93854.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=VMC66 {ECO:0000313|EMBL:EFX93854.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFX93854.1}. 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; AEVH01000012; EFX93854.1; -; Genomic_DNA. DR RefSeq; WP_002895577.1; NZ_GL831107.1. DR EnsemblBacteria; EFX93854; EFX93854; HMPREF9398_1344. DR PATRIC; 46667609; VBIStrSan169475_0588. DR OrthoDB; EOG6C019S; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFX93854.1}; KW Transferase {ECO:0000313|EMBL:EFX93854.1}. SQ SEQUENCE 315 AA; 34637 MW; B712A553CE264852 CRC64; MGKFKDLLEK QEIIILDGAL GTELESLSYD VSGKLWSAQY LLDQPRIIQD VHESYVRAGS DIITTSSYQA SIPAFIEAGL TPEKGYDLLK ETVFLAQKAI ENVWTGLSPE EQKQRPCPLV AGSVGPYAAY LADGSEYTGN YQLSEEEYRD FHRPRIQALL EAGSDLLAIE TIPNGVEAAA ILRLLAEEFP QAEAYLSFVA QSENAISDGT KIEELGNLAQ ESPQVLAVGF NCTAPHLIAS LLGELGQVCN KPFLTYPNSG ETYNGLTKTW HDDPEQERSL LENSKLWQNQ GVRLFGGCCR TRPEDIAQLA KGFKG // ID E8KW61_STRVE Unreviewed; 322 AA. AC E8KW61; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 01-OCT-2014, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFX95758.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EFX95758.1}; GN Name=mmuM {ECO:0000313|EMBL:EFX95758.1}; GN ORFNames=HMPREF9425_1343 {ECO:0000313|EMBL:EFX95758.1}; OS Streptococcus vestibularis ATCC 49124. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=889206 {ECO:0000313|EMBL:EFX95758.1}; RN [1] {ECO:0000313|EMBL:EFX95758.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 49124 {ECO:0000313|EMBL:EFX95758.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFX95758.1}. 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; AEVI01000063; EFX95758.1; -; Genomic_DNA. DR EnsemblBacteria; EFX95758; EFX95758; HMPREF9425_1343. DR PATRIC; 46672155; VBIStrVes170898_1175. DR OrthoDB; EOG6C019S; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFX95758.1}; KW Transferase {ECO:0000313|EMBL:EFX95758.1}. SQ SEQUENCE 322 AA; 35562 MW; 9553EE2A196468DA CRC64; MVRRPFMATF KDYLENNSPL ILHGALGTEM EALGYDISGK LWSAKYLLEK PEIIQEIHET YIAAGADLIT TSSYQATLPG LVEAGLTEKA AEQIIALTVR LAKAARDKVW VVLDETEKAK RPYPLISGDV GPYAAYLANG SEYSGDYGQI TIEELKDFHR PRIQILLDQG VDLLALETIP NRLEAQALIE LLAEEFPEAE AYISFTVQEP GTISDGTSLD EIAKLVSQSN QILAVGINCS SPLLYNQALA ILKNAGKVLI TYPNSGEVYD GNSQTWKTKD KDALTLVEHS KDWHAHFGVK ILGGCCRTRP NDIKALYQEF RT // ID E8LFR4_9FIRM Unreviewed; 785 AA. AC E8LFR4; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EFY04329.1}; GN ORFNames=HMPREF9443_01706 {ECO:0000313|EMBL:EFY04329.1}; OS Phascolarctobacterium succinatutens YIT 12067. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; OC Acidaminococcaceae; Phascolarctobacterium. OX NCBI_TaxID=626939 {ECO:0000313|EMBL:EFY04329.1}; RN [1] {ECO:0000313|EMBL:EFY04329.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=YIT 12067 {ECO:0000313|EMBL:EFY04329.1}; 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 (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. {ECO:0000313|EMBL:EFY04329.1}. 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; AEVN01000086; EFY04329.1; -; Genomic_DNA. DR RefSeq; WP_009146054.1; NZ_GL830919.1. DR EnsemblBacteria; EFY04329; EFY04329; HMPREF9443_01706. DR PATRIC; 46686414; VBIPhaSp142870_1540. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFY04329.1}; KW Transferase {ECO:0000313|EMBL:EFY04329.1}. SQ SEQUENCE 785 AA; 82748 MW; 786035DD8D9DCE9D CRC64; MNFKELLGKQ MLFFDGATGT QLQARGLQPG ELPESWNFTH PDIVEAVHRS YLDVGSNIVK SNTFGANPLK LAGSGLDCKE TIEAAVAIAK KACGGRENKF VALNLGPTGK LLAPYGDLPF EKAVEAYGEM VRYGAAAGAD LILIETMSDT YEIKAAVLAS KENCDLPICV TMTFDEDGKL LTGATVEAAA LMCEGLGVDA IGFNCGLGPV QVGKLFPQML EATSLPLIIN PNAGLPVQRD GKTCFDVGPE EYAELMYELA GKGASIVGGC CGTTPEHIAQ MIAKCKTLQP GGTRDCRLTA VSSYGKAVHL GEGPVIIGER INPTGKKRLK EALVNGDLDY VCRLGLEQIG VGAQILDVNV GTPGIDEAAM AAKAVPALQA ITDTPLQIDT SNYEAMERAL RLYNGKPMLN SVNGKEDSLQ HVLPLAKKYG AVLVALCLDD SGIPATAAGR IAVAEKIIAR AAEYGIESRN IVVDPLALTI STGAENAAIA CEVIRTMKAR GINTVMGVSN ISFGLPGRDA VNSTFFSMAM AAGLSCGIIN PQSKPMMDAY YGYRALAGYD EGCKEYVQHY ADAPKAAATT VSEMGLYDAI VKGLQGPARQ AAAKALESEK PLDIINKYMI PALDFVGHGF EKKTLFLPQL LMSADAAKAA FEVIREAVGV GETQGETVII ATVHGDIHDI GKNIVKVLLE NYGYRVLDLG KDVPVEAVVE AAKKTDAKVV GLSALMTTTV GAMEETIAAL HNECDCQVVV GGAVLTQEYA DTIGAEHYAP NAVSAVNYVN EILGK // ID E8LQE3_9VIBR Unreviewed; 1226 AA. AC E8LQE3; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EGA67101.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGA67101.1}; GN Name=metH {ECO:0000313|EMBL:EGA67101.1}; GN ORFNames=VIBR0546_01124 {ECO:0000313|EMBL:EGA67101.1}; OS Vibrio brasiliensis LMG 20546. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=945543 {ECO:0000313|EMBL:EGA67101.1}; RN [1] {ECO:0000313|EMBL:EGA67101.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 20546 {ECO:0000313|EMBL:EGA67101.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGA67101.1}. 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; AEVS01000016; EGA67101.1; -; Genomic_DNA. DR RefSeq; WP_006878046.1; NZ_AEVS01000016.1. DR EnsemblBacteria; EGA67101; EGA67101; VIBR0546_01124. DR PATRIC; 46704907; VBIVibBra176315_0709. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGA67101.1}; KW Transferase {ECO:0000313|EMBL:EGA67101.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1226 AA; 136320 MW; 8AE77F587B284399 CRC64; MGSNVRQQIE AQLKQRILLI DGGMGTMIQD YKLEEHDYRG ERFADWHCDL KGNNDLLVLS QPKLIKDIHA AYLEAGADIL ETNTFNATTI AMADYDMESL SEEINFAAAK LAREVADEWT AKTPDKPRYV AGVLGPTNRT CSISPDVNDP GYRNVSFDEL VEAYSESTRA LIKGGSDLIL IETIFDTLNA KACAFAVDSV FEEVGVELPI MISGTITDAS GRTLSGQTTE AFYNSLRHVN PISFGLNCAL GPDELRPYVE ELSRISESFV STHPNAGLPN AFGEYDLSPE DMAVHVKEWA ESGFLNLIGG CCGTTPEHIR HMANAVEGVK PRSLPELTVA CRLSGLEPLT IEKETLFVNV GERTNVTGSA RFKRLIKEEL YDEALEVARQ QVENGAQIID INMDEGMLDA EACMVRFLNL CASEPEISKV PIMVDSSKWE VIEAGLKCIQ GKGIVNSISL KEGKEKFVEQ AKLIRRYGAA VIVMAFDEVG QAETRERKLE ICTNAYNILV DEVGFPPEDI IFDPNIFAVA TGIEEHNNYA VDFIEAVADI KRDLPYAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK NGMDMGIVNA GQLEIYDNVP DKLREAVEDV VLNRRDDGTE RLLDIAAEYA GKGVGKEEDA SALEWRTWSV EKRLEHALVK GITEFIVEDT EEARVNASKP LEVIEGPLMD GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AHLEPFINKE KQAGSSNGKI LLATVKGDVH DIGKNIVGVV LQCNNYEIID LGVMVPCEQI LKVAKEENVD IIGLSGLITP SLDEMVHVAK EMERLDFDLP LLIGGATTSK AHTAVKIEQN YKNPVVYVNN ASRAVGVCTS LLSEELRPAF VEKLDADYVR VRDQHNRKKP RTKPVTLEQA RANKVAIDWD NYTPPVPAKP GVHVFDDFDI ATLRQYIDWT PFFMTWSLVG KYPAIFDHEE VGEEAQRLFK DANELLDRVE KEGLMQARGM CALFPAASIG DDIEVYTDES RTEVAKVLHN LRQQTEKPKG FNYCLSDYIA PKASGKKDWI GAFAVTGGIN ERELADEYKA QGDDYNAIMI QAVADRLAEA FAEYLHERVR KEIWGYAADE NLSNEELIRE KYQGIRPAPG YPACPEHTEK GPLWDLMNVE ETIGMTLTSS YAMYPGASVS GWYFSHPDSR YFAIAQIQQD QVESYADRKG WDMLEAEKWL GPNING // ID E8LVS8_9VIBR Unreviewed; 300 AA. AC E8LVS8; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EGA65184.1}; GN ORFNames=VIBR0546_09994 {ECO:0000313|EMBL:EGA65184.1}; OS Vibrio brasiliensis LMG 20546. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=945543 {ECO:0000313|EMBL:EGA65184.1}; RN [1] {ECO:0000313|EMBL:EGA65184.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 20546 {ECO:0000313|EMBL:EGA65184.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGA65184.1}. 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; AEVS01000073; EGA65184.1; -; Genomic_DNA. DR RefSeq; WP_006879951.1; NZ_AEVS01000073.1. DR EnsemblBacteria; EGA65184; EGA65184; VIBR0546_09994. DR PATRIC; 46708792; VBIVibBra176315_2574. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EGA65184.1}; KW Transferase {ECO:0000313|EMBL:EGA65184.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 204 204 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 279 279 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 280 280 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 300 AA; 33010 MW; 49C9B2E59E5F27C8 CRC64; MKQLTILDGG MGRELRRLGA PFSQPLWSAQ ALIESPQHVQ LAHQHFIDAG AEVIIANSYA CVPFHLGEDL YQSDGAKLAS QAAQIAKRVA SQADHPVLVA GAIPPAFGSY RPDLFQPQRA KEIFTTLFEA QDSEVDIWIA ETISSLEEFH AIQLVLSRTS KPCYYAFSLQ DTLTDSAVLR SGQSVSDAAL QVCQSEGQGI FFNCSIPEVM SQAICDVKQV MDKMGTEIEI GVYANNFAPI GNQHQANESM QTMRELSPQD YLNYCQQWYR LGATTIGGCC GIGPEHIQAL SDWKKRFSTT // ID E8M6A3_9VIBR Unreviewed; 299 AA. AC E8M6A3; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EGA70553.1}; GN ORFNames=VISI1226_00770 {ECO:0000313|EMBL:EGA70553.1}; OS Vibrio sinaloensis DSM 21326. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=945550 {ECO:0000313|EMBL:EGA70553.1}; RN [1] {ECO:0000313|EMBL:EGA70553.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 21326 {ECO:0000313|EMBL:EGA70553.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGA70553.1}. 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; AEVT01000058; EGA70553.1; -; Genomic_DNA. DR RefSeq; WP_008076550.1; NZ_AEVT01000058.1. DR EnsemblBacteria; EGA70553; EGA70553; VISI1226_00770. DR PATRIC; 46716199; VBIVibSin177761_1908. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EGA70553.1}; KW Transferase {ECO:0000313|EMBL:EGA70553.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 204 204 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 279 279 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 280 280 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 299 AA; 32708 MW; 3780EAC548545E6E CRC64; MKKLTILDGG MGRELKRVGA PFSQPLWSAQ ALIESPQHVA DVHQSFIDAG AEIIITNAYA CVPFHLGEQL YQSQGHQLAE TAVQIARTTA ELGSTPTLVA GCIPPAMGSY RPDLFDVEQA TPILQTLIAA QEPYIDVWMV ETLASIEEFE VNHRLLSHSQ KPAYYAFTLD DEPEGNALLR SGETVTQTAK RVATLGASGM LFNCSIPEVL EQAIVDAKKV FDDRNIDIEL GAYANNFEVI DTSHQANDEL QAMRSLTTDE YLQFAKRWYD AGATIIGGCC GIGPEYIKTL AEWKAALAD // ID E8M9N1_9VIBR Unreviewed; 1226 AA. AC E8M9N1; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EGA69260.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGA69260.1}; GN Name=metH {ECO:0000313|EMBL:EGA69260.1}; GN ORFNames=VISI1226_21841 {ECO:0000313|EMBL:EGA69260.1}; OS Vibrio sinaloensis DSM 21326. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=945550 {ECO:0000313|EMBL:EGA69260.1}; RN [1] {ECO:0000313|EMBL:EGA69260.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 21326 {ECO:0000313|EMBL:EGA69260.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGA69260.1}. 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; AEVT01000086; EGA69260.1; -; Genomic_DNA. DR RefSeq; WP_008078718.1; NZ_AEVT01000086.1. DR EnsemblBacteria; EGA69260; EGA69260; VISI1226_21841. DR PATRIC; 46718612; VBIVibSin177761_3076. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGA69260.1}; KW Transferase {ECO:0000313|EMBL:EGA69260.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1226 AA; 136464 MW; 9B1F360C04E15712 CRC64; MGSNVRQQIE AQLKQRILLI DGGMGTMIQG YKLEEEDYRG ERFSDWHCDL KGNNDLLVLT QPKLIKDIHL EYLEAGADIL ETNTFNATTI AMADYDMESL SEEINFAAAK LAREAADEWT LKTPDRPRYV AGVLGPTNRT CSISPDVNDP GYRNVSFDEL VTAYSESTRA LIKGGSDLIL IETIFDTLNA KACAFAVDSV FEELGVALPV MISGTITDAS GRTLSGQTTE AFYNSLRHVR PISFGLNCAL GPDELRPYVE ELSRISETFV STHPNAGLPN AFGEYDLSPE DMAIHVKEWA ESGFLNLIGG CCGTTPEHIR EMANAVEGVS PRQLPELVTA CRLSGLEPLT IEKDTLFVNV GERTNVTGSA RFKRLIKEEL YDEALEVARQ QVENGAQIID INMDEGMLDA EACMVRFLNL CASEPEISKV PIMVDSSKWE VIEAGLKCIQ GKGIVNSISL KEGKEKFVEQ AKLIRRYGAA VIVMAFDEVG QAETRERKLE ICTNAYRILV DEVGFPPEDI IFDPNIFAVA TGIEEHNNYA VDFIEAVADI KRDLPYAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK NGMDMGIVNA GQLEIYDNVP EKLREAVEDV VLNRREDGTE RLLDIAAEYA GKGVGKEEDA SALEWRTWSV EKRLEHALVK GITEFIVEDT EEARINASKP LEVIEGPLMD GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AHLEPFINAS KQAGASNGKI LLATVKGDVH DIGKNIVGVV LQCNNYEIID LGVMVPCEQI LKVAKEENVD IIGLSGLITP SLDEMVHVAK EMERLDFDLP LLIGGATTSK AHTAVKIEQN YKHPVVYVNN ASRAVGVCTS LLSDELRPAF VEKLDADYVR VRDQHNRKKP RTKPVTLEKA RANKVAIDWD NYTPPVPTKP GVHVFDDFDI STLREYIDWT PFFMTWSLVG KYPAIFEHEE VGEEAQRLFK DANELLDRVE KEGLMQARGM CALFPAASVG DDIEVYTDES RTQVAKVLHN LRQQTEKPKG FNYCLSDYVA PKESGKKDWI GAFAVTGGIN ERELADEYKA QGDDYNAIMI QAVADRLAEA FAEYLHEHVR KEIWGYAADE NLSNEELIRE KYQGIRPAPG YPACPEHTEK GPLWELMKVE ETIGMTLTSS YAMFPGASVS GWYFSHPESR YFAIAQIQQD QVESYADRKG WDMLEAEKWL GPNING // ID E8N1V9_ANATU Unreviewed; 296 AA. AC E8N1V9; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:BAJ62714.1}; GN OrderedLocusNames=ANT_06800 {ECO:0000313|EMBL:BAJ62714.1}; OS Anaerolinea thermophila (strain DSM 14523 / JCM 11388 / NBRC 100420 / OS UNI-1). OC Bacteria; Chloroflexi; Anaerolineae; Anaerolineales; Anaerolineaceae; OC Anaerolinea. OX NCBI_TaxID=926569 {ECO:0000313|EMBL:BAJ62714.1, ECO:0000313|Proteomes:UP000008922}; RN [1] {ECO:0000313|EMBL:BAJ62714.1, ECO:0000313|Proteomes:UP000008922} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14523 / JCM 11388 / NBRC 100420 / UNI-1 RC {ECO:0000313|Proteomes:UP000008922}; RA Narita-Yamada S., Kishi E., Watanabe Y., Takasaki K., Ankai A., RA Oguchi A., Fukui S., Takahashi M., Yashiro I., Hosoyama A., RA Sekiguchi Y., Hanada S., Fujita N.; RT "Whole genome sequence of Anaerolinea thermophila UNI-1."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012029; BAJ62714.1; -; Genomic_DNA. DR RefSeq; WP_013559108.1; NC_014960.1. DR RefSeq; YP_004173314.1; NC_014960.1. DR EnsemblBacteria; BAJ62714; BAJ62714; ANT_06800. DR KEGG; atm:ANT_06800; -. DR PATRIC; 46853062; VBIAnaThe181647_0711. DR HOGENOM; HOG000265278; -. DR BioCyc; ATHE926569:GH0F-694-MONOMER; -. DR Proteomes; UP000008922; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008922}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:BAJ62714.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008922}; KW Transferase {ECO:0000313|EMBL:BAJ62714.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 211 211 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 277 277 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 278 278 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 296 AA; 31357 MW; 1BB153F92D3160B2 CRC64; MNSSSFFALQ EGHGVVLLDG AMGTSLQQRG LPLGVPSDSW VLERPEEVLR VHEEFLAAGA QIILTNTFGS SRLRLRQAGM EEHFEIINRQ AVALARRASH GCSGVWVAAS LGPLGEWLEP LGALSPGQAR AFYREQAQIL IEAGIDALVI ETQMDLQEAL TAIEACFSAG NVPVVCSFSF NAQGRLIRGE RPAQVAQVLE QSGVFALGVN CGSSLEGNLQ ALAEMREVTS LPLWFKPNAG LPTVDEAGRV AYPIAPEQMG KGAVRAVEKG AKFVGGCCGA TPAHIRTIAK ALGKLG // ID E8N465_ANATU Unreviewed; 628 AA. AC E8N465; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 01-APR-2015, entry version 27. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=ANT_11950 {ECO:0000313|EMBL:BAJ63229.1}; OS Anaerolinea thermophila (strain DSM 14523 / JCM 11388 / NBRC 100420 / OS UNI-1). OC Bacteria; Chloroflexi; Anaerolineae; Anaerolineales; Anaerolineaceae; OC Anaerolinea. OX NCBI_TaxID=926569 {ECO:0000313|EMBL:BAJ63229.1, ECO:0000313|Proteomes:UP000008922}; RN [1] {ECO:0000313|EMBL:BAJ63229.1, ECO:0000313|Proteomes:UP000008922} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14523 / JCM 11388 / NBRC 100420 / UNI-1 RC {ECO:0000313|Proteomes:UP000008922}; RA Narita-Yamada S., Kishi E., Watanabe Y., Takasaki K., Ankai A., RA Oguchi A., Fukui S., Takahashi M., Yashiro I., Hosoyama A., RA Sekiguchi Y., Hanada S., Fujita N.; RT "Whole genome sequence of Anaerolinea thermophila UNI-1."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012029; BAJ63229.1; -; Genomic_DNA. DR RefSeq; WP_013559617.1; NC_014960.1. DR RefSeq; YP_004173829.1; NC_014960.1. DR EnsemblBacteria; BAJ63229; BAJ63229; ANT_11950. DR KEGG; atm:ANT_11950; -. DR PATRIC; 46854145; VBIAnaThe181647_1243. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR BioCyc; ATHE926569:GH0F-1217-MONOMER; -. DR Proteomes; UP000008922; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008922}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000008922}. SQ SEQUENCE 628 AA; 68092 MW; 1739AD82CFE5248F CRC64; MGGCMKFKEL LKEKRPLLSD GAMGTLLHQR GVDFSECFDA LNLTNPALVA DIHRAYIDAG SQIIQTNTFG ANRYKLAKHG LENQVAEINR AGVDLAQRVV LASFKDILIA GDVGPLGVRL APFGRVQLDQ AYDAFLEQIQ ALSDAGIDLL IIETMTDLYE VIEAIRAARA VDPDLPVVAS MTFTRDDRTM LGDSPEKVAR RIHEAGADVI GINCSGGPNQ ILRILKQMRQ AVPDAVYSVM PNAGWPEQVG GRIMYPAAPE YFGEYAQAFC EAGATLMGGC CGTTPKHIEA MAQALHTNPR PCLSDQILVI SNNHQEVTEQ PEHPTQLAQK LAQGQFVVAV EMDPPRGFST HKLLAGASLL AEAGADVIDV ADSPMARMRM SPWAVCDLIQ DKIGIETVLH FPTRGRNLLR VQGDLLAAHA LGIRNVFVVM GDPTAIGDYP TAMDNYDLVP SGLIQLIKQG FNAGVDHSGA DIGQPTSFFV GCALNLNPAD PDNEIKNLKR KLRAGADFIL TQPIYEIEPA KAFLEQIEVA LGGPLPIPLM VGILPLASSR HANFLHQEVP GITIPEEIRV RMEQAGENGA REGIRIAIEL AEQIHTIAQG IYIMPAFNRF DYAAEIIEAV KSKEPASR // ID E8N466_ANATU Unreviewed; 1172 AA. AC E8N466; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 29-APR-2015, entry version 29. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:BAJ63230.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:BAJ63230.1}; GN Name=metH {ECO:0000313|EMBL:BAJ63230.1}; GN OrderedLocusNames=ANT_11960 {ECO:0000313|EMBL:BAJ63230.1}; OS Anaerolinea thermophila (strain DSM 14523 / JCM 11388 / NBRC 100420 / OS UNI-1). OC Bacteria; Chloroflexi; Anaerolineae; Anaerolineales; Anaerolineaceae; OC Anaerolinea. OX NCBI_TaxID=926569 {ECO:0000313|EMBL:BAJ63230.1, ECO:0000313|Proteomes:UP000008922}; RN [1] {ECO:0000313|EMBL:BAJ63230.1, ECO:0000313|Proteomes:UP000008922} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14523 / JCM 11388 / NBRC 100420 / UNI-1 RC {ECO:0000313|Proteomes:UP000008922}; RA Narita-Yamada S., Kishi E., Watanabe Y., Takasaki K., Ankai A., RA Oguchi A., Fukui S., Takahashi M., Yashiro I., Hosoyama A., RA Sekiguchi Y., Hanada S., Fujita N.; RT "Whole genome sequence of Anaerolinea thermophila UNI-1."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP012029; BAJ63230.1; -; Genomic_DNA. DR RefSeq; WP_013559618.1; NC_014960.1. DR RefSeq; YP_004173830.1; NC_014960.1. DR EnsemblBacteria; BAJ63230; BAJ63230; ANT_11960. DR KEGG; atm:ANT_11960; -. DR PATRIC; 46854147; VBIAnaThe181647_1244. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR BioCyc; ATHE926569:GH0F-1218-MONOMER; -. DR Proteomes; UP000008922; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008922}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAJ63230.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008922}; KW Transferase {ECO:0000313|EMBL:BAJ63230.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 236 236 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 302 302 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 749 749 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1172 AA; 129525 MW; 7B3CF64FC4279B92 CRC64; MKRIYTNRRY LDLIQKRVAI FDGAMGTSLQ KQNLTAEHFG GERYVGCNDY LVLTYPQAVE TVHRSFLEAG VDVLETDTFR SNRITLAEYG LQNRVLDINR AAANLARRLA DEYTRKTGQM RLVAGSIGPS GKLPSMNDPE LSNITFDELA DVFREQARGL MEGGVDLLLI ETSQDILEVK AAITGIQQAF TETGIVIPLQ AQVTLDTTGR MLLGTDIAAV LAILEGMPID AIGLNCSTGP DYMREPIRYL AEHAPVPVSC IPNAGLPLNV DGQAVYPLEP EPFATALSEY VDRFGVGIVG GCCGTTPEHL RKLVEKIDAH PASHRPIFSL PKLASATQAV LMVQEPAPFL IGERLNTQGS ARFKKMILAE DFEGALEIAR QQVEAGAHGL DLCTALTERS DEGELMRRLI KTLAPTVRVP FVIDTTEPDV MEIALKTAPG RCLLNSVNLE AGAAKATRIL QLAKMYNAAV IALTIDEQGM AKTAQRKLEI ARRIYHLAVD EMGLRPQDLV FDALTFTLAT GDPEFSRSAM ETMDGIRLIK AELPGVLTSL GVSNVSFGLK PAARGVLNSV MLYHCVQAGL DMAIVNPAQI TPYPDIPAEE RELAEDLIFN RRPDALQRLI EYFESHGKEE QKTTAQHSAL EGKTAEERLH WRIVHRQKEG VEADIDEILQ RPSQQSRHET AVRVLNEVLL PAMKEVGDRF GAGELILPFV LQSAEVMKKA VSHLEQYLEK KEGVSKGTLV LATVYGDVHD IGKNLVKTIL SNNGYTVIDL GKQVPAETII TKAVEVKADA IGLSALLVST SKQMPLIVNE LHRRGLKFPV LIGGAAINRN FGRRILQTED GSFYDPGVFY CKDAFEGLST MDALMDAGTR LTLVQQIIRE AEIELGRRPA RERSLSSGIE RSETPAAPRI PQAPFWGAKV VHSMPLELVF QHLSINELFR LSWGAKNTHG EAWKQLEAEF TQRLEQMKRE ALKEGWLKPQ GVYGYFPAQS DGNDLVIYNP QSLDTGKPVE LVRFTFPRQP EGEKLCLADY FAPVESGQMD VVAFQVVTVG ESATEKFERL QEEGNYTEAY YVHGLAVQTA EATAAYLHNH IRRELGLDAE QGKRYSWGYP AIPDLADHQK VFQLLPAESA LKMSLSPAYQ LIPEQSTAAI IVHHPQAKYF NVGESRIEQL MR // ID E8NFC4_MICTS Unreviewed; 285 AA. AC E8NFC4; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Homocysteine/selenocysteine methylase {ECO:0000313|EMBL:BAJ75197.1}; GN OrderedLocusNames=MTES_2233 {ECO:0000313|EMBL:BAJ75197.1}; OS Microbacterium testaceum (strain StLB037). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Microbacteriaceae; Microbacterium. OX NCBI_TaxID=979556 {ECO:0000313|EMBL:BAJ75197.1, ECO:0000313|Proteomes:UP000008975}; RN [1] {ECO:0000313|EMBL:BAJ75197.1, ECO:0000313|Proteomes:UP000008975} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=StLB037 {ECO:0000313|EMBL:BAJ75197.1, RC ECO:0000313|Proteomes:UP000008975}; 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 ----------------------------------------------------------------------- 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; BAJ75197.1; -; Genomic_DNA. DR RefSeq; WP_013585322.1; NC_015125.1. DR RefSeq; YP_004225077.1; NC_015125.1. DR EnsemblBacteria; BAJ75197; BAJ75197; MTES_2233. DR KEGG; mts:MTES_2233; -. DR PATRIC; 46971539; VBIMicTes185510_2208. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; YGRSVTK; -. DR BioCyc; MTES979556:GJFH-3332-MONOMER; -. DR Proteomes; UP000008975; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008975}; KW Methyltransferase {ECO:0000313|EMBL:BAJ75197.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008975}; KW Transferase {ECO:0000313|EMBL:BAJ75197.1}. SQ SEQUENCE 285 AA; 29118 MW; DD6A60FA51B70C0B CRC64; MIDLASTLPA RAVVLDGGLG TLLEARGNDV SSSLWSARIL RDDPDEVRAA HAAFIDAGAE VVITSSYQVG FGVGIPDADV DTLLRRSVTL AREAGDVAVA ASVGPMGALR ADGSEYTGEY GLTLEQLRDR HRRRLRVLAD AGADLLAIET IPAELEVEAL SLELEGLGIP ALFSLSADST GFASAGSLDR ALRTAASAPG VIAVGVNCCA PETVLPALAG APGIPLVAYP NTGERWDATT RTWRGATAPL ADAAPDWVAA GARLVGGCCR SLPADIAAIA AAVRG // ID E8PJR6_THESS Unreviewed; 1182 AA. AC E8PJR6; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 33. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADW22021.1}; GN Name=metH {ECO:0000313|EMBL:ADW22021.1}; GN OrderedLocusNames=TSC_c14020 {ECO:0000313|EMBL:ADW22021.1}; OS Thermus scotoductus (strain ATCC 700910 / SA-01). OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; OC Thermus. OX NCBI_TaxID=743525 {ECO:0000313|EMBL:ADW22021.1, ECO:0000313|Proteomes:UP000008087}; RN [1] {ECO:0000313|Proteomes:UP000008087} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700910 / SA-01 {ECO:0000313|Proteomes:UP000008087}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001962; ADW22021.1; -; Genomic_DNA. DR RefSeq; WP_015717292.1; NC_014974.1. DR RefSeq; YP_004202570.1; NC_014974.1. DR EnsemblBacteria; ADW22021; ADW22021; TSC_c14020. DR KEGG; tsc:TSC_c14020; -. DR PATRIC; 47045637; VBITheSco147128_1354. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR BioCyc; TSCO743525:GCD4-1399-MONOMER; -. DR Proteomes; UP000008087; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008087}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 256 256 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1182 AA; 131155 MW; 5AD1FF42769BBC68 CRC64; MVEVHTCSPG CRHHLGGAGF GDAPLVRLGY NKEARAEKFP YLKALLQRPL VFDGAMGTEL QKRHLTPEDY GGEAYYGCPE VLNLTRPEVI QEIHRAYLEA GAEVIETNTF GALRHVLAEY GLGEKAEELA YLGARIAKEV AEPYGAFVAG ALGPGTKLIS LGQISWDELF TAYKEAVRGL LRGGVDLILL ETAQDILQVR CAVLAAREAM AEVGREVPLQ VQVTMEATGT MLVGTDEQAA LAALESLPID VVGMNCATGP DLMDAKIRYF AENATRFVSC LPNAGLPRNE GGKVVYDLTP EELAKWHLKF VTEYGVNAVG GCCGTGPEHI RKVAEVVKGK PAPKRKETFP PQVASLYQAV PLRQEASVFL VGERLNATGS KRFREMLFAR DLEGILALAR EQVEEGAHAL DLSVAWTGRD ELQDLAWLLP HLATAVTVPF MVDSTSPSAM EFALKHLPGR VLLNSANLED GLEKFDRVAS LAKAHGAALV VLTIDEKGMA KTQEEKVRVA LRMYERLTEH HGFRPEDLLF DLLTFPITQG DEESRPLARE TLLAMEELRE RLPGVGFILG VSNVSFGLKP RARRVLNSVF LDEARKKGLT AAIVDAGKIL PINQIPEEAY ALALDLIYDR RREGFDPLLA FMGYFETHRE DPALKEDAFQ ALPVLERLKR RVVEGRKGGL EADLDEALRE GHKPLDLING PLLSGMKEVG ELFGAGKMQL PFVLQAAEVM KRAVAHLEPH MERRGEGRGK MVLATVKGDV HDIGKNLVDI ILTNNGYQVI NLGIKVPIEE ILKAVEEHKP HAVGMSGLLV KSTVVMKENL EYMRDRGYTL PVILGGAALT RSYVEELKAI YPNVYYAEDA FEGLRLMEAL TSGEATSVRK EAQKPRVEAP KAVPKAKPVG EAPSVPRPPF FGVRVEENLD LATIAYYVNK LALFRGQWGY SRRGLTREEW QALVEREAEP VFRRLLREAM EEGWLRPKVL YGFFPVAREG EELLVFSPET GEVLERFAFP RQKGGGLSLV DYFRPRFAPP LGDEERWLPA YEAGARDVLG VQLVTMGEEP SRKAKALFEA GAYQDYLFVH GFSVEMTEAL AEYWHKRMRQ MWGIAGKDAT EIRKLFQQGY QGARYSFGYP ACPDLADQAK LDRLMDFSRV GVRLTENFQL DPEHSTSAIV VHHPEARYFN VD // ID E8R0S5_ISOPI Unreviewed; 1247 AA. AC E8R0S5; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 30. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ADV61260.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADV61260.1}; GN OrderedLocusNames=Isop_0668 {ECO:0000313|EMBL:ADV61260.1}; OS Isosphaera pallida (strain ATCC 43644 / DSM 9630 / IS1B). OC Bacteria; Planctomycetes; Planctomycetia; Planctomycetales; OC Planctomycetaceae; Isosphaera. OX NCBI_TaxID=575540 {ECO:0000313|EMBL:ADV61260.1, ECO:0000313|Proteomes:UP000008631}; 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] {ECO:0000313|EMBL:ADV61260.1, ECO:0000313|Proteomes:UP000008631} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43644 / DSM 9630 / IS1B RC {ECO:0000313|Proteomes:UP000008631}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002353; ADV61260.1; -; Genomic_DNA. DR RefSeq; WP_013563549.1; NC_014962.1. DR RefSeq; YP_004177809.1; NC_014962.1. DR EnsemblBacteria; ADV61260; ADV61260; Isop_0668. DR KEGG; ipa:Isop_0668; -. DR PATRIC; 46954743; VBIIsoPal14453_0876. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR BioCyc; IPAL575540:GI5T-676-MONOMER; -. DR Proteomes; UP000008631; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008631}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADV61260.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008631}; KW Transferase {ECO:0000313|EMBL:ADV61260.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 262 262 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 327 327 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 328 328 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 781 781 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1247 AA; 136563 MW; 4693A4C6FA5BBE9E CRC64; MNAILTPSSS RLDLPTTATL DLLQAMAAQR ILLLDGGMGT MIQQVPLGES DFRGRYFASH PKELKGNNDL LVMTRPEVIR SIHEAYLAAG SDIIETNTFN GTAISQAEYG LSHIAYDLNV EAARLARAAA DQWSDKTPDR PRLVAGAIGP TSCTLSISPD VNNPAFRPVS FDQLKEAYAE QARGLIDGGV DLILIETIFD TLNAKAALVA VEEAFELKGI RLPLMLSVTI VDKSGRNLSG QTVDAFWASV AHARPFSVGI NCALGAVEMR PYLAELARVA DVYVSCYPNA GLPNPLSDTG YDELPETTGA HLGEFARSGL VNIVGGCCGT TPDHIAAIAR AVRESPPRTL PKVPGRPERR AALYSGLETL AIRPDSGFLM IGERTNVTGS KKFAKLILAG DYQGALEVAR DQVRGGANIL DVNMDEAMLN GEEAMTTFLN LIATEPEIAR IPIMIDSSKW SIIEAGLKCV QGKPIVNSIS LKEGEEDFLE KARTVLKYGA GVVVMAFDEV GQADTVERKV EICQRAYKLL VEKLNFPPQD IIFDPNILAI ATGIEEHNNY AVNFIEATRI IKATCPGAKI SGGVSNLSFS FRGNDVVREA MHAAFLYHAI RAGMDMGIVN AGQLAIYDEI PADLKEHVED VIFNRRPDAT DRLLAFAETV KGKGKQRIAD DAWRSGTVQE RLQYALIHGI DAYVVADVEE ARAHYDRPLH IIEGPLMDGM RVVGDLFGAG KMFLPQVVKS ARVMKKAVAY LEPFMAAEKV ATGDMSAQGR VVLATVKGDV HDIGKNIVGV VLGCNNYEVI DLGVMVPMER ILQAAEEHQA DMIGLSGLIT PSLDEMVSIA AEMERRGMTI PLLIGGATTS KQHTAVKIAP KYSKATVHVL DASRAVNVVA SLLDKDNREA TIAAIKADQE RLRELHARQT ATVLLTQAQA IANRHAPDWS QADLPVPEFL GTRIIETPIA ELIDFIDWTF FFIAWELKGK FPAILQHPEY GPAARELHQN ALAMLDDLVK SQRLQARGVY GFWPANSDGE DVVLYTDESR TVEAVRFPML RRQTQAHRDT RNYSLADFVA PIESGRKDYV GAFAVTAGLG AEELAREFEA DHDDYRSIMI KALADRLAEA YAEWLHAKVR REWGYGRDEH LTNEQLINEE YRGIRPAFGY PACPDHTPKR DLFRLLGCEQ VGIRLTESCA MMPAASVSGL YFAHEHARYF AVGKVGRDQV EDYARRRGMP VAEVEKWLAP VLAYDPA // ID E8R4X3_ISOPI Unreviewed; 289 AA. AC E8R4X3; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 29-APR-2015, entry version 21. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADV61719.1}; GN OrderedLocusNames=Isop_1131 {ECO:0000313|EMBL:ADV61719.1}; OS Isosphaera pallida (strain ATCC 43644 / DSM 9630 / IS1B). OC Bacteria; Planctomycetes; Planctomycetia; Planctomycetales; OC Planctomycetaceae; Isosphaera. OX NCBI_TaxID=575540 {ECO:0000313|EMBL:ADV61719.1, ECO:0000313|Proteomes:UP000008631}; 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] {ECO:0000313|EMBL:ADV61719.1, ECO:0000313|Proteomes:UP000008631} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43644 / DSM 9630 / IS1B RC {ECO:0000313|Proteomes:UP000008631}; 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 ----------------------------------------------------------------------- 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; ADV61719.1; -; Genomic_DNA. DR RefSeq; WP_013564008.1; NC_014962.1. DR RefSeq; YP_004178268.1; NC_014962.1. DR EnsemblBacteria; ADV61719; ADV61719; Isop_1131. DR KEGG; ipa:Isop_1131; -. DR PATRIC; 46955900; VBIIsoPal14453_1448. DR BioCyc; IPAL575540:GI5T-1145-MONOMER; -. DR Proteomes; UP000008631; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 2. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008631}; KW Methyltransferase {ECO:0000313|EMBL:ADV61719.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008631}; KW Transferase {ECO:0000313|EMBL:ADV61719.1}. SQ SEQUENCE 289 AA; 30950 MW; 12D1C5AE75655376 CRC64; MTEPTRPAPI LFDGPMGTRL LARGLDLRVE EACEWSLDHP EEVEAIHRAD CLAGASLLRA NVFTAHRDGL ERRGQGRGAR LPRLLTQAVD LARRAGEGLP VVAALGPVGS HEEAAVHLVD HGVAAIWLET YTFLHALDQL PRLKRRIGQQ VPIWVTLFNW RDDPEQGPIT AQAARLIEAG AAAIGVNCVS CDDPQRIPLM TALRAAAGTR VPLIASPSIP PPPPDRPAPT PLEVAEQVLD WWRAGADGIG LCCGGNATHL AALHTLCADL PPRDPHSPLL LGDGPRPTT // ID E8RB73_DESPD Unreviewed; 307 AA. AC E8RB73; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADW18738.1}; GN OrderedLocusNames=Despr_2602 {ECO:0000313|EMBL:ADW18738.1}; OS Desulfobulbus propionicus (strain ATCC 33891 / DSM 2032 / 1pr3). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales; OC Desulfobulbaceae; Desulfobulbus. OX NCBI_TaxID=577650 {ECO:0000313|EMBL:ADW18738.1, ECO:0000313|Proteomes:UP000006365}; RN [1] {ECO:0000313|EMBL:ADW18738.1, ECO:0000313|Proteomes:UP000006365} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33891 / DSM 2032 / 1pr3 RC {ECO:0000313|Proteomes:UP000006365}; 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 ----------------------------------------------------------------------- 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; ADW18738.1; -; Genomic_DNA. DR RefSeq; WP_015725264.1; NC_014972.1. DR RefSeq; YP_004196029.1; NC_014972.1. DR EnsemblBacteria; ADW18738; ADW18738; Despr_2602. DR KEGG; dpr:Despr_2602; -. DR PATRIC; 46938946; VBIDesPro114934_2774. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR BioCyc; DPRO577650:GH80-2647-MONOMER; -. DR Proteomes; UP000006365; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006365}; KW Methyltransferase {ECO:0000313|EMBL:ADW18738.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006365}; KW Transferase {ECO:0000313|EMBL:ADW18738.1}. SQ SEQUENCE 307 AA; 32989 MW; 6331223A73F5B327 CRC64; MQPHDHEVLI LDGACGTNLQ EMHIPPSAWK GKEGCNELLN LTAPETITEL HASFVTAGAM VIETNTFGAN RIVLDEYGLQ DQVEAINRAG VDNARAAIGG KAHTYIAGSI GPGTKLPSLG HISVEDMANA YAEQIRALVL AGVDLLIIET CQDLLQIKTA MITCFDTLEA LGRDIPVMAS VTIERTGTML VGTDIAAAAT TFEPYPIFSF GLNCATGPLD MESHIRWLSR NWPGRISCVP NQGLPEVVNG KTCYPLDPKT YAQEMKRFVT EYGVSVVGGC CGTTPNHIRQ LVQTLTGVKP AVRRVNA // ID E8RS01_ASTEC Unreviewed; 354 AA. AC E8RS01; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADU13526.1}; GN OrderedLocusNames=Astex_1863 {ECO:0000313|EMBL:ADU13526.1}; 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 {ECO:0000313|EMBL:ADU13526.1, ECO:0000313|Proteomes:UP000001492}; RN [1] {ECO:0000313|Proteomes:UP000001492} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15261 / DSM 4724 / VKM B-1370 / CB 48 RC {ECO:0000313|Proteomes:UP000001492}; 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; ADU13526.1; -; Genomic_DNA. DR RefSeq; WP_013479356.1; NC_014816.1. DR RefSeq; YP_004087677.1; NC_014816.1. DR EnsemblBacteria; ADU13526; ADU13526; Astex_1863. DR KEGG; aex:Astex_1863; -. DR PATRIC; 45151688; VBIAstExc23432_1832. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR BioCyc; AEXC573065:GJ7A-1887-MONOMER; -. DR Proteomes; UP000001492; Chromosome 1. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001492}; KW Methyltransferase {ECO:0000313|EMBL:ADU13526.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001492}; KW Transferase {ECO:0000313|EMBL:ADU13526.1}. SQ SEQUENCE 354 AA; 38966 MW; 639562194B67882A CRC64; MTRQDRIDTL KAAAKERILI LDGSWGVMIQ RRGLDEQDFR GERFKDHVGQ MKGNNDILCL TRPDIITDLH NQYYAAGADI SETNTFSATT IAMDDYHLDA QACWDINFEG AKLARACADA WTAQQPEKPR FVAGSIGPLN KMLSMSSDVN DPGARSVTFD QVYAAYKHQI RALNEGGVDL YLVETITDTL NCKAALKAIM DLEDEGLDKL PIWISGTITD RSGRTLSGQT AEAFWNSVKH AKPFAIGFNC ALGADLMRPH IAELARVADT LVAAYPNAGL PNAMGQYDEQ PHETAHELHE WAKDGLINIL GGCCGTTPDH IKHVADEVRG IAPRVPPERP RALRLAGLEP FELN // ID E8SHT0_STAPH Unreviewed; 613 AA. AC E8SHT0; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 01-APR-2015, entry version 28. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=SPSINT_0021 {ECO:0000313|EMBL:ADV04550.1}; OS Staphylococcus pseudintermedius (strain HKU10-03). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=937773 {ECO:0000313|EMBL:ADV04550.1, ECO:0000313|Proteomes:UP000007469}; 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] {ECO:0000313|EMBL:ADV04550.1, ECO:0000313|Proteomes:UP000007469} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HKU10-03 {ECO:0000313|EMBL:ADV04550.1, RC ECO:0000313|Proteomes:UP000007469}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ADV04550.1; -; Genomic_DNA. DR RefSeq; WP_015728511.1; NC_014925.1. DR RefSeq; YP_004148186.1; NC_014925.1. DR EnsemblBacteria; ADV04550; ADV04550; SPSINT_0021. DR KEGG; ssd:SPSINT_0021; -. DR PATRIC; 45363184; VBIStaPse177932_0021. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; ITPFERI; -. DR BioCyc; SPSE937773:GH0P-21-MONOMER; -. DR Proteomes; UP000007469; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007469}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862, KW ECO:0000313|EMBL:ADV04550.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007469}. SQ SEQUENCE 613 AA; 67621 MW; 06A273D03723E810 CRC64; MSRLLNALKN NILVADGAMG TILYSEGLDT CPEAYNLTHP DKVESIHRSY IQAGADVIQT NTYGANFEKL QQFGLEHQVK AIHQAAVAIA KRAAGPDTFI LGTVGGFRST KQGELSLSAI QYHTDIQVDT LVAEGVDGLL FETYYDDEEL LNAIKQTRQK YDIPIIAQLT ASNIHYLVNG KEINSALQQL VEAGADIVGL NCHHGPHHMK RTFGHIELPD NAYLSCYPNA SLLDIDQQTF KYSDNAQYFG ETAEQLIQEG VQLIGGCCGT TPEHIRKIKA AVQGLKPIKE KKVIPIHQKP TSEAPKPTRQ NLAMRVRERP TIIVELDTPK HLDTTKFFQN VKALDDAQID AVTLADNSLA TVRVSNIAAA SLIKQQFNIE PLVHITCRDR NLIGLQSHLL GLSLIGVNEI LAITGDPSKV GHLPGATNVY DVNSKGLTEL ALRFNKGVNT DGDTLKVATQ FNIAGGFDPH VSNIKAAVRK METKIKSGMH YFITQPVFTK EKIVEIYEAT KHLDVPIFIG IMPITSYKNA LFLHHEVPGI KMSDDVLAQF EAVANDRQAT YELSLSLCKS LIDTVHTYFN GLYLITPFER IDYSLELAAY SKSITTSHQE AIL // ID E8T5Z7_THEA1 Unreviewed; 841 AA. AC E8T5Z7; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 30. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADU96581.1}; GN OrderedLocusNames=Theam_0609 {ECO:0000313|EMBL:ADU96581.1}; OS Thermovibrio ammonificans (strain DSM 15698 / JCM 12110 / HB-1). OC Bacteria; Aquificae; Desulfurobacteriales; Desulfurobacteriaceae; OC Thermovibrio. OX NCBI_TaxID=648996 {ECO:0000313|EMBL:ADU96581.1, ECO:0000313|Proteomes:UP000006362}; RN [1] {ECO:0000313|EMBL:ADU96581.1, ECO:0000313|Proteomes:UP000006362} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15698 / JCM 12110 / HB-1 RC {ECO:0000313|Proteomes:UP000006362}; 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 ----------------------------------------------------------------------- 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; ADU96581.1; -; Genomic_DNA. DR RefSeq; WP_013537367.1; NC_014926.1. DR RefSeq; YP_004151222.1; NC_014926.1. DR EnsemblBacteria; ADU96581; ADU96581; Theam_0609. DR KEGG; tam:Theam_0609; -. DR PATRIC; 45383540; VBITheAmm13058_0704. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR BioCyc; TAMM648996:GI3X-628-MONOMER; -. DR Proteomes; UP000006362; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006362}; KW Methyltransferase {ECO:0000313|EMBL:ADU96581.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006362}; KW Transferase {ECO:0000313|EMBL:ADU96581.1}. SQ SEQUENCE 841 AA; 89897 MW; E71EF892D5050D39 CRC64; MPTNPFKQEE KIWVLDGGMG TMLMAKGVDV NFAPELLNVE KPEVLKEIHS EYVEAGADII ETNTFGSNRI KLSHYGLENR VKELTAAGVK LAKEAARGRA LVALSVGPTG VFAEPVGDYT FDELVDVFKE QIEAGAEAGA DLVLIETMSD IKEAKAAVFA AREVCDLPVL VSMTYQEDGR TLLGTPPEVA AAVFEGFNVA AVGANCSLGP ESFVEIIKRT ASVTTTPIIV YANAGLPVLE NGKTVYPEPP ETFEKYAVEF VKAGANIIGG CCGTTPDHIR AIKRAVEGLK PVERNPVKGV KVASRTKLVL IGTGHPTRII GERINPTGKK KLQEALKAKD FSLVKQEAKK QVEEGADLLD VNVGVPGADE PSLMREAVKT VMEAVDVPLV IDTKDPKAVE EALKMCDGRP VVNSVSGEKK DVEQILPVAA KYGANVLLLA IDDEGLKEKA QERVEIIERL LKECEKVGVD RSSTVADVLN LAVSAMPDST VETLKAIRLV KERFGIATTL GVSNVSFGLP SRSLINSAFM AMAIYAGLDS GIVNPGDSRM VETIFASDVL VGKDRGAERF VSRFQNYSPK GEDAECRKAL ERICQIAGAV LGTVPQAFSH EAEEKAKGET TEEASDSEAP AGILGTIFKK VLEGDREGIV GPTEEALKEF DPVEVSDRAL IPALDVVGKR FEKGEIFLPQ MLRSAQAVQA AFEVLKREMK KKGGNLKLGG KIVMATVHGD VHEIGKNIVI TMLENSGFDV IDLGTNVPPA EVVRAAKEHN ADIVGLSALM TTTLPAMEET IKALRDAGVE VPVIVGGAVV TPEYAESIGG IYGGDAQEAV KIVKKLLKVE E // ID E8TI70_MESCW Unreviewed; 301 AA. AC E8TI70; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 01-APR-2015, entry version 22. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADV12454.1}; GN OrderedLocusNames=Mesci_3331 {ECO:0000313|EMBL:ADV12454.1}; OS Mesorhizobium ciceri bv. biserrulae (strain HAMBI 2942 / LMG 23838 / OS WSM1271). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=765698 {ECO:0000313|EMBL:ADV12454.1, ECO:0000313|Proteomes:UP000007471}; RN [1] {ECO:0000313|Proteomes:UP000007471} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HAMBI 2942 / LMG 23838 / WSM1271 RC {ECO:0000313|Proteomes:UP000007471}; 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; ADV12454.1; -; Genomic_DNA. DR RefSeq; WP_013531135.1; NC_014923.1. DR RefSeq; YP_004142504.1; NC_014923.1. DR EnsemblBacteria; ADV12454; ADV12454; Mesci_3331. DR GeneID; 10118808; -. DR KEGG; mci:Mesci_3331; -. DR PATRIC; 45256759; VBIMesCic160642_3828. DR HOGENOM; HOG000265278; -. DR OMA; PYVDVWL; -. DR BioCyc; MCIC765698:GHQ5-3369-MONOMER; -. DR Proteomes; UP000007471; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007471}; KW Methyltransferase {ECO:0000313|EMBL:ADV12454.1}; KW Transferase {ECO:0000313|EMBL:ADV12454.1}. SQ SEQUENCE 301 AA; 31759 MW; 4345065FFF1AAA15 CRC64; MKKIILTDGG MGQELVRRSQ SEPTPLWSAR VLIDEPDLVR DLHAEFIRAG ARVITINTYS ATPERLAREG AEDLFKPLQK RGIELARQAR DEAGDAAIAG CLSPLFGSYA PALTISFEET LEIYRRIVAE QADGVDLFLC ETMASADEAR AAVTAASESG KPVWVSWTLA DHGKPRLRSG EAIATAASAL DGLAVAARLV NCCRPEAIAA ALPELIGLGG PVGAYANGFT STEALKHGGT VDVLHARHDL GPDAYADQAI GWVEAGASIV GGCCEVGPPH IAALRDRLEQ AGYEISGVLH A // ID E8TIC6_MESCW Unreviewed; 345 AA. AC E8TIC6; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 07-JAN-2015, entry version 26. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADV12510.1}; GN OrderedLocusNames=Mesci_3387 {ECO:0000313|EMBL:ADV12510.1}; OS Mesorhizobium ciceri bv. biserrulae (strain HAMBI 2942 / LMG 23838 / OS WSM1271). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=765698 {ECO:0000313|EMBL:ADV12510.1, ECO:0000313|Proteomes:UP000007471}; RN [1] {ECO:0000313|Proteomes:UP000007471} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HAMBI 2942 / LMG 23838 / WSM1271 RC {ECO:0000313|Proteomes:UP000007471}; 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; ADV12510.1; -; Genomic_DNA. DR RefSeq; WP_013531191.1; NC_014923.1. DR RefSeq; YP_004142560.1; NC_014923.1. DR EnsemblBacteria; ADV12510; ADV12510; Mesci_3387. DR GeneID; 10118864; -. DR KEGG; mci:Mesci_3387; -. DR PATRIC; 45256873; VBIMesCic160642_3884. DR HOGENOM; HOG000265278; -. DR KO; K00548; -. DR OMA; GTNLFAM; -. DR BioCyc; MCIC765698:GHQ5-3425-MONOMER; -. DR Proteomes; UP000007471; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007471}; KW Methyltransferase {ECO:0000313|EMBL:ADV12510.1}; KW Transferase {ECO:0000313|EMBL:ADV12510.1}. SQ SEQUENCE 345 AA; 36191 MW; 9081EEB2929BD35E CRC64; MKANPMTTTN PIDALLAEKG VLLADGATGT NLFAMGLEAG EAPELLNETA PDTITSLHQN FVDAGADIIL TNSFGGTRHR LKLHHAQDRV HALNQRAAEI ARAVADRAGR KVIVAGSVGP TGELLVPLGA MTYDEAVDAF AEQIEGLKEG GAEVAWIETM SAPDEIRAAA EAAIRVGLPY TYTGSFDTAG RTMMGLLPRD IHGVTDGLSA APLGVGANCG VGASDILASL LDMTEAKPEA TVIVKGNCGI PEFRGTEIHY SGTPELMADY VRLAVDGGAK IIGGCCGTSF QHLAAMRKAL DAHTKADRPT VAAIVERIGP MRNKVATENT AETSEARRER RRSRA // ID E8TLA7_MESCW Unreviewed; 1269 AA. AC E8TLA7; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 29-APR-2015, entry version 33. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADV11531.1}; GN OrderedLocusNames=Mesci_2384 {ECO:0000313|EMBL:ADV11531.1}; OS Mesorhizobium ciceri bv. biserrulae (strain HAMBI 2942 / LMG 23838 / OS WSM1271). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=765698 {ECO:0000313|EMBL:ADV11531.1, ECO:0000313|Proteomes:UP000007471}; RN [1] {ECO:0000313|Proteomes:UP000007471} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HAMBI 2942 / LMG 23838 / WSM1271 RC {ECO:0000313|Proteomes:UP000007471}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002447; ADV11531.1; -; Genomic_DNA. DR RefSeq; WP_013530215.1; NC_014923.1. DR RefSeq; YP_004141581.1; NC_014923.1. DR EnsemblBacteria; ADV11531; ADV11531; Mesci_2384. DR GeneID; 10117854; -. DR KEGG; mci:Mesci_2384; -. DR PATRIC; 45254790; VBIMesCic160642_2858. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; MCIC765698:GHQ5-2415-MONOMER; -. DR Proteomes; UP000007471; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007471}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 266 266 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 329 329 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 330 330 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 791 791 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1269 AA; 138525 MW; 36A22FAD5D5A2960 CRC64; MSQNSASLDA LFGPVTAKPD GSEVLAALTA AARERILILD GAMGTQIQGL GFNEDQFRGE AFAGCACHQQ GNNDLLILTQ PGAIEEIHYQ YAIAGADILE TNTFSSTSIA QADYGMEDAV YALNRDGARL VRRAAVRAEQ QDGKRRFVAG ALGPTNRTAS MSPDVNNPGY RAVTFDDLRL AYGEQLRGLI DGGADIILIE TIFDTLNAKA AIFAAEEIFI EKGVRLPVMI SGTITDLSGR TLSGQTPTAF WHSVRHASPF TIGLNCALGA NAMRAHLAEI SGVADTFVCA YPNAGLPNEF GRYDESPDFM AAQIEDFARE GLVNVVGGCC GSTPEHIRAI AEAVRKYPPR AIPDIEPRMR LSGLEPFTLT DEIPFVNVGE RTNVTGSAKF RKLITAGDYV AALDVARDQV ANGAQIIDIN MDEGLIDSKK AMVEYLNLIA AEPDIARVPV MVDSSKWEII EAGLKCVQGK PLVNSISMKE GEEAFLHHAR LVRAYGAAVV VMAFDEDGQA DTKARKVEIC TRAYKLLTEQ AGFPPEDIVF DPNVFAIATG IEEHDNYGVD FIEAAGEITA TLPHVHISGG VSNLSFSFRG NEPVREAMHA VFLYHAIQRG MDMGIVNAGQ LAVYDTIEPD LREACEDVVL NRAPKAGGTA TERMLEIAER FKGTAGKEAQ ERDLAWREWT VEQRISHALV NGITEFIDAD TEEARLAAER PLHVIEGPLM AGMNVVGDLF GAGKMFLPQV VKSARVMKQA VAGLLPHMEA EKLANAANGI DNGERKTAGK ILMATVKGDV HDIGKNIVGV VLACNNYEII DLGVMVPAAR ILQTAREQNV DIIGLSGLIT PSLDEMAHMA AEMEREGFDI PLLIGGATTS RVHTAVKIHP RYSKGQTVYV TDASRAVGVV SSLLSNESKD GFVDTVRAEY KKVADAHARS EADKQRLPLA KARANAHRID WSEYEPPKPS FAGVKVFENW DLTELARYID WTPFFQTWEL KGRYPKILED EAQGAAARQL FEDAQAMLNK IIAEKWFAPR GVIGFWPANA VGDDIRLFTD EKRSQELATF FTLRQQLTKR DGKANVALAD FVAPAECGKP DYIGGFIVTA GIEEVAIAER FERANDDYSS IMVKALADRF AEAFAERMHE KVRKEFWGYA SDEALAPDEL IGEPYRGIRP APGYPAQPDH TEKATLFRLL DGEGNAGVRL TESYAMWPGS SVSGIYLAHP ESYYFGVAKV ERDQVEDYAR RKAMPLTEVE RWLGPILNYV PAHYAEAAE // ID E8TS65_ALIDB Unreviewed; 343 AA. AC E8TS65; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 30. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADU97903.1}; GN OrderedLocusNames=Alide_0117 {ECO:0000313|EMBL:ADU97903.1}; OS Alicycliphilus denitrificans (strain DSM 18852 / JCM 14587 / BC). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Alicycliphilus. OX NCBI_TaxID=596153 {ECO:0000313|EMBL:ADU97903.1, ECO:0000313|Proteomes:UP000006626}; RN [1] {ECO:0000313|Proteomes:UP000006626} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 14587 / BC {ECO:0000313|Proteomes:UP000006626}; 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; ADU97903.1; -; Genomic_DNA. DR RefSeq; WP_013517042.1; NC_014910.1. DR RefSeq; YP_004124791.1; NC_014910.1. DR EnsemblBacteria; ADU97903; ADU97903; Alide_0117. DR KEGG; adn:Alide_0117; -. DR PATRIC; 45138961; VBIAliDen149934_0217. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR BioCyc; ADEN596153:GHGY-117-MONOMER; -. DR Proteomes; UP000006626; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006626}; KW Methyltransferase {ECO:0000313|EMBL:ADU97903.1}; KW Transferase {ECO:0000313|EMBL:ADU97903.1}. SQ SEQUENCE 343 AA; 36835 MW; DA8371F8939330C4 CRC64; MTLPHYTRAQ QLPAILEQRI AILDGAMGTM IQRFKLTEEQ YRGERFKDFA RDVKGNNELL SLTRPNVIRD IHEGYLAAGA DLIETNTFGA TSIAQEDYGM ADLAYEMNLE SARLARAACG KFSTPDKPRF VAGALGPTPK TASISPDVND PGARNVTFEQ LRAAYLEQTL ALIAGGADVL LVETIFDTLN AKAALFAIDE AFEQTGECLP IMISGTVTDA SGRILSGQTV TAFWHSVRHA NPLSIGLNCA LGAALMRPYI QELAKAAPDT FISCYPNAGL PNPMSDTGFD ETPEVTSRLV HEFATERLVN IVGGCCGTTP DHIGAIARAV APVGARRLFS AVS // ID E8U945_DEIML Unreviewed; 1212 AA. AC E8U945; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADV67584.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADV67584.1}; GN OrderedLocusNames=Deima_1939 {ECO:0000313|EMBL:ADV67584.1}; 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 {ECO:0000313|EMBL:ADV67584.1, ECO:0000313|Proteomes:UP000008635}; RN [1] {ECO:0000313|Proteomes:UP000008635} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 21211 / LMG 22137 / NRRL B-23946 / LB-34 RC {ECO:0000313|Proteomes:UP000008635}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002454; ADV67584.1; -; Genomic_DNA. DR RefSeq; WP_013557089.1; NC_014958.1. DR RefSeq; YP_004171249.1; NC_014958.1. DR EnsemblBacteria; ADV67584; ADV67584; Deima_1939. DR KEGG; dmr:Deima_1939; -. DR PATRIC; 46924958; VBIDeiMar159729_1948. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR BioCyc; DMAR709986:GHZG-1985-MONOMER; -. DR Proteomes; UP000008635; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008635}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADV67584.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008635}; KW Transferase {ECO:0000313|EMBL:ADV67584.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1212 AA; 131499 MW; 685C90A0E7FEC6B1 CRC64; MTQRNDRTQE LLSIARERIL ILDGGWGTML QRRGLTEADY RRAEFAWDVQ YKGNHDVLQL TRPDVIREIH RLYFEAGADI TSTNTFSSTS IAQADYGLAH LARALNVAGA RLAREVADEL TAQDGKPRFV AGSVGPTNRT ATLSPDVERP EFRAVTFDDL AAAYEEAVEG LLEGGADLIL IETVFDTLNA KAALFACEAV FERLGRRAPV MLSGTITDAS GRTLSGQTPE AFTVSTEHAP LFSLGLNCAL GADLLRPHLR ALARSTDVLV SVHPNAGLPN AFGEYDETPE HTAGVLREFA EDGLVNIVGG CCGTTPEHIR AIAKAVRDVK PRVAAPLPRQ LRLSGLEAFT VTPEVNFVNV GERTNVTGSP KFSRAILEGD FDAGLKIARQ QVVSGAQVID INFDEGLLDG EAAMVRFLNL LAGEPDIARV PIMLDSSRWS VLEAGLKRIQ GKGIVNSLSL KEGEAAFLAQ ARTIRRYGAA VVVMAFDEQG QADTLERRTE ICARAYRLLT QQAGFAGHDI IFDPNVLTVA TGLPEHDRYA LDFIEATRWI KANLPGALVS GGISNVSFSF RGNNAVREAM HAVFLYHAIR AGLDMGIVNA GMLAVYDDLD PELREHVEDV ILARRADATE RLIELAERFK GEKRSASSNA ASWRDLPVRE RLSHALVQGI SDFVEVDAEE AYQLLGSPLA VIEGPLMDGM NVVGDLFGAG KMFLPQVVKS ARVMKRAVAH LTPYLEAEKA SGSSKGRVVM ATVKGDVHDI GKNIVGVVLA CNGFEVTDLG VMVSGERILD EAARLNADVI GLSGLITPSL DEMVNVAREM ERRGLNTPVL IGGATTSRAH TAVRIAPAYS GPVAHVLDAS RAVTVVQDLL GDPDGFKVRA DAEHERQRAR HADRTVRLTP LDAARANALK LTAPAQPSPR EPGRQVIEQP LGELRAFIDW TPFFIAWELP GVYPKILDDP RVGAEARQLL ADANALLDRA EREGLLTAQG VIRLAPATRD GDDILLADGT VLHTIRQQRE QQGPNVALSD FVADGGDHVG LFAVTIHGAE ALAVQFEEAH DDYNAILTKA VADRLAEAFA EKLHRDVRTR HWGYAADEQL DHAALIREKY VGIRPAPGYP AQPDHTEKRT IFAQLRAEEI GLTLTDSCAM LPAASVSGLY FAHPQSAYFA VGRIGEDQVR DYARRKGWTQ AEAERWLAPI LAYTPALTGG VR // ID E8UWM9_THEBF Unreviewed; 807 AA. AC E8UWM9; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADV79311.1}; GN OrderedLocusNames=Thebr_0717 {ECO:0000313|EMBL:ADV79311.1}; 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 {ECO:0000313|EMBL:ADV79311.1, ECO:0000313|Proteomes:UP000002062}; RN [1] {ECO:0000313|EMBL:ADV79311.1, ECO:0000313|Proteomes:UP000002062} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43586 / DSM 3389 / AKO-1 RC {ECO:0000313|Proteomes:UP000002062}; 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 ----------------------------------------------------------------------- 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; ADV79311.1; -; Genomic_DNA. DR RefSeq; WP_012269136.1; NC_014964.1. DR RefSeq; YP_004185694.1; NC_014964.1. DR ProteinModelPortal; E8UWM9; -. DR EnsemblBacteria; ADV79311; ADV79311; Thebr_0717. DR KEGG; tbo:Thebr_0717; -. DR PATRIC; 47039359; VBITheBro57020_0739. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR BioCyc; TBRO509193:GHWP-737-MONOMER; -. DR Proteomes; UP000002062; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002062}; KW Methyltransferase {ECO:0000313|EMBL:ADV79311.1}; KW Transferase {ECO:0000313|EMBL:ADV79311.1}. SQ SEQUENCE 807 AA; 88155 MW; F1FFC3822A63FBB4 CRC64; MLDIFKELSN RVIVFDGAMG TQLQERGLKT GECPEYMNIT HPEVVFDIHR SYIEAGADVI ETNTFGANRI KLAKYGLENE VFNIVTQAVK IAKEASKDKP VALSIGPIGE LLTPYGDMTF DEAYDVFKEV VIAAERAGAD IVLIETMSDM LEAKAAILAA KENSNMKVIC TMTFQEDGRT LMGSDPITVV VSLQGLGLDA IGVNCSTGPD KMVSVVEKMS QVSRIPIIAQ PNAGMPVIRD GKTVYDLKPE EFASFFPLLV EKGASIVGGC CGTTPHYIKL VKKAVKDLKP KVKVNKFTAV ASNTKTVFIG ENYLLRVIGE RINPTGKKKL SEAFLAGNVS LAVEEAIKQQ KCGAEILDVN VGVPGVNEEE LLPKVVSEIQ NVVDIPLQID STNIKAVEKA IRILRGRPII NSVSAKEESL KEVLPIVKKY GACVVGLTVG DKGLPKDRHE RIENAKKIIK KAEEYGIPKE DILIDCIVLT VSSEQEAAIE TLEAIKLAKE ELGVNTVVGL SNVSFGLPER RLINSTFLAM AASYGLTTAI INPCDEAMMD TLRASMVLLN KDKGSVNYLK IYGNRQKEEG KEKEQQKIQE EDLKSKFYIQ ILEGKKSGVE DIVKNILEEE VQPLSIVDNI IIPALKEVGD RYEKGIYFLP QLLSSAEVVQ SAFKIIKEKL PKGSVSKGKI ILATVEGDVH DIGKNIVKVL LENYGYDVID LGKDVKGEVI LEEVKRTGAP LVGLSALMTT TLFNMEKIIK LLKANTDVKI MVGGAVLTEE YAYKIGADYY GKTAQDAVKI ADKFFLKNAL LCKTCGI // ID E8UZC6_TERSS Unreviewed; 625 AA. AC E8UZC6; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 27. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=AciPR4_1320 {ECO:0000313|EMBL:ADV82144.1}; OS Terriglobus saanensis (strain ATCC BAA-1853 / DSM 23119 / SP1PR4). OC Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae; OC Terriglobus. OX NCBI_TaxID=401053 {ECO:0000313|EMBL:ADV82144.1, ECO:0000313|Proteomes:UP000006844}; RN [1] {ECO:0000313|EMBL:ADV82144.1, ECO:0000313|Proteomes:UP000006844} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-1853 / DSM 23119 / SP1PR4 RC {ECO:0000313|Proteomes:UP000006844}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ADV82144.1; -; Genomic_DNA. DR RefSeq; WP_013567877.1; NC_014963.1. DR RefSeq; YP_004182138.1; NC_014963.1. DR ProteinModelPortal; E8UZC6; -. DR EnsemblBacteria; ADV82144; ADV82144; AciPR4_1320. DR KEGG; tsa:AciPR4_1320; -. DR PATRIC; 46828368; VBITerSaa54836_1391. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR BioCyc; TSAA401053:GHYY-1333-MONOMER; -. DR Proteomes; UP000006844; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006844}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ADV82144.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000006844}; KW Transferase {ECO:0000313|EMBL:ADV82144.1}. SQ SEQUENCE 625 AA; 66435 MW; F735E32035374C37 CRC64; MKNVAADWLK SRTLLFDGAM GTMFYARGIF INRCYDELNL TEPEMVRELH EEYLMAGAEA IETNTFGATA PRLARYGLAE KVGAINRAAV VIAHRAVRHA KEKLAVDALV AGSIGPVADA ALSEDEVRNA YREQMAALVE GEGIDLFAIE TVMSLREARL ALEAAALAAP GIPSIVMVTV NEVGQCLDGT EVEEAVRFLE AAGAAAVGCN CSSGPEMILR TIERMRAVTT LPIAGMPNAG VPSCVDGRSI YLTSPEYMAS FARKALRAGA TIVGGCCGTT PAHIRSMRGA LRAVVAQQEG TASAGKGTKS DHAVAIVEPM PLAARSLLGG RIARKEFVTM VEIVPPKGID ASRELEGARM LHAMGVHAIN VPDSPRASAR MSAGALCIQI QQKIGVEVVL HSTCRDRNLL GLQSDLLGAA SLGLKNMLCL TGDPPKMGTY PDATAVFDVD AIGQLAMARE MNRGFDIGGN SIGASTNFVL ACAANPGLPD LDAEVRRFAA KVEAGAEFAI TQPVFDLRLL EDFLRRIEQF RIPVIAGIWP LTSVRNAEFM RNDLKVSVPE SIMTRMAACE TPESAREEGI LIAQEMLREA RPQVQGVQVS APFGKYELAA KVLDGFLSGG GNGDV // ID E8V7W8_TERSS Unreviewed; 384 AA. AC E8V7W8; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADV82892.1}; GN OrderedLocusNames=AciPR4_2089 {ECO:0000313|EMBL:ADV82892.1}; OS Terriglobus saanensis (strain ATCC BAA-1853 / DSM 23119 / SP1PR4). OC Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae; OC Terriglobus. OX NCBI_TaxID=401053 {ECO:0000313|EMBL:ADV82892.1, ECO:0000313|Proteomes:UP000006844}; RN [1] {ECO:0000313|EMBL:ADV82892.1, ECO:0000313|Proteomes:UP000006844} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-1853 / DSM 23119 / SP1PR4 RC {ECO:0000313|Proteomes:UP000006844}; 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; ADV82892.1; -; Genomic_DNA. DR RefSeq; WP_013568625.1; NC_014963.1. DR RefSeq; YP_004182886.1; NC_014963.1. DR EnsemblBacteria; ADV82892; ADV82892; AciPR4_2089. DR KEGG; tsa:AciPR4_2089; -. DR PATRIC; 46829958; VBITerSaa54836_2177. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR BioCyc; TSAA401053:GHYY-2112-MONOMER; -. DR Proteomes; UP000006844; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006844}; KW Methyltransferase {ECO:0000313|EMBL:ADV82892.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006844}; KW Transferase {ECO:0000313|EMBL:ADV82892.1}. SQ SEQUENCE 384 AA; 41786 MW; 70E25CA6B73B25BB CRC64; MHQERKRKMT LSQLHPLKKI LQDRIAIIDG AMGTTIRTYG MTEADIRGER FKDSTKDLLN NGDIFSLTQP DMICDIHRRF LEAGADIIET NTFGATSITQ SEFFVEDPRE HGGRKDPEFY QKILEDPMLS QLAWDINETS ARQCREWADR VGNATGRHRF VAGAIGPLTV SLSNSPDADD AGFRVVTFDQ VKIAYMEQIR ALMAGGSDLL LVETIFDSLN AKAALVAIRE VFDQDGKELP VMISAAVGRG GETLISAQTT EAFWNAVQHV KPLSVGLNCS LGPDLMYPFL SELSAKADVA ISCYPNAGLP NPLSETGFDL GPDDMARYLG DFARGGLINI AGGCCGNTPE HIAAIAKALE NQPPREFGTA ALVESFAGRS GTRG // ID E8W2J8_STRFA Unreviewed; 311 AA. AC E8W2J8; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADW02826.1}; GN OrderedLocusNames=Sfla_1386 {ECO:0000313|EMBL:ADW02826.1}; OS Streptomyces pratensis (strain ATCC 33331 / IAF-45CD). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=591167 {ECO:0000313|EMBL:ADW02826.1, ECO:0000313|Proteomes:UP000002066}; RN [1] {ECO:0000313|EMBL:ADW02826.1, ECO:0000313|Proteomes:UP000002066} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33331 / DSM 40990 / IAF-45CD RC {ECO:0000313|Proteomes:UP000002066}; 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 ----------------------------------------------------------------------- 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; ADW02826.1; -; Genomic_DNA. DR RefSeq; WP_014153496.1; NC_016114.1. DR RefSeq; YP_004922343.1; NC_016114.1. DR EnsemblBacteria; ADW02826; ADW02826; Sfla_1386. DR GeneID; 11369597; -. DR KEGG; sfa:Sfla_1386; -. DR KO; K00547; -. DR BioCyc; SFLA591167:GI5Y-1391-MONOMER; -. DR Proteomes; UP000002066; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002066}; KW Methyltransferase {ECO:0000313|EMBL:ADW02826.1}; KW Transferase {ECO:0000313|EMBL:ADW02826.1}. SQ SEQUENCE 311 AA; 32907 MW; EFDEC7A927A236CA CRC64; MHTVRTQEAR PRRTLGQALA EGTVLLDGGL SNQLEAQGCD LSDALWSAGL LSDEPRQIEA AHRAYARAGA QVLITASYQA TFEGFARRGI GRARAAELMA GSVELARRAG ADTGRESWVA ASVGPYGAML ADGSEYRGRY GMTVRELVRF HRPRVETLAA AGPDVLALET VPDADEAEAL LRAVQDLDVP VWLSYSVAGD RTRAGQPLAE AFGLAAGIDQ VVAVGVNCCD PADADRAVEV AAAATGKPVV VYPNSGEEWD ADGRDWTGRS TFEPGRVRHW RNAGARLVGG CCRVGPSNIE ALGARLRTPT A // ID E8W6W3_STRFA Unreviewed; 1170 AA. AC E8W6W3; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADW06578.1}; GN OrderedLocusNames=Sfla_5179 {ECO:0000313|EMBL:ADW06578.1}; OS Streptomyces pratensis (strain ATCC 33331 / IAF-45CD). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=591167 {ECO:0000313|EMBL:ADW06578.1, ECO:0000313|Proteomes:UP000002066}; RN [1] {ECO:0000313|EMBL:ADW06578.1, ECO:0000313|Proteomes:UP000002066} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33331 / DSM 40990 / IAF-45CD RC {ECO:0000313|Proteomes:UP000002066}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002475; ADW06578.1; -; Genomic_DNA. DR RefSeq; WP_014157187.1; NC_016114.1. DR RefSeq; YP_004926095.1; NC_016114.1. DR EnsemblBacteria; ADW06578; ADW06578; Sfla_5179. DR GeneID; 11368856; -. DR KEGG; sfa:Sfla_5179; -. DR KO; K00548; -. DR BioCyc; SFLA591167:GI5Y-5257-MONOMER; -. DR Proteomes; UP000002066; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002066}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 237 237 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 747 747 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1170 AA; 127626 MW; 3F58071338F14ECE CRC64; MASLPTPSAD SRTRAAALRE ALATRVVVAD GAMGTMLQAQ DPTLEDFENL EGCNEILNVT RPDIVRSVHE EYFAVGVDCV ETNTFGANAS ALGEYDIPGR IHELSEAGAR IARETADRFT ESTGQQRWVL GSIGPGTKLP TLGHAPYTVL RDGFQQNAEG LIAGGADALI IETTQDLLQT KAAVLGARRA LEAMGSDLLV LCSLAFETTG TMLLGSEIGA ALTALEPLGV DMIGLNCSTG PAEMSEHLRY LTRHSRIPLL CMPNAGLPVL TKDGAHFPLD AEGLADAQET FVQEYGLSLV GGCCGTTPEH LRRLVERVRG AALSTRDPRP EPGAASLYQT IPFRQDTSYL AIGERTNANG SKKFREAMLD ARWDDCVEMA RDQIREGAHM LDLCVDYVGR DGVADMEELA GRFATASTLP IVLDSTEVPV LRAGLEKLGG RAVLNSVNYE DGDGPESRFA KVAGLAAEHG AALIALTIDE EGQARTVEHK VAIAERLIED LTTNWGIRES DILIDCLTFT ICTGQEESRK DGIATIGAIR ELKRRRPDVQ TTLGLSNISF GLNPAARVVL NSVFLDECVK AGLDSAIVHA SKILPIARLE EEQVKVALDL IHDRREEGYD PLQRLMELFE GVNMKSMKQG KAEELLALPL DERLQRRIID GEKNGLEADL DEALLTTPAL EIVNDTLLAG MKVVGELFGS GQMQLPFVLQ SAEVMKSAVA HLEPHMEKTD AEGKGTIVLA TVRGDVHDIG KNLVDIILSN NGFNVVNLGI KQPVSAILDA AQEHRADVIG MSGLLVKSTV IMKENLEELN QRKLAADYPV ILGGAALTRA YVEQDLHEIY EGEVRYARDA FEGLRLMDAL VAVKRGVPGA ALPELKQRRV PKRDTPVAEA VEPEEGVRSD VSVTNPVPEP PFWGTRVIKG IQLKEYASWL DEGALFKGQW GLKQARAGDG PTYEELVERE GRPHLRGWLD KLHTENLLEA AVVYGYFPCV SKGDDLILLH EDGSERTRFT FPRQRRGRRL CLADFFRPEE SGETDVIGLQ VVTVGSKIGG ATAELFEANS YRDYLELHGL SVQLAEALAE YWHARVRSEL GFAGEDPSDV EDMFALKYRG ARFSLGYGAC PDLEDRAKIA ALLEPERIGV KLSEEFQLHP EQSTDAIVIH HPEAKYFNAR // ID E8WMU3_GEOS8 Unreviewed; 813 AA. AC E8WMU3; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 01-APR-2015, entry version 21. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADW11803.1}; GN OrderedLocusNames=GM18_0314 {ECO:0000313|EMBL:ADW11803.1}; OS Geobacter sp. (strain M18). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=443143 {ECO:0000313|EMBL:ADW11803.1, ECO:0000313|Proteomes:UP000001442}; RN [1] {ECO:0000313|EMBL:ADW11803.1, ECO:0000313|Proteomes:UP000001442} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M18 {ECO:0000313|EMBL:ADW11803.1, RC ECO:0000313|Proteomes:UP000001442}; 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; ADW11803.1; -; Genomic_DNA. DR RefSeq; WP_015718673.1; NC_014973.1. DR RefSeq; YP_004197079.1; NC_014973.1. DR EnsemblBacteria; ADW11803; ADW11803; GM18_0314. DR KEGG; geb:GM18_0314; -. DR PATRIC; 46944480; VBIGeoSp68312_0315. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR BioCyc; GSP443143:GHZL-322-MONOMER; -. DR Proteomes; UP000001442; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001442}; KW Methyltransferase {ECO:0000313|EMBL:ADW11803.1}; KW Transferase {ECO:0000313|EMBL:ADW11803.1}. SQ SEQUENCE 813 AA; 84757 MW; EB9FC2A453E3A3C3 CRC64; MKMPFMQAVK ERVLVLDGAM GTMLQERGLK AGQSPEEMNL TAPEVVAGVH RAYLEAGADI IVTNTFGGTK AKLEHYGLGD QVTRINAEAV RIAREVAGES AYVAGSIGPT GRFVEPVGDM SFDEACALFG EQAKALIDAG CDVISLETFL DIKEIRAALI AIRELSTDIP VIAMLTFEEK GRSVLGSPPE AAAITLEAAG ASMVGSNCGL GVDGIYDILC AMRKVTSLPL ISQANAGLPI LKDGVTVFPG TPDEMTAYHD RMIGLGVRVI GGCCGTTPVH ISAIKAALSG RQTPFTPKED DGTTWISSRG SFAPIGALHP VALIGERINP TGKKLYSQEL REGKVSYIRR EALEQTELGA TLLDVNVGTP GIDEPAAMER AVFCVTGAVQ TPLVLDSSSP QALEAGLKAA DGKVLINSVN GEEKSLAAVL PLAKKYGAAL VCLTLDESGI PAEAEGRVAV AQTIAGHAAA AGIKRSDLVV DCLTLTVSAE PKGALTALEA VRRVTELGLN TTLGVSNISF GLPCRPLISS SFFSMAMAAG LTSAIVNVKE APMMAAWRSS MVLLGKDVNA ARYIEAYKGQ VVTGSSQPAA AAAGSATVEA AAEPEGIRGR LSRAVINGEL EAVVPLVEEA LAEGLSPMQI SSEALLAGLD EVGRRFGNGS FFLPQVMVSA DTMKAAFARL KQELAGGGLE SLGKILMATV EGDIHDIGKN ILVTLLENNG FEVIDLGKNV PAARILEEAR AHQVDAVGLS ALMTTTMAQM DKVVSLLKSE GVKSFTMVGG AVVTQQYADE IGADLYAKDA MEAVARIKEL LAK // ID E8WQT0_GEOS8 Unreviewed; 609 AA. AC E8WQT0; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 01-APR-2015, entry version 30. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=GM18_3740 {ECO:0000313|EMBL:ADW15167.1}; OS Geobacter sp. (strain M18). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=443143 {ECO:0000313|EMBL:ADW15167.1, ECO:0000313|Proteomes:UP000001442}; RN [1] {ECO:0000313|EMBL:ADW15167.1, ECO:0000313|Proteomes:UP000001442} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M18 {ECO:0000313|EMBL:ADW15167.1, RC ECO:0000313|Proteomes:UP000001442}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {ECO:0000256|RuleBase:RU004255}. CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ADW15167.1; -; Genomic_DNA. DR RefSeq; WP_015721990.1; NC_014973.1. DR RefSeq; YP_004200443.1; NC_014973.1. DR ProteinModelPortal; E8WQT0; -. DR EnsemblBacteria; ADW15167; ADW15167; GM18_3740. DR KEGG; geb:GM18_3740; -. DR PATRIC; 46951421; VBIGeoSp68312_3710. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR BioCyc; GSP443143:GHZL-3808-MONOMER; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000001442; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004255}; KW Complete proteome {ECO:0000313|Proteomes:UP000001442}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ADW15167.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:ADW15167.1}. SQ SEQUENCE 609 AA; 63563 MW; 6E436983A64142FD CRC64; MKGTFLERIA AGVLIGDGAI GTMLYAKGVA PEANFEHLNL VRPELVLELH REYLAAGAQV IETNTFGANY AKLSAIGLGA KVAEINRKGA QLAKSAAAGR DVFVAGSIGP LGRGKSELTG EQAADCFRVQ SAALAEGGVD LLILETFSEL DELLTALAAA RETGLPVVAS LAFGEGGRLP GGILAESAAQ RLAAAGADLV GANCGAGPLE LLATVRRISA ACPLPLAAYP NSGFPEYLDG RYIYRTTPEY FADRAEELIA AGASLVGGCC GTTPEHIKVM AQRLQGRKPA ARVAVSVAGS ALEEERGEKV QVGFLDRWGT EPVITVELDP PKGLDCARVL AGSRALKDAG AHAINLAENP LARVRMGNLA LASLIRREVG IEVIAHVTCR DRNLIGMQSE LMGASLLGVS SILAVTGDPA SLGDEAGASS VFDLNSFTLI KLLSDLNRGV NALGNPIGAG TGFAIGAAFN PNTQKMEVQV GRLARKVANG ARFAQTQPIY DLERFEQMME QTAHLGIPIL PGVLPLVSGR NAEFLHNEVP GIVIPEGIRA RMAGKTGEEG VAEGLAIAKE FIEAAGAKAG GFYLIPPFGK YEIAVELVQF IKSLRRPLP // ID E8WRQ6_GEOS8 Unreviewed; 315 AA. AC E8WRQ6; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 01-APR-2015, entry version 17. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADW15271.1}; GN OrderedLocusNames=GM18_3845 {ECO:0000313|EMBL:ADW15271.1}; OS Geobacter sp. (strain M18). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=443143 {ECO:0000313|EMBL:ADW15271.1, ECO:0000313|Proteomes:UP000001442}; RN [1] {ECO:0000313|EMBL:ADW15271.1, ECO:0000313|Proteomes:UP000001442} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M18 {ECO:0000313|EMBL:ADW15271.1, RC ECO:0000313|Proteomes:UP000001442}; 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; ADW15271.1; -; Genomic_DNA. DR RefSeq; WP_015722093.1; NC_014973.1. DR RefSeq; YP_004200547.1; NC_014973.1. DR EnsemblBacteria; ADW15271; ADW15271; GM18_3845. DR KEGG; geb:GM18_3845; -. DR PATRIC; 46951643; VBIGeoSp68312_3816. DR HOGENOM; HOG000179103; -. DR OMA; CGLMSCR; -. DR BioCyc; GSP443143:GHZL-3917-MONOMER; -. DR Proteomes; UP000001442; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001442}; KW Methyltransferase {ECO:0000313|EMBL:ADW15271.1}; KW Transferase {ECO:0000313|EMBL:ADW15271.1}. SQ SEQUENCE 315 AA; 33612 MW; E6A6760A64CFED9E CRC64; MKENIPLPKF LEGNSCILGE GAVIERLRRG ELELDPYLVN AAFIYEPAKR AALESICRQY LDIGCGFGLP LLLSTPTWRA SRERIEAAGY AGTDVNGDNA RFMKGLQKGY GSYADKVIVC GLMSCRGNAY DPGEALDVTE AREYHAWQAG KLAETEVDFL LAATLPALGE ATGLALALAA TGKPYLVSFV VRQEGTLLDG TPLKDAVAAI DAAVTPHPVA YLINCTHASF ARSALTHERN SSTLVRQRII GLLANTAPLT PEELDESAAL VEEAPEEFGA SVAKLHSELG LKILGGCCGT DERHIMALAA RLAAI // ID E8WW85_GRATM Unreviewed; 365 AA. AC E8WW85; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 30. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADW68468.1}; GN OrderedLocusNames=AciX9_1410 {ECO:0000313|EMBL:ADW68468.1}; OS Granulicella tundricola (strain ATCC BAA-1859 / DSM 23138 / MP5ACTX9). OC Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae; OC Granulicella. OX NCBI_TaxID=1198114 {ECO:0000313|Proteomes:UP000000343}; RN [1] {ECO:0000313|Proteomes:UP000000343} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MP5ACTX9 {ECO:0000313|Proteomes:UP000000343}; 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; ADW68468.1; -; Genomic_DNA. DR RefSeq; WP_013579790.1; NC_015064.1. DR RefSeq; YP_004217248.1; NC_015064.1. DR EnsemblBacteria; ADW68468; ADW68468; AciX9_1410. DR KEGG; acm:AciX9_1410; -. DR PATRIC; 46820355; VBIAciSp155132_2088. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR Proteomes; UP000000343; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000343}; KW Methyltransferase {ECO:0000313|EMBL:ADW68468.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000343}; KW Transferase {ECO:0000313|EMBL:ADW68468.1}. SQ SEQUENCE 365 AA; 39505 MW; 7633AC70A5CD8E1E CRC64; MTKAPIHPLE KILAERIAII DGAMGTTIRT YGMTEADMRG ERFKNHNKDL QNNGDLFSLT QPKMIEDIHR RFLEAGADII ETNTFGATSI TQSEFFVDDP REHGGRKDPA FYQNIIEDKF LNDLAWEVNE TSARQCRAWA DRVANDTGRQ RFVAGAIGPL TVSLSNSPDA DDAGFRVVTF DQVKAAYIHQ IRALIAGGSD LLLVETIFDS LNAKAALVAI REVFDEDKVD LPIMISAAVG RGGETLISAQ TTEAFWNAVK HVKPLSVGLN CSLGPDLMYP FLSELSAKAD VAISCYPNAG LPNPLSETGF DLGPPDMARF LGGFAQDGLI NIAGGCCGNT PEHIAAIAKA LEGKAPRTLL REVAA // ID E8WWG5_GRATM Unreviewed; 637 AA. AC E8WWG5; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 29. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=AciX9_2604 {ECO:0000313|EMBL:ADW69629.1}; OS Granulicella tundricola (strain ATCC BAA-1859 / DSM 23138 / MP5ACTX9). OC Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae; OC Granulicella. OX NCBI_TaxID=1198114 {ECO:0000313|Proteomes:UP000000343}; RN [1] {ECO:0000313|Proteomes:UP000000343} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MP5ACTX9 {ECO:0000313|Proteomes:UP000000343}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ADW69629.1; -; Genomic_DNA. DR RefSeq; WP_013580944.1; NC_015064.1. DR RefSeq; YP_004218409.1; NC_015064.1. DR ProteinModelPortal; E8WWG5; -. DR EnsemblBacteria; ADW69629; ADW69629; AciX9_2604. DR KEGG; acm:AciX9_2604; -. DR PATRIC; 46822749; VBIAciSp155132_3264. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR Proteomes; UP000000343; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000343}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ADW69629.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000000343}; KW Transferase {ECO:0000313|EMBL:ADW69629.1}. SQ SEQUENCE 637 AA; 67908 MW; 4B1072C2ED795815 CRC64; MTEVETKTEL RGAAARLFTG GTVLCDGAMG SMLYGRGIFI NRCYDELNLS QPDLVRAVHT EYLQAGATVI ETNTFGGNRI RLERHGLEEK VREINRAGVR LARECVQQMA EKHASEAFVA GAMGPLGIRI GDGNKVTEEE AYAAFAVQVK ALVEGGPGVG ADLLILETLM AMNEARLAIQ AAKAEGQGLP VIAMVTVDVN GNCLDGTSAE EAARLMTEWG ADAVGCNCSD GPATVLAVIE RMRTATKLPL AAMPNAGNPR VIDGRHIYLT SPEYMASFAR KFIKAGATFV GGCCGTTPQH TRAMRGALRA IGAQETGVEV VENGGAAEAG AARAQSKVMP PDLKDRSRVG AKIATGEFVT LVEIVPPKGI DSSKELEGAE ELHKLGVDAI NVPDSPRASA RMSAMSLCVQ IQQRVGIETV LHYTCRDRNL LSIQSDLLGA SSIGLRNILC LTGDPPKMGT YPDATAVFDV DAIGLTKIVR DMNYGLDIGG HSIGQSCGFT IAVAANPGVV DIDNEVRRFA AKVEAGGEYG ITQPVFDLRL LEQFLKRIEQ FRIPMIAGIW PLTSVKNAEF MRDQLKVRMP EEILARMGAM PSPEHAKAEG IAIAQEMLEE SRAMVQGVQV SAPFGKYKAA AQVLGVL // ID E8X8U6_SALT4 Unreviewed; 1262 AA. AC E8X8U6; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 01-APR-2015, entry version 33. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:ADX19953.1}; GN Name=metH {ECO:0000313|EMBL:ADX19953.1}; GN OrderedLocusNames=STM474_4378 {ECO:0000313|EMBL:ADX19953.1}; OS Salmonella typhimurium (strain 4/74). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=909946 {ECO:0000313|EMBL:ADX19953.1, ECO:0000313|Proteomes:UP000008978}; RN [1] {ECO:0000313|EMBL:ADX19953.1, ECO:0000313|Proteomes:UP000008978} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4/74 {ECO:0000313|Proteomes:UP000008978}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002487; ADX19953.1; -; Genomic_DNA. DR RefSeq; WP_014344255.1; NC_016857.1. DR RefSeq; YP_005245152.1; NC_016857.1. DR EnsemblBacteria; ADX19953; ADX19953; STM474_4378. DR PATRIC; 47200537; VBISalEnt171491_4444. DR OMA; DYNSIMV; -. DR BioCyc; SENT909946:GLJU-4347-MONOMER; -. DR Proteomes; UP000008978; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008978}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 282 282 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 345 345 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 346 346 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 794 794 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1262 AA; 139662 MW; 82B8E2428501919A CRC64; MGGKLNMSHV ARCSLFRQHA LCQYGSLRGA LSGASVSSKV EQLRAQLNER ILVLDGGMGT MIQSYRLHEE DFRGERFADW PCDLKGNNDL LVLSKPEVIA AIHNAYFEAG ADIIETNTFN STTIAMADYR MESLSAEINY AAAKLARACA DEWTARTPEK PRFVAGVLGP TNRTASISPD VNDPAFRNIT FDQLVAAYRE STKALVEGGA DLILIETVFD TLNAKAAVFA VKEEFEALGV DLPIMISGTI TDASGRTLSG QTTEAFYNSL RHAEALTFGL NCALGPDELR QYVQELSRIA ECYVTAHPNA GLPNAFGEYD LDADTMAKQI REWAEAGFLN IVGGCCGTTP EHIAAMSRAV AGLLPRQLPD IPVACRLSGL EPLNIGDDSL FVNVGERTNV TGSAKFKRLI KEEKYSEALD VARQQVESGA QIIDINMDEG MLDAEAAMVR FLSLIAGEPD IARVPIMIDS SKWEVIEKGL KCIQGKGIVN SISMKEGVEA FIHHAKLLRR YGAAVVVMAF DEQGQADTRA RKIEICRRAY KILTEEVGFP PEDIIFDPNI FAVATGIEEH NNYAQDFIGA CEDIKRELPH ALISGGVSNV SFSFRGNDPV REAIHAVFLY YAIRNGMDMG IVNAGQLAIY DDLPAELRDA VEDVILNRRD DGTERLLDLA EKYRGSKTDE AANAQQAEWR SWDVKKRLEY SLVKGITEFI EQDTEEARQQ AARPIEVIEG PLMDGMNVVG DLFGEGKMFL PQVVKSARVM KQAVAYLEPF IEASKEKGSS NGKMVIATVK GDVHDIGKNI VGVVLQCNNY EIVDLGVMVP AEKILRTARE VNADLIGLSG LITPSLDEMV NVAKEMERQG FTIPLLIGGA TTSKAHTAVK IEQNYSGPTV YVQNASRTVG VVAALLSDTQ RDDFVARTRK EYETVRIQHA RKKPRTPPVT LEAARDNDLA FDWERYTPPV AHRLGVQEVE ASIETLRNYI DWTPFFMTWS LAGKYPRILE DEVVGVEAQR LFKDANDMLD KLSAEKLLNP RGVVGLFPAN RVGDDIEIYR DETRTHVLTV SHHLRQQTEK VGFANYCLAD FVAPKLSGKA DYIGAFAVTG GLEEDALADA FEAQHDDYNK IMVKAIADRL AEAFAEYLHE RVRKVYWGYA PNESLSNDEL IRENYQGIRP APGYPACPEH TEKGTIWQLL DVEKHTGMKL TESFAMWPGA SVSGWYFSHP ESKYFAVAQI QRDQVTDYAF RKGMSVEDVE RWLAPNLGYD AD // ID E8Y5K7_ECOKO Unreviewed; 1227 AA. AC E8Y5K7; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 39. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADX52864.1}; GN OrderedLocusNames=EKO11_4306 {ECO:0000313|EMBL:ADX52864.1}; OS Escherichia coli (strain ATCC 55124 / KO11). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=595495 {ECO:0000313|EMBL:ADX52864.1, ECO:0000313|Proteomes:UP000002250}; RN [1] {ECO:0000313|EMBL:ADX52864.1, ECO:0000313|Proteomes:UP000002250} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 55124 / KO11 {ECO:0000313|Proteomes:UP000002250}; 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. CC ----------------------------------------------------------------------- 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; ADX52864.1; -; Genomic_DNA. DR RefSeq; WP_000096010.1; NC_017660.1. DR RefSeq; YP_005279928.1; NC_016902.1. DR RefSeq; YP_006162800.1; NC_017660.1. DR ProteinModelPortal; E8Y5K7; -. DR SMR; E8Y5K7; 651-1227. DR EnsemblBacteria; ADX52864; ADX52864; EKO11_4306. DR EnsemblBacteria; AFH15448; AFH15448; KO11_02300. DR KEGG; ekf:KO11_02300; -. DR KEGG; eko:EKO11_4306; -. DR PATRIC; 48648791; VBIEscCol13896_4377. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; ECOL595495:GI1Q-4389-MONOMER; -. DR Proteomes; UP000002250; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002250}. SQ SEQUENCE 1227 AA; 135969 MW; 31A0CAA1E9127CD9 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID E8YL85_9BURK Unreviewed; 356 AA. AC E8YL85; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADX53670.1}; GN ORFNames=BC1001_0205 {ECO:0000313|EMBL:ADX53670.1}; OS Burkholderia sp. CCGE1001. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=640510 {ECO:0000313|EMBL:ADX53670.1, ECO:0000313|Proteomes:UP000007095}; RN [1] {ECO:0000313|EMBL:ADX53670.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCGE1001 {ECO:0000313|EMBL:ADX53670.1}; 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 ----------------------------------------------------------------------- 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; ADX53670.1; -; Genomic_DNA. DR RefSeq; WP_013586953.1; NC_015136.1. DR RefSeq; YP_004226730.1; NC_015136.1. DR EnsemblBacteria; ADX53670; ADX53670; BC1001_0205. DR KEGG; bug:BC1001_0205; -. DR PATRIC; 46892857; VBIBurSp1058_0215. DR KO; K00548; -. DR BioCyc; BSP640510:GI28-208-MONOMER; -. DR Proteomes; UP000007095; Chromosome 1. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007095}; KW Methyltransferase {ECO:0000313|EMBL:ADX53670.1}; KW Transferase {ECO:0000313|EMBL:ADX53670.1}. SQ SEQUENCE 356 AA; 38382 MW; 4FEB483094BF5ED2 CRC64; MNQPAQTAKP IRPESEYTRG AALPALLKSR ILILDGAMGT MIQRYKLDEA RYRGERFKDY GRDIKGNNEL LSITQPQIIS EIHEQYLAAG ADIIETNTFG ATTVAQADYG MESLAAEMNL ESAKLARAAC DKYSTPDKPR FVAGAIGPTP KTASISPDVN DPGARNVTFD ELRAAYYEQA KALLEGGADL FLVETIFDTL NAKAALFALD ELFEDTGERL PIMISGTVTD ASGRILSGQT VEAFWNSLRH AKPLTFGLNC ALGAALMRPY IAELAKLCDT YVSCYPNAGL PNPMSDTGFD ELPADTSGLL KEFAEAGLVN IAGGCCGTTP EHIAAIAKAL ADVKPRKWPT QYRDAA // ID E9A9F6_SALET Unreviewed; 1256 AA. AC E9A9F6; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CBY98375.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CBY98375.1}; GN Name=metH {ECO:0000313|EMBL:CBY98375.1}; GN ORFNames=SENTW_4294 {ECO:0000313|EMBL:CBY98375.1}; 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 {ECO:0000313|EMBL:CBY98375.1, ECO:0000313|Proteomes:UP000006374}; RN [1] {ECO:0000313|EMBL:CBY98375.1, ECO:0000313|Proteomes:UP000006374} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2007-60-3289-1 {ECO:0000313|EMBL:CBY98375.1}; RX PubMed=21296964; DOI=10.1128/JB.00123-11; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; FR775246; CBY98375.1; -; Genomic_DNA. DR RefSeq; WP_015633211.1; NT_187127.1. DR EnsemblBacteria; CBY98375; CBY98375; SENTW_4294. DR Proteomes; UP000006374; Contig 59. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006374}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CBY98375.1}; KW Transferase {ECO:0000313|EMBL:CBY98375.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 276 276 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 339 339 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 340 340 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 788 788 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1256 AA; 139147 MW; 3C562E6B982363C5 CRC64; MSHVARCSLF RQHALCQYGS LRGALSGASV SSKVEQLRAQ LNERILVLDG GMGTMIQSYR LHEDDFRGER FADWPCDLKG NNDLLVLSKP EVIAAIHNAY FEAGADIIET NTFNSTTIAM ADYRMESLSA EINYAAAKLA RACADEWTAR TPEKPRFVAG VLGPTNRTAS ISPDVNDPAF RNITFDQLVA AYRESTKALV EGGVDLILIE TVFDTLNAKA AVFAVKEEFE ALGVDLPIMI SGTITDASGR TLSGQTTEAF YNSLRHAEAL TFGLNCALGP DELRQYVQEL SRIAECYVTA HPNAGLPNAF GEYDLDADTM AKQIREWAEA GFLNIVGGCC GTTPEHIAAM SRAVAGLPPR QLPDIPVACR LSGLEPLNIG DDSLFVNVGE RTNVTGSAKF KRLIKEEKYS EALDVARQQV ESGAQIIDIN MDEGMLDAEA AMVRFLSLIA GEPDIARVPI MIDSSKWEVI EKGLKCIQGK GIVNSISMKE GVEAFIHHAK LLRRYGAAVV VMAFDEQGQA DTRERKIEIC RRAYKILTEE VGFPPEDIIF DPNIFAVATG IEEHNNYAQD FIGACEDIKR ELPHALISGG VSNVSFSFRG NDPVREAIHA VFLYYAIRNG MDMGIVNAGQ LAIYDDLPAE LRDAVEDVIL NRRDDGTERL LDLAEKYRGS KTDEAANAQQ AEWRSWDVKK RLEYSLVKGI TEFIEQDTEE ARQQASRPIE VIEGPLMDGM NVVGDLFGEG KMFLPQVVKS ARVMKQAVAY LEPFIEASKE KGSSNGKMVI ATVKGDVHDI GKNIVGVVLQ CNNYEIVDLG VMVPAEKILR TAREVNADLI GLSGLITPSL DEMVNVAKEM ERQGFTIPLL IGGATTSKAH TAVKIEQNYS GPTVYVQNAS RTVGVVAALL SDNQRDDFVA RTRKEYETVR IQHARKKPRT PPVTLEAARD NDLAFDWERY TPPVAHRLGV QEVEASIETL RNYIDWTPFF MTWSLAGKYP RILEDEVVGV EAQRLFKDAN DMLDKLSAEK LLNPRGVVGL FPANRVGDDI EIYRDETRTH VLTVSHHLRQ QTEKVGFANY CLADFVAPKL SGKADYIGAF AVTGGLEEDA LADAFEAQHD DYNKIMVKAI ADRLAEAFAE YLHERVRKVY WGYAPNESLS NDELIRENYQ GIRPAPGYPA CPEHTEKGTI WQLLDVEKHT GMKLTESFAM WPGASVSGWY FSHPESKYFA VAQIQRDQVT DYAFRKGMSV EDVERWLAPN LGYDAD // ID E9AL19_LEIMU Unreviewed; 1252 AA. AC E9AL19; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 01-APR-2015, entry version 24. DE SubName: Full=Cobalamin-dependent methionine synthase,putative {ECO:0000313|EMBL:CBZ23622.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CBZ23622.1}; GN ORFNames=LMXM_07_0090 {ECO:0000313|EMBL:CBZ23622.1}; OS Leishmania mexicana (strain MHOM/GT/2001/U1103). OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; OC Leishmaniinae; Leishmania. OX NCBI_TaxID=929439 {ECO:0000313|EMBL:CBZ23622.1, ECO:0000313|Proteomes:UP000007259}; RN [1] {ECO:0000313|Proteomes:UP000007259} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MHOM/GT/2001/U1103 {ECO:0000313|Proteomes:UP000007259}; RX PubMed=22038252; DOI=10.1101/gr.122945.111; RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A., RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D., RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F., RA Hertz-Fowler C., Mottram J.C.; RT "Chromosome and gene copy number variation allow major structural RT change between species and strains of Leishmania."; RL Genome Res. 21:2129-2142(2011). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; FR799560; CBZ23622.1; -; Genomic_DNA. DR RefSeq; XP_003872153.1; XM_003872104.1. DR GeneID; 13447024; -. DR KEGG; lmi:LMXM_07_0090; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR Proteomes; UP000007259; Chromosome 7. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007259}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CBZ23622.1}; KW Transferase {ECO:0000313|EMBL:CBZ23622.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 254 254 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 318 318 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 782 782 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1252 AA; 138721 MW; DCE175A5B2ABC64B CRC64; MSAMHGERSP VFEELEELFQ KRILVLDGGM GTMLQRYKLE EKDFRGEEFK NATKDLKGNN DLLCLTQPAK VRDVHYSYAI AGADVMETNT FNSQAVSQSD YGTQHLVRRI NLAAAKICRD AAEQASRETM RRIFVAGVLG PLNRTASISP SVERPDYRNI TYDEIVAAYT EQAAALLDGG VDVLLIETIF DSLNAKAALF AVNTLFEDKG YTRVPIMVSG TITDLSGRTL SGQTVDAFYS SMRHGNIIAI GLNCALGCRE MRPYIERLAE ISEGYVTCHP NAGLPNAMGE YDELPEDMAR DIRDFAVNGW VNLVGGCCGT TPDHIRAIAA AVKGIPPRLR GKPSETMVIS GLEALYFTRH IGFCNIGERC NISGSLRFKR LVKEGKWEEC LAVARQQVEE GAMVLDVNMD DGLIDGVTAM TRFLNMVASD PEVARVPVMI DSSKFHVIEA GLKCTQGTPI VNSISLKVGE EEFLRQARLI RRYGAAVVVM AFDENGQAAD YANKTRICKR AYDMLVADGF PPENIVFDPN VLTICTGMEE HNNYGIDFMN AATWIKANLP RAKVSGGISN LSFSFRGFEP IRMAMHSAFL KKMITDESLD MAIVNAGALP VYTDIEPDLL QLVEDAIYNR TPDSSERILE YAERLKAEKA SGGGAKEAKV SKVDEWRNAP VEERLSHALI KGIVEFIEDD VEEARTCGKY ERPLHIIEGP LMDGMGKVGE LFGSGKMFLP QVIKSARVMK KAVAVLVPYM EAEKAALMAD TNGASTSRAK RVLMATVKGD VHDIGKNIVG VVLGCNSYEV IDLGVMVSCE KILAAAREHD VHVIGLSGLI TPSLDEMVHV AKEMKRLGFK IPLMVGGATT SKQHTAVKIQ PHYDKTVHVL DASKAVVTIS NMLGNNEEEF WEEVHETYQE IAEDYLANLK DRIYKPLAFC RENALKIDFV ANPPAPPPKK LGTITISDYS LEMIATRIDW NPFFSVWQVR GTYPNRGFPK LFNCPTVGAE AKRLFDDAQE MVKDIIATRS FRAKAVVTLM PVNSVGDDIE VYKDDTRNEK IATFFGLRQQ AEKERGEPYL CISDFVAAKG VAPDYLASLV VGIFGADKMS EQYEKDNDSY RSIMIKALAD RFAEAFTEEV HRIIRTDLWG YAEKETTETA DLIQMQYQGI RPAPGYPSQP DHTEMDTIWR IGEVEERTGV KLSESYAMMP AASVSALIFA HAQSKYFAVG KIQNDQVKDY AERKGWNLDQ AESQLSSSLA YN // ID E9AU65_LEIMU Unreviewed; 320 AA. AC E9AU65; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Putative homocysteine S-methyltransferase {ECO:0000313|EMBL:CBZ26491.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:CBZ26491.1}; GN ORFNames=LMXM_36_6310 {ECO:0000313|EMBL:CBZ26491.1}; OS Leishmania mexicana (strain MHOM/GT/2001/U1103). OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; OC Leishmaniinae; Leishmania. OX NCBI_TaxID=929439 {ECO:0000313|EMBL:CBZ26491.1, ECO:0000313|Proteomes:UP000007259}; RN [1] {ECO:0000313|EMBL:CBZ26491.1, ECO:0000313|Proteomes:UP000007259} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MHOM/GT/2001/U1103 {ECO:0000313|EMBL:CBZ26491.1, RC ECO:0000313|Proteomes:UP000007259}; RX PubMed=22038252; DOI=10.1101/gr.122945.111; RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A., RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D., RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F., RA Hertz-Fowler C., Mottram J.C.; RT "Chromosome and gene copy number variation allow major structural RT change between species and strains of Leishmania."; RL Genome Res. 21:2129-2142(2011). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR799573; CBZ26491.1; -; Genomic_DNA. DR RefSeq; XP_003874989.1; XM_003874940.1. DR GeneID; 13448525; -. DR KEGG; lmi:LMXM_36_6310; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR Proteomes; UP000007259; Chromosome 20. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007259}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:CBZ26491.1}; KW Transferase {ECO:0000313|EMBL:CBZ26491.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 298 298 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 320 AA; 34289 MW; 650291B1A38CFEDD CRC64; METYLADPNH VVVLDGGLAT ELETRGCDLL DPLWSGKALL ESPQQIQDVA LEYLRAGARC IITASYQITP QSLMEHRGLT EDAAVAAIEE SVRIAQTVRE RHLKEKPQAA PVFVAGSVGP YGAYLSDGSE YRGDYVRSAE EFKEFHRLRI AALLRAGADV LAIETQPSAA EVRAIVALLQ EEHPHCRAWV SFTTSRISPV EAISDGTKWA DIISFLEKAP QVVAVGVNCI SMGEASAVLA HLHTLTTMPL VVYTNSGESY DTVTRTWHPI AMSDGTTMSL AAFAPEWASH GARLIGGCCR TGPSDIAGAA AALGSADFVV // ID E9B920_LEIDB Unreviewed; 1252 AA. AC E9B920; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 29-APR-2015, entry version 27. DE SubName: Full=Leishmania donovani BPK282A1 complete genome, chromosome 7 {ECO:0000313|EMBL:CBZ31743.1}; GN ORFNames=LDBPK_070240 {ECO:0000313|EMBL:CBZ31743.1}; OS Leishmania donovani (strain BPK282A1). OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; OC Leishmaniinae; Leishmania. OX NCBI_TaxID=981087 {ECO:0000313|Proteomes:UP000008980}; RN [1] {ECO:0000313|Proteomes:UP000008980} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BPK282A1 {ECO:0000313|Proteomes:UP000008980}; RA Downing T., Imamura H., Sanders M., Decuypere S., Hertz-Fowler C., RA Clark T.G., Rijal S., Sundar S., Quail M.A., De Doncker S., Maes I., RA Vanaerschot M., Stark O., Schonian G., Dujardin J.C., Berriman M.; RT "Whole genome sequencing of Leishmania donovani clinical lines reveals RT dynamic variation related to drug resistance."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; FR799594; CBZ31743.1; -; Genomic_DNA. DR RefSeq; XP_003858466.1; XM_003858418.1. DR GeneID; 13391853; -. DR KEGG; ldo:LDBPK_070240; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR Proteomes; UP000008980; Chromosome 7. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008980}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 254 254 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 318 318 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 782 782 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1252 AA; 138747 MW; 6FE28FB3790661FE CRC64; MSAMHGERSP VFEELEEIFQ KRILVLDGGM GTMLQRYKLE EKDFRGEEFK NATKDLKGNN DLLCLTQPAK VRDVHYKYAI AGADVMETNT FNSQAVSQSD YETQHLVRRI NLAAAKICRD AAEQASRETG RRIFVAGVLG PLNRTASISP SVERPDYRNI TYDEIVAAYT EQATALLDGG VDVLLIETIF DSLNAKAALF AVNTLFEDKG YTRVPIMVSG TITDLSGRTL SGQTVDAFYS SMRHGNIISI GLNCALGCRE MRPYVERLAE ISEAYVTCHP NAGLPNAMGE YDELPEDMAR DIRDFAVNGW VNLVGGCCGT TPDHIRAIAT AVKGIPPRLR GQPSETMVIS GLEALYFTHH IGFCNIGERC NISGSLKFKR LVKEGKWEEC LAVARQQVEE GAMVLDVNMD DGLIDGVTAM TRFLNMIASD PEVARVPVMI DSSKFHVIEA GLKCTQGTPI VNSISLKVGE EEFLRQARLI RRYGAAVVVM AFDENGQAAD YASKTRICKR AYDMLVADGF PPENIVFDPN VLTICTGMEE HNNYAIDFMN AAAWIKANLP RAKVSGGISN LSFSFRGFEA IRMAMHSAFL KKMIADGSLD MAIVNAGALP VYTDIEPDLL QLVEDAIYNR TPHSSERILE YAERLKAEKA SGGGAEEAKV SKVDEWRNAS VEERLSHALI KGIVEFIEDD VEEARTCGKY ERPLHIIEGP LMDGMGKVGE LFGSGKMFLP QVIKSARVMK KAVAVLVPYM EAEKAALMAD TNGASTSRAK RVLMATVKGD VHDIGKNIVG VVLGCNSYEV IDLGVMVSCE KILAAAKEHD VHVIGLSGLI TPSLDEMVHV AKEMKRMGFG IPLMVGGATT SKQHTAVKIQ PHYNKTVHVL DASKAVVTVS NMLGSSEEEF WEEVRETYQE IAEDYLANLK DRVYKPLAFC RENALKIDFV ANPPAPRPRK LGTITISDYS LEMIATRIDW NPFFSVWQVR GTYPNRGFPK LFNCPTVGAE AKRLFDDAQE MLKDIIATRS FRAKAVVTLM PVNSVGDDIE VYKDDTRNEK IATFFGLRQQ SEKERGEPYL CISDFIAPKG VAPDYLGSLA VGIFGADKMS EQYEKDNDSY RSIMIKALAD RFAEAFTEEM HRIIRTDLWG YAEKETAETV DLIRMQYQGI RPAPGYPSQP DHTEMDTMWR IGEVEERTGV RLSESYAMMP AASVSALVFA HAQSKYFAVG KIQKDQVKDY AERKGWNLDR AESQLSSSLA YN // ID E9BV13_LEIDB Unreviewed; 379 AA. AC E9BV13; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Leishmania donovani BPK282A1 complete genome, chromosome 36 {ECO:0000313|EMBL:CBZ39092.1}; GN ORFNames=LDBPK_366570 {ECO:0000313|EMBL:CBZ39092.1}; OS Leishmania donovani (strain BPK282A1). OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; OC Leishmaniinae; Leishmania. OX NCBI_TaxID=981087 {ECO:0000313|Proteomes:UP000008980}; RN [1] {ECO:0000313|Proteomes:UP000008980} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BPK282A1 {ECO:0000313|Proteomes:UP000008980}; RA Downing T., Imamura H., Sanders M., Decuypere S., Hertz-Fowler C., RA Clark T.G., Rijal S., Sundar S., Quail M.A., De Doncker S., Maes I., RA Vanaerschot M., Stark O., Schonian G., Dujardin J.C., Berriman M.; RT "Whole genome sequencing of Leishmania donovani clinical lines reveals RT dynamic variation related to drug resistance."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR799623; CBZ39092.1; -; Genomic_DNA. DR RefSeq; XP_003865768.1; XM_003865720.1. DR GeneID; 13386622; -. DR KEGG; ldo:LDBPK_366570; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR Proteomes; UP000008980; Chromosome 36. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008980}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 357 357 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 358 358 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 379 AA; 40772 MW; B9BCA31ED722E5ED CRC64; MECSSLFVSH LPHPTGIGCN PVSTVVAGTH AARARTHFTH MENHHFLCWG LLANWKVGGM EAYLADPNQV VMLDGGLATE LETRGCDLLD PLWSGKVLLE SPQRIRDVAL AYLRAGARCI ITASYQITPQ SLMEHRGLTE DAAVAAIEES VRIAQSVRER HLKEKPQAAP VFVAGSVGPY GAYLADGSEY RGDYVRSAEE FKEFHRLRIA ALLRAGADVL AIETQPSAAE VRAIVALLQE EHPNCRAWVS FTTSRISPVE AISDGTKWAD IISFLEKAPQ VVAVGVNCIP MAEASAVLAH LHTLTTMPLV VYTNSGESYD TVTRTWHPIP MRDGTTLSLA ALAREWASHG ARLVGGCCRT GPSDIAGAAA ALDSAGFVV // ID E9DBJ8_COCPS Unreviewed; 278 AA. AC E9DBJ8; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 07-JAN-2015, entry version 12. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EFW16150.1}; GN ORFNames=CPSG_07200 {ECO:0000313|EMBL:EFW16150.1}; 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 {ECO:0000313|Proteomes:UP000002497}; RN [1] {ECO:0000313|Proteomes:UP000002497} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RMSCC 757 / Silveira {ECO:0000313|Proteomes:UP000002497}; 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; GL636498; EFW16150.1; -; Genomic_DNA. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000002497; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002497}; KW Reference proteome {ECO:0000313|Proteomes:UP000002497}. SQ SEQUENCE 278 AA; 31138 MW; 4E735DCB52914A0D CRC64; MGTVLEEPPY GFTFSAQTPL WSSHLLLSHP TTLSEIHRSY VDAGADIVLT ATYQASFEGF ARTAIVPANV PADHKQDERH GHATYRPMDA TRYMRSAIPL AYSSFNFSSK PPRVALSLGP YGATMCPVSA EYTGIYPEEM SNTAALEAWH AKRLEVYMED PETWRKIEFL GFETVRRWDE VLAIRGAMGK LLQIAESGQS RKWWISGVFP QEDIDEEDVR RWTSAAFGST SENGLHPWGI GVNCTRLENI ERIVDIMEDE LGREKLTDNG ERASVGSS // ID E9DMP6_9STRE Unreviewed; 322 AA. AC E9DMP6; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 04-MAR-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFX54624.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EFX54624.1}; GN Name=mmuM {ECO:0000313|EMBL:EFX54624.1}; GN ORFNames=HMPREF0848_00219 {ECO:0000313|EMBL:EFX54624.1}; OS Streptococcus sp. C150. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=435842 {ECO:0000313|EMBL:EFX54624.1}; RN [1] {ECO:0000313|EMBL:EFX54624.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C150 {ECO:0000313|EMBL:EFX54624.1}; 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 ----------------------------------------------------------------------- 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; EFX54624.1; -; Genomic_DNA. DR EnsemblBacteria; EFX54624; EFX54624; HMPREF0848_00219. DR PATRIC; 46426819; VBIStrSp126103_1151. DR OrthoDB; EOG6C019S; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EFX54624.1}; KW Transferase {ECO:0000313|EMBL:EFX54624.1}. SQ SEQUENCE 322 AA; 35680 MW; B5F6A0030224018F CRC64; MVRRPFMATF KDYLENKFPL ILHGALGTEM EALGYDISGK LWSAKYLLEK PEVIQEIHET YVAAGADLIT TSSYQATLPG LMEAGLTERE AEQIIALTVQ LAKAARDKVW ATLDETEKAK RPYPLISGDV GPYAAYLANG SEYTGDYGQV TVETLKDFHR PRIQILLDQG VDLLALETIP NHLEAQALVE LLAEEFPEVE AYISFTIQVP DAISDGTSLD EMAKLVSQSN QILAVGINCS SPILYEQALP VLKKAGKALI TYPNSGEVYD GDSQTWKPKD KDALTLLEHS KDWHAHFGVQ ILGGCCRTRP NDIKALYQEF RT // ID E9EAJ9_METAQ Unreviewed; 343 AA. AC E9EAJ9; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 07-JAN-2015, entry version 16. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EFY87108.1}; GN ORFNames=MAC_06897 {ECO:0000313|EMBL:EFY87108.1}; 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 {ECO:0000313|Proteomes:UP000002499}; RN [1] {ECO:0000313|EMBL:EFY87108.1, ECO:0000313|Proteomes:UP000002499} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CQMa 102 {ECO:0000313|EMBL:EFY87108.1, RC ECO:0000313|Proteomes:UP000002499}; 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; GL698533; EFY87108.1; -; Genomic_DNA. DR RefSeq; XP_007813237.1; XM_007815046.1. DR GeneID; 19251208; -. DR KEGG; maw:MAC_06897; -. DR InParanoid; E9EAJ9; -. DR KO; K00547; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000002499; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002499}; KW Reference proteome {ECO:0000313|Proteomes:UP000002499}. SQ SEQUENCE 343 AA; 37848 MW; 7C006F155DBC16B2 CRC64; MKRILLLDGG LGTSLEQKYN LKFNSSKPLW SSDLLVSDPN TLLKCQSDFG AIPVDILLTA TYQVSIEGFA GTKSPRFPDG ISSLDIPQFL ETAVEVAENA TREHHGTVAL SLGPYGACMI PSQEYSGKYD DAHNSQEALY DWHRERMQLF SRVQGLASRI GYISMETIPR ADEIASMRRA LDQVPELAGV PFWMSCLYPG DNQRLPSGES PEAALRAMFD PRVAKSVPWG VGINCAKVWK LTPLLKQYES VVHALVQDGT LPEWPALVLY PDGTNGEAYN TVTQEWEVAD DAEDVTRVPW EEQLAEAVRG TEARGKWKQI VVGGCCMASS QDIARLRQAL PTA // ID E9EM19_METRA Unreviewed; 343 AA. AC E9EM19; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 04-MAR-2015, entry version 21. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EFZ03990.1}; GN ORFNames=MAA_01064 {ECO:0000313|EMBL:EFZ03990.1}; OS Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium OS anisopliae (strain ARSEF 23)). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Hypocreomycetidae; Hypocreales; Clavicipitaceae; OC mitosporic Clavicipitaceae; Metarhizium. OX NCBI_TaxID=655844 {ECO:0000313|EMBL:EFZ03990.1, ECO:0000313|Proteomes:UP000002498}; RN [1] {ECO:0000313|EMBL:EFZ03990.1, ECO:0000313|Proteomes:UP000002498} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498}; 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). RN [2] {ECO:0000313|EMBL:EFZ03990.1, ECO:0000313|Proteomes:UP000002498} RP GENOME REANNOTATION. RC STRAIN=ARSEF 23; RX PubMed=25368161; DOI=10.1073/pnas.1412662111; RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S., RA St Leger R.J., Wang C.; RT "Trajectory and genomic determinants of fungal-pathogen speciation and RT host adaptation."; RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(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. {ECO:0000313|EMBL:EFZ03990.1}. 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; ADNJ02000008; EFZ03990.1; -; Genomic_DNA. DR RefSeq; XP_007817253.1; XM_007819062.1. DR GeneID; 19255350; -. DR KEGG; maj:MAA_01064; -. DR KO; K00547; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000002498; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002498}; KW Methyltransferase {ECO:0000313|EMBL:EFZ03990.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002498}; KW Transferase {ECO:0000313|EMBL:EFZ03990.1}. SQ SEQUENCE 343 AA; 37604 MW; B4A20FEF42F06EF3 CRC64; MKRILILDGG LGTSLEQNYN TKFNPSTPLW SSDLLVSDPT TLLQCQSDFA AVPVDILLTA TYQVSIAGFA GTKTPKFPHG ISPLDIPPFM ETAVAVAENA TRAHHGSVAL SLGPYGACMI PSQEYSGEYD DAHDSQEALR EWHRERMQLF GRVRGLASRI GYISMETIPR ADEIAAMRAA LDQVPELAGV PFWMSCLYPG DGPCLPSGEA PETALRAMFD SRVAKSVPWG VGINCTKVWK LTALLKQYES VMDMLVRDGT LLEWPALVLY PDGTNGEVYN TVTQVWEVPG DVGDVSRVPW EEQLAEVVRG TEGRGKWRQI VVGGCCMASW QDIARLREIL LTA // ID E9G6S3_DAPPU Unreviewed; 1260 AA. AC E9G6S3; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 01-APR-2015, entry version 28. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EFX84792.1}; GN ORFNames=DAPPUDRAFT_314321 {ECO:0000313|EMBL:EFX84792.1}; OS Daphnia pulex (Water flea). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda; OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia. OX NCBI_TaxID=6669 {ECO:0000313|Proteomes:UP000000305}; RN [1] {ECO:0000313|EMBL:EFX84792.1, ECO:0000313|Proteomes:UP000000305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21292972; DOI=10.1126/science.1197761; RA Colbourne J.K., Pfrender M.E., Gilbert D., Thomas W.K., Tucker A., RA Oakley T.H., Tokishita S., Aerts A., Arnold G.J., Basu M.K., RA Bauer D.J., Caceres C.E., Carmel L., Casola C., Choi J.H., RA Detter J.C., Dong Q., Dusheyko S., Eads B.D., Frohlich T., RA Geiler-Samerotte K.A., Gerlach D., Hatcher P., Jogdeo S., RA Krijgsveld J., Kriventseva E.V., Kultz D., Laforsch C., Lindquist E., RA Lopez J., Manak J.R., Muller J., Pangilinan J., Patwardhan R.P., RA Pitluck S., Pritham E.J., Rechtsteiner A., Rho M., Rogozin I.B., RA Sakarya O., Salamov A., Schaack S., Shapiro H., Shiga Y., RA Skalitzky C., Smith Z., Souvorov A., Sung W., Tang Z., Tsuchiya D., RA Tu H., Vos H., Wang M., Wolf Y.I., Yamagata H., Yamada T., Ye Y., RA Shaw J.R., Andrews J., Crease T.J., Tang H., Lucas S.M., RA Robertson H.M., Bork P., Koonin E.V., Zdobnov E.M., Grigoriev I.V., RA Lynch M., Boore J.L.; RT "The ecoresponsive genome of Daphnia pulex."; RL Science 331:555-561(2011). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GL732533; EFX84792.1; -; Genomic_DNA. DR EnsemblMetazoa; EFX84792; EFX84792; DAPPUDRAFT_314321. DR InParanoid; E9G6S3; -. DR OMA; DYNSIMV; -. DR PhylomeDB; E9G6S3; -. DR Proteomes; UP000000305; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000305}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000305}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 257 257 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 320 320 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 782 782 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1260 AA; 139951 MW; A8D39905D2667DAA CRC64; MTISVNHNKA WSSEKSSRLE EELGRRILII DGAMGTMIQK HRLEEEDFRN EELAGHEKNL KGNNDLLSIT RPEIIYDIHT AYLEAGSDII ETNTFSGTWI AQADYGLEEW AYRLNFESAK LAARAVADHE KKTGKQCWVA GALGPTNRTL SISPSVERPD FRNITFDELV DAYTTQARAL LDGGADILLV ETIFDTANSK AALFAIENLF EKEYSRIPVM VSGTIVDKSG RTLSGQTGEA FVISVSHSNP LCIGLNCALG AREMRPFIET IGRSTSAYVI CYPNAGLPNT FGGYDETPDI MAESLRDFAS DGLVNIIGGC CGTTPDHIKA IKKIVEEYPP RKPSPNPYEG HMLLSGLEPF RIGKDTNFVN IGERCNVAGS RKFLRLIKEG KYDEALQIAK EQVENGAQVL DINMDEGMLD GVAAMTRFLN LISSEPDISK VPLCIDSSNF KVIEAGLKCN QGKCIVNSIS LKEGEEDFIH KATIVRKFGA AVVVMAFDEL GQAADTDRKV EICVRSYKLL VDKVGFNPND IIFDPNILTI ATGIEEHNTY GIDFIEACRR IKKVCPGCRV SGGVSNISFS FRGMEQIREA MHSVFLYHAI KAGLDMGIVN AGNLAVYDNI DSKLLQLCEA ILWNKDAHGT EKLLEFAQTA VKGEKTVEVD DSRSKPVEER IENALVKGID KYIVEDTEEA RLDTKKYPRP LNIIEGPLMK GMSVVGDLFG AGKMFLPQVI KSARVMKKAV GHLVPFMEKE REAAQAISGE VASENDRFAG TVVLATVKGD VHDIGKNIVA VVLGCNNFRV IDMGVMVPCD KILERAIQEK ADIVGLSGLI TPSLDEMIHV AKEMQRIKLK VPLLIGGATT SKAHTAVKIA PAYEHPVIHV LDASRSVVVS SALLDKNTIQ EYMEEIREDY EDVRQLHYET LRDRKYVSLE LARARRLKLN FTNQFTPVRP SFLGVKVFSD YDLESLIPYI DWKPFFDVWQ LRGKYPNRGY PKIFNDETVG AEAKKVFDDA QKLLKQIIDE KLLHAKGVLA FYPANSCGDD IMVYEDDDWP RDEPLARFCG LRQQAEKESK EEPHLCLSDF IAPLTSGVGD YIGMFAVTAG FGCEELCAKF EKENDDYNII MAKALADRLA EAFAEGLHEI VRTELWGYCS EERLAPSELH GIKYKGIRPA PGYPSQPDHT EKLTMWRLLQ AEPRTGIRLT DSLAMEPAAS VSGLYFAHPE SHYFGVGKIS KDQVIDYASR KEADVSLVEK TLSINLAYDL // ID E9H6P7_DAPPU Unreviewed; 325 AA. AC E9H6P7; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 07-JAN-2015, entry version 19. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EFX72546.1}; GN ORFNames=DAPPUDRAFT_308201 {ECO:0000313|EMBL:EFX72546.1}; OS Daphnia pulex (Water flea). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda; OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia. OX NCBI_TaxID=6669 {ECO:0000313|Proteomes:UP000000305}; RN [1] {ECO:0000313|EMBL:EFX72546.1, ECO:0000313|Proteomes:UP000000305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21292972; DOI=10.1126/science.1197761; RA Colbourne J.K., Pfrender M.E., Gilbert D., Thomas W.K., Tucker A., RA Oakley T.H., Tokishita S., Aerts A., Arnold G.J., Basu M.K., RA Bauer D.J., Caceres C.E., Carmel L., Casola C., Choi J.H., RA Detter J.C., Dong Q., Dusheyko S., Eads B.D., Frohlich T., RA Geiler-Samerotte K.A., Gerlach D., Hatcher P., Jogdeo S., RA Krijgsveld J., Kriventseva E.V., Kultz D., Laforsch C., Lindquist E., RA Lopez J., Manak J.R., Muller J., Pangilinan J., Patwardhan R.P., RA Pitluck S., Pritham E.J., Rechtsteiner A., Rho M., Rogozin I.B., RA Sakarya O., Salamov A., Schaack S., Shapiro H., Shiga Y., RA Skalitzky C., Smith Z., Souvorov A., Sung W., Tang Z., Tsuchiya D., RA Tu H., Vos H., Wang M., Wolf Y.I., Yamagata H., Yamada T., Ye Y., RA Shaw J.R., Andrews J., Crease T.J., Tang H., Lucas S.M., RA Robertson H.M., Bork P., Koonin E.V., Zdobnov E.M., Grigoriev I.V., RA Lynch M., Boore J.L.; RT "The ecoresponsive genome of Daphnia pulex."; RL Science 331:555-561(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; GL732598; EFX72546.1; -; Genomic_DNA. DR EnsemblMetazoa; EFX72546; EFX72546; DAPPUDRAFT_308201. DR InParanoid; E9H6P7; -. DR OMA; YGRSVTK; -. DR PhylomeDB; E9H6P7; -. DR Proteomes; UP000000305; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000305}; KW Reference proteome {ECO:0000313|Proteomes:UP000000305}. SQ SEQUENCE 325 AA; 36154 MW; 25272C5446FEDA99 CRC64; MSEKLLILDG GLGTLLYRRG AFVKGDPLWS VRCLVSKEQL EGRRQLLQAH LDYLAAGADI IKTNSYQMST ENLRKCLPGL SQEKALEMMK DSVRIARNAC QQFWQSIGEE KSGRRKPGVA GSIGPYGACK ADMSEYTGAY VDSMTEEELI QWHRPRLVAL LEAGVDYLAI ETFPALLEAK AILQLLKQEA PDIPAWISFS CKDEQHLCHG ETLDSVLKHV WVNKTPGLKA IGINCTPERL IGPLLRSLDG VDHVPVILYP NREESFEDEG PPVAAYPSRQ DEKCNNNLSK LAKEWLSIHP NVFALGGCCF YHPPDITILS CDFGN // ID E9ICG5_SOLIN Unreviewed; 322 AA. AC E9ICG5; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 07-JAN-2015, entry version 16. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EFZ21731.1}; DE Flags: Fragment; GN ORFNames=SINV_00334 {ECO:0000313|EMBL:EFZ21731.1}; OS Solenopsis invicta (Red imported fire ant) (Solenopsis wagneri). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; OC Vespoidea; Formicidae; Myrmicinae; Solenopsis. OX NCBI_TaxID=13686 {ECO:0000313|Proteomes:UP000006539}; RN [1] {ECO:0000313|EMBL:EFZ21731.1, ECO:0000313|Proteomes:UP000006539} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21282665; DOI=10.1073/pnas.1009690108; RA Wurm Y., Wang J., Riba-Grognuz O., Corona M., Nygaard S., Hunt B.G., RA Ingram K.K., Falquet L., Nipitwattanaphon M., Gotzek D., RA Dijkstra M.B., Oettler J., Comtesse F., Shih C.J., Wu W.J., Yang C.C., RA Thomas J., Beaudoing E., Pradervand S., Flegel V., Cook E.D., RA Fabbretti R., Stockinger H., Long L., Farmerie W.G., Oakey J., RA Boomsma J.J., Pamilo P., Yi S.V., Heinze J., Goodisman M.A., RA Farinelli L., Harshman K., Hulo N., Cerutti L., Xenarios I., RA Shoemaker D., Keller L.; RT "The genome of the fire ant Solenopsis invicta."; RL Proc. Natl. Acad. Sci. U.S.A. 108:5679-5684(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; GL762293; EFZ21731.1; -; Genomic_DNA. DR EnsemblMetazoa; SINV23663-RA; SINV23663-PA; SINV23663. DR InParanoid; E9ICG5; -. DR OMA; QCKDENT; -. DR Proteomes; UP000006539; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006539}; KW Reference proteome {ECO:0000313|Proteomes:UP000006539}. FT NON_TER 322 322 {ECO:0000313|EMBL:EFZ21731.1}. SQ SEQUENCE 322 AA; 35928 MW; 9F32596BAE35DEF0 CRC64; MMNGTHVKIL DGGFSGQLSR HVGTKIDGDP LWTARFLKTN VNAVHTTHLD FLRAGADIIE TNTYQASLPG MMRYLNTSER ESLDLFTTAV SLAKRAVEEY AREKHISPEQ RPLIAGSCGP YGAYLHNASE YTGSYGKNMS QQELMDWHRP RVKALLDAGV DLLALETIPC IKEAEALLKL LKEYPHARAW LSFSCRDDKF ISDGSVFQEM AVHCYRTLPL QIIAVGVNCI DPRHVTPLLK NINANALSKQ DFIPLVVYPN RGGSCSATGE WTAVPDDHSL NLPISEWLDL GVRYIGGCCK IFAEDIKTIR SEVIRYQARF IS // ID E9ICG8_SOLIN Unreviewed; 318 AA. AC E9ICG8; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EFZ21732.1}; DE Flags: Fragment; GN ORFNames=SINV_01371 {ECO:0000313|EMBL:EFZ21732.1}; OS Solenopsis invicta (Red imported fire ant) (Solenopsis wagneri). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; OC Vespoidea; Formicidae; Myrmicinae; Solenopsis. OX NCBI_TaxID=13686 {ECO:0000313|Proteomes:UP000006539}; RN [1] {ECO:0000313|EMBL:EFZ21732.1, ECO:0000313|Proteomes:UP000006539} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21282665; DOI=10.1073/pnas.1009690108; RA Wurm Y., Wang J., Riba-Grognuz O., Corona M., Nygaard S., Hunt B.G., RA Ingram K.K., Falquet L., Nipitwattanaphon M., Gotzek D., RA Dijkstra M.B., Oettler J., Comtesse F., Shih C.J., Wu W.J., Yang C.C., RA Thomas J., Beaudoing E., Pradervand S., Flegel V., Cook E.D., RA Fabbretti R., Stockinger H., Long L., Farmerie W.G., Oakey J., RA Boomsma J.J., Pamilo P., Yi S.V., Heinze J., Goodisman M.A., RA Farinelli L., Harshman K., Hulo N., Cerutti L., Xenarios I., RA Shoemaker D., Keller L.; RT "The genome of the fire ant Solenopsis invicta."; RL Proc. Natl. Acad. Sci. U.S.A. 108:5679-5684(2011). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL762293; EFZ21732.1; -; Genomic_DNA. DR EnsemblMetazoa; SINV23652-RA; SINV23652-PA; SINV23652. DR InParanoid; E9ICG8; -. DR OMA; SEWCKDG; -. DR Proteomes; UP000006539; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006539}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000006539}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 231 231 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 298 298 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT NON_TER 318 318 {ECO:0000313|EMBL:EFZ21732.1}. SQ SEQUENCE 318 AA; 35431 MW; 4C275C7B106A2BDA CRC64; MSKIRVLDGG FSTQLSTHVG EKIDGDPLWT ARFLITDPKA VFATHLDFLR AGADIIETNT YQATIDGFVK HLGISKEESL EIIRKAVDYA KDAVNVYSKE IEGNENVKNR KPLIAGSCGP YGACLHDGSE YTGSYCINVS REFLIDWHRP RIRALLEKGV DLLAIETIPC VREAEAVIDL LKEFPDTQAW LSFSCRDDGK SLADGSNFQE IAVRCYKNAL PGQILAIGIN CIAPQFVTTL LQDINKGKSD DLIPLVVYPN SGEKYIVSEG WKKEGESASL HEFIDEWLDF GVRYIGGCCR TYATDIKQIR SKVDQQRT // ID E9RU86_9FIRM Unreviewed; 806 AA. AC E9RU86; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 01-OCT-2014, entry version 17. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGC75400.1}; GN ORFNames=HMPREF0490_01017 {ECO:0000313|EMBL:EGC75400.1}; OS Lachnospiraceae bacterium 6_1_37FAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=658656 {ECO:0000313|EMBL:EGC75400.1}; RN [1] {ECO:0000313|EMBL:EGC75400.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=6_1_37FAA {ECO:0000313|EMBL:EGC75400.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGC75400.1}. 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; ADCR01000008; EGC75400.1; -; Genomic_DNA. DR EnsemblBacteria; EGC75400; EGC75400; HMPREF0490_01017. DR PATRIC; 46451199; VBILacBac17921_1787. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; SQ SEQUENCE 806 AA; 88385 MW; 1794F5526CB35F32 CRC64; MLLERLGKEL LFLDGGMGTL LQEKGLQPGE LPESWNLKRP EEVIAIHQNY FEAGSDIVLT NTFGANALKF HSEDCPLQEV VARAVENVRE AARRGVKDGR EIYVGLDIGP TGKLLKPMGD LAFEDAYEAF AEVMEYGEKA GADLIHIETM SDTYEVKAAV LAAKERTSLP VFATMIFDER GKLLTGGDVP SVVAMLEGLR VDALGINCGM GPEQMLSILE ELLTYTSLPV IVKPNAGLPK QRNGQTYYDV VPEEFASTMK LIVEKGACII GGCCGTTPAH IRQMTTLCQG MKAVPPVKKH HTLVSSYGTC ISFGRKPVII GERINPTGKK KLKQALKDGD FDYILKEGIM QQEKGAHILD VNVGLPDIDE VAVMEKVVTE LQSVTSLPLQ IDTVLPEAME RAMRIYNGKP MINSVNGKQE SMDQVFPLVQ KYGGVVVALT IDEDGIPDTA EGRLAIAEKI ICEAEKYGID RKDIVVDVLA MTISSEPEGA LVTLKALKLV REVCKVNTVL GVSNISFGLP KRPVINAHFY TMAMQQGLTS AILNPFSEEM MNSYYAFCAL MNYDENCASY IERYSKTVEE EQQSIAGSPT QAGQEMSRAE EMSLQTAIER GLKEEAGHLT RELVREKEPL AIIQEQLIPA LDVVGKGFEK GTVFLPQLLM SAEAAKEAFA VLKEVLERSG QKEQKKGKVI LATVKGDIHD IGKNIVKVLL ENYSFDVIDL GKDVDPEVIV HTAKQEGIRL VGLSALMTTT VVSMEETIRL LREHCPDCKV MVGGAVLNPE YAEMIGADFY GKDAMQSVYY AQRVFA // ID E9SG66_RUMAL Unreviewed; 788 AA. AC E9SG66; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Putative methionine synthase {ECO:0000313|EMBL:EGC01716.1}; GN ORFNames=CUS_7787 {ECO:0000313|EMBL:EGC01716.1}; OS Ruminococcus albus 8. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus. OX NCBI_TaxID=246199 {ECO:0000313|EMBL:EGC01716.1}; RN [1] {ECO:0000313|EMBL:EGC01716.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=8 {ECO:0000313|EMBL:EGC01716.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGC01716.1}. 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; ADKM02000122; EGC01716.1; -; Genomic_DNA. DR RefSeq; WP_002851957.1; NZ_ADKM02000122.1. DR EnsemblBacteria; EGC01716; EGC01716; CUS_7787. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; SQ SEQUENCE 788 AA; 85610 MW; 2D31B1D4EB608CEF CRC64; MGFRELLKQK EFVILDGAMG TMLQAKGLKM GETPEVMNIE KPEWLMDIHR QYIEAGSDII YANTFGANRH KLAKSGFSVD KIIGEGIKLA RKAVEGTDTL VALDIGSIGQ MLEPTGTLTF EEAYDIFKEM VIAGREADLV VFETMTDLYE FKAAILAAKE NSDLPIMCTM TFEENMRTFT GVDISAMCLT AEGLGVDAVG VNCSLGPKEL YPVVEKICQW TNLPVVVKPN AGLPDPVTNE YNCSAEEFAE FAEALIPLGI KVIGGCCGTD PTYIACLKKM LDGKKCVQRN VHIPAVCCSA TDVVVIDQPR IIGERINPTG KKRFKQALLE GDIDYILGQA IEQIDAGADI LDVNVGLPAI DEKAMMVKAV KALQGVVDVP LQLDSTIPEV MEAALRVYNG KPIVNSVNAE EKSLNTVLPL VKKYGAAVVG LTLDENGIPK TADERFNLAK KILDRAMAIG IRKEDVYIDC LTLTASAEQE NVMQTVNAVR RVKEELGLRT VLGVSNISFG LPSREIVNHN FLMMCLTSGL DLPIMNPNIA SMTATVRTYK LLTNIDKNSV DFIAHYGGDT SSPMQKAEKK SDIDLPYAIE HGLKGEGAEI TAKLLETTDS MVIINEMLVP ALDKAGEQFE KGKIFLPQLI QTAGVAQACF EVIKQKMLAD GGNSVSKGKI ILATVKGDIH DIGKNIVKVL LENYGYEVID LGKDVDYQTV VDAAIENDVH LVGLSALMTT TLVSMEETIK LLRANNVDCK IMVGGAVVTP DYAEQIGADF YSKDAKQSVD IARQVFGN // ID E9T695_RHOHA Unreviewed; 1189 AA. AC E9T695; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EGD22082.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGD22082.1}; GN Name=metH {ECO:0000313|EMBL:EGD22082.1}; GN ORFNames=HMPREF0724_14301 {ECO:0000313|EMBL:EGD22082.1}; OS Rhodococcus equi ATCC 33707. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Nocardiaceae; Rhodococcus. OX NCBI_TaxID=525370 {ECO:0000313|EMBL:EGD22082.1, ECO:0000313|Proteomes:UP000004245}; RN [1] {ECO:0000313|EMBL:EGD22082.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33707 {ECO:0000313|EMBL:EGD22082.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGD22082.1}. 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; ADNW02000024; EGD22082.1; -; Genomic_DNA. DR RefSeq; WP_005513248.1; NZ_CM001149.1. DR EnsemblBacteria; EGD22082; EGD22082; HMPREF0724_14301. DR Proteomes; UP000004245; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000004245}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGD22082.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000004245}; KW Transferase {ECO:0000313|EMBL:EGD22082.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 229 229 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 296 296 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 739 739 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1189 AA; 130213 MW; E33DC776E2373E4D CRC64; MSAPFHSALL DALKQRVVIG DGAMGTMLQA ADLTLDDFLG LEGCNEILNE TRPDVLRDIH RAYFEAGADA VETNTFGCNL PNLADYDIAH RIRDLSERGT RIAREVADEM GPGRDGMGRF VLGSMGPGTK LPTLGHAPFA VLRDAYTESA LGMIEGGADA ILVETCQDLL QVKAAIIGSQ HAMEKLGRRL PIITHVTVET TGTMLLGSEI GAALTALEPL GIDMIGLNCA TGPDEMSEHL RHLSRHSKLP VSVMPNAGLP QLGPNGAEYP LSAEELAVAL SGFVSEFGLS FVGGCCGTTP EHIRQVADAV RRVEQAKRTP EPEDGTSSLY QAVPFDQDAS ILMIGERTNS NGSKAFREAM IAEDYQKCID IAKDQTRDGA HMLDLNVDYV GRDGAADMAA LASRFATAST LPIMLDSTEP EVLRAGLEHL GGRCAVNSVN YEDGDGPNSR YQRIMKLVKE HGAAVVALTI DEEGQARTAE HKVRIAERLI QDITTTWGLS QSDIIIDALT FPISTGQEEV RRDGIETIEA IREIKRRYPD VHFTLGISNI SFGLNPAARQ VLNSVFLHEC TEAGLDTAIV HASKILPMAR IPDEQRETAL DLVYDRRREG YDPLQKLMEL FEGVSAASAR ESRAEELAAL PLFERLERRI VDGERNGLEA DLDAAMVERP PLEIINETLL SGMKTVGELF GSGQMQLPFV LQSAEVMKAA VAYLEPHMES TGDEGKGRIV LATVKGDVHD IGKNLVDIIL SNNGYEVVNI GIKQPIATIL DVALDKKADV IGMSGLLVKS TVVMKENLEE LNAKGVAEQF PVLLGGAALT RSYVENDLSD VYQGEVSYAR DAFEGLHLMD TIMAVKRGEG PAPDSPEAIA AAEKAAERKA RHERSKRIAE KRKAESAPVE VPERSDVAAD IVVPSPPFWG TRIVKGIALA EYSGLLDERA LFLGQWGLRG QRAGDGPTYE ELVETEGRPR LRYWLDRLST EGVLQHAAVV YGYFPAVSEG DDVIVLESPD PDAPERFRFT FPRQQRDRFL CIADFVRSRD DARKDGQVDV LPMNLVTMGQ PIADFANELF AANSYRDYLE VHGIGVQLTE ALAEYWHRRV REELVLPGGH NLAEQDPSDV EDFFKLEYRG ARYSFGYGAC PDLEDRRKLV ALLEPERIGV ELSEEVQLHP EQSTDAFVLH HPEAKYFNV // ID E9T8Q9_ECOLX Unreviewed; 1227 AA. AC E9T8Q9; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EGB90362.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGB90362.1}; GN Name=metH {ECO:0000313|EMBL:EGB90362.1}; GN ORFNames=HMPREF9542_00138 {ECO:0000313|EMBL:EGB90362.1}; OS Escherichia coli MS 117-3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=749539 {ECO:0000313|EMBL:EGB90362.1}; RN [1] {ECO:0000313|EMBL:EGB90362.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 117-3 {ECO:0000313|EMBL:EGB90362.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGB90362.1}. 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; ADTS01000012; EGB90362.1; -; Genomic_DNA. DR RefSeq; WP_000096055.1; NZ_GG772801.1. DR EnsemblBacteria; EGB90362; EGB90362; HMPREF9542_00138. DR PATRIC; 47810290; VBIEscCol157132_0124. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGB90362.1}; KW Transferase {ECO:0000313|EMBL:EGB90362.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136068 MW; 71F76336C7330F7E CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAD // ID E9UYC1_9ACTO Unreviewed; 1237 AA. AC E9UYC1; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 01-APR-2015, entry version 25. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGD41891.1}; GN ORFNames=NBCG_03784 {ECO:0000313|EMBL:EGD41891.1}; OS Nocardioidaceae bacterium Broad-1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Nocardioidaceae. OX NCBI_TaxID=408672 {ECO:0000313|EMBL:EGD41891.1}; RN [1] {ECO:0000313|EMBL:EGD41891.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Broad-1 {ECO:0000313|EMBL:EGD41891.1}; 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] {ECO:0000313|EMBL:EGD41891.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Broad-1 {ECO:0000313|EMBL:EGD41891.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGD41891.1}. 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; ADVI01000062; EGD41891.1; -; Genomic_DNA. DR RefSeq; WP_008361270.1; NZ_GL873265.1. DR EnsemblBacteria; EGD41891; EGD41891; NBCG_03784. DR PATRIC; 46521216; VBINocBac160729_3795. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 765 765 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1237 AA; 135112 MW; C7F7891683F4FE54 CRC64; MSLRPDVTET LTATLKERIM VLDGAMGTAI QRDRPDEAGY RGERFKDWHV DLIGNNDLLN LTQPQIIEGI HREYLEAGAD IIETNTFNAN AVSLIDYDMV DLAYEINYEA ARLARAAADA YSTSDKPRYV AGALGPTSRT ASISPDVNDP GARNVTYEQL RDAYAEATRA LLEGGSDLIF IETIFDTLNA KAAIFGVQQV FEEYGRRWPV VISGTITDAS GRTLSGQVTE AFWDSVRHAE PLLVGLNCAL GAQEMRPYIA ELARVADAFV SCYPNAGLPN AFGEYDEGPS DTAGHIHEFA TAGFVNLVGG CCGTTPAHIA EIAKQVEAVA PRDVPEVEPA LRLSGLEPFS VTEESLFVNV GERTNITGSA KFRNLIKAGD YDTALSVAAQ QVENGAQVID VNMDEGMIDG VAAMTRFLTL IASEPDISRV PIMIDSSKWE VIEAGLKLVQ GKPIVNSISL KEGVESFVEH AELCKRYGAA AVVMAFDEDG QADSYERRIA VCERAYRILV DEVGFDPEDI IFDPNVFAVA TGIEEHATYG VDFIEAVRWI KQNLPGAKVS GGISNVSFSF RGNNPVREAI HAVFLYHAIE AGLDMGIVNA GALVPYSEVD PELRDRIEDV VLNRRADAAE RLLEIASKYN KDSPEAEAKA EAWRELPVGE RITHALVKGL DAYVEADTEE LRAEISARGG RPIEVIEGPL MDGMNVVGDL FGAGKMFLPQ VVKSARVMKK AVAYLIPFIE AEKQPGDAET KNGTIVMATV KGDVHDIGKN IVGVVLQCNN YEVIDLGVMV PAQKILDAAK EHDADIIGLS GLITPSLDEM VGFATEMQRV GLDLPLLIGG ATTSRAHTAV KIDKAYDGPV VWVKDASRSV PTAAALLDAG RREKLMAEVK VDYDSLRARH AERSERASLT YVQAKANKPE VDFSTLPVAP SQPGVHTLLE YPIAELRDYI DWQPFFNAWE MKGRFPDILN NPATGEAARK LFDDAQEMLD KIIEENWLEA RGVYGLFPAN STGEDVVVYT DDSRTEERAT LFQLRQQGQH REGVANKSLA DYVAPVGEGS DHVGAFAVTA GIGLPERVKA FKDDLDDYSA IMLEALADRL AEAFAERLHQ RVRTEFWGYA ADEGGDGKLP NEDLIAEKYA GIRPAPGYPA CPDHTEKQTI WSLLDVEKNT GIELTESMAM WPGASVSGIY YGHPDSQYFV VGRLGQDQVA DYARRKGWTM AEAERWLSPN LGYDPED // ID E9V1H4_9ACTO Unreviewed; 287 AA. AC E9V1H4; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 01-OCT-2014, entry version 14. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGD40824.1}; GN ORFNames=NBCG_04914 {ECO:0000313|EMBL:EGD40824.1}; OS Nocardioidaceae bacterium Broad-1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Nocardioidaceae. OX NCBI_TaxID=408672 {ECO:0000313|EMBL:EGD40824.1}; RN [1] {ECO:0000313|EMBL:EGD40824.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Broad-1 {ECO:0000313|EMBL:EGD40824.1}; 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] {ECO:0000313|EMBL:EGD40824.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Broad-1 {ECO:0000313|EMBL:EGD40824.1}; 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. {ECO:0000313|EMBL:EGD40824.1}. 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; ADVI01000099; EGD40824.1; -; Genomic_DNA. DR RefSeq; WP_008363009.1; NZ_GL873268.1. DR EnsemblBacteria; EGD40824; EGD40824; NBCG_04914. DR PATRIC; 46523537; VBINocBac160729_4935. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGD40824.1}; KW Transferase {ECO:0000313|EMBL:EGD40824.1}. SQ SEQUENCE 287 AA; 29718 MW; 24DAC6BBA4CEE902 CRC64; MVTILDGGLS NALEARGHDV SGALWTARLL DESPAEIAAV HRAYYAAGAD VATTASYQAS VPGFVEAGMT ETYATELLRR SVRIAREVAA EGPGRLVAAS VGPYGAYLAD GSEYRGRYGV SAATLRDFHA PRLALLETED PDLIAVETIP DIEEAEVLVD LLDDIGLPVW FSYSCAGTRT RAGQPLADAL ALAAGIRSVV AVGVNCCDPA DVPAAVQLAT ATGEPAVVYP NTGETYADGA WTGTPHFRPG EALSWVSSGA AYVGGCCRVG PAEIALIAAE LSHLQGE // ID E9XS21_ECOLX Unreviewed; 1227 AA. AC E9XS21; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGB70454.1}; GN ORFNames=ERFG_03869 {ECO:0000313|EMBL:EGB70454.1}; OS Escherichia coli TW10509. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=656449 {ECO:0000313|EMBL:EGB70454.1}; RN [1] {ECO:0000313|EMBL:EGB70454.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TW10509 {ECO:0000313|EMBL:EGB70454.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGB70454.1}. 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; AEHW01000026; EGB70454.1; -; Genomic_DNA. DR RefSeq; WP_000096041.1; NZ_GL872205.1. DR EnsemblBacteria; EGB70454; EGB70454; ERFG_03869. DR PATRIC; 48022240; VBIEscCol161062_4060. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136026 MW; 3B764CF6D3962EA2 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID E9YKI9_ECOLX Unreviewed; 1227 AA. AC E9YKI9; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGB65049.1}; GN ORFNames=ERHG_04166 {ECO:0000313|EMBL:EGB65049.1}; OS Escherichia coli TA007. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=656429 {ECO:0000313|EMBL:EGB65049.1}; RN [1] {ECO:0000313|EMBL:EGB65049.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TA007 {ECO:0000313|EMBL:EGB65049.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGB65049.1}. 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; AEHY01000112; EGB65049.1; -; Genomic_DNA. DR RefSeq; WP_000095995.1; NZ_GL872117.1. DR ProteinModelPortal; E9YKI9; -. DR SMR; E9YKI9; 651-1227. DR EnsemblBacteria; EGB65049; EGB65049; ERHG_04166. DR PATRIC; 48044189; VBIEscCol162956_4378. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135983 MW; 7250C9EE48BA453B CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LSFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAD // ID E9YWJ1_ECOLX Unreviewed; 1227 AA. AC E9YWJ1; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGB61132.1}; GN ORFNames=ERJG_02903 {ECO:0000313|EMBL:EGB61132.1}; OS Escherichia coli M863. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=656420 {ECO:0000313|EMBL:EGB61132.1}; RN [1] {ECO:0000313|EMBL:EGB61132.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M863 {ECO:0000313|EMBL:EGB61132.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGB61132.1}. 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; AEHZ01000049; EGB61132.1; -; Genomic_DNA. DR RefSeq; WP_000096046.1; NZ_GL872045.1. DR EnsemblBacteria; EGB61132; EGB61132; ERJG_02903. DR PATRIC; 48052759; VBIEscCol163215_3031. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136070 MW; 89BFE38E1C7F3E7E CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG EEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID F0BF42_9XANT Unreviewed; 320 AA. AC F0BF42; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 11. DE SubName: Full=Homocysteine/selenocysteine methylase (S-methylmethionine-dependent) {ECO:0000313|EMBL:EGD08900.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EGD08900.1}; GN ORFNames=XVE_2822 {ECO:0000313|EMBL:EGD08900.1}; OS Xanthomonas vesicatoria ATCC 35937. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=925775 {ECO:0000313|EMBL:EGD08900.1}; RN [1] {ECO:0000313|EMBL:EGD08900.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35937 {ECO:0000313|EMBL:EGD08900.1}; 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. {ECO:0000313|EMBL:EGD08900.1}. 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; AEQV01000097; EGD08900.1; -; Genomic_DNA. DR RefSeq; WP_005993609.1; NZ_AEQV01000097.1. DR PATRIC; 46606324; VBIXanVes179409_2704. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGD08900.1}; KW Transferase {ECO:0000313|EMBL:EGD08900.1}. SQ SEQUENCE 320 AA; 33960 MW; 69462B577EDAEC03 CRC64; MTILPRQPRA DAPFSAALQH EGYVLLDGAL ATELEQRGCD LNDALWSARV LMEQPELIYQ VHRDYFAAGA QCAITASYQA TPLGFAARGL DLAQSQALIA RSVALAAQAR DDHLQAQPDA APLWVAGSVG PYGAYLADGS EYRGDYALPL AQLMEFHRPR IAALAAAGVD VLACETLPSA NEIVALRLLL EEFPHLHAWF SFTLRDADHL SDGTPLAHVI PALDACAQVI AVGINCIALD QVTAALQSLS ALTTLPLVVY PNSGEHYDAG DKRWHGGNAP GCSLADQHTR WLAAGARLIG GCCRTTPRDI AALAAARAVG // ID F0BLB3_9XANT Unreviewed; 379 AA. AC F0BLB3; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:EGD06735.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGD06735.1}; GN ORFNames=XVE_5087 {ECO:0000313|EMBL:EGD06735.1}; OS Xanthomonas vesicatoria ATCC 35937. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=925775 {ECO:0000313|EMBL:EGD06735.1}; RN [1] {ECO:0000313|EMBL:EGD06735.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35937 {ECO:0000313|EMBL:EGD06735.1}; 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. {ECO:0000313|EMBL:EGD06735.1}. 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; AEQV01000294; EGD06735.1; -; Genomic_DNA. DR RefSeq; WP_005998475.1; NZ_AEQV01000294.1. DR PATRIC; 46610871; VBIXanVes179409_4790. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGD06735.1}; KW Transferase {ECO:0000313|EMBL:EGD06735.1}. SQ SEQUENCE 379 AA; 40451 MW; EEA7DB46ECA0C44F CRC64; MTPAAIPNPP SPIPFSLPWL HPERAAKLTA ALRERILIID GAMGTMIQRH DLQEPDYRGT RFAAGYDSAH VHGPGCDHAH APEGHDLKGN NDLLLLTRPE IIAGIHRAYL DAGADLLETN TFNATSVSQA DYHLEHLVYE LNKAGAQVAR ACCDEVEALT PHKPRFVIGV LGPTSRTASI SPDVNDPGYR NTSFDALRQT YREAIEGLID GGADTLMVET IFDTLNAKAA LYAIEEVFET RGGRLPVMIS GTITDASGRT LSGQTAEAFY ASVAHGRPLS VGLNCALGAK DLRPHVETLA QIADGYVSAH PNAGLPNAFG EYDETPEEMA QTLREFAQAG LLNLVGGCCG TSPDHIRAIA EAVADLSPRQ LPGAQELAA // ID F0BW29_9XANT Unreviewed; 376 AA. AC F0BW29; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:EGD12867.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGD12867.1}; DE Flags: Precursor; GN ORFNames=XPE_3566 {ECO:0000313|EMBL:EGD12867.1}; OS Xanthomonas perforans 91-118. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=925776 {ECO:0000313|EMBL:EGD12867.1}; RN [1] {ECO:0000313|EMBL:EGD12867.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=91-118 {ECO:0000313|EMBL:EGD12867.1}; 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. {ECO:0000313|EMBL:EGD12867.1}. 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; AEQW01000198; EGD12867.1; -; Genomic_DNA. DR RefSeq; WP_008576539.1; NZ_AEQW01000198.1. DR EnsemblBacteria; EGD12867; EGD12867; XPE_3566. DR PATRIC; 46618266; VBIXanPer180062_3434. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGD12867.1}; KW Signal {ECO:0000313|EMBL:EGD12867.1}; KW Transferase {ECO:0000313|EMBL:EGD12867.1}. FT SIGNAL 1 22 Potential. {ECO:0000313|EMBL:EGD12867.1}. FT CHAIN 23 376 Potential. {ECO:0000313|EMBL:EGD12867.1}. FT /FTId=PRO_5000710645. SQ SEQUENCE 376 AA; 40059 MW; 0612EF2B6949141E CRC64; MTPAALHSPV AHALPWLRPE RAAKLTAALA ERILIIDGAM GTMIQRHDLQ EPDYRGTRFA EGYDSAHVHG PGCDHAHVPQ GHDLKGNNDL LLLTRPEIIA GIHRAYLDAG ADLLETNTFN ATSVSQADYH LEHLVYELNK AGAQVARACC DEVEALTPHK PRFVIGVLGP TSRTASISPD VNDPGYRNTS FDALRETYRE AIEGLIDGGA DTLMVETIFD TLNAKAALYA IEEVFEARGG RLPVMVSGTI TDASGRTLSG QTAEAFYASV AHGRPLSIGL NCALGAKDLR PHVETLAQIA DAYVSAHPNA GLPNAFGEYD ETPEEMASTL REFAQAGLLN LVGGCCGTSP DHIRAIAEAV ADLPPRQLPG APELAA // ID F0BZF0_9XANT Unreviewed; 321 AA. AC F0BZF0; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 12. DE SubName: Full=Homocysteine/selenocysteine methylase (S-methylmethionine-dependent) {ECO:0000313|EMBL:EGD11709.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EGD11709.1}; GN ORFNames=XPE_4795 {ECO:0000313|EMBL:EGD11709.1}; OS Xanthomonas perforans 91-118. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=925776 {ECO:0000313|EMBL:EGD11709.1}; RN [1] {ECO:0000313|EMBL:EGD11709.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=91-118 {ECO:0000313|EMBL:EGD11709.1}; 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. {ECO:0000313|EMBL:EGD11709.1}. 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; AEQW01000284; EGD11709.1; -; Genomic_DNA. DR RefSeq; WP_008578257.1; NZ_AEQW01000284.1. DR EnsemblBacteria; EGD11709; EGD11709; XPE_4795. DR PATRIC; 46620785; VBIXanPer180062_4604. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGD11709.1}; KW Transferase {ECO:0000313|EMBL:EGD11709.1}. SQ SEQUENCE 321 AA; 34071 MW; 8992C28D3DFDFC20 CRC64; MTILPRQPRA NAPFSQALQH DGYVVLDGAL ATELEQRGCD LNDALWSARV LMEQPELIYQ VHRDYFAAGA QCAITASYQA TPLGFAARGL DAAQAQALIA RSVALAAQAR ADHLTLHPYA APLWVAGSVG PYGAYLADGS EYRGDYVLPI EQLMDFHRPR IAALAEAGVD LLACETLPSA SEIVALRQLL QHEFPQLHAW FSFTLRDAAH LSDGTPLAQV VPALDACAQV IAVGINCIAL DQASAALHSL AALTALPLVV YPNSGEHYDA SDKRWHAGHG AALTLADQHA HWLAAGARLI GGCCRTAPRD IAALAAARAL G // ID F0C4V3_9XANT Unreviewed; 320 AA. AC F0C4V3; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 11. DE SubName: Full=Homocysteine/selenocysteine methylase (S-methylmethionine-dependent) {ECO:0000313|EMBL:EGD19457.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EGD19457.1}; GN ORFNames=XGA_1905 {ECO:0000313|EMBL:EGD19457.1}; OS Xanthomonas gardneri ATCC 19865. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=925777 {ECO:0000313|EMBL:EGD19457.1}; RN [1] {ECO:0000313|EMBL:EGD19457.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 19865 {ECO:0000313|EMBL:EGD19457.1}; 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. {ECO:0000313|EMBL:EGD19457.1}. 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; AEQX01000182; EGD19457.1; -; Genomic_DNA. DR RefSeq; WP_006450219.1; NZ_AEQX01000182.1. DR EnsemblBacteria; EGD19457; EGD19457; XGA_1905. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGD19457.1}; KW Transferase {ECO:0000313|EMBL:EGD19457.1}. SQ SEQUENCE 320 AA; 34087 MW; 48DCA90EE582DE58 CRC64; MTILPRRPRA DAPFSQALQH DGYVLLDGAL ATELEQRGCD LNDALWSARV LMEQPELIYQ VHRDYFAAGA QCAITASYQA TPLGFAARGL DLAQSQALIA RSVALAAQAR TDHLQSQPQA APLWVAGSVG PYGAYLADGS EYRGDYALPL AQLMDFHRPR IAALADAGVD LLACETLPSA NEIVALRLLL EEFPQLHAWF SFTLRDAAHL SDGTPLAQVI PALDACKQVI AVGINCIALE HVTAALQTLS ALTALPLVVY PNSGEHYDAG DKRWHAGSTT ACSLADQHAQ WLAAGARLIG GCCRTTPRDI AALAAARAAC // ID F0C5M2_9XANT Unreviewed; 377 AA. AC F0C5M2; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:EGD19189.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGD19189.1}; GN ORFNames=XGA_2185 {ECO:0000313|EMBL:EGD19189.1}; OS Xanthomonas gardneri ATCC 19865. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=925777 {ECO:0000313|EMBL:EGD19189.1}; RN [1] {ECO:0000313|EMBL:EGD19189.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 19865 {ECO:0000313|EMBL:EGD19189.1}; 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. {ECO:0000313|EMBL:EGD19189.1}. 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; AEQX01000205; EGD19189.1; -; Genomic_DNA. DR RefSeq; WP_006450495.1; NZ_AEQX01000205.1. DR EnsemblBacteria; EGD19189; EGD19189; XGA_2185. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGD19189.1}; KW Transferase {ECO:0000313|EMBL:EGD19189.1}. SQ SEQUENCE 377 AA; 40443 MW; AD03AAB6FE599F7B CRC64; MTSAQLPTPP IPFSLPWLHP ERAEKLRAAL RERILIIDGA MGTMIQRHDL QEPDYRGTRF ADGYDSAQVH VHGPGCDHAP QSHDLKGNND LLLLSSPEII SGIHRAYLDA GADLLETNTF NATSVSQADY HLEHLVYELN KAGAQVARAC CDEVEALTPH KPRFVIGVLG PTSRTASISP DVNDPGYRNT SFDALRETYR EAIDGLIDGG ADTLMVETIF DTLNAKAALY AIEEVFEARG GRLPVMISGT ITDASGRTLS GQTAEAFYAS VAHGRPLSVG LNCALGAKDL RPHVETLSQI ADAYVSAHPN AGLPNAFGEY DESPEETAAT LREFAQAGLL NLVGGCCGTS PDHIRAIAEA VADLPPRRLP SAYEQAA // ID F0EBP0_PSEDT Unreviewed; 1235 AA. AC F0EBP0; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 01-APR-2015, entry version 24. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EGB96161.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGB96161.1}; GN Name=metH {ECO:0000313|EMBL:EGB96161.1}; GN ORFNames=G1E_25009 {ECO:0000313|EMBL:EGB96161.1}; OS Pseudomonas sp. (strain TJI-51). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=985010 {ECO:0000313|EMBL:EGB96161.1}; RN [1] {ECO:0000313|EMBL:EGB96161.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TJI-51 {ECO:0000313|EMBL:EGB96161.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGB96161.1}. 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; AEWE01000865; EGB96161.1; -; Genomic_DNA. DR RefSeq; WP_009685909.1; NZ_AEWE01000865.1. DR EnsemblBacteria; EGB96161; EGB96161; G1E_25009. DR PATRIC; 46730915; VBIPseSp184914_4144. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGB96161.1}; KW Transferase {ECO:0000313|EMBL:EGB96161.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1235 AA; 135187 MW; 4F6A1147261E8D19 CRC64; MSDRSARLQA LQNALKERIL ILDGGMGTMI QSYRLEEHDY RGTRFADWPS DVKGNNDLLL LSRPDVIAAI EKAYLDAGAD ILETNTFNAT QISQADYGME SLVYELNVEG ARIARQVADA KTLETPDKPR FVAGVLGPTS RTCSISPDVN DPGYRNVTFD ELVVNYVEAT RGLIEGGADL ILIETIFDTL NAKAAIFAVQ QVFEEDSIEL PIMISGTITD ASGRTLSGQT TEAFWNSVRH AKPISVGLNC ALGAKDLRPY LEELSTKADT HVSAHPNAGL PNAFGEYDES PAEMAAVVEE FAASGFLNII GGCCGTTPGH IQAIAEAVAK YPPREIPEIA KACRLSGLEP FTIDRQSLFV NVGERTNITG SAKFARLIRE ENYTEALEVA LQQVEAGAQV IDINMDEGML DSQAAMVRFL NLIAGEPDIS RVPIMIDSSK WEVIEAGLKC IQGKGIVNSI SMKEGVEQFK HHARLCKRYG AAVVVMAFDE VGQADTAARK KEICQRSYDI LVNEVGFPPE DIIFDPNIFA VATGIEEHNN YAVDFIEACA YIRDHLPHAL SSGGVSNVSF SFRGNNPVRE AIHSVFLYHA IQNGLTMGIV NAGQLEIYDE IPAALREKVE DVVLNRTPHG TDALLAIAED YRGGGATKEV ENEEWRSLPV EKRLEHALVK GITAFIVEDT EACRQQCARP IEVIEGPLMN GMNVVGDLFG AGKMFLPQVV KSARVMKQAV AHLIPFIEAE KGDKPEAKGK ILMATVKGDV HDIGKNIVGV VLGCNGYDIV DLGVMVPAEK ILQTARDEKC DIIGLSGLIT PSLDEMVHVA REMQRQGFTL PLMIGGATTS KAHTAVKIEP KYSNDAVVYV TDASRAVGVA TQLLSRELKP GFIERTRQEY VEVRERTANR SARTERLSYA QAIAAKPQYD WAGYQPAVPS FTGVKVLEDI DLRTLAEYID WTPFFISWDL AGKFPRILTD EVVGEAATAL YNDAREMLDK LIDEKLISAR AVFGFWPANQ VADDDIEVYG ADGQTLATLH HLRQQTIKPD GKANWSLADF VAPKGSGVTD YVGGFITTAG IGAEEVAKAY QDKGDDYSSI MVKALADRLA EACAEWLHEQ VRKEHWGYAR DEQLDNEALI KEQYRGIRPA PGYPACPDHT EKETLFRLLD GTAIGETGPS GVFLTEHFAM FPAAAVSGWY FAHPQAQYFA VGKVDKDQIE CYSARKGQDV SVSERWLAPN LGYDS // ID F0EC67_PSEDT Unreviewed; 287 AA. AC F0EC67; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 04-MAR-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EGB96000.1}; GN ORFNames=G1E_25926 {ECO:0000313|EMBL:EGB96000.1}; OS Pseudomonas sp. (strain TJI-51). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=985010 {ECO:0000313|EMBL:EGB96000.1}; RN [1] {ECO:0000313|EMBL:EGB96000.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TJI-51 {ECO:0000313|EMBL:EGB96000.1}; 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. {ECO:0000313|EMBL:EGB96000.1}. 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; AEWE01000904; EGB96000.1; -; Genomic_DNA. DR EnsemblBacteria; EGB96000; EGB96000; G1E_25926. DR PATRIC; 46731249; VBIPseSp184914_4290. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGB96000.1}; KW Transferase {ECO:0000313|EMBL:EGB96000.1}. SQ SEQUENCE 287 AA; 30391 MW; AB14A67B002058FE CRC64; MGRELQRSGA PFRQPEWSAL ALTEAPEAVV GVHAAFIAAG AQVITSNSYA VVPFHIGEQR FATEGQQLAN TAGQLARHAA DNAAHPVKVA GSLPPLFGSY RPDLFQPERV EEVLKPLLAG LAPHVDLWLA ETQSAIAEVR AIHAHLPEDG RPFWVSFTLQ DEDVDTVPRL RSGEPVADAV QAVVGLGAAA VLFNCSQPEV IGAAIDVARA VIDKQGAGVA IGAYANAFPP QPKEATANDG LDELREDLDP PGYLAWAKDW RERGASMVGG CCGIGPEHIA ELKRNLG // ID F0EVH0_HAEPA Unreviewed; 1230 AA. AC F0EVH0; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EGC71536.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGC71536.1}; GN Name=metH {ECO:0000313|EMBL:EGC71536.1}; GN ORFNames=HMPREF9417_1864 {ECO:0000313|EMBL:EGC71536.1}; OS Haemophilus parainfluenzae ATCC 33392. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=888828 {ECO:0000313|EMBL:EGC71536.1, ECO:0000313|Proteomes:UP000005577}; RN [1] {ECO:0000313|EMBL:EGC71536.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33392 {ECO:0000313|EMBL:EGC71536.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGC71536.1}. 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; AEWU01000021; EGC71536.1; -; Genomic_DNA. DR RefSeq; WP_005696828.1; NZ_GL872339.1. DR EnsemblBacteria; EGC71536; EGC71536; HMPREF9417_1864. DR EnsemblBacteria; KFL98991; KFL98991; HMPREF9953_1883. DR PATRIC; 46751859; VBIHaePar172879_1393. DR Proteomes; UP000005577; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005577}; KW Methyltransferase {ECO:0000313|EMBL:EGC71536.1}; KW Transferase {ECO:0000313|EMBL:EGC71536.1}. SQ SEQUENCE 1230 AA; 136358 MW; 8E2D8545D9752809 CRC64; MSHNQTELLK KSLAERILIL DGAMGTMIQK YKLTEADFRG ERFKESAVDL RGNNDLLTLT QPLLISAIHE KYLQAGADII ETNTFSSTTI AQADYDLQSI AYELNFAGAK LARLAADKYS TPEKPRFVAG VLGPTNRTAS ISPDVNDPGF RNVTFMELVD AYAEATKGLI EGSADLIMIE TIFDTLNAKA AIFAIETVFE ELGVELPIMI SGTITDASGR TLSGQTTEAF YNSLRHAKPL TFGLNCALGP KELRQYVEQL SKISETYVSV HPNAGLPNAF GGYDLGAEEM AAHLKEWAES GFVNIVGGCC GTTPEHIKAF ADAMQGIAPR KLPEIKTAMR LSGLEPLNID DESLFVNVGE RNNVTGSAKF KRLIKEDKFA EAIEIAIDQV ENGAQVIDVN MDEALLDGKK CMTRFLNIMA TEPDAAKVPV MIDSSKWEVI EAGLQSVQGK PIVNSISLKE GEEIFIDHAK LVRKYGAAVV VMAFDEVGQA DTEDRKVEIC SRAYDILVNQ VGFPPEDIIF DPNIFAIGTG IEEHNNYGVD FINATGRIKR ALPHAKISGG VSNVSFSFRG NNVMREAIHA VFLYHAIKQG MDMGIVNAGQ LAIYDDLDPE LREIVEDAVL NRSPDATEKL LDIAEKYRNQ GNDESAVDSV AEWRTWPVEE RLKHALVKGI TTHIIEDTEE ARQKLPTPLE VIEGPLMAGM DVVGDLFGDG KMFLPQVVKS ARVMKQSVAY LEPFINATKQ KGSSNGKVVI ATVKGDVHDI GKNIVSVVLQ CNNFEVIDLG VMVPADKIIQ TAIDEKADLI GLSGLITPSL DEMEYFLGEM TRLGLNLPVL IGGATTSKEH TAIKLYPKYK QHGVFYTSNA SRAVTVCATL MNPEGRTALW EQFKKDYEKI QQSFSNRKPL RKQLSIKEAR ANRFDGFNGE WADYVPPTPK QTGIVEFKNV PIAELRKFID WSPFFRVWGL MGGYPDAFDH PESGEEARRV WNDAQAMLDA FEQNHKLNPS GVLGIFPAER VGDDVVLFSD EDRTQPIGTA YGLRQQTERG KNSKSQFNFA LSDFIADRES GKKDWMGMFA VCAGTEEMDL VEGYKAAGDD YNAILLQAVG DRLAEAMAEY LHFELRTRIW GYTQEEFDNQ GLINENYVGI RPAPGYPSCP EHTEKALIWD LLEVEQRIGM KLTESYAMWP AASVCGWYFT HPASNYFTLG RIDEDQAQDY AKRKGWDERE MMKWLGVAMK // ID F0FDI8_STRSA Unreviewed; 315 AA. AC F0FDI8; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGC23158.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EGC23158.1}; GN Name=mmuM {ECO:0000313|EMBL:EGC23158.1}; GN ORFNames=HMPREF9388_0770 {ECO:0000313|EMBL:EGC23158.1}; OS Streptococcus sanguinis SK353. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=888815 {ECO:0000313|EMBL:EGC23158.1}; RN [1] {ECO:0000313|EMBL:EGC23158.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK353 {ECO:0000313|EMBL:EGC23158.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGC23158.1}. 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; AEWY01000003; EGC23158.1; -; Genomic_DNA. DR RefSeq; WP_002897633.1; NZ_GL872307.1. DR EnsemblBacteria; EGC23158; EGC23158; HMPREF9388_0770. DR PATRIC; 53460383; VBIStrSan169859_0752. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGC23158.1}; KW Transferase {ECO:0000313|EMBL:EGC23158.1}. SQ SEQUENCE 315 AA; 34733 MW; F820A09183302F3A CRC64; MGKFKDLLGK QEIIILDGAL GTELESLGYD VSGKLWSAQY LLDQPQIIQD VHESYVRADS DIITTSSYQA SIPVFIEAGL TPEKAYDLLK ETVFLAQKAI ENTWQALSPE EQKQRPYPLV AGSVGPYAAY LADGSEYTGD YQLSEEEYRD FHRPRIQALL EAGSDLLAIE TIPNGAEAAA ILRLLAEEFP QAEAYLSFVA QSENAISDGT KIEELGNLAQ ESPQVLAVGF NCTAPHLITP LLDGLGQVCN KPFLTYPNSG ETYNGLTKTW HDDPEQERSL LENSKLWQNQ GVRLFGGCCR TRPEDITQLA RGLKG // ID F0FRB3_STRSA Unreviewed; 315 AA. AC F0FRB3; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGC27624.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EGC27624.1}; GN Name=mmuM {ECO:0000313|EMBL:EGC27624.1}; GN ORFNames=HMPREF9392_1210 {ECO:0000313|EMBL:EGC27624.1}; OS Streptococcus sanguinis SK678. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=888819 {ECO:0000313|EMBL:EGC27624.1, ECO:0000313|Proteomes:UP000003133}; RN [1] {ECO:0000313|EMBL:EGC27624.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK678 {ECO:0000313|EMBL:EGC27624.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGC27624.1}. 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; AEXA01000005; EGC27624.1; -; Genomic_DNA. DR RefSeq; WP_002900424.1; NZ_GL872319.1. DR EnsemblBacteria; EGC27624; EGC27624; HMPREF9392_1210. DR PATRIC; 53470426; VBIStrSan174340_1190. DR Proteomes; UP000003133; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000003133}; KW Methyltransferase {ECO:0000313|EMBL:EGC27624.1}; KW Transferase {ECO:0000313|EMBL:EGC27624.1}. SQ SEQUENCE 315 AA; 34600 MW; AD490EAB905F98C0 CRC64; MGKFKDLLDK QEIIILDGAL GTELESLGYD VSGKLWSAQY LLDQPQIIQD VHESYVRAGS DIITTSSYQA SIPAFIEAGL TPEKGYNLLK ETVFLAQKAI ENVWTGLSPE EQKQRPYPLV AGSVGPYAAY LADGSEYTGD YQLSEEEFRD FHRPRIQALL EAGSDLLAIE TIPNGAEAAA ILRLLAEEFP QAEAYLSFVA QSENAISDGT KIEELGNLAQ ESPQVLAVGF NCTAPHLIAP LLDVLGQVCN KPFLTYPNSG ETYNGLTKTW HDDPEQERSL LENSKLWQEQ GVQLFGGCCR TRPEDIAQLA RGLKG // ID F0GE85_9BURK Unreviewed; 356 AA. AC F0GE85; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGD00197.1}; GN ORFNames=B1M_32797 {ECO:0000313|EMBL:EGD00197.1}; OS Burkholderia sp. TJI49. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=987057 {ECO:0000313|EMBL:EGD00197.1}; RN [1] {ECO:0000313|EMBL:EGD00197.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TJI49 {ECO:0000313|EMBL:EGD00197.1}; 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] {ECO:0000313|EMBL:EGD00197.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TJI49 {ECO:0000313|EMBL:EGD00197.1}; 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. {ECO:0000313|EMBL:EGD00197.1}. 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; AEXE01002011; EGD00197.1; -; Genomic_DNA. DR EnsemblBacteria; EGD00197; EGD00197; B1M_32797. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 356 AA; 38112 MW; 54A3B8AD7872EFB0 CRC64; MSASPLAASA APLDASYTRG AELPALLKSR ILILDGAMGT MIQRYKLDEA AYRGERFKDF ARDIKGNNEL LSITQPQVIR EIHDQYFAAG ADIVETNTFG ATTVAQADYG MEDLVVEMNV ASAKLARESA AKYATPDKPR FVAGAIGPTP KTASISPDVN DPGARNVTFD ELRAAYYQQA KALLDGGVDL FLVETIFDTL NAKAALFALD ELFEDTGERL PIMISGTVTD ASGRILSGQT VEAFWNSLRH AKPLTFGLNC ALGAALMRPY IAELAKLCDT YVSCYPNAGL PNPMAETGFD ETPDVTSGLL KEFAQAGLVN LAGGCCGTTP EHIAEIAKAL ADVKPRRWPS QYGNDA // ID F0HS85_9ACTN Unreviewed; 300 AA. AC F0HS85; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Conserved domain protein {ECO:0000313|EMBL:EGC88016.1}; GN ORFNames=HMPREF9404_5831 {ECO:0000313|EMBL:EGC88016.1}; OS Eggerthella sp. HGA1. OC Bacteria; Actinobacteria; Coriobacteridae; Coriobacteriales; OC Coriobacterineae; Coriobacteriaceae; Eggerthella. OX NCBI_TaxID=910311 {ECO:0000313|EMBL:EGC88016.1, ECO:0000313|Proteomes:UP000006450}; RN [1] {ECO:0000313|EMBL:EGC88016.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HGA1 {ECO:0000313|EMBL:EGC88016.1}; 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. {ECO:0000313|EMBL:EGC88016.1}. 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; AEXR01000039; EGC88016.1; -; Genomic_DNA. DR RefSeq; WP_009609446.1; NZ_AEXR01000039.1. DR EnsemblBacteria; EGC88016; EGC88016; HMPREF9404_5831. DR PATRIC; 46789528; VBIEggSp172060_2807. DR Proteomes; UP000006450; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006450}. SQ SEQUENCE 300 AA; 31671 MW; 81831A2FE3F06721 CRC64; MPDIALRFHK DMLVLSSPVA VVLARQGFDV EHDLEFANLV EPEAVRDALR LNKMAGAQCL VANTEGIAPA RLAHRGMEDR AAEIVRTGLS LARELKSQHV LVEIGPCGLP LDAASKSSLN ENRDQYARAA HACDGQEFDA FFLNGFANPA DLKCALMGVR QVSGAPVFAS VDVDADGMLA DGRHTLEDAL AVMVDYEASV VGFATAAPLD AAVTFARRAS GAGRLPVLAQ LIVREHNPKQ GDVTHENPYY CPDVLVGAAV QLRAAGAQFL RAAGAATPAY AGALAAASEG FDVVRSDVEE // ID F0HWV2_LACDL Unreviewed; 319 AA. AC F0HWV2; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 01-OCT-2014, entry version 12. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGD26957.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EGD26957.1}; GN Name=mmuM {ECO:0000313|EMBL:EGD26957.1}; GN ORFNames=HMPREF5505_1399 {ECO:0000313|EMBL:EGD26957.1}; OS Lactobacillus delbrueckii subsp. lactis DSM 20072. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=888027 {ECO:0000313|EMBL:EGD26957.1}; RN [1] {ECO:0000313|EMBL:EGD26957.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 20072 {ECO:0000313|EMBL:EGD26957.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGD26957.1}. 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; AEXU01000116; EGD26957.1; -; Genomic_DNA. DR EnsemblBacteria; EGD26957; EGD26957; HMPREF5505_1399. DR PATRIC; 53488455; VBILacDel173930_1267. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGD26957.1}; KW Transferase {ECO:0000313|EMBL:EGD26957.1}. SQ SEQUENCE 319 AA; 34210 MW; 9EBE10B73081CF90 CRC64; MITHYGGKTM ADLPTLLTQG PVTLDGSMST PLEAWGEDTN SDLWTAKALA DNPDLVYRVH QEYFKAGARV TITDSYQASL SAFMKHGLSE DAARGLIRES AAVAIKARDD FEKATGIHNF VAGSVGPYGA YLADGSEYRG DYALSHEEYV DFHAPRIEEL VAGGVDCLAV ETQPKLSEVR AILDHLKAKY PDLPVYVSFS LKDPATISEG LPLTEAVEEV SAYAQVFAAG ANCFKLAWTV DVVKNLRASK LPIVVYPNSG AEYDPSVKKW VYPPEAADFG QAGADWLAAG AKLVGGCCTT MPEDIAGLAA AVKKVYTAF // ID F0I1W0_STRSA Unreviewed; 315 AA. AC F0I1W0; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGD29419.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EGD29419.1}; GN Name=mmuM {ECO:0000313|EMBL:EGD29419.1}; GN ORFNames=HMPREF9381_0932 {ECO:0000313|EMBL:EGD29419.1}; OS Streptococcus sanguinis SK72. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=888809 {ECO:0000313|EMBL:EGD29419.1}; RN [1] {ECO:0000313|EMBL:EGD29419.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK72 {ECO:0000313|EMBL:EGD29419.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGD29419.1}. 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; AEXV01000007; EGD29419.1; -; Genomic_DNA. DR RefSeq; WP_002904441.1; NZ_GL872376.1. DR EnsemblBacteria; EGD29419; EGD29419; HMPREF9381_0932. DR PATRIC; 53491538; VBIStrSan171123_0914. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGD29419.1}; KW Transferase {ECO:0000313|EMBL:EGD29419.1}. SQ SEQUENCE 315 AA; 34610 MW; 6D38EEF800C3E14C CRC64; MGKFKDLLEK QEIIILDGAL GTELESLGYD VSGKLWSAQY LLDQPQIIQD VHESYVRAGS DIITTSSYQA SISAFIEAGL TPEKGYDFLK ETAFLAKKAI ENVWQALSPE EQKQRPYPLV AGSVGPYAAY LADGSEYTGD YQLSEEEFQE FHRPRIQALL EAGCDLLAIE TIPNGAEAAA ILRLLAEEFP QAEAYLSFVA QSETAISDGT KIEDLGNLAQ KSPQVLAVGF NCTAPHLISP LLDGLGQVCN KTFLTYPNSG ETYNGLTKTW HDDPEQERSL LENSKLWQEQ GVQLFGGCCR TRPEDIAQLA KGFKG // ID F0I7T6_STRSA Unreviewed; 315 AA. AC F0I7T6; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGD31771.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EGD31771.1}; GN Name=mmuM {ECO:0000313|EMBL:EGD31771.1}; GN ORFNames=HMPREF9382_0725 {ECO:0000313|EMBL:EGD31771.1}; OS Streptococcus sanguinis SK115. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=888810 {ECO:0000313|EMBL:EGD31771.1}; RN [1] {ECO:0000313|EMBL:EGD31771.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK115 {ECO:0000313|EMBL:EGD31771.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGD31771.1}. 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; AEXW01000005; EGD31771.1; -; Genomic_DNA. DR RefSeq; WP_002906632.1; NZ_GL872408.1. DR EnsemblBacteria; EGD31771; EGD31771; HMPREF9382_0725. DR PATRIC; 53495850; VBIStrSan174933_0706. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGD31771.1}; KW Transferase {ECO:0000313|EMBL:EGD31771.1}. SQ SEQUENCE 315 AA; 34657 MW; EE376F5DC44C77A5 CRC64; MGKFKDLLDK QEIIILDGAL GTELESLGYD VSGKLWSAQY LLDQPQIIQD MHESYVRAGS DIITTSSYQA SIPAFIEAGL TSEKGYDLLK ETVFLAQKAI ENVWTGLSPE EQKQRPCPLV AGSVGPYAAY LADGSEYTGN YQLSEEEYRD FHRPRIQALL EAGSDLLAIE TIPNGAEAAA ILRLLTEEFP QAETYLSFVA QSENAISDGT KIEELGNLAQ ESPQVLAVGF NCTAPHLIAP LLDALGQVCN KPFLTYPNSG ETYNGLTKTW HDDPEQERSL LENSKLWQNQ GVRLFGGCCR TRPEDIAQLA RGFKG // ID F0IML7_STRSA Unreviewed; 315 AA. AC F0IML7; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGD36487.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EGD36487.1}; GN Name=mmuM {ECO:0000313|EMBL:EGD36487.1}; GN ORFNames=HMPREF9383_1370 {ECO:0000313|EMBL:EGD36487.1}; OS Streptococcus sanguinis SK150. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=888811 {ECO:0000313|EMBL:EGD36487.1}; RN [1] {ECO:0000313|EMBL:EGD36487.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK150 {ECO:0000313|EMBL:EGD36487.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGD36487.1}. 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; AEXY01000013; EGD36487.1; -; Genomic_DNA. DR RefSeq; WP_002909819.1; NZ_GL872442.1. DR EnsemblBacteria; EGD36487; EGD36487; HMPREF9383_1370. DR PATRIC; 53501804; VBIStrSan172741_1350. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGD36487.1}; KW Transferase {ECO:0000313|EMBL:EGD36487.1}. SQ SEQUENCE 315 AA; 34690 MW; EA570F78D08316AE CRC64; MGKFKDLLDK QEIIILDGAL GTELESRGYD VSGKLWSAQY LLDQPQIIQD VHESYVRAGS DIITTSSYQA SIPAFIEAGL APEKAYDLLK ETVFLAQKAI ENVWQELSPE EQKQRPYPLI AGSVGPYAAY LADGSEYTGD YQLSEGEFQE FHRPRIQALL EVGCDLLAIE TIPNGAEAAA ILRLLAEEFP QAEAYLSFVA QSENAISDGT KIEELGNLAQ ESSQVLAVGF NCTAPHLIAP LLDGLGQVCN KPFLTYPNSG ETYNGLTKTW HDDPEQERSL LENSKLWQNQ GVRLFGGCCR TRPEDIAQLA KGLKD // ID F0IUR8_STRSA Unreviewed; 315 AA. AC F0IUR8; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGD38323.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EGD38323.1}; GN Name=mmuM {ECO:0000313|EMBL:EGD38323.1}; GN ORFNames=HMPREF9384_1580 {ECO:0000313|EMBL:EGD38323.1}; OS Streptococcus sanguinis SK160. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=888812 {ECO:0000313|EMBL:EGD38323.1}; RN [1] {ECO:0000313|EMBL:EGD38323.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK160 {ECO:0000313|EMBL:EGD38323.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGD38323.1}. 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; AEXZ01000010; EGD38323.1; -; Genomic_DNA. DR RefSeq; WP_002912356.1; NZ_GL872447.1. DR EnsemblBacteria; EGD38323; EGD38323; HMPREF9384_1580. DR PATRIC; 53506876; VBIStrSan173006_1560. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGD38323.1}; KW Transferase {ECO:0000313|EMBL:EGD38323.1}. SQ SEQUENCE 315 AA; 34641 MW; 4DEC640B955C1382 CRC64; MGKFKDLLDK QEIIILDGAL GTELESLGYD VSGKLWSAQY LLDQPQIIQD MHESYVRAGS DIITTSSYQA SIPAFIEAGL TSEKGYDLLK ETVFLAQKAI ENVWTGLSPE EQKQRPCPLV AGSVGPYAAY LADGSEYTGN YQLSEEEYRD FHRPRIQALL EAGSDLLAIE TIPNGAEAAA LLRLLAEEFP QAEAYLSFVA QSENAISDGT KIEELGNLAQ ESPQALAVGF NCTAPHLIAP LLDRLGQVCN KPFLTYPNSG ETYNGLTKTW HDDPEQERSL LENSKLWQEQ GVRLFGGCCR TRPEDIAQLA KGFKG // ID F0IZ81_ACIMA Unreviewed; 1171 AA. AC F0IZ81; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 29-APR-2015, entry version 29. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:BAJ81091.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:BAJ81091.1}; GN Name=metH {ECO:0000313|EMBL:BAJ81091.1}; GN OrderedLocusNames=ACMV_17440 {ECO:0000313|EMBL:BAJ81091.1}; OS Acidiphilium multivorum (strain DSM 11245 / JCM 8867 / NBRC 100883 / OS AIU301). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acidiphilium. OX NCBI_TaxID=926570 {ECO:0000313|EMBL:BAJ81091.1, ECO:0000313|Proteomes:UP000007100}; RN [1] {ECO:0000313|EMBL:BAJ81091.1, ECO:0000313|Proteomes:UP000007100} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11245 / JCM 8867 / AIU301 RC {ECO:0000313|Proteomes:UP000007100}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP012035; BAJ81091.1; -; Genomic_DNA. DR RefSeq; WP_013640156.1; NC_015186.1. DR RefSeq; YP_004283973.1; NC_015186.1. DR EnsemblBacteria; BAJ81091; BAJ81091; ACMV_17440. DR KEGG; amv:ACMV_17440; -. DR PATRIC; 46812349; VBIAciMul178205_2138. DR KO; K00548; -. DR BioCyc; AMUL926570:GI8V-1772-MONOMER; -. DR Proteomes; UP000007100; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007100}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAJ81091.1}; KW Transferase {ECO:0000313|EMBL:BAJ81091.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 234 234 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 301 301 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 742 742 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1171 AA; 129302 MW; 8AAD2F5AB1112654 CRC64; MWRASYIPTT MSRPSLLEAL RHRVLLCDGG MGSRVQALTL DTERDFWGKE NCTEVLNLSR PDLVREIHRG YYEAGADMVE TNSFGGSPIT LAEFELGDRA REINRIAAEL AREAAETFAD GRDRYVIGSV GPGTKLPTLG NIEYDPLEAG LAEQCRGLIE GGVDAILIET CQDTLQIKAA VNGARIARAE QKRDTPIFVQ VTVETTGTLL VGPDIAAAAT VIQALDVPLI GLNCATGPQE MAEHVRYLAQ NWPGLISVQP NAGLPELVDG KTHYPLTPDE LATWLERFIR EDGINLIGGC CGTSTPHIAA LDAMLRRLGE VRPAPVPRKP VWIPSVASLY GSTPLRQENA YFSIGERCNA NGSKKWRELQ ERHDWDGCIA MGREQVAEAS NALDICTAFV GRDELGEMSE IITRFTSSVN APLVIDSTET PVIEAALKLH GGKPIINSIN FEDGEHIAEE RMLLARKFGA AVIALTIDET GMAKEPAQKL EIATRLVDFA CRKHGLPQSD LLIDPLTFTI ATGNEDDRKL GLWTLEGIRL IRDAFPDIQI ILGLSNISFG LNPAARAVLN SVFLDHAVKA GMTGAIVHVS KIRPLHLIPP EEVRVMEDLI FDRRREDYDP LQRVLEMFAD RKAADAVKKV KADTVEGRLR DRIVDGDRKG LADDLDEAMK SHAPLDIINN LLLDGMKTVG ELFGAGKMQL PFVLQSAETM KAAVAYLEPY MERVEGQQKG TIVLATVKGD VHDIGKNLVD IILTNNGYRV VNLGIKVPLA DMVAAAKEHR AHAIGMSGLL VKSTVVMREN LEEMSRQGLD IPVLLGGAAL TRNYVEEDCV AAYASGRVAY ARDAFDGLHL MDRVTGNGFD DYLAALQSKR RGKARNTKRT LGQADARGFA PVDISAAQAR RRRLTRETPV PTPPFWGARI IEAPQKALVP YINERSLFQF QWGFRKQGKS LEDFMGWARQ ELRPVMKRML DLCAADSILK PQAIYGYWKA AGQGNDLILF AEDGATELAR FTLPRQPRDD GECIADFFRD VDDAERDVIG LQVVTMGAKA SETARAWFEE SRYQDYLYLH GLSVEMAEAM AEYTHKRIRA ELGFAAEDDR DMEKMLAQSY RGSRYSFGYP ACPNLEDQSL LLRLLDAERI GVSLSDEHQL HPEQSTSAIV VLNPHAKYFS V // ID F0JH92_DESDE Unreviewed; 803 AA. AC F0JH92; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGB15207.1}; GN ORFNames=DND132_2001 {ECO:0000313|EMBL:EGB15207.1}; OS Desulfovibrio desulfuricans ND132. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=641491 {ECO:0000313|EMBL:EGB15207.1, ECO:0000313|Proteomes:UP000007845}; RN [1] {ECO:0000313|EMBL:EGB15207.1, ECO:0000313|Proteomes:UP000007845} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ND132 {ECO:0000313|EMBL:EGB15207.1}; 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 ----------------------------------------------------------------------- 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; EGB15207.1; -; Genomic_DNA. DR RefSeq; WP_014322634.1; NC_016803.1. DR RefSeq; YP_005168010.1; NC_016803.1. DR EnsemblBacteria; EGB15207; EGB15207; DND132_2001. DR KEGG; ddn:DND132_2001; -. DR PATRIC; 46638036; VBIDesSp116210_2060. DR KO; K00548; -. DR BioCyc; DDES641491:GH21-2042-MONOMER; -. DR Proteomes; UP000007845; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007845}; KW Methyltransferase {ECO:0000313|EMBL:EGB15207.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007845}; KW Transferase {ECO:0000313|EMBL:EGB15207.1}. SQ SEQUENCE 803 AA; 85594 MW; 4F5E2403BBA49A81 CRC64; MPDFRSILDD DRIYYFDGGY GTLLQSRGLP AGLSPELWGL KEPDVIRAVH RDYIEAGADI LTTNTFGGSR PKLGLGVDPF ELNRAMTAIA REVAGDRAFV AASIGPTGHF VKPLGEMTFR ELVDIFKEQI RGCVAGGADL ILGETHFDLA EAKAVVVAAR LVCDLPVAIS MTFEGEASLT GTSPMTFVDT MQNMGVELIG TNCSAGPEQM RDTLRAWAPR LSTPTFAEAN AGLPELNAEG KTVFRLQPEP FAEKAAAFVE LGAKFIGGCC GTTPEHIRAL RDKVGDARWQ RPVRTDNAQL VLTSRSVSVP VGFDHRGVII GERINPTGKK QLTAELQESV FSEALRLAAE QAELGAPVLD VNVGAPLVDE AALLPELVTA LLGRVTTPLA IDSNDPAAVE AGLWAYPGSP LVNSISGEPG KMERLGPLCK LFGAPFILLP IVGRKLPVTA AERLKVIEDL LAQADALGIP RRLILVDALA LTVSSKPEAA RHSMEVMRQC RDRWGLPTTI GLSNISFGLP ARELLNSTFL SLSMASGLCS FIGNPNSARI RETLHAAEVL LDRDPQAARY IDNFSGWVGG GGVQAATSQA APSGAASLPP VQAAVVKGDK DNVVRLVEAE LDKGMAAMEI VNDLLIPGIL IVGDKYETKE YFLPQLLQSA ETMQTAFQRL KPLLEEAGGA GARPVVVMAT VEGDIHDIGK NIVCLMLKNY GFDVVDLGKD VPAEKIVAAA EEHDAALIGL SALMTTTMVR MEDTVKLVAE RNLRAKVIIG GAVVTEKFCK AIGAHGWSTD AVAAVKLAQR LTQ // ID F0JN36_ESCFE Unreviewed; 1227 AA. AC F0JN36; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EGC97427.1}; GN Name=metH {ECO:0000313|EMBL:EGC97427.1}; GN ORFNames=ECD227_3665 {ECO:0000313|EMBL:EGC97427.1}; OS Escherichia fergusonii ECD227. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=981367 {ECO:0000313|EMBL:EGC97427.1, ECO:0000313|Proteomes:UP000010293}; RN [1] {ECO:0000313|EMBL:EGC97427.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ECD227 {ECO:0000313|EMBL:EGC97427.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CM001142; EGC97427.1; -; Genomic_DNA. DR RefSeq; WP_000096030.1; NZ_CM001142.1. DR EnsemblBacteria; EGC97427; EGC97427; ECD227_3665. DR Proteomes; UP000010293; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000010293}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136085 MW; 6898C218086EB469 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG EEAKRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAE // ID F0JZD3_LACD2 Unreviewed; 187 AA. AC F0JZD3; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADY84393.1}; GN OrderedLocusNames=LBU_0208 {ECO:0000313|EMBL:ADY84393.1}; OS Lactobacillus delbrueckii subsp. bulgaricus (strain 2038). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=353496 {ECO:0000313|EMBL:ADY84393.1, ECO:0000313|Proteomes:UP000008126}; RN [1] {ECO:0000313|Proteomes:UP000008126} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2038 {ECO:0000313|Proteomes:UP000008126}; RX PubMed=21264216; DOI=10.1371/journal.pone.0015964; RA Hao P., Zheng H., Yu Y., Ding G., Gu W., Chen S., Yu Z., Ren S., RA Oda M., Konno T., Wang S., Li X., Ji Z.S., Zhao G.; RT "Complete sequencing and pan-genomic analysis of Lactobacillus RT delbrueckii subsp. bulgaricus reveal its genetic basis for industrial RT yogurt production."; RL PLoS ONE 6:E15964-E15964(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; CP000156; ADY84393.1; -; Genomic_DNA. DR RefSeq; WP_014564562.1; NC_017469.1. DR RefSeq; YP_005851417.1; NC_017469.1. DR EnsemblBacteria; ADY84393; ADY84393; LBU_0208. DR KEGG; ldl:LBU_0208; -. DR PATRIC; 47128474; VBILacDel183177_0235. DR KO; K00547; -. DR BioCyc; LDEL353496:GLF6-215-MONOMER; -. DR Proteomes; UP000008126; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008126}; KW Methyltransferase {ECO:0000313|EMBL:ADY84393.1}; KW Transferase {ECO:0000313|EMBL:ADY84393.1}. SQ SEQUENCE 187 AA; 21252 MW; 665DC9FA000EDF89 CRC64; MSDELERQGV KTNNKLWTAT ALINELDKVY QAHWDYFTAG AELVITDTYQ ANVQVFTQVG YSEQEAEKFI RDAVKVAKKA RDDYEQKTGK HNYVAGTVGS YGAYLADGNE YRGDYELSEL EYLAFHLPRL RQILAEKPDL IALETQPKLD EPLAVLNWLK ENASDYPVYV SFTLKDATHI SDGTTLE // ID F0JZH2_LACD2 Unreviewed; 305 AA. AC F0JZH2; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADY84432.1}; GN OrderedLocusNames=LBU_0247 {ECO:0000313|EMBL:ADY84432.1}; OS Lactobacillus delbrueckii subsp. bulgaricus (strain 2038). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=353496 {ECO:0000313|EMBL:ADY84432.1, ECO:0000313|Proteomes:UP000008126}; RN [1] {ECO:0000313|Proteomes:UP000008126} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2038 {ECO:0000313|Proteomes:UP000008126}; RX PubMed=21264216; DOI=10.1371/journal.pone.0015964; RA Hao P., Zheng H., Yu Y., Ding G., Gu W., Chen S., Yu Z., Ren S., RA Oda M., Konno T., Wang S., Li X., Ji Z.S., Zhao G.; RT "Complete sequencing and pan-genomic analysis of Lactobacillus RT delbrueckii subsp. bulgaricus reveal its genetic basis for industrial RT yogurt production."; RL PLoS ONE 6:E15964-E15964(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; CP000156; ADY84432.1; -; Genomic_DNA. DR RefSeq; WP_014564580.1; NC_017469.1. DR RefSeq; YP_005851456.1; NC_017469.1. DR EnsemblBacteria; ADY84432; ADY84432; LBU_0247. DR KEGG; ldl:LBU_0247; -. DR PATRIC; 47128572; VBILacDel183177_0279. DR KO; K00547; -. DR BioCyc; LDEL353496:GLF6-254-MONOMER; -. DR Proteomes; UP000008126; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008126}; KW Methyltransferase {ECO:0000313|EMBL:ADY84432.1}; KW Transferase {ECO:0000313|EMBL:ADY84432.1}. SQ SEQUENCE 305 AA; 33226 MW; 28649662B185FEB1 CRC64; MADLPTLLAQ GPVTLDGSMS TPLEAWGEDT NSDLWTAKAL ADNPDLVYRV HQEYFKAGAR VTITDSYQAS LPAFMKHGLS EDAARALIRE SAAVAIKARD DFEKATGIHN FVAGSVGPYG AYLADGSEYR GDYALSHEEY VDFHAPRIEE LVAGGVDCLA VETQPKLSEV RAILDYLKAK YPDLPVYVSF SLKDPATISE GLPLTEAVEE VSAYAQVFAA GANCFKLAWT VDVVKNLRAS KLPIVVYPNS GAEYDPSVKK WVYPPEAADF GQAGAAARQC RKISPDLPPQ SKRFILLFKI FLILD // ID F0KG73_ACICP Unreviewed; 292 AA. AC F0KG73; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Putative homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:ADY80787.1}; GN Name=hmt-1 {ECO:0000313|EMBL:ADY80787.1}; GN OrderedLocusNames=BDGL_000201 {ECO:0000313|EMBL:ADY80787.1}; OS Acinetobacter calcoaceticus (strain PHEA-2). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=871585 {ECO:0000313|EMBL:ADY80787.1, ECO:0000313|Proteomes:UP000007477}; 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] {ECO:0000313|EMBL:ADY80787.1, ECO:0000313|Proteomes:UP000007477} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PHEA-2 {ECO:0000313|EMBL:ADY80787.1, RC ECO:0000313|Proteomes:UP000007477}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; ADY80787.1; -; Genomic_DNA. DR RefSeq; WP_014206015.1; NC_016603.1. DR RefSeq; YP_004994469.1; NC_016603.1. DR EnsemblBacteria; ADY80787; ADY80787; BDGL_000201. DR GeneID; 11638377; -. DR KEGG; acc:BDGL_000201; -. DR PATRIC; 47078438; VBIAciCal168233_0200. DR OMA; PYVDVWL; -. DR BioCyc; ACAL871585:GH86-208-MONOMER; -. DR Proteomes; UP000007477; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007477}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ADY80787.1}; KW Transferase {ECO:0000313|EMBL:ADY80787.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 202 202 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 275 275 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 276 276 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 292 AA; 32053 MW; 138D21956EDD5C2D CRC64; MKILDGGLGR ELARRGAPFR QPEWSALALI EAPETVKEVH LDFINAGSEV ITTNNYAVVP FHIGQERFET DGVRLIKVAI EQAKNAVKES GKNVKIAGCL PPLFGSYRAD LFQPEQAKSL AEPIINTLAP EVDFWLAETQ SCLKEVETVH ALLPQDGKDY WVSFTLQDEI KQEQALLRSG ENMQQVADFI KQSNAKAVLF NCCQPEVILQ AINEIKGLIP ESVQIGAYAN AFPPQDESAT ANDGLDEIRK DLDAPAYLGF AKQWQQAGAS LVGGCCGIGP EHIAELSQFF KE // ID F0KGC3_ACICP Unreviewed; 940 AA. AC F0KGC3; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 32. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADY80837.1}; GN Name=metH {ECO:0000313|EMBL:ADY80837.1}; GN OrderedLocusNames=BDGL_000251 {ECO:0000313|EMBL:ADY80837.1}; OS Acinetobacter calcoaceticus (strain PHEA-2). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=871585 {ECO:0000313|EMBL:ADY80837.1, ECO:0000313|Proteomes:UP000007477}; 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] {ECO:0000313|EMBL:ADY80837.1, ECO:0000313|Proteomes:UP000007477} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PHEA-2 {ECO:0000313|EMBL:ADY80837.1, RC ECO:0000313|Proteomes:UP000007477}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002177; ADY80837.1; -; Genomic_DNA. DR RefSeq; WP_014206053.1; NC_016603.1. DR RefSeq; YP_004994519.1; NC_016603.1. DR EnsemblBacteria; ADY80837; ADY80837; BDGL_000251. DR GeneID; 11638427; -. DR KEGG; acc:BDGL_000251; -. DR PATRIC; 47078542; VBIAciCal168233_0250. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR BioCyc; ACAL871585:GH86-258-MONOMER; -. DR Proteomes; UP000007477; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007477}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 940 AA; 102936 MW; ED179BA0031BF64B CRC64; MSTLATLKAL LAKRILIIDG AMGTMIQRHK LEEADYRGER FADWAHDLKG NNDLLVLTQP QIIQGIHEAY LDAGADIIET NSFNGTRVSM SDYHMEDLVP EINREAARLA KAACEKYSTP EKPRFVAGVL GPTSRTCSIS PNVNDPAFRN ITFDELKENY IEATHALIEG GADIILIETV FDTLNCKAAI FAVKEVFKEI GRELPIMISG TITDASGRTL TGQTAEAFWN SVRHGDLLSI GFNCALGADA MRPHVKTISD VADTFVSAHP NAGLPNAFGE YDETPEQTAA FLKEFAESGL INITGGCCGT TPDHIRAIAN AVKDIAPRQV PETVPACRLS GLEPFNIYDD SLFVNVGERT NVTGSKKFLR LIREENFAEA LEVAQQQVEA GAQIIDINMD EGMLDSQNAM VHFLNLVASE PDISRVPIMI DSSKWEIIEA GLKCVQGKPV VNSISLKEGY DEFVEKARLC RQYGAAIIVM AFDETGQADT AARKREICKR SYDILVNDVG FPAEDIIFDP NVFAVATGIE EHNNYGVDFI EATGWIKQNL PHAMISGGVS NVSFSFRGNE PVREAIHSVF LYHAIKQGMT MGIVNAGQMA IYDDIPAELK QAVEDVILNQ NQGESGQAAT EKLLEVAEKY RGQGGATKEA ENLEWRNESV EKRLEYALVK GITTYIDEDT EEARLKAKRP LDVIEGALMD GMNVVGDLFG SGKMFLPQVV KSARVMKQAV AWLNPYIEAE KTGSQSKGKV LMATVKGDVH DIGKNIVGVV LGCNGYDIVD LGVMVPCEKI LQTAIDEKCD IIGLSGLITP SLDEMVFVAK EMQRKGFNIP LLIGGATTSK AHTAVKIDPQ YQNDAVIYVA DASRAVGVAT TLLSKEMRGN FIAEHRAEYA KIRERLANKQ PKAAKLTYKE SVENGFKIDE SYVPPKPNHQ LPSCNPCRLF // ID F0L8C2_AGRSH Unreviewed; 1262 AA. AC F0L8C2; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 01-APR-2015, entry version 33. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:ADY65061.1}; GN Name=metH {ECO:0000313|EMBL:ADY65061.1}; GN OrderedLocusNames=AGROH133_07572 {ECO:0000313|EMBL:ADY65061.1}; 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 {ECO:0000313|EMBL:ADY65061.1, ECO:0000313|Proteomes:UP000007455}; RN [1] {ECO:0000313|EMBL:ADY65061.1, ECO:0000313|Proteomes:UP000007455} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H13-3 {ECO:0000313|EMBL:ADY65061.1, RC ECO:0000313|Proteomes:UP000007455}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002248; ADY65061.1; -; Genomic_DNA. DR RefSeq; WP_013636547.1; NC_015183.1. DR RefSeq; YP_004279381.1; NC_015183.1. DR EnsemblBacteria; ADY65061; ADY65061; AGROH133_07572. DR KEGG; agr:AGROH133_07572; -. DR PATRIC; 46849021; VBIAgrSp164909_2103. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; ASP861208:GH59-2102-MONOMER; -. DR Proteomes; UP000007455; Chromosome circular. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007455}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 265 265 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 328 328 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 329 329 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 781 781 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1262 AA; 139229 MW; EC0CDDFFE592600F CRC64; MRSAPVFDDL FGPEGAKRDG AEILRALRQA ASERILILDG AMGTQIQGLG FDEDNFRGDR FIGCACHQQG NNDLLILTQP DAIEEIHYRY AMAGADILET NTFSSTRIAQ ADYEMENAVY DLNREGAQIV RRAAQRAERE DGRRRFVAGA IGPTNRTASI SPDVNNPGYR AVSFDDLRIA YGEQIDGLID GGADIILIET IFDTLNAKAA IFACEERFEA KGIRLPVMIS GTITDLSGRT LSGQTPSAFW NSVRHANPFT IGLNCALGAD AMRPHLQELS DVADTFVCAY PNAGLPNEFG QYDETPEMMA RQVQGFARDG LVNIVGGCCG STPEHIRAIA EAVKDYKPRP IPEHKPFMSL SGLEPFVLTK DIPFVNVGER TNVTGSARFR KLITAGDYTA ALAVARDQVE NGAQIIDINM DEGLIDSQKA MVEFLNLIAA EPDIARVPVM IDSSKFEIIE AGLKCVQGKS IVNSISLKEG EEKFLQQARL VHNYGAAVVV MAFDEVGQAD TYQRKVEICT RAYKLLTEKA GLSPEDIIFD PNVFAVATGI EEHNNYGVDF IEATKTIRET MPLTHISGGV SNLSFSFRGN EPVREAMHAV FLYHAIQVGM DMGIVNAGQL AVYDNIDAEL REACEDVVLN RRDDATERLL DVAERFRGTG EKQAKVQDLS WRELSVEKRL QHALVNGITE FIEADTEEAR QQAARPLHVI EGPLMAGMNV VGDLFGSGKM FLPQVVKSAR VMKQAVAVLL PYMEEEKRLN GGEQNKAAGK VLMATVKGDV HDIGKNIVGV VLACNNYEII DLGVMVPTTK ILETAIAEKV DVIGLSGLIT PSLDEMVHVA AEMERQGFNI PLLIGGATTS RVHTAVKIHP RYEQGQAIYV TDASRAVGVV SALLSAEQKP AYIDGIRAEY AKVAEAHARN EREKQRLPLS RARENAHKID WSTYSVVKPQ FFGTKVFETY DLEELSRYID WTPFFQTWEL KGRYPAILED EKQGEAARQL YADAQAMLKK IIEEKWFRPR AVIGFWPANA VGDDIRLFTD ENRSEELATF FTLRQQLSKR DGRPNVALSD FVAPVDSGVA DYVGGFVVTA GIEEVAIAER FERANDDYSS ILVKALADRF AEAFAERMHE RVRKEFWGYA PEEALAGDEL IGEAYAGIRP APGYPAQPDH TEKKTLFSLL DATNAAGVEL TESYAMWPGS SVSGLYIGHP ESYYFGVAKV ERDQVLDYAR RKDMPLVQVE RWLGPVLNYV PVNGAEEIDS AA // ID F0L9C7_AGRSH Unreviewed; 304 AA. AC F0L9C7; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=S-methyltransferase {ECO:0000313|EMBL:ADY65257.1}; GN OrderedLocusNames=AGROH133_08100 {ECO:0000313|EMBL:ADY65257.1}; 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 {ECO:0000313|EMBL:ADY65257.1, ECO:0000313|Proteomes:UP000007455}; RN [1] {ECO:0000313|EMBL:ADY65257.1, ECO:0000313|Proteomes:UP000007455} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H13-3 {ECO:0000313|EMBL:ADY65257.1, RC ECO:0000313|Proteomes:UP000007455}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002248; ADY65257.1; -; Genomic_DNA. DR RefSeq; WP_013636680.1; NC_015183.1. DR RefSeq; YP_004279577.1; NC_015183.1. DR EnsemblBacteria; ADY65257; ADY65257; AGROH133_08100. DR KEGG; agr:AGROH133_08100; -. DR PATRIC; 46849430; VBIAgrSp164909_2303. DR OMA; PYVDVWL; -. DR BioCyc; ASP861208:GH59-2300-MONOMER; -. DR Proteomes; UP000007455; Chromosome circular. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007455}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ADY65257.1}; KW Transferase {ECO:0000313|EMBL:ADY65257.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 304 AA; 31921 MW; 732E2F449E47124E CRC64; MGTIRILDGG MSRELQRLGA ELKQPEWSAL ALINSPDIVR QVHQEFIEAG ADVVTTNSYA LVPFHIGEER FQKDGESLIA LSGRLAREAA DASGRDVLVA GSLPPIFGSY EPQNFDATRV QDYLKVLVDN LGSFVDVWLG ETLSLIAEGE AVREAVAATG KPFWISFTLN DDAAATGGGE PALRSGETVK AAAEWAAQSG AAALLFNCSK PEIMKAAVET ASAVFAEKGV SLEIGVYANA FEGEQGDSAA NEGLHGTRTD LTDDVYSRFA CSWADAGATM IGGCCGIGAA HIHTVATALR RAAA // ID F0LWU3_VIBFN Unreviewed; 1226 AA. AC F0LWU3; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:ADT88232.1}; GN OrderedLocusNames=vfu_A03127 {ECO:0000313|EMBL:ADT88232.1}; OS Vibrio furnissii (strain DSM 14383 / NCTC 11218). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=903510 {ECO:0000313|EMBL:ADT88232.1, ECO:0000313|Proteomes:UP000007456}; RN [1] {ECO:0000313|EMBL:ADT88232.1, ECO:0000313|Proteomes:UP000007456} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14383 / NCTC 11218 {ECO:0000313|Proteomes:UP000007456}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002377; ADT88232.1; -; Genomic_DNA. DR RefSeq; WP_014205872.1; NC_016602.1. DR RefSeq; YP_004994244.1; NC_016602.1. DR EnsemblBacteria; ADT88232; ADT88232; vfu_A03127. DR KEGG; vfu:vfu_A03127; -. DR PATRIC; 45430492; VBIVibFur169925_3031. DR KO; K00548; -. DR BioCyc; VFUR903510:GHFS-3095-MONOMER; -. DR Proteomes; UP000007456; Chromosome 1. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007456}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADT88232.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007456}; KW Transferase {ECO:0000313|EMBL:ADT88232.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1226 AA; 136204 MW; A105DF40923771B6 CRC64; MGTNVRHQIE SQLQQRILLI DGGMGTMIQG YKLEEQDYRG ERFADWHSDL KGNNDLLVLT QPQLIKEIHT AYLEAGADIL ETNTFNATTI AMADYDMQSL SAEINLAAAK LAREAADEWT AKTPHKPRYV AGVLGPTNRT CSISPDVNDP GYRNVTFDQL VEAYSESTRA LIKGGSDLIL IETIFDTLNA KACAFAVESV FEELGIELPV MISGTITDAS GRTLSGQTTE AFYNALRHVR PISFGLNCAL GPDELRQYVE ELSRIAECHV SAHPNAGLPN AFGEYDLSAE EMAEHIEEWA KTGFLNLVGG CCGTTPEHIA AMAKAVDGVT PRALPTLNVE CRLSGLEPLN IAKETLFVNV GERTNVTGSA RFKRLIKEEL YDEALDVARE QVENGAQIID INMDEGMLDA EACMVRFLNL CASEPEISKV PVMVDSSKWE VIEAGLKCIQ GKGIVNSISL KEGKEKFVQQ AKLVRRYGAA VIVMAFDEVG QADTRERKLE ICRRAYHILV DEVGFPPEDI IFDPNIFAVA TGIDEHNNYA LDFINAVADI KRDLPHAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK NGMDMGIVNA GQLEIYDNVP ETLREAVEDV ILNRHNDATE RLLEIADAYR ENAVGKQDDA SALEWRTWPV AKRLEHALVK GITEFIVEDT EEARVNASKP LEVIEGPLMD GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AHLEPYINAE KQSGSTNGKI LLATVKGDVH DIGKNIVGVV LQCNNYEIID LGVMVPCEQI LKVAREQNVD IIGLSGLITP SLDEMVHVAK EMERQGFDLP LLIGGATTSK AHTAVKIEQN YHQPVVYVNN ASRAVGVCTS LLSNELRPAF IEKLDLDYER TRDQHARKTP KTRPVTLAEA RANKAPIDWD SYTPPVPAKP GIHVFEHFEL STLRQYIDWT PFFMTWSLMG KYPAILQHEE VGEEAQRLFK DANELLDKVE REGLLKASGM CALFPAASVG DDIEVYRDES RTEVAHTLYN LRQQTHKPKG ANYCLSDYIA PKSSGKKDWI GAFTVTGGIG ERELADQYKA QGDDYNAIMI QAVADRLAEA FAEYLHEKVR KEIWGYATDE NLSNDELIRE KYQGIRPAPG YPACPEHTEK GTLWEMLKVE ETIGMSLTTS YAMWPGASVS GWYFSHPDSR YFAIAQIQDD QVQSYAQRKG WDHLEAEKWL GPNING // ID F0LY12_VIBFN Unreviewed; 294 AA. AC F0LY12; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADT88811.1}; GN OrderedLocusNames=vfu_B00584 {ECO:0000313|EMBL:ADT88811.1}; OS Vibrio furnissii (strain DSM 14383 / NCTC 11218). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=903510 {ECO:0000313|EMBL:ADT88811.1, ECO:0000313|Proteomes:UP000007456}; RN [1] {ECO:0000313|EMBL:ADT88811.1, ECO:0000313|Proteomes:UP000007456} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14383 / NCTC 11218 {ECO:0000313|Proteomes:UP000007456}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002378; ADT88811.1; -; Genomic_DNA. DR RefSeq; WP_014257578.1; NC_016628.1. DR RefSeq; YP_005049131.1; NC_016628.1. DR EnsemblBacteria; ADT88811; ADT88811; vfu_B00584. DR KEGG; vfu:vfu_B00584; -. DR PATRIC; 45431714; VBIVibFur169925_3626. DR BioCyc; VFUR903510:GHFS-3683-MONOMER; -. DR Proteomes; UP000007456; Chromosome 2. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007456}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ADT88811.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007456}; KW Transferase {ECO:0000313|EMBL:ADT88811.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 198 198 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 275 275 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 276 276 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 294 AA; 31737 MW; 8651D2A9BA1CCE89 CRC64; MGRELEKRGA PFRQPEWSAL AMIEAPEIVR DVHRAFIQSG ADVITTNSYA LVPFHIGEAR FHQEAQLLAH RAGDVARQAV QLEGQATRVA GSIPPLFGSY RADLFDASRV AEIATPLING LAPHVDFWLA ETQSLIGESV AVKALLDELD TQHKPLWVSF TLEDAEPTDV PRLRSGETVA EAIHAMIALN VSAILFNCCQ PEVIEEALAI AASILKTTGA QQIQLGAYAN AFPPQPKDAT ANDGLDELRA DLTPPAYLLW AEKWQQQGAS LIGGCCGIGP EHIATLSQHF SHAG // ID F0M474_ARTPP Unreviewed; 323 AA. AC F0M474; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 01-APR-2015, entry version 20. DE SubName: Full=Homocysteine/selenocysteine methylase (S-methylmethionine-dependent) {ECO:0000313|EMBL:ADX72297.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ADX72297.1}; DE Flags: Precursor; GN OrderedLocusNames=Asphe3_11150 {ECO:0000313|EMBL:ADX72297.1}; 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 {ECO:0000313|EMBL:ADX72297.1, ECO:0000313|Proteomes:UP000008639}; RN [1] {ECO:0000313|EMBL:ADX72297.1, ECO:0000313|Proteomes:UP000008639} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18606 / JCM 16027 / LMG 23796 / Sphe3 RC {ECO:0000313|Proteomes:UP000008639}; 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 ----------------------------------------------------------------------- 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; ADX72297.1; -; Genomic_DNA. DR RefSeq; WP_013600236.1; NC_015145.1. DR RefSeq; YP_004240431.1; NC_015145.1. DR EnsemblBacteria; ADX72297; ADX72297; Asphe3_11150. DR KEGG; apn:Asphe3_11150; -. DR PATRIC; 46860545; VBIArtPhe178037_1106. DR KO; K00547; -. DR BioCyc; APHE930171:GJHZ-1112-MONOMER; -. DR Proteomes; UP000008639; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008639}; KW Methyltransferase {ECO:0000313|EMBL:ADX72297.1}; KW Signal {ECO:0000313|EMBL:ADX72297.1}; KW Transferase {ECO:0000313|EMBL:ADX72297.1}. FT SIGNAL 1 30 Potential. {ECO:0000313|EMBL:ADX72297.1}. FT CHAIN 31 323 Potential. {ECO:0000313|EMBL:ADX72297.1}. FT /FTId=PRO_5000714296. SQ SEQUENCE 323 AA; 33984 MW; E0B5292F89E9A546 CRC64; MRIVITMSSS APLPSLLESV GILPADGALA TELEARGCNL DDPLWSAKVL LEQPHLIKEV HRDYFRAGAR IATTASYQAT PQGFAPRGIS EQEALELVAL SVRLADEARR EHLAANPGAG PLLVAGSVGP YGAYLADGSE YSGDYVLSTT EFQDFHRPRI TALVEAGADF LACETLPSFP EAQALLALTK EFDVESWFSF SLRDGGHISD GTPLTTVAAV LGAEPLVAAI GVNCVPLHLV TPALAALHRE TDKPLVAYPN SGETYDPATK TWGQAAASGR GRDGTPATPA DGAVTWRDLG ARIIGGCCRT TPRDIAAVVD VLS // ID F0M4M2_ARTPP Unreviewed; 1190 AA. AC F0M4M2; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 30. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ADX74569.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADX74569.1}; GN OrderedLocusNames=Asphe3_34670 {ECO:0000313|EMBL:ADX74569.1}; 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 {ECO:0000313|EMBL:ADX74569.1, ECO:0000313|Proteomes:UP000008639}; RN [1] {ECO:0000313|EMBL:ADX74569.1, ECO:0000313|Proteomes:UP000008639} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18606 / JCM 16027 / LMG 23796 / Sphe3 RC {ECO:0000313|Proteomes:UP000008639}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002379; ADX74569.1; -; Genomic_DNA. DR RefSeq; WP_013602457.1; NC_015145.1. DR RefSeq; YP_004242703.1; NC_015145.1. DR EnsemblBacteria; ADX74569; ADX74569; Asphe3_34670. DR KEGG; apn:Asphe3_34670; -. DR PATRIC; 46865355; VBIArtPhe178037_3456. DR KO; K00548; -. DR BioCyc; APHE930171:GJHZ-3457-MONOMER; -. DR Proteomes; UP000008639; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008639}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADX74569.1}; KW Transferase {ECO:0000313|EMBL:ADX74569.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 217 217 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 744 744 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1190 AA; 129159 MW; 51873F76FEA63D56 CRC64; MNHRVVIADG AMGTMLQGRD LSLETDFQNL EGCNEILNDT RPDVIADIHD AYFATGIDAV ETNTFGANWS NLSDYGIDDR IAELALKGAK IARERAEAAE ETDGRMRWVL GSMGPGTKLP SLGHTSYDYL KQTFALQAEG LIDGGADAFL IETSQDLLQT KAAVNGCKQA IVSRGIRLPI FVEVTVETTG TMLMGSEIGA ALTALEPLGV DAIGLNCATG PDEMSEHLRH LSKQSSVAIA CMPNAGLPIL GANGAHYPLT PTELATAHEQ FVREFGLGLV GGCCGTTPEH MAAVVERLAP FRTRKTDAVS SGPARVPTER EAGVASLYQH VNFDQDASYL AIGERTNANG SKAFRQAMLE ERWDDCVDIA REQIRVGAHL LDVCIDYVGR DGVADIKEVV SRFASASTLP LVIDSTEPPV LKAGLELIGG RPVVNSVNYE DGDGPDSRFA RIMPLVKEHG TAVIALTIDE QGQARTTEGK VAIASRLVDA LVGEWGMRVE DIIVDALTFP VATGQEETRR DGIETIEAIR QITAKYPGIN TTLGVSNVSF GLNPAARIVL NSVFLHEAVQ AGLTSGIIDA AKIVPLASLP EEQRKVALDL VWDRREYDAE GNTTYDPLAI MLDMFAGVDT AALKDQRAAE LAALPTGARL ERRIIDGEGK GLEEDLDLAR SEGMTPLGII NDHLLEGMKV VGERFGAGEM QLPFVLQSAE VMKNAVALLE PHMEKSDSSG KGTMVIATVR GDVHDIGKNL VDIILTNNGY KVVNIGIKQG IAEIMAAAEE HNADVIGMSG LLVKSTVVMK ENLAELQSRG LAKKWPVILG GAALTRAYVE QDLAEQFDGV VRYAKDAFEG LALMEPLVRV ARGESPDDVG LPPLKKRIHK GGAKFTVTEP EAMPGRSDVA TDNPVPAPPF WGTRIVRGVS LHEYAAFLDE RATFMGQWGL KPGRGEDGAS YEELVEREGR PRLRYWLDRI LGEGMLDASV AYGYFPVVSE GEQVVVLHHG EDHDGVLGTP GLLAPDGGSG GPIGTDRLRF DFPRQRRDRH LCLADFVKSR ESGQIDVLPV QLVTAGSKIE EFTSKMFAAN QYRDYYELNG LVMQLTEALA EFWHARIRKE LGFAAEEPKD TAGYFKLDYR GARFSLGYPA CPDMEDRRKV TELLKPERMG VVLSDELMLH PEQSTDAFVF HHPEAQYFKV // ID F0PW57_BACT0 Unreviewed; 1132 AA. AC F0PW57; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 31. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:ADY23420.1}; GN OrderedLocusNames=YBT020_20960 {ECO:0000313|EMBL:ADY23420.1}; OS Bacillus thuringiensis subsp. finitimus (strain YBT-020). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=930170 {ECO:0000313|EMBL:ADY23420.1, ECO:0000313|Proteomes:UP000007483}; RN [1] {ECO:0000313|EMBL:ADY23420.1, ECO:0000313|Proteomes:UP000007483} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YBT-020 {ECO:0000313|EMBL:ADY23420.1, RC ECO:0000313|Proteomes:UP000007483}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002508; ADY23420.1; -; Genomic_DNA. DR RefSeq; WP_000649696.1; NC_017200.1. DR RefSeq; YP_005567838.1; NC_017200.1. DR EnsemblBacteria; ADY23420; ADY23420; YBT020_20960. DR KEGG; btf:YBT020_20960; -. DR PATRIC; 47094111; VBIBacThu177620_4169. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; BTHU930170:GL8S-4280-MONOMER; -. DR Proteomes; UP000007483; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007483}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADY23420.1}; KW Transferase {ECO:0000313|EMBL:ADY23420.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 125884 MW; 63F8E3CC0EF76CD2 CRC64; MKCIEEKLQN NILILDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYELSHLDE ELNEKAARLA KQAVEESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGE VDVLLVETSQ DMRNVKAAYI GIQAAFDELN TVVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWVN IIGGCCGTTP EHIKAMKSAL MSLKPREQQE RAGHGVSGLE ALQYDDSMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEI ARAQVKKNAH IIDICMADPD RDEIEDMENF LAEVTKVLKV PIMIDSTDEH VMERALTYIQ GKAVINSINL EDGEERFKKV TPLLRKYGAA IVVGTIDEDG MAVSAERKLE IAKRSYELLT TKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPDE EKRLADALLF ETTQETLEKF TNFYRVAKKK DVVVQETLTL DERLANYIVE GTKQGLHEDL SLALTEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILA NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAADIDIPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV TKEEKKVEIP AVIEPLPKAE VIVPDSTKRI VLRDVPVSHL APFLNRQMLL GHHLGLKGSV KKLLREGDKR AHELNDLIDE LLQEGQSWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRVIE RFTFPRQGKA PYRTLGDYLR PVGDEMDYVA FLSVTVGEGV RDIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID F0PW58_BACT0 Unreviewed; 610 AA. AC F0PW58; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 26. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=YBT020_20965 {ECO:0000313|EMBL:ADY23421.1}; OS Bacillus thuringiensis subsp. finitimus (strain YBT-020). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=930170 {ECO:0000313|EMBL:ADY23421.1, ECO:0000313|Proteomes:UP000007483}; RN [1] {ECO:0000313|EMBL:ADY23421.1, ECO:0000313|Proteomes:UP000007483} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YBT-020 {ECO:0000313|EMBL:ADY23421.1, RC ECO:0000313|Proteomes:UP000007483}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ADY23421.1; -; Genomic_DNA. DR RefSeq; WP_000770336.1; NC_017200.1. DR RefSeq; YP_005567839.1; NC_017200.1. DR EnsemblBacteria; ADY23421; ADY23421; YBT020_20965. DR KEGG; btf:YBT020_20965; -. DR PATRIC; 47094113; VBIBacThu177620_4170. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR BioCyc; BTHU930170:GL8S-4281-MONOMER; -. DR Proteomes; UP000007483; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007483}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ADY23421.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:ADY23421.1}. SQ SEQUENCE 610 AA; 67210 MW; DEA6BF12CD1281D2 CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNISDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTE INRAAVKLAK ASVTDRNAIL GTIGGMKHIG AVTTTDMERE FMLLEQASAL LEEQVDGLLL ETFYDEFELL HAVQVLRKET NIPIVAQLAL HEAGTTQNGN DVNEILKQLL DYGANVVGLN CQLGPLHMTE AFKMISIPKN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPKFIEQGI RLLGGCCGTT PEHIESMKRA TLNVTPVIEK DTVQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRISNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSVL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIA LIEEVYEVTK HLEQPIFIGI MPLISKRNAD FLHFEVPGIT LPEAVRERMD GHETKEAAIE EGIRISQELI DAAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID F0Q201_ACIAP Unreviewed; 354 AA. AC F0Q201; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADX44132.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADX44132.1}; GN OrderedLocusNames=Acav_0206 {ECO:0000313|EMBL:ADX44132.1}; 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 {ECO:0000313|EMBL:ADX44132.1, ECO:0000313|Proteomes:UP000002482}; RN [1] {ECO:0000313|Proteomes:UP000002482} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19860 / DSM 7227 / JCM 20985 / NCPPB 1011 RC {ECO:0000313|Proteomes:UP000002482}; 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; ADX44132.1; -; Genomic_DNA. DR RefSeq; WP_013592719.1; NC_015138.1. DR RefSeq; YP_004232699.1; NC_015138.1. DR EnsemblBacteria; ADX44132; ADX44132; Acav_0206. DR KEGG; aaa:Acav_0206; -. DR PATRIC; 46834967; VBIAciAve68977_0209. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR BioCyc; AAVE643561:GHRD-206-MONOMER; -. DR Proteomes; UP000002482; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002482}; KW Methyltransferase {ECO:0000313|EMBL:ADX44132.1}; KW Transferase {ECO:0000313|EMBL:ADX44132.1}. SQ SEQUENCE 354 AA; 38174 MW; 17F4BA1899164F5D CRC64; MQPLHYTRAQ QLPGILAERI AILDGAMGTM IQRFKLGEAQ YRGEGYSGPG GAGDRFKDFP RDVKGNNELL SLTRPDVIRD IHERYLAAGA DLIETNTFGA TTIAQEDYHM ADLAREMNLA SARLARAACD KFSTQGKPRF VAGALGPTPK TASISPDVND PGARNVDFEQ LRAAYYEQTQ ALVEGGADVL LVETIFDTLN AKAALFAIDE YFEASGERLP LIISGTVTDA SGRILSGQTV TAFWHSVRHS RPLAIGLNCA LGATLMRPYI QELNRVAEDT FISCYPNAGL PNPMSDTGFD ETPEVTSRLV HEFAAEGLVN IVGGCCGTTP DHIAAIGRAV APVPARRLFY PEAA // ID F0R3V0_BACSH Unreviewed; 916 AA. AC F0R3V0; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADY34637.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADY34637.1}; GN OrderedLocusNames=Bacsa_0021 {ECO:0000313|EMBL:ADY34637.1}; OS Bacteroides salanitronis (strain DSM 18170 / JCM 13567 / BL78). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=667015 {ECO:0000313|EMBL:ADY34637.1, ECO:0000313|Proteomes:UP000007486}; RN [1] {ECO:0000313|EMBL:ADY34637.1, ECO:0000313|Proteomes:UP000007486} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18170 / JCM 13567 / BL78 RC {ECO:0000313|Proteomes:UP000007486}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002530; ADY34637.1; -; Genomic_DNA. DR RefSeq; WP_013616099.1; NC_015164.1. DR RefSeq; YP_004257110.1; NC_015164.1. DR EnsemblBacteria; ADY34637; ADY34637; Bacsa_0021. DR KEGG; bsa:Bacsa_0021; -. DR PATRIC; 46875897; VBIBacSal140776_0023. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR BioCyc; BSAL667015:GHA0-111-MONOMER; -. DR Proteomes; UP000007486; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007486}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADY34637.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007486}; KW Transferase {ECO:0000313|EMBL:ADY34637.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 243 243 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 916 AA; 100903 MW; F7D96EB1A825B518 CRC64; MKTIQEQINE RILVLDGAMG TMIQQYGLTE EDFRGERFRE VPGMLKGCND VLCLTRPDVI ADIHRKYLDA GADIIETNTF NATRVSMADY HLEGYCAEIN REAARLARRL ADEYTAKNPE KPRWVAGSVG PTNKTCSMSP DVNNPAYRAL TFDGLAGAYL EQMTALLEGG VDTILIETIF DTLNAKAAIC AAEQAMERCG RKVPLMLSVT VSDTGGRTLS GQTLDAFLAS VQHADIFSIG LNCSFGARQL KPFLEQLARR APYYISAYPN AGLPNTLGQY DQTPEEMEGE VKEYIDEGLV NIIGGCCGTT EAYIRRFASL VEGRKPHQRV DASKYLWLSG LELLEVTPEI NFVNVGERCN VAGSRKFLRL INEKKYEEAL SIARKQVEDG ALVIDINMDD GLLDAAQEMT TFLNLIASEP DIARVPIMID SSKWDVILAG LKCVQGKGIV NSISLKEGEA VFIERARTIK RYGAAVIVMA FDEKGQADTY ERKIEVCSRA YRILTEQVGF RPQDIIFDPN VLAVATGMEE HNNYAVDFIR ATGWIRKNLP GAHISGGVSN LSFAFRGNNY IREAMHAVFL YHAIAQGMDM GIVNPASSVL YTDIPADILE RIEDVVLNRR ADAAERLIEM AEKLKTEKEN AGAVQGAETH LAWRNGTDVD SRLQYALVKG IGDYLEEDLQ EALHTYPDAV SIIEGPLMEG MNRVGELFGS GKMFLPQVVK TARTMKKAVS ILQPYIEAQK KEGAKKAGKV LVATVKGDVH DIGKNIVSVV MACNNYEIID LGVMVPAEKI VETAIREKVD IVGLSGLITP SLEEMVHVVR ELDRAGVHIP VMIGGATTSK LHTALKIAPV YHGPVIYMKD ASLNAPVAAR LLNPATHDAF VKELAGEYEA LREGNKEKQV RLTSLEEARK NKLELF // ID F0RD97_CELLC Unreviewed; 372 AA. AC F0RD97; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADY29798.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADY29798.1}; GN OrderedLocusNames=Celly_1976 {ECO:0000313|EMBL:ADY29798.1}; 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 {ECO:0000313|EMBL:ADY29798.1, ECO:0000313|Proteomes:UP000007487}; RN [1] {ECO:0000313|EMBL:ADY29798.1, ECO:0000313|Proteomes:UP000007487} 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 {ECO:0000313|Proteomes:UP000007487}; 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; ADY29798.1; -; Genomic_DNA. DR RefSeq; WP_013621543.1; NC_015167.1. DR RefSeq; YP_004262669.1; NC_015167.1. DR EnsemblBacteria; ADY29798; ADY29798; Celly_1976. DR KEGG; cly:Celly_1976; -. DR PATRIC; 46918244; VBICelLyt164863_1972. DR KO; K00548; -. DR BioCyc; CLYT867900:GHJM-2013-MONOMER; -. DR Proteomes; UP000007487; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007487}; KW Methyltransferase {ECO:0000313|EMBL:ADY29798.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007487}; KW Transferase {ECO:0000313|EMBL:ADY29798.1}. SQ SEQUENCE 372 AA; 40813 MW; 95E25E25DA46CDDB CRC64; MARLSAVFFG FSKQVLQTVA TKKMPHQSLT HNTILYGTMK RIQDILKERI LVLDGAMGTM LQRYKFTEED FRGKRFADWE HPLQGNNDLL SLTQPEAIAE VHRKYFAAGA DIVETNTFSG TTIAMADYFM EDLVYELNYE SARIAKQVAD EFTAKEPHKP RFVAGSIGPT NKTASMSPDV NDPGFRGVTF DELRIAYKQQ VEALLDGGSD ILLVETIFDT LNAKAALFAI EEVKEERNID VPIMVSGTIT DASGRTLSGQ TAEAFLISIS HIPILSVGFN CALGASQLVP HLEVLAAKTD FGVSAHPNAG LPNAFGEYDE TAEQMAAQIK EYLDKSLVNI VGGCCGTTPE HINAIANLVK DYKPRNIALE TV // ID F0RPU7_DEIPM Unreviewed; 1232 AA. AC F0RPU7; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 29-APR-2015, entry version 35. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADY27403.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADY27403.1}; GN OrderedLocusNames=Deipr_2277 {ECO:0000313|EMBL:ADY27403.1}; OS Deinococcus proteolyticus (strain ATCC 35074 / DSM 20540 / JCM 6276 / OS NBRC 101906 / NCIMB 13154 / VKM Ac-1939 / CCM 2703). OG Plasmid pDEIPR01 {ECO:0000313|EMBL:ADY27403.1, OG ECO:0000313|Proteomes:UP000007718}. OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; OC Deinococcaceae; Deinococcus. OX NCBI_TaxID=693977 {ECO:0000313|EMBL:ADY27403.1, ECO:0000313|Proteomes:UP000007718}; RN [1] {ECO:0000313|EMBL:ADY27403.1, ECO:0000313|Proteomes:UP000007718} 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 {ECO:0000313|Proteomes:UP000007718}, and RC Plasmid pDEIPR01 {ECO:0000313|Proteomes:UP000007718}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002537; ADY27403.1; -; Genomic_DNA. DR RefSeq; WP_013623135.1; NC_015169.1. DR RefSeq; YP_004264263.1; NC_015169.1. DR EnsemblBacteria; ADY27403; ADY27403; Deipr_2277. DR KEGG; dpt:Deipr_2277; -. DR PATRIC; 46933036; VBIDeiPro159979_2578. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; DPRO693977:GCFA-2334-MONOMER; -. DR Proteomes; UP000007718; Plasmid pDEIPR01. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007718}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADY27403.1}; KW Plasmid {ECO:0000313|EMBL:ADY27403.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007718}; KW Transferase {ECO:0000313|EMBL:ADY27403.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 261 261 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 325 325 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 769 769 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1232 AA; 134416 MW; 521720EC8FFD0E90 CRC64; MTYTPPTPAQ PPLTAQPSLA AHPLHRALQE RILILDGAMG TMIQRHRLTE ADFRGERLRD HPLPLQGAND LLTLTQPQLI EEIHAAYFGA GADIAETNTF SSSRLGLAEY GVDDLIYELN VQGARLARRA AERYSTPERP RWVAGAIGPT NRTASMSPDV NRPGFRAVTF DELVSSYSEQ IHGLLDGGVD ALLIETVFDT LNAKAALYAA EEVFGQQGRQ VPIMVSGTIT DASGRTLSGQ TLGAFLASIS HLPLLSVGLN CALGPAELRG HVQELSASTP FFTSAYPNAG LPNALGGYDE TPQTMLDVMD EWLEQGWVNI VGGCCGTTPE HIRAFAAAAQ RRSPRVPPHP SGLPTYAGLE VLTLRPESNF LNVGERTNVT GSRRFLRLIR DRQFDEALDV AREQVEGGAQ MIDINMDEAM LDSQEAMVEF LNLIASEPDI ARVPIMLDSS RFSVIEAGLK RVQGKAVVNS ISLKEGEAEF LRQAGVLRRY GAAAVVMAFD EQGQADTLER RIAICQRAYT LLTAHGFPPQ DIIFDPNIFP VGTGIPEHDR YALDFFEAAR WIKANLPGAL VSGGVSNVSF SFRGNSAVRE AMNAAFLYHA RQAGMDMGIV NPSTLEVYSE IEPELLERVE DVLLARRPDA TERLLEYSEH VAGGAAKKER DLSWREQPVA KRLEHALVRG ITEFIVEDAE AARLELGGAL KVIEGPLMDG MNVVGDLFGS GKMFLPQVVK SARVMKQAVA HLEPYLQEGQ GQRQSAGRVV LATVKGDVHD IGKNIVGVVL ACNGFEVHDL GVMVPAERIL DEAERLQADI IGLSGLITPS LDEMVGVAEE MQRRGLGARS GGLPLLIGGA TTSRVHTAVK IAPQYGGLTV HVLDASRSVG VTARAISEQE RPGLAEEVAE QYAKAREQFA QRGERRQILP LAQARAGAPQ LSYAPVRPSF LGERPVTFNL KDLLPFIDWT PFFIGWELAG RFPQILDDEV VGEQARSLYT DAQQALRDLV EGGRLEARGV VGFWPAERRG DDVQLFTDDT RREEGATLHT LRQQGQQREG RPNRALADFV APSGDYIGGF AVGIHGAEEI IAGHKARHDD YAAIMTGLLA DRLAEAFAEA LHRQVRRELW GYAPDEELSN DDLIRERYQG IRPAPGYPAC PDHTEKGTLF RLLNARELAG LDLTESYAMT PPSAVSGLYF AHPDSGYFGV GKLGTDQVED YAARKGWSVA EAQRWLRPNL AE // ID F0RX30_SPHGB Unreviewed; 1171 AA. AC F0RX30; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADY11880.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADY11880.1}; GN OrderedLocusNames=SpiBuddy_0034 {ECO:0000313|EMBL:ADY11880.1}; OS Sphaerochaeta globosa (strain ATCC BAA-1886 / DSM 22777 / Buddy) OS (Spirochaeta sp. (strain Buddy)). OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; OC Sphaerochaeta. OX NCBI_TaxID=158189 {ECO:0000313|EMBL:ADY11880.1, ECO:0000313|Proteomes:UP000008466}; RN [1] {ECO:0000313|Proteomes:UP000008466} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1886 / DSM 22777 / Buddy RC {ECO:0000313|Proteomes:UP000008466}; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Zeytun A., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Pagani I., RA Ritalahti K.M., Loeffler F.E., Woyke T.; RT "Complete sequence of Spirochaeta sp. Buddy."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002541; ADY11880.1; -; Genomic_DNA. DR RefSeq; WP_013605733.1; NC_015152.1. DR RefSeq; YP_004246074.1; NC_015152.1. DR EnsemblBacteria; ADY11880; ADY11880; SpiBuddy_0034. DR KEGG; sbu:SpiBuddy_0034; -. DR PATRIC; 47019323; VBISpiSp132844_0038. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; SGLO158189:GHAO-34-MONOMER; -. DR Proteomes; UP000008466; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008466}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADY11880.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008466}; KW Transferase {ECO:0000313|EMBL:ADY11880.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 240 240 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 751 751 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1171 AA; 128343 MW; E5A1A5DECF08F762 CRC64; MNRTEYLKSL LSQRIVLLDG AMGTMIQSQG LAIEDFTFEG LSAYGCNEVL NLTRGEILFS IHQQYLEAGS DIIETNTFCA NAFNLAEYGL QAHVQTINQA ACEIAREAAA DFEANNEGYA FVAGVLGPTN RSLSFSPKVE DPAYRQSDFA DFHAMYLEQA RVLVQAGVDL ILIETVFDTL AAKSAILACQ DAMKEENRSL PIMVSVTFSD QSQRTLSGQT LQAFVTSLSS FDLFSLGLNC STGPDEMLPL IEQLDALCPF FVSAHPNAGF PDKEGAYALS AEGMAAQLAR AIKEQQLNIL GGCCGTTPAH IAALKAATSQ AKGRIKPQEN QNLKLSGLDD ISIDEHSLLV IGERTNVAGS RKFARLIKEG KWEEALAIAR EQVKEGAQVL DICMDASMLD AKISMRSFLR HIAGDPSVSK AAIMIDSSDW SVIEAALGEV QGRGIVNSIS LKEGEQIFIQ HAKQVSSYGH AMVVMLFDEE GQAATFERKM AIAKRSFELL TASGIKEQDI IFDANVLSIA TGIEEHDTYA RDFILATRAL KKLYPLCHTS GGVSNLSFSF RGNDAIRTAM HAVFLSLAEL DMAIINPSSL IAFESLDEKT RTIIQKALLA EDGDLSTIRA NLIALALEMQ EDEKPQLQKA DRRERSASQR LFDAILAGDH AYLEPDLKEL EGENPLTLVE GTLMDGMKEV GRLFGLGKLF LPQVVRSART MKLAVDILQP RITEYLELNT NETGSQKKPV AVMATVKGDV HDIGKNIVNL ILRCNGFEVI DLGVMVPPEA IWEAAIRHKA DLVGLSGLIT PSLKEMETVI KLFEKKGSSL PIFVGGATTS EIHTAVKLSV LYSEAVIQTK DASAMALAAK QVVGPQSLAY KNEVRTTYQQ LRKDHELPLK EKTTSGYEQA LIQSKQKQQG SKAASYGVFT KTDFCLKDLS AHINWRMYCS AWKVPFESQE GRNLIEEAKE LLDKPEICAL FEHGCSIVYG LFPASSDRLE VRVGQRSFYF LRDELSGLCL ADMIATDDTV GLFVSTSSLA LAPYLEQLQA EGNTMQLFSL KLLGDRLAEV LAQTAENLLK QAWEADELSF IRPAPGYPSW NDHSEKQTLF SLLDATQNIG VRLTESFAMD PPSSVCGMLI GGENLRYFGL KQVSEEQYSL YAKRKGVSAQ MLATLLSGME Y // ID F0S0B5_DESTD Unreviewed; 844 AA. AC F0S0B5; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 29-APR-2015, entry version 26. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADY73794.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADY73794.1}; GN OrderedLocusNames=Dester_1158 {ECO:0000313|EMBL:ADY73794.1}; OS Desulfurobacterium thermolithotrophum (strain DSM 11699 / BSA). OC Bacteria; Aquificae; Desulfurobacteriales; Desulfurobacteriaceae; OC Desulfurobacterium. OX NCBI_TaxID=868864 {ECO:0000313|EMBL:ADY73794.1, ECO:0000313|Proteomes:UP000007102}; RN [1] {ECO:0000313|Proteomes:UP000007102} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11699 / BSA {ECO:0000313|Proteomes:UP000007102}; 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 ----------------------------------------------------------------------- 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; ADY73794.1; -; Genomic_DNA. DR RefSeq; WP_013638746.1; NC_015185.1. DR RefSeq; YP_004281853.1; NC_015185.1. DR EnsemblBacteria; ADY73794; ADY73794; Dester_1158. DR KEGG; dte:Dester_1158; -. DR PATRIC; 46943016; VBIDesThe167085_1199. DR KO; K00548; -. DR OMA; TWTFPRQ; -. DR BioCyc; DTHE868864:GHGF-1193-MONOMER; -. DR Proteomes; UP000007102; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007102}; KW Methyltransferase {ECO:0000313|EMBL:ADY73794.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007102}; KW Transferase {ECO:0000313|EMBL:ADY73794.1}. SQ SEQUENCE 844 AA; 91962 MW; BC0E2A53B136BDAF CRC64; MKENPFRDSE KIWVLDGGMG TMLMRKGVDV NYAPELLNME KPEILKEIHR EYIEAGADII ETNTFGSNRI KLSHYGLENR VKELTAAGVR IAKEAAKDKA LVALSVGPTG VFVEPVGDYT FDELVDVFKE QIEAGAEAGA DLVLIETMSD TKEAKAAVVA AQEVCDLPIM VSMTYQADGR TLLGTPPEVS AAIFEGFGVA AIGANCSLGP ESFVDLIKRM ANITDTPIII YANAGLPVLK DGKTYYPEPP ETFEKYAPLF VEAGANIIGG CCGTTPEHIK AIKEAVKTLK PIKKNPTKGL KVASRTELVI IGTNHPTRII GERINPTGKK KLQEALKKKD FSLVKEEAKK QVEEGADILD VNVGVPGINE AQAMEKAVRT VIETVNVPIM IDSKDPEAVE RALKMCDGKP IVNSCSGEEK DIKNILPLVK KYGANILVLG IDDEGLKEKA EDRAAIIDKL VEECQKLEIP KDFIIADVLN LAASAMQEAT RETLKAIRIV KERHGIATTL GVSNVSFGLP GRSLLNSSFM AMAIEAGLDS GIVNPADSRM VETIYASDVL VGKDKGATRY VEKFQNYKPK TEDKECRELL RKICQISCAF LEGEKISFEV ESEGKKKKKS LEEDKSKEDE SIPPGILGKI FKKVLEGDKE GIIKPTEEAL KEFEPMEISD KALIPALDVV GQRFEKGEIF LPQMLRSAQA VQSAFEIIKR EVKKRGGNVK VDGKIVMATV YGDVHEIGKN IVITMLENSG FEVIDLGTNV PPEKIVEVAK KEKADVVGLS ALMTTTLPSM EETIKKLREA GLDVPVIVGG AVVTPEYAKE IGGHYSEDAQ EAVKIVRKIL NISD // ID F0SDG7_PEDSD Unreviewed; 1216 AA. AC F0SDG7; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 32. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ADY53950.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADY53950.1}; GN OrderedLocusNames=Pedsa_3416 {ECO:0000313|EMBL:ADY53950.1}; 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 {ECO:0000313|EMBL:ADY53950.1, ECO:0000313|Proteomes:UP000000310}; RN [1] {ECO:0000313|Proteomes:UP000000310} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51119 / DSM 12145 / JCM 21818 / LMG 10337 / NBRC 100064 / RC NCIMB 13643 {ECO:0000313|Proteomes:UP000000310}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002545; ADY53950.1; -; Genomic_DNA. DR RefSeq; WP_013634433.1; NC_015177.1. DR RefSeq; YP_004275772.1; NC_015177.1. DR EnsemblBacteria; ADY53950; ADY53950; Pedsa_3416. DR KEGG; psn:Pedsa_3416; -. DR PATRIC; 47007778; VBIPedSal163994_3545. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; PSAL762903:GHB2-3480-MONOMER; -. DR Proteomes; UP000000310; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000310}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADY53950.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000310}; KW Transferase {ECO:0000313|EMBL:ADY53950.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 242 242 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 753 753 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1216 AA; 135281 MW; E83E0EFB38BEC932 CRC64; MDIREELKKR ILVIDGAMGT MIQNYKLTEQ DFRGERFKDH TCDVKGNNDL LNITRPDIIK AIHKEYLLAG ADIIETNTFS TQRISMADYH MEDLSYELSY EGAKIAKEVA TEVTALNPDK PRFVAGAIGP TNRTLSISPN VNDPGFRAIS FDELESAYYE QVRGLVDGGA DLLLVETIFD TLNAKAAIFA IKKYEQVIGR KIEIMISGTI TDASGRTLSG QTTEAFWNSM RHGDLLSIGL NCALGAKDMR PYIQELSELA DVFVSAYPNA GLPNEFGQYD ETAEQTAGLL DDFLSSGFLN MVGGCCGTTP QHIKRIAETA AKYTPRKIAQ PERWMRLSGL EAVNIKPDSI FVNIGERTNI TGSPKFSKLI LSGDYETALS VARQQVEGGA QVIDVNMDEG MLDSVAAMTK FLNLISSEPD ICKVPVMVDS SKWEVIEAGL KCLQGKGIVN SISLKEGEEK FKESARKIKQ YGAATVVMAF DEKGQADNYE RRIEICKRSY DILVNEVNFP AEDIIFDPNI LTVGTGLEEH ANYAVDFINA TRWIKENLPY AKVSGGVSNI SFSFRGNNPV REAMHSAFLF HAIKAGLDMG IVNAGMLEVY EEIEPELLIK VEDVLLNRRP DATEILVDFA ETVKNKGKVI VKDEEWRKGT VEERLSHALV KGIVAHIDED VEEARLKYAR PLEIIEGPLM DGMGVVGDLF GSGKMFLPQV VKSARVMKKA VAILLPYIEA EKVEGESSSA GKILMATVKG DVHDIGKNIV GVVLACNNFE IIDLGVMVPA TTILEEARKH NVDIIGCSGL ITPSLDEMVH IAKEMEREGF KIPLMIGGAT TSRIHTAVKI DPNYSGPVIH VLDASRSVTV CSNLLNTETN AEYKQQIKED YAKTRDNYNK KRVDKTLRDI KTAREEQFKI DWNEGLPKVP NFIGTKTIEG YPLEELLPYI DWTPFFHAWE LRGAYPRILQ DETVGKEAQK LFDDAQTLLK RIIEEKLLTA KAVFGLWPAN SKGDDIVLNV EGNETVIHTL RQQNQKPAGE PYYALSDFIA PESTGLQDYF GAFAVSTGFG CDELVAEFEK DFDDYNSIMT KALADRLAEA FAEKLHELVR TEYWGYATQE KLSNEELIKE KYQGIRPAPG YPACPDHTEK GTLFSMLDVE NRIGLKLTES FAMYPTAAVS GYYFAHPQSR YFGVGKIAKD QVEDYAKRKG MDLETTEKWL SPNLGY // ID F0SLW7_PLABD Unreviewed; 1226 AA. AC F0SLW7; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ADY59892.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADY59892.1}; GN OrderedLocusNames=Plabr_2290 {ECO:0000313|EMBL:ADY59892.1}; 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 {ECO:0000313|EMBL:ADY59892.1, ECO:0000313|Proteomes:UP000006860}; RN [1] {ECO:0000313|Proteomes:UP000006860} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49424 / DSM 5305 / JCM 21570 / NBRC 103401 / IFAM 1448 RC {ECO:0000313|Proteomes:UP000006860}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002546; ADY59892.1; -; Genomic_DNA. DR RefSeq; WP_013628616.1; NC_015174.1. DR RefSeq; YP_004269914.1; NC_015174.1. DR EnsemblBacteria; ADY59892; ADY59892; Plabr_2290. DR KEGG; pbs:Plabr_2290; -. DR PATRIC; 47013692; VBIPlaBra152897_2469. DR KO; K00548; -. DR BioCyc; PBRA756272:GH5Q-2323-MONOMER; -. DR Proteomes; UP000006860; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006860}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADY59892.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006860}; KW Transferase {ECO:0000313|EMBL:ADY59892.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 249 249 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 762 762 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1226 AA; 136987 MW; 086F0B774B5512B4 CRC64; MTAVLQNNTF DALNQILEDR ILLLDGAMGS MILDHRPTED DYRGEQFKNH HIDLKNANDV LCLTQPDLIR KLHREYFEAG SDIVESNTFN ANVISMEEFG LAEYTYEINK RAIELAKEVA DEFTKKNPDK PRFVAGSIGP TKVQLSMNAN EAGTRPVTYD QMVTSYREQI NGMIDGGVDI LLPETSFDTL NTKACLFAIS QIFAERNIFL PVMVSGTIFP GGRSLTAQTV GAFYTSVSHF PLFSVGLNCA LGPKQMRPFV EELAKIAQCR ISCYPNAGMP DGMGGFDSSP QEVAAALREF AQDKWVNLVG GCCGTTPDYI REIGKQTSDL KSRAYPAYPR HSSYSGLERY EVRPETNFLM VGERTNVTGS RKFARLIREE KYDEALSVAR EQVEAGANII DVNMDEGLLD SVACMRKFLW LISDDGDISV PIMIDSSNWE VIEEGLKCVQ GKPIVNSISI KDDEARFIAQ AKKIRQYGAA VVVMAFDEQG QADTADRKVE ICKRAYKILT EQVGFPPEDI IFDPNILTVG TGMEEHNNYA VEFFEAVRRI KQECPGALTS GGVSNVSFSF RGNNVVREAM NAAFLYHAIQ AGLDMGIVNA SQLEVYEEID KELLEYIEDV LLNRREDATE RLLEYADKIK DQNQDPATAK KVAEWRNGTV EERLQHALLK GITDYIDEDT AEALEKYGRP LNVIQGPLMD GMNVVGELFG TGKMFLPQVV KSARVMKKSV AYLTPFMEAE KEAAGTGARG TFLIATVKGD VHDIGKNIVA VVLRCNNFDV IDLGVMVPAD KILDTAVEVG ADVIGLSGLI TPSLEEMVAV AQEMKRRGMT TPLLIGGATT SAKHTAVKIA PEYDHIVAHV GDASLSVPVV ESLIDAERKV AFDEKNRAAQ QRDRDMFGKR QERTMIPYTD ALERRFQTDW DNIDIPTPEF LGLRNLEDFP LAEIREYIDW SPFFMTWGLI GKYPKIFKDE QVGEEAKKIY KDANDLLDKV IAEKWLTAKG VYGFWPANSD GDDILVFDPE DAEREICRFP MLRQQWERRG QKDFRSLADY IAPLSSGRKD YLGAFAVTGG LGIEEPLARL EKDNDDYTSI MLKAVADRLA EAFAECLHAR ARREWHYGKT EGLTNEQLIA EKYRGIRPAF GYPACPDHTP KRALFDLLEA TPRAQIELTE SMAMMPASSV SGLYFAHPES RYFSVMHITE DQLVDYAPRA GMDLETARKW LAPVLS // ID F0SMI0_PLABD Unreviewed; 293 AA. AC F0SMI0; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADY57742.1}; GN OrderedLocusNames=Plabr_0112 {ECO:0000313|EMBL:ADY57742.1}; 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 {ECO:0000313|EMBL:ADY57742.1, ECO:0000313|Proteomes:UP000006860}; RN [1] {ECO:0000313|Proteomes:UP000006860} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49424 / DSM 5305 / JCM 21570 / NBRC 103401 / IFAM 1448 RC {ECO:0000313|Proteomes:UP000006860}; 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 ----------------------------------------------------------------------- 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; ADY57742.1; -; Genomic_DNA. DR RefSeq; WP_013626486.1; NC_015174.1. DR RefSeq; YP_004267764.1; NC_015174.1. DR EnsemblBacteria; ADY57742; ADY57742; Plabr_0112. DR KEGG; pbs:Plabr_0112; -. DR PATRIC; 47008959; VBIPlaBra152897_0133. DR KO; K00547; -. DR BioCyc; PBRA756272:GH5Q-115-MONOMER; -. DR Proteomes; UP000006860; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006860}; KW Methyltransferase {ECO:0000313|EMBL:ADY57742.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006860}; KW Transferase {ECO:0000313|EMBL:ADY57742.1}. SQ SEQUENCE 293 AA; 31150 MW; 2CABCC561A4821AA CRC64; MQRSISQFLA ETEDWILLDG PMGTRLAELG YSVDRQPGWS AQALVDVPEL VEQVHREYVA AGATAVTANT FRTHAVNLAA WGMQTKAKSL TSLAVQLARQ AAEGKAWVLG SQAPVGDCYS PNETPSAGEL RAAHREMAEN LNAAGVDAVL LETHVSQQEA LIALEAVTET GLPALLSVVA RDETHLLDGS SLQDLAEQAA EYRPLAIGAN CIPVERMGGA LNALQSGFAG PLIAYANTGE MLPDGSWRPT AGSDPEVHSE FAQRWISQGV RILGTCCGCG PRWIEKISCL PGH // ID F0SRN2_PLABD Unreviewed; 316 AA. AC F0SRN2; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 29-APR-2015, entry version 19. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADY59155.1}; GN OrderedLocusNames=Plabr_1544 {ECO:0000313|EMBL:ADY59155.1}; 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 {ECO:0000313|EMBL:ADY59155.1, ECO:0000313|Proteomes:UP000006860}; RN [1] {ECO:0000313|Proteomes:UP000006860} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49424 / DSM 5305 / JCM 21570 / NBRC 103401 / IFAM 1448 RC {ECO:0000313|Proteomes:UP000006860}; 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 ----------------------------------------------------------------------- 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; ADY59155.1; -; Genomic_DNA. DR RefSeq; WP_013627883.1; NC_015174.1. DR RefSeq; YP_004269177.1; NC_015174.1. DR EnsemblBacteria; ADY59155; ADY59155; Plabr_1544. DR KEGG; pbs:Plabr_1544; -. DR PATRIC; 47012028; VBIPlaBra152897_1650. DR BioCyc; PBRA756272:GH5Q-1566-MONOMER; -. DR Proteomes; UP000006860; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006860}; KW Methyltransferase {ECO:0000313|EMBL:ADY59155.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006860}; KW Transferase {ECO:0000313|EMBL:ADY59155.1}. SQ SEQUENCE 316 AA; 34485 MW; 0BC55EB520FF02D1 CRC64; MTVTRDSNRS PLPEAGQFYV TAAGFETELL FLDKIELPEF CSGILLESPA GRKRLRDYCQ QFISLATRHQ CGLVLGTPTW RLNPDWAEKL GFNAIEQRRL HYAAVQLLED LRYNGPVPAE QFVISGNIGP RFDGYMVANV MSPAEAADYH SQQIRLLGEA GVDCIAALTM TTSNEAAGVA LAAQQAEIPV IISFTVETDG RMPSGETLGE AIQSVDEAAP GAVAYYGINC AHPTHFRNEL EKGAGWRARI GALWANASTM SHAELDNCTE LDSGDPDDLA ERYRQLKALL PGLRVFGGCC GTDIRHVSRI CETCCE // ID F0SRN3_PLABD Unreviewed; 316 AA. AC F0SRN3; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADY59156.1}; GN OrderedLocusNames=Plabr_1545 {ECO:0000313|EMBL:ADY59156.1}; 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 {ECO:0000313|EMBL:ADY59156.1, ECO:0000313|Proteomes:UP000006860}; RN [1] {ECO:0000313|Proteomes:UP000006860} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49424 / DSM 5305 / JCM 21570 / NBRC 103401 / IFAM 1448 RC {ECO:0000313|Proteomes:UP000006860}; 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 ----------------------------------------------------------------------- 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; ADY59156.1; -; Genomic_DNA. DR RefSeq; WP_013627884.1; NC_015174.1. DR RefSeq; YP_004269178.1; NC_015174.1. DR PRIDE; F0SRN3; -. DR EnsemblBacteria; ADY59156; ADY59156; Plabr_1545. DR KEGG; pbs:Plabr_1545; -. DR PATRIC; 47012030; VBIPlaBra152897_1651. DR BioCyc; PBRA756272:GH5Q-1567-MONOMER; -. DR Proteomes; UP000006860; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006860}; KW Methyltransferase {ECO:0000313|EMBL:ADY59156.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006860}; KW Transferase {ECO:0000313|EMBL:ADY59156.1}. SQ SEQUENCE 316 AA; 34997 MW; 56ECD2E1029EA2C0 CRC64; MNTGTSTQRV KLPEAGRFFV TDAGLETELV FLDEWDLPEF CAATLLETPE GRNRLRRYFS DFIELAKRHA CGIVLETPTW RLNPDWAEKL GYSGTDRRRL NFAAVHLLQD LRLAASLPED QFVVSGNLGP RFDGYKADRV MTPQEAAAYH GDQVETLRDA GVDCITAMTI TNSNEAAGIA MAAREAGMPA VVSFTVETDG RLPSEETMRE AIEAVEKYAP EAVSYFGINC AHPTHFHEAL QAEEEWLSRI GFIRANASTM SHAELDNCSE LYAGDPGDLA ERYRQLKALL PGLRVFGGCC GTDVRHVSHI CETCCQ // ID F0SYH1_SYNGF Unreviewed; 1161 AA. AC F0SYH1; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 29-APR-2015, entry version 28. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ADY57083.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADY57083.1}; GN OrderedLocusNames=Sgly_2813 {ECO:0000313|EMBL:ADY57083.1}; OS Syntrophobotulus glycolicus (strain DSM 8271 / FlGlyR). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Syntrophobotulus. OX NCBI_TaxID=645991 {ECO:0000313|EMBL:ADY57083.1, ECO:0000313|Proteomes:UP000007488}; RN [1] {ECO:0000313|Proteomes:UP000007488} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 8271 / FlGlyR {ECO:0000313|Proteomes:UP000007488}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002547; ADY57083.1; -; Genomic_DNA. DR RefSeq; WP_013625903.1; NC_015172.1. DR RefSeq; YP_004267084.1; NC_015172.1. DR EnsemblBacteria; ADY57083; ADY57083; Sgly_2813. DR KEGG; sgy:Sgly_2813; -. DR PATRIC; 47036663; VBISynGly105927_3018. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; SGLY645991:GHJ4-2876-MONOMER; -. DR Proteomes; UP000007488; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007488}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADY57083.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007488}; KW Transferase {ECO:0000313|EMBL:ADY57083.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 225 225 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 720 720 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1161 AA; 128619 MW; F4126A6F926EDF98 CRC64; MDLFKTQLEK KILILDGAMG TMLQRHQLKP DDFGQPEYDG CNEILNLSQP DLIKAIHEAY LDAGADIIET NSFGATNVVL EEYGLADRDI ELNEISARLA REAADARSTK AWPRFVAGSM GPTIRMLTLS AGITFEELEE AYYRQALGLI KGGADLLLVE TCQDTLNVKA AGIGIGRAFH GLGKEIPIMI SCTIEPSGTM LAGQNIQAFY LSVKHLNPAV IGLNCGTGAD GMREHVRTLA GIASCAVSCH ANAGLPDEEG NYLEQPRAFA AKQAEFARNG WLNIAGGCCG TTPEHIKALA EELRDCRPRA GKQKAESAVS GIEPLWLEKT GRPILVGERS NVIGSRLFRD LIVGEHYEEG SEVARGQVKK GAHVVDICVA NPDRDEYHDM VNFLSYVVKK VKVPLMLDST DAQVVEAGLK MIQGKAIINS INLENGLERF EQIVPLIHKY GAAIVVGLID EQGMALSRED KLRVAERSCQ LLTERYALQP GDIIFDPLTF PVGTGDPKYL GSAKETIEGL RLIKEKIPAC KTILGVSNVS FGLPTVGREV LNAVFVHHNT LAGLDYAIVN AEKHKSYADI PEEERKLAED LLFQTNDRTL KNFTDFYRDK KAVPVHVQEQ LSWDQRLARN IVDGSKEGLE ADLSEGLKTH TPLELINGPL LKGMDEVGRL FNRNMLIVAE VLQSAEVMKA AVGILEKHMD KTEEAIKGKL ILATVKGDVH DIGKNLVEII LSNNGYQVIN LGVKVSPEEI IKACREHKPD AVGLSGLLVK SVQQMLVTAQ EMRAENIKVP LILGGAALSR KFTEEKIAPA YDAPAFYCQD AMEGLKVLQE YLYAHKDTVI KANQDKGIDR RDEEARKRKT FAQESRDTHP LNETGLLRSQ TDQIARPLPG PIYVPSDLQR HVLLDFPLQE IIRDIDVKSL MKFYLGIGKK KPDTLQEMGS GFVRDTREEE LAHTIQQLFN EIVDQKMIKA RGVYRFLPAR SAGNLVRILN PENHEEIQAE FLFPRQTAEP FLSPADYIQN PINGKTDYLG LFTVTTGVGL REKAQALKDG GQYLKSYLLQ VISLKMAEAM AEKVHEIMRK EWGLPEREVS GNKEKNRRRY QGIRLSPGYP LCPDLEAQRQ IFKLLQPEDI GITLTESLMM DPEASVSALV FAHPEARIFS L // ID F0SZ11_SYNGF Unreviewed; 613 AA. AC F0SZ11; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 26. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=Sgly_2859 {ECO:0000313|EMBL:ADY57129.1}; OS Syntrophobotulus glycolicus (strain DSM 8271 / FlGlyR). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Syntrophobotulus. OX NCBI_TaxID=645991 {ECO:0000313|EMBL:ADY57129.1, ECO:0000313|Proteomes:UP000007488}; RN [1] {ECO:0000313|Proteomes:UP000007488} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 8271 / FlGlyR {ECO:0000313|Proteomes:UP000007488}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ADY57129.1; -; Genomic_DNA. DR RefSeq; WP_013625949.1; NC_015172.1. DR RefSeq; YP_004267130.1; NC_015172.1. DR EnsemblBacteria; ADY57129; ADY57129; Sgly_2859. DR KEGG; sgy:Sgly_2859; -. DR PATRIC; 47036754; VBISynGly105927_3063. DR OMA; NEVPGIQ; -. DR BioCyc; SGLY645991:GHJ4-2922-MONOMER; -. DR Proteomes; UP000007488; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007488}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ADY57129.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000007488}; KW Transferase {ECO:0000313|EMBL:ADY57129.1}. SQ SEQUENCE 613 AA; 68099 MW; A4AD66421E14F67D CRC64; MKKGSHQTQV KTKQEQRNEV EMNIREYLKT NTLIFDGAMG TYYAQLEKKP LVKCEMANIH DEEAILRIHH EYIRAGCMAI KTNTFGANVT CLDCPFEGVE EVIRKGYELA RRAVAGSGVY LFADIGPIPF RDNENLFAEY QKIADLFLDL GAVNFLFETF SSAEYLAQIA AYIKEKSPQA FIITEFAVSP DGYTRQGNSG FQIFEELSGE NSIDAIGFNC ISGPYHLLQL AKKLEAKDKF VSIMPNAGYP TVIDNRTFFE NNAGYFADQM LEMAKEGIAI LGGCCGTAPE FIRKTAAKIK SLSLPEPAVK RIKITEGKPA AQAENPLMEK IRQGEKIIAV ELDPPANTDI DFLMRSAQKL QENKVDAITI ADCPIARARV DSSLLACKLK KELGVTPIPH MTCRDRNINA TKALLLGLNI EGVNNVLVVT GDPIPSAQRD EVKARSNFNS AILANYIRTL NENTFARPFT IYGALNVNAR NFEAQLKHAR KKIENGVSVF LTQPILTKKA LENLQEASRV LPAKILGGIL PIVSYKNACF MNNEISGIDV SPEIMDLYEN ASKEQARNLA VDISTRMVRE ISAYVDGYYL ITPFQRLDIV TDILENMLQS QAG // ID F0TEU5_LACA3 Unreviewed; 331 AA. AC F0TEU5; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:ADZ07161.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ADZ07161.1}; GN Name=mmuM {ECO:0000313|EMBL:ADZ07161.1}; GN OrderedLocusNames=LAC30SC_05050 {ECO:0000313|EMBL:ADZ07161.1}; OS Lactobacillus acidophilus (strain 30SC). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=891391 {ECO:0000313|EMBL:ADZ07161.1, ECO:0000313|Proteomes:UP000007491}; RN [1] {ECO:0000313|EMBL:ADZ07161.1, ECO:0000313|Proteomes:UP000007491} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=30SC {ECO:0000313|EMBL:ADZ07161.1, RC ECO:0000313|Proteomes:UP000007491}; RX PubMed=21478365; DOI=10.1128/JB.00343-11; RA Oh S., Roh H., Ko H.J., Kim S., Kim K.H., Lee S.E., Chang I.S., RA Kim S., Choi I.G.; RT "Complete genome sequencing of Lactobacillus acidophilus 30SC, RT isolated from swine intestine."; RL J. Bacteriol. 193:2882-2883(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=30SC; RA Roh H., Ko H.-J., Kim S.-H., Choi I.-G., Oh S.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002559; ADZ07161.1; -; Genomic_DNA. DR RefSeq; WP_013641836.1; NC_015214.1. DR RefSeq; YP_004292100.1; NC_015214.1. DR EnsemblBacteria; ADZ07161; ADZ07161; LAC30SC_05050. DR KEGG; lai:LAC30SC_05050; -. DR PATRIC; 46964792; VBILacAci171603_1002. DR KO; K00547; -. DR OMA; SEWCKDG; -. DR BioCyc; LACI891391:GHOY-1031-MONOMER; -. DR Proteomes; UP000007491; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007491}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ADZ07161.1}; KW Transferase {ECO:0000313|EMBL:ADZ07161.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 223 223 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 331 AA; 37338 MW; 55EA2E00B8AFF51F CRC64; MDLIKQISSK GLVLDGAMST ALEKQGIDTN TDLWTAVALD KDLDKVYKVH MNYFQAGAQM AITDTYQANV QAFEKHGYSE DKAKEMIADA VKIAKKARDD FEKKTGIHNY VAASVGSYGA YLAEGDEFRG DYDLTKKQYL DFHLPRLQVL LQNKPDCLAI ETQPKLDEVV VLLDWLKENA PEMPVYVSFT LHDTTKISDG TPLKKVMEKI NEYDQVFAVG ANCFKPFLAT TAIDKMREFT KKNIIVYPNL GGIYNEFERN WIPFNAKFDF GKLSKECYEH GACIIGGCCS TGVKEISQIA AFYKILNNQK SKQKLDLKPN INLMKSTRSK V // ID F0VH67_NEOCL Unreviewed; 431 AA. AC F0VH67; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 29-APR-2015, entry version 18. DE SubName: Full=Complete genome, chromosome VIIb {ECO:0000313|EMBL:CBZ53061.1}; GN ORFNames=NCLIV_028500 {ECO:0000313|EMBL:CBZ53061.1}; OS Neospora caninum (strain Liverpool). OC Eukaryota; Alveolata; Apicomplexa; Conoidasida; Coccidia; OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Neospora. OX NCBI_TaxID=572307 {ECO:0000313|EMBL:CBZ53061.1, ECO:0000313|Proteomes:UP000007494}; RN [1] {ECO:0000313|Proteomes:UP000007494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Liverpool {ECO:0000313|Proteomes:UP000007494}; RX PubMed=22457617; DOI=10.1371/journal.ppat.1002567; RA Reid A.J., Vermont S.J., Cotton J.A., Harris D., Hill-Cawthorne G.A., RA Konen-Waisman S., Latham S.M., Mourier T., Norton R., Quail M.A., RA Sanders M., Shanmugam D., Sohal A., Wasmuth J.D., Brunk B., RA Grigg M.E., Howard J.C., Parkinson J., Roos D.S., Trees A.J., RA Berriman M., Pain A., Wastling J.M.; RT "Comparative genomics of the apicomplexan parasites Toxoplasma gondii RT and Neospora caninum: Coccidia differing in host range and RT transmission strategy."; RL PLoS Pathog. 8:e1002567-e1002567(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; FR823389; CBZ53061.1; -; Genomic_DNA. DR RefSeq; XP_003883093.1; XM_003883044.1. DR GeneID; 13443170; -. DR InParanoid; F0VH67; -. DR Proteomes; UP000007494; Chromosome VIIb. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 3. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 3. DR SUPFAM; SSF82282; SSF82282; 3. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007494}; KW Reference proteome {ECO:0000313|Proteomes:UP000007494}. SQ SEQUENCE 431 AA; 45876 MW; 2A0C97BD521FB484 CRC64; MPGSCFTEDV VLLDGGLGTH LRALGAEFNG DPLWASKAVL VAPDLVRRAH YDFYHAGADV AITATYQASL TGFAKIGLSP SNAHEAVALA INLAAEARQL DEDGDAPACS SAGDERENEG PEARTPEAPS TAGKGGFQEV HARDADRPRR RRNRKIFVSN GSYGSALGGG AEYRGNYGVS EEVFHDYHRW RLQAALELEH LVDGVVFETL PESAEAKAIV SLLREFPSLR GKTWISFTCK SPTQLANGED FRSAVADVLK LDGRDCYISG IGVNCLPVST TVPLLCSPPL RDSLAVSLEK SRDPWNLHVV CYPNNEGARN AAATSAKPES PEVCQELVHG AAPRECDLVD RTTASAPTKM TYLAESAPDG QCGHATLPAN PSSRDFSLKH PLASQVSAWL KGGVSAVGGC CGTSPEDVKE IGAVLENLRV R // ID F0WMI1_9STRA Unreviewed; 354 AA. AC F0WMI1; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 01-OCT-2014, entry version 14. DE SubName: Full=Putative uncharacterized protein ALNC14_086560 {ECO:0000313|EMBL:CCA22513.1}; GN ORFNames=ALNC14_086560 {ECO:0000313|EMBL:CCA22513.1}; OS Albugo laibachii Nc14. OC Eukaryota; Stramenopiles; Oomycetes; Albuginales; Albuginaceae; OC Albugo. OX NCBI_TaxID=890382 {ECO:0000313|EMBL:CCA22513.1}; RN [1] {ECO:0000313|EMBL:CCA22513.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=21750662; DOI=10.1371/journal.pbio.1001094; RA Kemen E., Gardiner A., Schultz-Larsen T., Kemen A.C., Balmuth A.L., RA Robert-Seilaniantz A., Bailey K., Holub E., Studholme D.J., RA Maclean D., Jones J.D.; RT "Gene gain and loss during evolution of obligate parasitism in the RT white rust pathogen of Arabidopsis thaliana."; RL PLoS Biol. 9:e1001094-e1001094(2011). RN [2] {ECO:0000313|EMBL:CCA22513.1} RP NUCLEOTIDE SEQUENCE. RA MacLean D.; 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; FR824202; CCA22513.1; -; Genomic_DNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 354 AA; 39660 MW; A273F2C77272AD4A CRC64; MRVFQFKSER FPNANASIHK KSLLHNVLIL DGGLSTEIEN YDGIRLSEGC LWSARLLLPQ NAHLQQAIVH AHSNYFRSGA EIATTSSYQV SLDGLLREFK GDIGTAQPLL LPMLNKSIEL ASIARDTQYR IQDNSNKPMI AASIGCFGAA LADGSEYRGQ YTLNVDQLVS WHLDRFRALA LHPQTDILIF ETIPCIIEVE AIVRLLNSHS EMIQKRQLKV IIAVACRNES QLNSGEPIFK LTETIQSIRC QENLIGIGIN CTNPKFVESL LKSFSCSCDK IVYPNSGEEW NANAKQWERP NGTQSATACL TDWETYLPRW YDAGARIFGG CCRTSPKDIA AIRNYFTNTP NQMN // ID F0WPV1_9STRA Unreviewed; 381 AA. AC F0WPV1; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 01-OCT-2014, entry version 14. DE SubName: Full=Putative uncharacterized protein AlNc14C191G8442 {ECO:0000313|EMBL:CCA23352.1}; GN Name=AlNc14C191G8442 {ECO:0000313|EMBL:CCA23352.1}; GN ORFNames=ALNC14_094950 {ECO:0000313|EMBL:CCA23352.1}; OS Albugo laibachii Nc14. OC Eukaryota; Stramenopiles; Oomycetes; Albuginales; Albuginaceae; OC Albugo. OX NCBI_TaxID=890382 {ECO:0000313|EMBL:CCA23352.1}; RN [1] {ECO:0000313|EMBL:CCA23352.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=21750662; DOI=10.1371/journal.pbio.1001094; RA Kemen E., Gardiner A., Schultz-Larsen T., Kemen A.C., Balmuth A.L., RA Robert-Seilaniantz A., Bailey K., Holub E., Studholme D.J., RA Maclean D., Jones J.D.; RT "Gene gain and loss during evolution of obligate parasitism in the RT white rust pathogen of Arabidopsis thaliana."; RL PLoS Biol. 9:e1001094-e1001094(2011). RN [2] {ECO:0000313|EMBL:CCA23352.1} RP NUCLEOTIDE SEQUENCE. RA MacLean D.; 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; FR824236; CCA23352.1; -; Genomic_DNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 2. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 381 AA; 42297 MW; B11A310A316E1501 CRC64; MSSDVKRTVS MFLSTALSII EKFQENQNAT FFKSSLKRHF HLFTVSPSKT IMPSPHEKQS TFVIAGGIRE ELFSRGLQDN LNLRSASALV DPKKHSSILN IHEEYLLAGA SHLITCNYDV VPGRGFTPDE IVQFTRLAGR LALTARTNAE SNEANFPATV CGSLPPLYPS FRYDRTFDAE GLKRTYLLIA ESLWSFCDVY IAESMSSIAE AKLAFEAVEH LGKPIIVSFA LNTAGGLRSG QDVIQAYEQM ILFHKSRVEL ERETASPKLE AILFDSSQPE DIAKAIKRLS KSESILAQMR EHSIHWGGYG DHISPTSRAG FLEERIAPGA LNSKLDVEIF NGFMQKWKAL GARYVGGCCG IGPEYIQVLR QNLSTPTCLR P // ID F0XQN6_GROCL Unreviewed; 380 AA. AC F0XQN6; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 07-JAN-2015, entry version 14. DE SubName: Full=Homocysteine s-methyltransferase {ECO:0000313|EMBL:EFW99907.1}; GN ORFNames=CMQ_225 {ECO:0000313|EMBL:EFW99907.1}; 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 {ECO:0000313|Proteomes:UP000007796}; RN [1] {ECO:0000313|EMBL:EFW99907.1, ECO:0000313|Proteomes:UP000007796} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=kw1407 / UAMH 11150 {ECO:0000313|Proteomes:UP000007796}; 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; GL629807; EFW99907.1; -; Genomic_DNA. DR InParanoid; F0XQN6; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000007796; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007796}; KW Methyltransferase {ECO:0000313|EMBL:EFW99907.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007796}; KW Transferase {ECO:0000313|EMBL:EFW99907.1}. SQ SEQUENCE 380 AA; 41299 MW; E8A307443359F722 CRC64; MANCPIRILD GGLGTSLQDR YGVEFSSAAT PLWSSHLLAT GPQSEPETLL QRCQADFCRA GADVLETATY QISTAGLART RVLPDHPDGI VEPADVYQFL ERAVAVAEAA GNVETEAKTT KHETAPSIAL SLGPYGACMI PSTEYSGAYD FDGRNTTALR RWHADRLRLF DVGVNRLADR VRYLAFETVP RLDEIVAVRQ LYNVSGNHGD TDTIPSRLAA LPYWISCVFP GDSAHEPPAT LPDGSTVEQA VEAMLTSSSS THLPWGIGIN CTKIGRLPQL IERYEAAVES LVATGRLSDW PALVLYPDGT NGEVYNTTTQ RWEMPAGVSA PKDPWEAQLS QMVLDAASRG KWREILVGGC CKATDRDIKA LKASLREPRP // ID F0YQ22_AURAN Unreviewed; 342 AA. AC F0YQ22; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 04-FEB-2015, entry version 23. DE SubName: Full=Putative uncharacterized protein HMT1 {ECO:0000313|EMBL:EGB02788.1}; DE Flags: Fragment; GN Name=HMT1 {ECO:0000313|EMBL:EGB02788.1}; GN ORFNames=AURANDRAFT_34875 {ECO:0000313|EMBL:EGB02788.1}; OS Aureococcus anophagefferens (Harmful bloom alga). OC Eukaryota; Stramenopiles; Pelagophyceae; Pelagomonadales; Aureococcus. OX NCBI_TaxID=44056 {ECO:0000313|Proteomes:UP000002729}; RN [1] {ECO:0000313|EMBL:EGB02788.1, ECO:0000313|Proteomes:UP000002729} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCMP 1984 {ECO:0000313|Proteomes:UP000002729}; RX PubMed=21368207; DOI=10.1073/pnas.1016106108; RA Gobler C.J., Berry D.L., Dyhrman S.T., Wilhelm S.W., Salamov A., RA Lobanov A.V., Zhang Y., Collier J.L., Wurch L.L., Kustka A.B., RA Dill B.D., Shah M., VerBerkmoes N.C., Kuo A., Terry A., Pangilinan J., RA Lindquist E.A., Lucas S., Paulsen I.T., Hattenrath-Lehmann T.K., RA Talmage S.C., Walker E.A., Koch F., Burson A.M., Marcoval M.A., RA Tang Y.Z., Lecleir G.R., Coyne K.J., Berg G.M., Bertrand E.M., RA Saito M.A., Gladyshev V.N., Grigoriev I.V.; RT "Niche of harmful alga Aureococcus anophagefferens revealed through RT ecogenomics."; RL Proc. Natl. Acad. Sci. U.S.A. 108:4352-4357(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; GL833315; EGB02788.1; -; Genomic_DNA. DR RefSeq; XP_009042513.1; XM_009044265.1. DR GeneID; 20221512; -. DR InParanoid; F0YQ22; -. DR Proteomes; UP000002729; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002729}; KW Reference proteome {ECO:0000313|Proteomes:UP000002729}. FT NON_TER 342 342 {ECO:0000313|EMBL:EGB02788.1}. SQ SEQUENCE 342 AA; 38184 MW; 5C04EDCDBEB6F37B CRC64; MTKVSRDHVP NPYSYDGLDH PLILKAREKR PSLAVSQFDD LRASWAQPKD THPEGFPYFV RGRDSVRSYI TELFQTRITM YDGAMGTMIQ KHKLDEPDFR AERFKDYDML IKGNNDLLSI TQPHIIRDIY KKYLVEGGSQ LIGTNTFSST TIAQADYKME DLVYELNYDS ARLAREACDE VTAMDPTKPR FVCGAIGPTN RTASISPDVN DPTTRNCDFD ELVEAYYEQC VGLADGGCDI FIIETIFDTL NAKAACFAVN EFLEHTGIDI PLFISGTLVD QSGRTLSGQT GEAFYVSIRH AKPMCVGLNC ALGAKAMAPF LKRLSDCAEC FVHVYSNAGL PN // ID F0Z5M5_9CLOT Unreviewed; 797 AA. AC F0Z5M5; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 01-OCT-2014, entry version 15. DE SubName: Full=Vitamin B12-dependent methionine synthase family protein {ECO:0000313|EMBL:EGB90708.1}; GN ORFNames=HMPREF0240_04431 {ECO:0000313|EMBL:EGB90708.1}; OS Clostridium sp. D5. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=556261 {ECO:0000313|EMBL:EGB90708.1}; RN [1] {ECO:0000313|EMBL:EGB90708.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=D5 {ECO:0000313|EMBL:EGB90708.1}; 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; GL870823; EGB90708.1; -; Genomic_DNA. DR RefSeq; WP_009005701.1; NZ_GL870823.1. DR EnsemblBacteria; EGB90708; EGB90708; HMPREF0240_04431. DR PATRIC; 46448630; VBICloSp105178_4822. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; SQ SEQUENCE 797 AA; 86019 MW; 3F648AE2DAD0625D CRC64; MILDRLGKEL LFFDGGMGTL LQAGGLKPGE LPETWNMTHP EKITGIHRKY IEAGSDIILT NTFGANALKF HDDSCSLCDI VTSAVGHVKR AAEQAELNGR QVYTALDIGP TGKLLKPMGD LEFEEAYEAF REVVRYGAEA GADLIHIETM SDTYELKAAV LAAKENTDLP VFVTTIFDER GKLLTGADVP AVVALLEGLR VDALGINCGL GPGQMLPILE QILEYTSLPV IVKPNAGLPK QVERETVYDV LPQDFAMTMQ KIIGQGAAVA GGCCGTTPEH IKSMVDLCRG MEPLPIIQKD ITIVSSYGKS VCLGTGSKII GERINPTGKK KFRQALKEHD MDYILREGIM QQDMGAHILD VNVGLPDIDE ASMMQDVLVE LQSVTSLPLQ IDTVDTKAME AALRIYNGKA MVNSVSGKQE SMDAVFPLIQ KYGGVVIGLT LDESGIPDTA EGRVEIARHI IEEAAKYGIQ KKDIVIDVLA MTISSDPEGA KVTLEALKKV RYGLGVNTVL GVSNISFGLP SRTVINANFY TMAMQNGLSA GIINPSSEEM MKSYYAYHAL MNLDSNCEAY IAKYAGQAAE SSASPAVSGD MPLNRAIEKG LKEEAHHITG LLVKEQAPLD IINTYLIPAL DNVGKGFEKG TVFLPQLLMS AEAAKAAFTI LKESLAATGQ QDEKKEKVVL ATVKGDIHDI GKNIVKVLLE NYGFDVIDLG KDVAPGLVVE KVLAEDVHLV GLSALMTTTV VSMEETIQQL RQKAPGCRVM VGGAVLNQEY ADMIGADFYG KDAMQSVYYA QKLLQNK // ID F0ZS97_DICPU Unreviewed; 1253 AA. AC F0ZS97; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 01-APR-2015, entry version 25. DE SubName: Full=Cobalamin-dependent methionine synthase {ECO:0000313|EMBL:EGC33169.1}; GN ORFNames=DICPUDRAFT_98639 {ECO:0000313|EMBL:EGC33169.1}; OS Dictyostelium purpureum (Slime mold). OC Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; Dictyostelium. OX NCBI_TaxID=5786 {ECO:0000313|Proteomes:UP000001064}; RN [1] {ECO:0000313|Proteomes:UP000001064} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064}; RX PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20; RG US DOE Joint Genome Institute (JGI-PGF); RA Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., RA Dalin E., Tu H., Huang E., Barry K., Lindquist E., Shapiro H., RA Bruce D., Schmutz J., Salamov A., Fey P., Gaudet P., Anjard C., RA Babu M.M., Basu S., Bushmanova Y., van der Wel H., Katoh-Kurasawa M., RA Dinh C., Coutinho P.M., Saito T., Elias M., Schaap P., Kay R.R., RA Henrissat B., Eichinger L., Rivero F., Putnam N.H., West C.M., RA Loomis W.F., Chisholm R.L., Shaulsky G., Strassmann J.E., RA Queller D.C., Kuspa A., Grigoriev I.V.; RT "Comparative genomics of the social amoebae Dictyostelium discoideum RT and Dictyostelium purpureum."; RL Genome Biol. 12:R20.1-R20.23(2011). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GL871154; EGC33169.1; -; Genomic_DNA. DR RefSeq; XP_003290289.1; XM_003290241.1. DR GeneID; 10504654; -. DR KEGG; dpp:DICPUDRAFT_98639; -. DR InParanoid; F0ZS97; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR Proteomes; UP000001064; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001064}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001064}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 253 253 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 316 316 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 773 773 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1253 AA; 139550 MW; F880F58B6D8F25BA CRC64; MAKQKESETF EIIRKILNER IMVLDGAMGT EIQKFKLKDH HYRGEEFKDF PHELGGNNDL LVLTQPEIIR EIHCKYLEAG ADFIETNTFN GNIFSQADYK MEHLVKRINI EASKLAKSAC EEYTKKDPSR PRFVCGAIGP TNKTASISPS VERPEARNVT FDELVAGYLE QIEALVEGGV DILLVETVFD SLNAKAGLFA IEEFFNKNDI PRLPVFVSGT IVDKSGRTLS GQTGEAFYTS VASANLMVFG LNCALGAQEM RPFLQNISKV SECYVSCYPN AGLPNTFGGY DETPEMMAEQ IKEFAVSGLL NIVGGCCGTS PDHIRAFCEA IKGVPPREIP QLPQLTTVSG LEPLIFTPEL NFVNVGERCN VSGSRRFANL IKANKYEEAL SVARQQVEAG AQIIDINMDE GMIDAVSAIT KFLFFIGSEP EISKVPIMLD SSNFAVVEAG LKCVQGKCIV NSISLKVGEE LFIEQARIVK QYGASVVVMA FDENGQATSK EEKVRICYRS YKILTEQVGF YPQDIIFDPN ILTIATGLEE HNNYGIEFIE ATREIKRIMP LTRVSGGVSN LSFSFRGNEP LREAMHSAFL YHAIKAGMDM GIVNAGALPI YDDIPKDLLI LVEDAILNRT NDATEKLLEY AQKNSKTEKA AVEVEEWRNK SVTDRIAHAL VKGITTYIIE DTEEARLTLP SSLSVIEGPL MGGMNVVGDL FGAGKMFLPQ VIKSARVMKK AVAHLIPFME EEKSRKRLET GSTAEEPENA GVVVLATVKG DVHDIGKNIV GVVLGCNNYK VIDCGVMTPC EKIIEAIIQN KADVVGLSGL ITPSLDEMIF VASELERQKF KIPLMIGGAT TSQIHTAVKI SPHYTQPTVH VLDASRSVTV VSSLLDPKNK EIFAEDIEQQ YSELREKHYA SLKDRKYTSL EKARQHRPKI NWSAITPVKP SFIGKQVFKE YSLEKLCTKI DWNPFFVTWQ LRGKYPNRGY PRIFKDETVG AEAKKLFDDA QAMLKEIVEK KLLNARGVIG FYPANSENED ILLYTDDTRT TVGATLHGLR QQSEKETEEP YLSYGDYIAP VSSGVKDYIG LFAVSAGFGL DEMVEKYKNE NDDYSSIMAK ALADRLAEAL AEALHEDVRK IHWGYEKDEN LSSEDLFKVK YKGIRPAPGY PAQPDHTEMK AIWSLMDVKN QTDIELTDHM AMVPGAAVSG IYFSHEHAKY FSVGKITKEQ IEDYSKRKQI PVEEAEKWLS SILAYDRLPF VKK // ID F1C7F9_PERFV Unreviewed; 121 AA. AC F1C7F9; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 29-OCT-2014, entry version 14. DE SubName: Full=Betaine homocysteine s-methyltansferase {ECO:0000313|EMBL:ADX97219.1}; DE Flags: Fragment; GN Name=BHMT {ECO:0000313|EMBL:ADX97219.1}; OS Perca flavescens (American yellow perch) (Morone flavescens). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Percoidei; Percidae; Percinae; Perca. OX NCBI_TaxID=8167 {ECO:0000313|EMBL:ADX97219.1}; RN [1] {ECO:0000313|EMBL:ADX97219.1} RP NUCLEOTIDE SEQUENCE. RA Pierron F., Normandeau E., Campbell P.G.C., Bernatchez L., Couture P.; RT "Effects of chronic metal exposure on wild fish populations revealed RT by high-throughput cDNA sequencing."; 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; HQ206621; ADX97219.1; -; mRNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; FT NON_TER 121 121 {ECO:0000313|EMBL:ADX97219.1}. SQ SEQUENCE 121 AA; 13028 MW; E0D1CC8F172EDE51 CRC64; MAPGKKGIIE RLNAGEVVIG DGGFVFALEK RGYVKAGPWT PEASVTHPEA VRQLHREFLR AGSNVMQTFT FYASDDKLEN RGQNLRLSGV QINEAACDLA REVASEGDAM VAGGVCQTPS Y // ID F1KS55_ASCSU Unreviewed; 1254 AA. AC F1KS55; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 01-APR-2015, entry version 23. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADY40709.1}; OS Ascaris suum (Pig roundworm) (Ascaris lumbricoides). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Ascaridida; OC Ascaridoidea; Ascarididae; Ascaris. OX NCBI_TaxID=6253 {ECO:0000313|EMBL:ADY40709.1}; RN [1] {ECO:0000313|EMBL:ADY40709.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=21685128; DOI=10.1101/gr.121426.111; RA Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J., RA Davis R.E.; RT "Deep small RNA sequencing from the nematode Ascaris reveals RT conservation, functional diversification, and novel developmental RT profiles."; RL Genome Res. 21:1462-1477(2011). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; JI164984; ADY40709.1; -; mRNA. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 2: Evidence at transcript level; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 251 251 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 315 315 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 777 777 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1254 AA; 139269 MW; 448C5846360B8475 CRC64; MMKRRQEVFE TISRIARERI LIIDGAMGTM LQREHLQEAD FRADILKDHP KPLKGNNDIL SLTRPDIVYK IHKLYLEAGA DFIETNTFSG TAVAQADYQC EHLVHDINYR SAQIARKAAD EIYEQTGVRR FVCGAIGPTN KTLSISPSVE HPEFRNITFQ ELVKAYDEQA RSLIEGGVDV LLVETVFDSA NAKAALFAIR TLFEEGGIEE VPVFLSGTIV DLSGRTLSGQ TGEAFLISTR QGRPVAVGLN CALGAKEMRP FIETIAMNTT ALVLCYPNAG LPNALGGYDE RPEDMAAALL SYASDGLVNI VGGCCGTTPD HIRAIAVAVK GVVPRKPPTS VNSGYMMLAG LEPFVIGAHT NFVNIGERCN VAGSRRFCNL IKKNKYEDAI GVARKQVENG AQILDINVDD GLLDGPSTMT KFLRLIASEP DVAKVPICVD SSNFEVLIAG LESCQGKCIV NSISLKEGEE VFLQKARLVK RYGAALVVMA FDEEGQATDI ERKYKICERS YRLLIEEAAF DPCDIIFDPN ILTIATGMEE HSEYGINFIE GTRLIKENLP GCFVSGGVSN FSFSFRGMEP VREAMHSVFL YHAIKAGMDM GIVNAGALPL YTDIRPDLLK LCEDLLWNKD SNATEKMLAL AHELVSGDKK AQSECDSWRQ ESVEKRLEYA LVKGIDSHIV EDTEEARQNT SKYPRPLNVI EQPLMAGMAV VGELFGSGKM FLPQVIKSAR VMKKAVAHLI PFMDKEREEN LKSKIAVSNE SPYQGTFVIA TVKGDVHDIG KNIVAVVLGC NNFRVIDLGV MTPCEKIIKT AIDEKADFIG CSGLITPSLD EMVHVAREMQ RAGLSIPLLI GGATTSKTHT AVKIAPRYSG PVIHCLDASK TVVACSSLCD PKTRDEFLAD ILEEYEEVRI EHYESMKERR FVSLKAARSR ALKLDFTHFQ PGKPTFLGRK AFKKFDLNLV VPFIDWKPFF DVWQLRGKYP NRNYPRIFND DDVGAEARRV FDDAQVTLHR LIDKEELKAS AVIAFFECCA YGDDILIFDD ETRQHNATLF GLRQQCDKEY DQPCMCLSDF VAPGDHSNPT DYIGVFACTA GIGSRELCNT LEKDRLDDYS SIMVKALADR LSEAMAEYLH MQVRRELWGY SLDEDLDTAD LLSIKYKGIR PAPGYPSQPD HTEKVTLWRL LDAENLAGIK LTESFAMEPA ASICGLYFAH PQSQYFAVGK VDKDQVEDYA LRKGESVQSI EYWLAPILGY DVEK // ID F1LC77_ASCSU Unreviewed; 122 AA. AC F1LC77; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 01-OCT-2014, entry version 12. DE SubName: Full=Homocysteine S-methyltransferase 3 {ECO:0000313|EMBL:ADY47731.1}; OS Ascaris suum (Pig roundworm) (Ascaris lumbricoides). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Ascaridida; OC Ascaridoidea; Ascarididae; Ascaris. OX NCBI_TaxID=6253 {ECO:0000313|EMBL:ADY47731.1}; RN [1] {ECO:0000313|EMBL:ADY47731.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=21685128; DOI=10.1101/gr.121426.111; RA Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J., RA Davis R.E.; RT "Deep small RNA sequencing from the nematode Ascaris reveals RT conservation, functional diversification, and novel developmental RT profiles."; RL Genome Res. 21:1462-1477(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; JI177236; ADY47731.1; -; mRNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 2: Evidence at transcript level; KW Methyltransferase {ECO:0000313|EMBL:ADY47731.1}; KW Transferase {ECO:0000313|EMBL:ADY47731.1}. SQ SEQUENCE 122 AA; 13391 MW; 1E438F3E62FA87BF CRC64; MLAFETIPAE KEGIAILKAL DLLPANVKCW ISFSCRDGTQ TNHCESFAKV VSEVTKHPKV IAVGINCTPP KYISSLLRSA KSSCNGKPFV VYPNSGETYN VETKSWSDDK STMRSIASYV NE // ID F1LMG2_RAT Unreviewed; 362 AA. AC F1LMG2; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 2. DT 27-MAY-2015, entry version 32. DE SubName: Full=S-methylmethionine--homocysteine S-methyltransferase BHMT2 {ECO:0000313|Ensembl:ENSRNOP00000058419}; GN Name=Bhmt2 {ECO:0000313|Ensembl:ENSRNOP00000058419, GN ECO:0000313|RGD:1359418}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000058419, ECO:0000313|Proteomes:UP000002494}; RN [1] {ECO:0000313|Ensembl:ENSRNOP00000058419, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000058419, RC ECO:0000313|Proteomes:UP000002494}; RX PubMed=15057822; DOI=10.1038/nature02426; RG Rat Genome Sequencing Project Consortium; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., RA Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., RA Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., RA Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., RA Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., RA Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., RA Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., RA Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., RA Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., RA D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., RA Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., RA Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., RA Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., RA Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., RA Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., RA Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., RA Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., RA Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., RA Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., RA Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., RA Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., RA Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., RA Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., RA Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., RA Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., RA Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., RA Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., RA Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., RA Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., RA Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., RA Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., RA Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., RA Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., RA Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., RA Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into RT mammalian evolution."; RL Nature 428:493-521(2004). RN [2] {ECO:0000313|Ensembl:ENSRNOP00000058419} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000058419}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSRNOP00000058419}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AABR06012038; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PRIDE; F1LMG2; -. DR Ensembl; ENSRNOT00000061708; ENSRNOP00000058419; ENSRNOG00000040120. DR RGD; 1359418; Bhmt2. DR GeneTree; ENSGT00390000003122; -. DR OMA; PEGDMHD; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR UniPathway; UPA00051; UER00083. DR NextBio; 35575493; -. DR Proteomes; UP000002494; Chromosome 2. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0061627; F:S-methylmethionine-homocysteine S-methyltransferase activity; IEA:Ensembl. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl. DR GO; GO:0046500; P:S-adenosylmethionine metabolic process; IEA:Ensembl. DR GO; GO:0033477; P:S-methylmethionine metabolic process; IEA:Ensembl. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000002494}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Proteomics identification {ECO:0000213|PeptideAtlas:F1LMG2}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 207 207 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 362 AA; 39788 MW; ACFDCEF4EC5035B2 CRC64; MAPAGGPRVK KGILERLDSG EVVVGDGGFL FTLEKRGFVK AGLWTPEAVV EYPSAVRQLH TEFLRAGADV LQTFTFSAAE DRMESKWEAV NAAACDLAQE VADGGAALVA GGICQTSLYK YHKDETRIKN IFRLQLGVFA RKNVDFLIAE YFEHVEEAVW AVEVLREVGA PVATMCIGPE GDMHGVTPGE CAVRLSRAGA NIIGVNCRFG PWTSLQTMKL MKEGLRDAGL QAHLMVQCLG FHTPDCGKGG FVDLPEYPFG LEPRVATRWD IQKYAREAYN LGVRYIGGCC GFEPYHIRAI AEELAPERGF LPPASEKHGI WGSGLDMHTK PWIRARARRE YWETLLPASG RPFCPSLSKP DA // ID F1N0S3_BOVIN Unreviewed; 1265 AA. AC F1N0S3; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 2. DT 27-MAY-2015, entry version 35. DE SubName: Full=Methionine synthase {ECO:0000313|Ensembl:ENSBTAP00000016262}; GN Name=MTR {ECO:0000313|Ensembl:ENSBTAP00000016262}; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000016262, ECO:0000313|Proteomes:UP000009136}; RN [1] {ECO:0000313|Ensembl:ENSBTAP00000016262, ECO:0000313|Proteomes:UP000009136} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000016262, RC ECO:0000313|Proteomes:UP000009136}; RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42; RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., RA Puiu D., Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., RA Marcais G., Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.; RT "A whole-genome assembly of the domestic cow, Bos taurus."; RL Genome Biol. 10:R42.01-R42.10(2009). RN [2] {ECO:0000313|Ensembl:ENSBTAP00000016262} RP IDENTIFICATION. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000016262}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 1}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSBTAP00000016262}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DAAA02061490; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; DAAA02061491; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; DAAA02061492; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSBTAT00000016262; ENSBTAP00000016262; ENSBTAG00000012251. DR GeneTree; ENSGT00420000029824; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG7TF786; -. DR TreeFam; TF312829; -. DR Reactome; REACT_316684; Cobalamin (Cbl, vitamin B12) transport and metabolism. DR Reactome; REACT_347665; Methylation. DR Reactome; REACT_351398; Sulfur amino acid metabolism. DR Proteomes; UP000009136; Chromosome 28. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IBA:GO_Central. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000009136}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000009136}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 260 260 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 785 785 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1265 AA; 140487 MW; 95659D4D51A7D228 CRC64; MAPTLQDLTP SAGMKKTLQD EIEAILQERI MVLDGGMGTM IQQHKLSEED FRGQEFKDHA RPLKGNNDIL SITQPSVIYQ IHKEYLLAGA DIIETNTFSS TSIAQADYGL EHLAYRMNMC SAGVARKAAE DISLQTGIKR YVAGALGPTN KTLSVSPSVE RPDYRNITFD ELVEAYKEQA KGLLDGGVDI LLIETIFDTA NAKAALFAVQ KLFEEEYVPR PVFISGTIVD KSGRTLSGQT GEAFVISVSH ADPLCIGLNC ALGAAEMRPF IETIGKCTTA YVLCYPNAGL PNTFGDYDET PHVMAMHLKD FAVDGLVNIV GGCCGTTPDH IREIAEAVKN CKPRVPPATV FEGHMLLSGL EPFRIGPYTN FVNIGERCNV AGSRRFAKLI MAGNYEEALS VAKMQVEMGA QVLDINMDDG MLDGPSAMTR FCNFIASEPD IAKVPLCIDS SNFAVIEAGL KCCQGKCIVN SISLKEGEDD FLEKARKIKK FGAAVVVMAF DEEGQATETD TKIRVCTRAY HLLLKKLGFN PNDIIFDPNI LTIGTGMEEH NLYAVNFINA TKVIKETLPG AKVSGGLSNL SFSFRGMEAI REAMHGVFLY HAIKFGMDMG IVNAGSLPVY DDIHKELLQL CEDLIWNRDP EATEKLLHYA QTQGKGGKKV IQTDEWRNGP LEERLEYALV KGIEKYIIED TEEARLNQEK YPRPLNIIEG PLMNGMKIVG DLFGAGKMFL PQVIKSARVM KKAVGHLIPF MEKEREETKV LTGKIEDEDP YQGTIVLATV KGDVHDIGKN IVGVVLGCNN FRVIDLGVMT PCDKILKAAL DHKADIIGLS GLITPSLDEM IFVAKEMERL AIKIPLLIGG ATTSRTHTAV KIAPRYSAPV IHVLDASKSV VVCSQLLDEN LKDEYFEEIL EEYEDIRQDH YESLKERRYL TLRQARENGF HIDWLSEPPP VKPTFLGTRV FEDYDLQKLV DYIDWKPFFD VWQLRGKYPN RGFPKIFDDK TVGEEAKKVY DDAQNMLQAL ISQKKLQARG VVGFWPAQSI QDDIHLYAEG AVPQASEPIA TFYGLRQQAE KDSASSDPYL CLSDFIAPLH SGIPDYLGLF AVACFGVEEL SKAYEEECDD YSSIMVKALG DRLAEAFAEE LHERVRRELW GYCSGEQLAV ADLRRLRYEG IRPAPGYPSQ PDHTEKLTMW RLADVEQRTG IRLTESLAMA PASAVSGLYF SNLKSKYFAV GKISKDQIED YASRKNMSVA EVEKWLGPIL GYDTD // ID F1N4C6_BOVIN Unreviewed; 360 AA. AC F1N4C6; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 2. DT 27-MAY-2015, entry version 29. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSBTAP00000045884}; DE Flags: Fragment; GN Name=BHMT2 {ECO:0000313|Ensembl:ENSBTAP00000045884}; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000045884, ECO:0000313|Proteomes:UP000009136}; RN [1] {ECO:0000313|Ensembl:ENSBTAP00000045884, ECO:0000313|Proteomes:UP000009136} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000045884, RC ECO:0000313|Proteomes:UP000009136}; RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42; RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., RA Puiu D., Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., RA Marcais G., Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.; RT "A whole-genome assembly of the domestic cow, Bos taurus."; RL Genome Biol. 10:R42.01-R42.10(2009). RN [2] {ECO:0000313|Ensembl:ENSBTAP00000045884} RP IDENTIFICATION. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000045884}; RG Ensembl; RL Submitted (MAY-2011) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSBTAP00000045884}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DAAA02027819; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSBTAT00000048928; ENSBTAP00000045884; ENSBTAG00000038234. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; F1N4C6; -. DR OMA; AHHKDEV; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR Proteomes; UP000009136; Chromosome 10. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IBA:GO_Central. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IBA:GO_Central. DR GO; GO:0061627; F:S-methylmethionine-homocysteine S-methyltransferase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl. DR GO; GO:0032259; P:methylation; IBA:GOC. DR GO; GO:0046500; P:S-adenosylmethionine metabolic process; IEA:Ensembl. DR GO; GO:0033528; P:S-methylmethionine cycle; IBA:GO_Central. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009136}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000009136}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 204 204 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 287 287 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSBTAP00000045884}. SQ SEQUENCE 360 AA; 39876 MW; 9ABBB85F89D18EB3 CRC64; LETAFRKNKK KGLLEHLDSG EVVVGDGSFL LTLEKRGYVK AGLWTPEAVV EHPNAGMING SHMEFLRVGS DVMQTFTFSA SENNMESLWE AVNTTACDLA REVANKGDAL VAGGICRTSL YAHHKDEVRI KKLFRLQLEI FARKNVDFLI AEYFEHAVEV LKESGEPVAA TMCIGPEGDM HGVTPGECAV KLVKAGASVV GVNCRFGPWT SLKTMSLMKE ARQAAELKAP LMVWSLGFHM PDCGKGGFLD LPEYPFVLEP RVATRWDIQK NAREAYNLGV RYIGGCCGFE PYHIRAIAEE LAPEKGFLSP ASEKHGSWGS GLNMHTKPWI RARHRARREY WENLRLASGR PCPSLSKPDA // ID F1NLY0_CHICK Unreviewed; 1242 AA. AC F1NLY0; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 2. DT 27-MAY-2015, entry version 34. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGALP00000017592}; DE Flags: Fragment; GN Name=MTR {ECO:0000313|Ensembl:ENSGALP00000017592}; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; OC Phasianidae; Phasianinae; Gallus. OX NCBI_TaxID=9031 {ECO:0000313|Ensembl:ENSGALP00000017592, ECO:0000313|Proteomes:UP000000539}; RN [1] {ECO:0000313|Ensembl:ENSGALP00000017592, ECO:0000313|Proteomes:UP000000539} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Red jungle fowl {ECO:0000313|Ensembl:ENSGALP00000017592, RC ECO:0000313|Proteomes:UP000000539}; RX PubMed=15592404; DOI=10.1038/nature03154; RG International Chicken Genome Sequencing Consortium; RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., RA Ponting C.P., Bork P., Burt D.W., Groenen M.A.M., Delany M.E., RA Dodgson J.B., Chinwalla A.T., Cliften P.F., Clifton S.W., RA Delehaunty K.D., Fronick C., Fulton R.S., Graves T.A., Kremitzki C., RA Layman D., Magrini V., McPherson J.D., Miner T.L., Minx P., Nash W.E., RA Nhan M.N., Nelson J.O., Oddy L.G., Pohl C.S., Randall-Maher J., RA Smith S.M., Wallis J.W., Yang S.-P., Romanov M.N., Rondelli C.M., RA Paton B., Smith J., Morrice D., Daniels L., Tempest H.G., RA Robertson L., Masabanda J.S., Griffin D.K., Vignal A., Fillon V., RA Jacobbson L., Kerje S., Andersson L., Crooijmans R.P., Aerts J., RA van der Poel J.J., Ellegren H., Caldwell R.B., Hubbard S.J., RA Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M., Arakawa H., RA Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K., RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E., RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M., RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., RA Miller M.M., Inoko H., Shiina T., Kaufman J., Salomonsen J., RA Skjoedt K., Wong G.K.-S., Wang J., Liu B., Wang J., Yu J., Yang H., RA Nefedov M., Koriabine M., Dejong P.J., Goodstadt L., Webber C., RA Dickens N.J., Letunic I., Suyama M., Torrents D., von Mering C., RA Zdobnov E.M., Makova K., Nekrutenko A., Elnitski L., Eswara P., RA King D.C., Yang S.-P., Tyekucheva S., Radakrishnan A., Harris R.S., RA Chiaromonte F., Taylor J., He J., Rijnkels M., Griffiths-Jones S., RA Ureta-Vidal A., Hoffman M.M., Severin J., Searle S.M.J., Law A.S., RA Speed D., Waddington D., Cheng Z., Tuzun E., Eichler E., Bao Z., RA Flicek P., Shteynberg D.D., Brent M.R., Bye J.M., Huckle E.J., RA Chatterji S., Dewey C., Pachter L., Kouranov A., Mourelatos Z., RA Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M., RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O., RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., RA Betran E., Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., RA Furey T.S., Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., RA Eyras E., Castelo R., Abril J.F., Castellano S., Camara F., Parra G., RA Guigo R., Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., RA Mardis E.R., Wilson R.K.; RT "Sequence and comparative analysis of the chicken genome provide RT unique perspectives on vertebrate evolution."; RL Nature 432:695-716(2004). RN [2] {ECO:0000313|Ensembl:ENSGALP00000017592} RP IDENTIFICATION. RC STRAIN=Red jungle fowl {ECO:0000313|Ensembl:ENSGALP00000017592}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 1}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSGALP00000017592}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AADN03003104; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSGALT00000017613; ENSGALP00000017592; ENSGALG00000014464. DR GeneTree; ENSGT00420000029824; -. DR InParanoid; F1NLY0; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG7TF786; -. DR TreeFam; TF312829; -. DR Reactome; REACT_290598; Cobalamin (Cbl, vitamin B12) transport and metabolism. DR Reactome; REACT_315068; Methylation. DR Reactome; REACT_340922; Sulfur amino acid metabolism. DR Proteomes; UP000000539; Chromosome 3. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IBA:GO_Central. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000539}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000539}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 249 249 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 772 772 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSGALP00000017592}. SQ SEQUENCE 1242 AA; 138397 MW; 2D7CF508CA1D7249 CRC64; ADTQESVEDE IESVLRERIM ILDGGMGTMI QQHALSEEDF RGHEFKDHSK PLKGNNDLLS ITQPDIICDI HKEYLLAGAD IIETNTFSST RVAQADYGLE HLAYRLNRIS AEVARKAADD VTAQTGIKRY VAGSIGPTNR TLSVSPSVER PDYRNITFDE LVEAYTEQAK GLLDGGVDVM LVETIFDTAN AKAALFALHK LFEEEYAPRP IFVSGTIVDK SGRTLSGQTG EAFVISVSHS KPLCIGLNCA LGAVEMRPFI ETIGKCTTAY VICYPNAGLP NTFGGYDETP EVTAKHIKNF ALDGLVNIVG GCCGTTPAHI RKIAEAVKLC KPRVPPPLCQ GYMLLSGLEP FRIGPYTNFV NIGERCNVAG SRKFAKLIMA GNYEEALTVA KSQVEMGAQI LDINMDDGML DGPSAMTRFC NLISSEPDIA KVPLCIDSSN FVIEAGLKCC QGKCIVNSIS LKEGEEDFLE KARKIKLYGA AVVVMAFDEV GQATETETKI AICSRAYHLL VEKVHFNPND IIFDPNILTI GTGMEEHNLY AINFINATKT IKETLPGVRI SGGLSNLSFS FRGMDAIREA MHGVFLYHAI RYGMDMGIVN AGNLPVYDDI HKELLQLCEN LIWNKDPDAT EKLLRYAQNH AQGGKKVMQT DEWRNSTVEE RLEYALVKGI EKYVTADTEE ARLNQEKYPR PLNIIEGPLM NGMKIVGDLF GAGKMFLPQV IKSARVMKKA VGHLIPYMEK EREERRAKQG SSEEEDPYNG TIVLATVKGD VHDIGKNIVG VVLGCNNFRV IDLGVMTPCD KILRAAVENK ADIIGLSGLI TPSLDEMIFV AKEMERLAIK IPLLIGGATT SKTHTAVKIA PRYSAPVIHV LDASKSVVVC SQLLDESVKD DFFEEILEEY EEIRQEHYES LKERRYLSLQ QARRKGFHND WLSDHKPVKP KFIGTKVFED YDLKRLVEYI DWKPFFDVWQ LRGKYPNRGF PKVFKDKTVG EEAQKVYNDA QNLLKILINQ KKLQARGVDD IYLYAVEEAV GSSEPIAKFC GLRQQAEKDS ACTDPYYCLS DFIAPLDSGV CDYLGLFAVA CFGVDELCNE FRRQDDEYNI IMVKALGDRL AEAFAEELHE RVRREFWAYC SDEQLDLSEL RKIKYEGIRP APGYPSQPDH TEKLTMWKLA NIEETTGIGL TESLAMTPAS AVSGLYFSSP KSKYFAVGKI CKDQVEDYAL RKKLSVAEVE KWLGPILGYD TE // ID F1QF71_DANRE Unreviewed; 307 AA. AC F1QF71; F1RAY3; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 29-APR-2015, entry version 29. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSDARP00000098456}; GN ORFNames=zgc:172121 {ECO:0000313|Ensembl:ENSDARP00000098456, GN ECO:0000313|ZFIN:ZDB-GENE-030131-9545}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000098456, ECO:0000313|Proteomes:UP000000437}; RN [1] {ECO:0000313|Ensembl:ENSDARP00000098456} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000098456}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. RN [2] {ECO:0000313|Ensembl:ENSDARP00000098456, ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000098456, RC ECO:0000313|Proteomes:UP000000437}; RX PubMed=23594743; DOI=10.1038/nature12111; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., RA Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., RA McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., RA Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T., RA Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., RA Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., RA Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., RA Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G., RA Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., RA Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., RA Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., RA Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., RA Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., RA Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., RA Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., RA Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., RA Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., RA Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., RA Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., RA Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., RA Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., RA Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., RA Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., RA Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., RA Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., RA Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the RT human genome."; RL Nature 496:498-503(2013). CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSDARP00000098456}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL928701; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSDART00000043496; ENSDARP00000043495; ENSDARG00000034430. DR Ensembl; ENSDART00000112099; ENSDARP00000098456; ENSDARG00000034430. DR ZFIN; ZDB-GENE-030131-9545; zgc:172121. DR GeneTree; ENSGT00510000049619; -. DR OrthoDB; EOG7GQXW0; -. DR TreeFam; TF313927; -. DR Proteomes; UP000000437; Chromosome 6. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000437}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}. SQ SEQUENCE 307 AA; 33841 MW; 5EB95B52B4B334D2 CRC64; MDSSPFILDG GLATELEASG FQLQGDPLWS ARVLHTDSQA IKDVHYRYLQ SGSDVITTAT YQASIEGFVK YLGVQPEEAQ HMMMSAVQLA KETVSEFISQ SPMSDRREPL VAGSVGPYGS FLHDGSEYTG AYEDKMTVEE LKDWHRPQIQ CLVKAGADLV AMETIPGLKE AEALVEVLKE FPETKAWLSF SCKDNNSISS GRRFSEAVEM ACRSTQLVAV GVNCCPALLV KPLLESAKSH KRADLSWVVY PNSGEGWDVT TGWKTEMRTS FANLSLEWKA QGALWIGGCC RVRPADITEL KQLHVQP // ID F1QU55_DANRE Unreviewed; 400 AA. AC F1QU55; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 33. DE SubName: Full=Betaine--homocysteine S-methyltransferase 1 {ECO:0000313|Ensembl:ENSDARP00000040421}; GN Name=bhmt {ECO:0000313|Ensembl:ENSDARP00000040421, GN ECO:0000313|ZFIN:ZDB-GENE-030131-947}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000040421, ECO:0000313|Proteomes:UP000000437}; RN [1] {ECO:0000313|Ensembl:ENSDARP00000040421} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000040421}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. RN [2] {ECO:0000313|Ensembl:ENSDARP00000040421, ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000040421, RC ECO:0000313|Proteomes:UP000000437}; RX PubMed=23594743; DOI=10.1038/nature12111; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., RA Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., RA McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., RA Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T., RA Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., RA Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., RA Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., RA Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G., RA Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., RA Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., RA Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., RA Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., RA Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., RA Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., RA Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., RA Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., RA Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., RA Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., RA Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., RA Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., RA Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., RA Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., RA Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., RA Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., RA Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., RA Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the RT human genome."; RL Nature 496:498-503(2013). CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSDARP00000040421}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CABZ01102096; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PRIDE; F1QU55; -. DR Ensembl; ENSDART00000040422; ENSDARP00000040421; ENSDARG00000013430. DR ZFIN; ZDB-GENE-030131-947; bhmt. DR GeneTree; ENSGT00390000003122; -. DR OMA; EVKNIFR; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR Reactome; REACT_342706; Sulfur amino acid metabolism. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000000437; Chromosome 21. DR Bgee; F1QU55; -. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000000437}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Proteomics identification {ECO:0000213|PeptideAtlas:F1QU55}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 212 212 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 400 AA; 44082 MW; F04D3F67F0C4BC72 CRC64; MAPVGSKRGV LERLNAGEVV IGDGGFVFAL EKRGYVKAGP WTPEAAAEHP EAVRQLHREF LRAGSNVMQT FTFYASDDKL ENRGNKLSFT GQQINEAACD LAREVANEGD ALVAGGVSQT PSYLSCKSEE EVKKTFKKQL DVFIKKNVDL LIAEYFEHVE EAEWAVQVLK ATGKPVAATL CIGPDGDMHG VTPGECAVRL VKAGADIVGV NCHFDPLTCV KTVVMMKAAV EKAGLKAHYM TQPLAYHTPD CSCQGFIDLP EFPFALEPRI LTRWEMQQYA REAYKAGIRY IGGCCGFEPY HIRAVAEELS AERGFLPEAS QKHGLWGSGL EMHTKPWVRA RARRDYWEKL KPASGRPLCP SMSTPDGWGV TRGHAALMQQ KEATTAEQLR PLFQQADAKH // ID F1RHM1_PIG Unreviewed; 1264 AA. AC F1RHM1; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 33. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSSSCP00000010817}; DE Flags: Fragment; GN Name=MTR {ECO:0000313|Ensembl:ENSSSCP00000010817}; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; OC Sus. OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000010817, ECO:0000313|Proteomes:UP000008227}; RN [1] {ECO:0000313|Ensembl:ENSSSCP00000010817, ECO:0000313|Proteomes:UP000008227} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG Porcine genome sequencing project; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSSSCP00000010817} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2011) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 1}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSSSCP00000010817}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU467009; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CU468604; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSSSCT00000011105; ENSSSCP00000010817; ENSSSCG00000010143. DR GeneTree; ENSGT00420000029824; -. DR InParanoid; F1RHM1; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG7TF786; -. DR TreeFam; TF312829; -. DR Reactome; REACT_307543; Sulfur amino acid metabolism. DR Reactome; REACT_310217; Methylation. DR Reactome; REACT_341405; Cobalamin (Cbl, vitamin B12) transport and metabolism. DR Proteomes; UP000008227; Chromosome 14. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IBA:GO_Central. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008227}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008227}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 260 260 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 784 784 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSSSCP00000010817}. SQ SEQUENCE 1264 AA; 140542 MW; 823207BC9EA55E73 CRC64; LSLCKVKFLL KAGMKKTLQD DIEAILQERI MVLDGGMGTM IQRHKLSEDD FRGQEFQDHA RPLKGNNDIL SITQPDIIYQ IHKDYLLAGA DIIETNTFSS TNIAQADYGL EHLAYRMNKC SAGVARKAAE EISLQTGIKR FVAGALGPTN KTLSVSPSVE KPDYRNITFD ELVEAYKEQA KGLLDGGVDI LLIETIFDTA NAKAALFAVQ KLFEEEYAPQ PIFISGTIVD KSGRTLSGQT GEAFVISVSH ADPLCIGLNC ALGAAEMRPF IETIGKCTTA YVLCYPNAGL PNTFGDYDET PHMMAMHLKD FATDGLVNIV GGCCGTTPAH IREIAEAVKN YKPRVPPATV FEGHMLLSGI SPFRIGPYTN FNIGERCNVA GSRKFAKLIM EGKYEEALSV AKMQVEMGAQ VLDINMDDGM LDGPSAMARF CNFIASEPDI AKVPLCIDSS NFAVIEAGLK CCQGKCIVNS ISLKEGEDDF LEKARRVKKF GAAVVVMAFD EEGQATETDT KIRVCTRAYH LLVNKLSFNP NDIIFDPNIL TIGTGMEEHS LYAVNFIYAT KVIKETLPGA KVSGGLSNLS FSFRGMEAIR EAMHGVFLYH AIQFGMDMGI VNAGSLPVYD DIHKELLQLC EDLIWNKDPE ATEKLLRYAQ TQGKGGKKVI QTDEWRNGPI EERLEYALVK GIEKYIIEDT EEARLNQEKY PRPLNIIEGP LMNGMKIVGD LFGAGKMFLP QVIKSARVMK KAVGHLIPFM EKEREENQVL TGIVEDEDPY QGTIVLATVK GDVHDIGKNI VGVVLGCNNF RVIDLGVMTP CDKILKAALD HKADIIGLSG LITPSLDEMI FVAKEMERLA IKIPLLIGGA TTSRTHTAVK IAPRYSAPVI HVLDASKSVV VCSQLLDENL KDEYFEEIME EYEDIRQDHY ESLKERRYLT LRQAREKGFH IDWLSEPHPV KPTFLGTRVF EDYDLQKLVD YIDWKPFFDV WQLRGKYPNR GFPKIFNDKT IGEEAKKVYD DAQNMLQELI SQKKLQARGV VGFWPAQSVE DDIHLYAEGT VPQAAEPIAT FYGLRQQAEK DSASTDPYLC LSDFIAPLHS GVPDYLGLFA VACFGVEELS KAYEAECDDY SIIMVKALGD RLAEAFAEEL HERVRKELWG YCGGEQLAVA DLRRLRFEGI RPAPGYPSQP DHTEKLTMWK LADVERLTGI RLTESLAMAP ASAVSGLYFS NVKSKYFAVG KISKDQIEDY ALRKNMTVAE VEKWLGPILG YDTD // ID F1T967_9FIRM Unreviewed; 811 AA. AC F1T967; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGD49049.1}; GN ORFNames=Cpap_3478 {ECO:0000313|EMBL:EGD49049.1}; OS [Clostridium] papyrosolvens DSM 2782. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminiclostridium. OX NCBI_TaxID=588581 {ECO:0000313|EMBL:EGD49049.1}; RN [1] {ECO:0000313|EMBL:EGD49049.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 2782 {ECO:0000313|EMBL:EGD49049.1}; 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., 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. {ECO:0000313|EMBL:EGD49049.1}. 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; ACXX02000002; EGD49049.1; -; Genomic_DNA. DR RefSeq; WP_004617131.1; NZ_ACXX02000002.1. DR EnsemblBacteria; EGD49049; EGD49049; Cpap_3478. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGD49049.1}; KW Transferase {ECO:0000313|EMBL:EGD49049.1}. SQ SEQUENCE 811 AA; 88664 MW; 1C70933A1798B796 CRC64; MDKVQFKKLV SQKIQILDGA TGTELQKRGM PTGVCPEQWV IENPNAIKEI QKAYIDAGSN IIYTCTFGGN RVKLEEFGLG ERTFEINQRL AQLSKETAAG KCLVAGDLAS TGRFIKPLGD MSFEACVDIY KEQVQGLLAG GVDLFVIETM LDIQEARAAL LAVKESCDLP VCVSMSFDES MRTLTGTDPV TALITLQSLG ADAVGCNCST GPEHMVEIIT RMKPYARVPL MAKPNAGLPK LVNNVTVFDM GPEEFGSFAE NFIQAGVNII GGCCGTSPEY IKELYRNCGD LKPRHFEYSE YSAITSSAKT VFFGINKPVA IVGERINPTG KKKLQAELKE GSTNEIRRFA LEQMEKGADI LDVNVGMPGI DEKEVMLNTV RLLGSVCDAP LCLDSSSPEV LEAALRIYPG RALINSISQE KVKLDKLLPV AAKYGAMFIL LPLNDEGVPE KAIQRQVIVQ EVFNQASDYG YKKSDIVVDG LVMTVSSNQE AALETLKLIQ WCREEFGCGT IVGLSNVSFG LPERGWVNAA FLSMAIAKGL TMAIANPSSD LLMCIKMACD VIMTNDVNSR NYISYFSSMD KPVKDGNEKK EAEKKTCDKI FDAVLNGDNE GIDKLIEKAI AEKTPPQDIV DIYLIPAINQ VGKLFDEKKY FLPQLIQSAE TMKSGFTFLE PLLKQKGEKE EKEDIVVVIA TVKGDIHDIG KNIVGLMLRN YGFKVHDLGK DVSAERIIDE AKKLKAHIVG LSALMTTTMV EMEEVIKLAK EKNVGCKFMI GGAVVDDDYA KTIGADGYSK DAYEAVKLAK KLSIKQAAEC N // ID F1TGC2_9FIRM Unreviewed; 585 AA. AC F1TGC2; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=Cpap_0740 {ECO:0000313|EMBL:EGD46487.1}; OS [Clostridium] papyrosolvens DSM 2782. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminiclostridium. OX NCBI_TaxID=588581 {ECO:0000313|EMBL:EGD46487.1}; RN [1] {ECO:0000313|EMBL:EGD46487.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 2782 {ECO:0000313|EMBL:EGD46487.1}; 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., 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGD46487.1}. 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; ACXX02000013; EGD46487.1; -; Genomic_DNA. DR RefSeq; WP_004621197.1; NZ_ACXX02000013.1. DR ProteinModelPortal; F1TGC2; -. DR EnsemblBacteria; EGD46487; EGD46487; Cpap_0740. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 585 AA; 64613 MW; 8D66118FFB37F6FD CRC64; MNIFSDRDYF LFDGAMGTYY SAKNKINTPC EFANISEREN ILNIHLEYIE AGANAIKTNT FGANRYSLGC QQSEVDRIIK SGYDIAVQAC LGQDVAVFAD IGPIPDGKGA NVEEEYKKIV DVFLECGAKN FLFETFAGTD ILTGIAAYIR LRLPETVIIT SFAVYPDGYS KEGFFYIDIM EKMYASGLVD AVGFNCISGP AHMYRLIKKA DIRGKNIIIM PNSGYPGSER GRTVYYDNSE YYAEKLVEIK NLGVKILGGC CGTTPRHIAA AAKLLTSPQS TEANTAISTH IETCELANES IIDKLIKNKK PILVEIDPPF DTNWEYMLRD ALILKQAGAD IITIADSPLA KARAESTIMA AKIQREVAIP VMPHITCRDK NLLGIKASLL GVHIEGIRNV LVITGDPIAD IERSRIKGVF SFNSSNLANY IKSLNSNVFC GQDIKIAGAL NVNAVNFGAE LKKAFTKIEN GISCFLTQAI YTKSAVENLL KAVETLNIPI FAGFMPIVSY KNAQFINNEV PGIDIDAEII EKFRDKSREE SEKLGMEITM DIVEKIYPHV SGFYLMTPLK RTGVICELIK KIKEL // ID F1YR35_9PROT Unreviewed; 1187 AA. AC F1YR35; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGE48766.1}; GN Name=metH {ECO:0000313|EMBL:EGE48766.1}; GN ORFNames=APO_0357 {ECO:0000313|EMBL:EGE48766.1}; OS Acetobacter pomorum DM001. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acetobacter. OX NCBI_TaxID=945681 {ECO:0000313|EMBL:EGE48766.1, ECO:0000313|Proteomes:UP000018454}; RN [1] {ECO:0000313|EMBL:EGE48766.1, ECO:0000313|Proteomes:UP000018454} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DM001 {ECO:0000313|EMBL:EGE48766.1}; 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). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGE48766.1}. 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; AEUP01000005; EGE48766.1; -; Genomic_DNA. DR RefSeq; WP_006115389.1; NZ_AEUP01000005.1. DR EnsemblBacteria; EGE48766; EGE48766; APO_0357. DR Proteomes; UP000018454; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000018454}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 756 756 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1187 AA; 130924 MW; 1AE52026F96A8BA7 CRC64; MLCGVGKALF PFLLYFMVAM SSRLPLLDAL RDQVLLCDGG MGSRIQMLDL DVQRDYWGQE NCTEILTLSR PELIREIHRG YFEAGADMVE TNTFGGSPIT LGEFGLTDRT REINKNSALL AREAAESFAD GRARYVLGSM GPGTKLPSLG NIDYDSLEAA LAEQARGLIE GGVDAILIET CQDTLQIKAA VNGVKIARAE LGASTPIFVQ VTVETTGTLL VGPDIAAAAT VIHSLDVDLM GLNCATGPQE MAEHVKWLSE NWPRLISVQP NAGLPELVNG QTHYPLTPAE MATWVERFIT EDGLNLIGGC CGTSTPHTEA LDAMLRRRAE GTGRLRPAPV PRTSVWVPSV ASLYSQVPLR QENAYFSIGE RCNANGSKKW RELQEAHDWD GCVTVGREQI REGSNALDIC TAFVGRNERA EMDEVIKRFT SSVNAPLVID STETPVIEAA LKLHGGKPII NSINFEDGEG PASDRMTLAR KFGAAVVALT IDEEGMARKP EDKLRIASRL VEFACEKYGL PQSDLMIDPL TFTIATGAED DRKLGQWTLE GIKMIRDAFP DIQIVLGLSN ISFGLNPAAR AVLNSVYLDH AVRAGMTAAI VHVSKIRPLH LIAPEEVKIA EDLIFDRRTE DYDPLQTLLA MFADRKAADA VKRKRAETAE ERLKDRIVDG DRKGLEADLE EAMQNMAPLD IINTVLLDGM KVVGELFGAG KMQLPFVLQS AETMKAAVAY LEPHMERTDG QQRGTIVLAT VKGDVHDIGK NLVDIILTNN GYRVVNLGIK VPVQDMIEAA RKEKADAIGM SGLLVKSTVI MRENLEEISR AGLDTPVLLG GAALTRNYVE EDCVAAYAPT GRVAYARDAF DGLTLMDQVS QKNFDDYLAA IQKRREGKAT RTNTRAPETA ETRGFGPVDV AAARARRERL TADEPPMVPP FWGSRVLEAT PEAVLPFLNE RALYQFQWGF RKQGRSLDDF LIWARQELRP ILRRMLDLTA KENILKPQAI YGYWKAAGDG NDLVLFEEDG TTEACRFTLP RQPKADGECI ADFVRDISNP ERDVIGLQVV TVGQKASDIA RDWFEENRYQ DYLYLHGLSV EMAEAMAEYT HKRIRAELGF AGEDARDMEK LLQQGYRGSR YSFGYPACPR LEDQHPILAL LDAERIGVSL TDGDQLHPEQ STSALVILNK HAKYFTI // ID F1Z8F0_9SPHN Unreviewed; 328 AA. AC F1Z8F0; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGD59075.1}; GN ORFNames=Y88_1137 {ECO:0000313|EMBL:EGD59075.1}; OS Novosphingobium nitrogenifigens DSM 19370. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Novosphingobium. OX NCBI_TaxID=983920 {ECO:0000313|EMBL:EGD59075.1}; RN [1] {ECO:0000313|EMBL:EGD59075.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 19370 {ECO:0000313|EMBL:EGD59075.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGD59075.1}. 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; AEWJ01000037; EGD59075.1; -; Genomic_DNA. DR RefSeq; WP_008065629.1; NZ_GL876926.1. DR EnsemblBacteria; EGD59075; EGD59075; Y88_1137. DR PATRIC; 46733891; VBINovNit182528_0342. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EGD59075.1}; KW Transferase {ECO:0000313|EMBL:EGD59075.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 241 241 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 328 AA; 34150 MW; 82AEB3FD05B086CF CRC64; MRVFVAPASP LDHAPSLAET CAPILKGEPA VSDTSAASPL IILDGGTGRE LNRIGAPFEQ PEWSALALIE GPEFVSRVHQ SYVDAGADVI TTNSYAVVPF HIGEERFAAR GHELAALAGK LARDVADAAP RKITVAGSLP PICGSYRPDL VDIDRARPIL AVLVEALAPY VDQWQAETLS SLIEAKLVAE LVKPTGKPLW LSFTLEDAHP DGEPRLRSGE SVTEAAKLAQ DLGASAILFN CSQPEVMAAA VRAAHAAASL PVGVYANAFP PMDEEAEANA GLSEIRADLD PAGYAAFARG WAGEGATILG GCCGIGPEHI AALRALTA // ID F1ZCL0_9SPHN Unreviewed; 353 AA. AC F1ZCL0; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:EGD57653.1}; GN ORFNames=Y88_2979 {ECO:0000313|EMBL:EGD57653.1}; OS Novosphingobium nitrogenifigens DSM 19370. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Novosphingobium. OX NCBI_TaxID=983920 {ECO:0000313|EMBL:EGD57653.1}; RN [1] {ECO:0000313|EMBL:EGD57653.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 19370 {ECO:0000313|EMBL:EGD57653.1}; 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. {ECO:0000313|EMBL:EGD57653.1}. 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; AEWJ01000054; EGD57653.1; -; Genomic_DNA. DR RefSeq; WP_008071096.1; NZ_GL876934.1. DR EnsemblBacteria; EGD57653; EGD57653; Y88_2979. DR PATRIC; 46739875; VBINovNit182528_3261. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 353 AA; 37862 MW; F9EA778D5BB41F2D CRC64; MTLVPSAARA AFLAEAAKRI LITDGAFGTE IQRRGLTEAD YAGSLGLSHD QKGNNDILAL TRPEVPEAIH RAYFEAGADI AETNTFSANR ISQADYGAEH LVRDINVASA RLARRVADEF TARDGRPRFV AGAIGPTNKT LSLSPDVNDP GYREIDWDTL VDVYAEQATA LVEGGADFIL VETVFDTLNA KAAIMAVRQV ERTLGREVPL MLSMTLTDLS GRNLSGHTVE AFWYAVRHAR PVTVGLNCSF GASQLRPHVR TLSEIAETLI MIYPNAGLPN ELGQYDEAPR TTAGLVGEWA EHGQVNVLGG CCGSTPDHIA AMAQAVAGLK PRALPDVPVE TRLAGLEPFI MAS // ID F1ZQD1_ECOLX Unreviewed; 1227 AA. AC F1ZQD1; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGE62074.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGE62074.1}; GN Name=metH {ECO:0000313|EMBL:EGE62074.1}; GN ORFNames=ECSTEC7V_4757 {ECO:0000313|EMBL:EGE62074.1}; OS Escherichia coli STEC_7v. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=754082 {ECO:0000313|EMBL:EGE62074.1}; RN [1] {ECO:0000313|EMBL:EGE62074.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=STEC_7v {ECO:0000313|EMBL:EGE62074.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AEXD01000026; EGE62074.1; -; Genomic_DNA. DR RefSeq; WP_000096046.1; NZ_AEXD01000026.1. DR EnsemblBacteria; EGE62074; EGE62074; ECSTEC7V_4757. DR PATRIC; 48186477; VBIEscCol149628_4605. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGE62074.1}; KW Transferase {ECO:0000313|EMBL:EGE62074.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136070 MW; 89BFE38E1C7F3E7E CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG EEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID F1ZYL4_THEET Unreviewed; 807 AA. AC F1ZYL4; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGD50800.1}; GN ORFNames=TheetDRAFT_2404 {ECO:0000313|EMBL:EGD50800.1}; OS Thermoanaerobacter ethanolicus JW 200. OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Thermoanaerobacter. OX NCBI_TaxID=509192 {ECO:0000313|EMBL:EGD50800.1}; RN [1] {ECO:0000313|EMBL:EGD50800.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=JW 200 {ECO:0000313|EMBL:EGD50800.1}; 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., 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGD50800.1}. 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; AEYS01000041; EGD50800.1; -; Genomic_DNA. DR RefSeq; WP_003871153.1; NZ_AEYS01000041.1. DR EnsemblBacteria; EGD50800; EGD50800; TheetDRAFT_2404. DR PATRIC; 46800138; VBITheEth54201_2545. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGD50800.1}; KW Transferase {ECO:0000313|EMBL:EGD50800.1}. SQ SEQUENCE 807 AA; 88136 MW; 7159B1A5BFD87F71 CRC64; MLDIFKELSN RVIVFDGAMG TQLQERGLKS GECPEYMNIT HPEVVFDIHR SYIEAGADVI ETNTFGANRI KLAKYGLENE VFNIVTQAVK IAKEASKDKP VALSIGPIGE LLTPYGDMTF DEAYDVFKEV VIAAERAGAD IVLIETMSDM LEAKAAILAA KENSNMKVIC TMTFQEDGRT LMGSDPITVV VSLQGLGLDA IGVNCSTGPD KMVSVVEKMS QVSRIPIIAQ PNAGMPVIRD GKTVYDLKPE EFASFFPLLV EKGASIVGGC CGTTPHYIKL VKKAVKDLKP KVKVNKFTAV ASNTKTVFIG ENYLLRVIGE RINPTGKKKL SEAFLAGDVS LAVEEAIKQQ KCGAEILDVN VGVPGVNEEE LLPKVVSEIQ NVVDIPLQID STNIKAVEKA IRILRGRPII NSVSAKEESL KEVLPIVKKY GACVVGLTVG DKGLPKDRHE RIENAKKIIK KAEEYGIPKE DILIDCIVLT VSSEQEAAIE TLEAIKLAKE ELGVNTVVGL SNVSFGLPER RLINSTFLAM AASYGLTTAI INPCDEAMMD TLRASMVLLN KDKGSVNYLN IYGKKQKEEI KEKEQQKIQE EDLKSKLYIQ ILEGKKSGVE DIVKNILEEE VQPLSIVDNI IIPALKEVGD RYEKGIYFLP QLLSSAEVVQ SAFKIIKEKL PKGSVSKGKI ILATVEGDVH DIGKNIVKVL LENYGYDVID LGKDVKGEVI LEEVKRTGAP LVGLSALMTT TLFNMEKIIK LLKANTDVKI MVGGAVLTEE YAYKIGADYY GKTAQDAVKI ADKFFLKNAL LCKTCGI // ID F2A473_RHIET Unreviewed; 319 AA. AC F2A473; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGE60660.1}; GN ORFNames=RHECNPAF_1360034 {ECO:0000313|EMBL:EGE60660.1}; OS Rhizobium etli CNPAF512. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=993047 {ECO:0000313|EMBL:EGE60660.1}; RN [1] {ECO:0000313|EMBL:EGE60660.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CNPAF512 {ECO:0000313|EMBL:EGE60660.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGE60660.1}. 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; AEYZ01000047; EGE60660.1; -; Genomic_DNA. DR EnsemblBacteria; EGE60660; EGE60660; RHECNPAF_1360034. DR PATRIC; 53537202; VBIRhiEtl185341_0944. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EGE60660.1}; KW Transferase {ECO:0000313|EMBL:EGE60660.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 226 226 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 302 302 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 319 AA; 34365 MW; 1CCF926DCA3B1F29 CRC64; MKSPPPATAR RPEWRPFMST TRILDGGMSR ELLRLGAELK QPEWSALALI NSPEIVREVH KEFIAAGSEI ITTNSYALVP FHIGEDRFQT EGAALIRLAG RLAREAADSV PGRKVLVAGS LPPIFGSYEP QNFQPKRVQD YLKVLVENLA PFVDIWLGET LSLIAEGEAV RQAVAESGKP FWISFTLADD KADIESGEPK LRSGESVEDA ASWAASSGAE AFLFNCSKPE VMEAAVATAA AAFRKMDAGI EIGVYANAFE GEQGESAANE GLHETRDDLN DDAYSRFACS WAEAGATIIG GCCGIGAAHI HRLGKTLRS // ID F2AWE5_RHOBT Unreviewed; 1234 AA. AC F2AWE5; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EGF26028.1}; GN ORFNames=RBWH47_01223 {ECO:0000313|EMBL:EGF26028.1}; OS Rhodopirellula baltica WH47. OC Bacteria; Planctomycetes; Planctomycetia; Planctomycetales; OC Planctomycetaceae; Rhodopirellula. OX NCBI_TaxID=991778 {ECO:0000313|EMBL:EGF26028.1}; RN [1] {ECO:0000313|EMBL:EGF26028.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=WH47 {ECO:0000313|EMBL:EGF26028.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGF26028.1}. 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; AFAR01000198; EGF26028.1; -; Genomic_DNA. DR RefSeq; WP_007327955.1; NZ_AFAR01000198.1. DR EnsemblBacteria; EGF26028; EGF26028; RBWH47_01223. DR PATRIC; 53609337; VBIRhoBal184597_4291. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 251 251 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 315 315 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 767 767 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1234 AA; 137711 MW; D507F7A154278843 CRC64; MLQATSTDQL LAELIRERIL MLDGAMGTMI QRLELDEAAV RSDRFADHHK DLKNFSDILC LTHPEKITEI HSKYYEAGSD IVETNSFGAS PIGMVEFDLP LELVNEINVA AVACARKAAD QWTEKTPDKP RFVAGSIGPT TMQLAISTDV EDAAFRATTF DKLADSYYAQ VKSLCEAGVD ILLPETAIDT LNLKSCLFAI QRYFDEGGRR VPVMVSGTFD KGGRTFVSGQ SVEAFVTALS HFPVLSVGMN CALGPDIMRP HVEEMSKATG LPISCHPNAG LPNEMGAFDL DPKPMAEIVG EYADNGWINI LGGCCGTTPD HIRAMTERVQ GCKPKQEDKS GPVWTRLSGQ LPMVMRPEIP FTMVGERTNV TGSRKFARLI RNEEYDEAVE VAREQVENGA TIIDVNFDDA LLDGVEAMTR FLRLIAGDSV VAAVPVMIDS SRWEVIEAGL QNVQGKAIVN SISLKDGEEE FLRRARLVRQ YGAATVVMAF DEEGQAADED NKVRICKRAY DLLVNEVHFP PEDIIFDPNI LTVATGMEEH NNYAVDFVNA VERIKKECPG AKTSGGVSNI SFSFRGNDPV REAIHSAFLY RAVKAGLDMG IVNAGQLEVY EEIPKDLLEH VEDVLWNRRD DATDRMLEFA ETVKGSGKKK SGEDLTWREN SIEERMKHAL IKGIDKYIVE DTEEARQHYD KCLHIIEGPL MAGMSVVGDL FGQGKMFLPQ VVKSARVMKK AVAYLEPFME QEKIESGTQD HKARGKFLIA TVKGDVHDIG KNIVGVVLQC NNYEVIDLGV MVSSEKILEE AVKQDADMIG LSGLITPSLD EMVHVAREMK RIGMKKPLLV GGATTSAKHT AVRIAPAYDG PVLHVLDASR SVGVVEKLLS DDSRDAFLEA NVSEQEKLVS SFRERKQTLV PYEQALEKRF QTDWETVRID QPEFIGTKVL EDFPLATLRE YIDWSPYFMT WELKGKYPKI FQDETVGPIA KEVFEKANKM LDRVIDEKLI RAKGVYGFWP AASDGDDIIV YTDESRTEER TRFHCLRQQW ERRGQKDFRS LADYIAPVDS GRKDYLGGFA VTAGLGAEEL SMRFKKELDD ESSIIASAVA DRCAEAFAEY LHQQVRQQWQ YGKEENLSNE DMIAEKYRGI RPAAGYPACP DHTEKRTLFD LLEAEKNTGI NLTESYAMSP GASVSGLYFS HPDAKYFTVD RMTKDQIESY AARKGWPISE VERWLSPNLA YDPS // ID F2BS92_STRSA Unreviewed; 315 AA. AC F2BS92; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGF06767.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EGF06767.1}; GN Name=mmuM {ECO:0000313|EMBL:EGF06767.1}; GN ORFNames=HMPREF9394_1382 {ECO:0000313|EMBL:EGF06767.1}; OS Streptococcus sanguinis SK1057. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=888821 {ECO:0000313|EMBL:EGF06767.1}; RN [1] {ECO:0000313|EMBL:EGF06767.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK1057 {ECO:0000313|EMBL:EGF06767.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGF06767.1}. 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; AFBA01000007; EGF06767.1; -; Genomic_DNA. DR RefSeq; WP_004187028.1; NZ_GL878514.1. DR EnsemblBacteria; EGF06767; EGF06767; HMPREF9394_1382. DR PATRIC; 53625992; VBIStrSan171647_1360. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGF06767.1}; KW Transferase {ECO:0000313|EMBL:EGF06767.1}. SQ SEQUENCE 315 AA; 34669 MW; 5CADA744F382AC9F CRC64; MGKFKDLLDK QEIIILDGAL GTELESRGYD VSGKLWSAQY LLDQPQIIQN VHESYVRAGS DIITTSSYQA SIPAFVEAGL TPEKAYDLLK ETVFLAQKAI ENVWTGLSPE EQKQRPYPLV AGSVGPYAAY LADGSEYTGD YQLSEEEFQE FHRPRIQALL EAGCDLLAIE TIPNGAEAAA ILRLLAEEFP QAEAYLSFVA QSETAISDGT KIEDLGNLAQ ESPQVLAVGF NCTAPHLITP LLDGLGQVCN KPFLTYPNSG ETYNGLTKTW HDDPEQERSL LENSKLWQNQ GVRLFGGCCR TRPEDIDQLA KGFKG // ID F2BXA7_9FIRM Unreviewed; 306 AA. AC F2BXA7; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 12. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGF13664.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EGF13664.1}; GN Name=mmuM {ECO:0000313|EMBL:EGF13664.1}; GN ORFNames=HMPREF9083_0787 {ECO:0000313|EMBL:EGF13664.1}; OS Dialister micraerophilus DSM 19965. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Dialister. OX NCBI_TaxID=888062 {ECO:0000313|EMBL:EGF13664.1}; RN [1] {ECO:0000313|EMBL:EGF13664.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 19965 {ECO:0000313|EMBL:EGF13664.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGF13664.1}. 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; AFBB01000016; EGF13664.1; -; Genomic_DNA. DR RefSeq; WP_007556093.1; NZ_GL878519.1. DR EnsemblBacteria; EGF13664; EGF13664; HMPREF9083_0787. DR PATRIC; 55001179; VBIDiaMic173032_0774. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGF13664.1}; KW Transferase {ECO:0000313|EMBL:EGF13664.1}. SQ SEQUENCE 306 AA; 34129 MW; 2A59FC2A855A668B CRC64; MSTIIELLKE KKLLVIDGSF ASELEKAGLN LCDSLWSAKA LYENPELVTK VHENYFESGA DIAITGSYQA HVQGFLGKGF THEKAIELIK LSVKLAKKAK ENCLKKHPER KLAIAAAVGP YGAYLADGSE YVGNYGLSVK ELEEFHEEKI ESLASENPDF FAFETIPSFD EARAYVNILK RHENITGWFT FSCKDEKHIS EGVEISEVAK FLDKENQVHA IGVNCTKPEY IEPLICEIKK ATDKSVAVYS NTGENYDPVT KTWSGELADF TKYAKRWYES GAKLIGGCCR TLPEEIKAVC KFAKSI // ID F2C6C0_STRSA Unreviewed; 315 AA. AC F2C6C0; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGF15577.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EGF15577.1}; GN Name=mmuM {ECO:0000313|EMBL:EGF15577.1}; GN ORFNames=HMPREF9386_0724 {ECO:0000313|EMBL:EGF15577.1}; OS Streptococcus sanguinis SK330. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=888813 {ECO:0000313|EMBL:EGF15577.1}; RN [1] {ECO:0000313|EMBL:EGF15577.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK330 {ECO:0000313|EMBL:EGF15577.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGF15577.1}. 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; AFBD01000002; EGF15577.1; -; Genomic_DNA. DR RefSeq; WP_002915297.1; NZ_GL878548.1. DR EnsemblBacteria; EGF15577; EGF15577; HMPREF9386_0724. DR PATRIC; 53629351; VBIStrSan170642_0709. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGF15577.1}; KW Transferase {ECO:0000313|EMBL:EGF15577.1}. SQ SEQUENCE 315 AA; 34626 MW; 18F91DE030732734 CRC64; MGKFKDLLDK QEIIILDGAL GTELESRGYD VSGKLWSAQY LLDQPQIIQD VHESYVRAGS DIITTSSYQA SIPAFIEAGL TPEKGYDLLK ETVFLAQKAI ENVWQELSPE EQKQRSYPLV AGSVGPYAAY LADGSEYTGN YQLSEAEFRE FHCPRIQALL EAGSDLLAIE TIPNGAEAAA ILRLLAEEFP QAEAYLSFVA QSENAISDGT KIEELGNLAQ ESPQVLAVGF NCTAPHLIAP LLDALGQVCN KPFLTYPNSG ETYNGLTKTW HDDPEQERSL LENSKLWQNQ GVRLFGGCCR TRPEDIAQLA KGFKG // ID F2CDB9_STRSA Unreviewed; 315 AA. AC F2CDB9; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGF19559.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EGF19559.1}; GN Name=mmuM {ECO:0000313|EMBL:EGF19559.1}; GN ORFNames=HMPREF9391_0785 {ECO:0000313|EMBL:EGF19559.1}; OS Streptococcus sanguinis SK408. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=888818 {ECO:0000313|EMBL:EGF19559.1, ECO:0000313|Proteomes:UP000004826}; RN [1] {ECO:0000313|EMBL:EGF19559.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK408 {ECO:0000313|EMBL:EGF19559.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGF19559.1}. 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; AFBE01000005; EGF19559.1; -; Genomic_DNA. DR RefSeq; WP_002917304.1; NZ_GL878559.1. DR EnsemblBacteria; EGF19559; EGF19559; HMPREF9391_0785. DR PATRIC; 53634294; VBIStrSan170070_0754. DR Proteomes; UP000004826; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000004826}; KW Methyltransferase {ECO:0000313|EMBL:EGF19559.1}; KW Transferase {ECO:0000313|EMBL:EGF19559.1}. SQ SEQUENCE 315 AA; 34694 MW; 3A0CAEAAC987E114 CRC64; MGKFKDLLDK QEIIILDGAL GTELESRGYD VSGKLWSAQY LLDQPQIIQN VHESYVRAGS DIITTSSYQA SIPAFVEAGL TPEKAYDLLK ETVFLAQKAI ENVWTGLSPE EQKQRPYPLV AGSVGPYAAY LADGSEYTGD YQLSEEEFRD FHRPRIQALL EAGSDLLAIE TTPNGAEAAA ILRLLAEEFP QAEAYLSFVA QSENAISDGT KIEELGNLAQ ESPQVLAVGF NCTAPHLIAP LLDGLGQVCN KPFLTYPNSS ETYNGLTKTW HDDPVQERSL LENSKLWQNQ GVRLFGGCCR TRPEDIDQLA KGFKV // ID F2D1S5_HORVD Unreviewed; 325 AA. AC F2D1S5; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Predicted protein {ECO:0000313|EMBL:BAJ89046.1}; OS Hordeum vulgare var. distichum (Domesticated barley). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; OC Pooideae; Triticeae; Hordeum. OX NCBI_TaxID=112509 {ECO:0000313|EMBL:BAJ89046.1}; RN [1] {ECO:0000313|EMBL:BAJ89046.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Shoot {ECO:0000313|EMBL:BAJ89046.1}, and RC Shoot and root {ECO:0000313|EMBL:BAJ94521.1}; 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; AK357832; BAJ89046.1; -; mRNA. DR EMBL; AK363317; BAJ94521.1; -; mRNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; SQ SEQUENCE 325 AA; 35136 MW; 6E8A497A104AD4B5 CRC64; MGGGVVEELV KKAGGCAVID GGFATQLEAL GADINDPLWS AACLITKPHL IKEVHMQYLE AGADVIISSS YQATIPGFLA RGLLLEEAEG LLRTSVQLAL EARDEFWKST LRKSKPVYNR ALVAASVGSY GAYLADGSEY SGSYGDDVTA EKLKDFHRRR LQVLASAGPD LIAFEAIPNK MEAQALVELL EEEDIQVPSW ICFSSVDGKH LCSGESFGDC LEILNASDKV AIVGVNCTPP QFVEGIIRDF KKQTEKAIAV YPNSGEVWDG RAKRWLPVEC FGRKSFDAMA RRWQEAGASL VGGCCRTTPS TIRAVSKALK SRNGL // ID F2E6K4_HORVD Unreviewed; 343 AA. AC F2E6K4; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 04-MAR-2015, entry version 16. DE SubName: Full=Predicted protein {ECO:0000313|EMBL:BAK02976.1}; OS Hordeum vulgare var. distichum (Domesticated barley). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; OC Pooideae; Triticeae; Hordeum. OX NCBI_TaxID=112509 {ECO:0000313|EMBL:BAK02976.1}; RN [1] {ECO:0000313|EMBL:BAK02976.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Shoot and root {ECO:0000313|EMBL:BAK02976.1}; 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; AK371778; BAK02976.1; -; mRNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; SQ SEQUENCE 343 AA; 36714 MW; 50A74DA9C587AA2E CRC64; MVVKSAGGGG GGGGAEEGAA GAAVRRWVEA GGGRLVLDGG LATELEAHGA DLNDPLWSAK CILSSPHLIR KVHLDYIEAG ANIIITASYQ ATIQGFEAKG FSKEQGENLL TKSVEIAHEA REMFLKEHPD QSTALRPILV AASIGSYGAY LADGSEYSGD YGEAGTLEFL KDFHRRRLQV LAEARPDLIA FETIPNKLEA QAYVELLDEC NINIPSWFSF NSKDGVNVVS GDSLIECANI ANACAKVGAV GINCTPPRFI HSLILSIRKV TDKPILIYPN SGERYDAEKK EWVESTGVSD GDFVSYVGEW CKDGAALIGG CCRTTPNTIR AISRSLNQYY PAA // ID F2EGB7_HORVD Unreviewed; 360 AA. AC F2EGB7; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Predicted protein {ECO:0000313|EMBL:BAK06389.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:MLOC_58603.8}; OS Hordeum vulgare var. distichum (Domesticated 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] {ECO:0000313|EMBL:BAK06389.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Seed {ECO:0000313|EMBL:BAK06389.1}; 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). RN [2] {ECO:0000313|EnsemblPlants:MLOC_58603.8} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Morex {ECO:0000313|EnsemblPlants:MLOC_58603.8}; RA Scholz U.; RT "The genome sequence of Hordeum vulgare subsp. vulgare."; RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EnsemblPlants:MLOC_58603.8} RP IDENTIFICATION. RC STRAIN=subsp. vulgare {ECO:0000313|EnsemblPlants:MLOC_58603.8}; RG EnsemblPlants; RL Submitted (FEB-2015) 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; AK375194; BAK06389.1; -; mRNA. DR EnsemblPlants; MLOC_58603.8; MLOC_58603.8; MLOC_58603. DR InParanoid; F2EGB7; -. DR OMA; YGRSVTK; -. DR Proteomes; UP000011116; Unassembled WGS sequence. DR ExpressionAtlas; F2EGB7; baseline. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Complete proteome {ECO:0000313|Proteomes:UP000011116}; KW Reference proteome {ECO:0000313|Proteomes:UP000011116}. SQ SEQUENCE 360 AA; 38095 MW; 4E2B7C0CB75DFC74 CRC64; MGRGDGHDDA LRRWLREAGG WLVVDGALGT ELEAHGADLQ DELWSARCLV SAPHLIRKVH LDYLEAGANI ITTASYQATL QGFQSRGVSR EQGEALLRRS VQIAQEARAI FVEGRSKGPY AARDEKDAVA SGARRPVLVA ASVGSYGAYL ADGSEYTGDY GRSVTKEALK NFHRRRLQVL ADAGPDLIAF ETIPNKLEAQ AYAELLEEND IRIPAWFSFT SKDGASAASG DPITECAAVA DSCRRVAAVG INCTVPRLIN GLILSISKVT SKPIVVYPNT GETYVAETKE WVDSAGAGAG GGGAPGTDFV SCVGKWRQAG ASLVGGCCRT APATVRAISR ALREADAADT DDEFPAVAVL // ID F2F7E4_SOLSS Unreviewed; 614 AA. AC F2F7E4; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 22. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=SSIL_0446 {ECO:0000313|EMBL:BAK14869.1}; OS Solibacillus silvestris (strain StLB046) (Bacillus silvestris). OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; OC Solibacillus. OX NCBI_TaxID=1002809 {ECO:0000313|EMBL:BAK14869.1, ECO:0000313|Proteomes:UP000006691}; RN [1] {ECO:0000313|Proteomes:UP000006691} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=StLB046 {ECO:0000313|Proteomes:UP000006691}; RA Morohoshi T., Someya N., Ikeda T.; RT "Genome sequence of Solibacillus silvestris StLB046."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:BAK14869.1, ECO:0000313|Proteomes:UP000006691} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=StLB046 {ECO:0000313|EMBL:BAK14869.1, RC ECO:0000313|Proteomes:UP000006691}; RX PubMed=22019407; DOI=10.1016/j.jbiosc.2011.09.006; RA Morohoshi T., Tominaga Y., Someya N., Ikeda T.; RT "Complete genome sequence and characterization of the N-acylhomoserine RT lactone-degrading gene of the potato leaf-associated Solibacillus RT silvestris."; RL J. Biosci. Bioeng. 113:20-25(2012). CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; BAK14869.1; -; Genomic_DNA. DR RefSeq; WP_008408494.1; NC_018065.1. DR RefSeq; YP_006461015.1; NC_018065.1. DR EnsemblBacteria; BAK14869; BAK14869; SSIL_0446. DR KEGG; siv:SSIL_0446; -. DR KO; K00547; -. DR Proteomes; UP000006691; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006691}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000006691}. SQ SEQUENCE 614 AA; 67997 MW; 43E3C24A17344A0E CRC64; MGLLEELQTR VLTADGAIGT LLYSYGLDYC HEEMNIARPD IIEKIHSEYI AAGADIIQTN TYGANRIKLA RYGYENRVKE FNEAALKIAK RAASLDGQYV LATIGGIRGI RKSDATLDEI LAAFQEQAEV LLAGEPDGFL LETYYDFEEL SHCVHLLRSM TDLPIIAQVT MQEPGVLQNL MTLNEAFQDL ERLGADIVGS NCRLGPFHTI QAFEGVNLPN KAFLSAYPNA SLLDIEDGRV VYESETDYFA RAAVELVNQG VRLIGGCCGT TPKHIAAVKK RLANMQPIET KEEKHRSTQF VRIPEPRKQE PLHEKAKRER SVIVELDTPR HLEIDGFVEG AKQLSKAGAD VIMMADNSLA SPRISNIAMA AILKEQGIRS LPHLTCRDRN LIGLQSHLMG LDALELHDIL VVTGDPTKVG DFPGATSVYD VSSMELISLI KQLNKGGSFT GKSLRKQANF SVAAAFNPNV RVLDRAVARL EKKIEHGADY FISQPVYTKE KIIEIYEATK HLETPIYIGI MPLTSSRSAE FLHHEVPGIK LSDEVLARMA ACGDDKEAST AEGIAIAKEL LDTACEYFNG IYLITPFLRY DMTLELMDYV KQYDVESKGV QSNV // ID F2F7E5_SOLSS Unreviewed; 1143 AA. AC F2F7E5; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 01-APR-2015, entry version 26. DE SubName: Full=Methionine synthase I, cobalamin-binding domain {ECO:0000313|EMBL:BAK14870.1}; GN OrderedLocusNames=SSIL_0447 {ECO:0000313|EMBL:BAK14870.1}; OS Solibacillus silvestris (strain StLB046) (Bacillus silvestris). OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; OC Solibacillus. OX NCBI_TaxID=1002809 {ECO:0000313|EMBL:BAK14870.1, ECO:0000313|Proteomes:UP000006691}; RN [1] {ECO:0000313|Proteomes:UP000006691} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=StLB046 {ECO:0000313|Proteomes:UP000006691}; RA Morohoshi T., Someya N., Ikeda T.; RT "Genome sequence of Solibacillus silvestris StLB046."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:BAK14870.1, ECO:0000313|Proteomes:UP000006691} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=StLB046 {ECO:0000313|EMBL:BAK14870.1, RC ECO:0000313|Proteomes:UP000006691}; RX PubMed=22019407; DOI=10.1016/j.jbiosc.2011.09.006; RA Morohoshi T., Tominaga Y., Someya N., Ikeda T.; RT "Complete genome sequence and characterization of the N-acylhomoserine RT lactone-degrading gene of the potato leaf-associated Solibacillus RT silvestris."; RL J. Biosci. Bioeng. 113:20-25(2012). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP012157; BAK14870.1; -; Genomic_DNA. DR RefSeq; WP_014822554.1; NC_018065.1. DR RefSeq; YP_006461016.1; NC_018065.1. DR EnsemblBacteria; BAK14870; BAK14870; SSIL_0447. DR KEGG; siv:SSIL_0447; -. DR KO; K00548; -. DR BioCyc; SSIL1002809:GLKA-800-MONOMER; -. DR Proteomes; UP000006691; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006691}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006691}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 725 725 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1143 AA; 125984 MW; 4B01D0A95D8591C3 CRC64; MYNHPIHEQL QKRILIIDGA MGTMLQAENL TYEDFGGEDL DGCNENLVLT RPDVLGKIHR EYLAAGADII CTNTFGGTPL VLDEYDLGDK AVEINKRAVE IALEAAKEFS TPEWPRFVAG AIGPTTKTLS VTGGITFEEL EENFYIQAKA LIEAGADLLL METSQDMLNV KAGTIAIHRA FEELGKELPV MISGTIEPMG TTLAGQSIEA FYISIEHIKP LSVGLNCATG PEFMTDHIRS LAELSNGYIS CYPNAGLPDE EGCYHETPDS LSKKLQGFAE KGWLNIVGGC CGTTPAHIAA IREAVDGYKP REPKDVTHGH VVSGIEPLQY DESMRPLFIG ERTNVIGSRK FKNLIVDGKF EEAAEIARAQ VKNGAHVIDI CLANPDRDEV EDMKNFMQEV VKKVKVPLVI DSTDEKVMEV ALKFSQGKAI INSINLEDGE ERFDAVMPLV KKYGASLVVG TIDETGMAIT REQKLEVAKR SYKLLTEKWG MSAEDIIFDP LMFPVGTGDE QYIGAAEETI EGIRLIKEHL PGCLTVLGVS NVSFGLPPVG REVLNAVYLY HCTQAGLDYA IVNTEKLERY ASIPEEEIKL ANDLIFNTND ETLAVFTDFY RDKKKDAVVK ELPATVEERL AYYILEGTKE GLIEDLNAAL EKFDTPLDII NGPLMAGMAE VGKLFNENQL IVAEVLQSAG VMKAAVAHLE QFMEKGDTSA NKGTMVLATV KGDVHDIGKN LVDIILSNNG YRVVDLGIKV TPAQLIETIR REKPDFIGLS GLLVKSAQQM VITAQDFKEA GIDIPILVGG AALSRRFTET KIADQYDGPV IYSKDAMQGL EQANRLMNTN ERHVFIEELR DAREKRLESD AKRAARPAVA VLEKPVRTVG DAAVWKPKDL VPHIKPDYSV AHLHPYVNMR TLIGHHLGLK GNLEQLLADQ DERAILLTDL VNGYLTSGGL SASGMYQFFP AQSDGDDVVV YSPDNAKTEI KRFTFPRQQA APFLCLSDYL KPVDSGEMDY IALMVVTAGK GVSEKANELK QAGKFLESHA LQATALELAE GFAERIHQEI RDQWGFPDAT DFTMRDRFAA KYQGQRFSFG YPACPNLEDQ EKLFSLLKPE KIGVHLTEGF MMEPEASVSA IVFAHPDARY FNV // ID F2G407_ALTMD Unreviewed; 355 AA. AC F2G407; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AEA97349.1}; GN OrderedLocusNames=MADE_1006035 {ECO:0000313|EMBL:AEA97349.1}; OS Alteromonas macleodii (strain DSM 17117 / Deep ecotype). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Alteromonas. OX NCBI_TaxID=314275 {ECO:0000313|EMBL:AEA97349.1, ECO:0000313|Proteomes:UP000001870}; RN [1] {ECO:0000313|EMBL:AEA97349.1, ECO:0000313|Proteomes:UP000001870} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17117 / Deep ecotype {ECO:0000313|Proteomes:UP000001870}; 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 ----------------------------------------------------------------------- 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; AEA97349.1; -; Genomic_DNA. DR RefSeq; WP_012517691.1; NC_011138.3. DR RefSeq; YP_004426347.1; NC_011138.3. DR ProteinModelPortal; F2G407; -. DR EnsemblBacteria; AEA97349; AEA97349; MADE_1006035. DR GeneID; 10556546; -. DR KEGG; amc:MADE_1006035; -. DR OMA; AQEDYKM; -. DR BioCyc; AMAC314275:GHA7-1221-MONOMER; -. DR Proteomes; UP000001870; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001870}; KW Methyltransferase {ECO:0000313|EMBL:AEA97349.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001870}; KW Transferase {ECO:0000313|EMBL:AEA97349.1}. SQ SEQUENCE 355 AA; 38598 MW; FFF30033F99C4BA5 CRC64; MSKNTISSAQ TTLTKAAKER ILILDGAMGT MIQRHKLEED DYRGTQFSDW HCDVKGNNDM LVITQPDIIY QIHCDYFEAG ADIIETNTFN ATTIAMADYD MQAHSRDINV AAAKLARKAA DEFTAKTPNK PRFVAGVLGP TNRTASISPD VNDPGKRNVT FDELVDAYSE STEALIEGGV DLIMLETIFD TLNAKAAAYA VESVFEKLGK SLPVMVSGTI TDASGRTLSG QTAEAFYYSM RHISPFSFGL NCALGPDLLR QYVDEVAAIS ECFISAHPNA GLPNEFGEYD MEGPEMAEHI KEWAQSGLVN IVGGCCGSTP DHIREIANAV AGIAPRNVPA FEPKMRLSGL EPFVH // ID F2H6T5_BACTU Unreviewed; 1132 AA. AC F2H6T5; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 31. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AEA17932.1}; GN Name=metH {ECO:0000313|EMBL:AEA17932.1}; GN ORFNames=CT43_CH4270 {ECO:0000313|EMBL:AEA17932.1}; OS Bacillus thuringiensis serovar chinensis CT-43. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=541229 {ECO:0000313|EMBL:AEA17932.1, ECO:0000313|Proteomes:UP000008135}; RN [1] {ECO:0000313|EMBL:AEA17932.1, ECO:0000313|Proteomes:UP000008135} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CT-43 {ECO:0000313|EMBL:AEA17932.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001907; AEA17932.1; -; Genomic_DNA. DR RefSeq; WP_000649720.1; NC_017208.1. DR RefSeq; YP_005574223.1; NC_017208.1. DR EnsemblBacteria; AEA17932; AEA17932; CT43_CH4270. DR KEGG; btc:CT43_CH4270; -. DR PATRIC; 54161551; VBIBacThu155232_4403. DR KO; K00548; -. DR BioCyc; BTHU541229:GL8T-4368-MONOMER; -. DR Proteomes; UP000008135; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008135}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEA17932.1}; KW Transferase {ECO:0000313|EMBL:AEA17932.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 125985 MW; 3BA40F322F8A7B3F CRC64; MKCIEEKLQN SILILDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYELSHLDE ELNEKAALLA KQAVKESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGE VDVLLVETSQ DMRNVKAAYI GIQAAFEELK KTVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWIN IIGGCCGTTP EHIKAMKEAL ASLKPRDHHE REGHGISGLE ALQYDESMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMEKF LTEVTKVLKV PIMIDSTDEN VMARALTYIQ GKAVINSINL EDGEERFEKV TPLLRKYGAA IVVGTIDEDG MAVSAERKLE IAKRSYELLT TKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPEE EKHLADALLF ETTKETLEEF TNFYRVAKKK DVVVQETLTL DERLANYIVE GTKQGLHEDL SLALEEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILA NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAANIDVPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV KKEEKKVEIP AVIEPLPKAE VMVPDSTKRI VLRDIPALHL APFLNRQMLL GHHLGLKGNV KKLLKEGDKR AHELNDLIDE LLQEGQSWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRVIE RFTFPRQGKA PYRTLGDYLR PIGDEMDYVA FLSVTVGEGV RDIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID F2H6T6_BACTU Unreviewed; 610 AA. AC F2H6T6; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 26. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=CT43_CH4271 {ECO:0000313|EMBL:AEA17933.1}; OS Bacillus thuringiensis serovar chinensis CT-43. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=541229 {ECO:0000313|EMBL:AEA17933.1, ECO:0000313|Proteomes:UP000008135}; RN [1] {ECO:0000313|EMBL:AEA17933.1, ECO:0000313|Proteomes:UP000008135} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CT-43 {ECO:0000313|EMBL:AEA17933.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; AEA17933.1; -; Genomic_DNA. DR RefSeq; WP_000770353.1; NC_017208.1. DR RefSeq; YP_005574224.1; NC_017208.1. DR ProteinModelPortal; F2H6T6; -. DR EnsemblBacteria; AEA17933; AEA17933; CT43_CH4271. DR KEGG; btc:CT43_CH4271; -. DR PATRIC; 54161553; VBIBacThu155232_4404. DR KO; K00547; -. DR BioCyc; BTHU541229:GL8T-4369-MONOMER; -. DR Proteomes; UP000008135; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008135}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:AEA17933.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:AEA17933.1}. SQ SEQUENCE 610 AA; 67159 MW; D96AD95B688315AB CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNVSDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTE INRAAVKLAK ASVTDKNAIL GTIGGMKHIG AVTTTDMERE FMLLEQAGAL LEEQVDGLLL ETFYDEFELL HAVKVLRKQT NIPIVAQLAL HEAGTTQNGN DVNEILKQLI DYGANVVGLN CQLGPLHMTE AFKMISIPQN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPRFIEQGI RLLGGCCGTT PEHIQSMKHA VANVTPVIEK DTIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRISNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIA LIEEVYEATK HLEQPIFIGI MPLVSKRNAD FLHFEVPGIT LPEEIRERMD GHETKEAAIE EGIRISQELI DAAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID F2HVE1_BRUMM Unreviewed; 1261 AA. AC F2HVE1; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:ADZ65277.1}; GN Name=metH {ECO:0000313|EMBL:ADZ65277.1}; GN OrderedLocusNames=BM28_A0201 {ECO:0000313|EMBL:ADZ65277.1}; OS Brucella melitensis (strain M28). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=941967 {ECO:0000313|EMBL:ADZ65277.1, ECO:0000313|Proteomes:UP000007457}; RN [1] {ECO:0000313|EMBL:ADZ65277.1, ECO:0000313|Proteomes:UP000007457} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M28 {ECO:0000313|EMBL:ADZ65277.1, RC ECO:0000313|Proteomes:UP000007457}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002459; ADZ65277.1; -; Genomic_DNA. DR RefSeq; WP_014489317.1; NC_017244.1. DR RefSeq; YP_005596286.1; NC_017244.1. DR EnsemblBacteria; ADZ65277; ADZ65277; BM28_A0201. DR KEGG; bmz:BM28_A0201; -. DR PATRIC; 47097899; VBIBruMel176544_0199. DR KO; K00548; -. DR BioCyc; BMEL941967:GL9M-202-MONOMER; -. DR Proteomes; UP000007457; Chromosome 1. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007457}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 263 263 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 326 326 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 327 327 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 783 783 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1261 AA; 138728 MW; 4368957A89144FA8 CRC64; MASSLDDLFG ATAAKPDGSE VLAALTQAAR ERILILDGAM GTQIQGLGFH EEHFRGDRFA TCDCQLQGNN DLLTLTQPKA IEEIHYAYAM AGADILETNT FSSTSIAQAD YGMEAMVYDL NRDGARLARR AALRAEQKDG RRRFVAGALG PTNRTASLSP DVNNPGFRAV TFDDLRIAYS EQIRGLIDGG SDIILIETIF DTLNAKAAVF ATEEVFAEKG VRLPVMISGT ITDLSGRTLS GQTPTAFWYS LRHARPFTIG LNCALGANAM RAHLDELSGI ADTFICAYPN AGLPNEFGQY DETPEAMAAQ IEGFARDGLV NVVGGCCGST PDHIRAIAQA VAKYEPRKPA KVPPLMRLSG LEPFTLTKDI PFVNIGERTN VTGSARFRKL VKAGDFAAAL DVARDQVANG AQIIDINMDE GLIDSEKAMV EFLNLIAAEP DIARVPIMLD SSKWEVIEAG LKCVQGKAVV NSISLKEGEE AFLHHARLVR AYGAAVVIMA FDETGQADTQ ARKIEICTRA YKILTEQVGF PPEDIIFDPN IFAVATGIEE HNNYGVDFIE ATREIVRTLP HVHISGGVSN LSFSFRGNEP VREAMHAVFL YHAIQAGMDM GIVNAGQLAV YDTIDAELRE ACEDVVLNRP TKTGESATER LLEIAERFRD SGSREARTQD LSWREWPVEK WLEHALVNGI TEYIEADTEE ARLAAERPLH VIEGPLMAGM NVVGDLFGSG KMFLPQVVKS ARVMKQAVAV LLPFMEEEKR LNGGEGRQSA GKVLMATVKG DVHDIGKNIV GVVLACNNYE IIDLGVMVPS QKILQVARDE KVDIIGLSGL ITPSLDEMAH VAAEMEREGF DIPLLIGGAT TSRVHTAVKI HSRYERGQAV YVVDASRAVG VVSNLLSPEG KQAYIDGLRN EYAKVAAAHA RNEAEKQRLP IARARANPHQ LDWENYEPVK PTFTGTKVFE TYDLAEIARY IDWTLFFQTW ELRGRYPAIL EDEKQGEAAR QLWADAQAML RKIIDEKWFT PRAVVGFWPA NAVGDDIRLF TDESRKEELA TLFTLRQQLT KRDGRPNVAM ADFVAPVESG KQDYVGGFVV TAGIGEIAIA ERFERANDDY SAILVKALAD RFAEAFAELM HERVRKEFWA YAPDEAFTPE ELISEPYKGI RPAPGYPAQP DHTEKTTLFR LLDATANTGV ELTESYAMWP GSSVSGLYIG HPESYYFGVA KVERDQVEDY ARRKDMDVEA VERWLTPILN YVPGASKDEA A // ID F2I2C0_PELSM Unreviewed; 296 AA. AC F2I2C0; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AEA81306.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:AEA81306.1}; GN OrderedLocusNames=SAR11G3_00831 {ECO:0000313|EMBL:AEA81306.1}; OS Pelagibacter sp. (strain IMCC9063). OC Bacteria; Proteobacteria; Alphaproteobacteria; SAR11 cluster; OC Candidatus Pelagibacter. OX NCBI_TaxID=1002672 {ECO:0000313|EMBL:AEA81306.1, ECO:0000313|Proteomes:UP000009181}; RN [1] {ECO:0000313|EMBL:AEA81306.1, ECO:0000313|Proteomes:UP000009181} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IMCC9063 {ECO:0000313|EMBL:AEA81306.1, RC ECO:0000313|Proteomes:UP000009181}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; AEA81306.1; -; Genomic_DNA. DR RefSeq; WP_013695471.1; NC_015380.1. DR RefSeq; YP_004358045.1; NC_015380.1. DR EnsemblBacteria; AEA81306; AEA81306; SAR11G3_00831. DR KEGG; pel:SAR11G3_00831; -. DR PATRIC; 54521231; VBICanPel201843_0821. DR OMA; DVITANS; -. DR BioCyc; CPEL1002672:GHAA-847-MONOMER; -. DR Proteomes; UP000009181; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009181}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:AEA81306.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000009181}; KW Transferase {ECO:0000313|EMBL:AEA81306.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 282 282 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 296 AA; 33035 MW; C491768E36DBFA4E CRC64; MDKNFFNTTR ILDGGMGQEL LNRGVKPEGT LWGATALLHK KYHKIIVDTH LDFIKAGAEV IVTNSFGSRK RRMIENGVLS KFKSANKTAG ILAKRAVQES KKKILIAGSL PPQHFTYFSD MGTDLNVIKE YFYEQAKILN PYVDFFYLDV MSSFKECEIA IKAIAPLKKD FLVGIHIREG EKLPSGEDFV SVVKKLSKLN PLGVVVACVS VEHLEPLIKK ILKIKIPFGF KINAFQHIPA GWKPDSNNPN VKLGKRKDLT PATFYSISKK IHKAGATILG GCCEITPKHI ARLKKI // ID F2I9R9_FLUTR Unreviewed; 335 AA. AC F2I9R9; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEA43065.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEA43065.1}; GN OrderedLocusNames=Fluta_1067 {ECO:0000313|EMBL:AEA43065.1}; OS Fluviicola taffensis (strain DSM 16823 / RW262 / RW262). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Cryomorphaceae; Fluviicola. OX NCBI_TaxID=755732 {ECO:0000313|EMBL:AEA43065.1, ECO:0000313|Proteomes:UP000007463}; RN [1] {ECO:0000313|Proteomes:UP000007463} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16823 / RW262 / RW262 {ECO:0000313|Proteomes:UP000007463}; 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; AEA43065.1; -; Genomic_DNA. DR RefSeq; WP_013685837.1; NC_015321.1. DR RefSeq; YP_004343903.1; NC_015321.1. DR EnsemblBacteria; AEA43065; AEA43065; Fluta_1067. DR KEGG; fte:Fluta_1067; -. DR PATRIC; 54416439; VBIFluTaf147081_1079. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR BioCyc; FTAF755732:GHMH-1087-MONOMER; -. DR Proteomes; UP000007463; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007463}; KW Methyltransferase {ECO:0000313|EMBL:AEA43065.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007463}; KW Transferase {ECO:0000313|EMBL:AEA43065.1}. SQ SEQUENCE 335 AA; 36797 MW; 7AC3165035E7EB9E CRC64; MKDIKQLLKE RILILDGAMG TMIQRYNLDE DDFRKGWFED HPHKLKGDND LLVLTRPDII KEIHAQYLEA GADIIETNTF GGTTVAQADY HLEHAVYDIN YHGAKIAREV CDEFTAKEPH KPRFVAGSMG PTTKLASMSP DVNDPGFRAI TFNELVVSFK EQATGLMDGG ADFLLVETIT DTLNSKAAMF AIDELSVERG IEIPIMISGT ITDQSGRTLT GQTTEAFLVS VSHMPLLSIG LNCALGADAM RPYLQILSNQ APFAISAHPN AGLPNEFGQY DETAEMMGEQ IEEFLQEGLI NIIGGCCGTT PEHIRKMAEI ASKYSPRKIS ETANA // ID F2J1F3_POLGS Unreviewed; 1242 AA. AC F2J1F3; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 01-APR-2015, entry version 27. DE SubName: Full=Probable 5-methyltetrahydrofolate--homocysteine methyltransferase (Methionine synthase, vitamin-B12 dependent isozyme) protein {ECO:0000313|EMBL:ADZ69735.1}; GN OrderedLocusNames=SL003B_1307 {ECO:0000313|EMBL:ADZ69735.1}; OS Polymorphum gilvum (strain LMG 25793 / CGMCC 1.9160 / SL003B-26A1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Polymorphum. OX NCBI_TaxID=991905 {ECO:0000313|EMBL:ADZ69735.1, ECO:0000313|Proteomes:UP000008130}; RN [1] {ECO:0000313|EMBL:ADZ69735.1, ECO:0000313|Proteomes:UP000008130} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 25793 / CGMCC 1.9160 / SL003B-26A1 RC {ECO:0000313|Proteomes:UP000008130}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002568; ADZ69735.1; -; Genomic_DNA. DR RefSeq; WP_013652052.1; NC_015259.1. DR RefSeq; YP_004303035.1; NC_015259.1. DR EnsemblBacteria; ADZ69735; ADZ69735; SL003B_1307. DR KEGG; pgv:SL003B_1307; -. DR PATRIC; 47180500; VBIPolGil182274_1343. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; PGIL991905:GJ0L-1327-MONOMER; -. DR Proteomes; UP000008130; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008130}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADZ69735.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008130}; KW Transferase {ECO:0000313|EMBL:ADZ69735.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 765 765 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1242 AA; 135983 MW; 99B47788A9A2B566 CRC64; MLKKSDVFDR LKAVADERIL ILDGAMGTEI QALRLDEAAF RGARFADWPQ DVRGNNDLLN LTRGEAIRDI HLAYYRAGAH IVATNTFSST TIAQADYGME ALAYELNLEG ARLACAARDR YRADHPDRPA FVAGALGPTN RTASISPDVN NPGYRAVSFD DLRQAYGEAA RGLIEGGADI LLVETIFDTL NAKAALFAID EVFEERGLRL PVMISGTITD LSGRTLSGQT PEAFWNSLRH AEPFTIGLNC ALGAKEMRAH IAELARVADT LVCAYPNAGL PNEFGDYDES PEHMAGLLGE FARAGLVNVV GGCCGTTPAH IRAIAEAVAP HRPRALPDVP RHMRLSGLEP FVVTPQTNFV NVGERTNVTG SARFRKLVKE GDYTAALDVA RSQVENGAQI IDVNMDEGLL DSEAAMVTFL NLVAAEPDIA RVPVMIDSSK WSVIEAGLKC IQGKGVVNSI SMKEGEAAFV AQARLVRRYG AAVVVMAFDE QGQADTFARK TEICARSYKL LTEQVGFPPE DIIFDPNIFA VATGIEEHDN YGVDFIEATG WIRETLPHAH VSGGVSNLSF SFRGNESVRE AMHSVFLYHA IARGMDMGIV NAGQLAIYDD LDPELRDLCE DVVLNRRKDA TDRLLEAAER WKGEGGRKKE ADLAWRGWPV ARRLEHALVN GITDFIEEDT EEARRSFERP LHVIEGPLMD GMNVVGDLFG SGKMFLPQVV KSARVMKKAV AYLMPFMEAE KRELGQEGQS SAGRILMATV KGDVHDIGKN IVGVVLQCNN FEVIDLGVMV PAARILETAR AEKVDIIGLS GLITPSLDEM CHVAAELERE GLDVPLLIGG ATTSRIHTAV RIHPNYARGQ AIYVTDAGRA VGVCSRLMSE GQRAPYFAEV REEYARIAEE HAAGRRAGQR VSLTEARANA FQADFSLAPV RPRRLGTTVF DSFPLEDLVP VIDWTPFFAT WEIKGRYPGV LTDNRYGPAA RALYDDARRM LDEIVEGKLL TARGVAGFWP AASRGDDIVL YADEGREAER AVLHTLRQQM ARAGGGRANV ALSDFIAPEG VGVADWIGGF AVTAGHGEDE LAARYARAGD DYSKILSQAL ADRLAEAFAE KLHQIVRTEL WGYTPDERLS AEELIEEKYQ GIRPAPGYPA QPDHTEKATL FDLLDAEAAT GIRLTESYAM WPGSSVSGLY FSHRDSHYFG VGRIERDQVE DYAARKGWDV GLAERWLAPI LNYDPHRMEA AE // ID F2JGX5_CELLD Unreviewed; 793 AA. AC F2JGX5; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADZ85315.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADZ85315.1}; GN OrderedLocusNames=Clole_3632 {ECO:0000313|EMBL:ADZ85315.1}; 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 {ECO:0000313|EMBL:ADZ85315.1, ECO:0000313|Proteomes:UP000008467}; RN [1] {ECO:0000313|EMBL:ADZ85315.1, ECO:0000313|Proteomes:UP000008467} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49066 / DSM 5427 / NCIMB 11756 / RHM5 RC {ECO:0000313|Proteomes:UP000008467}; 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 ----------------------------------------------------------------------- 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; ADZ85315.1; -; Genomic_DNA. DR RefSeq; WP_013658591.1; NC_015275.1. DR RefSeq; YP_004310513.1; NC_015275.1. DR EnsemblBacteria; ADZ85315; ADZ85315; Clole_3632. DR KEGG; cle:Clole_3632; -. DR KO; K00548; -. DR BioCyc; CCLO642492:GIWK-3776-MONOMER; -. DR Proteomes; UP000008467; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008467}; KW Methyltransferase {ECO:0000313|EMBL:ADZ85315.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008467}; KW Transferase {ECO:0000313|EMBL:ADZ85315.1}. SQ SEQUENCE 793 AA; 86918 MW; 2F31E6570FF4E271 CRC64; MVCNVLGKRR LYFDGAMGTA VQSRGLKLGE VPELFNITHP EIIEEIHRAY LEAGSNFVTT NTFGANRYKI EEKGYTVEQI ISKAVEIAKA AKEDFPDSYI ALDIGPSGKV LRPVGDVEFE EVYEIFKEQV IAGEKAGCDV ILCETFTDLY ELKAAVLAAK ENTSLPVFCT MSFEENGRTF FGTSIESMIL TLEGLGVSAL GVNCSLGPKQ LKEIVKRITK LSHIPVMVQP NAGLPVMQGE NVHYDITAEE FAEIMKEFAE DGVSILGGCC GTTPEYIEKT VDKTKDIPYE LLEREKVTGI CSSSEVVYFD DVVVIGERLN PTGKKMLQQA LRNHDMDYVL REAIKQQEQG AHILDVNMGL PDIDEVEMLK QAVVEVQSIV GLPLQIDSSN VDALEAAVRI YNGKPLINSV NGKKESLEAV LPIAKRYGAC ILGLTLDEKG IPETAEERLI VAKRIVDAAV REGIPKEDIF IDCLVVTASA QQSLVKETLK AVRLVKEELG VKTILGVSNV SFGLPQRPII NKTMLAMALI EGLDAPIMNP GDAGMMEAIS AYRVLMGKDQ DSKAYIDKYS GENSSIGAAM SNVIHNETIM SMNLAIKKGL KEEAKTVTLE LMKEKSPLEM IELDIIPALN EVGKLYETGV IFLPQLIKSA EAAKAAFEIL QVEMSKQNVE ARTTKTKVVL ATVYGDIHDI GKNIVKVIME NYNFEVIDLG KDVPSERVIE AVKKHEVRIV GLSALMTTTV NSMKDTITLL RKECEEVKVI VGGAVLTPEL AQYVGADYFA KDAMETVRIA SSL // ID F2JJA7_CELLD Unreviewed; 1222 AA. AC F2JJA7; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADZ84400.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADZ84400.1}; GN OrderedLocusNames=Clole_2700 {ECO:0000313|EMBL:ADZ84400.1}; 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 {ECO:0000313|EMBL:ADZ84400.1, ECO:0000313|Proteomes:UP000008467}; RN [1] {ECO:0000313|EMBL:ADZ84400.1, ECO:0000313|Proteomes:UP000008467} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49066 / DSM 5427 / NCIMB 11756 / RHM5 RC {ECO:0000313|Proteomes:UP000008467}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002582; ADZ84400.1; -; Genomic_DNA. DR RefSeq; WP_013657693.1; NC_015275.1. DR RefSeq; YP_004309598.1; NC_015275.1. DR EnsemblBacteria; ADZ84400; ADZ84400; Clole_2700. DR KEGG; cle:Clole_2700; -. DR KO; K00548; -. DR BioCyc; CCLO642492:GIWK-2813-MONOMER; -. DR Proteomes; UP000008467; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008467}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADZ84400.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008467}; KW Transferase {ECO:0000313|EMBL:ADZ84400.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 757 757 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1222 AA; 136329 MW; B29E1D093E0836D0 CRC64; MDKNELISIL KQRILVLDGA MGTSIQGYQL TEEDYRSERF KTFHRDQKGN NDLLSLTKPE VIKKIHRSFL KAGADMIETN TFNATVISQA DYDLGELIYE LNYESARIAR EVADEMTKKE PHKPRFVAGA IGPTNKTASL SPDVENPGFR NISFDELVSA YSEQIAGLIA GGVDCLLIET IFDTLNARAA IVAAQEVYEA QNMTLPIMIS GTLTDKSGRT LSGQKLEAFA QSVRNEHVIS IGLNCSFGGA DLMPFIKELS KTQNLYVSVY PNAGLPNVLG AYDEAPYMTA QYIEALAKGQ YVNIVGGCCG TTPEHIAAIA KCVEGVKPRT IPTLPKESIY CGLETVKSHK ANNFINIGER TNVAGSAKFA RLIRERNYEE ALLIAKEQVE NGAQIIDVNF DDGLLNSEEE MAYFLKLIAS EPDIASKPIM IDSSKWSVIE AGLKSIQGKP IVNSISLKNG EEEFLEHAKV VKAFGAAVVV MAFDERGQAD TFERKIEICE RAYRLLVDTL HFPPEDIIFD PNILAIATGM EEHNHYAAYY IEATRWIKEH LPYAKVSGGV SNLSFSFRGN NVIREAMHSV FLYHAIEAGM DMGIVNPGMI QIYDDIQKAL LELVEDVIFN KREDAAERLL EQAENYKQDQ DKVTIQQNEW RQWQLDDRLS YALVKGTTEF IEDDLAEAVT VYPKALHIIE GPLMAGMTKV GDLFGEGKMF LPQVVKSARV MKKAVGFLLP YMEKDKEEGA SHKAGKILIA TVKGDVHDIG KNIVGVVLAC NNFEIIDLGV MTPCETILDT AIKEKVDIIG LSGLITPSLD EMAHVAEEME RRGMTIPLII GGATTSKLHT ALKIAPHYSG PTVYGYDASK TVEICKKLLG KEKEVFVAEV KKEYEEKRQS YGSVPKKLVS LEEARSKKLK IDWEHRAISE PTFKGIKTID HYTIRDLRPY IDWTFFFIGW EMKKLYPAIL EDEVYGEAAR QLFEDANKML DVLASEKIID LRGVLGLFKA NSVEDDIELY HQDGTLAATF NCIRQQKLQN QDQYLCLSDF ISPKALGKED YIGGFIVTAG LGAEAYANEL KAKGDEYGAI MVKLLCDRLA EAFAEKLHQD VRQNDWGYAK DEQLGINDLL KGKYRGIRPA FGYPSLIDQS QMQKLFDLLE GEKITGVSLT ESFMMNPVAS VCGLYFASED AKYFDAMLLD RDQVQNYATR CQLSTAVIEK RLARYLAYGL EI // ID F2K2Q2_MARM1 Unreviewed; 1244 AA. AC F2K2Q2; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 01-APR-2015, entry version 27. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADZ91185.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADZ91185.1}; GN OrderedLocusNames=Marme_1936 {ECO:0000313|EMBL:ADZ91185.1}; OS Marinomonas mediterranea (strain ATCC 700492 / JCM 21426 / NBRC 103028 OS / MMB-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Marinomonas. OX NCBI_TaxID=717774 {ECO:0000313|EMBL:ADZ91185.1, ECO:0000313|Proteomes:UP000001062}; RN [1] {ECO:0000313|Proteomes:UP000001062} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1 RC {ECO:0000313|Proteomes:UP000001062}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002583; ADZ91185.1; -; Genomic_DNA. DR RefSeq; WP_013661090.1; NC_015276.1. DR RefSeq; YP_004313021.1; NC_015276.1. DR EnsemblBacteria; ADZ91185; ADZ91185; Marme_1936. DR KEGG; mme:Marme_1936; -. DR PATRIC; 47228678; VBIMarMed159599_1996. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; MMED717774:GCPW-1987-MONOMER; -. DR Proteomes; UP000001062; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001062}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADZ91185.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001062}; KW Transferase {ECO:0000313|EMBL:ADZ91185.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 765 765 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1244 AA; 138055 MW; 794D6FD761ABA57D CRC64; MVVKSRSYEA IENRLKENIL ILDGAMGTMI QDYKFEEADF RGERFADWKS ELKGNNDLLS LTQPQVIKAI HTAYLEAGAD IVETNTFNAN AISMLDYHME ELSYEINYES AKLARQAADE ITAKEPHKPR FVAGAIGPTS RTCTISPDVN DPGYRNVHFD ELVAAYDTAL DGLIKGGVDL ILIETIFDTL NAKAAIYAAL EYFEKTGVRY PIMISGTITD ASGRTLSGQT TEAFWNSIAH AKPISVGLNC ALGPKDLRQY IDELSRIADT QVSAHPNAGL PNAFGEYDES PEEMLEEIQG WVDSGFLNII GGCCGTTPEH IAVFAEAFKE SAPRTIPEIE KACRLSGLEP FNIDESSLFV NVGERTNVTG SARFKRLIKE GDYDAALEVA RQQVENGAQI IDINMDEGML DSQAAMERFL KLIASEPDIS RVPIMLDSSK WEILEAGLKW VQGKGVVNSI SLKEGEEKFV EQARKLMKYG AAVIVMAFDE VGQADTRERK IEICRRSYDV LVNKVGFSPE DIIFDPNIFA IATGIEEHNR YALDFIEATG DIKRELPYAK ISGGVSNVSF SFRGNNPVRE AIHAVFLYHA IKQGMTMGIV NAGQLAVYED IPPRLRDAVE DAVLNRTPDA TDTLLSIAGE FVGTGETVEA ETQEWRSFDV SERLSHALVK GITEFIDEDT EEARQQYDRP LEVIEGPLMA GMSIVGDLFG AGKMFLPQVV KSARVMKKAV AYLMPFIEEE KARNSDTASS SAGKVIMATV KGDVHDIGKN IVGVVLQCNN FEVIDLGVMV PAEKILRTAR EENADIIGLS GLITPSLDEM VHVAKEMERQ EFDLPVMIGG ATTSKAHTAV KIEQNYKRNQ VVHVTNASRS VSVASSLLTK DEERRKEFID TIKDDYEKTR KRFKDRASAG RRVSLNKARE NKTPVDFSSV VTPKKLGITV FKESDIDFNI VQNYIDWTPF FQTWELAGAY PRILTDKVVG EEATRLFADA KAMLAKVIEE GNLDAKAVVG LFPAAQVNHD DVVIYEDESR QTERMTLSFL RNQNELKTPG KYNQCLSDFV APKDSGVNDY MGAFACAAGF GIDPIVEAYE ADHDDYNSIM VKAVADRLAE ATAEYLHEKV RKELWGYAED ETLTNEELIK ERYKGIRPAP GYPACPDHTE KAKLWDLLNV KENADIDLTE SFAMWPTAAV SGWYFGNAES NYFGVGKIGP DQVESYAERK GMSKDDAERW LAPNLGYDPE DDRV // ID F2K3Z7_MARM1 Unreviewed; 303 AA. AC F2K3Z7; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 29-APR-2015, entry version 19. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ADZ91339.1}; GN OrderedLocusNames=Marme_2091 {ECO:0000313|EMBL:ADZ91339.1}; OS Marinomonas mediterranea (strain ATCC 700492 / JCM 21426 / NBRC 103028 OS / MMB-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Marinomonas. OX NCBI_TaxID=717774 {ECO:0000313|EMBL:ADZ91339.1, ECO:0000313|Proteomes:UP000001062}; RN [1] {ECO:0000313|Proteomes:UP000001062} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1 RC {ECO:0000313|Proteomes:UP000001062}; 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 ----------------------------------------------------------------------- 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; ADZ91339.1; -; Genomic_DNA. DR RefSeq; WP_013661244.1; NC_015276.1. DR RefSeq; YP_004313175.1; NC_015276.1. DR EnsemblBacteria; ADZ91339; ADZ91339; Marme_2091. DR KEGG; mme:Marme_2091; -. DR PATRIC; 47228998; VBIMarMed159599_2153. DR OMA; DVITANS; -. DR BioCyc; MMED717774:GCPW-2144-MONOMER; -. DR Proteomes; UP000001062; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001062}; KW Methyltransferase {ECO:0000313|EMBL:ADZ91339.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001062}; KW Transferase {ECO:0000313|EMBL:ADZ91339.1}. SQ SEQUENCE 303 AA; 33091 MW; D7AE0D90349D0485 CRC64; MNAPSVTILD GGMGRELNRR NAPFQQPEWS ALAMMQAPEI VKEVHHDFIE SGARVIATNS YSLVPFHIGE EVFAEQGYSL AELSGEVARQ AAAESKHNVL VAGSLPPLFG SYRADLFRAD RVEEVATPLI QALNNNVDVW LNETQCLVEE VKAVKSLVDK HDSESKPFWV SFTLEDSEPT IEPQLRSGEL VREAIKAMVD IKVAAILFNC SQPEIIGEAI KITRDILAEL GCDTIEIGAY ANAFPPQPKE ATANDGLDEL REDLSPPAYL DWVKHWVADG ATLVGGCCGI GPEHIEAMSN ELA // ID F2K746_PSEBN Unreviewed; 299 AA. AC F2K746; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Putative homocysteine S-methyltransferase {ECO:0000313|EMBL:AEA72123.1}; GN ORFNames=PSEBR_a5588 {ECO:0000313|EMBL:AEA72123.1}; OS Pseudomonas brassicacearum (strain NFM421). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=994484 {ECO:0000313|EMBL:AEA72123.1, ECO:0000313|Proteomes:UP000006692}; RN [1] {ECO:0000313|EMBL:AEA72123.1, ECO:0000313|Proteomes:UP000006692} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NFM421 {ECO:0000313|EMBL:AEA72123.1, RC ECO:0000313|Proteomes:UP000006692}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; AEA72123.1; -; Genomic_DNA. DR RefSeq; WP_003206973.1; NC_015379.1. DR RefSeq; YP_004357127.1; NC_015379.1. DR EnsemblBacteria; AEA72123; AEA72123; PSEBR_a5588. DR KEGG; pba:PSEBR_a5588; -. DR PATRIC; 54519362; VBIPseBra188168_5962. DR OMA; PYVDVWL; -. DR BioCyc; PBRA994484:GJWC-6089-MONOMER; -. DR Proteomes; UP000006692; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006692}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:AEA72123.1}; KW Transferase {ECO:0000313|EMBL:AEA72123.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 207 207 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 299 AA; 31440 MW; 3F15C82B802F7B34 CRC64; MGSATTVILD GGMGRELQRR GAPFRQPEWS ALALSEAPQA VEAVHAAYIA SGANVITSNS YAVVPFHIGE ARFAEEGQAL AALAGELAQR AVRASGKAVQ VAGSLPPLFG SYRPDLFDAS RASELLAPLV NGLAPHVDLW LAETQSSTVE ARAIHAGLPK DGKPFWLSFT LKDEDTDEVP RLRSGEPVAD AAAVAAELGV EVLLFNCSQP EVIGAAIDAA RDTFARLGVK IHIGAYANAF PPQPKEATAN DGLDPLREDL DPPGYLQWAA DWQKRGASHL GGCCGIGPEH IAVLAQKLV // ID F2KE23_PSEBN Unreviewed; 151 AA. AC F2KE23; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 01-APR-2015, entry version 20. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AEA67500.1}; GN ORFNames=PSEBR_a1312 {ECO:0000313|EMBL:AEA67500.1}; OS Pseudomonas brassicacearum (strain NFM421). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=994484 {ECO:0000313|EMBL:AEA67500.1, ECO:0000313|Proteomes:UP000006692}; RN [1] {ECO:0000313|EMBL:AEA67500.1, ECO:0000313|Proteomes:UP000006692} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NFM421 {ECO:0000313|EMBL:AEA67500.1, RC ECO:0000313|Proteomes:UP000006692}; 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 ----------------------------------------------------------------------- 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; AEA67500.1; -; Genomic_DNA. DR RefSeq; WP_013692474.1; NC_015379.1. DR RefSeq; YP_004352504.1; NC_015379.1. DR EnsemblBacteria; AEA67500; AEA67500; PSEBR_a1312. DR KEGG; pba:PSEBR_a1312; -. DR BioCyc; PBRA994484:GJWC-1407-MONOMER; -. DR Proteomes; UP000006692; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006692}. SQ SEQUENCE 151 AA; 16903 MW; 2F12578DF24F7501 CRC64; MNLIPKIRTF KYGDFHLDLS AELKAVQADV VAKAIETNSA VELPPPPPAR TLEQAANSPL ASLIYSFNEV EAALNDVAKK HQIDTKSEFE THRHIMRALL EKGLVDDLTF STYARLAELR KAVNMSQEVT YTDAVNMSVM CKWLIEKLST I // ID F2KEU3_PSEBN Unreviewed; 1236 AA. AC F2KEU3; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Methionine synthase (5-methyltetrahydrofolate--homocysteine methyltransferase) {ECO:0000313|EMBL:AEA68169.1}; GN ORFNames=PSEBR_a1946 {ECO:0000313|EMBL:AEA68169.1}; OS Pseudomonas brassicacearum (strain NFM421). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=994484 {ECO:0000313|EMBL:AEA68169.1, ECO:0000313|Proteomes:UP000006692}; RN [1] {ECO:0000313|EMBL:AEA68169.1, ECO:0000313|Proteomes:UP000006692} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NFM421 {ECO:0000313|EMBL:AEA68169.1, RC ECO:0000313|Proteomes:UP000006692}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002585; AEA68169.1; -; Genomic_DNA. DR RefSeq; WP_003200194.1; NC_015379.1. DR RefSeq; YP_004353173.1; NC_015379.1. DR EnsemblBacteria; AEA68169; AEA68169; PSEBR_a1946. DR KEGG; pba:PSEBR_a1946; -. DR PATRIC; 54511434; VBIPseBra188168_2075. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; PBRA994484:GJWC-2081-MONOMER; -. DR Proteomes; UP000006692; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006692}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEA68169.1}; KW Transferase {ECO:0000313|EMBL:AEA68169.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1236 AA; 135373 MW; F4BF7D45D39536B2 CRC64; MSDRSARLYL LQQALKERIL ILDGGMGTMI QSYKLEEQDY RGKRFADWPS DVKGNNDLLV LSRPDVIGAI EKAYLDAGAD ILETNTFNAT QVSQADYGMQ GLAYELNLEG ARLARKVADA KTLETPDKPR FVAGVLGPTS RTCSLSPDVN NPGYRNVTFD ELVENYTEAT KGLIEGGADL ILIETIFDTL NAKAAIFAVQ GVYEELGVEL PIMISGTITD ASGRTLSGQT TEAFWNSVAH AKPISVGLNC ALGASELRPY LEELSNKAST HVSAHPNAGL PNEFGEYDEL PAETAKVIEE FAQSGFLNIV GGCCGTTPAH IESIAKAVAG YAPRPIPEIP RACRLSGLEP FTIDRSSLFV NVGERTNITG SAKFARLIRE DNYTEALEVA LQQVEAGAQV IDINMDEGML DSKKAMVTFL NLIAGEPDIS RVPIMIDSSK WEVIEAGLKC IQGKGIVNSI SMKEGVEQFI HHAKLCKRYG AAVVVMAFDE AGQADTEARK KEICKRSYDI LVNEVGFPPE DIIFDPNIFA VATGIEEHNN YAVDFINACA YIRDELPYAL TSGGVSNVSF SFRGNNPVRE AIHSVFLLYA IRAGLTMGIV NAGQLEIYDQ IPAELRDAVE DVILNRTPEG TDALLAIADK YKGDGSVKEA ETEEWRGWEV NKRLEHALVK GITTHIVEDT EESRLSFARP IEVIEGPLMA GMNIVGDLFG AGKMFLPQVV KSARVMKQAV AHLIPFIEAE KGDKPEAKGK ILMATVKGDV HDIGKNIVGV VLGCNGYDIV DLGVMVPAEK ILQVAKEQKC DIIGLSGLIT PSLDEMVHVA REMQRQGFHL PLMIGGATTS KAHTAVKIEP KYSNDAVIYV TDASRAVGVA TQLLSKELKP AFVEKTRLDY IDVRERTSNR SARTERLSYP AAVAKKPQFD WSSYQPVKPT FTGAKVLDNI DLNVLAEYID WTPFFISWDL AGKYPRILTD EVVGEAATAL YADARAMLRK LIDEKLISAR AVFGFWPANQ VHDDDLEVYG DDGKPLARLH HLRQQIIKTD GKPNFSLADF VAPKDSGVTD YVGGFITTAG IGAEEVAKAY QEAGDDYNSI MVKALADRLA EACAEWLHQQ VRKDYWGYAQ DESLDNDALI KEQYTGIRPA PGYPACPDHT EKATLFRLLD PEASELKAGR SGVFLTEHYA MFPAAAVSGW YFAHPQAQYF AVGKIDKDQV QSYTARKGQD LSVTERWLSP NLGYDN // ID F2LE94_BURGS Unreviewed; 365 AA. AC F2LE94; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=Methionine synthase I, methyltransferase domain protein {ECO:0000313|EMBL:AEA62211.1}; GN OrderedLocusNames=bgla_1g36080 {ECO:0000313|EMBL:AEA62211.1}; OS Burkholderia gladioli (strain BSR3). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=999541 {ECO:0000313|EMBL:AEA62211.1, ECO:0000313|Proteomes:UP000008316}; RN [1] {ECO:0000313|EMBL:AEA62211.1, ECO:0000313|Proteomes:UP000008316} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BSR3 {ECO:0000313|EMBL:AEA62211.1, RC ECO:0000313|Proteomes:UP000008316}; 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; AEA62211.1; -; Genomic_DNA. DR RefSeq; WP_013699527.1; NC_015381.1. DR RefSeq; YP_004362167.1; NC_015381.1. DR EnsemblBacteria; AEA62211; AEA62211; bgla_1g36080. DR KEGG; bgd:bgla_1g36080; -. DR PATRIC; 54505592; VBIBurGla188977_7236. DR KO; K00548; -. DR OMA; VLTCTFN; -. DR BioCyc; BGLA999541:GHSQ-3683-MONOMER; -. DR Proteomes; UP000008316; Chromosome 1. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008316}; KW Methyltransferase {ECO:0000313|EMBL:AEA62211.1}; KW Transferase {ECO:0000313|EMBL:AEA62211.1}. SQ SEQUENCE 365 AA; 39356 MW; 14F7046AA22FBDE7 CRC64; MAFSPIRRPS AMPTSLPARS APAASYTRGA DLPALLARRI LILDGAMGTM IQQYKFDEAA YRGERFADFG RDIKGNNELL SITQPATIRE IHDQYFAAGA DIVETNTFGA TTIAQADYEM EHLVVEMNVA SARLARESAL KYSTPDKPRF VAGAIGPTPK TASISPDVND PGARNVTYDE LRDAYYQQAK ALLDGGVDLF LVETIFDTLN AKAALFALDQ LFEDTGENLP IMISGTVTDA SGRILSGQTV EAFWNSLRHA RPLTFGLNCA LGAALMRPYI AELAKLCDTY VSCYPNAGLP NPMAETGFDE TPDVTSSLLK EFAQAGLVNL AGGCCGTTPA HIAEIARALA EVKPRRWPSQ YSEAA // ID F2LK08_BURGS Unreviewed; 353 AA. AC F2LK08; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AEA62633.1}; GN OrderedLocusNames=bgla_2g01550 {ECO:0000313|EMBL:AEA62633.1}; OS Burkholderia gladioli (strain BSR3). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=999541 {ECO:0000313|EMBL:AEA62633.1, ECO:0000313|Proteomes:UP000008316}; RN [1] {ECO:0000313|EMBL:AEA62633.1, ECO:0000313|Proteomes:UP000008316} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BSR3 {ECO:0000313|EMBL:AEA62633.1, RC ECO:0000313|Proteomes:UP000008316}; 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; AEA62633.1; -; Genomic_DNA. DR RefSeq; WP_013688965.1; NC_015376.1. DR RefSeq; YP_004348145.1; NC_015376.1. DR EnsemblBacteria; AEA62633; AEA62633; bgla_2g01550. DR KEGG; bgd:bgla_2g01550; -. DR PATRIC; 54491176; VBIBurGla188977_0178. DR KO; K00548; -. DR OMA; VERPEYP; -. DR BioCyc; BGLA999541:GHSQ-4120-MONOMER; -. DR Proteomes; UP000008316; Chromosome 2. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008316}; KW Methyltransferase {ECO:0000313|EMBL:AEA62633.1}; KW Transferase {ECO:0000313|EMBL:AEA62633.1}. SQ SEQUENCE 353 AA; 38047 MW; B0D53AD48DD95FD0 CRC64; MARHPAIDID YTRGAGLARL LQTRIAILDG AMGTMIQRER LGEAEFRGER FRDYPRDLKG NNELLSLTRP QLIREIHDAY FAAGADIAET NTFGATSIAQ ADYGLEALVR EMNLESARLA RASADRHATP GQPRYVAGAM GPTPRTASIS PDVNDPGARN VSFDELREAY HQQAAALLEG GVDLFLVETV FDTLNAKAAL FALDELFEQT GERLPIMISG TVTDASGRVL SGQTVEAFWN SLRHARPLTF GLNCAMGAAL MRPYLAELAK HCETYISCYP NAGLPNPMSE TGFDETPDVT SSLLGEFAEA GLLNIAGGCC GTTPEHIAAI ARVMRSKAPR ALPGRPVAVE PEA // ID F2LVY3_HIPMA Unreviewed; 806 AA. AC F2LVY3; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 01-APR-2015, entry version 21. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEA33917.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEA33917.1}; GN OrderedLocusNames=Hipma_0948 {ECO:0000313|EMBL:AEA33917.1}; OS Hippea maritima (strain ATCC 700847 / DSM 10411 / MH2). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfurellales; OC Desulfurellaceae; Hippea. OX NCBI_TaxID=760142 {ECO:0000313|EMBL:AEA33917.1, ECO:0000313|Proteomes:UP000008139}; RN [1] {ECO:0000313|Proteomes:UP000008139} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700847 / DSM 10411 / MH2 RC {ECO:0000313|Proteomes:UP000008139}; 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 ----------------------------------------------------------------------- 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; AEA33917.1; -; Genomic_DNA. DR RefSeq; WP_013681958.1; NC_015318.1. DR RefSeq; YP_004339976.1; NC_015318.1. DR EnsemblBacteria; AEA33917; AEA33917; Hipma_0948. DR KEGG; hmr:Hipma_0948; -. DR PATRIC; 54412603; VBIHipMar155866_0964. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR BioCyc; HMAR760142:GHVE-980-MONOMER; -. DR Proteomes; UP000008139; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008139}; KW Methyltransferase {ECO:0000313|EMBL:AEA33917.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008139}; KW Transferase {ECO:0000313|EMBL:AEA33917.1}. SQ SEQUENCE 806 AA; 88553 MW; 0DBC9A5840E32A31 CRC64; MRNFREELGR KILILDGAMG TQLQEKGILK TGSCPDYLNV THPKEIGEIH KTYLDAGADI IVTNTFGANP IKLEEFNLQD KVYQINYEAV RIAKEVVKDK GFVSLSIGPT GKFIEPVGEE NFDYIKDIFK KQVRPAVDAD VDLFSLETFM DIKELKAAII AIREITDKPI IAMMTFAEDG RTILGTSPEV FAKTIEPMEV DVIGANCSVG PDLLNEFVKK MAQVTDKPLI IQPNAGIPRL VNGKTIFPVG AEEFASYAND FKEYAAIVAG CCGTGPEHIK LLAEKLKGKP VKKRTIQKAT VLTSRSQMVE IGYSRPVVFI GERLNPTGKK HLKEQLKEGK TGLYRKEAIE QVEHGAMVLD INVGVPMIDE PTTMKKCVLA VESVVSVPLV IDSSNIEALE AGLKAADGKV LINSVNGSQE SMEAILPLAK KYGAAILALL LDETGIPETA EDRLKILDKI VKNAKELGIK EEDIVADALA LTIGSDKKRA LETLRAIKLI KEKYGITTIL GLSNVSFGLP NRKLINSSFM AMAIYNGLDS AIVNPYDELL WQIKYASDLI VDRDKDSSIY INNSSDITLK NKTTDNAKLE LIKSPFDKGT LEDKLFMCVI EGNEEEIELL TKQALKNKEP LKISNEILIP ALDAVGKLYD KGIYFLPQMI KSANAMKKAF NILKEIIKKK ATKQKTGKTI VMATVKGDIH DIGKNIVSLL LETNGFEVVD LGKNVDDETI LKAIEEYHAD AVGLSALMTT TMINMKNVID EIKMKGLNVK IMVGGAAVTE EFAKKIGADM YAKDAIEAVR LAKENV // ID F2LZF4_LACAL Unreviewed; 331 AA. AC F2LZF4; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:AEA31957.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:AEA31957.1}; GN Name=mmuM {ECO:0000313|EMBL:AEA31957.1}; GN OrderedLocusNames=LAB52_05015 {ECO:0000313|EMBL:AEA31957.1}; OS Lactobacillus amylovorus (strain GRL 1118). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=695562 {ECO:0000313|EMBL:AEA31957.1, ECO:0000313|Proteomes:UP000008140}; RN [1] {ECO:0000313|EMBL:AEA31957.1, ECO:0000313|Proteomes:UP000008140} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GRL 1118 {ECO:0000313|Proteomes:UP000008140}; RX PubMed=21478337; DOI=10.1128/JB.00423-11; RA Kant R., Paulin L., Alatalo E., de Vos W.M., Palva A.; RT "Genome sequence of Lactobacillus amylovorus GRL1118, isolated from RT pig ileum."; RL J. Bacteriol. 193:3147-3148(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GRL 1118; RA Kant R., Paulin L., Alatalo E., de Vos W.M., Palva A.; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002609; AEA31957.1; -; Genomic_DNA. DR RefSeq; WP_014565801.1; NC_017470.1. DR RefSeq; YP_005853962.1; NC_017470.1. DR EnsemblBacteria; AEA31957; AEA31957; LAB52_05015. DR KEGG; lay:LAB52_05015; -. DR PATRIC; 54150335; VBILacAmy156066_0996. DR KO; K00547; -. DR BioCyc; LAMY695562:GLF1-1024-MONOMER; -. DR Proteomes; UP000008140; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008140}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:AEA31957.1}; KW Transferase {ECO:0000313|EMBL:AEA31957.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 223 223 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 331 AA; 37421 MW; F5FE3A00B8AFEE69 CRC64; MDLIKQISSK GLVLDGAMST ALEKQGIDTN TDLWTAVALD KDLDKVYKVH MNYFQAGAQM AITDTYQANV QAFEKHGYSE DKAKEMIADA VKIAKKARDD FEKKTGIHNY VAASVGSYGA YLAEGDEFRG DYDLTKKQYL DFHLPRLQVL LQNKPDCLAI ETQPKLDEVV VLLDWLKENA PEMPVYVSFT LHDTTKISDG TPLKKVMEKI NEYDQVFAVG ANCFKPFLAT TAIDKMREFT KKNIIVYPNL GGIYNEFERN WIPFNAKFDF GKLSKEWYEH GACIIGGCCS TGVKEISQIA AFYKILNNQK SKQKLDLKPN INLMKSTRSK V // ID F2LZH7_LACAL Unreviewed; 306 AA. AC F2LZH7; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 01-APR-2015, entry version 22. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:AEA31980.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:AEA31980.1}; GN Name=mmuM {ECO:0000313|EMBL:AEA31980.1}; GN OrderedLocusNames=LAB52_05130 {ECO:0000313|EMBL:AEA31980.1}; OS Lactobacillus amylovorus (strain GRL 1118). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=695562 {ECO:0000313|EMBL:AEA31980.1, ECO:0000313|Proteomes:UP000008140}; RN [1] {ECO:0000313|EMBL:AEA31980.1, ECO:0000313|Proteomes:UP000008140} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GRL 1118 {ECO:0000313|Proteomes:UP000008140}; RX PubMed=21478337; DOI=10.1128/JB.00423-11; RA Kant R., Paulin L., Alatalo E., de Vos W.M., Palva A.; RT "Genome sequence of Lactobacillus amylovorus GRL1118, isolated from RT pig ileum."; RL J. Bacteriol. 193:3147-3148(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GRL 1118; RA Kant R., Paulin L., Alatalo E., de Vos W.M., Palva A.; 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; CP002609; AEA31980.1; -; Genomic_DNA. DR RefSeq; WP_014565819.1; NC_017470.1. DR RefSeq; YP_005853985.1; NC_017470.1. DR EnsemblBacteria; AEA31980; AEA31980; LAB52_05130. DR KEGG; lay:LAB52_05130; -. DR PATRIC; 54150379; VBILacAmy156066_1018. DR KO; K00547; -. DR BioCyc; LAMY695562:GLF1-1047-MONOMER; -. DR Proteomes; UP000008140; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008140}; KW Methyltransferase {ECO:0000313|EMBL:AEA31980.1}; KW Transferase {ECO:0000313|EMBL:AEA31980.1}. SQ SEQUENCE 306 AA; 34799 MW; 7094FC0F2C75996B CRC64; MSLIEDAKSG IVLDGAMSDE LEKQGVETDN KLWTATALVD QLNKVYNAHQ DYFRAGAELV ITDTYQANVQ AFEESGYSKK EAEKFIRDAV KVAKKARDDY QKETGKYNYV AGTIGSYGAY LADGNEYRGD YNLSEKEYLD FHLPRLKLVL KERPDLIALE TQPKITEPVA VLNWLETNYP DMPIYVSFTL KDSKHVSDGT SIEHATQEIS KYKQVFAIGI NCVSPKLVDQ ALKEFAKYTS KPLVVYPNLG ATYDPKIKKW RSFKEKFDFA ELTQKWYEDG AHLIGGCRTT GPKEIKEIRQ SIDKLR // ID F2N3R9_PSEU6 Unreviewed; 1230 AA. AC F2N3R9; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 29-APR-2015, entry version 29. DE SubName: Full=MetH protein {ECO:0000313|EMBL:AEA84138.1}; GN Name=metH {ECO:0000313|EMBL:AEA84138.1}; GN OrderedLocusNames=PSTAA_2250 {ECO:0000313|EMBL:AEA84138.1}; OS Pseudomonas stutzeri (strain DSM 4166 / CMT.9.A). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=996285 {ECO:0000313|EMBL:AEA84138.1, ECO:0000313|Proteomes:UP000000481}; RN [1] {ECO:0000313|EMBL:AEA84138.1, ECO:0000313|Proteomes:UP000000481} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 4166 / CMT.9.A {ECO:0000313|Proteomes:UP000000481}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002622; AEA84138.1; -; Genomic_DNA. DR RefSeq; WP_014596771.1; NC_017532.1. DR RefSeq; YP_005938880.1; NC_017532.1. DR EnsemblBacteria; AEA84138; AEA84138; PSTAA_2250. DR KEGG; psr:PSTAA_2250; -. DR PATRIC; 54286253; VBIPseStu183391_2256. DR KO; K00548; -. DR BioCyc; PSTU996285:GLIZ-2252-MONOMER; -. DR Proteomes; UP000000481; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000481}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1230 AA; 134867 MW; 57C779CD83419E22 CRC64; MSARNARLQA LQHALSQRIL ILDGGMGTMI QSYKLEESDY RGERFADWPS DVKGNNDLLL LSRPNVIQAI EKAYLDAGAD ILETNTFNAT RVSQADYGME ELVYELNVEG ARLAREVADA KTAETPDRPR FVAGVLGPTS RTCSISPDVN NPGYRNVTFD LLVENYTEAT RGLIEGGADL ILIETIFDTL NAKAAIFAVQ QVFEEDGVEL PIMISGTITD ASGRTLSGQT TEAFWNSVRH AKPISVGLNC ALGAKDLRPY LEELANKADT HVSAHPNAGL PNAFGEYDET PAEMAAVVEE FAASGFLNII GGCCGTTPAH IQAIAEAVAK YPPRVIPDIP KACRLSGLEP FTIDRSSLFV NVGERTNITG SAKFARLIRE ENYTEALEVA LQQVEAGAQV IDINMDEGML DSKAAMVTFL NLIAGEPDIS RVPIMIDSSK WEVIEAGLKC IQGKGIVNSI SMKEGVEQFK HHAHLCKRYG AAVVVMAFDE AGQADTAARK REICQRSYDI LVNEVGFPPE DIIFDPNIFA IATGIEEHNN YAVDFIEACA FIRDNLPYAL TSGGVSNVSF SFRGNNPVRE AIHSVFLFHA IKAGLTMGIV NAGQLEIYDE IPKELRDAVE DVVLNRSAGG TEALLEIADK YKGDGSVKEA ETEEWRNLPV DKRLEHALVK GITAFIVEDT EECRQQCARP IEVIEGPLMS GMNVVGDLFG AGKMFLPQVV KSARVMKQAV AHLIPFIEAE KGDKPEAKGK ILMATVKGDV HDIGKNIVGV VLGCNGYDVV DMGVMVPAEK ILQTAIAEKC DIIGLSGLIT PSLDEMVHVA KEMQRQGFSL PLMIGGATTS KAHTAVKIDP QYSNDAVVYV TDASRAVGVA TTLLSKELKP AFVDKTREEY AMIRERTANR SARTERLSYL DAIANKPPFD WSGYAPVKPS FTGRQVLEDI DLRTLVDYID WTPFFIAWDL AGKYPRILED EVVGEAATSL FNDAQAMLKK LVDEKLIRAR AVFGFWPANQ VQDDDLEVYG DNGEKLATLH HLRQQTIKPD AKPNLSLADF VAPKSTGITD YVGGFICTAG IGAEELAKVY QDKGDDYNSI MVKALADRLA EACAEWLHEQ VRKHYWGYAP DERLSNEELI REQYKGIRPA PGYPACPDHT EKGTLFQLLD ADGISQVTLT EHYAMLPTAA VSGWYFAHPE AQYFAVGKID KDQVESYSQR KGHELAISER WLMPNLGYDN // ID F2NAD6_CORGP Unreviewed; 309 AA. AC F2NAD6; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 01-APR-2015, entry version 23. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AEB06322.1}; GN OrderedLocusNames=Corgl_0195 {ECO:0000313|EMBL:AEB06322.1}; 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 {ECO:0000313|EMBL:AEB06322.1, ECO:0000313|Proteomes:UP000006851}; RN [1] {ECO:0000313|Proteomes:UP000006851} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 49209 / DSM 20642 / JCM 10262 / PW2 RC {ECO:0000313|Proteomes:UP000006851}; 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; AEB06322.1; -; Genomic_DNA. DR RefSeq; WP_013708065.1; NC_015389.1. DR RefSeq; YP_004372137.1; NC_015389.1. DR EnsemblBacteria; AEB06322; AEB06322; Corgl_0195. DR KEGG; cgo:Corgl_0195; -. DR PATRIC; 54443828; VBICorGlo157054_0205. DR KO; K00548; -. DR OMA; VLTCTFN; -. DR BioCyc; CGLO700015:GH6A-200-MONOMER; -. DR Proteomes; UP000006851; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006851}; KW Methyltransferase {ECO:0000313|EMBL:AEB06322.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006851}; KW Transferase {ECO:0000313|EMBL:AEB06322.1}. SQ SEQUENCE 309 AA; 32464 MW; 0B4BB5BFD209825C CRC64; MPSTEIQADF ETAYYNRSGA EELMSRLVDE VLLAQGPMGS VLMSEEGASD VPAAYWNEVE PQEVSRIHEL YAASGAQLLI TNTFQASTPA LGRAGISSSA QQVNRAAVDC ARVACPQHLA GSIGPCGVDW LTVRSAEFRR ARDAYREQAH ALLACGVDAL MLETFTSVRD LEPALLGAGD VADGMPLLVS FAIDGSADLV GDGLSIEGAI LFAEKHGASA VGVNSCSIDA ANAAVRRMAR AARTPIMVRP GGDVPVRDDD KGLIWAEDPE AFERACRGWI EGGAHLIGGC CGTTARTTAS LAEALDRGR // ID F2NW07_TRES6 Unreviewed; 857 AA. AC F2NW07; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 29-APR-2015, entry version 26. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEB14734.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEB14734.1}; GN OrderedLocusNames=Tresu_1844 {ECO:0000313|EMBL:AEB14734.1}; OS Treponema succinifaciens (strain ATCC 33096 / DSM 2489 / 6091). OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema. OX NCBI_TaxID=869209 {ECO:0000313|EMBL:AEB14734.1, ECO:0000313|Proteomes:UP000006852}; RN [1] {ECO:0000313|Proteomes:UP000006852} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33096 / DSM 2489 / 6091 RC {ECO:0000313|Proteomes:UP000006852}; 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 ----------------------------------------------------------------------- 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; AEB14734.1; -; Genomic_DNA. DR RefSeq; WP_013702015.1; NC_015385.1. DR RefSeq; YP_004366031.1; NC_015385.1. DR EnsemblBacteria; AEB14734; AEB14734; Tresu_1844. DR KEGG; tsu:Tresu_1844; -. DR PATRIC; 54430429; VBITreSuc166698_1932. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR BioCyc; TSUC869209:GHSS-1886-MONOMER; -. DR Proteomes; UP000006852; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006852}; KW Methyltransferase {ECO:0000313|EMBL:AEB14734.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006852}; KW Transferase {ECO:0000313|EMBL:AEB14734.1}. SQ SEQUENCE 857 AA; 93519 MW; 088FFD93B0A7B031 CRC64; MSEFKNFLFN KIQKHEPVFF DGGMGTMIQK ISGLSYSIPE DLNFYNPEAI KDIHKKYILA GSNICTTNTF GANPIKLENA SHSAQEFIEK GIALVKGAIA ECKKQNENII CFTAWDSGQI GKLLEPNGPL TFDEAYNSYK AAAIAAEKSG ADLAIIETMS DLYEVKAAVL AIKENTNLPV IATMTFQPNC RTLTGADVLT CVTYLESLHV DVLGFNCGGS LEEDIELANQ FCKYSHIPIL SQPNAGLPEV INGKDVFKVT PEEFTNAQEK ILESGVSIFG GCCGTTPDHI KTMAEKLSEK KLKAKKEKFQ SFICSYNKTV QAGGAAGPVI IGERINPTGK KKCKEALQNN DMQFIIDEAD SQINSGAHIL DVNVGLPGIN EKEMMLQAVK SVQKIFNTPL QLDSSESDVL EYALRYYNGK ALVNSVNGKQ EVMDKVFPLI KHYGGAVVAL CIDEDGISQT AEGRVKVAEK IIQEAAKYGI PIRDIFIDTL TLTVSSEQKT SLETVKAIRI LKEKFGKEGI QFVLGVSNIS FGLPRRDIIN SRFFMLALEA GLSAAIINPA SIPMMDTYRA YRALGCFDEN CLDYIQTYTG TLDPTTEKAR QKILSDAVND GTISIQINGT PIASPKKETE KKNTLTETIG AEKNTEEKEL IQIIEKGFKD KAADATARLL EKNAPVKIID NCIVPALDNV GKDFETGKKF LPQLLLSAET VGNSFLKIKE TLAASGKEQE EKGTIAIATV FGDIHDIGKN IVKAMLENYG YKVIDLGKNV PAETVVKTVI ENKIQLVGLS ALMTTTVANM EETINQLHKA LKENNLECKI VVGGAVLTPD YAKKIGADFY AKDAMETVSA AKEVFGK // ID F2PAG2_PHOMO Unreviewed; 1223 AA. AC F2PAG2; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:GAA04898.1}; GN Name=metH {ECO:0000313|EMBL:GAA04898.1}; GN ORFNames=PMSV_3393 {ECO:0000313|EMBL:GAA04898.1}; OS Photobacterium leiognathi subsp. mandapamensis svers.1.1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Photobacterium. OX NCBI_TaxID=1001530 {ECO:0000313|EMBL:GAA04898.1}; RN [1] {ECO:0000313|EMBL:GAA04898.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Svers.1.1. {ECO:0000313|EMBL:GAA04898.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; DF093597; GAA04898.1; -; Genomic_DNA. DR RefSeq; WP_008987818.1; NZ_DF093597.1. DR EnsemblBacteria; GAA04898; GAA04898; PMSV_3393. DR GeneID; 23786372; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1223 AA; 135806 MW; 3F53EEEFD2549F23 CRC64; MLNSKELLHK RLEQQILIID GGMGTMIQGY KLEEEDYRGQ RFADWHSDLK GNNDLLVLTQ PQLIKDIHLS YLEAGADILE TNTFNATTIA MADYDMESLS AEINFEAARL ARAAADEWTA KTPNKPRYVA GVLGPTNRTC SISPDVNDPG YRNVSFDELV EAYSESTRAL IKGGSDLILI ETIFDTLNAK ACAFAVDCVF EEMGITLPVM ISGTITDASG RTLSGQTTEA FYNSLRHIKP LSFGLNCALG PDELRPYVDE LSRISETFVS AHPNAGLPNA FGEYDLSPED MAEHVKEWAE SGFLNLIGGC CGTTPEHIRQ MAQAVENVKP RSLPEINVAC RLSGLEPLTI EKESLFINVG ERTNVTGSAR FKRLIKEELY DEALDVARQQ VENGAQIIDI NMDEGMLDAE ACMVRFLNLC ASEPEISKVP IMVDSSKWEV IEAGLKCIQG KGIVNSISLK EGKGKFVEQA KLIRRYGAAV IVMAFDEVGQ AETRERKLEI CTKAYRILVD EVGFPPEDII FDPNIFAVAT GIEEHNNYAV DFIEAVADIK RDLPHAMISG GVSNVSFSFR GNNYVREAIH AVFLYHCFKN GMDMGIVNAG QLEIYDNVPD KLREAVEDVV LNRRDDGTER LLDIAAEYAG KGVGKEDDAS ALEWRTWAVE KRLEHALVKG ITEFIVEDTE EARVNATKPL EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA HLEPYINAEK QAGSTNGKIL LATVKGDVHD IGKNIVGVVL QCNNYEIIDL GVMVPCDQIL KVAKEENVDI IGLSGLITPS LDEMVHVAKE MERLGFDLPL LIGGATTSKA HTAVKIEQNY NQPVVYVNNA SRAVGVCSSL LSDTLKPGFV EKLQADYDIV REQHARKRPR TKPVTLEKAR ANKVAIDWDA YTPPVPVKPG IHIFDDFDIA TLRNYIDWTP FFMTWSLVGK YPKIFEHEEV GEEAKRLFAD ANELLDRVEK EGLLKARGMC GLFPAASVGD DIEVYTDESR TEVATVLHNL RQQTEKPKGF NYCTSDYIAP KESGKPDWIG AFAVTGGIGE RELADEYKAQ GDDYNAIMIQ AVADRLAEAF AEYLHERVRK EIWGYAADEN LSNEDLIREK YQGIRPAPGY PACPEHTEKA PLWELMNVEE NIGMSLTTSY AMYPGASVSG WYFSHPDSRY FAVAQIQQDQ LESYADRKGW DLIEAEKWLG PNL // ID F2QYJ8_PICP7 Unreviewed; 315 AA. AC F2QYJ8; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 29-APR-2015, entry version 23. DE SubName: Full=MmuM protein {ECO:0000313|EMBL:CCA40476.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:CCA40476.1}; GN Name=mmuM {ECO:0000313|EMBL:CCA40476.1}; GN OrderedLocusNames=PP7435_Chr4-0305 {ECO:0000313|EMBL:CCA40476.1}; 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; Phaffomycetaceae; Komagataella. OX NCBI_TaxID=981350 {ECO:0000313|EMBL:CCA40476.1, ECO:0000313|Proteomes:UP000006853}; RN [1] {ECO:0000313|EMBL:CCA40476.1, ECO:0000313|Proteomes:UP000006853} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 76273 / CBS 7435 / CECT 11047 / NRRL Y-11430 / Wegner 21-1 RC {ECO:0000313|Proteomes:UP000006853}; 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; FR839631; CCA40476.1; -; Genomic_DNA. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000006853; Chromosome 4. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006853}; KW Methyltransferase {ECO:0000313|EMBL:CCA40476.1}; KW Transferase {ECO:0000313|EMBL:CCA40476.1}. SQ SEQUENCE 315 AA; 34910 MW; 1443558C0466533B CRC64; MDSWLKQKRC RVLDGALGTE LEKLGIDIKS RLWSGKALFY SPETITQIHS SYIQAGAELI LTCTYQLSDQ GLKDLGIDDP DVYDRAVKLA KDAVDQNEGE NKAKIVGSIG SYGAYLSGGE EYTGEYGAIS KSELEEFHRV RLQSLLTNPD VDLIGFETIP NILEAETLVV LFNALATSLN VDKGYYMSFN CREESNQSVI ADGTSIPEVS DRLSKLDVSR MYAIGTNCCS ISTANGAVEL FSKHTNLPLI VYPNSGERYD KTEKKWLPGE CDQKITDIVV NWLQLNVKII GGCCRTNPHF IRQLRDIVDN SSRSG // ID F2R9M5_STRVP Unreviewed; 307 AA. AC F2R9M5; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=SVEN_5782 protein {ECO:0000313|EMBL:CCA59068.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:CCA59068.1}; GN OrderedLocusNames=SVEN_5782 {ECO:0000313|EMBL:CCA59068.1}; 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 {ECO:0000313|EMBL:CCA59068.1, ECO:0000313|Proteomes:UP000006854}; RN [1] {ECO:0000313|Proteomes:UP000006854} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 / RC PD 04745 {ECO:0000313|Proteomes:UP000006854}; RX PubMed=21463507; DOI=10.1186/1471-2164-12-175; RA Pullan S.T., 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 ----------------------------------------------------------------------- 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; CCA59068.1; -; Genomic_DNA. DR RefSeq; WP_015036963.1; NC_018750.1. DR RefSeq; YP_006881327.1; NC_018750.1. DR EnsemblBacteria; CCA59068; CCA59068; SVEN_5782. DR KEGG; sve:SVEN_5782; -. DR KO; K00547; -. DR BioCyc; SVEN953739-WGS:GSXO-5862-MONOMER; -. DR Proteomes; UP000006854; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006854}; KW Methyltransferase {ECO:0000313|EMBL:CCA59068.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006854}; KW Transferase {ECO:0000313|EMBL:CCA59068.1}. SQ SEQUENCE 307 AA; 31550 MW; 2830A85D34E80E5F CRC64; MRPVRTLAEA LGDGALVLDG GLSNQLEAQG CDLSDALWSA RLLADGPEQI EAAHAAYVRA GARVLITSSY QATVEGFARR GVGRAAAERL LARSVELARA AARGVREEVW VAASVGPYGA MLADGSEYRG RYGLSVRELE AFHRPRIEVL AAAEPDVLAL ETVPDAEEAE ALLRAAEGCG VPVWLSYTVE GGRTRAGQDL AEAFAVAAGN DQVVAVGVNC CDPAEAGAAV ALAAAVTGRP GVVYPNSGER WDARARGWRG AVAFDPALAT GWAASGARLV GGCCRVGPET IAALATTLTP SADASDA // ID F2RDZ7_STRVP Unreviewed; 1176 AA. AC F2RDZ7; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 29-APR-2015, entry version 25. DE SubName: Full=SVEN_1250 protein {ECO:0000313|EMBL:CCA54537.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CCA54537.1}; GN OrderedLocusNames=SVEN_1250 {ECO:0000313|EMBL:CCA54537.1}; 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 {ECO:0000313|EMBL:CCA54537.1, ECO:0000313|Proteomes:UP000006854}; RN [1] {ECO:0000313|Proteomes:UP000006854} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 / RC PD 04745 {ECO:0000313|Proteomes:UP000006854}; RX PubMed=21463507; DOI=10.1186/1471-2164-12-175; RA Pullan S.T., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; FR845719; CCA54537.1; -; Genomic_DNA. DR RefSeq; WP_015032455.1; NC_018750.1. DR RefSeq; YP_006876796.1; NC_018750.1. DR EnsemblBacteria; CCA54537; CCA54537; SVEN_1250. DR KEGG; sve:SVEN_1250; -. DR KO; K00548; -. DR BioCyc; SVEN953739-WGS:GSXO-1259-MONOMER; -. DR Proteomes; UP000006854; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006854}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CCA54537.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006854}; KW Transferase {ECO:0000313|EMBL:CCA54537.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 237 237 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 753 753 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1176 AA; 128389 MW; FE5BF941AE6FB8B9 CRC64; MASLPTPSAD SRNRVAALRE ALASRVVVAD GAMGTMLQAQ DPTLEDFQNL EGCNEILNVT RPDIVRSVHQ EYFEAGVDCV ETNTFGSNHS AAGEYEIADR IFELSEAGAR IAREVADEFA AADGRQRWVL GSIGPGTKLP SLGHIAYDVL RDGYQQNAEG LLAGGADALI VETTQDLLQT KSSLIGARRA MDALGVDVPL ICSLAFETTG VMLLGSEIGA ALTALEPLGI DLIGLNCSTG PAEMSEHLRY LARHSRTPLM CMPNAGLPVL TKDGAYFPLT PPEMADAQEN FVRDYGLSLI GGCCGSTPEH LRQVVERVQG LAPAVRDPRP EPGAASLYQT VPFRQDTAYM AIGERTNANG SKKFREAMLE ARWDDCVEMA RDQIREGAHM LDLCVDYVGR DGVADMQELA GRFATASTLP IVLDSTEVDV LRAGLEKLGG RAVINSVNYE DGDGPESRFA KVTRLAQEHG AALIALTIDE EGQARTAEHK VAIAERLIED LTGNWGILES DILIDTLTFT ICTGQEESRK DGIATIEAIR ELKRRRPDVQ TTLGLSNISF GLNPAARILL NSVFLDECVK AGLDSAIVHA SKILPIARFD EEQVTTALDL IYDRRRPQQG DEPAYDPLQK LMALFEGATT KSLKAGKAEE LLALPLDERL KRRIVDGEKN GLEADLDEAL TTTPALDIVN NILLDGMKTV GELFGSGQMQ LPFVLQSAEV MKTAVAYLEP HMEKSDADGK GTIVLATVRG DVHDIGKNLV DIILSNNGYN VVNIGIKQPV SAILEAAEEH KADVIGMSGL LVKSTVIMKE NLEELNQREL AAKYPVILGG AALTRAYVEQ DLHEIYQGEV RYARDAFEGL RLMDALIGVK RGVPGAVLPE LKQRRVAKKD AAALQVDEPE PAGRSDVAVD NPVPTPPFWG TRVVKGIPLK DYASWLDEGA LFKGQWGLKQ NRAGDGPAYE ELVETEGRPR LRGWLDKLHT ENLLEAAVVH GYFPCVSKGD DLIILDEAGH ERTRFTFPRQ RRGRRLCLAD FFRPEESGET DVVGLQVVTV GSKIGEATAK LFESDSYRDY LELHGLSVQL AEALAEYWHA RVRAELGFAG EDPENVADMF DLKYRGARFS LGYGACPDLE DRAKIAELLR PERIGVHLSE EFQLHPEQST DAIVIHHPEA KYFNAR // ID F2RH40_STRVP Unreviewed; 1153 AA. AC F2RH40; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=SVEN_4082 protein {ECO:0000313|EMBL:CCA57368.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CCA57368.1}; GN OrderedLocusNames=SVEN_4082 {ECO:0000313|EMBL:CCA57368.1}; 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 {ECO:0000313|EMBL:CCA57368.1, ECO:0000313|Proteomes:UP000006854}; RN [1] {ECO:0000313|Proteomes:UP000006854} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 / RC PD 04745 {ECO:0000313|Proteomes:UP000006854}; RX PubMed=21463507; DOI=10.1186/1471-2164-12-175; RA Pullan S.T., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; FR845719; CCA57368.1; -; Genomic_DNA. DR RefSeq; WP_015035279.1; NC_018750.1. DR RefSeq; YP_006879627.1; NC_018750.1. DR EnsemblBacteria; CCA57368; CCA57368; SVEN_4082. DR KEGG; sve:SVEN_4082; -. DR KO; K00548; -. DR BioCyc; SVEN953739-WGS:GSXO-4147-MONOMER; -. DR Proteomes; UP000006854; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006854}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CCA57368.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006854}; KW Transferase {ECO:0000313|EMBL:CCA57368.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 737 737 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1153 AA; 125123 MW; 3921F54B8C39AD72 CRC64; MTVVRSSLRE EFARRVVVAD GAMGTMLQAA DPSMDDFTGL EGCNEILNLT RPDIVASVHD AYFSVGVDCV ETNTFGANLA ALAEYGIEHQ VYELSEAGAR IARAAADAHT AADGRPRWVL GSMGPGTKLP TLGHVTYEPL REAFQQNAEG LIRGGADALL IETSQDLLQT KAAVIGARRA LDWVGVDLPV IVQVTVETTG TMLLGSEIGA ALTALEPLGI DMIGLNCATG PAEMAEHLRY LSRHARVPLS VMPNAGLPVL TSDGAHYPLS PAELADAQEA FVREYGPALV GGCCGTTPEH LREIVGRVRG AAVLDRRPEP EPGASSLYSH VPFRQDTAYL AIGERTNANG SKKFREAMLE ARWDDCVEMA RDQIREGAHM LDLCVDYVGR DGVADMQELA GRFATASTLP IVLDSTEVDV LRAGLEKLGG RAVVNSVNYE DGDGPESRFA QVTALAKEHG AALMALTIDE EGQARTVGAK VAIAERLIAD LTGNWGIRES DILIDTLTFT ICTGQEESRG DGVATIEAIR ELKRRHPDVQ TTLGLSNISF GLNPAARIVL NSVFLDECVK AGLDSAIVHA SKILPIARLE PEQVEVALDL IHDRRREGYD PLQRFLEMFE GATAKSLKAG KTEELLALPL DERLKRRIVD GEKNGLEADL DEALTTTPAL DIVNNILLDG MKTVGELFGS GQMQLPFVLQ SAEVMKTAVA YLEPHMEKSD ADGKGTIVLA TVRGDVHDIG KNLVDIILSN NGYNVVNIGI KQPVSAILEA AEEHKADVIG MSGLLVKSTV IMKENLQELN GRGLAARYPV ILGGAALTRA YVEQDLHELY EGEVRYARDA FEGLRLMDAL MGVKRGVPGA VLPPLKQRRV AARPPVAEVR EPEPAGRSDV AEDNPVPEPP FLGTRVVKGI PLAEYAPWLD ESALFKGQWG LKDPETIETE GRPRLRAWLD RLQTDHLLEA AVVYGWFPCV SKGDDLIVLD EDGGERTRFS FPRQQRGRRL CLADFHRAED SGEIDAVAMQ VVTVGSRIGE ETAKLFAADA YRDYLELHGL SVQLAEALAE YWHARVRSEW GIGDRDPAGI GGMLRTEYQG CRYSLGYPAC PDLEDRAKIA ALLRPERIGV ELSEEYQLHP EQSTDAIVVH HPEAGYFNAG GRR // ID F2TYS4_SALR5 Unreviewed; 1262 AA. AC F2TYS4; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 01-APR-2015, entry version 26. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGD78748.1}; GN ORFNames=PTSG_01727 {ECO:0000313|EMBL:EGD78748.1}; OS Salpingoeca rosetta (strain ATCC 50818 / BSB-021). OC Eukaryota; Choanoflagellida; Salpingoecidae; Salpingoeca. OX NCBI_TaxID=946362 {ECO:0000313|Proteomes:UP000007799}; RN [1] {ECO:0000313|Proteomes:UP000007799} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 50818 {ECO:0000313|Proteomes:UP000007799}; RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N., RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., RA 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 "Annotation of Salpingoeca rosetta."; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GL832957; EGD78748.1; -; Genomic_DNA. DR RefSeq; XP_004997705.1; XM_004997648.1. DR GeneID; 16078301; -. DR InParanoid; F2TYS4; -. DR Proteomes; UP000007799; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007799}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007799}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 254 254 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 318 318 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 783 783 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1262 AA; 139476 MW; 4E87F3302FC748C3 CRC64; MAAKHVEETT AALRALLEER IMFFDGGMGT MIQQLSLQEK DFRGELFKEH PKALQGNNDL LVLTQPEAIV NIHKQFLLAG ADFVETNTFS STRIAQADYA TEDHVYKLNV EAAKLAKRAC EEVEAQGHGR KFVAGSLGPT NRTLSISPSV EQPELRNVKF DELVEAYAEQ ARGLMDGGVD VLLVETIFDT ANAKAALFAV EKLFEDEPEK YPRRPIFISG TITDRSGRTL SGQTAEAFSI SVSHGRPMAL GLNCALGATD MRPYLEEIAK TTDAYIICYP NAGLPNAMGG YDETPDITGS HLADFARSGL VNIVGGCCGT TPAHIAAIVK MCSSFPPRQR PPKPFADHML LSGLEPARIG PDTNFVNIGE RCNVAGSRRF CRLIKTDEYD EALAVAKLQV ENGAQILDIN MDDGLLDGVK AMTKFCNLIA SEPDIAKVPL CIDSSDFAVV EAGLKCTQGK CIVNSISLKS GEEEFIKVAR TIRRYGAAVV VMAFDEKGQA ADLEGKIRIC TRSYKILVEK VGFNPNDIIF DPNILTIGTG IEEHNEYAIN FINCIRPIKE QCPGCHISGG VSNLSFSFRG MNVVREAMHS VFLYHAIQKG MDFGIVNAGA MPIYSEIDPK LVELCENIIW NKHPNATEEL LTYAQEHGKE AKTKKQDDSW RDAPVEKRLE HALIKGIDKF VVADTEEARQ NTALYPKPLN VIEGPLMAGM SIVGDLFGAG KMFLPQVIKS ARVMKKAVAH LIPFMEEERE ASLRAQGIDP EVADESDMYN GTVVIATVKG DVHDIGKNIV AVVLGCNNFK VVDLGVMVPA NKILEAVDKH KADIVGLSGL ITPSLDEMVF VAKELERTGH KLPLLIGGAT TSKMHTAVKI APKYSSPTVH VLDASRSVVT VSALLDQGNR EDFVEDIAEE YEEIREEYLE SLTDRVYLSL DAARKQRFAI DFNKKPPVKP AMTGVKVIES LDLERCIKYI DWKPFFEVWQ LRGRYPNRSY PKIFDDEAVG SEAKKVFDDA QALLKRIVSE KLLRGKGVFG IFPANTVGDD IEIYEDESRT TVKETLYGLR QQAEKVDKTD PYFCHSDFIA PKESGIADYI GMFAVTCGLG ADELSKQFLN DHDDYNSIMV KALADRLAEA FAEMLHEDVR RKYWAYATDE GFTAKELHQL KYAGIRPAPG YPSQPDHTEK EAYWRLLDAE ANAEMSLTES FSMMPAASVS GLYFAHPDSE YFAVGKIDRD QAADYAKRKG SDLQTVERWL APILSYDPDE SQ // ID F2UKC1_SALR5 Unreviewed; 460 AA. AC F2UKC1; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 07-JAN-2015, entry version 16. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:EGD77570.1}; GN ORFNames=PTSG_08668 {ECO:0000313|EMBL:EGD77570.1}; OS Salpingoeca rosetta (strain ATCC 50818 / BSB-021). OC Eukaryota; Choanoflagellida; Salpingoecidae; Salpingoeca. OX NCBI_TaxID=946362 {ECO:0000313|Proteomes:UP000007799}; RN [1] {ECO:0000313|Proteomes:UP000007799} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 50818 {ECO:0000313|Proteomes:UP000007799}; RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N., RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., RA 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 "Annotation of Salpingoeca rosetta."; 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; GL832978; EGD77570.1; -; Genomic_DNA. DR RefSeq; XP_004990458.1; XM_004990401.1. DR GeneID; 16071014; -. DR InParanoid; F2UKC1; -. DR Proteomes; UP000007799; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 4. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 2. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007799}; KW Methyltransferase {ECO:0000313|EMBL:EGD77570.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007799}; KW Transferase {ECO:0000313|EMBL:EGD77570.1}. SQ SEQUENCE 460 AA; 48904 MW; AD615D0628616612 CRC64; MVSPLVLDGG LSSLLELERG PLHPTLWSAA LLVASTGGQG KEAGERAGKD GHNNDDDDDD DDDDDGTSHV FSDTNHRAVI DAHRAFLEAG ADILTTVSYQ GTVAGFKRDM GLSEEEASHA IALSVTLART AIHEHQQAQQ QQQQQQHIER DKHSSSSSQA PRTLSSSWAS SRHLLLHPPP HGTQQHPQEQ QHEQQHEQQQ EQQPRPLVAA SIGPYGAFLA DGSEYRGGYD AERLAQFHHE KALILWRARP DVLAFETIPQ ASEALAIVGM MQETLPEAPY WLSFQCCDAH RLASGDDVTA AVASLVTAFD EQRAGSLIGI GVNCISPAIA APLVTAIARC VGRRRLHVLC YPNKGEAWDA DTRTWGPIPT ADVGDGDGVG GFGNGGDGGD VGDGGDGGDG DTAGPCALTS RAWVRRIKAA GCTVVGGCCR VFPADLAQMV RCVKGDIEGG NRRDKAGVHG // ID F2V090_ACTVI Unreviewed; 325 AA. AC F2V090; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGE37844.1}; GN ORFNames=HMPREF0059_02115 {ECO:0000313|EMBL:EGE37844.1}; OS Actinomyces viscosus C505. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Actinomycineae; Actinomycetaceae; Actinomyces. OX NCBI_TaxID=562973 {ECO:0000313|EMBL:EGE37844.1}; RN [1] {ECO:0000313|EMBL:EGE37844.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C505 {ECO:0000313|EMBL:EGE37844.1}; 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] {ECO:0000313|EMBL:EGE37844.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C505 {ECO:0000313|EMBL:EGE37844.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGE37844.1}. 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; ACRE02000009; EGE37844.1; -; Genomic_DNA. DR RefSeq; WP_004565257.1; NZ_KI391967.1. DR EnsemblBacteria; EGE37844; EGE37844; HMPREF0059_02115. DR OrthoDB; EOG6C019S; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 325 AA; 34201 MW; 72A95EA5704BA88B CRC64; MRTLSVSATS FEREPVRLSD LLARGPVVLD GAMGTELDAR GVDTRNALWS ARALTMAPDV VREVHSDYLD AGARVITTNT YQATLPALVR SGEDAAGARR VIAAGARLAK EAARQFSKEH PEEPVLVAGG LGPYGAYLAD GSEYTGAYGI DILEDPGFQE VHLPRIEVLA GEGIDLFALE TLPRLDEARA LASMVKGLAP QAECWVSFQV RPDGATLADG TPLAEAAAWA AQEEIVVAVG INCVAPGVVA RALPVLRAVT NKPLVAYPNA GDLYDPATKT WQSTGDGAGI PELAPSWIDA GVRLVGGCCR TRPAQIRQLA RAVCP // ID F2ZJS9_9PSED Unreviewed; 298 AA. AC F2ZJS9; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EGI02669.1}; GN ORFNames=POR16_13055 {ECO:0000313|EMBL:EGI02669.1}; OS Pseudomonas coronafaciens pv. oryzae str. 1_6. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas coronafaciens. OX NCBI_TaxID=563797 {ECO:0000313|EMBL:EGI02669.1}; RN [1] {ECO:0000313|EMBL:EGI02669.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_6 {ECO:0000313|EMBL:EGI02669.1}; 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] {ECO:0000313|EMBL:EGI02669.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_6 {ECO:0000313|EMBL:EGI02669.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGI02669.1}. 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; ABZR01000365; EGI02669.1; -; Genomic_DNA. DR EnsemblBacteria; EGI02669; EGI02669; POR16_13055. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EGI02669.1}; KW Transferase {ECO:0000313|EMBL:EGI02669.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 207 207 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 298 AA; 31482 MW; 18A6D278915CA9CF CRC64; MTQGTTVILD GGMGRELQRR GAPFRQPEWS ALALSEAPEA VSAVHTAYID SGAQVITSNS YAVVPFHIGE ERFAREGQAL AALAGQLARA AADASGGRAR VAGSIPPLFG SYRPDLYKPE QAADVLKPLV AGLSPHVDLW LAETQSCILE AQTIRAGLPA DGKPFWLSFT LQDEDTDEVP RLRSGEPVAD AAKAAVEMGV ATLLFNCSQP EVIGGAIDAA REVFEALGVD IAIGAYANAF PPQPKDAKAN DGLDELREDL DPEGYQQWAA DWVKRGATHI GGCCGIGPEH IAVLSRSL // ID F2ZMG8_9PSED Unreviewed; 1239 AA. AC F2ZMG8; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EGI03608.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGI03608.1}; GN Name=metH {ECO:0000313|EMBL:EGI03608.1}; GN ORFNames=POR16_17843 {ECO:0000313|EMBL:EGI03608.1}; OS Pseudomonas coronafaciens pv. oryzae str. 1_6. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas coronafaciens. OX NCBI_TaxID=563797 {ECO:0000313|EMBL:EGI03608.1}; RN [1] {ECO:0000313|EMBL:EGI03608.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_6 {ECO:0000313|EMBL:EGI03608.1}; 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] {ECO:0000313|EMBL:EGI03608.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_6 {ECO:0000313|EMBL:EGI03608.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGI03608.1}. 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; ABZR01000509; EGI03608.1; -; Genomic_DNA. DR EnsemblBacteria; EGI03608; EGI03608; POR16_17843. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGI03608.1}; KW Transferase {ECO:0000313|EMBL:EGI03608.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1239 AA; 136171 MW; 4A2B4F98966290B3 CRC64; MSDRSARHQA FLTALKQRIL ILDGGMGTMI QSYRLEEQDY RGKRFSDWPS DVKGNNDLLI LTRPDVIGAI EKAYLDAGAD ILETNTFNAT QVSQADYGME SIVYELNVEG ARLARKVADA KTLETPDKPR FVAGVLGPTS RTCSLSPDVN NPGYRNVTFD ELVENYTEAT KGLIEGGADL ILIETIFDTL NAKAAIFAVQ GVFEELGFEL PIMISGTITD ASGRTLSGQT TEAFWNSISH AKPVSVGLNC ALGASELRPY LQELANKANT HVSAHPNAGL PNAFGEYDEL PSQTAKIIEE FAQSGFLNIV GGCCGTTPAH IKAIAEAVSG YAPREIPDIP KACRLSGLEP FTIDRQSLFV NVGERTNITG SARFARLIRE DNYTEALEVA LQQVEAGAQV IDINMDEGML DSKKAMVTFL NLIAGEPDIS RVPIMIDSSK WEVIEAGLKC IQGKGIVNSI SMKEGVEQFI HHARLCKRYG AAVVVMAFDE QGQADTEARK KEICKRSYDI LVNEVGFPPE DIIFDPNIFA IATGIEEHNN YAVDFINACA YIRDELPHAL TSGGVSNVSF SFRGNNPVRE AIHSVFLLHA IRNGLSMGIV NAGQLEIYDQ IPAELRDCVE DVVLNRNPEG TDALLAIADK YKGDGSVKEA ETEEWRSWPV NQRLEHALVK GITTHIVQDT EESRLGFKRP IEVIEGPLMS GMNVVGDLFG AGKMFLPQVV KSARVMKQAV AHLIPFIELE KGDKPEAKGK ILMATVKGDV HDIGKNIVGV VLGCNGYDIV DLGVMVPAEK ILQVAREQKC DIIGLSGLIT PSLDEMVHVA REMQRQDFHL PLMIGGATTS KAHTAVKIEP KYSNDAVIYV TDASRAVGVA TQLLSKELKP AFIEKTRLEY VEVRERTSAR SARTERLSYG AAVAKKPQFD WENYTPAQPT FTGTRILQDI DLNVLAEYID WTPFFISWDL AGKYPRILTD EVVGEAATAL FEDARQMLRK LIDEKLISAR AVFGFWPANQ VNDDDLEVYG DDGKPLARLH HLRQQTIKPD GKPNFSLADF VAPKDSGLTD YIGGFITTAG IGAEEVAKAY QDNGDDYNSI MVKALADRLA EACAEWLHQQ VRKEYWGYAK DEALDNEALI KEQYMGIRPA PGYPACPDHT EKGTLFALLD PLPEGTPEHT PGKSGVFLTE HYAMFPAAAV SGWYFAHPQA QYFAVGKVDK DQVESYTARK GQDLSVTERW LAPNLGYDE // ID F3A1W4_9BACL Unreviewed; 613 AA. AC F3A1W4; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HMPREF0428_00722 {ECO:0000313|EMBL:EGF85558.1}; OS Gemella haemolysans M341. OC Bacteria; Firmicutes; Bacilli; Bacillales; OC Bacillales Family XI. Incertae Sedis; Gemella. OX NCBI_TaxID=562981 {ECO:0000313|EMBL:EGF85558.1}; RN [1] {ECO:0000313|EMBL:EGF85558.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M341 {ECO:0000313|EMBL:EGF85558.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGF85558.1}. 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; ACRO01000008; EGF85558.1; -; Genomic_DNA. DR RefSeq; WP_003146750.1; NZ_GL883582.1. DR EnsemblBacteria; EGF85558; EGF85558; HMPREF0428_00722. DR PATRIC; 54842780; VBIGemHae124407_0714. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 613 AA; 68035 MW; 6403B83861DD7F38 CRC64; MRNLLERLEQ NVLVADGAMG TALYSNGLES CHEYNNISNP DSVEKIHKAY IEAGADIIQT NTYAAKKCQL KTYGYDDKFE EINIRAAEIA RKAAGEDTIV FGTIGAIRGL RECELSLETI VKETIDQVKV LLSTNKIDAL LFETYYDQEE IRAVLTEARK ITDLPIITNI SLLEAGITQN GEKVTDALSA LVNLGADIVG LNCHLGPYHM IKSLKQVPLF AQSYLSAYPN ASLLQLTQTI NGNEYRFRKN SSYFEQSAKL LVEEGVRLIG GCCGTTPEHI RAIKKGIKGL KPVKRKVITP LPAEEELVRV ANNKPTIVDK VKKQVTIIAE LDPPKHLNVD KFIEGAKAID KKNIEAITLA DNSLASTRIC NLSAATLLKE HITTPTLLHL TCRDHNLIGL QSRLMGFDLL GINNVLALTG DPSKLGDFPG ATSVYDMTSL KLIPFIKQLN EGLGYNGASL KKTTNFTVAA AYNPNVRDLS KTKRLVEKKI KAGTDYFITQ PVFEAEKIEQ LAELAADYPD TPFFVGIMPI TSYNNAVFLH NEVPGIKLSE EFLAKLEEVK DDKELCQKVA LEESKKLLDV ALKHFKGIYL ITPFLRYDLT LELIDYVEEN KDK // ID F3ADZ0_9FIRM Unreviewed; 287 AA. AC F3ADZ0; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGG83874.1}; GN ORFNames=HMPREF0992_01285 {ECO:0000313|EMBL:EGG83874.1}; OS Lachnospiraceae bacterium 6_1_63FAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=658083 {ECO:0000313|EMBL:EGG83874.1}; RN [1] {ECO:0000313|EMBL:EGG83874.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=6_1_63FAA {ECO:0000313|EMBL:EGG83874.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGG83874.1}. 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; ACTV01000015; EGG83874.1; -; Genomic_DNA. DR RefSeq; WP_003022344.1; NZ_GL890551.1. DR EnsemblBacteria; EGG83874; EGG83874; HMPREF0992_01285. DR PATRIC; 54851524; VBILacBac91825_1303. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 203 203 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 287 AA; 30865 MW; 497B5867DD114AD9 CRC64; MTREEFRELI GREIVILDGA TGSNLMKAGM PKGICTEKWI CENPQPLMNL QSAYQQAGSQ IVYAPTFSAN KISLANHGLE NQVHSLNKQL VEISRSAVGE NCMVAGDLTT TGKQDAEYET LLDAYKEQIE AQLEAGVDLL VAETMLGVTE PMAVLDAARE LCSLPVLCTL TVESDGSLFF GGNIYDSAEL LEEMGADAVG INCSTGPDQL LSVVENIRKR IHIPLIVKPN AGNPVIDAMG NPVYSMGAEE FARHIKRLID AGANLVGGCC GTTPAYIEQL VKLKSSF // ID F3AI63_9FIRM Unreviewed; 806 AA. AC F3AI63; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 01-OCT-2014, entry version 18. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGG90262.1}; GN ORFNames=HMPREF0987_00137 {ECO:0000313|EMBL:EGG90262.1}; OS Lachnospiraceae bacterium 9_1_43BFAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=658088 {ECO:0000313|EMBL:EGG90262.1}; RN [1] {ECO:0000313|EMBL:EGG90262.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=9_1_43BFAA {ECO:0000313|EMBL:EGG90262.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGG90262.1}. 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; ACTX01000001; EGG90262.1; -; Genomic_DNA. DR RefSeq; WP_009261767.1; NZ_GL890571.1. DR EnsemblBacteria; EGG90262; EGG90262; HMPREF0987_00137. DR PATRIC; 54854616; VBILacBac68115_0141. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; SQ SEQUENCE 806 AA; 88388 MW; EB0B81DB4FDE35C4 CRC64; MLLERLGKEL LFLDGGMGTL LQEKGLQPGE LPESWNLKRP EEVIAIHQNY FEAGSDIVLT NTFGANALKF HSEDCPLQEV VTRAVENVRE AARRGVKDGR EIYVGLDIGP TGKLLKPMGD LAFEDAYEAF AEVMEYGEKA GADLIHIETM SDTYEVKAAV LAAKERTSLP VFATMIFDER GKLLTGGDVP SVVAMLEGLR VDALGINCGM GPEQMLSILE ELLTYTSLPV IVKPNAGLPK QRDGQTYYDV VPEEFASTMK LIVEKGACII GGCCGTTPAH IRQMTTLCQG MRAVPPVKKH HTLVSSYGTC ISFGRKPVII GERINPTGKK KLKQALKDGD FDYILKEGIM QQEKGAHILD VNVGLPDIDE VAVMEKVVTE LQSVTSLPLQ IDTVLPEAME RAMRIYNGKP MINSVNGKQE SMDQVFPLVQ KYGGVVVALT IDEDGIPDTA EGRLAIAEKI ICEAEKYGID RKDIVVDVLA MTISSEPEGA LVTLKALKLV REVCKVNTVL GVSNISFGLP KRPVINAHFY TMAMQQGLTS AIINPFSEEM MNSYYAFCAL MNYDENCASY IERYSKTVEE EQQSIAGSPT QAGQETSRAG EMSLQTAIER GLKEEAGHLT RELVREKEPL AIIQEQLIPA LDVVGKGFEK GTIFLPQLLM SAEAAKEAFA VLKEVLERSG QKEQKKGKVI LATVKGDIHD IGKNIVKVLL ENYSFDVIDL GKDVDPEMIV HTAKQEGIRL VGLSALMTTT VVSMEETIRL LREHCPDCKV MVGGAVLNPE YAEMIGADFY GKDAMQSVYY AQRVFA // ID F3AQN4_9FIRM Unreviewed; 826 AA. AC F3AQN4; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGG83616.1}; GN ORFNames=HMPREF1025_00038 {ECO:0000313|EMBL:EGG83616.1}; OS Lachnospiraceae bacterium 3_1_46FAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=665950 {ECO:0000313|EMBL:EGG83616.1, ECO:0000313|Proteomes:UP000005376}; RN [1] {ECO:0000313|EMBL:EGG83616.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_46FAA {ECO:0000313|EMBL:EGG83616.1}; 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 3_1_46FAA."; 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. {ECO:0000313|EMBL:EGG83616.1}. 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; ACWP01000004; EGG83616.1; -; Genomic_DNA. DR RefSeq; WP_004844944.1; NZ_GL890520.1. DR ProteinModelPortal; F3AQN4; -. DR EnsemblBacteria; EGG83616; EGG83616; HMPREF1025_00038. DR PATRIC; 54860198; VBILacBac142657_0037. DR Proteomes; UP000005376; Unassembled WGS sequence. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005376}. SQ SEQUENCE 826 AA; 90755 MW; A9D2C7AB0EC769C4 CRC64; MIRQRLGKDL LFFDGGMGTL LQEKGLAPGE LPETWNLTHS EEIYKIHRQY IEAGSDIILT NTFGANALKF HDDSCSLEEI IKAAVSHVKK AEREALLQTG DERKIYTALD VGPTGKLLKP MGDLEFETAY EAFKEVVILG EQAGADLIHI ETMSDTYELK AAVLAAKENT SLPVFATVIF DERKKLLTGA DVSSVVALLE GLGVDALGIN CAMGPKEMLP VLEELIKYSS VPIIVKPNAG LPKQRDGKTY YDVTEDEFAA YMEQIVRMGA CVIGGCCGTT PEHIRAMRKR CENAELVPVT EKEFTVVSSY GQSVILGEGS KIIGERINPT GKKRFKQALK EHDLDYILRE GITQQDQGAH ILDVNVGLPD IDEPALMEEV VQELQSVVNI PLQIDTVDEK AMEKALRIYN GKAMVNSVSG KKESMEKVFP LVKKYGGVVI GLTLDEDGIP ADADGRVRIA EKIIKTAEKF GIKKKDIVID ALAMTISSEP EGAKVTLETL RRLRDEIGVN TVLGVSNISF GLPCRPIVNA AFYTMAMLNG LSAGIINPSS EDMMKSWYAY HALMNLDNNC EQYIQKYANS VVSTNIMKTS ELSETKLKGE NDRSRKSSSK MTLQEAIEKG LRDDAGKITT DMIATEAPLD IINEELIPAL NHVGDGFEKG TVFLPQLLMS AEAAKSAFSV LKEKMEKSGE IREKKGRVIL ATVKGDIHDI GKNIVKVLLE NYSFDVIDLG KDVSPEKIVE TACEKQVPLV GLSALMTTTV VSMEETIKML REKKPDCKVM VGGAVLNQEY ADMIGADFYG KDAMQSVHYA EKIFKDALQK SADKKE // ID F3B1E0_9FIRM Unreviewed; 590 AA. AC F3B1E0; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 20. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HMPREF0491_00842 {ECO:0000313|EMBL:EGG89712.1}; OS Lachnospiraceae oral taxon 107 str. F0167. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=575593 {ECO:0000313|EMBL:EGG89712.1}; RN [1] {ECO:0000313|EMBL:EGG89712.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0167 {ECO:0000313|EMBL:EGG89712.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGG89712.1}. 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; ADDS01000006; EGG89712.1; -; Genomic_DNA. DR RefSeq; WP_009219114.1; NZ_GL890584.1. DR EnsemblBacteria; EGG89712; EGG89712; HMPREF0491_00842. DR PATRIC; 54868135; VBILacOra53760_0846. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 590 AA; 65831 MW; 0C1FA7709FC349CA CRC64; MENIREYLKN NVLLFDGAMG TYYDELTDDG IGCELANIKN SELIRGIHKE YIEAGAKAIL TNTFATGIDA FLGDRDLQKK VINAGIDIAI EAAKEEAYVF ADMGSLSADS NNAAFEEYKI IADIFLEKGI KNFFFETRNS TIGLKSIGEY IKEKSPDSFI IVSFAVMPDG YSSEGYYYKT MFKEICESGF FDAVGLNCMT GANHMAKLLK DVNTEGLYLV AMPNAGYPIV RDNRIYYGSL ANYFATQIED ILDMGVNIVG GCCGTTPKHI ELLKKSMSGK LIKPRRAIKQ EKGITQNIRL NRFKNKLELG QKAIAVELDS PIDTNVAKFM ENTKKLKLAG ADIVTIADNP IARARMDSCL LACKVRNELD FDVLPHMTCR DRNVNAAKGL LLGASAFGVD NVLVITGDPI PNAQRDEIRS VFEFNSVKFA NFIKSLNDEV FESPMNICAA LNVNSRNFSA ELKKAKRKQE NGVEVLFTQP VLTKRAVENL KTARENLDIK IMGGIIPIVS ERNARYMQSE VNGIYITDDI VEKYIGKERE EAEEIALSMS KEIANEIYDL VDGYYLITVL NRVSLMEKLI KTVKEVCENR // ID F3B1E1_9FIRM Unreviewed; 788 AA. AC F3B1E1; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGG89713.1}; GN ORFNames=HMPREF0491_00843 {ECO:0000313|EMBL:EGG89713.1}; OS Lachnospiraceae oral taxon 107 str. F0167. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=575593 {ECO:0000313|EMBL:EGG89713.1}; RN [1] {ECO:0000313|EMBL:EGG89713.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0167 {ECO:0000313|EMBL:EGG89713.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGG89713.1}. 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; ADDS01000006; EGG89713.1; -; Genomic_DNA. DR RefSeq; WP_009219115.1; NZ_GL890584.1. DR EnsemblBacteria; EGG89713; EGG89713; HMPREF0491_00843. DR PATRIC; 54868137; VBILacOra53760_0847. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; SQ SEQUENCE 788 AA; 85886 MW; 6F14B09516A88D80 CRC64; MHNLLILDGA MGTMLQAAGM KAGEHPEVFG FDNPDIVKNI HLKYIESGSN VIYTNTFGAN AHKLEGCKID VDTAIATAIK SAKEAVAESK EQVKVALDIG PIGELLEPLG VLRFEDAYEI YKEMVVAGEK YGADIIIFET FTDLYDVRAG VLAAKENTNL PVWVTMTYET TGRTFTGTKI ESMAVTLEGL GVDAVGFNCS LGPKEILPLA KKLKEWTNLP IIIKPNAGLP NPSTGEYDLL ASDFAKLMAD FGEIGIEYAG GCCGTSPEFI SELKKEFENR KFSKIKPIKV KTGICSGNEM VELNGVRVVG ERLNPTGKKR FQEALLNHEM EYICKVAIEE EESGADILDI NVGVPGGDEV ALMIEAVKAV QSVVNIPLQI DSSNPEAIEA GLRVYNGRAI VNSVNAEDER LDLILPIVKK YGAAVIGLAL NENGIPTTAQ ERFDNAKHIL DKAIEHGLKK EDVIIDCLTL TVSAQQDQAK ETLEAVRRVT RELGLHTTLG VSNISFGLPA RSHITENFLI QAMYAGLDLP IVNPNIEGIM DAIYSFKVLS GEDKDSAKYI DRFAAVKAET KIIQVSATGE VTKEVVQDAI LKGLKEETYN NAKKLLESHS ELEIINEYLI PALDKVGDLY EKQIIFLPQL INAANAASSA FELIKEEIAK KGDKNVSKGK IVVCTVKGDI HDIGKNIVKV ILENYGYRMI DLGRDVDIQR VVDTVIREDV KLVGLSALMT TTLPAMKSTI EEIRKVSNDC KIWVGGAVLT KEYADEMGAD FYAPDARSSV DIAKTVLG // ID F3B9Y0_9FIRM Unreviewed; 792 AA. AC F3B9Y0; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 01-OCT-2014, entry version 18. DE SubName: Full=Methylmalonyl-CoA mutase domain-containing protein {ECO:0000313|EMBL:EGG84252.1}; GN ORFNames=HMPREF9477_00750 {ECO:0000313|EMBL:EGG84252.1}; OS Lachnospiraceae bacterium 2_1_46FAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=742723 {ECO:0000313|EMBL:EGG84252.1}; RN [1] {ECO:0000313|EMBL:EGG84252.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=2_1_46FAA {ECO:0000313|EMBL:EGG84252.1}; 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., 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 Lachnospiraceae bacterium 2_1_46FAA."; RL Submitted (DEC-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. {ECO:0000313|EMBL:EGG84252.1}. 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; ADLB02000007; EGG84252.1; -; Genomic_DNA. DR RefSeq; WP_009757163.1; NZ_KE150017.1. DR EnsemblBacteria; EGG84252; EGG84252; HMPREF9477_00750. DR PATRIC; 54874397; VBILacBac154101_0746. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; SQ SEQUENCE 792 AA; 86712 MW; 02F286D821A1231D CRC64; MILEQLGKKL LFLDGGMGTL LQAEGLLPGE LPETWNAKRR ETVINIHRQY FEAGSDIVLT NTFGANAIKF HDDFYSLENI IKQAVANVHE GAKKCNKSKE EYCVALDIGP TGKLMEPMGD LSFEDAYNTF AEVMQYGKEA GADLIHIETM SDTYELKAAV LAAKENTNLP VFATMIFNEN GKLLTGGDVP SAVSMLEGLR VDAIGLNCGM GPKQMLPILK EMRKYTSLPI IVKANAGLPK QKNGETYYDV NPEEFANAMA EIVEEGGCVI GGCCGTTPEH ISEMKKMCGN KQIKVPQKRS ETIVSSYGKA VVFGEKPIII GERINPTGKS KMKQALKENQ LEYLLKEAIT QQEKGADILD VNVGLPDINE PEMMKKVIPE IQSVTNLPLQ IDTVNVAALE GAMRLYNGKP MVNSVTGKQE SMDKVFPLIQ KYGGVVVGLT LDEAGIPKTA EGRLEIAKKI IREAEKYGID KKDIVIDVLT MTISSEPEGA KTTLEALEMV RTICGVHTVL GVSNISFGLP TRPIINANFY TMAMQKGLSA GIINPSSEEM MNSYYAFCAL MNLDENCENY IANCMPKTVE TKPVTTLTLK MAIEKGLKEE TVQSVKSLIQ TEKPLEIINN YLIPALDTVG KGFEKGTVFL PQLLMSAESA KEAFAILKEE LSKSGQTDAK KEKVILATVK GDIHDIGKNI VKVLLENYAF DVVDLGKDVP PEKVVEAAKE NNVKLVGLSA LMTTTVVSME ETIKQLRKEV PDCKVMVGGA VLNQEYADMI GADFYGKDAM QSVHYARKIL KH // ID F3BET0_PSEHA Unreviewed; 357 AA. AC F3BET0; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EGI74851.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGI74851.1}; GN ORFNames=PH505_ac00220 {ECO:0000313|EMBL:EGI74851.1}; OS Pseudoalteromonas haloplanktis ANT/505. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=722419 {ECO:0000313|EMBL:EGI74851.1}; RN [1] {ECO:0000313|EMBL:EGI74851.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ANT/505 {ECO:0000313|EMBL:EGI74851.1}; 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. {ECO:0000313|EMBL:EGI74851.1}. 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; ADOP01000003; EGI74851.1; -; Genomic_DNA. DR RefSeq; WP_002958119.1; NZ_ADOP01000003.1. DR EnsemblBacteria; EGI74851; EGI74851; PH505_ac00220. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGI74851.1}; KW Transferase {ECO:0000313|EMBL:EGI74851.1}. SQ SEQUENCE 357 AA; 38961 MW; 80DF95468CE5BB3C CRC64; MPNNAPTNNK QAEISAALKE RILILDGAMG TMIQDYKLEE EDYRGERFKD WHVLIKGNND LLSLTKPDLI TDIHRGFLSA GADIIETNTF NSTTISMEDY DMANLSREIN VESAKLARAI CDEFTAKTPE KPRYVAGVLG PTSKTCSISP DVNDPGYRNV TFDKLVTAYV ESTLALMEGG ADLILIETIF DTLNAKAASF GVEEAFEQAG RKLPVMISGT ITDASGRTLS GQTTEAFYNS IRHIKPISIG LNCALGPDLL RQYVEELSRV CETFTSVHPN AGLPNEFGEY DLEAPEMAAE IIDWGKSGFI NIVGGCCGTT PAHIRAFAKG LAGVKPRQLP ELEVRMRLSG LEACNLN // ID F3BQ16_PSEHA Unreviewed; 301 AA. AC F3BQ16; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGI71294.1}; GN ORFNames=PH505_dw00050 {ECO:0000313|EMBL:EGI71294.1}; OS Pseudoalteromonas haloplanktis ANT/505. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=722419 {ECO:0000313|EMBL:EGI71294.1}; RN [1] {ECO:0000313|EMBL:EGI71294.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ANT/505 {ECO:0000313|EMBL:EGI71294.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGI71294.1}. 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; ADOP01000101; EGI71294.1; -; Genomic_DNA. DR RefSeq; WP_002963087.1; NZ_ADOP01000101.1. DR EnsemblBacteria; EGI71294; EGI71294; PH505_dw00050. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EGI71294.1}; KW Transferase {ECO:0000313|EMBL:EGI71294.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 205 205 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 280 280 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 281 281 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 301 AA; 32808 MW; 378BAB5EA13AEB13 CRC64; MKKVTILDGG MGRELKRIGA PFSQPLWSAQ ALIEAPHFVA QAHQGFIDAG AEIITVNSYA CVPFHLGEER YESQGALLAE QAALIANKAA NNAKQNVLVA GSLPPAFGSY RPDLFESERA FTILNTLYNA QNPHVDLWLG ETISSIEEAQ VMASVLKGST KPCYYAFTLS DEVTEQATLR SGELVTDAIT ALLEQQNIAG IFFNCSIPEV IEQALRDTNN VLTKQNKKVT LGAFANSFTP ISSAHKANEA VQDYRDLSPN EYLEFAKQWH SLGANIIGGC CGINPSHIEA LVQWRNAIEK P // ID F3C912_PSESG Unreviewed; 298 AA. AC F3C912; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EGH15716.1}; GN ORFNames=Pgy4_21787 {ECO:0000313|EMBL:EGH15716.1}; OS Pseudomonas savastanoi pv. glycinea str. race 4. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=875330 {ECO:0000313|EMBL:EGH15716.1}; RN [1] {ECO:0000313|EMBL:EGH15716.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Race 4 {ECO:0000313|EMBL:EGH15716.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGH15716.1}. 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; ADWY01001042; EGH15716.1; -; Genomic_DNA. DR EnsemblBacteria; EGH15716; EGH15716; Pgy4_21787. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EGH15716.1}; KW Transferase {ECO:0000313|EMBL:EGH15716.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 207 207 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 298 AA; 31407 MW; DF3D9CCFA2D4E829 CRC64; MTQGTTVILD GGMGRELQRR GAPFRQPEWS ALALSEAPEA VSAVHAAYIE SGAQVITSNS YAVVPFHIGE ERFAREGQAL AALAGRLARE TADASGGRAQ VAGSIPPLFG SYRPDLYKPE LAADVLRPLV AGLSPYVDLW LAETQSCILE AQTIRAGLPN DGKPFWLSFT LQDEDTDEVP RLRSGEPVAD AAKAAAGMGV ATLLFNCSQP EVIGGAIDAA REVFKALNVD IAIGAYANAF PPQPKDAKAN DGLDELREDL DPQGYQQGAA DWVTRGATHI GGCCGIGPEH IAVLSKSL // ID F3DEF2_PSEA0 Unreviewed; 1239 AA. AC F3DEF2; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EGH02695.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGH02695.1}; GN Name=metH {ECO:0000313|EMBL:EGH02695.1}; GN ORFNames=PSYAE_12178 {ECO:0000313|EMBL:EGH02695.1}; OS Pseudomonas amygdali pv. aesculi str. 0893_23. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas amygdali. OX NCBI_TaxID=629258 {ECO:0000313|EMBL:EGH02695.1}; RN [1] {ECO:0000313|EMBL:EGH02695.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=0893_23 {ECO:0000313|EMBL:EGH02695.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGH02695.1}. 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; AEAD01000211; EGH02695.1; -; Genomic_DNA. DR RefSeq; WP_005732817.1; NZ_GL384636.1. DR EnsemblBacteria; EGH02695; EGH02695; PSYAE_12178. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGH02695.1}; KW Transferase {ECO:0000313|EMBL:EGH02695.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1239 AA; 135952 MW; C8BD63CFFEE9F450 CRC64; MSDRSARHQA FLTALKQRIL ILDGGMGTMI QSYRLEEHDY RGKRFADWPS DVKGNNDLLI LTRPDVIGAI EKAYLDAGAD ILETNTFNAT QVSQADYGME SIVYELNVEG ARLARKVADA KTLETPDKPR FVAGVLGPTS RTCSLSPDVN NPGFRNVTFD ELVENYSEAT KGLIEGGADL ILIETIFDTL NAKAAIFAVQ GVFEEVGFEL PIMISGTITD ASGRTLSGQT TEAFWNSISH AKPISVGLNC ALGASELRPY LQELANKANT HVSAHPNAGL PNAFGEYDEL PSQTAKIIEE FAQSGFLNIV GGCCGTTPAH IKAIAEAVSG YAPREIPDIP KACRLSGLEP FTIDRQSLFV NVGERTNITG SARFARLIRE DNYTEALEVA LQQVEAGAQV IDINMDEGML DSKKAMVTFL NLIAGEPDIS RVPIMIDSSK WEVIEAGLKC IQGKGIVNSI SMKEGVEQFI HHARLCKRYG AAVVVMAFDE QGQADTEARK KEICKRSYDI LVNEVGFPPE DIIFDPNIFA IATGIEEHNN YAVDFINACA YIRDELPYAL TSGGVSNVSF SFRGNNPVRE AIHSVFLLHA IRNGLSMGIV NAGQLEIYDQ IPAELRDCVE DVVLNRNPEG TDALLAIADK FKGDGSVKEA ETEEWRSWPV NQRLEHALVK GITTHIVQDT EESRLAFTRP IEVIEGPLMA GMNVVGDLFG AGKMFLPQVV KSARVMKQAV AHLIPFIELE KGDKPEAKGK ILMATVKGDV HDIGKNIVGV VLGCNGYDIV DLGVMVPAEK ILQVARDEKC DIIGLSGLIT PSLDEMVHVA REMQRQDFHL PLMIGGATTS KAHTAVKIEP KYSNDAVIYV TDASRAVGVA TQLLSKELKP AFIEKTRLEY VEVRERTSAR SARTERLSYG AAVAKKPQFD WENYTPAQPT FTGTRVLQDI DLNVLAEYID WTPFFISWDL AGKYPRILTD EVVGEAATAL YADATQMLRK LIDEKLISAR AVFGFWPANQ VNDDDLEVYG DDGKPLAKLH HLRQQTIKPD GKPNFSLADF VAPKDSGLTD YVGGFITTAG IGAEEVAKAY QDKGDDYNSI MVKALADRLA EACAEWLHQQ VRKEYWGYAK DEALDNEALI KEQYMGIRPA PGYPACPDHT EKGTLFALLD PLPEGTPEHT SGKSGVFLTE HYAMFPAAAV SGWYFAHPQA QYFAVGKVDK DQVESYTARK GQDLSVTERW LAPNLGYDE // ID F3DFT7_PSEA0 Unreviewed; 298 AA. AC F3DFT7; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EGH03181.1}; GN ORFNames=PSYAE_14735 {ECO:0000313|EMBL:EGH03181.1}; OS Pseudomonas amygdali pv. aesculi str. 0893_23. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas amygdali. OX NCBI_TaxID=629258 {ECO:0000313|EMBL:EGH03181.1}; RN [1] {ECO:0000313|EMBL:EGH03181.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=0893_23 {ECO:0000313|EMBL:EGH03181.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGH03181.1}. 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; AEAD01000252; EGH03181.1; -; Genomic_DNA. DR RefSeq; WP_005733241.1; NZ_GL384642.1. DR EnsemblBacteria; EGH03181; EGH03181; PSYAE_14735. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EGH03181.1}; KW Transferase {ECO:0000313|EMBL:EGH03181.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 207 207 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 298 AA; 31464 MW; 3AE4452E32B8C027 CRC64; MTQGTTVILD GGMGRELQRR GAPFRQPEWS ALALSEAPEA VSAVHAAYIE SGAQVITSNS YAVVPFHIGE ERFAREGQAL AALAGRLARE SADASGGRAQ VAGSIPPLFG SYRPDLYKPE LAAGVLRPLV AGLSPYVDLW LAETQSCILE AQTIRAGLPN DGKPFWLSFT LQDEDTDEVP RLRSGEPVAD AAKAAAGMGV ATLLFNCSQP EVIGGAIDAA REVFKALNVD IAIGAYANAF PPQPKDAKAN DGLDELREDL DPQGYQQWAA DWVTRGATHI GGCCGIGPEH IAVLSKSL // ID F3DQQ6_PSEA0 Unreviewed; 298 AA. AC F3DQQ6; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EGH07408.1}; GN ORFNames=PSYMP_03021 {ECO:0000313|EMBL:EGH07408.1}; OS Pseudomonas amygdali pv. morsprunorum str. M302280. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas amygdali. OX NCBI_TaxID=629259 {ECO:0000313|EMBL:EGH07408.1}; RN [1] {ECO:0000313|EMBL:EGH07408.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M302280 {ECO:0000313|EMBL:EGH07408.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGH07408.1}. 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; AEAE01000041; EGH07408.1; -; Genomic_DNA. DR RefSeq; WP_005736545.1; NZ_GL384710.1. DR EnsemblBacteria; EGH07408; EGH07408; PSYMP_03021. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EGH07408.1}; KW Transferase {ECO:0000313|EMBL:EGH07408.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 207 207 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 298 AA; 31548 MW; D4FD64F896913FE2 CRC64; MTQRSTVILD GGMGRELQRR GAPFRQPEWS ALALSEAPDA VSAVHAAYIE SGAQVITSNS YAVVPFHIGE ERFAREGQAL AALAGRLARG CADASGGRAL VAGSIPPLFG SYRPDLYQPE LAADVLKPLV AGLSPYVDLW LAETQSCILE AQTIRAGLPA DGKPFWLSFT LQDEDADDVP RLRSGEPVAD AAKAAAEMGV ATLLFNCSQP EVIGGAIDAA REVFKALNVD IAIGAYANAF PPQPKDAKAN DGLDELREDL DPQGYQQWAA DWVKRGATHI GGCCGIGPEH IAVLSQKL // ID F3DU67_PSEA0 Unreviewed; 1239 AA. AC F3DU67; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EGH09261.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGH09261.1}; GN Name=metH {ECO:0000313|EMBL:EGH09261.1}; GN ORFNames=PSYMP_09155 {ECO:0000313|EMBL:EGH09261.1}; OS Pseudomonas amygdali pv. morsprunorum str. M302280. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas amygdali. OX NCBI_TaxID=629259 {ECO:0000313|EMBL:EGH09261.1}; RN [1] {ECO:0000313|EMBL:EGH09261.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M302280 {ECO:0000313|EMBL:EGH09261.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGH09261.1}. 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; AEAE01000187; EGH09261.1; -; Genomic_DNA. DR RefSeq; WP_005737708.1; NZ_GL384714.1. DR EnsemblBacteria; EGH09261; EGH09261; PSYMP_09155. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGH09261.1}; KW Transferase {ECO:0000313|EMBL:EGH09261.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1239 AA; 136070 MW; EE7127CCD29A71A4 CRC64; MSDRSARHQA FITALKQRIL ILDGGMGTMI QSYRLEEEDY RGKRFADWPS DVKGNNDLLI LTRPDVIGAI EKAYLDAGAD ILETNTFNAT QVSQADYGME SIVYELNVEG ARLARKVADA KTLETPDKPR FVAGVLGPTS RTCSLSPDVN NPGYRNVTFD ELVENYTEAT KGLIQGGADL ILIETIFDTL NAKAAIFAVQ GVFEELGFEL PIMISGTITD ASGRTLSGQT TEAFWNSISH AKPVSVGLNC ALGASELRPY LQELANKANT HVSAHPNAGL PNAFGEYDEL PSQTAKIIEE FAQSGFLNIV GGCCGTTPAH IKAIAEAVSG YAPREIPDIP KACRLSGLEP FTIDRQSLFV NVGERTNITG SARFARLIRE DNYTEALEVA LQQVEAGAQV IDINMDEGML DSKKAMVTFL NLIAGEPDIS RVPIMIDSSK WEVIEAGLKC IQGKGIVNSI SMKEGVEQFI HHARLCKRYG AAVVVMAFDE QGQADTEARK KEICKRSYDI LVNEVGFPPE DIIFDPNIFA IATGIEEHNN YAVDFINACA YIRDELPHAL TSGGVSNVSF SFRGNNPVRE AIHSVFLLHA IRNGLSMGIV NAGQLEIYDQ IPAELRDCVE DVVLNRNPEG TDALLAIADK YKGDGSVKEA ETEEWRSWPV NQRLEHALVK GITTHIVQDT EESRLGFTRP IEVIEGPLMS GMNVVGDLFG AGKMFLPQVV KSARVMKQAV AHLIPFIELE KGDKPEAKGK ILMATVKGDV HDIGKNIVGV VLGCNGYDIV DLGVMVPAEK ILQVARDEKC DIIGLSGLIT PSLDEMVHVA REMQRQDFHL PLMIGGATTS KAHTAVKIEP KYSNDAVIYV TDASRAVGVA TQLLSKELKP AFIEKTRLEY VEVRERTSAR SARTERLSYG AAVAKKPKFD WESYTPAKPT FTGTRVLHDI DLNVLADYID WTPFFISWDL AGKYPRILTD EVVGEAATAL FEDARQMLRK LIDEKLISAR AVFGFWPTNQ VNDDDLEVYG EDGKPLAKLH HLRQQTIKPD GKPNFSLADF VAPKDSGLTD YIGGFITTAG IGAEEVAKAY QDNGDDYNSI MVKALADRLA EACAEWLHQQ VRKDYWGYAK DEALDNEALI KEQYMGIRPA PGYPACPDHT EKGTLFALLD PLPEGTPEHT PGKSGVFLTE HYAMFPAAAV SGWYFAHPQA QYFAVGKVDK DQVESYTARK GQDLSVTERW LAPNLGYDE // ID F3EB71_PSEAV Unreviewed; 1239 AA. AC F3EB71; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EGH83404.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGH83404.1}; GN Name=metH {ECO:0000313|EMBL:EGH83404.1}; GN ORFNames=PLA107_09763 {ECO:0000313|EMBL:EGH83404.1}; OS Pseudomonas amygdali pv. lachrymans str. M301315. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas amygdali. OX NCBI_TaxID=629260 {ECO:0000313|EMBL:EGH83404.1, ECO:0000313|Proteomes:UP000006426}; RN [1] {ECO:0000313|EMBL:EGH83404.1, ECO:0000313|Proteomes:UP000006426} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M301315 {ECO:0000313|EMBL:EGH83404.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGH83404.1}. 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; AEAF01000095; EGH83404.1; -; Genomic_DNA. DR RefSeq; WP_005743588.1; NZ_GG775129.1. DR EnsemblBacteria; EGH83404; EGH83404; PLA107_09763. DR Proteomes; UP000006426; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006426}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGH83404.1}; KW Transferase {ECO:0000313|EMBL:EGH83404.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1239 AA; 135956 MW; 295F1AF808A25DB8 CRC64; MSDRSARHQA FLTALKQRIL ILDGGMGTMI QSYRLEEQDY RGKRFADWPS DVKGNNDLLI LTRPDVIGAI EKAYLDAGAD ILETNTFNAT QVSQADYGME SIVYELNVEG ARLARKVADA KTLETPDKPR FVAGVLGPTS RTCSLSPDVN NPGYRNVTFD ELVENYSEAT KGLIEGGADL ILIETIFDTL NAKAAIFAVQ GVFEEVGFEL PIMISGTITD ASGRTLSGQT TEAFWNSISH AKPISVGLNC ALGASELRPY LQELANKANT HVSAHPNAGL PNAFGEYDEL PSQTAKIIEE FAQSGFLNIV GGCCGTTPAH IKAIAEAVSG YAPREIPNIP KACRLSGLEP FTIDRQSLFV NVGERTNITG SARFARLIRE DNYTEALEVA LQQVEAGAQV IDINMDEGML DSKKAMVTFL NLIAGEPDIS RVPIMIDSSK WEVIEAGLKC IQGKGIVNSI SMKEGVEQFI HHARLCKRYG AAVVVMAFDE QGQADTEARK KEICKRSYDI LVNEVGFPPE DIIFDPNIFA IATGIEEHNN YAVDFINACA YIRDELPYAL TSGGVSNVSF SFRGNNPVRE AIHSVFLLHA IRNGLSMGIV NAGQLEIYDQ IPAELRDCVE DVVLNRNAEG TDALLAIADK FKGDGSVKEA ETEEWRSWPV NQRLEHALVK GITTHIVQDT EESRLAFTRP IEVIEGPLMA GMNVVGDLFG AGKMFLPQVV KSARVMKQAV AHLIPFIELE KGDKPEAKGK ILMATVKGDV HDIGKNIVGV VLGCNGYDIV DLGVMVPAEK ILQVARDEKC DIIGLSGLIT PSLDEMVHVA REMQRQDFHL PLMIGGATTS KAHTAVKIEP KYSNDAVIYV TDASRAVGVA TQLLSKELKP AFIEKTRLEY VEVRERTSAR SARTERLSYG AAVAKKPQFD WENYTPAQPT FTGTRVLQDI DLNVLAEYID WTPFFISWDL AGKYPRILTD EVVGEAATAL YADATQMLRK LIDEKLISAR AVFGFWPANQ VNDDDLEVYG DDGKPLAKLH HLRQQTIKPD GKPNFSLADF VAPKDSGLTD YIGGFITTAG IGAEEVAKAY QDKGDDYNSI MVKALADRLA EACAEWLHQQ VRKEYWGYAK DEALDNEALI KEQYMGIRPA PGYPACPDHT EKGTLFALLD PLPEGTPEHT PGKSGVFLTE HYAMFPAAAV SGWYFAHPQA QYFAVGKVDK DQVESYTARK GQDLSVTERW LAPNLGYDE // ID F3EKH6_PSEAV Unreviewed; 298 AA. AC F3EKH6; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EGH86682.1}; GN ORFNames=PLA107_26380 {ECO:0000313|EMBL:EGH86682.1}; OS Pseudomonas amygdali pv. lachrymans str. M301315. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas amygdali. OX NCBI_TaxID=629260 {ECO:0000313|EMBL:EGH86682.1, ECO:0000313|Proteomes:UP000006426}; RN [1] {ECO:0000313|EMBL:EGH86682.1, ECO:0000313|Proteomes:UP000006426} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M301315 {ECO:0000313|EMBL:EGH86682.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGH86682.1}. 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; AEAF01000356; EGH86682.1; -; Genomic_DNA. DR RefSeq; WP_005746207.1; NZ_GG775155.1. DR EnsemblBacteria; EGH86682; EGH86682; PLA107_26380. DR Proteomes; UP000006426; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006426}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EGH86682.1}; KW Transferase {ECO:0000313|EMBL:EGH86682.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 207 207 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 298 AA; 31551 MW; ACD911AD0F25584C CRC64; MTQGTTVILD GGMGRELQRR GAPFRQPEWS ALALSEAPEA VSAVHAAYIE SGAQVITSNS YAVVPFHIGE ERFAREGQAL AALAGRLARE TADASAGRAQ VAGSIPPLFG SYRPDLYKPE LAADVLRPLV AGLSPYVDLW LAETQSCLLE AQTIRAGLPN DGKPFWLSFT LKDEDTDEVP RLRSGEPVAD AAKAAAGMGV ATLLFNCSQP EVIGGAIDAA REVFKALNVD IAIGAYANAF PPQPKDAKAN DGLDELREDL DPQGYQQWAA DWVTRGATHI GGCCGIGPEH IAVLSKSL // ID F3ERB7_PSEA0 Unreviewed; 298 AA. AC F3ERB7; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EGH20499.1}; GN ORFNames=PSYMO_02959 {ECO:0000313|EMBL:EGH20499.1}; OS Pseudomonas amygdali pv. mori str. 301020. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas amygdali. OX NCBI_TaxID=629261 {ECO:0000313|EMBL:EGH20499.1}; RN [1] {ECO:0000313|EMBL:EGH20499.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=301020 {ECO:0000313|EMBL:EGH20499.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGH20499.1}. 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; AEAG01000122; EGH20499.1; -; Genomic_DNA. DR RefSeq; WP_005753006.1; NZ_GL384774.1. DR EnsemblBacteria; EGH20499; EGH20499; PSYMO_02959. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EGH20499.1}; KW Transferase {ECO:0000313|EMBL:EGH20499.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 207 207 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 298 AA; 31474 MW; 7C8A3F6FB0EFB196 CRC64; MTQGTTVILD GGMGRELQRR GAPFRQPEWS ALALSEAPEA VSAVHAAYIE SGAQVITSNS YAVVPFHIGE ERFAREGQAL AALAGRLARE TADAFGGRAQ VAGSIPPLFG SYRPDLYKPE LAADVLRPLV AGLSPYVDLW LAETQSCILE AQTICAGLPN DGKPFWLSFT LQDEDTDEVP RLRSGESVAD AAKAAAGMGV ATLLFNCSQP EVIGGAIDAA REVFKALDVD IAIGAYANAS PPQPKDAKAN DGLDELREDL DPQGYQQWAA DWVTRGATHI GGCCGLGPEH IAVLSKSL // ID F3EZQ4_PSEA0 Unreviewed; 1239 AA. AC F3EZQ4; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EGH23436.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGH23436.1}; GN Name=metH {ECO:0000313|EMBL:EGH23436.1}; GN ORFNames=PSYMO_19013 {ECO:0000313|EMBL:EGH23436.1}; OS Pseudomonas amygdali pv. mori str. 301020. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas amygdali. OX NCBI_TaxID=629261 {ECO:0000313|EMBL:EGH23436.1}; RN [1] {ECO:0000313|EMBL:EGH23436.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=301020 {ECO:0000313|EMBL:EGH23436.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGH23436.1}. 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; AEAG01000735; EGH23436.1; -; Genomic_DNA. DR RefSeq; WP_005757274.1; NZ_GL384788.1. DR EnsemblBacteria; EGH23436; EGH23436; PSYMO_19013. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGH23436.1}; KW Transferase {ECO:0000313|EMBL:EGH23436.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1239 AA; 135996 MW; 5215FBD1ECE35EA3 CRC64; MSDRSARHQA FLTALKQRIL ILDGGMGTMI QSYRLEEQDY RGKRFADWPS DVKGNNDLLI LTRPDVIGAI EKAYLDAGAD ILETNTFNAT QVSQADYGME SIVYELNLEG ARLARKVADA KTLETPDKPR FVAGVLGPTS RTCSLSPDVN NPGYRNVTFD ELVENYSEAT KGLIEGGADL ILIETIFDTL NAKAAIFAVQ GVFEEVGFEL PIMISGTITD ASGRTLSGQT TEAFWNSISH AKPISVGLNC ALGASELRPY LQELANKANT HVSAHPNAGL PNAFGEYDEL PSQTAKIIEE FAQSGFLNIV GGCCGTTPAH IKAIAEAVWG YAPREIPDIP KACRLSGLEP FTIDRQSLFV NVGERTNITG SARSARLIRE DNYTEALEVA LQQVEAGAQV IDINMDEGML DSKKAMVTFL NLIAGEPDIS RVPIMIDSSK WEVIEAGLKC IQGKGIVNSI SMKEGVEQFI HHARLCKRYG AAVVVMAFDE QGQADTEARK KEICKRSYDI LVNEVGFPPE DIIFDPNIFA IATGIEEHNN YAVDFINACA YIRDELPYAL TSGGVSNVSF SFRGNNPVRE AIHSVFLLHA IRNGLSMGIV NAGQLEIYDQ IPAELRDCVE DVVLNRNAEG TDALLAIADK FKGDGSVKEA ETEEWRSWPV NQRLEHALVK GITTHIVQDT EESRLAFTRP IEVIEGPLMA GMNVVGDLFG AGKMFLPQVV KSARVMKQAV AHLIPFIELE KGDKPEAKGK ILMATVKGDV HDIGKNIVGV VLGCNGYDIV DLGVMVPAEK ILQVARDEKC DIIGLSGLIT PSLDEMVHVA REMQRQDFHL PLMIGGATTS KAHTAVKIEP KYSNDAVIYV TDASRAVGVA TQLLSKELKP AFIEKTRLEY VEVRERTSAR SARTERLSYG AGVAKKPQFD WENYTPAQPT FTGTRVLQDI DLNVLAEYID WTPFFISWDL AGKYPRILTD EVVGEAATAL YADATQMLRK LIDEKLISAR AVFGFWPANQ VNDDDLEVYG DDGKPLAKLH HLRQQTIKPD GKPNFSLADF VAPKDSGLTD YIGGFITTAG IGAEEVAKAY QDKGDDYNSI MVKALADRLA EACAEWLHQQ VRKEYWGYAK DEALDNEALI KEQYMGIRPA PGYPACPDHT EKGTLFALLD PLPEGTPEHT PGKSGVFLTE HYAMFPAAAV SGWYFAHPQA QYFAVGKVDK DQVESYTARK GQDLSVTERW LAPNLGYDE // ID F3FPY0_PSESX Unreviewed; 298 AA. AC F3FPY0; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGH32272.1}; GN ORFNames=PSYJA_26265 {ECO:0000313|EMBL:EGH32272.1}; OS Pseudomonas syringae pv. japonica str. M301072. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae. OX NCBI_TaxID=629262 {ECO:0000313|EMBL:EGH32272.1}; RN [1] {ECO:0000313|EMBL:EGH32272.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M301072 {ECO:0000313|EMBL:EGH32272.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGH32272.1}. 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; AEAH01001189; EGH32272.1; -; Genomic_DNA. DR EnsemblBacteria; EGH32272; EGH32272; PSYJA_26265. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EGH32272.1}; KW Transferase {ECO:0000313|EMBL:EGH32272.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 207 207 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 298 AA; 31640 MW; 01E6AD91E2E028B4 CRC64; MKQGTTVILD GGMGRELQRR GAPFRQPEWS ALALSEAPEA VSAVHAAYIE SGAQVITSNS YAVVPFHIGE ERFAREGQAL AALAGQLARE SADASGGRAR VAGSIPPLFG SYRPDLYQPQ LAADVLKPLV AGLSPYVDLW LAETQSCILE AQTIRAGLPN DGKPFWLSFT LQDEDTDEVP RLRSGEPVAD AARAAAAMGV ATLLFNCSQP EVIGGAIDAA REVFTSLNVD IAIGAYANAF PPQPKDATAN DGLDELREDL DPQGYQQWAA DWVKRGATHI GGCCGIGPEH IAVLFRSL // ID F3GCY0_PSESJ Unreviewed; 298 AA. AC F3GCY0; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGH44930.1}; GN ORFNames=PSYPI_22212 {ECO:0000313|EMBL:EGH44930.1}; OS Pseudomonas syringae pv. pisi str. 1704B. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae. OX NCBI_TaxID=629263 {ECO:0000313|EMBL:EGH44930.1}; RN [1] {ECO:0000313|EMBL:EGH44930.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=1704B {ECO:0000313|EMBL:EGH44930.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGH44930.1}. 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; AEAI01001125; EGH44930.1; -; Genomic_DNA. DR EnsemblBacteria; EGH44930; EGH44930; PSYPI_22212. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EGH44930.1}; KW Transferase {ECO:0000313|EMBL:EGH44930.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 207 207 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 298 AA; 31565 MW; 6B4DDD8D93A46DB5 CRC64; MKQGTTVILD GGMGRELQRR GAPFRQPEWS ALALSEAPEA VSAVHAAYIE SGAQVITSNS YAVVPFHIGE ERFAREGQAL AALAGQLARE SADASGGRAR VAGSIPPLFG SYRPDLYQPQ LAADVLKPLV AGLSPYVDLW LAETQSCILE AQTIRAGLPN DGKPFWLSFT LQDEDTDEVP RLRSGEPVAD AARAAAAMGV ATLLFNCSQP EVIGGAIDAA RDVFTSLNVD IAIGAYANAF PPQPKDATAN DGLDELREDL DPQGYQQWAA DWVKRGATHI GGCCGIGPEH IAVLSRSL // ID F3GH18_PSESJ Unreviewed; 840 AA. AC F3GH18; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 01-APR-2015, entry version 20. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EGH46368.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGH46368.1}; DE Flags: Fragment; GN Name=metH {ECO:0000313|EMBL:EGH46368.1}; GN ORFNames=PSYPI_30301 {ECO:0000313|EMBL:EGH46368.1}; OS Pseudomonas syringae pv. pisi str. 1704B. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae. OX NCBI_TaxID=629263 {ECO:0000313|EMBL:EGH46368.1}; RN [1] {ECO:0000313|EMBL:EGH46368.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=1704B {ECO:0000313|EMBL:EGH46368.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGH46368.1}. 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; AEAI01001585; EGH46368.1; -; Genomic_DNA. DR EnsemblBacteria; EGH46368; EGH46368; PSYPI_30301. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGH46368.1}; KW Transferase {ECO:0000313|EMBL:EGH46368.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. FT NON_TER 840 840 {ECO:0000313|EMBL:EGH46368.1}. SQ SEQUENCE 840 AA; 91496 MW; 9795A36F42F38419 CRC64; MSDRSARHQA FLTALKQRIL ILDGGMGTMI QSYRLEEQDY RGKRFADWPS DVKGNNDLLI LTRPDVIGAI EKAYLDAGAD ILETNTFNAT QVSQADYGME SIVYELNVEG ARLARKVADA KTLETPDKPR FVAGVLGPTS RTCSLSPDVN NPGYRNVTFD ELVENYTEAT KGLIEGGADL ILIETIFDTL NAKAAIFAVQ GVFEEVGFEL PIMISGTITD ASGRTLSGQT TKAFWNSISH AKPISVGLNC ALGASELRPY LQELANKANT HVSAHPNAGL PNAFGEYDEL PSQTAKIIEE FAQSGFLNIV GGCCGTTPAH IKAIAEAVSG YAPREIPDIP KACRLSGLEP FTIDRQSLFV NVGERTNITG SARFARLIRE DNYTEALEVA LQQVEAGAQV IDINMDEGML DSKKAMVTFL NLIAGEPDIS RVPIMIDSSK WEVIEAGLKC IQGKGIVNSI SMKEGVEQFI HHARLCKRYG AAVVVMAFDE QGQADTEARK KEICKRSYDI LVNEVGFPPE DIIFDPNIFA IATGIEEHNN YAVDFINACA YIRDELPYAL TSGGVSNVSF SFRGNNPVRE AIHSVFLLHA IRNGLSMGIV NAGQLEIYDQ IPAELRDCVE DVVLNRNPEG TDALLAIADK FKGDGSVKEA ETEEWRSWPV NQRLEHALVK GITTHIVQDT EESRLGFARP IEVIEGPLMA GMNVVGDLFG AGKMFLPQVV KSARVMKQAV AHLIPFIELE KGDKPEAKGK ILMATVKGDV HDIGKNIVGV VLGCNGYDIV DLGVMVPAEK ILQVARDEKC DIIGLSGLIT PSLDEMVHVA REMQRQDFHL PLMIGGATTS // ID F3GW80_PSESX Unreviewed; 298 AA. AC F3GW80; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGH51333.1}; GN ORFNames=PSYCIT7_06640 {ECO:0000313|EMBL:EGH51333.1}; OS Pseudomonas syringae Cit 7. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae. OX NCBI_TaxID=629264 {ECO:0000313|EMBL:EGH51333.1}; RN [1] {ECO:0000313|EMBL:EGH51333.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Cit 7 {ECO:0000313|EMBL:EGH51333.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGH51333.1}. 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; AEAJ01000223; EGH51333.1; -; Genomic_DNA. DR RefSeq; WP_003365569.1; NZ_GL385012.1. DR EnsemblBacteria; EGH51333; EGH51333; PSYCIT7_06640. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EGH51333.1}; KW Transferase {ECO:0000313|EMBL:EGH51333.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 207 207 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 298 AA; 31527 MW; AAF15BD4AD983C38 CRC64; MTQGTTVILD GGMGRELQRR GAPFRQPEWS ALALSEAPEA VSAVHAAYIE SGAQVITSNS YAVVPFHIGE ERFAREGQAL AALAGQLARE SADASGGRAR VAGSIPPLFG SYRPDLYQPE QAADVLKPLV AGLSPYVDLW LAETQSCILE AQTIRAGLPN DGKPFWLSFT LQDEDTDETP RLRSGEPVAD AARAAAAMGV ATLLFNCSQP EVIGGAIDAA REVFKSLDVD IAIGAYANAF PPQPKDATAN DGLDELREDL DPQGYQRWAA DWVKRGATHI GGCCGIGPEH IAVLSGSL // ID F3H2S3_PSESX Unreviewed; 1239 AA. AC F3H2S3; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EGH53636.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGH53636.1}; GN Name=metH {ECO:0000313|EMBL:EGH53636.1}; GN ORFNames=PSYCIT7_18756 {ECO:0000313|EMBL:EGH53636.1}; OS Pseudomonas syringae Cit 7. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae. OX NCBI_TaxID=629264 {ECO:0000313|EMBL:EGH53636.1}; RN [1] {ECO:0000313|EMBL:EGH53636.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Cit 7 {ECO:0000313|EMBL:EGH53636.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGH53636.1}. 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; AEAJ01000633; EGH53636.1; -; Genomic_DNA. DR RefSeq; WP_003369393.1; NZ_GL385018.1. DR EnsemblBacteria; EGH53636; EGH53636; PSYCIT7_18756. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGH53636.1}; KW Transferase {ECO:0000313|EMBL:EGH53636.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1239 AA; 135739 MW; ABA953432B635711 CRC64; MSDRSARHQA FLTALKQRIL ILDGGMGTMI QSYRLEEQDY RGKRFADWPS DVKGNNDLLI LTRPDVIGAI EKAYLDAGAD ILETNTFNAT QVSQADYGME SIVYELNVEG ARLARKVADA KTLETPDKPR FVAGVLGPTS RTCSLSPDVN NPGYRNVTFD ELVENYTEAT KGLIEGGADL ILIETIFDTL NAKAAIFAVQ GVFEEVGFEL PIMISGTITD ASGRTLSGQT TGAFWNSISH AKPISVGLNC ALGASELRPY LQELANKANT HVSAHPNAGL PNAFGEYDEL PSQTAKIIEE FAQSGFLNIV GGCCGTTPAH IKAIAEAVSG YAPREIPDIP KACRLSGLEP FTIDRQSLFV NVGERTNITG SARSARLIRE DNYTEALEVA LQQVEAGAQV IDINMDEGML DSKKAMVTFL NLIAGEPDIS RVPIMIDSSK WEVIEAGLKC IQGKGIVNSI SMKEGVEQFI HHARLCKRYG AAVVVMAFDE QGQADTEARK KEICKRSYDI LVNEVGFPPE DIIFDPNIFA IATGIEEHNN YAVDFINACA YIRDELPYAL TSGGVSNVSF SFRGNNPVRE AIHSVFLLHA IRNGLSMGIV NAGQLEIYDQ IPAELRDCVE DVVLNRNPEG TDALLAIADK FKGDGSAKEA ETEEWRSWPV NQRLEHALVK GITTHIVQDT EESRLAFTRP IEVIEGPLMA GMNVVGDLFG AGKMFLPQVV KSARVMKQAV AHLIPFIELE KGDKPEAKGK ILMATVKGDV HDIGKNIVGV VLGCNGYDIV DLGVMVPAEK ILQVARDEKC DIIGLSGLIT PSLDEMVHVA REMQRQDFHL PLMIGGATTS KAHTAVKIEP KYSNDAVIYV TDASRAVGVA TQLLSKELKP AFIEKTRLEY VEVRERTSAR SARTERLSYG AAVAKKPQFD WENYTPAQPT FTGTRVLQDI DLNVLAEYID WTPFFISWDL AGKFPRILTD EVVGEAATAL YADATQMLRK LIDENLISAR AVFGFWPANQ VNDDDLEVYG DDGKPLARLH HLRQQTIKPD GKPNFSLADF VAPKDSGLTD YIGGFIATAG IGAEEVAKAY QDKGDDYNSI MVKALADRLA EACAEWLHQQ VRKEYWGYAQ DEALDNEALI KEQYMGIRPA PGYPACPDHT EKGTLFALLD PLPEGSAEHT AGKSGVFLTE HYAMFPAAAV SGWYFAHPQA QYFAVGKVDK DQVESYTARK GQDLSVTERW LAPNLGYDE // ID F3HPD6_PSEYM Unreviewed; 1239 AA. AC F3HPD6; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EGH61206.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGH61206.1}; GN Name=metH {ECO:0000313|EMBL:EGH61206.1}; GN ORFNames=PMA4326_20627 {ECO:0000313|EMBL:EGH61206.1}; OS Pseudomonas syringae pv. maculicola str. ES4326. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=629265 {ECO:0000313|EMBL:EGH61206.1}; RN [1] {ECO:0000313|EMBL:EGH61206.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ES4326 {ECO:0000313|EMBL:EGH61206.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGH61206.1}. 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; AEAK01000391; EGH61206.1; -; Genomic_DNA. DR RefSeq; WP_007251832.1; NZ_GL385045.1. DR EnsemblBacteria; EGH61206; EGH61206; PMA4326_20627. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGH61206.1}; KW Transferase {ECO:0000313|EMBL:EGH61206.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1239 AA; 136019 MW; BF676029573B33AB CRC64; MSDRSARHQA FLDALKQRIL ILDGGMGTMI QSYRLEEQDY RGKRFADWPS DVKGNNDLLI LTRPDVIGAI EKAYLDAGAD ILETNTFNAT QVSQADYGME SIVYELNVEG ARLARKVADA KTLETPDKPR FVAGVLGPTS RTCSLSPDVN NPGYRNVTFD ELVENYTEAT KGLIEGGADL ILIETIFDTL NAKAAIFAVQ GVFEELGVEL PIMISGTITD ASGRTLSGQT TEAFWNSISH AKPISVGLNC ALGASELRPY LQELANKANT HVSAHPNAGL PNAFGEYDEL PSQTAKIIEE FAQSGFLNIV GGCCGTTPAH IKAIAEAVSG YAPREIPDIP KACRLSGLEP FTIDRQSLFV NVGERTNITG SARFARLIRE DNYTEALEVA LQQVEAGAQV IDINMDEGML DSKKAMVTFL NLIAGEPDIS RVPIMIDSSK WEVIEAGLKC IQGKGIVNSI SMKEGVEQFI HHARLCKRYG AAVVVMAFDE QGQADTEARK KEICKRSYDI LVDEVGFPPE DIIFDPNIFA IATGIEEHNN YAVDFINACA YIRDELPYAL TSGGVSNVSF SFRGNNPVRE AIHSVFLLHA IRNGLSMGIV NAGQLEIYDQ IPAELRDCVE DVVLNRTADG TDALLAIADK YKGDGSVKEA ETEEWRSWPV NQRLEHALVK GITTHIVQDT EESRLGFTRP IEVIEGPLMA GMNVVGDLFG AGKMFLPQVV KSARVMKQAV AHLIPFIELE KGDKPEAKGK ILMATVKGDV HDIGKNIVGV VLGCNGYDIV DLGVMVPAEK ILQVARDEKC DIIGLSGLIT PSLDEMVHVA REMQRQDFHL PLMIGGATTS KAHTAVKIEP KYSNDAVIYV TDASRAVGVA TQLLSKELKP AFIEKTRLEY IEVRERTSAR SARTERLSYG AAVAKKPQFD WENYTPAKPT FTGTRVLQDI DLNVLAEYID WTPFFISWDL AGKYPRILTD EVVGEAATAL FEDARQMLRK LIDEKLISAR AVFGFWPANQ VNDDDLQVYA DDGKPLATLH HLRQQTIKPD GKPNLSLADF VAPKNSGLTD YIGGFITTAG IGAEEIAKAY QDKGDDYNSI MVKALADRLA EACAEWLHQQ VRKEYWGYAK DEALDNESLI KEQYMGIRPA PGYPACPDHT EKGTLFALLD PLPEGTPEHT PGKSGVFLTE HYAMFPAAAV SGWYFAHPQA QYFAVGKVDK DQVESYTARK GQDLSVTERW LAPNLGYDE // ID F3HRP6_PSEYM Unreviewed; 298 AA. AC F3HRP6; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGH62016.1}; GN ORFNames=PMA4326_24715 {ECO:0000313|EMBL:EGH62016.1}; OS Pseudomonas syringae pv. maculicola str. ES4326. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=629265 {ECO:0000313|EMBL:EGH62016.1}; RN [1] {ECO:0000313|EMBL:EGH62016.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ES4326 {ECO:0000313|EMBL:EGH62016.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGH62016.1}. 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; AEAK01000480; EGH62016.1; -; Genomic_DNA. DR RefSeq; WP_007252594.1; NZ_GL385050.1. DR EnsemblBacteria; EGH62016; EGH62016; PMA4326_24715. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EGH62016.1}; KW Transferase {ECO:0000313|EMBL:EGH62016.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 207 207 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 298 AA; 31534 MW; 46183E86857696DE CRC64; MTQGTTVILD GGMGRELQRR GAPFRQPEWS ALALSEAPEA VSAVHAAYIE SGAQVITSNS YAVVPFHIGE ERFAREGQAL AALAGRLARE SADASNGRAR VAGSIPPLFG SYRPDLYKPE LAADVLKPLV AGLAPYVDLW LAETQSCILE AQTIRAGLPA DGKPFWLSFT LQDEDTDEVP RLRSGEPVAD AARAAAAMGV ATLLFNCSQP EVIGGAIDAA REVFESLGVA IALGAYANAF PPQPKDAKAN DGLDELREDL DPQGYQQWAA DWVKRGATHI GGCCGIGPEH IAVLSRSL // ID F3IBR7_PSEAV Unreviewed; 1239 AA. AC F3IBR7; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EGH94405.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGH94405.1}; GN Name=metH {ECO:0000313|EMBL:EGH94405.1}; GN ORFNames=PLA106_00580 {ECO:0000313|EMBL:EGH94405.1}; OS Pseudomonas amygdali pv. lachrymans str. M302278. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas amygdali. OX NCBI_TaxID=629267 {ECO:0000313|EMBL:EGH94405.1}; RN [1] {ECO:0000313|EMBL:EGH94405.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M302278 {ECO:0000313|EMBL:EGH94405.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGH94405.1}. 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; AEAM01000018; EGH94405.1; -; Genomic_DNA. DR RefSeq; WP_005762566.1; NZ_GL385192.1. DR EnsemblBacteria; EGH94405; EGH94405; PLA106_00580. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGH94405.1}; KW Transferase {ECO:0000313|EMBL:EGH94405.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1239 AA; 136096 MW; 5AB63B7DD7093C5E CRC64; MSDRSARHQA FITALKQRIL ILDGGMGTMI QSYRLEEEDY RGKRFADWPS DVKGNNDLLI LTRPDVIGAI EKAYLDAGAD ILETNTFNAT QVSQADYGME SIVYELNVEG ARLARKVADA KTLETPDKPR FVAGVLGPTS RTCSLSPDVN NPGYRNVTFD ELVENYTEAT KGLIEGGADL ILIETIFDTL NAKAAIFAVQ GVFEELGFEL PIMISGTITD ASGRTLSGQT TEAFWNSISH AKPVSVGLNC ALGASELRPY LQELANKANT HVSAHPNAGL PNAFGEYDEL SSQTAKIIEE FAQSGFLNIV GGCCGTTPEH IKAIAEAVSG YAPREIPDIP KACRLSGLEP FTIDRQSLFV NVGERTNITG SARFARLIRE DNYTEALEVA LQQVEAGAQV IDINMDEGML DSKKAMVTFL NLIAGEPDIS RVPIMIDSSK WEVIEAGLKC IQGKGIVNSI SMKEGVEQFI HHARLCKRYG AAVVVMAFDE QGQADTEARK KEICKRSYDI LVNEVGFPPE DIIFDPNIFA IATGIEEHNN YAVDFINACA YIRDELPHAL TSGGVSNVSF SFRGNNPVRE AIHSVFLLHA IRNGLSMGIV NAGQLEIYDQ IPAELRDCVE DVVLNRNPEG TDALLAIADK YKGDGSVKEA ETEEWRSWPV NQRLEHALVK GITTHIVQDT EESRLGFTRP IEVIEGPLMS GMNVVGDLFG AGKMFLPQVV KSARVMKQAV AHLIPFIELE KGDKPEAKGK ILMATVKGDV HDIGKNIVGV VLGCNGYDIV DLGVMVPAEK ILQVARDEKC DIIGLSGLIT PSLDEMVHVA REMQRQDFHL PLMIGGATTS KAHTAVKIEP KYSNDAVIYV TDASRAVGVA TQLLSKELKP AFIEKTRLEY VEVRERTSAR SARTERLSYG AAVAKKPKFD WESYTPAKPT FTGTRVLQDI DLNVLADYID WTPFFISWDL AGKYPRILTD EVVGEAATAL FEDAQQMLRK LIDEKLISAR AVFGFWPTNQ INDDDLEVYG EDGKPLAKLH HLRQQTIKPD GKPNFSLADF VAPKDSGLTD YIGGFITTAG IGAEEVAKAY QDNGDDYNSI MVKALADRLA EACAEWLHQQ VRKDYWGYAK DEALDNEALI KEQYMGIRPA PGYPACPDHT EKGTLFALLD PLPEGTPEHT PGKSGVFLTE HYAMFPAAAV SGWYFAHPQA QYFAVGKVDK DQVESYTARK GQDLSVTERW LAPNLGYDE // ID F3ILY6_PSEAV Unreviewed; 298 AA. AC F3ILY6; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EGH98152.1}; GN ORFNames=PLA106_18829 {ECO:0000313|EMBL:EGH98152.1}; OS Pseudomonas amygdali pv. lachrymans str. M302278. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas amygdali. OX NCBI_TaxID=629267 {ECO:0000313|EMBL:EGH98152.1}; RN [1] {ECO:0000313|EMBL:EGH98152.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M302278 {ECO:0000313|EMBL:EGH98152.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGH98152.1}. 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; AEAM01000339; EGH98152.1; -; Genomic_DNA. DR RefSeq; WP_005768811.1; NZ_GL385215.1. DR ProteinModelPortal; F3ILY6; -. DR EnsemblBacteria; EGH98152; EGH98152; PLA106_18829. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EGH98152.1}; KW Transferase {ECO:0000313|EMBL:EGH98152.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 207 207 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 298 AA; 31533 MW; 05756320D2F4984D CRC64; MTQRSTVILD GGMGRELQRR GAPFRQPEWS ALALSEAPDA VSAVHAAYIE SGAQVITSNS YAVVPFHIGE ERFAREGQAL AALAGQLARG SADASGGRAL VAGSIPPLFG SYRPDLYQPE LAADVLKPLV AGLSPYVDLW LAETQSCILE AQTIRAGLPA DGKPFWLSFT LQDEDTDDVP RLRSGEPVAD AAKAAAEMGV ATLLFNCSQP EVIGAAIDAA REVFNALNVD IAIGAYANAF PPQPKDAKAN DGLDELREDL DPQGYQQWAA DWVKRGATHI GGCCGIGPEH IAVLSQKL // ID F3IU48_PSEAP Unreviewed; 298 AA. AC F3IU48; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGH75669.1}; GN ORFNames=PSYAP_02922 {ECO:0000313|EMBL:EGH75669.1}; OS Pseudomonas syringae pv. aptata str. DSM 50252. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae. OX NCBI_TaxID=629268 {ECO:0000313|EMBL:EGH75669.1}; RN [1] {ECO:0000313|EMBL:EGH75669.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 50252 {ECO:0000313|EMBL:EGH75669.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGH75669.1}. 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; AEAN01000126; EGH75669.1; -; Genomic_DNA. DR EnsemblBacteria; EGH75669; EGH75669; PSYAP_02922. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EGH75669.1}; KW Transferase {ECO:0000313|EMBL:EGH75669.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 207 207 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 298 AA; 31579 MW; 01E6AD8D92E028B4 CRC64; MKQGTTVILD GGMGRELQRR GAPFRQPEWS ALALSEAPEA VSAVHAAYIE SGAQVITSNS YAVVPFHIGE ERFAREGQAL AALAGQLARE SADASGGRAR VAGSIPPLFG SYRPDLYQPQ LAADVLKPLV AGLSPYVDLW LAETQSCILE AQTIRAGLPN DGKPFWLSFT LQDEDTDEVP RLRSGEPVAD AARAAAAMGV ATLLFNCSQP EVIGGAIDAA REVFTSLNVD IAIGAYANAF PPQPKDATAN DGLDELREDL DPQGYQQWAA DWVKRGATHI GGCCGIGPEH IAVLSRSL // ID F3J7A3_PSEAP Unreviewed; 897 AA. AC F3J7A3; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 01-APR-2015, entry version 20. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EGH80279.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGH80279.1}; DE Flags: Fragment; GN Name=metH {ECO:0000313|EMBL:EGH80279.1}; GN ORFNames=PSYAP_27069 {ECO:0000313|EMBL:EGH80279.1}; OS Pseudomonas syringae pv. aptata str. DSM 50252. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae. OX NCBI_TaxID=629268 {ECO:0000313|EMBL:EGH80279.1}; RN [1] {ECO:0000313|EMBL:EGH80279.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 50252 {ECO:0000313|EMBL:EGH80279.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGH80279.1}. 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; AEAN01001155; EGH80279.1; -; Genomic_DNA. DR EnsemblBacteria; EGH80279; EGH80279; PSYAP_27069. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGH80279.1}; KW Transferase {ECO:0000313|EMBL:EGH80279.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 203 203 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 266 266 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 267 267 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 714 714 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. FT NON_TER 1 1 {ECO:0000313|EMBL:EGH80279.1}. FT NON_TER 897 897 {ECO:0000313|EMBL:EGH80279.1}. SQ SEQUENCE 897 AA; 97607 MW; 715E4F1C8C1344DD CRC64; WPSDVKGNND LLILTRPDVI GAIEKAYLDA GADILETNTF NATQVSQADY GMESIVYELN VEGARLARKV ADAKTLETPD KPRFVAGVLG PTSRTCSLSP DVNNPGYRNV TFDELVENYT EATKGLIEGG ADLILIETIF DTLNAKAAIF AVQGVFEEVG FELPIMISGT ITDASGRTLS GQTTEAFWNS ISHAKPISVG LNCALGASEL RPYLQELANK ANTHVSAPPN AGLPNAFGEY DELPSQTAKI IEEFAQSGFL NIVGGCCGTP PAHIKAIAEA VSGYAPREIP DIPKACRLSG LEPFTIDRQS LFVNVGERTN ITGSARFARL IREDNYTEAL EVALQQVEAG AQVIDINMDE GMLDSKKAMV TFLNLIAGEP DISRVPIMID SSKWEVIEAG LKCIQGKGIV NSISMKEGVE QFIHHARLCK RYGAAVVVMA FDEQGQADTE ARKKEICKRS YDILVNEVGF PPEDIIFDPN IFAIATGIEE HNNYAVDFIN ACAYIRDELP YALTSGGVSN VSFSFRGNNP VREAIHSVFL LHAIRNGLSM GIVNAGQLEI YDQIPAELRD CVEDVVLNRN PGGTDALLAI ADKFKGDGSV KEAETEEWRS WPVNQRLEHA LVKGITTHIV QDTEESRLGF ARPIEVIEGP LMAGMNVVGD LFGAGKMFLP QVVKSARVMK QAVAHLIPFI ELEKGDKPEA KGKILMATVK GDVHDIGKNI VGVVLGCNGY DIVDLGVMVP AEKILQVARD EKCDIIGLSG LITPSLDEMV HVAREMQRQD FHLPLMIGGA TTSKAHTAVK IEPKYSNDAV IYVTDASRAV GVATQLLSKE LKPAFIEKTR LEYIEVRERT SARSARTERL SYGAAVAKKP QFDWENYTPA QPTFTGTRVL QDIDLNV // ID F3JAJ5_PSEAP Unreviewed; 46 AA. AC F3JAJ5; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 29-OCT-2014, entry version 14. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EGH81421.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGH81421.1}; DE Flags: Fragment; GN Name=metH {ECO:0000313|EMBL:EGH81421.1}; GN ORFNames=PSYAP_33135 {ECO:0000313|EMBL:EGH81421.1}; OS Pseudomonas syringae pv. aptata str. DSM 50252. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae. OX NCBI_TaxID=629268 {ECO:0000313|EMBL:EGH81421.1}; RN [1] {ECO:0000313|EMBL:EGH81421.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 50252 {ECO:0000313|EMBL:EGH81421.1}; 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. {ECO:0000313|EMBL:EGH81421.1}. 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; AEAN01001831; EGH81421.1; -; Genomic_DNA. DR EnsemblBacteria; EGH81421; EGH81421; PSYAP_33135. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGH81421.1}; KW Transferase {ECO:0000313|EMBL:EGH81421.1}. FT NON_TER 46 46 {ECO:0000313|EMBL:EGH81421.1}. SQ SEQUENCE 46 AA; 5360 MW; 28DA6EE14DA23AD2 CRC64; MSDRSARHQA FLTALKQRIL ILDGGMGTMI QSYRLEEQDY RGKRFA // ID F3JC46_PSESX Unreviewed; 298 AA. AC F3JC46; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGH69419.1}; GN ORFNames=PSYAR_02539 {ECO:0000313|EMBL:EGH69419.1}; OS Pseudomonas syringae pv. aceris str. M302273. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae. OX NCBI_TaxID=629270 {ECO:0000313|EMBL:EGH69419.1}; RN [1] {ECO:0000313|EMBL:EGH69419.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M302273 {ECO:0000313|EMBL:EGH69419.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGH69419.1}. 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; AEAO01000052; EGH69419.1; -; Genomic_DNA. DR RefSeq; WP_004406908.1; NZ_GL385308.1. DR EnsemblBacteria; EGH69419; EGH69419; PSYAR_02539. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EGH69419.1}; KW Transferase {ECO:0000313|EMBL:EGH69419.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 207 207 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 298 AA; 31598 MW; DA39391AA45DF16F CRC64; MTQGTTVILD GGMGRELQRR GAPFRQPEWS ALALSEAPEA VSAVHAAYIE SGAQVITSNS YAVVPFHIGE ERFAREGQAL AALAGQLARE SADASGGRAR VAGSIPPLFG SYRPDLYKPE QATDVLKPLV AGLSPYVDLW LAETQSCILE AQTIRAGLPN DGKPFWLSFT LQDEDTDEVP RLRSGEPVAD AARAAAAMGV ATLLFNCSQP EVIGGAIDAA REVFTSLNVD IAIGAYANAF PPQPKDATAN DGLDELREDL DPQGYQQWAA DWVKRGATHI GGCCGIGPEH IAVLSRSL // ID F3JHM1_PSESX Unreviewed; 1239 AA. AC F3JHM1; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EGH71344.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGH71344.1}; GN Name=metH {ECO:0000313|EMBL:EGH71344.1}; GN ORFNames=PSYAR_12349 {ECO:0000313|EMBL:EGH71344.1}; OS Pseudomonas syringae pv. aceris str. M302273. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae. OX NCBI_TaxID=629270 {ECO:0000313|EMBL:EGH71344.1}; RN [1] {ECO:0000313|EMBL:EGH71344.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M302273 {ECO:0000313|EMBL:EGH71344.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGH71344.1}. 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; AEAO01000289; EGH71344.1; -; Genomic_DNA. DR RefSeq; WP_003402783.1; NZ_GL385315.1. DR EnsemblBacteria; EGH71344; EGH71344; PSYAR_12349. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGH71344.1}; KW Transferase {ECO:0000313|EMBL:EGH71344.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1239 AA; 135946 MW; 92F051E6A39D6A1B CRC64; MSDRSARHQA FLTALKQRIL ILDGGMGTMI QSYRLEEQDY RGKRFADWPS DVKGNNDLLI LTRPDVIGAI EKAYLDAGAD ILETNTFNAT QVSQADYGME SIVYELNVEG ARLARKVADA KTLETPDRPR FVAGVLGPTS RTCSLSPDVN NPGYRNVTFD ELVENYTEAT KGLIEGGADL ILIETIFDTL NAKAAIFAVQ GVFEEVGFEL PIMISGTITD ASGRTLSGQT TEAFWNSISH AKPISVGLNC ALGASELRPY LQELANKANT HVSAHPNAGL PNAFGEYDEL PSQTAKIIEE FAQSGFLNIV GGCCGTTPAH IKAIAEAVSG YAPREIPDIP KACRLSGLEP FTIDRQSLFV NVGERTNITG SARFARLIRE DNYTEALEVA LQQVEAGAQV IDINMDEGML DSKKAMVTFL NLIAGEPDIS RVPIMIDSSK WEVIEAGLKC IQGKGIVNSI SMKEGVEQFI HHARLCKRYG AAVVVMAFDE QGQADTEARK KEICKRSYDI LVDEVGFPPE DIIFDPNIFA IATGIEEHNN YAVDFINACA YIRDELPYAL TSGGVSNVSF SFRGNNPVRE AIHSVFLLHA IRNGLSMGIV NAGQLEIYDQ IPAELRDCVE DVVLNRNPEG TDALLAIADK FKGDGSVKEA ETEEWRSWPV NQRLEHALVK GITTHIVQDT EESRAGFARP IEVIEGPLMA GMNVVGDLFG AGKMFLPQVV KSARVMKQAV AHLIPFIELE KGDKPEAKGK ILMATVKGDV HDIGKNIVGV VLGCNGYDIV DLGVMVPAEK ILQVARDEKC DIIGLSGLIT PSLDEMVHVA REMQRQDFHL PLMIGGATTS KAHTAVKIEP KYSNDAVIYV TDASRAVGVA TQLLSKELKP AFIEKTRLEY VEVRERTSAR SARTERLSYG AAVAKKPQFD WENYTPAQPT FTGTRVLQDI DLNVLAEYID WTPFFISWDL AGKYPRILTD EVVGEAATAL YADATQMLRK LIDEKLISAR AVFGFWPANQ VNDDDLEVYD DDGKPLAKLH HLRQQTIKPD GKPNFSLADF VAPKDSGLTD YIGGFITTAG IGAEEVAKAY QDKGDDYNSI MVKALADRLA EACAEWLHQQ VRKEYWGYAQ DEALDNEALI KEQYMGIRPA PGYPACPDHT EKGTLFALLD PLPEGSAEHT AGKSGVFLTE HYAMFPAAAV SGWYFAHPQA QYFAVGKIDK DQVESYTARK GQDLSVTERW LAPNLGYDE // ID F3JUM3_PSEAJ Unreviewed; 1239 AA. AC F3JUM3; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EGH88614.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGH88614.1}; GN Name=metH {ECO:0000313|EMBL:EGH88614.1}; GN ORFNames=PSYTB_02399 {ECO:0000313|EMBL:EGH88614.1}; OS Pseudomonas amygdali pv. tabaci str. ATCC 11528. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas amygdali. OX NCBI_TaxID=573066 {ECO:0000313|EMBL:EGH88614.1, ECO:0000313|Proteomes:UP000002942}; RN [1] {ECO:0000313|EMBL:EGH88614.1, ECO:0000313|Proteomes:UP000002942} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 11528 {ECO:0000313|EMBL:EGH88614.1}; 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. {ECO:0000313|EMBL:EGH88614.1}. 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; AEAP01000043; EGH88614.1; -; Genomic_DNA. DR RefSeq; WP_005777559.1; NZ_GL385365.1. DR EnsemblBacteria; EGH88614; EGH88614; PSYTB_02399. DR EnsemblBacteria; KEZ63466; KEZ63466; C1E_0231085. DR PATRIC; 25619966; VBIPseSyr56650_5600. DR Proteomes; UP000002942; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002942}; KW Methyltransferase {ECO:0000313|EMBL:EGH88614.1}; KW Transferase {ECO:0000313|EMBL:EGH88614.1}. SQ SEQUENCE 1239 AA; 135970 MW; B341C27DD9203423 CRC64; MSDRSARHQA FLTALKQRIL ILDGGMGTMI QSYRLEEQDY RGKRFADWPS DVKGNNDLLI LTRPDVIGAI EKAYLDAGAD ILETNTFNAT QVSQADYGME SIVYELNLEG ARLARKVADA KTLETPDKPR FVAGVLGPTS RTCSLSPDVN NPGYRNVTFD ELVENYSEAT KGLIEGGADL ILIETIFDTL NAKAAIFAVQ GVFEEVGFEL PIMISGTITD ASGRTLSGQT TEAFWNSISH AKPISVGLNC ALGASELRPY LQELANKANT HVSAHPNAGL PNAFGEYDEL PSQTAKIIEE FAQSGFLNIV GGCCGTTPAH IKAIAEAVSG YAPREIPDIP KACRLSGLEP FTIDRQSLFV NVGERTNITG SARFARLIRE DNYTEALEVA LQQVEAGAQV IDINMDEGML DSKKAMVTFL NLIAGEPDIS RVPIMIDSSK WEVIEAGLKC IQGKGIVNSI SMKEGVEQFI HHARLCKRYG AAVVVMAFDE QGQADTEARK KEICKRSYDI LVNEVGFPPE DIIFDPNIFA IATGIEEHNN YAVDFINACA YIRDELPYAL TSGGVSNVSF SFRGNNPVRE AIHSVFLLHA IRNGLSMGIV NAGQLEIYDQ IPAELRDCVE DVVLNRNAEG TDALLAIADK FKGDGSVKEA ETEEWRSWPV NQRLEHALVK GITTHIVQDT EESRLAFTRP IEVIEGPLMA GMNVVGDLFG AGKMFLPQVV KSARVMKQAV AHLIPFIELE KGDKPEAKGK ILMATVKGDV HDIGKNIVGV VLGCNGYDIV DLGVMVPAEK ILQVARDEKC DIIGLSGLIT PSLDEMVHVA REMQRQDFHL PLMIGGATTS KAHTAVKIEP KYSNDAVIYV TDASRAVGVA TQLLSKELKP AFIEKTRLEY VEVRERTSAR SARTERLSYG AAVAKKPQFD WENYTPAQPT FTGTRVLQDI DLNVLAEYID WTPFFISWDL AGKYPRILTD EVVGEAATAL YADATQMLRK LIDEKLISAR AVFGFWPANQ VNDDDLEVYG DDGKPLAKLH HLRQQTIKPD GKPNFSLADF VAPKDSGLTD YIGGFITTAG IGAEEVAKAY QDKGDDYNSI MVKALADRLA EACAEWLHQQ VRKEYWGYAK DEALDNEALI KEQYMGIRPA PGYPACPDHT EKGTLFALLD PLPEGTPEHT PGKSGVFLTE HYAMFPAAAV SGWYFAHPQA QYFAVGKVDK NQVESYTARK GQDLSVTERW LAPNLGYDE // ID F3JVK7_PSEAJ Unreviewed; 298 AA. AC F3JVK7; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EGH88948.1}; GN ORFNames=PSYTB_04165 {ECO:0000313|EMBL:EGH88948.1}; OS Pseudomonas amygdali pv. tabaci str. ATCC 11528. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas amygdali. OX NCBI_TaxID=573066 {ECO:0000313|EMBL:EGH88948.1, ECO:0000313|Proteomes:UP000002942}; RN [1] {ECO:0000313|EMBL:EGH88948.1, ECO:0000313|Proteomes:UP000002942} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 11528 {ECO:0000313|EMBL:EGH88948.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGH88948.1}. 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; AEAP01000076; EGH88948.1; -; Genomic_DNA. DR RefSeq; WP_005777989.1; NZ_GL385366.1. DR EnsemblBacteria; EGH88948; EGH88948; PSYTB_04165. DR EnsemblBacteria; KEZ70781; KEZ70781; C1E_0202135. DR PATRIC; 25609688; VBIPseSyr56650_0321. DR Proteomes; UP000002942; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002942}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EGH88948.1}; KW Transferase {ECO:0000313|EMBL:EGH88948.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 207 207 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 298 AA; 31564 MW; 6D0A3E43B3F7361A CRC64; MKQGTTVILD GGMGRELQRR GAPFRQPEWS ALALSEAPEA VSAVHAAYIE SGAQVITSNS YAVVPFHIGE ERFAREGQAL AALAGRLARE TADASGGRAQ VAGSIPPLFG SYRPDLYKPE LAADVLRPLV AGLSPYVDLW LAETQSCILE AQTIRAGLPN DGKPFWLSFT LQDEDTDEVP RLRSGEPVAD AAKAAAGMGV ATLLFNCSQP EVIGGAIDAA REVFKALNVD IAIGAYANAF PPQPKDAKAN DGLDELREDL DPQGYQQWAA DWVTRGATHI GGCCGIGPEH IAVLSKSL // ID F3KDB2_9GAMM Unreviewed; 635 AA. AC F3KDB2; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 04-FEB-2015, entry version 25. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=imdm_870 {ECO:0000313|EMBL:EGG99644.1}; OS gamma proteobacterium IMCC2047. OC Bacteria; Proteobacteria; Gammaproteobacteria. OX NCBI_TaxID=434085 {ECO:0000313|EMBL:EGG99644.1}; RN [1] {ECO:0000313|EMBL:EGG99644.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=IMCC2047 {ECO:0000313|EMBL:EGG99644.1}; RX PubMed=21602327; DOI=10.1128/JB.05226-11; RA Kang I., Kang D., Oh H.M., Kim H., Kim H.J., Kang T.W., Kim S.Y., RA Cho J.C.; RT "Genome sequence of strain IMCC2047, a novel marine member of the RT Gammaproteobacteria."; RL J. Bacteriol. 193:3688-3689(2011). RN [2] {ECO:0000313|EMBL:EGG99644.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=IMCC2047 {ECO:0000313|EMBL:EGG99644.1}; RA Kang D.M., Oh H.M., Cho J.C.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {ECO:0000256|RuleBase:RU004255}. CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGG99644.1}. 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; AEGL01000201; EGG99644.1; -; Genomic_DNA. DR EnsemblBacteria; EGG99644; EGG99644; imdm_870. DR PATRIC; 56462699; VBIGamPro26839_0744. DR UniPathway; UPA00193; -. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004255}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 635 AA; 69339 MW; 79555B819AD65280 CRC64; MSDFITDLLS NPLLADGASG SFLFERSGRL SEVNHVYEAL NADNPDAIRD IHLAYLQSGA RCLTTNTFGA NSAYLKIMGE AGRVAELNNA GVKRAQEAIA RFKEHTHSEK NYYILGSIGP SCDDELTAEE AAEIYLEQVE ALIAAGVDAL LLETFNSLAE VKTLLELINT LPNKPPVIVQ MALQQNANND WNVAPTSYVE TAAELGVSVV GVNCCTPWDA SAFIEQANSL DVVKEHKVLL SAMPNAGGFQ RIGHRFMTAV NPEFMGKQAR TFAAQGVRLI GGCCEVHPEH ILEMNNYLQG SQVNQNSVQV RSQDAMEPNG PEAKADNGPF SRKLMNGEFV VSVELLPSRG TSAAVLKHKI DFVKQLADSG LADALDITDG SRGIPLIPPG DFIGNIRQTL GWTAETGDKL ELIPHFTTRD LNIMGLQSRL MGYYSQRINN VVFITGDPPK MSPTYPRSTA VFDANSVDML NYTQHCLNAG VDFGGQRLGK QKDPRTHFTV GAGFEPEALD SKSEIAKLER KIDAGADYIM TQPAFRNDAL SILEPYRQRV AVLIGVMVLT GLEHAKRVGQ VPGVTIPGSI LERLARFDNI EDQAKAGQEI AMEQIRWVRD NNWPGLYLMS PASHDRVIDT LSALK // ID F3KKJ5_9ARCH Unreviewed; 299 AA. AC F3KKJ5; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGG42115.1}; GN ORFNames=Nlim_1015 {ECO:0000313|EMBL:EGG42115.1}; OS Candidatus Nitrosoarchaeum limnia SFB1. OC Archaea; Thaumarchaeota; Nitrosopumilales; Nitrosopumilaceae; OC Candidatus Nitrosoarchaeum. OX NCBI_TaxID=886738 {ECO:0000313|EMBL:EGG42115.1, ECO:0000313|Proteomes:UP000004348}; RN [1] {ECO:0000313|EMBL:EGG42115.1, ECO:0000313|Proteomes:UP000004348} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SFB1 {ECO:0000313|EMBL:EGG42115.1}; RX PubMed=21364937; DOI=10.1371/journal.pone.0016626; RA Blainey P.C., Mosier A.C., Potanina A., Francis C.A., Quake S.R.; RT "Genome of a low-salinity ammonia-oxidizing archaeon determined by RT single-cell and metagenomic analysis."; RL PLoS ONE 6:E16626-E16626(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. {ECO:0000313|EMBL:EGG42115.1}. 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; AEGP01000038; EGG42115.1; -; Genomic_DNA. DR RefSeq; WP_007402141.1; NZ_CM001158.1. DR EnsemblBacteria; EGG42115; EGG42115; Nlim_1015. DR Proteomes; UP000004348; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000004348}; KW Methyltransferase {ECO:0000313|EMBL:EGG42115.1}; KW Transferase {ECO:0000313|EMBL:EGG42115.1}. SQ SEQUENCE 299 AA; 33024 MW; F1A7A69BCE5E41B9 CRC64; MGTEIQKYDP KPEDFPNNQD GFNDGLVLTH PEWIKQIHRN YLDAGSDCIE TNSFGSNKIK LDEYGFGDQT IEFNKKIASL AVEVCSEYND KPRYVIGSMG PSGYLPSSND PDLGQKPLDE IRDAFELQAE GLILGGVDAL LIETSQDILE VKLVIEACHK AMKKTGKKIP IIANTTLDQY GKMLLGTNIQ AAYTTVSDMG IDVFGLNCST GPVEMTPSVR WLDEQNEHNI LVVPNAGMPE NQGGRAVYKM TPEKMGEVLG DFLKQYKKVR IIGGCCGTNP QHIAALRKVI DEKDYSIKS // ID F3KSX6_9BURK Unreviewed; 322 AA. AC F3KSX6; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 11. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:EGI77195.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EGI77195.1}; GN Name=mmuM {ECO:0000313|EMBL:EGI77195.1}; GN ORFNames=HGR_07776 {ECO:0000313|EMBL:EGI77195.1}; OS Hylemonella gracilis ATCC 19624. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Hylemonella. OX NCBI_TaxID=887062 {ECO:0000313|EMBL:EGI77195.1}; RN [1] {ECO:0000313|EMBL:EGI77195.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 19624 {ECO:0000313|EMBL:EGI77195.1}; 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. {ECO:0000313|EMBL:EGI77195.1}. 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; AEGR01000052; EGI77195.1; -; Genomic_DNA. DR RefSeq; WP_006297592.1; NZ_AEGR01000052.1. DR EnsemblBacteria; EGI77195; EGI77195; HGR_07776. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGI77195.1}; KW Transferase {ECO:0000313|EMBL:EGI77195.1}. SQ SEQUENCE 322 AA; 34666 MW; C723F71ECD2B26DA CRC64; MNTPTHPLQQ ALDEQGLFVL DGALATELER RGADLKDPLW SAKLLIEQPD LIRQVHLDYF VAGADVSTTA SYQATFEAFA RRGLGHDEAA DLMRRSVQLA CEARDAFWSD PKHRAGRRKP LVAASVGPYG AMLADGSEYR GYPGVSRAAL AAFHRPRLQV LAHSGADLLA CETLPCLAEA LAITDLLPEF PGVQAWISFS CRDGEHNSQG EPLADCVAAL DPVPQVAAVG VNCTAPEFVP SLVERARART SKPIVVYPNS GEHYDAVGKV WQGEGQAHDF AAQAMRWHNR GARLIGGCCR TGPDDIRALR QAALACGAIG PR // ID F3KWZ4_9BURK Unreviewed; 357 AA. AC F3KWZ4; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Homocysteine s-methyltransferase {ECO:0000313|EMBL:EGI75781.1}; GN ORFNames=HGR_14914 {ECO:0000313|EMBL:EGI75781.1}; OS Hylemonella gracilis ATCC 19624. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Hylemonella. OX NCBI_TaxID=887062 {ECO:0000313|EMBL:EGI75781.1}; RN [1] {ECO:0000313|EMBL:EGI75781.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 19624 {ECO:0000313|EMBL:EGI75781.1}; 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. {ECO:0000313|EMBL:EGI75781.1}. 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; AEGR01000093; EGI75781.1; -; Genomic_DNA. DR RefSeq; WP_006299106.1; NZ_AEGR01000093.1. DR EnsemblBacteria; EGI75781; EGI75781; HGR_14914. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGI75781.1}; KW Transferase {ECO:0000313|EMBL:EGI75781.1}. SQ SEQUENCE 357 AA; 38345 MW; 8B67E4F6C219F972 CRC64; MKPLAYTRAR ELPGTLQQRI AILDGAMGTM IQRFKLSEMQ YRGEGGPAEA LARFRDFPRD LKGNNELLSL TRPDVISAIH EKYLAAGADL IETNTFGATR IAQSDYDMAG LAREMNLASA RLARAACDKF STPQQPRYVA GALGPTPRTA SISPDVNDPG ARNVDFEELR ASYFEQTVAL IEGGSDVLLV ETIFDTLNAK AALFAIDEAF EATGECLPIL ISGTVTDASG RILSGQTVTA FWHSVRHARP LAIGLNCALG ATLMRPYIQE LAKAAPDTFI SCYPNAGLPN PMSDTGFDET PDVTSRLLHE FAAEGLVNIV GGCCGTTPEH IGAIRQAMVP MPTRALNASG SFYREAA // ID F3L143_9GAMM Unreviewed; 1227 AA. AC F3L143; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 01-APR-2015, entry version 22. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EGG29988.1}; GN ORFNames=IMCC3088_1135 {ECO:0000313|EMBL:EGG29988.1}; OS gamma proteobacterium IMCC3088. OC Bacteria; Proteobacteria; Gammaproteobacteria; OMG group; OM60 clade. OX NCBI_TaxID=876044 {ECO:0000313|EMBL:EGG29988.1}; RN [1] {ECO:0000313|EMBL:EGG29988.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=IMCC3088 {ECO:0000313|EMBL:EGG29988.1}; RX PubMed=21551310; DOI=10.1128/JB.05111-11; RA Jang Y., Oh H.M., Kang I., Lee K., Yang S.J., Cho J.C.; RT "Genome sequence of strain IMCC3088, a proteorhodopsin-containing RT marine bacterium belonging to the OM60/NOR5 clade."; RL J. Bacteriol. 193:3415-3416(2011). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGG29988.1}. 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; AEIG01000026; EGG29988.1; -; Genomic_DNA. DR RefSeq; WP_009575425.1; NZ_AEIG01000026.1. DR EnsemblBacteria; EGG29988; EGG29988; IMCC3088_1135. DR PATRIC; 54942260; VBIGamPro169569_1032. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGG29988.1}; KW Transferase {ECO:0000313|EMBL:EGG29988.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135106 MW; FD22BE093478D906 CRC64; MPIQRPTLEQ ALQERILIID GAMGTMIQGY KLAESDYRGS RFADFNGDLK GNNDLLCLTR PDLIIDIHKA FLEAGADLIE TNSFNSTAVA QSDYGLESLA DELNRAAARL AREAADHYSA LTPDKPRYVA GILGPTPRTA SISPDVNDPG ARNIDYDSLV QDYRVAAVAL LEEGVDIIMI ETIFDTLNAK AALFAVEAAF GVTGIKRPIM LSVTFPDTSG RILSGQTAEA FWNSIAHAKP LIVGTNCGRR FKEVRPYVEA LANAADCYFS GHFNAGLPNA FGEYDETPED MFADLQDFAQ RGFLNLVGGC CGTRPEHIKA IAEAVGSAKP RELPKLEPGC YLSGLEPFNI TAESLFVNVG ERCNVTGSAA FKRLIINEQY EDALAVARTQ VEDGAQIIDI NMDEGMLDAQ KAMVTFLNLA ASEPEISRVP FMLDSSRWDA IEAGLKCVQG KCIVNSISLK EGVAEFLEKA RLCQRFGAAV VVMAFDEDGQ ADTFERKTEI CQRSYTLLTE ELGFNPNDII FDPNIFAVAT GIDEHNNYAV DFIEATRWIK QNLPGAMVSG GVSNVSFSFR GNNPVREAIH SVFLYHAIKA GLDMGIVNAG QLAVYDELPA ALKEAVEDVI LNRRDDATER LLDIAEEYRG DGAATKKVED LEWRTWPVAK RIEHALVKGI NTYVIEDAEE ARQAFSRPIE VIEGPLMDGM NVVGDLFGEG KMFLPQVVKS ARVMKQAVAY LQPFIEAEKT EGSGSNGKIL MATVKGDVHD IGKNIVGVVL QCNNFEVIDL GVMVHCETIL QAAREHQVDI IGLSGLITPS LDEMAHVASE MQRQGFNIPL MIGGATTSKA HTAVKIAPQY QNDVAVYVPD ASRSVSVATA LLGEQKPSFQ RNLAQEYETV RERVANRQPL KPALTYSEAL RRRFQPNWAE YAPTKPSYLG TQAIEVPLAD LVPYIDWTPF FLTWELAGKF PAILDDEIVG EQATLLYQDA RAMLEQMVRE EWSTGKAVVG FWPASSLGDD IVLYTDDTRT QVQEVLHQVR QQANPGDDSK PTYSLADFLP PQGNDLHDYL GGFCVTTGHG IDERAKAYEA DGDDYNSIMV KALADRLAEA LAEYMHQHVR TTLWAYAPNE DLDNAQLIKE QYQGIRPAPG YPACPDHSEK DTLFRLLKAT ELCGVELTDS YAMTPTAAVS GYYFANPETR YFNVGKISQE QVESLALRKK ESVATIEQWL RPNLAYK // ID F3LCR5_9GAMM Unreviewed; 344 AA. AC F3LCR5; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EGG95313.1}; GN ORFNames=IMCC1989_854 {ECO:0000313|EMBL:EGG95313.1}; OS gamma proteobacterium IMCC1989. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales. OX NCBI_TaxID=937772 {ECO:0000313|EMBL:EGG95313.1}; RN [1] {ECO:0000313|EMBL:EGG95313.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=IMCC1989 {ECO:0000313|EMBL:EGG95313.1}; 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. {ECO:0000313|EMBL:EGG95313.1}. 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; AEVK01000018; EGG95313.1; -; Genomic_DNA. DR RefSeq; WP_009668635.1; NZ_AEVK01000018.1. DR EnsemblBacteria; EGG95313; EGG95313; IMCC1989_854. DR PATRIC; 54955897; VBIGamPro175983_0305. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGG95313.1}; KW Transferase {ECO:0000313|EMBL:EGG95313.1}. SQ SEQUENCE 344 AA; 37322 MW; 3E40370FAA07CC7B CRC64; MSTSISTSTS TSVTHQLQEI LKNRIMLLDG AMGTMIQRHS LGEDDFRGKH FPDHPSSLKG DNDLLAITRP DIIQSIHEEY FEVGSDFATT NSFNATTIAQ ADYDMEAAVY DINYQSAQCA RRAADVWTAK TPDKPRFVIG ALGPTNRTAS LSPDVNDPGK RLVTFDELRQ AYFDAANALL EGGADILMIE TVFDTLNAKA GLYAMAEIRD KWGEVPVMVS GTITDASGRT LSGQTAEAFW ISMMHGELLS VGLNCALGAN EMLPYVKRLD AIASCFVSAH PNAGLPNEFG EYDESPEQMA DQVEQFVKGG HVNILGGCCG TTPEHIAALA DLAKKYSPRT LKES // ID F3LP47_9BURK Unreviewed; 310 AA. AC F3LP47; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 11. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:EGJ10115.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EGJ10115.1}; GN Name=mmuM {ECO:0000313|EMBL:EGJ10115.1}; GN ORFNames=RBXJA2T_07290 {ECO:0000313|EMBL:EGJ10115.1}; OS Rubrivivax benzoatilyticus JA2 = ATCC BAA-35. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Rubrivivax. OX NCBI_TaxID=987059 {ECO:0000313|EMBL:EGJ10115.1}; RN [1] {ECO:0000313|EMBL:EGJ10115.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=JA2 {ECO:0000313|EMBL:EGJ10115.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGJ10115.1}. 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; AEWG01000063; EGJ10115.1; -; Genomic_DNA. DR RefSeq; WP_009856681.1; NZ_AEWG01000063.1. DR EnsemblBacteria; EGJ10115; EGJ10115; RBXJA2T_07290. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGJ10115.1}; KW Transferase {ECO:0000313|EMBL:EGJ10115.1}. SQ SEQUENCE 310 AA; 33244 MW; 488BFD3BD5911972 CRC64; MIATTLAAQD IVVLDGALAT ELERRGADLK DPLWSARLLI ERPELIREVH LDYFRAGADV ATTASYQATF EGFARRGFSH DEAVALMRRS VALAIEARDA FWAEPANRAG RRRPLVAASV GPYGAMLADG SEYRGYPGVT REQLAAFHRP RLEVLAAAGA DLLACETIPC LDEALAIASL LPTLQPALPA WISFSCRDGE HVSQGERFAD CAAALDGLPG VAAVGLNCTA PEYVPALIAA AQARTRLPIV VYPNSGEQWD AVAKCWHGER DAADFAAQAE RWRRGGARLI GGCCRTGPDE IRALRAALLA // ID F3LUK0_9BURK Unreviewed; 352 AA. AC F3LUK0; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGJ12033.1}; GN ORFNames=RBXJA2T_16962 {ECO:0000313|EMBL:EGJ12033.1}; OS Rubrivivax benzoatilyticus JA2 = ATCC BAA-35. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Rubrivivax. OX NCBI_TaxID=987059 {ECO:0000313|EMBL:EGJ12033.1}; RN [1] {ECO:0000313|EMBL:EGJ12033.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=JA2 {ECO:0000313|EMBL:EGJ12033.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGJ12033.1}. 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; AEWG01000149; EGJ12033.1; -; Genomic_DNA. DR RefSeq; WP_009858598.1; NZ_ATUI01000002.1. DR EnsemblBacteria; EGJ12033; EGJ12033; RBXJA2T_16962. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGJ12033.1}; KW Transferase {ECO:0000313|EMBL:EGJ12033.1}. SQ SEQUENCE 352 AA; 37849 MW; B39B64DC73CE4CEB CRC64; MNARTPAYTR GQALADLLPR RIVVIDGAMG TMIQRWKLGE ADFRNDALRE HPKDLKGNND LLSITRPDVI REIHAQYLAA GADIIETNTF GATTVAQEDY DLAPMAREMN LASARVAREA ADAAATPDKP RFVAGALGPT PRTASISPDV NDPGARNITF DQLRDAYREQ AEALLDGGVD LFLVETIFDT LNAKAAIFAL DELMEARGER LPVIVSGTVT DASGRILSGQ TVGAFWHSVR HARPLAIGLN CALGAALMRP YIEELSRIAD DTYVSCYPNA GLPNPMSETG FDETPPVTGA LMADFAKAGF LNIVGGCCGT TPDHIAEIAR RVSAYRPRSR RDPLFTGLVA AA // ID F3MAZ6_9BACL Unreviewed; 623 AA. AC F3MAZ6; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 07-JAN-2015, entry version 19. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HMPREF9412_3133 {ECO:0000313|EMBL:EGG35518.1}; OS Paenibacillus sp. HGF5. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=908341 {ECO:0000313|EMBL:EGG35518.1}; RN [1] {ECO:0000313|EMBL:EGG35518.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HGF5 {ECO:0000313|EMBL:EGG35518.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGG35518.1}. 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; AEXS01000097; EGG35518.1; -; Genomic_DNA. DR RefSeq; WP_009592609.1; NZ_AEXS01000097.1. DR EnsemblBacteria; EGG35518; EGG35518; HMPREF9412_3133. DR PATRIC; 54970753; VBIPaeSp172377_3227. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EGG35518.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EGG35518.1}. SQ SEQUENCE 623 AA; 68382 MW; 27E1324ED6A7F8FE CRC64; MKPNLRQAWE NQVLVGDGAM GTYLYQKGFP VGISYEELNL TSPEVIGNVH RQYVEAGAQV IETNTFSANY DKLSKYGLEA RAGEINRAGV RIAREAAGDH GYVVGAVGSI RAGKRSNIST SELKRYFEEQ LSVLIAEGVD GILLETFYDV DEMQLALAQA RMLSDLPVIC QFAVEDIART LDGFTMPDAY RILSQEGADV IGFNCRTGPN GIMRALETLN GIMNLPASVY PNAGIADYVD GEYRYGASPE YFGKTALEFA DRGARIIGGC CGTTPEHIAE ISSALSGYVP SPLPAVEEAE INRIVIHETA QEQFYERSGE PTIVDIVKER HTVIVELDPP RDLDITKFMK GAEALKKAGA DALTLADNSL AVTRMSNMAL GHLVQARTGL RPLIHIACRD RNLIGTQSHM MGFDALGIDH VLAVTGDPAR FGDLPDSSSV YDMTSFEIIR MIKQLNDGIA FSGKPLKQKA KFVVGAAFNP NVRHLDKAVA RLEKKIASGA DYVMTQPVYD PELMVRLREA TAHLDIPIFI GIMPLASGRN AEYLHNEVPG IQLSDEVRSR MAGLEGEAGR AMGVKIGKEL LDVATEHFNG IYLMTPFMFY EMSVQLMEYV WEKSGRRLTP LFH // ID F3MK33_9BACL Unreviewed; 1146 AA. AC F3MK33; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 01-APR-2015, entry version 22. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGG31065.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGG31065.1}; GN Name=metH {ECO:0000313|EMBL:EGG31065.1}; GN ORFNames=HMPREF9412_4084 {ECO:0000313|EMBL:EGG31065.1}; OS Paenibacillus sp. HGF5. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=908341 {ECO:0000313|EMBL:EGG31065.1}; RN [1] {ECO:0000313|EMBL:EGG31065.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HGF5 {ECO:0000313|EMBL:EGG31065.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGG31065.1}. 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; AEXS01000184; EGG31065.1; -; Genomic_DNA. DR RefSeq; WP_009596014.1; NZ_AEXS01000184.1. DR EnsemblBacteria; EGG31065; EGG31065; HMPREF9412_4084. DR PATRIC; 54977201; VBIPaeSp172377_6365. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGG31065.1}; KW Transferase {ECO:0000313|EMBL:EGG31065.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 722 722 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1146 AA; 125985 MW; 3DD2AD257040FFAD CRC64; MNKPSLQEVL KERILILDGA MGTMIQQEDL SAEDFGGPEL DGCNEMLVIH RPDVIQKIHE QYLEAGADLI ETNTFGATSV VLAEYDIPEL AREINLKAAH LARAAVEKYS TPDSPRYVVG AMGPTTKTLS VTGGVTFAEL IKSYEEQAVA LIEGGVDALL LETSQDTLNV KAGSIGIRQA FDKTGVTLPI MISGTIEPMG TTLAGQNIEA FYISLEHLNP VSIGLNCATG PEFMRDHIRS LSEMSRSAIS CYPNAGLPDE NGQYHESPES LAQKMGAFAE KGWLNIAGGC CGTTPDHIRA LKQTMDGFTP RPLEGGHLPA LSGIEPVYIE QENRPYMVGE RTNVLGSRKF KRLIVEGKYE EASEIARAQV KNGAHVIDVC VQDPDREEAE DMIQFLELVV KKVKVPLMID TTDPAVIDLA LQYSQGKAII NSINLEDGEE KFEHVTPLVH KYGAAVVVGT IDESGQAIHR DDKLKVAQRS YDLLVNKYGI SPEDIIFDTL VFPVGTGDEQ YIGSAKETIE GIRMIKEAMP KVHTILGISN VSFGLPEAGR EVLNSVYLYE CTKAGLDYAI VNTEKLERYA SIPEEERRLA EELIYRTNDE TLAAFVAAFR DKKVEKKVKV SNLTLEERLA SYVVEGSKEG LIPDLDVALT KYGALEIING PLMAGMTEVG RLFNNNELIV AEVLQSAEVM KASVAYLESF MEKNESSVKG KIMLATVKGD VHDIGKNLVE IILSNNGYQI INLGIKVPPE QIIEAYRREQ PDAIGLSGLL VKSAQQMVST AQDLKNAGIS VPIMVGGAAL TRKFTKTRIR PEYDGMVLYA KDAMDGLALA NQLSDPVLRT QMAEEIKAEQ EADAAAPQVV KVMPKLSEGL RSKISTEAPV YIPPDMERHV LRNYPISHIL PYINMQMLLG HHLGLKGSVE QLLKANDPKA VSLKETVDGI LEEAVQSGII QAHAMYRFFP AQSRGNDIII YDPKDASKIL HTFTFPRQQV EPYLCLADFL KSVDSGVMDY VGFLVVTAGH GVGKLSGEWK DKGDYLRSHA LQSVALETAE GLAERIHHMM RDTWGYPDPA DMTMKQRLGA RYQGIRVSFG YPACPDLEDQ EPLFKLMQPE DIGVHLTEGF MMEPEASVSA MVFSHPEAHY FNVDKA // ID F3NLF5_9ACTO Unreviewed; 1183 AA. AC F3NLF5; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGG45881.1}; GN ORFNames=SGM_3969 {ECO:0000313|EMBL:EGG45881.1}; OS Streptomyces griseoaurantiacus M045. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=996637 {ECO:0000313|EMBL:EGG45881.1}; RN [1] {ECO:0000313|EMBL:EGG45881.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M045 {ECO:0000313|EMBL:EGG45881.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGG45881.1}. 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; AEYX01000039; EGG45881.1; -; Genomic_DNA. DR RefSeq; WP_006141757.1; NZ_AEYX01000039.1. DR EnsemblBacteria; EGG45881; EGG45881; SGM_3969. DR PATRIC; 54985880; VBIStrGri184913_4188. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 251 251 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 318 318 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1183 AA; 128849 MW; CAFE22BCA45EC5C9 CRC64; MASSPNPSAS SAPSERPGGT PAADARARTD ALREALATRV VVADGAMGTM LQAQDPTLED FQGLEGCNEV LNITRPDIVR SVHQAYFSVG VDCVETNTFG ANHTAATEYE IADRVHELSE AGARIAREVA DEHGARDGRQ RWVLGSIGPG TKLPTLGHVG YTTIRDGYQA NAEGLLAGGA DALIVETTQD LLQTKASVLG ARRAMAATGT EVPLLVSMAF ETTGTMLLGS EIGAALTALE PLGIDMIGLN CSTGPAEMSE HLRYLTRHSR IPLLCMPNAG LPVLTKDGAH FPLDAEGLAD AQETFVQDYG LSLIGGCCGT TPEHLRQVVE RVRETTPAER SPQPEPGAAS LYQTVPFRQD TAYLAIGERT NANGSKKFRD AMLEGRWDDC VEMARDQIRE GAHMLDLCVD YVGRDGVADM RELAGRFATA STLPIVLDST EVDVLRAGLE MLGGRAVINS VNYEDGAGPE SRFAKVTALA KEHGAALIAL TIDEEGQART AEKKVEIAER LIEDLTGNWG IHEEDILVDC LTFTICTGQE ESRKDGLATI EGIRRLKERH PKVQTTLGLS NISFGLNPAA RILLNSVFLD ECVKAGLDSA IVHASKILPI ARFDEEQVTT ALDLIHDRRR EGYDPLQKLM QLFEGATAKS LKAGKAEELA ALPLDERLKR RIIDGEKNGL EADLDEALES RPALAIVNET LLDGMKVVGE LFGSGQMQLP FVLQSAEVMK TAVAHLEPHM EKSDEAGKGT IVLATVRGDV HDIGKNLVDI ILSNNGYNVV NLGIKQPVSA ILEAAEEHKA DVIGMSGLLV KSTVIMKENL EELNQRGMAT DFPVILGGAA LTRAYVEQDL HEIYEGEVRY ARDAFEGLRL MDALIGVKRG VPGAKLPELR QRRVRAATVE IEDRPEEGAV RSDVATDNPV PEPPFRGSRV IKGIQLKEYA GWLDEGALFK GQWGLKQARS GEGPTYEELV EREGRPRLRG LLDRLQTDNL LEAAVVYGYF PCVSKDDDLI VLDEDGNERT RFTFPRQRRG RRLCLADFFR PEESGEVDVV GFQVVTVGSR IGAETAKLFE ANAYRDYLEL HGLSVQLAEA LAEYWHARVR GELGYAGEDP AAMEDMFALK YRGARFSLGY GACPDLEDRA KIAELLQPER IGVHLSEEFQ LHPEQSTDAI VIHHPEAKYF NAR // ID F3NPI6_9ACTO Unreviewed; 308 AA. AC F3NPI6; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:EGG44998.1}; GN ORFNames=SGM_5050 {ECO:0000313|EMBL:EGG44998.1}; OS Streptomyces griseoaurantiacus M045. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=996637 {ECO:0000313|EMBL:EGG44998.1}; RN [1] {ECO:0000313|EMBL:EGG44998.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M045 {ECO:0000313|EMBL:EGG44998.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGG44998.1}. 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; AEYX01000042; EGG44998.1; -; Genomic_DNA. DR RefSeq; WP_006142892.1; NZ_AEYX01000042.1. DR EnsemblBacteria; EGG44998; EGG44998; SGM_5050. DR PATRIC; 54988086; VBIStrGri184913_5270. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGG44998.1}; KW Transferase {ECO:0000313|EMBL:EGG44998.1}. SQ SEQUENCE 308 AA; 32200 MW; DA6AC182A693AB23 CRC64; MSSDTRPSLT EALAAGTLVL DGGLSNQLEA AGHDLGDALW SARLLAEAPE AVVEAHLAYF EAGANVAITA SYQATFEGFA RYGLTRARTA ELLAYSVESA REAARRARER GVARPLWTAA SAGPYGAMLA DGSEYRGRYG LSVDELADFH RPRLEALAAA RPDVLALETV PDTEEARALL RAVRGLGVPA WLSYTVAGSR TRAGQPLEEA FALAAEAEEI VAVGVNCCAP KDVEPAVALA AQVTGKPVVA YPNSGETWHA DTAGWTGPVT FTPEAVRNWR RAGARLIGGC CRVGPTGVRG VAEALGAT // ID F3P103_9ACTO Unreviewed; 394 AA. AC F3P103; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGG27239.1}; GN ORFNames=PA08_1482 {ECO:0000313|EMBL:EGG27239.1}; OS Propionibacterium humerusii P08. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=999892 {ECO:0000313|EMBL:EGG27239.1}; RN [1] {ECO:0000313|EMBL:EGG27239.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=P08 {ECO:0000313|EMBL:EGG27239.1}; 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] {ECO:0000313|EMBL:EGG27239.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=P08 {ECO:0000313|EMBL:EGG27239.1}; RA Matsen F., Hoffman N., Butler-Wu S., Kittichotirat W., Bumgarner R.; 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. {ECO:0000313|EMBL:EGG27239.1}. 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; AFAM01000008; EGG27239.1; -; Genomic_DNA. DR RefSeq; WP_002526794.1; NZ_AFAM01000008.1. DR EnsemblBacteria; EGG27239; EGG27239; PA08_1482. DR PATRIC; 53597748; VBIProSp187533_1442. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; SQ SEQUENCE 394 AA; 41646 MW; 8C0EA9A7EE075D04 CRC64; MTLRTALSQN VLIIDGAMGT MLQSSDVTMD AFQGLEGCNE ILNVTRPDVI SGIHDAYLDA GADIIETNTF GANLPALTDY GIASRASELA SAATKLAREA ADKRTDKPRY VVGSIGPGTK LPTLRQIGFA AIRDVYQQVI EAMIDAGIDG VQIETCQDLL QARAAIIGAH RAAAAHKVDL PVLVDFTVET TGTMLMGSET GAALTVLESL GVDAIGLNCA TGPAEMAEHL RTLSRGARVP IMCMPNAGLP EITGEGRVTR WAPMTWPQFL TNTSIATGWP SSVAAVVPLP IIPGPLRSGC PVDRFLSETF TTSMPLLLYT ATSRSVRIPL IWPSANALMP TVPGRSVRPC WLRSGTSAST LPKPKPAMVP IYLICALTTS GATAFRTCQS CRPV // ID F3PBX2_9ACTO Unreviewed; 293 AA. AC F3PBX2; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 01-OCT-2014, entry version 12. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGF52250.1}; GN ORFNames=HMPREF9056_02566 {ECO:0000313|EMBL:EGF52250.1}; OS Actinomyces sp. oral taxon 170 str. F0386. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Actinomycineae; Actinomycetaceae; Actinomyces. OX NCBI_TaxID=762963 {ECO:0000313|EMBL:EGF52250.1}; RN [1] {ECO:0000313|EMBL:EGF52250.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0386 {ECO:0000313|EMBL:EGF52250.1}; 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 (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. {ECO:0000313|EMBL:EGF52250.1}. 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; AFBL01000068; EGF52250.1; -; Genomic_DNA. DR EnsemblBacteria; EGF52250; EGF52250; HMPREF9056_02566. DR PATRIC; 55010773; VBIActSp161325_2130. DR OrthoDB; EOG6C019S; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGF52250.1}; KW Transferase {ECO:0000313|EMBL:EGF52250.1}. SQ SEQUENCE 293 AA; 30702 MW; FCBC86835DFC8282 CRC64; MGTELDARGV DTHNALWSAL ALTAAPEAVY AVHTDYLDAG ARVITTNTYQ ATLPGLRQAG HDTVGARDVI AAGARLANDA ARCFEREHPE EPVLVAGGLG PYGAYLADGS EYTGAYDVDV SEDSGFQEVH LPRIEVLVGE GVDLFALETL PRLNEAQALV TMVKGLSPQA ECWVSFQVRP DGVRLADGTP LVEAAAWAAG EEAVVAVGVN CVAPDVVGRA LPVLREVTAK PLVAYSNSGD NYDPGTKTWK AGDEGGGFTA LAPSWIAAGV RLIGGCCRTR PAQIREIAHA VRT // ID F3PE68_9BACE Unreviewed; 923 AA. AC F3PE68; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EGF54618.1}; GN ORFNames=HMPREF9445_00277 {ECO:0000313|EMBL:EGF54618.1}; OS Bacteroides clarus YIT 12056. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=762984 {ECO:0000313|EMBL:EGF54618.1}; RN [1] {ECO:0000313|EMBL:EGF54618.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=YIT 12056 {ECO:0000313|EMBL:EGF54618.1}; 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 (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGF54618.1}. 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; AFBM01000004; EGF54618.1; -; Genomic_DNA. DR RefSeq; WP_009120486.1; NZ_GL882583.1. DR EnsemblBacteria; EGF54618; EGF54618; HMPREF9445_00277. DR PATRIC; 55012253; VBIBacCla162388_0264. DR GO; GO:0000786; C:nucleosome; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000558; Histone_H2B. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SMART; SM00427; H2B; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGF54618.1}; KW Transferase {ECO:0000313|EMBL:EGF54618.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 243 243 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 767 767 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 923 AA; 101201 MW; 33A60FBFC13DF634 CRC64; MASIETLVRE RILVLDGAMG TMIQQYNLTE EDFRGERFVQ IPGQLKGNND ILCLTRPDVI QDIHRKYLVA GADIIETNTF SSTSVSMADY HVQEYVREIN LAAVRLAREV ADEFTALTPD KPRFVAGSIG PTNKTCSMSP DVNNPAFRAL TYDELAAAYR EQMEAMLEAG VDALLIETIF DTLNAKAAIY AAEQAMEAIG VRVPLMLSVT VSDIGGRTLS GQTLEAFLAS VQHADIFSVG LNCSFGARQL KPFLEQLAAR APYYISAYPN AGLPNSLGTY DQTPAEMADE IREYVHEGLV NIIGGCCGTT DEYIAAYSSL IAGAVPHIPA SVPDNLWLSG LELLEVKPEN NFINVGERCN VAGSRKFLRL INEKKYDEAL SIARQQVEDG AQIIDINMDD GLLDAEKEMT TFLNLIASEP EIARVPVMID SSKWDVIVAG LKCAQGKSIV NSISLKEGEE KFLEHARTIK RYGAAAVVMA FDEQGQADTY ERRIEVCERA YRLLVDKVGF NPQDIIFDPN VLAVATGMDE HNNYAVDFIR ATGWIRKNLS GAHVSGGVSN LSFSFRGNNY IREAMHAVFL YHAIREGMDM GIVNPATSVL YTDIPVDILE RIEDVVLNRR PDAAERLIET AERLKAEAEA AKSSLSDGRS QLPAPNSQLA WREDTVEERL KYALTKGIGD YLEEDLAEAL KVYPKAVDII EGPLMAGMNH VGDLFGAGKM FLPQVVKTAR TMKKAVAVLQ PVIESEKQEG AASAGRVLLA TVKGDVHDIG KNIVSVVMAC NGYEIIDLGV MVPAETIVQR AIEEKVNMIG LSGLITPSLD EMVHVAIELE KAGLDIPLLI GGATTSPLHT ALKIAPVYHA PVIHLKDASQ NATVAARLMN PTQKEELVKK LSNEYQRLRE KNQEKQLETV SLEEAKANRL KLF // ID F3PQ17_9BACE Unreviewed; 920 AA. AC F3PQ17; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EGF59059.1}; GN ORFNames=HMPREF9446_00809 {ECO:0000313|EMBL:EGF59059.1}; OS Bacteroides fluxus YIT 12057. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=763034 {ECO:0000313|EMBL:EGF59059.1}; RN [1] {ECO:0000313|EMBL:EGF59059.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=YIT 12057 {ECO:0000313|EMBL:EGF59059.1}; 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 (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGF59059.1}. 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; AFBN01000013; EGF59059.1; -; Genomic_DNA. DR RefSeq; WP_009124066.1; NZ_GL882614.1. DR EnsemblBacteria; EGF59059; EGF59059; HMPREF9446_00809. DR PATRIC; 55019669; VBIBacFlu160465_0765. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGF59059.1}; KW Transferase {ECO:0000313|EMBL:EGF59059.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 243 243 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 764 764 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 920 AA; 101360 MW; C5E48A63F355B4DD CRC64; MASIEKLVRE RILILDGAMG TMIQQYNLTE EDFRGDRFLR IPGQLKGNND LLCLTRPDVV QDIHRKYLLA GADIIETNTF NSTRVSMADY HVQEYVREIN LAAAGLARRM ADEFTALTPG KPRFVAGSVG PTNKTCSMSP DVNNPAYRAL TYDALAADYR EQMEALLEGG VDALLVETIF DTLNAKAAVF AATQAMETTG IRVPLMLSVT VSDTVGRTLS GQTLEAFLAS VQHADVFSIG LNCSFGARQL KPFLEQLARR APYYISAYPN AGLPNSLGKY DQTPADMAHE IKEYIHEGLV NIIGGCCGTT DAYIAEYTAL VEGVTPHVPA PKPENLWLSG LELLEVRPEN NFVNVGERCN VAGSRKFLRL INEKKYDEAL SIARQQVEDG AQVIDINMDD GLLDTRTEMI TFLNLIASEP EIARVPVMID SSKWDVIVAG LKCLQGKSIV NSISLKEGEE KFLEHARTIQ QYGAAVVVMA FDEKGQADTF QRKIEVCERA YRLLTDKIGF NPHDIIFDPN VLAVATGMDE HNNYAVDFIK AAGWIRKNLP GAHVSGGVSN LSFSFRGHNY IREAMHAVFL YHAVREGMDM GIVNPATSVL YTDIPEDILE RLEDVVLNRR PDAAERLIET AERLKAETDT AKASGNVRHA VQSQLSWREN ATVEERLKYA LTKGIGDYLE EDLAEALEQY AKAVDIIEGP LMAGMNHVGD LFGAGKMFLP QVVKTARTMK KAVAILQPVI ESEKQEGSVS AGRVLLATVK GDVHDIGKNI VSVVMACNGY EIIDLGVMVP AETIVQRAME EKVDMIGLSG LITPSLDEMV HVALELEKSG LDIPLLIGGA TTSQLHTALR IAPVYHAPVI HLKDASQNAA VAAKLMNPES KEELSEELNE EYRRLREKNS ERQVKTVSLE EAQKNRLNLF // ID F3QYY2_9BACT Unreviewed; 920 AA. AC F3QYY2; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EGG50129.1}; GN ORFNames=HMPREF9442_03428 {ECO:0000313|EMBL:EGG50129.1}; OS Paraprevotella xylaniphila YIT 11841. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Paraprevotella. OX NCBI_TaxID=762982 {ECO:0000313|EMBL:EGG50129.1}; RN [1] {ECO:0000313|EMBL:EGG50129.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=YIT 11841 {ECO:0000313|EMBL:EGG50129.1}; 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 (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGG50129.1}. 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; AFBR01000095; EGG50129.1; -; Genomic_DNA. DR RefSeq; WP_008630251.1; NZ_GL883888.1. DR EnsemblBacteria; EGG50129; EGG50129; HMPREF9442_03428. DR PATRIC; 55049105; VBIParXyl161988_3077. DR OrthoDB; EOG6091CH; -. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGG50129.1}; KW Transferase {ECO:0000313|EMBL:EGG50129.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 242 242 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 764 764 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 920 AA; 100557 MW; F794AF9E7431B60F CRC64; MRLEEIVKER ILILDGAMGT MIQRYGLTEA DFRGGRFRDV PGLMAGNNDL LSLTRPDVIR DIHRKYLAAG ADIIETNTFS SQRVSMADYH VEDYCREINL AACRIARELA DEFTALNPEK PRFVAGSVGP TNKTCSMSPD VNNPAYRALT FDELVAAYRE QMEALLEGGV DALLVETIFD TLNAKAAIYA AEASMQTSGR KVPLMLSVTV SDKSGRTLSG QTMEAFLASV SHADIFSLGL NCSFGAHDLI PFLQVLAHRS PYYISVYPNA GLPNSMGEYD QTPTQMAEEM KFFVDKGWVN IIGGCCGTTD EYIARFPALA AQGRPHVPAG RAETLCLSGL EQFELTPEVR FVNVGERCNV AGSRKFLRLV KEKNYEEALE IARKQVEDGA LVIDINMDDG LLDARQEMVT FLNLLASEPE ISRVPVMIDS SKWDVITAGL KCVQGKSIVN SISLKEGEEV FLAHAREVKR LGAAVVVMAF DEKGQADTYE RKIEVCARAY RLLVDEVGFN PHDIIFDPNV LAIATGMEEH DNYAVDFIRA TGWIRRNLPG AHVSGGVSNL SFSFRGNNYI REAMHAVFLY HACREGMDMG IVNPATSVMY GDIPSDILTV IEDVVLNRRP DAAERLIELA DKLKAEAEAA KAGLSGAGGG GVPVTDAWRG GSVEERLQHA LVKGIDSYLQ EDLEEAAQSY PHAVDIIEGP LMKGMNTVGE LFGAGKMFLP QVVKTARTMK KAVGILQPRI EAGKKEGAAR AGLVLVATVK GDVHDIGKNI VSVVMACNNY EIVDLGVMTP AEEIVAKAKE LHPDIIGLSG LITPSLEEMV HVVGELKRAG LSIPVMIGGA TTSRLHTALK IAPVYDGPVI WMKDASQNAL TAARFLNPDT EGEAFRELRE EQERLRESAG TRRVETVSIE EARQKKLNLF // ID F3S4L9_9PROT Unreviewed; 1181 AA. AC F3S4L9; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 01-APR-2015, entry version 24. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGG78393.1}; GN ORFNames=SXCC_00990 {ECO:0000313|EMBL:EGG78393.1}; OS Gluconacetobacter sp. SXCC-1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Gluconacetobacter. OX NCBI_TaxID=1004836 {ECO:0000313|EMBL:EGG78393.1}; RN [1] {ECO:0000313|EMBL:EGG78393.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SXCC-1 {ECO:0000313|EMBL:EGG78393.1}; 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] {ECO:0000313|EMBL:EGG78393.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SXCC-1 {ECO:0000313|EMBL:EGG78393.1}; RA Du X., Jia S., Yang Y., Wang S.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGG78393.1}. 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; AFCH01000029; EGG78393.1; -; Genomic_DNA. DR RefSeq; WP_007396973.1; NZ_AFCH01000029.1. DR EnsemblBacteria; EGG78393; EGG78393; SXCC_00990. DR PATRIC; 55057270; VBIGluSp188091_0696. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 237 237 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 749 749 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1181 AA; 129783 MW; F83AD3EEACFD1AEC CRC64; MPCPLSADFR ITMTIRPHLL DALRDQVLLC DGGMGSRVQL LDLEVERDYW GQENCTEILN LSRPELVREI HRGYFEAGAD MVETNSFGGS PITLAEFGLA DRAREINRTA GHLAREAAET FADGRHRYVV GSIGPGTKLP SLGNIDYDTL EAGLTEQCRG LIEGGVDCFL IETCQDTLQI KAAVNGAKIA RAEMGVDTPI FVQVTVETTG TLLVGPDIAA AATVINALDV PLMGLNCATG PQEMAEHVRW LAENWPGLLS VQPNAGLPEL VNGTTHYPLT PAEMASWVER FITEDGLNLI GGCCGTSTPH TQALDQMLRK RAEGTGRIRP APVPRRPVWI PSVASLYSQV PLRQENSYFS IGERCNANGS KKWRQLQEAG DWDGCVALGR EQVAEGSNAL DICTAFVGRD EMREMNAVVT RFTSSVNAPL VIDSTETPVI EAALKLHGGK PIINSINFED GEAIATERML LARKFGASVI ALTIDEVGMA KTAEDKLRIA TRLVEFACEK HGLPQSDLMI DPLTFTIGTG TEDDRKLGEW TLEGIRLIRE RFPDIQIVLG LSNISFGLNP AARAVLNSVF LDHAVRAGMT AAIVHVSKIR PLHLIPAEEV KVAEDLIFDR RAEGYDPLQR ILEIFADRKA ADAVKKARAE TAPERLKDRI VDGDRKGLED DLAEAMRDMA PLDIINTVLL DGMKVVGELF GAGKMQLPFV LQSAETMKAA VAWLEPHMER TEGQARGTMV LATVKGDVHD IGKNLVDIIL TNNGYQVINL GIKVPVADMI AAARAHKADA IGMSGLLVKS TVIMRENLEE MQRQGLDVPV MLGGAALTRN YVEEDCTAAY GEGGRVAYAR DAFDGLSLMD KVVQGEFDTY LAAIQSRRAG KATRTSRTQD IEAAETRGFG PVDVAAARAR REKLTADEPV LVPPFWGPRV LEATPEAVLP FLNERSLYQF QWGFRKQGRS LDDFMVWARK ELRPVLRHML ALCAEQDILH PRASYGYWKA AGEGNDLVLF GEDGTNAVAR FTLPRQPRAD GACIADFVRD IDDAQRDVIG LQVVTVGQDA SDRAREWFEA DRYKDYLYLH GLSVEMAEAM AEYTHKRIRA EMGFAAEDDR DMAKLLQQGY RGSRYSFGYP ACPRLEEQEP ILKLLDAERI GVSLTDGFQL HPEQSTSALV ILNPHAKYFS I // ID F3SHV3_STRSA Unreviewed; 315 AA. AC F3SHV3; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 12. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGG40286.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EGG40286.1}; GN Name=mmuM {ECO:0000313|EMBL:EGG40286.1}; GN ORFNames=HMPREF9397_0725 {ECO:0000313|EMBL:EGG40286.1}; OS Streptococcus sanguinis SK1087. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=888824 {ECO:0000313|EMBL:EGG40286.1}; RN [1] {ECO:0000313|EMBL:EGG40286.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK1087 {ECO:0000313|EMBL:EGG40286.1}; 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 (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. {ECO:0000313|EMBL:EGG40286.1}. 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; AFDP01000009; EGG40286.1; -; Genomic_DNA. DR RefSeq; WP_002897633.1; NZ_GL883609.1. DR EnsemblBacteria; EGG40286; EGG40286; HMPREF9397_0725. DR PATRIC; 53718030; VBIStrSan172262_0708. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGG40286.1}; KW Transferase {ECO:0000313|EMBL:EGG40286.1}. SQ SEQUENCE 315 AA; 34733 MW; F820A09183302F3A CRC64; MGKFKDLLGK QEIIILDGAL GTELESLGYD VSGKLWSAQY LLDQPQIIQD VHESYVRADS DIITTSSYQA SIPVFIEAGL TPEKAYDLLK ETVFLAQKAI ENTWQALSPE EQKQRPYPLV AGSVGPYAAY LADGSEYTGD YQLSEEEYRD FHRPRIQALL EAGSDLLAIE TIPNGAEAAA ILRLLAEEFP QAEAYLSFVA QSENAISDGT KIEELGNLAQ ESPQVLAVGF NCTAPHLITP LLDGLGQVCN KPFLTYPNSG ETYNGLTKTW HDDPEQERSL LENSKLWQNQ GVRLFGGCCR TRPEDITQLA RGLKG // ID F3UB28_STRSA Unreviewed; 315 AA. AC F3UB28; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 12. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGJ39129.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EGJ39129.1}; GN Name=mmuM {ECO:0000313|EMBL:EGJ39129.1}; GN ORFNames=HMPREF9393_0751 {ECO:0000313|EMBL:EGJ39129.1}; OS Streptococcus sanguinis SK1056. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=888820 {ECO:0000313|EMBL:EGJ39129.1}; RN [1] {ECO:0000313|EMBL:EGJ39129.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK1056 {ECO:0000313|EMBL:EGJ39129.1}; 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 (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. {ECO:0000313|EMBL:EGJ39129.1}. 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; AFFL01000002; EGJ39129.1; -; Genomic_DNA. DR RefSeq; WP_002921364.1; NZ_GL890990.1. DR EnsemblBacteria; EGJ39129; EGJ39129; HMPREF9393_0751. DR PATRIC; 53781950; VBIStrSan174925_0732. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGJ39129.1}; KW Transferase {ECO:0000313|EMBL:EGJ39129.1}. SQ SEQUENCE 315 AA; 34717 MW; 49DA62974F8459A4 CRC64; MGKFKDLLDK QEIIILDGAL GTELESLGYN VSGKLWSAQY LLDQPQIIQN VHESYVRAGS DIITTSSYQA SIPAFIEAGL TPEKAYNLLK ETVFLAQKAI ENIWIGLSPE EQKQRPYPLV AGSVGPYAAY LADGSEYTGD YQLSEEEYRD FHRPRIQALL EAGSDLLAIE TIPNGAETAA ILRLLVEEFP QAEAYLSFVA QSENAISDGT KIEELGNLAQ ESPQVLAVGF NCTAPHLIAS LLGRLGQVCN KPLLTYPNSG ETYNGLTKTW HDDPEQERSL LENSKLWQEQ GVRLFGGCCR TRPEDIAQLS KGFKG // ID F3US34_STRSA Unreviewed; 315 AA. AC F3US34; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 12. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGJ38566.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EGJ38566.1}; GN Name=mmuM {ECO:0000313|EMBL:EGJ38566.1}; GN ORFNames=HMPREF9389_1642 {ECO:0000313|EMBL:EGJ38566.1}; OS Streptococcus sanguinis SK355. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=888816 {ECO:0000313|EMBL:EGJ38566.1}; RN [1] {ECO:0000313|EMBL:EGJ38566.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK355 {ECO:0000313|EMBL:EGJ38566.1}; 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 (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. {ECO:0000313|EMBL:EGJ38566.1}. 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; AFFN01000025; EGJ38566.1; -; Genomic_DNA. DR RefSeq; WP_002930349.1; NZ_GL890993.1. DR EnsemblBacteria; EGJ38566; EGJ38566; HMPREF9389_1642. DR PATRIC; 53793424; VBIStrSan170366_1609. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGJ38566.1}; KW Transferase {ECO:0000313|EMBL:EGJ38566.1}. SQ SEQUENCE 315 AA; 34683 MW; 0C5158E0779F51C1 CRC64; MGKFKDLLEK QEIIILDGAL GTELESLGYD VSGKLWSAQY LLDQPQIIQD VHESYVRAGS DIITTSSYQA SISAFIEAGL TPEKGYDLLK ETVFLAQKAI ENVWQELSPE EQKQRPYPLI AGSVGPYAAY LADGSEYTGD YQLSEGEFQE FHRPRIQALL EVGCDLLAIE TIPNGAEAAA ILRLLAEEFP QAEAYLSFVA QSENAISDGT KIEELGNLAQ ESPQVLAVGF NCTAPHLIAP LLDGLGQVCN KPFLTYPNSG ETYNGLTKTW HDDPEQKRSL LENSKLWQEQ GVQLFGGCCR TRPEDIAQLG KGFKD // ID F3UXY4_STRSA Unreviewed; 315 AA. AC F3UXY4; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 12. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGJ38504.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EGJ38504.1}; GN Name=mmuM {ECO:0000313|EMBL:EGJ38504.1}; GN ORFNames=HMPREF9380_1361 {ECO:0000313|EMBL:EGJ38504.1}; OS Streptococcus sanguinis SK49. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=888808 {ECO:0000313|EMBL:EGJ38504.1}; RN [1] {ECO:0000313|EMBL:EGJ38504.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SK49 {ECO:0000313|EMBL:EGJ38504.1}; 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 (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. {ECO:0000313|EMBL:EGJ38504.1}. 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; AFFO01000010; EGJ38504.1; -; Genomic_DNA. DR RefSeq; WP_002933835.1; NZ_GL890985.1. DR EnsemblBacteria; EGJ38504; EGJ38504; HMPREF9380_1361. DR PATRIC; 53797540; VBIStrSan170133_1328. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGJ38504.1}; KW Transferase {ECO:0000313|EMBL:EGJ38504.1}. SQ SEQUENCE 315 AA; 34750 MW; 8D5E247EEA37EEDB CRC64; MGKFKDLLDK QEIIILDGAL GTELERLGYD VSGKLWSAQY LLDQPQIIQD VHESYVRADS DIITTSSYQA SIPAFIEAGL TPEKGYNLLK ETVFLAQKAI ENIWIGLSPE EQKQRPYSLV AGSVGPYAAY LADGSEYTGD YQLSEEEYRN FHRPRIQALL EAGSDLLAIE TIPNGAEAAA ILQLLAEEFP QAEAYLSFVA QSENAISDGT KIEELGNLAQ ESPQVLAVGF NCTAPHLIAP LLDGLGQVCN KPFLTYPNSG ETYNGLTKTW HDDPEQGRSL LENSKLWQNQ GVRLFGGCCR TRPEDIAQLS KRFKG // ID F3VE91_SHIDY Unreviewed; 1130 AA. AC F3VE91; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 01-APR-2015, entry version 21. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGI89536.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGI89536.1}; GN Name=metH {ECO:0000313|EMBL:EGI89536.1}; GN ORFNames=SD15574_5042 {ECO:0000313|EMBL:EGI89536.1}; OS Shigella dysenteriae 155-74. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=766142 {ECO:0000313|EMBL:EGI89536.1}; RN [1] {ECO:0000313|EMBL:EGI89536.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=155-74 {ECO:0000313|EMBL:EGI89536.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AFFZ01000105; EGI89536.1; -; Genomic_DNA. DR EnsemblBacteria; EGI89536; EGI89536; SD15574_5042. DR PATRIC; 53816748; VBIShiDys163707_4981. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGI89536.1}; KW Transferase {ECO:0000313|EMBL:EGI89536.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1130 AA; 124982 MW; ABD99B140307C8B4 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAKWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG EEAKRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY // ID F3WQY0_SHIBO Unreviewed; 1227 AA. AC F3WQY0; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGI89055.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGI89055.1}; GN Name=metH {ECO:0000313|EMBL:EGI89055.1}; GN ORFNames=SB521682_4818 {ECO:0000313|EMBL:EGI89055.1}; OS Shigella boydii 5216-82. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=766141 {ECO:0000313|EMBL:EGI89055.1}; RN [1] {ECO:0000313|EMBL:EGI89055.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=5216-82 {ECO:0000313|EMBL:EGI89055.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AFGE01000071; EGI89055.1; -; Genomic_DNA. DR RefSeq; WP_000095998.1; NZ_AFGE01000071.1. DR EnsemblBacteria; EGI89055; EGI89055; SB521682_4818. DR PATRIC; 53853493; VBIShiBoy163146_4687. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGI89055.1}; KW Transferase {ECO:0000313|EMBL:EGI89055.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135971 MW; 1897151A02AA4119 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKD MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG EEAKRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID F3X015_9SPHN Unreviewed; 348 AA. AC F3X015; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EGI54422.1}; GN ORFNames=SUS17_2773 {ECO:0000313|EMBL:EGI54422.1}; OS Sphingomonas sp. S17. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingomonas. OX NCBI_TaxID=1007104 {ECO:0000313|EMBL:EGI54422.1}; RN [1] {ECO:0000313|EMBL:EGI54422.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=S17 {ECO:0000313|EMBL:EGI54422.1}; 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. {ECO:0000313|EMBL:EGI54422.1}. 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; AFGG01000014; EGI54422.1; -; Genomic_DNA. DR RefSeq; WP_007405891.1; NZ_AFGG01000014.1. DR EnsemblBacteria; EGI54422; EGI54422; SUS17_2773. DR PATRIC; 53859944; VBISphSp187231_2674. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGI54422.1}; KW Transferase {ECO:0000313|EMBL:EGI54422.1}. SQ SEQUENCE 348 AA; 37504 MW; 62F4B44E400C76EC CRC64; MTTRDIFLAE AATRILITDG AFGTEIQNWK LDEAAYAGTL GLTHDQKGNN DILALTKPEV PEAIHRAYFE AGADIAETNT FSANRISQAD YGAEHLVREI NVESAKLARR IADEFQAKDG RPRFVAGAIG PTNKTLSLSP DVNDPGYREI DFDYLKDVYR EQIDALVEGG ADFILIETVF DTLNAKAGIM ATIEAGEALG REIPIMLSMT LTDLSGRNLS GHTVEAFWHA VRHAKPLTIG LNCSFGAEQL RPHVKTLSEI CDTLIMIYPN AGLPNELGAY DEAPVTTAGL VGEWAVEGQV NVLGGCCGST PAHIKAIADK VKGMKPRTIP TPPVVTRLAG LEPFTMAA // ID F3Z3X5_DESAF Unreviewed; 802 AA. AC F3Z3X5; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGJ50427.1}; GN ORFNames=Desaf_2098 {ECO:0000313|EMBL:EGJ50427.1}; OS Desulfovibrio africanus str. Walvis Bay. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=690850 {ECO:0000313|EMBL:EGJ50427.1, ECO:0000313|Proteomes:UP000007844}; RN [1] {ECO:0000313|EMBL:EGJ50427.1, ECO:0000313|Proteomes:UP000007844} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Walvis Bay {ECO:0000313|EMBL:EGJ50427.1}; 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 ----------------------------------------------------------------------- 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; EGJ50427.1; -; Genomic_DNA. DR RefSeq; WP_014260171.1; NC_016629.1. DR RefSeq; YP_005052086.1; NC_016629.1. DR EnsemblBacteria; EGJ50427; EGJ50427; Desaf_2098. DR KEGG; daf:Desaf_2098; -. DR KO; K00548; -. DR BioCyc; DAFR690850:GHYW-2128-MONOMER; -. DR Proteomes; UP000007844; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007844}; KW Reference proteome {ECO:0000313|Proteomes:UP000007844}. SQ SEQUENCE 802 AA; 85297 MW; F9291E218A3DBA55 CRC64; MPDFRTALND QALHLFDGAY GTLLQKRGLP AGMSPELFGL ERPDVLRGLH EEYLAAGARI LTTNTFGGTA PKLGKGVDVR AFNRATVEIA RQAADDRAFV AGSVGPTGLF VEPLGPISFR DMVALFIEQI RGLVEGGADL IKAETHFDLA EAKAVVVAAR EVCDLPVLVS MTYEGKTSLT GTPPDTFVDT MQNLGVDVVG VNCGTGPEEM AALVELMRRR LETRYHVQPN AGLPRLENGR TVFPLGPEEF ATKTARFAEL GAKFLGGCCG TSPEHIAALA AALQGKTWTR LAPPENPCLV LTTRGGSVAV DHALPLVLIG ERINPTGKKK LAEELQSGVF GEALSMAAEQ LATGAGILDV NVGAPMVKEA EVLPALVKAL SERFDAPLAI DTTDIQAMAA SLWACAGSPL VNSISGEPGR LEELGPLCKK LGTPFILLPL AGKKLPVTAS ERLAAIESLL RKADDLGIPR RLIMVDALAL TVSSKPEAAK SCFSVIRHCR DVWRLPTVLG LSNISFGLPA RELVNSTFLA MCMAEGLTAC IANPGSTRLR EALAAAEVLL GRDPQAGRFI AGFSAWKPGE AGPSAGLRMS GPDAAAATPR EAVIRGDKER LVPLLEAALE RGDNPFDLVD KELIPGIMEV GEKYERREYF LPQLMLSAET VQLGFERLRP LLEQSGRDEA RPRIVMATVE GDIHDIGKNI VCLLLRNHGF DVLDLGKDVP AAAIVDAARC HDARLIGLSA LMTTTMVRME EVVKLVRESG LQAKIIIGGA VVSQRYAEAI GADGYAKDAV AAVRLAKQLV SA // ID F3Z6H0_9ACTO Unreviewed; 1171 AA. AC F3Z6H0; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 01-APR-2015, entry version 22. DE SubName: Full=Putative 5-methyltetrahydrofolate:homocysteine S-methyltransferase {ECO:0000313|EMBL:EGJ78487.1}; GN ORFNames=STTU_5698 {ECO:0000313|EMBL:EGJ78487.1}; OS Streptomyces sp. Tu6071. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=355249 {ECO:0000313|EMBL:EGJ78487.1, ECO:0000313|Proteomes:UP000003955}; RN [1] {ECO:0000313|Proteomes:UP000003955} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21705604; DOI=10.1128/JB.00377-11; RA Erxleben A., Wunsch-Palasis J., Gruning B.A., Luzhetska M., RA Bechthold A., Gunther S.; RT "Genome sequence of Streptomyces sp. strain Tu6071."; RL J. Bacteriol. 193:4278-4279(2011). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CM001165; EGJ78487.1; -; Genomic_DNA. DR RefSeq; WP_007828970.1; NZ_CM001165.1. DR EnsemblBacteria; EGJ78487; EGJ78487; STTU_5698. DR Proteomes; UP000003955; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000003955}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGJ78487.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000003955}; KW Transferase {ECO:0000313|EMBL:EGJ78487.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 237 237 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 747 747 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1171 AA; 127374 MW; 6A7B84DA0AEF0CC7 CRC64; MAHPSPHAAD DATRVTALRE ALASRVVVAD GAMGTMLQAQ NPTLEDFQDL EGCNEVLNVT RPDIVRSVHE AYFDVGVDCV ETNTFGANHS AFGEYEIADR IHELSEAGAR LARETADSYT ARDGRTRWVL GSIGPGTKLP TLGHLPYGVL RDGFQQNAEG LLAGGADALI VETTQDLLQT KASVLGARRA LDALGADVPL IVSLAFETTG TMLLGSEIGA ALTALEPLGI DLIGLNCSTG PAEMSEHLRY LAQHSRIPLT CMPNAGLPVL TKDGAHFPLT APEMADWQES FVNDYRLSLV GGCCGSTPEH LRQVVERVRG MAPGTREPQP EPGAASLYQT VPFRQDTSYL AIGERTNANG SKKFREAMLE ARWDDCVEMA REQIREGAHM LDLCVDYVGR DGVADMRELA GRFATASTLP LVLDSTEVDV LEAGLEMLGG RAVINSVNYE DGDGPESRFA QVTSLAREHG AALIALTIDE EGQARTVETK VAVAERLIAD LTGNWGIHES DILVDCLTFT ICTGQEESRK DGIATIEAIR ELKRRHPDVQ TTLGLSNISF GLNPAARILL NSVFLDECVK AGLDSAIVHA SKILPIARFS EEEVATALDL VHDRRAEGYD PLQKLMRLFE GATAKSLKAG KAEELAALPL DERLKRRIID GERNGLEADL DEALQTRPAL DIVNATLLDG MKVVGELFGS GQMQLPFVLQ SAEVMKTAVA HLEPHMEKSD AEGKGTIVLA TVRGDVHDIG KNLVDIILSN NGYNVVNLGI KQPVSAILEA AEEHRADVIG MSGLLVKSTV IMKENLQELN QRGMAADYPV ILGGAALTRA YVEQDLHEIY EGEVRYARDA FEGLRLMDAL IGVKRGVPGA TLPELKQRRV RPTASAVVTE LAEEEGQVRS DVATDNPVPA PPFWGSRVVK GIPLKDYASW LDEGALFKGQ WGLKQNRTGE GPGYEELAET EGRPRLRGWL DHLQTENLLE AAVVYGYFPC VSKGDDVILL GEDGSERTRF TFPRQRRGRR LCLADFFRPE ESGETDVIGL QVVTVGSRIG EATGKLFAAD AYRDYLELHG LSVQLAEALA EYWHARVRAE LGFAGEDPAD VEDMFALKYR GARFSLGYGA CPNLEDRAKI AALLEPERIG VQLSEEFQLH PEQSTDALVI HHPEAKYFNA R // ID F3ZSM4_9BACE Unreviewed; 1227 AA. AC F3ZSM4; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGJ70898.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGJ70898.1}; GN ORFNames=Bcop_0680 {ECO:0000313|EMBL:EGJ70898.1}; OS Bacteroides coprosuis DSM 18011. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=679937 {ECO:0000313|EMBL:EGJ70898.1, ECO:0000313|Proteomes:UP000018439}; RN [1] {ECO:0000313|EMBL:EGJ70898.1, ECO:0000313|Proteomes:UP000018439} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 18011 {ECO:0000313|EMBL:EGJ70898.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CM001167; EGJ70898.1; -; Genomic_DNA. DR RefSeq; WP_006744054.1; NZ_CM001167.1. DR EnsemblBacteria; EGJ70898; EGJ70898; Bcop_0680. DR Proteomes; UP000018439; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000018439}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGJ70898.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000018439}; KW Transferase {ECO:0000313|EMBL:EGJ70898.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 764 764 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 137015 MW; 162A0F2AB0D14C0F CRC64; MNSNFDLIRN LIQEKILVLD GAMGTMLQSY SFSEKDFRGT LFTDSTIPLK GNNDVLSLTQ PQAVQAIHEA YLEVGADIIE TNTFSSTTIA QNDYNLGEYV YELNFKSAQL AKKAAEHYTQ LTPNKPRFVA GTLGPTNKTA SLSPDVNRPS YRAVSFQDLY VAYKQQAEAL IDGGCDLLLV ETVFDTLNAK AALFAITDIN KERNISIPIM LSGTITDASG RILSGQTIEA FAISVSHIPL LSIGLNCAQG AKQLIPYLIQ LGKEVRIPLS VHPNAGLPNE FGHYDQTPEQ MGNDILSFIN NPQVRIVGGC CGTTPKHIKC IALLVDKQNQ QTPLFKQAEE AQILKLSGLE PFRYTDNITF VNIGERTNVT GSKKFLRLIQ NKNYEEALEI AREQVEGGAQ ILDVNMDEGL LNGTEEMTTF LNLIASEPDI ARIPIMIDSS KWEVIEAGLQ CLQGKGVVNS ISLKEGEKKF ITYAQKIKQY GAAVVVMAFD ENGQADSLER RIEICQRSYN LLVHKVHFPA ANIIFDPNVF PVATGMEEHK NNAIDFFKST KWIKNNLPFA NISGGISNVS FSFRGNNTVR EAMHSIFLYH GIKHGLTMGI LNPTILEIYN EIEPRLLELI ENVFFNRKKN ATDTLLQYAE SLKGKVENTA TPNLVWREGC LQERINHALI KGISTFIEQD VEEARQSVEH PIQIIEGHLM IAMNLVGQLF GDGKMFLPQV VKSARVMKQA VTYLLPFIEK LKAQDQLNAS KPKIVLATVK GDVHDIGKNI VSVVLACNNY HIIDLGVMVP TENIIQTVLA EQADIIGLSG LITPSLDEMI HVAQELEKAQ CTIPLMIGGA TTTKLHTALK IAPEYSAPVI HVKDASRSVS VASLLLNPET APTFINQIKE EYEGICIQYK NRKEPRKFIP LDEARKNKFS TNWNLYTPIL PKDKGIQVKQ LDVQQLIPYI DWTPFFSAWE LHGKFPDLLD DAVVGESATS LYQDAKAFLK KIIENKWILP KAIYEFLPAN QVNEDDIEVY DEQGKILETI PTLRQQMKKN NGSPNFALAD FIAPKSSGKK DYIGFFCVSS GFGVDEKVQK LKKEGDDYTA LLLSSLSDRL AEASAEYLHE YVRKKAWGYV PDESLSYKDL LDETYQGIRP APGYPACPDH QQKGTLWKLL QIDKNIGVRI TTNYAMHPAS SISGYYFSHP QSKYFAIGKI NSDQIEDYAK RRGQKPEEIQ HWLAAYI // ID F3ZX27_MAHA5 Unreviewed; 618 AA. AC F3ZX27; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 27. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=Mahau_0258 {ECO:0000313|EMBL:AEE95476.1}; 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 {ECO:0000313|EMBL:AEE95476.1, ECO:0000313|Proteomes:UP000008457}; RN [1] {ECO:0000313|Proteomes:UP000008457} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15567 / CIP 107919 / 50-1 BON RC {ECO:0000313|Proteomes:UP000008457}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; AEE95476.1; -; Genomic_DNA. DR RefSeq; WP_013779909.1; NC_015520.1. DR RefSeq; YP_004462298.1; NC_015520.1. DR EnsemblBacteria; AEE95476; AEE95476; Mahau_0258. DR KEGG; mas:Mahau_0258; -. DR PATRIC; 54629064; VBIMahAus157719_0268. DR KO; K00547; -. DR BioCyc; MAUS697281:GH33-260-MONOMER; -. DR Proteomes; UP000008457; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008457}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:AEE95476.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000008457}; KW Transferase {ECO:0000313|EMBL:AEE95476.1}. SQ SEQUENCE 618 AA; 66838 MW; 55C55F77A026DB18 CRC64; MRGEKDFLTA LKYKTLLCDG AMGTMLRERG ADSEACLEYM NISQPDMVLT LHKDYIGAGA DIIETNTFGA NRFKLAIYGL EDRVADINRQ AVKLARQAAG NNIWVLGAVG PIGLPLIPVN EKDRGDIYEA YGEQIEALCC EGVDAIIAET MGSTLEAEMA IKAAKDAADI PVICQFSLLP DGFDSSGESL QSVAEFLKHC NADVVGLNCG SGPRDMVEFM KFIAEYTDGS KFLSIQPNAG FAYYAQGRLQ YKAKADYFAS YVKDYIGLKV NIIGGCCGTT PQHIAAMRSV LNENTSLETS NMIAMEPGTI TAEVSRSELT QAGIAMAGNI LEKIKQKFVV TVEMDPPKGT DIEKALAGAR ALKSCGVDAV NIADSPMARV RVSPIALAAR IKQEVGLDAI LHFTCRDRNL IGIQSELIGA AVLGINNVLA LTGDPPSIGD HPKATGVFDI TSEGLVYILG ALNQGRDYMG NVLEGSTNFA IGVAFNPNAD DLKAELEKLD KKIENGANFI QTQPIYDMQT VEKMVKNIAD YNIPVLMGVL PLRSYKHAEF LHNEVPGITI PLDIRQRMKN AGDNALDEGV AIAAELIKQC RGMVSGVYIM PPFGRYDMVE KIMAEIAW // ID F4A0H5_MAHA5 Unreviewed; 413 AA. AC F4A0H5; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 01-APR-2015, entry version 18. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AEE95854.1}; GN OrderedLocusNames=Mahau_0651 {ECO:0000313|EMBL:AEE95854.1}; 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 {ECO:0000313|EMBL:AEE95854.1, ECO:0000313|Proteomes:UP000008457}; RN [1] {ECO:0000313|Proteomes:UP000008457} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15567 / CIP 107919 / 50-1 BON RC {ECO:0000313|Proteomes:UP000008457}; 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 ----------------------------------------------------------------------- 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; AEE95854.1; -; Genomic_DNA. DR RefSeq; WP_013780287.1; NC_015520.1. DR RefSeq; YP_004462676.1; NC_015520.1. DR EnsemblBacteria; AEE95854; AEE95854; Mahau_0651. DR KEGG; mas:Mahau_0651; -. DR PATRIC; 54629903; VBIMahAus157719_0670. DR KO; K00548; -. DR BioCyc; MAUS697281:GH33-670-MONOMER; -. DR Proteomes; UP000008457; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008457}; KW Methyltransferase {ECO:0000313|EMBL:AEE95854.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008457}; KW Transferase {ECO:0000313|EMBL:AEE95854.1}. SQ SEQUENCE 413 AA; 43921 MW; D66288D703855380 CRC64; MGKDFIPYLN EHFVIFDGAM GTMLQQKKAG IDRCPEELNI ADPDVIISIH KAYKNAGSDV IETNTFGANA LKLARWGLSA QADAINAAAV KLARDVMGDD GWVAVSVGPT GHLMRPFGDL SFDDAYNAFK SQILAAASAG ADIICIETMS DINEARAAIL AAKENTGLPI TATMTFEANG RTLMGNDAVS ATLALESAGA DVVGVNCSGG VEVAYEAIKQ MADYSSVPLM AQPNAGMPHD QDGITVYPLG PEEMLRWMDD FAKAGAAVLG GCCGTTPEHI KLLADKFKGR KRSPAVNPKM TNIISSGSKS VDVSRIESLC EINVACDDPT SSVMNAVSEA ADAIVLDFTA WDGSESDVYE LLNDITSLCR IPLIFKNARY DILAWLLRYY GGVAGVIGDA DRALVNRYKA VIM // ID F4A5B5_CLOBO Unreviewed; 788 AA. AC F4A5B5; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase, putative {ECO:0000313|EMBL:AEB76662.1}; GN ORFNames=CbC4_1990 {ECO:0000313|EMBL:AEB76662.1}; OS Clostridium botulinum BKT015925. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=929506 {ECO:0000313|EMBL:AEB76662.1, ECO:0000313|Proteomes:UP000007806}; RN [1] {ECO:0000313|EMBL:AEB76662.1, ECO:0000313|Proteomes:UP000007806} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BKT015925 {ECO:0000313|EMBL:AEB76662.1}; 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; AEB76662.1; -; Genomic_DNA. DR RefSeq; WP_013726174.1; NC_015425.1. DR RefSeq; YP_004396659.1; NC_015425.1. DR EnsemblBacteria; AEB76662; AEB76662; CbC4_1990. DR KEGG; cbn:CbC4_1990; -. DR PATRIC; 54459308; VBICloBot178872_2308. DR KO; K00548; -. DR BioCyc; CBOT929506:GHKW-2023-MONOMER; -. DR Proteomes; UP000007806; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007806}; KW Methyltransferase {ECO:0000313|EMBL:AEB76662.1}; KW Transferase {ECO:0000313|EMBL:AEB76662.1}. SQ SEQUENCE 788 AA; 86880 MW; 299FC866806E372B CRC64; MIDINKFLLK KHIFFDGAMG TMLQNRGISL GEVPPEIYNI LNPKVIKDIH KKYIDAGVDI ITTNTFGANE LKLKDSGYSV EKVIEAGVKL AKEVSNGKLV ALDIGPTGEM LEPMGDLKFE RAYEIFKSQV IAGVNAGCDI ILIETISDLY EAKAAILAAK ENSSLPVFCT MTFGEDGRTF TGTDPITMVS VLEGLSVDAL GINCSLGPKE MLPVMEKIIK YSSIPVIAQP NAGLPRVVDG KTIFDITPEE FAFYQKQMAS LGVSILGGCC GTTDKYIKVV IDELKNSIPK KILKKDKTMI SSYCKTVILG EGIKVVGERI NPTGKEEFKE AIKSNNISYI LNEAISQRAC GAHILDINVG LPGIDEKDIM VKTIKNLQST VDIPLQIDSA DCDVIEAATR IYNGKPIINS VNGKQESMKN IFPIVKKYGA CVIALTLDEN GIPTTIEDRV KIAEKIINTA KEYGIDKKDI IVDCLVLTAS AQQKEVMETL DALGIIKEKF KVKTILGISN ISFGLPKREL MNRTFLTMAL TKGLDVPILN PNDRDIMETI KSFEVLANID TNCENYIGEI SNLKKEVKYN NKKINLKDIV VNGVLDEVEN VTKELLKTKD GVEIIEKYLI PALDLVGNDY EEGKIFLPQL IKCGETVKKS FQIIKDNIKK YNKKDVVKGK IVLATVKDDI HDIGKNIVKL LLENYGFEVV DLGKNVSVET ILEVVKKYNI KLVGLSALMT TTVKSMEETI SRLKEVNPIC KVFVGGAVLN EEYAKQIGAD YYAKDARESV LIANEIFK // ID F4ALJ2_GLAS4 Unreviewed; 296 AA. AC F4ALJ2; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AEE23821.1}; GN OrderedLocusNames=Glaag_2884 {ECO:0000313|EMBL:AEE23821.1}; OS Glaciecola sp. (strain 4H-3-7+YE-5). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Glaciecola. OX NCBI_TaxID=983545 {ECO:0000313|EMBL:AEE23821.1, ECO:0000313|Proteomes:UP000006544}; RN [1] {ECO:0000313|EMBL:AEE23821.1, ECO:0000313|Proteomes:UP000006544} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4H-3-7+YE-5 {ECO:0000313|EMBL:AEE23821.1, RC ECO:0000313|Proteomes:UP000006544}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; AEE23821.1; -; Genomic_DNA. DR RefSeq; WP_013754198.1; NC_015497.1. DR RefSeq; YP_004435089.1; NC_015497.1. DR EnsemblBacteria; AEE23821; AEE23821; Glaag_2884. DR KEGG; gag:Glaag_2884; -. DR PATRIC; 54579534; VBIGlaSp182133_3048. DR BioCyc; GSP983545:GH3Q-2948-MONOMER; -. DR Proteomes; UP000006544; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006544}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:AEE23821.1}; KW Transferase {ECO:0000313|EMBL:AEE23821.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 204 204 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 275 275 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 276 276 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 296 AA; 31952 MW; 493669B0235AA1D4 CRC64; MSKITLLDGG MGQELLRRSS REVTPMWSAD IMLNEPTLVR DLHCEFIESG ARVITLNTYT ATPQRLKREN ELAQLEHLHH AAMRAAQDAI KLSQRNDVAI AGSLPPLVAS YHPEVSLSFE DSLETYRQLV QLQSPASDIF ICETMSSVNE AKAACTAAKE SGKPVWVAFS VSDSHPEQLR SGESLKEALA ALETLAPEAI LLNCSQPEAI SACWPLMQAS GAKIGAYANG FVSIDALYPG DTVEALEMRN DLSPAHYAAH AMNWVDNGAS IIGGCCEIGP AHIKALALKL QSEGLL // ID F4ATM0_GLAS4 Unreviewed; 352 AA. AC F4ATM0; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AEE22269.1}; GN OrderedLocusNames=Glaag_1308 {ECO:0000313|EMBL:AEE22269.1}; OS Glaciecola sp. (strain 4H-3-7+YE-5). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Glaciecola. OX NCBI_TaxID=983545 {ECO:0000313|EMBL:AEE22269.1, ECO:0000313|Proteomes:UP000006544}; RN [1] {ECO:0000313|EMBL:AEE22269.1, ECO:0000313|Proteomes:UP000006544} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4H-3-7+YE-5 {ECO:0000313|EMBL:AEE22269.1, RC ECO:0000313|Proteomes:UP000006544}; 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; AEE22269.1; -; Genomic_DNA. DR RefSeq; WP_007989932.1; NC_015497.1. DR RefSeq; YP_004433537.1; NC_015497.1. DR EnsemblBacteria; AEE22269; AEE22269; Glaag_1308. DR KEGG; gag:Glaag_1308; -. DR PATRIC; 54576111; VBIGlaSp182133_1373. DR BioCyc; GSP983545:GH3Q-1341-MONOMER; -. DR Proteomes; UP000006544; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006544}; KW Methyltransferase {ECO:0000313|EMBL:AEE22269.1}; KW Transferase {ECO:0000313|EMBL:AEE22269.1}. SQ SEQUENCE 352 AA; 38106 MW; 0F51EB2D0F952179 CRC64; MSRVSSEQAL IDAAKSRILV LDGAMGTMIQ AHDFQENDYR GERFADWHSD VKGNNDLLTL TQPEAIYNIH CAYFAAGADI IETNTFNATT ISMADYNMQS LAKEINIESA KLARKAADKF TAQTPEKPRF VAGVLGPTSR TASISPNVND PGERNVTFDE LVEAYVEATH GLIEGGVDLI MVETIFDTLN AKAALFAVDT VFESLGKTLP IMISGTITDA SGRTLSGQTA EAFYYSMRHT SPFSFGLNCA LGPDLLRQYV DEVSTVAECL VSAHPNAGLP NEFGEYDLES DEMAEHIREW AQSGLVNIVG GCCGSTPEHI AAIAQAVEGV APRVIPQHDI KLRLSGLEPF VH // ID F4AV61_DOKS4 Unreviewed; 332 AA. AC F4AV61; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AEE18734.1}; GN OrderedLocusNames=Krodi_0750 {ECO:0000313|EMBL:AEE18734.1}; OS Dokdonia sp. (strain 4H-3-7-5) (Krokinobacter sp. (strain 4H-3-7-5)). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Dokdonia. OX NCBI_TaxID=983548 {ECO:0000313|EMBL:AEE18734.1, ECO:0000313|Proteomes:UP000008290}; RN [1] {ECO:0000313|EMBL:AEE18734.1, ECO:0000313|Proteomes:UP000008290} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4H-3-7-5 {ECO:0000313|EMBL:AEE18734.1, RC ECO:0000313|Proteomes:UP000008290}; 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). RN [2] {ECO:0000313|Proteomes:UP000008290} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4H-3-7-5 {ECO:0000313|Proteomes:UP000008290}; 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 [3] 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; AEE18734.1; -; Genomic_DNA. DR RefSeq; WP_013750242.1; NC_015496.1. DR RefSeq; YP_004430002.1; NC_015496.1. DR EnsemblBacteria; AEE18734; AEE18734; Krodi_0750. DR KEGG; kdi:Krodi_0750; -. DR PATRIC; 54568579; VBIKroSp190710_0780. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR BioCyc; KSP983548:GHAF-762-MONOMER; -. DR Proteomes; UP000008290; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008290}; KW Methyltransferase {ECO:0000313|EMBL:AEE18734.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008290}; KW Transferase {ECO:0000313|EMBL:AEE18734.1}. SQ SEQUENCE 332 AA; 36200 MW; AE2F11307022C51F CRC64; MKSQLTRALQ ERILVLDGAM GTMLQAYNFS EEDFRGERFK DFHLSVKGNN DMLSLTQPAA IAEVHRKYFE AGADIVETNT FSSTTIAMAD YEMEEYVYDL NYASAKIAKE VAQSFTEKEP HKPRFVAGSI GPTNKTASMS PDVNDPGYRA VSFEELRVAY KQQVEALLDG GVDMLLVETV FDTLNAKACL FAIEEVKEER NSGIPIMVSG TITDASGRTL SGQTAVAFLI SISHIPLLSV GFNCALGASQ LQPHLEAIAN VTNYGISAHP NAGLPNAFGE YDETPEQMAT QIKKYIDKNL VNIVGGCCGT TPAHIKAIAQ LVENVTPRKC KL // ID F4C4Y7_SPHS2 Unreviewed; 1230 AA. AC F4C4Y7; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 01-APR-2015, entry version 26. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADZ76961.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADZ76961.1}; GN OrderedLocusNames=Sph21_0379 {ECO:0000313|EMBL:ADZ76961.1}; OS Sphingobacterium sp. (strain 21). OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Sphingobacterium. OX NCBI_TaxID=743722 {ECO:0000313|EMBL:ADZ76961.1, ECO:0000313|Proteomes:UP000007808}; RN [1] {ECO:0000313|Proteomes:UP000007808} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=21 {ECO:0000313|Proteomes:UP000007808}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002584; ADZ76961.1; -; Genomic_DNA. DR RefSeq; WP_013663690.1; NC_015277.1. DR RefSeq; YP_004315631.1; NC_015277.1. DR EnsemblBacteria; ADZ76961; ADZ76961; Sph21_0379. DR KEGG; shg:Sph21_0379; -. DR PATRIC; 47234420; VBISphSp165585_0413. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; SSP743722:GH04-388-MONOMER; -. DR Proteomes; UP000007808; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007808}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADZ76961.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007808}; KW Transferase {ECO:0000313|EMBL:ADZ76961.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 763 763 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1230 AA; 136190 MW; 54BE33DDAC285C40 CRC64; MSIREELNKR ILIIDGAMGT MIQPYGLSEA DFRGERFINH PCEVKGNNDL LNITQPLIIK EIHEAYLEAG ADIIETNTFS SQVISMADYQ MESLVYELNY EGARIAKEAA TQFTHKNPAK PRFVAGAIGP TNRTASLSPD VNDPGYRAVT FDDLVNAYYE QVRGLIDGGA DVLLIETIFD TLNAKAAIFA IIQYENELKA AGKRSESIDI MISGTITDAS GRTLSGQTVE AFLNSINHGN ILSIGLNCAL GAKEMRPHIE ELSEKAGCYV SAYPNAGLPN EFGGYDEQPH ETAHLIEDFI ESGFVNIVGG CCGTTPKHIR CIADKAAKAK PRKVPKPEPF LRLSGLEPIT YTPNSVFMNI GERTNVTGSP KFAKLILSGD FEAALSVARQ QVEGGAQVID VNMDEGMLDS EAAMTRFLNL IASEPDIAKL PIMVDSSKWS VIEAGLKCLQ GKGIVNSISL KEGEDLFKER ATTIMHYGAA VVVMAFDEVG QADSYERRIE ICKRSYDILV NEVGFPPQDI IFDPNILTVA TGLEEHNNYA VDFINATQWI KQNLPLAKVS GGVSNISFSF RGNNVVREAM HAAFLYHAIK AGLDMGIVNA GMLEVYEEID PTLLTYVEDV LLNRREDATE RLVEFAETVK SKDKAEVKSA EWRSGPVEER LSHALVKGII EFLDDDVEEA RLKYPRPLEV IEGPLMDGMN IVGDLFGAGK MFLPQVVKSA RVMKKAVAYL LPFIEAEKAK NPSAGDRKNA GKILMATVKG DVHDIGKNIV GVVLACNNFE IIDLGVMVPS QKILDEARKH QVDIIGLSGL ITPSLDEMVH VAKEAEREGF KIPIMIGGAT TSRIHAAVKI APNYSGTIVH VLDASRSVTV ASNLLNPESK ESYAATIRAE YDQARENHLR KKSEKKLVPI EEARAKRFQI NWESYQAPKP AFLGTKVFDD FPLDDLLPYI DWTPFFHTWE LRGSYPRILT DKTVGTEASK LFDDAKKLLQ EIVSNKLLTA KGVIGFWPAN TAGDDIVLYK DEERKEILTR IHTLRQQAEK AKDQPYYALS DFIAPVGSRV NDYWGGFAVT TGIGCDKLVA EYEKNYDDYN SIMVKALADR LAEAFAEKMH EMVRKEYWGY SSDEQLSNEE LIKEQYAGIR PAPGYPACPE HTEKITLFNI LDAEENTGIY LTESLAMHPT AAVSGFYFSH PESRYFGVGK LGKDQIEDYA KRKNETVEVV ERWLGPNLGY // ID F4CJ93_PSEUX Unreviewed; 603 AA. AC F4CJ93; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 30. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=Psed_2107 {ECO:0000313|EMBL:AEA24332.1}; 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 {ECO:0000313|EMBL:AEA24332.1, ECO:0000313|Proteomes:UP000007809}; RN [1] {ECO:0000313|EMBL:AEA24332.1, ECO:0000313|Proteomes:UP000007809} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 55486 / DSM 44775 / JCM 13855 / CB1190 RC {ECO:0000313|Proteomes:UP000007809}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {ECO:0000256|RuleBase:RU004255}. CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; AEA24332.1; -; Genomic_DNA. DR RefSeq; WP_013674263.1; NC_015312.1. DR RefSeq; YP_004332185.1; NC_015312.1. DR EnsemblBacteria; AEA24332; AEA24332; Psed_2107. DR KEGG; pdx:Psed_2107; -. DR PATRIC; 54395677; VBIPseDio141225_2122. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR BioCyc; PDIO675635:GHMF-2141-MONOMER; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000007809; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004255}; KW Complete proteome {ECO:0000313|Proteomes:UP000007809}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:AEA24332.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000007809}; KW Transferase {ECO:0000313|EMBL:AEA24332.1}. SQ SEQUENCE 603 AA; 62425 MW; 56DEE8FF7A86A182 CRC64; MNVRELLTTS VLVGDGAMGT MLHAAGNSLD QALPALNLTE PELVRTIHDS YVGAGVDLVQ TNTFGASRLR LAEYGAADDV ARINAAGARL AREAAARADR AVLVAGSVAP AVSVHQRRRV AAEERRAAVR EQVEVLVGAG VDVVLLETFG HLDELVEASE VALEVARRTG DVPVIAQATF GSDRHTLSGH TPHEVVTALA GFPLAAMGVN CTLGPQGCLA VLRELRVHTA VPLTVQPNAG LPRRVGPARF EYDIDADYFV RYTRQLLDAG AALVGGCCGT TPSQLAAAAA AVAEHRSQRA AEVAERVAAT AVVPERPETD GPFSAPGHVV AVELRPAPTG GVDEALELAA ELQQAGVGLV SVAASSSPRA QVNSVDLALH LHNRLGLTTL ASVTTWDRTI MALQADLLGA HALGVRGVVC ETGTPPLLGD YPHVDGIWDV DSLGLIELLA GLNDGTDYHG LRLGTKTSFE IGARVNPGSR DPGRAAAGAL DKIAAGAQFL ITRPVHELAG LERVLEAVDG RVPVLVAVRP LTGFDEADYL AHEVPDVTIP AATLAALQDA GPDARAAGID LAVALADQVR GMAKGVVVTG GSDVVEAVRR LLG // ID F4CX75_PSEUX Unreviewed; 1190 AA. AC F4CX75; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEA25516.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEA25516.1}; GN OrderedLocusNames=Psed_3326 {ECO:0000313|EMBL:AEA25516.1}; 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 {ECO:0000313|EMBL:AEA25516.1, ECO:0000313|Proteomes:UP000007809}; RN [1] {ECO:0000313|EMBL:AEA25516.1, ECO:0000313|Proteomes:UP000007809} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 55486 / DSM 44775 / JCM 13855 / CB1190 RC {ECO:0000313|Proteomes:UP000007809}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002593; AEA25516.1; -; Genomic_DNA. DR RefSeq; WP_013675436.1; NC_015312.1. DR RefSeq; YP_004333369.1; NC_015312.1. DR EnsemblBacteria; AEA25516; AEA25516; Psed_3326. DR KEGG; pdx:Psed_3326; -. DR PATRIC; 54398193; VBIPseDio141225_3376. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; PDIO675635:GHMF-3362-MONOMER; -. DR Proteomes; UP000007809; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007809}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEA25516.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007809}; KW Transferase {ECO:0000313|EMBL:AEA25516.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 231 231 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 297 297 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 298 298 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 741 741 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1190 AA; 129363 MW; 350C3E0EB9DCC67A CRC64; MPELNPDGHD TSFLDTLARR VVVADGAMGT MLQAADLTLD DFAGLDGCNE ILNDTRPDVV RRIHTGYLEA GADAVETNSF GANLPNLAEY DIAERIRELA EKGARLAREA ADELSTPDRP RYVLGSVGPG TKLPTLGHES FARLRDAYTE CGIGLLAGGA DAFVIETCQD LLQVKAAVLG VRRAMAAEGR RIPIITQVTV ETTGTMLLGS EIGAALTAIE PLGVDLIGLN CATGPAEMSE HLRTLSKHAR IPLSVMPNAG LPQLGPNGAV YPLSPDELAE ALSTFVRDYG LRLVGGCCGT TPDHVRAVSE AVAAVTPAVR DPRPEPGVSS LYASVPFRQD TSVLMVGERT NANGSKAFRE AMIEERWEDC VAIAREQTRD GAHMLDLNVD YVGRDGVADM AELAGRLATA STLPIMIDST ETEVVQAGLE HLGGRCIVNS VNYEDGDGPG SRFQRTMAVV REHGAAVVAL CIDEEGQART AEWKVRVADR LIRDLTANHG MRVEDIVVDA LTFPITTGQE EVRRDALETI EAIRELKRQY PTVQTTLGIS NVSFGLNAAA RQVLNSVFLH ECVTAGLDTA IVHASKILPM SKIPDEQRSV ALDLVYDRRR EGYDPLARFM ELFEGVTASS AKAGRAEELA ALPLFERLER RIVDGERVGL EADLDAALEE RPALEIINDV LLSGMKTVGE LFGSGQMQLP FVLQSAEVMK TAVAHLEPHM EKTDAAGKGT IVLATVKGDV HDIGKNLVDI ILSNNGYTVV NLGIKQPIST ILSAAQEHGA HAVGMSGLLV KSTVIMKENL EEMNSRGVAE QLPVLLGGAA LTRSYVENDL AELYRGRVSY ARDAFEGLRL MDATMARARG DAPAVDPAEE QKIAERKARH ERSKRIAAKR RAAEAEAAGP LPERSDVALD NPLPTPPFWG TRVVKGIAVA EYSGMIDERA LFLGQWGLRG AKGGSGPSYE ELVETEGRPR LRYWLERLAT EGVLANAAVV YGYFPAVAVR DELVVLTEPR ADAPERHRFA FPRQRRDRHL CLADFWRPRD LAIAAGEIDV LPLHLVTMGQ PIADYANELF AKDSYRDYLE VHGLGVQLTE ALAEYWHRRV REELTWSTGR TLAEDDPDDV EDFFKLGYRG ARYSLGYGAC PNLEDRTKIV EMLEPGRIGV GLSEELQLHP EQSTDALVAH HPEAKYFNAG // ID F4DVK5_PSEMN Unreviewed; 1236 AA. AC F4DVK5; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 29-APR-2015, entry version 28. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:AEB58591.1}; GN OrderedLocusNames=MDS_2560 {ECO:0000313|EMBL:AEB58591.1}; OS Pseudomonas mendocina (strain NK-01). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1001585 {ECO:0000313|EMBL:AEB58591.1, ECO:0000313|Proteomes:UP000008306}; RN [1] {ECO:0000313|EMBL:AEB58591.1, ECO:0000313|Proteomes:UP000008306} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NK-01 {ECO:0000313|EMBL:AEB58591.1, RC ECO:0000313|Proteomes:UP000008306}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002620; AEB58591.1; -; Genomic_DNA. DR RefSeq; WP_013715665.1; NC_015410.1. DR RefSeq; YP_004380343.1; NC_015410.1. DR EnsemblBacteria; AEB58591; AEB58591; MDS_2560. DR KEGG; pmk:MDS_2560; -. DR PATRIC; 54485807; VBIPseMen187712_2606. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; PMEN1001585:GIWS-2592-MONOMER; -. DR Proteomes; UP000008306; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008306}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1236 AA; 135131 MW; 53CCC629D0CF3295 CRC64; MSDRSARLQA LQQALKERIL ILDGGMGTMI QSYKLEEADY RGARFADWPS DVKGNNDLLL LTQPQIIAAI EKAYLDAGAD ILETNTFNAT RVSQADYDME ELVYELNVAG ARVAREVADA KTLETPDRPR FVAGVLGPTS RTCSISPDVN DPGYRNVTFD ELVENYTEAT RGLIEGGADL ILIETIFDTL NAKAAIFAVQ QVFDEDGVEL PIMISGTITD ASGRTLSGQT TEAFWNSVAH AKPISVGLNC ALGAADLRPY LEELSNKAGT HVSAHPNAGL PNAFGEYDET PAQMAAVVEE FAASGFLNII GGCCGTTPGH IQAIAEAVAK YAPRPIPDIP KACRLSGLEP FTIDRQSLFV NVGERTNITG SAKFARLIRE ENYTEALEVA LQQVEAGAQV IDINMDEGML DSKAAMVRFL NLIAGEPDIS RVPIMIDSSK WEVIEAGLKC IQGKGIVNSI SMKEGVEQFK HHAKLCKRYG AAVVVMAFDE VGQADTAARK KEICQRSYDI LVNEVGFPPE DIIFDPNIFA VATGIEEHNN YAVDFIEACA FIRDNLPYAL SSGGVSNVSF SFRGNNPVRE AIHSVFLYYA IQNGLSMGIV NAGQLEIYDE IPKELRDAVE DVVLNRNDGA TEALLAIADK YKGDGAAKEV ENEEWRSLPV DKRLEHALVK GITAFIVEDT EECRQQCARP IEVIEGPLMA GMNVVGDLFG SGKMFLPQVV KSARVMKQAV AHLIPFIEAE KGDKPEAKGK ILMATVKGDV HDIGKNIVGV VLGCNGYDIV DLGVMVPAEK ILQTAIAEKC DIIGLSGLIT PSLDEMVHVA KEMQRQGFKL PLMIGGATTS KAHTAVKIDP QYSNDAVVYV TDASRAVGVA TQLLSKELKA DFVQKTRDEY VVVRERTAAR ATRTERLSYD NAIANKPAFD WNGYVAPKPS FTGAKVLDDI DLNVLAEYID WTPFFISWDL AGKYPRILTD EIVGEAATSL FNDAQAMLRK LIDEKLIKAR AVFGFWPANQ VRDDDIEVYG DNGEQLATLH HLRQQTIKPD GKPNLSLADF VAPKDSGVTD YVGGFITTAG IGAEEVAKAY EAKGDDYNSI MVKALADRLA EACAEWLHER VRKEYWGYAK DEQLDNEALI REQYKGIRPA PGYPACPDHT EKGTLFKLLD PEADYNKAGR SGVFLTEHYA MFPAAAVSGW YFAHPEAQYF AVGKVDKDQI ESYTARKGQD IAVSERWLAP NLGYDD // ID F4F7P9_VERMA Unreviewed; 1167 AA. AC F4F7P9; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEB45686.1}; GN OrderedLocusNames=VAB18032_22930 {ECO:0000313|EMBL:AEB45686.1}; OS Verrucosispora maris (strain AB-18-032). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micromonosporineae; Micromonosporaceae; Verrucosispora. OX NCBI_TaxID=263358 {ECO:0000313|EMBL:AEB45686.1, ECO:0000313|Proteomes:UP000008308}; RN [1] {ECO:0000313|EMBL:AEB45686.1, ECO:0000313|Proteomes:UP000008308} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AB-18-032 {ECO:0000313|EMBL:AEB45686.1, RC ECO:0000313|Proteomes:UP000008308}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002638; AEB45686.1; -; Genomic_DNA. DR RefSeq; WP_013734338.1; NC_015434.1. DR RefSeq; YP_004406286.1; NC_015434.1. DR EnsemblBacteria; AEB45686; AEB45686; VAB18032_22930. DR KEGG; vma:VAB18032_22930; -. DR PATRIC; 54475730; VBIVerMar92278_3731. DR KO; K00548; -. DR BioCyc; VMAR263358:GI1P-3692-MONOMER; -. DR Proteomes; UP000008308; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008308}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008308}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 219 219 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 730 730 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1167 AA; 126820 MW; F2FE97DB3740581F CRC64; MLDALADRIL ITDGAMGTML QAADLSLDDF DGLEGCNEIL NVTRPDVVRG VHEAYLAAGA DCIETNTFGA NLPNLAEYDI ADRIWELSEA GARLAREAAD AYETPERPRW VLGSIGPGTK LPTLGHASYA SLRDAYQQNA GGLIAGGADA LIIETCQDLL QVKAAVIGSK RAMAEAGRQV PIICHVAVET TGTMLLGSEI GAALTAIEPL GVDLIGLNCS TGPAEMGEHL RYLSQHSTVP VSVMPNAGLP VLTSDGAYFP LGPEDMAEAL ERFVVDYGVA LVGGCCGTTP EHIRVLAERL RDVAPVAREP RIDAGVSSIY HHVPFAQDAS VLMVGERTNA NGSKAFREAM LAADWQACVE IARSQARDGS HLLDLCVDYV GRDGTVDMRE LAGRFATAST LPIMLDSTEP AVIEAGLEML GGRCVVNSVN FEDGDGPDSR YARVMPVVAE HGAAVVALLI DEEGQARTAE WKVRVAERLI NDLTERWGLR RADILIDALT FPIATGQEET RRDGIETIEA IREIARRWPG VNFTLGISNV SFGLNPAARQ VLNSVFLHEC VQAGLTSAIV HASKILPMAK IPEQQREIAL DLIYDRRREG YDPVQRFIEV FEGVDAASAR ATRAEELAAL PLNERLKRRI IDGERNGLEA DLDAAMAAGT APLAIINDIL LDGMKVVGEL FGSGQMQLPF VLQSAEVMKT AVAYLEPHME KADDGGKGRI VLATVKGDVH DIGKNLVDII LSNNGYEVVN IGIKQPISAI LDAAEQHRAD AIGMSGLLVK STVIMKENLA EMASRGVAER WPVLLGGAAL TRAYVEDDLR SMFPGQVHYA RDAFEGLSLM DRVMTAKRGG APVIDPEREA ALAARRARRE RQRAVVAESL PELTDTSVRS DVAADVPVPT APFYGTRVVK GVPLADYAAL LDERATFMGQ WGLRGARGGK GPSYVELVET EGRPRLRYWL DRLIADQVLE AAVVYGYFPA YSEGNDLVVL DENGHAERAR FTFPRQRQER RLCLADFFRP RGEELDVVAL QLVTVGQPVS EYAAKLFARN EYRDYLEVHG LSVQLTEALA EYWHKRVRAE LTLPDGRTVA DDDPTDLAGL LRTDYRGCRY AFGYPACPDL EDRAKIVELL GAERIGVQLS EEFQLMPEQA TDAIVVHHPE ASYFNAK // ID F4GCU3_ALIDK Unreviewed; 343 AA. AC F4GCU3; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEB82546.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEB82546.1}; GN OrderedLocusNames=Alide2_0108 {ECO:0000313|EMBL:AEB82546.1}; OS Alicycliphilus denitrificans (strain DSM 14773 / CIP 107495 / K601). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Alicycliphilus. OX NCBI_TaxID=596154 {ECO:0000313|EMBL:AEB82546.1, ECO:0000313|Proteomes:UP000007938}; RN [1] {ECO:0000313|EMBL:AEB82546.1, ECO:0000313|Proteomes:UP000007938} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14773 / CIP 107495 / K601 RC {ECO:0000313|Proteomes:UP000007938}; 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; AEB82546.1; -; Genomic_DNA. DR RefSeq; WP_013721162.1; NC_015422.1. DR RefSeq; YP_004386062.1; NC_015422.1. DR EnsemblBacteria; AEB82546; AEB82546; Alide2_0108. DR KEGG; adk:Alide2_0108; -. DR PATRIC; 54522744; VBIAliDen79014_0110. DR KO; K00548; -. DR BioCyc; ADEN596154:GHU6-108-MONOMER; -. DR Proteomes; UP000007938; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007938}; KW Methyltransferase {ECO:0000313|EMBL:AEB82546.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007938}; KW Transferase {ECO:0000313|EMBL:AEB82546.1}. SQ SEQUENCE 343 AA; 36806 MW; B7387AA8D92058EE CRC64; MTLPHYTRAQ QLPAILEQRI AILDGAMGTM IQRFKLTEEQ YRGERFKDFA RDVKGNNELL SLTRPDVIRD IHEGYLAAGA DLIETNTFGA TSIAQEDYGM ADLAYEMNLE SARLARAACG KFSTPDKPRF VAGALGPTPK TASISPDVND PGARNVTFEQ LRAAYLEQAL ALIAGGADVL LVETIFDTLN AKAALFAIDE AFEQTGECLP IMISGTVTDA SGRILSGQTV TAFWHSVRHA NPLSIGLNCA LGAALMRPYI QELAKAAPDT FISCYPNAGL PNPMSDTGFD ETPEVTSRLV HEFATERLVN IVGGCCGTTP DHIGAIARAV APVGARRLFS AVS // ID F4GR48_PUSST Unreviewed; 1257 AA. AC F4GR48; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 01-APR-2015, entry version 28. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEC21938.1}; GN OrderedLocusNames=PT7_3398 {ECO:0000313|EMBL:AEC21938.1}; OS Pusillimonas sp. (strain T7-7). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Pusillimonas. OX NCBI_TaxID=1007105 {ECO:0000313|EMBL:AEC21938.1, ECO:0000313|Proteomes:UP000008737}; RN [1] {ECO:0000313|EMBL:AEC21938.1, ECO:0000313|Proteomes:UP000008737} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T7-7 {ECO:0000313|EMBL:AEC21938.1, RC ECO:0000313|Proteomes:UP000008737}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002663; AEC21938.1; -; Genomic_DNA. DR RefSeq; WP_013744457.1; NC_015458.1. DR RefSeq; YP_004418562.1; NC_015458.1. DR EnsemblBacteria; AEC21938; AEC21938; PT7_3398. DR KEGG; put:PT7_3398; -. DR PATRIC; 54561070; VBIPusSp189076_3350. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; PSP1007105:GJAF-3448-MONOMER; -. DR Proteomes; UP000008737; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008737}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008737}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 256 256 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 789 789 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1257 AA; 138589 MW; BBEC0C9B9F34A6F6 CRC64; MSYPSLPYPL SSYTHGVEFA RLLGERILIL DGAMGTMIQQ YKLSETDFRG ERFAEHVKDV KGNNELLSLV RPDIITAIHR EYLEAGADVI ETNTFGATAI AQGDYGLSEL AYELNVESAR LARAACDEYS TPERPRFVAG AMGPQPKTAS ISPDVNDPAA RNVTFEQLRD AYTEQLNGLL DGGIDIVLIE TIFDTLNAKA AIFAVETVFE ERGVRLPVMV SGTVTDASGR ILSGQTVEAF WNSVRHARPI TIGLNCALGA ALMRPYVAEL SKICDTYLCV YPNAGLPNPM AETGFDETPQ DTSSLLEEFA QAGLVNMAGG CCGTTPEHIR AIADKVASLP VRQVPQVPVK TRLSGLEALN IDADSLFVNV GERTNVTGSK MFLRLIREEK YDEALAVARQ QVENGAQIID INMDEAMLDS AVCMRRFLNM IASEPDIARV PIMIDSSKWE VIEQGLRCVQ GKAVVNSISM KEGEAAFLEH ARLCRKYGAA AIIMAFDEKG QADNLQRRKD ICERAYRLLV DEVGFPPEDI IFDPNVFAIA TGIEEHNHYA VDFIEATAWI TQNLPHARVS GGVSNVSFSF RGNEAMREAI HAVFLYYAIQ QGMTMGIVNA GQLGVYQDID KKVLDMVEDV VLDRAEPLGR TDPSDELTST ERLVELAETI KGSGAKKEED LSWREQAVEG RISHALVHGI TAFIVEDTEE VRAKIAAAGG RPIQVIEGPL MDGMNIVGDL FGAGKMFLPQ VVKSARVMKQ AVAHLIPFIE EEKRQIEAAG GDVRSKGKIV IATVKGDVHD IGKNIVSVVL ECNNFEVVNM GVMVPCSEIL AKAKEENCNM VGLSGLITPS LEEMAYVASE MQRDEYFSSR KLPLLVGGAT TSRVHTAVKI APNYEGPVIY VPDASRSVGV ATNLMSDNAD AYLAEVAEEY ELVRTRHANR KATPLVSLAE ARAGRPEIDW AGYTPPRPKF IGRRTFKNYD LSEVVQFLDW TPFFQTWSLF GQFPAILDDK VVGEQARKVY EEGQAMLKKI IEGRWLTASG VVAFYPANTV NDDDIEIYRD ESRSEVLLTW RNVRQQTVKR EGVDNKCLAD YIAPKETGIA DYIGMFAVTG GLGIEKHDKA FLDDNDDYSS IMLKSIADRL AEGFAECLHA RVRRDLWGYV PDESLSNEAV IAEKYQGIRP APGYPACPEH VVKKDMFEVL EAEEIGMQLT EGYAMYPASS VSGFYFSHPK SQYFNVGNIG DDQVKDYVQR SGRDEDDVRR SLASTLR // ID F4J0X9_ARATH Unreviewed; 293 AA. AC F4J0X9; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 31. DE SubName: Full=Homocysteine S-methyltransferase 2 {ECO:0000313|EMBL:AEE80455.1}; GN Name=HMT2 {ECO:0000313|EMBL:AEE80455.1}; GN OrderedLocusNames=At3g63250 {ECO:0000313|EMBL:AEE80455.1, GN ECO:0000313|TAIR:AT3G63250}; 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 {ECO:0000313|EMBL:AEE80455.1, ECO:0000313|Proteomes:UP000006548}; RN [1] {ECO:0000313|EMBL:AEE80455.1, ECO:0000313|Proteomes:UP000006548} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548}; RX PubMed=11130713; DOI=10.1038/35048706; RG European Union Chromosome 3 Arabidopsis Sequencing Consortium; RG Institute for Genomic Research; RG Kazusa DNA Research Institute; RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., RA Fartmann B., Valle G., Blocker H., Perez-Alonso M., Obermaier B., RA Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., RA De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P., RA Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., RA Schafer M., Muller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., RA Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., RA Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., RA Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., RA Kauer G., Lohnert T.H., Nordsiek G., Reichelt J., Scharfe M., RA Schon O., Bargues M., Terol J., Climent J., Navarro P., Collado C., RA Perez-Perez A., Ottenwalder B., Duchemin D., Cooke R., Laudie M., RA Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., RA Alcaraz J.P., Cottet A., Casacuberta E., Monfort A., Argiriou A., RA flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., RA Rudd S., Zaccaria P., Mewes H.W., Mayer K.F., Kaul S., Town C.D., RA Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., RA Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., RA Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., RA Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., RA Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., RA Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., RA Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., RA Tabata S.; RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis RT thaliana."; RL Nature 408:820-822(2000). RN [2] {ECO:0000313|Proteomes:UP000006548} RP GENOME REANNOTATION. RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548}; 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; CP002686; AEE80455.1; -; Genomic_DNA. DR RefSeq; NP_974482.1; NM_202753.2. DR UniGene; At.21554; -. DR ProteinModelPortal; F4J0X9; -. DR SMR; F4J0X9; 16-293. DR PRIDE; F4J0X9; -. DR DNASU; 825500; -. DR EnsemblPlants; AT3G63250.2; AT3G63250.2; AT3G63250. DR GeneID; 825500; -. DR KEGG; ath:AT3G63250; -. DR TAIR; AT3G63250; -. DR KO; K00547; -. DR Proteomes; UP000006548; Chromosome 3. DR ExpressionAtlas; F4J0X9; baseline and differential. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006548}; KW Methyltransferase {ECO:0000313|EMBL:AEE80455.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006548}; KW Transferase {ECO:0000313|EMBL:AEE80455.1}. SQ SEQUENCE 293 AA; 32267 MW; 2188902778B837B6 CRC64; MIDCSLLSCL YFLMEQVHLD YLEAGADIIS SASYQATIQG FEAKGFSREE SESLLKKSVE IATEARNSYY DKCGTSSSMD DKILKKRPIL VAASVGSYGA YLADGSEYSG IYGDSITLEK LKDFHRRRLQ VLAESGADLI AFETIPNKIE AQAFADLLEE GDVKIPGWFS FNSKDGVNVV SGDSIKECIS IAENCEKVVA VGINCTPPRF IEGLVLEIEK VTSKPILVYP NSGESYDADR KEWVENTGVG DEDFVSYVEK WMDAGVSLLG GCCRTTPTTI RAIHKRLVNR RSL // ID F4JBA7_ARATH Unreviewed; 306 AA. AC F4JBA7; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 07-JAN-2015, entry version 29. DE SubName: Full=Homocysteine S-methyltransferase 1 {ECO:0000313|EMBL:AEE77088.1}; GN Name=HMT-1 {ECO:0000313|EMBL:AEE77088.1}; GN OrderedLocusNames=At3g25900 {ECO:0000313|EMBL:AEE77088.1, GN ECO:0000313|TAIR:AT3G25900}; 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 {ECO:0000313|EMBL:AEE77088.1, ECO:0000313|Proteomes:UP000006548}; RN [1] {ECO:0000313|EMBL:AEE77088.1, ECO:0000313|Proteomes:UP000006548} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548}; RX PubMed=11130713; DOI=10.1038/35048706; RG European Union Chromosome 3 Arabidopsis Sequencing Consortium; RG Institute for Genomic Research; RG Kazusa DNA Research Institute; RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., RA Fartmann B., Valle G., Blocker H., Perez-Alonso M., Obermaier B., RA Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., RA De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P., RA Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., RA Schafer M., Muller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., RA Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., RA Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., RA Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., RA Kauer G., Lohnert T.H., Nordsiek G., Reichelt J., Scharfe M., RA Schon O., Bargues M., Terol J., Climent J., Navarro P., Collado C., RA Perez-Perez A., Ottenwalder B., Duchemin D., Cooke R., Laudie M., RA Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., RA Alcaraz J.P., Cottet A., Casacuberta E., Monfort A., Argiriou A., RA flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., RA Rudd S., Zaccaria P., Mewes H.W., Mayer K.F., Kaul S., Town C.D., RA Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., RA Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., RA Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., RA Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., RA Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., RA Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., RA Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., RA Tabata S.; RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis RT thaliana."; RL Nature 408:820-822(2000). RN [2] {ECO:0000313|Proteomes:UP000006548} RP GENOME REANNOTATION. RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548}; 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; CP002686; AEE77088.1; -; Genomic_DNA. DR RefSeq; NP_001189977.1; NM_001203048.1. DR UniGene; At.23868; -. DR ProteinModelPortal; F4JBA7; -. DR SMR; F4JBA7; 22-306. DR PRIDE; F4JBA7; -. DR EnsemblPlants; AT3G25900.3; AT3G25900.3; AT3G25900. DR GeneID; 822186; -. DR KEGG; ath:AT3G25900; -. DR TAIR; AT3G25900; -. DR KO; K00547; -. DR Proteomes; UP000006548; Chromosome 3. DR ExpressionAtlas; F4JBA7; baseline and differential. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 2. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006548}; KW Methyltransferase {ECO:0000313|EMBL:AEE77088.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006548}; KW Transferase {ECO:0000313|EMBL:AEE77088.1}. SQ SEQUENCE 306 AA; 33739 MW; A82632E6116F524C CRC64; MVLEKKSALL EDLIKKCGGC AVVDGGFATQ LEIHGAAIND PLWSAVSLIK NPELIKRVHM EYLEAGADIV VTSSYQATIP GFLSRGLSIE ESESLLQKSV ELAVEARDRF WEKVSKVSGH SYNRALVAAS IGSYGAYLAD GSEYSGHYGE NVSLDKLKDF HRRRLQVLVE AGPDLLAFET IPNKLEAQAC VELLEEEKVQ IPAWICFTSV DGEKAPSGES FEECLEPLNK SNNIYALTKK AIVVYPNSGE VWDGKAKQWL PSQCFGDDEF EMFATKWRDL GAKLIGGCCR TTPSTINAIS RDLKRR // ID F4JBA8_ARATH Unreviewed; 268 AA. AC F4JBA8; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 36. DE SubName: Full=Homocysteine S-methyltransferase 1 {ECO:0000313|EMBL:AEE77086.1}; GN Name=HMT-1 {ECO:0000313|EMBL:AEE77086.1}; GN OrderedLocusNames=At3g25900 {ECO:0000313|EMBL:AEE77086.1, GN ECO:0000313|TAIR:AT3G25900}; 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 {ECO:0000313|EMBL:AEE77086.1, ECO:0000313|Proteomes:UP000006548}; RN [1] {ECO:0000313|EMBL:AEE77086.1, ECO:0000313|Proteomes:UP000006548} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548}; RX PubMed=11130713; DOI=10.1038/35048706; RG European Union Chromosome 3 Arabidopsis Sequencing Consortium; RG Institute for Genomic Research; RG Kazusa DNA Research Institute; RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., RA Fartmann B., Valle G., Blocker H., Perez-Alonso M., Obermaier B., RA Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., RA De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P., RA Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., RA Schafer M., Muller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., RA Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., RA Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., RA Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., RA Kauer G., Lohnert T.H., Nordsiek G., Reichelt J., Scharfe M., RA Schon O., Bargues M., Terol J., Climent J., Navarro P., Collado C., RA Perez-Perez A., Ottenwalder B., Duchemin D., Cooke R., Laudie M., RA Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., RA Alcaraz J.P., Cottet A., Casacuberta E., Monfort A., Argiriou A., RA flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., RA Rudd S., Zaccaria P., Mewes H.W., Mayer K.F., Kaul S., Town C.D., RA Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., RA Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., RA Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., RA Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., RA Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., RA Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., RA Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., RA Tabata S.; RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis RT thaliana."; RL Nature 408:820-822(2000). RN [2] {ECO:0000313|Proteomes:UP000006548} RP GENOME REANNOTATION. RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548}; RG The Arabidopsis Information Resource (TAIR); RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002686; AEE77086.1; -; Genomic_DNA. DR RefSeq; NP_974361.1; NM_202632.1. DR UniGene; At.23868; -. DR ProteinModelPortal; F4JBA8; -. DR SMR; F4JBA8; 22-242. DR PRIDE; F4JBA8; -. DR EnsemblPlants; AT3G25900.2; AT3G25900.2; AT3G25900. DR GeneID; 822186; -. DR KEGG; ath:AT3G25900; -. DR TAIR; AT3G25900; -. DR KO; K00547; -. DR Proteomes; UP000006548; Chromosome 3. DR ExpressionAtlas; F4JBA8; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006548}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:AEE77086.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006548}; KW Transferase {ECO:0000313|EMBL:AEE77086.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 241 241 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 268 AA; 29437 MW; 5109BA6733E5D341 CRC64; MVLEKKSALL EDLIKKCGGC AVVDGGFATQ LEIHGAAIND PLWSAVSLIK NPELIKRVHM EYLEAGADIV VTSSYQATIP GFLSRGLSIE ESESLLQKSV ELAVEARDRF WEKVSKVSGH SYNRALVAAS IGSYGAYLAD GSEYSGHYGE NVSLDKLKDF HRRRLQVLVE AGPDLLAFET IPNKLEAQAC VELLEEEKVQ IPAWICFTSV DGEKAPSGES FEECLEPLNK SNNIYAVGIN CAPPQFIENL IRKFAKATDE ESNRCLPE // ID F4KQJ4_HALH1 Unreviewed; 1226 AA. AC F4KQJ4; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 30. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEE49983.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEE49983.1}; GN OrderedLocusNames=Halhy_2098 {ECO:0000313|EMBL:AEE49983.1}; OS Haliscomenobacter hydrossis (strain ATCC 27775 / DSM 1100 / LMG 10767 OS / O). OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Saprospiraceae; Haliscomenobacter. OX NCBI_TaxID=760192 {ECO:0000313|EMBL:AEE49983.1, ECO:0000313|Proteomes:UP000008461}; RN [1] {ECO:0000313|EMBL:AEE49983.1, ECO:0000313|Proteomes:UP000008461} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27775 / DSM 1100 / LMG 10767 / O RC {ECO:0000313|Proteomes:UP000008461}; RX PubMed=21886862; DOI=10.4056/sigs.1964579; RG US DOE Joint Genome Institute (JGI-PGF); RA Daligault H., Lapidus A., Zeytun A., Nolan M., Lucas S., Del Rio T.G., RA Tice H., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., RA Liolios K., Pagani I., Ivanova N., Huntemann M., Mavromatis K., RA Mikhailova N., Pati A., Chen A., Palaniappan K., Land M., Hauser L., RA Brambilla E.M., Rohde M., Verbarg S., Goker M., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., RA Woyke T.; RT "Complete genome sequence of Haliscomenobacter hydrossis type strain RT (O)."; RL Stand. Genomic Sci. 4:352-360(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 1100; 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 Pagani I., Daligault H., Detter J.C., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Verbarg S., RA Frueling A., Brambilla E., Klenk H.-P., Eisen J.A.; RT "Complete sequence of chromosome of Haliscomenobacter hydrossis DSM RT 1100."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002691; AEE49983.1; -; Genomic_DNA. DR RefSeq; WP_013764536.1; NC_015510.1. DR RefSeq; YP_004446856.1; NC_015510.1. DR EnsemblBacteria; AEE49983; AEE49983; Halhy_2098. DR KEGG; hhy:Halhy_2098; -. DR PATRIC; 54600834; VBIHalHyd147579_2267. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; HHYD760192:GI21-2116-MONOMER; -. DR Proteomes; UP000008461; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008461}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEE49983.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008461}; KW Transferase {ECO:0000313|EMBL:AEE49983.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 756 756 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1226 AA; 136045 MW; 7FAA671AD279BE09 CRC64; MKPDIREQLK QRILVIDGAM GTMIQRYKLG EAEYRGERFA NFHRDVKGNN DLLSITQPQI IEEIHRAYLE AGADIIETNT FSGTSIAQAD YEMQAYVYDL NYYSAQVAKK AADDYTTKTP HKPRYVAGAM GPTNRTASLS PDVNNPGYRA VTFKELKEAF YEQAKGLIEG GVDLLLLETI IDTLNVKAAL FAIEDLFEEL GYRIPVMVSG TITDASGRIL SGQTAEAFWI SVSHVPLLSV GLNCALGAEE MRPYLEALSN IADTFVSAYP NAGLPNEFGQ YDQSAEEMQV YIRDFAASGF VNMIGGCCGT TPDHIRAMVE AVKGLPPRQI PVSPGYTMLS GLEPLIIRPE TNFVNVGERT NVTGSRQFAR LIREGKYNDA LIVAQQQVEA GAQMIDVNMD EGLLDSEKAI VEFLNLMMSE PDIAKLPIMI DSSKFSVIEA GLQCVQGKCV VNSISLKEGE ESFIHHAKLV RRYGAAAVVM AFDEDGQADT IERKVSICER AYKILTQQVG FKPQDIIFDP NIFAVATGID EHNDYAIYFI EATRQIKQRC PGAKISGGVS NISFSYRGND PVREAMHSAF LYHAIQAGMD MGIVNAGMIE VYANIPPDLL ERVEDVLFNR RNDATERLTE FAESIKNDGG RVLQKDLAWR EGTLGERITH ALVKGITDYI DEDTEEARQQ FPHALNVIEG PLMDGMNVVG DLFGAGKMFL PQVVKSARVM KKSVAYLTPF IEEEKAATGG STKGKILLAT VKGDVHDIGK NIVGVVLACN NFDIVDLGVM VPADKILKAA KEQNVDIIGL SGLITPSLDE MVHMAKEMER LGFTLPLLVG GATTSKTHTA VKIEPQYSGP VIHVLDASRS VGVAAALLSD DQDYRNNLII DTKKDYERIR EQRAGRQTSK AFIDLDKARE NKVAIQWEGY HPPVPKKLGI TVFEDYDLNE LSEYIDWTPF FSSWQLAGKF PAILKDEIVG TEAQKLYNDA RSLLRRVIDE KWLSARAVIG LFPANMVHHD DIEVYNNDER SEVKAVLHQL RQQLKKAAGQ PNFCLADFIA PKGKAEDYIG AFAVTAGIGI EKWVAKFEAE HDDYNAIMLK ALADRLAEAL AERMHERVRK EFWGYAVAES LSSDDMIKEE YQGIRPAPGY PACPEHTEKR TLWSLLDVEN NTGMILTESF AMYPAASVSG WYFAHPESKY FGLGQIGKDQ ITDYARRKGM SVAETERWLA PVLNYE // ID F4LNB4_TREBD Unreviewed; 862 AA. AC F4LNB4; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEE17872.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEE17872.1}; GN OrderedLocusNames=Trebr_2466 {ECO:0000313|EMBL:AEE17872.1}; OS Treponema brennaborense (strain DSM 12168 / CIP 105900 / DD5/3). OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema. OX NCBI_TaxID=906968 {ECO:0000313|EMBL:AEE17872.1, ECO:0000313|Proteomes:UP000006546}; RN [1] {ECO:0000313|Proteomes:UP000006546} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 12168 / CIP 105900 / DD5/3 RC {ECO:0000313|Proteomes:UP000006546}; 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 Pagani I., Teshima H., Detter J.C., Tapia R., Han C., Land M., RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., RA Gronow S., Wellnitz S., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Treponema brennaborense DSM 12168."; 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; CP002696; AEE17872.1; -; Genomic_DNA. DR RefSeq; WP_013759573.1; NC_015500.1. DR RefSeq; YP_004441003.1; NC_015500.1. DR EnsemblBacteria; AEE17872; AEE17872; Trebr_2466. DR KEGG; tbe:Trebr_2466; -. DR PATRIC; 54595999; VBITreBre169731_2687. DR KO; K00548; -. DR BioCyc; TBRE906968:GHVD-2525-MONOMER; -. DR Proteomes; UP000006546; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006546}; KW Methyltransferase {ECO:0000313|EMBL:AEE17872.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006546}; KW Transferase {ECO:0000313|EMBL:AEE17872.1}. SQ SEQUENCE 862 AA; 91228 MW; BCCAB862F7A4CD1A CRC64; MKRTDIRNLL GKQVLFFDGG TGSVLQAQGL KPGELPETWN LSEREKIVAL HYGYYRAGCN IVKTNTFGAN RLKFSAPGEL ESVVLAALEN AAEARRRIEN EPIPEAELET LRAASLAPAS VNPAELPHFI ALDVGPAGKL LEPLGDLPFS GAVELFSDTI RAALSSARRE AVDLILIETM NDCYEAKAAV VAAKETCAAL NVRLPIIVTT VYDESAKLLT GADPETMTAV LEGLGVDAFG MNCSLGPHQM QPILDRLSAA ASIPLAVNPN AGLPRSENGR TVYDVTPAEF ARVTAGFVDR GAALVGGCCG TTSEHICRLV NACAGKPCPV RRDTGVTLIS SYTKTVAFGK KPILVGERIN PTGKKRFKQA LREHDIQYII REGLAQEEKG AHVLDVNVGL PEIDETELLV TVVTELQSVT DLPLQLDTSD PAAMEAALRV YNGKALVNSV NGKREVMDAV FPLVKKYGGA VVALMLDEDG IPETAEGRLR IVRKIYAAAA EYGIARKDIV IDPLAMAVSS DPGAAAVTLE TLRAVRDEFG GRSILGVSNV SFGLPQRELI TASFFTMAMQ NGLSAAIMNP NSAEMMKAYA CFCALSGYDP HCSDYIAFAE SYGAAPPPLS AGGAQSAAAV HRVPATAAAQ SAPATAAGSG SVQSAPPQTL EYAVIRGLKE DAAARTRTLL GTTEALDIIN NHLIPALDVV GKGFEAKKVY LPQLLMSAEA AKAAFSVIKE TLAAAGKTDE SKGTVVLATV KGDIHDIGKN IVKVLLENYG FTVVDLGKDV SPERIAEICA EKRVRLAGLS ALMTTTVPAM EATITLLRAR APWCKVCVGG AVLTPEYADM IGADFYGKDA LETVKYAQSV FS // ID F4LV47_TEPAE Unreviewed; 793 AA. AC F4LV47; L0S341; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 31. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CCP27670.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CCP27670.1}; GN OrderedLocusNames=TEPIRE1_2798 {ECO:0000313|EMBL:CCP27670.1}; OS Tepidanaerobacter acetatoxydans (strain DSM 21804 / JCM 16047 / Re1). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Tepidanaerobacter. OX NCBI_TaxID=1209989 {ECO:0000313|EMBL:CCP27670.1, ECO:0000313|Proteomes:UP000010802}; RN [1] {ECO:0000313|Proteomes:UP000010802} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23469343; DOI=10.1128/genomeA.00213-12; RA Manzoor S., Bongcam-Rudloff E., Schnurer A., Muller B.; RT "First genome sequence of a syntrophic acetate-oxidizing bacterium, RT Tepidanaerobacter acetatoxydans strain Re1."; RL Genome Announc. 1:E00213-E00213(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; HF563609; CCP27670.1; -; Genomic_DNA. DR RefSeq; WP_013779613.1; NC_019954.2. DR RefSeq; YP_004462001.1; NC_015519.1. DR EnsemblBacteria; AEE92694; AEE92694; TepRe1_2596. DR EnsemblBacteria; CCP27670; CCP27670; TepiRe1_2798. DR KEGG; tae:TepiRe1_2798; -. DR KEGG; tep:TepRe1_2596; -. DR PATRIC; 54628414; VBITepSp18581_2727. DR KO; K00548; -. DR OMA; CNIADEL; -. DR BioCyc; TSP499229:GHS2-2654-MONOMER; -. DR Proteomes; UP000010802; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000010802}; KW Methyltransferase {ECO:0000313|EMBL:CCP27670.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000010802}; KW Transferase {ECO:0000313|EMBL:CCP27670.1}. SQ SEQUENCE 793 AA; 85864 MW; A802DD7E7CEB3BCC CRC64; MSKRIDFSNF IVFDGAMGTM LQTHGLKAGE LPESYNILHP EIIEKIHGEY LDAGADVITT NTFGANRIKL SKYGYDIGEI VKSGVKIALK AAGKRLVALD IGPIGQLMKP YGTLSFSEAY ELFREQVIAG ADAGADLILI ETMSDIYEMK AAILAAKENC NLPVVATMTF QQDKRTLTGT DPLTMVNVIC GLGVNALGIN CSLGPKEILP LIEEVLSCSK IPVIAQPNAG MPKIIDGKTV FNVEPDEFAR YAKIMAEKGV TILGGCCGTN PEHIRALRHV LAGLEPIKRK VEPITAASSF SKTVIIGEGI TVIGEKLNPT GRKHLKEALK SNDMEYVLRQ ALAQQDAGAH ILNVNAGLPE IDEKAVMINI IRELQSTVSV PLQIDSTDSD VIEAAVRIYN GRPIINSVNG KLKVMEEIFP IAKKYGACVV GLTLDENGIP SKAKDRFKIA ENIVKTASKY GIAKEDLIID CLVIAASAQQ DEVREIIKAT RLVKERLGVK TILGVSNISF GLPNRTLLNR TFLALALEAG LDAPIIDPAD EEVMGTINAF NVLWGYDKYA NNYIAAYAPK DKKPAVKAFS ATDVADIEDI IINGLKEEAA PKVRAMLKAM SPTQIIDEHL VPSLDIVGRK YEAGEIFLPQ LIQSAETAKR AFEAIKHHII ETNGGKAEFS KGKIILATVR GDIHDIGKNI VKILLENYGF EVIDLGKDVP EDEIIQRIKQ DNVSLVGLSA LMTTTAQNMA NTIKAIRKAG LGCKIMVGGA VVNAEFAKSI GADYYGRDAQ ESVRIAQEFF SPS // ID F4N226_YEREN Unreviewed; 1245 AA. AC F4N226; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 01-APR-2015, entry version 19. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:CBX72134.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CBX72134.1}; GN Name=metH {ECO:0000313|EMBL:CBX72134.1}; GN ORFNames=YEW_BH06500 {ECO:0000313|EMBL:CBX72134.1}; OS Yersinia enterocolitica W22703. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=913028 {ECO:0000313|EMBL:CBX72134.1}; RN [1] {ECO:0000313|EMBL:CBX72134.1} 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; FR718682; CBX72134.1; -; Genomic_DNA. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CBX72134.1}; KW Transferase {ECO:0000313|EMBL:CBX72134.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 266 266 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 329 329 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 330 330 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 777 777 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1245 AA; 137798 MW; 5CB8FF835413FD43 CRC64; MLNGLFLQQG KEATVVDTVI NNKVKELHQQ LAQRILVLDG GMGTMIQSYR LEEADYRGAR FADWPSDLKG NNDLLVLSKP EVITAIHNAY LEAGADILET NTFNSTSIAM ADYQMESLSA EINYEAARLA RICADEWTAR TPDKPRYVAG VLGPTNRTAS ISPKVNDPAF RNVSFDQLVE AYRESTRALI EGGVDLIMIE TVFDTLNAKA ATFAVESEFE AMGVLLPVMI SGTITDASGR TLSGQTTEAF YNSLRHVKPL SFGLNCALGP DELRQYVAEL SRISEYYVSA HPNAGLPNAF GEYDLEAKEM AEQIGEWARA GFLNIVGGCC GTTPRHIAAM VKAVAGVAPR PLPEIPVACR LAGLEPLTID ANTLFVNVGE RTNVTGSARF KRLIKEEKYG EALDVARQQV ESGAQIIDIN MDEGMLDAEA AMVRFLNLIA GEPDIARVPI MIDSSKWDVI EKGLKCIQGK GIVNSISMKE GVDAFIHHAK LVRRYGAAMV VMAFDEQGQA DTRARKIEIC RRAYKILTET VGFPPEDIIF DPNIFAVATG IEEHNNYAVD FIEACADIKA ELPHAMISGG VSNVSFSFRG NDPVREAIHA VFLYYAIRNG MDMGIVNAGQ LAIYDDLSDE LRNAVEDVIL NRRDDSTERL LDLAEKYRGS KSDEVAVQQA EWRGWPVKKR LEYSLVKGIT EFIELDTEEA RQEADRPIEV IEGPLMAGMN VVGDLFGEGK MFLPQVVKSA RVMKQAVAYL EPYIEASKQK GATAGKILLA TVKGDVHDIG KNIVGVVLQC NNYEIIDLGV MVPTEKILRT AREEKVDIIG LSGLITPSLD EMVNVAKEME RQGFTLPLLI GGATTSKAHT AVKIEQNYSG STTYVSNASR SVGVVSALLS DTQRDDFIAK TRKEYETVRI QHARKKPRTP PVSLQVARDN QTVIDWENYT PPVAHKLGVQ AVEASIETLR NYIDWTPFFM TWSLAGKYPR ILEDEVVGEE AKRLFADANE MLDKLSAEGL LHPKGVVGLF PANSVGDDIE IYRDERRDDV LVVSHHLRQQ TEKTDFPNYC LADYVAPKSS GKADYYGAFA VTGGLEEDAL ADAYDAQHDD YNKIMIKALS DRLAEAFAEY LHERVRKVYW GFAPNENLSN EELVRENYQG IRPAPGYPAC PEHTEKGQIW QLLDVETHTG MKLTESYAMW PGASVSGWYF SHPDSKYFAV AQIQRDQVED YAARKGMAVS EVERWLAPNL GYDAD // ID F4NJT9_ECOLX Unreviewed; 1227 AA. AC F4NJT9; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EGJ06420.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGJ06420.1}; GN Name=metH {ECO:0000313|EMBL:EGJ06420.1}; GN ORFNames=SSJG_02469 {ECO:0000313|EMBL:EGJ06420.1}; OS Escherichia coli D9. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=556266 {ECO:0000313|EMBL:EGJ06420.1}; RN [1] {ECO:0000313|EMBL:EGJ06420.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=D9 {ECO:0000313|EMBL:EGJ06420.1}; 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., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GG657386; EGJ06420.1; -; Genomic_DNA. DR RefSeq; WP_000096014.1; NZ_GG657386.1. DR EnsemblBacteria; EGJ06420; EGJ06420; SSJG_02469. DR PATRIC; 30980856; VBIShiSp107483_2395. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGJ06420.1}; KW Transferase {ECO:0000313|EMBL:EGJ06420.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136022 MW; 30C43F2B4EF29A84 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIKI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFPN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAD // ID F4PVY7_DICFS Unreviewed; 1204 AA. AC F4PVY7; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Cobalamin-dependent methionine synthase {ECO:0000313|EMBL:EGG20151.1}; GN Name=mtr {ECO:0000313|EMBL:EGG20151.1}; GN ORFNames=DFA_07271 {ECO:0000313|EMBL:EGG20151.1}; OS Dictyostelium fasciculatum (strain SH3) (Slime mold). OC Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; Dictyostelium. OX NCBI_TaxID=1054147 {ECO:0000313|Proteomes:UP000007797}; RN [1] {ECO:0000313|EMBL:EGG20151.1, ECO:0000313|Proteomes:UP000007797} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SH3 {ECO:0000313|EMBL:EGG20151.1, RC ECO:0000313|Proteomes:UP000007797}; RA Gloeckner G., Schaap P., Noegel A.A., Felder M., Eichinger L., RA Heidel A.J., Platzer M.; RT "Living fossils from the dawn of multicellularity."; 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; GL883013; EGG20151.1; -; Genomic_DNA. DR RefSeq; XP_004367134.1; XM_004367077.1. DR GeneID; 14871842; -. DR KEGG; dfa:DFA_07271; -. DR KO; K00548; -. DR Proteomes; UP000007797; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 2. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 2. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007797}; KW Reference proteome {ECO:0000313|Proteomes:UP000007797}. SQ SEQUENCE 1204 AA; 133730 MW; 9875725669E53FDD CRC64; MTIPETPIFN QLRKILDERI MILDGAMGTE IQKYKLKDAD YRGEEFKDFP HELGGNNDLL VLTRPHIIKE IHLKYLLAGA DIIETNTFNG NIFSQADYKM EHLVKRLNIE AAKLAKDACI EVMAQDPTRQ CYVAGAVGPT NKTASISPSV ERPEARNVKF DELVDGYYEQ VEALVEGGID IILVETVFDS LNCKAALFAI ENYFVKHNTV LPVFVSGTIV DKSGRTLSGQ TGEAFFTSVQ HARPMVFGLN CALGATEMRP FLANVSKCSD CYVSCYPNAG LPNTFGGYDE TPEMMAGKIL EFAQSGFLNI VGGCCGTSPD HIRAFVEATR GVQPRRIPTI APYTTVSGLE PLAFTPQLNF VNVGERCNVS GSRRFANLIK ANKYEEAISV ARQQVEAGAQ IIDINMDEGK CIVNSISLKV GEELFIEQAR ICHQYGAAVV VMAFDENGQA VDKNDKVRIC YRSYKILTEV VGFKPQDIIF DPNILTIATG LEEHNNYAVE FIEATREIKQ LMPLTKVSGG VSNLSFSFRG NEPLREAMHS AFLFHAIRAG MDMGIVNAGA LPIYDDIDKD LLLMCEDAIL NRSNDSTERL LEYAQRSKGS EGAGKAAEVE EWRTKPVQER ISHALVKGIT SHIIEDTEEA RLTMPSALRV IEGPLMSGMD VVGDLFGAGK MFLPQVIKSA RVMKKAVAHL IPFMEEEKLA KRARGEVAED QENAGVVVLA TVKGDVHDIG KNIVGVVLGC NNYKVIDLGV MTPCEKILQQ AIEQKADIIG LSGLITPSLD EMIYVASEMQ RAGFKVPLMI GGATTSQIHT AVKISPHYRE PVVHVLDASR SVTVVSSLLD KNNKEAFFED IQHQYSELRE KHYASLKDRN YMSLEKARAL APKTNWNTVE ITRPTFIGKQ VFAEYPLEQL IPKIDWNPFF ATWQLRGKYP NRGYPRIFND ATVGAEAKKL FDDAQAMLKL IVDKKLLNAR GVIGFYPANS VNEDIEVYSD ETRSTVVGTL HGLRQQSEKE TEEPYIAIGD YIAPKSTGKT DYIGLFAVSA GFGLDALVEQ YNAQNDDYSS IMAKALADRL AEALAEHVHL DVRVKHWGYQ VNEQLSPDDL FKIKYRGIRP APGYPAQPDH TEMQTIWNIM NVQQDTDIEL TESMAMLPGA AVCGLYFAHE HAKYFSVGKI TKDQVESYAK RKGISINEAE RWLSPILSYD RQFN // ID F4QHQ7_9CAUL Unreviewed; 359 AA. AC F4QHQ7; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGF92794.1}; GN ORFNames=ABI_12320 {ECO:0000313|EMBL:EGF92794.1}; OS Asticcacaulis biprosthecum C19. OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Asticcacaulis. OX NCBI_TaxID=715226 {ECO:0000313|EMBL:EGF92794.1}; RN [1] {ECO:0000313|EMBL:EGF92794.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C19 {ECO:0000313|EMBL:EGF92794.1}; 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; EGF92794.1; -; Genomic_DNA. DR RefSeq; WP_006271976.1; NZ_GL883077.1. DR EnsemblBacteria; EGF92794; EGF92794; ABI_12320. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 359 AA; 39410 MW; 25B0CC92B1E838E8 CRC64; MTSRAANIAE RIAVLKQAAK ERILILDGSW GVMIQRRGLD ESDFRGERFA AHDGQLKGNN DILCITRPDV IADLHHQYFA AGADISETNT FSATTIAQDD YRLSLQDCID INLEGARIAR KVADEWTAKE PHKPRFVAGS IGPLNKMLSM SSDVNDPGAR LVTFDQVYQA YREQVQALYE GGVDLYLIET ITDTLNCKAA IKAILDLEDE GQETLPIWIS GTITDRSGRT LSGQTAEAFW NSVRHAKPFA VGFNCALGAD LMRPHIAELA RVADCLVAAY PNAGLPNAMG QYDEQPHETA HELHEWAKDG IVNILGGCCG TTPDHIQHVA DEVRGVTPRQ IPDRPKALRL AGLEPFELA // ID F4R1N8_BREDI Unreviewed; 358 AA. AC F4R1N8; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGF94280.1}; GN ORFNames=BDIM_10980 {ECO:0000313|EMBL:EGF94280.1}; OS Brevundimonas diminuta ATCC 11568. OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Brevundimonas. OX NCBI_TaxID=751586 {ECO:0000313|EMBL:EGF94280.1}; RN [1] {ECO:0000313|EMBL:EGF94280.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 11568 {ECO:0000313|EMBL:EGF94280.1}; 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 ----------------------------------------------------------------------- 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; EGF94280.1; -; Genomic_DNA. DR RefSeq; WP_003164675.1; NZ_GL883086.1. DR EnsemblBacteria; EGF94280; EGF94280; BDIM_10980. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 358 AA; 39463 MW; 242C51D48E55C92F CRC64; MTSPLTRAER IAALHAAAKE RILVLDGSWG VMIQRRDLTE EDFRGERFRD HNHPQKGNND LLILTRPDIV ADLHDVYYAA GADISETNTF SSTTIAQADY GLEDAVYDLN YEGARIAREV ADRWAQKEPH KPRFVAGAIG PTNRTLSLSP DVNDPGYRAV TYDEVYEAYK QQARALHHGG VDIFLIETVF DTLNCKAAIK AIKDLEDEGL EPLPLWISGT ITDRSGRTLS GQTAEAFWNS IRHAKPFAVG FNCALGAELM RPHIAELSRV ADTLVSAYPN AGLPNAMGQY DEQPHETAHF LEEWAQSGLV NIVGGCCGTT PDHIRHVAEE VAGVKPRAVP ERPTALRLSG LEPFELVS // ID F4RLQ3_MELLP Unreviewed; 358 AA. AC F4RLQ3; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 07-JAN-2015, entry version 18. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EGG06711.1}; DE Flags: Fragment; GN ORFNames=MELLADRAFT_26682 {ECO:0000313|EMBL:EGG06711.1}; 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 {ECO:0000313|Proteomes:UP000001072}; RN [1] {ECO:0000313|Proteomes:UP000001072} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=98AG31 / pathotype 3-4-7 {ECO:0000313|Proteomes:UP000001072}; 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; GL883107; EGG06711.1; -; Genomic_DNA. DR RefSeq; XP_007410151.1; XM_007410089.1. DR EnsemblFungi; EGG06711; EGG06711; MELLADRAFT_26682. DR GeneID; 18926963; -. DR KEGG; mlr:MELLADRAFT_26682; -. DR InParanoid; F4RLQ3; -. DR KO; K00547; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000001072; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 2. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001072}; KW Reference proteome {ECO:0000313|Proteomes:UP000001072}. FT NON_TER 1 1 {ECO:0000313|EMBL:EGG06711.1}. FT NON_TER 358 358 {ECO:0000313|EMBL:EGG06711.1}. SQ SEQUENCE 358 AA; 39519 MW; 914F31DFF69771AD CRC64; LVLLDGGNGT TLADDPGNEL DTGLWSATLL VKHPEKIARL HQSWEKAGAD IITSCSYQAT VQGFENYLLK QTHTEQNDVE KPSKEADENA THLPRLNSPL DFLRSSIGVA HKSLSTAKVG LSLGPFGATL TPPQDYAGIY PSPYNQLEPL KNFHLDRLLD YANDEATWRK VDMVIFETIP NLLEALAVRS AWSTLLQSLE DRYEKTECIK WWVKPWVLSF VFAGSSGQFA SGASPTEVLN AALGLSKDLD QLSLPRPSAV GVNCTKLQFI DKIVSAWTDL TETQSLRTLE SPAPWLWMYP DGGLVYDVER RCWSGGQIGT DQWARQLMNI AQQASLHWPG VVVGGCCKTG PTHIRALK // ID F4SS74_ECOLX Unreviewed; 1232 AA. AC F4SS74; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 01-APR-2015, entry version 22. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGI07968.1}; GN ORFNames=ECHG_03974 {ECO:0000313|EMBL:EGI07968.1}; OS Escherichia coli H736. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=656414 {ECO:0000313|EMBL:EGI07968.1}; RN [1] {ECO:0000313|EMBL:EGI07968.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=H736 {ECO:0000313|EMBL:EGI07968.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GL883800; EGI07968.1; -; Genomic_DNA. DR EnsemblBacteria; EGI07968; EGI07968; ECHG_03974. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 252 252 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 315 315 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 316 316 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 764 764 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1232 AA; 136368 MW; 1F710B4B7DC3BF86 CRC64; MSGASVSSKV EQLRAQLNER ILVLDGGMGT MIQSYRLNEA DFRGERFADW PCDLKGNNDL LVLSKPEVIA AIHNAYFEAG ADIIETNTFN STTIAMADYQ MESLSAEINF AAAKLARACA DEWTARTPEK PRYVAGVLGP TNRTASISPD VNDPAFRNIT FDGLVAAYRE STKALVEGGA DLILIETVFD TLNAKAAVFA VKTEFEALGV ELPIMISGTI TDASGRTLSG QTTEAFYNSL RHAEALTFGL NCALGPDELR QYVQELSRIA ECYVTAHPNA GLPNAFGEYD LDADTMAKQI REWAQAGFLN IVGGCCGTTP QHIAAMSRAV EGLAPRKLPE IPVACRLSGL EPLNIGEDSL FVNVGERTNV TGSAKFKRLI KEEKYSEALD VARQQVENGA QIIDINMDEG MLDAEAAMVR FLNLIAGEPD IARVPIMIDS SKWDVIEKGL KCIQGKGIVN SISMKEGVDA FIHHAKLLRR YGAAVVVMAF DEQGQADTRA RKIEICRRAY KILTEEVGFP PEDIIFDPNI FAVATGIEEH NNYAQDFIGA CEDIKRELPH ALISGGVSNV SFSFRGNDPV REAIHAVFLY YAIRNGMDMG IVNAGQLAIY DDLPAELRDA VEDVILNRRD DGTERLLELA EKYRGSKTDD TANAQQAEWR SWEVNKRLEY SLVKGITEFI EQDTEEARQQ ATRPIEVIEG PLMDGMNVVG DLFGEGKMFL PQVVKSARVM KQAVAYLEPF IEASKEQGKT NGKMVIATVK GDVHDIGKNI VGVVLQCNNY EIVDLGVMVP AEKILRTAKE VNADLIGLSG LITPSLDEMV NVAKEMERQG FTIPLLIGGA TTSKAHTAVK IEQNYSGPTV YVQNASRTVG VVAALLSDTQ RDDFVARTRK EYETVRIQHG RKKPRTPPVT LEAARDNDFA FDWQAYTPPV AHRLGVQEVE AGIETLRNYI DWTPFFMTWS LAGKYPRILE DEVVGVEAQR LFKDANDMLD KLSAEKTLNP RGVVGLFPAN RVGDDIEIYR DETRTHVINV SHHLRQQTEK TGFANYCLAD FVAPKLSGKA DYIGAFAVTG GLEEDALADA FEAQHDDYNK IMVKALADRL AEAFAEYLHE RVRKVYWGYA PNENLSNEEL IRENYQGIRP APGYPACPEH TEKATIWELL EVEKHTGMKL TESFAMWPGA SVSGWYFSHP DSKYYAVAQI QRDQVEDYAR RKGMSVTEVE RWLAPNLGYD AD // ID F4T6Q0_ECOLX Unreviewed; 1232 AA. AC F4T6Q0; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 01-APR-2015, entry version 22. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGI13404.1}; GN ORFNames=ECIG_05233 {ECO:0000313|EMBL:EGI13404.1}; OS Escherichia coli M605. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=656417 {ECO:0000313|EMBL:EGI13404.1}; RN [1] {ECO:0000313|EMBL:EGI13404.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M605 {ECO:0000313|EMBL:EGI13404.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GL883927; EGI13404.1; -; Genomic_DNA. DR EnsemblBacteria; EGI13404; EGI13404; ECIG_05233. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 252 252 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 315 315 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 316 316 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 764 764 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1232 AA; 136516 MW; 9D4ED5079AE8BAD5 CRC64; MSGASVSSKV EQLRAQLNER ILVLDGGMGT MIQSYRLNEA DFRGERFADW PCDLKGNNDL LVLSKPEVIA AIHNAYFEAG ADIIETNTFN STTIAMADYQ MESLSAEINF AAAKLARACA DEWTARTPEK PRYVAGVLGP TNRTASISPD VNDPAFRNIT FDQLVAAYRE STKALVEGGA DLILIETVFD TLNAKAAVFA VKTEFEALGV ELPIMISGTI TDASGRTLSG QTTEAFYNSL RHAEALTFGL NCALGPDELR QYVQELSRIA ECYVTAHPNA GLPNAFGEYD LDADTMAKQI REWAEAGFLN IVGGCCGTTP QHIAAMSRAV EGLAPRKLPE IPVACRLSGL EPLNIGDDSL FVNVGERTNV TGSAKFKRLI KEEKYSEALD VARQQVENGA QIIDINMDEG MLDAEAAMVR FLNLIAGEPD IARVPIMIDS SKWDVIEKGL KCIQGKGIVN SISMKEGVDA FIHHAKLLRR YGAAVVVMAF DEQGQADTRA RKIEICRRAY KILTEEVGFP AEDIIFDPNI FAVATGIEEH NNYAQDFIGA CEDIKRELPH ALISGGVSNV SFSFRGNDPV REAIHAVFLY YAIRNGMDMG IVNAGQLAIY DDLPTELRDA VEDVILNRRD DGTERLLELA EKYRGSKTDD TANTQQAEWR SWEVNKRLEY SLVKGITEFI EQDTEEARQQ ATRPIEVIEG PLMDGMNVVG DLFGEGKMFL PQVVKSARVM KQAVAYLEPF IEASKEQGKT NGKMVIATVK GDVHDIGKNI VGVVLQCNNY EIVDLGVMVP AEKILRTAKE VNADLIGLSG LITPSLDEMV NVAKEMERQG FTIPLLIGGA TTSKAHTAVK IEQNYSGPTV YVQNASRTVG VVAALLSDTQ RDDFVARTRK EYETVRIQHG RKKPRTPPVT LEAARDNDFA FDWQAYTPPV AHRLGVQEVE ASIETLRNYI DWTPFFMTWS LAGKYPRILE DEVVGVEAQR LFKDANDMLD KLSAEKMLNP RGVVGLFPAN RVGDDIEIYR DETRTHVINV SHHLRQQTEK TGFANYCLAD FVAPKLSGKA DYIGAFAVTG GLEEDALADA FEAQHDDYNK IMVKALADRL AEAFAEYLHE RVRKVYWGYA PNENLSNEEL IRENYQGIRP APGYPACPEH TEKATIWELL EVEKHTGMKL TESFAMWPGA SVSGWYFSHP DSKYYAVAQI QRDQVEDYAH RKGMSVTEVE RWLAPNLGYD AE // ID F4TNQ2_ECOLX Unreviewed; 1232 AA. AC F4TNQ2; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 01-APR-2015, entry version 22. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGI18272.1}; GN ORFNames=ECJG_04194 {ECO:0000313|EMBL:EGI18272.1}; OS Escherichia coli M718. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=656419 {ECO:0000313|EMBL:EGI18272.1}; RN [1] {ECO:0000313|EMBL:EGI18272.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M718 {ECO:0000313|EMBL:EGI18272.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GL884142; EGI18272.1; -; Genomic_DNA. DR EnsemblBacteria; EGI18272; EGI18272; ECJG_04194. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 252 252 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 315 315 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 316 316 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 764 764 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1232 AA; 136482 MW; 49C36E25BE0D7FE3 CRC64; MSGASVSSKV EQLRAQLNER ILVLDGGMGT MIQSYRLNEA DFRGERFADW PCDLKGNNDL LVLSKPEVIA AIHNAYFEAG ADIIETNTFN STTIAMADYQ MESLSAEINF AAAKLARACA DEWTARTPEK PRYVAGVLGP TNRTASISPD VNDPAFRNIT FDQLVAAYRE STKALVEGGA DLILIETVFD TLNAKAAVFA VKTEFEALGV ELPIMISGTI TDASGRTLSG QTTEAFYNSL RHAEALTFGL NCALGPDELR QYVQELSRIA ECYVTAHPNA GLPNAFGEYD LDADTMAKQI REWAQAGFLN IVGGCCGTTP QHIAAMSRAV EGLAPRKLPE IHVACRLSGL EPLNIGEDSL FVNVGERTNV TGSAKFKRLI KEEKYSEALD VARQQVENGA QIIDINMDEG MLDAEAAMVR FLNLIAGEPD IARVPIMIDS SKWDVIEKGL KCIQGKGIVN SISMKEGVDA FIHHAKLLRR YGAAVVVMAF DEQGQADTRA RKIEICRRAY KILTEEVGFP PEDIIFDPNI FAVATGIEEH NNYAQDFIGA CEDIKRELPH ALISGGVSNV SFSFRGNDPV REAIHAVFLY YAIRNGMDMG IVNAGQLAIY DDLPAELRDA VEDVILNRRD DGTERLLELA EKYRGSKTDD TANAQQAEWR SWEVNKRLEY SLVKGITEFI EQDTEEARQQ ATRPIEVIEG PLMDGMNVVG DLFGEGKMFL PQVVKSARVM KQAVAYLEPF IEASKEQGKT NGKMVIATVK GDVHDIGKNI VGVVLQCNNY EIVDLGVMVP AEKILRTAKE VNADLIGLSG LITPSLDEMV NVAKEMERQG FTIPLLIGGA TTSKAHTAVK IEQNYSGPTV YVQNASRTVG VVAALLSDTQ RDDFVARTRK EYETVRIQHG RKKPRTPPVT LEAARDNDFA FDWQAYTPPV AHRLGVQEVE ASIETLRNYI DWTPFFMTWS LAGKYPRILE DEVVGVEAQR LFKDANDMLD KLSAEKTLNP RGVVGLFPAN RVGDDIEIYR DETRTHVINV SHHLRQQTEK TGFANYCLAD FVAPKLSGKA DYIGAFAVTG GLEEDALADA FEAQHDDYNK IMVKALADRL AEAFAEYLHE RVRKVYWGYA PNENLSNEEL IRENYQGIRP APGYPACPEH TEKATIWELL EVEKHTGMKL TESFAMWPGA SVSGWYFSHP DSKYYAVAQI QRDQVEDYAR RKGMSVSDVE RWLAPNLGYD AD // ID F4V902_ECOLX Unreviewed; 1232 AA. AC F4V902; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGI38683.1}; GN ORFNames=ECNG_04713 {ECO:0000313|EMBL:EGI38683.1}; OS Escherichia coli TA280. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=656444 {ECO:0000313|EMBL:EGI38683.1}; RN [1] {ECO:0000313|EMBL:EGI38683.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TA280 {ECO:0000313|EMBL:EGI38683.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GL884382; EGI38683.1; -; Genomic_DNA. DR RefSeq; WP_001316778.1; NZ_GL884382.1. DR EnsemblBacteria; EGI38683; EGI38683; ECNG_04713. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 252 252 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 315 315 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 316 316 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 764 764 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1232 AA; 136500 MW; 4A7478019BC38B0F CRC64; MSGASVSSKV EQLRAQLNER ILVLDGGMGT MIQSYRLNEA DFRGERFADW PCDLKGNNDL LVLSKPEVIA AIHNAYFEAG ADIIETNTFN STTIAMADYQ MESLSAEINF AAAKLARACA DEWTARTPEK PRYVAGVLGP TNRTASISPD VNDPAFRNIT FDQLVAAYRE STKALVEGGA DLILIETVFD TLNAKAAVFA VKTEFEALGV ELPIMISGTI TDASGRTLSG QTTEAFYNSL RHAEALTFGL NCALGPDELR QYVQELSRIA ECYVTAHPNA GLPNAFGEYD LDADTMAKQI REWAQAGFLN IVGGCCGTTP QHIAAMSRAV EGLAPRKLPE IPVACRLSGL EPLNIGEDSL FVNVGERTNV TGSAKFKRLI KEEKYSEALD VARQQVENGA QIIDINMDEG MLDAEAAMVR FLNLIAGEPD IARVPIMIDS SKWDVIEKGL KCIQGKGIVN SISMKEGVDA FIHHAKLLRR YGAAVVVMAF DEQGQADTRA RKIEICRRAY KILTEEVGFP PEDIIFDPNI FAVATGIEEH NNYAQDFIGA CEDIKRELPH ALISGGVSNV SFSFRGNDPV REAIHAVFLY YAIRNGMDMG IVNAGQLAIY DDLPAELRDA VEDVILNRRD DGTERLLELA EKYRGSKTDD TANAQQAEWR SWEVNKRLEY SLVKGITEFI EQDTEEARQQ ATRPIEVIEG PLMDGMNVVG DLFGEGKMFL PQVVKSARVM KQAVAYLEPF IEASKEQGKT NGKMVIATVK GDVHDIGKNI VGVVLQCNNY EIVDLGVMVP AEKILRTAKE VNADLIGLSG LITPSLDEMV NVAKEMERQG FTIPLLIGGA TTSKAHTAVK IEQNYSGPTV YVQNASRTVG VVAALLSDTQ RDDFVARTRK EYETVRIQHG RKKPRTPPVT LEAARDNDFA FDWQAYTPPV AHRLGVQEVE ASIETLRNYI DWTPFFMTWS LAGKYPRILE DEVVGVEAQR LFKDANDMLD KLSAEKTLNP RGVVGLFPAN RVGDDIEIYR DETRTHVINV SHHLRQQTEK TGFANYCLAD FVAPKLSGKA DYIGAFAVTG GLEEDTLADA FEAQHDDYNK IMVKALADRL AEAFAEYLHE RVRKVYWGYA PNENLSNEEL IRENYQGIRP APGYPACPEH TEKATIWELL EVEKHTGMKL TESFAMWPGA SVSGWYFSHP DSKYYAVAQI QRDQVEDYAR RKGMSVTEVE RWLAPNLGYD AD // ID F4VM02_ECOLX Unreviewed; 1232 AA. AC F4VM02; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 01-APR-2015, entry version 22. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGI42940.1}; GN ORFNames=ECPG_01267 {ECO:0000313|EMBL:EGI42940.1}; OS Escherichia coli H591. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=656408 {ECO:0000313|EMBL:EGI42940.1}; RN [1] {ECO:0000313|EMBL:EGI42940.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=H591 {ECO:0000313|EMBL:EGI42940.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GL884471; EGI42940.1; -; Genomic_DNA. DR EnsemblBacteria; EGI42940; EGI42940; ECPG_01267. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 252 252 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 315 315 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 316 316 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 764 764 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1232 AA; 136398 MW; C103CC20677573CA CRC64; MSGASVSSKV EQLRAQLNER ILVLDGGMGT MIQSYRLNEA DFRGERFADW PCDLKGNNDL LVLSKPEVIA AIHNAYFEAG ADIIETNTFN STTIAMADYQ MESLSAEINF AAAKLARACA DEWTARTPEK PRYVAGVLGP TNRTASISPD VNDPAFRNIT FDGLVAAYRE STKALVEGGA DLILIETVFD TLNAKAAVFA VKTEFEALGV ELPIMISGTI TDASGRTLSG QTTEAFYNSL RHAEALTFGL NCALGPDELR QYVQELSRIA ECYVTAHPNA GLPNAFGEYD LDADTMAKQI REWAQAGFLN IVGGCCGTTP QHIAAMSRAV EGLAPRKLPE IPVACRLSGL EPLNIGEDSL FVNVGERTNV TGSAKFKRLI KEEKYSEALD VARQQVENGA QIIDINMDEG MLDAEAAMVR FLNLIAGEPD IARVPIMIDS SKWDVIEKGL KCIQGKGIVN SISMKEGVDA FIHHAKLLRR YGAAVVVMAF DEQGQADTRA RKIEICRRAY KILTEEVGFP PEDIIFDPNI FAVATGIEEH NNYAQDFIGA CEDIKRELPH ALISGGVSNV SFSFRGNDPV REAIHAVFLY YAIRNGMDMG IVNAGQLAIY DDLPAELRDA VEDVILNRRD DGTERLLELA EKYRGSKTDD TANAQQAEWR SWEVNKRLEY SLVKGITEFI EQDTEEARQQ ATRPIEVIEG PLMDGMNVVG DLFGEGKMFL PQVVKSARVM KQAVAYLEPF IEASKEQGKT NGKMVIATVK GDVHDIGKNI VGVVLQCNNY EIVDLGVMVP AEKILRTAKE VNADLIGLSG LITPSLDEMV NVAKEMERQG FTIPLLIGGA TTSKAHTAVK IEQNYSGPTV YVQNASRTVG VVAALLSDTQ RDDFVARTRK EYETVRIQHG RKKPRTPPVT LEAARDNDFA FDWQAYTPPV AHRLGVQEVE ASIETLRNYI DWTPFFMTWS LAGKYPRILE DEVVGVEAQR LFKDANDMLD KLSAEKTLNP RGVVGLFPAN RVGDDIEIYR DETRTHVINV SHHLRQQTEK TGFANYCLAD FVAPKLSGKA DYIGAFAVTG GLEEDALADA FEAQHDDYNK IMVKALADRL AEAFAEYLHE RVRKVYWGYA PNENLSNEEL IRENYQGIRP APGYPACPEH TEKATIWELL EVEKHTGMKL TESFAMWPGA SVSGWYFSHP DSKYYAVAQI QRDQVEDYAR RKGMSVTEVE RWLAPNLGYD AD // ID F4W2U2_ECOLX Unreviewed; 1227 AA. AC F4W2U2; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGI48173.1}; GN ORFNames=ECOG_05211 {ECO:0000313|EMBL:EGI48173.1}; OS Escherichia coli H299. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=656393 {ECO:0000313|EMBL:EGI48173.1}; RN [1] {ECO:0000313|EMBL:EGI48173.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=H299 {ECO:0000313|EMBL:EGI48173.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GL884549; EGI48173.1; -; Genomic_DNA. DR RefSeq; WP_000096051.1; NZ_GL884549.1. DR EnsemblBacteria; EGI48173; EGI48173; ECOG_05211. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136062 MW; AAADBC336756B69C CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPAEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EYYARRKGMS VSDVERWLAP NLGYDAD // ID F4W3V2_ACREC Unreviewed; 317 AA. AC F4W3V2; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 07-JAN-2015, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase ybgG {ECO:0000313|EMBL:EGI71120.1}; GN ORFNames=G5I_00051 {ECO:0000313|EMBL:EGI71120.1}; OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex OS octospinosus echinatior). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; OC Vespoidea; Formicidae; Myrmicinae; Acromyrmex. OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755}; RN [1] {ECO:0000313|Proteomes:UP000007755} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21719571; DOI=10.1101/gr.121392.111; RA Nygaard S., Zhang G., Schiott M., Li C., Wurm Y., Hu H., Zhou J., RA Ji L., Qiu F., Rasmussen M., Pan H., Hauser F., Krogh A., RA Grimmelikhuijzen C.J., Wang J., Boomsma J.J.; RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key RT adaptations to advanced social life and fungus farming."; RL Genome Res. 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; GL887473; EGI71120.1; -; Genomic_DNA. DR InParanoid; F4W3V2; -. DR Proteomes; UP000007755; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007755}; KW Methyltransferase {ECO:0000313|EMBL:EGI71120.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007755}; KW Transferase {ECO:0000313|EMBL:EGI71120.1}. SQ SEQUENCE 317 AA; 35159 MW; 250CB7805E915679 CRC64; MSEIKVLEGG ATQLFINAGG ETDGDPLWAA RYLVTKPEAI LATHLDFLRA GSNIIRTVTY QATIDGFVKY LGITKEESLE IIRKAVDYAK EAVKIYTKEI ENNKNVTNQK PLIAGSCGPY GASLHDGSEY TGSYCTSVSR EFLMDWHRPR IQALLEKGVD VLAMETIPCA YEAEAIIDLL KEFPDARAWL SFSCKDGKSL ADGSNFQETA VRCYKNAAPG QILAIGTNCI APKYVTSLFQ GINRDKSDDF IPLVVYPNSG EKYTESEGWN KEGDAPTLHE FIDEWLNLGV RYIGGCCRTC ATDVKLIRAK VDQRFKH // ID F4WUN8_ACREC Unreviewed; 322 AA. AC F4WUN8; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 07-JAN-2015, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase ybgG {ECO:0000313|EMBL:EGI62035.1}; GN ORFNames=G5I_09615 {ECO:0000313|EMBL:EGI62035.1}; OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex OS octospinosus echinatior). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; OC Vespoidea; Formicidae; Myrmicinae; Acromyrmex. OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755}; RN [1] {ECO:0000313|Proteomes:UP000007755} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21719571; DOI=10.1101/gr.121392.111; RA Nygaard S., Zhang G., Schiott M., Li C., Wurm Y., Hu H., Zhou J., RA Ji L., Qiu F., Rasmussen M., Pan H., Hauser F., Krogh A., RA Grimmelikhuijzen C.J., Wang J., Boomsma J.J.; RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key RT adaptations to advanced social life and fungus farming."; RL Genome Res. 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; GL888375; EGI62035.1; -; Genomic_DNA. DR InParanoid; F4WUN8; -. DR Proteomes; UP000007755; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007755}; KW Methyltransferase {ECO:0000313|EMBL:EGI62035.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007755}; KW Transferase {ECO:0000313|EMBL:EGI62035.1}. SQ SEQUENCE 322 AA; 36120 MW; 72EE67F464D6A086 CRC64; MMEHCQNAPK ILDGGFSGQL SRHVNTKIDG DPLWTARFLK TNVDAIYATH LDFLRAGADI IETNTYQASV PGMMKYLNIS EHESLNLLKT SVNLARKAVD DYIREESIPF ESRPMVAGSC GPYGAYLHNG SEYTGSYGKN ISRQELIDWH RPRVKALLNA DTDLLAFETI PCVEEAEAIL ELLKEYPHAR AWLSFSCRDG QFMSDGSVFQ NTAVRCYRTL PLQIVAVGVN CIDPKYVTPL LKGINESASS EQDFIPLVVY PNRGGSYSTN GEWIAVQDDH SLNLPMSEWL DLGIRYIGGC CKIFAEDIKL IRSEVNRHSK KF // ID F4WUP0_ACREC Unreviewed; 318 AA. AC F4WUP0; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 07-JAN-2015, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase ybgG {ECO:0000313|EMBL:EGI62037.1}; GN ORFNames=G5I_09617 {ECO:0000313|EMBL:EGI62037.1}; OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex OS octospinosus echinatior). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; OC Vespoidea; Formicidae; Myrmicinae; Acromyrmex. OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755}; RN [1] {ECO:0000313|Proteomes:UP000007755} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21719571; DOI=10.1101/gr.121392.111; RA Nygaard S., Zhang G., Schiott M., Li C., Wurm Y., Hu H., Zhou J., RA Ji L., Qiu F., Rasmussen M., Pan H., Hauser F., Krogh A., RA Grimmelikhuijzen C.J., Wang J., Boomsma J.J.; RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key RT adaptations to advanced social life and fungus farming."; RL Genome Res. 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; GL888375; EGI62037.1; -; Genomic_DNA. DR InParanoid; F4WUP0; -. DR Proteomes; UP000007755; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007755}; KW Methyltransferase {ECO:0000313|EMBL:EGI62037.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007755}; KW Transferase {ECO:0000313|EMBL:EGI62037.1}. SQ SEQUENCE 318 AA; 35678 MW; 363294DE7847C286 CRC64; MSKIKVLDGG FSTQLSTHLD EKINGDPLWT ARFLITKPKA VFATHLDFLR AGADIIETNT YQATTDGFVK HLGITEEESL EIIRKAVDYA KDAVNVYSKE IENDKNVRNR KPLIAGSCGP YGACLHDGSE YIGSYCINVS REFLINWHRP RIRALLERGV DLLAIETIPC VREAEAIIDL LKEFPDTQAW LSFSCRNDGK SLADGNNFQE LAVRCYKNAL PGQILAIGVN CIAPQCVTTL LQDINKNKLN DLIPLIVYPN SGEKYTVSEG WKKEGEIASL HEFIDEWLDL GVRYIGGCCR TYAMDIKQIR SKVDQCRT // ID F4XDD6_9FIRM Unreviewed; 794 AA. AC F4XDD6; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 2. DT 01-OCT-2014, entry version 15. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|EMBL:EGJ46832.2}; GN ORFNames=HMPREF0866_01857 {ECO:0000313|EMBL:EGJ46832.2}; OS Ruminococcaceae bacterium D16. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC unclassified Ruminococcaceae. OX NCBI_TaxID=552398 {ECO:0000313|EMBL:EGJ46832.2}; RN [1] {ECO:0000313|EMBL:EGJ46832.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=D16 {ECO:0000313|EMBL:EGJ46832.2}; 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.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EGJ46832.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=D16 {ECO:0000313|EMBL:EGJ46832.2}; RG The Broad Institute Genomics Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Sibley C.D., White A.P., RA Crowley S., Surette M.G., Strauss J.C., Ambrose C.E., Allen-Vercoe E., RA Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M., RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., RA Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J., RA McCowan C., Murphy C., Pearson M., Poon T.W., 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 Ruminococcaceae bacterium D16."; 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. {ECO:0000313|EMBL:EGJ46832.2}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADDX02000003; EGJ46832.2; -; Genomic_DNA. DR RefSeq; WP_020989898.1; NZ_KI391948.1. DR EnsemblBacteria; EGJ46832; EGJ46832; HMPREF0866_01857. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGJ46832.2}; KW Transferase {ECO:0000313|EMBL:EGJ46832.2}. SQ SEQUENCE 794 AA; 83750 MW; 06A03D69B09FB65F CRC64; MEFLELLKTD RPVLLDGGMG TMLQARGLPV GATPELVALE HPDWLRDIHT AYLDAGSQII YANTFGANRE KLERTGRTVE EIVTAAVTVA KEAATGRGLV ALDIGPCGQL LEPTGMLGFE DAVDLFAQVV RAGVKAGADL IAIETMTDLQ EARAALLAAK ENSNLPVLVT MTYEASGRTF LGCSPAAAAL TLEGLGADAV GVNCSLGPRE MPPLVEELLK WTNLPIVLKP NAGLPHPDGS GYDITPLEFA QSLAALADMG VKVFGGCCGT TPEYIALLSK ELTGKTVKAV PRHVPAAVCS ATQAVPIDRV RVIGERINPT GKKLMKEALR RGDVDYMLGQ ALAQTEAGAD ILDVNVGLPE IDEADMMVRT VKALQGVTDA PLQLDSTDPK VLEQALRVYC GKAIVNSVNG ESASLETILP LVKKYGAAVV GLTLDENGIP KNAQARFEVA KRILERAMAL GIRREDVYID CLTLTVSAEQ AAASQTLEAL HRVKTELGLK TVLGVSNISF GLPARPLVNQ NFLTMAMSAG LDLPIINPNV DAMMAAVRCF HLLTNVDTDA REFIAAYANA SVSTSITAGS APAAPQSTGR SLKDLVIAGL KGEAGQATRA LLETTAPMDI VDNVLIPALD QVGADFEQNK VFLPQLIQSA GAAQAAFEVI REKLSTGEGG NVSRGNVVLA TVKGDIHDIG KNIVKVLLEN YGYTVIDLGR DVDPAAVVEA ARKYEAPLVG LSALMTTTLK SMAQTIAQLH DAGLPCKIMV GGAVLTPEYA KEISADFYAR DAKESVDIAK RVVG // ID F4XRI5_9CYAN Unreviewed; 1196 AA. AC F4XRI5; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Methionine synthase, B12-dependent {ECO:0000313|EMBL:EGJ32828.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGJ32828.1}; GN ORFNames=LYNGBM3L_75820 {ECO:0000313|EMBL:EGJ32828.1}; OS Moorea producens 3L. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Moorea. OX NCBI_TaxID=489825 {ECO:0000313|EMBL:EGJ32828.1}; RN [1] {ECO:0000313|EMBL:EGJ32828.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=3L {ECO:0000313|EMBL:EGJ32828.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GL890901; EGJ32828.1; -; Genomic_DNA. DR RefSeq; WP_008183867.1; NZ_GL890901.1. DR EnsemblBacteria; EGJ32828; EGJ32828; LYNGBM3L_75820. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGJ32828.1}; KW Transferase {ECO:0000313|EMBL:EGJ32828.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 228 228 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 737 737 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1196 AA; 132968 MW; 1D0BE396C7EDC8CE CRC64; MNSPFLNHLH SPKRPVIVFD GATGTSLQTQ NLTAEDFGGP EYEGCNEYLV HTKPEAVEKV HRGFLEVGAD VIETDTFGGT SIVLAEYDLA DQAYYLNKAA AELAKRMAAE YSTPEKPRFV AGSMGPGTKL PTLGHIDFDT LKNAYVEQAL GLYDGGSDLL IVETCQDVLQ IKAALNAIEE VFEKKGARLP LMVSITMEVM GTMLVGSEIN AALTILEPYP IDILGLNCAT GPEQMKEHIK YLSECSPFVV SCIPNAGLPE NVGGHAHYRL TPMELRMALM HFVEDLGVQV IGGCCGTRPA HIEQLAEFAQ TLTPKERNPK HEPSAASIYS SQPYEQDNSF LIVGERLNAS GSKKCRTMLN AEDWDGLVSL AKSQIREGAN VLDVNVDYVG RDGVRDMNEL ASRLVTNSTL PLMLDSTEWE KMEAGLKVVG GKCILNSTNY EDGEPRFYKV LELAKIYGAG VVIGTIDEDG MARTADKKFE IAKRAYNDAI AYGIPAHELF FDTLALPIST GIEEDRENGK ATIESIRRIR EELPGCHVML GVSNISFGLN PAARIVLNSM FLHEAMQVGM DAAIVSASKI LPLAKIEPEH QEVCRKLIYD QREFDGDVCT YDPLTKLTTL FEGKTTKRDR SQDENLSVEE RLKRHIIDGE RIGLEEQLEK AREKYPPLEI INTFLLDGMK VVGELFGSGQ MQLPFVLQSA QTMKAAVAYL EPYMEKSEAG KNAKGTFVIA TVKGDVHDIG KNLVDIILSN NGYEVINLGI KQPVDNIIDA YEKHNADCIA MSGLLVKSTA FMKDNLETFN ERGITVPVIL GGAALTPKFV HKDCQNTYNG QVVYGKDAFS DLHFMDKLMP AKAAGNWDDS KGFIDELENG VAVEASSELK VDKLQENGSK DNSQPATPLS TPVDTNRSEG VTLDIERPTP PFWGTKILQP EDISFEEVLW YLDLQALIAG QWQFRKPKDQ SREEYNQFLK EKVDPILDKW KEKTLAENLL HPQVVYGYFP CLAEGNSLII YDAKGMNPEG AKDSQELQEV ARFEFPRQRS GKRLCIADFF LPKELAGAGQ FDVFPMQAVT VGDIATEYAK ELFDGDQYTD YLYYHGLAVQ MAEALAEWSH ARIRRELGFA DQEPDSIRDV LAQRYQGSRY SFGYPACPNL QDQYKQLDLL ECDRIKLYMD ESEQLYPEQS TTAIVAYHPI ARYFTA // ID F5HD22_CRYNB Unreviewed; 381 AA. AC F5HD22; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 29-APR-2015, entry version 19. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EAL18452.1}; GN OrderedLocusNames=CNBJ0940 {ECO:0000313|EMBL:EAL18452.1}; 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 {ECO:0000313|EMBL:EAL18452.1, ECO:0000313|Proteomes:UP000001435}; RN [1] {ECO:0000313|Proteomes:UP000001435} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B-3501A {ECO:0000313|Proteomes:UP000001435}; 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., Koo H.L., Krzywinski M.I., RA Kwon-Chung J.K., 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. {ECO:0000313|EMBL:EAL18452.1}. 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; AAEY01000049; EAL18452.1; -; Genomic_DNA. DR RefSeq; XP_773099.1; XM_768006.1. DR ProteinModelPortal; F5HD22; -. DR GeneID; 4938434; -. DR KEGG; cnb:CNBJ0940; -. DR EuPathDB; FungiDB:CNBJ0940; -. DR KO; K00547; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000001435; Chromosome 10. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 2. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001435}. SQ SEQUENCE 381 AA; 41541 MW; F0AF5A63A64E5BA3 CRC64; MSSNILVLDG GMGTTLESLG VDISSPLWGS EALRTNPDVI RKVHEGYVQG GADLVETATY QLTPQNLCDH LHCPREEAEC ILCSGVKLVA SCIASCSSRN EEHNTKSKGG NKSKVVLSFG PYGSTLQPGQ EYGGIYPPPF GPSTSTNAFP PDSNDEEEAA IQALAYHHLD KLEAISHDGA AWREVEWIAF ETIPVLHEVR GIRRAMAILR GKLSALYADG DNIDLWWEKK FWITSPFPMG QHPQLLPDGS HASIPQVIHS LFSGPDPIPN GIGINCTNPS YLHFLSSSFT SHLPFEFFGK VEMVIYPDGG QMYDTTTRAW VVAPQSPENA EKWAEVVGDV AKGVRGAERE GKGVWKGVVV GGCCKSSFDE IRALRRFVDS Q // ID F5HYF3_ACIBA Unreviewed; 292 AA. AC F5HYF3; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGJ60572.1}; GN ORFNames=HMPREF0021_01730 {ECO:0000313|EMBL:EGJ60572.1}; OS Acinetobacter baumannii 6013150. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=525243 {ECO:0000313|EMBL:EGJ60572.1}; RN [1] {ECO:0000313|EMBL:EGJ60572.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=6013150 {ECO:0000313|EMBL:EGJ60572.1}; 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 (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGJ60572.1}. 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; ACYQ02000038; EGJ60572.1; -; Genomic_DNA. DR RefSeq; WP_000696108.1; NZ_GL891651.1. DR ProteinModelPortal; F5HYF3; -. DR EnsemblBacteria; EGJ60572; EGJ60572; HMPREF0021_01730. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EGJ60572.1}; KW Transferase {ECO:0000313|EMBL:EGJ60572.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 202 202 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 275 275 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 276 276 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 292 AA; 32064 MW; EB1B58B1EF96D60A CRC64; MKILDGGLGR ELARRGAPFR QPEWSALALI EAPETVKEVH LDFINAGAEV ITTNNYAVVP FHIGQERFET DGVRLIKVAI EQAKNAVKES GKNVKIAGCL PPLFGSYRAD LFQPEQAKNL AEPIINTLAP EVDFWLAETQ SCLKEVETVH ALLPQDGKDY WVSFTLQDEI KQEQALLRSG ENMQQVADFI KQSNAKAVLF NCCQPEVILQ AINEIKGLIP ESVQIGAYAN AFPPQDESAT ANDGLDEIRK DLDAPAYLGF AKQWQQAGAS LVGGCCGIGP EHIAELSQFF KE // ID F5I0N4_ACIBA Unreviewed; 1228 AA. AC F5I0N4; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EGJ59904.1}; GN ORFNames=HMPREF0021_02519 {ECO:0000313|EMBL:EGJ59904.1}; OS Acinetobacter baumannii 6013150. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=525243 {ECO:0000313|EMBL:EGJ59904.1}; RN [1] {ECO:0000313|EMBL:EGJ59904.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=6013150 {ECO:0000313|EMBL:EGJ59904.1}; 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 (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGJ59904.1}. 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; ACYQ02000070; EGJ59904.1; -; Genomic_DNA. DR RefSeq; WP_000105326.1; NZ_GL891683.1. DR ProteinModelPortal; F5I0N4; -. DR SMR; F5I0N4; 654-893. DR EnsemblBacteria; EGJ59904; EGJ59904; HMPREF0021_02519. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGJ59904.1}; KW Transferase {ECO:0000313|EMBL:EGJ59904.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1228 AA; 135817 MW; DDD77AD11982DA91 CRC64; MSTLATLKAL LAKRILIIDG AMGTMIQRHK LEEADYRGER FADWAHDLKG NNDLLVLTQP QIIQGIHEAY LDAGADIIET NSFNGTRVSM SDYHMEDLVP EINREAARLA KAACEKYSTP DKPRFVAGVL GPTSRTCSIS PDVNNPAFRN ISFDELKENY IEATHALIEG GADIILIETV FDTLNCKAAI FAVKEVFKQI GRELPIMISG TITDASGRTL TGQTAEAFWN SVRHGDLLSI GFNCALGADA MRPHVKTISD VADTFVSAHP NAGLPNAFGE YDETPEQTAA FLKEFAESGL INITGGCCGT TPDHIRAIAN AVKDIAPRQV PETVPACRLS GLEPFNIYDD SLFVNVGERT NVTGSKKFLR LIREENFAEA LEVAQQQVEA GAQIIDINMD EGMLDSQNAM VHFLNLVASE PDISRVPIMI DSSKWEIIEA GLKCVQGKPV VNSISLKEGY DEFVEKARLC RQYGAAIIVM AFDEVGQADT AERKREICKR SYDILVNEVG FPAEDIIFDP NVFAVATGIE EHNNYAVDFI EATGWIKQNL PHAMISGGVS NVSFSFRGNE PVREAIHSVF LYHAIKQGMT MGIVNAGQMA IYDDIPTELK EAVEDVILNQ NQGESGQAAT EKLLEVAEKY RGQGGATKEA ENLEWRNESV EKRLEYALVK GITTYIDQDT EEARLKSKRP LDVIEGPLMD GMNVVGDLFG SGKMFLPQVV KSARVMKQAV AWLNPYIEAE KTEGQSKGKV LMATVKGDVH DIGKNIVGVV LGCNGYDIVD LGVMVPCEKI LQTAIDEKCD IIGLSGLITP SLDEMVFVAK EMQRKGFNIP LLIGGATTSK AHTAVKIDPQ YQNDAVIYVA DASRAVGVAT TLLSKEMRGA FIEEHRAEYA KIRERLANKQ PKAAKLTYKE SVENGFKIDE SYVPPKPNLL GTQVLKNYPL ATLVDYFDWT PFFISWSLTG KFPKILEDEV VGEAATDLYN QAQAMLKDII DNNRFDARAV FGMFPAQRTD ADTVSVFDEA GQNVTHTFEH LRQQSDKVTG KPNLSLADYI RADREQQDYL GGFTVSIFGA EELANEYKAK GDDYSAILVQ SLADRFAEAF AEHLHERIRK EFWGYKADEQ LSNEELIKEK YVGIRPAPGY PACPEHSEKA VLFDWLGSTD KIGTKLTEHF AMMPPSSVSG FYYSHPQSEY FNVGKISQDQ LEDYAKRKGW TLDEAKRWLA PNLDDSIV // ID F5IDS8_ACIBA Unreviewed; 1228 AA. AC F5IDS8; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EGJ63264.1}; GN ORFNames=HMPREF0020_03183 {ECO:0000313|EMBL:EGJ63264.1}; OS Acinetobacter baumannii 6013113. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=592014 {ECO:0000313|EMBL:EGJ63264.1}; RN [1] {ECO:0000313|EMBL:EGJ63264.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=6013113 {ECO:0000313|EMBL:EGJ63264.1}; 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 (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGJ63264.1}. 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; ACYR02000205; EGJ63264.1; -; Genomic_DNA. DR RefSeq; WP_000105326.1; NZ_GL891608.1. DR ProteinModelPortal; F5IDS8; -. DR SMR; F5IDS8; 654-893. DR EnsemblBacteria; EGJ63264; EGJ63264; HMPREF0020_03183. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGJ63264.1}; KW Transferase {ECO:0000313|EMBL:EGJ63264.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1228 AA; 135817 MW; DDD77AD11982DA91 CRC64; MSTLATLKAL LAKRILIIDG AMGTMIQRHK LEEADYRGER FADWAHDLKG NNDLLVLTQP QIIQGIHEAY LDAGADIIET NSFNGTRVSM SDYHMEDLVP EINREAARLA KAACEKYSTP DKPRFVAGVL GPTSRTCSIS PDVNNPAFRN ISFDELKENY IEATHALIEG GADIILIETV FDTLNCKAAI FAVKEVFKQI GRELPIMISG TITDASGRTL TGQTAEAFWN SVRHGDLLSI GFNCALGADA MRPHVKTISD VADTFVSAHP NAGLPNAFGE YDETPEQTAA FLKEFAESGL INITGGCCGT TPDHIRAIAN AVKDIAPRQV PETVPACRLS GLEPFNIYDD SLFVNVGERT NVTGSKKFLR LIREENFAEA LEVAQQQVEA GAQIIDINMD EGMLDSQNAM VHFLNLVASE PDISRVPIMI DSSKWEIIEA GLKCVQGKPV VNSISLKEGY DEFVEKARLC RQYGAAIIVM AFDEVGQADT AERKREICKR SYDILVNEVG FPAEDIIFDP NVFAVATGIE EHNNYAVDFI EATGWIKQNL PHAMISGGVS NVSFSFRGNE PVREAIHSVF LYHAIKQGMT MGIVNAGQMA IYDDIPTELK EAVEDVILNQ NQGESGQAAT EKLLEVAEKY RGQGGATKEA ENLEWRNESV EKRLEYALVK GITTYIDQDT EEARLKSKRP LDVIEGPLMD GMNVVGDLFG SGKMFLPQVV KSARVMKQAV AWLNPYIEAE KTEGQSKGKV LMATVKGDVH DIGKNIVGVV LGCNGYDIVD LGVMVPCEKI LQTAIDEKCD IIGLSGLITP SLDEMVFVAK EMQRKGFNIP LLIGGATTSK AHTAVKIDPQ YQNDAVIYVA DASRAVGVAT TLLSKEMRGA FIEEHRAEYA KIRERLANKQ PKAAKLTYKE SVENGFKIDE SYVPPKPNLL GTQVLKNYPL ATLVDYFDWT PFFISWSLTG KFPKILEDEV VGEAATDLYN QAQAMLKDII DNNRFDARAV FGMFPAQRTD ADTVSVFDEA GQNVTHTFEH LRQQSDKVTG KPNLSLADYI RADREQQDYL GGFTVSIFGA EELANEYKAK GDDYSAILVQ SLADRFAEAF AEHLHERIRK EFWGYKADEQ LSNEELIKEK YVGIRPAPGY PACPEHSEKA VLFDWLGSTD KIGTKLTEHF AMMPPSSVSG FYYSHPQSEY FNVGKISQDQ LEDYAKRKGW TLDEAKRWLA PNLDDSIV // ID F5IDX7_ACIBA Unreviewed; 292 AA. AC F5IDX7; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGJ63189.1}; GN ORFNames=HMPREF0020_03232 {ECO:0000313|EMBL:EGJ63189.1}; OS Acinetobacter baumannii 6013113. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=592014 {ECO:0000313|EMBL:EGJ63189.1}; RN [1] {ECO:0000313|EMBL:EGJ63189.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=6013113 {ECO:0000313|EMBL:EGJ63189.1}; 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 (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGJ63189.1}. 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; ACYR02000206; EGJ63189.1; -; Genomic_DNA. DR RefSeq; WP_000696108.1; NZ_GL891608.1. DR ProteinModelPortal; F5IDX7; -. DR EnsemblBacteria; EGJ63189; EGJ63189; HMPREF0020_03232. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EGJ63189.1}; KW Transferase {ECO:0000313|EMBL:EGJ63189.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 202 202 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 275 275 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 276 276 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 292 AA; 32064 MW; EB1B58B1EF96D60A CRC64; MKILDGGLGR ELARRGAPFR QPEWSALALI EAPETVKEVH LDFINAGAEV ITTNNYAVVP FHIGQERFET DGVRLIKVAI EQAKNAVKES GKNVKIAGCL PPLFGSYRAD LFQPEQAKNL AEPIINTLAP EVDFWLAETQ SCLKEVETVH ALLPQDGKDY WVSFTLQDEI KQEQALLRSG ENMQQVADFI KQSNAKAVLF NCCQPEVILQ AINEIKGLIP ESVQIGAYAN AFPPQDESAT ANDGLDEIRK DLDAPAYLGF AKQWQQAGAS LVGGCCGIGP EHIAELSQFF KE // ID F5IVZ6_9PORP Unreviewed; 1230 AA. AC F5IVZ6; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGK02796.1}; GN ORFNames=HMPREF9455_01046 {ECO:0000313|EMBL:EGK02796.1}; OS Dysgonomonas gadei ATCC BAA-286. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Dysgonomonas. OX NCBI_TaxID=742766 {ECO:0000313|EMBL:EGK02796.1}; RN [1] {ECO:0000313|EMBL:EGK02796.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-286 {ECO:0000313|EMBL:EGK02796.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGK02796.1}. 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; ADLV01000015; EGK02796.1; -; Genomic_DNA. DR RefSeq; WP_006798561.1; NZ_GL891980.1. DR EnsemblBacteria; EGK02796; EGK02796; HMPREF9455_01046. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 243 243 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 756 756 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1230 AA; 137236 MW; B9E439F76ADDD8CE CRC64; MSKIHDILKD RILILDGAMG TMIQRYKLTE EDFRGDRFKD STTLLKGNND LLCLTRPDVI EAIHREYLEA GADIIETNTF NATSISMEDY HMSDLVKEIN TEAARLAKKA AVDYTKRNPD KPRFVAGSIG PTNKTASMSP KVENPIFRAV TFDDLYYAYK EQIEGLADGG VDLLLIETIF DTLNAKAALF AADEVRKERN IDLPIMISVT LSDKGGRTLS GQTVGAFVAS VSHIDFLSIG LNCSFGASDM KPFLKELGRI APNFISAYPN AGLPNQFGEY DETPEIMAGQ IKEYIDEGLV NILGGCCGTT PDHIAKYVDL IQGATPHKPA RKPEYMWLSG LELLEAKPEI NFINIGERLN VAGSRKFLRL IKEEKYEEAL TIAHKQVEDG AQVLDVNMDE GLLDGVKEMT TFLNLMASDP DVSRIPVMID SSKWEVLEAG LKCVQGKPIV NSISLKGGEE DFLRQARLVK AYGAAVIVMA FDETGQADTF ARRIEICKRA YNLLVNDGFN PLDIIFDPNI LAIATGIEEH RGYAVDFLET ITWIKENLPH AKISGGVSNL SFSFRGNDYV REAMHAVFLY YAIQRGMDMG IVNPGQSVVY DDIPTDLRNL VEDVIFNRRA EATDELIEYA EKIKNENTGQ TEQKVEEWRS YPLDERIQYS LIKGISDYLE EDLTEALQVY PKAVDIIDKP LMDGMNKVGD LFGSGKMFLP QVVKTARTMK RAVAILQPTL EAQKASSAGS NKAGKLVIAT VKGDVHDIGK NIVSIILACN NYEVIDLGVM TPPEVIIQKV KEEQPDILCL SGLITPSLEE MSIVAHEMEK AGFTIPLMIG GATTSKLHTA IKIDPKYNNG SVVYVKDASQ APAAVGKLIN PKTKEDYIKD VRTEYASLRD TAGDKKADLL PLCEVLDKGM KLNWGDYKTP EPQVKGRQTL KHIPVETIVP YIDWKFFFHS WNLSARYATV QNIDDCPSCK ATWLNSFPEY EREKAAEGMQ LYKDAKALLD QLVYDKAGYI NAVFGVYESY SDNESLYIDG IRFPMLRQQK KNDKKEYLSL CDFVAPKSSG KKDYVGGFTV TAGVGANELM SEYERQGDEY KVLLLKSVLD RLAEATTEWL HAEIRRKYWA FAPDENISVN DMFTLKYQGI RPAVGYPSIP DQSINFLLNK DLLQSEEIGV ELTENGVMLP NASVSGIIIS HPKSKYFNIG NILDDQLQAY IERRGEDAEQ IRKFLSANLI // ID F5J695_9RHIZ Unreviewed; 1257 AA. AC F5J695; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 01-APR-2015, entry version 23. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EGL66622.1}; GN Name=metH {ECO:0000313|EMBL:EGL66622.1}; GN ORFNames=AGRO_0697 {ECO:0000313|EMBL:EGL66622.1}; OS Agrobacterium sp. ATCC 31749. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium. OX NCBI_TaxID=82789 {ECO:0000313|EMBL:EGL66622.1}; RN [1] {ECO:0000313|EMBL:EGL66622.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 31749 {ECO:0000313|EMBL:EGL66622.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGL66622.1}. 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; AECL01000008; EGL66622.1; -; Genomic_DNA. DR RefSeq; WP_006310514.1; NZ_AECL01000008.1. DR EnsemblBacteria; EGL66622; EGL66622; AGRO_0697. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 260 260 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 776 776 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1257 AA; 138692 MW; 4517E93F172D3DD2 CRC64; MFDDLFGPEG AKRDGAEIFK ALRDAASERI LILDGAMGTQ IQGLGFDEDH FRGDRFIGCA CHQKGNNDLL ILTQPDAIEE IHYRYAMAGA DILETNTFSS TRIAQADYEM ENAVYDLNRE GAAIVRRAAQ RAEREDGRRR FVAGAIGPTN RTASISPDVN NPGYRAVSFD DLRIAYGEQI DGLIDGGADI ILIETIFDTL NAKAAIFACE ERFEAKGIRL PVMISGTITD LSGRTLSGQT PSAFWNSVRH ANPFTIGLNC ALGADAMRPH LQELSDVADT FVCAYPNAGL PNEFGQYDET PEMMARQVEG FVRDGLVNIV GGCCGSTPEH IRAIAEAVKN YKPREIPEHK PFMSLSGLEP FVLTKDIPFV NVGERTNVTG SARFRKLITA GDYTAALAVA RDQVENGAQI IDINMDEGLI DSEKAMVEFL NLIAAEPDIA RVPVMIDSSK FEIIEAGLKC VQGKSIVNSI SLKEGEEKFL QQARLVHNYG AAVVVMAFDE VGQADTYQRK VEICARAYKL LTEKAGLSPE DIIFDPNVFA VATGIEEHNN YGVDFIEATK TIRETMPLTH ISGGVSNLSF SFRGNEPVRE AMHAVFLYHA IQAGMDMGIV NAGQLAVYDN IDAELREACE DVVLNRRDDA TERLLEVAER FRGTGEKQAK VQDLSWREYP VEKRLEHALV NGITDYIEAD TEEARQQAAR PLHVIEGPLM AGMNVVGDLF GSGKMFLPQV VKSARVMKQA VAVLLPYMEE EKRLNGGSER SAAGKVLMAT VKGDVHDIGK NIVGVVLACN NYEIIDLGVM VPTTKILETA IAEKVDVIGL SGLITPSLDE MVHVAAEMER QGFDIPLLIG GATTSRVHTA VKIHPRYEQG QAIYVTDASR AVGVVSALLS EEQKPAYIDG IRAEYAKVAE AHARNEREKQ RLPLSRAREN AHKIDWSSYS VVKPQFFGTK VFETYNLEEL SRYIDWTPFF QTWELKGRFP AILEDEKQGE AARQLYADAQ AMLAKIIEEK WFRPRAVIGF WPANAVGDDI RLFTDESRNE ELATFFTLRQ QLSKRDGRPN VALSDFVAPV DSGVADYVGG FVVTAGIEEV AIAERFERAN DDYSSILVKA LADRFAEAFA ERMHERVRKE FWGYAPDEAL AGDDLIGEAY AGIRPAPGYP AQPDHTEKKT LFALLDATNA AGVELTESYA MWPGSSVSGL YIGHPESYYF GVAKVERDQV LDYARRKDMP VTEVERWLGP VLNYVPTNGE EKIDSAA // ID F5J962_9RHIZ Unreviewed; 304 AA. AC F5J962; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=S-methyltransferase {ECO:0000313|EMBL:EGL65572.1}; GN ORFNames=AGRO_1687 {ECO:0000313|EMBL:EGL65572.1}; OS Agrobacterium sp. ATCC 31749. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium. OX NCBI_TaxID=82789 {ECO:0000313|EMBL:EGL65572.1}; RN [1] {ECO:0000313|EMBL:EGL65572.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 31749 {ECO:0000313|EMBL:EGL65572.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGL65572.1}. 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; AECL01000026; EGL65572.1; -; Genomic_DNA. DR RefSeq; WP_006311749.1; NZ_AECL01000026.1. DR EnsemblBacteria; EGL65572; EGL65572; AGRO_1687. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EGL65572.1}; KW Transferase {ECO:0000313|EMBL:EGL65572.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 304 AA; 31821 MW; 67C655C8477A5CB7 CRC64; MGTIRILDGG MSRELQRLGA ELKQPEWSAL ALINAPDIVR QVHAEFIEAG ADVVTTNSYA LVPFHIGEER FQKDGASLIA LSGQLAREAA DASGRKVLVA GSLPPIFGSY EPQNFDATRV QDYLKVLVDN LAPSVDVWLG ETLSLIAEGE AVREAVAATD KPFWISFTLN DDATAVAGGE PALRSGEPVK AAAEWAAQSG AAALLFNCSK PEIMKAAVET ASAVFADKGV SLEIGVYANA FEGEQGDSAA NEGLHGTRTD LTDDVYSRFA CSWADAGATM IGGCCGIGAA HIHTVATALR RAAA // ID F5L0L2_9FIRM Unreviewed; 341 AA. AC F5L0L2; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 01-OCT-2014, entry version 10. DE SubName: Full=Putative homocysteine S-methyltransferase {ECO:0000313|EMBL:EGL77250.1}; GN ORFNames=HMPREF9323_0048 {ECO:0000313|EMBL:EGL77250.1}; OS Veillonella parvula ACS-068-V-Sch12. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Veillonella. OX NCBI_TaxID=768727 {ECO:0000313|EMBL:EGL77250.1}; RN [1] {ECO:0000313|EMBL:EGL77250.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ACS-068-V-Sch12 {ECO:0000313|EMBL:EGL77250.1}; 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. {ECO:0000313|EMBL:EGL77250.1}. 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; AEXI01000012; EGL77250.1; -; Genomic_DNA. DR EnsemblBacteria; EGL77250; EGL77250; HMPREF9323_0048. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGL77250.1}; KW Transferase {ECO:0000313|EMBL:EGL77250.1}. SQ SEQUENCE 341 AA; 37082 MW; F706B05914E7C92C CRC64; MGGMMAKRSA FLDIIKEKGA LVLDGALGTE LERYGCDIQH KLWSAKVLMD QPEIIKKIHI SYLAAGADII QSSGYQATVA GFKGLGYGTE EAIELVKLSV RLAVQARNEF LEAKASGALT LHGIKLGEET PEGVRYFSEG ALPKPLVAAS VGPYGAFLAD GSEYRGYPDV QTEYLEIFHI PRLALFCEEH PDILSFETIP SYAEAIAIAR AMSDPFTSKG IPGWIAFSCK DGHHVSSGET IIKCAQMIDK VHPITGIGIN CSKPEYVESL IKDIRTVTDK PIAVYPNLGE SYDSKTKTWY GDAASFVDYV EVWRKAGAEI IGGCCRTTPE IIGDIAKKIH N // ID F5L0R9_9FIRM Unreviewed; 813 AA. AC F5L0R9; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 01-APR-2015, entry version 16. DE SubName: Full=Putative methionine synthase {ECO:0000313|EMBL:EGL77163.1}; GN ORFNames=HMPREF9323_0972 {ECO:0000313|EMBL:EGL77163.1}; OS Veillonella parvula ACS-068-V-Sch12. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Veillonella. OX NCBI_TaxID=768727 {ECO:0000313|EMBL:EGL77163.1}; RN [1] {ECO:0000313|EMBL:EGL77163.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ACS-068-V-Sch12 {ECO:0000313|EMBL:EGL77163.1}; 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. {ECO:0000313|EMBL:EGL77163.1}. 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; AEXI01000013; EGL77163.1; -; Genomic_DNA. DR EnsemblBacteria; EGL77163; EGL77163; HMPREF9323_0972. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; SQ SEQUENCE 813 AA; 87239 MW; F8DB354D41EEF814 CRC64; MFMYIFDGAM GTMLQAAGLE EGYCPELFNI ERPEVVKDIH AQYLQHGSDV ITTNTFGACG LKLEDYDLQD RVREINIAAV KVAKEAIAET KPTARVAGSM GPTGRFLQPL GNMSFDSIYD TYREQAEALI EGGVDFIIIE TIIDVQEMRA ALLASLDARE AAGKTKDDVQ IICQFSFSED GRTITGTPPA VATTIVEAIG ADIIGINCSL GPEQITPLIE EIASVTNLLI SCQPNAGMPQ LINKQTVFPL SAEEMGPLML PIVDAGASYV GGCCGTTPAH IQSISDAVKA HTPKERAHIA PKTIITSRTK LLELGHHTKP LIIGERINPT GRKVLAQELR DGSFIRVKRD ALDQVEAGAD ILDVNMGVAG MDQSPLMERA IFELSMLVET PLSIDTLDPV AMEIALKNYP GRALINSVNG EEESITHVMP LAKRYGAALL CLPICSGDLP EKAEDRVALA ESIVNRAYGY GLHPHDLLLD PLVLTLASGE DSARQTLRTL QLYKEKFGFP TVMGLSNISF GMPQRPYLNG QFLTMALACG LTTPIMNPLN YPAKKAFVSS TTLLGWDPGS AEFIKEYGYE DETTAPGNSA PKGPDKKSFD SNDPLANIRA CVEQGEKEAI IDLVKKALAD GIDPLDLTKK GLSEAMNVVG DKFGSGKLFL PQVMLAAETM QAAFNTIKEI IPASESLDKG TVVVATVKGD IHDLGKNIVA ALLENNGYKI VDLGKDVDPE VIVQAIKDNK AALVGICSLM TTTMPQIDNT IAAIRAAGLK TKVMVGGAVV SQDYADQAGA DIYAKDGIAA VNHANDFFET LEK // ID F5L7C1_9BACI Unreviewed; 623 AA. AC F5L7C1; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 22. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=CathTA2_1721 {ECO:0000313|EMBL:EGL82782.1}; OS Caldalkalibacillus thermarum TA2.A1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; OC Caldalkalibacillus. OX NCBI_TaxID=986075 {ECO:0000313|EMBL:EGL82782.1}; RN [1] {ECO:0000313|EMBL:EGL82782.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TA2.A1 {ECO:0000313|EMBL:EGL82782.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGL82782.1}. 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; AFCE01000139; EGL82782.1; -; Genomic_DNA. DR RefSeq; WP_007504800.1; NZ_AFCE01000139.1. DR EnsemblBacteria; EGL82782; EGL82782; CathTA2_1721. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EGL82782.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EGL82782.1}. SQ SEQUENCE 623 AA; 68659 MW; CBC035A15AFD098C CRC64; MALLDDLQAR VLIADGAMGT LLYSYGVGHC YEELNISQPE QIQAIHQAYL DAGAQVIQTN TYAANYAKLS RYGLEDMVKE INVHAVRLAK AAANGRAYVL GTIGGIRGAG RKATPLEEIK RSFREQLFWL LQEEPDGLIL ETYYDLEELS TVLQIARKET PLPIIAQVSL HEAGVLQGGI PLSEALNQLE ELGADVIGVN CRLGPHHMLR SLEQVPLPRR AYLSAYPNAS LLNYVDGRLI YQSEPDYFAQ QARAIVEQGV RLIGGCCGTT PAHIQAMAGA LKDVKPVTEK EVQPQLVQIE EISLPPGPPG HKEQLQDVVA ERKSVIVELD PPKHLDTGRF MEGASALKQA GIDALTMADN SLATPRISNM AMAALIQQQL GVRPLVHVTC RDRNLIGLQS HLLGLYCLGI DHVLAVTGDP TKIGDFPGAT SVYDLSSIEL IQLIKQMNEG LSFSGKPLKR KTSFSVAAAF NPNVRHLERA VARLEKKIEA GADYFISQPV YDHAHLHEIY EATKHLPVPI YIGIMPLTSS RNAEFLHHEV PGIKLTDEIR QRMAAVAHDP RLSQQEGLAI AKALIDTAYK LFNGIYLITP FMRYEISVEL VNYIHAKQQT GKERELSHGR HIV // ID F5L7C2_9BACI Unreviewed; 1148 AA. AC F5L7C2; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGL82783.1}; GN ORFNames=CathTA2_1722 {ECO:0000313|EMBL:EGL82783.1}; OS Caldalkalibacillus thermarum TA2.A1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; OC Caldalkalibacillus. OX NCBI_TaxID=986075 {ECO:0000313|EMBL:EGL82783.1}; RN [1] {ECO:0000313|EMBL:EGL82783.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TA2.A1 {ECO:0000313|EMBL:EGL82783.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGL82783.1}. 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; AFCE01000139; EGL82783.1; -; Genomic_DNA. DR RefSeq; WP_007504802.1; NZ_AFCE01000139.1. DR EnsemblBacteria; EGL82783; EGL82783; CathTA2_1722. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 723 723 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1148 AA; 126074 MW; CAE1DFCB52635FC4 CRC64; MADTLFEQQL KQKILIIDGA MGTMLQQAGL TAEDFGGEEY EGCNEYLNLT APHIVEQIHR AYLEAGADII ETNTFGGTAL VLNEYNLGHL ALEINRTAAE IARKVADEYS TPGWPRFVAG SMGPTTKSLS VTGGTTFEEL VAHYREQATG LLLGGVDLLL LETSQDMRNV KAGYIGICQA FEKVGRKVPL LVSGTIEPMG TTLAGQNIEA FYLSLEHMQP AAVGLNCATG PEFMTDHLRS LSQLATTAVF CYPNAGLPDE EGNYHESPES LAQKLAAFAE KGWLNMTGGC CGTTPEHIKA VAEAVKPYAP RQIPEDHPHA VSGIEPLIYD TSMRPLLVGE RTNVIGSRKF KRLIAEGKYE EAAEIARAQV KGGAHVIDIC LADPDRDELA DMEQFLKHVI NKVKVPLMID STDEKVIEKA LTYCQGKAII NSINLEDGEE RFKKVVPLIK RFGAAVVVGT IDEQGMAVKA EDKLRIARRS YDLLVNKYGL NPKDIIFDPL VFPVGTGDKQ YIGSAKATID GLRMIKEAFP ECPTILGISN VSFGLPPVGR EVLNAVFLYH CTQAGLDYAI VNTEKLERFA SIPEEEVKLA ETLIFEMSDE ALANFTAHFR GMRAKEKKQT SQMSLEERLA NYVVEGTKEG LYADLDQALA KYPNPLDIIN GPLMEGMAEV GRLFNDNQLI VAEVLQSAEV MKAAVAYLEP HMEKTSDSGK GKVILATVKG DVHDIGKNLV DIILSNNGYK VIDLGINVAP TTLIEVVRQE QPDIIGLSGL LVKSAQQMVL TAQDLKAANI AVPILVGGAA LSRQFTEHKI APEYEGLVLY AKDAMDGLSL ANRLQSAEER EKIILEKQEQ QAKRAARPLA AAGPQAQTAT AVKVRSNVSP DVPVYVPADL ERHVLKDYSI AHIQPYINMQ MLLGHHLGLK GKVARLLEEG DERALELKEL VDSLLAEAKA NGLISAHGVY QFFPAQSDGD DVLIYDPADR QTVIERFHFP RQTKAPYLCL ADYLKPADSG EMDYVGCFAV TAGKGIREQA LKLKEQGDYL RSHALQALAL ELAEGFAERI HQLMRDKWGF PDPPDFTMQD RFAAKYQGQR YSFGYPACPN LEDQAKLFRL IRPEEIGIKL TEGYMMEPEA SVTAIVFAHP EARYFNVL // ID F5LF75_9BACL Unreviewed; 630 AA. AC F5LF75; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 17. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HMPREF9413_3161 {ECO:0000313|EMBL:EGL18952.1}; OS Paenibacillus sp. HGF7. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=944559 {ECO:0000313|EMBL:EGL18952.1, ECO:0000313|Proteomes:UP000003445}; RN [1] {ECO:0000313|EMBL:EGL18952.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HGF7 {ECO:0000313|EMBL:EGL18952.1}; 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: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGL18952.1}. 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; AFDH01000033; EGL18952.1; -; Genomic_DNA. DR RefSeq; WP_009672606.1; NZ_AFDH01000033.1. DR EnsemblBacteria; EGL18952; EGL18952; HMPREF9413_3161. DR Proteomes; UP000003445; Unassembled WGS sequence. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003445}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EGL18952.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EGL18952.1}. SQ SEQUENCE 630 AA; 69403 MW; 7AB607BBCA7F0928 CRC64; MKPELRQVLA QKILIGDGAM GTYLYQQGFP VGISYEELNL IQSEVVADVH RRYYEAGARL IETNTFSANR EKLSKYGLEQ EVEAINRAGV ELARSSVGED AYVVGAIGPI RAGMRKNVRT ADVEDALREQ ILVLLDTQVD GLLLETFYDL EEMLIALRLI RQLSSIPVIC QFATEGINTT HDGISLQDAF LRLKEEGADV IGFNCRTGPN GILRSLQGVA QLSDIPFSVF PNAGIPDYVD GRYSYAATPE YFAESALRFA DLGARIIGGC CGTTPEHIAA MVKALQGYEP NRSEVYAAES VSAAERAVVT EAAPQTSVRE ADVEPTLVDL VKQRHTVIVE LDPPRDLDIG KFMEGTKALQ DVHVDAITMA DNSLAVTRMS NLALGMLVKE QHGARPLIHI ACRDRNSIGT QSHLMGLHAL GIDHVLAVTG DPARFGDLPG ASSVYDMTSF EMIRMIKQLN EGIAFSGKPL KKKANFIVGA AFNPNVKYLD KAVQRLERKI ESGADYIMTQ PVYDPKLIER MHEATKHLDV PVFIGIMPLA SGRNAEYLHN EVPGIQLSDE VRARMTGLEG EAGRKEGVAI AKELLDAAMP LFNGIYFMTP FLFYDMSVQL TQYVWQKAER RELLLSPLLK // ID F5LK27_9BACL Unreviewed; 1147 AA. AC F5LK27; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EGL17275.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGL17275.1}; GN Name=metH {ECO:0000313|EMBL:EGL17275.1}; GN ORFNames=HMPREF9413_3072 {ECO:0000313|EMBL:EGL17275.1}; OS Paenibacillus sp. HGF7. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=944559 {ECO:0000313|EMBL:EGL17275.1, ECO:0000313|Proteomes:UP000003445}; RN [1] {ECO:0000313|EMBL:EGL17275.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HGF7 {ECO:0000313|EMBL:EGL17275.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGL17275.1}. 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; AFDH01000074; EGL17275.1; -; Genomic_DNA. DR RefSeq; WP_009674370.1; NZ_AFDH01000074.1. DR EnsemblBacteria; EGL17275; EGL17275; HMPREF9413_3072. DR Proteomes; UP000003445; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000003445}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGL17275.1}; KW Transferase {ECO:0000313|EMBL:EGL17275.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 226 226 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 721 721 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1147 AA; 126894 MW; 63E407DFF81139CC CRC64; MKPSLKEQLQ KKILILDGAM GTMIQQEDLS AEDFGGEELD GCNEMLVLTR PDVIQRIHEK YFEAGSDIVE TNTFGATSVV LAEYDIPEKA REINLVAAKL AVEAARKYST PEWPRYVAGA LGPTTKTLSV TGGVTFEDLE ESYYEQTIAL IESGVDAILL ETSQDTLNVK AGGIAIQRAF KTTGIELPIM ISGTIEPMGT TLAGQNIESF YISLEHLNPI SVGLNCATGP EFMRDHIRTL SGLAGTYISC YPNAGLPDEN GHYHESPESL AKKMAAFAEQ GWLNIAGGCC GTTPAHIRAL AETLSAYKPR TELGTHPSAV SGIETVYIEP ENRPYMVGER TNVLGSRKFK RLIAEGKYEE ASEIARAQVK GGAHVIDVCL QDPDRDETED MIKFLELVVK KIKVPLMIDS TDTRVIELGL KHSQGKAIIN SINLEDGEEK FEKVLPLIHR YGAAAVVGTI DERGQAITRE DKLEVAQRSH DLLVHKYGMN AEDIIFDPLV FPVGTGDQQY IGSAKETIEG IRLIKEAMPA TKTILGLSNV SFGLPEAGRE VLNAVYLYHC TKAGLDYAIV NTEKLERYAS IPEEERTLAE KLIYETNDET LAEFVAHFRV KKVEKKEKIS TLTLEERLAS YVVEGTKEGL LPDLEQALQK YSPLEVINGP LMEGMAEVGR LFNNNELIVA EVLQSAEVMK ASVAYLEQFM EKNESAVKGK IILATVKGDV HDIGKNLVEI ILSNNGYQIV NLGIKVPPEQ LIEAFRKEKP DAIGLSGLLV KSAQQMIITA QDLRNAGIDV PIMVGGAALT RKFTKTRISP EYDGLVLYAK DAMDGLDIAN KLSDPVQRER LIQELRESKD SDVMEAGRKE GTEMPVLTRV FSSTVDRTLP VAVPPDLDRH VLRDYPIGHL MPYVNMQMLL GHHLGLKGKV DKLIAEQDPK AMQLKDTVDT ILYEAQKNGI IRTQGMYRFF PAQGDGNDVV VYDPADTSKV LKRFTFPRQG TEPFLCLADY LKPVDSGVMD YIGFLVVTAG QGVSELAREW REQGDYLRSH ALQSTALEVA EAFAERVHHI MRDVWGIPDF AEMTMQERFG AKYTGQRFSF GYPACPNLED QEPLFELMKP EDIGIELTEG CMMEPEASVS AIVFAHPQAR YFNVDKV // ID F5N7Y4_SHIFL Unreviewed; 1223 AA. AC F5N7Y4; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGK17679.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGK17679.1}; GN Name=metH {ECO:0000313|EMBL:EGK17679.1}; GN ORFNames=SFVA6_4238 {ECO:0000313|EMBL:EGK17679.1}; OS Shigella flexneri VA-6. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=766145 {ECO:0000313|EMBL:EGK17679.1, ECO:0000313|Proteomes:UP000004258}; RN [1] {ECO:0000313|EMBL:EGK17679.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=VA-6 {ECO:0000313|EMBL:EGK17679.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AFGW01000060; EGK17679.1; -; Genomic_DNA. DR EnsemblBacteria; EGK17679; EGK17679; SFVA6_4238. DR Proteomes; UP000004258; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000004258}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGK17679.1}; KW Transferase {ECO:0000313|EMBL:EGK17679.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 243 243 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 755 755 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1223 AA; 135641 MW; B3579516F747DFA2 CRC64; MEQLRAQLNE RILVLDGGMG TMIQSYRLNE ADFRGERFAD WPCDLKGNND LLVLSKPEVI AAIHNAYFEA GADIIETNTF NSTTIAMVDY QMESLSAEIN FAAAKLARAR ADEWTARTPE KPRYVAGVLG PTNRTASISS DVNDPAFRNI TFDQLVAAYR ESTKALVEGG ADLILIETVF DTLNAKAAVF AVKTEFEALG VELPIMISGT ITDASGRTLS GQTTEAFYNS LRHAEALTFG LNCALGPDEL RQYVQELSRI AECYVTAHPN AGLPNAFGEY DLDADTMAKQ IREWAQAGFL NIVGGCCGTM PQHIAAMSRA VEGLAPRKLP EIPVACRLSG LEPLNIGDDS LFVNVGERTN VTGSAKFKRL IKEEKYSEAL DVARQQVENG AQIIDINMDE GMLDAEAAMV RFLNLIAGEP DIARVPIMID SSKWDVIEKG LKCIQGKGIV NSISMKEGVD AFIHHAKLLR RYGAAVVVMA FDEQGQADTR ARKIEICRRA YKILTEEVGF PPEDIIFDPN IFAVATGIEE HNNYAQDFIG ACEDIKRELP HALISGGVSN VSFSFRGNDP VREAIHAVFL YYAIRNGMDM GIVNAGQLAI YDDLPAELRD AVEDVILNRR DDGTERLLEL AEKYRGSKAD DTANAQQAEW RSWDVNKRLE YSLVKGITEF IEQDTEEARQ QATRPIEVIE GPLMDGMNVV GDLFGEGKMF LPQVVKSARV MKQAVAYLEP FIEASKEQGK TNGKMVIATV KGDVHDIGKN IVGVVLQCNN YEIVDLGVMV PAEKILRIAK EVNADLIGLS GLITPSLDEM VNVAKEMERQ GFTIPLLIGG ATTSKAHTAV KIEQNYSGPT VYVQNASRTV GVVAALLSDT QRDDFVARTC KEYETVRIQH GRKKPRTPPV TLEAARDNDF AFDWQAYTPP VAHRLGVQEV EASIETLRNY IDWTPFFMTW SLAGKYPRIL EDEVVGVEAQ RLFKDANDML DKLSAEKTLN PRGVVGLFPA NRVGDDIEIY RDETRTHVIN VSHHLRQQTE KTGFANYCLA DFVAPKLSGK ADYIGAFAVT GGLEEDALAD AFEAQHDDYN KIMVKALADR LAEAFAEYLH ERVRKVYWGY APNENLSNEE LIRENYQGIR PAPGYPACPE HTEKATIWEL LEVEKHTGMK LTESFAMWPG ASVSGWYFSH PDSKYYAVAQ IQRDQVEDYA RRKGMSVSDV ERWLAPNLGY DAD // ID F5P0T8_SHIFL Unreviewed; 1227 AA. AC F5P0T8; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGK33815.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGK33815.1}; GN Name=metH {ECO:0000313|EMBL:EGK33815.1}; GN ORFNames=SFK227_4061 {ECO:0000313|EMBL:EGK33815.1}; OS Shigella flexneri K-227. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=766147 {ECO:0000313|EMBL:EGK33815.1, ECO:0000313|Proteomes:UP000004520}; RN [1] {ECO:0000313|EMBL:EGK33815.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=K-227 {ECO:0000313|EMBL:EGK33815.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AFGY01000052; EGK33815.1; -; Genomic_DNA. DR RefSeq; WP_000096039.1; NZ_AFGY01000052.1. DR EnsemblBacteria; EGK33815; EGK33815; SFK227_4061. DR Proteomes; UP000004520; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000004520}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGK33815.1}; KW Transferase {ECO:0000313|EMBL:EGK33815.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136024 MW; CD2FF21C04EB90B1 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKADDTANAQ QAEWRSWDVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RIAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPMVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID F5RGW6_METUF Unreviewed; 1227 AA. AC F5RGW6; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGK70170.1}; GN ORFNames=METUNv1_03558 {ECO:0000313|EMBL:EGK70170.1}; OS Methyloversatilis universalis (strain ATCC BAA-1314 / JCM 13912 / OS FAM5). OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Rhodocyclaceae; Methyloversatilis. OX NCBI_TaxID=1000565 {ECO:0000313|EMBL:EGK70170.1}; RN [1] {ECO:0000313|EMBL:EGK70170.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FAM5 {ECO:0000313|EMBL:EGK70170.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGK70170.1}. 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; AFHG01000058; EGK70170.1; -; Genomic_DNA. DR RefSeq; WP_008064051.1; NZ_AFHG01000058.1. DR EnsemblBacteria; EGK70170; EGK70170; METUNv1_03558. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 249 249 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 762 762 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 134165 MW; 5FF93C3FB014C489 CRC64; MIRPDCTEQL KALMARRILI LDGAMGTMVQ KHRLVEADYR GTRFADHPKD LKGNNDLLLL TRPDVIRGIH AAYLEAGADI IETNTFNATK ISQAEYGLEA IVHELNVEGA RIAREACDEY TAKNPDKPRF VAGVLGPTSR TCSLSPDVND PGFRNVTFDQ LVEDYVAAAR GLTEGGADLL LVETIFDTLN AKAALFALEQ FFDEAGRRWP IMISGTITDA SGRTLSGQTA EAFWNSLRHS NPISFGFNCA LGPKDMRQHV EELAHLADTH VSAHPNAGLP NAFGEYDETP ADMVNHLREW AQSGFLNIVG GCCGTTPDHI AAFAKAMDGM PPRAVPEIER KLRLSGLEAF NVGADALFVN VGERTNVTGS RAFAKMILES RFDDALAVAR QQVENGAQVI DINMDEAMLD SVAAMERFLK LIASEPDISR VPIMLDSSKW SVIEAGLKCI QGKGVINSIS MKEGEAEFLR QATLARRYGA AVIVMAFDEK GQADTYQRKT EICQRAYTLL TEQVGFPPED IIFDPNIFAI ATGIAEHDNY AVDYIEAVGW IHRNLPYAKT SGGVSNVSFS FRGNDPVREA IHTVFLYHAI RNGLSMGIVN AGQLGVYEDI PQPLRDKVED VVLNRHPGAG DALVEFAITV KGQAKESTQD LAWREWPVDK RLEHALVKGI TEFVVEDTEE VRARLEAEGK PPLAVIEGPL MAGMNHVGDL FGAGKMFLPQ VVKSARVMKQ AVAHLQPYIE ASKKVGETKG RVIMATVKGD VHDIGKNIVG VVLGCNGYEV IDLGVMVACE RILQAARDHK ADIIGLSGLI TPSLEEMSHV ASEMTREGFD IPLLIGGATT SRAHTAIKIA PNYAHPVVYV PDASRAVGVA TSLLSKDQRA AYAEEVAADY VKIREQHAAK KGQKLVSLND ARDNAYCCGW GTEVIPEKPN TVGRQVILDQ DLAALVDYID WGPFFQTWEL SGPYPAILDD AVVGEEARKL LADAQAMLQQ IIAGKWLTAR AVYGLWPANS RGDDIEFYTD ETRLNTAMTW HNLRQQHERP AGKPHYCLSD FVAPRASGVA DWAGAFVVTA GIGIEAKLAE FEKTHDDYSS IMLKALADRL AEAFAEYLHA KVRREDWGYA RDEQLDNAAL IAEKYRGIRP APGYPACPDH TEKGDLFRLL DAEAAIGVSL TESYAMLPTA AVSGFYLAHP DAQYFAITKV GADQVADLAA RKGLPEPVMK RWLAPVI // ID F5RLH7_9FIRM Unreviewed; 818 AA. AC F5RLH7; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Vitamin B12-dependent methionine synthase {ECO:0000313|EMBL:EGK60100.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGK60100.1}; GN ORFNames=HMPREF9081_1113 {ECO:0000313|EMBL:EGK60100.1}; OS Centipeda periodontii DSM 2778. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Centipeda. OX NCBI_TaxID=888060 {ECO:0000313|EMBL:EGK60100.1}; RN [1] {ECO:0000313|EMBL:EGK60100.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 2778 {ECO:0000313|EMBL:EGK60100.1}; 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. {ECO:0000313|EMBL:EGK60100.1}. 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; AFHQ01000030; EGK60100.1; -; Genomic_DNA. DR RefSeq; WP_006306045.1; NZ_GL892076.1. DR EnsemblBacteria; EGK60100; EGK60100; HMPREF9081_1113. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGK60100.1}; KW Transferase {ECO:0000313|EMBL:EGK60100.1}. SQ SEQUENCE 818 AA; 87953 MW; 01470AE2F862DB00 CRC64; MPGRGKNLKT LNRRYEMSDI IILDGGMGTQ LQARGLAPGE RPELFGLDHP EVIEEIHRNY IAAGSRVIYS NTFGANGHKL EGTGKSVAEV IEENVRTARR AGENSGVSGV RVALDIGPIG ELVEPLGTLS FEDAYELFRE MVVAGAEAGA DLVIFETLTD LYEVKAAVLA AKEHTQLPIW VTMTFEQNGR TFLGAAVPSV AVTLDALGVA ALGVNCSLGP VELLPIVDAL MEWTDLPIIV KPNAGLPDPR TGAYEMTAED FGREMAEFAR RGAVIMGGCC GTTPDFIRAL SASVAAGAAE RPVRKKRKGI ASPARVAEYG KLNVIGERIN PTGKKRLQQA LLEEDYGYIK KLAISQQEAG AQVLDINVGA QGVDEEKIIP YVVKAVQSVV DLPLQIDSAN PRVIEAALRV TNGRVIINSV SGERERMDAI FPLAKHYGAA VLGLAMDEKG LPETAAERVA IAERIVAEAE KYGLDREDII IDCLTLTVSA QQEQAMETLR AVREVHERLG LHCALGVSNI SFGLPARGHM TENFLIQAMH VGLDFPIINP NTKGVMDAVV SFRAVSGEDV DCAAYIERFA PEQAEMRRRK ELGITGDESA GAVQTVAAES ADAVDPLMDA IIRGLSDDAE RITRKLLTEM APMEIIQEKV IPALDIVGDR YEKEIIFLPQ LINAANAATA GLELIKVRLA EEGQGVSKGK IILATVEGDI HDIGKNIVKV VLENYGYQII DLGRDVPVTR VVEVAIEKKV GLIGLSALMT TTVTAMKRTI DALHEAGHPC ETVVGGAVLT EDYAKEIGAD YYAGDARSIV EIARRVLG // ID F5RLH8_9FIRM Unreviewed; 597 AA. AC F5RLH8; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 18. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HMPREF9081_1114 {ECO:0000313|EMBL:EGK60101.1}; OS Centipeda periodontii DSM 2778. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Centipeda. OX NCBI_TaxID=888060 {ECO:0000313|EMBL:EGK60101.1}; RN [1] {ECO:0000313|EMBL:EGK60101.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 2778 {ECO:0000313|EMBL:EGK60101.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGK60101.1}. 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; AFHQ01000030; EGK60101.1; -; Genomic_DNA. DR RefSeq; WP_006306046.1; NZ_GL892076.1. DR EnsemblBacteria; EGK60101; EGK60101; HMPREF9081_1114. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 597 AA; 64649 MW; 99D19D9935CDB44A CRC64; MTQERIDIRE HIRKEPLVFD GGMGTYYAQR THTRGKGVEL ANIETPLVVE EIHTEYLRAG AHAIKTNTFA ANRIVYQGDT PLVEGILRTG WTLAARAAEP FGAYVFADIG PVTGLPPADI VEEYRFLSDI FLAAGARHFI FETNSSAEGL VETAAHIKQI CPEAFVLTSF SAFPGGYTRD GFFIEELVRV VTESGYIDAV GFNCVSGVQS MKELVHLLGA CSLPLSLMPN AGHPIVIDGR TFYESAPKYF GEGLAALVRD GVSIVGGCCG TTPEHIRALC AALADRGHAS EDAGAWQTRT ELVPSRSPFF DALKAGEMPI AVELDPPDTG NADKFMAGAR ELQAAGVSAI TIADNPIARA RMDAAMLAGR VHRSLGLEPI PHMTCRDRNL NAIKSILLGL SAEGVHNMIA ITGDPIPTAE RDEVKSVYQF NSRKLSAFIT NLGERGDVVP FHIFGALNVN SQHFPSQLGL AKKKMEAGMT GFFTQPVLSA RAKENMRTAR DTLPGALILG GIMPVVSERN ARFMESEISG IHVEERIINA YHGLDRAEAE ELAVKLSLEI AKDIEPYIDG YYIITPFART ALVARIVAGI KARRSGQ // ID F5RP14_9FIRM Unreviewed; 308 AA. AC F5RP14; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 11. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGK58404.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EGK58404.1}; GN Name=mmuM {ECO:0000313|EMBL:EGK58404.1}; GN ORFNames=HMPREF9081_2000 {ECO:0000313|EMBL:EGK58404.1}; OS Centipeda periodontii DSM 2778. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Centipeda. OX NCBI_TaxID=888060 {ECO:0000313|EMBL:EGK58404.1}; RN [1] {ECO:0000313|EMBL:EGK58404.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 2778 {ECO:0000313|EMBL:EGK58404.1}; 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. {ECO:0000313|EMBL:EGK58404.1}. 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; AFHQ01000047; EGK58404.1; -; Genomic_DNA. DR RefSeq; WP_006307064.1; NZ_GL892076.1. DR EnsemblBacteria; EGK58404; EGK58404; HMPREF9081_2000. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGK58404.1}; KW Transferase {ECO:0000313|EMBL:EGK58404.1}. SQ SEQUENCE 308 AA; 33722 MW; 8DE094CF4D67384C CRC64; MNVIEERLAV QDVIVLDGAF ATEIEARGFS VNDALWSAKA LFERPDLVRE VHLDYLRAGA DVVTSASYQA TVEGFMKRGF SKEEAAALIQ KSIQLAQEAC DLYLAEREEN GRVPFVAASV GPYGAYLADG SEYRGDYGID EDALVAFHAE RLALLASAQP DLLACETLPC LVEARAIVRV LREKKIRIPA WFSFSCRDAA HISDGMEIAV CARWLDTVPE AAAIGLNCTA PQYVESLIGE IRRETTKPIV VYPNSGETYD ASDKSWHGAA EDFGTIARRW RTAGARLIGG CCRTTPREIA DIAAWAKN // ID F5RV85_9ENTR Unreviewed; 351 AA. AC F5RV85; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 01-OCT-2014, entry version 10. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGK62000.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EGK62000.1}; GN Name=mmuM {ECO:0000313|EMBL:EGK62000.1}; GN ORFNames=HMPREF9086_1542 {ECO:0000313|EMBL:EGK62000.1}; OS Enterobacter hormaechei ATCC 49162. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex. OX NCBI_TaxID=888063 {ECO:0000313|EMBL:EGK62000.1}; RN [1] {ECO:0000313|EMBL:EGK62000.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 49162 {ECO:0000313|EMBL:EGK62000.1}; 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. {ECO:0000313|EMBL:EGK62000.1}. 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; AFHR01000024; EGK62000.1; -; Genomic_DNA. DR EnsemblBacteria; EGK62000; EGK62000; HMPREF9086_1542. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGK62000.1}; KW Transferase {ECO:0000313|EMBL:EGK62000.1}. SQ SEQUENCE 351 AA; 38347 MW; 21A6FED0B11439D8 CRC64; MSQNNPLTAL LENQPFIVLD GAMATELEAR GCNLADSLWS AKVLMENPEL IRDVHLDYYR AGAQVAITAS YQATPAGFAA RGLDEAQSRA LIGKSVELAR KAREAYLAEN AQAGTLLVAG SVGPYGAYLA DGSEYRGDYV RRAEEFTEFH RPRVEALLDA GADLLACETL PSFPEIKALA ALLTAYPRAR AWFSFTLRDS EHLSDGTPLR DVVSVLENYP QVVALGINCI ALENTTAALT HLHSLTSLPL VVYPNSGEHY DAVSKTWHHH GEACETLAGY LPQWLEAGAK LIGGCCRTTP KDIAELKRSA TRRNNRTKPT ILSRFFSKNE SSLAILFYSF IKLPAPEILP P // ID F5RX36_9ENTR Unreviewed; 1227 AA. AC F5RX36; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGK61052.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGK61052.1}; GN Name=metH {ECO:0000313|EMBL:EGK61052.1}; GN ORFNames=HMPREF9086_2194 {ECO:0000313|EMBL:EGK61052.1}; OS Enterobacter hormaechei ATCC 49162. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex. OX NCBI_TaxID=888063 {ECO:0000313|EMBL:EGK61052.1}; RN [1] {ECO:0000313|EMBL:EGK61052.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 49162 {ECO:0000313|EMBL:EGK61052.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGK61052.1}. 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; AFHR01000038; EGK61052.1; -; Genomic_DNA. DR RefSeq; WP_006810508.1; NZ_GL892086.1. DR EnsemblBacteria; EGK61052; EGK61052; HMPREF9086_2194. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGK61052.1}; KW Transferase {ECO:0000313|EMBL:EGK61052.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135840 MW; 2CC17A604808F5E4 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQGY RLSEDDFRGE RFADWPCDLK GNNDLLVLSK PSVIRDIHNA YFEAGADIVE TNTFNSTTIA MADYQMESLS AEINFEAARL ARACADEWTA RTPDKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGSDLILI ETVFDTLNAK AAIYAVKEEF EALGIDLPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LSFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAAQIREWAE SGFLNIVGGC CGTTPEHIAA MSRAVAGLPP RKLPELPVAC RLSGLEPLTI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VESGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDTFIHHA KRVRRYGAAV VVMAFDEVGQ ADTRERKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDATER MLDLAEKYRG SKSDESANVQ QAEWRAWDVK KRLEYSLVKG ITEFIEQDTE EARQQAARPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EKGSSNGRMV IATVKGDVHD IGKNIVGVVL QCNNYEIIDL GVMVPADKIL KTAREVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVSAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVSLQAAR DNDLAFDWSS YTPPVAHRLG VQDVTASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG EEAKRLFKDA NDMLDRLSAE KALNPRGVVG LFPANRVGDD VEIYRDETRT HVLAVSHHLR QQTEKVGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFDAQH DDYNKIMVKA IADRLAEAFA EYLHERVRKV HWGYAANENL SNEELIRENY QGIRPAPGYP ACPEHTEKGT IWKLLDVEAH TGMKLTESFA MWPGASVSGW YFSHPDSKYF AVAQLQRDQI EDYALRKGMS VSEVERWLAP NLGYDAD // ID F5SG92_9BACL Unreviewed; 629 AA. AC F5SG92; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 07-JAN-2015, entry version 17. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HMPREF9374_2133 {ECO:0000313|EMBL:EGK11064.1}; OS Desmospora sp. 8437. OC Bacteria; Firmicutes; Bacilli; Bacillales; Thermoactinomycetaceae; OC Desmospora. OX NCBI_TaxID=997346 {ECO:0000313|EMBL:EGK11064.1}; RN [1] {ECO:0000313|EMBL:EGK11064.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=8437 {ECO:0000313|EMBL:EGK11064.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGK11064.1}. 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; AFHT01000087; EGK11064.1; -; Genomic_DNA. DR RefSeq; WP_009710199.1; NZ_GL892032.1. DR EnsemblBacteria; EGK11064; EGK11064; HMPREF9374_2133. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EGK11064.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EGK11064.1}. SQ SEQUENCE 629 AA; 69633 MW; 9BAC3ADBFA11ABC3 CRC64; MQCDRGGEEM THHPDLRAAL TDSLLVGDGA MSTYLYQQGI PVGMTAEELS LSRPDWIEEV HRQYVEAGAQ LIETNTYGAD RERLSRYGLE GKVSRINRES VAIARRAAEG KAYVAGAVGS INAGRVPRWS PAEYRDLYEE QATALLYGGV DGIILETFFD LEELLLALEV IRPLTDRPIL AQLTMLEVGR TRDGHTLTKA FVELQKQGVD GVGLNCRVGP LQMEQALEKT AVPDGLILTA FPNAGRLGRR DGEYQYESTP EYFGNRAKAL REQGVRLIGG CCGTTPDHIR KVAEALQGLP PVPRVNPELP EEEVVSLPLQ VRSRPTVVEQ VRKETTVIVE FDPPRDLEIH DFLQGAEALH HAGADAITLA DNSMATPRMS NMALASILKS RTKVEPLVHI TCRDRNLLGQ QSHLMGLHAL DIDQILVVTG DPTRIGDLPG ASSIYDVNSF DLIRMVKQLN EGISFSGKPL RQRGRFVVGA AFNPHVSRME AAIRRLEKKV EAGADFIMTQ PVYDVETLKL VHEATRHIPI PIFIGVMPLT GHRNALFLHH ELPGVKIPAT VMERMRDLKG PEGRETGVGL AGELLDEAVS LFNGIYLITP FHYWEMTAEL TRRIRKRGKI RPIAAVHRS // ID F5SG93_9BACL Unreviewed; 1165 AA. AC F5SG93; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 01-APR-2015, entry version 21. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|EMBL:EGK11065.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGK11065.1}; GN Name=metH {ECO:0000313|EMBL:EGK11065.1}; GN ORFNames=HMPREF9374_2134 {ECO:0000313|EMBL:EGK11065.1}; OS Desmospora sp. 8437. OC Bacteria; Firmicutes; Bacilli; Bacillales; Thermoactinomycetaceae; OC Desmospora. OX NCBI_TaxID=997346 {ECO:0000313|EMBL:EGK11065.1}; RN [1] {ECO:0000313|EMBL:EGK11065.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=8437 {ECO:0000313|EMBL:EGK11065.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGK11065.1}. 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; AFHT01000087; EGK11065.1; -; Genomic_DNA. DR RefSeq; WP_009710200.1; NZ_GL892032.1. DR EnsemblBacteria; EGK11065; EGK11065; HMPREF9374_2134. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGK11065.1}; KW Transferase {ECO:0000313|EMBL:EGK11065.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 238 238 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 301 301 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 302 302 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 737 737 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1165 AA; 129409 MW; 525DA9A40E304583 CRC64; MERGGDGMSR RMEKKPVQQR LEEKILVLDG AMGTQLQGAA LTAEDFGGEE VDGCNEYLNI TRPDLIRAIH EEYLEAGADV IETNTFGATR VVLAEYGLEE RAEEINQRAA ELAVEAATGY TTPEHPRYVA GALGPTTKTL SVTGGVTFDQ LVDSYREQAR ALIRGGVDLL LLETSQDTLN VKAAGIGIRQ AFAELGREVP LMISGTIEPM GTMLAGQNVE AFYLSIQHLN PLTVGLNCAT GPEFMRDHLR TLSGLAHCGV SCYPNAGLPD EEGRYHETPR GLAQKLAGFA EQGWLNVAGG CCGTTPEHIR AIAEALADRE PRRSNPSRFP AVSGIEPLYP EADNRPILVG ERTNVIGSRK FRNMIREEQY EEAAGIARRQ VKGGAQVIDI CLADPDRDEL EDMERFLHFA VNKVKVPLMI DSTDPHVIER ALRYSQGKAI INSINLENGE DRFREVAPLI HRYGAAVVVG TIDEEGMAVQ AEQKLAVARR SYDLLVNHYR IPPEDIIFDP LIFPVGTGDR AYIGSAGETV EGIRRIKEAM PECSTILGVS NVSFGLPTAG REVLNAVCLY HCTRAGLDYA IVNTERLERY ASISEAERKQ AELFLFGTDA ENYDDVLAEF AAFYRDKKPT QKKEVQNLPL EERLARYVVE GSKDGLIPDL DKALQKYKAL EIINGPLMKG MDEVGRLFND NQLIVAEVLQ SAEVMKASVS FLEPHMEKTS QKSKGKILLA TVKGDVHDIG KNLVEIILSN NGFDVINLGI KVPPEQLIEA CRRENPDMVG LSGLLVKSAQ QMVLTAQDMK AANLDLPVLV GGAALTRKFT DQRIAPQYEG LVLYAKDAMN GLELANRLRD DEKRRQLVTE VQRNREKARS RRSGTSTREE IGGHVATKVR VSTVNREAPV YPPPDYRSHI LRNYPISHLE PYINKQMLLG KHLGLKGNVE QLLLEGDPRA TDLKRELDEM VAELREAGEL RADGIYQFFP AQSHGETIEI YDPEFPGEKV LETFTFPRQS KAPYLCLADF LRPKDSGVVD TVGFLTVTAG YGIRERAEAW KRSGDYLRSH MVQALALELA EAFAERLHHM MRDGWGFPDP PEMTMRERFS ARYQGIRVSF GYPACPDLED QAKLFRLIRP ERIGVKLTEG FMMEPEASVS AMVFSHPEAR YFNAV // ID F5SNQ4_9GAMM Unreviewed; 1272 AA. AC F5SNQ4; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 01-APR-2015, entry version 20. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGK14745.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGK14745.1}; GN Name=metH {ECO:0000313|EMBL:EGK14745.1}; GN ORFNames=HMPREF9373_0687 {ECO:0000313|EMBL:EGK14745.1}; OS Psychrobacter sp. 1501(2011). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Psychrobacter. OX NCBI_TaxID=1002339 {ECO:0000313|EMBL:EGK14745.1}; RN [1] {ECO:0000313|EMBL:EGK14745.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=1501 {ECO:0000313|EMBL:EGK14745.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGK14745.1}. 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; AFHU01000056; EGK14745.1; -; Genomic_DNA. DR RefSeq; WP_007394048.1; NZ_GL892048.1. DR EnsemblBacteria; EGK14745; EGK14745; HMPREF9373_0687. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGK14745.1}; KW Transferase {ECO:0000313|EMBL:EGK14745.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 352 352 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 353 353 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 804 804 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1272 AA; 140784 MW; 8CD41A0AA2048409 CRC64; MAHCSHPEHN TQKESSENTP KKGHNPDNFN LVPPANFPFK EQQLTARQRI VEQLDQRILM LDGAMGTQIQ TFKLQEADYR GERFADFGQD VQGNNDLLVL TQPQIIKSIH TDHLAAGADI IETNTFNATQ ISMSDYGMEH LVPEINREAA LLARAAADEF TAQNPDKPRF VAGVIGPTSR TCSLSPDVND PAYRNVTFDE LVDNYTEALF ALIEGGIDLV LIETIFDTLN AKAAIFAVTG VFDTIGFELP IMISGTITDA SGRTLSGQTA EAFYNSIRHA KPLSVGFNCA LGADALRPHI QTLSDIADTY VSAHPNAGLP NEFGEYDETP EETAALLNGF GKAGILNIVG GCCGTRPEHI KAISDVMKQY PPRQIPTIPP ACRLSGLEPF TITKDSLFVN VGERTNVTGS KKFLRLIKTG EFTEALDVAR DQVDGGAQIV DINMDEGMLD SKGAMIHFLN LVAGEPDISR VPLMIDSSKW DIIEEGLKRT QGKAVVNSIS LKEGYDEFVE RAKLCMRYGA AVIVMAFDED GQADTYERKI QICQRSYDVL VNDVGFPSED IIFDPNIFAV ATGIPEHNNY GADFINATQW ITDNLPNAMV SGGVSNVSFS FRGNPIREAI NAVFLYHAIK AGLTMGIVNP AMLEVYDEIP KEAREAIEDV MLNRNQGESG QDATERLMTI AEAYVAGGKK NDGTVDLSWR EQSVEKRIEH ALVKGITTYI DEDTEEARLK YPKPLHVIEG PLMDGMNVVG DLFGAGKMFL PQVVKSARVM KRAVAVLNPY IEAEKVEGEV KGKVVMATVK GDVHDIGKNI VGVVLGCNGY DVVDLGVMVP CDKILDTAIA EKADIIGLSG LITPSLDEMV YVAKQMQERG MDLPLMIGGA TTSKAHTAVK IEPNYQNDAV IYVSDASRSV GVVTKLLSKE HRVELIRETR EEYEKVRERL ANRKPKAAKL SYEESIEQGF QFDWETYTPP TPNELGQVVF DSYPIENLIP YIDWTPFFIS WGLVGKYPKI FDDEVVGEEA KDLFGNAKEL LQKFMDENLV TPKGVFKIMP AKRTDHDTVT VYDKPPSEGG QPTHVFEHLR QQSDKASGKP NYSLADFISP SDEHTDYLGG FTVSIEGAQE LSDAYKEAGD DYNAIMVQAL CDRLAEAFAE HLHELIRTKY WGYQPTEQLS NEELIKEKYV GIRPAPGYPA CPEHTEKGKL FDWLDTTNAI GTYLTESFAM WPASSVSGFY YSHPESVYFN VGKIDRDQLE DYAKRKDWDM KTAEKWLNPN LA // ID F5T2E6_9GAMM Unreviewed; 1232 AA. AC F5T2E6; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Methionine synthase I, cobalamin-binding domain containing protein {ECO:0000313|EMBL:EGL53444.1}; GN ORFNames=MAMP_01069 {ECO:0000313|EMBL:EGL53444.1}; OS Methylophaga aminisulfidivorans MP. OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Piscirickettsiaceae; Methylophaga. OX NCBI_TaxID=1026882 {ECO:0000313|EMBL:EGL53444.1}; RN [1] {ECO:0000313|EMBL:EGL53444.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MP {ECO:0000313|EMBL:EGL53444.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGL53444.1}. 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; AFIG01000003; EGL53444.1; -; Genomic_DNA. DR RefSeq; WP_007146694.1; NZ_AFIG01000003.1. DR EnsemblBacteria; EGL53444; EGL53444; MAMP_01069. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 246 246 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1232 AA; 136529 MW; 2F2580746B27B202 CRC64; MTVLQQIKSL LEQRILILDG GMGTLIQSYK LEEKDFRGAR FADHPCDVKG NNDLLSLTQP QIIRDIHRAY FEAGADIVET NTFNGTSIAM ADYQMEDLVY ELNKVSAELA KEVAAEFTAK NPDKPRFVTG VLGPTNRTAS ISPDVNNPGF RNVSFDELVE AYLEAIRGLV DGGADLLLVE TVFDTLNAKA ALFAIDQFCE QNNVHIPVMI SGTITDASGR TLSGQTAEAF WNSLAHIQPL SIGLNCALGA EQLRQYVEEL SNVVTCHVSA HPNAGLPNEF GEYDESPEVM AAQIKEWAQS GFLNIVGGCC GTAPAHIKAI ADAVAGIKPR QPKANLHHCR LSGLEPLNIT PDSLFVNVGE RTNVTGSARF AKLIKEGDYD TALEVARQQV ENGAQIIDIN MDEGMLDSKE AMVTFLNLLA AEPDISRVPV MIDSSKWEVI EAGLKCIQGK GIVNSISLKE GEEKFIEQAK LVRRYGAAVI VMAFDEVGQA DTRQRKLEIC RRSYEVLTEK VHFPPEDIIF DPNIFAVATG IEEHNNYAVD FIEAVHDIKQ SLPHALISGG VSNVSFSFRG NNPVREAIHA VFLYHAIKAG MDMGIVNAGQ LAIYDDLPEE LREAVEDVVQ NRRDDSTDRL LELAEKYKGE GGSVAKQEDL AWRELPVIKR LEHALVKGIA DYVEDDTEEA RQQYAKPLEV IEGPLMDGMN VVGDLFGEGK MFLPQVVKSA RVMKKAVAYL MPFIEAAKEE GDTSKNNGKI LMATVKGDVH DIGKNIVGVV LQCNNFEVID LGVMVPAQKI LDTAREENVD IIGLSGLITP SLDEMVHVAK EMERLGMETP LMIGGATTSL IHTAVKIEPN YHGCSIYVKD ASRAVGVAQR LVTKDTRDAF IADLKKDYEE KRSRHKGRKS SRRQLSIAEA RANKTKIDWA AYQPTKPAKL GLEVFDDYPL AELVERIDWT PFFQSWELAG KFPRILTDEV VGEHATHLFE DAKKMLQQIV DEKWLTAKAV IGLFAANSIN DDDIEVYRDD NRDEVLMTLH SLRQQTERPP GRPNAALADF IAPKETGVND YIGAFAVTAG IGIDEHVARF EEDHDDYHSI MLKALADRLA EAFAERMHER VRKEFWGYAK QEQLDNEALI DEKYQGIRPA PGYPACPDHT EKGLLWDLID PVTHAGMTIT ESYAMLPTAA VSGFYFAHPE SRYFGLGKID QDQVEDYAQR KGWDKQTAER WLGPALSYDG DD // ID F5UL57_9CYAN Unreviewed; 1183 AA. AC F5UL57; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGK85553.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGK85553.1}; GN ORFNames=MicvaDRAFT_4859 {ECO:0000313|EMBL:EGK85553.1}; OS Microcoleus vaginatus FGP-2. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Microcoleus. OX NCBI_TaxID=756067 {ECO:0000313|EMBL:EGK85553.1}; RN [1] {ECO:0000313|EMBL:EGK85553.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FGP-2 {ECO:0000313|EMBL:EGK85553.1}; 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] {ECO:0000313|EMBL:EGK85553.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FGP-2 {ECO:0000313|EMBL:EGK85553.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGK85553.1}. 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; AFJC01000011; EGK85553.1; -; Genomic_DNA. DR RefSeq; WP_006634534.1; NZ_AFJC01000011.1. DR EnsemblBacteria; EGK85553; EGK85553; MicvaDRAFT_4859. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGK85553.1}; KW Transferase {ECO:0000313|EMBL:EGK85553.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 228 228 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 737 737 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1183 AA; 130860 MW; 88089AEF37DF9631 CRC64; MNSRFLDRLH HPSRPVIVFD GAMGTNLQVQ NLTAEDFGGK EYEGCNEYLV HTKPEAVANV HRGFLEAGAD VIETDTFGAA SIVLAEYDLA DKAYYLNKTA AELAKGIAAE FSTPEKPRFV AGSIGPGTKL PTLGHIDFDT LTAAFAEQAE GLYDGGVDLF IVETCQDVLQ IKSALNAIEE VFKKKGARIP LMVSVTMEAT GTMLVGSDIS AALAILQPYP IDILGLNCAT GPDRMAEHVK YLSEHSPFVV SCVPNAGLPE NIGGHAHYKL TPIELKMALM RFVEDLGVQV IGGCCGTRYD HIRELAEIGK TLKPKIREIT WEPSAASIYS AQPYEQENSF LIVGERLNAS GSKKCRDLLN AEDWDGLVAM AREQVREGAH ILDVNVDYVG RDGVRDMKEL VSRVVTNATL PLMLDSTEWE KMEAGLKVAG GKCLLNSTNY EDGEPRFYQV LELAKKYGAG IVIGTIDEDG MARTADQKFA IAQRAYNAAV AYGIPAEEIF FDTLALPIST GIEEDRKNGK ATIESIRRIR QELPGCHVIL GVSNISFGLN PAARQVLNSM FLHEAMQAGM DSAIVSANKI LPLAKIDPKH QEICRKLIYD EREFDGDICV YDPLGDLTTV FAGKTTKRDR TEDASLPVEE RLKQHIIDGE RIGLDIQLAK ALESYPPLHI INTFLLDGMK VVGELFGSGQ MQLPFVLQSA ETMKAAVAYL EPHMEKSESG DNAKGTFIIA TVKGDVHDIG KNLVDIILSN NGYRVINLGI KQSVDNIIEA YEKHKADCIA MSGLLVKSTA FMKENLEVFN QKGITVPVIL GGAALTPKFV HEDCQNTYKG KVVYGKDAFS DLHFMDKLMP AKSAGKWEDL QGFLDEREDD NGAVKEAKAA PETSVEDAKK ADTPVVIDTR RSEAVAGDID RPTPPFWGTK LLQGEDIPFE EIFWHLDLQA LVAGQWQFRK PKDQSREEYD AFLAEKVYPI LEEWKHKVIA EKLLYPQAIY GYFPCQAEGN SLYLYDPEIM AGGQDVSTPA ATLTFPRQKS GRRLCIADFF APKESGKIDV FPMQVATVGE IATEYAQKLF ANNQYSDYLY FHGLAVQTAE AVAEWTHARI RRELGFGSEE PDNIRDMLAQ RYRGSRYSFG YPACPNMADQ YKQLELLKCD RINLYMDESE QLYPEQSTTA IITYHPAAKY FSA // ID F5VDM2_9LACO Unreviewed; 307 AA. AC F5VDM2; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGL98940.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EGL98940.1}; GN ORFNames=NIAS840_00656 {ECO:0000313|EMBL:EGL98940.1}; OS Lactobacillus salivarius NIAS840. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1029822 {ECO:0000313|EMBL:EGL98940.1}; RN [1] {ECO:0000313|EMBL:EGL98940.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NIAS840 {ECO:0000313|EMBL:EGL98940.1}; RX PubMed=21914873; DOI=10.1128/JB.05688-11; RA Ham J.S., Kim H.W., Seol K.H., Jang A., Jeong S.G., Oh M.H., Kim D.H., RA Kang D.K., Kim G.B., Cha C.J.; RT "Genome Sequence of Lactobacillus salivarius NIAS840, Isolated from RT Chicken Intestine."; RL J. Bacteriol. 193:5551-5552(2011). RN [2] {ECO:0000313|EMBL:EGL98940.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NIAS840 {ECO:0000313|EMBL:EGL98940.1}; RA Ham J.-S., Kim H.-W., Seol K.-H., Jang A., Jeong S.-G., Oh M.-H., RA Kim D.-H., Jo C., Kim B.-B., Cha C.-J.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGL98940.1}. 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; AFMN01000001; EGL98940.1; -; Genomic_DNA. DR RefSeq; WP_003705587.1; NZ_AFMN01000001.1. DR EnsemblBacteria; EGL98940; EGL98940; NIAS840_00656. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EGL98940.1}; KW Transferase {ECO:0000313|EMBL:EGL98940.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 223 223 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 307 AA; 34518 MW; BFFC712B1C00509B CRC64; MDFTEFLTNH TVVLDGAMST PLERLGADTN NDLWTAKALI DNEELVYEVH KMYFEAGADL IITDTYQANI QAFEKVGYSE KEARNLIKKA VKIAQKARDD YENRTGKHNY IAGTIGPYGA YLANGSEYRG DYELSTKEYQ QFHLPRIEEL VTTGVDILAI ETQPKLDEVL AILELLKKKY PQQKVYVSYT LSDDDTISDG TSLPRAIHAL EDYSQVIAVG INCVKLELVE PALKNMKEIT DKHLIVYPNS SAVYDPKSKT WSQPKTSATF EELIPNWYEA GARIIGGCCT TGPKEIKAVA DFIKRNK // ID F5VNN9_CROSK Unreviewed; 1227 AA. AC F5VNN9; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EGL71997.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGL71997.1}; GN Name=metH {ECO:0000313|EMBL:EGL71997.1}; GN ORFNames=CSE899_14402 {ECO:0000313|EMBL:EGL71997.1}; OS Cronobacter sakazakii E899. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Cronobacter. OX NCBI_TaxID=930780 {ECO:0000313|EMBL:EGL71997.1}; RN [1] {ECO:0000313|EMBL:EGL71997.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=E899 {ECO:0000313|EMBL:EGL71997.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGL71997.1}. 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; AFMO01000250; EGL71997.1; -; Genomic_DNA. DR RefSeq; WP_004387514.1; NZ_AFMO01000250.1. DR EnsemblBacteria; EGL71997; EGL71997; CSE899_14402. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGL71997.1}; KW Transferase {ECO:0000313|EMBL:EGL71997.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136011 MW; 79C76015F27FE4ED CRC64; MSSKSEQLHR QLAERIMVLD GGMGTMIQSY RLDEEDFRGE RFADWPCDLK GNNDLLVLTK PDIIAAIHYA YFEAGADIIE TNTFNSTTIA MADYQMELLS AEINYEAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFEQLV EAYRESTRAL IEGGADLILI ETVFDTLNAK AAIFAVKAEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHADA LTFGLNCALG PDELRQYVAE LSRIAECYVT AHPNAGLPNA FGEYDLDADV MAAQIREWAE SGFLNIVGGC CGTTPEHIAA MSRAVEGLPP RKLPDIPVAC RLAGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVEAFVHHA KLVRRYGAAV VVMAFDEVGQ ADTRERKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIDEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPT ELRDAVEDVI LNRRADGTER LLALAEKYRG SKADNAADAQ QAEWRTWDVK KRLEYSLVKG ITEFIEQDTE EARQQAARPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPYIQASK EVGKSNGKIV LATVKGDVHD IGKNIVGVVL QCNNYEIIDL GVMVPTDKIL KTAREVNADI IGLSGLITPS LDEMVNVAKE MERQGFTLPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVSAL LSDTLRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLAAAR ENDLAFDWES YTPPAAHRLG VEEVTASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG EEAQRLFKDA NEMLDKLSAE KSLMPRGVVG LFPANRVGDD IEIYRDETRT HVLSVSHHLR QQTEKVGFAN YCLADFVAPK YSGKADYLGA FAVTGGLEED ALAEAFDAQH DDYNKIMVKA VADRLAEAFA EYLHERVRKV LWGYAPYENL SNEELIRENY QGIRPAPGYP ACPEHTEKSV IWDLLDVENR IGMKLTESYA MWPGASVSGW YFSHPESKYF AVAQIQRDQV EDYAQRKGMS VSEVERWLAA NLGYDAD // ID F5X1E7_STRG1 Unreviewed; 315 AA. AC F5X1E7; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:BAK28108.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:BAK28108.1}; GN Name=mmuM {ECO:0000313|EMBL:BAK28108.1}; GN OrderedLocusNames=SGGB_1246 {ECO:0000313|EMBL:BAK28108.1}; OS Streptococcus gallolyticus (strain ATCC 43143 / F-1867). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=981539 {ECO:0000313|Proteomes:UP000007945}; RN [1] {ECO:0000313|Proteomes:UP000007945} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43143 / F-1867 {ECO:0000313|Proteomes:UP000007945}; 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 ----------------------------------------------------------------------- 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; BAK28108.1; -; Genomic_DNA. DR RefSeq; WP_012962044.1; NC_017576.1. DR RefSeq; YP_006034067.1; NC_017576.1. DR EnsemblBacteria; BAK28108; BAK28108; SGGB_1246. DR GeneID; 12630447; -. DR KEGG; sgt:SGGB_1246; -. DR KO; K00547; -. DR BioCyc; SGAL981539:GLL2-1313-MONOMER; -. DR Proteomes; UP000007945; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007945}; KW Methyltransferase {ECO:0000313|EMBL:BAK28108.1}; KW Transferase {ECO:0000313|EMBL:BAK28108.1}. SQ SEQUENCE 315 AA; 34531 MW; 1A15D5B3F5741AD2 CRC64; MGTFKELLAS QDYVILDGAL GTELEKRGYD VSGKLWSAKY LLENPSVIQD LHDVYLRSGA DILTTSSYQA TVQGLKDFGL SEKEALDIIS LTVTLARQAR DNFWNGLSDE AKKKRPYPLI SGDIGPYAAY LADGSEYNGN YQLTQEEYQA FHRPRIQALL SAGSDFLGIE TIPNVAEAKA LLDLLATEFP QTEAYISFTA QDDKHISDGT PIEEVVALCE QSPQILAFGI NCSSPAVISG LLKRIRTVSP KPLVTYPNSG EIYDGATQTW KSIPDNSHTL LENSRAWHQL GAKIVGGCCR TSPEDIACLA QAFRE // ID F5X1K8_STRG1 Unreviewed; 618 AA. AC F5X1K8; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 25. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN Name=yitJ {ECO:0000313|EMBL:BAK28169.1}; GN OrderedLocusNames=SGGB_1309 {ECO:0000313|EMBL:BAK28169.1}; OS Streptococcus gallolyticus (strain ATCC 43143 / F-1867). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=981539 {ECO:0000313|Proteomes:UP000007945}; RN [1] {ECO:0000313|Proteomes:UP000007945} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43143 / F-1867 {ECO:0000313|Proteomes:UP000007945}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; BAK28169.1; -; Genomic_DNA. DR RefSeq; WP_012962089.1; NC_017576.1. DR RefSeq; YP_006034128.1; NC_017576.1. DR ProteinModelPortal; F5X1K8; -. DR EnsemblBacteria; BAK28169; BAK28169; SGGB_1309. DR GeneID; 12630510; -. DR KEGG; sgt:SGGB_1309; -. DR KO; K00547; -. DR BioCyc; SGAL981539:GLL2-1376-MONOMER; -. DR Proteomes; UP000007945; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007945}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:BAK28169.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862, KW ECO:0000313|EMBL:BAK28169.1}; KW Transferase {ECO:0000313|EMBL:BAK28169.1}. SQ SEQUENCE 618 AA; 68086 MW; DE3D69A66E5AA632 CRC64; MSRLLERLKT DILVADGAMG TLLYANGLDN CYEAYNLTHP DKISAIHHAY LEAGADIIQT NTYAAKRHRL KGYAYDDQVK EINQAGVRIA REAAGDDAFV LGTVGALRGL KQCDLTLDEI IEETLEQVGY LIETNQIDGL LFETYYDEEE IIEVLKAVRP ITDLPIITNI ALHEAGITEN GRPLVEILGK LVMLGADVVG LNCHLGPYHM IKSLKQVPLF AQSYLSVYPN ASLLSFVDDN GSGQYGFSQN ADYFGKSAEL LVAEGARLIG GCCGTTPDHI RAVKRAVKGL KPVERKFVTP MVEEAELIKA AKQSETLVDR VKREVTIIAE LDPPKTLDIA KFTEGVKALD KAGISAITLA DNSLAKTRIC NVSIAALLKN EISTPFLLHL SCRDHNMIGL QSRLLGMDVL GFNHVLAITG DPSKIGDFPG ATSVYDATSF KLLALIKQLN KGQGYSGASI KKETNFTAAA AFNPNVKNLS RCGRLIERKV AAGADYFITQ PVFNTEIIDE LADLTRDYEA PFFVGIMPIT SYNNAIFLHN EVPGIQLSDE FLAKLEAVKD DKETCQKLAL EESKQLIDRA LEHFNGIYLI TPFMRYDLTV ELIDYIHQKV ELKNQRIS // ID F5X781_STRPX Unreviewed; 618 AA. AC F5X781; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 24. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN Name=yitJ {ECO:0000313|EMBL:BAK30271.1}; GN OrderedLocusNames=SGPB_1218 {ECO:0000313|EMBL:BAK30271.1}; OS Streptococcus pasteurianus (strain ATCC 43144 / JCM 5346 / CDC OS 1723-81). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=981540 {ECO:0000313|Proteomes:UP000007946}; RN [1] {ECO:0000313|Proteomes:UP000007946} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43144 / JCM 5346 / CDC 1723-81 RC {ECO:0000313|Proteomes:UP000007946}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; BAK30271.1; -; Genomic_DNA. DR RefSeq; WP_013851978.1; NC_015600.1. DR RefSeq; YP_004559357.1; NC_015600.1. DR EnsemblBacteria; BAK30271; BAK30271; SGPB_1218. DR KEGG; stb:SGPB_1218; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR BioCyc; SPAS981540:GJYA-1285-MONOMER; -. DR Proteomes; UP000007946; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007946}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:BAK30271.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862, KW ECO:0000313|EMBL:BAK30271.1}; KW Transferase {ECO:0000313|EMBL:BAK30271.1}. SQ SEQUENCE 618 AA; 68011 MW; 1BE91CEA5078A880 CRC64; MSRLLERLKT DILVADGAMG TLLYANGLDN CYEAYNLTHP DKISAIHHAY LEAGADIIQT NTYAAKRHRL KGYAYDDQVK EINQAGVKIA REAAGDDAFV LGTVGALRGL KQCNLTLDEI IEETLEQVGY LIETNQIDGL LFETYYDEEE IIEVLKAVRP ITDLPIITNI ALHEAGITEN GRPLVEILGK LVMLGADVVG LNCHLGPYHM IKSLKQVPLF AQSYLSVYPN ASLLSFVDDN GSGQYGFSQN ADYFGKSAEL LVAEGARLIG GCCGTTPDHI RAVKRAVKGL KPVERKFVTP MVEEVELIKA AKQSETLVDR VKREVTIIAE LDPPKTLDIA KFTEGVKALD KAGISAITLA DNSLAKTRIC NVSIAALLKN EISTPFLLHL SCRDHNMIGL QSRLLGMDVL GFNHVLAITG DPSKIGDFPG ATSVYDATSF KLLALIKQLN KGQGYSGASI KKEANFTAAA AFNPNVKNLS RCGRLIERKV AAGADYFITQ PVFNTEIIDG LADLTRDYEA PFFVGIMPIT SYNNAIFLHN EVPGIQLSDE FLAKLEAVKD DKETCQKLAL EESKQLIDRA LEHFKGIYLI TPFMRYDLTI ELIDYIHQKV ELKNQRIS // ID F5XH04_MICPN Unreviewed; 1282 AA. AC F5XH04; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:BAK35636.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:BAK35636.1}; GN Name=metH {ECO:0000313|EMBL:BAK35636.1}; GN OrderedLocusNames=MLP_26220 {ECO:0000313|EMBL:BAK35636.1}; 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 {ECO:0000313|EMBL:BAK35636.1, ECO:0000313|Proteomes:UP000007947}; RN [1] {ECO:0000313|EMBL:BAK35636.1, ECO:0000313|Proteomes:UP000007947} 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 {ECO:0000313|Proteomes:UP000007947}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP012204; BAK35636.1; -; Genomic_DNA. DR RefSeq; WP_013863505.1; NC_015635.1. DR RefSeq; YP_004573039.1; NC_015635.1. DR EnsemblBacteria; BAK35636; BAK35636; MLP_26220. DR KEGG; mph:MLP_26220; -. DR KO; K00548; -. DR BioCyc; MPHO1032480:GHBY-2644-MONOMER; -. DR Proteomes; UP000007947; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007947}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAK35636.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007947}; KW Transferase {ECO:0000313|EMBL:BAK35636.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 265 265 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 328 328 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 329 329 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 783 783 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1282 AA; 141195 MW; 89A61F4F79C84596 CRC64; MSDLREEGAA APVDRPTFPA RPDATDELTA LMRRRVLLLD GSMGVYIQRK GLSEAEFRGE RFADWPQDLT GNNDLLSITQ PEVIRSIHDS YLEAGADIIE TNTFSAQRIS MADYGMEELS YELNLVSAQL ARAACDAYAT PGHPRFVAGA LGPTNRTASI SPDVNDPGAR NIDYQELVEA YLEQARGLVD GGSDLLLVET IFDTLNAKAA IFALETLFEE RGRRWPVFIS GTITDASGRT LSGQVTEAFW NSIRHARPLA VGFNCALGAA DMRPYVAELA RVADCFTFCY PNAGLPNAFG EYDETPEQMG AVVGAFAHDK LINVAGGCCG TTPEHIAELE RQVAGLAPRE PIEVAPALRL SGLEPVNITD QSLFVNVGER TNITGSARFR KLIKAGDYPT ALAVARQQVE VGAQVIDVNM DEGMIDGIAA MDRFTKLIAS EPDICRVPMM IDSSKWEVIE AGLRCVQGKP IVNSISMKEG VESFVEHARL CRKYGAAIVV MAFDEDGQAD NLERRKQICE RAYRILIDEV GFPAEDIIFD PNIFAVATGI EEHANYGVDF IEATRWIKQN LPGALVSGGV SNVSFSFRGN NPVREAIHSV FLYHAIAAGM DMGIVNAGAL VVYDEIEPEL RDRIEDVILN RRADATERLL EIAEAHNRAS EKVDDAAALA WRDAPVRERI THALVKGIDD FIVDDTEQMR VELAAEGKRP LEVIEGPLMD GMGVVGDLFG AGKMFLPQVV KSARVMKKAV AHLIPFIEAE RKPGDAATSN GRIVMATVKG DVHDIGKNIV GVVLQCNNYE VIDLGVMVPG QKILDTAREV GADIIGLSGL ITPSLDEMVS VASEMERQGF TIPLLLGGAT TSRAHTAVKV EPKYSHPVVW VKDASRSVPT AAALLSDGER REQLLAEVAA DYEAIRRRHA AKKNDRPLLT YQQALDARTP IDWGGYQPPR PRFLLQQAKE FLLQQAKDVC TEPHCGGHAR SYTRTFRDYP VEVLREYIDW QPFFNAWEMK GSFPDILHNP ASGEAARRLF EDANTMLDRI IDQGWLRPQG VVGLFPANAV GDDIEIYTDE HRHEIRTVLH HLRQQGQHRH GIPNKSLADF IAPKETGLPD YIGGFAVTAG IGAAEKIMQF KAELDDYSAI LLESVADRLA EAFAERMHAV VRHDLWGYAA DEQLTNDELI AEAYRGIRPA PGYPACPDHT EKQAIWDLLD VETQTGIELT ESMAMWPGAS VSGWYFSHPQ SQYFVVGRLG RDQVEDYAAR KGWSLRQAEK WLAPNLGYEP ED // ID F5XHH0_MICPN Unreviewed; 310 AA. AC F5XHH0; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 29-APR-2015, entry version 19. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:BAK38178.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:BAK38178.1}; GN Name=mmuM {ECO:0000313|EMBL:BAK38178.1}; GN OrderedLocusNames=MLP_51640 {ECO:0000313|EMBL:BAK38178.1}; 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 {ECO:0000313|EMBL:BAK38178.1, ECO:0000313|Proteomes:UP000007947}; RN [1] {ECO:0000313|EMBL:BAK38178.1, ECO:0000313|Proteomes:UP000007947} 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 {ECO:0000313|Proteomes:UP000007947}; 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 ----------------------------------------------------------------------- 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; BAK38178.1; -; Genomic_DNA. DR RefSeq; WP_013865992.1; NC_015635.1. DR RefSeq; YP_004575581.1; NC_015635.1. DR EnsemblBacteria; BAK38178; BAK38178; MLP_51640. DR KEGG; mph:MLP_51640; -. DR KO; K00547; -. DR BioCyc; MPHO1032480:GHBY-5197-MONOMER; -. DR Proteomes; UP000007947; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007947}; KW Methyltransferase {ECO:0000313|EMBL:BAK38178.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007947}; KW Transferase {ECO:0000313|EMBL:BAK38178.1}. SQ SEQUENCE 310 AA; 31764 MW; C7DBE8D6A3EEFE47 CRC64; MTGRRRSLAA AIAAGPVLMD GGLGTELESS GCDVTGILWS GQLLLDAPEV VEAAHRRFFA AGAQVAISGS YQLSFEGLAA VGVDRAAAET MLRRSVAVAS AAREAAVDPD QTWVAASVGP YGATLADGSE FRGTYGKTVT ELQQWHRPRL TVLAEAGADV LAIETIPCLA EVEALLRDID GSGVPSWLSL TCASATTTRA GEPVAEAFAM AADVAEVIAV GVNCLPPGDA RDLVATAARS SGKPVVVYPN SGEEWDAVHK SWYGDGSLLA GEIAGWLADG ARLVGGCCRV RPAEIEKLAA ELSAAESGAA // ID F5Y3B0_RAMTT Unreviewed; 367 AA. AC F5Y3B0; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Candidate Methionine synthase {ECO:0000313|EMBL:AEG91197.1}; GN Name=metH {ECO:0000313|EMBL:AEG91197.1}; GN OrderedLocusNames=Rta_01340 {ECO:0000313|EMBL:AEG91197.1}; 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 {ECO:0000313|EMBL:AEG91197.1, ECO:0000313|Proteomes:UP000008385}; RN [1] {ECO:0000313|Proteomes:UP000008385} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-407 / DSM 14655 / LMG 21543 / TTB310 RC {ECO:0000313|Proteomes:UP000008385}; 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; AEG91197.1; -; Genomic_DNA. DR RefSeq; WP_013899430.1; NC_015677.1. DR RefSeq; YP_004617216.1; NC_015677.1. DR EnsemblBacteria; AEG91197; AEG91197; Rta_01340. DR KEGG; rta:Rta_01340; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR BioCyc; RTAT365046:GHCU-138-MONOMER; -. DR Proteomes; UP000008385; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008385}; KW Reference proteome {ECO:0000313|Proteomes:UP000008385}. SQ SEQUENCE 367 AA; 39581 MW; B4A69A3223ED9B96 CRC64; MVGLSPAAHA TACSYNPTTM QPIAYTRGQA LPGLLEQRIV ILDGAMGTMI QRFRLTEEQV RGERFKDHGK DLKNNGELLS ITRPDVIRDI HEGFLAAGAD IIETNTFGAT SIAQDDYELG PLARELNLAS ARVARAAADK FSTPDKPRFV AGALGPTPRT ASISPDVNDP GARNVDFEQL RAAYYEQVQA LVEGGVDLLL VETIFDTLNA KAALFAIDEF FEASGERLPL IISGTVTDAS GRILSGQTVT AFWYSVRHAQ PLAIGLNCAL GAALMRPYIQ ELNRAAPDTF ISCYPNAGLP NPMSETGFDE TPEVTSRLLH EFAAQGLVNI VGGCCGTTPE HIGAIRQAVA PEKARSLRRD FFYKEAA // ID F5YF48_TREAZ Unreviewed; 430 AA. AC F5YF48; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEF81863.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEF81863.1}; GN OrderedLocusNames=TREAZ_2517 {ECO:0000313|EMBL:AEF81863.1}; OS Treponema azotonutricium (strain ATCC BAA-888 / DSM 13862 / ZAS-9). OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema. OX NCBI_TaxID=545695 {ECO:0000313|EMBL:AEF81863.1, ECO:0000313|Proteomes:UP000009222}; RN [1] {ECO:0000313|Proteomes:UP000009222} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-888 / DSM 13862 / ZAS-9 RC {ECO:0000313|Proteomes:UP000009222}; 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; AEF81863.1; -; Genomic_DNA. DR RefSeq; WP_015713007.1; NC_015577.1. DR RefSeq; YP_004528906.1; NC_015577.1. DR EnsemblBacteria; AEF81863; AEF81863; TREAZ_2517. DR KEGG; taz:TREAZ_2517; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR BioCyc; TAZO545695:GHPL-3485-MONOMER; -. DR Proteomes; UP000009222; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009222}; KW Methyltransferase {ECO:0000313|EMBL:AEF81863.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000009222}; KW Transferase {ECO:0000313|EMBL:AEF81863.1}. SQ SEQUENCE 430 AA; 46021 MW; 4D753DC0E6500C3D CRC64; MDTRSLLNQI ASERIIILDG AMGSMLQALH PGPVDGCNDM LNITKPGLIT GIHEAYLEAG ADIIETCSFN ATSISLKDYD LENRAYEISR AAGAIAKKAA DKFSTAQKPR FAAGSLGPTA KSASITSDID NPLNRAVAWD GLEAAYYDNA RGLIDGGVDL LFIETVFDSL NAKAALFAIR RIEQERGVSI PVMVSATLSE GGRLLTGQTL EGFCRAMLPA NPWALSLNCS FGADSLKPHL ARLSAASPCL VGAYPNAGLP DRQGNYSQTP AIMASHIESY LKEGLVNIIG GCCGSTPAHI AAIASLAKNY KPRVPASVNA FQAAIDSGDY EEAVELAREK AERGAKTLIL NTDKSRDPGG TAKNFIFLSN CFPVLAELQL IIESENWETI EAALKCVQGC ALVRYKNAKE DSAEYREKVR LIRDYGGRII // ID F5YN83_TREPZ Unreviewed; 1243 AA. AC F5YN83; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEF83900.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEF83900.1}; GN Name=metH {ECO:0000313|EMBL:AEF83900.1}; GN OrderedLocusNames=TREPR_0120 {ECO:0000313|EMBL:AEF83900.1}; OS Treponema primitia (strain ATCC BAA-887 / DSM 12427 / ZAS-2). OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema. OX NCBI_TaxID=545694 {ECO:0000313|EMBL:AEF83900.1, ECO:0000313|Proteomes:UP000009223}; RN [1] {ECO:0000313|Proteomes:UP000009223} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2 RC {ECO:0000313|Proteomes:UP000009223}; 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 primitia strain ZAS-2."; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001843; AEF83900.1; -; Genomic_DNA. DR RefSeq; WP_015706351.1; NC_015578.1. DR RefSeq; YP_004529220.1; NC_015578.1. DR EnsemblBacteria; AEF83900; AEF83900; TREPR_0120. DR KEGG; tpi:TREPR_0120; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; TPRI545694:GH5L-150-MONOMER; -. DR Proteomes; UP000009223; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000009223}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEF83900.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000009223}; KW Transferase {ECO:0000313|EMBL:AEF83900.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 764 764 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1243 AA; 134229 MW; E1CA8FE623AEED75 CRC64; MTIREQLTDI ASRRILVLDG AMGTMIQRYK LTETEFRGGK FEDHPTSILG CNDVLCLTKP DIISSIHEAY LKAGADIIET CSFNATAVSL ADYGLDHLAW EISRASAEIA RKQADKFSTP GVPRFVAGIL GGAAKSASIS PDMNDPGKRS VTWDELEAAY YDNARGLLDG GVDILMVETI YDTLNAKAAI FAISRLFEER NIDVPLMISA TVADVSGRIL AGQTLEAFCV SVLHAKPWSM GLNCSFGAGS LKKHVQELAA LVPCFVSAHP NAGLPNRFGE YDETPETMAA VVEEYLKEGL VNIIGGCCGS TPDHIAAIAA KAKNYGPRPL PVQAPRKGTV FAGLEPLRVS RDGGLTKIGE RTNVAGCRKF LKLIKDENYG EALGLVREMI EQGASLINVG MDDPFLDAKA CMTRFLNLAL ADPDIARLPI VVDSSRWEVI ETGLKLLQGK GLVNSLSLKE GDGELLRKAR LARRYGAAVV VMLFDEQGQA AGYERKIEIA KRSYDLLTGD GFPPEDIVFD PNILSVATGI PEHDRYALDF IHACEWITAN CPGAQISGGV TNLSFSFRGN DTVREAMHAV FLKHGIKAGL SMAIVNPGAL VPYENLESGL RDAVESLLLC KSPDAVDRLL SIAVALKDAG EGQGAGTAAK SASWRSLDVE ERVVHAMVKG IDDYIEGDVL ELRPRYARPL ELVEGPLMRG MGEVSRLFGE GKMFLPQVIR SARVMKKAVA VLEPFMERER LASGNTDTAG NEKILLATVK GDVHDIGKNI VGVVLGCNGY TVLDLGIMVP AEDILAAAEK EGAKIIGLSG LITPSLEEMV RTAREMEKRG MKIPLIIGGA TTSLAHTALR IAPEYSGPVV YVSDAGQSAG TVRALLAETD RPRFLKDLEQ RYREAAEQHE RIVAKTELLS LEGARKNRGS QAVSGQAPKS RGLQDLNGYA LERVIPFIDW EGFLRIWELD REQHSPEKDV AKEKLLEDAR KILDQVRTEK LLQLRGVAGI FPACADGDDV LVYGSGPEPV RFAFLRNQEK KRAGGANLCL ADFLPSGHSG GGNPGASPRD GNPGVSSGDG NPGVSGGGWL GLFALSAGFG LEEAAAAFRS RNDDYGALLL GTLADSLAEA FAEEVHLRIR REWWGYGEGE TLSVEDVFKG KYSGIRPAFG YPPCPDHQDK RIAFDLLEAQ KRCGLTLTES AMIIPAASVC GMVFSNPEAR YFSAAPVGDD QLQDWAKRKG IKAEEARRRL GRI // ID F5YY70_MYCSD Unreviewed; 312 AA. AC F5YY70; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 01-APR-2015, entry version 16. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:AEF35449.1}; GN OrderedLocusNames=JDM601_1449 {ECO:0000313|EMBL:AEF35449.1}; OS Mycobacterium sp. (strain JDM601). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=875328 {ECO:0000313|EMBL:AEF35449.1, ECO:0000313|Proteomes:UP000009224}; RN [1] {ECO:0000313|EMBL:AEF35449.1, ECO:0000313|Proteomes:UP000009224} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JDM601 {ECO:0000313|EMBL:AEF35449.1, RC ECO:0000313|Proteomes:UP000009224}; 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 gnome sequence of a novel clinical isolate, the RT nontuberculous Mycobacterium strain JDM601."; RL J. Bacteriol. 193:4300-4301(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; CP002329; AEF35449.1; -; Genomic_DNA. DR RefSeq; WP_013828385.1; NC_015576.1. DR RefSeq; YP_004522703.1; NC_015576.1. DR EnsemblBacteria; AEF35449; AEF35449; JDM601_1449. DR KEGG; mjd:JDM601_1449; -. DR KO; K00547; -. DR BioCyc; MSP875328:GHLX-1476-MONOMER; -. DR Proteomes; UP000009224; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009224}; KW Methyltransferase {ECO:0000313|EMBL:AEF35449.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000009224}; KW Transferase {ECO:0000313|EMBL:AEF35449.1}. SQ SEQUENCE 312 AA; 32283 MW; 17AD485F242589ED CRC64; MANVGFAVPD DTVIVADGGL ATELEARGFD LSGDLSDPLW SARLLLDAPD DVAAVHAAFF AAGAAIATTA SYQASFDGFA ARGIDRRTAE RLLRRSVDLA RLAGGGARGH RVAASVGPYG AARADGSEYV GRYGLSVSEL TAWHRPRLEV LADAGADVLA LETVPDVDEA EALMRLVSEA GVPAWLSYTI EGTSTRAGQP LTDAFAVAAG VPQIVAVGVN CCAPDDVLPA IEIAREITGK PVIVYPNSGE SWDGHRWVGP KTFSARFAAQ WVAAGARIVG GCCRVGPADI AAAAAALRRT CTQRENPAGD SQ // ID F5Z1U9_MYCSD Unreviewed; 1242 AA. AC F5Z1U9; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 01-APR-2015, entry version 24. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase MetH {ECO:0000313|EMBL:AEF35775.1}; GN Name=metH {ECO:0000313|EMBL:AEF35775.1}; GN OrderedLocusNames=JDM601_1775 {ECO:0000313|EMBL:AEF35775.1}; OS Mycobacterium sp. (strain JDM601). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=875328 {ECO:0000313|EMBL:AEF35775.1, ECO:0000313|Proteomes:UP000009224}; RN [1] {ECO:0000313|EMBL:AEF35775.1, ECO:0000313|Proteomes:UP000009224} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JDM601 {ECO:0000313|EMBL:AEF35775.1, RC ECO:0000313|Proteomes:UP000009224}; 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 gnome sequence of a novel clinical isolate, the RT nontuberculous Mycobacterium strain JDM601."; RL J. Bacteriol. 193:4300-4301(2011). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002329; AEF35775.1; -; Genomic_DNA. DR RefSeq; WP_013828711.1; NC_015576.1. DR RefSeq; YP_004523029.1; NC_015576.1. DR EnsemblBacteria; AEF35775; AEF35775; JDM601_1775. DR KEGG; mjd:JDM601_1775; -. DR KO; K00548; -. DR BioCyc; MSP875328:GHLX-1806-MONOMER; -. DR Proteomes; UP000009224; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000009224}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEF35775.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000009224}; KW Transferase {ECO:0000313|EMBL:AEF35775.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 253 253 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 316 316 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 771 771 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1242 AA; 136221 MW; B457EF491CF6431A CRC64; MTNFEPNIQP DCTEELTAAL RRRIVVIDGA MGTAIQRDRP DEAGYRGERF SEWPTPLQGN NDLLTLTQPE IIEGIHREYL EAGADILETN TFNANAISLS DYDMADLSYE LNYAGAALAR KAADEYSTGD KPRYVAGTIG PTTRTASISP DVNDPGARNV SYDQLVAAYL EAANGLVDGG ADIILIETIF DSLNAKAAVF AVETLFEERG RRWPVIISGT ITDASGRTLS GQVTEAFWNS IRHARPIAVG LNCALGAPEM RPYIAEMARI ADTHVSCYPN AGLPNAFGEY DEDPERQASY IAEFAEAGLV NLVGGCCGTA PEHIAEIAKV VEGKPPRELP TIEVATRLAG LEPLNITDDS LFVNIGERTN ITGSARFRNL IKAEDYDTAL SVALQQVEVG AQVIDINMDE GMIDGVAAMD RFTKLIASEP DISRVPVMID SSKWEVIEAG LKNVQGKPIV NSISMKEGEE KFIREARLCR KYGAAVVVMA FDEQGQADNL ERRKEICGRA YRVLTEQVGF PAEDIIFDPN CFALATGIEE HATYGIDFIE ACAWIKENLP GVHISGGISN VSFSFRGNNP VREAIHAVFL YHAIKAGLDM GIVNAGALVP YDSIDSELRE RIEDVVLNRR PDAAERLLEI AERFNSSGEG TRDADLAEWR NLPARERITH ALVKGIDAHV DEDTEELRAE IAAAGGRPIE VIEGPLMDGM NVVGDLFGAG KMFLPQVVKS ARVMKKAVAY LLPYIEAEKQ PGEDDHTNGT IVMATVKGDV HDIGKNIVGV VLQCNNYTVV DLGVMVPAEK ILTAAREYDA DMIGLSGLIT PSLEEMAGFA AEMEREGLEI PLLIGGATTS SAHTAVKIAP RRSAPVIWVK DASRSVPVVA ALLDDKQRPA LLESTAADYA SLRERHAQKN ERPMVPLEKA RANRTPIEWD GYTPPVPVIG TGVWEFLDYD LAELREYIDW QPFFNAWEMK GRFPDILNNP ASGEAARKLY NEAQQMLDTA IEEKWLTANA VIGFFPANAV GDDVEVYTDD TRTEVLTMFH NLRQQGAHRP GIPNRSLGDY IAPKETGLAD YIGAFAVTAG LGSGEKIAEF KEALDDYSAI LLESVADRLA EAFAERMHQR VRKEFWGFQP DEALDNDALI AEKYQGIRPA PGYPACPEHT EKATIWKLMD VQERTRIELT DSMAMWPGAA VSGLYFSHPQ SQYFVIGRLA QDQVADYAKR KGWTLAEAER WLGSNLGYNP ED // ID F5Z6D5_ALTSS Unreviewed; 316 AA. AC F5Z6D5; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 01-APR-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:AEF05448.1}; GN OrderedLocusNames=ambt_19785 {ECO:0000313|EMBL:AEF05448.1}; OS Alteromonas sp. (strain SN2). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Alteromonas. OX NCBI_TaxID=715451 {ECO:0000313|EMBL:AEF05448.1, ECO:0000313|Proteomes:UP000000683}; RN [1] {ECO:0000313|EMBL:AEF05448.1, ECO:0000313|Proteomes:UP000000683} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SN2 {ECO:0000313|EMBL:AEF05448.1, RC ECO:0000313|Proteomes:UP000000683}; 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 ----------------------------------------------------------------------- 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; AEF05448.1; -; Genomic_DNA. DR RefSeq; WP_013786358.1; NC_015554.1. DR RefSeq; YP_004469250.1; NC_015554.1. DR EnsemblBacteria; AEF05448; AEF05448; ambt_19785. DR KEGG; alt:ambt_19785; -. DR BioCyc; ASP715451:GHV1-3963-MONOMER; -. DR Proteomes; UP000000683; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000683}; KW Methyltransferase {ECO:0000313|EMBL:AEF05448.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000683}; KW Transferase {ECO:0000313|EMBL:AEF05448.1}. SQ SEQUENCE 316 AA; 34088 MW; A11CB5A859565A9E CRC64; MVTTTLTGKT ASASSTTASS NVLILDGGLG RELERVGAPF RQPEWSALSL MEAPDLVAQV HQNFVDAGAK IITTNTYALV PFHIGQKQFD EQAFSLAARA ASIASTVAKK NDISVAGCIP PAFGSYKPEL FCAEQLSSIL LPLIEAQTPY IDFWLVETVS SVEEANAVTS LIKEHSSKPI WLSYSLSNRH NFSNPVTLRS GESLNAILPT LDNLDAVLFN CSQPEEMEAA ITFTHLHNTD MHIGVYANSF SEHVRKHDAN EMLSTLREDV TPEKYLAYAQ TWVNAGATIV GGCCGIGPDH IKALAQGLAN HSKIAD // ID F5ZE37_ALTSS Unreviewed; 355 AA. AC F5ZE37; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:AEF04149.1}; GN OrderedLocusNames=ambt_13155 {ECO:0000313|EMBL:AEF04149.1}; OS Alteromonas sp. (strain SN2). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Alteromonas. OX NCBI_TaxID=715451 {ECO:0000313|EMBL:AEF04149.1, ECO:0000313|Proteomes:UP000000683}; RN [1] {ECO:0000313|EMBL:AEF04149.1, ECO:0000313|Proteomes:UP000000683} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SN2 {ECO:0000313|EMBL:AEF04149.1, RC ECO:0000313|Proteomes:UP000000683}; 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 ----------------------------------------------------------------------- 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; AEF04149.1; -; Genomic_DNA. DR RefSeq; WP_013785079.1; NC_015554.1. DR RefSeq; YP_004467951.1; NC_015554.1. DR EnsemblBacteria; AEF04149; AEF04149; ambt_13155. DR KEGG; alt:ambt_13155; -. DR BioCyc; ASP715451:GHV1-2653-MONOMER; -. DR Proteomes; UP000000683; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000683}; KW Reference proteome {ECO:0000313|Proteomes:UP000000683}. SQ SEQUENCE 355 AA; 38686 MW; 5C9BA0597BD8E50C CRC64; MSQHPVSSAQ ATLLRAAQQR ILVLDGAMGT MIQQHKLEEE DYRGTQFADW HCDVKGNNDL LAITQPDIIY QIHCDYFEAG ADIVETNTFN ATTIAMADYD MEAQSRDINI AAAKLARKAA DEFTAKTPDK PRFVAGVLGP TNRTASISPD VNDPGKRNVT FDALVEAYTE STEALIEGGV DLIMLETIFD TLNAKAAAFA VETVFEKLGK YLPVMISGTI TDASGRTLSG QTSEAFYYSM RHISPFSFGL NCALGPDLLR QYVEEVSTIS ECLVSAHPNA GLPNEFGEYD LEAPEMAEHI KEWAESGLVN IVGGCCGSTP EHIRAIAEAV SSIAPRKVPK FEPKMRLSGL EPFVH // ID F6AAC8_PSEF1 Unreviewed; 298 AA. AC F6AAC8; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AEF24355.1}; GN OrderedLocusNames=Psefu_4403 {ECO:0000313|EMBL:AEF24355.1}; OS Pseudomonas fulva (strain 12-X). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=743720 {ECO:0000313|EMBL:AEF24355.1, ECO:0000313|Proteomes:UP000000686}; RN [1] {ECO:0000313|EMBL:AEF24355.1, ECO:0000313|Proteomes:UP000000686} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=12-X {ECO:0000313|Proteomes:UP000000686}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; AEF24355.1; -; Genomic_DNA. DR RefSeq; WP_013793477.1; NC_015556.1. DR RefSeq; YP_004476449.1; NC_015556.1. DR EnsemblBacteria; AEF24355; AEF24355; Psefu_4403. DR KEGG; pfv:Psefu_4403; -. DR OMA; PYVDVWL; -. DR BioCyc; PFUL743720:GHQV-4483-MONOMER; -. DR Proteomes; UP000000686; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000686}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:AEF24355.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000686}; KW Transferase {ECO:0000313|EMBL:AEF24355.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 207 207 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 298 AA; 31988 MW; D85E07173EB4AED5 CRC64; MSEQPLILLD GGMGRELQRR GAPFRQPEWS ALALTEAPEQ VEAVHAAYIA SGSRVITSNS YAVVPFHIGE QRFAAEGRAL AERAGQLARS AADKAGNGVR VAGSLPPLFG SYRPDLFQPE RVTEVLTPLL DGLAPHVDLW LAETQSAIAE ARAIHAHLPK DGKPFWLSFT LRDEDVDEVP RLRSGEPVAE AARAAAELGV EVLLFNCSQP EVIGDAIDAA RDVFTSLGAN IAIGAYANAF PPQPEEATAN DGLDPLREDL DPPGYLRWVA DWRARGASHL GGCCGIGPEH IAELARRL // ID F6AC67_PSEF1 Unreviewed; 1238 AA. AC F6AC67; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEF22249.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEF22249.1}; GN OrderedLocusNames=Psefu_2282 {ECO:0000313|EMBL:AEF22249.1}; OS Pseudomonas fulva (strain 12-X). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=743720 {ECO:0000313|EMBL:AEF22249.1, ECO:0000313|Proteomes:UP000000686}; RN [1] {ECO:0000313|EMBL:AEF22249.1, ECO:0000313|Proteomes:UP000000686} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=12-X {ECO:0000313|Proteomes:UP000000686}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002727; AEF22249.1; -; Genomic_DNA. DR RefSeq; WP_013791378.1; NC_015556.1. DR RefSeq; YP_004474343.1; NC_015556.1. DR EnsemblBacteria; AEF22249; AEF22249; Psefu_2282. DR KEGG; pfv:Psefu_2282; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; PFUL743720:GHQV-2315-MONOMER; -. DR Proteomes; UP000000686; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000686}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEF22249.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000686}; KW Transferase {ECO:0000313|EMBL:AEF22249.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 252 252 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 315 315 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 316 316 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 763 763 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1238 AA; 135356 MW; 92AF7310F0DB3F7B CRC64; MPLSDRSARL QALQQALKER ILILDGGMGT MIQSYKLEEA DYRGERFADW PSDVKGNNDL LLLTQPQIIA DIEKAYLDAG ADILETNTFN ATQVSQADYD MESIVYELNV AGARVAREVA DAKTLETPDR PRFVAGVLGP TSRTCSISPD VNDPGYRNVT FDELVENYTE ATRGLIEGGA DLILIETIFD TLNAKAAIFA VQQVFDEDGV TLPIMISGTI TDASGRTLSG QTTEAFWNSV AHAKPISVGL NCALGAKELR PYLAELAAKA GTHVSAHPNA GLPNAFGEYD ETPAQMAEVV EEFAASGLLN IIGGCCGTTP GHIQAIAEAV AKYQPRPIPE IPKACRLSGL EPFTIDRNSL FVNVGERTNI TGSAKFARLI REENYTEALE VALQQVEAGA QVIDINMDEG MLDSKAAMVR FLNLIAGEPD ISRVPIMIDS SKWEVIEAGL KCIQGKGIVN SISMKEGVEQ FKHHAKLCKR YGAAVVVMAF DEVGQADTAA RKKEICQRSY DILVNEVGFP PEDIIFDPNI FAVATGIEEH NNYAVDFIEA CAYIRDQLPY ALSSGGVSNV SFSFRGNNPV REAIHSVFLY YAIQNGLSMG IVNAGQLEIY DEIPKELRDA VEDVVLNRND GATEALLAIA DKYKGDGAAK EVENEEWRSL PVDKRLEHAL VKGITAFIVE DTEECRRQCA RPIEVIEGPL MSGMNVVGDL FGSGKMFLPQ VVKSARVMKQ AVAHLIPFIE AEKGDKPEAK GKILMATVKG DVHDIGKNIV GVVLGCNGYD IVDLGVMVPA EKILQTAIAE KCDIIGLSGL ITPSLDEMVH VAKEMQRQGF KLPLMIGGAT TSKAHTAVKI DPQYSNDAVV YVTDASRAVG VATQLLSKEL KADFVQKTRD EYVVVRERTA ARATRTERLS YDNAVANKPA FDWNGYVAPK PSFTGAQVLD DIDLNVLAEY IDWTPFFISW DLAGKYPRIL TDEIVGEAAT SLFNDAQAML RKLIDEKLIK ARAVFGFWPA NQVRDDDIEV YGDNGEQLAT LHHLRQQTIK PDGKPNLSLA DFVAPKDSGV TDYVGGFITT AGIGAEEVAK AYEAKGDDYN AIMVKALADR LAEACAEWLH ERVRKEHWGY AADEQLDNEA LIREQYKGIR PAPGYPACPD HTEKGTLFKL LDPEADYNKA GRSGVFLTEH YAMFPAAAVS GWYFAHPEAQ YFAVGKVDKD QIESYTARKA QDIAVSERWL APNLGYDD // ID F6B071_DELSC Unreviewed; 354 AA. AC F6B071; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEF87213.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEF87213.1}; GN OrderedLocusNames=DelCs14_0171 {ECO:0000313|EMBL:AEF87213.1}; OS Delftia sp. (strain Cs1-4). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Delftia. OX NCBI_TaxID=742013 {ECO:0000313|EMBL:AEF87213.1, ECO:0000313|Proteomes:UP000009225}; RN [1] {ECO:0000313|Proteomes:UP000009225} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Cs1-4 {ECO:0000313|Proteomes:UP000009225}; 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; AEF87213.1; -; Genomic_DNA. DR RefSeq; WP_013800062.1; NC_015563.1. DR RefSeq; YP_004485568.1; NC_015563.1. DR EnsemblBacteria; AEF87213; AEF87213; DelCs14_0171. DR KEGG; del:DelCs14_0171; -. DR KO; K00548; -. DR BioCyc; DSP742013:GH2F-171-MONOMER; -. DR Proteomes; UP000009225; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009225}; KW Methyltransferase {ECO:0000313|EMBL:AEF87213.1}; KW Transferase {ECO:0000313|EMBL:AEF87213.1}. SQ SEQUENCE 354 AA; 38034 MW; C2237208D99C615C CRC64; MSLPQYTRAK ELPTILAKRL VILDGAMGTM IQRFKLGEAQ YRGQGYTGPG SVGDRFKDFP HDVKGNNELL SLTRPDVIRD IHEKYLAAGA DLIETNTFGA TTIAQDDYHM ADLAREMNLK SAQLARAACD KYSTPGHPRY VAGALGPTPK TASISPDVND PGARNVNFEQ LRQAYLEQTL ALIEGGSDVI LVETIFDTLN AKAALFAVDE AFEQSGECLP IMISGTVTDA SGRILSGQTV TAFWHSVRHA NPLSIGLNCA LGAALMRPYV QELNKAAPET FISCYPNAGL PNPMSDTGFD ETPEVTSRLV HEFASEGLVN IVGGCCGTTP DHIGAIAKAV GSTPTRRLFY PESA // ID F6B728_DESCC Unreviewed; 799 AA. AC F6B728; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEF94453.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEF94453.1}; GN OrderedLocusNames=Desca_1600 {ECO:0000313|EMBL:AEF94453.1}; 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 {ECO:0000313|EMBL:AEF94453.1, ECO:0000313|Proteomes:UP000009226}; RN [1] {ECO:0000313|Proteomes:UP000009226} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14880 / VKM B-2319 / CO-1-SRB RC {ECO:0000313|Proteomes:UP000009226}; 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 ----------------------------------------------------------------------- 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; AEF94453.1; -; Genomic_DNA. DR RefSeq; WP_013810274.1; NC_015565.1. DR RefSeq; YP_004497365.1; NC_015565.1. DR EnsemblBacteria; AEF94453; AEF94453; Desca_1600. DR KEGG; dca:Desca_1600; -. DR KO; K00548; -. DR BioCyc; DCAR868595:GHXC-1665-MONOMER; -. DR Proteomes; UP000009226; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009226}; KW Methyltransferase {ECO:0000313|EMBL:AEF94453.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000009226}; KW Transferase {ECO:0000313|EMBL:AEF94453.1}. SQ SEQUENCE 799 AA; 85247 MW; 8FEF2F140629FCD9 CRC64; MSFKDRVRKE VLVIDGAMGT LLQQRGLPPG WCPEEWNVSH PEVVKEIHKL YLNVGADIIT TNTFGAIKAK LADYGMQDRV KEFNLAAVRL AQEVAHPVGA MVAGSVGPLG KFLQPLGPLT FDEVYRQFLE QCQALVEAGV DLIILETFGD IGEMRAALIA AADAGDVPVV ASFTFDETGR TFTGTDPETA AVVVERLGAS AVGVNCSVGP GQLEKVVQQL TQSTNLPVLV SPNAGMPEMV DGRTVFRETP AVMADYAGRF VEYGASILGG CCGTTPEHIG AIHQRVKGMT PKIRSNQFGL RVASRVKTVT IHPAGLPVAI GERLNPTGKK ALQAEIKEGK TEITRRDALA QVEAGAEILD VNVGVAGVDQ VAAMERAINA LQVLVDAPLC IDSTDPEVIE QALKLYHGKA IINSVNGEEK SLKTILPLAK RYGAALIALT LDDQGIPPTA SERLAVARKI VQRAEEMGIP REDIMVDCLV LTVSAQPEGV PETLKAISMV KQELGLTTSL GVSNVSFGLP NRPLINAAFF AMALAAGLDA AILNPQDQRM METLRASAVL TGRDVRAEKY IAREQANTGT AVPTAASPKS AASPLEVLYQ AVLSGDKDNI ISYIDQALAQ GLNAMELLDK ALIPGIEEVG RRYGEGTYFL PQLMMAGETM TKSFERLRPE LAKNPTKRVG TVVLATVKGD VHDIGKNIVS VMLANHGFEV IDLGKNVDNE EVIKAAREHR ADIIGLSALM TTTMVHMPTV IKRVKELGLN CKVMVGGAAV TAQYAKEIGA DGYAQDAVEA VRLAKELVG // ID F6BIX7_THEXL Unreviewed; 799 AA. AC F6BIX7; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 29-APR-2015, entry version 20. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEF17862.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEF17862.1}; GN OrderedLocusNames=Thexy_1842 {ECO:0000313|EMBL:AEF17862.1}; 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 {ECO:0000313|EMBL:AEF17862.1, ECO:0000313|Proteomes:UP000007239}; RN [1] {ECO:0000313|Proteomes:UP000007239} 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 ----------------------------------------------------------------------- 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; AEF17862.1; -; Genomic_DNA. DR RefSeq; WP_013788595.1; NC_015555.1. DR RefSeq; YP_004471534.1; NC_015555.1. DR EnsemblBacteria; AEF17862; AEF17862; Thexy_1842. DR KEGG; txy:Thexy_1842; -. DR KO; K00548; -. DR BioCyc; TXYL858215:GHCH-1916-MONOMER; -. DR Proteomes; UP000007239; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007239}; KW Methyltransferase {ECO:0000313|EMBL:AEF17862.1}; KW Transferase {ECO:0000313|EMBL:AEF17862.1}. SQ SEQUENCE 799 AA; 86901 MW; 877DB50694FAB8E1 CRC64; MDIFKNLKNS IIVFDGAMGT MLQKKGLKTG ECPEYYNLLH PDIVYEIHKS YIDAGADVIE TNTFGANRIK LRSYNLSDKL PEIVKSAVQI ARKAAGDKAV ALSMGPIGEL MEPFGKLTFD EAYNAFAEVA VEGEKAGADL ALIETMSDIL EAKAAILAVK ENANLKVICT MTFQEDGRTL MGTDPVTAVV SLQGLGLDAI GVNCSTGPDM MADIVKKMAE VSRIPILAQP NAGMPHLEDG LTLYDITKEK FAVETKKLLE CGASIVGGCC GTTPEFIKLL KAEIHDTEKK TAVKEYTAVS SNTKTVFIGS DYPVCVIGER INPTGKKKLS AAIKEGNFNL IYDEAVSQEK LGASVLDVNI GVPGINEEEL MPRIVSQVQN IVNVPLQIDS SNVRAIEKAV RIVRGKPIIN SVSAKEKSLQ EVLPIVKKYG TSVIGLTISD DGLPKDADER LRNAEKIVKA ALEYGIPKED IIIDCIALTV SSEQTAAIET LKAIKLVKSK LGVSTVIGLS NVSYGLPERQ LINTAFLAMA ISYGLDAVIV NPNDKITMDI LNASMVLSSR DKRCERYINT YKKDDGINKT SVLSVEKKTD SNAREVLYRD ILEGKKADID RLVLEILNEG VEPLSIVDNT IIPALKDVGD KYDKGIYFLP QLLNSAEVVE SAFKVLKEKM PKGMGSKGKI ILATVEGDIH DIGKNIVKVL LENYGYEVID LGKDVKPSKI ADEVKRTNAK LIGLSALMTT TLNNMEKTIK ILREKYDIKI MVGGAVLTKD YAMKIGADYY GSNAQEAVRI ADKVFSEIN // ID F6CB09_LACKZ Unreviewed; 330 AA. AC F6CB09; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:AEG40366.1}; GN Name=mmuM {ECO:0000313|EMBL:AEG40366.1}; GN OrderedLocusNames=WANG_0671 {ECO:0000313|EMBL:AEG40366.1}; OS Lactobacillus kefiranofaciens (strain ZW3). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1033837 {ECO:0000313|EMBL:AEG40366.1, ECO:0000313|Proteomes:UP000009228}; RN [1] {ECO:0000313|EMBL:AEG40366.1, ECO:0000313|Proteomes:UP000009228} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ZW3 {ECO:0000313|EMBL:AEG40366.1, RC ECO:0000313|Proteomes:UP000009228}; RX PubMed=21705607; DOI=10.1128/JB.05306-11; RA Wang Y., Wang J., Ahmed Z., Bai X., Wang J.; RT "Complete genome sequence of Lactobacillus kefiranofaciens ZW3."; RL J. Bacteriol. 193:4280-4281(2011). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002764; AEG40366.1; -; Genomic_DNA. DR RefSeq; WP_013854160.1; NC_015602.1. DR RefSeq; YP_004562468.1; NC_015602.1. DR EnsemblBacteria; AEG40366; AEG40366; WANG_0671. DR KEGG; lke:WANG_0671; -. DR KO; K00547; -. DR BioCyc; LKEF1033837:GHZJ-704-MONOMER; -. DR Proteomes; UP000009228; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009228}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:AEG40366.1}; KW Transferase {ECO:0000313|EMBL:AEG40366.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 223 223 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 330 AA; 37136 MW; B1029CF7462251CE CRC64; MDLINQVANR GLIIDGAMST ALEHEEIDTN NDLWTAIALE KDLDKIYQVH LKYFKAGAQL AITDTYQANV QAFVKHGFTK KQAATMIANA VKVAKKARDD YEVQTGIHNF VAGSVGSYGA YLADGDEFRG DYSLTDRQYL DFHLPRLRVI LANQPDCLAI ETQPKLDEPV AILNWLKENT PTIPVYVSFT LHDTTKISDG TPLKKAMQKL NDYDQVFAVG VNCFKPFLAT AAIDKMREFT DKQIVVYPNL GGVYNEFERN WIPFNAKFDF KKLSQEWYEH GARMIGGCCS TGVKEISQIA AFFKTIHSQK TQPKSIKLDF NHLKSSSSNT // ID F6CUS2_MARPP Unreviewed; 303 AA. AC F6CUS2; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AEF54182.1}; GN OrderedLocusNames=Mar181_1134 {ECO:0000313|EMBL:AEF54182.1}; OS Marinomonas posidonica (strain CECT 7376 / NCIMB 14433 / IVIA-Po-181). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Marinomonas. OX NCBI_TaxID=491952 {ECO:0000313|EMBL:AEF54182.1, ECO:0000313|Proteomes:UP000009230}; RN [1] {ECO:0000313|EMBL:AEF54182.1, ECO:0000313|Proteomes:UP000009230} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CECT 7376 / NCIMB 14433 / IVIA-Po-181 RC {ECO:0000313|Proteomes:UP000009230}; 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 ----------------------------------------------------------------------- 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; AEF54182.1; -; Genomic_DNA. DR RefSeq; WP_013795658.1; NC_015559.1. DR RefSeq; YP_004481101.1; NC_015559.1. DR EnsemblBacteria; AEF54182; AEF54182; Mar181_1134. DR KEGG; mpc:Mar181_1134; -. DR BioCyc; MPOS491952:GI6N-1168-MONOMER; -. DR Proteomes; UP000009230; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009230}; KW Methyltransferase {ECO:0000313|EMBL:AEF54182.1}; KW Transferase {ECO:0000313|EMBL:AEF54182.1}. SQ SEQUENCE 303 AA; 33067 MW; 2E3BDE4807430B55 CRC64; MTAITILDGG MGRELERLGA PFKQPEWSAL ALMEAPETVK AVHQSFINSG SQVITTNSYS LVPFHIGEDV FQQRARELTH LSGKLAREAA DEADHKVQVA ASVAPLFGSY RADLYQADRV TEIATPIIEE LAPFADLWLL ETQCLMDESS RVIALIEQID TAKKPIWVSF TLEDSEQTAE PILRSGETVI DAVKAMQKLG VDAILFNCSQ PEIIGEAIEL THNVLGELGA NTIQIGAYAN AFPPTPKDAT ANDGLDELRE DLTPPAYLTW VQQWQTKGAS LIGGCCGIGP EHILAIKEYT QNH // ID F6D083_MARPP Unreviewed; 307 AA. AC F6D083; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AEF55907.1}; GN OrderedLocusNames=Mar181_2878 {ECO:0000313|EMBL:AEF55907.1}; OS Marinomonas posidonica (strain CECT 7376 / NCIMB 14433 / IVIA-Po-181). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Marinomonas. OX NCBI_TaxID=491952 {ECO:0000313|EMBL:AEF55907.1, ECO:0000313|Proteomes:UP000009230}; RN [1] {ECO:0000313|EMBL:AEF55907.1, ECO:0000313|Proteomes:UP000009230} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CECT 7376 / NCIMB 14433 / IVIA-Po-181 RC {ECO:0000313|Proteomes:UP000009230}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; AEF55907.1; -; Genomic_DNA. DR RefSeq; WP_013797378.1; NC_015559.1. DR RefSeq; YP_004482826.1; NC_015559.1. DR EnsemblBacteria; AEF55907; AEF55907; Mar181_2878. DR KEGG; mpc:Mar181_2878; -. DR BioCyc; MPOS491952:GI6N-2970-MONOMER; -. DR Proteomes; UP000009230; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009230}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:AEF55907.1}; KW Transferase {ECO:0000313|EMBL:AEF55907.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 307 AA; 33670 MW; E7CE3B0CC03309FE CRC64; MNNLTLLDGG IGRELKRIGA PFSQPLWSAQ SLIEAPHYVT QVHENFIQAG ADIITVNSYA CVPFHLGETL YQQQGATLAR QAAIIAKDAA NNAPHPVLVA GSLPPPLGSY RPDLFEQQQA LDILTTLFEA QDEHVDLWLA ETIASIGEAN TLVNVLKNST KPCYYAFTLS DELGETARLR SGESVAEAID AMLTTTNQEQ AIQIKENDGI FFNCSIPEAM EQAIRDTTSQ LEKHHRQLNI GVYANSFTPI SQGHEANLTT QASRDLSPEE YLVFAKKWHH LGANIIGGCC GINPNHIKAL AEWKHAF // ID F6D0M7_MARPP Unreviewed; 1244 AA. AC F6D0M7; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEF54825.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEF54825.1}; GN OrderedLocusNames=Mar181_1787 {ECO:0000313|EMBL:AEF54825.1}; OS Marinomonas posidonica (strain CECT 7376 / NCIMB 14433 / IVIA-Po-181). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Marinomonas. OX NCBI_TaxID=491952 {ECO:0000313|EMBL:AEF54825.1, ECO:0000313|Proteomes:UP000009230}; RN [1] {ECO:0000313|EMBL:AEF54825.1, ECO:0000313|Proteomes:UP000009230} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CECT 7376 / NCIMB 14433 / IVIA-Po-181 RC {ECO:0000313|Proteomes:UP000009230}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002771; AEF54825.1; -; Genomic_DNA. DR RefSeq; WP_013796300.1; NC_015559.1. DR RefSeq; YP_004481744.1; NC_015559.1. DR EnsemblBacteria; AEF54825; AEF54825; Mar181_1787. DR KEGG; mpc:Mar181_1787; -. DR KO; K00548; -. DR BioCyc; MPOS491952:GI6N-1857-MONOMER; -. DR Proteomes; UP000009230; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000009230}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEF54825.1}; KW Transferase {ECO:0000313|EMBL:AEF54825.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 249 249 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 764 764 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1244 AA; 137558 MW; B466C180F9C8BFCE CRC64; MTKSVSYSVL EQRLSENVLI LDGAMGTMIQ AYKLEEQDYR GERFADWQSD LKGNNDLLSI TQPNIIKEIH AQYLSAGADI IETNTFNANF ISMLDYHMED LSYELNYQSA RLAREMADEY TAKNPTKPRF VAGAVGPTSR TCTISPDVND PGFRNIHFDE LVEAYTTAVD GLIKGGVDII LIETIFDTLN AKAAIYAVLD YFDTTGVRYP IMISGTITDA SGRTLSGQTT EAFWNSVAHA KPISVGLNCA LGPKELRQYV EELSRIADTH VSAHPNAGLP NAFGEYDESP EEMLAEIQGW VDSGFLNILG GCCGTAPEHI ATFANAFSDA TPRLIPEIEK ACRLSGLEPF NIDGNSLFVN VGERTNVTGS AMFKRLIKEG DFDTALDVAR LQVENGAQII DINMDEGMLD SQAAMERFLK LIASEPDISR VPIMLDSSKW EILEAGLKWI QGKGVVNSIS IKEGEEKFKE QAKKLMKYGA AVIVMAFDEA GQADTRQRKI EICRRSYKIL VEEIGFPAQD IIFDPNIFAI ATGIEEHNRY ALDFIEATGD ITRELPYAKV SGGVSNVSFS FRGNNPVREA IHAVFLYHAI KQGMTMGIVN AGQLALYEDI PPKLRDAVED AVLNRTPDAT DNLLAIAGEF AGTGEVAEKE TQEWRGLPVS DRLSHALVKG ITEFIDEDTE EARQHFDRPL EVIEGPLMDG MGIVGDLFGS GKMFLPQVVK SARVMKKAVA YLMPFIEEEK ARNMDTASSS NGKIVMATVK GDVHDIGKNI VGVVLQCNNF EVVDLGVMVS SETILRTAKE QGAHLIGLSG LITPSLDEMV HVAKEMERQH FDLPVMIGGA TTSKAHTAVK IEQNYKRNQV VHVTNASRSV GVASTLLSKD ESKRQAFIED IQSDYEKTRI RYKDRAKAGR RVSIDKARQN KAPVTFEHQV VRPKQLGVTV LTEKDIDLGV VKDYIDWTPF FQTWELAGAY PRILSDAVVG EEATRVYQDA LVMLDQVIES ASLQARAVVG LFPANQVGDD DIEIYADDTR QEVIETLSFL RIQNELTAPG KYNHSLADFI APKESGVTDY MGAFACAAGY GIASLVEQYE ADHDDYNSIM IKAVADRLAE ATAEYLHEKV RMELWAYAPT ETLTNEQLIK EKYQGIRPAP GYPACPDHTE KSKLWSLLQA EARIGMQLTE SFAMLPTAAV SGWYFAHPDA SYFGVGKIGP DQVEEYAERK NMTKEDAERW LAPNLGYDPE DDRV // ID F6DB73_THICA Unreviewed; 1237 AA. AC F6DB73; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 29-APR-2015, entry version 28. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEG30813.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEG30813.1}; GN OrderedLocusNames=Thicy_0037 {ECO:0000313|EMBL:AEG30813.1}; OS Thioalkalimicrobium cyclicum (strain DSM 14477 / JCM 11371 / ALM1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Piscirickettsiaceae; Thioalkalimicrobium. OX NCBI_TaxID=717773 {ECO:0000313|EMBL:AEG30813.1, ECO:0000313|Proteomes:UP000009232}; RN [1] {ECO:0000313|EMBL:AEG30813.1, ECO:0000313|Proteomes:UP000009232} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14477 / JCM 11371 / ALM1 RC {ECO:0000313|Proteomes:UP000009232}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002776; AEG30813.1; -; Genomic_DNA. DR RefSeq; WP_013834602.1; NC_015581.1. DR RefSeq; YP_004536292.1; NC_015581.1. DR EnsemblBacteria; AEG30813; AEG30813; Thicy_0037. DR KEGG; tcy:Thicy_0037; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR Proteomes; UP000009232; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000009232}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEG30813.1}; KW Transferase {ECO:0000313|EMBL:AEG30813.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1237 AA; 136312 MW; 00A6561F21472181 CRC64; MTRVERIAQL KQLLTERVVV LDGAMGTMIQ GLQLTEDDFR GELFADYHMD IKGNNDILVM TKPEVIRDIH LGFLRQGVDI LETNSFNATT IAQADYDMQD QVRAINICAA KVAREACDIA AAEDGKPRFV AGVLGPTNRT ASISPDVNDP GFRNTSFDEL VGAYVQATEA LLEGGADVIL IETIFDTLNA KAAIFAVKQV EDALGEELPI MISGTITDAS GRTLSGQTTE AFYNAIRHAK PLSVGLNCAL GPKELRPYVE ELSRIAECYV SVHPNAGLPN EFGEYDETPE QMAAEVQTWA QAGWLNIIGG CCGTTPDHVE AMAKAALAHP QRIIPTIKKA CRLSGLEPMT IDDTTLFVNV GERNNVTGSA LFKRLIIEDN YEQAVEIAVK QVNDGAQIID VNMDEGMLDA KACMSRFLNM MAGEPDAARV PVMIDSSKWE AIEAGLKCIQ GKGIVNSISL KEGEENFLAQ AKLIQRYGAA TIVMAFDEDG QADTFARKKE ICQRSYDLLV ANGFPPEDII FDPNIFAVAT GIEEHNNYAV DFIEATGWIK QNLPYAMISG GVSNVSFSFR GNNPVREAIH SVFLYYAIQQ GMDMGIVNAG QMAIYDDLDP ELKQAVEDVI LNKDPEAADR LLEVAEKFRG DGSVQGKESD IKWREASVEK RLEHALVKGI TDFIEDDTEE ARTTLGSPLQ VIEGPLMDGM NVVGDLFGAG KMFLPQVVKS ARVMKRAVAY LQPFLEAEKS SGQAKGKIVM ATVKGDVHDI GKNIVGVVLQ CNNFEVIDLG VMVPAEKILD TALREGANVI GLSGLITPSL EEMVHVAKEM QRRGMSIPLL IGGATTSKAH TAVKIEPQYE HPVVYVKDAS RAVGVAQSLI SNDLKVDFAI KIREEYVQLR EERKARAQQV KRVPLNKARD NAIPIDWSDY TPPKPKFLGK KVFDNIDLAD LMPRIDWSPF FQSWDLHGLY PRILDDKVVG EEAKKVFADA QAMLKQIIDE KWLTARAVIG FYPANAVGDD IELYTDDKRA TLLTRLHNLR QQAEKKPGQY NQCLSDYIAP KDVKEQPGLV IPDYIGAFAV TAGIGIDEHI ARFEAAHDDY NSIMVKALAD RLAEALAEHM HELVRKEFWG YAADEALTNE ELIKEKYQGI RPAPGYPANP EHTEKGTLWE LLQPDSEIGL ELTSSYAMTP TAAVSGWYFA HPKSKYFGVG SIGRDQAEDY AHRKGWSIAE AEKWLAPILG YDPEDFN // ID F6DF89_THETG Unreviewed; 1186 AA. AC F6DF89; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEG33047.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEG33047.1}; GN OrderedLocusNames=Ththe16_0624 {ECO:0000313|EMBL:AEG33047.1}; OS Thermus thermophilus (strain SG0.5JP17-16). OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; OC Thermus. OX NCBI_TaxID=762633 {ECO:0000313|EMBL:AEG33047.1, ECO:0000313|Proteomes:UP000009233}; RN [1] {ECO:0000313|Proteomes:UP000009233} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SG0.5JP17-16 {ECO:0000313|Proteomes:UP000009233}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002777; AEG33047.1; -; Genomic_DNA. DR RefSeq; WP_014510041.1; NC_017272.1. DR RefSeq; YP_005640174.1; NC_017272.1. DR EnsemblBacteria; AEG33047; AEG33047; Ththe16_0624. DR KEGG; tts:Ththe16_0624; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; TTHE762633:GLMG-652-MONOMER; -. DR Proteomes; UP000009233; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000009233}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEG33047.1}; KW Transferase {ECO:0000313|EMBL:AEG33047.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 256 256 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1186 AA; 130928 MW; 7FB1AECD22999794 CRC64; MVEVHACSPG CRHHLGGAGW GDAPLVRLGY NKEARAKKFP YLKALLERPL VFDGAMGTEL QKRDLTPEDY GGEAYFGCPE VLNRTRPEVV REIHLAYLEA GAEVIETNTF GCLRHVLAEY GLGDEAETLA YLGAKVAREA ADPYGAFVAG ALGPGTKLVS LGQISWDELY RAYKEAARGL LKGGVDLILL ETAQDILQVR CAVLAAREAM AEVGREVPLQ VQVTLEATGT MLVGSDEVAA LAALESLPID VVGMNCATGP DLMDAKIRYF AENSTRFVSC LPNAGLPRNE GGRVVYDLTP EELAHWHRKF VLEYGVNAVG GCCGTGPEHI RKVAEAVRGA PARPRPAAFP PQVASLYQAV PLRQEASVLL VGERLNATGS KRFREMLFAR DLEGILALAR EQVEEGAHAL DLSVAWTGRD ELEDLAWLLP SLATAVTVPF VVDSTSPEAM ELVLKHLPGR LILNSANLED GLEKFDRVAS LAKAHGAALV VLAIDEKGMA KTWEEKVRVA LRMYERLTEH HGLRPEDLLF DLLTFPITQG DEESRPLAKE TLLAIEELRE RLPGVGFILG VSNVSFGLKP RARRVLNSVF LDEARKKGLT AAIVDAGKIL PISQIPEEAY ALALDLIYDR RKEGFDPLLA FMAYFEAHKE DPGKREDAFL ALPLLERLKR RVVEGRKQGL EADLEEALKA GHKPLDLING PLLAGMKEVG DLFGAGKMQL PFVLQAAEVM KRAVAYLEPH MEKKGEGKGT LVLATVKGDV HDIGKNLVDI ILSNNGYRVV NLGIKVPIEE ILKAVEAHKP HAVGMSGLLV KSTLVMKENL EYMRERGYTL PVILGGAALT RSFVEEDLRA IYPNVYYAED AFEGLRLMEE LTGHAPPELT RKAPQRPKRE APKAAPRARP VGEAPAVPRP PFFGVRVEEG LDLATIAHYV NKLALYRGQW GYSRKGLSRE AWQALVEREA EPVFQRLLKE AMAEGWLEPK VLYGFFPVAR EGEELLVFSP ETGEVLERFR FPRQKGGGLS LVDYFRPRFA APLGDEADWM PKEAFRAGAR DVLGVQLVTM GEAPSRKAQA LFQSGAYQDY LFVHGFSVEM TEALAEYWHK RMRQMWGIAH KDATEIQKLF QQGYQGARYS FGYPACPDLS DQAKLDRLMG FHRVGVRLTE NFQLDPEHAT SALVVHHPEA RYFSVD // ID F6DRQ1_DESRL Unreviewed; 799 AA. AC F6DRQ1; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 01-APR-2015, entry version 20. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AEG59812.1}; GN OrderedLocusNames=Desru_1547 {ECO:0000313|EMBL:AEG59812.1}; OS Desulfotomaculum ruminis (strain ATCC 23193 / DSM 2154 / NCIB 8452 / OS DL). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfotomaculum. OX NCBI_TaxID=696281 {ECO:0000313|EMBL:AEG59812.1, ECO:0000313|Proteomes:UP000009234}; RN [1] {ECO:0000313|Proteomes:UP000009234} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23193 / DSM 2154 / NCIB 8452 / DL RC {ECO:0000313|Proteomes:UP000009234}; 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 ----------------------------------------------------------------------- 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; AEG59812.1; -; Genomic_DNA. DR RefSeq; WP_013841580.1; NC_015589.1. DR RefSeq; YP_004545098.1; NC_015589.1. DR EnsemblBacteria; AEG59812; AEG59812; Desru_1547. DR KEGG; dru:Desru_1547; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR Proteomes; UP000009234; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009234}; KW Methyltransferase {ECO:0000313|EMBL:AEG59812.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000009234}; KW Transferase {ECO:0000313|EMBL:AEG59812.1}. SQ SEQUENCE 799 AA; 85754 MW; 2006DF5541CA7F0E CRC64; MSFKDRVQRE ILIVDGAMGT LLQERGLPAG WCPEEWNVSH PEVIKEVHGL YLRAGADIIT TNTFGAIPLK LEEYDMPDRV REFNLAAGRL AREAAKPFGA MVAGSVGPLG KFLQPLGTLS FDEAYQQFLV QCRALVEAEV DLILFETFGD IGEMRAALIA AADAGSVPVV ASFTFDESGR TFTGTDPETA AVVAERLGVA AVGVNCSVGP RQLEGVVRQL TRSTNLPVLI SPNAGMPEIV EGRTVFRETP EVLADYAARF VDYGASLLGG CCGTTPEHIK AISQAVKDLE IKTRNKSFGL RVASRVKTVA IHPAGMPVAI GERLNPTGKK ALQAEIKEGK TEITRRDALA QVEAGAEILD VNVGVGGVDP IAAMERAIHA VQVLVDAPLC IDSTDPAVIE HALKLYHGKA IINSVNGEDQ SMETILPLAK RYGAALIGLT LDERGIPPTA EERLAVAGKI VARAEEMGIP REDIMIDCLV LTVSAQPEGV PETLKAISLV KQELGLATSL GVSNVSFGLP NRKLINSAFF AMALSAGLDA AILNPQEERM METLRASAVL TGRDLRAEKY IVREQVRAEA PVKQKEDEKK ASTPREILYR AVLSGDKDNI IRYIEEALGQ GMGPLEMLDK ALIPAIEEVG RRYAQGVYFL PQLIMAGETM TKSFECLRPA LAKGLTKKVA TVVLATVKGD IHDIGKNIVS VMLANHGFEV IDLGKNVDNQ RIIEAVREHR AGLIGLSALM TTTMIHMPEL IKDVKEAGLA CKVMVGGAAV TAQYAKEIGA DGYAEDAVEA VRIAKELIS // ID F6EKP5_AMYSD Unreviewed; 297 AA. AC F6EKP5; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:AEF40181.1}; GN Name=mmuM {ECO:0000313|EMBL:AEF40181.1}; GN OrderedLocusNames=AS9A_1732 {ECO:0000313|EMBL:AEF40181.1}; OS Amycolicicoccus subflavus (strain DSM 45089 / DQS3-9A1). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Amycolicicoccus. OX NCBI_TaxID=443218 {ECO:0000313|EMBL:AEF40181.1, ECO:0000313|Proteomes:UP000009235}; RN [1] {ECO:0000313|EMBL:AEF40181.1, ECO:0000313|Proteomes:UP000009235} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 45089 / DQS3-9A1 {ECO:0000313|Proteomes:UP000009235}; 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 ----------------------------------------------------------------------- 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; AEF40181.1; -; Genomic_DNA. DR RefSeq; WP_013806530.1; NC_015564.1. DR RefSeq; YP_004492981.1; NC_015564.1. DR EnsemblBacteria; AEF40181; AEF40181; AS9A_1732. DR KEGG; asd:AS9A_1732; -. DR KO; K00547; -. DR OMA; YGRSVTK; -. DR BioCyc; ASUB443218:GH9R-1760-MONOMER; -. DR Proteomes; UP000009235; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009235}; KW Methyltransferase {ECO:0000313|EMBL:AEF40181.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000009235}; KW Transferase {ECO:0000313|EMBL:AEF40181.1}. SQ SEQUENCE 297 AA; 31137 MW; 5ECBE87625029017 CRC64; MATFTDALLA RALVCDGGLA TALEARGHNL AGGLWSARLL LDTPDEIAAV HRAFFAAGAD IAITASYQAS FRGFANCGIG RRGTERLLRR SVRIAADVRD EFGRGFVAAS IGPYGAAAAD GSEYKGRYGL SVRELRAWHR PRFEILADTG ADVLAVETIP DLDEAEALAS LISEFRVPAW LSYTIAGART RAGQPVSDAF EVASEIDSIV AVGVNCCAPA DVIPTIDTAQ HSGKPVIVYP NSGEGWDAEA GRWTGKSEFS VKLARQWAAA GAQIIGGCCR VGAGDIAQVA SALSRPT // ID F6ENE1_AMYSD Unreviewed; 1187 AA. AC F6ENE1; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEF40412.1}; GN Name=metH {ECO:0000313|EMBL:AEF40412.1}; GN OrderedLocusNames=AS9A_1963 {ECO:0000313|EMBL:AEF40412.1}; OS Amycolicicoccus subflavus (strain DSM 45089 / DQS3-9A1). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Amycolicicoccus. OX NCBI_TaxID=443218 {ECO:0000313|EMBL:AEF40412.1, ECO:0000313|Proteomes:UP000009235}; RN [1] {ECO:0000313|EMBL:AEF40412.1, ECO:0000313|Proteomes:UP000009235} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 45089 / DQS3-9A1 {ECO:0000313|Proteomes:UP000009235}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002786; AEF40412.1; -; Genomic_DNA. DR RefSeq; WP_013806761.1; NC_015564.1. DR RefSeq; YP_004493212.1; NC_015564.1. DR EnsemblBacteria; AEF40412; AEF40412; AS9A_1963. DR KEGG; asd:AS9A_1963; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; ASUB443218:GH9R-1996-MONOMER; -. DR Proteomes; UP000009235; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000009235}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000009235}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 737 737 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1187 AA; 130014 MW; A86CA78CFA078B31 CRC64; MSVRTSLLDA LTQRVVIGDG AMGTMLQAAH LTLDDFRELE GCNEILNDTR PDVLREIHLA YLEAGADAIE TNTFGCNLPN LADYDIADRI RELAEKGTRI AREAADETGP SADGMPRFIL GSVGPGTKLP TLGHAPFASL RDAYAECALG MIDGGADAIL IETCQDLLQV KAAIIGAQHA MDQANTRLPI ITHVTVETTG TMLLGSEIGA ALTALEPLGI DLIGLNCATG PEEMSEHLRH LSKHSRLPVS VMPNAGLPVL GANGAEYPLT AEELGVALSG FVREFGLALV GGCCGTTPEH IRQLRAAVLE TRQAERHPRP EPGVASLYSH VPFKQDSSIL MIGERTNANG SKAFREAMLA GDFQKCLDIA KDQTRDGAHM LDLCIDYVGR NGAEDMSELA SRLATSSTLP IMLDSTEPEV LRAGLEHLGG RCAINSVNYE DGDGPDSRFY RIMRLVKEHG AAVVALCIDE NGQARTAEDK VRVAERLIDD ITGNWGLRDE DIIVDCLTFT IGTGMEESRK DGAATIEAIR QLKERRPRVH TTLGLSNISF GLNPAARQVL NSVFLHECVE AGLDTAIVHA SKILPMSKIG EEQREVALDL VYDRRREGYD PLQKFMDLFE GVSAASARES RAQQLAALPL FERLERRIID GERNGLDTDL EEAMKEKPPL AIINENLLAG MKVVGELFGS GQMQLPFVLT SAEVMKTAVA HLEPHMEATG DSGKGRIVLA TVKGDVHDIG KNLVDIILSN NGYEVINLGI KQPIANILDA AVEKKADVIG MSGLLVKSTV VMKENLEELN SRGFADKFPV LLGGAALTRS YVENDLTAVY HGDVLYARDA FEGLRLMDTI MAEKRGEGPD PNSPEAVAAR EKEEERKARH ERSKRIAEKR KAEQAPVVVP ERSDVAEDLD VPVPPFWGTR IVKGISLAEY STTLDERALF LGQWGLRGVR GGEGPSYEEL VESEGRPRLR YWLDRLSTEG ILAHAAVVYG YFPAVSEGDS VFVLESPEPD APVRFEFEFP RQQRDRFLCV SDFVRSRARA RATNQVDVLP FQLVTMGQPI ADFANELFAE DQYRDYLEVH GIGVQLTEAL AEYWHQRVRE ELIMPSGAAV AREDPADVQE FFRLGYRGAR YSFGYGACPN LEDRVKLVEL LEPGRIGVAL SEELQLHPEQ STDAFVLHHP EAKYFNV // ID F6ET72_SPHCR Unreviewed; 348 AA. AC F6ET72; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEG50446.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEG50446.1}; GN ORFNames=Sphch_2811 {ECO:0000313|EMBL:AEG50446.1}; OS Sphingobium chlorophenolicum L-1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingobium. OX NCBI_TaxID=690566 {ECO:0000313|EMBL:AEG50446.1, ECO:0000313|Proteomes:UP000007150}; RN [1] {ECO:0000313|EMBL:AEG50446.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=L-1 {ECO:0000313|EMBL:AEG50446.1}; 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; AEG50446.1; -; Genomic_DNA. DR RefSeq; WP_013848681.1; NC_015593.1. DR RefSeq; YP_004554952.1; NC_015593.1. DR EnsemblBacteria; AEG50446; AEG50446; Sphch_2811. DR KEGG; sch:Sphch_2811; -. DR KO; K00548; -. DR BioCyc; SCHL690566:GJJA-2864-MONOMER; -. DR Proteomes; UP000007150; Chromosome 1. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007150}; KW Methyltransferase {ECO:0000313|EMBL:AEG50446.1}; KW Transferase {ECO:0000313|EMBL:AEG50446.1}. SQ SEQUENCE 348 AA; 37425 MW; 31BC6CE1AE39A902 CRC64; MTPEQQFRAV AAEKIMIFDG GYGTSIQKHG LTEADYRGSL DLPKDQKGNN DLLCLTRPDI VEGIHAAYLD AGADMIETNT FSSTKIAMAD YGCEHLVRDI NIAAAKLARA ACEKATAKDG RPRFVAGSIG PTNKTLSISP DVNDPAYREV DYDTLKADYR EQCDALIEGG VDFLLVETCF DTLNAKAAGM AAREAEAAAG RPVPLMLSFT ITDMSGRNLS GHTINAFWYS LRHLKPLTIG VNCAFGADLL RPYLSELAKN ADTLILAYPN AGLPNELGQY DELPETTAKL IRQWVDEGLV NMVGGCCGTT PAHIGAVARA LAGQKPRQVP ELPVVTRLAG LEPMHIAA // ID F6FWH1_ISOV2 Unreviewed; 1191 AA. AC F6FWH1; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 29-APR-2015, entry version 23. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEG44545.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEG44545.1}; GN OrderedLocusNames=Isova_1799 {ECO:0000313|EMBL:AEG44545.1}; OS Isoptericola variabilis (strain 225). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Promicromonosporaceae; Isoptericola. OX NCBI_TaxID=743718 {ECO:0000313|Proteomes:UP000009236}; RN [1] {ECO:0000313|EMBL:AEG44545.1, ECO:0000313|Proteomes:UP000009236} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=225 {ECO:0000313|Proteomes:UP000009236}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002810; AEG44545.1; -; Genomic_DNA. DR RefSeq; WP_013838937.1; NC_015588.1. DR RefSeq; YP_004542439.1; NC_015588.1. DR EnsemblBacteria; AEG44545; AEG44545; Isova_1799. DR KEGG; iva:Isova_1799; -. DR KO; K00548; -. DR BioCyc; IVAR743718:GI39-1832-MONOMER; -. DR Proteomes; UP000009236; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000009236}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEG44545.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000009236}; KW Transferase {ECO:0000313|EMBL:AEG44545.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 235 235 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 301 301 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 302 302 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 755 755 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1191 AA; 129576 MW; 31D8F09AAB86D5A9 CRC64; MTSTLDVSAA DARADALLQA MRTRVVVADG AMGTMIQDAD PTLEDYEGHE GCNEVLNVSR PDIIRSVHDA YLEVGVDAIE TNTFGANWSN LSDYGIEDRI RELARAGAEL ARERADAWST PEHPRWVLGS MGPGTKLPSL GHTTYAHLKA TFAEQAAGLL EGGADAILVE TSQDLLQAKA AVNGAREAMA AVGRRVPVIV SVTVETTGTM LMGSEIGAAL TTLQALGVDA IGLNCATGPD QMSEHLRHLA RHSEVPVACM PNAGLPELGP KGAVYPLTAP ELATAHAQFV EEFSLGLVGG CCGTTPEHLR QVVEAVRGRE LTARPVEREN GVASLYSHTD LHQDASYLAI GERTNANGSK AFREAMLDGR WDDVVDIARA QTRDGAHLLD VCVDYVGRDG VADVREVVSR LASASTLPLV IDSTEPEVIK AGLELVGGRA VVNSVNFEDG DGPTSRFARI MPLVKEHGAA VIALTIDEEG QARTAEKKVA IASRLIDTLT GDWGMRVDDI IVDALTFPIA TGQEETRRDA IETIEAIREI TRRYPGVHTT LGVSNVSFGL NPAARTVLNS VFLHEAVQAG LDSAIVHAAK ILPRTAIPDE QWEAAEDLVR DRRRYDDEGN LVHDPLSHLL ELFSGVDSAS LRDQRAAELA ALPVGERLER RIIDGARKGL EDDVEEALAL GMKALDIVNT HLLGGMKVVG ELFGSGQMQL PFVLQSAEVM KAAVALLEPH MERVAGGPDE TKGTIVLATV RGDVHDIGKN LVDIILTNNG YKVVNIGIKQ PISAMIEAAE QHDADVIGMS GLLVKSTVVM KENLEELVSR GLEKKWPILL GGAALTRTYV EDDLASMFPG TVRYARDAFE GLRLMEPLVR IARGASPDDV GLPPLRKRRH DVVKVTETAP EELPARSDVA TDNPVPTPPF WGTRIVKGVQ LADYAAFLDE RATFMGQWGL KPGRGDDGAS YEELVETEGR PRLAEWLERI RTESILDPTV VYGYFPVWSE GNDLVVGHHE GPDGGSGGPV GTERLRFRFP RQRRDRHLCL ADFVKPRSWA EETGRFDVLP VQLVTVGDSV SQHTARLFEA NRYREYMELH GLSVQLTEAL AEFWHARVRD ELGFADEDPS DVEGMFKLAY RGARFSLGYP ACPDMEDRRK VVELLRPERV GVVLSDELQL HPEQSTDAFV FHHPEAKYFS V // ID F6G4D8_RALS8 Unreviewed; 346 AA. AC F6G4D8; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase protein {ECO:0000313|EMBL:AEG70402.1}; GN Name=metHa {ECO:0000313|EMBL:AEG70402.1}; GN OrderedLocusNames=RSPO_c03110 {ECO:0000313|EMBL:AEG70402.1}; OS Ralstonia solanacearum (strain Po82). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=1031711 {ECO:0000313|EMBL:AEG70402.1, ECO:0000313|Proteomes:UP000007953}; RN [1] {ECO:0000313|EMBL:AEG70402.1, ECO:0000313|Proteomes:UP000007953} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Po82 {ECO:0000313|EMBL:AEG70402.1, RC ECO:0000313|Proteomes:UP000007953}; 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; AEG70402.1; -; Genomic_DNA. DR RefSeq; WP_014618115.1; NC_017574.1. DR RefSeq; YP_006030938.1; NC_017574.1. DR EnsemblBacteria; AEG70402; AEG70402; RSPO_c03110. DR KEGG; rsn:RSPO_c03110; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR BioCyc; RSOL1031711:GLJ5-3157-MONOMER; -. DR Proteomes; UP000007953; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007953}; KW Methyltransferase {ECO:0000313|EMBL:AEG70402.1}; KW Transferase {ECO:0000313|EMBL:AEG70402.1}. SQ SEQUENCE 346 AA; 37436 MW; 11E9FF346C7B16C4 CRC64; MTAPLPYTRA ANLPALLRQR ILILDGAMGT MIQRYKLTEA QYRGERFAGH PVDVKGNNEL LLLTAPEVIR EIHEQYLAAG ADLIETNTFG ATTVAQEDYK MAELAYEMNV VAARLAREAC DKYSTPDKPR FVAGAFGPTP KTASISPDVN DPGARNINFD QLRDAYYEQG KALLEGGADV FLVETIFDTL NAKAALFAID QLFEDLGERV PVMISGTVTD ASGRILSGQT VEAFWNSLRH AKPITFGLNC ALGAALMRPY IAELAKVCDT AVSCYPNAGL PNPMSDTGFD ETPDVTSSLV DEFAAAGLVN LVGGCCGTTP EHIQAIAERV AQRKPRAWPG QYREAA // ID F6HDS7_VITVI Unreviewed; 319 AA. AC F6HDS7; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:CCB50448.1}; GN OrderedLocusNames=VIT_05s0020g03860 {ECO:0000313|EMBL:CCB50448.1}; 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 {ECO:0000313|Proteomes:UP000009183}; RN [1] {ECO:0000313|Proteomes:UP000009183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183}; 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; FN595749; CCB50448.1; -; Genomic_DNA. DR EnsemblPlants; VIT_05s0020g03860.t01; VIT_05s0020g03860.t01; VIT_05s0020g03860. DR InParanoid; F6HDS7; -. DR Proteomes; UP000009183; Chromosome 5. DR GO; GO:0005886; C:plasma membrane; IEA:EnsemblPlants/Gramene. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009183}; KW Reference proteome {ECO:0000313|Proteomes:UP000009183}. SQ SEQUENCE 319 AA; 34757 MW; CE97EC8EAA6AFE41 CRC64; MADFIRQSGG YAVIDGGLAT ELERHGADLN DPLWSATCLI HSPDLIRRVH LDYLEAGASI IITASYQATI QGFEAKGLSR EEAEVLLRRS VEIACEARDI YHERCAKGTC LEQRPILVAA SVGSYGAYLA DGSEYSGHYG AAVTLETLKD FHRRRVQVLA ESGADLIAFE TIPNKLEAKA YAELLDEENI KIPAWFSFTS LDGINVVSGD SLIECASIAD SCKQVVAVGI NCTPPRFIHG LILLIQKVTT KPVVIYPNSG ETYDGVRKEW VKSSGVQDGD FVSYVSKWRE AGASLFGGCC RTSPHTIRAI SMTLSSYLQ // ID F6HI62_VITVI Unreviewed; 345 AA. AC F6HI62; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:CCB51908.1}; GN OrderedLocusNames=VIT_07s0151g00520 {ECO:0000313|EMBL:CCB51908.1}; 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 {ECO:0000313|Proteomes:UP000009183}; RN [1] {ECO:0000313|Proteomes:UP000009183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183}; 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; FN595764; CCB51908.1; -; Genomic_DNA. DR RefSeq; XP_010651998.1; XM_010653696.1. DR UniGene; Vvi.11292; -. DR ProteinModelPortal; F6HI62; -. DR EnsemblPlants; VIT_07s0151g00520.t01; VIT_07s0151g00520.t01; VIT_07s0151g00520. DR GeneID; 100852835; -. DR KEGG; vvi:100852835; -. DR InParanoid; F6HI62; -. DR KO; K00547; -. DR Proteomes; UP000009183; Chromosome 7. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008283; P:cell proliferation; IEA:EnsemblPlants/Gramene. DR GO; GO:0006306; P:DNA methylation; IEA:EnsemblPlants/Gramene. DR GO; GO:0006260; P:DNA replication; IEA:EnsemblPlants/Gramene. DR GO; GO:0051567; P:histone H3-K9 methylation; IEA:EnsemblPlants/Gramene. DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:EnsemblPlants/Gramene. DR GO; GO:0043687; P:post-translational protein modification; IEA:EnsemblPlants/Gramene. DR GO; GO:0000394; P:RNA splicing, via endonucleolytic cleavage and ligation; IEA:EnsemblPlants/Gramene. DR GO; GO:0033528; P:S-methylmethionine cycle; IEA:EnsemblPlants/Gramene. DR GO; GO:0010050; P:vegetative phase change; IEA:EnsemblPlants/Gramene. DR GO; GO:0009616; P:virus induced gene silencing; IEA:EnsemblPlants/Gramene. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009183}; KW Reference proteome {ECO:0000313|Proteomes:UP000009183}. SQ SEQUENCE 345 AA; 37768 MW; F6326586BE07B25D CRC64; MGHVDLQPSS FISDFLLQTG GVAVIDGGLA TELERHGADL NDPLWSAKCL LSSPHLIRTV HLDYLEAGAD IIITASYQAT IQGFEARGFS RGESEALLRK SVEIACEARK MYYDRCIEFA CDDSEDGRIL KHRPILVAAS VGSYGAYLAD GSEYSGIYGD EITVETLKDF HRRRVQILAD AGADLIAFET VPNKLEAQAY AELLEEENIK IPAWFSFNSK DGVHVVSGDS LLECVSIAES CKKVVSVGIN CTPPRFIHGL ILSIKKVTTK PILIYPNSGE SYDPEQKEWV QKTGVSVEDF VSYVNKWCEV GASLVGGCCR TTPNTIRAIY RTLSNNRSAT ASLKS // ID F6IJG5_9SPHN Unreviewed; 353 AA. AC F6IJG5; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Main chromosome, complete replicon {ECO:0000313|EMBL:CCA94219.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CCA94219.1}; GN ORFNames=PP1Y_AT35039 {ECO:0000313|EMBL:CCA94219.1}; OS Novosphingobium sp. PP1Y. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Novosphingobium. OX NCBI_TaxID=702113 {ECO:0000313|EMBL:CCA94219.1, ECO:0000313|Proteomes:UP000009242}; RN [1] {ECO:0000313|EMBL:CCA94219.1, ECO:0000313|Proteomes:UP000009242} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PP1Y {ECO:0000313|EMBL:CCA94219.1}; RX PubMed=21685292; DOI=10.1128/JB.05349-11; 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 ----------------------------------------------------------------------- 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; CCA94219.1; -; Genomic_DNA. DR RefSeq; WP_013834378.1; NC_015580.1. DR RefSeq; YP_004536037.1; NC_015580.1. DR EnsemblBacteria; CCA94219; CCA94219; PP1Y_AT35039. DR KEGG; npp:PP1Y_AT35039; -. DR KO; K00548; -. DR BioCyc; NSP702113:GJD2-3308-MONOMER; -. DR Proteomes; UP000009242; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009242}; KW Methyltransferase {ECO:0000313|EMBL:CCA94219.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000009242}; KW Transferase {ECO:0000313|EMBL:CCA94219.1}. SQ SEQUENCE 353 AA; 37847 MW; 9A74DD8FD93FAACC CRC64; MSPRETFLAE AAKRILITDG AFGTEIQNWK LAEADYAGNL GLSHEQKGNN DILALSKPEV PEAIHRAYFE AGADIAETNT FSANRISQAD YGAEHLVREI NVESARLARK VADEFQAKDA ASGISRPRFV AGAIGPTNKT LSLSPDVNDP GYREIDWDTL VDVYKEQAAA LVEGGADFIL IETVFDTLNA KAGIMAVKQL EAELGREVPI MLSMTLTDLS GRNLSGHTVE AFWHAVRHAR PITIGLNCSF GATQLRPHVK TLSEIADTLI MIYPNAGLPN ELGAYDEMPD TTAGFVGEWA VAGQVNVLGG CCGSTPAHIA AIARQVKGVA PRKVPSLEPV TRLAGLEPFI MAA // ID F6IZ17_LACPE Unreviewed; 304 AA. AC F6IZ17; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 01-OCT-2014, entry version 11. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:CCB83938.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:CCB83938.1}; GN ORFNames=LPE_03000 {ECO:0000313|EMBL:CCB83938.1}; OS Lactobacillus pentosus MP-10. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1028490 {ECO:0000313|EMBL:CCB83938.1}; RN [1] {ECO:0000313|EMBL:CCB83938.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MP-10 {ECO:0000313|EMBL:CCB83938.1}; 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR871830; CCB83938.1; -; Genomic_DNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:CCB83938.1}; KW Transferase {ECO:0000313|EMBL:CCB83938.1}. SQ SEQUENCE 304 AA; 32364 MW; DC7D21460D6313DB CRC64; MISLTDLLTK GPVVSDGAMA TELEKRGVET NSALWSATAM LDHPAAIQAV HQSYLDAGAQ IMTTNTYQTN VPAFEQAGIP AEQARQLIQK AVTVAHDARD ASAATGAVIA GSIGPYGAYL ADGSEYTGDY QLSPAAYQAF HQERLELMID AGVDVLALET MPRLDEVQAL VDLVTTQWPK QPYWVSFSIR DPQRLCDGTS LATAAQWVAA QPNVVAVGVN CTALENIEPA LATLRAAVTI PLIVYPNSGD QYDPVTKTWQ PTDLSHQFAS FVPKWLAAGA QIIGGCCRTT PADIATVAQV VAHK // ID F6IZ53_LACPE Unreviewed; 618 AA. AC F6IZ53; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 07-JAN-2015, entry version 18. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=LPE_03038 {ECO:0000313|EMBL:CCB83976.1}; OS Lactobacillus pentosus MP-10. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1028490 {ECO:0000313|EMBL:CCB83976.1}; RN [1] {ECO:0000313|EMBL:CCB83976.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MP-10 {ECO:0000313|EMBL:CCB83976.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR871834; CCB83976.1; -; Genomic_DNA. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862, KW ECO:0000313|EMBL:CCB83976.1}. SQ SEQUENCE 618 AA; 66751 MW; 893F4A0BDB5DFC0C CRC64; MNLKQALQQR VLVADGAMGT LLYGNYGINS AFENLNLTHP DTILRVHQSY IQAGADIIQT NTYAANRLKL TRYDLQDQVT TINQAAVKIA VTAREHADHP VYILGTIGGL AGDTDAAVQR ATQAEIAANV TEQLTALLAT EQLDGILLET YYDLSELLAA LKIVKAHTDL PVITNVSMLA AGVLRNGTSF TDAIVQLHAA GADVIGTNCR LGPYYLAQSF ENLAIPADVK LAVYPNSGLP GTDQDGAIVY DGEPSYFEEY AERFRQLGLS IIGGCCGTTP LHTAATVRGL SSRSLVPHNA PTHVAQAPTL VTTKSQHRFL HKVATEKTVL VELDPPRDFD TRKFFRGAER LKAAGVDGIT LSDNSLATVR IANTAIAAQL KLNYGITPIV HLTTRDHNLI GLQSEIMGSH SLGIEDILAV TGDPAKLGDF PGATSVGDVR SVELMKLIKQ FNSGIGPTGK SLKEASDFRV AGAFNPNAYR TDVSTKSISR KLSYGCDYII TQPVYDLANV DALADALAAN QIDVPVFVGV MPLVSRRNAE FLHHEVHGIR LPKSVLERMQ QAELDGNERA VGITIAKELI DGICARFNGV HIVTPFNRFK TVLELVNYVQ QKNLTKVQ // ID F6KMG0_EPICO Unreviewed; 308 AA. AC F6KMG0; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 04-MAR-2015, entry version 18. DE SubName: Full=Betaine homocysteine S-methyltansferase {ECO:0000313|EMBL:AEG78334.1}; DE Flags: Fragment; OS Epinephelus coioides (Orange-spotted grouper) (Epinephelus nebulosus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Serranoidei; Serranidae; Epinephelinae; OC Epinephelini; Epinephelus. OX NCBI_TaxID=94232 {ECO:0000313|EMBL:AEG78334.1}; RN [1] {ECO:0000313|EMBL:AEG78334.1} RP NUCLEOTIDE SEQUENCE. RA Wu M.-S., Chen C.-W., Huang H.-H., Chang C.-Y.; RT "Differential gene expression of grouper iridovirus/LPS/poly I:C RT treated orange-spotted grouper (Epinephelus coioides)."; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HQ441033; AEG78334.1; -; mRNA. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 117 117 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 199 199 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 200 200 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT NON_TER 1 1 {ECO:0000313|EMBL:AEG78334.1}. SQ SEQUENCE 308 AA; 33981 MW; 877DD618E673E6BA CRC64; ARGCDLAREV ASEGDAMVAG GVSQTPSYLS CKSETEVKAI FKKQLEVFMK KNVDFLIAEY FEHVEEAEWA VQVLKTSGKP VAASLCIGPE GDMHGVSPAE CAVRLVKAGA QIIGVNCHFD PMTCVKAVKM MKEGVEKARL KAHYMVQPLA FHTPDCNCQG FIDLPEFPFA LEPRILTRWD MHAYARAAYQ AGIRFIGGCC GFEPYHIRAI AEELAPERGI MAAASEKHGM WGAGLEMHTK PWVRARARRD YWEQLSPASG RPKCPSMSTP EGWGVTKGHA DLLQHKEATT SQEMKHVLEM QKKAKSTA // ID F6QW01_CALJA Unreviewed; 363 AA. AC F6QW01; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCJAP00000036750}; GN Name=BHMT2 {ECO:0000313|Ensembl:ENSCJAP00000036750}; OS Callithrix jacchus (White-tufted-ear marmoset). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Platyrrhini; Cebidae; Callitrichinae; Callithrix. OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000036750, ECO:0000313|Proteomes:UP000008225}; RN [1] {ECO:0000313|Ensembl:ENSCJAP00000036750, ECO:0000313|Proteomes:UP000008225} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCJAP00000036750} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2011) to UniProtKB. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSCJAP00000036750}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACFV01075854; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSCJAT00000038811; ENSCJAP00000036750; ENSCJAG00000019766. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; F6QW01; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000008225; Chromosome 2. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0061627; F:S-methylmethionine-homocysteine S-methyltransferase activity; IEA:Ensembl. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl. DR GO; GO:0046500; P:S-adenosylmethionine metabolic process; IEA:Ensembl. DR GO; GO:0033477; P:S-methylmethionine metabolic process; IEA:Ensembl. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008225}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Reference proteome {ECO:0000313|Proteomes:UP000008225}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 208 208 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 363 AA; 40388 MW; 355F790236F274C7 CRC64; MAPAGRPGAK KGILERLESG EVVIGDGSFL ITLEKRGYVK AGLWTPEAVI EHPDAVRQLH MEFLRAGSNV MQTFTFSASE DNMESKWEDV NAAACDLARE VAGKGDALVA GGICQTSVYR YHKDEARIKK LFRLQLQVFV QKNVDFLIAE YFEYVEEAVW AVEVLKESDR PVAVTMCIGP EGDMHDLTPG ECAVRLVKAG ASIVGVNCRF GPETSLKTMK LMKEGLERAG LKAYLMVQPL VFHTPDCGKE GFVDLPEYPF GLEPRVATRW DIQKYAREAY NLGVRYIGGC CGFEPYHVRA IAEELAPERG FLPPASEKHG SWGSGLDMHT KPWVRARARR EYWENLLPAS GRPFCPSLSK PDD // ID F6R4P4_CALJA Unreviewed; 406 AA. AC F6R4P4; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCJAP00000036745}; GN Name=BHMT {ECO:0000313|Ensembl:ENSCJAP00000036745}; OS Callithrix jacchus (White-tufted-ear marmoset). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Platyrrhini; Cebidae; Callitrichinae; Callithrix. OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000036745, ECO:0000313|Proteomes:UP000008225}; RN [1] {ECO:0000313|Ensembl:ENSCJAP00000036745, ECO:0000313|Proteomes:UP000008225} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCJAP00000036745} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2011) to UniProtKB. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSCJAP00000036745}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACFV01075851; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_002744876.1; XM_002744830.3. DR Ensembl; ENSCJAT00000038806; ENSCJAP00000036745; ENSCJAG00000019752. DR GeneID; 100393375; -. DR KEGG; cjc:100393375; -. DR CTD; 635; -. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; F6R4P4; -. DR KO; K00544; -. DR OMA; WGVTKGT; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000008225; Chromosome 2. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006577; P:amino-acid betaine metabolic process; IEA:Ensembl. DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008225}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Reference proteome {ECO:0000313|Proteomes:UP000008225}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 217 217 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 406 AA; 45000 MW; 1C67542ADF4B8863 CRC64; MPPVGGKKAK KGILERLNAG EIVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAVRQLH REFLRAGSNV MQTFTFYASE DKLENRGNYV LEKISGQKVN EAACDIARQV ADEGDALVAG GVSQTPSYLS CKSETEVKKV FLQQLEVFMK KNVDFLIAEY FEHVEEAVWA VETLIASGKP VAATMCIGPE GDLHGVPPGE CAVRLVKAGA SIVGVNCHFD PTISLQTVKL MKEGLEAARL KAHLMSQPLA YHTPDCNKQG FIDLPEFPFG LEPRVATRWD IQKYAREAYN LGVRYIGGCC GFEPYHIRAI AEELAPERGF LPLASEKHGS WGSGLDMHTK PWVRARARKE YWENLRIASG RPYNPSMSKP DGWGVTKGTA ELMQQKEATT EQQLKELFEK QKFKSQ // ID F6R5P0_CALJA Unreviewed; 363 AA. AC F6R5P0; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 04-MAR-2015, entry version 20. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCJAP00000036738}; DE Flags: Fragment; GN Name=BHMT2 {ECO:0000313|Ensembl:ENSCJAP00000036738}; OS Callithrix jacchus (White-tufted-ear marmoset). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Platyrrhini; Cebidae; Callitrichinae; Callithrix. OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000036738, ECO:0000313|Proteomes:UP000008225}; RN [1] {ECO:0000313|Ensembl:ENSCJAP00000036738, ECO:0000313|Proteomes:UP000008225} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCJAP00000036738} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSCJAP00000036738}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACFV01075854; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSCJAT00000038798; ENSCJAP00000036738; ENSCJAG00000019766. DR GeneTree; ENSGT00390000003122; -. DR OMA; PEGDMHD; -. DR Proteomes; UP000008225; Chromosome 2. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008225}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000008225}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 208 208 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSCJAP00000036738}. SQ SEQUENCE 363 AA; 40548 MW; 124A248088B1240D CRC64; KLEALSPTQE KGILERLESG EVVIGDGSFL ITLEKRGYVK AGLWTPEAVI EHPDAVRQLH MEFLRAGSNV MQTFTFSASE DNMESKWEDV NAAACDLARE VAGKGDALVA GGICQTSVYR YHKDEARIKK LFRLQLQVFV QKNVDFLIAE YFEYVEEAVW AVEVLKESDR PVAVTMCIGP EGDMHDLTPG ECAVRLVKAG ASIVGVNCRF GPETSLKTMK LMKEGLERAG LKAYLMVQPL VFHTPDCGKE GFVDLPEYPF GLEPRVATRW DIQKYAREAY NLGVRYIGGC CGFEPYHVRA IAEELAPERG FLPPASEKHG SWGSGLDMHT KPWVRARARR EYWENLLPAS GRPFCPSLSK PDD // ID F6T0P5_MACMU Unreviewed; 1185 AA. AC F6T0P5; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMMUP00000013174}; DE Flags: Fragment; GN Name=MTR {ECO:0000313|Ensembl:ENSMMUP00000013174}; OS Macaca mulatta (Rhesus macaque). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000013174, ECO:0000313|Proteomes:UP000006718}; RN [1] {ECO:0000313|Ensembl:ENSMMUP00000013174, ECO:0000313|Proteomes:UP000006718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000013174, RC ECO:0000313|Proteomes:UP000006718}; RX PubMed=17431167; DOI=10.1126/science.1139247; RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M., RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., RA Wilson R.K., Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., RA Hardison R.C., Makova K.D., Miller W., Milosavljevic A., Palermo R.E., RA Siepel A., Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J., RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., RA Dinh H.H., Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., RA Godfrey J., Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., RA Jhangiani S.N., Joshi V., Khan Z.M., Kirkness E.F., Cree A., RA Fowler R.G., Lee S., Lewis L.R., Li Z., Liu Y.-S., Moore S.M., RA Muzny D., Nazareth L.V., Ngo D.N., Okwuonu G.O., Pai G., Parker D., RA Paul H.A., Pfannkoch C., Pohl C.S., Rogers Y.-H.C., Ruiz S.J., RA Sabo A., Santibanez J., Schneider B.W., Smith S.M., Sodergren E., RA Svatek A.F., Utterback T.R., Vattathil S., Warren W., White C.S., RA Chinwalla A.T., Feng Y., Halpern A.L., Hillier L.W., Huang X., RA Minx P., Nelson J.O., Pepin K.H., Qin X., Sutton G.G., Venter E., RA Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P., Jones S.M., RA Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L., Csuros M., RA Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H., Liu Y., RA Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E., RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J., RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J., RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A., RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., RA Denby A., Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., RA Marklein A., Nielsen R., Vallender E.J., Clark A.G., Ferguson B., RA Hernandez R.D., Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., RA Pu L.-L., Ren Y., Smith D.G., Wheeler D.A., Schenck I., Ball E.V., RA Chen R., Cooper D.N., Giardine B., Hsu F., Kent W.J., Lesk A., RA Nelson D.L., O'brien W.E., Pruefer K., Stenson P.D., Wallace J.C., RA Ke H., Liu X.-M., Wang P., Xiang A.P., Yang F., Barber G.P., RA Haussler D., Karolchik D., Kern A.D., Kuhn R.M., Smith K.E., RA Zwieg A.S.; RT "Evolutionary and biomedical insights from the rhesus macaque RT genome."; RL Science 316:222-234(2007). RN [2] {ECO:0000313|Ensembl:ENSMMUP00000013174} RP IDENTIFICATION. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000013174}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 1}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSMMUP00000013174}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSMMUT00000014067; ENSMMUP00000013174; ENSMMUG00000010073. DR GeneTree; ENSGT00420000029824; -. DR InParanoid; F6T0P5; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG7TF786; -. DR TreeFam; TF312829; -. DR Proteomes; UP000006718; Chromosome 1. DR ExpressionAtlas; F6T0P5; baseline. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:Ensembl. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006718}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006718}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 178 178 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 241 241 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 242 242 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 705 705 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSMMUP00000013174}. SQ SEQUENCE 1185 AA; 131558 MW; 16594C00064E585C CRC64; QEYLLAGADI IETNTFSSTS IAQADYGLEH LAYRMNKCSA GVARKAAEEI TLQTGIKRFV AGALGPTNKT LSVSPSVERP DYRNIKFDEL VEAYQEQAKG LLDGGVDILL IETIFDTANA KAAVFALQNL FEEKYAPRPI FISGTIVDKS GRTLSGQTGE AFVISLSHAE PLCIGLNCAL GAAEMRPFIE MIGKCTTAYV LCYPNAGLPN TFGDYDETPS TMAKHLKDFA MDGLVNIVGG CCGSTPDHIR EIAEAVKNCK PRVPLATVFE GHMLLSGLEP FRIGQYTNFV NIGERCNVAG SRKFAKLIMA GNYEEALGVA RVQVEMGAQV LDINMDDGML DGPSAMTRFC NLIASEPDIA KVPLCIDSSN FAVIEAGLKC CQGKCIVNSI SLKEGEDDFL EKARKIKKFG AAMVVMAFDE EGQATETDTK IRVCTRAYHL LVKKLGFNPN DIIFDPNILT IGTGMEEHNL YAINFIHATK VIKETLPGAR ISGGLSNLSF SFRGMEAIRE AMHGVFLYHA IKSGMDMGIV NAGNLPVYDD IHKELLQLCE DLIWNKDPEA TEKLLRYAQT QGTGGKKVIQ TDEWRNGPVE ERLEYALVKG IEKHIIEDTE EARLNQERYP RPLNIIEGPL MNGMKIVGDL FGAGKMFLPQ VIKSARVMKK AVGHLIPFME KEREETRVLN GTTEEEATDP YQGTIVLATV KGDVHDIGKN IVGVVLGCNN FRVIDLGVMT PCDKILKAAL DHKADIIGLS GLITPSLDEM IFVAKEMERL AIKIPLLIGG ATTSRTHTAV KIAPRYSAPV IHVLDASKSV VVCSQLLDEN LKDEYFEEIM EEYEDIRQDH YESLKERRYL PLSQARKSGF QMDWLSEPHP VKPTFIGTQV FEDYDLQKLV DYIDWKPFFD VWQLRGKYPN RGFPKIFNDK TVGEEAKKVY DDAQNMLNTL INQKKLQARG VVGFWPAQSI QDDIHLYTES AVPQAAEPIA TFYGLRQQAE KDSASTEPYY CLSDFIAPLH SGIRDYLGLF AVACFGVEEL SKAYEDDGDD YSSIMVKALG DRLAEAFAEE LHERVRRELW AYCGSEQLDV ADLRRLRYEG IRPAPGYPSQ PDHTEKLTMW RLADIEQSTG IRLTESLAMA PASAVSGLYF SNLKSKYFAV GKISRDQVED YALRKNMAVA EVEKWLGPIL GYDTD // ID F6T886_CIOIN Unreviewed; 375 AA. AC F6T886; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 2. DT 27-MAY-2015, entry version 30. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCINP00000015488}; GN Name=LOC100182838 {ECO:0000313|Ensembl:ENSCINP00000015488}; OS Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis). OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Enterogona; OC Phlebobranchia; Cionidae; Ciona. OX NCBI_TaxID=7719 {ECO:0000313|Ensembl:ENSCINP00000015488, ECO:0000313|Proteomes:UP000008144}; RN [1] {ECO:0000313|Ensembl:ENSCINP00000015488} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12481130; DOI=10.1126/science.1080049; RA Dehal P., Satou Y., Campbell R.K., Chapman J., Degnan B., RA De Tomaso A., Davidson B., Di Gregorio A., Gelpke M., Goodstein D.M., RA Harafuji N., Hastings K.E., Ho I., Hotta K., Huang W., Kawashima T., RA Lemaire P., Martinez D., Meinertzhagen I.A., Necula S., Nonaka M., RA Putnam N., Rash S., Saiga H., Satake M., Terry A., Yamada L., RA Wang H.G., Awazu S., Azumi K., Boore J., Branno M., Chin-Bow S., RA DeSantis R., Doyle S., Francino P., Keys D.N., Haga S., Hayashi H., RA Hino K., Imai K.S., Inaba K., Kano S., Kobayashi K., Kobayashi M., RA Lee B.I., Makabe K.W., Manohar C., Matassi G., Medina M., RA Mochizuki Y., Mount S., Morishita T., Miura S., Nakayama A., RA Nishizaka S., Nomoto H., Ohta F., Oishi K., Rigoutsos I., Sano M., RA Sasaki A., Sasakura Y., Shoguchi E., Shin-i T., Spagnuolo A., RA Stainier D., Suzuki M.M., Tassy O., Takatori N., Tokuoka M., Yagi K., RA Yoshizaki F., Wada S., Zhang C., Hyatt P.D., Larimer F., Detter C., RA Doggett N., Glavina T., Hawkins T., Richardson P., Lucas S., RA Kohara Y., Levine M., Satoh N., Rokhsar D.S.; RT "The draft genome of Ciona intestinalis: insights into chordate and RT vertebrate origins."; RL Science 298:2157-2167(2002). RN [2] {ECO:0000313|Ensembl:ENSCINP00000015488} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSCINP00000015488}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EAAA01000348; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_002131974.1; XM_002131938.2. DR Ensembl; ENSCINT00000015488; ENSCINP00000015488; ENSCING00000007560. DR GeneID; 100182838; -. DR KEGG; cin:100182838; -. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; F6T886; -. DR KO; K00544; -. DR OMA; VEECEWA; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR Proteomes; UP000008144; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008144}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000008144}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 215 215 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 375 AA; 41314 MW; 6F37E1CA609735B0 CRC64; MSKITAQKKG LLERLKEGPV VGDGSMCMTL EKRGYCRAGP WTPEAVIAYP DAVKQLLREY LRAGADVLQT PCFYCSDGML KKGTASGETV AYTTDAINEA ACKIAHEVAA EGNALVCGGL SPVLSYLRER DSAKTRAEFD AQLDVFIKYK VDFVLAEFFA HVEELEICVD VMKKAKMPIA CSMRIGPMGD SNGVSVEECA VRMAKTGADL IGINCLYDFD TCLKTLKRMR DALDKEGLKT PLMCQPLGWR CPEVEDKLIG YLDLPETPLA LDPRTATRFE VHEFTRAAYN LGTRYIGGCC GMEPHHIRAI AQELAPERKR DPPVQDMCPP TGFMQFSGLS NIKEKASMDF WTNTKPGSGR PFNPASTQTE GGRFM // ID F6V492_XENTR Unreviewed; 1266 AA. AC F6V492; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSXETP00000039980}; DE Flags: Fragment; GN Name=mtr {ECO:0000313|Ensembl:ENSXETP00000039980}; OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; OC Silurana. OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000039980, ECO:0000313|Proteomes:UP000008143}; RN [1] {ECO:0000313|Ensembl:ENSXETP00000039980} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20431018; DOI=10.1126/science.1183670; RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J., RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., RA Blitz I.L., Blumberg B., Dichmann D.S., Dubchak I., Amaya E., RA Detter J.C., Fletcher R., Gerhard D.S., Goodstein D., Graves T., RA Grigoriev I.V., Grimwood J., Kawashima T., Lindquist E., Lucas S.M., RA Mead P.E., Mitros T., Ogino H., Ohta Y., Poliakov A.V., Pollet N., RA Robert J., Salamov A., Sater A.K., Schmutz J., Terry A., Vize P.D., RA Warren W.C., Wells D., Wills A., Wilson R.K., Zimmerman L.B., RA Zorn A.M., Grainger R., Grammer T., Khokha M.K., Richardson P.M., RA Rokhsar D.S.; RT "The genome of the Western clawed frog Xenopus tropicalis."; RL Science 328:633-636(2010). RN [2] {ECO:0000313|Ensembl:ENSXETP00000039980} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2011) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 1}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSXETP00000039980}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAMC01027580; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01027581; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSXETT00000039980; ENSXETP00000039980; ENSXETG00000018453. DR Xenbase; XB-GENE-1001004; mtr. DR GeneTree; ENSGT00420000029824; -. DR InParanoid; F6V492; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG7TF786; -. DR TreeFam; TF312829; -. DR Reactome; REACT_279575; Methylation. DR Reactome; REACT_313856; Sulfur amino acid metabolism. DR Reactome; REACT_331894; Cobalamin (Cbl, vitamin B12) transport and metabolism. DR Proteomes; UP000008143; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008143}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008143}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 260 260 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 325 325 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 786 786 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSXETP00000039980}. SQ SEQUENCE 1266 AA; 140563 MW; F2D172BA386B474A CRC64; ISSGLSDLPP AGVRKRNLQE ELDSVLRERI MVLDGGMGTM IQQHTLQEES FRGQEFIDHA KPLKGNNDLL SITQSEIIYK IHKEYLTCGA DIVETNTFSS TSIAQADYGL EHLAYRLNKV SAEVARRAAD DVTAETGMKR YVAGAMGPTN KTLSVSPSVE RPDYRNVTFD ELVDAYAEQA RGLLDGGVDI LLVETIFDTA NAKAALFAIQ KLFEEDYEPR PIFISGTIVD KSGRTLSGQT GEAFVVSVSH AEPLCIGLNC ALGAIEMRPF IEAIGKCTTS YVICYPNAVG LPNTFGGYDE TPEVTAKHIK DFALDGLVNI VGGCCGTTPA HIREIAEAVK NCKPRIPPTS VFDGYMLLSG LEPFRIGPYT NFVNIGERCN VAGSRRFAKL IMSDNYEEAL SVAKAQVEMG AQILDINVDD GMLDGPTAMA RFCNYIASEP DIAKVPLCID SSNFNVIEAG LKCCQGKCIV NSISLKEGEE DFLAKAKKIK QFGAAVVIMA FDEVGQATDT ETKVSVCTRA YNLLVEKLNF NPNDIIFDPN ILTIGTGMEE HDKYAINFIE ATKSIKESLK GARVSGGLSN LSFSFRGMEA IREAMHGVFL YHAIKAGMDM GIVNAGNLPV YDDIDKELLT LCEDLIWNRD PDGTEKLLKY AQTKAKGGKK VIQTDEWRNG SVEERLEYAL IKGIEKFVIE DTEEARANKE KYSRPLHIIE GPLMNGMKVV GELFGAGKMF LPQVIKSARV MKKSVGHLIP FMEKEREAMR AISGTLEEDN PYQGTIVLAT VKGDVHDIGK NIVGVVLGCN NFRVIDLGVM TPCDKILRAA IENKADIIGL SGLITPSLDE MIFVAKEMER LGIRTPLLIG GATTSRTHTA VKIAPRYNAP VIHCLDASKS VVVCSQLLDE NVRDDFLEEI TEEYEDIRQD HYESLRERRY LTLEQARNKG LHIDWLSHPK PVRPKLIGTE VYSNYDLEKL RHYIDWKPFF DVWQLRGKYP NRAFPKIFND KTVGEEAKRL YEDAQNMLNM VISEKKFEAR GVVGIWPAHS VQDDILLYAD EGNMSSTEAI ATFYGLRQQA EKDSASTDPY YCLSDFIAPQ HSGVKDYLGV FAVACFGVEE LSKVYEKQGD DYSSIMAKAL GDRLVEAFAE ELHERVRKDL WGYCSEEQLN VSDLRRIRYE GIRPAPGYPS QPDHIEKVTM WKLADVERTT GIKLTESLAM SPASSVSGLM FSSPMSKYFA VGKISKDQVE DYACRKNMPV CEVEKWLGPI LSYDPE // ID F6VYL8_HORSE Unreviewed; 407 AA. AC F6VYL8; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSECAP00000013444}; GN Name=BHMT {ECO:0000313|Ensembl:ENSECAP00000013444}; OS Equus caballus (Horse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus. OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000013444, ECO:0000313|Proteomes:UP000002281}; RN [1] {ECO:0000313|Ensembl:ENSECAP00000013444, ECO:0000313|Proteomes:UP000002281} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000013444, RC ECO:0000313|Proteomes:UP000002281}; RX PubMed=19892987; DOI=10.1126/science.1178158; RG Broad Institute Genome Sequencing Platform; RG Broad Institute Whole Genome Assembly Team; RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F., RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., RA Distl O., Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., RA Penedo M.C.T., Raison J.M., Sharpe T., Vogel J., Andersson L., RA Antczak D.F., Biagi T., Binns M.M., Chowdhary B.P., Coleman S.J., RA Della Valle G., Fryc S., Guerin G., Hasegawa T., Hill E.W., Jurka J., RA Kiialainen A., Lindgren G., Liu J., Magnani E., Mickelson J.R., RA Murray J., Nergadze S.G., Onofrio R., Pedroni S., Piras M.F., RA Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A., Searle S., Skow L., RA Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J., Vaudin M., RA White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.; RT "Genome sequence, comparative analysis, and population genetics of the RT domestic horse."; RL Science 326:865-867(2009). RN [2] {ECO:0000313|Ensembl:ENSECAP00000013444} RP IDENTIFICATION. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000013444}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSECAP00000013444}. 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_001504702.1; XM_001504652.2. DR PRIDE; F6VYL8; -. DR Ensembl; ENSECAT00000016635; ENSECAP00000013444; ENSECAG00000015626. DR GeneID; 100073265; -. DR KEGG; ecb:100073265; -. DR CTD; 635; -. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; F6VYL8; -. DR KO; K00544; -. DR OMA; WGVTKGT; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000002281; Chromosome 14. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006577; P:amino-acid betaine metabolic process; IEA:Ensembl. DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002281}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Reference proteome {ECO:0000313|Proteomes:UP000002281}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 217 217 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 407 AA; 45075 MW; 2588D2541B83B7B2 CRC64; MAPVGGKKAK RGILERLNSG EVVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAVRQLH REFLRAGSNV MQAFTFYASE DKLENRGNYV AEKISGKKVN EAACDIARQV ADEGDALVAG GVSQTPSYLS CKSETEVKKV FEQQLEVFLK KNVDFLIAEY FEHVEEAVWA VEALKASGKP VAATMCIGPE GDLHGVSPGE CAVRLVKAGA SIVGVNCHFD PTISLQTVKL MKEGLEAARL KAHLMSQPLA YHTPDCNKQG FIDLPEFPFG LEPRVTTRWD IQKYAREAYN LGVRYIGGCC GFEPYHIRAI AEELAPERGF LPPASEKHGS WGSGLDMHTK PWIRARARKE YWENLRIASG RPYNPSLSKP DAWGMTKGTS ELMQQKEATT EQQLRELFEK QKFKSAQ // ID F6X4U1_MONDO Unreviewed; 363 AA. AC F6X4U1; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMODP00000024623}; GN Name=BHMT2 {ECO:0000313|Ensembl:ENSMODP00000024623}; OS Monodelphis domestica (Gray short-tailed opossum). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Metatheria; Didelphimorphia; Didelphidae; Monodelphis. OX NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000024623, ECO:0000313|Proteomes:UP000002280}; RN [1] {ECO:0000313|Ensembl:ENSMODP00000024623, ECO:0000313|Proteomes:UP000002280} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17495919; DOI=10.1038/nature05805; RA Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., RA Duke S., Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., RA Kamal M., Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., RA Benos P.V., Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., RA Deakin J.E., Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., RA Gu W., Hore T.A., Huttley G.A., Kleber M., Jirtle R.L., Koina E., RA Lee J.T., Mahony S., Marra M.A., Miller R.D., Nicholls R.D., Oda M., RA Papenfuss A.T., Parra Z.E., Pollock D.D., Ray D.A., Schein J.E., RA Speed T.P., Thompson K., VandeBerg J.L., Wade C.M., Walker J.A., RA Waters P.D., Webber C., Weidman J.R., Xie X., Zody M.C., Baldwin J., RA Abdouelleil A., Abdulkadir J., Abebe A., Abera B., Abreu J., RA Acer S.C., Aftuck L., Alexander A., An P., Anderson E., Anderson S., RA Arachi H., Azer M., Bachantsang P., Barry A., Bayul T., Berlin A., RA Bessette D., Bloom T., Bloom T., Boguslavskiy L., Bonnet C., RA Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S., RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., RA Costello M., D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., RA Dhargay N., Dooley K., Dooley E., Doricent M., Dorje P., Dorjee K., RA Dupes A., Elong R., Falk J., Farina A., Faro S., Ferguson D., RA Fisher S., Foley C.D., Franke A., Friedrich D., Gadbois L., Gearin G., RA Gearin C.R., Giannoukos G., Goode T., Graham J., Grandbois E., RA Grewal S., Gyaltsen K., Hafez N., Hagos B., Hall J., Henson C., RA Hollinger A., Honan T., Huard M.D., Hughes L., Hurhula B., Husby M.E., RA Kamat A., Kanga B., Kashin S., Khazanovich D., Kisner P., Lance K., RA Lara M., Lee W., Lennon N., Letendre F., LeVine R., Lipovsky A., RA Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y., Lubonja R., RA Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C., RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O., RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., RA Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., RA Nicol R., Norbu C., Norbu N., Novod N., O'Neill B., Osman S., RA Markiewicz E., Oyono O.L., Patti C., Phunkhang P., Pierre F., RA Priest M., Raghuraman S., Rege F., Reyes R., Rise C., Rogov P., RA Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L., Shih D., RA Sparrow T., Spaulding J., Stalker J., Stange-Thomann N., RA Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T., RA Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T., RA Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., RA Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A., RA Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C., RA Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M., RA Samollow P.B., Lander E.S., Lindblad-Toh K.; RT "Genome of the marsupial Monodelphis domestica reveals innovation in RT non-coding sequences."; RL Nature 447:167-177(2007). RN [2] {ECO:0000313|Ensembl:ENSMODP00000024623} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSMODP00000024623}. 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_001367524.1; XM_001367487.3. DR Ensembl; ENSMODT00000025059; ENSMODP00000024623; ENSMODG00000025328. DR GeneID; 100019792; -. DR KEGG; mdo:100019792; -. DR CTD; 23743; -. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; F6X4U1; -. DR OMA; PEGDMHD; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000002280; Chromosome 3. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0061627; F:S-methylmethionine-homocysteine S-methyltransferase activity; IEA:Ensembl. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl. DR GO; GO:0046500; P:S-adenosylmethionine metabolic process; IEA:Ensembl. DR GO; GO:0033477; P:S-methylmethionine metabolic process; IEA:Ensembl. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002280}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Reference proteome {ECO:0000313|Proteomes:UP000002280}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 208 208 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 363 AA; 39974 MW; CDF228F53E7FFE96 CRC64; MAPVGGKRAK KGILERLHSG EVVIGDGSFL FTLEKRGYVK AGLWTPEATV EHPEAVRQLH TEYLRAGSNV MQTFTFFAGK DNLESKWKEV NEAACDLARE VAEKGDALVA GGISQTSLYK SHGSEPEIKE NFQLQLEVFT RKNVDFLIAE YFEYCEEAVW AVEVLKGSGK PVAATMCIGP EGDMNNLTPG ECAVRLVKAG ASIVGVNCRF GPEISLATVK LMKEGLEASG LKAYLMVQSL GFHTPDCGKG GFVDLPQYPF GMEPRVATRW DIQKYAREAY KLGVRYIGGC CGFEPYHIRA IAEELAPERG FLPDASEKHG SWGSGLNMHT KPWVRARAQK EYWKNLLPAS GRPYFPSLSK PNA // ID F6X4V0_MONDO Unreviewed; 408 AA. AC F6X4V0; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 2. DT 27-MAY-2015, entry version 30. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMODP00000024622}; GN Name=BHMT {ECO:0000313|Ensembl:ENSMODP00000024622}; OS Monodelphis domestica (Gray short-tailed opossum). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Metatheria; Didelphimorphia; Didelphidae; Monodelphis. OX NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000024622, ECO:0000313|Proteomes:UP000002280}; RN [1] {ECO:0000313|Ensembl:ENSMODP00000024622, ECO:0000313|Proteomes:UP000002280} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17495919; DOI=10.1038/nature05805; RA Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., RA Duke S., Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., RA Kamal M., Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., RA Benos P.V., Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., RA Deakin J.E., Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., RA Gu W., Hore T.A., Huttley G.A., Kleber M., Jirtle R.L., Koina E., RA Lee J.T., Mahony S., Marra M.A., Miller R.D., Nicholls R.D., Oda M., RA Papenfuss A.T., Parra Z.E., Pollock D.D., Ray D.A., Schein J.E., RA Speed T.P., Thompson K., VandeBerg J.L., Wade C.M., Walker J.A., RA Waters P.D., Webber C., Weidman J.R., Xie X., Zody M.C., Baldwin J., RA Abdouelleil A., Abdulkadir J., Abebe A., Abera B., Abreu J., RA Acer S.C., Aftuck L., Alexander A., An P., Anderson E., Anderson S., RA Arachi H., Azer M., Bachantsang P., Barry A., Bayul T., Berlin A., RA Bessette D., Bloom T., Bloom T., Boguslavskiy L., Bonnet C., RA Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S., RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., RA Costello M., D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., RA Dhargay N., Dooley K., Dooley E., Doricent M., Dorje P., Dorjee K., RA Dupes A., Elong R., Falk J., Farina A., Faro S., Ferguson D., RA Fisher S., Foley C.D., Franke A., Friedrich D., Gadbois L., Gearin G., RA Gearin C.R., Giannoukos G., Goode T., Graham J., Grandbois E., RA Grewal S., Gyaltsen K., Hafez N., Hagos B., Hall J., Henson C., RA Hollinger A., Honan T., Huard M.D., Hughes L., Hurhula B., Husby M.E., RA Kamat A., Kanga B., Kashin S., Khazanovich D., Kisner P., Lance K., RA Lara M., Lee W., Lennon N., Letendre F., LeVine R., Lipovsky A., RA Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y., Lubonja R., RA Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C., RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O., RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., RA Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., RA Nicol R., Norbu C., Norbu N., Novod N., O'Neill B., Osman S., RA Markiewicz E., Oyono O.L., Patti C., Phunkhang P., Pierre F., RA Priest M., Raghuraman S., Rege F., Reyes R., Rise C., Rogov P., RA Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L., Shih D., RA Sparrow T., Spaulding J., Stalker J., Stange-Thomann N., RA Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T., RA Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T., RA Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., RA Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A., RA Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C., RA Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M., RA Samollow P.B., Lander E.S., Lindblad-Toh K.; RT "Genome of the marsupial Monodelphis domestica reveals innovation in RT non-coding sequences."; RL Nature 447:167-177(2007). RN [2] {ECO:0000313|Ensembl:ENSMODP00000024622} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSMODP00000024622}. 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_001381586.1; XM_001381549.2. DR ProteinModelPortal; F6X4V0; -. DR Ensembl; ENSMODT00000025058; ENSMODP00000024622; ENSMODG00000019726. DR GeneID; 100032615; -. DR KEGG; mdo:100032615; -. DR CTD; 635; -. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; F6X4V0; -. DR KO; K00544; -. DR OMA; WGVTKGT; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR Proteomes; UP000002280; Chromosome 3. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006577; P:amino-acid betaine metabolic process; IEA:Ensembl. DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002280}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000002280}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 217 217 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 408 AA; 45027 MW; 385460FC02FB14DC CRC64; MVPAGGKKMK KGILQRLDSG EIVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAVRQLH REFLRAGSNV MQTFTFYASE DKLENRGNYV AEKISGQKVN EAACDIALQV AAEGDALVAG GVSQTPSYLS CKSETEVKKI FRQQLTVFMK KNVDFLIAEY FEHVEEAVWA VEALKESGKP VAATMCIGPE GDLHGVTPGE CAVRLVKAGA SIVGVNCHFD PTISLKTVKL MKEGLEAAKL KAYLMTQPLA YHTPDCGKQG FIDLPEFPFG LEPRVATRWD IQKYAREAYK LGVRYIGGCC GFEPYHIRAI AEELAPERGF LPDASEKHGS WGSGLNMHTK PWVRARARRE YWESLPLASG RPYCPSMSKP DAWGVTKGTA ELMQQKEATT DQQLKELFEK QKFKSSVA // ID F6XC87_CIOIN Unreviewed; 256 AA. AC F6XC87; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 2. DT 27-MAY-2015, entry version 24. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCINP00000023732}; DE Flags: Fragment; GN Name=LOC100176817 {ECO:0000313|Ensembl:ENSCINP00000023732}; OS Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis). OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Enterogona; OC Phlebobranchia; Cionidae; Ciona. OX NCBI_TaxID=7719 {ECO:0000313|Ensembl:ENSCINP00000023732, ECO:0000313|Proteomes:UP000008144}; RN [1] {ECO:0000313|Ensembl:ENSCINP00000023732} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12481130; DOI=10.1126/science.1080049; RA Dehal P., Satou Y., Campbell R.K., Chapman J., Degnan B., RA De Tomaso A., Davidson B., Di Gregorio A., Gelpke M., Goodstein D.M., RA Harafuji N., Hastings K.E., Ho I., Hotta K., Huang W., Kawashima T., RA Lemaire P., Martinez D., Meinertzhagen I.A., Necula S., Nonaka M., RA Putnam N., Rash S., Saiga H., Satake M., Terry A., Yamada L., RA Wang H.G., Awazu S., Azumi K., Boore J., Branno M., Chin-Bow S., RA DeSantis R., Doyle S., Francino P., Keys D.N., Haga S., Hayashi H., RA Hino K., Imai K.S., Inaba K., Kano S., Kobayashi K., Kobayashi M., RA Lee B.I., Makabe K.W., Manohar C., Matassi G., Medina M., RA Mochizuki Y., Mount S., Morishita T., Miura S., Nakayama A., RA Nishizaka S., Nomoto H., Ohta F., Oishi K., Rigoutsos I., Sano M., RA Sasaki A., Sasakura Y., Shoguchi E., Shin-i T., Spagnuolo A., RA Stainier D., Suzuki M.M., Tassy O., Takatori N., Tokuoka M., Yagi K., RA Yoshizaki F., Wada S., Zhang C., Hyatt P.D., Larimer F., Detter C., RA Doggett N., Glavina T., Hawkins T., Richardson P., Lucas S., RA Kohara Y., Levine M., Satoh N., Rokhsar D.S.; RT "The draft genome of Ciona intestinalis: insights into chordate and RT vertebrate origins."; RL Science 298:2157-2167(2002). RN [2] {ECO:0000313|Ensembl:ENSCINP00000023732} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSCINP00000023732}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EAAA01000259; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSCINT00000023978; ENSCINP00000023732; ENSCING00000012789. DR GeneTree; ENSGT00510000049619; -. DR InParanoid; F6XC87; -. DR OMA; AINTHNE; -. DR OrthoDB; EOG7GQXW0; -. DR TreeFam; TF313927; -. DR Proteomes; UP000008144; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008144}; KW Reference proteome {ECO:0000313|Proteomes:UP000008144}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSCINP00000023732}. SQ SEQUENCE 256 AA; 28438 MW; BB09109A459BB71B CRC64; LLINCPSKQE KAMEDIKILD GGLCTDLFIN GGFNQKDPLW SARVLYEKPE EIMKAHLRFI KAGSDVVSTC SYQASVQGYM EHAQVTKEKA EKIIGSSVDV AKQAVQESGR RVLVAGSISP YGAILHDMSE YTGSYIDTTS EQQLSDFHKT NIRILASKGV DLFAFETLPS LKEALVLAEI LREYPTLKAW VSFSNKNGTH TCYGEPFEEV FKALGNYHQI IAIGLNCCKS ETISSFIQLA HGNLAKHQRL IIYPNN // ID F6YK88_MACMU Unreviewed; 405 AA. AC F6YK88; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMMUP00000012956}; GN Name=BHMT {ECO:0000313|Ensembl:ENSMMUP00000012956}; OS Macaca mulatta (Rhesus macaque). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000012956, ECO:0000313|Proteomes:UP000006718}; RN [1] {ECO:0000313|Ensembl:ENSMMUP00000012956, ECO:0000313|Proteomes:UP000006718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000012956, RC ECO:0000313|Proteomes:UP000006718}; RX PubMed=17431167; DOI=10.1126/science.1139247; RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M., RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., RA Wilson R.K., Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., RA Hardison R.C., Makova K.D., Miller W., Milosavljevic A., Palermo R.E., RA Siepel A., Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J., RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., RA Dinh H.H., Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., RA Godfrey J., Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., RA Jhangiani S.N., Joshi V., Khan Z.M., Kirkness E.F., Cree A., RA Fowler R.G., Lee S., Lewis L.R., Li Z., Liu Y.-S., Moore S.M., RA Muzny D., Nazareth L.V., Ngo D.N., Okwuonu G.O., Pai G., Parker D., RA Paul H.A., Pfannkoch C., Pohl C.S., Rogers Y.-H.C., Ruiz S.J., RA Sabo A., Santibanez J., Schneider B.W., Smith S.M., Sodergren E., RA Svatek A.F., Utterback T.R., Vattathil S., Warren W., White C.S., RA Chinwalla A.T., Feng Y., Halpern A.L., Hillier L.W., Huang X., RA Minx P., Nelson J.O., Pepin K.H., Qin X., Sutton G.G., Venter E., RA Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P., Jones S.M., RA Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L., Csuros M., RA Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H., Liu Y., RA Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E., RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J., RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J., RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A., RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., RA Denby A., Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., RA Marklein A., Nielsen R., Vallender E.J., Clark A.G., Ferguson B., RA Hernandez R.D., Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., RA Pu L.-L., Ren Y., Smith D.G., Wheeler D.A., Schenck I., Ball E.V., RA Chen R., Cooper D.N., Giardine B., Hsu F., Kent W.J., Lesk A., RA Nelson D.L., O'brien W.E., Pruefer K., Stenson P.D., Wallace J.C., RA Ke H., Liu X.-M., Wang P., Xiang A.P., Yang F., Barber G.P., RA Haussler D., Karolchik D., Kern A.D., Kuhn R.M., Smith K.E., RA Zwieg A.S.; RT "Evolutionary and biomedical insights from the rhesus macaque RT genome."; RL Science 316:222-234(2007). RN [2] {ECO:0000313|Ensembl:ENSMMUP00000012956} RP IDENTIFICATION. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000012956}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSMMUP00000012956}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSMMUT00000013826; ENSMMUP00000012956; ENSMMUG00000009897. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; F6YK88; -. DR OMA; WGVTKGT; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000006718; Chromosome 6. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006577; P:amino-acid betaine metabolic process; IEA:Ensembl. DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006718}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Reference proteome {ECO:0000313|Proteomes:UP000006718}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 216 216 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 298 298 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 405 AA; 45225 MW; 856F47A375D6EB30 CRC64; MPPVGGKKAK KGILERLNAG EIVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAVRQLH REFLRAGSNV MQTFTFYASE DKLENRGNYV LEKISGQKVN EAACDIARQV ADEGDALVAG GVSQTPSYLS CKSETEVKKV FLQQLEVFMK KNVDFLIAEY FEHVEEAVWA VETLIASGKP PDMVAYTCTG PAGLWYIPKA IMFFPLTGAS IIGVNCHFDP TISLQTVKLM KEALEAARLK AHLMSQPLAY HTPDCNKQGF IDLPEFPFGL EPRVATRWDI QKYAREAYNL GVRYIGGCCG FEPYHIRAIA EELAPERGFL PPASEKHGSW GSGLDMHTKP WVRARARKEY WENLRIASGR PYNPSMSKPD GWGVTKGTAE LMQQKEATTE QQLKELFEKQ KFKSQ // ID F7A7C7_HORSE Unreviewed; 1266 AA. AC F7A7C7; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSECAP00000019784}; GN Name=MTR {ECO:0000313|Ensembl:ENSECAP00000019784}; OS Equus caballus (Horse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus. OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000019784, ECO:0000313|Proteomes:UP000002281}; RN [1] {ECO:0000313|Ensembl:ENSECAP00000019784, ECO:0000313|Proteomes:UP000002281} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000019784, RC ECO:0000313|Proteomes:UP000002281}; RX PubMed=19892987; DOI=10.1126/science.1178158; RG Broad Institute Genome Sequencing Platform; RG Broad Institute Whole Genome Assembly Team; RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F., RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., RA Distl O., Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., RA Penedo M.C.T., Raison J.M., Sharpe T., Vogel J., Andersson L., RA Antczak D.F., Biagi T., Binns M.M., Chowdhary B.P., Coleman S.J., RA Della Valle G., Fryc S., Guerin G., Hasegawa T., Hill E.W., Jurka J., RA Kiialainen A., Lindgren G., Liu J., Magnani E., Mickelson J.R., RA Murray J., Nergadze S.G., Onofrio R., Pedroni S., Piras M.F., RA Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A., Searle S., Skow L., RA Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J., Vaudin M., RA White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.; RT "Genome sequence, comparative analysis, and population genetics of the RT domestic horse."; RL Science 326:865-867(2009). RN [2] {ECO:0000313|Ensembl:ENSECAP00000019784} RP IDENTIFICATION. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000019784}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 1}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSECAP00000019784}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSECAT00000023851; ENSECAP00000019784; ENSECAG00000021661. DR GeneTree; ENSGT00420000029824; -. DR InParanoid; F7A7C7; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG7TF786; -. DR TreeFam; TF312829; -. DR Proteomes; UP000002281; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:Ensembl. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002281}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002281}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 260 260 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 786 786 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1266 AA; 140546 MW; D8357B4D24EAFC48 CRC64; MSPALRDLTP SAGMKKTLQD EIEAILQEKI MVLDGGMGTM IQRLKLSEDD FRGQEFGDHA RPLKGNNDIL SITKPDVIYQ IHKDYLLAGA DIIETNTFSS TSIAQADYGL ERLAYQMNKC SAGVARKAAE EITLQTGIKR FVAGALGPTN KTLSVSPSVE RPDYRNITFD ELVEAYKEQA EGLLDGGVDI LLVETIFDTA NAKAALFAIQ NLFEEKYAPR PIFISGTIVD KSGRTLSGQT GEAFVISVSH ADPLCIGLNC ALGAAEMRPF IETIGKCTTA YVLCYPNAGL PNTFGDYDET PHMMAMHLKD FAADGLVNIV GGCCGTTPDH IREIAEAVKK YKPRVPPATV FEGHMLLSGL EPFRIGPYTN FVNIGERCNV AGSRKFAKLI MAGNYEEALS IAKVQVEMGA QVLDINMDDG MLDGPSAMTR FCNFIASEPD IAKVPLCIDS SNFAVIEAGL KCCQGKCIVN SISLKEGEDD FLEKARKIKK FGAAVVVMAF DEEGQATETD TKTRVCTRAY HLLVKKLGFN PNDIIFDPNI LTIGTGMEEH NLYAVNFIHA TKAIKETLPG AKISGGLSNL SFSFREMEAI REAMHGVFLS HATKFGMDMG IVNAGLPVYD DIHKDLLQLC EDLIWNKDPE ATEKLLRYAQ THGKGGKKVI QTDEWRNGPI EERLEYALVK GIEKYIIEDT EEARLNQEKY PRPLNIIEGP LMNGMKVVGD LFGAGKMFLP QVIKSARVMK KAVGHLIPFM EKEREETRVL TGAVEEEASD PYHGTIVLAT VKGDVHDIGK NIVGVVLGCN NFRVIDLGVM TPCDKILKAA LDHKADIIGL SGLITPSLDE MIFVAKEMER LAIKIPLLIG GATTSRTHTA VKIAPRYSAP VIHVLDASKS VVVCSQLLDE NLKDEYFEEI MEEYEDIRQD HYESLKERRY LTLSQARKNG FHIDWLSEPP PVTPTFLGTR VFEDYDLQKL VDYIDWKPFF DVWQLRGKYP NRGFPKIFND KTVGEEAKRV YDDAQNMLKA LISQKKLQAR GVVGFWPAQS VQDDICLYAE DAEPQSAEPI ATFYGLRQQA EKDSASTDPY HCLSDFIAPL HSGIRDYLGL FAVACFGVEE LSKTYEGECD DYSSIMVKAL GDRLAEAFAE ELHERVRREL WAYCGSEQLD IADLRRLRYE GIRPAPGYPS QPDHTEKLTM WRLADIERCT GIRLTESLAM APASAVSGLY FSNLKSKYFS VGKISKDQIE DYALRKNMSV AEVEKWLGPI LGYDTD // ID F7AGD8_XENTR Unreviewed; 406 AA. AC F7AGD8; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Betaine--homocysteine S-methyltransferase 1 {ECO:0000313|Ensembl:ENSXETP00000059123}; GN Name=bhmt {ECO:0000313|Ensembl:ENSXETP00000059123}; OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; OC Silurana. OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000059123, ECO:0000313|Proteomes:UP000008143}; RN [1] {ECO:0000313|Ensembl:ENSXETP00000059123} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20431018; DOI=10.1126/science.1183670; RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J., RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., RA Blitz I.L., Blumberg B., Dichmann D.S., Dubchak I., Amaya E., RA Detter J.C., Fletcher R., Gerhard D.S., Goodstein D., Graves T., RA Grigoriev I.V., Grimwood J., Kawashima T., Lindquist E., Lucas S.M., RA Mead P.E., Mitros T., Ogino H., Ohta Y., Poliakov A.V., Pollet N., RA Robert J., Salamov A., Sater A.K., Schmutz J., Terry A., Vize P.D., RA Warren W.C., Wells D., Wills A., Wilson R.K., Zimmerman L.B., RA Zorn A.M., Grainger R., Grammer T., Khokha M.K., Richardson P.M., RA Rokhsar D.S.; RT "The genome of the Western clawed frog Xenopus tropicalis."; RL Science 328:633-636(2010). RN [2] {ECO:0000313|Ensembl:ENSXETP00000059123} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2011) to UniProtKB. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSXETP00000059123}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAMC01100977; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSXETT00000063814; ENSXETP00000059123; ENSXETG00000000523. DR Xenbase; XB-GENE-1008382; bhmt. DR GeneTree; ENSGT00390000003122; -. DR OMA; WGVTKGT; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000008143; Unassembled WGS sequence. DR Bgee; F7AGD8; -. DR ExpressionAtlas; F7AGD8; baseline. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008143}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Reference proteome {ECO:0000313|Proteomes:UP000008143}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 217 217 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 406 AA; 44524 MW; CC2D9059129B4D3F CRC64; MAPTGAKKLK EGLLERLDAG EVVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAVRQLH REFLRAGANV MQTFTFYASD DKLENRGNYV AKKISGQKVN EAACDIAREV ANEGDALVAG GVSQTPSYLS CKSEVEVKGI FRKQLDVFIK KNVDFLIAEY FEHVEEAVWA VEVLKESGKP VAATLCIGPQ GDLNGVTPGE CAVRLAKAGA SVVGVNCHFD PMTCIATVKL MKEGLVAAKV KAHLMTQPLA YHTPDCGKQG FIDLPEFPFA LEPRIVTRWD IHKYAREAYN LGVRYIGGCC GFEPYHTRAI AEELAPERGF LPPGSEKHGS WGSGLEMHTK PWVRARARRD YWEKLPPASG RPCCPSMSKP DAWGVTKGDA DLMQQKEATT EQQLIDLFAK QCIKSN // ID F7ASM4_HORSE Unreviewed; 353 AA. AC F7ASM4; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSECAP00000016031}; DE Flags: Fragment; GN Name=BHMT2 {ECO:0000313|Ensembl:ENSECAP00000016031}; OS Equus caballus (Horse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus. OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000016031, ECO:0000313|Proteomes:UP000002281}; RN [1] {ECO:0000313|Ensembl:ENSECAP00000016031, ECO:0000313|Proteomes:UP000002281} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000016031, RC ECO:0000313|Proteomes:UP000002281}; RX PubMed=19892987; DOI=10.1126/science.1178158; RG Broad Institute Genome Sequencing Platform; RG Broad Institute Whole Genome Assembly Team; RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F., RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., RA Distl O., Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., RA Penedo M.C.T., Raison J.M., Sharpe T., Vogel J., Andersson L., RA Antczak D.F., Biagi T., Binns M.M., Chowdhary B.P., Coleman S.J., RA Della Valle G., Fryc S., Guerin G., Hasegawa T., Hill E.W., Jurka J., RA Kiialainen A., Lindgren G., Liu J., Magnani E., Mickelson J.R., RA Murray J., Nergadze S.G., Onofrio R., Pedroni S., Piras M.F., RA Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A., Searle S., Skow L., RA Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J., Vaudin M., RA White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.; RT "Genome sequence, comparative analysis, and population genetics of the RT domestic horse."; RL Science 326:865-867(2009). RN [2] {ECO:0000313|Ensembl:ENSECAP00000016031} RP IDENTIFICATION. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000016031}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSECAP00000016031}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSECAT00000019579; ENSECAP00000016031; ENSECAG00000018440. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; F7ASM4; -. DR OMA; PEGDMHD; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR Proteomes; UP000002281; Chromosome 14. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0061627; F:S-methylmethionine-homocysteine S-methyltransferase activity; IEA:Ensembl. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl. DR GO; GO:0046500; P:S-adenosylmethionine metabolic process; IEA:Ensembl. DR GO; GO:0033477; P:S-methylmethionine metabolic process; IEA:Ensembl. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002281}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000002281}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 198 198 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 280 280 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 281 281 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSECAP00000016031}. SQ SEQUENCE 353 AA; 38925 MW; DA2619FD8D205190 CRC64; QGILERLESG EVVVGDGSFL ITLEKRGCVK AGLWTPEAVA EHPDAVRQLH MEFLRAGSNV MQTFTFSASE ENMESKWEEV NAAACDLARE VAGKGDALVA GGICQTSMYK HLKDEARIKK LFRQQLEVFA RKNVDFLIAE YFEHAEEAVW AVEVLKESGK PVAATMCIGP EGDMRDVPPG ECAAKLVRAG AAIVGVNCRF GPRTSLKTMT LMKEGLQAAG LTAHLMVQSL GFHTPDCGKG GFVDLPEYPF ALEPRLATRW DIQNYAREAY NLGVRYIGGC CGFEPYHIRA IAEELAPERG FWPPASDKHG SWGSGLNMHT KPWIRARARR EYWENLLPAS GRPFCPPLSK PDA // ID F7AUB9_CIOIN Unreviewed; 364 AA. AC F7AUB9; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 2. DT 27-MAY-2015, entry version 28. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCINP00000023368}; DE Flags: Fragment; GN Name=LOC100179692 {ECO:0000313|Ensembl:ENSCINP00000023368}; OS Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis). OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Enterogona; OC Phlebobranchia; Cionidae; Ciona. OX NCBI_TaxID=7719 {ECO:0000313|Ensembl:ENSCINP00000023368, ECO:0000313|Proteomes:UP000008144}; RN [1] {ECO:0000313|Ensembl:ENSCINP00000023368} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12481130; DOI=10.1126/science.1080049; RA Dehal P., Satou Y., Campbell R.K., Chapman J., Degnan B., RA De Tomaso A., Davidson B., Di Gregorio A., Gelpke M., Goodstein D.M., RA Harafuji N., Hastings K.E., Ho I., Hotta K., Huang W., Kawashima T., RA Lemaire P., Martinez D., Meinertzhagen I.A., Necula S., Nonaka M., RA Putnam N., Rash S., Saiga H., Satake M., Terry A., Yamada L., RA Wang H.G., Awazu S., Azumi K., Boore J., Branno M., Chin-Bow S., RA DeSantis R., Doyle S., Francino P., Keys D.N., Haga S., Hayashi H., RA Hino K., Imai K.S., Inaba K., Kano S., Kobayashi K., Kobayashi M., RA Lee B.I., Makabe K.W., Manohar C., Matassi G., Medina M., RA Mochizuki Y., Mount S., Morishita T., Miura S., Nakayama A., RA Nishizaka S., Nomoto H., Ohta F., Oishi K., Rigoutsos I., Sano M., RA Sasaki A., Sasakura Y., Shoguchi E., Shin-i T., Spagnuolo A., RA Stainier D., Suzuki M.M., Tassy O., Takatori N., Tokuoka M., Yagi K., RA Yoshizaki F., Wada S., Zhang C., Hyatt P.D., Larimer F., Detter C., RA Doggett N., Glavina T., Hawkins T., Richardson P., Lucas S., RA Kohara Y., Levine M., Satoh N., Rokhsar D.S.; RT "The draft genome of Ciona intestinalis: insights into chordate and RT vertebrate origins."; RL Science 298:2157-2167(2002). RN [2] {ECO:0000313|Ensembl:ENSCINP00000023368} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSCINP00000023368}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EAAA01000348; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSCINT00000023614; ENSCINP00000023368; ENSCING00000012545. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; F7AUB9; -. DR OMA; VGINCHL; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR Proteomes; UP000008144; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008144}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000008144}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 209 209 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSCINP00000023368}. SQ SEQUENCE 364 AA; 40166 MW; D186CEA0F2E8AD14 CRC64; KKGLLERLKE GPVVGDGSMC MTLEKRGYCR AGQWTPEAVL EYPDAVKQLL REYLRAGADV LQTPCYASSD GRLKRGNIIY TKKSQTSEIN EAACEIAHEI AQEGNALVCG GLTPVVSYSK GKDETIVKGE FEGQLAGFIK RKDIIDFILA EFFGHVEELE ICVDVMKKAK LPIACTMKLG PIGDLNGVSV EECAVRMAKT GAVLIGINCL FDLDTCLKTL KRMRDALDKE GLKTPLMCQP LGWRCPETAN MKKGYLMLPE FPFALESRQV TRFEVHKFAR EAYNLGAHYI GGCCGMEPHH IRAIAQELAA ERKLDPPVQG TCPPLGYLHN ALSLRKEKLK KEFWMSLKAG SGAPFNAACV EPYA // ID F7BDU0_CIOIN Unreviewed; 385 AA. AC F7BDU0; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 2. DT 27-MAY-2015, entry version 30. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCINP00000023324}; DE Flags: Fragment; GN Name=LOC100181849 {ECO:0000313|Ensembl:ENSCINP00000023324}; OS Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis). OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Enterogona; OC Phlebobranchia; Cionidae; Ciona. OX NCBI_TaxID=7719 {ECO:0000313|Ensembl:ENSCINP00000023324, ECO:0000313|Proteomes:UP000008144}; RN [1] {ECO:0000313|Ensembl:ENSCINP00000023324} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12481130; DOI=10.1126/science.1080049; RA Dehal P., Satou Y., Campbell R.K., Chapman J., Degnan B., RA De Tomaso A., Davidson B., Di Gregorio A., Gelpke M., Goodstein D.M., RA Harafuji N., Hastings K.E., Ho I., Hotta K., Huang W., Kawashima T., RA Lemaire P., Martinez D., Meinertzhagen I.A., Necula S., Nonaka M., RA Putnam N., Rash S., Saiga H., Satake M., Terry A., Yamada L., RA Wang H.G., Awazu S., Azumi K., Boore J., Branno M., Chin-Bow S., RA DeSantis R., Doyle S., Francino P., Keys D.N., Haga S., Hayashi H., RA Hino K., Imai K.S., Inaba K., Kano S., Kobayashi K., Kobayashi M., RA Lee B.I., Makabe K.W., Manohar C., Matassi G., Medina M., RA Mochizuki Y., Mount S., Morishita T., Miura S., Nakayama A., RA Nishizaka S., Nomoto H., Ohta F., Oishi K., Rigoutsos I., Sano M., RA Sasaki A., Sasakura Y., Shoguchi E., Shin-i T., Spagnuolo A., RA Stainier D., Suzuki M.M., Tassy O., Takatori N., Tokuoka M., Yagi K., RA Yoshizaki F., Wada S., Zhang C., Hyatt P.D., Larimer F., Detter C., RA Doggett N., Glavina T., Hawkins T., Richardson P., Lucas S., RA Kohara Y., Levine M., Satoh N., Rokhsar D.S.; RT "The draft genome of Ciona intestinalis: insights into chordate and RT vertebrate origins."; RL Science 298:2157-2167(2002). RN [2] {ECO:0000313|Ensembl:ENSCINP00000023324} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSCINP00000023324}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EAAA01001798; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSCINT00000023570; ENSCINP00000023324; ENSCING00000012516. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; F7BDU0; -. DR OMA; CKELNER; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR Proteomes; UP000008144; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008144}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000008144}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 218 218 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 302 302 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSCINP00000023324}. SQ SEQUENCE 385 AA; 43036 MW; 98647502626AFBB0 CRC64; WSWLQKMTET SGILQKLSKG PVVGDGSVLL TLEKRGYCRA GAWTPEAVIK YPEAVRQLLR EFVRAGADAI QAPCFNFTEG SWKTNKQNER KQQQYSVEEI NKAACIMAKE VASEGGALVY ASIGPVSSFV RGENEKETKQ SFEKLLKLYL KHKVDYFVAE YFAHIEELEI CVEVLKRGNL PVACTMRIGP TGDLNGVSVE ECAIRMAKTG ADIIGINCLY DPVVALKTMQ RIKSAVDKAG LSPYLMCQPL GWMCPEVEHH KMGHLALHEF PFALDSRSVN RFEFGQFARK AFELGVKYIG GCCGTEPHHI RAIAQELQPE RGIDPPVNDM CPQLGFFADA SLSNYKKKYC RSEADYWKKL VPGTGRMFGP PLSYGFQKPT VWVKS // ID F7BIR6_CIOIN Unreviewed; 191 AA. AC F7BIR6; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 2. DT 27-MAY-2015, entry version 22. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCINP00000017966}; GN Name=Cin.44670 {ECO:0000313|Ensembl:ENSCINP00000017966}; OS Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis). OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Enterogona; OC Phlebobranchia; Cionidae; Ciona. OX NCBI_TaxID=7719 {ECO:0000313|Ensembl:ENSCINP00000017966, ECO:0000313|Proteomes:UP000008144}; RN [1] {ECO:0000313|Ensembl:ENSCINP00000017966} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12481130; DOI=10.1126/science.1080049; RA Dehal P., Satou Y., Campbell R.K., Chapman J., Degnan B., RA De Tomaso A., Davidson B., Di Gregorio A., Gelpke M., Goodstein D.M., RA Harafuji N., Hastings K.E., Ho I., Hotta K., Huang W., Kawashima T., RA Lemaire P., Martinez D., Meinertzhagen I.A., Necula S., Nonaka M., RA Putnam N., Rash S., Saiga H., Satake M., Terry A., Yamada L., RA Wang H.G., Awazu S., Azumi K., Boore J., Branno M., Chin-Bow S., RA DeSantis R., Doyle S., Francino P., Keys D.N., Haga S., Hayashi H., RA Hino K., Imai K.S., Inaba K., Kano S., Kobayashi K., Kobayashi M., RA Lee B.I., Makabe K.W., Manohar C., Matassi G., Medina M., RA Mochizuki Y., Mount S., Morishita T., Miura S., Nakayama A., RA Nishizaka S., Nomoto H., Ohta F., Oishi K., Rigoutsos I., Sano M., RA Sasaki A., Sasakura Y., Shoguchi E., Shin-i T., Spagnuolo A., RA Stainier D., Suzuki M.M., Tassy O., Takatori N., Tokuoka M., Yagi K., RA Yoshizaki F., Wada S., Zhang C., Hyatt P.D., Larimer F., Detter C., RA Doggett N., Glavina T., Hawkins T., Richardson P., Lucas S., RA Kohara Y., Levine M., Satoh N., Rokhsar D.S.; RT "The draft genome of Ciona intestinalis: insights into chordate and RT vertebrate origins."; RL Science 298:2157-2167(2002). RN [2] {ECO:0000313|Ensembl:ENSCINP00000017966} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSCINP00000017966}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EAAA01002021; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSCINT00000017966; ENSCINP00000017966; ENSCING00000008828. DR GeneTree; ENSGT00420000029824; -. DR InParanoid; F7BIR6; -. DR OMA; EVANEFT; -. DR OrthoDB; EOG7TF786; -. DR Proteomes; UP000008144; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008144}; KW Reference proteome {ECO:0000313|Proteomes:UP000008144}. SQ SEQUENCE 191 AA; 21032 MW; 222B5A2A2655CAA1 CRC64; MAGLATYSEI ESTLQKRIMI FDGGMGTMIQ NLRLEEEDFC GDRFKDHSKP LKGNNDLLSL TKPESIYEIH KAYLEAGADF IETNTFSGTS IAQADYALEH VVYELNYESA KIAKRAARDV SNATGVKRYV AGSVGPTNKT LSVSPSVEKP EYRNITFDEL VTSYSEQVRG LLDGGADVLL VETIFDTANA K // ID F7BQK3_HORSE Unreviewed; 1245 AA. AC F7BQK3; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 01-APR-2015, entry version 25. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSECAP00000019867}; GN Name=MTR {ECO:0000313|Ensembl:ENSECAP00000019867}; OS Equus caballus (Horse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus. OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000019867, ECO:0000313|Proteomes:UP000002281}; RN [1] {ECO:0000313|Ensembl:ENSECAP00000019867, ECO:0000313|Proteomes:UP000002281} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000019867, RC ECO:0000313|Proteomes:UP000002281}; RX PubMed=19892987; DOI=10.1126/science.1178158; RG Broad Institute Genome Sequencing Platform; RG Broad Institute Whole Genome Assembly Team; RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F., RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., RA Distl O., Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., RA Penedo M.C.T., Raison J.M., Sharpe T., Vogel J., Andersson L., RA Antczak D.F., Biagi T., Binns M.M., Chowdhary B.P., Coleman S.J., RA Della Valle G., Fryc S., Guerin G., Hasegawa T., Hill E.W., Jurka J., RA Kiialainen A., Lindgren G., Liu J., Magnani E., Mickelson J.R., RA Murray J., Nergadze S.G., Onofrio R., Pedroni S., Piras M.F., RA Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A., Searle S., Skow L., RA Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J., Vaudin M., RA White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.; RT "Genome sequence, comparative analysis, and population genetics of the RT domestic horse."; RL Science 326:865-867(2009). RN [2] {ECO:0000313|Ensembl:ENSECAP00000019867} RP IDENTIFICATION. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000019867}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 1}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSECAP00000019867}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSECAT00000023943; ENSECAP00000019867; ENSECAG00000021661. DR GeneTree; ENSGT00420000029824; -. DR Proteomes; UP000002281; Chromosome 1. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002281}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002281}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 773 773 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1245 AA; 138364 MW; B128C1DC2B7B0823 CRC64; MKKTLQDEIE AILQEKIMVL DGGMGTMIQR LKLSEDDFRG QEFGDHARPL KGNNDILSIT KPDVIYQIHK DYLLAGADII ETNTFSSTSI AQADYGLERL AYQMNKCSAG VARKAAEEIT LQTGIKRFVA GALGPTNKTL SVSPSVERPD YRNITFDELV EAYKEQAEGL LDGGVDILLV ETIFDTANAK AALFAIQNLF EEKYAPRPIF ISGTIVDKSG RTLSGQTGEA FVISVSHADP LCIGLNCALG AAEMRPFIET IGKCTTAYVL CYPNAGLPNT FGDYDETPHM MAMHLKDFAA DGLVNIVGGC CGTTPDHIRE IAEAVKKYKP RVPPATVFEG HMLLSGLEPF RIGPYTNFVN IGERCNVAGS RKFAKLIMAG NYEEALSIAK VQVEMGAQVL DINMDDGMLD GPSAMTRFCN FIASEPDIAK VPLCIDSSNF AVIEAGLKCC QGKCIVNSIS LKEGEDDFLE KARKIKKFGA AVVVMAFDEE GQATETDTKT RVCTRAYHLL VKKLGFNPND IIFDPNILTI GTGMEEHNLY AVNFIHATKA IKETLPGAKI SGGLSNLSFS FREMEAIREA MHGVFLSHAT KFGMDMGIVN AGLPVYDDIH KDLLQLCEDL IWNKDPEATE KLLRYAQTHG KGGKKVIQTD EWRNGPIEER LEYALVKGIE KYIIEDTEEA RLNQEKYPRP LNIIEGPLMN GMKVVGDLFG AGKMFLPQVI KSARVMKKAV GHLIPFMEKE REETRVLTGA VEEEASDPYH GTIVLATVKG DVHDIGKNIV GVVLGCNNFR VIDLGVMTPC DKILKAALDH KADIIGLSGL ITPSLDEMIF VAKEMERLAI KIPLLIGGAT TSRTHTAVKI APRYSAPVIH VLDASKSVVV CSQLLDENLK DEYFEEIMEE YEDIRQDHYE SLKERRYLTL SQARKNGFHI DWLSEPPPVT PTFLGTRVFE DYDLQKLVDY IDWKPFFDVW QLRGKYPNRG FPKIFNDKTV GEEAKRVYDD AQNMLKALIS QKKLQARGSV QDDICLYAED AEPQSAEPIA TFYGLRQQAE KDSASTDPYH CLSDFIAPLH SGIRDYLGLF AVACFGVEEL SKTYEGECDD YSSIMVKALG DRLAEAFAEE LHERVRRELW AYCGSEQLDI ADLRRLRYEG IRPAPGYPSQ PDHTEKLTMW RLADIERCTG IRLTESLAMA PASAVSGLYF SNLKSKYFSV GKISKDQIED YALRKNMSVA EVEKWLGPIL GYDTD // ID F7CB89_XENTR Unreviewed; 307 AA. AC F7CB89; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSXETP00000054282}; GN Name=MGC75760 {ECO:0000313|Ensembl:ENSXETP00000054282}; OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; OC Silurana. OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000054282, ECO:0000313|Proteomes:UP000008143}; RN [1] {ECO:0000313|Ensembl:ENSXETP00000054282} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20431018; DOI=10.1126/science.1183670; RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J., RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., RA Blitz I.L., Blumberg B., Dichmann D.S., Dubchak I., Amaya E., RA Detter J.C., Fletcher R., Gerhard D.S., Goodstein D., Graves T., RA Grigoriev I.V., Grimwood J., Kawashima T., Lindquist E., Lucas S.M., RA Mead P.E., Mitros T., Ogino H., Ohta Y., Poliakov A.V., Pollet N., RA Robert J., Salamov A., Sater A.K., Schmutz J., Terry A., Vize P.D., RA Warren W.C., Wells D., Wills A., Wilson R.K., Zimmerman L.B., RA Zorn A.M., Grainger R., Grammer T., Khokha M.K., Richardson P.M., RA Rokhsar D.S.; RT "The genome of the Western clawed frog Xenopus tropicalis."; RL Science 328:633-636(2010). RN [2] {ECO:0000313|Ensembl:ENSXETP00000054282} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2011) to UniProtKB. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSXETP00000054282}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAMC01018292; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01018293; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; F7CB89; -. DR Ensembl; ENSXETT00000054282; ENSXETP00000054282; ENSXETG00000025468. DR GeneTree; ENSGT00510000049619; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000008143; Unassembled WGS sequence. DR Bgee; F7CB89; -. DR ExpressionAtlas; F7CB89; baseline. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008143}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Reference proteome {ECO:0000313|Proteomes:UP000008143}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 307 AA; 33314 MW; C1174DA4ED8B7D6F CRC64; MAEAVKILSG GLSTELENSG FLLQGDPLWS ARLLQTNPQA IKNVHTSFLK SGAEVLSTAT YQASVKGFQE HLGLSIDEVA ELFHVGVRLA KEAAAEIKDN RNILIAGSIG PYGAFLSDGS EYTGNYLRNM SVEELKDWHR LQMQCLASAG IELFALETIP GQKEAEALLE LLREFPNTNA WLSYSCRDMS STSYGDAFEK AVGIAHKSKQ LVAVGMNCCP PTFVSSLLTS ANKNRGLDIG WIVYPNSGKI WDHNLGWQGG GTEKTLSEYA LEWVNLGAKW IGGCCTTTPS AIATLLHTLR PHAADLH // ID F7CB95_XENTR Unreviewed; 318 AA. AC F7CB95; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSXETP00000054280}; DE Flags: Fragment; GN Name=MGC75760 {ECO:0000313|Ensembl:ENSXETP00000054280}; OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; OC Silurana. OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000054280, ECO:0000313|Proteomes:UP000008143}; RN [1] {ECO:0000313|Ensembl:ENSXETP00000054280} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20431018; DOI=10.1126/science.1183670; RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J., RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., RA Blitz I.L., Blumberg B., Dichmann D.S., Dubchak I., Amaya E., RA Detter J.C., Fletcher R., Gerhard D.S., Goodstein D., Graves T., RA Grigoriev I.V., Grimwood J., Kawashima T., Lindquist E., Lucas S.M., RA Mead P.E., Mitros T., Ogino H., Ohta Y., Poliakov A.V., Pollet N., RA Robert J., Salamov A., Sater A.K., Schmutz J., Terry A., Vize P.D., RA Warren W.C., Wells D., Wills A., Wilson R.K., Zimmerman L.B., RA Zorn A.M., Grainger R., Grammer T., Khokha M.K., Richardson P.M., RA Rokhsar D.S.; RT "The genome of the Western clawed frog Xenopus tropicalis."; RL Science 328:633-636(2010). RN [2] {ECO:0000313|Ensembl:ENSXETP00000054280} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2011) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSXETP00000054280}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAMC01018292; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01018293; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSXETT00000054280; ENSXETP00000054280; ENSXETG00000025468. DR GeneTree; ENSGT00510000049619; -. DR InParanoid; F7CB95; -. DR OMA; SYIGKWR; -. DR OrthoDB; EOG7GQXW0; -. DR TreeFam; TF313927; -. DR Proteomes; UP000008143; Unassembled WGS sequence. DR Bgee; F7CB95; -. DR ExpressionAtlas; F7CB95; baseline. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008143}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000008143}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 296 296 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSXETP00000054280}. SQ SEQUENCE 318 AA; 34436 MW; 1C49E4951CB3D3A9 CRC64; NIKIMAEAVK ILSGGLSTEL ENSGFLLQGD PLWSARLLQT NPQAIKNVHT SFLKSGAEVL STATYQASVK GFQEHLGLSI DEVAELFHVG VRLAKEAAAE IKGNQGPLSD NRNILIAGSI GPYGAFLSDG SEYTGNYLRN MSVEELKDWH RLQMQCLASA GIELFALETI PGQKEAEALL ELLREFPNTN AWLSYSCRDM SSTSYGDAFE KAVGIAHKSK QLVAVGMNCC PPTFVSSLLT SANKNRGLDI GWIVYPNSGK IWDHNLGWQG GGTEKTLSEY ALEWVNLGAK WIGGCCTTTP SAIATLLHTL RPHAADLH // ID F7DB09_MONDO Unreviewed; 1263 AA. AC F7DB09; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 2. DT 27-MAY-2015, entry version 31. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMODP00000009254}; GN Name=MTR {ECO:0000313|Ensembl:ENSMODP00000009254}; OS Monodelphis domestica (Gray short-tailed opossum). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Metatheria; Didelphimorphia; Didelphidae; Monodelphis. OX NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000009254, ECO:0000313|Proteomes:UP000002280}; RN [1] {ECO:0000313|Ensembl:ENSMODP00000009254, ECO:0000313|Proteomes:UP000002280} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17495919; DOI=10.1038/nature05805; RA Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., RA Duke S., Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., RA Kamal M., Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., RA Benos P.V., Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., RA Deakin J.E., Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., RA Gu W., Hore T.A., Huttley G.A., Kleber M., Jirtle R.L., Koina E., RA Lee J.T., Mahony S., Marra M.A., Miller R.D., Nicholls R.D., Oda M., RA Papenfuss A.T., Parra Z.E., Pollock D.D., Ray D.A., Schein J.E., RA Speed T.P., Thompson K., VandeBerg J.L., Wade C.M., Walker J.A., RA Waters P.D., Webber C., Weidman J.R., Xie X., Zody M.C., Baldwin J., RA Abdouelleil A., Abdulkadir J., Abebe A., Abera B., Abreu J., RA Acer S.C., Aftuck L., Alexander A., An P., Anderson E., Anderson S., RA Arachi H., Azer M., Bachantsang P., Barry A., Bayul T., Berlin A., RA Bessette D., Bloom T., Bloom T., Boguslavskiy L., Bonnet C., RA Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S., RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., RA Costello M., D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., RA Dhargay N., Dooley K., Dooley E., Doricent M., Dorje P., Dorjee K., RA Dupes A., Elong R., Falk J., Farina A., Faro S., Ferguson D., RA Fisher S., Foley C.D., Franke A., Friedrich D., Gadbois L., Gearin G., RA Gearin C.R., Giannoukos G., Goode T., Graham J., Grandbois E., RA Grewal S., Gyaltsen K., Hafez N., Hagos B., Hall J., Henson C., RA Hollinger A., Honan T., Huard M.D., Hughes L., Hurhula B., Husby M.E., RA Kamat A., Kanga B., Kashin S., Khazanovich D., Kisner P., Lance K., RA Lara M., Lee W., Lennon N., Letendre F., LeVine R., Lipovsky A., RA Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y., Lubonja R., RA Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C., RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O., RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., RA Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., RA Nicol R., Norbu C., Norbu N., Novod N., O'Neill B., Osman S., RA Markiewicz E., Oyono O.L., Patti C., Phunkhang P., Pierre F., RA Priest M., Raghuraman S., Rege F., Reyes R., Rise C., Rogov P., RA Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L., Shih D., RA Sparrow T., Spaulding J., Stalker J., Stange-Thomann N., RA Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T., RA Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T., RA Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., RA Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A., RA Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C., RA Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M., RA Samollow P.B., Lander E.S., Lindblad-Toh K.; RT "Genome of the marsupial Monodelphis domestica reveals innovation in RT non-coding sequences."; RL Nature 447:167-177(2007). RN [2] {ECO:0000313|Ensembl:ENSMODP00000009254} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 1}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSMODP00000009254}. 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_001378323.1; XM_001378286.2. DR Ensembl; ENSMODT00000009435; ENSMODP00000009254; ENSMODG00000007459. DR GeneID; 100028236; -. DR KEGG; mdo:100028236; -. DR CTD; 4548; -. DR GeneTree; ENSGT00420000029824; -. DR InParanoid; F7DB09; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG7TF786; -. DR TreeFam; TF312829; -. DR Proteomes; UP000002280; Chromosome 2. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:Ensembl. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002280}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002280}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 258 258 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 783 783 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1263 AA; 140235 MW; 3F05C7221C63EA15 CRC64; MPPTLEGQQP PGKKIPKYDI EAILQQRIMV LDGGMGTMIQ RYTLTEEDFR GQDLKNHAKP LKGNNDLLSI TRPDIICNIH KEYLMAGADI IETNTFSSTR VAQADYGLEH LAYRLNKCSA EVARKAADDV TSQTGIKRFV AGSMGPTNKT LSVSPSVERP DYRNITFDEL VEAYQEQARG LLDGGVDILL VETIFDTANA KAALFALQKL FEEGYDPRPI FVSGTIVDKS GRTLSGQTGE AFVISVSHAE PLCLGLNCAL GALEMRPFIE TLGKCTSAYV LCYPNAGLPN TFGEYDETPE MTAMHIKNFA LDGLVNVVGG CCGTTPAHIR EIVEAVKNCK PRVPPASISE GYMLLSGLEP FRIGPYTNFV NIGERCNVAG SRKFAKLIMA GNYEEALSVA KAQVEMGAQV LDVNMDDGML DGPSAMTRFC NFIASEPDIA KVPLCIDSSN FAVIEAGLKC CQGKCIVNSI SLKEGEDDFL EKARKIKKYG AAVVVMAFDE VGQATETNNK IEVCTRAYHL LVKKVGFNPN DIIFDPNILT IGTGMEEHNL YAVNFINAIK TIKATLPGAK ISGGLSNLSF SFRGMEAIRE AMHGVFLYHA IKFGMDMGIV NAGSLPVYDD IHKDLLQLCE DLIWNKDPEA TEKLLRYAQT HGTGGKKAIQ TDEWRNGPVE ERLEYALVKG IEKHIVEDTE EARMKKDKYP RPLNIIEGPL MNGMKVVGDL FGAGKMFLPQ VIKSARVMKK AVGYLIPFME KEREEARALT GSVEEEDPYQ GTIVLATVKG DVHDIGKNIV GVVLGCNNFR VIDLGVMTPC DKILRAALDN KADIIGLSGL ITPSLDEMIF VAKEMERLDI KIPLLIGGAT TSRTHTAVKI APRYSAPVIH VLDASKSVVV CSQLLDENLK DDFFEEIIEE YEDIRQDHYE SLKERRYLTL DQARKKGFHV DWLSEPPPVK PKFFGTQVFE DYDLQRLVDY IDWKPFFDVW QLRGKYPNRG FPKIFNDKTV GEEAKKVYDD AQTMLKELIS KKKIQARGLV GFWPAQSVQD DIHLYAEDAI PQSAEPVAKF YGLRQQAEKD SASTDPYYCL SDFIAPLESG IRDYLGLFAV ACFGVDELSK AYEEQYDVYS SIMAKALGDR LAEAFAEELH ERVRKDLWAY SGSEQLDVAD LRRIRYGGIR PAPGYPSQPD HTEKLTMWRL GHIEETTGIT LTESLAMAPA SAVSGLYFAN LKSKYFSVGK ISRDQIEDYA LRKNMSVDEV ERWLGPILGY DAD // ID F7DS96_ORNAN Unreviewed; 365 AA. AC F7DS96; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSOANP00000012575}; DE Flags: Fragment; GN Name=BHMT2 {ECO:0000313|Ensembl:ENSOANP00000012575}; OS Ornithorhynchus anatinus (Duckbill platypus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Monotremata; Ornithorhynchidae; Ornithorhynchus. OX NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000012575, ECO:0000313|Proteomes:UP000002279}; RN [1] {ECO:0000313|Ensembl:ENSOANP00000012575} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000012575}; RX PubMed=18464734; DOI=10.1038/nature06936; RA Warren W.C., Hillier L.W., Marshall Graves J.A., Birney E., RA Ponting C.P., Grutzner F., Belov K., Miller W., Clarke L., RA Chinwalla A.T., Yang S.P., Heger A., Locke D.P., Miethke P., RA Waters P.D., Veyrunes F., Fulton L., Fulton B., Graves T., Wallis J., RA Puente X.S., Lopez-Otin C., Ordonez G.R., Eichler E.E., Chen L., RA Cheng Z., Deakin J.E., Alsop A., Thompson K., Kirby P., RA Papenfuss A.T., Wakefield M.J., Olender T., Lancet D., Huttley G.A., RA Smit A.F., Pask A., Temple-Smith P., Batzer M.A., Walker J.A., RA Konkel M.K., Harris R.S., Whittington C.M., Wong E.S., Gemmell N.J., RA Buschiazzo E., Vargas Jentzsch I.M., Merkel A., Schmitz J., Zemann A., RA Churakov G., Kriegs J.O., Brosius J., Murchison E.P., RA Sachidanandam R., Smith C., Hannon G.J., Tsend-Ayush E., McMillan D., RA Attenborough R., Rens W., Ferguson-Smith M., Lefevre C.M., Sharp J.A., RA Nicholas K.R., Ray D.A., Kube M., Reinhardt R., Pringle T.H., RA Taylor J., Jones R.C., Nixon B., Dacheux J.L., Niwa H., Sekita Y., RA Huang X., Stark A., Kheradpour P., Kellis M., Flicek P., Chen Y., RA Webber C., Hardison R., Nelson J., Hallsworth-Pepin K., Delehaunty K., RA Markovic C., Minx P., Feng Y., Kremitzki C., Mitreva M., Glasscock J., RA Wylie T., Wohldmann P., Thiru P., Nhan M.N., Pohl C.S., Smith S.M., RA Hou S., Nefedov M., de Jong P.J., Renfree M.B., Mardis E.R., RA Wilson R.K.; RT "Genome analysis of the platypus reveals unique signatures of RT evolution."; RL Nature 453:175-183(2008). RN [2] {ECO:0000313|Ensembl:ENSOANP00000012575} RP IDENTIFICATION. RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000012575}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSOANP00000012575}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSOANT00000012577; ENSOANP00000012575; ENSOANG00000007897. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; F7DS96; -. DR OMA; NINEAAC; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR Proteomes; UP000002279; Unplaced. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0061627; F:S-methylmethionine-homocysteine S-methyltransferase activity; IEA:Ensembl. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl. DR GO; GO:0046500; P:S-adenosylmethionine metabolic process; IEA:Ensembl. DR GO; GO:0033477; P:S-methylmethionine metabolic process; IEA:Ensembl. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002279}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000002279}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 210 210 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 292 292 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSOANP00000012575}. SQ SEQUENCE 365 AA; 39889 MW; CD5CDA5328322FD2 CRC64; YSPVGAETPG PVQGILERLN GGKVVIGDGG FVFALEKRGY VKAGPWTPEA VVEHPEAVLQ LHREFLRAGS NVMQTFTFFA GEDSLDCKWK KINEAACDLA REVAKDGDAL VAGGISQTPS YKSRKGEAEI KKVFQQQLEV FVRKNVDFLI AEYFEHVEEA VWAVEVLKAS GKPVAATMCI GPEGDMHGIP PGECAVRLVK AGASLVGVNC RFGPETSLKT VSLMKQGLKS AGLKAHLMVQ TLAFHTPDCG KAGFVDLPEY PFGLEPRVAS RWDIQKYARE AYELGVRYIG GCCGFEPYHV RAIAEELAPE RGFLPPASDK HGSWGSGLDM HTKPWIRARA RKEYWQNLPL ASGRPYCPSL SRPDA // ID F7DZ43_ORNAN Unreviewed; 406 AA. AC F7DZ43; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSOANP00000012573}; DE Flags: Fragment; GN Name=BHMT {ECO:0000313|Ensembl:ENSOANP00000012573}; OS Ornithorhynchus anatinus (Duckbill platypus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Monotremata; Ornithorhynchidae; Ornithorhynchus. OX NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000012573, ECO:0000313|Proteomes:UP000002279}; RN [1] {ECO:0000313|Ensembl:ENSOANP00000012573} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000012573}; RX PubMed=18464734; DOI=10.1038/nature06936; RA Warren W.C., Hillier L.W., Marshall Graves J.A., Birney E., RA Ponting C.P., Grutzner F., Belov K., Miller W., Clarke L., RA Chinwalla A.T., Yang S.P., Heger A., Locke D.P., Miethke P., RA Waters P.D., Veyrunes F., Fulton L., Fulton B., Graves T., Wallis J., RA Puente X.S., Lopez-Otin C., Ordonez G.R., Eichler E.E., Chen L., RA Cheng Z., Deakin J.E., Alsop A., Thompson K., Kirby P., RA Papenfuss A.T., Wakefield M.J., Olender T., Lancet D., Huttley G.A., RA Smit A.F., Pask A., Temple-Smith P., Batzer M.A., Walker J.A., RA Konkel M.K., Harris R.S., Whittington C.M., Wong E.S., Gemmell N.J., RA Buschiazzo E., Vargas Jentzsch I.M., Merkel A., Schmitz J., Zemann A., RA Churakov G., Kriegs J.O., Brosius J., Murchison E.P., RA Sachidanandam R., Smith C., Hannon G.J., Tsend-Ayush E., McMillan D., RA Attenborough R., Rens W., Ferguson-Smith M., Lefevre C.M., Sharp J.A., RA Nicholas K.R., Ray D.A., Kube M., Reinhardt R., Pringle T.H., RA Taylor J., Jones R.C., Nixon B., Dacheux J.L., Niwa H., Sekita Y., RA Huang X., Stark A., Kheradpour P., Kellis M., Flicek P., Chen Y., RA Webber C., Hardison R., Nelson J., Hallsworth-Pepin K., Delehaunty K., RA Markovic C., Minx P., Feng Y., Kremitzki C., Mitreva M., Glasscock J., RA Wylie T., Wohldmann P., Thiru P., Nhan M.N., Pohl C.S., Smith S.M., RA Hou S., Nefedov M., de Jong P.J., Renfree M.B., Mardis E.R., RA Wilson R.K.; RT "Genome analysis of the platypus reveals unique signatures of RT evolution."; RL Nature 453:175-183(2008). RN [2] {ECO:0000313|Ensembl:ENSOANP00000012573} RP IDENTIFICATION. RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000012573}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSOANP00000012573}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSOANT00000012575; ENSOANP00000012573; ENSOANG00000007895. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; F7DZ43; -. DR OMA; WGVTKGT; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR Proteomes; UP000002279; Unplaced. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006577; P:amino-acid betaine metabolic process; IEA:Ensembl. DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002279}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000002279}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 217 217 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSOANP00000012573}. SQ SEQUENCE 406 AA; 44886 MW; C86F42FF8386A5A2 CRC64; AAPLGNNTRA QGILERLNGG EVVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAVRQLH REFLRSGSNV MQTFTFYASE DKLENRGNYV AQKISGQKVN EAACDIARQV ADEGDALVAG GVSQTPSYLS CKSETEVKKI FRQQLEVFTK KNVDFLIAEY FEHVEEAVWA VEALKESGKP VAATMCIGPE GDLHGIPPGE CAVRLVKAGA SIVGVNCHFD PTTSLKTVKL MKEGLERAKL KAHLMAQPLA YHTPDCGKQG FIDLPEFPFG LEPRVTTRWD IQKYAREAYE LGVRYIGGCC GFEPYHVRAI AEELAPERGF LPPASDKHGS WGSGLDMHTK PWIRARARKE YWQNLPLASG RPYCPSMSRP DAWGVTKGTA ELMQQKEATT DQQLKDLFQK QRFKSG // ID F7ED20_CALJA Unreviewed; 1265 AA. AC F7ED20; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 01-APR-2015, entry version 25. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCJAP00000032620}; GN Name=MTR {ECO:0000313|Ensembl:ENSCJAP00000032620}; OS Callithrix jacchus (White-tufted-ear marmoset). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Platyrrhini; Cebidae; Callitrichinae; Callithrix. OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000032620, ECO:0000313|Proteomes:UP000008225}; RN [1] {ECO:0000313|Ensembl:ENSCJAP00000032620, ECO:0000313|Proteomes:UP000008225} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCJAP00000032620} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2011) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 1}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSCJAP00000032620}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACFV01028010; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01028011; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01028012; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01028013; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01028014; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01028015; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01028016; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01028017; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_002760925.1; XM_002760879.2. DR Ensembl; ENSCJAT00000034476; ENSCJAP00000032620; ENSCJAG00000017612. DR GeneID; 100407279; -. DR KEGG; cjc:100407279; -. DR CTD; 4548; -. DR GeneTree; ENSGT00420000029824; -. DR KO; K00548; -. DR OrthoDB; EOG7TF786; -. DR Proteomes; UP000008225; Chromosome 19. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008225}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008225}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 260 260 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 785 785 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1265 AA; 140706 MW; E4EA89AF0E2B510D CRC64; MSPALQDLSQ PAGLKKTLWN EIDAILQKRI MVLDGGMGTM IQRHKLNEEH FRGQEFQDHA RPLKGNNDIL SITQPDVIYQ IHKEYLLAGA DIIETNTFSS TSIAQADYGL EHLAYQMNKC SAGVARKAAE EITLQTGIKR FVAGALGPTN KTLSVSPSVE RPDYRNITFD ELVGAYQEQA RGLLDGGVDI LLIETIFDTA NAKAALFALQ KLFEETYAPR PIFISGTIVD KSGRTLSGQT GEAFVINVSH ADPLCIGLNC ALGAAEMRPF IEIIGKCTTA YVLCYPNAGL PNTFGDYDET PSMMAKHLKD FAMDGLVNIV GGCCGSTPDH IREIAEAVKN CKPRVPPDAV FEGHMLLSGL EPFRIGPYTN FVNIGERCNV AGSRKFAKLI MAGNYEEALC VAKVQVEMGA QVLDINMDDG MLDGPSAMTQ FCNLIASEPD IAKVPLCIDS SNFAVIEAGL KCCQGKCIVN SISLKEGEED FLEKARKIRK FGAAVVVMAF DEEGQATETD NKIRICTRAY HLLVKKLGFN PNDIIFDPNI LTIGTGMEEH NLYAINFIQA TKIIKETLPG ARISGGLSNL SFSFRGMDAI REAMHGVFLY HAIKFGMDMG IVNAGNLPVY DDIHKELLQL CEDLIWNKDP EATEKLLRYA QTHGQGGKKV IQTDEWRNGP VEERLEYALV KGIEKHIIED TEEARLNQEK YPRPLNIIEG PLMNGMKIVG DLFGAGKMFL PQVIKSARVM KKAVGHLIPF MEKEREETRV LNSTIEEEDP YQGTIVLATV KGDVHDIGKN IVGVVLGCNN FRVIDLGVMT PCDKILKAAL DHKADIIGLS GLITPSLDEM IFVAKEMERL AIKIPLLIGG ATTSRTHTAV KIAPRYSAPV IHVLDASKSV VVCSQLLDEN LKDEYFEEIM EEYEDIRQDH YESLKDRRYL PLNQARKSGF RMDWLSEPHP VKPTFIGTQV FEDYDLQRLV DYIDWKPFFD VWQLRGKYPN RGFPKIFNDK TVGEEAKKVY DDAQNMLNSL ISQKKLQARG VVGFWPAQSV QDDIHLYAEG AVPQAAEPIA TFYGLRQQAE KDSASTEPYY CLSDFIAPLH SGIRDYLGLF AVACFGVEEL SKAYEDDGDD YSSIMVKALG DRLAEAFAEE LHERVRRELW AYCGSEQLDV ADLRRLRYEG IRPAPGYPSQ PDHTEKLTMW RLADIEQSTG IRLTESLAMA PAAAVSGLYF SNLKSKYFAV GKISKDQVED YALRKNMSVA EIEKWLGPIL GYDTD // ID F7EDB4_CALJA Unreviewed; 1214 AA. AC F7EDB4; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCJAP00000032619}; GN Name=MTR {ECO:0000313|Ensembl:ENSCJAP00000032619}; OS Callithrix jacchus (White-tufted-ear marmoset). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Platyrrhini; Cebidae; Callitrichinae; Callithrix. OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000032619, ECO:0000313|Proteomes:UP000008225}; RN [1] {ECO:0000313|Ensembl:ENSCJAP00000032619, ECO:0000313|Proteomes:UP000008225} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCJAP00000032619} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2011) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSCJAP00000032619}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACFV01028010; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01028011; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01028012; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01028013; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01028014; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01028015; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01028016; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01028017; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSCJAT00000034475; ENSCJAP00000032619; ENSCJAG00000017612. DR GeneTree; ENSGT00420000029824; -. DR Proteomes; UP000008225; Chromosome 19. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008225}; KW Reference proteome {ECO:0000313|Proteomes:UP000008225}. SQ SEQUENCE 1214 AA; 134972 MW; 42BD9D3BF7415669 CRC64; MSPALQDLSQ PAGLKKTLWN EIDAILQKRI MVLDGGMGTM IQRHKLNEEH FRGQEFQDHA RPLKGNNDIL SITQPDVIYQ IHKEYLLAGA DIIETNTFSS TSIAQADYGL EHLAYQMNKC SAGVARKAAE EITLQTGIKR FVAGALGPTN KTLSVSPSVE RPDYRNITFD ELVGAYQEQA RGLLDGGVDI LLIETIFDTA NAKAALFALQ KLFEETYAPR PIFISGTIVD KSGRTLSGQT GEAFVINVSH ADPLCIGLNC ALGAAEMRPF IEIIGKCTTA YVLCYPNAGL PNTFGDYDET PSMMAKHLKD FAMDGLVNIV GGCCGSTPDH IREIAEAVKN CKPRVPPDAV FEGHMLLSGL EPFRIGPYTN FVNIGERCNV AGSRKFAKLI MAGNYEEALC VAKVQVEMGA QVLDINMDDG MLDGPSAMTQ FCNLIASEPD IAKVPLCIDS SNFAVIEAGL KCCQGKCIVN SISLKEGEED FLEKARKIRK FGAAVVVMAF DEEGQATETD NKIRICTRAY HLLVKKLGFN PNDIIFDPNI LTIGTGMEEH NLYAINFIQA TKIIKETLPG ARISGGLSNL SFSFRGMDAI REAMHGVFLY HAIKFGMDMG IVNAGNLPVY DDIHKELLQL CEDLIWNKDP EATEKLLRYA QTHGQGGKKV IQTDEWRNGP VEERLEYALV KVIKSARVMK KAVGHLIPFM EKEREETRVL NSTIEEEDPY QGTIVLATVK GDVHDIGKNI VGVVLGCNNF RVIDLGVMTP CDKILKAALD HKADIIGLSG LITPSLDEMI FVAKEMERLA IKIPLLIGGA TTSRTHTAVK IAPRYSAPVI HVLDASKSVV VCSQLLDENL KDEYFEEIME EYEDIRQDHY ESLKDRRYLP LNQARKSGFR MDWLSEPHPV KPTFIGTQVF EDYDLQRLVD YIDWKPFFDV WQLRGKYPNR GFPKIFNDKT VGEEAKKVYD DAQNMLNSLI SQKKLQARGV VGFWPAQSVQ DDIHLYAEGA VPQAAEPIAT FYGLRQQAEK DSASTEPYYC LSDFIAPLHS GIRDYLGLFA VACFGVEELS KAYEDDGDDY SSIMVKALGD RLAEAFAEEL HERVRRELWA YCGSEQLDVA DLRRLRYEGI RPAPGYPSQP DHTEKLTMWR LADIEQSTGI RLTESLAMAP AAAVSGLYFS NLKSKYFAVG KISKDQVEDY ALRKNMSVAE IEKWLGPILG YDTD // ID F7ERP0_CALJA Unreviewed; 1284 AA. AC F7ERP0; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCJAP00000032605}; DE Flags: Fragment; GN Name=MTR {ECO:0000313|Ensembl:ENSCJAP00000032605}; OS Callithrix jacchus (White-tufted-ear marmoset). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Platyrrhini; Cebidae; Callitrichinae; Callithrix. OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000032605, ECO:0000313|Proteomes:UP000008225}; RN [1] {ECO:0000313|Ensembl:ENSCJAP00000032605, ECO:0000313|Proteomes:UP000008225} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCJAP00000032605} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 1}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSCJAP00000032605}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACFV01028010; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01028011; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01028012; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01028013; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01028014; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01028015; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01028016; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01028017; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSCJAT00000034461; ENSCJAP00000032605; ENSCJAG00000017612. DR GeneTree; ENSGT00420000029824; -. DR InParanoid; F7ERP0; -. DR OMA; DYNSIMV; -. DR TreeFam; TF312829; -. DR Proteomes; UP000008225; Chromosome 19. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:Ensembl. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008225}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008225}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 260 260 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 787 787 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSCJAP00000032605}. SQ SEQUENCE 1284 AA; 142936 MW; B4A98BE67A10A175 CRC64; VGPGVFDIYQ KTGLKKTLWN EIDAILQKRI MVLDGGMGTM IQRHKLNEEH FRGQEFQDHA RPLKGNNDIL SITQPDVIYQ IHKEYLLAGA DIIETNTFSS TSIAQADYGL EHLAYQMNKC SAGVARKAAE EITLQTGIKR FVAGALGPTN KTLSVSPSVE RPDYRNITFD ELVGAYQEQA RGLLDGGVDI LLIETIFDTA NAKAALFALQ KLFEETYAPR PIFISGTIVD KSGRTLSGQT GEAFVINVSH ADPLCIGLNC ALGAAEMRPF IEIIGKCTTA YVLCYPNAGL PNTFGDYDET PSMMAKHLKD FAMDGLVNIV GGCCGSTPDH IREIAEAVKN CKPRVPPDAV FEGHMLLSER GVEPFMIGPY TNFVNIGERC NVAGSRKFAK LIMAGNYEEA LCVAKVQVEM GAQVLDINMD DGMLDGPSAM TQFCNLIASE PDIAKVPLCI DSSNFAVIEA GLKCCQGKCI VNSISLKEGE EDFLEKARKI RKFGAAVVVM AFDEEGQATE TDNKIRICTR AYHLLVKKLG FNPNDIIFDP NILTIGTGME EHNLYAINFI QATKIIKETL PGARISGGLS NLSFSFRGMD AIREAMHGVF LYHAIKFGMD MGIVNAGNLP VYDDIHKELL QLCEDLIWNK DPEATEKLLR YAQTHGQGGK KVIQTDEWRN GPVEERLEYA LVKGIEKHII EDTEEARLNQ EKYPRPLNII EGPLMNGMKI VGDLFGAGKM FLPQVIKSAR VMKKAVGHLI PFMEKEREET RVLNSTIEEE DPYQGTIVLA TVKGDVHDIG KNIVGVVLGC NNFRVIDLGV MTPCDKILKA ALDHKAVDII GLSGLITPSL DEMIFVAKEM ERLAIKIPLL IGGATTSRTH TAVKIAPRYS APVIHVLDAS KSVVVCSQLL DENLKDEYFE EIMEEYEDIR QDHYESLKDR RYLPLNQARK SGFRMDWLSE PHPVKPTFIG TQVFEDYDLQ RLVDYIDWKP FFDVWQLRGK YPNRGFPKIF NDKTVGEEAK KVYDDAQNML NSLISQKKLQ ARGVVGFWPA QSVQDDIHLY AEGAVPQAAE PIATFYGLRQ QAEKDSASTE PYYCLSDFIA PLHSGIRDYL GLFAVACFGV EELSKAYEDD GDDYSSIMVK ALGDRLAEAF AEELHERVRR ELWAYCGSEQ LDVADLRRLR YEGIRPAPGY PSQPDHTEKL TMWRLADIEQ STGIRLTESL AMAPAAAVSG LYFSNLKSKY FAVGKISKDQ VEDYALRKNM SVAEIEKWLG PILGYDTDFF FAFFILDAPQ GNTT // ID F7ES55_ORNAN Unreviewed; 507 AA. AC F7ES55; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 2. DT 27-MAY-2015, entry version 25. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSOANP00000026724}; DE Flags: Fragment; GN Name=MTR {ECO:0000313|Ensembl:ENSOANP00000026724}; OS Ornithorhynchus anatinus (Duckbill platypus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Monotremata; Ornithorhynchidae; Ornithorhynchus. OX NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000026724, ECO:0000313|Proteomes:UP000002279}; RN [1] {ECO:0000313|Ensembl:ENSOANP00000026724} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000026724}; RX PubMed=18464734; DOI=10.1038/nature06936; RA Warren W.C., Hillier L.W., Marshall Graves J.A., Birney E., RA Ponting C.P., Grutzner F., Belov K., Miller W., Clarke L., RA Chinwalla A.T., Yang S.P., Heger A., Locke D.P., Miethke P., RA Waters P.D., Veyrunes F., Fulton L., Fulton B., Graves T., Wallis J., RA Puente X.S., Lopez-Otin C., Ordonez G.R., Eichler E.E., Chen L., RA Cheng Z., Deakin J.E., Alsop A., Thompson K., Kirby P., RA Papenfuss A.T., Wakefield M.J., Olender T., Lancet D., Huttley G.A., RA Smit A.F., Pask A., Temple-Smith P., Batzer M.A., Walker J.A., RA Konkel M.K., Harris R.S., Whittington C.M., Wong E.S., Gemmell N.J., RA Buschiazzo E., Vargas Jentzsch I.M., Merkel A., Schmitz J., Zemann A., RA Churakov G., Kriegs J.O., Brosius J., Murchison E.P., RA Sachidanandam R., Smith C., Hannon G.J., Tsend-Ayush E., McMillan D., RA Attenborough R., Rens W., Ferguson-Smith M., Lefevre C.M., Sharp J.A., RA Nicholas K.R., Ray D.A., Kube M., Reinhardt R., Pringle T.H., RA Taylor J., Jones R.C., Nixon B., Dacheux J.L., Niwa H., Sekita Y., RA Huang X., Stark A., Kheradpour P., Kellis M., Flicek P., Chen Y., RA Webber C., Hardison R., Nelson J., Hallsworth-Pepin K., Delehaunty K., RA Markovic C., Minx P., Feng Y., Kremitzki C., Mitreva M., Glasscock J., RA Wylie T., Wohldmann P., Thiru P., Nhan M.N., Pohl C.S., Smith S.M., RA Hou S., Nefedov M., de Jong P.J., Renfree M.B., Mardis E.R., RA Wilson R.K.; RT "Genome analysis of the platypus reveals unique signatures of RT evolution."; RL Nature 453:175-183(2008). RN [2] {ECO:0000313|Ensembl:ENSOANP00000026724} RP IDENTIFICATION. RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000026724}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSOANP00000026724}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSOANT00000030525; ENSOANP00000026724; ENSOANG00000009396. DR GeneTree; ENSGT00420000029824; -. DR InParanoid; F7ES55; -. DR OrthoDB; EOG7TF786; -. DR Proteomes; UP000002279; Unplaced. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0008705; F:methionine synthase activity; IEA:Ensembl. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002279}; KW Reference proteome {ECO:0000313|Proteomes:UP000002279}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSOANP00000026724}. SQ SEQUENCE 507 AA; 53512 MW; CDE99FD3E516A2F3 CRC64; APRGAGLASP PALGTGPGTQ EAPNGYRRRH FFNPHLTGEG ARAGEAKRLA RGPAGREPAS SRSPAGGLAA EPRRFPCPRG REGRGGEEAG QASRPAPLPP RQDYLLAGAD IIETNTFSGT RVAQADYGLE HLAYELNRTS AEVARRAADD VAAQTGTKRF VAGALGPTNK TLSVSPSVER PDFRNITFDE LAEAYREQAR GLLDGGVDIV LVETVFDTAN AKAALFALQE LFEEEYPPKP IFVSQTSVFG RDVNGVGLGR RGGGGVNKRS KLSARCVRLG LNCALGAGEM RPFMEAVGKC TAAYVLCYPN AGRRRTFGSV QQYLSGACRA QSTVAGAGPT GRDRPCPTTG RRPKRGRRAA EPASPSRAGI PPSPWPNRLF QALRRGAPGE RSGNPRQGRD GRSGAREVVP TDGLLVASPR QEALSVAKAQ VDMGAQILDI NVDDGMLDGP RAMARFCNSV ASEPDVARVP LCIDSSDFAV IEAGLKCSQG KCVVNSISLK EGEGDFL // ID F7FWS1_CALJA Unreviewed; 1118 AA. AC F7FWS1; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCJAP00000032579}; GN Name=MTR {ECO:0000313|Ensembl:ENSCJAP00000032579}; OS Callithrix jacchus (White-tufted-ear marmoset). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Platyrrhini; Cebidae; Callitrichinae; Callithrix. OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000032579, ECO:0000313|Proteomes:UP000008225}; RN [1] {ECO:0000313|Ensembl:ENSCJAP00000032579, ECO:0000313|Proteomes:UP000008225} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCJAP00000032579} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSCJAP00000032579}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACFV01028010; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01028011; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01028012; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01028013; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01028014; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01028015; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01028016; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01028017; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSCJAT00000034434; ENSCJAP00000032579; ENSCJAG00000017612. DR GeneTree; ENSGT00420000029824; -. DR Proteomes; UP000008225; Chromosome 19. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008225}; KW Reference proteome {ECO:0000313|Proteomes:UP000008225}. SQ SEQUENCE 1118 AA; 124246 MW; 7D7904C070D8F656 CRC64; MSPALQDLSQ PAGLKKTLWN EIDAILQKRI MVLDGGMGTM IQRHKLNEEH FRGQEFQDHA RPLKGNNDIL SITQPDVIYQ IHKEYLLAGA DIIETNTFSS TSIAQADYGL EHLAYQMNKC SAGVARKAAE EITLQTGIKR FVAGALGPTN KTLSVSPSVE RPDYRNITFD ELVGAYQEQA RGLLDGGVDI LLIETIFDTA NAKAALFALQ KLFEETYAPR PIFISGTIVD KSGRTLSGQT GEAFVINVSH ADPLCIGLNC ALGAAEMRPF IEIIGKCTTA YVLCYPNAGL PNTFGDYDET PSMMAKHLKD FAMDGLVNIV GGCCGSTPDH IREIAEAVKN CKPRVPPDAV FEGHMLLSGL EPFRIGPYTN FVNIGERCNV AGSRKFAKLI MAGNYEEALC VAKVQVEMGA QVLDINMDDG MLDGPSAMTQ FCNLIASEPD IAKVPLCIDS SNFAVIEAGL KCCQGKCIVN SISLKEGEED FLEKARKIRK FGAAVVVMAF DEEGQTHGQG GKKVIQTDEW RNGPVEERLE YALVKGIEKH IIEDTEEARL NQEKYPRPLN IIEGPLMNGM KIVGDLFGAG KMFLPQVIKS ARVMKKAVGH LIPFMEKERE ETRVLNSTIE EEDPYQGTIV LATVKGDVHD IGKNIVGVVL GCNNFRVIDL GVMTPCDKIL KAALDHKADI IGLSGLITPS LDEMIFVAKE MERLAIKIPL LIGGATTSRT HTAVKIAPRY SAPVIHVLDA SKSVVVCSQL LDENLKDEYF EEIMEEYEDI RQDHYESLKD RRYLPLNQAR KSGFRMDWLS EPHPVKPTFI GTQVFEDYDL QRLVDYIDWK PFFDVWQLRG KYPNRGFPKI FNDKTVGEEA KKVYDDAQNM LNSLISQKKL QARGVVGFWP AQSVQDDIHL YAEGAVPQAA EPIATFYGLR QQAEKDSAST EPYYCLSDFI APLHSGIRDY LGLFAVACFG VEELSKAYED DGDDYSSIMV KALGDRLAEA FAEELHERVR RELWAYCGSE QLDVADLRRL RYEGIRPAPG YPSQPDHTEK LTMWRLADIE QSTGIRLTES LAMAPAAAVS GLYFSNLKSK YFAVGKISKD QVEDYALRKN MSVAEIEKFN FVHYKIGE // ID F7H1C4_MACMU Unreviewed; 363 AA. AC F7H1C4; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAY-2015, entry version 32. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMMUP00000008933}; GN Name=BHMT2 {ECO:0000313|Ensembl:ENSMMUP00000008933}; GN ORFNames=EGK_16627 {ECO:0000313|EMBL:EHH26611.1}; OS Macaca mulatta (Rhesus macaque). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000008933, ECO:0000313|Proteomes:UP000006718}; RN [1] {ECO:0000313|Ensembl:ENSMMUP00000008933, ECO:0000313|Proteomes:UP000006718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000008933, RC ECO:0000313|Proteomes:UP000006718}; RX PubMed=17431167; DOI=10.1126/science.1139247; RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M., RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., RA Wilson R.K., Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., RA Hardison R.C., Makova K.D., Miller W., Milosavljevic A., Palermo R.E., RA Siepel A., Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J., RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., RA Dinh H.H., Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., RA Godfrey J., Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., RA Jhangiani S.N., Joshi V., Khan Z.M., Kirkness E.F., Cree A., RA Fowler R.G., Lee S., Lewis L.R., Li Z., Liu Y.-S., Moore S.M., RA Muzny D., Nazareth L.V., Ngo D.N., Okwuonu G.O., Pai G., Parker D., RA Paul H.A., Pfannkoch C., Pohl C.S., Rogers Y.-H.C., Ruiz S.J., RA Sabo A., Santibanez J., Schneider B.W., Smith S.M., Sodergren E., RA Svatek A.F., Utterback T.R., Vattathil S., Warren W., White C.S., RA Chinwalla A.T., Feng Y., Halpern A.L., Hillier L.W., Huang X., RA Minx P., Nelson J.O., Pepin K.H., Qin X., Sutton G.G., Venter E., RA Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P., Jones S.M., RA Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L., Csuros M., RA Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H., Liu Y., RA Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E., RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J., RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J., RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A., RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., RA Denby A., Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., RA Marklein A., Nielsen R., Vallender E.J., Clark A.G., Ferguson B., RA Hernandez R.D., Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., RA Pu L.-L., Ren Y., Smith D.G., Wheeler D.A., Schenck I., Ball E.V., RA Chen R., Cooper D.N., Giardine B., Hsu F., Kent W.J., Lesk A., RA Nelson D.L., O'brien W.E., Pruefer K., Stenson P.D., Wallace J.C., RA Ke H., Liu X.-M., Wang P., Xiang A.P., Yang F., Barber G.P., RA Haussler D., Karolchik D., Kern A.D., Kuhn R.M., Smith K.E., RA Zwieg A.S.; RT "Evolutionary and biomedical insights from the rhesus macaque RT genome."; RL Science 316:222-234(2007). RN [2] {ECO:0000313|EMBL:EHH26611.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CR-5 {ECO:0000313|EMBL:EHH26611.1}; RX PubMed=22002653; DOI=10.1038/nbt.1992; RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., RA Li Q., Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., RA Huang Z., Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., RA Huang Y., Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., RA Li B., Liu X., Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., RA Li Y., Wang W., Katze M.G., Su B., Nielsen R., Yang H., Wang J., RA Wang X., Wang J.; RT "Genome sequencing and comparison of two nonhuman primate animal RT models, the cynomolgus and Chinese rhesus macaques."; RL Nat. Biotechnol. 29:1019-1023(2011). RN [3] {ECO:0000313|Ensembl:ENSMMUP00000008933} RP IDENTIFICATION. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000008933}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001258; EHH26611.1; -; Genomic_DNA. DR RefSeq; XP_001103987.1; XM_001103987.2. DR UniGene; Mmu.20580; -. DR ProteinModelPortal; F7H1C4; -. DR Ensembl; ENSMMUT00000009506; ENSMMUP00000008933; ENSMMUG00000006796. DR GeneID; 714308; -. DR KEGG; mcc:714308; -. DR CTD; 23743; -. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; F7H1C4; -. DR OMA; PEGDMHD; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR UniPathway; UPA00051; UER00083. DR NextBio; 19981551; -. DR Proteomes; UP000006718; Chromosome 6. DR ExpressionAtlas; F7H1C4; baseline. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0061627; F:S-methylmethionine-homocysteine S-methyltransferase activity; IEA:Ensembl. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl. DR GO; GO:0046500; P:S-adenosylmethionine metabolic process; IEA:Ensembl. DR GO; GO:0033477; P:S-methylmethionine metabolic process; IEA:Ensembl. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006718}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Reference proteome {ECO:0000313|Proteomes:UP000006718}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 208 208 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 363 AA; 40333 MW; CE911F88B30FA4FD CRC64; MAPAGRPGAK KGILERLESG EVVIGDGSFL ITLEKRGYVK AGLWTPEAVI EHPDAVRQLH MEFLRAGSNV MQTFTFSASE DNMESKWEDV NAAACDLARE VAGKGDALVA GGICQTSIYK YHKDETRIKK LFRQQLEVFA WKKVDFLIAE YFEHVEEAVW AVEVLKESDR PVAVTMCIGP EGDMHDTTPG ECAVRLVKAG ASIVGVNCRF GPETSLKTME LMKEGLERAG LKAHLMVQPL GFHTPDCGKE GFVDLPEYPF GLESRVATRW DIQKYAREAY NLGVRYIGGC CGFEPYHIRA IAEELAPERG FLPPASEKHG SWGSGLDMHT KPWIRARARR EYWENLLPAS GRPFCPSLSK PDA // ID F7JI91_9FIRM Unreviewed; 823 AA. AC F7JI91; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 01-OCT-2014, entry version 17. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGN38533.1}; GN ORFNames=HMPREF0988_00045 {ECO:0000313|EMBL:EGN38533.1}; OS Lachnospiraceae bacterium 1_4_56FAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=658655 {ECO:0000313|EMBL:EGN38533.1}; RN [1] {ECO:0000313|EMBL:EGN38533.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_4_56FAA {ECO:0000313|EMBL:EGN38533.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGN38533.1}. 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; ACTN01000001; EGN38533.1; -; Genomic_DNA. DR RefSeq; WP_009266026.1; NZ_GL945163.1. DR EnsemblBacteria; EGN38533; EGN38533; HMPREF0988_00045. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; SQ SEQUENCE 823 AA; 89525 MW; 9B23760DF50F5C2C CRC64; MIREDLREKR LFFDGGMGTL LQEKGLKAGE LPEIWNLEHS EEVISIHQAY IEAGSDIILT NTFGANALKF HDGVYSLEEI TKTAVAHGKE AVRRSAGGRN VYVALDVGPT GKLLKPMGDL AFEEAYEAFR EVMQYGEEAG ADLIHIETMS DTYEIKAAVL AAKENTNLPV FVTAVFDERK KLLTGADVPA FVSLLEGLRV DALGINCGMG PEQMIPILEE LQRYSSTPVI VKPNAGLPKQ RDGETVFDVE PDAFAQTMRK IAGSGAAVIG GCCGTTPEHI RAMTAVCLEI PYEPAGKKNL TMVSSYGKTV IFGEESKIIG ERINPTGKKK FKQALVERDM DYILREGIRQ EDNGAHILDV NVGLPDIDEV SMMKEAVTAL QGVTSLPLQI DTVDPRAMEE ALRVYNGKPM VNSVSGKQES MDAVFPLIQK YGGVVVGLTL DETGIPETAD GRVEIAERIL KEAEKYGIEK KDIVIDVLAM TVSSEPQGAI VTLEALRRVR RELGVHTVLG VSNISFGLPF RPVINANFYT LALYNGLSAG IINPSSEDMM QSYDAYHALM GLDENCSRYV AKYGAKAAAQ KEAAQREAAQ KAMTQETAKS LGNAVPGGEK GAEMLSGELT LKTAIERGLK EEAPQMADAL LKTEQPLEII NTYLIPALDH VGKGFEEGTV FLPQLLMSAD AAKAAFEVLK AKIASEESGT EKKEKIILAT VKGDIHDIGK NIVKVLLENY SFDVIDLGKD VAPELILQTA KEQEVRLVGL SALMTTTVAS MEETIRLLKK ELPECKIMVG GAVLNQEYAD MIGADFYGKD AMKSVYYAQE LLK // ID F7K168_9FIRM Unreviewed; 712 AA. AC F7K168; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 01-OCT-2014, entry version 20. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGN44111.1}; GN ORFNames=HMPREF0991_03131 {ECO:0000313|EMBL:EGN44111.1}; OS Lachnospiraceae bacterium 2_1_58FAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=658082 {ECO:0000313|EMBL:EGN44111.1}; RN [1] {ECO:0000313|EMBL:EGN44111.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=2_1_58FAA {ECO:0000313|EMBL:EGN44111.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGN44111.1}. 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; ACTO01000055; EGN44111.1; -; Genomic_DNA. DR RefSeq; WP_009245811.1; NZ_GL945346.1. DR EnsemblBacteria; EGN44111; EGN44111; HMPREF0991_03131. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; SQ SEQUENCE 712 AA; 77900 MW; 36D39FB1B3D8E5E7 CRC64; MILERLGKEL LFFDGGMGTL LQAKGLLPGE LPETWNLTHA EAVRQIHRSY FEAGSDIVLT NTFGANALKF HDESCSLKEI IFSAVSHVKE AAKQGVRDNR EVYTALDIGP TGKLLKPMGD LEFETAYEAF KEVMIYGEQA GADLIHIETM SDTYELKAAV LAAKENTTLP VFVTTIFDER GKLLTGADVP SVVALLEGLR VDALGINCGM GPEQMMPILH EILEYTSLPV IVKPNAGLPK QRDGETYYDV EPEQFAKTME MIVETGACVI GGCCGTTPDH IRAMIAQCKD LLIKTPEKKV HTIVSSYGQA VMLGTGSRII GERINPTGKK KFKQALKDHD LDYILKEGIM QQDNGAHILD VNVGLPDIDE VSMMKEVITE LQSVTSLPLQ IDTVDIQAME QAMRIYNGKP MVNSVSGKQE SMDAVFPLIQ KYGGVVIGLT LDEDGIPETA DGRVAIAEKI IREAAKYGID KKDLVIDVLA MTVSSEPEGA KITLEALHRV RYDLGVNTVL GVSNISFGLP GRPIINANFY TMAMFQGLSA GIINPASEDM MRSYYAYHVL MNLDPNCENY IGRYGSANVE FASAPGSITT GAGRTAGGMM TLQAAIEKGL KEEAHQITNV LMQEKKPLDI INEHLIPALD TVGKGFEKGT VFLPQLLMSA EAAKTAFAVL KEGLENSGDV QEKKKNRACD SQRRYSRYWQ EYCKSSSGEL QF // ID F7KA65_9FIRM Unreviewed; 849 AA. AC F7KA65; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 01-OCT-2014, entry version 17. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGN40718.1}; GN ORFNames=HMPREF0994_02735 {ECO:0000313|EMBL:EGN40718.1}; OS Lachnospiraceae bacterium 3_1_57FAA_CT1. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=658086 {ECO:0000313|EMBL:EGN40718.1}; RN [1] {ECO:0000313|EMBL:EGN40718.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_57FAA_CT1 {ECO:0000313|EMBL:EGN40718.1}; 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.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EGN40718.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_57FAA_CT1 {ECO:0000313|EMBL:EGN40718.1}; RG The Broad Institute Genomics Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., 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 Lachnospiraceae bacterium 3-1-57FAA CT1."; RL Submitted (APR-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. {ECO:0000313|EMBL:EGN40718.1}. 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; ACTP02000001; EGN40718.1; -; Genomic_DNA. DR RefSeq; WP_009252636.1; NZ_KE150405.1. DR EnsemblBacteria; EGN40718; EGN40718; HMPREF0994_02735. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; SQ SEQUENCE 849 AA; 91059 MW; 924230EBD4305CC1 CRC64; MTKQEFREFI KDRMVFLDGA TGSNLMLRGM PGGVCPEKWI MENTQVLIGL QKEYVAAGAN ILYAPTFTAN RCKLKEYGLE GQLRQINAVM VAASREAAGG KALVAGDLTM TGEQLAPIGS MDFEELIDIY KEQIACIKEA GADLLVVETM MSLQESRAAL LAAKEICPGL PVMVTMTFEG DGRSLYGTDA ATAAVVLESL GAAAIGANCS TGPEQMAGII RQMASVTRIP VIAKPNAGLP SLNEEGKTVY EMRPREFAEE MQAVYEAGAS IIGGCCGTTP EHIADLHESF AGKMPAQVNR RPSGIRYLTS ERKTIAFGLD DPFLIIGERI NPTGKKKLQA QLREGSFEMV TRFAEEQEAG GASVLDVNMG MSGIDEKEMM LRALEEVGGV SQLPLSLDSS HVEVLEAALR RYPGRALINS ISLEKEKFEK LIPMAQKYGA MFILLPLSDA GLPESLQEKK EIIETILERA FACGLAKEDI IVDGLVTTVG ANPKAALETL ETIRYCKEKQ LATVCGLSNI SFGLPERSYV NSVFLTMAIQ AGLTMAIANP SQELLVASAF ASDMLLCKEE SALRYIEYAG TCTGIKPVSS AAPTAENSGQ KENNPGRQSS GNGGSGTAAS GEKSSGEKFP FSAVYEAVLK GNRSGIEQIT RRALEEGASA RELLDTCLLP AINQVGELFD KGKYFLPQLI SSAEAMKLSI GVLEPLLSSD GKQEKMPVVV IATVEGDIHD IGKNLVALML RNYGFEVIDL GKDVPKEKII QAAKEHGAGI IGLSALMTTT MQEMRHVVEL AHEEGLDSKI IIGGAVVTQD YADEIHADGY AKDAADTVRL AKRLLGLNEE TQGDSHGNE // ID F7KCW3_9FIRM Unreviewed; 310 AA. AC F7KCW3; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 01-OCT-2014, entry version 14. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGN38856.1}; GN ORFNames=HMPREF0994_03692 {ECO:0000313|EMBL:EGN38856.1}; OS Lachnospiraceae bacterium 3_1_57FAA_CT1. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=658086 {ECO:0000313|EMBL:EGN38856.1}; RN [1] {ECO:0000313|EMBL:EGN38856.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_57FAA_CT1 {ECO:0000313|EMBL:EGN38856.1}; 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.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EGN38856.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_57FAA_CT1 {ECO:0000313|EMBL:EGN38856.1}; RG The Broad Institute Genomics Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., 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 Lachnospiraceae bacterium 3-1-57FAA CT1."; RL Submitted (APR-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. {ECO:0000313|EMBL:EGN38856.1}. 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; ACTP02000012; EGN38856.1; -; Genomic_DNA. DR RefSeq; WP_009253593.1; NZ_KE150407.1. DR EnsemblBacteria; EGN38856; EGN38856; HMPREF0994_03692. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 310 AA; 34749 MW; F286DE236719CBC9 CRC64; MGKTQLEICF DSNKLILTEG AVGQRMEHEF SLKPDADIMY ASLIYSAEGR DALAAIYRSY LQAAEDYRLP ILLMTNTRRA NKDRVLRSEY RDKNMMRDYA CFLRELASGY TCPVFIGGMM GCKGDAYSGS EGLSTDEAIE YHSWQRNMFD TDSIDFLFAG IMPALPEALG MAEVMEESKL PYIISLMINE HGTLLDGNTI HEAISVIDTH TEANPLCYMT NCVHPAILRS ALSQPENRTE AVRARFCGIQ ANAACLSLQE LDNSCALKTS DAKELAEEFR LLHRDFPLKI YGGCCGTDES HIREMIKVLQ // ID F7KQ89_9FIRM Unreviewed; 795 AA. AC F7KQ89; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 01-OCT-2014, entry version 17. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGN30633.1}; GN ORFNames=HMPREF0993_01133 {ECO:0000313|EMBL:EGN30633.1}; OS Lachnospiraceae bacterium 5_1_57FAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=658085 {ECO:0000313|EMBL:EGN30633.1}; RN [1] {ECO:0000313|EMBL:EGN30633.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=5_1_57FAA {ECO:0000313|EMBL:EGN30633.1}; 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. {ECO:0000313|EMBL:EGN30633.1}. 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; ACTR01000008; EGN30633.1; -; Genomic_DNA. DR RefSeq; WP_009248494.1; NZ_GL945247.1. DR EnsemblBacteria; EGN30633; EGN30633; HMPREF0993_01133. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; SQ SEQUENCE 795 AA; 86454 MW; D6C9C31BB3E5224A CRC64; MILERLGKEL LYFDGGMGTL LQSKGLKPGE LPEVWNIEHA DEVVDIHRQY FEAGSDIVLA NTFGANALKF HDASYDLKEI VNAAIENVKK GASLGADAGR RTYTALDVGP TGKLLKPMGD LGFEDAYEAF REVMKYGEEA GADLIHIETM SDTYEVKAAV LAAKETTDLP VFATMIFDEK GKLLTGGDVP SVVALLEGLR VDALGINCGM GPEQMLPILE EILAYTSLPV IVKPNAGLPK QKDGQVYYDV DPDQFAQTME KIVHMGACVI GGCCGTTPGH IRAMVERTKG LSVILPSHKD LTIVSSYGKA VMLGEKPVII GERINPTGKK KFKQALKDHD LDYILKEGIT QQDKGAHILD VNVGLPDIDE SAMMQEVVTQ LQSVTSLPLQ IDTVDAKAME TAMRIYNGKP MVNSVNGKKE SMDEVFPLIR KYGGVVIGLT IDEDGIPQTA EGRVKVAGKI IEEAGKYGID KKDIVIDVLA MTISSEPEGA KVTLDALKGV REAYGVRTVL GVSNISFGLP YRPAINSNFY TMAMQNGLSA GIINPSSEDM MRSYYSFLAL MNYDSNCEAY IRQYGSQPVP PAASSGSRMT LKEAIEKGLK EEAHHATRTL LKEQEPLSII NQYLIPALDV VGKGFEKGTI FLPQLLMSAD AAKIAFAVLK DELAKSGGDM EKKDKIILAT VKGDIHDIGK NIVKVLLENY SFDVIDLGKD VPPKTIVETA IKEEVSLVGL SALMTTTVTS MEETIRLLRK HKPDCKVMVG GAVLNQDYAD MIGADFYGKD AMQSVYYAQR VFGHE // ID F7L2F2_FUSNU Unreviewed; 764 AA. AC F7L2F2; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EGN65682.1}; GN ORFNames=HMPREF0401_01996 {ECO:0000313|EMBL:EGN65682.1}; OS Fusobacterium nucleatum subsp. animalis 11_3_2. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=457403 {ECO:0000313|EMBL:EGN65682.1}; RN [1] {ECO:0000313|EMBL:EGN65682.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=11_3_2 {ECO:0000313|EMBL:EGN65682.1}; 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. {ECO:0000313|EMBL:EGN65682.1}. 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; ACUO01000032; EGN65682.1; -; Genomic_DNA. DR EnsemblBacteria; EGN65682; EGN65682; HMPREF0401_01996. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGN65682.1}; KW Transferase {ECO:0000313|EMBL:EGN65682.1}. SQ SEQUENCE 764 AA; 85009 MW; 28FAF94673E5B9C0 CRC64; MFEIEKDLKE RILVLDGAMG TVLQKYELSA EDFNGAKGCY EILNETRSDI IFEVHKKYIE AGADIIETNS FNCNAISLKD YHLEDKVYDL AKKSAEIARD AVKESGKKVY IFGSVGPTNK SLSFPVGDTP FKRAVSFDEM KEVIKVQVAG LIDGGVDGIL LETIFDGLTA KAALLATEEV FEEKNVKLPI SISATVNKQG KLLTGQSMES LIVALDRDSV TSFGFNCSFG AKDLVPLVIK IKELTTKFVT LHANAGLPNQ NGDYVETAQK MKNDLLPLIE NQAINILGGC CGTSYDHIKA IAELVKGEKP RVLPEKNLLE TCLSGNEIYN FKDKFTCVGE RNNISGSKLF RTMIEEHNYL KALDVARQQI DAGAKVLDIN VDDAILDSVE EMKNFLRVLQ NDSFIAKVPI MIDSSDFAVI EEGLKNTAGK AIVNSISLKE GEENFLRKAK IIRKYGASII VMAFDENGQG VSAERKIEIC QRAYNLLKSI GIKNSDIVFD PNILSVGTGQ EADRYHAREF LKTIDYIHKN LKGCGIVGGL SNLSFAFRGN NILRAAFHHI FLEEAIPRGF NFAILNPKEK APQWTDEERE KIKSFIFGDS TNIEDLLSLN LVKRKEDAQI FAETPEDRIR KALIQGGSES LQEVIEELLK KYKALEILEN ILMSAMQEIG RLFEQGELYL PQLIRSASVM NNCVNILTPY LEKVDRTLSK GKILMATVDG DVHDIGKNIV KTVLECNGYE VIDLGVMVPR EKIVEVAKKI MWIL // ID F7LDS0_BACOV Unreviewed; 915 AA. AC F7LDS0; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 01-APR-2015, entry version 19. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGN01792.1}; GN ORFNames=HMPREF1017_03463 {ECO:0000313|EMBL:EGN01792.1}; OS Bacteroides ovatus 3_8_47FAA. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=665954 {ECO:0000313|EMBL:EGN01792.1}; RN [1] {ECO:0000313|EMBL:EGN01792.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_8_47FAA {ECO:0000313|EMBL:EGN01792.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGN01792.1}. 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; ACWH01000016; EGN01792.1; -; Genomic_DNA. DR EnsemblBacteria; EGN01792; EGN01792; HMPREF1017_03463. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 915 AA; 99982 MW; F84F782829BB3F21 CRC64; MKKTISQIVS ERILILDGAM GTMIQQYNLK EEDFRGERFA HIPGQLKGNN DLLCLTRPDV IQDIHRKYLE AGADIIETNT FSSTTVSMAD YHVEEYVREM NLAAVKLARD LADEYTAQNP DKPRFVAGSV GPTNKTCSMS PDVNNPAYRA LSYDELAASY QQQMEAMLEG GVDAILIETI FDTLNAKAAI FAAEQAMKMT GIEVPIMLSV TVSDIGGRTL SGQTLDAFLA SVQHANIFSV GLNCSFGARQ LKPFLEQLAS RAPYYISAYP NAGLPNSLGK YDQTPADMAH EVREYIEEGL INIIGGCCGT TDAYIAEYPA LVEGAKPHVP ASAPDCMWLS GLELLEVKPE INFVNVGERC NVAGSRKFLR LINEKKYDEA LSIARQQVED GALVVDVNMD DGLLDAKTEM TIFLNLIMSE PEIARVPIMI DSSKWEVIEA GLKCLQGKSI VNSISLKEGE EAFLEHARII RQYGAAAVVM AFDEKGQADT AARKIEVCQR AYRLLVDKIG FNPHDIIFDP NVLAVATGIE EHNNYAVDFI EATAWIKKNL PGAHISGGVS NLSFSFRGNN YIREAMHAVF LYHAIQQGMD MGIVNPGTSV LYTDIPADVL EKIEDVVLNR RLDAAERLIE LAESLKANMS ETAGQPAVKQ DAWREGTVQE RLKYALMKGI GDFLEQDLAE ALPLYDKAVD VIEGPLMDGM NHVGELFGAG KMFLPQVVKT ARTMKKAVAI LQPIIESEKV EGSASAGKVL LATVKGDVHD IGKNIVAVVM ACNGYDIVDL GVMVPAETIV QRAIEEKVDM IGLSGLITPS LEEMAHVAVE LEKAGLDIPL LIGGATTSKM HTALKIAPVY HAPVVHLKDA SQNASVASKL LNPQAKAELV NELETEYEAL REKSGLMKRE TVSLEEAQKN KLNLF // ID F7LTA4_9BACE Unreviewed; 318 AA. AC F7LTA4; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGN05628.1}; GN ORFNames=HMPREF1018_03372 {ECO:0000313|EMBL:EGN05628.1}; OS Bacteroides sp. 2_1_56FAA. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=665938 {ECO:0000313|EMBL:EGN05628.1}; RN [1] {ECO:0000313|EMBL:EGN05628.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=2_1_56FAA {ECO:0000313|EMBL:EGN05628.1}; 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. {ECO:0000313|EMBL:EGN05628.1}. 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; ACWI01000025; EGN05628.1; -; Genomic_DNA. DR RefSeq; WP_005814689.1; NZ_GL945045.1. DR EnsemblBacteria; EGN05628; EGN05628; HMPREF1018_03372. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 318 AA; 36002 MW; 10BA640E8AED0044 CRC64; MEQLSFIESF RTSPFILTEG AIVERLRHEF HISPDKHIAH AALIYDDSHR EILASIYRQY LQIATEFRLP LMLMTPTRRA NIEQIAASDY RHKNVLADTM AFLSRFRDEA STPVYIGGLA GCRGNAYDGR YYLSVEEAME FHFPTVRTLA QSGADYLFAG IMPQLTEAIG MANAMAATGL PYIISFMVCR DGRLIDGTFI HDAIDAIEKE TSTRPLCYMA NCVHPDVLHQ ALLHPRNDTP LVRQRFQGIQ ANAANLSPEE LDGCDHLISS SPEELADRLM TLLWDFPLKI CGGCCGTNQQ HMHRFAEMLA YRRDNKAW // ID F7LTV3_9BACE Unreviewed; 932 AA. AC F7LTV3; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 01-APR-2015, entry version 20. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGN05170.1}; GN ORFNames=HMPREF1018_03552 {ECO:0000313|EMBL:EGN05170.1}; OS Bacteroides sp. 2_1_56FAA. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=665938 {ECO:0000313|EMBL:EGN05170.1}; RN [1] {ECO:0000313|EMBL:EGN05170.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=2_1_56FAA {ECO:0000313|EMBL:EGN05170.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGN05170.1}. 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; ACWI01000029; EGN05170.1; -; Genomic_DNA. DR EnsemblBacteria; EGN05170; EGN05170; HMPREF1018_03552. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 260 260 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 776 776 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 932 AA; 102142 MW; 0C2491044687C8A1 CRC64; MIWTGCLNDD RFVPLAMKKT IQQLVLERIL ILDGAMGTMI QQYNLREEDF RNERFAHIPG QLKGNNDLLC LTRPDVIRDI HRKYLEAGAD IIETNTFSST TISMADYHVQ EYVREMNQAA VKLAREVADE YTALNPDKPR FVAGSVGPTN KTCSMSPDVN NPAYRAVTYD EMADAYQQQM EAMLESGVDA LLIETIFDTL NAKAAILAAE RAMKATGVKV PVMLSVTVSD TGGRTLSGQT LEAFLASVQH ADIFSVGLNC SFGARQLKPF LEQLAARAPY YISAYPNAGL PNSLGKYDQT PADMAHEVKE YVHEGLINII GGCCGTTDAY IAEYPALIAG AKPHIPVCKP DCMWLSGLEL LEVKPEINFV NVGERCNVAG SRKFLRLINE KKYDEALSIA RKQVEDGALI IDVNMDDGLL DAKEEMTTFL NLVASEPEIA RVPVMIDSSK WEVIEAGLKC LQGKSIVNSI SLKEGEEKFL EHARTVRQYG AAVVVMAFDE KGQADTATRK IEVCERAYHL LVDKIGFNPH DIIFDPNVLA VATGIEEHNN YAVDFIEATA WIKKNLPGAH ISGGVSNLSF SFRGNNYIRE AMHAVFLYHA IQKGMDMGIV NPGTSVLYTD IPADVLERIE DVVLNRRSDA AERLIELADR LKESSAGNTS AGQPVKHDAW RDGTVEERLQ YALVKGIGDF LEEDLAEALP KYDKAVDVIE GPLMNGMNHV GELFGAGKMF LPQVVKTART MKKAVAILQP IIESEKVEGT ASAGKVLLAT VKGDVHDIGK NIVSVVMACN GYDIIDLGVM VPAESIVQKA IEEKVDMIGL SGLITPSLEE MVHVAMELEK AGLDIPLLIG GATTSKLHTA LKIAPVYHAP VVHLKDASQN AGVAARLMSP KSKEELAKEL SGEYEALRDK SGMMKRETVS LKEAQENRLK LF // ID F7M5Z2_9BACE Unreviewed; 915 AA. AC F7M5Z2; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 01-APR-2015, entry version 20. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGN02562.1}; GN ORFNames=HMPREF0127_02876 {ECO:0000313|EMBL:EGN02562.1}; OS Bacteroides sp. 1_1_30. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=457387 {ECO:0000313|EMBL:EGN02562.1}; RN [1] {ECO:0000313|EMBL:EGN02562.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_1_30 {ECO:0000313|EMBL:EGN02562.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGN02562.1}. 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; ADCL01000058; EGN02562.1; -; Genomic_DNA. DR EnsemblBacteria; EGN02562; EGN02562; HMPREF0127_02876. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 915 AA; 99926 MW; 4E0E33F4841BBC1D CRC64; MKKTISQVVS ERILILDGAM GTMIQQYNLK EEDFRGERFA HIPGQLKGNN DLLCLTRPDV IQDIHRKYLE AGADIIETNT FSSTTVSMAD YHVEEYVREM NLAAVKLARD LADEYTAKNP DKPRFVAGSV GPTNKTCSMS PDVNNPAYRA LSYDELAASY QQQMEAMLEG GVDAILIETI FDTLNAKAAI FAAEQAMKTI GVEVPVMLSV TVSDIGGRTL SGQTLDAFLA SVQHANIFSV GLNCSFGARQ LKPFLEQLAA RAPYYISAYP NAGLPNSLGK YDQTPADMAH EVREYIEEGL INIIGGCCGT TDAYIAEYPA LVKGAKPHVP ALAPDCMWLS GLELLEVKPE INFVNVGERC NVAGSRKFLR LINEKKYDEA LSIARQQVED GALVIDVNMD DGLLDAKEEM TTFLNLIMSE PEIARVPVMI DSSKWEVIEA GLKCLQGKSI VNSISLKEGE EVFLEHARII RQYGAAAVVM AFDEKGQADT AARKIEVCER AYRLLVDKVG FNPHDIIFDP NVLAVATGIE EHNNYAVDFI EATAWIKKNL PGAHISGGVS NLSFSFRGNN YIREAMHAVF LYHAIQQGMD MGIVNPGTSV LYSDIPTDVL EKIEDVVLNR RPDAAERLIE LAESLKATMS GTAGQPAAKQ DAWREESVQE RLKYALMKGI GDFLEQDLAE ALPLYDKAVD VIEGPLMDGM NYVGELFGAG KMFLPQVVKT ARTMKKAVAI LQPIIESEKV EGSAAAGKVL LATVKGDVHD IGKNIVAVVM ACNGYDIVDL GVMVPAETIV QRAIEEKVDM IGLSGLITPS LEEMAHVALE LEKAGLDIPL LIGGATTSKM HTALKIAPVY HAPVVHLKDA SQNASVASKL LNPQLKAELV NELNSEYEAL REKSGLLKRE TVSLEEAQKN KLNLF // ID F7MN46_CLOBO Unreviewed; 265 AA. AC F7MN46; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGO87777.1}; DE Flags: Fragment; GN ORFNames=CBCST_09706 {ECO:0000313|EMBL:EGO87777.1}; OS Clostridium botulinum C str. Stockholm. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=929505 {ECO:0000313|EMBL:EGO87777.1}; RN [1] {ECO:0000313|EMBL:EGO87777.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Stockholm {ECO:0000313|EMBL:EGO87777.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGO87777.1}. 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; AESA01000100; EGO87777.1; -; Genomic_DNA. DR RefSeq; WP_003380761.1; NZ_AESA01000100.1. DR EnsemblBacteria; EGO87777; EGO87777; CBCST_09706. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; FT NON_TER 265 265 {ECO:0000313|EMBL:EGO87777.1}. SQ SEQUENCE 265 AA; 28842 MW; 41B52BFEE58AA190 CRC64; MIDINKILLK KHIFFDGAMG TMLQNRGISL GEIPPEIYNI LNPKVIKDIH KKYIDAGVDI ITTNTFGANE LKLKDSGYSV EEVIEAGVKL AKEVSNGSIV ALDIGPTGEM LEPIGNLKFN RAYEIFKRQV IAGVNAGCDI ILIETISDLY EAKAAILAAK ENSELPVFCT MTFGEDGRTF TGTDPLTMVS VLESLSVDAL GVNCSLGPKE ILGVVEEIIK YSSIPIIVQP NAGLPRVENN KTIFDITPKE FAFYEKVMAN KGVSI // ID F7N410_ECOLX Unreviewed; 1227 AA. AC F7N410; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGP22519.1}; GN ORFNames=PPECC33_40050 {ECO:0000313|EMBL:EGP22519.1}; OS Escherichia coli PCN033. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1001989 {ECO:0000313|EMBL:EGP22519.1}; RN [1] {ECO:0000313|EMBL:EGP22519.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PCN033 {ECO:0000313|EMBL:EGP22519.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGP22519.1}. 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; AFAT01000083; EGP22519.1; -; Genomic_DNA. DR RefSeq; WP_000096053.1; NZ_AFAT01000083.1. DR EnsemblBacteria; EGP22519; EGP22519; PPECC33_40050. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136040 MW; D1A76336C7330E3D CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID F7NIH1_9FIRM Unreviewed; 799 AA. AC F7NIH1; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Methionine synthase, putative {ECO:0000313|EMBL:EGO64201.1}; GN ORFNames=ALO_09369 {ECO:0000313|EMBL:EGO64201.1}; OS Acetonema longum DSM 6540. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Acetonema. OX NCBI_TaxID=1009370 {ECO:0000313|EMBL:EGO64201.1}; RN [1] {ECO:0000313|EMBL:EGO64201.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 6540 {ECO:0000313|EMBL:EGO64201.1}; 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. {ECO:0000313|EMBL:EGO64201.1}. 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; AFGF01000074; EGO64201.1; -; Genomic_DNA. DR RefSeq; WP_004094995.1; NZ_AFGF01000074.1. DR EnsemblBacteria; EGO64201; EGO64201; ALO_09369. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; SQ SEQUENCE 799 AA; 84384 MW; 045D68110A04672B CRC64; MIYLFDGAMG TMLQQAGLPA GACPELWNLE YPDQIAAIHR QYVEAGADII ETNTFGGSRI KLSHYGLEGQ VAAINRAAVQ AARQACGPHT KVAGSVGPTG RFIEPLGDLS FQDAFNAFAE QITALDQAGA DMMIIETIID IQEMRAALLA AKSVCRKPVI CQLTFETDGR TFTGTDAHTA AVILSPLGAD VIGANCSLGP AQLLLVLETL VKATHKPISI QPNAGLPTLE GDQTHFPMGP EEFSHWIPKL IAAGAHYVGG CCGTTPQHIK AAREAIDATG ATRQSPLLPQ PSPYVALASR SKTVYIGQQY PTVVIGERIN PTGRRKLAAE IKEGSFTTVK KDALGQLQAG ARVLDVNMGV PGIDQAAAMK KAVQELSMLV DAPLAIDTTD PQALEAGLAA FPGRALVNSV SAEPERLEHF LPLAKKYGAA ILCLPLAAGG LPATARERVA IAQNIVAAAL AAGLSENDLM LDALTLTIAT DGEAARQTLA TLQLYRQHFG YPTVMGLSNI SYGLPRRDMI NAAFCAMSLH AGLDAPILNP YDPLMQDILA TSAVLLGHDA HARQFSARYA YTPPGFPGAP HEIDTSHILG KIKHCVIQGE KEAVAPLIEQ AIQEGYQPLT ITDEALTVAM NEVGQAFSAG RSFLPHVMLS AETMRSAFQA IKTYLPAHSV RSLGKVVLAT VKGDIHDLGK NIVAALLENN GFTVIDLGKD VPADTIVAAC REHQPDIVGL CALMTTTLPQ IDHTIRELRA AGSPAHTFTI VGGAVLTKEY AAQAGADAYA ANGVVAVELC KSMIASRHL // ID F7NU08_9GAMM Unreviewed; 354 AA. AC F7NU08; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Cobalamin-dependent methionine synthase I {ECO:0000313|EMBL:EGM78677.1}; GN ORFNames=Rhein_1249 {ECO:0000313|EMBL:EGM78677.1}; OS Rheinheimera sp. A13L. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Rheinheimera. OX NCBI_TaxID=506534 {ECO:0000313|EMBL:EGM78677.1}; RN [1] {ECO:0000313|EMBL:EGM78677.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A13L {ECO:0000313|EMBL:EGM78677.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGM78677.1}. 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; AFHI01000009; EGM78677.1; -; Genomic_DNA. DR RefSeq; WP_008898134.1; NZ_AFHI01000009.1. DR EnsemblBacteria; EGM78677; EGM78677; Rhein_1249. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 354 AA; 38521 MW; FD39F3042C35DD30 CRC64; MTNRSVLTPD ALRALLGQRI LVLDGAMGTM IQQYKLQEED YRGTEFANWS TDLKGNNDLL VLTKPELILD IHRQYLAAGA DILETNSFNA TPIAMADYDM SHLSARINRE SAALARQACD EYSTPDKPRF VAGVLGPTNR TASISPDVND PGYRNVDFDT LVEAYCESTH ALIEGGADII MLETIFDTLN AKAAAFAVLK VFDELGFSLP VMISGTITDA SGRTLSGQTT EAFYHSLAHV QPVSFGLNCA LGPDLLRPYV ETLSGISECY VSVHPNAGLP NEFGEYDLDA VEMAKEIADW AEQGFLNIVG GCCGTTPEHI RAISDVVAGK PARQPKEKTH QFHLSGLEAF GLEW // ID F7QIR4_9BRAD Unreviewed; 1285 AA. AC F7QIR4; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 01-APR-2015, entry version 21. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EGP08877.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGP08877.1}; GN ORFNames=CSIRO_1448 {ECO:0000313|EMBL:EGP08877.1}; OS Bradyrhizobiaceae bacterium SG-6C. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae. OX NCBI_TaxID=709797 {ECO:0000313|EMBL:EGP08877.1, ECO:0000313|Proteomes:UP000003148}; RN [1] {ECO:0000313|EMBL:EGP08877.1, ECO:0000313|Proteomes:UP000003148} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SG-6C {ECO:0000313|EMBL:EGP08877.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGP08877.1}. 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; AFOF01000016; EGP08877.1; -; Genomic_DNA. DR RefSeq; WP_009735109.1; NZ_CM001195.1. DR EnsemblBacteria; EGP08877; EGP08877; CSIRO_1448. DR Proteomes; UP000003148; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000003148}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGP08877.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000003148}; KW Transferase {ECO:0000313|EMBL:EGP08877.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 251 251 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 315 315 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 771 771 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1285 AA; 141223 MW; C00FFF8D623E3427 CRC64; MSSRPISPIA EKFRALAREK ILVLDGAMGT MIQGLQFDEA AFRGERFKDF HRDVKGNNDL LILTQAQAIE DIHYAYLKAG ADIVATNTFS STSIAQADYD MSDLAYEMNR EGARLARNAA KRAEADDGKP RFVAGALGPT NRTASISPDV ANPGYRAVTF DDLRISYSEQ INGLLDGGAD LLLVETIFDT LNAKAALYAI AEITEARGIH VPVMVSGTIT DKSGRLLSGQ LPEAFWYSVQ HANPITIGFN CALGAEDLRA HIADIGRVAD TLVCAYPNAG LPNEFGQYDE TPEYMARLVG EFAQAGLVNV VGGCCGTTPA HIKAIADACA PHKPRVVPEI PPLLRLSGLE PFNLTSDIPF VNVGERTNVT GSARFRKLIK NGDYTAALQV ARDQVENGAQ VIDINMDEGL LDSKQAMIDY LNLVASEPDI ARVPVMIDSS KFDVIEAGLK CVQGKPIVNS ISMKEGEEKF LHEAAIARRH GAAVVVMAFD EVGQADTFER KTEICARAYK LLVEKLDFPP QDIIFDPNIF AIATGLEEHN NYGVDFIEAT RWIRQNLPHA HISGGVSNLS FSFRGNEPVR EAMHSVFLYH AIKAGMDMGI VNAGQMVIYD DIDPELRQVC EDTILNRDPG ASERLLELAE KFRGQEKQEK VQDLAWREWP VEKRLSHALV NGITEYIDAD TEAARLTVER PLNVIEGPLM DGMNIVGDLF GAGKMFLPQV VKSARVMKQA VAYLMPFMEE EKARNQAAGI AGDGRNSAGK IVLATVKGDV HDIGKNIVGI VLQCNNFEVV DLGVMVPASK IIETAKAENA DIIGLSGLIT PSLDEMVFLA SELERQGLDL PLLIGGATTS RVHTAVKIDP AYQRGPVVHV NDASRAVGVA SSLLSPEKKA EYAREVRADY AKISAAHFRA QQNKNRLSLA AARANAHTID WSKTRPTKPA FIGLKSFSDY SLRELADYID WTPFFQTWEL AGRFPAILDD PKVGEAARAL YDDARKMLDR IIEENWFKAN ATIGFWPANA EGDDIVLYSD EARTRPITTL HTLRQQLEKR EGRHNAALSD FIAPVSSGVP DYIGMFVVTA GIGEDVIADR FKNSNDDYSS ILVKALADRL AEAFAERMHE RVRKEFWGYA PDENLSSDEM IREEYQGIRP APGYPAQPDH TEKATLFRLL DAERTAGVTL TESFAMWPGS SVSGLYFSHP ESYYFGVGKI ERDQVEDYAE RKGMTPEEIE RWLAPILNYI PSRDARPDAD EPDVVDLPLA KHPPGCACAM HLRMNGKPVA DAVAR // ID F7QT41_9LACO Unreviewed; 307 AA. AC F7QT41; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:EGM51889.1}; GN ORFNames=LSGJ_00309 {ECO:0000313|EMBL:EGM51889.1}; OS Lactobacillus salivarius GJ-24. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1041521 {ECO:0000313|EMBL:EGM51889.1}; RN [1] {ECO:0000313|EMBL:EGM51889.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=GJ-24 {ECO:0000313|EMBL:EGM51889.1}; RX PubMed=21742893; DOI=10.1128/JB.05616-11; RA Cho Y.J., Choi J.K., Kim J.H., Lim Y.S., Ham J.S., Kang D.K., Chun J., RA Paik H.D., Kim G.B.; RT "Genome Sequence of Lactobacillus salivarius GJ-24, a Probiotic Strain RT Isolated from Healthy Adult Intestine."; RL J. Bacteriol. 193:5021-5022(2011). RN [2] {ECO:0000313|EMBL:EGM51889.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=GJ-24 {ECO:0000313|EMBL:EGM51889.1}; RA Cho Y.-J., Choi J.K., Kim J.-H., Kim G.-B.; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGM51889.1}. 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; AFOI01000002; EGM51889.1; -; Genomic_DNA. DR RefSeq; WP_003707473.1; NZ_AFOI01000002.1. DR EnsemblBacteria; EGM51889; EGM51889; LSGJ_00309. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EGM51889.1}; KW Transferase {ECO:0000313|EMBL:EGM51889.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 223 223 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 307 AA; 34597 MW; E49B8B1FCC22A92F CRC64; MDFTEFLTNH TVVLDGAMST PLERLGADTN NDLWTAKALI DNEELVYEVH KMYFEAGADL IITDTYQANV QAFEKVGYSE KEARNLIKKA VKIAQKARDD YENRTGKHNY IAGTIGPYGA YLANGSEYRG DYELSVEEYQ QFHLPRIEEL VNAEVDILAI ETQPKLDEVL AILELLKEKY PQQKVYVSYT LSDDDTISDG TPLPRAIHAL EDYSQVIAVG INCVKLELVE PALKNMKEIT DKHLIVYPNS SAVYDPKSKT WSQPKTSATF EELIPNWYEA GARIIGGCCT TGPKEIKAVA DFIKRNR // ID F7RJH1_9GAMM Unreviewed; 1244 AA. AC F7RJH1; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 01-APR-2015, entry version 19. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EGM71596.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGM71596.1}; GN ORFNames=SOHN41_00512 {ECO:0000313|EMBL:EGM71596.1}; OS Shewanella sp. HN-41. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=327275 {ECO:0000313|EMBL:EGM71596.1}; RN [1] {ECO:0000313|EMBL:EGM71596.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HN-41 {ECO:0000313|EMBL:EGM71596.1}; 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] {ECO:0000313|EMBL:EGM71596.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HN-41 {ECO:0000313|EMBL:EGM71596.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGM71596.1}. 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; AFOZ01000013; EGM71596.1; -; Genomic_DNA. DR RefSeq; WP_007645192.1; NZ_AFOZ01000013.1. DR EnsemblBacteria; EGM71596; EGM71596; SOHN41_00512. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGM71596.1}; KW Transferase {ECO:0000313|EMBL:EGM71596.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 258 258 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 774 774 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1244 AA; 138007 MW; 7046627FF7E5537A CRC64; MAISTHRASQ ILADIRNQLS KRILILDGAM GTMIQGYKLE EEDYRGERFK DWHTDVKGNN DLLVLTQPHI IKQIHTDYLN AGADIIETNT FNATTIAMAD YDMQSLSAEI NREGARLARE ACDEIAAATG IPRYVAGVLG PTNRTCSISP DVNDPGYRNV SFDELVTAYK ESTKALIEGG ADIIMVETIF DTLNAKAALF AIESVFDDLF GQHSNDRLPI MISGTITDAS GRTLTGQTTE AFYNSLRHIK PLSIGLNCAL GPKELRPYVE ELSRIAECYV SAHPNAGLPN EFGGYDETPE DMANVIEDWA REGMLNIIGG CCGSTPEHIR VIRQAVERYS PRTLPDIPVA CRLSGLEPLT IDAQTLFVNV GERTNVTGSA KFLKLVKEGK FEQALDVARE QVESGAQIID INMDEGMLDG VEIMHKFLNL IASEPDISRV PIMIDSSKWE VIEAGLKCIQ GKGIVNSISL KEGEAKFIEQ ATLVKRYGAA AIIMAFDEQG QADTKARKIE ICTRAYRVLV DKVGFPPEDI IFDPNIFAIA TGIDEHDNYA VDFIDAIKEI KATLPHAMIS GGVSNVSFSF RGNNPVREAI HAVFLYHAIK VGMDMGIVNA GQLAIYDDID PELKERVENV VLNLPCPVEG SSNTEQLLEI AEKFRGDGST GAKKEDLEWR SWPVNERLAH ALVKGITEFI DEDTEAARQG ASRPLDVIEG PLMDGMNIVG DLFGSGKMFL PQVVKSARVM KKAVAYLNPF IEKEKVAGQS NGKILMVTVK GDVHDIGKNI VGVVLACNGF EVFDLGVMVS VERILEAVKE HNIDIIGMSG LITPSLDEMV HNVKTFHREG LTIPAIIGGA TCSKIHTAVK IAPHYPHGAI YIADASRAVP MVSKLVNNET RQATIDETYA EYDDMRTKRL SQAKRKEIVS LEAARDNRCQ HDWANYTPFT PKVLGRQVFE DYPLTDLVDR IDWTPFFRAW ELHGHYPEIL TDKVVGVEAQ KLFADGQAML KKIIEEKWLT AKGVIGLFPA NTVNFDDIEL YTDESRTEVE MTTHHLRMQL ERVGNDNFCL ADFVAPKDSG VADYMGGFAV TAGHGIDEHV ARFEANHDDY NAIMLKCLAD RLAEAFAERM HERVRKEFWG YAADEQLDNE ALIREKYKGI RPAPGYPACP DHTEKGLLWE LLKPNETIDL NITESYAMFP TAAVSGWYFA HPKSRYFGVS NIGRDQVEDY AKRKGMTVAE TEKWLAPVLD YDPE // ID F7S3X5_9PROT Unreviewed; 1141 AA. AC F7S3X5; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 01-APR-2015, entry version 19. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGO96146.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGO96146.1}; GN ORFNames=APM_1026 {ECO:0000313|EMBL:EGO96146.1}; OS Acidiphilium sp. PM. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acidiphilium. OX NCBI_TaxID=1043206 {ECO:0000313|EMBL:EGO96146.1}; RN [1] {ECO:0000313|EMBL:EGO96146.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PM {ECO:0000313|EMBL:EGO96146.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGO96146.1}. 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; AFPR01000096; EGO96146.1; -; Genomic_DNA. DR RefSeq; WP_007422180.1; NZ_AFPR01000096.1. DR EnsemblBacteria; EGO96146; EGO96146; APM_1026. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGO96146.1}; KW Transferase {ECO:0000313|EMBL:EGO96146.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 204 204 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 270 270 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 271 271 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 712 712 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1141 AA; 125902 MW; C2017DAA0B0160FA CRC64; MGSRVQALTL DTERDFWGKE NCTEVLNLSR PDLVREIHRG YYEAGADMVE TNSFGGSPIT LAEFELGDRA REINRIAAEL AREAAETFAD GRDRYVIGSV GPGTKLPTLG NIEYDPLEAG LAEQCRGLIE GGVDAILIET CQDTLQIKAA VNGARIARAE QKRDTPIFVQ VTVETTGTLL VGPDIAAAAT VIQALDVPLI GLNCATGPQE MAEHVRYLAQ NWPGLISVQP NAGLPELVDG KTHYPLTPDE LATWLERFIR EDGINLIGGC CGTSTPHIAA LDAMLRRLGE VRPAPVPRKP VWIPSVASLY GSTPLRQENA YFSIGERCNA NGSKKWRELQ EKHDWDGCIA MGREQVAEAS NALDICTAFV GRDELGEMSE IITRFTSSVN APLVIDSTET PVIEAALKLH GGKPIINSIN FEDGEHIAEE RMLLARKFGA AVIALTIDET GMAKEPAQKL EIATRLVDFA CRKHGLPQSD LLIDPLTFTI ATGNEDDRKL GLWTLEGIKL IRDAFPDIQI ILGLSNISFG LNPAARAVLN SVFLDHAVKA GMTGAIVHVS KIRPLHLIPP EEVRVMEDLI FDRRREDYDP LQRVLEMFAD RKAADAVKKA RADTVEGRLR DRIVDGDRKG LADDLDEAMK THAPLDIINN LLLDGMKTVG ELFGAGKMQL PFVLQSAETM KAAVAYLEPY MERVEGQQKG TIVLATVKGD VHDIGKNLVD IILTNNGYRV VNLGIKVPLA DMVAAAREHR AHAIGMSGLL VKSTVVMREN LEEMSRQGLD IPVLLGGAAL TRNYVEEDCV AAYASGRVAY ARDAFDGLHL MDRVTGNGFD DYLAALQSKR RGKARNTKRT LGQADARGFA PVDISAAQAR RRRLTRETPV PTPPFWGARI IEAPQKALVP YINERSLFQF QWGFRKQGKS LEDFMGWARQ ELRPVMKRML DLCAADSILK PQAIYGYWKA AGQGNDLILF AEDGATELAR FTLPRQPRDD GECIADFFRD VDDAERDVIG LQVVTMGAKA SETARAWFEE NRYQDYLYLH GLSVEMAEAM AEYTHKRIRA ELGFAAEDDR DMEKMLAQSY RGSRYSFGYP ACPNLEDQSL LLRLLDAERI GVSLSDEHQL HPEQSTSAIV VLNPHAKYFS V // ID F7SIQ0_9GAMM Unreviewed; 123 AA. AC F7SIQ0; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 29-OCT-2014, entry version 12. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:EGP21454.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EGP21454.1}; DE Flags: Fragment; GN Name=mmuM {ECO:0000313|EMBL:EGP21454.1}; GN ORFNames=GME_01789 {ECO:0000313|EMBL:EGP21454.1}; OS Halomonas sp. TD01. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=999141 {ECO:0000313|EMBL:EGP21454.1}; RN [1] {ECO:0000313|EMBL:EGP21454.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TD01 {ECO:0000313|EMBL:EGP21454.1}; 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. {ECO:0000313|EMBL:EGP21454.1}. 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; AFQW01000005; EGP21454.1; -; Genomic_DNA. DR RefSeq; WP_009721628.1; NZ_GL949754.1. DR EnsemblBacteria; EGP21454; EGP21454; GME_01789. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGP21454.1}; KW Transferase {ECO:0000313|EMBL:EGP21454.1}. FT NON_TER 123 123 {ECO:0000313|EMBL:EGP21454.1}. SQ SEQUENCE 123 AA; 13139 MW; 1186311F9A59766D CRC64; MSELNPIKAL LADVPFMVID GAMATELETL GCDLNDALWS ARLLAQAPEK IRQVHQAYFE AGADCAITAS YQATVPGFMQ AGLTAQEARE LIQLSVTLAQ QARDAVWQPG QTDRPKPLVA GAG // ID F7SIQ1_9GAMM Unreviewed; 182 AA. AC F7SIQ1; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 29-OCT-2014, entry version 12. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:EGP21343.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EGP21343.1}; DE Flags: Fragment; GN Name=mmuM {ECO:0000313|EMBL:EGP21343.1}; GN ORFNames=GME_01794 {ECO:0000313|EMBL:EGP21343.1}; OS Halomonas sp. TD01. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=999141 {ECO:0000313|EMBL:EGP21343.1}; RN [1] {ECO:0000313|EMBL:EGP21343.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TD01 {ECO:0000313|EMBL:EGP21343.1}; 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. {ECO:0000313|EMBL:EGP21343.1}. 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; AFQW01000006; EGP21343.1; -; Genomic_DNA. DR RefSeq; WP_009721629.1; NZ_GL949754.1. DR EnsemblBacteria; EGP21343; EGP21343; GME_01794. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGP21343.1}; KW Transferase {ECO:0000313|EMBL:EGP21343.1}. FT NON_TER 1 1 {ECO:0000313|EMBL:EGP21343.1}. SQ SEQUENCE 182 AA; 19108 MW; AD4EF11ABBF7FEF0 CRC64; AGLVAFHRER FELLLAAGAD LLAAETLPSL DEALAITDLL AEHPGAQAWI TFSAKDGKHI SDGTPIEECA AALANCPGVA AIGVNCTALP HIESLIQAIR RQCDLPVLVY PNSGEVYDAV TKTWHPATCD HTASGPSALA QGVEQWLAAG ASAIGGCCRT APADIQALAQ WRRSRPLSES YR // ID F7SRQ3_9GAMM Unreviewed; 1231 AA. AC F7SRQ3; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 01-APR-2015, entry version 20. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EGP18690.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGP18690.1}; GN Name=metH {ECO:0000313|EMBL:EGP18690.1}; GN ORFNames=GME_15915 {ECO:0000313|EMBL:EGP18690.1}; OS Halomonas sp. TD01. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=999141 {ECO:0000313|EMBL:EGP18690.1}; RN [1] {ECO:0000313|EMBL:EGP18690.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TD01 {ECO:0000313|EMBL:EGP18690.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGP18690.1}. 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; AFQW01000075; EGP18690.1; -; Genomic_DNA. DR RefSeq; WP_009724406.1; NZ_GL949760.1. DR EnsemblBacteria; EGP18690; EGP18690; GME_15915. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGP18690.1}; KW Transferase {ECO:0000313|EMBL:EGP18690.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1231 AA; 136061 MW; E2060EDA6F7B7BA7 CRC64; MAASDLTASL TQRLAQRILI LDGGMGTMLQ NAELSEDDFR SDRFRDWPSD LKGNNDLLAL TCPDLVVRIH RDYLEAGADI IETNTFNSTR LSQSDYGMED LVPELNRESA RLARNVCDAV AAETNIPRYV AGVLGPTSRT ASLSPDVNDP SKRNVTFDEL RENYYEAASA LIEGGADLIM IETIFDTLNA KAAIYALEEL FDDLGTRLPV MISGTITDAS GRTLSGQTTE AFWNSVRHAQ PLSVGLNCAL GAEELRPYIE ELSTKADTFV SAHPNAGLPN EFGEYDQTPE EMAAIVSEFA ESGLVNIIGG CCGSTPEHIQ AIAEAVSSMA PRKVARRSHA CRLSGLEPFN IEADSLFVNV GERTNVTGSA RFKRLIVEED FTTALEVALE QVENGAQIID INMDEGMLES QEAMVRFLNL IAGEPDIARV PIMIDSSKWD IIEAGLKCVQ GKAVVNSISL KEGEAAFREQ ATKCRRFGAA IVVMAFDEEG QADTFARKTE ICERAYRLLV DDIGFPAEDI IFDPNIFAIA TGIDEHNNYA VDFIEATQWI REHLPHAMIS GGVSNVSFSF RGNNPVREAI HSVFLYHAIR AGLSMGIVNA GQLAVYDDLP AELRDAVEDV VLNRRSDGTE RLLDLADKYK GDGSGAAKKE DLEWRSWPVN KRIEHALVKG VTAYIEDDTE QARAEAARPI EVIEGPLMDG MNVVGDLFGA GKMFLPQVVK SARVMKQAVA YLIPYIEAEK SEETKAKGKI VMATVKGDVH DIGKNIVGVV LQCNNYEVID LGVMVPTEKI LQAALDHNAD IIGLSGLITP SLDEMVHVAK EMKRRGMNLP LLIGGATTSK AHTAVKIEPQ YDHPVIYVTD ASRAVGVAGR LLAPNLKAAY VAEIREEYEK VRERNAKRRP KAADLDYTQA RKRRFRTDWN SLTPVKPQVL GLKTFDDYDL EELVERIDWT PFFMSWQLAG KYPKILEDKV VGEAARNLFA DAKVMLRKLI DEKRVQARGV IGLWPANSVD DDVIEVYADE SRTEVVERLH HIRQQTTKGR DGICYSLADF IAPKESGKAD WIGGFAVTTG HGVDELSKAY EAAGDDYNAI MVQALTDRLA EAFAERMHER VRKEFWGYVP EETLDNDALI AEKYQGIRPA PGYPACPDHT EKATLFRLLD ATENTGLALT ENFAMWPAAA VSGWYFAHPQ SKYFSTGKIT RDQVEAIAQR KQMPLVEMER WLSPVLSYDP S // ID F7T108_9BURK Unreviewed; 1257 AA. AC F7T108; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EGP45989.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGP45989.1}; GN Name=metH {ECO:0000313|EMBL:EGP45989.1}; GN ORFNames=AXXA_13084 {ECO:0000313|EMBL:EGP45989.1}; OS Achromobacter insuavis AXX-A. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Achromobacter. OX NCBI_TaxID=1003200 {ECO:0000313|EMBL:EGP45989.1}; RN [1] {ECO:0000313|EMBL:EGP45989.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AXX-A {ECO:0000313|EMBL:EGP45989.1}; RA Bador J., Amoureux L., Neuwirth C.; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGP45989.1}. 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; AFRQ01000047; EGP45989.1; -; Genomic_DNA. DR RefSeq; WP_006392641.1; NZ_GL982453.1. DR EnsemblBacteria; EGP45989; EGP45989; AXXA_13084. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGP45989.1}; KW Transferase {ECO:0000313|EMBL:EGP45989.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 256 256 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 789 789 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1257 AA; 138552 MW; 9CEFA14711745B69 CRC64; MSYPRLPYPP ERFTRGGDFA RLLGQRILIL DGAMGTMIQR YKLGEADFRG ERFADHGKDL KGDNELLSLV RPDVISEIHR QYLEAGADVI ETNTFGATSI AQGDYDLPEL AYELNLVSAR LAREACDQYS TPDKPRFVAG ALGPQPKTAS ISPDVNDPGA RNVTFDELRV AYIEQLNGLL DGGIDIVLIE TIFDTLNAKA AIFATEEVFE QRGIRLPVMI SGTVTDASGR ILSGQTVEAF WNSVRHARPV TIGLNCALGA ALMRPYVAEL SKICDTYVCV YPNAGLPNPM AETGFDETPA DTSALLEEFA RAGLVNMSGG CCGTTPDHIR AIADKVTALT PRVVPDIPVK TRLSGLEPLN IDEDTLYVNV GERTNVTGSK MFARLIREEK YDEALAVARQ QVENGAQIID INMDEAMLDS VACMHRFLNL IASEPDIARV PVMIDSSKWD VIETGLKCVQ GKPVVNSISM KEGLEPFRHH ARLCRRYGAA VVVMAFDELG QADTLERRKE ICGRAYKILV EEEGFPPEDI IFDPNVFAVA TGIDEHNHYA VDFIEGTRWI RENLPHARIS GGVSNVSFSF RGNEPMREAI HTVFLYYAVK EGMTMGIVNA GQLGVYADLD PKLRDLVEDV VLDRAEPVGK TDPADERTPT ERLVQFADTV KGSGAKKEED LAWRNAEVEA RLSHALVHGI TAFIVEDTEE VRQKIAARGG RPIEVIEGPL MDGMNVVGDL FGEGKMFLPQ VVKSARVMKQ AVAHLIPFIE EEKRQIAAAG GDVRAKGKIV IATVKGDVHD IGKNIVSVVL QCNNFEVVNM GVMVPCAQIL EKAKEENADI VGLSGLITPS LEEMAYVASE MQRDEYFRSR KVPLMIGGAT TSRVHTAVKI APNYEGPVIY VPDASRSVGV ATNLMSDQSD AYLAELAEEY EDVRRRHANR KAAPILPLAE ARASRPRIDW DSYTPPRPKF IGRRTFKSYD LAEIAKYVDW GPFFQTWSLF GPFPAILDDK VVGEQARKVY ADGLAMLKRI VEGRWLTANG VVGFYPANSV NDEDIEVYKD ESRSEVLFTY RNLRQQGAKR EGVSNKSLSD FIAPKASGKL DYIGMFAVTA GLGIEKKEAE FEKALDDYSG IMLKSLADRL AEAFAECLHA RVRQDLWGYA ADEALSNDDM IAEKYVGIRP APGYPACPEH VVKTDMFRVL DGADIGMMLT DSYAMFPASS VSGFYFSHPQ SQYFNVGIIG EDQLQDYAAR SGRSIEDLKR TLAPNLG // ID F7U800_RHIRD Unreviewed; 1257 AA. AC F7U800; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EGP56459.1}; GN Name=metH {ECO:0000313|EMBL:EGP56459.1}; GN ORFNames=Agau_C200267 {ECO:0000313|EMBL:EGP56459.1}; OS Agrobacterium tumefaciens F2. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium; OC Agrobacterium tumefaciens complex. OX NCBI_TaxID=1050720 {ECO:0000313|EMBL:EGP56459.1}; RN [1] {ECO:0000313|EMBL:EGP56459.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F2 {ECO:0000313|EMBL:EGP56459.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGP56459.1}. 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; AFSD01000002; EGP56459.1; -; Genomic_DNA. DR RefSeq; WP_003494782.1; NZ_AFSD01000002.1. DR EnsemblBacteria; EGP56459; EGP56459; Agau_C200267. DR GeneID; 23241157; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 260 260 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 776 776 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1257 AA; 138651 MW; C2522F66AE347CC9 CRC64; MFDDLFGPEG AKRDGAEILQ ALRAAASERI LILDGAMGTQ IQGLGFDEDH FRGDRFIGCA CHQKGNNDLL ILTQPDAIED IHYRYAMAGA DILETNTFSS TRIAQADYEM ENAVYDLNRE GAAIVRRAAQ RAEREDGRRR FVAGAIGPTN RTASISPDVN NPGYRAVSFD DLRIAYGEQI DGLIDGGADI ILIETIFDTL NAKAAIFACE ERFEAKGIRL PVMISGTITD LSGRTLSGQT PSAFWNSVRH ANPFTIGLNC ALGADAMRPH LQELSDVADT FVCAYPNAGL PNEFGQYDET PEMMARQVQG FVRDGLVNIV GGCCGSTPEH IRAIAEAVKG YKPREIPEHK PFMSLSGLEP FVLTKDIPFV NVGERTNVTG SARFRKLITA GDYTAALAVA RDQVENGAQI IDINMDEGLI DSEKAMVEFL NLIAAEPDIA RVPVMIDSSK FEIIEAGLKC VQGKSIVNSI SLKEGEEKFL QQARLVHNYG AAVVVMAFDE VGQADTYQRK VEICSRAYKL LTEKAGLSPE DIIFDPNVFA VATGIEEHNN YGVDFIEATK TIRETMPLTH ISGGVSNLSF SFRGNEPVRE AMHAVFLYHA IQVGMDMGIV NAGQLAVYDN IDAELREACE DVVLNRRDDA TERLLEVAER FRGTGEKQAK VQDLSWREFS VEKRLEHALV NGITEFIDAD TEEARQKAAR PLHVIEGPLM AGMNVVGDLF GSGKMFLPQV VKSARVMKQA VAVLLPYMEE EKRLNGGSER SAAGKVLMAT VKGDVHDIGK NIVGVVLACN NYEIIDLGVM VPTTKILETA IAEKVDVIGL SGLITPSLDE MVHVAAEMER QGFNIPLLIG GATTSRVHTA VKIHPRYEQG QAIYVTDASR AVGVVSALLS AEQKPAYIDG IRSEYAKVAE AHARNEREKQ RLPLTRAREN AHKIDWSSYS VVKPQFFGTR VFETYDLEEL SRYIDWTPFF QTWELKGRYP AILEDEKQGE AARQLYSDAQ AMLKKIIDEK WFRPRAVIGF WPANAVGDDI RLFTDESRKE ELATFFTLRQ QLSKRDGRPN VALSDFVAPV DSGVADYVGG FVVTAGIEEV AIAERFERAN DDYSSILVKA LADRFAEAFA ERMHERVRKE FWGYAPEESL AGEELIGEAY AGIRPAPGYP AQPDHTEKKT LFSLLDATNA AGVELTESYA MWPGSSVSGL YIGHPESYYF GVAKVERDQV LDYARRKDMP VEEVERWLGP VLNYVPTSGA EEIDSAA // ID F7V1U9_CLOSS Unreviewed; 587 AA. AC F7V1U9; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 01-APR-2015, entry version 25. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=CXIVA_07610 {ECO:0000313|EMBL:BAK46728.1}; OS Clostridium sp. (strain SY8519). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1042156 {ECO:0000313|Proteomes:UP000008937}; RN [1] {ECO:0000313|Proteomes:UP000008937} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SY8519 {ECO:0000313|Proteomes:UP000008937}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; BAK46728.1; -; Genomic_DNA. DR RefSeq; WP_013976710.1; NC_015737.1. DR RefSeq; YP_004707830.1; NC_015737.1. DR EnsemblBacteria; BAK46728; BAK46728; CXIVA_07610. DR KEGG; cls:CXIVA_07610; -. DR KO; K00547; -. DR BioCyc; CSP1042156:GHDR-785-MONOMER; -. DR Proteomes; UP000008937; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008937}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000008937}. SQ SEQUENCE 587 AA; 64995 MW; 44D9A02B226CBD3C CRC64; MNIRESIEQE VLVFDGAFGT YYTEKYPEEK LPCETANINH PERVLTIHRE YLEAGCRALK TNTFGAYPEN LGKADQEAVI KEGYRLAQEA AAGKAYVFAD LGPAPGNDAP ERAEAFCQAA EIFIRCGAQN FLMETNCSNE GIPEALQFIR ERVPDAFILV SYAAFPDGYT REGFYFKKLM TEISDTGLCD VVGLNCVCGS RHMGELLGRL GGTDMKLFAM PNAGYPTMRG NRTFYDGNAE YFASQTADFV SSGVRIIGGC CGTTPKHMEL VVGRLSGQRV PKLLRQPAHG TAKEPAVRAE NPFFEKISQG KKVIAVELDS PKDTNLEKFM GCARDLKEAG ADAMTIADCP IAQARMDSTL LACKVKRELN LDVLPHMTCR DRNINAAKAL LLAAHAEQIR NVLIITGDPI PTAQREEIPS VFQFNSVKMA AYLQSLNEEL FEDPFRVFGA LNINAVNFDS ELKRAKKKEE AGMVGFLTQP VLSEEAKENL IRAHEELSGK ILGGIIPVVS ERNARFMESE VNGIHVSEEI IARYVGKDRE EAENLACEIS CRIAEEIAPY VDGYYLMTPF QRTKLMRRII SGISHLC // ID F7V424_CLOSS Unreviewed; 464 AA. AC F7V424; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 01-APR-2015, entry version 21. DE SubName: Full=Methionine synthase I , methyltransferase domain {ECO:0000313|EMBL:BAK47503.1}; GN Name=MetH {ECO:0000313|EMBL:BAK47503.1}; GN OrderedLocusNames=CXIVA_15370 {ECO:0000313|EMBL:BAK47503.1}; OS Clostridium sp. (strain SY8519). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1042156 {ECO:0000313|Proteomes:UP000008937}; RN [1] {ECO:0000313|Proteomes:UP000008937} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SY8519 {ECO:0000313|Proteomes:UP000008937}; 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; BAK47503.1; -; Genomic_DNA. DR RefSeq; WP_013977467.1; NC_015737.1. DR RefSeq; YP_004708605.1; NC_015737.1. DR EnsemblBacteria; BAK47503; BAK47503; CXIVA_15370. DR KEGG; cls:CXIVA_15370; -. DR KO; K00548; -. DR BioCyc; CSP1042156:GHDR-1579-MONOMER; -. DR Proteomes; UP000008937; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008937}; KW Methyltransferase {ECO:0000313|EMBL:BAK47503.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008937}; KW Transferase {ECO:0000313|EMBL:BAK47503.1}. SQ SEQUENCE 464 AA; 49607 MW; B32D075693EC7533 CRC64; MDIRERMKQG FLCYDGGMGT ALIRRGLQSG ERSERWNIDH PEEVTAVHLE FLRAGADIIL ANTFGANRFH YTQEELEQVI RAGIRCAKEA VAQSGKEAWV ALDIGSTGHL LPPMGMLPFE EAVEIFGEIV RIGADAGADL VQIETMNDVY ELKAAVLAAR ENCDLPVFAT AVFDETAHML TGTSPESAVA LLEGLGCSAV GLNCGVGPEA AEKALRIMSE YASLPLIAKP NAGLPRVENG ETYFDVTPKA FAAQMRKIME IPGVQLVGGC CGTTAEHIRQ TCEAAGEQRM LPAADKPVAL ISSYQSCVNL GDSGLQISTA IDPAKDSELL EDLQDGAIDT VLDLADEALD DEADVLSIRL AAEGVDEAAC MKEAVMELQN INTMPFAIDS TDPAAVEAGI RIYNGKALVN AGEASGETLE RICRIAARYG AVVNSQRTDR EAVRTAARDS GLKEKDLVFG LYPA // ID F7VBA1_9PROT Unreviewed; 1171 AA. AC F7VBA1; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:GAA07646.1}; GN ORFNames=ATPR_0650 {ECO:0000313|EMBL:GAA07646.1}; OS Acetobacter tropicalis NBRC 101654. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acetobacter. OX NCBI_TaxID=749388 {ECO:0000313|EMBL:GAA07646.1}; RN [1] {ECO:0000313|EMBL:GAA07646.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NBRC 101654 {ECO:0000313|EMBL:GAA07646.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:GAA07646.1}. 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; BABS01000012; GAA07646.1; -; Genomic_DNA. DR RefSeq; WP_006557662.1; NZ_BABS01000012.1. DR EnsemblBacteria; GAA07646; GAA07646; ATPR_0650. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 228 228 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 740 740 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1171 AA; 129133 MW; 8536BCCF69A1E50D CRC64; MDAMSSRLPL LDALRDQVLL CDGGMGSRIQ MLDLDLTRDY WGQENCTEIL TLSRPELIRE IHRGYYEAGA DMVETNTFGG SPITLGEFGL TDKAREINRT SAILAREAAD SFADGRARYV IGSVGPGTKL PSLGNIDYDT LEAALTEQGR GLIEGGVDAI LIETCQDTLQ IKAAVNGMKI ARAEMGTTTP IFVQVTVETT GTLLVGPDIA AATTVIHSLD VDLMGLNCAT GPQEMAEHVR WLSENWPRLI SVQPNAGLPE LVDGQTRYPL SPEEMAVWVE RFIVEDGLNL IGGCCGTSTP HIAALDAMLR RRAEGTGKHR PAPVARTSVW VPSVASLYTQ VPLRQENAYF SIGERCNANG SKKWRELQEA HDWDGCVALG REQAKEGSNA LDICTAFVGR NERAEMDEVI KRFTSSVNAP LVIDSTETPV IEAALKLHGG KPIINSINFE DGEGPAADRL TLARKFGAAV VALTIDEEGM ARRPEDKLRI ATRLIEFACD TYGLPQSDLM IDPLTFTIAT GAEDDRKLGQ WTLEGIKMIR DAFPDVQIVL GLSNISFGLN PAARAVLNSV YLDHAVRAGM TAAIVHVSKI RPLHMIAPEE VKVAEDLIFD RRTADYDPLQ KLLELFADRK ASEAVKRKRA ETVEERLKDR IVDGDRKGLE TDLEEAMAKM PPLEIINTVL LDGMKVVGEL FGAGKMQLPF VLQSAETMKA AVAWLEPHME RIEGQQRGTI VLATVKGDVH DIGKNLVDII LTNNGYKVVN LGIKVPVADM IEAAKKEKAH AIGMSGLLVK STVIMRENLE EISREGLDVP VLLGGAALTR NYVEEDCVAA YSPTGRVAYA RDAFDGLTLM DQITQNGFDD YLAAISKRRA GKATRKNART PEQAETRGYT PIDPAVARTR RARMTADEPC LKPPFWGSKV IEAPTEAVIP FLNERSLYQF QWGFRKQGRS LDDFMVWAKQ ELRPILRRML DLTAKENILR PQAAYGYWKA AGDGNDLILF EEDGVTEAAR FTLPRQPRED GECIADFVRD VSDPERDVVA LQVVTVGQKA SDIARDWFEE NRYQDYLYLH GLSVEVAEAM AEYTHKRIRA ELGFSSEDSR DLDALLQQGY RGSRYSFGYP ACPRLEDQHP ILGLLGAERI GVSLTDGDQL HPEQSTSALV ILNKHAKYFT I // ID F7VQY2_SORMK Unreviewed; 357 AA. AC F7VQY2; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 29-APR-2015, entry version 20. DE SubName: Full=WGS project CABT00000000 data, contig 2.4 {ECO:0000313|EMBL:CCC07915.1}; GN ORFNames=SMAC_01479 {ECO:0000313|EMBL:CCC07915.1}; 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 {ECO:0000313|EMBL:CCC07915.1, ECO:0000313|Proteomes:UP000001881}; RN [1] {ECO:0000313|EMBL:CCC07915.1, ECO:0000313|Proteomes:UP000001881} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell RC {ECO:0000313|Proteomes:UP000001881}; RC TISSUE=Mycelium {ECO:0000313|EMBL:CCC07915.1}; RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891; RA Nowrousian M., Stajich J.E., 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.D., Seiler S., Smith K.M., 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. {ECO:0000313|EMBL:CCC07915.1}. 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; CABT02000004; CCC07915.1; -; Genomic_DNA. DR RefSeq; XP_003352645.1; XM_003352597.1. DR GeneID; 10810270; -. DR KEGG; smp:SMAC_01479; -. DR EuPathDB; FungiDB:SMAC_01479; -. DR InParanoid; F7VQY2; -. DR KO; K00547; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000001881; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001881}; KW Reference proteome {ECO:0000313|Proteomes:UP000001881}. SQ SEQUENCE 357 AA; 39023 MW; A8BC9C8C8B3E98D2 CRC64; MVTPIPVQIL DGGLGTTLED LHGITFSFET PLWSSHLLVS GEEDKLLDCH EAFQKAGANI ISTATYQTSI NGFAATKAPK SGAPDGIGKE GIPHFLNRAV VLAANAAGKE GKVALALGPY GATMIPSTEY SGKYDPGHQD ARALEEWHKK RLDLFKDVNT NQVNYIAFET VPRLDEIVAI RNLLSTDKIP TSLRGRPVWI SSLYPNDDEK LPDGSTVEEV VRAALTRREG LETPWGIGIN CTKVEKLDSL VRRYEAALQS CIDNGEPMDW PSLVLYPDGT NGEVYNTINK TWELPPGQKQ PEAPWEVILT NVVGAARQRG KWKSIIVGGC CKTSPELIRK LQKTLQDRGY MSTSPAA // ID F7X5Y2_SINMM Unreviewed; 337 AA. AC F7X5Y2; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Betaine-homocysteine methyltransferase {ECO:0000313|EMBL:AEH78634.1}; GN Name=bmt {ECO:0000313|EMBL:AEH78634.1}; GN OrderedLocusNames=SM11_chr1358 {ECO:0000313|EMBL:AEH78634.1}; OS Sinorhizobium meliloti (strain SM11). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=707241 {ECO:0000313|EMBL:AEH78634.1, ECO:0000313|Proteomes:UP000009045}; RN [1] {ECO:0000313|EMBL:AEH78634.1, ECO:0000313|Proteomes:UP000009045} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM11 {ECO:0000313|EMBL:AEH78634.1, RC ECO:0000313|Proteomes:UP000009045}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; AEH78634.1; -; Genomic_DNA. DR RefSeq; WP_003530700.1; NC_017325.1. DR RefSeq; YP_005719895.1; NC_017325.1. DR ProteinModelPortal; F7X5Y2; -. DR EnsemblBacteria; AEH78634; AEH78634; SM11_chr1358. DR KEGG; smx:SM11_chr1358; -. DR KO; K00548; -. DR BioCyc; SMEL707241:GLKB-1358-MONOMER; -. DR Proteomes; UP000009045; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009045}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:AEH78634.1}; KW Transferase {ECO:0000313|EMBL:AEH78634.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 215 215 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 281 281 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 282 282 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 337 AA; 35069 MW; 121A703F6038BDD7 CRC64; MSVAAHALSD LLAQKGVLLA DGATGTSLFA MGLEAGEAPE IWNETKPDNI TKLHQDFVDA GADIILTNSF GGTRHRLKLH QAEDRVHQLN KRAAEIARAV ADKAPRKVIT AGSVGPTGEL LIPLGALSYE DAVAAFVEQI EGLKAGGAEV AWIETMSSPD EIRAAAEAAA KVGLPYVYTG SFDTAGKTMM GLHPKDIHGV AADIGEGPVA VGANCGVGAS DILSSLLDMT AASPEATIVV KGNCGIPEFR GSEIHYSGTP PLMAEYARLA VDAGAKIIGG CCGTSCNHLA AMRLAIDNHT RGERPTLETI VEKIGPLRNK SANEGPAAPA RERRRRA // ID F7XAA6_SINMM Unreviewed; 1257 AA. AC F7XAA6; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=5-methyltetrahydrofolate--homocysteinemethyltransferase {ECO:0000313|EMBL:AEH80394.1}; GN Name=metH {ECO:0000313|EMBL:AEH80394.1}; GN OrderedLocusNames=SM11_chr3156 {ECO:0000313|EMBL:AEH80394.1}; OS Sinorhizobium meliloti (strain SM11). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=707241 {ECO:0000313|EMBL:AEH80394.1, ECO:0000313|Proteomes:UP000009045}; RN [1] {ECO:0000313|EMBL:AEH80394.1, ECO:0000313|Proteomes:UP000009045} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM11 {ECO:0000313|EMBL:AEH80394.1, RC ECO:0000313|Proteomes:UP000009045}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001830; AEH80394.1; -; Genomic_DNA. DR RefSeq; WP_010970331.1; NC_017325.1. DR RefSeq; YP_005721655.1; NC_017325.1. DR ProteinModelPortal; F7XAA6; -. DR SMR; F7XAA6; 668-1247. DR EnsemblBacteria; AEH80394; AEH80394; SM11_chr3156. DR KEGG; smx:SM11_chr3156; -. DR KO; K00548; -. DR BioCyc; SMEL707241:GLKB-3155-MONOMER; -. DR Proteomes; UP000009045; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000009045}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEH80394.1}; KW Transferase {ECO:0000313|EMBL:AEH80394.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 262 262 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 325 325 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 326 326 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 779 779 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1257 AA; 138077 MW; DC4B8906DE121E60 CRC64; MSAADALFGN VSPKPDGSEV FRQLAQAAAE RILIMDGAMG TEIQQLGFVE DHFRGERFGG CACHQQGNND LLTLTQPKAI EDIHYHYAIA GADILETNTF SSTRIAQADY GMEDMVYDLN RDGARLARRA AKRAEAEDGR RRFVAGALGP TNRTASISPD VNNPGYRAVS FDDLRLAYAE QVRGLIDGGA DIILIETIFD TLNAKAAIFA TQEVFAEKGV RLPVMISGTI TDLSGRTLSG QTPTAFWYSV RHADPFTIGL NCALGANAMR AHIDELSAVA DTLVCAYPNA GLPNEFGRYD ESPEQMAAQV EGFARDGLVN IVGGCCGSTP AHIRAIAEAV AKYPPRRVPE IDRRMRLSGL EPFTLTDEIP FVNVGERTNV TGSAKFRKLI TAGDYAAALD VARDQVANGA QIIDVNMDEG LIDSKQVMVE FLNLVASEPD IARVPVMIDS SKWEVIEAGL KCVQGKALVN SISLKEGEAA FLHHARLVRA YGAAVVVMAF DEKGQADTKT RKVEICRRAY RLLTEEVGFP PEDIIFDPNI FAVATGIEEH NNYGVDFIEA THEIIAALPH VHVSGGVSNL SFSFRGNEPV REAMHAIFLY HAIQAGMDMG IVNAGQLAVY DAIDPELRET CEDVVLNRRA DSTERLLEIA ERYRGKGGSQ GKEKDLAWRE WPVEKRLEHA LVNGITEFIE ADTEEARLAA ERPLHVIEGP LMAGMNVVGD LFGSGKMFLP QVVKSARVMK QAVAVLLPHM EEEKRANGGG EARESAGKIL MATVKGDVHD IGKNIVGVVL ACNNYEIIDL GVMVPSAKIL EVAREQKVDI VGLSGLITPS LDEMAHVASE LEREGFDVPL LIGGATTSRV HTAVKINPRY SLGQTVYVTD ASRAVGVVSS LLSPEVRDSY KKTVRAEYLK VADAHARNEA EKRRLPLSQA RANAFRIDWD AHQPKVPSFL GTRVFEGWDL AELARYIDWT PFFQTWELKG VFPKILDDER QGAAARQLFE DAQAMVEKIV AEAWFAPKAV IGFWPAASMG DDVRLFADEV REAELATFFT LRQQMVKRDG RPNVALADFV APAASGKRDY VGGFVVTAGI EEVAIAERFE RANDDYSSIM VKALADRFAE AFAERMHEYV RKELWGYAPD EAFTPQELIA EPYAGIRPAP GYPAQPDHTE KETLFRLLDA EAAIGVRLTE SYAMWPGSSV SGLYVGHPDS YYFGVAKIER DQVEDYADRK RMSVREVERW LSPILNYVPM PETEAAE // ID F7Y147_MESOW Unreviewed; 299 AA. AC F7Y147; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AEH88260.1}; GN OrderedLocusNames=Mesop_3822 {ECO:0000313|EMBL:AEH88260.1}; OS Mesorhizobium opportunistum (strain LMG 24607 / HAMBI 3007 / WSM2075). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=536019 {ECO:0000313|EMBL:AEH88260.1, ECO:0000313|Proteomes:UP000001623}; RN [1] {ECO:0000313|EMBL:AEH88260.1, ECO:0000313|Proteomes:UP000001623} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 24607 / HAMBI 3007 / WSM2075 RC {ECO:0000313|Proteomes:UP000001623}; 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; AEH88260.1; -; Genomic_DNA. DR RefSeq; WP_013894943.1; NC_015675.1. DR RefSeq; YP_004612354.1; NC_015675.1. DR EnsemblBacteria; AEH88260; AEH88260; Mesop_3822. DR KEGG; mop:Mesop_3822; -. DR BioCyc; MOPP536019:GH56-3859-MONOMER; -. DR Proteomes; UP000001623; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001623}; KW Methyltransferase {ECO:0000313|EMBL:AEH88260.1}; KW Transferase {ECO:0000313|EMBL:AEH88260.1}. SQ SEQUENCE 299 AA; 31505 MW; 1BFF4CE177A91FA6 CRC64; MKTVILTDGG MGQELVRRSK SEPTPLWSAR VLIDEPDLVR GLHAEFIRAG ARVITINTYS ATPERLAREG AEDLFKPLQK RGIELARQAR DAAGDATIAG CLSPLFGSYA PALTISYQET LDIYRRIVAE QADGVDLFLC ETMASSDEAR AAVTAASESG KPVWVSWTLA DHGAPRLRSG ETIAGASSAL DGLTVAARLL NCCRPEAIAA ALPELIDLGG PVGAYANGFT STEALKHGGT VDVLHARHDL GPDAYADQAT GWVEAGATIV GGCCEVGPPH IAALRDRLEQ AGYEISGVQ // ID F7Y2B2_MESOW Unreviewed; 340 AA. AC F7Y2B2; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AEH88309.1}; GN OrderedLocusNames=Mesop_3871 {ECO:0000313|EMBL:AEH88309.1}; OS Mesorhizobium opportunistum (strain LMG 24607 / HAMBI 3007 / WSM2075). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=536019 {ECO:0000313|EMBL:AEH88309.1, ECO:0000313|Proteomes:UP000001623}; RN [1] {ECO:0000313|EMBL:AEH88309.1, ECO:0000313|Proteomes:UP000001623} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 24607 / HAMBI 3007 / WSM2075 RC {ECO:0000313|Proteomes:UP000001623}; 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; AEH88309.1; -; Genomic_DNA. DR RefSeq; WP_013894992.1; NC_015675.1. DR RefSeq; YP_004612403.1; NC_015675.1. DR EnsemblBacteria; AEH88309; AEH88309; Mesop_3871. DR KEGG; mop:Mesop_3871; -. DR KO; K00548; -. DR BioCyc; MOPP536019:GH56-3908-MONOMER; -. DR Proteomes; UP000001623; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001623}; KW Methyltransferase {ECO:0000313|EMBL:AEH88309.1}; KW Transferase {ECO:0000313|EMBL:AEH88309.1}. SQ SEQUENCE 340 AA; 35769 MW; DABD98A819D585DB CRC64; MTTTNPIDAL LAEKGVLLAD GATGTNLFAM GLEAGEAPEL LNETAPDTIT SLHQNFVDAG ADIILTNSFG GTRHRLKLHH AQDRVHALNK RAAEIARAVA DKAGRKVIVA GSVGPTGELL MPLGAMTYDE AVDAFAEQIE GLKEGGAEVA WIETMSAPDE IRAAAEAAIR VGLPYTYTGS FDTAGRTMMG LLPKDIHGVT DGLSQSPLGV GANCGVGASD ILASLLDMTD AKPEATVIVK GNCGIPEFRG AEIHYSGTPE LMADYVRLAV DAGAKIVGGC CGTSFQHLAA MRKALDAHTK ADRPTVEKIV ERIGPMRNKV ATQNTAETSE ARRERRRSRA // ID F7YIP8_VIBA7 Unreviewed; 1225 AA. AC F7YIP8; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AEH34332.1}; GN OrderedLocusNames=VAA_01748 {ECO:0000313|EMBL:AEH34332.1}; OS Vibrio anguillarum (strain ATCC 68554 / 775) (Listonella anguillarum). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=882102 {ECO:0000313|EMBL:AEH34332.1, ECO:0000313|Proteomes:UP000006800}; RN [1] {ECO:0000313|EMBL:AEH34332.1, ECO:0000313|Proteomes:UP000006800} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 68554 / 775 {ECO:0000313|Proteomes:UP000006800}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002284; AEH34332.1; -; Genomic_DNA. DR RefSeq; WP_013857901.1; NC_015633.1. DR RefSeq; YP_004567374.1; NC_015633.1. DR EnsemblBacteria; AEH34332; AEH34332; VAA_01748. DR GeneID; 10776610; -. DR KEGG; van:VAA_01748; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; LANG882102:GIWG-2832-MONOMER; -. DR Proteomes; UP000006800; Chromosome I. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006800}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEH34332.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006800}; KW Transferase {ECO:0000313|EMBL:AEH34332.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1225 AA; 136504 MW; A9FE9D194AD12CDB CRC64; MGREVRSQIE AQLQQRILLI DGGMGTMIQS YKLEEQDYRG DRFAHWPSDL KGNNDLLVLT QPQLIKEIHS AYLEAGADIL ETNTFNATSI AMADYDMQAI SDEINFAAAK LARQAADEWT AKTPDKPRYV AGVLGPTNRT CSLSPDVNDP GFRNISFEQL VEAYSESTRA LIRGGSDLIL IETIFDTLNA KACAFAVDCV FEELGYKLPV MISGTITDAS GRTLSGQTTE AFYNALRHVE PISFGLNCAL GPDELRQYVE ELSRISECYV SAHPNAGLPN AFGEYDLEAD EMAQHIGEWA RAGFLNLVGG CCGTTPEHIR QMAKVVEGVK PRALPDIPVA CRLSGLEPLT ITKESLFINV GERTNVTGSA RFKRLIKDEQ YDEALHVARE QVENGAQIID INMDEGMLDA QACMVRFLNL CASEPDISKV PIMVDSSKWE VIEAGLKCIQ GKGIVNSISL KEGKEKFVEQ AKLIRRYGAA VIVMAFDEVG QADTRERKLE ICTKAYRILV DEVGFPAEDI IFDPNIFAVA TGIDEHNNYA VDFIEAVADI KRNLPHAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK NGMDMGIVNA GQLEIYDNVP EKLREAVEDI ILNRRSDGTE RLLDIAAEYA NKGVGKEEDA SALEWRSWPV AKRLEHALVK GITEYIVEDT EEARQNATRP LDVIEGPLMD GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AHLEPYINAL KQAGSNNGKI LLATVKGDVH DIGKNIVGVV LQCNNYEIID LGVMVPCEQI LKVAKEQNVD IIGLSGLITP SLDEMVHVAK EMERQGFKLP LLIGGATTSK AHTAVKIEQN YHQPVVYVNN ASRAVGVCSS LLSDELRPAF VEKLNIDYER TRDQHHRKTP RTKPVSLEVA RANKAVIDWD NYTPPVPAKL GVHVFDDFDV ATLRRYIDWT PFFMTWSLMG KYPTIFEHEE VGEEAQSLFH DANALLDRVE REGLLKARGI CALFPAASVG DDIEVYRDES RTEVAHVLHH LRQQTEKPKG YNYCLSDYIA PKESGKRDWI GAFAVTGGIG ERELADQYKA QGDDYNAIMI QAVADRLAEA FAEYLHQQVR KEIWGYAADE ELSNDDLIRE KYQGIRPAPG YPACPEHTEK GTLWEMLQVE QTIDMSLTTS YAMWPGASVS GWYFSHPDSR YFAIAQIQQD QMQDYAQRKG WNAQEAEKWL GPNLD // ID F7YLU1_VIBA7 Unreviewed; 299 AA. AC F7YLU1; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AEH33571.1}; GN OrderedLocusNames=VAA_02314 {ECO:0000313|EMBL:AEH33571.1}; OS Vibrio anguillarum (strain ATCC 68554 / 775) (Listonella anguillarum). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=882102 {ECO:0000313|EMBL:AEH33571.1, ECO:0000313|Proteomes:UP000006800}; RN [1] {ECO:0000313|EMBL:AEH33571.1, ECO:0000313|Proteomes:UP000006800} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 68554 / 775 {ECO:0000313|Proteomes:UP000006800}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; AEH33571.1; -; Genomic_DNA. DR RefSeq; WP_013857202.1; NC_015633.1. DR RefSeq; YP_004566613.1; NC_015633.1. DR EnsemblBacteria; AEH33571; AEH33571; VAA_02314. DR GeneID; 10775815; -. DR KEGG; van:VAA_02314; -. DR OMA; PYVDVWL; -. DR BioCyc; LANG882102:GIWG-2037-MONOMER; -. DR Proteomes; UP000006800; Chromosome I. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006800}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:AEH33571.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006800}; KW Transferase {ECO:0000313|EMBL:AEH33571.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 203 203 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 278 278 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 279 279 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 299 AA; 32556 MW; 135EC9621742D455 CRC64; MSKLTLLDGG MGRELKRIGA PFSQPLWSAQ ALIESPQHVR LAHQGFIDSG ADIITVNSYA CVPFHLGESL YQTDGARLAN LAAQIAAEVA QQSERPILVA GSMPPAMGSY RPDLFQAEVA RAISLTLYQA QDPYVDVWLA ETIASLEELS MIQSVFASST KPCYYALTLK DDSNIAQLRS GQSVSEAAEQ IYSAGGAGIF FNCSIPEVMA DAIQQVKMVL EGRAQKIEIG VYANSFTPIK SDHAANQTVQ AMREFSAEDY LAFAKQWYAL GATVIGGCCG ITPRHIQALY EWRRSFEKS // ID F7YVJ5_9THEM Unreviewed; 117 AA. AC F7YVJ5; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 29-APR-2015, entry version 18. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AEH51650.1}; GN ORFNames=Theth_1598 {ECO:0000313|EMBL:AEH51650.1}; OS Thermotoga thermarum DSM 5069. OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=688269 {ECO:0000313|EMBL:AEH51650.1, ECO:0000313|Proteomes:UP000006804}; RN [1] {ECO:0000313|EMBL:AEH51650.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 5069 {ECO:0000313|EMBL:AEH51650.1}; 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., 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., Spring S., Schroeder M., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Thermotoga thermarum DSM 5069."; 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; CP002351; AEH51650.1; -; Genomic_DNA. DR RefSeq; WP_013932862.1; NC_015707.1. DR RefSeq; YP_004660746.1; NC_015707.1. DR EnsemblBacteria; AEH51650; AEH51650; Theth_1598. DR KEGG; tta:Theth_1598; -. DR BioCyc; TTHE688269:GHXV-1631-MONOMER; -. DR Proteomes; UP000006804; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006804}; KW Methyltransferase {ECO:0000313|EMBL:AEH51650.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006804}; KW Transferase {ECO:0000313|EMBL:AEH51650.1}. SQ SEQUENCE 117 AA; 13222 MW; 80CCF4F499F4EDD3 CRC64; MKRSEFKNLL QERVLFLDGA YGTEFFKSEY KIDLIEFLNI KEPSAVAKIQ KEYILAGADI LLINAFSANR LKLRAHGYEE RNKHIGSAVK IAKSVANGKL VFGGIFSLCV IDLQKKK // ID F7YXH9_9THEM Unreviewed; 773 AA. AC F7YXH9; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 01-APR-2015, entry version 22. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:AEH50620.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEH50620.1}; GN ORFNames=Theth_0531 {ECO:0000313|EMBL:AEH50620.1}; OS Thermotoga thermarum DSM 5069. OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=688269 {ECO:0000313|EMBL:AEH50620.1, ECO:0000313|Proteomes:UP000006804}; RN [1] {ECO:0000313|EMBL:AEH50620.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 5069 {ECO:0000313|EMBL:AEH50620.1}; 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., 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., Spring S., Schroeder M., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Thermotoga thermarum DSM 5069."; 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; CP002351; AEH50620.1; -; Genomic_DNA. DR RefSeq; WP_013931843.1; NC_015707.1. DR RefSeq; YP_004659716.1; NC_015707.1. DR EnsemblBacteria; AEH50620; AEH50620; Theth_0531. DR KEGG; tta:Theth_0531; -. DR KO; K00548; -. DR BioCyc; TTHE688269:GHXV-544-MONOMER; -. DR Proteomes; UP000006804; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006804}; KW Methyltransferase {ECO:0000313|EMBL:AEH50620.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006804}; KW Transferase {ECO:0000313|EMBL:AEH50620.1}. SQ SEQUENCE 773 AA; 85738 MW; 16FBDAD7F6B1AF26 CRC64; MKREEFHEML KQRVLFLDGA YGTEFFKRGY KVDLIELLNV KNPQAVAQLQ KEYVQAGADI LLTNTFSANR AKLKAHGYEE LFEKINVEAV KIAKSVANGR LVFGDISSTG SFVKPLGEMD FDEAYFIFKE QAQLLIESGV DGIIIETMSD LKELKAAILA VRDVSKDIPL IASMTFDANG KSVTGTSVEI FSTLMNDLDV DVASINCTLE PKDMLNVFIQ LAKYCNKYLC VEPNAGKPIL RGNVLEYKTT PDEFAIYMRD FVEFGANIVG GCCGTGPKHI KSMVEYIGNQ KPKSKEPSKR QFVSSRTVMK PVEDFLIIGE RINASGKKKL QVQIQQKDFS TIVQLAQEQE KEGCAVIDVN LGIEKLLEKD HFKQVIIELD RVSALPLSLD IQNLEFLETA AKEYVGRPMI NSALAREDHL IERLKILKRY GGILIVLTME KDIPKTPEER FKLALKAVEI IKKEGVDLDR IFFDPLVLPV GAGNDYRVTV KTIELLNSAG LKTCIGLSNL SFGMPEREKV NAAFLALCME AGLKAAILNS KETTTMNIIE GMLLLKGKEL AKTKVEFEDP LVEWIVKGQK DKVMDFVKEK LKDLDPLTVS QQILAKAMER VGKLYSEGVI FLPQLILAAE TVQPVFEYLN SLLTDSKVKL GTVVLATVQG DIHDIGKKIV ATVLRSGGFE VYDLGKDVPA DKILESVKKI KPDIVGLSAM MTTTVGRVKE VADLLKENGV NVVVIAGGAS MNKELAEKFG VLYAKDALEG LEVCKKIVEE RRT // ID F7Z1X0_BACC6 Unreviewed; 209 AA. AC F7Z1X0; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AEH52388.1}; GN OrderedLocusNames=BCO26_0329 {ECO:0000313|EMBL:AEH52388.1}; OS Bacillus coagulans (strain 2-6). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=941639 {ECO:0000313|EMBL:AEH52388.1, ECO:0000313|Proteomes:UP000005637}; RN [1] {ECO:0000313|EMBL:AEH52388.1, ECO:0000313|Proteomes:UP000005637} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2-6 {ECO:0000313|EMBL:AEH52388.1, RC ECO:0000313|Proteomes:UP000005637}; 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 ----------------------------------------------------------------------- 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; AEH52388.1; -; Genomic_DNA. DR RefSeq; WP_013858287.1; NC_015634.1. DR RefSeq; YP_004567774.1; NC_015634.1. DR EnsemblBacteria; AEH52388; AEH52388; BCO26_0329. DR KEGG; bck:BCO26_0329; -. DR KO; K00547; -. DR BioCyc; BCOA941639:GHC1-345-MONOMER; -. DR Proteomes; UP000005637; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005637}; KW Methyltransferase {ECO:0000313|EMBL:AEH52388.1}; KW Transferase {ECO:0000313|EMBL:AEH52388.1}. SQ SEQUENCE 209 AA; 23203 MW; 4E859E5F5964E11E CRC64; MDFLETLKNR ILVADGAMGT LLYAYGADTC YESFNLSHPE DIHAIHRAYI EAGASVIQTN TYSANYIKLA QYGLEEKVKD INKAAVRIAK EAANRDTFIL GTVGGIRGQR KTEATLAEIK RTFREQIFHL LNEGVDALLL ETYFDAEELY TVVDIAKKEA DVPVIAQFSL IEPGVLQNGT PVRDAFKELE NRGADVTGLN CRLGPHHMI // ID F7Z1X1_BACC6 Unreviewed; 1154 AA. AC F7Z1X1; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 29-APR-2015, entry version 27. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEH52390.1}; GN OrderedLocusNames=BCO26_0331 {ECO:0000313|EMBL:AEH52390.1}; OS Bacillus coagulans (strain 2-6). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=941639 {ECO:0000313|EMBL:AEH52390.1, ECO:0000313|Proteomes:UP000005637}; RN [1] {ECO:0000313|EMBL:AEH52390.1, ECO:0000313|Proteomes:UP000005637} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2-6 {ECO:0000313|EMBL:AEH52390.1, RC ECO:0000313|Proteomes:UP000005637}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002472; AEH52390.1; -; Genomic_DNA. DR RefSeq; WP_013858289.1; NC_015634.1. DR RefSeq; YP_004567776.1; NC_015634.1. DR EnsemblBacteria; AEH52390; AEH52390; BCO26_0331. DR KEGG; bck:BCO26_0331; -. DR KO; K00548; -. DR BioCyc; BCOA941639:GHC1-347-MONOMER; -. DR Proteomes; UP000005637; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000005637}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 724 724 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1154 AA; 125992 MW; B4329B6D8A4E6C72 CRC64; MGETIFEQQL ANRILILDGA MGTMIQQQHL TAADFGGEAY EGCNEYLNLT APDLIRSIHE AYLEAGADII ETNTFGATSI VLNEYGLGHF AEKINIEAAR IAKQAAGKFS TPGRPRFVAG SMGPTTKTLS VTGGTTFDAL KTAYQEQACG LIKGGADVLL LETSQDVLNV KAAFLGITDA FNETGKKLPL LISGTIEPMG TTLAGQNIEA FYISVAHMQP AAVGLNCATG PEFMADSIRT LAGLAKTAVS CYPNAGLPDE EGHYHETPDS LAVKMKGFAE KGWLNIAGGC CGTTPAHIKA LNEALAGLPP RQPAKEEHHA VSGIEPFIYD DPSTRPIFVG ERTNVIGSRK FRRLIAEGKW EEASEIARTQ VKNGAQIIDI CLADPDRDEI SDMENFISIA VKKVKVPFMI DSTDENVIEK AFTYCQGKSI VNSINLENGT ERFEKVVPLL KKYGGAVVVG TIDEEGMAVT AERKLEIARR SYDLLVHTYG LNPRDLIFDP LVFPAGTGDK QYFGAAKETV EGIRLIKEAM PECQTILGVS NVSFGLPPAG REVLNSVFLY HCTKAGLDYA IVNTEKLERF ASIPEENVKM AEKLLFETSD EALAAFTEYY RGKVQEKKAP KSTMTLAERL ANDVVEGTKE GLIPDLEQAL KEYPDPLAII NGPLMDGMAE VGRLFNDNQL IVAEVLQSAE VMKASVAFLE PFMEKNETST KGKVLLATVK GDVHDIGKNL VDIILSNNGY KVVDLGIKVA PADLIHAVRK EKPDVIGLSG LLVKSAQQMV VTAQDLREAG IRQPILVGGA ALSRKFTLNK IAPQYEGLVL YAKDAMEGLT LANKLQDESE RSSLETELAN QRSGGTRVAA ANAGGAPVAT LPRRSSVSPD ARVYQPADLK RHVLRNYPLS HIEPYVNMQM LLGHHLGLKG RVKKLLAEGD ERAIKLKQQV DELREWVMKE KLLQPSAVYQ FFPAQSDGND LIVYEPAGEP GALNPKSLSI LERFTFPRQA KPPYLCLADY VRSVDSGVVD YVGMFAVVAG KNIRHHARYL KEAGEYFKSH ALQALALETA EGFAERLHEL MRGQWGFPDP AGFTMQQRFA AKYQGQRYSF GYPACPNLED QAKLFKLLQP QKIGLHLTEG YMMEPEAAVT ALVFSHPEAR YFAV // ID F7Z770_BACC6 Unreviewed; 389 AA. AC F7Z770; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 25. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=BCO26_0330 {ECO:0000313|EMBL:AEH52389.1}; OS Bacillus coagulans (strain 2-6). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=941639 {ECO:0000313|EMBL:AEH52389.1, ECO:0000313|Proteomes:UP000005637}; RN [1] {ECO:0000313|EMBL:AEH52389.1, ECO:0000313|Proteomes:UP000005637} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2-6 {ECO:0000313|EMBL:AEH52389.1, RC ECO:0000313|Proteomes:UP000005637}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; AEH52389.1; -; Genomic_DNA. DR RefSeq; WP_013858288.1; NC_015634.1. DR RefSeq; YP_004567775.1; NC_015634.1. DR EnsemblBacteria; AEH52389; AEH52389; BCO26_0330. DR KEGG; bck:BCO26_0330; -. DR KO; K00547; -. DR BioCyc; BCOA941639:GHC1-346-MONOMER; -. DR Proteomes; UP000005637; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005637}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:AEH52389.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:AEH52389.1}. SQ SEQUENCE 389 AA; 42664 MW; 49F656735B1604E8 CRC64; MSAYPNASLL DYEEGRFTFT NNADYFKTCA EKLVEQGVRL IGGCCGTTPA HIKAIADGVQ GLLPVTEKTV RPPKIEIAAA PAQYEPPLHE IVKKRHSVIV ELDTPKTLNT ARFFEGAKAL HDAGIDALTM ADNSLASPRI SNTAIAAILK EKHGIRPLVH ITCRDRNLIG LQSHLMGLAA LGIDQVLAVT GDPSKIGDFP GATSVYDLSS MELIAMIKQF NDGISHSGKS LQRKTNFSVA AAFNPNVRNL DKTVGRLERK IRHGADYFIT QPVFSTEKIE QIHEATKHLD APIYLGIMPL TSYRNAVFLH NEVPGITLTD DILQAMEKTN GDPVKAREES LAISRTLIDA ALAYFNGIYL ITPLERYELT VECTRYIHEK TAVRSAGIF // ID F7ZAN7_ROSLO Unreviewed; 340 AA. AC F7ZAN7; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=Putative methionine synthase (B12 dependent) subunit 1 {ECO:0000313|EMBL:AEI94233.1}; GN OrderedLocusNames=RLO149_c022580 {ECO:0000313|EMBL:AEI94233.1}; 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 {ECO:0000313|EMBL:AEI94233.1, ECO:0000313|Proteomes:UP000001353}; RN [1] {ECO:0000313|EMBL:AEI94233.1, ECO:0000313|Proteomes:UP000001353} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49566 / DSM 6996 / JCM 21268 / NBRC 15278 / OCh 149 RC {ECO:0000313|Proteomes:UP000001353}; 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; AEI94233.1; -; Genomic_DNA. DR RefSeq; WP_013962157.1; NC_015730.1. DR RefSeq; YP_004691196.1; NC_015730.1. DR ProteinModelPortal; F7ZAN7; -. DR EnsemblBacteria; AEI94233; AEI94233; RLO149_c022580. DR KEGG; rli:RLO149_c022580; -. DR KO; K00548; -. DR BioCyc; RLIT391595:GJEH-2242-MONOMER; -. DR Proteomes; UP000001353; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001353}. SQ SEQUENCE 340 AA; 35912 MW; 83A5A4D96D109D02 CRC64; MPNPFSDLLE TNGVLLADGA TGTNLFNMGL MSGEAPELWN TQEPQKIKTL YKGAVDAGSD LFLTNSFGAN ASRLKLHNAE KRVHELSRVA AEIGREVADT AGRTVIVAGS VGPTGEIMEP VGTLSHALAV EMFHETADGL KAGGADIGWL ETISAPEEYR AAAEGFALAG LDWCGTMSFD TAGRTMMGLT SADMVKMVND LGDHAPLAFG ANCGTGASDL LRTVLGFAAQ GPERPIIAKG NAGIPKYVDG HIHYDGTPEL MADYAIMARA SGARIIGGCC GTMPEHLRHM REALDTRTMD HPPALEEIVD RLGAFSSAAD GTDKENTPAR RATRRSRRAS // ID F7ZDM7_ROSLO Unreviewed; 296 AA. AC F7ZDM7; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Putative homocysteine S-methyltransferase {ECO:0000313|EMBL:AEI95812.1}; GN OrderedLocusNames=RLO149_c039100 {ECO:0000313|EMBL:AEI95812.1}; 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 {ECO:0000313|EMBL:AEI95812.1, ECO:0000313|Proteomes:UP000001353}; RN [1] {ECO:0000313|EMBL:AEI95812.1, ECO:0000313|Proteomes:UP000001353} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49566 / DSM 6996 / JCM 21268 / NBRC 15278 / OCh 149 RC {ECO:0000313|Proteomes:UP000001353}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; AEI95812.1; -; Genomic_DNA. DR RefSeq; WP_013963694.1; NC_015730.1. DR RefSeq; YP_004692775.1; NC_015730.1. DR ProteinModelPortal; F7ZDM7; -. DR EnsemblBacteria; AEI95812; AEI95812; RLO149_c039100. DR KEGG; rli:RLO149_c039100; -. DR BioCyc; RLIT391595:GJEH-3883-MONOMER; -. DR Proteomes; UP000001353; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001353}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:AEI95812.1}; KW Transferase {ECO:0000313|EMBL:AEI95812.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 200 200 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 273 273 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 274 274 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 296 AA; 31218 MW; 0A29C81888BC247E CRC64; MTQITLLDGG MGQELVHRAG DKPTPLWSTQ VMVDHPGLVE AVHADYFAAG ATVATTNSYA IHHDRLEGTG MEDAFEDLYQ RALSEASAAR AKHGSGRIAG ALGPLVASYR PDLHPSREIA VPLFAEAAAL LAPVCDVLIL ETVASVAHAR DALEGARSTN LPVWLSLTVS DGDGMQLRSG EPLEDALEVA ANADAVLVNC SAPEAVTKAM PILAQSGKPF GGYANGFVQI SQDFLKEKPT VDTLETRRDM GPRAYAGYVM EWVAAGATIV GGCCEVGPKH IAELKKRLLA AEHTLA // ID F7ZEJ6_ROSLO Unreviewed; 313 AA. AC F7ZEJ6; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Putative homocysteine S-methyltransferase {ECO:0000313|EMBL:AEI95892.1}; GN OrderedLocusNames=RLO149_c039910 {ECO:0000313|EMBL:AEI95892.1}; 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 {ECO:0000313|EMBL:AEI95892.1, ECO:0000313|Proteomes:UP000001353}; RN [1] {ECO:0000313|EMBL:AEI95892.1, ECO:0000313|Proteomes:UP000001353} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49566 / DSM 6996 / JCM 21268 / NBRC 15278 / OCh 149 RC {ECO:0000313|Proteomes:UP000001353}; 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; AEI95892.1; -; Genomic_DNA. DR RefSeq; WP_013963772.1; NC_015730.1. DR RefSeq; YP_004692855.1; NC_015730.1. DR EnsemblBacteria; AEI95892; AEI95892; RLO149_c039910. DR KEGG; rli:RLO149_c039910; -. DR BioCyc; RLIT391595:GJEH-3964-MONOMER; -. DR Proteomes; UP000001353; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001353}; KW Methyltransferase {ECO:0000313|EMBL:AEI95892.1}; KW Transferase {ECO:0000313|EMBL:AEI95892.1}. SQ SEQUENCE 313 AA; 33895 MW; E2595B8B8D1CF4DB CRC64; MAIYRNTFPK VNADLLLAYV GMETDLIFNR GVDLPGFASY PLLETTEGRE LLEGYLKDMI ALGSEMGAGV ILESPTWVAN RDRAAALGYT RNSLKDLNQQ AVAMMAEMRA AHGDVPTVIS ANLGPRDDAY TPEAQMSPQD AERYHSEQIS ALADTAVDVI SGYTLAYPAE AIGIVRAARR SGLPVVISFT VETDGKLPTG SSLEDAILQV DAATNGYAAY FMINCAHPDH FRTVLEDRPW MQRVRGIIAN ASKCSHAELD EAEELDAGDP TELAQQLSEI RHTFPHIMVL GGCCGTDMRH MSKIANISGS ISA // ID F7ZL27_ROSLO Unreviewed; 314 AA. AC F7ZL27; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Homocysteine S-methyltransferase-like protein {ECO:0000313|EMBL:AEI94038.1}; GN OrderedLocusNames=RLO149_c020600 {ECO:0000313|EMBL:AEI94038.1}; 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 {ECO:0000313|EMBL:AEI94038.1, ECO:0000313|Proteomes:UP000001353}; RN [1] {ECO:0000313|EMBL:AEI94038.1, ECO:0000313|Proteomes:UP000001353} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49566 / DSM 6996 / JCM 21268 / NBRC 15278 / OCh 149 RC {ECO:0000313|Proteomes:UP000001353}; 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; AEI94038.1; -; Genomic_DNA. DR RefSeq; WP_013961964.1; NC_015730.1. DR RefSeq; YP_004691001.1; NC_015730.1. DR ProteinModelPortal; F7ZL27; -. DR EnsemblBacteria; AEI94038; AEI94038; RLO149_c020600. DR KEGG; rli:RLO149_c020600; -. DR BioCyc; RLIT391595:GJEH-2044-MONOMER; -. DR Proteomes; UP000001353; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001353}; KW Methyltransferase {ECO:0000313|EMBL:AEI94038.1}; KW Transferase {ECO:0000313|EMBL:AEI94038.1}. SQ SEQUENCE 314 AA; 34023 MW; 80A7F4DE49133AA9 CRC64; MSQPTPRLPH QTDEIFLTDG GTETWLMYKR GFALPEFSAF HLLNNDWSAE ALREYYTAFA DIAVKLGTPF IFDSLTYRAS RDWGALLGYS PEGLAEMNHK CFELYRECAA DAGLTAEKTV ISGCIGPKGD AYQTNQDLTA ESARAYHAEQ IDTFKAAGAD IVTALTLNTT AEAIGIARAS AEAGLLSVIS FTVEKDRKLR SGETLRQAIE TVDAATSSAP AYYMINCSHP VDFGPALATE PWANRIQGLR ANASSLDHGT LCQLGHLEEG DPDELASQYV DLRVAHPNMN VFGGCCGTDY VHVEKIGRAL LAAA // ID F7ZLG8_ROSLO Unreviewed; 347 AA. AC F7ZLG8; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Methionine synthase (B12-dependent) subunit B {ECO:0000313|EMBL:AEI92828.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEI92828.1}; GN Name=metHB {ECO:0000313|EMBL:AEI92828.1}; GN OrderedLocusNames=RLO149_c008010 {ECO:0000313|EMBL:AEI92828.1}; 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 {ECO:0000313|EMBL:AEI92828.1, ECO:0000313|Proteomes:UP000001353}; RN [1] {ECO:0000313|EMBL:AEI92828.1, ECO:0000313|Proteomes:UP000001353} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49566 / DSM 6996 / JCM 21268 / NBRC 15278 / OCh 149 RC {ECO:0000313|Proteomes:UP000001353}; 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; AEI92828.1; -; Genomic_DNA. DR RefSeq; WP_013960768.1; NC_015730.1. DR RefSeq; YP_004689791.1; NC_015730.1. DR EnsemblBacteria; AEI92828; AEI92828; RLO149_c008010. DR KEGG; rli:RLO149_c008010; -. DR KO; K00548; -. DR BioCyc; RLIT391595:GJEH-801-MONOMER; -. DR Proteomes; UP000001353; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001353}; KW Methyltransferase {ECO:0000313|EMBL:AEI92828.1}; KW Transferase {ECO:0000313|EMBL:AEI92828.1}. SQ SEQUENCE 347 AA; 36401 MW; F70C721E46442070 CRC64; MSLHDHHCVN ALNATARERI LIMDGAMGTM IQGLGLGEDD YTGHGTGTPC AHATDLPQKG NNDLLTLTQP QAIEQIHYDF AIAGADIVET NTFSSTAIAQ ADYGLEAAVH DLNVEAARVA RRALDRATAQ DGKPRYVAGA VGPTNRTASL SPDVSDPGYR AVTFDGLRLA YRDQIRGLII GGADLILIET IFDTLNAKAA IFAAIEACQA QGIRLPIMIS GTITDASGRT LSGQTPTAFW HSVAHARPFS VGLNCALGAG AMRPHMAELA GVVDTLTCAY PNAGLPNAFG QYDEGPEETA EQLAGFAQEG LLNVVGGCCG TTPEHIRAIA EAVAPFAPRQ LEKEQAA // ID F8AZR6_FRADG Unreviewed; 1191 AA. AC F8AZR6; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 29-APR-2015, entry version 26. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEH09675.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEH09675.1}; GN OrderedLocusNames=FsymDg_2275 {ECO:0000313|EMBL:AEH09675.1}; OS Frankia symbiont subsp. Datisca glomerata. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Frankineae; Frankiaceae; Frankia. OX NCBI_TaxID=656024 {ECO:0000313|EMBL:AEH09675.1, ECO:0000313|Proteomes:UP000001549}; RN [1] {ECO:0000313|EMBL:AEH09675.1, ECO:0000313|Proteomes:UP000001549} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4085684 {ECO:0000313|EMBL:AEH09675.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002801; AEH09675.1; -; Genomic_DNA. DR RefSeq; WP_013873607.1; NC_015656.1. DR RefSeq; YP_004583596.1; NC_015656.1. DR EnsemblBacteria; AEH09675; AEH09675; FsymDg_2275. DR KEGG; fsy:FsymDg_2275; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; FSYM656024:GHLT-2292-MONOMER; -. DR Proteomes; UP000001549; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001549}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEH09675.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001549}; KW Transferase {ECO:0000313|EMBL:AEH09675.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 223 223 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 752 752 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1191 AA; 128466 MW; 8D0D244ECEDA2D1B CRC64; MRGDLLSVLA ERVVVADGAM GTMLQAASLT LDDFDGHEGC NEILNVTRPD VVRAVHDAYF AVGCDAVETN TFGANLANLG EYGIADRIGE LAEAGARIAR EAADFWSRPG QPRFVLGSVG PGTKLPSLGH ITYRPLRDAY QRQAAGLLAG GVDAILVETA QDLLQAKAAI IGARRAMAEA GRRVALIAQV TVELTGTMLL GSETGAALTA LEPLGIDLIG LNCATGPAEM SEHLRYLSQQ ARVGLSVMPN AGLPELGRDG ATYPLTPAEL ADAQDAFTRD YGAALVGGCC GTTPEHLRQV VERVAGRGVR TRRPATWAGS PTAAGTGSPA VEAGQPAAAA SLYQSVPFRQ DTSVLMVGER TNTNGSRAFR DALIDGRWDD VVEIARAATR EGAHMIDVCV DYVGRDGTVD MREVASRYAT ASTLPVMLDS TEPPVIEAGL ECLGGRSVVN SVNFEDGDGP DSRIARVMPA VVEHGAAVVV MCIDEEGQAR TVERKVQIAE RTIDYLVDRW GMRTADIFVD TLTFTLGTGQ EESRGDGVAT IEAIRELKRR RPDVQTILGL SNISFGLKPA ARVVLNSVFL AECVAAGLDA AIVHASRILP TARIPDEQRE VALDLVHDRR RDGYDPLTRF LELFSEVDGS GAGPTRAQEL AALPLDERLK RRIIDGERTG LEADLDEAMR SRDPLAIIND TLLDGMKVVG DLFGSGQMQL PFVLQSAEVM KAAVAYLEPH MERTDSRGKG TLVLATVKGD VHDIGKNLVD IILSNNGYTV VNLGIKQPIG AILAAASEHD ADAIGMSGLL VKSTVVMKEN LAEMNTRGVA ATWPVLLGGA ALTRAYVEGD LAELYQGDVR YARDAFEGLA LMDAVMAAKR GQAPPLADDP RAAERRARRA RTERIRAARA EKRGEQPPTE APPRSDVATD NPVPTPPFWG DRIVKGIPLA DYASYLDERA TFLGQWGLRG ARGGEGPSYE ELVETEGRPR LRMWLDRIAS ERMLEAAVVY GYFPCVSKGE DLIVLSGDGA ERARFTFPRQ RRDRRLCLAD FYRSEESGQV DVVPFMIVTM GRRISEVTAE LFAANSYREY LELHGLSVQL TEALTEYWHK RIRAELLLPD GTPTGAADAD ELAAVFRQGY RGSRYSFGYP ACPDLEQQVG AFELLTPGRV GVELSEEFQL VPEQSTSAII AHHPEAKYFA T // ID F8CQA4_MYXFH Unreviewed; 1152 AA. AC F8CQA4; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AEI65433.1}; GN OrderedLocusNames=LILAB_17655 {ECO:0000313|EMBL:AEI65433.1}; OS Myxococcus fulvus (strain ATCC BAA-855 / HW-1). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Myxococcaceae; Myxococcus. OX NCBI_TaxID=483219 {ECO:0000313|EMBL:AEI65433.1, ECO:0000313|Proteomes:UP000000488}; RN [1] {ECO:0000313|EMBL:AEI65433.1, ECO:0000313|Proteomes:UP000000488} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-855 / HW-1 {ECO:0000313|Proteomes:UP000000488}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002830; AEI65433.1; -; Genomic_DNA. DR RefSeq; WP_013938577.1; NC_015711.1. DR RefSeq; YP_004666511.1; NC_015711.1. DR EnsemblBacteria; AEI65433; AEI65433; LILAB_17655. DR KEGG; mfu:LILAB_17655; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; MFUL483219:GJEO-3522-MONOMER; -. DR Proteomes; UP000000488; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000488}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEI65433.1}; KW Transferase {ECO:0000313|EMBL:AEI65433.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 226 226 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 720 720 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1152 AA; 125093 MW; 2199F7917C964AAD CRC64; MEALRAAMRE RVLVLDGAMG TLLQNEDLKA ADFGGPEYEG CNEHLVLTRP ELVESIHARY LAAGADVTET DSFGGTPLVL AEFGLGHKAL EINEVSARLA RNAAAAAEAK DGRMRWVAGS MGPTTKAISV TGGVTFEELV DNFAVQAEGL ALGGSDYLLI ETAQDTRNVK AALIGIERAF QKLGYVLPVA VSGTIEPMGT MLAGQSVESL AASLEHADLL YLGLNCATGP DFMTDHLRSL AAMSAFPVSC VPNAGLPDEN GHYLETPEML ARSVRRFCEQ GWLSVVGGCC GTHAGHIESL ARAVQGLKPR TGTPRPRASL SGVDYLEVTD ELRPLIVGER TNVIGSKKFK ELIVAGQFDD ASEIARAQVK RGAQVIDICL ANPDRDELED MRSFLEVVAK KVRVPLMIDS TDERVIEMAL TYSQGKAIIN SVNLEDGEER FEKVVPLARR FGAALVVGCI DEVGMAVTRQ RKLEVAERSY ELLTTKYGMK PEDLYFDPLV FPCASGDAQY TGSGVETIEG VRLIKQRFPR CKTVLGISNV SFGLPTAGRE VLNSVFLYHN VQAGLDMALV NSEKLERYPS LPEEERKLSE DLLYNRGPDP VTPFAAHFRE RKAARVQVST LPLEERLQRY IIEGTRDGLT ADLEVAMQKY TPLEIINGPL MKGMDEVGRL FGANELIVAE VLQSAESMKA AVGFLEPHMS KAQAAMRGKV VLATVKGDVH DIGKNLVEII LANNGFHVVN LGIKVPPEQL VQAVREHQPD ILGLSGLLVK SAHQMVATAE DLKRAGVETP ILVGGAALSR NFVDRNIAPA YGGGTVAYAQ DAMNGLELAK QIVDPSAHEK LRGDLAVRRE KLAREVKERP APAVVVARGR SAEVKVLDAV PSAPDFERHV LSNTPLDHIW KFINPVMLYG RHLGLRSSSR VLGTPAEAEL AKTEEGRKAL ALKEAVEELK GFLRGGVMQA RAVFQFYKAG SDGNRVVLFD GASGKEAASF DFPRQDREGG LCLADYLRPL EGGAPTDTVA MFVVTAGAGI RELAEELKAR GEFLKMHAVQ ALALETAEGY AELLHTQLRS MWGTPDRPDM TMLERFRAEY AGKRYSFGYP ACPRLEDQSK LFAALRPEDI GVQLTDGSMM EPEASVSAIV FHHPQASYFS VT // ID F8CZT4_GEOTC Unreviewed; 1136 AA. AC F8CZT4; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 01-APR-2015, entry version 25. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEH48980.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEH48980.1}; GN OrderedLocusNames=Geoth_3105 {ECO:0000313|EMBL:AEH48980.1}; OS Geobacillus thermoglucosidasius (strain C56-YS93). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=634956 {ECO:0000313|EMBL:AEH48980.1, ECO:0000313|Proteomes:UP000007149}; RN [1] {ECO:0000313|Proteomes:UP000007149} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C56-YS93 {ECO:0000313|Proteomes:UP000007149}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002835; AEH48980.1; -; Genomic_DNA. DR RefSeq; WP_013877326.1; NC_015660.1. DR RefSeq; YP_004589061.1; NC_015660.1. DR ProteinModelPortal; F8CZT4; -. DR EnsemblBacteria; AEH48980; AEH48980; Geoth_3105. DR KEGG; gth:Geoth_3105; -. DR KO; K00548; -. DR BioCyc; GTHE634956:GHH3-3154-MONOMER; -. DR Proteomes; UP000007149; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007149}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEH48980.1}; KW Transferase {ECO:0000313|EMBL:AEH48980.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 724 724 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1136 AA; 125812 MW; 7A2BCE48ABD2C3F2 CRC64; MGNITLQQQL EKKILIIDGA MGTMIQNAQL SADDFGGEQY EGCNEYLTLT APHVIKHIHE AYLQAGADII ETNTFGATSI VLDEYDLGHL ALELNIEAAK LARKAADAYS TPEWPRFVAG SMGPTTKTLS VTGGVTFEQL AAAYEEQARG LLLGGVDLLL LETCQDTLNV KAGFIGIMKA FAAVRKKVPI MISGTIEPMG TTLAGQTIES FFISVQHMKP FAVGLNCATG PEFMTDHLRT LASLADTAVS CYPNAGLPDE EGCYHETPEM LAKKIQRFAE KGWINIVGGC CGTTPEHIRA IAEAVRGIPP RPIPASFDVH AVSGIDPLIY DETMRPLFVG ERTNVIGSRK FKRLIAEGKY EEAAEIARAQ VKNGAHVIDI CLADPDRNEQ EDMEKFIQQV IKKVKVPLVI DSTDERVIEC ALTYSQGKAI INSINLEDGE ERFAKVVPLL HKYGAAVVVG TIDEQGMAIG AERKLEIALR SYDLLVNKYG VSPRDIIFDP LVFPVGTGDE QYIGAAKETI EGIRLIKERL PQCLTMLGIS NVSFGLPPLG REILNSVFLY HCTQAGLDYA IVNTEKLERF ASIPEEEVRL AEELLFNTND ETLNTFIQFY RNKMKEPKKA KTELSLEERL ANYVVEGTKD GLFADLEQAL QTYADPLDII NGPLMAGMDE VGRLFNDNQL IVAEVLQSAE VMKAAVAFLE PYMEKKESST KGKVLLATVK GDVHDIGKNL VDIILSNNGF HVIDLGIKVT PQKLIEAIQA EKPDIIGLSG LLVKSAQQMV VTAQDLRQAG ISIPILVGGA ALTRKFTENK IAPEYDGIVL YAKDAMEGLA LANQLQQNEI EYTKTEKHET KPEKTAPTVI AAKSNVSTDV PVFVPADLER HVLKDISLPH IIPYVNWQMV LGHHLGLKGK VKRLLEEKDE KALMLKEVVD GLLEEAMQHD WITPAAVYQF FPAQSDGNRI YIYSPEDKRT MIETFEFPRQ QKAPYLCLAD YLKPVESGQI DYVGFFAVTA GKGIRELAQQ WKEDGEFLKS HAIQALALEI AEGLAERIHQ IMRDRWGFPD DPDFTMEERF AAKYQGQRYS FGYPACPNLE DQEKLFRLLR PEEIGIHLTD GYMMEPEASV SAIVFAHPEA RYFNVL // ID F8D0L5_GEOTC Unreviewed; 616 AA. AC F8D0L5; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 25. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=Geoth_3104 {ECO:0000313|EMBL:AEH48979.1}; OS Geobacillus thermoglucosidasius (strain C56-YS93). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=634956 {ECO:0000313|EMBL:AEH48979.1, ECO:0000313|Proteomes:UP000007149}; RN [1] {ECO:0000313|Proteomes:UP000007149} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C56-YS93 {ECO:0000313|Proteomes:UP000007149}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; AEH48979.1; -; Genomic_DNA. DR RefSeq; WP_003252425.1; NC_015660.1. DR RefSeq; YP_004589060.1; NC_015660.1. DR ProteinModelPortal; F8D0L5; -. DR EnsemblBacteria; AEH48979; AEH48979; Geoth_3104. DR KEGG; gth:Geoth_3104; -. DR KO; K00547; -. DR BioCyc; GTHE634956:GHH3-3153-MONOMER; -. DR Proteomes; UP000007149; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007149}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:AEH48979.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:AEH48979.1}. SQ SEQUENCE 616 AA; 68136 MW; F86253039CF63049 CRC64; MGLLQDLKER ILIADGAMGT LLYSHGVDRC FEELNLSKPE DILHIHEAYI AAGAEVIQTN TYGANYVKLA RYGLEDEVPS INRAAVRLAK QAAKHKAYVL GTIGGLRSIN KSAVSIDEIK RTFREQLFVL LNEDIDGLLL ETYYDLEELK TVLAIARKET DKPIIAHVSL HEVGVLQDGT PLAEALAQLE QLGADVVGLN CRLGPYYMIR SLEEVPLPDH AFLSAYPNAS LPDYRDGRLV YETNTDYFKE TALAFREQGV RLIGGCCGTT PKHIEAMANA LVNRTPITEK AVKQRHVSIS IQTNEPNAAP PLQDIVRERR SVIVELDPPK KLGIGKFLEG AKALKAANID ALTLADNSLA TPRISNVALG TIIKEQLGVR PLIHITCRDR NLIGLQSHLM GLHTLGITDV LAITGDPSKI GDFPGATSVY DLSSFDLIRL IRQFNEGLSY SGKPLGQKTN FSIAAAFNPN VRHLDKAVER LEKKIQCGAH YFITQPLYSE QKIEEVYEAT KHLQTPIYIG IMPLVSARNA DFLHHEVPGI TLSDEIRARM AACANDPVQS AREGIAIAKS LIDAAFELFN GIYLITPFLR YEMTVELVRY IHEKEQAAQE REVLHG // ID F8DRQ0_LACRS Unreviewed; 310 AA. AC F8DRQ0; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AEI56284.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:AEI56284.1}; GN Name=mmuM {ECO:0000313|EMBL:AEI56284.1}; GN OrderedLocusNames=HMPREF0538_20070 {ECO:0000313|EMBL:AEI56284.1}; OS Lactobacillus reuteri (strain ATCC 55730 / SD2112). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=491077 {ECO:0000313|EMBL:AEI56284.1, ECO:0000313|Proteomes:UP000001924}; RN [1] {ECO:0000313|Proteomes:UP000001924} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 55730 / SD2112 {ECO:0000313|Proteomes:UP000001924}; 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 Lactobacillus reuteri ATCC 55730 / SD2112."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002844; AEI56284.1; -; Genomic_DNA. DR RefSeq; WP_003672322.1; NC_015697.1. DR RefSeq; YP_004648574.1; NC_015697.1. DR ProteinModelPortal; F8DRQ0; -. DR EnsemblBacteria; AEI56284; AEI56284; HMPREF0538_20070. DR KEGG; lru:HMPREF0538_20070; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; LREU491077:GH1M-80-MONOMER; -. DR Proteomes; UP000001924; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001924}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:AEI56284.1}; KW Transferase {ECO:0000313|EMBL:AEI56284.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 223 223 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 310 AA; 33727 MW; 9C07AF7E4404A973 CRC64; MTKITAELTK PLLIDGAMST ALEQLGADTN NSLWTASVLA NQPALVKKVH QEYFKAGARL AITDTYQANV PAFIKNGYSK QEAHSLIQRA VALAKEARDE YQQETGIYNY VAGALGPYGA YLANGSEYSG DYHLSTTEYQ QFHRPRLTDI LTVGVDVIAI ETQPRLDEVL AELDLVKELA PETLCYVSFS LKDSTHLPDG TPLAVAARTV AKYPNVFAVG VNCIPLEEVT AAIETIHQAT DKPVIAYPNS SATYDPTTKT WSYPHGRRGL VDYLPQWLAA GLTIIGGCCT TTPQDIAALH EYLEGGAHHD // ID F8E275_CORRG Unreviewed; 1233 AA. AC F8E275; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=5-methyltetrahydrofolate-homocysteinemethyltransferase {ECO:0000313|EMBL:AEI09392.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEI09392.1}; GN Name=metH {ECO:0000313|EMBL:AEI09392.1}; GN OrderedLocusNames=CRES_1036 {ECO:0000313|EMBL:AEI09392.1}; OS Corynebacterium resistens (strain DSM 45100 / JCM 12819 / GTC 2026). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=662755 {ECO:0000313|EMBL:AEI09392.1, ECO:0000313|Proteomes:UP000000492}; RN [1] {ECO:0000313|EMBL:AEI09392.1, ECO:0000313|Proteomes:UP000000492} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 45100 / JCM 12819 / GTC 2026 RC {ECO:0000313|Proteomes:UP000000492}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002857; AEI09392.1; -; Genomic_DNA. DR RefSeq; WP_013888407.1; NC_015673.1. DR RefSeq; YP_004605556.1; NC_015673.1. DR EnsemblBacteria; AEI09392; AEI09392; CRES_1036. DR KEGG; crd:CRES_1036; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; CRES662755:GIVW-1061-MONOMER; -. DR Proteomes; UP000000492; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000492}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEI09392.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000492}; KW Transferase {ECO:0000313|EMBL:AEI09392.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 241 241 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 781 781 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1233 AA; 133610 MW; D2061CA857ECA88E CRC64; MTNAKTLSAP AQPAFDHPFL NALRERVLIG DGAMGTQLQA VELDLDKDFL GLEGCNEILN ETRPDVLRDI HRAYFEAGAD LVETNTFGCN LPNLADYDIA DRIEDLAYRG AKIAREVADE MGPRPDDGMP SFVVGSMGPG TKLPSLGHAP YAALRDAYVE SARGLIRGGC DAILIETCQD LLQVKAAVLG AKQAFEELET RVPIVVHVTV ETTGTMLLGS EVGAALTALE PLGIDMIGMN CATGPDEMSE HLRYLSNNTS LPVSVMPNAG LPVLGANGAE YPLTAPELGV ALRGFVADYG LSMVGGCCGT TPEHITAVRE AVLGTQSVSS GASETKEKGP IAHSELAPPV APAVQAKRTV NVNNNVASLY QAVPLTQDTG ITMIGQRTNA NGSKAFREAM LAGDLEKCLE IAKDQVRDGA HMVDLCIDYV GRDGTEDMAR LAALLATNST LPIMIDSTEP DVIRVGLEHL GGRSAVNSVN FEDGDGPDSR YQRIMRLVKQ HGAAVVALTI DEEGQARTAE KKVEIAERLI ADITGSWGVP EEDIIVDCLT FPISTGQEET RKDGIETINA IRELKKRHPA VHTTLGLSNI SFGLNPAARQ VLNSVFLNEC IEAGLDTAIA HSSKILPMNR IDEEQRKVAL DMVYDRRTEG YDPLQTFMQL FEGVSAASAK DARAEALAAM PLFERLAQRI IDGDRNGLTD DLDEAMKEKD PVAIINEDLL AGMKTVGDLF GSGEMQLPFV LQSAETMKAA VANLEPHMES EAGSGASKGK MVIATVKGDV HDIGKNLVDI ILSNNGYDVV NIGIKQPISA ILEAAEENNA DVIGMSGLLV KSTVVMKENL EELNRLGKSH YPVMLGGAAL TRPYVEDDLT EVYDGDVYYS KDAFEALTVL DGIMAGLRGE HTEESAEVTV KREKRRARRE RSKAIAAKRK TNAEPVEVPA RSDVAIDVPL ATPPFWGPRI VKGISLADYL PNLDERALFR GQWGLMPSRA EAGPTYEELV ETDGRPRLRA LLDELKSNGV LDAAAVVYGY FPAVSEGDTV HFLPTPSSPA ASADPHAKPI HSFTFPRQQR GRFLNIADFI CSRERAIELG QTDVMPFQLV TMGQPIADFA NELFAKDAYR EYLEVHGVGV QLTEALAEYW HSRIRSELKF ADGTTAGDED SANMEDFFDL QYRGARFSFG YGSCPDMEDR RALVDMLEAE KLGVVLSEEL QLHPEQSTDA FVLYHPEAKY FNV // ID F8E4D9_FLESM Unreviewed; 1123 AA. AC F8E4D9; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEI15566.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEI15566.1}; GN OrderedLocusNames=Flexsi_1937 {ECO:0000313|EMBL:AEI15566.1}; OS Flexistipes sinusarabici (strain DSM 4947 / MAS 10). OC Bacteria; Deferribacteres; Deferribacterales; Deferribacteraceae; OC Flexistipes. OX NCBI_TaxID=717231 {ECO:0000313|EMBL:AEI15566.1, ECO:0000313|Proteomes:UP000006621}; RN [1] {ECO:0000313|Proteomes:UP000006621} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 4947 / MAS 10 {ECO:0000313|Proteomes:UP000006621}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002858; AEI15566.1; -; Genomic_DNA. DR RefSeq; WP_013887022.1; NC_015672.1. DR RefSeq; YP_004604134.1; NC_015672.1. DR EnsemblBacteria; AEI15566; AEI15566; Flexsi_1937. DR KEGG; fsi:Flexsi_1937; -. DR KO; K00548; -. DR BioCyc; FSIN717231:GI70-1973-MONOMER; -. DR Proteomes; UP000006621; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006621}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEI15566.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006621}; KW Transferase {ECO:0000313|EMBL:AEI15566.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 216 216 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 282 282 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 715 715 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1123 AA; 124616 MW; E95DC50557A41BAB CRC64; MFRKFAEKNI VVFDGGMGTT IQNESIPEAL WGDFYGCNEY LNISAPEIMK NIHRKYFQAG ADVAETNTFG ATRLILSEYG LEDQVYEINV AGAKLARGAA DEFSDKFVFG SMGPGTKLPS LSQISFDDLY EMYKEQSKGL MDGGVDGLIV ETSQDLLQIK SALKAIFDNL EELKIDLPVC VSITVESTGT MLVGSDISAA AALIGSYPVF SLGLNCGLGP DMMHKPLSEL TKYWNRSVSC IPNAGLPENV NGKTVYTMTP GKMAEIFKGL LDELPLNIIG GCCGTGYEHI KQLKNIAKSI NPSKPSGTAA ALSSSLYSST SLTQTPPPAI IGERANANGS KAFRELLLNN DYEGMLNVAK EQEDAGAHFI DVCVAYAGRD EMFDMQHFVS LLNKTLSAPI VIDSTEPPVI ETALKNYSGK PIINSINLED GGGKLHKILK LVHDYPANVI ALTIDENGMA MTADEKFKIA EKIYNIWTKQ YNLAPEGLIF DPLTFSIGSG DTSLKFAAVE TLNAIKMIKD RLKGAKTVLG VSNVSFGLSK ESRIFLNAVF LEEAVENGLD MAIVHASKLI NLSSMDKHEI NLCKNLIYGR ENALNEFISH FSGKSLQREE EVEEDITEEE ALVKKLKKGD KKDLEKIIDT LLQKYKPFEI INDILMPGMK EIGELFGSGK MLLPFVLQSA EVMKKSVTYL KKFINKEDTE TKGKVILATV KGDVHDIGKN LVEIILSNNG YEVYNLGIKV SVDEMIERAK EVKADAIGMS GLLVKSTGIM KENIAEIAQR QLDTTVLLGG AALTEGFVKN ECEPLLKGKV HYCADAFSAL KYLKTKPSQR RKISGKPQIN QVKSDTTGDE QIRNDLSTDD IPIPPFWGSK IEENIDINDA LKFMNRQTLY KTRWGYKKSS VSTEAEYIEL LKNEADSEYN EILLKLNNEI KINPKVSYGY FKCQSSDETL NIYDADEKLL ADVVFPRSSK PPFLSIPDYF KDIQSATFDV LPLQIVTLGS EPAEYTKQLK ENNRYKKYFL LHGFFTELTE ALAEFWHKRI REELKIDNKD ADSIDGILNG KYRGLRYSFG YPSCPDLYGN KIIGDLLSME KININLTETY QMVPEFSTSA LIAHNSKAEY FTL // ID F8E5A8_FLESM Unreviewed; 348 AA. AC F8E5A8; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Betaine--homocysteine S-methyltransferase {ECO:0000313|EMBL:AEI14604.1}; DE EC=2.1.1.5 {ECO:0000313|EMBL:AEI14604.1}; GN OrderedLocusNames=Flexsi_0945 {ECO:0000313|EMBL:AEI14604.1}; OS Flexistipes sinusarabici (strain DSM 4947 / MAS 10). OC Bacteria; Deferribacteres; Deferribacterales; Deferribacteraceae; OC Flexistipes. OX NCBI_TaxID=717231 {ECO:0000313|EMBL:AEI14604.1, ECO:0000313|Proteomes:UP000006621}; RN [1] {ECO:0000313|Proteomes:UP000006621} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 4947 / MAS 10 {ECO:0000313|Proteomes:UP000006621}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; AEI14604.1; -; Genomic_DNA. DR RefSeq; WP_013886094.1; NC_015672.1. DR RefSeq; YP_004603172.1; NC_015672.1. DR EnsemblBacteria; AEI14604; AEI14604; Flexsi_0945. DR KEGG; fsi:Flexsi_0945; -. DR KO; K00544; -. DR BioCyc; FSIN717231:GI70-958-MONOMER; -. DR Proteomes; UP000006621; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006621}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:AEI14604.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006621}; KW Transferase {ECO:0000313|EMBL:AEI14604.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 209 209 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 297 297 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 298 298 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 348 AA; 39222 MW; 70D6A13337D2BED7 CRC64; MKKPLLQRLD EGPVICGEGY LFELERRGYL QAGSFVPEVA LNNPEVLEEV HRDFVKAGSD IVQAFTYNGH REKMRIIGKE EKLESLNRSA IRVAKKVASD FNDEPLVAGN VSNTNIFNPS DHSSKEKVRL MFSEMIGWCK EEDVDMIIGE TFYYLEEALL ALEVMKQHNF TSVITLGIMA ENILEDGYTP TEACKILKDS GADVVGLNCF RGPETMLDIA LDIRRNVSGH IAVLPVTYRT TAEEPTFFNI TDKKRTACPQ HGRCFPDALE PLYCNRYEIA EFAKKAYEND IRYLGLCCGC NPAFLRAMAE AVGRNTINSE YSPDITKHFL YGKDPTLKKH IQDLGNKA // ID F8EMU3_RUNSL Unreviewed; 1300 AA. AC F8EMU3; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEI51593.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEI51593.1}; GN OrderedLocusNames=Runsl_5296 {ECO:0000313|EMBL:AEI51593.1}; 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 {ECO:0000313|EMBL:AEI51593.1, ECO:0000313|Proteomes:UP000000493}; RN [1] {ECO:0000313|Proteomes:UP000000493} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29530 / DSM 19594 / LMG 11500 / NCIMB 11436 / LSU 4 RC {ECO:0000313|Proteomes:UP000000493}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002859; AEI51593.1; -; Genomic_DNA. DR RefSeq; WP_013930863.1; NC_015703.1. DR RefSeq; YP_004658725.1; NC_015703.1. DR EnsemblBacteria; AEI51593; AEI51593; Runsl_5296. DR KEGG; rsi:Runsl_5296; -. DR KO; K00548; -. DR BioCyc; RSLI761193:GHKZ-5344-MONOMER; -. DR Proteomes; UP000000493; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 2. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 2. DR SUPFAM; SSF82282; SSF82282; 2. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000493}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEI51593.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000493}; KW Transferase {ECO:0000313|EMBL:AEI51593.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 265 265 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 328 328 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 329 329 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 779 779 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1300 AA; 144143 MW; 17B104E9F06B5E2F CRC64; MQNPNIQEIL KSRILVLDGA MGSMIQRYTL ADADYRGERF KDFPHELKGN NDLLSLTRPD VIREIHEAYL EAGADIIETN TFSGTTIAMA DYHMEDLVYE LNYESARLAR EACDKYAALN PDKPRFVAGS IGPTNRTASL SPDVNDPGFR AVTFDELVDA YYEQVQALTD GGADVMLVET IFDTLNAKAA LYAIDLYFDD VKKGTVRPIR GAFRPASVNT TKIQLPIMVS GTITDASGRT LSGQTTEAFL TSVSHMPLLS IGLNCALGAD LMRPYVQTLA TQAPFYTSAH PNAGLPNEMG EYDQTPEQMA VIIDDFLQNG FINIIGGCCG TTPPHIKAIA EVAAKYEPRD IPENDHVQKL SGLEPLKITK ETNFVNIGER CNVTGSKKFA RLIREGNYDA AIAVAREQVD TGAQVIDINM DEGMIDGVQA MTKFCNLLMA EPDIARVPFM VDSSKWEVIE AGLKCLQGKA IVNSISLKEG EEKFIQQAEK VRRYGASVVV MAFDEVGQAD NYERRLEICE RAYWILVNKV GFPPQDIIFD PNILTVGTGM EEHNNYAVDF INATRWIKEH LPYAKVSGGV SNVSFSFRGN EPVREAIHTV FLYHAIKAGM DMGIVNAGQL GVYDDLPKDM LEHCEDLILN RRPDATERML AFAETVKSKG KEQVIDTAWR DQPVAKRLEH ALIKGLTEYI DQDVEEARQT VDKPLHVIEG PLMDGMNVVG DLFGEGKMFL PQVVKSARVM KKAVAYLLPF IEEEKNASPS TTESGGSKIL LATVKGDVHD IGKNIVGVVL ACNNYEIIDL GVMVPTDKIL AAAKEHNVDI IGLSGLITPS LDEMVGVAKE MERQGFKVPL LIGGATTSRI HTAVKIDPHY SGPVIHVLDA SRAVPVAGKL TQNEQTYAEA LADIKKEYAK LREDHAKRQQ AKEAVTIEAA RANKTKIDWE TFTPVKPAFL GNRYFYDYPL EEIAKYIDWT PFFQTWQLHG KYPKIFDDAV VGNEAKKLYN DAKAMLAEII QNKSLKANAV IGFYPANSVG DDIVLHDFEE VEVRFAGQGQ KKRTEYRVVL SSGASEVGTS QKTETDFQSA QTVLHHLRQQ NQKAANLPNL CLSDYIMPLS GDKPEAINDG ITNPAEPLRT DYIGAFAVTA GIGIEALLEK YEADHDDYNS IMVKAVADRL AEAFTELMHE RVRKEYWGYV KDEALSNEEL ISEKYQGIRP APGYPACPEH TEKRTLFDLL DAEAQIGIQL TESFAMYPAS SVSGWYFAHP DSRYFALGKI AKDQVQDYAA RKGMTLEEAE KWLSPVLNYD // ID F8EV46_ZYMMT Unreviewed; 351 AA. AC F8EV46; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AEI38264.1}; GN OrderedLocusNames=Zymop_1374 {ECO:0000313|EMBL:AEI38264.1}; 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 {ECO:0000313|EMBL:AEI38264.1, ECO:0000313|Proteomes:UP000000491}; RN [1] {ECO:0000313|EMBL:AEI38264.1, ECO:0000313|Proteomes:UP000000491} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29192 / JCM 10191 / NBRC 13757 / NCIMB 11200 / NRRL B-4491 RC {ECO:0000313|Proteomes:UP000000491}; 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; AEI38264.1; -; Genomic_DNA. DR RefSeq; WP_013934653.1; NC_015709.1. DR RefSeq; YP_004662554.1; NC_015709.1. DR EnsemblBacteria; AEI38264; AEI38264; Zymop_1374. DR KEGG; zmp:Zymop_1374; -. DR KO; K00548; -. DR BioCyc; ZMOB579138:GJDN-1427-MONOMER; -. DR Proteomes; UP000000491; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000491}; KW Methyltransferase {ECO:0000313|EMBL:AEI38264.1}; KW Transferase {ECO:0000313|EMBL:AEI38264.1}. SQ SEQUENCE 351 AA; 38168 MW; 1B46532A0B53E30E CRC64; MEESAAAKRL REEASKRVLL TDGAFGTMIQ RYNLNEAAYR GHYSLNHEQK GNNDLLVLTR PDVIDAITRA YLDAGSDIVS TNSFNANKIS QSDYQAEALV TEMNQQAAAI ARKAADEYQA RDGRPRFVAG AVGPTNKTLS LSPDVNDPGY RAITFDELRE VYAHQIAGLI AGGADFILIE TIFDTLNAKA AVMAVMQESQ RLEKEIPMMI SMTITDMSGR NLSGHSIEAF WYSIRHAKPL TIGLNCSFGA DKLRPHVKTL SALADTLLMA YPNAGLPNDL GQYDEMPETT GALIHEWAES GLVNIVGGCC GSTPDHIAAM ARAVKGYPPR KLALLRPAMR LSGLDPMIIP A // ID F8F2E4_TRECH Unreviewed; 1270 AA. AC F8F2E4; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 01-APR-2015, entry version 26. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEJ20926.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEJ20926.1}; GN OrderedLocusNames=Spica_2832 {ECO:0000313|EMBL:AEJ20926.1}; OS Treponema caldaria (strain ATCC 51460 / DSM 7334 / H1) (Spirochaeta OS caldaria). OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema. OX NCBI_TaxID=744872 {ECO:0000313|EMBL:AEJ20926.1, ECO:0000313|Proteomes:UP000000503}; RN [1] {ECO:0000313|Proteomes:UP000000503} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 51460 / DSM 7334 / H1 {ECO:0000313|Proteomes:UP000000503}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002868; AEJ20926.1; -; Genomic_DNA. DR RefSeq; WP_013970204.1; NC_015732.1. DR RefSeq; YP_004699434.1; NC_015732.1. DR EnsemblBacteria; AEJ20926; AEJ20926; Spica_2832. DR KEGG; scd:Spica_2832; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; SCAL744872:GHIK-2892-MONOMER; -. DR Proteomes; UP000000503; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000503}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEJ20926.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000503}; KW Transferase {ECO:0000313|EMBL:AEJ20926.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 799 799 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1270 AA; 138633 MW; 9CE655C22B56DF7A CRC64; MTVREQLDVL AAKRILLLDG AMGTMIQKFG LTEADFRGAE FQNHPKPLLG CNDILCITKP SVIASIHQAY LRAGSDIIET NSFNANAISL ADYNLESYAF EISRAAARVA RESADLYSTA ERPRFVAGVL GPTSKTASIS PDVNDPGARA VTWEELEAAY YDNARGLLAG GADILMIETI FDTLNAKAAI AAIQRLFEAR ASAGLPEVPI MISGTIVDAA GRTLSGQTVE AFCVSVMHAK PWSIGLNCSL GAERLYPHVA ALSEIAPCLV SAHPNAGLPN RFGQYDESAQ TMAGFIEAFL RDGLVNIVGG CCGSTPAHIA EIARVTMNYQ PRVIPALPRK TVLAGLEPLV VDPAIGFIDV GERTNVAGSR KFLRLIKEER YDEALSIARD MVEAGASIID VCMDDALLDA PRAMQKFLNL ALADPEIARL PVMVDSSRWE AIEAGLKCLQ GKGIVNSISL KEGEEAFLRK SRIARRMGAA VVVMLFDERG QADSYERKVE VAQRSYQLLI QDGMKGEDII FDPNVLAIAT GIPEHDRYAL DFIKACRWIR ANCPGAKISG GVSNLSFSFR GYDLVREAMH AVFLKYAIEA GLTMAIVNPA GLVPYDELEP RLREVAEDVV LARRSDAAER LLALALELKE ASDVADGHGT VGSDSSTGST HSAADKNVWR TLPVEERLQY ALVKGIEDYI EPDILEARSR YQRSLDVIEG PLMKGMNEVG DRFGAGKMFL PQVIRSARVM KKAVAVLEPF IQEEKLADAR LTSQDAVKRS EDGSEKKSEP KRKSGATKII MATVKGDVHD IGKNIVGVVL GCNGYEVHDL GVMIPPDEIA EAIIREQADL VGLSGLITPS LDEMVHTARE LERRGVSIPL LIGGATTSEA HTALRIAPAY SGPVVYVKDA SRAAAVVRAL LSNTEKARFL EELETKYAEA ITRHETIQDR IELIPIEKAR SNKLPTDWSH MEIVEPRQKG LVTFHDFPLE SLVPYIDWSY FFYGWDLGHG FERILEDPEK GEAARKLYDD AQVLLDRLVS EHILTAHGVA GFFSAQSLGD DILLFSADPS GADLNGFGTP IARFSFLRNQ EKKLAGGFNP CLSDFIAPES SGRTDWIGLF AVTAGHGLET FVADCKARGD DYTALLAASL ADRLAEAFAE KLHALVRTEL WGYVAEENLN AKELFEGKYR GIRPAFGYPA CPDHHDKRIA CKVLEAEQRC GIKLTESSMM QPAASVCGMY FAHPASYYFG VGRVGEDQLE DWARRKGISI EDARDRIGRL // ID F8F5R5_PAEMK Unreviewed; 1180 AA. AC F8F5R5; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEI41479.1}; GN OrderedLocusNames=KNP414_02921 {ECO:0000313|EMBL:AEI41479.1}; OS Paenibacillus mucilaginosus (strain KNP414). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1036673 {ECO:0000313|EMBL:AEI41479.1, ECO:0000313|Proteomes:UP000006620}; RN [1] {ECO:0000313|Proteomes:UP000006620} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KNP414 {ECO:0000313|Proteomes:UP000006620}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002869; AEI41479.1; -; Genomic_DNA. DR RefSeq; WP_013916640.1; NC_015690.1. DR RefSeq; YP_004641349.1; NC_015690.1. DR EnsemblBacteria; AEI41479; AEI41479; KNP414_02921. DR KEGG; pms:KNP414_02921; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; PMUC1036673:GJD1-2921-MONOMER; -. DR Proteomes; UP000006620; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006620}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 263 263 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 326 326 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 327 327 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1180 AA; 129952 MW; DF267CB453F96C2E CRC64; MREGPFAAAA DALPQRKAGL SFRVVKEKDG RGRGSVMSKP SLQEQLKKKI MILDGAMGTM IQQENLTEAD FGSEDLDGCN EILVVTRPDV IQKIHEAYFA AGADMVETNT FGATSVVLAE YDLQDRAREL NLAAAKLAIE AANKYSTPEW PRYVIGAMGP TTKTLSVTGG VTFDELVESY QEQAEALIEA GVDALLLETS QDTLNVKAGS IGIRSAFDKL GVKLPLMISG TIEPMGTTLA GQNIESFYVS LEHLNPVSFG LNCATGPEFM RDHIRTLSEI AGTAVSCYPN AGLPDENGKY HESPESLALK LAGFAEQGWL NIAGGCCGTT PDHIRAMAET LGKFEPRKQA GVHPPAISGI ETVYVEPDNR PIMVGERTNI SGSRKFKRLI KEGKFEEASE IARTQVKNGA HIIDINLQDT DIDEAYAINE FLPQVVKKVK VPLMIDSTYD HIIELGLKYS QGKAIVNSIN LEDGESKFEA IVPLLHKYGA AVVMILIDER GQAVSRQAKM EVADRAYELL TKKYGMKPQD IIFDPNMFPV GSGDPQYIGS AVETIEGIRM IKEKYPETMT ILGLSNISFG LPDAGREVLN SVYLYHCTKA GLDYAIVNTE KLERYASIPE EERALAEELI FNTNDDTLAK FVAYFRVKKV EKKEKISNLT LEERLASYVV EGTKEGLIPD LEEALKKYAP LDIINGPLMK GMEEVGRLFN NNELIVAEVL QSAEVMKASV AHLEQYMEKA DSAVKGKIIL ATVKGDVHDI GKNLVEIILS NNGYKIVNLG IKVPPEQLIE AYRKEKPDAI GLSGLLVKSA QQMVVTAQDM KNAGIDVPIL VGGAALTRKF TKTRIAPEYD GMVLYAKDAM GGLDIANKLS DPEQRQVLIR ELRESMDSDV KEAGRKEESM PALTRVMTST VDRTVPVQVP PDLERRVLRD YPISHLVPYV NMQMLLGHHL GLKGKVENLI AEKDPKALQL KETVDGILAE AQQAGIIKAQ GMYRFFPAQS DGNDVLIYDP EDTGRVVQKF TFPRQEKEPY LCLADYLKPV SSGEMDYVGF LVVTAGHGVS ELSAQWREKG DYLRSHALQA AALELAEGFA ERVHQMMRDQ WGFPDPAEMT MAERFGAKYR GQRFSFGYPA CPNLDDQQQL FALLHPEDIG VTLTEGSMME PEASVSAIVF AHPQARYFNA // ID F8FC39_PAEMK Unreviewed; 627 AA. AC F8FC39; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 22. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=KNP414_05916 {ECO:0000313|EMBL:AEI44440.1}; OS Paenibacillus mucilaginosus (strain KNP414). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1036673 {ECO:0000313|EMBL:AEI44440.1, ECO:0000313|Proteomes:UP000006620}; RN [1] {ECO:0000313|Proteomes:UP000006620} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KNP414 {ECO:0000313|Proteomes:UP000006620}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; AEI44440.1; -; Genomic_DNA. DR RefSeq; WP_013919591.1; NC_015690.1. DR RefSeq; YP_004644310.1; NC_015690.1. DR EnsemblBacteria; AEI44440; AEI44440; KNP414_05916. DR KEGG; pms:KNP414_05916; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR BioCyc; PMUC1036673:GJD1-5916-MONOMER; -. DR Proteomes; UP000006620; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006620}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:AEI44440.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:AEI44440.1}. SQ SEQUENCE 627 AA; 68018 MW; 9047563C5163022C CRC64; MKPGLREALR SQVLVGDGAM GTYLYQMGFP IGISYEELNL LKPDVIMDVH RRYYEAGARL IETNTFSANR EKLSKFGLEG EVEAINRAGV ELARRAVGED AYVVGAVGSI RAGKRKNVRT NKVREDLREQ ISILCDTKVD GLLLESFLDL DEMLIALKEV RRISDLPVIC QFATEGAGVT QDGVPLKEAF AKLLEAGADV VGLNCRSGPN GLLRSLEGAA AAEADHPPYS VFPNAGLADY VDGRYSFPAT PQYFGETARR FADLGTRIIG GCCGTTPEHI AAVAGALAGY VPNPEAAKRA AAAPAAEVAE RAAAGAGAEV PTEPSIVDLV RQRHTVIVEL DPPKDLDIGK FMEGTEALKK AGVDALTMAD NSLAVTRMSN LALGSIVKER TGIRPLIHIA CRDRNLIGTQ SHMMGLHALG IDHVLAVTGD PARFGDLPGS SSVYDLTSFE IIRMIKQLNE GIAFSGKPLK KQANFIIGAA FNPNVKYLDK AVQRLERKVE AGADYIMTQP VYNAELIEQV YEATKHLSVP IFIGIMPLAS GNNAEYLHNE VPGIQLSDDV RKRMSGLRGE EGRAMGVQIG RELLDAAMRR FNGIYLMTPF LAYEMTVQLT EYVWEKAGRR HLSPLPK // ID F8FRW4_PSEP6 Unreviewed; 294 AA. AC F8FRW4; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 29-APR-2015, entry version 17. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:AEJ11241.1}; GN ORFNames=PPS_0658 {ECO:0000313|EMBL:AEJ11241.1}; OS Pseudomonas putida (strain S16). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1042876 {ECO:0000313|EMBL:AEJ11241.1, ECO:0000313|Proteomes:UP000000502}; RN [1] {ECO:0000313|EMBL:AEJ11241.1, ECO:0000313|Proteomes:UP000000502} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S16 {ECO:0000313|EMBL:AEJ11241.1, RC ECO:0000313|Proteomes:UP000000502}; 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 ----------------------------------------------------------------------- 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; AEJ11241.1; -; Genomic_DNA. DR RefSeq; WP_013970800.1; NC_015733.1. DR RefSeq; YP_004700121.1; NC_015733.1. DR EnsemblBacteria; AEJ11241; AEJ11241; PPS_0658. DR KEGG; ppt:PPS_0658; -. DR BioCyc; PPUT1042876:GH0R-652-MONOMER; -. DR Proteomes; UP000000502; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000502}; KW Methyltransferase {ECO:0000313|EMBL:AEJ11241.1}; KW Transferase {ECO:0000313|EMBL:AEJ11241.1}. SQ SEQUENCE 294 AA; 31279 MW; F56CCC044142F5B9 CRC64; MVILDGGMGR ELQRSGAPFR QPEWSALALS EAPEAVVGVH AAFIAAGAQV ITSNSYAVVP FHIGEERFAK EGRQLANIAG QLARHAADTA AHPVKVAGSL PPLFGSYRPD LFQPERVEEV LAPLLQGLAP HVDLWLAETQ SSVAEVRAIH GQLPADGRPF WVSFTLQDEE VDEVPRLRSG EPVADAIEAV VGLGAAAVLF NCSQPEVIGA ALDVARSVIE RHNADIAIGA YANAFPPQPK EATANDGLDE LREDLDPPGY LAWASDWRER GASMIGGCCG IGPEHIAELK RNLA // ID F8FYT9_PSEP6 Unreviewed; 1235 AA. AC F8FYT9; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:AEJ12528.1}; GN ORFNames=PPS_1961 {ECO:0000313|EMBL:AEJ12528.1}; OS Pseudomonas putida (strain S16). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1042876 {ECO:0000313|EMBL:AEJ12528.1, ECO:0000313|Proteomes:UP000000502}; RN [1] {ECO:0000313|EMBL:AEJ12528.1, ECO:0000313|Proteomes:UP000000502} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S16 {ECO:0000313|EMBL:AEJ12528.1, RC ECO:0000313|Proteomes:UP000000502}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002870; AEJ12528.1; -; Genomic_DNA. DR RefSeq; WP_013971946.1; NC_015733.1. DR RefSeq; YP_004701408.1; NC_015733.1. DR EnsemblBacteria; AEJ12528; AEJ12528; PPS_1961. DR KEGG; ppt:PPS_1961; -. DR KO; K00548; -. DR BioCyc; PPUT1042876:GH0R-1939-MONOMER; -. DR Proteomes; UP000000502; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000502}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1235 AA; 135414 MW; 811E37C4BFFB15F6 CRC64; MSDRSARLQA LQNALKERIL ILDGGMGTMI QSYRLEEHDY RGTRFADWPS DVKGNNDLLL LSRPDVIAAI EKAYLDAGAD ILETNTFNAT QISQADYGME SLVYELNVEG ARIARQVADA KTLETPHKPR FVAGVLGPTS RTCSISPDVN DPGYRNVTFD ELVTNYIEAT RGLIEGGADL LLIETIFDTL NAKAAIFAVQ QVFEEDGIEL PIMISGTITD ASGRTLSGQT TEAFWNSVRH AKPISVGLNC ALGAKDLRPY LEELATKADT HVSAHPNAGL PNAFGEYDET PAEMAVVVEE FAASGFLNII GGCCGTTPGH IQAIAEAVAK YKPREIPEIA KACRLSGLEP FTIDRQSLFV NVGERTNITG SAKFARLIRE ENYTEALEVA LQQVEAGAQV IDINMDEGML DSQAAMVRFL NLIAGEPDIS RVPIMIDSSK WEVIEAGLKC IQGKGIVNSI SMKEGVEQFK HHARLCKRYG AAVVVMAFDE VGQADTAARK KEICQRSYDI LVNEVGFPPE DIIFDPNIFA VATGIEEHNN YAVDFIEACA YIRDHLPHAL SSGGVSNVSF SFRGNNPVRE AIHSVFLYHA IQNGLTMGIV NAGQLEIYDE IPPALREKVE DVVLNRTPHG TDALLAIADD YKGGGATREV ENEEWRSLPV EKRLEHALVK GITAFIVEDT EECRQQCARP IEVIEGPLMN GMNVVGDLFG AGKMFLPQVV KSARVMKQAV AHLIPFIEAE KGDKPEAKGK ILMATVKGDV HDIGKNIVGV VLGCNGYDIV DLGVMVPAEK ILQTARDEKC DIIGLSGLIT PSLDEMVHVA REMQRQGFQL PLMIGGATTS KAHTAVKIEP KYSNDAVVYV TDASRAVGVA TQLLSKELKA GFVEKTRQEY EEVRERTANR SARTERLSYA QAIAAKPQYD WAGYQPAVPS FTGVKVLEDI DLRTLAEYID WTPFFISWDL AGKFPRILTD EVVGEAATAL YKDAREMLDK LIDEKLISAR AVFGFWPANQ VADDDIEVYG EDGQALATLH HLRQQTIKPD GKPNWSLADF VAPKASGVTD YVGGFITTAG IGAEEVAKAY QDKGDDYSSI MVKALADRLA EACAEWLHEQ VRKEHWGYAR DEHLDNEALI KEQYRGIRPA PGYPACPDHT EKETLFRLLD GTAIGETGPS GVFLTDHFAM FPAAAVSGWY FAHPQAQYFA VGKVDKDQIE RYSARKGQDV SVSERWLAPN LGYDS // ID F8G7T0_FRAST Unreviewed; 353 AA. AC F8G7T0; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 01-APR-2015, entry version 20. DE SubName: Full=Betaine--homocysteine S-methyltransferase {ECO:0000313|EMBL:AEI35046.1}; DE EC=2.1.1.5 {ECO:0000313|EMBL:AEI35046.1}; GN OrderedLocusNames=F7308_0118 {ECO:0000313|EMBL:AEI35046.1}; OS Francisella sp. (strain TX077308). OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Francisellaceae; Francisella. OX NCBI_TaxID=573569 {ECO:0000313|EMBL:AEI35046.1, ECO:0000313|Proteomes:UP000000490}; RN [1] {ECO:0000313|Proteomes:UP000000490} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TX077308 {ECO:0000313|Proteomes:UP000000490}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; AEI35046.1; -; Genomic_DNA. DR RefSeq; WP_013921907.1; NC_015696.1. DR RefSeq; YP_004646646.1; NC_015696.1. DR EnsemblBacteria; AEI35046; AEI35046; F7308_0118. DR KEGG; frt:F7308_0118; -. DR KO; K00544; -. DR BioCyc; FSP573569:GHZ6-118-MONOMER; -. DR Proteomes; UP000000490; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000490}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:AEI35046.1}; KW Transferase {ECO:0000313|EMBL:AEI35046.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 213 213 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 302 302 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 353 AA; 39744 MW; F6FBD175A4BD9FFE CRC64; MKKENLLERL DKGPVICAEG FLFEIERRGY MSSGEFVPMV SLEHPEVLEN LHRDFQHAGS DIVEAFTYNG HREKLRVIGK EHLLEKLNRE ALRIAKKVAD TTPEGVQPNL LAGNISNSNI WKQGDQESQK EVTRMFDEMI TWATEEGADI LIGETFYYAE EAFRALEIMK KANLPTVLTI APMAQNTMRD GWSIVDTCKE LEQLGADVVG LNCFRGPQTM LPDLKKIREA VKCHVAGLPI PYRTTDSHPT FFNLPDNNGC GCPAPHGRTF PTALDPLYCN RYEIRDFAKE AYDFGANYLG VCCGASPMLI REVADAVGLT VPGSKYKEKM ENHFMYGTNK RIAKHMQEYG SKA // ID F8GH06_NITSI Unreviewed; 1236 AA. AC F8GH06; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 01-APR-2015, entry version 25. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEJ02488.1}; GN OrderedLocusNames=Nit79A3_2732 {ECO:0000313|EMBL:AEJ02488.1}; OS Nitrosomonas sp. (strain Is79A3). OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Nitrosomonadaceae; Nitrosomonas. OX NCBI_TaxID=261292 {ECO:0000313|EMBL:AEJ02488.1, ECO:0000313|Proteomes:UP000000501}; RN [1] {ECO:0000313|EMBL:AEJ02488.1, ECO:0000313|Proteomes:UP000000501} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Is79A3 {ECO:0000313|EMBL:AEJ02488.1, RC ECO:0000313|Proteomes:UP000000501}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002876; AEJ02488.1; -; Genomic_DNA. DR RefSeq; WP_013966720.1; NC_015731.1. DR RefSeq; YP_004695887.1; NC_015731.1. DR EnsemblBacteria; AEJ02488; AEJ02488; Nit79A3_2732. DR KEGG; nii:Nit79A3_2732; -. DR KO; K00548; -. DR BioCyc; NSP261292:GH7H-2765-MONOMER; -. DR Proteomes; UP000000501; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000501}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000501}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 249 249 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 315 315 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 767 767 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1236 AA; 136123 MW; 0B848B5878BAC821 CRC64; MTRESRTALL ESLFAQRILI LDGAMGTMIQ TFKLTETDFR GQRFADFPHD LRGNNDLLTL TQPQVIRSIH TGYLEAGADI LETNTFNSNA ASMADYHMQD LVYELNCSAA KLAREAAQSF EARTPEKPRF VAGVIGPTTK TASISPDVND PGFRGITYDQ LVVDYTESIR GLVDGGVDIL LVETIFDSLN AKAALFAIDQ FFEDHGIRLP IMISVTITDA SGRTLSGQTP EAFWNSVSHT RPISVGINCA LGAELMRPYI EELAGVADVY TSVHPNAGLP NPLSDTGYDE SPEYTANQIK GFAQSGFVNI VGGCCGTTPA HIKAIAQAVS DIAPRKIPEI PKKLRLSGLE PLNIGDDSLF VNVGERTNVT GSRAFARLIL NDDYAEALNV ARSQVESGAQ IIDINMDEAM LDSQKAMVTF LNLVAAEPDI CKVPIMLDSS KWTVIEAGLK CVQGKSIINS ISMKEGEEEF IKHAKLARRY GAAVIVMAFD EQGQADTLKR KVDICTRSYR LLVDQVGFPP EDIIFDPNIF AIATGIEEHN NYGVDFIDAT RIIKQTLPYA KVSGGVSNVS FSFRGNEPIR EAIHTAFLYH AIKAGMTMGI VNAGQLGVYT DIPAELLEKV EDVILNRRAD ATEHLVEFAE NFKGKKKEQV EDLAWRAEPL QQRLTHALVR GIDTFIVEDT EAARVEIENK GGRPIQVIEG PLMEGMSVVG DLFGAGKMFL PQVVKSARVM KQAVAHLLPF IEAEKKLSGD NKPKGKIVIA TVKGDVHDIG KNIVTVVLQC NNYEVINMGV MVPSAQILDM ARREKADIIG LSGLITPSLE EMAHVAKEMQ REGFTIPLLI GGATTSRVHT AVKIAPHYEG ATVWVPDASR AVGVCTNLLS RDLLAGYVQE IKEEYEKVRT QHKNKKGTAK LLTLAQARAN AYQTDWANYH PYQPELIGVR TLNNYPLDKI VPYIDWTPFF QAWELAGRYP DILQDEVVGE TASQLFRDAQ TMLKKIVEQK WLNANAVIGL FPANSVGDDI EIYTDQTRSK LAMTYHCLRQ QDQKPTGKPN RCLSDFIAPK ETGIKDTIGL FAVGAGFGID ERVKAFEDAN DDYSAIVLKA LADRLAEAFA EHMHARVRRE FWGYAKDETL SNEQLINEEY KGIRPAPGYP ACPDHTEKGP LFAVLNASEN AGIIITESFA MVPTAAVSGF YFAHPESTFF AVGKIGKDQV EDYAKRKGWT VEETEKWLAP VLAYER // ID F8GZC6_PSEUT Unreviewed; 1230 AA. AC F8GZC6; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 29-APR-2015, entry version 29. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:AEJ05387.1}; GN Name=metH {ECO:0000313|EMBL:AEJ05387.1}; GN OrderedLocusNames=PSTAB_2106 {ECO:0000313|EMBL:AEJ05387.1}; 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 {ECO:0000313|EMBL:AEJ05387.1, ECO:0000313|Proteomes:UP000008932}; 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] {ECO:0000313|Proteomes:UP000008932} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17588 / DSM 5190 / CCUG 11256 / JCM 5965 / LMG 11199 / RC NCIMB 11358 / Stanier 221 {ECO:0000313|Proteomes:UP000008932}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002881; AEJ05387.1; -; Genomic_DNA. DR RefSeq; WP_013982880.1; NC_015740.1. DR RefSeq; YP_004714476.1; NC_015740.1. DR EnsemblBacteria; AEJ05387; AEJ05387; PSTAB_2106. DR KEGG; psz:PSTAB_2106; -. DR KO; K00548; -. DR BioCyc; PSTU96563:GHIN-2153-MONOMER; -. DR Proteomes; UP000008932; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008932}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1230 AA; 134871 MW; 2DF13D055383CA94 CRC64; MSARIARLQA LQHALSQRIL ILDGGMGTMI QSYKLEESDY RGERFADWPS DVKGNNDLLL LSRPDVIQAI EKAYLDAGAD ILETNTFNAT RVSQADYGME ELVYELNVEG ARLAREVADA KTAETPDRPR FVAGVLGPTS RTCSISPDVN NPGYRNVTFD LLVENYIEAT RGLIEGGADL ILIETIFDTL NAKAAIFAVQ QVFEEDGVEL PIMISGTITD ASGRTLSGQT TEAFWNSVRH AKPISVGLNC ALGAKDLRPY LEELANKADT HVSAHPNAGL PNAFGEYDET PAEMAAVVEE FAASGFLNII GGCCGTTPAH IQAIAEAVAK YPPRVIPDIP KACRLSGLEP FTIDRSSLFV NVGERTNITG SAKFARLIRE ENYTEALEVA LQQVEAGAQV IDINMDEGML DSKAAMVTFL NLIAGEPDIS RVPIMIDSSK WEVIEAGLKC IQGKGIVNSI SMKEGVEQFK HHAHLCKRYG AAVVVMAFDE AGQADTAARK REICQRSYDI LVNEVGFPPE DIIFDPNIFA IATGIEEHNN YAVDFIEACA FIRDNLPYAL TSGGVSNVSF SFRGNNPVRE AIHSVFLFHA IKAGLTMGIV NAGQLEIYDE IPKELRDAVE DVVLNRSAGG TEALLEIADK YKGDGSVKEA ETEEWRSLPV DKRLEHALVK GITAFIVEDT EECRQQCARP IEVIEGPLMS GMNVVGDLFG AGKMFLPQVV KSARVMKQAV AHLIPFIEAE KGDKPEAKGK ILMATVKGDV HDIGKNIVGV VLGCNGYDVV DMGVMVPAEK ILQTAIAEKC DIIGLSGLIT PSLDEMVHVA KEMQRQGFSL PLMIGGATTS KAHTAVKIDP QYSNDAVVYV TDASRAVGVA TTLLSKELKP AFVDKTREEY AMIRERTANR SARTERLSYL DAIANKPPFD WSGYIPVKPS FTGRQVLEDI DLRTLVDYID WTPFFIAWDL AGKYPRILED EVVGEAATSL FNDAQAMLKK LVDEKLIRAR AVFGFWPANQ IQDDDLEVYG DNGEKLATLH HLRQQTIKPD AKPNLSLADF VAPKSTGITD YVGGFICTAG IGAEELAKAY QDKGDDYNSI MVKALADRLA EACAEWLHEQ VRKHYWGYAP DERLSNEELI REQYKGIRPA PGYPACPDHT EKGTLFQLLD ADGISQVTLT EHYAMLPTAA VSGWYFAHPE AQYFAVGKID KDQVESYSQR KGQELAISER WLMPNLGYDN // ID F8HET8_STRE5 Unreviewed; 316 AA. AC F8HET8; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Homocysteine S-methyltransferase 1 {ECO:0000313|EMBL:AEJ53841.1}; GN Name=mmuM {ECO:0000313|EMBL:AEJ53841.1}; GN OrderedLocusNames=Ssal_01576 {ECO:0000313|EMBL:AEJ53841.1}; OS Streptococcus salivarius (strain 57.I). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1046629 {ECO:0000313|EMBL:AEJ53841.1, ECO:0000313|Proteomes:UP000000293}; RN [1] {ECO:0000313|EMBL:AEJ53841.1, ECO:0000313|Proteomes:UP000000293} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=57.I {ECO:0000313|EMBL:AEJ53841.1, RC ECO:0000313|Proteomes:UP000000293}; RX PubMed=21914897; DOI=10.1128/JB.05670-11; RA Geng J., Huang S.C., Li S., Hu S., Chen Y.Y.; RT "Complete genome sequence of the ureolytic Streptococcus salivarius RT strain 57.I."; RL J. Bacteriol. 193:5596-5597(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; CP002888; AEJ53841.1; -; Genomic_DNA. DR RefSeq; WP_014633424.1; NC_017594.1. DR RefSeq; YP_006068704.1; NC_017594.1. DR EnsemblBacteria; AEJ53841; AEJ53841; Ssal_01576. DR KEGG; stf:Ssal_01576; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR BioCyc; SSAL1046629:GLLG-1431-MONOMER; -. DR Proteomes; UP000000293; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000293}; KW Methyltransferase {ECO:0000313|EMBL:AEJ53841.1}; KW Transferase {ECO:0000313|EMBL:AEJ53841.1}. SQ SEQUENCE 316 AA; 34784 MW; 73D42C80833F47B2 CRC64; MAIFKDYLEN KSPLILHGAL GTEMESLGYD ISGKLWSAKY LLEKPEVIQK IHETYVAAGS DLITTSSYQA TLPGLIDAGL TKEEAEQIIA LTVQLAKDAR DKVWATLDET EKAKRPYPLI SGDVGPYAAY LANGSEYTGD YGQITIKELK EFHRPRIQIL LDQGVDLLAL ETIPNRLEAQ ALIELLAEEF PEAEAYISFT VQEPGTISDG TSLDEIAQLV GQSDQILALG INCSSPLLYN QALAILKNAG KALITYPNSG EVYDGSTQTW KPKDKDALTL VEHSKDWHTQ FGVKILGGCC RTRPNDIKAL YAEFRT // ID F8I657_SULAT Unreviewed; 623 AA. AC F8I657; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 29-APR-2015, entry version 24. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN Name=mmuM {ECO:0000313|EMBL:AEJ41095.1}; GN OrderedLocusNames=TPY_2937 {ECO:0000313|EMBL:AEJ41095.1}; OS Sulfobacillus acidophilus (strain TPY). OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Clostridiales Family XVII. Incertae Sedis; Sulfobacillus. OX NCBI_TaxID=1051632 {ECO:0000313|EMBL:AEJ41095.1, ECO:0000313|Proteomes:UP000000291}; RN [1] {ECO:0000313|EMBL:AEJ41095.1, ECO:0000313|Proteomes:UP000000291} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TPY {ECO:0000313|EMBL:AEJ41095.1, RC ECO:0000313|Proteomes:UP000000291}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; AEJ41095.1; -; Genomic_DNA. DR RefSeq; WP_013987811.1; NC_015757.1. DR RefSeq; YP_004720838.1; NC_015757.1. DR EnsemblBacteria; AEJ41095; AEJ41095; TPY_2937. DR KEGG; say:TPY_2937; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR BioCyc; SACI1051632:GH78-2935-MONOMER; -. DR Proteomes; UP000000291; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000291}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:AEJ41095.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000000291}; KW Transferase {ECO:0000313|EMBL:AEJ41095.1}. SQ SEQUENCE 623 AA; 66617 MW; FD75FDFDF7DC4761 CRC64; MKPLAEALSH GLWLADGAIG TWFLSQGVEP HQLPLLPLDH PDLVIRCHLE YLQAGAQIIE THSFSANRSK LAAMGWDGSV GELNRRAAQL ARHARDIFGE PAYVLGSLGP LAVPVDSPIV PGLDRAEAET VYREAVAGLL AGGVDGFLVE TMSDLATVEA AVSAIRAESD LPIVVSFAFS PLGTTLYGIT PEAAVEAVMT LPGGPPAAIG ANCGSGPSPL LDAVIRMAEK ARTYQLPVVA YPNAGEPALR DGHVHYPASP DYMATIAPAL KAAGCAVIGG CCGTTPSHIR AIRQNMQGDL HPQLTARPGW SLTEDVVPKS PDPEWSRPPR LVHELLAQQF VLSVELDPPR GPNLTRLVDA ARQLEEEQVD VINVADSPMA RVRLGALATA RLIQERTRLA TILHFTTRDR NLMGLQSDLL GAFALGLTNI LCLTGDPPGL GDYAHATAVY DLDSIGLTKV LAGFNQGLDA LGQPLGSPTV FSIGVGVNPT ADPLEKEIER FRQKVAAGAH YAMSQPIYAP EQFYRFLDAL GGPLPIPLIL GIMPLVSYRQ ALYLHNEVPG ITIPPEVLSR FESVQDGVHV GIELALELIQ ALRAGIHGIY LVPSFNRVEP LVPLIREIRR LTR // ID F8IJ89_ALIAT Unreviewed; 641 AA. AC F8IJ89; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 25. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN Name=mmuM {ECO:0000313|EMBL:AEJ43409.1}; GN OrderedLocusNames=TC41_1476 {ECO:0000313|EMBL:AEJ43409.1}; OS Alicyclobacillus acidocaldarius (strain Tc-4-1) (Bacillus OS acidocaldarius). OC Bacteria; Firmicutes; Bacilli; Bacillales; Alicyclobacillaceae; OC Alicyclobacillus. OX NCBI_TaxID=1048834 {ECO:0000313|EMBL:AEJ43409.1, ECO:0000313|Proteomes:UP000000292}; RN [1] {ECO:0000313|Proteomes:UP000000292} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tc-4-1 {ECO:0000313|Proteomes:UP000000292}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; AEJ43409.1; -; Genomic_DNA. DR RefSeq; WP_014464280.1; NC_017167.1. DR RefSeq; YP_005517928.1; NC_017167.1. DR EnsemblBacteria; AEJ43409; AEJ43409; TC41_1476. DR KEGG; aad:TC41_1476; -. DR KO; K00547; -. DR BioCyc; AACI1048834:GL7E-1482-MONOMER; -. DR Proteomes; UP000000292; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000292}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:AEJ43409.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:AEJ43409.1}. SQ SEQUENCE 641 AA; 69450 MW; 042ACEC391BC4B2F CRC64; MSDAVWREWR RPPRDVEGSL GVFVIFDGAM STYLHQLGVP IGTPVEQLNL TSPDLVARVH RRYVESGCTV LQTNTFMGNR VALERHGLSV DVASLNRRGV EIARSAAHGE ASVYGTMGPA MGGYRYGALL QDDERDLLAH VYAEQAEALV SAGIDGLILE TFPDLEEALV AIAAVRPLLG DLPLVVNLSP EEIGVTRDGV PLAEAFRRIR AAGADVVGLN CRLGPYGILR SYEQAGLSAE GPYAAVPNAG ILQRSEADEI AYTGDTEDFS RLMLRIAQLG VRWLGGCCGT TPEYIRSLRD ALMRADRKPH GATVPADTRG PSGPSRVTLG AGGYHEGVSV VEIAREKKAI VVELDPPKHL SIARFLDGAE ALARAGADLI TMADNSLGSV RVSNMALASL LKQRGIEPLV HVTCRDRNLI GQQSHLMGLA VLGIRNVLLV TGDPSRYGEL PGATSVYDVS SMDLTKMVRR LNEGIGFSGQ PLKQPSRFVI GTAFNPHVHN FRKAVERLQR KVEAGADFVM TQPVFDPDLM AAIAEATRDL GVPVFVGIMP LTSARNAEFL HHQVPGIRLS EQALRRMQEA APEEAPAVGE AIARELVEVA IRLFPGLYLV TPFLRYEMTV RLTEYARRLE ATLVSRPHGH A // ID F8JWM9_STREN Unreviewed; 302 AA. AC F8JWM9; G8X3H6; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:AEW97027.1}; GN OrderedLocusNames=SCATT_46560 {ECO:0000313|EMBL:AEW97027.1}; 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 {ECO:0000313|EMBL:AEW97027.1, ECO:0000313|Proteomes:UP000007842}; RN [1] {ECO:0000313|Proteomes:UP000007842} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35852 / DSM 46488 / JCM 4925 / NBRC 14057 / NRRL 8057 RC {ECO:0000313|Proteomes:UP000007842}; 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. CC ----------------------------------------------------------------------- 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; AEW97027.1; -; Genomic_DNA. DR RefSeq; WP_014145368.1; NC_017586.1. DR RefSeq; YP_004914155.1; NC_016111.1. DR RefSeq; YP_006056549.1; NC_017586.1. DR EnsemblBacteria; AEW97027; AEW97027; SCATT_46560. DR EnsemblBacteria; CCB77352; CCB77352; SCAT_4664. DR KEGG; sct:SCAT_4664; -. DR KEGG; scy:SCATT_46560; -. DR KO; K00547; -. DR BioCyc; SCAT1003195:GJCM-4702-MONOMER; -. DR Proteomes; UP000007842; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007842}; KW Methyltransferase {ECO:0000313|EMBL:AEW97027.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007842}; KW Transferase {ECO:0000313|EMBL:AEW97027.1}. SQ SEQUENCE 302 AA; 31641 MW; 48A701A5ADCEAFB1 CRC64; MSSVPLGDAL MAGPVVLDGG LSNQLADQGC DLSDALWSAR LLADAPEQIE AAHAAYLRAG ARVLITSSYQ ATYEGFARRG LERRAAGELL RRSVRLARRA AGGRDDVWVA ASVGPYGAML ADGSEYRGRY GLSVAELTRF HRPRIETLAE AAPDVLALET VPDADEAEAL LRAVEGTGVP VWLSYTVAGD RTRAGQPLAD AFALAAGVPQ VIAVGVNCCS AEDAGPAVAL ARQVTGKPVV VYPNSGERWD AEARAWRGGA TFDPSRVEGW TAAGARLIGG CCRVGPRRIA ELASALRPAP RP // ID F8K2K8_STREN Unreviewed; 1167 AA. AC F8K2K8; G8WVJ5; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEW97519.1}; GN OrderedLocusNames=SCATT_51480 {ECO:0000313|EMBL:AEW97519.1}; 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 {ECO:0000313|EMBL:AEW97519.1, ECO:0000313|Proteomes:UP000007842}; RN [1] {ECO:0000313|Proteomes:UP000007842} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35852 / DSM 46488 / JCM 4925 / NBRC 14057 / NRRL 8057 RC {ECO:0000313|Proteomes:UP000007842}; 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. CC ----------------------------------------------------------------------- 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; AEW97519.1; -; Genomic_DNA. DR RefSeq; WP_014145858.1; NC_017586.1. DR RefSeq; YP_004914646.1; NC_016111.1. DR RefSeq; YP_006057041.1; NC_017586.1. DR EnsemblBacteria; AEW97519; AEW97519; SCATT_51480. DR EnsemblBacteria; CCB77843; CCB77843; SCAT_5155. DR KEGG; sct:SCAT_5155; -. DR KEGG; scy:SCATT_51480; -. DR KO; K00548; -. DR BioCyc; SCAT1003195:GJCM-5196-MONOMER; -. DR Proteomes; UP000007842; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007842}; KW Reference proteome {ECO:0000313|Proteomes:UP000007842}. SQ SEQUENCE 1167 AA; 127040 MW; 99FE4EAEAA327350 CRC64; MASPSQQTAQ QSRAAALREA LATRVVVADG AMGTMLQAQD PTLDDFQGYE GCNEVLNVTR PDIVRSVHEE YFQAGVDCVE TNTFGANLAA LGEYGIAERI HELAEAGARL AREVADSYAT AERPRWVLGS VGPGTKLPTL GHAPYTALRD AYRTEVAGLV AGGADAILVE TTQDLLQTKA ALIGARQALR ESGLDLPLIC SVTVETTGTM LLGSEIGAAL TALEPLGIDM IGLNCATGPA EMSEHLRYLA RHARIGVSAM PNAGLPVLGK DGAHYPLSPA ELADAQELFV DEYGLTLVGG CCGTTPEHLR QVVQRVRGRE VAPRDPRPEP GAASLYQSVP FRQDTSYLAI GERTNANGSK KFRTAMLEGR WDDCVEMARE QIREGAHLLD LCVDYVGRDG AADMREIAGR LATASTLPIV LDSTEPAVLQ AGLELLGGRA VVNSVNYEDG DGPESRFARI TSLAVEHGAA LMALTIDEEG QARTVERKVA VAERLIADLT GNWGIRECDI IIDCLTFTIC TGQEESRKDG ANTIEAIREL KRRHPEVQTT LGLSNISFGL NPAARMVLNS VFLHECVAAG LDSAIVHAAK IVPIARIPEE QREVALDLIH DRRREGYDPL QRFLEIFEGV DTKSVKAGRA EELAALPLEE RLRRRIIDGE RNGLEADLDE ALAGRPALDI VNDTLLEGMK VVGELFGSGQ MQLPFVLQSA EVMKTAVAYL EPHMEKTDDA GKGTIVLATV RGDVHDIGKN LVDIILSNNG YTVVNLGIKQ PVSAILEAAE EHRADVIGMS GLLVKSTVIM KENLEELNQR GLAARFPVIL GGAALTRAYV EQDLHEIYEG EVRYARDAFE GLRLMDALIA VKRGVPGATL PELKQRRVAR REAEVEEQAP TLGQVRSDVA TDNPVPVPPF WGTRVVKGVQ LKEYASWLDE GALFKGQWGL KQSRAGGPSY EELVESEGRP RLRGLLDRLQ TEGLLEAAVV YGYFPCVSKG DDLIVLGEDG AERTRFTFPR QRRGRRLCLA DFFRPQESGE TDVVGFQVVT VGSKVSEAAN ELFARDNYRD YLELHGLSVQ LAEALAEYWH ARVRAELGFG GEDPVDVEDM FALKYRGARF SLGYGACPDL EDRAKIAALL EPERIGVRLS EEFQLHPEQS TDAIVIHHPE AKYFNAR // ID F8KGM8_LACRE Unreviewed; 310 AA. AC F8KGM8; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 11. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:CCC04628.1}; GN ORFNames=LRATCC53608_1875 {ECO:0000313|EMBL:CCC04628.1}; OS Lactobacillus reuteri ATCC 53608. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=927703 {ECO:0000313|EMBL:CCC04628.1}; RN [1] {ECO:0000313|EMBL:CCC04628.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 53608 {ECO:0000313|EMBL:CCC04628.1}; 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] {ECO:0000313|EMBL:CCC04628.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 53608 {ECO:0000313|EMBL:CCC04628.1}; RA Davey R.; 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; FR854371; CCC04628.1; -; Genomic_DNA. DR RefSeq; WP_003676707.1; NZ_FR854371.1. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:CCC04628.1}; KW Transferase {ECO:0000313|EMBL:CCC04628.1}. SQ SEQUENCE 310 AA; 33628 MW; 75B69EAF7D0276F1 CRC64; MTKITAELTK PLLIDGAMST ALEQLGADTN NSLWTASVLA NQPALVKKVH QEYFKAGARL AITDTYQANV PAFIKNGYSK QEAHSLIQRA VALAKEARDE YQQETGIYNY VAGALGPYGA YLANGSEYTG DYHLSTVEYQ QFHRPRLTDI LTVGVDVIAI ETQPRLDEVL AELDLVKELA PDTLCYVSFS LKDSTRLPDG TPLAVAARTV AKYPNVFAVG VNCIPLEEVT AAIETVHQAT DKPVIAYPNS SAIYDPTTKT WSYPHGGRGL VDYLPQWLAA GLTIVGGCCT TTPQDIAALH EYLKGGAHHD // ID F8LKA4_STREH Unreviewed; 316 AA. AC F8LKA4; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=HMT-1 protein {ECO:0000313|EMBL:CCB93774.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:CCB93774.1}; GN Name=hMT-1 {ECO:0000313|EMBL:CCB93774.1}; GN OrderedLocusNames=SALIVB_1503 {ECO:0000313|EMBL:CCB93774.1}; OS Streptococcus salivarius (strain CCHSS3). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1048332 {ECO:0000313|EMBL:CCB93774.1, ECO:0000313|Proteomes:UP000000508}; RN [1] {ECO:0000313|Proteomes:UP000000508} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCHSS3 {ECO:0000313|Proteomes:UP000000508}; RX PubMed=21742894; DOI=10.1128/JB.05416-11; RA Delorme C., Guedon E., Pons N., Cruaud C., Couloux A., Loux V., RA Chiapello H., Poyart C., Gautier C., Sanchez N., Almeida M., RA Kennedy S.P., Ehrlich S.D., Gibrat J.F., Wincker P., Renault P.; RT "Complete genome sequence of the clinical Streptococcus salivarius RT strain CCHSS3."; RL J. Bacteriol. 193:5041-5042(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; FR873481; CCB93774.1; -; Genomic_DNA. DR RefSeq; WP_002885890.1; NC_015760.1. DR RefSeq; YP_004728298.1; NC_015760.1. DR EnsemblBacteria; CCB93774; CCB93774; SALIVB_1503. DR GeneID; 10972247; -. DR KEGG; ssr:SALIVB_1503; -. DR KO; K00547; -. DR BioCyc; SSAL1048332:GI6B-1481-MONOMER; -. DR Proteomes; UP000000508; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000508}; KW Methyltransferase {ECO:0000313|EMBL:CCB93774.1}; KW Transferase {ECO:0000313|EMBL:CCB93774.1}. SQ SEQUENCE 316 AA; 34854 MW; AEE493FE5A69C341 CRC64; MAIFKDYLEN KSPLILHGAL GTEMESLGYD ISGKLWSAKY LLDKPEVIQK IHETYVAAGS DLITTSSYQA TLPGLIDAGL TEKEAEQIIA LTVQLAKNAR DKVWATLDDS EKAKRPYPLI SGDVGPYAAY LANGSEYTGD YGRITIKELK EFHRPRIQIL LDQGVDLLAL ETIPNHLEAQ ALIELLAEEF PEAEAYISFT VQEPGTISDG TSLDEITQLV SQSDQILALG INCSSPLLYN QALTILKNAG KALITYPNSG EVYDGSTQTW KPKDKDALTL VEHSKDWHDQ FGVKILGGCC RTRPNDIKAL YAEFRT // ID F8LNK5_STRE8 Unreviewed; 316 AA. AC F8LNK5; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=HMT-1 protein {ECO:0000313|EMBL:CCB94925.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:CCB94925.1}; GN Name=hMT-1 {ECO:0000313|EMBL:CCB94925.1}; GN OrderedLocusNames=SALIVA_0595 {ECO:0000313|EMBL:CCB94925.1}; OS Streptococcus salivarius (strain JIM8777). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=347253 {ECO:0000313|EMBL:CCB94925.1, ECO:0000313|Proteomes:UP000000507}; RN [1] {ECO:0000313|EMBL:CCB94925.1, ECO:0000313|Proteomes:UP000000507} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JIM8777 {ECO:0000313|EMBL:CCB94925.1, RC ECO:0000313|Proteomes:UP000000507}; RX PubMed=21742871; DOI=10.1128/JB.05390-11; RA Guedon E., Delorme C., Pons N., Cruaud C., Loux V., Couloux A., RA Gautier C., Sanchez N., Layec S., Galleron N., Almeida M., RA van de Guchte M., Kennedy S.P., Ehrlich S.D., Gibrat J.F., Wincker P., RA Renault P.; RT "Complete genome sequence of the commensal Streptococcus salivarius RT strain JIM8777."; RL J. Bacteriol. 193:5024-5025(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; FR873482; CCB94925.1; -; Genomic_DNA. DR RefSeq; WP_014634110.1; NC_017595.1. DR RefSeq; YP_006069760.1; NC_017595.1. DR EnsemblBacteria; CCB94925; CCB94925; SALIVA_0595. DR KEGG; stj:SALIVA_0595; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR BioCyc; SSAL347253:GLLH-595-MONOMER; -. DR Proteomes; UP000000507; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000507}; KW Methyltransferase {ECO:0000313|EMBL:CCB94925.1}; KW Transferase {ECO:0000313|EMBL:CCB94925.1}. SQ SEQUENCE 316 AA; 34698 MW; 83ECDF65B3EFE685 CRC64; MAIFKDYLEN KSPLILHGAL GTEMESLGYD ISGKLWSAKY LLEKPEVIQK IHETYVAAGS DLITTSSYQA TLPGLIDAGL TEKEAEQIIA LTVQLAKAAR DKVWATLDDS EKAKRPYPLI SGDVGPYAAY LANGSEYTGD YGQITTEALK DFHRPRIQIL LDQGVDLLAL ETIPNHLEAQ ALIELLAEEF SEAEAYISFT VQEPGTISDR TSLDEIAQLV GQSDQILALG INCSSPLLYN QALTILKNAG KALITYPNSG EVYDGSTQTW KPKDKDALTL VEHSKDWHAQ FGVKILGGCC RTRPNDIKAL YAEFRT // ID F8LW48_STRTR Unreviewed; 316 AA. AC F8LW48; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=MmuM protein {ECO:0000313|EMBL:CCC19485.1}; GN Name=mmuM {ECO:0000313|EMBL:CCC19485.1}; GN ORFNames=STH8232_0768 {ECO:0000313|EMBL:CCC19485.1}; OS Streptococcus thermophilus JIM 8232. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1051074 {ECO:0000313|EMBL:CCC19485.1, ECO:0000313|Proteomes:UP000000300}; RN [1] {ECO:0000313|EMBL:CCC19485.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=JIM 8232 {ECO:0000313|EMBL:CCC19485.1}; RA Renault P., Loux V.; RT "Complete genome sequence of Streptococcus thermophilus strain RT JIM8232."; 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; FR875178; CCC19485.1; -; Genomic_DNA. DR RefSeq; WP_011680907.1; NC_017581.1. DR RefSeq; YP_006040440.1; NC_017581.1. DR ProteinModelPortal; F8LW48; -. DR EnsemblBacteria; CCC19485; CCC19485; STH8232_0768. DR KEGG; stu:STH8232_0768; -. DR KO; K00547; -. DR BioCyc; STHE1051074:GLLQ-734-MONOMER; -. DR Proteomes; UP000000300; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000300}. SQ SEQUENCE 316 AA; 34768 MW; 65A819AEB99CDBB2 CRC64; MATFKDYLEN NSLLILHGAL GTEMEALGYD ISGKLWSAKY LLEKSEVIQE LHETYVAAGA DLITTSSYQA TLPGLVEAGL TEKAAEQIIA LTVRLAKAAR DKVWGALDET EKAKRPYPLI SGDVGPYAAY LANGSEYSGD YGQITIKELK DFHRPRIQIL LDQGVDLLAL ETIPNRLETQ ALIELLAEEF PEAEAYMSFT VQIPDAISDG TSLAEMAKLV SQSNQILAVG INCSSPLLYN QALAFLKNAG KALITYPNSG EVYDGDSQTW KPKDKDALTL VEHSKYWHAH FGVKILGGCC RTRPNDIKAL YQEFRT // ID F8M234_MYCA0 Unreviewed; 302 AA. AC F8M234; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=MmuM protein {ECO:0000313|EMBL:CCC27545.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:CCC27545.1}; GN Name=mmuM {ECO:0000313|EMBL:CCC27545.1}; GN OrderedLocusNames=MAF_24750 {ECO:0000313|EMBL:CCC27545.1}; OS Mycobacterium africanum (strain GM041182). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=572418 {ECO:0000313|EMBL:CCC27545.1, ECO:0000313|Proteomes:UP000000298}; RN [1] {ECO:0000313|EMBL:CCC27545.1, ECO:0000313|Proteomes:UP000000298} RP NUCLEOTIDE SEQUENCE. RC STRAIN=GM041182 {ECO:0000313|EMBL:CCC27545.1, RC ECO:0000313|Proteomes:UP000000298}; 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 ----------------------------------------------------------------------- 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; CCC27545.1; -; Genomic_DNA. DR RefSeq; WP_003412639.1; NC_015758.1. DR RefSeq; YP_004724128.1; NC_015758.1. DR ProteinModelPortal; F8M234; -. DR EnsemblBacteria; CCC27545; CCC27545; MAF_24750. DR KEGG; maf:MAF_24750; -. DR KO; K00547; -. DR BioCyc; MAFR572418:GJCK-2489-MONOMER; -. DR Proteomes; UP000000298; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000298}; KW Methyltransferase {ECO:0000313|EMBL:CCC27545.1}; KW Transferase {ECO:0000313|EMBL:CCC27545.1}. SQ SEQUENCE 302 AA; 31533 MW; D8174BFD6FDE55BD CRC64; MELVSDSVLI SDGGLATELE ARGHDLSDPL WSARLLVDAP HAITAVHTAY FRAGAQIATT ASYQASFEGF AARGIGHDDA TVLLRRSVEL AQAARDEVGV GGLSVAASVG PYGAALADGS EYRGCYGLSV AALMKWHLPR LEVLVDAGAD MLALETIPDI DEAEALVNLV RRLATPAWLS YTINGTRTRA GQPLTDAFAV AAGVPEIVAV GVNCCAPDDV LPAIAFAVAH TGKPVIVYPN SGEGWDGRRR AWVGPRRFSG SSGQLAREWV AAGARIVGGC CRVRPIDIAE IGRALTTAPP RG // ID F8MZD2_NEUT8 Unreviewed; 361 AA. AC F8MZD2; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 01-APR-2015, entry version 18. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EGO52023.1}; GN ORFNames=NEUTE1DRAFT_89911 {ECO:0000313|EMBL:EGO52023.1}; 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 {ECO:0000313|Proteomes:UP000008065}; RN [1] {ECO:0000313|Proteomes:UP000008065} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FGSC 2508 / P0657 {ECO:0000313|Proteomes:UP000008065}; 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; GL891382; EGO52023.1; -; Genomic_DNA. DR RefSeq; XP_009855669.1; XM_009857367.1. DR GeneID; 20831269; -. DR KEGG; nte:NEUTE1DRAFT89911; -. DR KO; K00547; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000008065; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008065}. SQ SEQUENCE 361 AA; 39768 MW; 172785728C24F4D9 CRC64; MATPIPVQIL DGGMGTTLED MHDITFSFET PLWSSHLLVS GEEDKLSDCH EAFKQAGANI ISTATYQISI NGFAATKAPK SGTLDVEREG IDKEEIPRFL SRAVVLAANA AGTEGKVALS LGPYGATMIP STEYSGRYDP EHQDVQALEK WHKERLNLFK DVDPNHVNYI AFETVPRLDE IVAIRNLLSV DNIPTSLRGR PVWISTPYPN DDGKLPDGST VEEAVKAVLT HREGLETPWG IGINCTKVEK LDSLVKRYED AIQTCIKNGE RMAWPSLVLY PDGTKGEVYN TATKTWELSP GHKQTETPWE TVLAGVVEAA RQRGNWKSIV VGGCCKASPE HIRRLRRTLQ DYGHMSTSPA A // ID F8NCU9_9BACT Unreviewed; 920 AA. AC F8NCU9; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:EGN58134.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGN58134.1}; GN ORFNames=Premu_2788 {ECO:0000313|EMBL:EGN58134.1}; OS Prevotella multisaccharivorax DSM 17128. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=688246 {ECO:0000313|EMBL:EGN58134.1}; RN [1] {ECO:0000313|EMBL:EGN58134.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17128 {ECO:0000313|EMBL:EGN58134.1}; 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., Pagani I., 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., Gronow S., RA Wellnitz S., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The draft genome of Prevotella multisaccharivorax DSM 17128."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GL945017; EGN58134.1; -; Genomic_DNA. DR RefSeq; WP_007576155.1; NZ_GL945017.1. DR EnsemblBacteria; EGN58134; EGN58134; Premu_2788. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGN58134.1}; KW Transferase {ECO:0000313|EMBL:EGN58134.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 241 241 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 762 762 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 920 AA; 101504 MW; 35785577DCE78588 CRC64; MKRLQDIVKE KVLILDGALG TVIQGLGLTE ADFRGERFKD IEGQTKGNND MLNLTRPDVI LGIHRRYLQA GADIIETNTF SSQRISQADY HLEGSARDMA LAGARLARQA TDTFTTEAWP RFVAGSVGPT NKTLSLSADV TDPASRELTY DELWAAYSEQ IDGLVEGGVD AILIETIFDS LNAKCAIDAA LQVMRERGVE LPIMVSISVS DLAGRTLSGQ TLDAFLGSIS SYPIFSVGLN CSFGAREMRP FLEDLARKAS YYISAYPNAG MPNAMGQYDE TAESMSPLIR EWMEDRLVNI IGGCCGTDET FIHQYFLLSQ GMKPHKPQPK PTTLWLSGLE LLDINSDVRF VNVGERCNVA GSRKFLRLIK EKNYDEALSI ARKQVEDGAL VIDVNMDDAL LDARKEMVNF LNLIASEPDI SRVPVMIDSS KWEVVTAGLK CLQGKCIVNS ISLKEGEEVF LSHARDVMRF GSAVVVMCFD EQGQATTYER RIEIAERAYR LLTEKVGMNP LDIIFDPNIL SIATGIEEHD SYAVEFIRAT KWIRTHLKGA HVSGGVSNLS FSFRGNNYIR ESMHAVFLYY AIKAGMDFGI VNPSTRITYS DIPENDLKII EDAILNRYSG AAEKLTELAE HILAEKEAQK AANNGVSPKA SIADEWRTES LHDRLVYALR KGIGDYLQED LNEALNQFPH AVDIIEGPLM DGMNIVGKLF GDGKMFLPQV VKTARTMKQA VAILQPYIEA ERTGAASTAG CVVMATVKGD VHDIGKNIVG VVMGCNNYEV IDLGVMVPAD QIVKKAISEH ADVVGLSGLI TPSLDEMVNT VREMGKAGLR IPVLIGGATT SELHTALKIA PAYEGPVVWQ KDASQSAVIL AKLMNDKERQ PFLDTLYERY AKLRDGYHQE QVKLNSLDEA RKNRLNLFQN // ID F8NV22_SERL9 Unreviewed; 398 AA. AC F8NV22; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 07-JAN-2015, entry version 15. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EGO25977.1}; GN ORFNames=SERLADRAFT_466856 {ECO:0000313|EMBL:EGO25977.1}; 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 {ECO:0000313|Proteomes:UP000008064}; RN [1] {ECO:0000313|Proteomes:UP000008064} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S7.9 {ECO:0000313|Proteomes:UP000008064}; 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; EGO25977.1; -; Genomic_DNA. DR RefSeq; XP_007318099.1; XM_007318037.1. DR GeneID; 18819133; -. DR KEGG; sla:SERLADRAFT_466856; -. DR InParanoid; F8NV22; -. DR KO; K00547; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000008064; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 2. DR SUPFAM; SSF82282; SSF82282; 3. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008064}. SQ SEQUENCE 398 AA; 43539 MW; 99EFED4B5B436854 CRC64; MSFGSLYSDQ SVNVLDGGLG TTLEDIFHED IAHTPLWSAK SIDENSETLI QVHLSFLGAG ARTILTSTYQ CAFTTFERAG YSREDATRIM RKSVEVAREA KRRFCDQNRN VLPGDIRIAL SLGPFGATLY PAQEFDGFYP PPYGPKAFSS SGQNENVFGD DVAQRESSID ALAHFHSERL QVFTSDRECW DAVDCIAFET VPLAREVKAI RRAMGMLGGA VADNGEWKPW WISTVFPGGH YPERKTPGGE YLSASEVLNA VLGEENDGRI GEVVRQPLTL PSGIGINCTG IEFLPDLLSD FERALNNAEE KARLGGRPWL VLYPNGGDVY DPVSRTWRGS NETQKGRVWG EQLGQIVDSA RGNGTWGGIL VGGCCRTGPA EIRALVDALR LPSAELCP // ID F8PUA6_SERL3 Unreviewed; 398 AA. AC F8PUA6; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 07-JAN-2015, entry version 13. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EGO00419.1}; GN ORFNames=SERLA73DRAFT_181000 {ECO:0000313|EMBL:EGO00419.1}; 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 {ECO:0000313|Proteomes:UP000008063}; RN [1] {ECO:0000313|Proteomes:UP000008063} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=strain S7.3 {ECO:0000313|Proteomes:UP000008063}; 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; EGO00419.1; -; Genomic_DNA. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000008063; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 2. DR SUPFAM; SSF82282; SSF82282; 3. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008063}; KW Reference proteome {ECO:0000313|Proteomes:UP000008063}. SQ SEQUENCE 398 AA; 43539 MW; 99EFED4B5B436854 CRC64; MSFGSLYSDQ SVNVLDGGLG TTLEDIFHED IAHTPLWSAK SIDENSETLI QVHLSFLGAG ARTILTSTYQ CAFTTFERAG YSREDATRIM RKSVEVAREA KRRFCDQNRN VLPGDIRIAL SLGPFGATLY PAQEFDGFYP PPYGPKAFSS SGQNENVFGD DVAQRESSID ALAHFHSERL QVFTSDRECW DAVDCIAFET VPLAREVKAI RRAMGMLGGA VADNGEWKPW WISTVFPGGH YPERKTPGGE YLSASEVLNA VLGEENDGRI GEVVRQPLTL PSGIGINCTG IEFLPDLLSD FERALNNAEE KARLGGRPWL VLYPNGGDVY DPVSRTWRGS NETQKGRVWG EQLGQIVDSA RGNGTWGGIL VGGCCRTGPA EIRALVDALR LPSAELCP // ID F8QPI4_9FABA Unreviewed; 339 AA. AC F8QPI4; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 01-APR-2015, entry version 11. DE SubName: Full=Selenocysteine methyltransferase {ECO:0000313|EMBL:AEI53593.1}; GN Name=SMTA {ECO:0000313|EMBL:AEI53593.1}; OS Astragalus chrysochlorus. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; OC Galegeae; Astragalus. OX NCBI_TaxID=675724 {ECO:0000313|EMBL:AEI53593.1}; RN [1] {ECO:0000313|EMBL:AEI53593.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Stem {ECO:0000313|EMBL:AEI53593.1}; RA Ari S., Cakir O., Turgut-Kara N.; RT "Selenium tolerance in Astragalus chrysochlorus: identification of a RT cDNA fragment encoding a putative Selenocysteine methyltransferase."; RL Acta Physiol. Plant. 32:1085-1092(2010). RN [2] {ECO:0000313|EMBL:AEI53593.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Stem {ECO:0000313|EMBL:AEI53593.1}; RA Turgut-Kara N., Cakir O., Ari S.; 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; GQ844862; AEI53593.1; -; mRNA. DR BRENDA; 2.1.1.280; 13526. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Methyltransferase {ECO:0000313|EMBL:AEI53593.1}; KW Transferase {ECO:0000313|EMBL:AEI53593.1}. SQ SEQUENCE 339 AA; 36948 MW; ECBEA0E925414755 CRC64; MSSSLITDFL HQNGGTAVID GGLATELERH GADLNDPLWS AKCLLSSPHL IRQVHLDYLE NGADIIITAS YQATIQGFKA KGFSDEEGEA LLRRSVEIAR EARDLYYQRC AESSSDNNGD DSRILKQRPI LIAGSVGSYG AYLADGSEYS GNYGDAIKLE TLKDFHRRRV QILADSGADL LAFETIPNKL EAQAYADLLE EENITTPAWF TFNSKDGTNV VSGDSIEECG SIAESCNKVV AVGINCTPPR FIHDLILLLK KVTAKPIVIY PNSGETYDGI RKEWMQNSGV TDEDFVSYVD KWCESGASLV GGCCRTTPDT IRGIYKILSS GQSPALATK // ID F8U8P9_CHELB Unreviewed; 94 AA. AC F8U8P9; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 29-OCT-2014, entry version 13. DE SubName: Full=Betaine homocysteine methyltrasnferase {ECO:0000313|EMBL:AEI16517.1}; DE Flags: Fragment; OS Chelon labrosus (Thicklip grey mullet) (Mugil chelo). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Mugilomorphae; Mugilidae; Chelon. OX NCBI_TaxID=48171 {ECO:0000313|EMBL:AEI16517.1}; RN [1] {ECO:0000313|EMBL:AEI16517.1} RP NUCLEOTIDE SEQUENCE. RA Diaz De Cerio O., Bilbao E., Cajaraville M.P., Cancio I.; RT "Toxicology tailored low density oligonucleotide microarray for the RT thicklip grey mullet Chelon labrosus: development, production and RT validation."; 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; JF732771; AEI16517.1; -; mRNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; FT NON_TER 1 1 {ECO:0000313|EMBL:AEI16517.1}. FT NON_TER 94 94 {ECO:0000313|EMBL:AEI16517.1}. SQ SEQUENCE 94 AA; 10142 MW; CAD436F9D4438EB2 CRC64; VKAGPWTPEA AAEHPEAVRQ LHREFLRAGA NVMQTFTFYA SDDKLENRGN KLTFTGAQIN EAACDLAREV ANEGDALVAG GVCQTPSYLS CKSE // ID F8WYP8_9PORP Unreviewed; 1230 AA. AC F8WYP8; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGK03990.1}; GN ORFNames=HMPREF9456_01018 {ECO:0000313|EMBL:EGK03990.1}; OS Dysgonomonas mossii DSM 22836. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Dysgonomonas. OX NCBI_TaxID=742767 {ECO:0000313|EMBL:EGK03990.1}; RN [1] {ECO:0000313|EMBL:EGK03990.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 22836 {ECO:0000313|EMBL:EGK03990.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGK03990.1}. 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; ADLW01000004; EGK03990.1; -; Genomic_DNA. DR RefSeq; WP_006842389.1; NZ_GL892005.1. DR EnsemblBacteria; EGK03990; EGK03990; HMPREF9456_01018. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 243 243 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 756 756 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1230 AA; 137499 MW; 9C28CC8D4C587B05 CRC64; MQKIQDILKE RILILDGAMG SLIQQYKLKE EDFRGERFRD SAILQKGNND LLNLTRPDII EEIHRKYLDA GADIIETNTF NATAISLEDY NMSHLAKEIN REAAKIAKKA AIDYTNLNPD KPRFVAGSIG PTNKTASMSP KVENPIYRAV TFDDLSSAYK EQIEGLADGG VDLLLIETIF DTLNAKAALF AAEEVRKERN IELPIMISVT LSDKAGRTLS GQTIGGFLAS VNHIDYLSVG LNCSFGASDM KPFLKELARM APSFISAYPN AGLPNQFGEY DQTPDIMAEQ ISEFIGEGLV NIIGGCCGTT PEHIAKYVDL VKDAKPHKPA EKPKYMWLSG LELLEAKPEI NFINIGERLN VAGSRKFLRL IKEEKYEEAL TIAHKQVEDG AQVLDVNMDE GLLDGVKEMT TFLNMMASDP DVSRIPVMID SSKWEVLEAG LKCVQGKAIV NSISLKGGEE EFLRHARLVR QYGAAVIIMA FDETGQADTF SRRIEICERA YKLLVNDGFD PLDIIFDPNI LAIATGIEEH RNYAVDFLET ITWIKKNLPH AKISGGVSNL SFSFRGNDYV REAMHAVFLY YAIQRGMDMG IVNPGQSVVY DDIPLELKDL VEDVIFNRRP EATDELIEYA ERIKNEKNGQ TEQKVEEWRS FPLDERIQYS LIKGISDHLE EDLEEALKVY PKAVDIIDKP LMDGMNKVGD LFGSGKMFLP QVVKTARTMK RAVAILQPTL EAQKSSSAGS NKAGKLVIAT VKGDVHDIGK NIVAIILACN NYEVIDLGVM TPPEVIIQKV KEEQPDILCL SGLITPSLEE MSIVAHEMEK AGFSIPLMIG GATTSKLHTA IKIDPKYNNG SVVYVKDASQ APAAVSKLIN PNTKENYINE VKQEYSQLRD NAGDKKADLL PLSEVLDKGM PIDWSEYKTP EPKVKGRQVL KKILVDEIVP YVDWKFFFHS WNLSARYASV QHIDDCSSCR TSWLNSFPEH EREKASEGMQ LYKDAKALLD QLIFDKVGYI NAVFGVFEAY SENECLYIDD VCFPMLRQQK KNDRGEYLSL CDFVAPKSSG KKDYVGGFTV TAGVGSNELM SEFEQQGDEY KVLLLKSVLD RLAEATTEWL HAKIRREYWG FAADENISVN DMFTLKYQGI RPAVGYPSIP DQSINFLLNN DLLQSKEIGV ELTENGVMLP NASVSGIIIS HPKSKYFNIG NILDDQMESY VERRGEEAEV IRKFLSANLI // ID F8X8K2_ECOLX Unreviewed; 1227 AA. AC F8X8K2; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGU98843.1}; GN ORFNames=HMPREF9349_01073 {ECO:0000313|EMBL:EGU98843.1}; OS Escherichia coli MS 79-10. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=796392 {ECO:0000313|EMBL:EGU98843.1}; RN [1] {ECO:0000313|EMBL:EGU98843.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS 79-10 {ECO:0000313|EMBL:EGU98843.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGU98843.1}. 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; ADWR01000007; EGU98843.1; -; Genomic_DNA. DR RefSeq; WP_000096053.1; NZ_ADWR01000007.1. DR EnsemblBacteria; EGU98843; EGU98843; HMPREF9349_01073. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136040 MW; D1A76336C7330E3D CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID F8Y1F4_STRAG Unreviewed; 314 AA. AC F8Y1F4; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:EGS27853.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EGS27853.1}; GN Name=mmuM {ECO:0000313|EMBL:EGS27853.1}; GN ORFNames=FSLSAGS3026_07585 {ECO:0000313|EMBL:EGS27853.1}; OS Streptococcus agalactiae FSL S3-026. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=876138 {ECO:0000313|EMBL:EGS27853.1}; RN [1] {ECO:0000313|EMBL:EGS27853.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FSL S3-026 {ECO:0000313|EMBL:EGS27853.1}; 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] {ECO:0000313|EMBL:EGS27853.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FSL S3-026 {ECO:0000313|EMBL:EGS27853.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGS27853.1}. 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; AEXT01000007; EGS27853.1; -; Genomic_DNA. DR RefSeq; WP_000532327.1; NZ_ANCL01000025.1. DR EnsemblBacteria; EGS27853; EGS27853; FSLSAGS3026_07585. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGS27853.1}; KW Transferase {ECO:0000313|EMBL:EGS27853.1}. SQ SEQUENCE 314 AA; 33925 MW; 5ECEF31ACC194FD5 CRC64; MGRFKELLES KKALILHGAL GTELESRGCD VSGKLWSAKY LIEDPAAIQT IHEGYIRAGA DIVTTSTYQA TLQGLAQVGV SESQAEDLIR LTVQLAKAAR EQVWKSLTKE EKSERIYPLI SGDVGPYAAF LADGSEYTGL YDIDKEGLKN FHRHRIELLL DEGVDLLALE TIPSAQEAEA LIELLAEDFP QVEAYMSFTS QDGKTISDGS AVADLAKAID VSPQVVALGI NCSSPSLVAD FLQAIAEQTN KPLVTYPNSG EVYDGASQSW QSSPDHSHTL LENTSDWQKL GAQVVGGCCR TRPADIADLS AHLT // ID F8Y3N1_STRAG Unreviewed; 614 AA. AC F8Y3N1; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 20. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=FSLSAGS3026_11685 {ECO:0000313|EMBL:EGS27028.1}; OS Streptococcus agalactiae FSL S3-026. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=876138 {ECO:0000313|EMBL:EGS27028.1}; RN [1] {ECO:0000313|EMBL:EGS27028.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FSL S3-026 {ECO:0000313|EMBL:EGS27028.1}; 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] {ECO:0000313|EMBL:EGS27028.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FSL S3-026 {ECO:0000313|EMBL:EGS27028.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGS27028.1}. 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; AEXT01000008; EGS27028.1; -; Genomic_DNA. DR RefSeq; WP_000032994.1; NZ_ANCL01000099.1. DR ProteinModelPortal; F8Y3N1; -. DR EnsemblBacteria; EGS27028; EGS27028; FSLSAGS3026_11685. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EGS27028.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EGS27028.1}. SQ SEQUENCE 614 AA; 68034 MW; 960409F963928115 CRC64; MSKFLEKLKT DILVADGAMG TLLYTYGLDT CHESYNVTHP EKVLAIHQAY IEAGADVIQT NTYGAQRHRL KNYGLEDQVV SINQAAVNLA HQATLGKETF ILGTVGGFRS QRQCDLTLDN IVEETLEQVE ALLATGQLDG LLFETYYDIE EITTVLKIVR EMTDLPIITN ISLHEAGVTS NGKPIVEALS QLVMLGADVI GLNCHLGPYH MIQSLKQVPL FAQSYLSVYP NASQLSLDGE NSQYQFSQNS EYFGKSAELL VAEGVRLIGG CCGTTPDHIR AVKRSIRGLK PIERKVVTPI IPVKDFVRRI RRTDTLVDKV KKEVTIIAEL DPPKHLDIVQ FQKAIRAIDQ KGIAAITLAD NSLSNTRICN LSIASLLKDE ISTPFLLHIA CRDHNLIGLQ SRLLGMELLG FNHILAITGD PTKLGDFPGA TSVYDVTSFK LLSLIKQLNQ GLSYSGASLR RPTDFTVAAA FNPNVKNLTR TVKLIEKKVA SGADYFMTQP IFDHSVLKEL ADLTKTVEQP FFIGIMPITS YNNAVFLHNE VPGIKLSESF LSALEKVKDD KEACLTLALN ESKSLIDEAL NYFNGIYLIT PFLRYDLTLE LIDYIQKKQV RKSS // ID F9CZ33_9ARCH Unreviewed; 320 AA. AC F9CZ33; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGP94191.1}; GN ORFNames=MY1_1435 {ECO:0000313|EMBL:EGP94191.1}; OS Candidatus Nitrosoarchaeum koreensis MY1. OC Archaea; Thaumarchaeota; Nitrosopumilales; Nitrosopumilaceae; OC Candidatus Nitrosoarchaeum. OX NCBI_TaxID=1001994 {ECO:0000313|EMBL:EGP94191.1}; RN [1] {ECO:0000313|EMBL:EGP94191.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MY1 {ECO:0000313|EMBL:EGP94191.1}; RX PubMed=21914867; DOI=10.1128/JB.05717-11; RA Kim B.K., Jung M.Y., Yu D.S., Park S.J., Oh T.K., Rhee S.K., Kim J.F.; RT "Genome Sequence of an Ammonia-Oxidizing Soil Archaeon, "Candidatus RT Nitrosoarchaeum koreensis" MY1."; RL J. Bacteriol. 193:5539-5540(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. {ECO:0000313|EMBL:EGP94191.1}. 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; AFPU01000001; EGP94191.1; -; Genomic_DNA. DR RefSeq; WP_007551121.1; NZ_AFPU01000001.1. DR EnsemblBacteria; EGP94191; EGP94191; MY1_1435. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGP94191.1}; KW Transferase {ECO:0000313|EMBL:EGP94191.1}. SQ SEQUENCE 320 AA; 35206 MW; 20DBED3B032931A6 CRC64; MVQKEPFLTA LQNRILLFDG AMGTEIQKYN PKPEDFPNNQ DGFNDGLVIT HPDWIKKIHK NYLDAGSDCI ETNSFGSNKI KLDEYGFGDQ TIEFNKKIAQ LAVEVCSEYT DKPRYVIGSM GPSGYLPSSN DPDLGQKPLG EIRNAFELQA EGLILGGVDA LLIETSQDIL EVKLVIEACH NAMKKTGKKV PIIANTTLDQ YGKMLLGTNI QAAYTTVSDM GIDVFGLNCS TGPAEMTPSV RWLDEQNEHN LLVVPNAGMP ENQGGQAVYK MTPQKMGELL GDFLKQYKKV RIIGGCCGTN PEHIAVLRKV IDEKAYSVKG // ID F9D186_PREDD Unreviewed; 922 AA. AC F9D186; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AGB28108.1}; DE SubName: Full=Exopolyphosphatase {ECO:0000313|EMBL:EGQ16387.1}; DE EC=3.6.1.11 {ECO:0000313|EMBL:EGQ16387.1}; GN Name=ppx {ECO:0000313|EMBL:EGQ16387.1}; GN OrderedLocusNames=Prede_0762 {ECO:0000313|EMBL:AGB28108.1}; GN ORFNames=HMPREF9136_0614 {ECO:0000313|EMBL:EGQ16387.1}; OS Prevotella dentalis (strain ATCC 49559 / DSM 3688 / JCM 13448 / NCTC OS 12043 / ES 2772) (Mitsuokella dentalis). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=908937 {ECO:0000313|EMBL:EGQ16387.1}; RN [1] {ECO:0000313|EMBL:EGQ16387.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 3688 {ECO:0000313|EMBL:EGQ16387.1}; 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. RN [2] {ECO:0000313|Proteomes:UP000010862} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49559 / DSM 3688 / JCM 13448 / NCTC 12043 / ES 2772 RC {ECO:0000313|Proteomes:UP000010862}; 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 Chertkov O., 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., Gronow S., Wellnitz S., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "Complete sequence of chromosome 1 of Prevotella dentalis DSM 3688."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:AGB28108.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 3688 {ECO:0000313|EMBL:AGB28108.1}; 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., Peters L., Mikhailova N., RA Chertkov O., 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., Gronow S., Wellnitz S., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "Complete sequence of chromosome 1 of Prevotella dentalis DSM 3688."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP003368; AGB28108.1; -; Genomic_DNA. DR EMBL; AFPW01000007; EGQ16387.1; -; Genomic_DNA. DR RefSeq; WP_005844267.1; NZ_GL982488.1. DR RefSeq; YP_007278138.1; NC_019960.1. DR EnsemblBacteria; AGB28108; AGB28108; Prede_0762. DR EnsemblBacteria; EGQ16387; EGQ16387; HMPREF9136_0614. DR KEGG; pdt:Prede_0762; -. DR KO; K00548; -. DR OrthoDB; EOG6091CH; -. DR Proteomes; UP000007820; Unassembled WGS sequence. DR Proteomes; UP000010862; Chromosome 1. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0004309; F:exopolyphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000010862}; KW Hydrolase {ECO:0000313|EMBL:EGQ16387.1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AGB28108.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000010862}; KW Transferase {ECO:0000313|EMBL:AGB28108.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 243 243 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 766 766 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 922 AA; 101162 MW; A19D5CC70FE87930 CRC64; MNSGLLDSIA REKILILDGA MGTMIQDCRL TEADFRRRLF RDVPGQMKGN NDVLNLTRPD IISDIHRKYL EAGADIIETN TFSSQRISQA DYHLEAHSRE IARQGAVLAK EAARRFSTDA WPRFVAGSIG PTNKTCSLSP DVSSPAARAM TYDELLAAYV EQAEALIDGG VDLFLIETIF DTLNAKCAID ACNQAMASRG AALPIMLSVT VSDLAGRTLS GQTLEAFLAS VSCYDIFSVG LNCSFGARQM KPYLKQLAQK APYYISAYPN AGLPNSMGEY DETVESMSPQ IAEFVDEGLV NILGGCCGTT DAFIRSYYQL SQGKRPHVPQ PKPRTLWLSG LELLDVTPEV NFVNVGERCN VAGSRKFLRL IKEKKYDEAL DIARRQVEDG ALVIDVNMDD GLLDAEAEMV TFLNLIASEP DIARVPVMID SSKWDVVLAG LKCVQGKCIV NSISLKEGEE TFLAHARDVK RFGAAVVVMC FDEQGQAATY ERRIEIAERA YRLLTEKAGF NPLDIIFDPN VLAIATGMEE HDDYAVNFIR ATHWIKANLP GAHVSGGVSN LSFSFRGNNY IREAMHAVFL YHAIREGMDF GIVNPATKVT YSDIPADHLQ IIEDVVLNRR KNAAEDLIEL AEHIKAEQLA LQEASQGNGA ATPLPTVEAW RQDDLHARLV YALRKGIATH LDEDLHEALE QYPHAVDIIE GPLMDGMNKV GELFGSGKMF LPQVVKTART MKQAVAILQP YIEAEKAGSA ASAGRIILAT VKGDVHDIGK NIVSVVLACN NFEMVDMGVM VPPGHIVKKA IETQADIVGL SGLITPSLDE MVNTAVEMKR AGLTIPILIG GATTSQLHVA LKIAPHYDGP VVWTKDAAQC VLASARLLNP TERPKFEQEL ADKYEVLRTQ YAQEQQHILS LEEARKNKLQ LF // ID F9DUC6_9BACL Unreviewed; 620 AA. AC F9DUC6; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 17. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HMPREF9372_2407 {ECO:0000313|EMBL:EGQ24724.1}; OS Sporosarcina newyorkensis 2681. OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; OC Sporosarcina. OX NCBI_TaxID=1027292 {ECO:0000313|EMBL:EGQ24724.1}; RN [1] {ECO:0000313|EMBL:EGQ24724.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=2681 {ECO:0000313|EMBL:EGQ24724.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGQ24724.1}. 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; AFPZ01000071; EGQ24724.1; -; Genomic_DNA. DR RefSeq; WP_009499091.1; NZ_GL982999.1. DR EnsemblBacteria; EGQ24724; EGQ24724; HMPREF9372_2407. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EGQ24724.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EGQ24724.1}. SQ SEQUENCE 620 AA; 68405 MW; 35CFCA0E1EC7D886 CRC64; MMSLLEKLQT NVLTADGAMG TILYSYGIDY CYEELNIEKP EIIEKIHHDY IEAGADIIQT NTYSANAVKL ARYGLENRVT EFNKAAIQIA KRAAAPGGQF VLGTIGGLRG IRKSDASLDE VRQVVLEQAN ALLTGDPDGL LLETYYDFEE LSSVVSTLRQ ITDVPLIAQV SMHDPGVLQN GLSLNDALHQ LESLGASIVG VNCRLGPYHT IQAFENVKLP ENAFLSAYPN ASLLDVEDGR IVYESEAEYF GRAAVLLRDQ GVRLIGGCCG TTPKHIKAAK TRLAGLSPIT KKVVEPTKPI VIQEAGPVKH QPLHEKAKTE RTVIVELDTP RHLETEDYIK GANLLYDAGV DAVTMADNSL ASPRISNMAM GSIIKMQHNI RPLVHLTCRD HNLIGLQSHL MGLDALGIHD ILAVTGDPTK VGDFPGATSV YDVSSMELLQ LIKQLNEGIS FSGKPLRKKT NFSVSAAFNP NVRVLDRAVQ RLEKKIEAGA DYFITQPVYT KEKIIDVYEA TKHLDTPIFI GIMPLTNIRN AEFLHHEVPG IKLSDEVLER MRACGDDRAK ATETGIQIAK ELIDTAAQYF NGLYLITPFL RYDMTLELHD YIKQIDKQKE SELSHAETSY // ID F9DUC7_9BACL Unreviewed; 1146 AA. AC F9DUC7; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|EMBL:EGQ24725.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGQ24725.1}; GN Name=metH {ECO:0000313|EMBL:EGQ24725.1}; GN ORFNames=HMPREF9372_2408 {ECO:0000313|EMBL:EGQ24725.1}; OS Sporosarcina newyorkensis 2681. OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; OC Sporosarcina. OX NCBI_TaxID=1027292 {ECO:0000313|EMBL:EGQ24725.1}; RN [1] {ECO:0000313|EMBL:EGQ24725.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=2681 {ECO:0000313|EMBL:EGQ24725.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGQ24725.1}. 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; AFPZ01000071; EGQ24725.1; -; Genomic_DNA. DR RefSeq; WP_009499092.1; NZ_GL982999.1. DR EnsemblBacteria; EGQ24725; EGQ24725; HMPREF9372_2408. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGQ24725.1}; KW Transferase {ECO:0000313|EMBL:EGQ24725.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 725 725 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1146 AA; 126782 MW; 802D7AA54CEE934D CRC64; MQRHPIEEQL DKRILIIDGA MGTMLQAEDL STEDFGGEDY DGCNEYLNVL RPDILEKIHD EYLEAGADII CTNTFGGTPL VLNEFALGHR AHEINTKAVE IAKASAAKYS TAEWPRFVAG AIGPTTKTLS ITGGITFDEL SNDFYVQAKA LVEAGSDLIL METSQDMLNV KAGTIGIKKA FEELGREVPI MISGTIEPMG TTLAGQSIEA FYISIGHVNP LSVGLNCATG PEFMTDHLRS LSDLATSYVT CYPNAGLPDE EGHYHESPES LSKKLEGFAE KGWLNMVGGC CGTTPEHIRA IREAVKDKAP RQMPEKELGH AVSGIEPLLY DDTLRPLLIG ERTNVIGSRK FKKLIIEEKF EEASEIARAQ VKRGAHVLDI CLANPDRDEL IDMTRFMKEV VKKVKVPLVI DSTDENVIAE ALKYSQGKAI INSINLEDGE ERFDAVLPLV KKYGAAVVVG TIDEIGMAVT RERKLEIALR SYDLLVNKWG IAPEDIIFDP LVFPVGTGDE QYIGSAVETI EGIRLIKEKL PRTLTTLGVS NVSFGLPPVG REVLNAVYLY HCTQAGLDYA IVNTEKLERY ASIPEAEIKL ANDLLFTTTD ETLADFADFY RDKKKEKTED DIPKTVPERL AYYVVEGTKE GLIPDLEAAL QTYDAPLDII NGPLMEGMAE VGRLFNDNQL IVAEVLQSAE VMKASVSYLE QFMEKKEDDS GKGKIILATV KGDVHDIGKN LVDIILSNNG FKVIDIGIKV TPAALIEVIR KEKPDIVGLS GLLVKSAQQM VLTAQDFKAA GIDLPVMVGG AALTRRFTET KIAPEYDGPV IFAKDAMQGL DLANRLQSKD KGALLEELQE SLEKREANDA IKASRGNTAV AVAARPVKTV RTDVPVFVPT DLRRRVIKDY SVAHLHPYVN MRTLIGHHLG LRGNVDKMLE KKEERAVQLH EMVTGFLQSD KLTASGIYQF FPAQADGDDV IIYDPEDATT EIERFTFPRQ EKEPFLCLAD YLKTVDSGEM DYVAFMQVTA GKGVRDYANQ LKEQGKFLES HAFQATALEL AEGFAERIHQ EIRDQWGFPD PTDFTMRERF AAKYQGQRFS FGYPACPNLE DQAKLFGLIK PEDHGVILTE EFMMEPEASV SAIVFAHPDA RYFNVE // ID F9E0P4_STRSA Unreviewed; 315 AA. AC F9E0P4; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 11. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGQ20699.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EGQ20699.1}; GN Name=mmuM {ECO:0000313|EMBL:EGQ20699.1}; GN ORFNames=HMPREF8573_0770 {ECO:0000313|EMBL:EGQ20699.1}; OS Streptococcus sanguinis ATCC 29667. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=997356 {ECO:0000313|EMBL:EGQ20699.1, ECO:0000313|Proteomes:UP000006220}; RN [1] {ECO:0000313|EMBL:EGQ20699.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29667 {ECO:0000313|EMBL:EGQ20699.1}; 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. {ECO:0000313|EMBL:EGQ20699.1}. 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; AFQA01000012; EGQ20699.1; -; Genomic_DNA. DR RefSeq; WP_002924831.1; NZ_GL982553.1. DR EnsemblBacteria; EGQ20699; EGQ20699; HMPREF8573_0770. DR Proteomes; UP000006220; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006220}; KW Methyltransferase {ECO:0000313|EMBL:EGQ20699.1}; KW Transferase {ECO:0000313|EMBL:EGQ20699.1}. SQ SEQUENCE 315 AA; 34537 MW; A715B902FD4AF432 CRC64; MGKFKDLLDK QEIIILDGAL GTELESLGYD VSGKLWSAQY LLDQPQIIQD VHESYVRAGI DIITTSSYQA SIPAFIEAGL TPEKACDLLK ETVFLAQKAI ENVWTGLSPE EQKQRPCPLV AGSVGPYAAY LADGSEYTGN YQLSEEEYRD FHRPRIQALL EAGSDLLAIE TIPNGAEAAA LLRLLAEEFP QAEAYLSFVA QSETAISDGT KIEELGNLAQ KSPQVLAVGF NCTAPHLIAP LLDGLGQVCN KPFLTYPNSG ETYNGLTKTW HDNPEQERSL LENSKLWKEQ GVRLFGGCCR TRPEDIAQLA KGLKD // ID F9EHT8_9ACTO Unreviewed; 325 AA. AC F9EHT8; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 11. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGQ73459.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EGQ73459.1}; GN Name=mmuM {ECO:0000313|EMBL:EGQ73459.1}; GN ORFNames=HMPREF9062_2010 {ECO:0000313|EMBL:EGQ73459.1}; OS Actinomyces sp. oral taxon 448 str. F0400. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Actinomycineae; Actinomycetaceae; Actinomyces. OX NCBI_TaxID=888056 {ECO:0000313|EMBL:EGQ73459.1}; RN [1] {ECO:0000313|EMBL:EGQ73459.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0400 {ECO:0000313|EMBL:EGQ73459.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGQ73459.1}. 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; AFQC01000051; EGQ73459.1; -; Genomic_DNA. DR RefSeq; WP_009749908.1; NZ_GL985606.1. DR EnsemblBacteria; EGQ73459; EGQ73459; HMPREF9062_2010. DR OrthoDB; EOG6C019S; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGQ73459.1}; KW Transferase {ECO:0000313|EMBL:EGQ73459.1}. SQ SEQUENCE 325 AA; 34472 MW; 89B8DAE33E33B1D9 CRC64; MRSPPAPDGR RPRILLSDLM AAGPVVLDGA MGTELGARGV DTTSGLWSAL ALTEAPEAIA AVHADYLTAG ARVICTNSYQ AVVPALLRAG RTEDEARAVI AASARLALGA RDRYTAVQPR EAVLVAGSIG PYGAWLADGS EYTGAYGMRA PDFARVHLPR LEVLAAEGLR LFAIETQPRL DEARWLTERI GERLPDAECW VSFQVRPDGA HLADGTPLAR AAAWAQRARN VVAVGLNCVA PPVVDRALPV LRAAADKPLV AYPNSGDVYD PVTRTWRATV GRGRLTASTS AWLDAGVRLI GGCCRTTPAD TAELRDAVRS TARPR // ID F9EP11_FUSNU Unreviewed; 1081 AA. AC F9EP11; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 01-APR-2015, entry version 17. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGQ79307.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGQ79307.1}; GN Name=metH {ECO:0000313|EMBL:EGQ79307.1}; GN ORFNames=HMPREF9094_1666 {ECO:0000313|EMBL:EGQ79307.1}; OS Fusobacterium nucleatum subsp. animalis ATCC 51191. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=997347 {ECO:0000313|EMBL:EGQ79307.1}; RN [1] {ECO:0000313|EMBL:EGQ79307.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 51191 {ECO:0000313|EMBL:EGQ79307.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGQ79307.1}. 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; AFQD01000280; EGQ79307.1; -; Genomic_DNA. DR EnsemblBacteria; EGQ79307; EGQ79307; HMPREF9094_1666. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGQ79307.1}; KW Transferase {ECO:0000313|EMBL:EGQ79307.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 723 723 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1081 AA; 120826 MW; 5B904191F172E005 CRC64; MFEIEKDLKE RILVLDGAMG TVLQKYELSA EDFNGAKGCY EILNESRPDI IFEVHKKYIE AGADIIETNS FNCNAISLKD YHLEDKVYDL AKKSAEIARD AVKESGKKVY IFGSVGPTNK SLSFPVGDIP FKRAVSFDEM KEVIKVQVAG LIDGGVDGIL LETIFDGLTA KAALLATEEV FEEKNVKLPI SISATVNKQG KLLTGQSMES LIVALDRDSV TSFGFNCSFG AKDLVPLVLK IKELTTKFVT LHANAGLPNQ NGDYVETAQK MKNDLLPLIE NQAINILGGC CGTSYDHIKA IAELVKGQKP RVLPEKNLLE TCLSGNEIYN FKDKFTCVGE RNNISGSKLF RTMIEEHNYL KALDVARQQI DAGAKVLDIN VDDAILDSVE EMKNFLRVLQ NDSFIAKVPI MIDSSDFAVI EEGLKNTAGK AIVNSISLKE GEENFLRKAK IIRKYGASII VMAFDENGQG VSAERKIEIC QRAYNLLKSI GIKNSDIVFD PNILSVGTGQ EADRYHAREF LKTIDYIHKN LKGCGTVGGL SNLSFAFRGN NILRAAFHHI FLEEAIPRGF NFAILNPKEK APQWTDEERE KIKSFIFGDS TNIEDLLSLN LVKRKEDTQI FAETPEDRIR KALIQGGSES LQEVIEELLK KYKALEILEN ILMSAMQEIG RLFEQGELYL PQLIRSASVM NNCVNILTPY LEKVDRTSSK GKILMATVDG DVHDIGKNIV KTVLECNGYE VIDLGVMVPR EKIVEVAKKN NVDIVTLSGL ISPSLKEMER VADSFQKVGM QIPILIAGAA TSKLHTGLKV LPNYDYSLHV TDAMDTITVV SQLLSTKRKD FLEAKQNQLR KIAKRYIENN NQTGEKKVLP EVKKTVSYIP KVLGKQFLSL PVKILKDDLK WDIAFYALRV KNTPEEEKTL NDLKKIYEKL IEEKVEFRAA YGYFRCKKTE TFLEMEGMTF EVSPNIARYI EKEDYLGAFV VSVKSEIFKD DKYLGLLETL LCNVIAEAAS EYMERRVSKD IVPTFLRPAV GYPILPDHSL KKVVFDLIDG EKTGAKLSPA FAMSPLSSVC GFYLCNDNAK Y // ID F9GC68_FUSOF Unreviewed; 342 AA. AC F9GC68; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 07-JAN-2015, entry version 19. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGU73226.1}; GN ORFNames=FOXB_16251 {ECO:0000313|EMBL:EGU73226.1}; 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 {ECO:0000313|EMBL:EGU73226.1, ECO:0000313|Proteomes:UP000002489}; RN [1] {ECO:0000313|EMBL:EGU73226.1, ECO:0000313|Proteomes:UP000002489} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU73226.1, RC ECO:0000313|Proteomes:UP000002489}; RX PubMed=21942452; DOI=10.1094/MPMI-08-11-0212; RA Thatcher L.F., Gardiner D.M., Kazan K., Manners J.M.; 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. {ECO:0000313|EMBL:EGU73226.1}. 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; AFQF01004887; EGU73226.1; -; Genomic_DNA. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000002489; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002489}; KW Reference proteome {ECO:0000313|Proteomes:UP000002489}. SQ SEQUENCE 342 AA; 37569 MW; EE0D9B7F5DADED1D CRC64; MSSKILILDG GLGTSLESKY SITFSRSTPL WSSHLLVSDQ STLQSCQSDF GAVPVDVLLT ATYQVSLHGF ADTRTDDFPE GIPRETVPRF LDDAVSIAQR AVGDKGCVAL SIGPYGACMI PGQEYSGKYD AEHDSLADLE AWHRERLGVF AEVSDIQKRV GYVALETIPR VDEIIAMRKA LAATPTLSDL PYWTACLSPE KDLKMPDGNS IEAAVEAMLD PEVSTKLPWG IGINCTKVDK LDQLLQIFER TVAGMVEKGK ITEWPALVLY PDGTNGEVYN TTTQKWEMPD GVETHRRSSW EHQLETVVKA TEDRGNWPAI LVGGCCRAGS EDIKKLRDCL VK // ID F9GKQ6_HAEHA Unreviewed; 1229 AA. AC F9GKQ6; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Homocysteine-N5-methyltetrahydrofolate transmethylase, B12-dependent {ECO:0000313|EMBL:EGT75766.1}; GN ORFNames=GG7_1413 {ECO:0000313|EMBL:EGT75766.1}; OS Haemophilus haemolyticus M19107. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=1028802 {ECO:0000313|EMBL:EGT75766.1}; RN [1] {ECO:0000313|EMBL:EGT75766.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M19107 {ECO:0000313|EMBL:EGT75766.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGT75766.1}. 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; AFQN01000090; EGT75766.1; -; Genomic_DNA. DR RefSeq; WP_005628990.1; NZ_AFQN01000090.1. DR EnsemblBacteria; EGT75766; EGT75766; GG7_1413. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGT75766.1}; KW Transferase {ECO:0000313|EMBL:EGT75766.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 757 757 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1229 AA; 136170 MW; 64E0B6E126CB4C60 CRC64; MVNKTAQLKQ ALENRILILD GAMGTMIQKY KLTETDFRGE KFKESAVDLR GNNDLLTLTQ PLLISAIHEK YLAAGADIIE TNTFSSTTIA QADYDLQSIA YELNFAGAKL ARLAADKYGT PEKPRFVAGV LGPTNRTASI SPDVNDPGFR NVTFMELVDA YAEATKGLIE GGADLIMIET IFDTLNAKAA IFAIETVFEE LGVELPIMIS GTITDASGRT LSGQTTEAFY NSLRHAKPLT FGLNCALGPK ELRQYVEQLS KISETYVSVH PNAGLPNAFG GYDLGAEEMA AHLKEWAESG FVNIIGGCCG TTPEHIKAFA EAVENIPPRK LPQIKTAMRL SGLEPLNIDD ESLFVNVGER NNVTGSAKFK RLIKEDKFAE AIEIAIDQVE NGAQVIDVNM DEALLDGKKC MTRFLNIMAT EPDAAKVPVM IDSSKWEVIE AGLQSVQGKP IVNSISLKEG EEKFIHQAKL VRKYGAAVVV MAFDEVGQAD TEDRKVEICS RAYDMLVNQV GFPPEDIIFD PNIFAIGTGI EEHNNYGVDF INATGRIKRA LPHAKISGGV SNVSFSFRGN NVMREAIHAV FLYHAIKQGM DMGIVNAGQL AIYDDLDPEL REIVEDAVLN RSPDATEKLL DIAEKYRNQG NDESAVDSVA EWRTWPVEER LKHALVKGIT TYIVEDTEEA RQTLPSPLDV IEGPLMAGMD VVGDLFGDGK MFLPQVVKSA RVMKQSVAYL EPFINATKQK GSSNGKVVIA TVKGDVHDIG KNIVSVVMQC NNFEVIDLGV MVPADKIIQT AIDEKADIIA LSGLITPSLD EMEYFLGEMT RLGLNLPVMI GGATTSKEHT AIKLYPKYKE HGVFYTSNAS RAVTVCATLM NPESRAALWE QFKKDYEKIQ QSFSNRKPLR KQLSIEEARA NRFDGFSGEW ADYVPPKPNQ TGIVEFKNVP IAELRKFIDW SPFFRIWGLM GGYPDAFDYP EGGEEARKVW NDAQVVLDEL EQNHKLNPSG ILGIFPAERV GDDVVLFSDE EHTQPIGTAY GLRQQTERGK NSKSPFNFAL SDFIADRESG KKDWMGMFAV CAGIEEMALV EGYKAAGDDY NAILLQAVGD RLAEAMAEYL HFELRTRIWG YTQEEFDNQG LINENYVGIR PAPGYPSCPE HTEKALIWDL LEVEQRIGMK LTESYAMWPA ASVCGWYFTH PASNYFTLGR IDEDQAQDYA KRKGWDEREM MKWLGVAMK // ID F9GW43_HAEHA Unreviewed; 1229 AA. AC F9GW43; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGT75084.1}; GN ORFNames=GGA_1566 {ECO:0000313|EMBL:EGT75084.1}; OS Haemophilus haemolyticus M21127. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=1028804 {ECO:0000313|EMBL:EGT75084.1}; RN [1] {ECO:0000313|EMBL:EGT75084.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M21127 {ECO:0000313|EMBL:EGT75084.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGT75084.1}. 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; AFQP01000022; EGT75084.1; -; Genomic_DNA. DR RefSeq; WP_005635785.1; NZ_AFQP01000022.1. DR EnsemblBacteria; EGT75084; EGT75084; GGA_1566. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 757 757 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1229 AA; 136369 MW; 75AEBB39F915CE26 CRC64; MVNKTAQLKQ ALENRILILD GAMGTMIQKY KLTEADFRGE KFKESAVDLR GNNDLLTLTQ PLLISAIHEK YLAAGADIIE TNTFSSTTIA QADYDLQSIA YELNFVGAKL ARLAADKYST PEKPRFVAGV LGPTNRTASI SPDVNDPSFR NVTFMELVDA YAQATKGLIE GGADLIMIET IFDTLNAKAA VFAIESVFEE LGVELPIMIS GTITDASGRT LSGQTTEAFY NSLRHANPLT FGLNCALGPK ELRQYVEQLS KISETYVSVH PNAGLPNAFG GYDLGTEEMA AHLKEWAESG FVNIIGGCCG TTPEHIKAFA EAVENIPPRK LPQIKTAMRL SGLEPLNIDD ESLFVNVGER NNVTGSAKFK RLIKEDKFAE AIEIAIDQVE NGAQVIDVNM DEALLDGKKC MTRFLNIMAT EPDAAKVPVM IDSSKWEVIE AGLQSVQGKP IVNSISLKEG EEKFIHQAKL VRKYGAAVVV MAFDEVGQAD TEERKVEICT RAYNILVNQV GFPPEDIIFD PNIFAIGTGI EEHNNYGVDF INATGRIKRS LPHAKISGGV SNVSFSFRGN NVMREAIHAV FLYHAIKQGM DMGIVNAGQL AIYDDLDPEL RNVIEDAVLN RTPDGTERLL DIAEKYRNQG NDESAVDSVA EWRTWPVEER LKHALVKGIT THIIEDTEEA RQKLPTPLEV IEGPLMSGMD VVGDLFGDGK MFLPQVVKSA RVMKQSVAYL EPFINATKQK GSSNGKVVIA TVKGDVHDIG KNIVSVVLQC NNFEVIDLGV MVPADKIIQT AIDEKADIIG LSGLITPSLD EMEYFLGEMT RLGLDLPVLI GGATTSKEHT AIKLYPKYKQ HGVFYTSNAS RAVTVCATLM NPEGRVALWE QFKKDYEKIQ QSFSNRKPLR KQLSIEEARA NRFDGFSGEW ADYVPPTPKQ TGIVEFKNVP IAELRKFIDW SPFFRIWGLM GGYPDAFDYP EGGEEARKVW NDAQVVLDEL EQNHKLNPSG ILGIFPAERV GDDVVLFSDE ERTQIIGTAY GLRQQTERGK NSKSPFNFCL SDFIADHESG KKDWFGMFAV CAGIEEMELV EGYKAAGDDY NAILLQAVGD RLAEAMAEYL HFELRTRIWG YTQEEFDNQG LINENYVGIR PAPGYPSCPE HTEKALIWDL LEVEQRIGMK LTESYAMWPA ASVCGWYFTH PASNYFTLGR IDEDQAQDYA KRKGWDEREM MKWLGVAMK // ID F9GXJ1_HAEHA Unreviewed; 1229 AA. AC F9GXJ1; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGT82012.1}; GN ORFNames=GGC_0165 {ECO:0000313|EMBL:EGT82012.1}; OS Haemophilus haemolyticus M21621. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=1028805 {ECO:0000313|EMBL:EGT82012.1}; RN [1] {ECO:0000313|EMBL:EGT82012.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M21621 {ECO:0000313|EMBL:EGT82012.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGT82012.1}. 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; AFQQ01000001; EGT82012.1; -; Genomic_DNA. DR RefSeq; WP_005636333.1; NZ_AFQQ01000001.1. DR EnsemblBacteria; EGT82012; EGT82012; GGC_0165. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 757 757 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1229 AA; 136207 MW; B68E86B2CA8637F9 CRC64; MVNKTAQLKQ ALENRILILD GAMGTMIQKY KLTEADFRGE KFKESAVDLR GNNDLLTLTQ PLLISAIHEK YLAAGADIIE TNTFSSTTIA QADYDLQSIA YELNFVGAKL ARLAADKYST PEKPRFVAGV LGPTNRTASI SPDVNDPGFR NVTFMELVDA YAQATKGLIE GGADLIMIET IFDTLNAKAA VFAIESVFEE LGVELPIMIS GTITDASGRT LSGQTTEAFY NSLRHAKPLT FGLNCALGPK ELRQYVEQLS KISETYVSVH PNAGLPNAFG GYDLGAEDMA AQLKEWAESG FVNIIGGCCG TTPEHIKAFA EAVENIPPRK LPQIKTAMRL SGLEPLNIDD ESLFVNVGER NNVTGSAKFK RLIKEDKFAE AIEIAIDQVE NGAQVIDVNM DEALLDGKKC MTRFLNIMAT EPDAAKVPVM IDSSKWEVIE AGLQSVQGKT IVNSISLKEG EEKFIHQAKL VRKYGAAVVV MAFDEVGQAD TEERKVEICT RAYNILVNQV GFPPEDIIFD PNIFAIGTGI EEHNNYGVDF INATGRIKRS LPHAKISGGV SNVSFSFRGN NVMREAIHAV FLYHAIKQGM DMGIVNAGQL AIYDDLDPEL RNVIEDAVLN RTPDGTERLL DIAEKYRNQG NDESAVDSVA EWRTWPVEER LKHALVKGIT TYIVEDTEEA RQKLPTPLEV IEGPLMAGMD VVGDLFGDGK MFLPQVVKSA RVMKQSVAYL EPFINATKQK GSSNGKVVIA TVKGDVHDIG KNIVSVVLQC NNFEVIDLGV MVPADKIIQT AIDEKADIIG LSGLITPSLD EMEYFLGEMT RLGLNLPVLI GGATTSKEHT AIKLYPKYKQ HGVFYTSNAS RAVTVCATLM NSEGRAALWE QFKKDYEKIQ QSFANRKPLR KQLSIEEARS NRFDGFSGEW ANYVPPTPKQ TGIVEFKNVP IAELRKFIDW SPFFRIWGLM GGYPDAFDYP EGGEEARKVW NDAQVVLDEL EQNHKLNPSG ILGIFPAERV GDDVVLFSDE ERTQTIGTAY GLRQQTERGK NSKSPFNFAL SDFIADRESG KKDWFGMFAV CAGVEEMDLV EGYKAAGDDY NAILLQAVGD RLAEAMAEYL HFELRTRIWG YTQEEFDNQG LINENYVGIR PAPGYPSCPE HTEKALIWDL LEVEQRIGMK LTESYAMWPA ASVCGWYFTH PASNYFTLGR IDEDQAQDYA KRKGWDEREM MKWLGVAMK // ID F9H7R8_HAEHA Unreviewed; 1240 AA. AC F9H7R8; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGT79678.1}; GN ORFNames=GGE_1861 {ECO:0000313|EMBL:EGT79678.1}; OS Haemophilus haemolyticus M21639. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=1028806 {ECO:0000313|EMBL:EGT79678.1}; RN [1] {ECO:0000313|EMBL:EGT79678.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M21639 {ECO:0000313|EMBL:EGT79678.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGT79678.1}. 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; AFQR01000036; EGT79678.1; -; Genomic_DNA. DR RefSeq; WP_005643096.1; NZ_AFQR01000036.1. DR EnsemblBacteria; EGT79678; EGT79678; GGE_1861. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 757 757 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1240 AA; 137544 MW; 4EDB5AD0FD1F38EF CRC64; MVNKTAQLKQ ALENRILILD GAMGTMIQKY KLTEADFRGE RFKESAVDLR GNNDLLTLTQ PLLISAIHEK YLAAGADIIE TNTFSSTTIA QADYDLQSIA YELNFVGTKL ARLAADKYST PEKPRFVAGV LGPTNRTASI SPDVNDPGFR NVTFMELVDA YAQATKGLIE GGADLIMIET IFDTLNAKAA VFAIESVFEE LGVELPIMIS GTITDASGRT LSGQTTEAFY NSLRHAKPLT FGLNCALGPK ELRQYVEQLS KISETYVSVH PNAGLPNAFG GYDLGAEEMA AHLKEWAESG FVNIIGGCCD TTPEHIKAFA EAVENIPPRK LPQIKTAMRL SGLEPLNIDD ESLFVNVGER NNVTGSAKFK RLIKEDKFAE AIEIAIDQVE NGAQVIDVNM DEALLDGKKC MTRFLNIMAT EPDAAKVPVM IDSSKWEVIE AGLQSVQGKP IVNSISLKEG EEKFIHQAKL VRKYGSVVVV MAFDEVGQAD TEERKVEICT RAYNILVNQV GFPPEDIIFD PNIFAIGTGI EEHNNYGVDF INATGRIKRS LPHAKISGGV SNVSFSFRGN NVMREAIHAV FLYHAIKQGM DMGIVNAGQL AIYDDLDPEL RNIIEDAVLN RTPDGTERLL DIAEKYRNQG NDESAVDSVA EWRTWPVEER LKHALVKGIT THIIEDTEEA RQKLPTPLEV IEGPLMAGMD VVGDLFGDSK MFLPQVVKSA RVMKQSVAYL EPFINATKQK GSSNGKVVIA TVKGDVHDIG KNIVSVVLQC NNFEVIDLGV MVPADKIIQT AIDEKADIIG LSGLITPSLD EMEYFLGEMT RLGLNLPVLI GGATTSKEHT AIKLYPKYKQ HGVFYTSNAS RAVTVCATLM NPEGRAALWE KFKKDYEKIQ QSFSNRKPLR KQLSIKEARA NRFDGFSGEW ADYVPPTPKQ TGIVEFKNVP IAELRKFIDW SPFFHIWGLM GGYPDAFDYP EGGEEARRVW NDAQVVLDEL EQNHKLNPSG ILGIFPAERV SDDVVLFADE ERTQPIGTAY GLRQQTERGK NSKSPFNFCL SDFIADRESG KKDWFGMFAV CAGIEEMDLV EGYKAAGDDY NAILLQAVGD RLAEAMAEYL HFELRTRIWG YTQEEFDNQG LINENYVGIR PALGYPSCPE HTEKALIWDL LEVEQRIGMK LTESYAMWPA ASVCGWYFTH PASNYFTLGR INEDQAQDYA NRKGWDERDD EMVGCGDEVK THQKLTVLVG // ID F9MNC8_9FIRM Unreviewed; 815 AA. AC F9MNC8; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 01-OCT-2014, entry version 15. DE SubName: Full=Putative methionine synthase {ECO:0000313|EMBL:EGS35486.1}; GN ORFNames=HMPREF1040_1253 {ECO:0000313|EMBL:EGS35486.1}; OS Megasphaera sp. UPII 135-E. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Megasphaera. OX NCBI_TaxID=1000569 {ECO:0000313|EMBL:EGS35486.1}; RN [1] {ECO:0000313|EMBL:EGS35486.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UPII 135-E {ECO:0000313|EMBL:EGS35486.1}; 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. {ECO:0000313|EMBL:EGS35486.1}. 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; AFUG01000011; EGS35486.1; -; Genomic_DNA. DR RefSeq; WP_007392342.1; NZ_AFUG01000011.1. DR EnsemblBacteria; EGS35486; EGS35486; HMPREF1040_1253. DR OrthoDB; EOG6091CH; -. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; SQ SEQUENCE 815 AA; 88964 MW; 5249FE4239DFC94A CRC64; MKRDEFHAWL KEGILFLDGA TGTNLQAAGM PVGVCPEAWI LENKQTIIAL QQQFVQAGTD ILYAPTFTGN RIKLAEYGLE DKIVEINTQL VSFSKEAAQG NAKVAGDMTM TGQQLYPLGE LTFEELVDVY REQAQILYDA GVDLFVVETM MSLQETRACV LAIRECCDLP IMASLTFEAD GRTLYGTPPE VAVVVLQAMG VDAVGLNCST GPEDMVEIVK TMHAYASIPI LAKPNAGLPE LEQGHTVYKT TPEVFAEAGT ALVHAGARII GGCCGTTPEH IKALKEAMKH LSPLPYKAEH RRIVTSERKI QEIDLHGSFC VIGERINPTG KKKLQEELRA GSLRLVRTMA REQEERGAAI LDINMGTNGI DEKDMMVRAI YEVTSVTGLP LCIDSSYPEV LEAALRIYPG RALINSISLE TDKIKQVLPL AKKYGAMFIA LPVSDEGIPQ TIEEKHAIIE QIVEKAKEFH LTEADIVVDG LVATAGATPT AALDCLATFT YCKKRNLATV CGLSNISFGL PQRTYVNMTF LAMAISGGLN LAIANPSQDM LMNVAAAANM LMHRPESDIA YIKQIQLFEK HLAEEKTMIK RTQITNTTST LESAPKKENE NKVYRAVLEG EKDEIVSFAQ EELNKGMKPE DIINHLLIPA INEVGELYNK QLYFLPQLIA SANTMEQAIS FLEPQIKRAS NKMAMPTIVI ATVEGDVHDI GKNLVGLMLR NYGYHVIDLG KDVPAETILD TALKEHAAII GLSALMTTTM MRMKDVVLLA KEKAYTGKII IGGAAVTPSF AEEIGADGYS KDAADCVKLV NTLLA // ID F9MSC5_9FIRM Unreviewed; 777 AA. AC F9MSC5; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 12. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGS30511.1}; GN ORFNames=HMPREF9130_0553 {ECO:0000313|EMBL:EGS30511.1}; OS Peptoniphilus sp. oral taxon 375 str. F0436. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptoniphilaceae; OC Peptoniphilus. OX NCBI_TaxID=879308 {ECO:0000313|EMBL:EGS30511.1}; RN [1] {ECO:0000313|EMBL:EGS30511.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0436 {ECO:0000313|EMBL:EGS30511.1}; 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. {ECO:0000313|EMBL:EGS30511.1}. 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; AFUH01000001; EGS30511.1; -; Genomic_DNA. DR RefSeq; WP_009430897.1; NZ_AFUH01000001.1. DR EnsemblBacteria; EGS30511; EGS30511; HMPREF9130_0553. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGS30511.1}; KW Transferase {ECO:0000313|EMBL:EGS30511.1}. SQ SEQUENCE 777 AA; 85367 MW; 22FAFB4062003625 CRC64; MFLTNKIILL DGAMGTQIQK RGIHQRPESI NISHGEVIEE IQRAYVQAGS DIIYSNTFGA HGRNYPDPEE LRKTIHTGLQ IAKRAAGTKA KVAFDMGPLG ELLEPMGTMS FQRAYELFEQ NIQIALEEGF DLVVIETMSS LLELRAAILA VKAHYDGPLL TTMTFEKDGR TFSGVSPQAF AIMADKLGVD ALGVNCSLGP FEIQAILKSI NQVTNKPLIV KANAGLPDEE GNYHMEDDLF IEGIQGMLDL GVQYIGGCCG TTEKTIQGLA KHFKGKEALL QNKEIKQYVA SSSRVVTLDQ TRYVGEVINP TGKTRLKESL EKKNMEEVLR LGVLQDQKGA DLLDVNVSLP GTDEVYLLRK AALHLQALVD LPLQLDSSNV EALEAALMVT PGRPVINSVN GTQESLDAVL PLAKKYGAMV VGLALDEDGI PKTSEKRLAI AEKIVKTAES YGLEKRDVLI DPLVLTIASN KDSAKLALET IEKLTKKGYL TTMGTSNISF GLPKRSLVTA SFLQAALAKG CSMPIVNPLD PRIQEVIHTH RLLMGQDEKA MGYIAFMEDK KEASASLEEE EGDFSPYQAM RRSQKTELLN YVKGAIQEKD PMEIISEELI PALDAIGQDY EKKEIYLPQL IGAASAAQEA FLFLRDQLRV KGDGKGEKIL LATVKGDIHD IGKNIAKVLL ENYGYDVYDL GRDVSKEEIL QTVEEEDIHL VGLSALMTTT VSSMEETIQL LKEKRPDLKI MVGGAVLTQA YAYEIGAHYY CKDAKEDIEI AKNVFKD // ID F9MSC6_9FIRM Unreviewed; 578 AA. AC F9MSC6; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 16. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HMPREF9130_0554 {ECO:0000313|EMBL:EGS30952.1}; OS Peptoniphilus sp. oral taxon 375 str. F0436. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptoniphilaceae; OC Peptoniphilus. OX NCBI_TaxID=879308 {ECO:0000313|EMBL:EGS30952.1}; RN [1] {ECO:0000313|EMBL:EGS30952.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0436 {ECO:0000313|EMBL:EGS30952.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGS30952.1}. 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; AFUH01000001; EGS30952.1; -; Genomic_DNA. DR RefSeq; WP_009431322.1; NZ_AFUH01000001.1. DR EnsemblBacteria; EGS30952; EGS30952; HMPREF9130_0554. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EGS30952.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EGS30952.1}. SQ SEQUENCE 578 AA; 64770 MW; 4CFFE26470348F68 CRC64; MTEFTGSKSK PLIFDGAMGT YLQKISPSDL TIEEYNIEKP AIIEEIHRQY IEAGAQAIKT NTFGANPIQY DRDLCRTYLE AGAKIALKFQ DQAEVYGSIG PMETTDPQDY LCVAEVLYQA GIRKFLWETF PEADKLLEVI DRFCKDHADT LHITSFAVFP SGETRLGVLA QEALEAADKN PHVQAMGLNC ISGPYHLVQL VKNLPTFQTP MGLMPNSGYP TMVDGRLQYK ENPSYFSQAL AQGLNYGLSY LGGCCGTDPS YILELSQHLK EVPDQLENLE KEEKVLEKTE SNLKKKLKSG KQVMVVEYDP PQEATRDYFK KLSLLRQMEV DAVTLADCPI GRPRMDASLT SLILKKDYGL DSVVHMTCRD RNINAIKALL LGLSLEGIQD ILLITGDPVP SVDREDVKAV FQFNSARLAA FVKTLNRDLE NPFTISGALN INAQNFDSEL DKAKRKIESG VELFFTQPIM GKNAIVQLRR AQKELDVPIL AGIMPLVSYR NAQYLHNQVS GMQVDQEVLD SFHEGLSREE GEALGIQWAL EFMNEIGDEV AGFYLITPFQ RLHVIERLLK DYGQGKEK // ID F9N5I0_9FIRM Unreviewed; 808 AA. AC F9N5I0; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGS34986.1}; GN ORFNames=HMPREF9200_1208 {ECO:0000313|EMBL:EGS34986.1}; OS Veillonella sp. oral taxon 780 str. F0422. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Veillonella. OX NCBI_TaxID=944564 {ECO:0000313|EMBL:EGS34986.1}; RN [1] {ECO:0000313|EMBL:EGS34986.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0422 {ECO:0000313|EMBL:EGS34986.1}; 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. {ECO:0000313|EMBL:EGS34986.1}. 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; AFUJ01000036; EGS34986.1; -; Genomic_DNA. DR RefSeq; WP_009353586.1; NZ_AFUJ01000036.1. DR EnsemblBacteria; EGS34986; EGS34986; HMPREF9200_1208. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGS34986.1}; KW Transferase {ECO:0000313|EMBL:EGS34986.1}. SQ SEQUENCE 808 AA; 86409 MW; 2661FEF933322456 CRC64; MVYIIDGGMG TMLQAAGLGD GACPELFNVE HPDVVEHIHA EYLRHGSDII TTNTFGGTAL KLDEYQLGHR MDEINRAAVK VAQAARDKIN PNAKIAGDMG PSGRFMAPLG VAQFDEIYET FRDQARALID AGVDYLIIET IIDIQEMRAA LLGAKDARDE LGKTKEDVKI ICQFSFSEDG RTITGTPPEA AAILMDAMEA DIVGINCSLG PEQLLPLVER MAAVTNLPIS IQPNAGMPQL VGKETIFPLG PEEMGKYAPR FLDAGATYLG ACCGSTPKHI ESIAKAARAH TPAERPHVEP FTAFTSRTSV VKVGLQEKPI IIGERINPTG RKVLAEEIRK GSFLMVKKDA LAQVEAGADV LDVNMGVTGV DPGETMKRAI EELTMLVEVP LSIDTLDPVA MEAGLKAYPG RPLLNSVNAE PEQLEAVLPL AKRYGAALLC LPLGKKELPE TAEERVSLAK EIVLEAYNYG LRPNDLLLDP LVLTLASSQH AARETLKTLK LYAETFGFPT VMGLSNISFG LPQRAYLNAQ FLTMALSSGL TCPIMNPMNE IVRKAFITGR TFMGFDPAAA DFIAEYGDDD ENAVVTKKVK ATAEAFHSDD PIECIKHAVE QGEKEAVVPL VKEALAQGLD PLEVTRRGLS DAMAVVGEKF GSGKAFLPQV MLAAETMQAA FTTIKEVLPE GTAEKKATII LATVKGDIHD LGKNIVSALL ENNGYQIVDL GKDVSPEEIV AAAKEHNAPI IGIASLMTTT MPMINETIAA IRESGVDAKV LVGGAVLSQA YADEAGADSY AKDGISAVNI VKGLLGDE // ID F9N6J1_9FIRM Unreviewed; 421 AA. AC F9N6J1; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGS33480.1}; DE Flags: Fragment; GN ORFNames=HMPREF9200_0795 {ECO:0000313|EMBL:EGS33480.1}; OS Veillonella sp. oral taxon 780 str. F0422. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Veillonella. OX NCBI_TaxID=944564 {ECO:0000313|EMBL:EGS33480.1}; RN [1] {ECO:0000313|EMBL:EGS33480.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0422 {ECO:0000313|EMBL:EGS33480.1}; 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. {ECO:0000313|EMBL:EGS33480.1}. 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; AFUJ01000054; EGS33480.1; -; Genomic_DNA. DR RefSeq; WP_009353975.1; NZ_AFUJ01000054.1. DR EnsemblBacteria; EGS33480; EGS33480; HMPREF9200_0795. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGS33480.1}; KW Transferase {ECO:0000313|EMBL:EGS33480.1}. FT NON_TER 421 421 {ECO:0000313|EMBL:EGS33480.1}. SQ SEQUENCE 421 AA; 45211 MW; 91AB5CACA959D8CB CRC64; MVYIIDGGMG TMLQAAGLGD GACPELFNVE HPDVVEHIHA EYLRHGSDII TTNTFGGTAL KLDEYQLGHR MDEINRAAVK VAQAARDKIN PNAKIAGDMG PSGRFMAPLG VAQFDEIYET FRDQARALID AGVDYLIIET IIDIQEMRAA LLGAKDARDE LGKTKEDVKI ICQFSFSEDG RTITGTPPEA AAILMDAMEA DIVGINCSLG PEQLLPLVER MAAVTNLPIS IQPNAGMPQL VGKETIFPLG PEEMGKYAPR FLDAGATYLG ACCGSTPKHI ESIAKAARAH TPAERPHVEP FTAFTSRTSV VKVGLQEKPI IIGERINPTG RKVLAEEIRK GSFLMVKKDA LAQVEAGADV LDVNMGVTGV DPGETMKRAI EELTMLVEVP LSIDTLDPVA MEAGLKAYPG RPLLNSVNAE P // ID F9PJ78_9ACTO Unreviewed; 308 AA. AC F9PJ78; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 11. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGV14037.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EGV14037.1}; GN Name=mmuM {ECO:0000313|EMBL:EGV14037.1}; GN ORFNames=HMPREF9058_1990 {ECO:0000313|EMBL:EGV14037.1}; OS Actinomyces sp. oral taxon 175 str. F0384. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Actinomycineae; Actinomycetaceae; Actinomyces. OX NCBI_TaxID=944560 {ECO:0000313|EMBL:EGV14037.1}; RN [1] {ECO:0000313|EMBL:EGV14037.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0384 {ECO:0000313|EMBL:EGV14037.1}; 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. {ECO:0000313|EMBL:EGV14037.1}. 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; AFUR01000001; EGV14037.1; -; Genomic_DNA. DR RefSeq; WP_009406132.1; NZ_AFUR01000001.1. DR EnsemblBacteria; EGV14037; EGV14037; HMPREF9058_1990. DR OrthoDB; EOG6C019S; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGV14037.1}; KW Transferase {ECO:0000313|EMBL:EGV14037.1}. SQ SEQUENCE 308 AA; 32359 MW; 9BF23AE35C79D645 CRC64; MSDLLDRGPV VLDGAMGTEL DARGIDTRNA LWSARALTTA PDVVREVHSD YLDAGARVIT TNTYQATLPA LIHSGEDAAG ARRVIAAGAR LAKGAARQFS KEHPEEPVLV AGGLGPYGAY LADGSEYTGT YGIDILEDPG FQEVHLPRIE VMVGEGLDLF ALETLPRLDE ARALASMVTD LAPQAQCWVS FQVRPDGSTL ADGTPLAEAA AWAEQEEIVV AVGINCVAPG VVARALPVLR AATGKPLVAY PNVGDLYDPA TKTWQSTGDG AGIPELAPSW IAEGVRLVGG CCRTRPAQIR QLARAVCP // ID F9QAR7_9PAST Unreviewed; 1228 AA. AC F9QAR7; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGV05345.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGV05345.1}; GN Name=metH {ECO:0000313|EMBL:EGV05345.1}; GN ORFNames=HMPREF9952_1210 {ECO:0000313|EMBL:EGV05345.1}; OS Haemophilus pittmaniae HK 85. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=1035188 {ECO:0000313|EMBL:EGV05345.1}; RN [1] {ECO:0000313|EMBL:EGV05345.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HK 85 {ECO:0000313|EMBL:EGV05345.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGV05345.1}. 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; AFUV01000017; EGV05345.1; -; Genomic_DNA. DR RefSeq; WP_007243179.1; NZ_AFUV01000017.1. DR EnsemblBacteria; EGV05345; EGV05345; HMPREF9952_1210. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGV05345.1}; KW Transferase {ECO:0000313|EMBL:EGV05345.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 756 756 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1228 AA; 136169 MW; 663D4C710B2D8864 CRC64; MRNPAELLKK SLAERILILD GAMGTMIQKY KLTEADFRGE RFKDSTVDLR GNNDLLTLTQ PLLISAIHEK YLAAGADIIE TNTFSSTTIA QADYDLQSIA YELNFAGAKL ARLAADKYST PEKPRFVAGV LGPTNRTASI SPDVNDPGFR NITFMELVDA YAEATKGLIE GGADLIMIET IFDTLNAKAA IFAIETVFEE LGVELPIMIS GTITDASGRT LSGQTTEAFY NSLRHAKPLT FGLNCALGPK ELRQYVEQLS KISETYVSVH PNAGLPNAFG GYDLGAEEMA AHLKEWAESG FVNIVGGCCG TTPEHIKAFA DAMQGIAPRK LPEIKTAMRL SGLEPLNIDD ESLFVNVGER NNVTGSAKFK RLIKEDKFAE AIEIAIDQVE NGAQVIDVNM DEALLDGKKC MTRFLNIMAT EPDAAKVPVM IDSSKWEVIE AGLQSVQGKP IVNSISLKEG EEIFIDHAKQ VRKYGAAVVV MAFDEVGQAD TEDRKVEICS RAYDILVNQV GFPPEDIIFD PNIFAIGTGI EEHNNYGVDF INATGRIKRA LPHAKISGGV SNVSFSFRGN NVMREAIHAV FLYHAIKQGM DMGIVNAGQL AIYDDLDPEL REIVEDAVLN RSPDATEKLL DIAEKYRNQG TTQEDNTIAE WRTWPVEERL KHALVKGITT HIVEDTEEAR QQLPSPLDVI EGPLMAGMDV VGDLFGDGKM FLPQVVKSAR VMKQSVAYLE PFINATKQKG SSNGKVVIAT VKGDVHDIGK NIVSVVLQCN NFEVIDLGVM VPADKIIQTA IDEKADIIGL SGLITPSLDE MEYFLGEMTR LGLNLPVLIG GATTSKEHTA IKLYPKYKEH GVFYTSNASR AVTVCATLMN PESRVELWER FKQDYEKIQQ SFANRKPLRK QLSIEEARAN RFDGFSGEWA DYVPPKPNQT GIVEFKNVPI ATLRKFIDWS PFFRIWGLMG GYPDAFDYPE GGEEARKVWN DAQVVLDELE QNHKLNPSGI LGIFPAERVG DDVVLFADEE RSQPIGTAYG LRQQTERGKN SKSPFNFALS DFIADRKSGK KDWMGMFAVC AGIEEMDLVE GYKAAGDDYN AILLQAVGDR LAEAMAEYLH FELRTRIWGY TQEEFDNQGL INENYVGIRP APGYPSCPEH TEKALIWDLL EVEQRIGMKL TESYAMWPAA SVCGWYFTHP ASNYFTLGRI DEDQAQDYAK RKGWDEREMM KWLGVAMK // ID F9RAW0_VIBSN Unreviewed; 1225 AA. AC F9RAW0; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 01-APR-2015, entry version 19. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EGU34660.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGU34660.1}; GN Name=metH {ECO:0000313|EMBL:EGU34660.1}; GN ORFNames=VIBRN418_11200 {ECO:0000313|EMBL:EGU34660.1}; OS Vibrio sp. (strain N418). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=701176 {ECO:0000313|EMBL:EGU34660.1}; RN [1] {ECO:0000313|EMBL:EGU34660.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=N418 {ECO:0000313|EMBL:EGU34660.1}; RA Strain E.A., Brown E., Allard M.W.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGU34660.1}. 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; AFWD01000040; EGU34660.1; -; Genomic_DNA. DR RefSeq; WP_009385789.1; NZ_AFWD01000040.1. DR EnsemblBacteria; EGU34660; EGU34660; VIBRN418_11200. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGU34660.1}; KW Transferase {ECO:0000313|EMBL:EGU34660.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1225 AA; 136364 MW; 5E325C67E6F55E7E CRC64; MGSKIRQQIE AQLKRRILLI DGGMGTMIQD YKLEEQEYRG ERFADWHCDL KGNNDLLVLS QPKLIKDIHL DYLEAGADIL ETNTFNATTI AMADYDMESL SAEINFVAAK LAREAADEWT AKTPDKPRYV AGVLGPTNRT CSISPDVNDP GYRNVSFDEL VEAYSESTHA LIRGGADLIL LETIFDTLNA KACAFAVETV FEELGYSLPV MISGTITDAS GRTLSGQTTE AFYNSLRHVK PISFGLNCAL GPDELRPYVV ELSRISETFV SVHPNAGLPN AFGEYDLSPE DMAEHVTEWA QSGFLNLIGG CCGTTPEHIR QMALAVEGVT PRSLPDLPVA CRLSGLEPLT IEKDTLFLNV GERTNVTGSA RFKRLIKEEL YEEALDVARQ QVENGAQIID INMDEGMIDA EACMVRFLNL CASEPEISKV PIMVDSSKWE VIEAGLKCIQ GKGIVNSISL KEGKEKFVAQ AKLVRRYGAA IIVMAFDEVG QAETRERKLE ICTNAYRILV DEVGFPPEDI IFDPNIFAVA TGIEEHNNYA VDFIEAVADI KRDLPHAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK NGMDMGIVNA GQLEIYDNVP ETLREAVEDV VLNRRDDSTE RLLDIAQEYL DKAVGKVEDA SSLEWRTWPV EKRLEHSLVK GITEFIVEDT EEARVNASRP IEVIEGPLMD GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AHLEPFINAS KEVGSTNGKI LLATVKGDVH DIGKNIVGVV LQCNNYEIID LGVMVPCEKI LKVAQEENVD IIGLSGLITP SLDEMVHVAK EMERQGFELP LLIGGATTSK AHTAVKIEQN YHKPVVYVNN ASRAVGVCTS LLSKELYPAF VEKLDADYEV VRDQHRRKKP RTRPVTLERA RANKVAIDWA SYTPPAPAKP GVHIFKDFDI ATLRQYIDWT PFFMTWSLVG KYPAILEHEE VGEEAKRLFK DANELLDRVE REKLLEARGM CALLPAASVG DDIEVYTDES RTEVAKVLYN LRQQTEKPKG FNYCLSDYIA PKESGKLDWI GAFAVTGGIG ERELADQYKA AGDDYNAIMI QAVADRLAEA FAEYLHEKVR KEIWGYASDE ALSNDDLIRE KYQGIRPAPG YPACPEHTEK GALWELLNVE ESIEMSLTSS YAMWPGAAVS GWYFSHPDSR YFAIAQIQQD QAESYADRKG WDMLEAEKWL GPNMN // ID F9RKK8_9VIBR Unreviewed; 1225 AA. AC F9RKK8; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EGU39573.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGU39573.1}; GN Name=metH {ECO:0000313|EMBL:EGU39573.1}; GN ORFNames=VIS19158_10174 {ECO:0000313|EMBL:EGU39573.1}; OS Vibrio scophthalmi LMG 19158. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=870967 {ECO:0000313|EMBL:EGU39573.1}; RN [1] {ECO:0000313|EMBL:EGU39573.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 19158 {ECO:0000313|EMBL:EGU39573.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGU39573.1}. 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; AFWE01000066; EGU39573.1; -; Genomic_DNA. DR RefSeq; WP_005593694.1; NZ_AFWE01000066.1. DR EnsemblBacteria; EGU39573; EGU39573; VIS19158_10174. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGU39573.1}; KW Transferase {ECO:0000313|EMBL:EGU39573.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1225 AA; 136361 MW; B0A6FB6A37250823 CRC64; MGSKIRQQIE AQLKRRILLI DGGMGTMIQD YKLEEQEYRG ERFADWHCDL KGNNDLLVLS QPKLIKDIHL DYLEAGADIL ETNTFNATTI AMADYDMESL SAEINFAAAK LAREAADEWT AKTPDKPRYV AGVLGPTNRT CSISPDVNDP GYRNVSFDEL VEAYSESTHA LIRGGADLIL LETIFDTLNA KACAFAVETV FEELGYSLPV MISGTITDAS GRTLSGQTTE AFYNSLRHVK PISFGLNCAL GPDELRPYVV ELSRISETFV SVHPNAGLPN AFGEYDLSPE DMAEHVTEWA QSGFLNLIGG CCGTTPEHIR QMALAVEGVT PRALPDLPVA CRLSGLEPLT IEKDTLFLNV GERTNVTGSA RFKRLIKEEL YEEALDVARQ QVENGAQIID INMDEGMIDA EACMVRFLNL CASEPEISKV PIMVDSSKWE VIEAGLKCIQ GKGIVNSISL KEGKEKFVAQ AKLVRRYGAA IIVMAFDEVG QAETRERKLE ICTNAYRILV DEVGFPPEDI IFDPNIFAVA TGIEEHNNYA VDFIEAVADI KRDLPHAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK NGMDMGIVNA GQLEIYDNVP ETLREAVEDV VLNRRDDSTE RLLDIAQEYL DKAVGKVEDA SSLEWRTWPV EKRLEHSLVK GITEFIVEDT EEARVNASRP IEVIEGPLMD GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AHLEPFINAS KEVGSTNGKI LLATVKGDVH DIGKNIVGVV LQCNNYEIID LGVMVPCEKI LKIAQEENVD IIGLSGLITP SLDEMVHVAK EMERQGFELP LLIGGATTSK AHTAVKIEQN YHKPVVYVNN ASRAVGVCTS LLSKELYPAF VEKLDADYEV VRDQHRRKKP RTRPVTLERA RANKVAIDWA SYTPPAPAKP GVHIFKDFDI ATLRQYIDWT PFFMTWSLVG KYPAILEHKE VGEEAKRLFK DANELLDRVE REKLLEARGM CALLPAASVG DDIEVYTDES RTEVAKVLYN LRQQTEKPKG FNYCLSDYIA PKESGKLDWI GAFAVTGGIG ERELADQYKA AGDDYNAIMI QAVADRLAEA FAEYLHEKVR KEIWGYASDE VLSNDDLIRE KYQGIRPAPG YPACPEHTEK GALWELLNVE ESIEMSLTSS YAMWPGAAVS GWYFSHPDSR YFAIAQIQQD QAESYADRKG WDMLEAEKWL GPNMN // ID F9S4Y2_9VIBR Unreviewed; 1225 AA. AC F9S4Y2; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EGU36337.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGU36337.1}; GN Name=metH {ECO:0000313|EMBL:EGU36337.1}; GN ORFNames=VII00023_11776 {ECO:0000313|EMBL:EGU36337.1}; OS Vibrio ichthyoenteri ATCC 700023. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=870968 {ECO:0000313|EMBL:EGU36337.1}; RN [1] {ECO:0000313|EMBL:EGU36337.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 700023 {ECO:0000313|EMBL:EGU36337.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGU36337.1}. 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; AFWF01000213; EGU36337.1; -; Genomic_DNA. DR RefSeq; WP_006713567.1; NZ_AFWF01000213.1. DR EnsemblBacteria; EGU36337; EGU36337; VII00023_11776. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGU36337.1}; KW Transferase {ECO:0000313|EMBL:EGU36337.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1225 AA; 136517 MW; 06BD3FBD7FB7B0F1 CRC64; MGSKIRQQIE AQLKQRILLI DGGMGTMIQD YKLEEQEYRG ERFADWHCDL KGNNDLLVLS QPKLIKDIHL DYLEAGADIL ETNTFNATTI AMADYDMENL SAEINFAAAK LAREAADEWT AKTPSKPRFV AGVLGPTNRT CSISPDVNDP GYRNVSFDEL VVAYSESTHA LIRGGADLIL LETIFDTLNA KACAFAVETV FEELGYSLPV MISGTITDAS GRTLSGQTTE AFYNSLRHVK PISFGLNCAL GPDELRPYVV ELSRISETFV SVHPNAGLPN AFGEYDLSPD DMAEHVKEWA QSGYLNLIGG CCGTTPEHIR QMALAVEGMQ PRILPDLPVA CRLSGLEPLT IEKETLFLNV GERTNVTGSA RFKRLIKEEL YEEALDVARQ QVENGAQIID INMDEGMIDA EACMVRFLNL CASEPEISKV PIMVDSSKWE VIEAGLKCIQ GKGIVNSISL KEGKEKFIAQ AKLVRRYGAA IIVMAFDEVG QAETRERKLE ICTNAYRILV DEVGFPPEDI IFDPNIFAVA TGIDEHNNYA VDFIEAVADI KRELPHAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK NGMDMGIVNA GQLEIYDNVP ETLREAVEDV VLNRRDDSTE RLLDIAQEYL DKAVGKVEDT SALEWRTWPV EKRLEHSLVK GITEFIVEDT EEARVNAARP IEVIEGPLMD GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AHLEPFINAS KEVGSTNGKI LLATVKGDVH DIGKNIVGVV LQCNNYEIID LGVMVPCEKI LKVAKEENVD IIGLSGLITP SLDEMVHVAK EMERQGFELP LLIGGATTSK AHTAVKIEQN YHKPVVYVNN ASRAVGVCTS LLSKELYPAF VEKLDADYEV VRDQHRRKKP RTRPVTLERA RANKVAIDWA NYTPPAPAKP GVHIFKEFDI ATLRQYIDWT PFFMTWSLVG KYPAILDHEE VGEEAQRLFK DANDLLDRVE REKLLEARGM CALLPAASVG DDIEVYTDES RTEVAKVLYN LRQQTEKPKG FNYCLSDYIA PKESGKLDWI GAFAVTGGIG ERELADQYKA DGDDYNAIMI QAVADRLAEA FAEYLHEKVR KEIWGYSSDE ALSNDDLIRE KYQGIRPAPG YPACPEHTEK GSLWELLNVE ENIEMSLTSS YAMWPGAAVS GWYFSHPDSR YFAIAQIQQD QAESYADRKG WDMLEAEKWL GPNMN // ID F9S958_VIBSP Unreviewed; 301 AA. AC F9S958; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EGU45733.1}; GN ORFNames=VISP3789_21173 {ECO:0000313|EMBL:EGU45733.1}; OS Vibrio splendidus ATCC 33789. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=1051645 {ECO:0000313|EMBL:EGU45733.1}; RN [1] {ECO:0000313|EMBL:EGU45733.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33789 {ECO:0000313|EMBL:EGU45733.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGU45733.1}. 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; AFWG01000001; EGU45733.1; -; Genomic_DNA. DR RefSeq; WP_004736832.1; NZ_AFWG01000001.1. DR EnsemblBacteria; EGU45733; EGU45733; VISP3789_21173. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EGU45733.1}; KW Transferase {ECO:0000313|EMBL:EGU45733.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 204 204 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 279 279 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 280 280 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 301 AA; 32802 MW; B7855EA5A8D959EB CRC64; MKTLTILDGG MGRELKEIGA PFSQPLWSAQ ALIEAPDFVS QAHQNFVDAG AEIIITNSYA CVPFHLGEEL FAQRGFELAA LSGELAKAIA DQAPQAVKVA GSIPPPFGSY RPDLFKVEEA ASIIQTLYDA QEPNIDLWLV ETLSSVQEFE SIHGVLKQST KPCYYAFSLE DTKGDSASIR SGESVKEAVK LVCQSNATGI MFNCSVPEVM DQAIIDTKQV MDELGQDLEI GVYANNFAPI SSEHEANDML QEMRELDGQG YLTYAKRWHA LGANIIGGCC GIGPKHIKAL ADWKLEVIEE K // ID F9SHW1_VIBSP Unreviewed; 1225 AA. AC F9SHW1; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EGU41438.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGU41438.1}; GN Name=metH {ECO:0000313|EMBL:EGU41438.1}; GN ORFNames=VISP3789_16307 {ECO:0000313|EMBL:EGU41438.1}; OS Vibrio splendidus ATCC 33789. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=1051645 {ECO:0000313|EMBL:EGU41438.1}; RN [1] {ECO:0000313|EMBL:EGU41438.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33789 {ECO:0000313|EMBL:EGU41438.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGU41438.1}. 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; AFWG01000034; EGU41438.1; -; Genomic_DNA. DR RefSeq; WP_004740868.1; NZ_AFWG01000034.1. DR EnsemblBacteria; EGU41438; EGU41438; VISP3789_16307. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGU41438.1}; KW Transferase {ECO:0000313|EMBL:EGU41438.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1225 AA; 135990 MW; 99AAB0D3280DB545 CRC64; MGSNVRQKID ALLKQRILLI DGGMGTMIQD YKLEEQDYRG ERFADWHSDL KGNNDLLVLT QPKLIKDIHS QYLEAGADIL ETNTFNATTI AMADYDMESL SEEINFAAAK LAREAADEWT AKTPEKPRFV AGVLGPTNRT CSISPDVNDP GYRNVSFDEL VKAYSESTRA LIKGGSDLIL IETIFDTLNA KACAFAVESV FEEVGVTLPV MISGTITDAS GRTLSGQTTE AFYNALRHVK PISFGLNCAL GPDELREYVG EMSRISESYV SAHPNAGLPN AFGEYDLSSE DMAEHVKEWA ESGFLNLIGG CCGTTPEHIR QMAEAVEGVA PRQLPDLPVS CRLSGLEPLT IAKESLFVNV GERTNVTGSA RFKRLIKEEL YDEALSVARE QVENGAQIID INMDEGMLDA EACMVKFLNL CASEPEISKV PVMVDSSKWE VIEAGLKCIQ GKGIVNSISL KEGKEKFVEQ AKLVRRYGAA VIVMAFDEVG QADTRERKVE ICTNAYNILV DEVGFPPEDI IFDPNIFAVA TGIEEHNNYA VDFIDAIGDI KRDLPHAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK NGMDMGIVNA GQLEIYDNVP EDLRDAVEDV VLNRREDSTE RLLDMATEYL ERAVGKVEDK SALEWRTWPV EKRLEHSLVK GITDFIVEDT EEARVNSARP IEVIEGPLMD GMNVVGDLFG AGKMFLPQVV KSARVMKQAV AHLEPFINAS KQVGASNGKI LLATVKGDVH DIGKNIVGVV LQCNNYDIID LGVMVSCEQI LKVAKEENVD IIGLSGLITP SLDEMVHVAK EMERQGFELP LLIGGATTSK AHTAVKIEQN YSEPVVYVNN ASRAVGVCTS LLSEELKPAF VEKLDLDYER VRDQHNRKKP RTKPVTLEQA RANKVAIDWD AYTPPAPAKP GVHVFNDFDV ATLRNYIDWT PFFMTWSLVG KYPAILDHEE VGEEAKRLFK DANELLDRVE KEKLLEARGM CAMFPANSVG DDIEVYTDES RTEVLKVLHN LRQQTEKPKG FNYCLSDYIA PKESGKADWI GGFAVTGGIG ERELADEYKA NGDDYNAIMI QAVADRLAEA FAEYLHQEVR KDIWGYAPDE DLSNDDLIRE KYQGIRPAPG YPACPEHTEK GTLWELMDVE KTIDMSLTSS YAMWPGASVS GMYFSHPDSR YFAIAQIQQD QVDSYADRKG WDMLEAEKWL GPNIN // ID F9TCW8_9VIBR Unreviewed; 1225 AA. AC F9TCW8; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AIW12904.1}; GN ORFNames=IX91_01540 {ECO:0000313|EMBL:AIW12904.1}; OS Vibrio tubiashii ATCC 19109. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=1051646 {ECO:0000313|EMBL:AIW12904.1, ECO:0000313|Proteomes:UP000030071}; RN [1] {ECO:0000313|EMBL:AIW12904.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 19109 {ECO:0000313|EMBL:AIW12904.1}; RA Richards G.P., Needleman D.S., Watson M.A., Bono J.L.; RT "First Complete Genome Sequence of the Shellfish Pathogen Vibrio RT tubiashii."; RL Submitted (AUG-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; CP009354; AIW12904.1; -; Genomic_DNA. DR RefSeq; WP_004748610.1; NZ_AFWI01000207.1. DR EnsemblBacteria; AIW12904; AIW12904; IX91_01540. DR EnsemblBacteria; EGU47541; EGU47541; VITU9109_11686. DR GeneID; 23443393; -. DR Proteomes; UP000030071; Chromosome 1. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000030071}. SQ SEQUENCE 1225 AA; 136131 MW; 0172E17D7480B181 CRC64; MGSNVRQQIE AQLKQRILLI DGGMGTMIQD YKLEEQDYRG ERFADWHCDL KGNNDLLVLS QPQLIKDIHS AYLEAGADIL ETNTFNATTI AMADYEMESL SEEINFAAAK LAREAADEWT AKTPEKPRYV AGVLGPTNRT CSISPDVNDP GYRNVSFDEL VEAYSESTRA LIKGGSDLIL IETIFDTLNA KACAFAVDTV FEELGSKLPV MISGTITDAS GRTLSGQTTE AFYNSLRHVN PISFGLNCAL GPDELRPYVE ELSRISETFV STHPNAGLPN AFGEYDLSPE DMAVHVKEWA ESGFLNLIGG CCGTTPEHIR QMAIAVEGVK PRALPELITA CRLSGLEPLT IEKETLFVNV GERTNVTGSA RFKRLIKEEL YDEALEVARQ QVENGAQIID INMDEGMLDA EACMVRFLNL CASEPEISKV PIMVDSSKWE VIEAGLKCIQ GKGIVNSISL KEGKEKFVEQ AKLIRRYGAA VIVMAFDEVG QAETRERKLE ICTNAYNILV DEIGFPPEDI IFDPNIFAVA TGIEEHNNYA VDFIEAVADI KRDLPYAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK NGMDMGIVNA GQLEIYDNVP DKLREAVEDV VLNRRDDGTE RLLDIAAEYA GKGVGKEEDA SALEWRTWSV EKRLEHALVK GITEFIVEDT EEARVNASKP LEVIEGPLMD GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AHLEPYINAS KQAGSSNGKI LLATVKGDVH DIGKNIVGVV LQCNNYEIID LGVMVPCEQI LKVAKEENVD IIGLSGLITP SLDEMVHVAK EMERLDFDLP LLIGGATTSK AHTAVKIEQN YKHPVVYVNN ASRAVGVCTS LLSDELRPAF VEKLDADYVR VRDQHNRKKP RTKPVILEQA RANKVAIDWE CYTPPEPAKP GVHVFDDFDV ATLRNYIDWT PFFMTWSLVG KYPAILDHEE VGEEAKRLFK DANDLLDRVE NEGLLKARGM CALFPAASVG DDIEVYTDES RTEVAKVLYN LRQQTEKPKG FNYCLSDYIA PKESGKKDWI GAFAVTGGIG ERELADQYKA AGDDYNAIMI QAVADRLAEA FAEYLHEQVR KEIWGYSADE NLSNDELIRE KYQGIRPAPG YPACPEHTEK GSLWELLKVE ETIDMSLTTS YAMWPGASVS GWYFSHPDSR YFAIAQIQQD QAQSYADRKG WDMLEAEKWL GPNLN // ID F9U7H6_9GAMM Unreviewed; 350 AA. AC F9U7H6; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGV20202.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGV20202.1}; GN ORFNames=ThimaDRAFT_0878 {ECO:0000313|EMBL:EGV20202.1}; OS Thiocapsa marina 5811. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Thiocapsa. OX NCBI_TaxID=768671 {ECO:0000313|EMBL:EGV20202.1}; RN [1] {ECO:0000313|EMBL:EGV20202.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=5811 {ECO:0000313|EMBL:EGV20202.1}; 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 ----------------------------------------------------------------------- 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; EGV20202.1; -; Genomic_DNA. DR RefSeq; WP_007191755.1; NZ_AFWV01000002.1. DR EnsemblBacteria; EGV20202; EGV20202; ThimaDRAFT_0878. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGV20202.1}; KW Transferase {ECO:0000313|EMBL:EGV20202.1}. SQ SEQUENCE 350 AA; 38228 MW; BD34F6A547FB88CA CRC64; MPDSRTRLTE LADRRILILD GAMGTMIQRH QLDEADYRGE RFKDWPSDLK GNNDLLSLTK PEVIRAIHDQ YLEAGADILE TNTFNGNRLS QADYGLQDYT AEIVTAAARL AREVADAWTA KTPDKPRFVA GVLGPTSKTA SISPDVNDPG ARNTNFDELV AVYAEATRAL IAADVDIILI ETIFDTLNAK AAAFAVEQVF EEDGVILPVM ISGTITDASG RTLSGQTVEA FYNSLRHVKP FAIGLNCALG PDLLRPHVED MARVAESYTT FHPNAGLPNE MGGYDMTPDQ MAEQIEEWAQ SGFLNIIGGC CGSTPDHIRA IAHAVDGKRP RSPVKEDHRM RLSGLEAFNA // ID F9UN77_LACPL Unreviewed; 309 AA. AC F9UN77; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CCC78666.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:CCC78666.1}; GN Name=metH {ECO:0000313|EMBL:CCC78666.1}; GN OrderedLocusNames=lp_1298 {ECO:0000313|EMBL:CCC78666.1}; OS Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=220668 {ECO:0000313|EMBL:CCC78666.1, ECO:0000313|Proteomes:UP000000432}; RN [1] {ECO:0000313|EMBL:CCC78666.1, ECO:0000313|Proteomes:UP000000432} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1 RC {ECO:0000313|Proteomes:UP000000432}; 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., Stiekema W., Lankhorst R.M., Bron P.A., Hoffer S.M., RA Groot M.N., Kerkhoven R., de Vries M., Ursing B., de Vos W.M., RA Siezen R.J.; RT "Complete genome sequence of Lactobacillus plantarum WCFS1."; RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WCFS1; RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M., RA Kleerebezem M., van Hijum S.A.F.T.; RT "Complete resequencing and reannotation of the Lactobacillus plantarum RT WCFS1 genome."; 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; AL935263; CCC78666.1; -; Genomic_DNA. DR RefSeq; WP_011101343.1; NC_004567.2. DR RefSeq; YP_004889180.1; NC_004567.2. DR ProteinModelPortal; F9UN77; -. DR EnsemblBacteria; CCC78666; CCC78666; lp_1298. DR GeneID; 1062765; -. DR KEGG; lpl:lp_1298; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR BioCyc; LPLA220668-WGS:GSPK-1124-MONOMER; -. DR Proteomes; UP000000432; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000432}; KW Methyltransferase {ECO:0000313|EMBL:CCC78666.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000432}; KW Transferase {ECO:0000313|EMBL:CCC78666.1}. SQ SEQUENCE 309 AA; 32891 MW; B0C85992D25C1333 CRC64; MLSLTEQLNR GPVVSDGAMA TELEKRGVAT NSALWSATAM LDHPDAIQAV HQSYLDAGAK IMTTNTYQAN VPAFEQAGIA AVQARQLIQQ AVTIAHTARD ASHVTDAVIA GSIGPYGAYL ADGSEYTGAY QLTPSAYQDF HRERLALIMA AGVDVLALET MPRLDEVQAL VQLITTTWPQ QPYWVSFSIK DPQTLCDGTS LAVAAKWVAA QPNVVAVGVN CTTLENIAPA LTTLKAAVAV PLIVYPNSGD QYDPVTKTWQ ETHLSHQFAS FVPQWLAAGA RIIGGCCRTT PKDIATVARA LSVSDSAKL // ID F9UND4_LACPL Unreviewed; 618 AA. AC F9UND4; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 25. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=lp_1374 {ECO:0000313|EMBL:CCC78723.1}; OS Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=220668 {ECO:0000313|EMBL:CCC78723.1, ECO:0000313|Proteomes:UP000000432}; RN [1] {ECO:0000313|EMBL:CCC78723.1, ECO:0000313|Proteomes:UP000000432} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1 RC {ECO:0000313|Proteomes:UP000000432}; 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., Stiekema W., Lankhorst R.M., Bron P.A., Hoffer S.M., RA Groot M.N., Kerkhoven R., de Vries M., Ursing B., de Vos W.M., RA Siezen R.J.; RT "Complete genome sequence of Lactobacillus plantarum WCFS1."; RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WCFS1; RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M., RA Kleerebezem M., van Hijum S.A.F.T.; RT "Complete resequencing and reannotation of the Lactobacillus plantarum RT WCFS1 genome."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; CCC78723.1; -; Genomic_DNA. DR RefSeq; WP_011101376.1; NC_004567.2. DR RefSeq; YP_004889237.1; NC_004567.2. DR ProteinModelPortal; F9UND4; -. DR EnsemblBacteria; CCC78723; CCC78723; lp_1374. DR GeneID; 1062572; -. DR KEGG; lpl:lp_1374; -. DR KO; K00548; -. DR OMA; NEVPGIQ; -. DR BioCyc; LPLA220668-WGS:GSPK-1183-MONOMER; -. DR Proteomes; UP000000432; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000432}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:CCC78723.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862, KW ECO:0000313|EMBL:CCC78723.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000432}; KW Transferase {ECO:0000313|EMBL:CCC78723.1}. SQ SEQUENCE 618 AA; 66781 MW; 254AA5ABFBAB662D CRC64; MKFKQALQQR VLVADGAMGT LLYGNYGINS AFENLNLTHP DTILRVHRSY IRAGADIIQT NTYAANRLKL TRYDLQDQVT TINQAAVKIA ATAREHADHP VYILGTIGGL AGDTDATVQR ATPATIAASV TEQLTALLAT NQLDGILLET YYDLPELLAA LKIVKAHTDL PVITNVSMLA PGVLRNGTSF TDAIVQLNAA GADVIGTNCR LGPYYLAQSF ENLAIPANVK LAVYPNAGLP GTDQDGAVVY DGEPSYFEEY AERFRQLGLN IIGGCCGTTP LHTSATVRGL SNRSIVAHDQ PATKPQPPTL VTTKSQHRFL QKVATQKTAL VELDPPRDFD TTKFFRGAER LKAAGVDGIT LSDNSLATVR IANTTIAAQL KLNYGITPIV HLTTRDHNLI GLQSEIMGLH SLGIEDILAI TGDPAKLGDF PGATSVSDVR SVELMKLIKQ FNSGIGPTGK SLKEASDFRV AGAFNPNAYR TSISTKSISR KLSYGCDYII TQPVYDLANV DALADALAAN HVNVPVFVGV MPLVSRRNAE FLHHEVHGIR IPEPILTRMA EAEQTGNERA VGIAIAKELI DGICARFNGV HIVTPFNRFK TVIELVDYIQ QKNLIKVQ // ID F9V4Q1_MYCBI Unreviewed; 1192 AA. AC F9V4Q1; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 01-APR-2015, entry version 20. DE SubName: Full=Probable 5-methyltetrahydrofolate--homocystein methyltransferase MetH (Methionine synthase, vitamin-B12 dependent isozyme) (MS) {ECO:0000313|EMBL:CCC64718.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CCC64718.1}; GN Name=metH {ECO:0000313|EMBL:CCC64718.1}; GN ORFNames=BCGM_2125c {ECO:0000313|EMBL:CCC64718.1}; OS Mycobacterium bovis BCG str. Moreau RDJ. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=413996 {ECO:0000313|EMBL:CCC64718.1}; RN [1] {ECO:0000313|EMBL:CCC64718.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Moreau RDJ {ECO:0000313|EMBL:CCC64718.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AM412059; CCC64718.1; -; Genomic_DNA. DR ProteinModelPortal; F9V4Q1; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CCC64718.1}; KW Transferase {ECO:0000313|EMBL:CCC64718.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 231 231 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 297 297 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 298 298 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 742 742 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1192 AA; 130309 MW; 46AAC38DFC5D05F5 CRC64; MTAADKHLYD TDLLDVLSQR VMVGDGAMGT QLQAADLTLD DFRGLEGCNE ILNETRPDVL ETIHRNYFEA GADAVETNTF GCNLSNLGDY DIADRIRDLS QKGTAIARRV ADELGSPDRK RYVLGSMGPG TKLPTLGHTE YAVIRDAYTE AALGMLDGGA DAILVETCQD LLQLKAAVLG SRRAMTRAGR HIPVFAHVTV ETTGTMLLGS EIGAALTAVE PLGVDMIGLN CATGPAEMSE HLRHLSRHAR IPVSVMPNAG LPVLGAKGAE YPLLPDELAE ALAGFIAEFG LSLVGGCCGT TPAHIREVAA AVANIKRPER QVSYEPSVSS LYTAIPFAQD ASVLVIGERT NANGSKGFRE AMIAEDYQKC LDIAKDQTRD GAHLLDLCVD YVGRDGVADM KALASRLATS STLPIMLDST ETAVLQAGLE HLGGRCAINS VNYEDGDGPE SRFAKTMALV AEHGAAVVAL TIDEEGQART AQKKVEIAER LINDITGNWG VDESSILIDT LTFTIATGQE ESRRDGIETI EAIRELKKRH PDVQTTLGLS NISFGLNPAA RQVLNSVFLH ECQEAGLDSA IVHASKILPM NRIPEEQRNV ALDLVYDRRR EDYDPLQELM RLFEGVSAAS SKEDRLAELA GLPLFERLAQ RIVDGERNGL DADLDEAMTQ KPPLQIINEH LLAGMKTVGE LFGSGQMQLP FVLQSAEVMK AAVAYLEPHM ERSDDDSGKG RIVLATVKGD VHDIGKNLVD IVLSNNGYEV VNIGIKQPIA TILEVAEDKS ADVVGMSGLL VKSTVVMKEN LEEMNTRGVA EKFPVLLGGA ALTRSYVEND LAEIYQGEVH YARDAFEGLK LMDTIMSAKR GEAPDENSPE AIKAREKEAE RKARHQRSKR IAAQRKAAEE PVEVPERSDV AADIEVPAPP FWGSRIVKGL AVADYTGLLD ERALFLGQWG LRGQRGGEGP SYEDLVETEG RPRLRYWLDR LSTDGILAHA AVVYGYFPAV SEGNDIVVLT EPKPDAPVRY RFHFPRQQRG RFLCIADFIR SRELAAERGE VDVLPFQLVT MGQPIADFAN ELFASNAYRD YLEVHGIGVQ LTEALAEYWH RRIREELKFS GDRAMAAEDP EAKEDYFKLG YRGARFAFGY GACPDLEDRA KMMALLEPER IGVTLSEELQ LHPEQSTDAF VLHHPEAKYF NV // ID F9V5N8_MYCBI Unreviewed; 302 AA. AC F9V5N8; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 01-OCT-2014, entry version 11. DE SubName: Full=Probable homocysteine S-methyltransferase mmuM {ECO:0000313|EMBL:CCC65055.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:CCC65055.1}; GN Name=mmuM {ECO:0000313|EMBL:CCC65055.1}; GN ORFNames=BCGM_2462 {ECO:0000313|EMBL:CCC65055.1}; OS Mycobacterium bovis BCG str. Moreau RDJ. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=413996 {ECO:0000313|EMBL:CCC65055.1}; RN [1] {ECO:0000313|EMBL:CCC65055.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Moreau RDJ {ECO:0000313|EMBL:CCC65055.1}; 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 ----------------------------------------------------------------------- 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; CCC65055.1; -; Genomic_DNA. DR ProteinModelPortal; F9V5N8; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:CCC65055.1}; KW Transferase {ECO:0000313|EMBL:CCC65055.1}. SQ SEQUENCE 302 AA; 31533 MW; D8174BFD6FDE55BD CRC64; MELVSDSVLI SDGGLATELE ARGHDLSDPL WSARLLVDAP HAITAVHTAY FRAGAQIATT ASYQASFEGF AARGIGHDDA TVLLRRSVEL AQAARDEVGV GGLSVAASVG PYGAALADGS EYRGCYGLSV AALMKWHLPR LEVLVDAGAD MLALETIPDI DEAEALVNLV RRLATPAWLS YTINGTRTRA GQPLTDAFAV AAGVPEIVAV GVNCCAPDDV LPAIAFAVAH TGKPVIVYPN SGEGWDGRRR AWVGPRRFSG SSGQLAREWV AAGARIVGGC CRVRPIDIAE IGRALTTAPP RG // ID F9W0G0_9ACTO Unreviewed; 1196 AA. AC F9W0G0; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:GAA14349.1}; GN Name=metH {ECO:0000313|EMBL:GAA14349.1}; GN ORFNames=GOALK_099_00890 {ECO:0000313|EMBL:GAA14349.1}; OS Gordonia alkanivorans NBRC 16433. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Gordoniaceae; Gordonia. OX NCBI_TaxID=1027371 {ECO:0000313|EMBL:GAA14349.1}; RN [1] {ECO:0000313|EMBL:GAA14349.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NBRC 16433 {ECO:0000313|EMBL:GAA14349.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; BACI01000099; GAA14349.1; -; Genomic_DNA. DR RefSeq; WP_006360416.1; NZ_BACI01000099.1. DR EnsemblBacteria; GAA14349; GAA14349; GOALK_099_00890. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 237 237 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 747 747 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1196 AA; 130682 MW; 7F64AA963F270361 CRC64; MSFENSGHRP SDFDTTFLSS MSRRVLIGDG AMGTMLQAAD LTLDDFHNLE GCNEILNDTR PDVLEGIHRA YFEAGADAVE TNTFGCNLSN LGDYDIADRI RELAYKGTAI ARGVADEMGP SADGTGRYVL GSMGPGTKLP SLGHTTFATI RDAYQECVIG MLEGGADAVL IETSQDLLQV KAAVIAAQRA MDRVGRRIPI ISHVTVETTG TMLLGSEIGA ALAAIEPLGV DLIGLNCATG PAEMSEHLRY LSKHARIPVS VMPNAGLPVL GANGAEYPLT PEELAESMAQ FVGEFGLSFV GGCCGTTPEH IRQVAEAVAQ VTPATRTPEH ESETSSLYTA VPFDQDASFL VIGERTNTNG SKAFREAMIA EDYQRCLDIA KDQTRDGAHM LDLNVDYVGR DGAADMTALA SRFATSSTLP IMLDSTEPEV IRAGLEALGG RCAVNSVNYE DGDGPDSRFN KIMQLVVEHG AAVVALTIDE EGQARTADWK VSVAERLIAD ITGNWGLAEE DIIIDALTFP ISTGQEEVRR DGIETIEAIR RLHETHPDVH FTLGISNISF GLNPAARQVL NSVFLHECVQ AGLDTAIVHA SKILPMARIP EEHRQVALDL VYDRRREGYD PLQKLMELFE GVSAASARES RAQELAKLPL FERLERRIVD GERNGLTDDL DEAMTQVPPL SIINDTLLSG MKTVGELFGS GQMQLPFVLQ SAEVMKAAVA HLEPHMEATG EDGKGRIVLA TVKGDVHDIG KNLVDIILSN NGYEVVNIGI KQPIATILDV AADKRVDVIG MSGLLVKSTV VMKENLEEIN TRGLADEYPV LLGGAALTRS YVENDLSDVY EGDVHYARDA FEGLRLMDDI MARKRGGGPD PDSDEAKAEA AKTAERKARH ERSKRIAAKR KAAEEPVEVP SRSDVAADNE IPTPPFWGSR IVKGVPIADY LQLLDERALF LGQWGLRGAR GGDGPSYEEL VESEGRPRLR YWIDRLATEN ILQHAAVVYG YYPAVSEGDT VHVLTEPDPD APVRFSFSFP RQQRSRFLCI ADFIQSREAA KAAGRVDVMP FQLVTMGQPI ADFANKLFAE DAYRDYLEVH GIGVQLTEAL AEYWHQRVRS ELKFGDRSMD SEDPEHAQGF FDLEYRGARF SFGYGACPDL EDRAKMIELL EPERIGVQLS EELQLHPEQS TDAFVLHHPE AKYFNT // ID F9WHU3_TRYCI Unreviewed; 432 AA. AC F9WHU3; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 07-JAN-2015, entry version 14. DE SubName: Full=WGS project CAEQ00000000 data, annotated contig 695 {ECO:0000313|EMBL:CCD16888.1}; GN ORFNames=TCIL3000_0_17710 {ECO:0000313|EMBL:CCD16888.1}; OS Trypanosoma congolense (strain IL3000). OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Trypanosoma; OC Nannomonas. OX NCBI_TaxID=1068625 {ECO:0000313|EMBL:CCD16888.1, ECO:0000313|Proteomes:UP000000702}; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IL3000; RA Jackson A.P., Berry A., Allison H.C., Burton P., Anderson J., RA Aslett M., Brown R., Corton N., Harris D., Hauser H., Gamble J., RA Gilderthorp R., McQuillan J., Quail M.A., Sanders M., van Tonder A., RA Ginger M.L., Donelson J.E., Field M.C., Barry J.D., Berriman M., RA Hertz-Fowler C.; RT "Divergent evolution of antigenic variation in African trypanosomes."; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000000702} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IL3000 {ECO:0000313|Proteomes:UP000000702}; RA Jackson A.P., Berry A., Allison H.C., Burton P., Anderson J., RA Aslett M., Brown R., Corton N., Harris D., Hauser H., Gamble J., RA Gilderthorp R., McQuillan J., Quail M.A., Sanders M., Van Tonder A., RA Ginger M.L., Donelson J.E., Field M.C., Barry J.D., Berriman M., RA Hertz-Fowler C.; RT "Divergent evolution of antigenic variation in African trypanosomes."; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:CCD16888.1, ECO:0000313|Proteomes:UP000000702} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IL3000 {ECO:0000313|EMBL:CCD16888.1, RC ECO:0000313|Proteomes:UP000000702}; RX PubMed=22331916; DOI=10.1073/pnas.1117313109; RA Jackson A.P., Berry A., Aslett M., Allison H.C., Burton P., RA Vavrova-Anderson J., Brown R., Browne H., Corton N., Hauser H., RA Gamble J., Gilderthorp R., Marcello L., McQuillan J., Otto T.D., RA Quail M.A., Sanders M.J., van Tonder A., Ginger M.L., Field M.C., RA Barry J.D., Hertz-Fowler C., Berriman M.; RT "Antigenic diversity is generated by distinct evolutionary mechanisms RT in African trypanosome species."; RL Proc. Natl. Acad. Sci. U.S.A. 109:3416-3421(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. {ECO:0000313|EMBL:CCD16888.1}. 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; CAEQ01002487; CCD16888.1; -; Genomic_DNA. DR Proteomes; UP000000702; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 3. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000702}; KW Reference proteome {ECO:0000313|Proteomes:UP000000702}. SQ SEQUENCE 432 AA; 47664 MW; FF901CDCFC4087ED CRC64; MEGKSNNTSH GDGSSVNEPR KRPNFFVLDG AMGTEIEERR PDLLPLGPMW SASVVHKEPS AVQSVHEAYV NAGADILLTS TYQINTKGCA TLGVAIPDLV DAAVRLLRNS ITPERTSATE QAKAKAKLDP SVKRRGASAV FAPLLYGIRD DPSKCPVLIG GSMSPYGSLA GYGQEYHGKY TVDETIIDEF YNQRVRAFID YTSDTPRPKV DFLMLETFPL LKEAVGVFSW LSHQRDGVLD TAPVCISFVS VLDGDRPSAD ADDAAVEEWW NSAESSIHLP DGNTYLQVLD TLMELRSPQL AGLGANCCSP LEVSVVASLL LKKKKKHVED PSLVLLLYSN SGEEFTEGEW RWRHKFERGS RLSKWKRGTV VPQQELRRMM LAADVDVQLC GLFAYQTLLQ RPEADDWLFD IVICGGCCRS NPKDIAKIRA LA // ID F9WYI9_ZYMTI Unreviewed; 437 AA. AC F9WYI9; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 04-MAR-2015, entry version 22. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGP91947.1}; GN ORFNames=MYCGRDRAFT_107675 {ECO:0000313|EMBL:EGP91947.1}; OS Zymoseptoria tritici (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 {ECO:0000313|EMBL:EGP91947.1, ECO:0000313|Proteomes:UP000008062}; RN [1] {ECO:0000313|EMBL:EGP91947.1, ECO:0000313|Proteomes:UP000008062} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062}; RX PubMed=21695235; DOI=10.1371/journal.pgen.1002070; RA Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., RA Crane C.F., Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., RA Aerts A., Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., RA van der Burgt A., Canto-Canche B., Churchill A.C.L., 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.H.J., 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.H., Ponomarenko A., Rudd J.J., Salamov A., RA Schmutz J., Schouten H.J., Shapiro H., Stergiopoulos I., RA Torriani S.F.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.J.; 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; CM001196; EGP91947.1; -; Genomic_DNA. DR RefSeq; XP_003856971.1; XM_003856923.1. DR EnsemblFungi; Mycgr3T107675; Mycgr3P107675; Mycgr3G107675. DR GeneID; 13398682; -. DR KEGG; ztr:MYCGRDRAFT_107675; -. DR InParanoid; F9WYI9; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000008062; Chromosome 1. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008062}; KW Reference proteome {ECO:0000313|Proteomes:UP000008062}. SQ SEQUENCE 437 AA; 48404 MW; D24C6F131F55E596 CRC64; MARWLTFSTR QFDCTTDHKG RLGIVTLLIL LHVHANNIVL PVLLSTLIAK AERKMLSQKE FESVLEARGT LILDGALATE LEVRGHDLNH PLWSAKILKD DPASIEEVHV DYYLAGADVA ITASYQAATL GLTEHFNMTE DESKALIKRS VSVAQSARSK AYASGIDSSR RLLVAGSVGP YGAYLSNGSE YRGDYARTEK EFQDFHRPRI QALINAGADL LAIETIPSIS EIQTILALLR SDFPDAIAWL SCTAHSAETL CDQTPWEDVL RLVEDHRDQI IGFGINCVPM AMADATLKYL SQLTSIPLVC YPNSGEVWDA VTKTWHGERP DEALTSEQSS ANDKALALEF DQWSKNGARM IGGCCRTQTW TTSLTYDPKR TGQNIWILSR EKSLRLTCWP GRLHAIDMNC EAPPRQLASK LKMELLACGA KRADIES // ID F9X919_ZYMTI Unreviewed; 309 AA. AC F9X919; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 04-MAR-2015, entry version 22. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGP88015.1}; GN ORFNames=MYCGRDRAFT_109163 {ECO:0000313|EMBL:EGP88015.1}; OS Zymoseptoria tritici (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 {ECO:0000313|EMBL:EGP88015.1, ECO:0000313|Proteomes:UP000008062}; RN [1] {ECO:0000313|EMBL:EGP88015.1, ECO:0000313|Proteomes:UP000008062} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062}; RX PubMed=21695235; DOI=10.1371/journal.pgen.1002070; RA Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., RA Crane C.F., Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., RA Aerts A., Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., RA van der Burgt A., Canto-Canche B., Churchill A.C.L., 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.H.J., 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.H., Ponomarenko A., Rudd J.J., Salamov A., RA Schmutz J., Schouten H.J., Shapiro H., Stergiopoulos I., RA Torriani S.F.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.J.; 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; CM001199; EGP88015.1; -; Genomic_DNA. DR RefSeq; XP_003853039.1; XM_003852991.1. DR EnsemblFungi; Mycgr3T109163; Mycgr3P109163; Mycgr3G109163. DR GeneID; 13397360; -. DR KEGG; ztr:MYCGRDRAFT_109163; -. DR InParanoid; F9X919; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000008062; Chromosome 4. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008062}; KW Reference proteome {ECO:0000313|Proteomes:UP000008062}. SQ SEQUENCE 309 AA; 33402 MW; 573D3070E38AB65B CRC64; MQSQRVMILD GGMSRELIRL EAPFRQPEWS ALALLEAPRF VRKVHDGFAA AGADVITTNT YALVPFHIGE ERFRDRGEEL AALAGRLARE TADSDAGRGK RVAGSLPPMF GSYEPQLYKP ELVQERLAVL VKGLGPYIDL WLGETLSLIA EAEAVRVAIH DSGKPLWIAF TLDDARADTA SAAPRLRSGE SVADAARWAL DAGVEALLFN CSQPEYMDAA VKDAHDVFSE ESGARSVPLI GVYANAFQAK DTDTAANESI SETRSELTPD LYLDFAQRWT SSGATIVGGC CGIGCETIAK MSDTFKAKS // ID F9Y766_KETVW Unreviewed; 1242 AA. AC F9Y766; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=Dihydropteroate synthase, DHPS:Homocysteine S-methyltransferase:Cobalamin-dependent methionine {ECO:0000313|EMBL:AEM42256.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEM42256.1}; GN Name=metH {ECO:0000313|EMBL:AEM42256.1}; GN OrderedLocusNames=KVU_2418 {ECO:0000313|EMBL:AEM42256.1}; OS Ketogulonicigenium vulgare (strain WSH-001). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Ketogulonicigenium. OX NCBI_TaxID=759362 {ECO:0000313|EMBL:AEM42256.1, ECO:0000313|Proteomes:UP000000692}; RN [1] {ECO:0000313|EMBL:AEM42256.1, ECO:0000313|Proteomes:UP000000692} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WSH-001 {ECO:0000313|EMBL:AEM42256.1, RC ECO:0000313|Proteomes:UP000000692}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002018; AEM42256.1; -; Genomic_DNA. DR RefSeq; WP_014538096.1; NC_017384.1. DR RefSeq; YP_005796252.1; NC_017384.1. DR EnsemblBacteria; AEM42256; AEM42256; KVU_2418. DR GeneID; 12375356; -. DR KEGG; kvl:KVU_2418; -. DR KO; K00548; -. DR BioCyc; KVUL759362:GLEX-2528-MONOMER; -. DR Proteomes; UP000000692; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000692}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEM42256.1}; KW Transferase {ECO:0000313|EMBL:AEM42256.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 257 257 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 320 320 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 773 773 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1242 AA; 135764 MW; 0FEA85CDF7F2DA7D CRC64; MTALPKSASF ARIVDAARQR ILVLDGAMGT QIQLLKMGED EYLGHGSAGC QCHIHSDHPQ KGNNDLLNLT QPEAIEEIHF RYAMAGADIV ETNTFSSTTI AQADYALEDQ VHALNVQGAR LARSGVDRAT AIDGRMRFVA GAVGPTNRTA SISPDVNDPG FRAVSFDDLR IAYAQQIRGL IEGGVDLILI ETIFDTLNAK AAIFAAEEVF IEIGERLPVM ISGTITDLSG RTLSGQTPTA FWHSVRHAGP FTIGLNCALG ANAMRAHLAE ISAIADTFVC VYPNAGLPNA MGDYDETPAF TAQQIEGFAR DGLVNIVGGC CGTSPEHIRA MAEAVAKYRP RAIPEHAPLM RLSGLEPFIL TPEIPFVNVG ERTNVTGSAK FRKMITAGDF ASALQVARDQ VENGAQIIDI NMDEGLIDSQ AAMVKFLNLV ASEPDIARVP VMIDSSKWDV IEAGLKCVQG KAIVNSISMK EGEAAFLHHA RLCRAYGAAV VVMAFDETGQ ADTEDRKVEI CSRAYKLLTE EVGFPPEDII FDPNVFAVAT GIEEHNNYGV DFINATRRIM EACPHVHISG GISNLSFSFR GNEPVREAMH AVFLYHAIQV GMDMGIVNAG QLAVYDQIDP ELREACEDVV LNRRDDATER LLDLAERYRG QGGAEKKERD LAWRDWDVAK RLEHALVNGI TEFIEGDTEE ARLAAQRPLH VIEGPLMDGM NVVGDLFGAG KMFLPQVVKS ARVMKQAVAV LLPYLEEEKA AGGGVGRQSA GKILMATVKG DVHDIGKNIV GVVLACNNYD IIDLGVMVSS EKILAAAREH DVDAIGLSGL ITPSLDEMVH VAAEMERQGF DIPLLIGGAT TSRVHTAVKI APAYQRGQVV YSVDASRAVG VAQNLLGSRS LAYQAEVRAE YEKVAEGYLR GEREKQRLPL ADARANPVKI DWAAYQAKVP SFLGTKVYDD WDLADLAQYI DWTPFFQSWE LKGVYPRILQ DEKYGETARS LFADAQAMLQ QIIDEKWFDP RAVVGFWPAN AVGDDIVLFA DETRSHILAT MHTLRQQLPR RDGRPNIAMS DFVAPMGQAE YIGGFVVTAG FKELEIAARF EAANDDYNAI MVKALADRFA EAFAERMHQH VRRELWAYAA DEVLPNDALI REEYAGIRPA PGYPAQPDHT EKLTLFRLLD AEAATGVKLT ESMAMWPGST VSGLYIAHPE SYYFGVAKVE EDQVADYAAR KGMDKAEAER WLAPILNYIP KA // ID F9ZAP2_ODOSD Unreviewed; 1172 AA. AC F9ZAP2; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 01-APR-2015, entry version 24. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADY34368.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADY34368.1}; GN OrderedLocusNames=Odosp_3416 {ECO:0000313|EMBL:ADY34368.1}; 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 {ECO:0000313|EMBL:ADY34368.1, ECO:0000313|Proteomes:UP000006657}; RN [1] {ECO:0000313|EMBL:ADY34368.1, ECO:0000313|Proteomes:UP000006657} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29572 / DSM 20712 / JCM 15291 / NCTC 10825 / 1651/6 RC {ECO:0000313|Proteomes:UP000006657}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002544; ADY34368.1; -; Genomic_DNA. DR RefSeq; WP_013613555.1; NC_015160.1. DR RefSeq; YP_004254548.1; NC_015160.1. DR EnsemblBacteria; ADY34368; ADY34368; Odosp_3416. DR KEGG; osp:Odosp_3416; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; OSPL709991:GI68-3481-MONOMER; -. DR Proteomes; UP000006657; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006657}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADY34368.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006657}; KW Transferase {ECO:0000313|EMBL:ADY34368.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 236 236 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 752 752 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1172 AA; 128479 MW; 3B7B1910B251AB19 CRC64; MIQDEIKKRI LILDGAMGTA IQQYGLTEAD FRGSEFISHP VNLKGNNDIL NLTCPEVIRQ IHRSYIEAGA DIIETNTFNS NAISQAEYRG EKLVYRLNYA GAKLAVTEAR AASHQVYVAG SMGPTSKTLS LSPDVNRPEF RPVDFDTLVS TYAEQVSGLI DGGVDLLLVE TVFDGLNAKA ALYAITQVQE EKRTSLPVML SATINDRSGR TLTGQSLEAL YTTVSHYPLF SFGLNCSFGA TDLLPFIERL SKTLPCPLSI YPNAGLPNEM GEYDESPELT ASCLKQMATA GLLNIAGGCC GTTPEHIRAI REALQAISPR QIPAIPAQLV VSGLDKVVVD KAQNNFINVG ERTNVAGSAK FAKLIHAKAY EEAARIARKQ IEDGASVIDI NMDDAMLDSA LEMSTFVRYI SNDPDIARAA LMIDSSDWNT ILAGLKNAQG KCIVNSISLK EGEDLFLAKA REIHHLGAAV VVMAFDEQGQ AVTYERKIEI CERAYRLLTR QAGFRAEDII FDVNILAIGT GLEEHNNYAV DFIRAIAWIK ANLPGCRTSG GISNLSFSFR GNNPVREAMH SVFLYHAIEA GMDMGIVNPA MLQVYDEIEP QLLEAVEEVV LNKHPEATER LIELAEQIKG QKTADGKAIK NEEWRTRTLS ERLNFALIKG NTEYLEADLA EALTVYASPV EIIEGPLMQG MDKVGTLFGE GKMFLPQVVK SAKAMKAAVA ILQPEIEKHN AGTGENIQRP KVVLATAKGD VHDIGKNIVS IVLTCNNFDV IDLGVMVDNQ KIVAAAKAHQ ADLIGVSGLI TPSLSEMEAL CELLQKEQLR IPLIVGGATT STVHTAVKLA PRYDYGVIQG GDASRTAGIM KRLLSDRSSY LAQVKAEQEK IRGQYYHKQD RLLPYTEAQA LAPVFDRESY RLPASFGEHN LLGKNMDLQD LIAKIDWTPF FHFWGFKGKF PEIIHQHEEA DRTYQAALEM LGTVIAGNEF EASIVVNFFD AYAEDDEIVL DNGHRLPMLR QQKAGQECLS LSDYICPKAY GTSTIGLFAL KVADKQGGCD CHDFSHLLRE SLCARLTEAL AEWMQEQLSE GLSLIRPAFG YSACPDHSLK KDVFDLLDAP SKIGVSLTTS YAIYPTTSLC GMLIAHPAAR YFSIGKIGAD QLTDYCTKRA ITLEEGKRLL GL // ID F9ZCU6_9PROT Unreviewed; 1236 AA. AC F9ZCU6; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 01-APR-2015, entry version 24. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ADZ25383.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADZ25383.1}; GN ORFNames=NAL212_0438 {ECO:0000313|EMBL:ADZ25383.1}; OS Nitrosomonas sp. AL212. OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Nitrosomonadaceae; Nitrosomonas. OX NCBI_TaxID=153948 {ECO:0000313|EMBL:ADZ25383.1, ECO:0000313|Proteomes:UP000001629}; RN [1] {ECO:0000313|EMBL:ADZ25383.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AL212 {ECO:0000313|EMBL:ADZ25383.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002552; ADZ25383.1; -; Genomic_DNA. DR RefSeq; WP_013646450.1; NC_015222.1. DR RefSeq; YP_004293545.1; NC_015222.1. DR EnsemblBacteria; ADZ25383; ADZ25383; NAL212_0438. DR KEGG; nit:NAL212_0438; -. DR KO; K00548; -. DR BioCyc; NSP153948:GHZ8-275-MONOMER; -. DR Proteomes; UP000001629; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001629}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ADZ25383.1}; KW Transferase {ECO:0000313|EMBL:ADZ25383.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 249 249 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 315 315 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 767 767 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1236 AA; 136138 MW; 8566956C685EEBDB CRC64; MTRDSRTALL KSLFAQRILI LDGAMGTMIQ TFKLSEADFR GQRFAAFPHD LRGNNDLLTL TQPNIIRSIH SGYLEAGADI IETNTFNSTA ASMADYHLQD VVYELNVAAA KLACEAARVY EEKTPDKPRF VAGVLGPTTK TASISPDVND PGFRGITFDQ LVADYTESIH GLVDGGVDIL LVETIFDSLN AKAALFAIDQ YFEDHDIRLP IMISVTITDA SGRTLSGQTP EAFWNSISHT RPLSVGINCA LGAELMRPYI EELAGVADVY TSVHPNAGLP NPLSETGYDE SPEYTANQIK GFAESGFVNI VGGCCGTTPA HIKAIAQAVA NIAPRQVLEI PKKLRLSGLE PLNIGDDSLF VNVGERTNVT GSRAFARLIL NDDYAEALNV ARSQVENGAQ IIDINMDEAM LDSQKAMVTF LNLLAAEPDI CKVPIMLDSS KWTVIEAGLK CVQGKPVINS ISMKEGEAEF FHHAKLARRY GAAVIVMAFD EQGQADTLQR KVEICNRSYR LLVDKIGFPP EDIIFDPNIF AIATGIEEHN NYGVDFIEAT RIIKQALPYA KVSGGVSNVS FSFRGNEPIR EAIHTAFLYH AVKAGMTMGI VNAGQLGVYS DIPAELLEKV EDVILNRRTD ATERLVEFAE NFKGQKKEQI EDLAWRDEPL QQRLTHALVK GISTFIVEDT EAARLEIDKQ GGRPIQVIEG PLMEGMSVVG DLFGAGKMFL PQVVKSARVM KQAVAHLLPF IEAEKKLSGD NKPKGKIVIA TVKGDVHDIG KNIVTVVLQC NNYEVINMGV MVPSAQILDM ARREKADIIG LSGLITPSLE EMAHVAKEMQ REGFTIPLLI GGATTSRVHT AVKIAPHYEG PTVWVPDASR AVGVCSNLLS QDLQVNYVQE IKDEYEKVRT QHKNKKGPAK LLTLAEARAN AFKTDWMNYH PYQPELIGIR TLNNYPLEKI VPYIDWTPFF QAWELAGRYP DILQDEVVGE TASQLFRDAQ TMLKKIIEQK WLSANAVIGL FPANSVGDDI EIYTDPSRNK LAMTYHCLRQ QDQKPSGKPN RCLSDFIAPR ETGIQDTIGL FAVGAGFGID ERVKAFEDAN DDYSAIVLKA LADRLAEAFA EHMHARVRRE FWGYAKDETL TNTQLINEEY RGIRPAPGYP ACPDHTEKGA LFSTLSATEN AGIIITESFA MVPTAAVSGF YFAHPDSTFF AVGKIGKDQV EDYAKRKGWA VEEAERWLAP VLAYER // ID G0A5L1_METMM Unreviewed; 1223 AA. AC G0A5L1; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEG02868.1}; GN OrderedLocusNames=Metme_4529 {ECO:0000313|EMBL:AEG02868.1}; OS Methylomonas methanica (strain MC09). OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales; OC Methylococcaceae; Methylomonas. OX NCBI_TaxID=857087 {ECO:0000313|EMBL:AEG02868.1, ECO:0000313|Proteomes:UP000008888}; 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] {ECO:0000313|Proteomes:UP000008888} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC09 {ECO:0000313|Proteomes:UP000008888}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002738; AEG02868.1; -; Genomic_DNA. DR RefSeq; WP_013821081.1; NC_015572.1. DR RefSeq; YP_004515367.1; NC_015572.1. DR EnsemblBacteria; AEG02868; AEG02868; Metme_4529. DR KEGG; mmt:Metme_4529; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; MMET857087:GH4A-4579-MONOMER; -. DR Proteomes; UP000008888; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008888}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008888}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 246 246 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1223 AA; 135511 MW; 3B5AD19E78168272 CRC64; MNSIQRLNQQ LKQRILYLDG AMGTMIQSYK LGEKDYRGTR FADWTSDLKG NNDLLSLTQP DIIKAIHKAY LEAGSDIIET NTFNATKIAM ADYHMEDLAY EINVASARLA KQAAEEISAL TPDKPRFVAG VLGPTNRTSS MSPDVNDPGF RNITFDDLVD AYSEATQGLI DGGADIILIE TVFDTLNAKA AIFAVENTFD KLGYKLPVMI SGTITDASGR TLSGQTAAAF WTSLKHVKPI SIGFNCALGA QELRQYIEEL SNIADTYVSA HPNAGLPNEF GEYDETPEQM AAELADWAAS GYLNIIGGCC GTSPDTIRAI VEAVGKYPPR QIPELEKRCH LAGLEAMSIG PETLFVNVGE RTNVTGSAIF KKMIIEERYE DALEVAKQQV ENGAQIIDIN MDEGMLDSKA AMVRFLNLLA AEPDIAKVPI MLDSSKWEIL EAGLKCIQGK GVVNSISIKE GEEAFIKHAK LVRRYGAAVI VMAFDEQGQA DTMQRKIEIC TRAYKILTEQ IGFPPEDIIF DPNIFAVATG IEEHNNYGVD FIEATRIIKQ TLPHALISGG VSNVSFSFRG NNPVREAIHA VFLYHAIQAG MDMGIVNAGQ LAIYADIPSE LRDTVEDVIL NRTPEGTEKL LEIAEKYRGT GQVAKQETLE WREWPVSKRL EHALVKGIAD YIDEDTEQAL QEAEKPLHVI EGPLMDGMNV VGDLFGEGKM FLPQVVKSAR VMKKAVAYLM PFMDAEVDGS VRQTNGKVLM ATVKGDVHDI GKNIVAVVLQ CNNYEVIDLG VMVPADTILK TAREEKVDVI GLSGLITPSL DEMVHVAKEM QRQGFTIPLM IGGATTSRAH TAVKIEPNYQ HPTIYVTDAS RSVGVVSALL SEDQKAEFVE KTRAEYEQVR ERHKGRHAKN PQLDLQKARH NKFDFAGYRP VKPKFLGIQV IDHFPLDSLV SYIDWTPFFQ TWELSGRYPA ILSDQVVGIE ASKLFADAQA MLKQLVDEQW LTAKAVIGFF PANSIDDDIV LYTDDSRTQQ RDVLHHLRQQ NVKAPGRPNY CLSDFIAPVG SGIADYMGGF AVTAGIGIET KLAEFEKDHD DYSSIMLKAL ADRLAEAFAE CMHQKVRKEY WGYAAEETHD NHDLIEEAYQ GIRPAPGYPA CPDHTEKAKL FELLNVTEST TIELTENFAM YPTAAVSGWY FSHPESQYFN VGKIDQDQLQ DYAKRKGINL EVAERWLAAH LHH // ID G0AFF3_COLFT Unreviewed; 1253 AA. AC G0AFF3; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 29-APR-2015, entry version 24. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AEK63961.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEK63961.1}; GN Name=metH {ECO:0000313|EMBL:AEK63961.1}; GN OrderedLocusNames=CFU_4139 {ECO:0000313|EMBL:AEK63961.1}; OS Collimonas fungivorans (strain Ter331). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae; Collimonas. OX NCBI_TaxID=1005048 {ECO:0000313|EMBL:AEK63961.1, ECO:0000313|Proteomes:UP000008392}; RN [1] {ECO:0000313|Proteomes:UP000008392} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ter331 {ECO:0000313|Proteomes:UP000008392}; RA Leveau J.H.; RT "Complete sequence of Collimonas fungivorans Ter331."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002745; AEK63961.1; -; Genomic_DNA. DR RefSeq; WP_014008113.1; NC_015856.1. DR RefSeq; YP_004754784.1; NC_015856.1. DR EnsemblBacteria; AEK63961; AEK63961; CFU_4139. DR KEGG; cfu:CFU_4139; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; CFUN1005048:GJNH-4180-MONOMER; -. DR Proteomes; UP000008392; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008392}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEK63961.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008392}; KW Transferase {ECO:0000313|EMBL:AEK63961.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 261 261 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 326 326 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 327 327 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 784 784 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1253 AA; 137837 MW; 22DA6E4D31A2054B CRC64; MTPTASTSTV STETRLRELL AQRILILDGA MGTMIQQYKL TEEDYRGGPK GRFIDFTGPG RELFVKGNNE LLSLTQPHII SAIHEEYLAA GADLIESNTF GATTVAQDDY HMAHLAYEMN VASARLARAA CDKYSTPDKP RFVAGALGPT PKTASISPDV NDPAARNVTF DQLVASYLEQ TRGLVEGGAD VLLVETIFDT LNCKAALFAI DTFFEESGLR LPIMISGTVT DASGRILSGQ TVPAFWNSIR HAKPLTVGLN CALGAALMRP YAEELSKIAD TFVCIYPNAG LPNPMSDTGF DETPDVTSSL LKDFAESGFV NIAGGCCGTT PPHIKAIADT VARIPPRAVP ETTHEMRLSG LEPFTIDDSS LFVNVGERTN VTGSKAFARL ILNEQYDEAL AVARQQVENG AQVIDINMDE AMLDSMAAMQ RFLNLIASEP DIARVPIMID SSKWTVIEAG LKCVQGKAIV NSISMKEGEP EFLRQAKLCR RYGAAVIVMA FDEKGQADTF ERKIEICERA YRLLVDQIGF PPEDIIFDPN IFAIATGIEE HNNYAVDFIN ATRWIRENLP HAKISGGVSN VSFSFRGNDP AREAIHTVFL YHAIKAGMTM GIVNAGMMGV YDNLPAELRE RVEDVVLNRR EDATERMIEI ASTLKAGDKK EEATLEWRSG TVQQRLAHAL VQGITQWIVE DTEEARQELL NNGGRPIHVI EGPLMDGMNI VGDLFGQGKM FLPQVVKSAR VMKQAVAHLI PYIEEEKRLH EELTGIAAKP KGKIVIATVK GDVHDIGKNI VSVVLQCNNF EVVNMGVMVP CSEILAMAKA ENADIIGLSG LITPSLEEMA HVAKEMQRDP YFRSVKMPLL IGGATTSRAH TAVKIAPNYE GPVVYVPDAS RSVSVAQSLL TPEQRDQYID EIAVDYERIR EQHANKKAVP LLTLAAAREN RTRLQFAPVK PKFIGRRVFK NVDLGTLARY IDWGPFFQTW DLAGPYPAIL KDEVVGEAAS KVFEEGQALL KKLIDGRWLI ANGVIALMPA NTVNDDDIEI YTDHTREKVA FTYYGLRQQT VKPVIDGVPR PNQCLSDFIA PKSSGIADYI GLFAVTSGIG IEKYEKRFED AHDDYSSIML KSLADRLAEA FAEYMHERVR KDLWGYVPDE SLSNEALIKE SYSGIRPAPG YPACPEHTVK ADMFQLLQCE EIGMQLTESF AMFPGAAVSG FYFAHPESKY FVVGKIGDDQ VSDMAARRGA GKDDVERWLA PNL // ID G0APY8_9GAMM Unreviewed; 300 AA. AC G0APY8; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AEG10539.1}; GN ORFNames=Sbal175_1262 {ECO:0000313|EMBL:AEG10539.1}; OS Shewanella baltica BA175. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=693974 {ECO:0000313|EMBL:AEG10539.1, ECO:0000313|Proteomes:UP000002249}; RN [1] {ECO:0000313|EMBL:AEG10539.1, ECO:0000313|Proteomes:UP000002249} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BA175 {ECO:0000313|EMBL:AEG10539.1}; 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; AEG10539.1; -; Genomic_DNA. DR RefSeq; WP_006082576.1; NC_017571.1. DR RefSeq; YP_006019845.1; NC_017571.1. DR EnsemblBacteria; AEG10539; AEG10539; Sbal175_1262. DR KEGG; sbb:Sbal175_1262; -. DR BioCyc; SBAL693974:GLK2-1308-MONOMER; -. DR Proteomes; UP000002249; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002249}; KW Methyltransferase {ECO:0000313|EMBL:AEG10539.1}; KW Transferase {ECO:0000313|EMBL:AEG10539.1}. SQ SEQUENCE 300 AA; 32035 MW; D13C23EA5ECBBECF CRC64; MDKQQLWVLD GGMGRELARR GAPFRQPEWS ALALIEAPQT VTEVHQAYVA SGAKVITTNS YALVPFHIGD ERFAAEGEAL AALAGKLAQD VADEHANSVR VAGSLPPLFG SYRADLFEAA RVSELALPLI RALSPSVDLW LAETMSLIAE PLAIKALLPE DGKPFWVSFT LEDETLGSEP TLRSGERVAD AIDALVAVGV DAILFNCCQP EVIEAALQVA SDRLSAQGRA DIRLGAYANA FPPQPKEATA NDGLDEIRAD LGPLDYLGWA ERWRAAGASL IGGCCGIGPE HIQALSTRLR // ID G0AZS9_9GAMM Unreviewed; 1244 AA. AC G0AZS9; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEG10281.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEG10281.1}; GN ORFNames=Sbal175_1004 {ECO:0000313|EMBL:AEG10281.1}; OS Shewanella baltica BA175. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=693974 {ECO:0000313|EMBL:AEG10281.1, ECO:0000313|Proteomes:UP000002249}; RN [1] {ECO:0000313|EMBL:AEG10281.1, ECO:0000313|Proteomes:UP000002249} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BA175 {ECO:0000313|EMBL:AEG10281.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002767; AEG10281.1; -; Genomic_DNA. DR RefSeq; WP_006082839.1; NC_017571.1. DR RefSeq; YP_006019587.1; NC_017571.1. DR EnsemblBacteria; AEG10281; AEG10281; Sbal175_1004. DR KEGG; sbb:Sbal175_1004; -. DR KO; K00548; -. DR BioCyc; SBAL693974:GLK2-1032-MONOMER; -. DR Proteomes; UP000002249; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002249}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEG10281.1}; KW Transferase {ECO:0000313|EMBL:AEG10281.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 258 258 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 774 774 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1244 AA; 138040 MW; 2ABF4BB75445C690 CRC64; MTIPSTKAGQ ILADIRKQLA ERILILDGAM GTMIQDHKLE EEDYRGERFK DWHTDVKGNN DLLVLSQPQI IKQIHTDYLN AGADIIETNT FNATTIAMAD YDMQSLSAEI NLAGARLARE ACDEVFAATG IPRYVAGVLG PTNRTCSISP DVNDPGYRNV SFDELVSAYR ESTKALIEGG ADIIMVETIF DTLNAKAALF AIESVFDDLF GQHSKDRLPI MISGTITDAS GRTLTGQTTE AFYNSLRHIK PLSIGLNCAL GPKELRPYVE ELSRIAECYV SAHPNAGLPN EFGGYDETPE DMANVIEDWA REGMLNIIGG CCGSTPEHIR VIREAVDRHN PRVLPDIPVA CRLAGLEPLT IDAQSLFVNV GERTNVTGSA KFLKLIKDGK FEQALDVARE QVESGAQIID INMDEGMLDG AEIMHKFLNL IASEPDISRV PIMIDSSKWE VIEAGLKCIQ GKGIVNSISL KEGEAKFIEQ ATLVKRYGAA AIIMAFDEQG QADTKARKIE ICTRAYRVLV DKVGFPPEDI IFDPNIFAIA TGIDEHDNYA VDFIDAIKAI KATLPHAMIS GGVSNVSFSF RGNNPVREAI HAVFLYHAIK VGMDMGIVNA GQLAIYDDID PELKVRVENV VLNLPCPVEG SSNTEQLLEI AEKFRGDGAQ VGKKEDLEWR SWPVSQRLSH ALVKGITEFI DEDTEAARQE AKRPLDVIEG ALMDGMNVVG DLFGSGKMFL PQVVKSARVM KKAVAYLNPY IELEKVEGQS NGKILMVTVK GDVHDIGKNI VGVVLACNGF EVFDLGVMVS VERILDAVKE HNIDIIGMSG LITPSLDEMV HNVKTFHREG LTIPAIIGGA TCSKIHTAVK IAPHYPHGAI YIADASRAVP MVSKLINNET RQATIDETYT EYDDMRTKRL SQAKRKEIVS LEAARDNRCQ HDWANYTPFT PNVLGRQVFD NYPLEDLVER IDWTPFFRSW ELHGHYPEIL TDKVVGEEAQ KLFADGHAML KQIIEEKWLT AKAVIGLFPA NTVNYDDIEL YTDESRTTVE MTTHHLRMQL ERVGNDNFCL SDFVAPKDSG VADYMGGFAV TTGHGIDEHV ARFEANHDDY NAIMLKCLAD RLAEAFAERM HERVRKEFWG YAADEQLSNE ALIREKYKGI RPAPGYPACP DHTEKGLLWD LLKPDETIDL NITESYAMFP TAAVSGWYFA HPKSRYFGVS NIGRDQVEDY AKRKGMTVAE TEKWLAPVLD YDPE // ID G0C9F0_XANCA Unreviewed; 379 AA. AC G0C9F0; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEL06677.1}; GN ORFNames=XCR_1780 {ECO:0000313|EMBL:AEL06677.1}; OS Xanthomonas campestris pv. raphani 756C. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=990315 {ECO:0000313|EMBL:AEL06677.1, ECO:0000313|Proteomes:UP000001633}; RN [1] {ECO:0000313|EMBL:AEL06677.1, ECO:0000313|Proteomes:UP000001633} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=756C {ECO:0000313|EMBL:AEL06677.1}; 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 ----------------------------------------------------------------------- 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; AEL06677.1; -; Genomic_DNA. DR RefSeq; WP_014507353.1; NC_017271.1. DR RefSeq; YP_005636795.1; NC_017271.1. DR EnsemblBacteria; AEL06677; AEL06677; XCR_1780. DR KEGG; xcp:XCR_1780; -. DR KO; K00548; -. DR BioCyc; XCAM990315:GLMR-1777-MONOMER; -. DR Proteomes; UP000001633; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001633}. SQ SEQUENCE 379 AA; 40459 MW; D272565E1CC4ABF8 CRC64; MTHLPIPTAE SPTPFSLPWL HPERAAKLTA ALRERILIID GAMGTMIQRH DLQESDYRGT RFAEGYDSAQ GHVHGAGCDH APQGHDLKGN NDLLLLSSPE IIAGIHRAYL DAGADLLETN TFNATSVSQA DYHLEHLVYE LNKAGAQVAR ACCDAVEALT PQKPRFVIGV LGPTSRTASI SPDVNDPGYR NTSFDALRET YREAIDGLID GGADTLMVET IFDTLNAKAA LYAIEEVFEA RGGRLPVMIS GTITDASGRT LSGQTAEAFY ASVAHGKPLS VGLNCALGAK ELRPHVETLS QIADAYVSAH PNAGLPNAFG EYDETPEEMA ETLREFAKSG LLNLVGGCCG TTPDHIRAIA EAVADLPPRQ LPNALEQAA // ID G0CKH4_XANCA Unreviewed; 320 AA. AC G0CKH4; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AEL06509.1}; GN ORFNames=XCR_1610 {ECO:0000313|EMBL:AEL06509.1}; OS Xanthomonas campestris pv. raphani 756C. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=990315 {ECO:0000313|EMBL:AEL06509.1, ECO:0000313|Proteomes:UP000001633}; RN [1] {ECO:0000313|EMBL:AEL06509.1, ECO:0000313|Proteomes:UP000001633} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=756C {ECO:0000313|EMBL:AEL06509.1}; 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 ----------------------------------------------------------------------- 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; AEL06509.1; -; Genomic_DNA. DR RefSeq; WP_014507217.1; NC_017271.1. DR RefSeq; YP_005636627.1; NC_017271.1. DR EnsemblBacteria; AEL06509; AEL06509; XCR_1610. DR KEGG; xcp:XCR_1610; -. DR KO; K00547; -. DR BioCyc; XCAM990315:GLMR-1608-MONOMER; -. DR Proteomes; UP000001633; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001633}; KW Methyltransferase {ECO:0000313|EMBL:AEL06509.1}; KW Transferase {ECO:0000313|EMBL:AEL06509.1}. SQ SEQUENCE 320 AA; 33726 MW; 327AAC3E4F76E706 CRC64; MTVVPRQPRV GAPFSDVLQR DGEVVLDGAL ATELEQRGCD LNDALWSARV LMEQPELIYQ VHRDYFAAGA QCAITASYQA TPQGFAARGL GLAQSQALIA RSVALAAQAR ADHLAAHPQA APLWVAGSVG PYGAYLADGS EYRGDYALPV AQMLDFHRPR IAALVDAGVD LLACETLPSA SEITALRLLL EEFPQVHAWF SFTLRDAAHL SDGTPLAQVI PALDACPQVV AVGINCIAIE QVTAALQSLA ALTSLPLVVY PNSGEHYDAS DKRWHAGTTA ACSLATQRAQ WHAAGARLIG GCCRTTPADI AALVAARTAG // ID G0CTM5_CORUB Unreviewed; 1199 AA. AC G0CTM5; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=5-methyltetrahydrofolate--homocysteinemethyltransferase {ECO:0000313|EMBL:AEG83832.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEG83832.1}; GN Name=metH {ECO:0000313|EMBL:AEG83832.1}; GN OrderedLocusNames=CULC22_01122 {ECO:0000313|EMBL:AEG83832.1}; OS Corynebacterium ulcerans (strain BR-AD22). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=945712 {ECO:0000313|EMBL:AEG83832.1, ECO:0000313|Proteomes:UP000008887}; RN [1] {ECO:0000313|EMBL:AEG83832.1, ECO:0000313|Proteomes:UP000008887} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BR-AD22 {ECO:0000313|EMBL:AEG83832.1, RC ECO:0000313|Proteomes:UP000008887}; 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., RA 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002791; AEG83832.1; -; Genomic_DNA. DR RefSeq; WP_013911484.1; NC_015683.1. DR RefSeq; YP_004629751.1; NC_015683.1. DR EnsemblBacteria; AEG83832; AEG83832; CULC22_01122. DR KEGG; cul:CULC22_01122; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; CULC945712:GHG6-1146-MONOMER; -. DR Proteomes; UP000008887; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008887}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEG83832.1}; KW Transferase {ECO:0000313|EMBL:AEG83832.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 233 233 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 750 750 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1199 AA; 130976 MW; 59E21599C7FC9C64 CRC64; MTTATIPFRT DFLDAMKDRV LIGDGAMGTQ LQAFDLDVDK DFLGLEGCNE ILNVTRPDVV ARIHRSYFEA GADLVETNTF GCNLPNLADY GISERCRELA YEGVRIARAV ADELGPGRDG LRRFVLGSMG PGTKLPSLGH APFEELREYY AEAATGMIEG GADAILVETA QDLLQVKAAI HGCQQAFEKI GIQIPIVCHV TVETTGTMLL GSEIGAALTA LEPLGIDMIG LNCATGPDEM SEHLRFLSRN AGIPVSVMPN AGLPVLGKNG AEYPLSAREL AAALKSFVND YGLSMVGGCC GTTPSHISAV RDAIVGTVDV PAAQQAQRNP AAGDAVSSLY TSVNLTQETG ITMIGERTNA NGSKAFREAM LAADWETCVD IAKQQTRDGA HMLDLCVDYV GRDGRQDMAQ LASLLSTSST LPIMIDSTEP SVIQVGLEHL GGRCAVNSVN FEDGDGPDSR YQRIMRLVKQ HGAAVVALTI DEEGQARTAA QKVAIAERLI TDITQTWGLK EDDIIVDCLT FPISTGQEET RRDGIETIEA IRELKKRYPR IHTTLGLSNI SFGLNPAARQ VLNSVFLNEC IGVGLDSAIA HSSKILPMNK IDEEQRRVAL DMVYDRRTAD YDPLQTFMQL FEGVSASSAK DARAEALAAM PLFERIAQRV IDGEKTGIET DLDQAMAEKE PLRIINEDLL EGMKTVGELF GSGQMQLPFV LQSAETMKHA VAYLEQFMEA EDDTGGNGTI VIATVKGDVH DIGKNLVDII LSNNGFNVIN IGIKQPISNI LDAAKKHNAD AIGMSGLLVK STVIMKENLQ EMNAAEASHF PVILGGAALT RAYVEDDLTE VYNGNVYYAK DAFESLRLMQ EFMARIRGEG LDPNSPDAIK AAQKKAERKA RKERSKNIAA ERKAKAEPVV VPTRSQVSET SPLATPPFWG TRIVKGLNLS EYLPLLDERA LFMGRWGLKA TRGAAGPSYE ELVETEGRPR LRYWIDRLKA EKILDHAAVI YGYFPAVSEG DDVILLESPD PSAAEIARFT FPRQQRSKFL CIADFIQSRT RCLEQGTVDV FPLQLVTMGQ PIADFANELF AADNYRDYLE VHGVGVQLTE AMAEYWHARV RSELTLSDGS SAGDKDAKNL QRFFDLDYLG ARYSFGYGSC PNLEDRKTLV ELLDTQRIGV ELSEELQLHP EQSTDAFVLY HPEAKYFNV // ID G0EQI0_BRAIP Unreviewed; 874 AA. AC G0EQI0; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AEM22081.1}; GN OrderedLocusNames=Bint_1462 {ECO:0000313|EMBL:AEM22081.1}; OS Brachyspira intermedia (strain ATCC 51140 / PWS/A) (Serpulina OS intermedia). OC Bacteria; Spirochaetes; Spirochaetales; Brachyspiraceae; Brachyspira. OX NCBI_TaxID=1045858 {ECO:0000313|EMBL:AEM22081.1, ECO:0000313|Proteomes:UP000008522}; RN [1] {ECO:0000313|EMBL:AEM22081.1, ECO:0000313|Proteomes:UP000008522} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51140 / PWS/A {ECO:0000313|Proteomes:UP000008522}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002874; AEM22081.1; -; Genomic_DNA. DR RefSeq; WP_014487909.1; NC_017243.1. DR RefSeq; YP_005594661.1; NC_017243.1. DR EnsemblBacteria; AEM22081; AEM22081; Bint_1462. DR KEGG; bip:Bint_1462; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR BioCyc; BINT1045858:GL9O-1469-MONOMER; -. DR Proteomes; UP000008522; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008522}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEM22081.1}; KW Transferase {ECO:0000313|EMBL:AEM22081.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 237 237 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 751 751 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 874 AA; 96446 MW; 8D9C642FB233DEB4 CRC64; MSNTKEKLKE LIKEKYLIID GATGTELQKK EIKKEFWIID GNNIEGCNEI LNITAPNIMK EIHIDYLNAN ANIIKTNSFG AIPWVLSEYD IADKAYELAK SAALIANDAR EEYLKNPNSK GDLNRDVFIA GSLGPGVKLP SLGQISFDEM YNGYIEAAKG LIDGGVDIIL LETAQDVLQL KAAILAVNDT AKKLNKEIPI MVSVTIEKEG TMLLGTDIET AYTILSNLDI FSIGMNCGTG PDMAMRHIKK LSEISCLPIS IHSNAGLPEN RGGKAYYSMT PEEFADINSK FFELDGLAFI GGCCGTTPLH IKALADKVKG MKPKNPALEK QRPYIASLFN VVSIKQNPAP LMIGERSNAT GSKIFRELMI AGDMDGMLDV GIKQVKAGSH AIDVNAAWAG RDEVEDITKI ISAYVKQISL PLVIDAIKPN VIEAALKVYG GKPIINSANM EQGEEKFDAI CSLAKRYGAS IMLLTIDEKS MAFTCEDKLK MAERMYDRAV NVHKILPHDI IFDPLTFTLA SGDEKSFLAG VETLNAIKEL SKKYPECSIS LGVSNISFGL KEEARKIMNS VFLYEAINHG LTTAIVNVAQ ILPLSKIDEK EIELARELIY NKSNTKEPLI NYINHFSDKK EKKELAGNEE NIKKPIREAI RDAMLDGEWK DMQNLLNEVK ENSEEFGGEK KFAQAIIDEI LLPTMADIGV KFGEGTIQLP FVLGSAEVMK KSVDFLSEFL EKKKQEKTAK IILGTVAGDV HDVGKNLVEI IIKNNGFETV NIGTKVPIEK FLEAYHEHNA DCIGMSGLLV KSTEVMKDNL AYIREKGLRI PIILGGAALT KEFVENDCKK VYGDTAKIFY CKDGFDDILA IKEIIADRDK ENNN // ID G0ESN6_CUPNN Unreviewed; 353 AA. AC G0ESN6; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase MetH {ECO:0000313|EMBL:AEI75510.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEI75510.1}; GN Name=metH1 {ECO:0000313|EMBL:AEI75510.1}; GN OrderedLocusNames=CNE_1c01410 {ECO:0000313|EMBL:AEI75510.1}; 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 {ECO:0000313|EMBL:AEI75510.1, ECO:0000313|Proteomes:UP000006798}; RN [1] {ECO:0000313|EMBL:AEI75510.1, ECO:0000313|Proteomes:UP000006798} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43291 / DSM 13513 / N-1 RC {ECO:0000313|Proteomes:UP000006798}; 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; AEI75510.1; -; Genomic_DNA. DR RefSeq; WP_013955235.1; NC_015726.1. DR RefSeq; YP_004683991.1; NC_015726.1. DR EnsemblBacteria; AEI75510; AEI75510; CNE_1c01410. DR KEGG; cnc:CNE_1c01410; -. DR KO; K00548; -. DR BioCyc; CNEC1042878:GH0Z-141-MONOMER; -. DR Proteomes; UP000006798; Chromosome 1. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006798}; KW Methyltransferase {ECO:0000313|EMBL:AEI75510.1}; KW Transferase {ECO:0000313|EMBL:AEI75510.1}. SQ SEQUENCE 353 AA; 38207 MW; D98D49AAF0D935E8 CRC64; MSAPESTAAA PRPYTRAAEL PRLLQERILI LDGAMGTMIQ RYKLTEADYR GARFAEHKVD VKGNNELLLL TRPQVISEIH EQYLAAGADL IETNTFGATR VAQEDYKMAD LAYEMNVEAA RLARAACDKY STPDKPRFVA GAFGPTPKTA SISPDVNDPG ARNVTFEELR DSYYEQGKGL LEGGADVFLV ETIFDTLNAK AALFAIDQLF EDTGERLPVM ISGTVTDASG RILSGQTVEA FWNSLRHARP ITFGLNCALG ATLMRPYIAE LAKVCDAAVS CYPNAGLPNP MSDTGFDETP EVTSSLVEEF AASGLVNLVG GCCGTTPEHI AAIAERVADK KPRTWPGQYR DAA // ID G0F9X7_ECOLX Unreviewed; 1227 AA. AC G0F9X7; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEJ59414.1}; GN Name=metH {ECO:0000313|EMBL:AEJ59414.1}; GN ORFNames=UMNF18_4972 {ECO:0000313|EMBL:AEJ59414.1}; OS Escherichia coli UMNF18. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1050617 {ECO:0000313|EMBL:AEJ59414.1}; RN [1] {ECO:0000313|EMBL:AEJ59414.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UMNF18 {ECO:0000313|EMBL:AEJ59414.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:AEJ59414.1}. 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; AGTD01000001; AEJ59414.1; -; Genomic_DNA. DR RefSeq; WP_000096007.1; NZ_AGTD01000001.1. DR EnsemblBacteria; AEJ59414; AEJ59414; UMNF18_4972. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136055 MW; BD0C34157B591196 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSDKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAD // ID G0FQN3_AMYMS Unreviewed; 1209 AA. AC G0FQN3; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:AEK43751.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEK43751.1}; GN Name=metH {ECO:0000313|EMBL:AEK43751.1}; GN OrderedLocusNames=RAM_26370 {ECO:0000313|EMBL:AEK43751.1}; OS Amycolatopsis mediterranei (strain S699) (Nocardia mediterranei). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Pseudonocardineae; Pseudonocardiaceae; Amycolatopsis. OX NCBI_TaxID=713604 {ECO:0000313|EMBL:AEK43751.1, ECO:0000313|Proteomes:UP000006138}; RN [1] {ECO:0000313|EMBL:AEK43751.1, ECO:0000313|Proteomes:UP000006138} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S699 {ECO:0000313|EMBL:AEK43751.1, RC ECO:0000313|Proteomes:UP000006138}; 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). CC ----------------------------------------------------------------------- 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; AEK43751.1; -; Genomic_DNA. DR RefSeq; WP_013227000.1; NC_018266.1. DR RefSeq; YP_005533208.1; NC_017186.1. DR RefSeq; YP_006551595.1; NC_018266.1. DR EnsemblBacteria; AEK43751; AEK43751; RAM_26370. DR EnsemblBacteria; AFO78649; AFO78649; AMES_5113. DR KEGG; amm:AMES_5113; -. DR KEGG; amn:RAM_26370; -. DR KO; K00548; -. DR Proteomes; UP000006138; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006138}; KW Methyltransferase {ECO:0000313|EMBL:AEK43751.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006138}; KW Transferase {ECO:0000313|EMBL:AEK43751.1}. SQ SEQUENCE 1209 AA; 131043 MW; 503FD8A049CA7467 CRC64; MNTPSESEAR LRELLDQRVA VLDGAWGTML QGAGLTPADY RGDRFGDHFH DVTGDPDLLN LTRPDVILDV HRQYLAAGAD ITTTNTFTAT SIGQADYGLQ AYVHEMNVRG AQLARQAADE AGGKFVAGSI GPLNVTLSLS PKVDDPAYRA VTFEQVKASY AEQIAGLAEG GVDLLLIETI FDTLNCKAAI AAAREVAPQL PLWISVTIVD LSGRTLSGQT VEAFWSSIEH AKPLVVGVNC SLGAEEMRPH VEELSRIAGT YVACHPNAGL PNAFGGYDQT PEETAGLIGG FARDGLVNLV GGCCGTTPAH IAKIAAAAKE AGPREVPAPR THMRFSGLEP FGIGADTGFV MIGERTNVTG SKRFRRLIES GDHQGAVDVA LEQVRGGANL LDVNMDADLL ESEQAMTTFL NLIATEPEVA RIPVMVDSSK WSVLEAGLRC LQGKGVVNSI SLKEGEEPFL AQARTIRNYG AGVVVMAFDE QGQADTADRK VAICGRAYDL LTQKAGFAGE DIIFDPNVLA VATGISEHNG YAKAFIEALP RIKERCPGAR TSGGISNLSF SFRGNDVVRE AMHSAFLFHA VQAGLDMGIV NAGQLAVYED IPKDLLELVE DVLFDRREDA TDRLVSFAEN VKGSGTKRVV DLSWREGTVG ERLSHALVHG IVDYIEDDTE EARQQLARPL DVIEGPLMDG MKIVGDLFGS GKMFLPQVVK SARVMKRSVA YLEPYMEAEK EKARQEGRLA STGGQGKIVL ATVKGDVHDI GKNIVGVVLG CNNYEVIDLG VMVPAAKILD TAVTEGADAV GLSGLITPSL DEMVAVATEM QRRGLKLPLL IGGATTSRQH TAVKIAPAYD NVTVHVLDAS RVVGVVSDLL DADRSIALAE KNRADQEVLR EQHASKQRRP MLTLEQARAN PEKVAFDGLP TPEFTGVRVL EPSIAELREM VDWQFLFLAW ELKGKYPAIL QQPVARELFD DANTLLDQII ADGSFTAKGA YAFWPAHREG DDILLDGEFA HVKFPMLRQQ TAKPADRANR CLADYIAPVG DHLGGFAVAI HGAEALAKRF EAEQDDYRAI MVKALADRLA EAFAEHIHLR ARRDWFEPDA QPKLEDLHAE RFRGIRPALG YPASPDHSQK RELFELLEAD ELGMALTESY AMTPAASVSG LIFAHPDSRY FTVGRLGRDQ VEDYARRKGV EIAEVEQWLR PNLAYDPEA // ID G0FY43_AMYMS Unreviewed; 1066 AA. AC G0FY43; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 29-APR-2015, entry version 26. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AEK43485.1}; GN OrderedLocusNames=RAM_25035 {ECO:0000313|EMBL:AEK43485.1}; OS Amycolatopsis mediterranei (strain S699) (Nocardia mediterranei). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Pseudonocardineae; Pseudonocardiaceae; Amycolatopsis. OX NCBI_TaxID=713604 {ECO:0000313|EMBL:AEK43485.1, ECO:0000313|Proteomes:UP000006138}; RN [1] {ECO:0000313|EMBL:AEK43485.1, ECO:0000313|Proteomes:UP000006138} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S699 {ECO:0000313|EMBL:AEK43485.1, RC ECO:0000313|Proteomes:UP000006138}; 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). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002896; AEK43485.1; -; Genomic_DNA. DR RefSeq; WP_014467176.1; NC_017186.1. DR RefSeq; YP_005532942.1; NC_017186.1. DR EnsemblBacteria; AEK43485; AEK43485; RAM_25035. DR KEGG; amn:RAM_25035; -. DR KO; K00548; -. DR Proteomes; UP000006138; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006138}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEK43485.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006138}; KW Transferase {ECO:0000313|EMBL:AEK43485.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 109 109 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 175 175 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 176 176 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 619 619 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1066 AA; 115627 MW; 5B402BA446D2C0FB CRC64; MLGSVGPGTK LPTLGHAPFT TLRDAYQEEV RGLLAGGADA VIVETTQDIL QTKASIIGAK RAMAAEGRFV PILASITVET TGTMLLGTEV GAALAALEPL GIDVIGLNCA TGPAEMSEHL RQLAKHARVP LSVMPNAGLP ELGPDGAVYP LGPEALVEAL TGFVREFGVG LVGGCCGTTD EHIRQLAAAV ADTPPVPRRP RPEPGVSSLY QAVPFKQDAS VLMIGERTNA NGSKAFRTAM LEGRWDDCVE IAREQTRDGA HLLDLCVDYV GRDGTADMAE LAGRLATAST LPIMLDSTEV PVLRAALQRL GGRCAVNSVN YEDGDGPESR FAQVMELVSE YGAAVVALTI DEEGQARTAQ KKADIATRLI EDITGNWGLR TSDVIIDALT FTIATGQEES RRDGIETIEA IREIKRRHPE VQTTLGLSNI SFGLNPAARQ VLNSVFLHEC VQAGLDTAIV HASKILPMAR IPDDQRAIAL DLIHDRRREG YDPLQELMAL FEGVSAASSK ASRAEELAAL PLFERLERRI VDGERTGLTD DLDAALEQRP ALEIINDTLL SGMKTVGELF GSGQMQLPFV LQSAEVMKAA VAHLEPHMET GDDSGKGRIV LATVRGDVHD IGKNLVDIIL SNNGYEVVNL GIKQPITTIL DAAEEHGADA IGMSGLLVKS TVIMKENLQE MNSRGVWARW PVLLGGAALT RSYVENDLSE LYLGDVRYAR DAFEGLRLMD ALMAAKRGES TLVDADAEKK RQERKERRER SLRIAEARKA RKADEEALEG PPPARSDVAT DVPLPVPPFW GSRVVKGIAL ADYAAMLDER ATFMGQWGLK GARGGAGPTY DELVESEGRP RLRYWLDRLT ADGVLAHAAV VYGYFPCVAE GDDLVVLTEP SLDAPERVRF TFPRQRRDRR LCLADFYRPR EAGEVDVVPF TVVTMGQPIA DYANELFAAD AYRDYLEVHG LGVQLTEALA EYWHCRIRGE LTFPGGVAVA SEDPDDVEDF FKLGYRGARF SLGYGACPDL EDRAKIVALL EPGRIGVKLS EEYQLHPEQS TDAIVCHHPE AKYFNT // ID G0GCR7_SPITZ Unreviewed; 1213 AA. AC G0GCR7; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 29-APR-2015, entry version 26. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEJ60486.1}; GN OrderedLocusNames=Spith_0199 {ECO:0000313|EMBL:AEJ60486.1}; OS Spirochaeta thermophila (strain ATCC 700085 / DSM 6578 / Z-1203). OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Spirochaeta. OX NCBI_TaxID=869211 {ECO:0000313|EMBL:AEJ60486.1, ECO:0000313|Proteomes:UP000007254}; RN [1] {ECO:0000313|EMBL:AEJ60486.1, ECO:0000313|Proteomes:UP000007254} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700085 / DSM 6578 / Z-1203 RC {ECO:0000313|Proteomes:UP000007254}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002903; AEJ60486.1; -; Genomic_DNA. DR RefSeq; WP_014623889.1; NC_017583.1. DR RefSeq; YP_006044203.1; NC_017583.1. DR EnsemblBacteria; AEJ60486; AEJ60486; Spith_0199. DR KEGG; stq:Spith_0199; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; STHE869211:GLKE-201-MONOMER; -. DR Proteomes; UP000007254; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007254}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007254}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1213 AA; 133798 MW; 7117749371EC3290 CRC64; MAHPIEELLK ERILILDGAM GTMIQRYHFS EADYRGVLFE KGPTVDGREV ALKGNHDLLA LTRPHVIEEI HRAYLEAGAD IIETNTFNAT RVSQREYGTE DLVERINLEA ARLARRVADE YSARTPHRPR FVAGVLGPTS KTLSLSPRAD DPAFRELSFG ELEEDYFGAV RALVEGGADL ILIETVFDTL NAKAALAAVA RFCRESGRAV PVMLSATISD AAGRLLSGQT PRAFLHSVLH GRPLSVGFNC AFGPEMMRPH LKAIQDAPCA VSVHPNAGLP NALGEYDQGP DQMAATLALY AREGLLNIAG GCCGTTPDHI RAIAEALEGI PPRPIPSPRP VAVFTGLEVL DQEEAGFILV GERTNVAGSA RFRRLLREER WEEALEVARA QISAGAQMID VNVDDPLLDP PRFMRRFLSL AASDPTVARV PVMIDSSDWE VLRAGLESLQ GKGVVNSLSL KDGEEVFLER ARVVREMGAA VLVMCFDEEG QAETFERKIA VAQRAYRLLV EEVGIPPWEI VIDPNIFAIG TGMEEHARYG LDYLEAVRWI KEHLPHARTS GGISNVSFAF RGHEGLRDAI HAVFLHHARA AGLDMAIVNP QRMMAYEEVP EEVRGLIEDL VFDRRRDATE RLLEAARGFS GAGPRVRGED RAWRDLPVEE RLAYALKEGI QAYLVEDLEE AHRKAGSALG VIEGPLLTGM EEVGRLFGEG RLFLPQVVRA ARVMREAVAI LEPRLKAEQG GVGKARGVVV LATVKGDVHD IGKNIVKVVL ECNGYRVVDL GVMVPPERVV EAARQGADAV GLSGLITPSL ERMRETAEAI DRAGPAVPLL IGGAATSRLH TALRIAPAYR GPVIHVRDAS EAVQVMGRLL SEGREEFVRE VRAEQARLRE QGVKGRGGVP GLGEARRRRL RPGPASPVEP RVRGPQVVRM GVAEVRPYLD WRMFYKGWGL PARTPERMRE AERAEAVRLR EEAEGVLARM EGRVRIEGVV GFFPARDVGE DCIGVLGWGG EGVIRRLPML RQQAVKEGEP TRSLVDFLPH EGHDYLGLFV ITAGKDIERF LAEEGPGEPY RELMVRLLAD RLAEAASEYL HMLVRTTLWG YAPEEHLSPE EVLAGRYRGI RPAPGHAACP DHSLKQDIFE LLGAEARLEV RLTESFMMVP PSSVAGFYFS HPESRYFAVG RITEEQLRDY ARRRERPVDE VRGWLDHIVV ADS // ID G0HBC2_CORVD Unreviewed; 325 AA. AC G0HBC2; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=5-methyltetrahydrofolate-homocysteinemethyltransferase {ECO:0000313|EMBL:AEK36640.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEK36640.1}; GN Name=metH {ECO:0000313|EMBL:AEK36640.1}; GN OrderedLocusNames=CVAR_1284 {ECO:0000313|EMBL:AEK36640.1}; 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 {ECO:0000313|EMBL:AEK36640.1, ECO:0000313|Proteomes:UP000006659}; RN [1] {ECO:0000313|EMBL:AEK36640.1, ECO:0000313|Proteomes:UP000006659} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44702 / JCM 12073 / NCIMB 30131 RC {ECO:0000313|Proteomes:UP000006659}; 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 ----------------------------------------------------------------------- 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; AEK36640.1; -; Genomic_DNA. DR RefSeq; WP_014009826.1; NC_015859.1. DR RefSeq; YP_004759713.1; NC_015859.1. DR EnsemblBacteria; AEK36640; AEK36640; CVAR_1284. DR KEGG; cva:CVAR_1284; -. DR KO; K00547; -. DR BioCyc; CVAR858619:GHOU-1341-MONOMER; -. DR Proteomes; UP000006659; Chromosome. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006659}; KW Methyltransferase {ECO:0000313|EMBL:AEK36640.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006659}; KW Transferase {ECO:0000313|EMBL:AEK36640.1}. SQ SEQUENCE 325 AA; 33897 MW; AF47732F5FEE4043 CRC64; MTDNDLLTIL THRAVILDGG LGTRLEDRGN DITGALWSAQ ILKDNPTEVR DAHADFFAAG AEVATACSYE VTVDGLVATG MSRADAVVES ELLLRRAVEV AREAASTAAE TAGAPRWVAA SVGPYGAGPG EGTEYDGAYG LTVDELADWH RDRIRILASA GADVLIAETV PSVREIEALA REFTAARVDA LLSVTVLPRT PGTLADGVTL SDGTELSEVA RIVAETPAFR TVGVNCVSAD AALAAVRELG AGLAAAGRPL PLSVYPNSGE LWDHVNRCWL PRTAEGTTSL IDAVPDFLDA GVRLIGGCCR VTPREITAIA QAVRG // ID G0J5A8_CYCMS Unreviewed; 347 AA. AC G0J5A8; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AEL26792.1}; GN OrderedLocusNames=Cycma_3064 {ECO:0000313|EMBL:AEL26792.1}; OS Cyclobacterium marinum (strain ATCC 25205 / DSM 745) (Flectobacillus OS marinus). OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cyclobacteriaceae; OC Cyclobacterium. OX NCBI_TaxID=880070 {ECO:0000313|EMBL:AEL26792.1, ECO:0000313|Proteomes:UP000001635}; RN [1] {ECO:0000313|Proteomes:UP000001635} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25205 / DSM 745 {ECO:0000313|Proteomes:UP000001635}; 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; AEL26792.1; -; Genomic_DNA. DR RefSeq; WP_014021082.1; NC_015914.1. DR RefSeq; YP_004775023.1; NC_015914.1. DR EnsemblBacteria; AEL26792; AEL26792; Cycma_3064. DR KEGG; cmr:Cycma_3064; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR BioCyc; CMAR880070:GHDK-3104-MONOMER; -. DR Proteomes; UP000001635; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001635}; KW Methyltransferase {ECO:0000313|EMBL:AEL26792.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001635}; KW Transferase {ECO:0000313|EMBL:AEL26792.1}. SQ SEQUENCE 347 AA; 37604 MW; EE71B4D77C31B526 CRC64; MANRTNLLLQ QLQKRILILD GAMGTMIQRY GLKEEDFRNQ ELATVKKSLK GNNDLLSLTR PDIIKAIHKA YFEAGADIVE TNTFSSTTIA QEDYGLAELA YKLNFESAKL AREVADEFSA DEPEKPRFVA GAIGPTNRTA SLSPDVNDPG FRAVSFDQLV SAYAEQVEGL LDGGVDTLLV ETVFDTLNAK AAIFAIQEVY EKRGLPLEPS EGGIPIMVSG TITDASGRTL SGQTTEAFLI SIAHVPLLSV GLNCALGAAE LRPYLKVLSD KSPFNVSVYP NAGLPNEFGE YDQGPEEMDK EVSLFLKEGW VNIVGGCCGT TPEHIAALAE SASKYPPRNL HVLTEED // ID G0JUX0_STEMA Unreviewed; 363 AA. AC G0JUX0; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEM51946.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEM51946.1}; GN ORFNames=BurJV3_2626 {ECO:0000313|EMBL:AEM51946.1}; OS Stenotrophomonas maltophilia JV3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Stenotrophomonas; OC Stenotrophomonas maltophilia group. OX NCBI_TaxID=868597 {ECO:0000313|EMBL:AEM51946.1, ECO:0000313|Proteomes:UP000000700}; RN [1] {ECO:0000313|EMBL:AEM51946.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=JV3 {ECO:0000313|EMBL:AEM51946.1}; 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 ----------------------------------------------------------------------- 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; AEM51946.1; -; Genomic_DNA. DR RefSeq; WP_014037756.1; NC_015947.1. DR RefSeq; YP_004793172.1; NC_015947.1. DR EnsemblBacteria; AEM51946; AEM51946; BurJV3_2626. DR KEGG; buj:BurJV3_2626; -. DR KO; K00548; -. DR BioCyc; SMAL868597:GHCG-2688-MONOMER; -. DR Proteomes; UP000000700; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000700}; KW Methyltransferase {ECO:0000313|EMBL:AEM51946.1}; KW Transferase {ECO:0000313|EMBL:AEM51946.1}. SQ SEQUENCE 363 AA; 38398 MW; B51471C890A2AC68 CRC64; MPALPWLHPD RANALLDALR ERILIIDGAM GTMIQRHGLQ EDDYRGERFA GGYDHLHGPG CDHGAPEGHD LKGNNDLLLL TRPQVIADIH TAYLDAGADL VETNTFNATS VSQADYHLEH LVYELNKAGA AVARTCCDAV AATTPGKPRF VIGVIGPTSR TASISPDVND PGFRNTSFDE LRDTYREAIE GLIDGGADTL MVETIFDTLN AKAALYALEE AFDARGARLP VMISGTITDA SGRTLSGQTA EAFHASLAHA RPLSIGLNCA LGADAMRPHV ETLSQVADCY VSAHPNAGLP NAFGEYDETP EDMAGTLRGF AEDGLLNLVG GCCGSTPDHI RAIAQAVAGL PPRALPGVQE QAA // ID G0L9X5_ZOBGA Unreviewed; 333 AA. AC G0L9X5; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Methionine synthase, homocysteine-binding module {ECO:0000313|EMBL:CAZ94902.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAZ94902.1}; GN Name=metH {ECO:0000313|EMBL:CAZ94902.1}; GN OrderedLocusNames=zobellia_837 {ECO:0000313|EMBL:CAZ94902.1}; OS Zobellia galactanivorans (strain DSM 12802 / CIP 106680 / NCIMB 13871 OS / Dsij). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Zobellia. OX NCBI_TaxID=63186 {ECO:0000313|EMBL:CAZ94902.1, ECO:0000313|Proteomes:UP000008898}; RN [1] {ECO:0000313|Proteomes:UP000008898} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 12802 / CIP 106680 / NCIMB 13871 / Dsij RC {ECO:0000313|Proteomes:UP000008898}; RG Genoscope - CEA; RT "Complete genome sequence of Zobellia galactanivorans Dsij."; 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; FP476056; CAZ94902.1; -; Genomic_DNA. DR RefSeq; WP_013992214.1; NC_015844.1. DR RefSeq; YP_004735293.1; NC_015844.1. DR GeneID; 10978152; -. DR KEGG; zga:zobellia_837; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR BioCyc; ZGAL63186:GJN9-838-MONOMER; -. DR Proteomes; UP000008898; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008898}; KW Methyltransferase {ECO:0000313|EMBL:CAZ94902.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008898}; KW Transferase {ECO:0000313|EMBL:CAZ94902.1}. SQ SEQUENCE 333 AA; 36666 MW; 2BD50D502F709A2E CRC64; MKKIQEILKE RILVLDGAMG TMLQRYKFTE EDFRGERFKD WEHPLQGNND LLSLTQPEAI ADVHRKYFAA GADIVETNTF SGTTIAMADY HMEDLVYELN YESARIAKEV ADEFTAKEPN KPRFVAGSIG PTNKTASMSP DVNDPGYRAV SFDELRIAYK QQVEALLDGG ADILLVETIF DTLNAKAALF AIEEVKEERN IEVPIMVSGT ITDASGRTLS GQTAEAFLIS ISHIPILSVG FNCALGANQL VPHLEVLSTR TEHAVSAHPN AGLPNAFGEY DETPEQMAEQ IKEYVEKGLV NIVGGCCGTT PEHITAIADL VRKYDPRKIA VES // ID G0M0V5_LACPE Unreviewed; 618 AA. AC G0M0V5; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 07-JAN-2015, entry version 17. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=LPENT_00578 {ECO:0000313|EMBL:CCC15882.1}; OS Lactobacillus pentosus IG1. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1042160 {ECO:0000313|EMBL:CCC15882.1}; RN [1] {ECO:0000313|EMBL:CCC15882.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=IG1 {ECO:0000313|EMBL:CCC15882.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; CCC15882.1; -; Genomic_DNA. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862, KW ECO:0000313|EMBL:CCC15882.1}. SQ SEQUENCE 618 AA; 66889 MW; B3AED244B96A8FFA CRC64; MNLRQALQQR VLVADGAMGT LLYGNYGINS AFENLNLTHP DTILRVHQSY IQAGADIIQT NTYAANRLKL TRYDLQDQVT TINQAAVRIA VTAREHADHP VYILGTIGGL AGDTDAAVQR ATQAEIAANV TEQLTALLAT EQLDGILLET YYDLSELLAV LKIVKAHTDL PVITNVSMLA AGVLRNGTSF TDAIVQLHAA GADVIGTNCR LGPYYLAQSF ENLAIPADVK LAVYPNSGLP GTDQDGAIVY DGEPSYFEEY AERFRQLGLS IIGGCCGTTP LHTAATVRGL SSRSLVPHNA PTHVAQAPTL VTTKSQHRFL HKVVTEKTVL VELDPPRDFD TRKFFRGAER LKAAGVDGIT LSDNSLATVR IANTAIAAQL KLNYGITPIV HLTTRDHNLI GLQSEIMGLH SLGIEDILAV TGDPAKLGDF PGATSVGDVR SVELMKLIKQ FNSGIGPTGK SLKEASDFRV AGAFNPNAYR TDVSTKSISR KLSYGCDYII TQPVYDLANV DALADALAAN QIDVPVFVGV MPLVSRRNAE FLHHEVHGIR LPKSVLERMQ QAELDGNERA VGITIAKELI DGICARFNGV HIVTPFNRFK TVLELVNYVQ QKNLTKVQ // ID G0M1F7_LACPE Unreviewed; 304 AA. AC G0M1F7; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 01-OCT-2014, entry version 10. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:CCC15976.1}; GN ORFNames=LPENT_00672 {ECO:0000313|EMBL:CCC15976.1}; OS Lactobacillus pentosus IG1. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1042160 {ECO:0000313|EMBL:CCC15976.1}; RN [1] {ECO:0000313|EMBL:CCC15976.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=IG1 {ECO:0000313|EMBL:CCC15976.1}; 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 ----------------------------------------------------------------------- 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; CCC15976.1; -; Genomic_DNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:CCC15976.1}; KW Transferase {ECO:0000313|EMBL:CCC15976.1}. SQ SEQUENCE 304 AA; 32394 MW; B60D5ADDB7281DC3 CRC64; MISLTDLLTK GPVVSDGAMA TELEKRGVAT NSALWSATAM LDHPAAIQAV HQSYLDAGAQ IMTTNTYQAN VPAFEQAGIP AEQARQLIQK AVTVAHDARD ASAATGAVIA GSIGPYGAYL ADGSEYTGDY QLSPAAYQAF HQERLELMID AGVDVLALET MPRLDEVQAL VDLVTTRWPD QPYWVSFSIR DPQRLCDGTS LATAAQWVAA QPNVVAVGVN CTALENIEPA LKTLRAAVTM PLIVYPNSGD QYDPVTKTWQ PTDLSHQFAS FVPKWLAAGA QIIGGCCRTT PADIATVAQV VAHR // ID G0MQ34_CAEBE Unreviewed; 1269 AA. AC G0MQ34; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EGT40868.1}; GN ORFNames=CAEBREN_10758 {ECO:0000313|EMBL:EGT40868.1}; OS Caenorhabditis brenneri (Nematode worm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068}; RN [1] {ECO:0000313|Proteomes:UP000008068} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068}; RG Caenorhabditis brenneri Sequencing and Analysis Consortium; RA Wilson R.K.; 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; GL379806; EGT40868.1; -; Genomic_DNA. DR EnsemblMetazoa; CBN10758; CBN10758; CBN10758. DR InParanoid; G0MQ34; -. DR Proteomes; UP000008068; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008068}; KW Reference proteome {ECO:0000313|Proteomes:UP000008068}. SQ SEQUENCE 1269 AA; 141225 MW; 5A039C9C9B14ACEA CRC64; MTRSSLFEEL AAIAKERIMI IDGAMGTMIQ REYMEEHDFR GEILKDHDKP LKGNNDLLSI TRPDIIYKIH KLYLEAGADF IETNTFSGTT IAQADYRCEH LVHEINYQSA QVARRACDDV GAATGRRRYV CGAIGPTNRT LSISPSVEKP DFRNVTFQEL VKAYGDQARS LIQGGVDVLL VETVFDSANA KAALFAIRTL FEDEGIPEVP VFLSGTIVDM SGRTLSGQTG EAFLVSTRQG DPMAVGLNCA LGAKDMRQFV DNMSKWSDRL ILCYPNAGLP NALGGYDETP EEMAEVLRQF ALDGLVNIIG GCCGTTPDHI NAMYKAVQGI SPRVPPSDPH AGKMVLSGLE PSIVGPETNF VNIGERCNVA GSRRFCNLIK NENYDTAIDV ARVQVDSGAQ ILDVNMDDGL LDGPYAMGKF LRLISSEPDV AKIPVCIDSS DFDVIIAGLE STQGKCVVNS ISLKEGEEKF KERASLVKRY XXXXVLTAKF KERARIVKRY GAAVVVMAFD EEGQAAETER KFEICERSYR ILTEEVGFNP NDIIFDANIL TIATGMEEHA NYGMYFIEAA RMIRENLPGA HVSGGVSNIS FSFRGMEAIR EAMHSVFLFY AIKAGMDMGI VNAGALPLYE DIDKPLLQLL EDLLFNRDPE ATEKLLVAAQ EMKKDGKKAD QKTDEWRNTS VEERLKYALV KGIDQFVVAD TEEARQNQEK YPRPLNVIER PLMDGMAVVG ELFGAGKMFL PQVIKSARVM KKAVAHLLPF MDAERQANIE KMGLAEDESP YQGTVVIATV KGDVHDIGKN IVAVVLGCNN FKVVDLGVMT PCENIIKAAI EEKADFIGLS GLITPSLDEM VHVAKEMKRV GLTIPLLIGG ATTSKTHTAV KIAPRYPHPV VHCLDASKSV VVCSSLSDMS VRDAFLQDLN EDYEDVRQEH YESLKDRRFT ALGKTREKKF VIDWDKFTAV KPSFIGRQEY QNFDLNELIP YIDWKPFFDV WQLRGKYPNR SYPKIFDDAD VGAEAKKVFD DAQTWLKKLI DEKILKANAV VSFLPAASEG DDIHVYDPET GNKVDTFFGL RQQSGREHDQ PHFCLSDFIK PLKNGAPDDY LGLFACTAGL GAEEYCKELE KNHDDYASIM VKALADRLAE AYAEYLHKEV RTNLWGYSTN EQLTESDLLS IKYEGIRPAC GYPSQPDHTE KRTLWKLTEA EKNGIILTEH LAMLPAASVS GLYFANPQSQ YFAVGKIDED QVIDYAARKQ VPKEEVERWL SPIIGYDLD // ID G0N7R1_CAEBE Unreviewed; 340 AA. AC G0N7R1; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 07-JAN-2015, entry version 16. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EGT54809.1}; GN ORFNames=CAEBREN_31638 {ECO:0000313|EMBL:EGT54809.1}; OS Caenorhabditis brenneri (Nematode worm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068}; RN [1] {ECO:0000313|Proteomes:UP000008068} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068}; RG Caenorhabditis brenneri Sequencing and Analysis Consortium; RA Wilson R.K.; 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; GL379848; EGT54809.1; -; Genomic_DNA. DR EnsemblMetazoa; CBN31638; CBN31638; CBN31638. DR InParanoid; G0N7R1; -. DR Proteomes; UP000008068; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008068}; KW Reference proteome {ECO:0000313|Proteomes:UP000008068}. SQ SEQUENCE 340 AA; 38914 MW; 855AAFB94C7854B2 CRC64; MKKYRLLDGS MSEQLKQFGY NCNDINNKPH WTFPANSDQS LMEKVYRSFL DIGVNNITTN TYHFGSILDK NLSGQEEKCK LYEKYFEDTC SLLCNLAQQY DDVQVWGSVG TFATKFHDCS EYNGKYMDNA GAEESAYEYY KTILTLFQER TTIRNLIFET IPSQLEGEVA LKVLKEFKEM KAVISFTFME NACLRHGEHV ADIAKKLKES EQIIGMGINC TDPKNVLPVL EAIKNCEFSD IFVYPNLGDA FFMVAEKGDF DDSDNYDHRL RSWIEHGATA LGGCCGIDLD MIQDLRSCVD ILNDILFADN NGKIESSQFE VLRESYSEHE NTNTLLQIYS // ID G0PXH8_STRGR Unreviewed; 305 AA. AC G0PXH8; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 10. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGE41187.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EGE41187.1}; GN ORFNames=SACT1_1823 {ECO:0000313|EMBL:EGE41187.1}; OS Streptomyces griseus XylebKG-1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=649189 {ECO:0000313|EMBL:EGE41187.1}; RN [1] {ECO:0000313|EMBL:EGE41187.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=XylebKG-1 {ECO:0000313|EMBL:EGE41187.1}; 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] {ECO:0000313|EMBL:EGE41187.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=XylebKG-1 {ECO:0000313|EMBL:EGE41187.1}; 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 ----------------------------------------------------------------------- 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; EGE41187.1; -; Genomic_DNA. DR RefSeq; WP_003965626.1; NZ_GL877172.1. DR EnsemblBacteria; EGE41187; EGE41187; SACT1_1823. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGE41187.1}; KW Transferase {ECO:0000313|EMBL:EGE41187.1}. SQ SEQUENCE 305 AA; 31844 MW; E0A883B51B68650D CRC64; MRTVRTLAEA LDAGPVLLDG GLSNQLEAQG CDLSDALWSA RLLADAPEQI EAAHLAYLRA GARVLITASY QATFEGFGRY GLDRAATGAL LARSVELARG AADAARRADP GREAWVAASV GPYGAMLADG SEYRGRYGLS VRELERFHRP RVAALAAAGP DALALETVPD LDEAEALVRV AEETGLPYWL SYSVADGRTR AGQPLQEAFA VAAGRDSVLA VGVNCCDPQE AQGAVEQAVA VTGRPAVVYP NSGEGWDAGA RGWTGHGTFD PGRVRAWTRA GAGLVGGCCR VGPDLITELD GRLEG // ID G0Q6E8_STRGR Unreviewed; 1170 AA. AC G0Q6E8; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGE45484.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGE45484.1}; GN ORFNames=SACT1_6180 {ECO:0000313|EMBL:EGE45484.1}; OS Streptomyces griseus XylebKG-1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=649189 {ECO:0000313|EMBL:EGE45484.1}; RN [1] {ECO:0000313|EMBL:EGE45484.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=XylebKG-1 {ECO:0000313|EMBL:EGE45484.1}; 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] {ECO:0000313|EMBL:EGE45484.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=XylebKG-1 {ECO:0000313|EMBL:EGE45484.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; GL877172; EGE45484.1; -; Genomic_DNA. DR RefSeq; WP_003970155.1; NZ_GL877172.1. DR ProteinModelPortal; G0Q6E8; -. DR EnsemblBacteria; EGE45484; EGE45484; SACT1_6180. DR GeneID; 6215386; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGE45484.1}; KW Transferase {ECO:0000313|EMBL:EGE45484.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 237 237 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 747 747 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1170 AA; 127832 MW; 1BA539CB913C0C3A CRC64; MASLPTSAAD SRTRADALRE ALATRVVVAD GAMGTMLQAQ DPTLEDFENL EGCNEILNIT RPDIVRSVHE EYFAVGVDCV ETNTFGANHS AANEYEIADR IFELSESGAR IAREVADEFG AKDGRQRWVL GSIGPGTKLP SLGHIAYDVL RDGYQKNAEG LLTGGSDALI VETTQDLLQT KSSIIGARRA MDALGVHVPL ICSLAFETTG VMLLGSEIGA ALTALEPLGI DLIGLNCSTG PDEMSEHLRY LARHSRTPLM CMPNAGLPVL TKDGAHFPLG PDGLADSQEN FVRDYGLSLI GGCCGTTPEH LRAVVDRARE LTPTERDPRP EPGAASLYQT IPFRQDTAYL AIGERTNANG SKKFREAMLE ARWDDCVEMA RDQIREGAHM LDLCVDYVGR DGVADMAELA GRFATASTLP IVLDSTELPV LRAGLEKLGG RAVLNSVNYE DGDGPESRFA QVSALAAEHG AALIALTIDE EGQARTVENK VAIAERLIED LTANWSIRES DILIDTLTFT ICTGQEESRG DGIATIGAIR ELKKRHPDVQ TTLGLSNISF GLNPAARVVL NSVFLDECVK AGLDSAIVHA SKILPIARLE EEQVKVALDL IYDRRAEGYD PLQKLMELFE GVNMKSMKAG KAEELMALPL DERLQRRIID GEKNGLEADL DEALQDTPAL DIVNNTLLEG MKVVGELFGS GQMQLPFVLQ SAEVMKSAVA HLEPHMEKSD DEGKGTIVLA TVRGDVHDIG KNLVDIILSN NGYNVVNLGI KQPVSAILEA AEEHRADVIG MSGLLVKSTV IMKENLQELN QRKMAADFPV ILGGAALTRA YVEQDLHEIY EGEVRYARDA FEGLRLMDAL IGVKRGVPGA ALPELKQRRV PKKDVAVLEV EEPEGSVRSD VSTTNPIPEP PFRGTRVIKG IPLKDYASWL DEGALFKGQW GLKQARTGDG PTYEELVETE GRPHLRGWLD HLQSNNLLEA AVVYGYFPCV SKGDDLVLLH EDGSERTRFT FPRQRRGRRL CLADFFRPEE SGETDVIGLQ IVTVGSRIGE ATAELFAANS YRDYLELHGL SVQLAEALAE YWHARVRSEL GFAGEDPEDV EDMFALKYRG ARFSLGYGAC PDLEDRAKIA DLLQPERIGV HLSEEFQLHP EQSTDAIVIH HPEAKYFNAR // ID G0RPP6_HYPJQ Unreviewed; 354 AA. AC G0RPP6; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 07-JAN-2015, entry version 16. DE SubName: Full=S-methylmethionine-dependent Homocysteine/selenocysteine methylase-like protein {ECO:0000313|EMBL:EGR46785.1}; DE Flags: Fragment; GN ORFNames=TRIREDRAFT_40758 {ECO:0000313|EMBL:EGR46785.1}; OS Hypocrea jecorina (strain QM6a) (Trichoderma reesei). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Hypocreomycetidae; Hypocreales; Hypocreaceae; OC Trichoderma. OX NCBI_TaxID=431241 {ECO:0000313|Proteomes:UP000008984}; RN [1] {ECO:0000313|EMBL:EGR46785.1, ECO:0000313|Proteomes:UP000008984} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=QM6a {ECO:0000313|EMBL:EGR46785.1, RC ECO:0000313|Proteomes:UP000008984}; 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; GL985071; EGR46785.1; -; Genomic_DNA. DR RefSeq; XP_006967186.1; XM_006967124.1. DR EnsemblFungi; EGR46785; EGR46785; TRIREDRAFT_40758. DR GeneID; 18484796; -. DR KEGG; tre:TRIREDRAFT_40758; -. DR KO; K00547; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000008984; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008984}; KW Methyltransferase {ECO:0000313|EMBL:EGR46785.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008984}; KW Transferase {ECO:0000313|EMBL:EGR46785.1}. FT NON_TER 1 1 {ECO:0000313|EMBL:EGR46785.1}. FT NON_TER 354 354 {ECO:0000313|EMBL:EGR46785.1}. SQ SEQUENCE 354 AA; 38733 MW; 99425AD7713EC1FB CRC64; IRILDGGLGT TLEQNHSVSF SPSSSPLWSS HLLVSDPETL LLCQKSFAEI PVDVLLTATY QVSIDGFART KTAQHPAGIA DVSHIPPLLE KAIQIAHEAA AAAAAATTTN GPPPPHPCAV ALSLGPYGAC MIPSQEYSGA YDAQHDSQEA LYLWHRQRME LFARVPDIRH SITYMALETI PRLDEIVALR RAVAAVPALS SGIPFWMSCL FPNEEDETTP DGSSPEAIIR AMLDPALAET AAVPWAVGIN CTKVWKLDSL LRRYEAAIRD LLHEGTIKKW PALVLYPDGT NGEVYNTTTQ QWEIPQGSEQ QHDRVPWEAQ LKQVVRATEA RGDWPEIIVG GCCRALPSDI KRLR // ID G0SV09_RHOG2 Unreviewed; 419 AA. AC G0SV09; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 07-JAN-2015, entry version 16. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGU13559.1}; GN ORFNames=RTG_00289 {ECO:0000313|EMBL:EGU13559.1}; 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 {ECO:0000313|EMBL:EGU13559.1, ECO:0000313|Proteomes:UP000006141}; RN [1] {ECO:0000313|EMBL:EGU13559.1, ECO:0000313|Proteomes:UP000006141} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204091 / IIP 30 / MTCC 1151 RC {ECO:0000313|Proteomes:UP000006141}; 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. {ECO:0000313|EMBL:EGU13559.1}. 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; AEVR02000023; EGU13559.1; -; Genomic_DNA. DR InParanoid; G0SV09; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000006141; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 2. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006141}; KW Reference proteome {ECO:0000313|Proteomes:UP000006141}. SQ SEQUENCE 419 AA; 44196 MW; A24600145BC643C7 CRC64; MDSLFPQDSY GTRPVLVLDG GMGTTLQAPP FELGLDSALW SSELLATEDG RAQLERLHKT WLGAGADIVE TCTYQSSLPL FLPASPSSAD QSTALSTMNA ALPLAVSCCS SHASSSSRKP TTALSLGPYG SALQPGQEYS GAYPPPFGPA ETAAKDAKPA CSQEALDLVP LPLDEVRAGL ASTASDEEVH LAAWHLQRLQ HFSQSPAFDE GIPLLAFETV PSLTEILAIR RAMHVFSTSS SHSNSPKKTF YISLVFPRIN EGTSAETVRF PDPSLAHLPT LADQAPLLVQ AALEPREGYA TPAGLGFNCT SPLHASFVVE ALSSAIASSS LSKAQTKPWL VFYPDGGAIY DVQTRTWHHP AGLTDDAWAS LVADAVMVGR EAGEGEVWGG VVVGGCCKAG PGAIRALKKE VVKRGWAKE // ID G0TMP7_MYCCP Unreviewed; 1192 AA. AC G0TMP7; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CCC44480.1}; GN Name=metH {ECO:0000313|EMBL:CCC44480.1}; GN OrderedLocusNames=MCAN_21481 {ECO:0000313|EMBL:CCC44480.1}; OS Mycobacterium canettii (strain CIPT 140010059). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=1048245 {ECO:0000313|EMBL:CCC44480.1, ECO:0000313|Proteomes:UP000008896}; RN [1] {ECO:0000313|EMBL:CCC44480.1, ECO:0000313|Proteomes:UP000008896} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIPT 140010059 {ECO:0000313|EMBL:CCC44480.1, RC ECO:0000313|Proteomes:UP000008896}; 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). RN [2] {ECO:0000313|EMBL:CCC44480.1, ECO:0000313|Proteomes:UP000008896} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIPT 140010059 {ECO:0000313|EMBL:CCC44480.1, RC ECO:0000313|Proteomes:UP000008896}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; HE572590; CCC44480.1; -; Genomic_DNA. DR RefSeq; WP_003900472.1; NC_015848.1. DR RefSeq; YP_004745585.1; NC_015848.1. DR ProteinModelPortal; G0TMP7; -. DR SMR; G0TMP7; 16-621, 637-1192. DR EnsemblBacteria; CCC44480; CCC44480; MCAN_21481. DR KEGG; mce:MCAN_21481; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; MCAN1048245:GJCJ-2163-MONOMER; -. DR Proteomes; UP000008896; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008896}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 231 231 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 297 297 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 298 298 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 742 742 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1192 AA; 130323 MW; 820450DCE77BE15B CRC64; MTAADKHLYD TDLLDVLSQR VMVGDGAMGT QLQAADLTLD DFRGLEGCNE ILNETRPDVL ETIHRNYFEA GADAVETNTF GCNLSNLGDY DIADRIRDLS QKGTAIARRV ADELGSPDRK RYVLGSMGPG TKLPTLGHTE YAVIRDAYTE AALGMLDGGA DAILVETCQD LLQLKAAVLG SRRAMTRAGR HIPVFAHVTV ETTGTMLLGS EIGAALTAVE PLGVDMIGLN CATGPAEMSE HLRHLSRHAR IPVSVMPNAG LPVLGAKGAE YPLLPDELAE ALAGFIAEFG LSLVGGCCGT TPAHIREVAA AVANIKRPER QVSYEPSVSS LYTAIPFAQD ASVLVIGERT NANGSKGFRE AMIAEDYQKC LDIAKDQTRD GAHLLDLCVD YVGRDGVADM KALASRLATS STLPIMLDST ETAVLQAGLE HLGGRCAINS VNYEDGDGPE SRFAKTMALV AEHGAAVVAL TIDEEGQART AQKKVEIAER LINDITGNWG VDESSILIDT LTFTIATGQE ESRRDGIETI EAIRELKKRH PDVQTTLGLS NISFGLNPAA RQVLNSVFLH ECQEAGLDSA IVHASKILPM NRIPEEQRNV ALDLVYDRRR EDYDPLQELM RLFEGVSAAS SKEDRLAELA GLPLFERLAQ RIVDGERNGL DADLDEAMTQ KPPLQIINEH LLAGMKTVGE LFGSGQMQLP FVLQSAEVMK AAVAYLEPHM ERSDDDSGKG RIVLATVKGD VHDIGKNLVD IILSNNGYEV VNIGIKQPIA TILEVAEDKS ADVVGMSGLL VKSTVVMKEN LEEMNTRGVA EKFPVLLGGA ALTRSYVEND LAEIYQGEVH YARDAFEGLK LMDTIMSAKR GEAPDENSPE AIKAREKEAE RKARHQRSKR IAAQRKAAEE PVEVPERSDV AADIEVPAPP FWGSRIVKGL AVADYTGLLD ERALFLGQWG LRGQRGGEGP SYEDLVETEG RPRLRYWLDR LSTDGILAHA AVVYGYFPAV SEGNDIVVLT EPKPDAPVRY RFHFPRQQRG RFLCIADFIR SRELAAERGE VDVLPFQLVT MGQPIADFAN ELFASNAYRD YLEVHGIGVQ LTEALAEYWH RRIREELKFS GDRAMAAEDP EAKEDYFKLG YRGARFAFGY GACPDLEDRA KMMALLEPER IGVTLSEELQ LHPEQSTDAF VLHHPEAKYF NV // ID G0TPE5_MYCCP Unreviewed; 302 AA. AC G0TPE5; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=MmuM protein {ECO:0000313|EMBL:CCC44828.1}; GN Name=mmuM {ECO:0000313|EMBL:CCC44828.1}; GN OrderedLocusNames=MCAN_24971 {ECO:0000313|EMBL:CCC44828.1}; OS Mycobacterium canettii (strain CIPT 140010059). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=1048245 {ECO:0000313|EMBL:CCC44828.1, ECO:0000313|Proteomes:UP000008896}; RN [1] {ECO:0000313|EMBL:CCC44828.1, ECO:0000313|Proteomes:UP000008896} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIPT 140010059 {ECO:0000313|EMBL:CCC44828.1, RC ECO:0000313|Proteomes:UP000008896}; 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). RN [2] {ECO:0000313|EMBL:CCC44828.1, ECO:0000313|Proteomes:UP000008896} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIPT 140010059 {ECO:0000313|EMBL:CCC44828.1, RC ECO:0000313|Proteomes:UP000008896}; 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 ----------------------------------------------------------------------- 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; CCC44828.1; -; Genomic_DNA. DR RefSeq; WP_003412639.1; NC_015848.1. DR RefSeq; YP_004745924.1; NC_015848.1. DR ProteinModelPortal; G0TPE5; -. DR EnsemblBacteria; CCC44828; CCC44828; MCAN_24971. DR KEGG; mce:MCAN_24971; -. DR KO; K00547; -. DR OMA; YGRSVTK; -. DR BioCyc; MCAN1048245:GJCJ-2516-MONOMER; -. DR Proteomes; UP000008896; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008896}. SQ SEQUENCE 302 AA; 31533 MW; D8174BFD6FDE55BD CRC64; MELVSDSVLI SDGGLATELE ARGHDLSDPL WSARLLVDAP HAITAVHTAY FRAGAQIATT ASYQASFEGF AARGIGHDDA TVLLRRSVEL AQAARDEVGV GGLSVAASVG PYGAALADGS EYRGCYGLSV AALMKWHLPR LEVLVDAGAD MLALETIPDI DEAEALVNLV RRLATPAWLS YTINGTRTRA GQPLTDAFAV AAGVPEIVAV GVNCCAPDDV LPAIAFAVAH TGKPVIVYPN SGEGWDGRRR AWVGPRRFSG SSGQLAREWV AAGARIVGGC CRVRPIDIAE IGRALTTAPP RG // ID G0UIW0_TRYCI Unreviewed; 432 AA. AC G0UIW0; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 01-OCT-2014, entry version 9. DE SubName: Full=Putative homocysteine S-methyltransferase {ECO:0000313|EMBL:CCC89310.1}; GN ORFNames=TCIL3000_1_760 {ECO:0000313|EMBL:CCC89310.1}; OS Trypanosoma congolense (strain IL3000). OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Trypanosoma; OC Nannomonas. OX NCBI_TaxID=1068625 {ECO:0000313|EMBL:CCC89310.1}; RN [1] {ECO:0000313|EMBL:CCC89310.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=IL3000 {ECO:0000313|EMBL:CCC89310.1}; RA Jackson A.P., Berry A., Aslett M., Allison H.C., Burton P., RA Vavrova-Anderson J., Brown R., Browne H., Corton N., Hauser H., RA Gamble J., Gilderthorp R., Marcello L., McQuillan J., Otto T.D., RA Quail M.A., Sanders M.J., van Tonder A., Ginger M.L., Field M.C., RA Barry J.D., Hertz-Fowler C., Berriman M.; RT "Antigenic diversity is generated by distinct evolutionary mechanisms RT in African trypanosome species."; RL Proc. Natl. Acad. Sci. U.S.A. 109:3416-3421(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; HE575314; CCC89310.1; -; Genomic_DNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 3. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:CCC89310.1}; KW Transferase {ECO:0000313|EMBL:CCC89310.1}. SQ SEQUENCE 432 AA; 47695 MW; C04D8CDB5F4AB22F CRC64; MEGKSNNTSH GDGSSVNEPR KRPNFFVLDG AMGTEIEERR PDLLPLGPMW SASVVHTEPS AVQSVHEAYV NAGADILLTS TYQINTKGCA TLGVAIPDLV DAAVRLLRNS ITPERTSATE QAKAKAKLDP SVKRRGASAV FAPLLYGIRD DPSKCPVLIG GSMSPYGSLA GYGQEYHGKY TVDETIIDEF YNQRVRAFID YTSDTPRPKV DFLMLETFPL LKEAVGVFSW LSHQRDGVLD TAPVCISFVS VLDGDRPSAD ADDAAVEEWW NSAESSIHLP DGNTYLQVLD TLMELRSPQL AGLGANCCSP LEVSVVASLL LKKKKKHVED PSLVLLLYSN SGEEFTEGEW RWRHKFERGS RLSKWKRGTV VPQQELRRMM LAADVDVQLC GLFAYQTLLQ RPEADDWLFD IVICGGCCRS NPKDIEKIRA LA // ID G0VET4_NAUCC Unreviewed; 327 AA. AC G0VET4; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 29-APR-2015, entry version 20. DE SubName: Full=NCAS0D04940 protein {ECO:0000313|EMBL:CCC70075.1}; GN Name=NCAS0D04940 {ECO:0000313|EMBL:CCC70075.1}; GN OrderedLocusNames=NCAS_0D04940 {ECO:0000313|EMBL:CCC70075.1}; 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 {ECO:0000313|EMBL:CCC70075.1, ECO:0000313|Proteomes:UP000001640}; RN [1] {ECO:0000313|EMBL:CCC70075.1, ECO:0000313|Proteomes:UP000001640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 76901 / CBS 4309 / NBRC 1992 / NRRL Y-12630 RC {ECO:0000313|Proteomes:UP000001640}; 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; HE576755; CCC70075.1; -; Genomic_DNA. DR RefSeq; XP_003676436.1; XM_003676388.1. DR GeneID; 11528349; -. DR KEGG; ncs:NCAS_0D04940; -. DR InParanoid; G0VET4; -. DR KO; K00547; -. DR OrthoDB; EOG7X9GHR; -. DR Proteomes; UP000001640; Chromosome 4. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001640}; KW Reference proteome {ECO:0000313|Proteomes:UP000001640}. SQ SEQUENCE 327 AA; 36968 MW; 22668FCEAB8D4F12 CRC64; MTRQSIKEYL QQNPDKVLVL DGGQGTELEN RGINVANPVW STIPFVSESF WSDKSSNDRQ IVKEMFEDFL AAGAEILMTT TYQTSFKSVS ENTDIKTLQE YNELLNRIVS FSRDCIGEQK YLIGCIGPWG AHVCAEFNGD YGAHPENIDY YQYFKPQLDN FFANENLDLI GFETVPNVNE LKAILSWDEK ILSKPFYIGL SVHENGVLRD GTTMEEIGNI FKSLGNKVNP NLLLLGINCV SFNHSPSILE DIHKNLPDMP LIAYPNSGEV YDTVKKIWLP QNSENSLTWE QVVKRYIEAG ARIIGGCCRT TPKDILEISK AVKKFSK // ID G0VQ82_MEGEL Unreviewed; 316 AA. AC G0VQ82; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Megasphaera elsdenii strain DSM 20460 draft genome {ECO:0000313|EMBL:CCC73610.1}; GN ORFNames=MELS_1389 {ECO:0000313|EMBL:CCC73610.1}; OS Megasphaera elsdenii DSM 20460. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Megasphaera. OX NCBI_TaxID=1064535 {ECO:0000313|EMBL:CCC73610.1, ECO:0000313|Proteomes:UP000010111}; RN [1] {ECO:0000313|EMBL:CCC73610.1, ECO:0000313|Proteomes:UP000010111} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20460 {ECO:0000313|EMBL:CCC73610.1}; RX PubMed=21914887; DOI=10.1128/JB.05861-11; 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). CC ----------------------------------------------------------------------- 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; CCC73610.1; -; Genomic_DNA. DR RefSeq; WP_014016340.1; NC_015873.1. DR RefSeq; YP_004766437.1; NC_015873.1. DR EnsemblBacteria; CCC73610; CCC73610; MELS_1389. DR KEGG; med:MELS_1389; -. DR KO; K00547; -. DR Proteomes; UP000010111; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000010111}; KW Reference proteome {ECO:0000313|Proteomes:UP000010111}. SQ SEQUENCE 316 AA; 34732 MW; FB503294F88E4807 CRC64; MKSTLKQILD REGILVLDGS MGTALENLGA DLNNKLWTAR VLADRPELVK EVHIQYFRAG ADAGITCSYQ ASLPGLMETG YSREQAEALI TRAVQVFLDA RQEWWDAEGK QAGRSWPLCL ASAGPYGAYL ADGSEYKGHY GVSADTLRDF HRRRAELLWQ AGADVLLFET EPSLMEAEVE AQIAEELGAP YWISFSCCDG RHNCEGQLLA DCARQLARNY PHLQAIGVNC TKPEYIASLI GELKGASDLP IIVYPNSGEE YDPQTKTWHG VGTDRRFGDY ALDYMKAGAV AVGGCCTTVA DHIRQVVAAR RTYTGK // ID G0VS27_MEGEL Unreviewed; 823 AA. AC G0VS27; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Megasphaera elsdenii strain DSM 20460 draft genome {ECO:0000313|EMBL:CCC74067.1}; GN ORFNames=MELS_1849 {ECO:0000313|EMBL:CCC74067.1}; OS Megasphaera elsdenii DSM 20460. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Megasphaera. OX NCBI_TaxID=1064535 {ECO:0000313|EMBL:CCC74067.1, ECO:0000313|Proteomes:UP000010111}; RN [1] {ECO:0000313|EMBL:CCC74067.1, ECO:0000313|Proteomes:UP000010111} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20460 {ECO:0000313|EMBL:CCC74067.1}; RX PubMed=21914887; DOI=10.1128/JB.05861-11; 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). CC ----------------------------------------------------------------------- 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; CCC74067.1; -; Genomic_DNA. DR RefSeq; WP_014016794.1; NC_015873.1. DR RefSeq; YP_004766894.1; NC_015873.1. DR EnsemblBacteria; CCC74067; CCC74067; MELS_1849. DR KEGG; med:MELS_1849; -. DR KO; K00548; -. DR Proteomes; UP000010111; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000010111}; KW Reference proteome {ECO:0000313|Proteomes:UP000010111}. SQ SEQUENCE 823 AA; 88559 MW; 3D2D93712A973831 CRC64; MTNEEFQHLL SRGVVMLDGA TGTNLQQAGM PIGVCPEKWI LENRQVMIDL QRHFVEAGSQ ILYAPTFTGN RIKLAEYGLD DQLAAINQGL VAISKEAAQG KALVAGDMTM TGQQLYPMGD LTFEELVDVY RQQAKVLYDA GVDLFIVETM MSLQETRACV LAIKEVCDLP IMATLTFEKD GRTLYGTPPE AAVVVLQHLG VAAVGLNCST GPADMVETVQ KMYEYATVPL IAKPNAGLPE WDGDKTVYKT TPEEFAQDGK LLIEAGAHIV GGCCGTTPDH IRALHDAVCQ MTPKAPHASH HRVLASERQV VEIQLDGSFQ VIGERINPTG KKKLQAELRA GKLDLVRAMA REQERNGAAI LDVNMGTNGI DEKEMMLKAI YEVTGVSGLP LSIDTSSPEI MEAALRIYPG RALVNSISCE TEKRKQLLPV VKKYGAMFIA LPVSDAGIPK TLEEKHAVLD ELLTDAYDHG FTPEDVVVDA LVATVGAAPT SALDCMATFS HCKRDLGLAT VCGLSNISFG LPDRMYVNAT FLGMAIASGL TMAIANPSQD LLMNTAAAAN MLMNKEGSDL AYIHRMQYFD KKEAEKKRQE EAELLARQGM PADVAAAGES QQTEQGPVNP VYQAVLEGEK DAVVSLAQAE LAKGMAPDAV INDLLIPAIT KVGDLYDKQV YFLPQLIASA NTMETAIAYL EPLIKKEPGQ QDMATIVIAT VEGDVHDIGK NLVGLMLRNY GYKVVDLGKD VPAGTIIETA LREKASVVGL SALMTTTMMH MKDVIAEAAD KHYDGKIIIG GAAVTPSFSD EIGADGYSKD AADCVKLVGR LLA // ID G0WC33_NAUDC Unreviewed; 329 AA. AC G0WC33; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 29-APR-2015, entry version 18. DE SubName: Full=NDAI0F00250 protein {ECO:0000313|EMBL:CCD25344.1}; GN Name=NDAI0F00250 {ECO:0000313|EMBL:CCD25344.1}; GN OrderedLocusNames=NDAI_0F00250 {ECO:0000313|EMBL:CCD25344.1}; 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 {ECO:0000313|EMBL:CCD25344.1, ECO:0000313|Proteomes:UP000000689}; RN [1] {ECO:0000313|EMBL:CCD25344.1, ECO:0000313|Proteomes:UP000000689} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639 RC {ECO:0000313|Proteomes:UP000000689}; 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; CCD25344.1; -; Genomic_DNA. DR RefSeq; XP_003670587.1; XM_003670539.1. DR GeneID; 11497181; -. DR KEGG; ndi:NDAI_0F00250; -. DR KO; K00547; -. DR OrthoDB; EOG7X9GHR; -. DR Proteomes; UP000000689; Chromosome 6. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000689}; KW Reference proteome {ECO:0000313|Proteomes:UP000000689}. SQ SEQUENCE 329 AA; 37132 MW; 45D671B7F59ADC64 CRC64; MTRQPIKDYL SENPKKILIL DGGQGTELEN RGINVANPVW STIPFVNDSF WSGQSSKDRE IVKQMFNDFL EAGAEILMTT TYQTSFKSVS ENTNIKTLKE YDELLTRIVN FSRDCIGENK YLIGCIGPWG AHICSEFTGN YGEHPELIDY YEYFKPQLVN FVQNDDLDII GFETIPNVYE LKTILSWGTD ILPKPFYIGL SVHENGVLRD GTTMSQVADI INSLSDKLNP NLVLLGINCV SLAHSPDILD SIHSNLPDLP LIVYPNSGEV YDTVKKIWLP PNDETYMSWD EVVERYLKAG ARIIGGCCRT TPNDIKQISD AVHKYSNTK // ID G1KBM2_ANOCA Unreviewed; 1271 AA. AC G1KBM2; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 2. DT 27-MAY-2015, entry version 30. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSACAP00000003091}; GN Name=MTR {ECO:0000313|Ensembl:ENSACAP00000003091}; OS Anolis carolinensis (Green anole) (American chameleon). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; OC Toxicofera; Iguania; Iguanidae; Polychrotinae; Anolis. OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000003091, ECO:0000313|Proteomes:UP000001646}; RN [1] {ECO:0000313|Ensembl:ENSACAP00000003091, ECO:0000313|Proteomes:UP000001646} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG The Genome Sequencing Platform; RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J., RA Lander E.S., Lindblad-Toh K.; RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard)."; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSACAP00000003091} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 1}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSACAP00000003091}. 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_003215894.1; XM_003215846.2. DR Ensembl; ENSACAT00000003170; ENSACAP00000003091; ENSACAG00000002970. DR GeneID; 100555904; -. DR CTD; 4548; -. DR GeneTree; ENSGT00420000029824; -. DR InParanoid; G1KBM2; -. DR OrthoDB; EOG7TF786; -. DR TreeFam; TF312829; -. DR Proteomes; UP000001646; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:Ensembl. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001646}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001646}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 266 266 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 329 329 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 330 330 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 791 791 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1271 AA; 142198 MW; 3003C5E49169AD2D CRC64; MSPTIPGRTE RRSSPPENAT KKTLKDEIES ILRQRIMVLD GGMGTMIQQH TLTEEDFQGQ EFKDHLKPLK GNNDLLSVTQ PDIIYKIHKE YLMFGADIIE TNTFSSTRIA QADYGLEHMA YRLNKMSAQV ARRAADDVTA ETGHKKYVAG AMGPTNKTLS VSPSVEKPDY RNVTFDELVE AYTEQAKGLL DGGVDIMLVE TIFDTANAKA ALFALQNLFE EEYEPRPLFV SGTIVDKSGR TLSGQTGEAF VISTSHSEPL CIGLNCALGA LEMRPFIETI GKCTTAYIIC YPNAGLPNTF GGYDETPEVT AKHLKTFALD GLVNIVGGCC GTTPAHIREI AEAVKGCKPR IPNSAFSEGY MLLSGLEPFR IGQYTNFVNI GERCNVAGSR RFAKLIMANK YEEALSVAKA QVEMGAQILD INMDDGMLDG PSAMARFCNY IASEPDIAKV PLCIDSSNFT VIEAGLKCCQ GKCIVNSISL KEGEEDFFAK ARKIRKYGAA VVVMAFDEVG QATETKEKIS ICTRAYRLLV NKVGFNPNDI IFDPNILTIG TGMEEHNLYA INFINATKTI KETLPGVKIS GGLSNLSFSF RGMDAIREAM HGVFLYHAIK CGMDMGIVNA GNLPVYDDIH KELLQLCEDL IWSKDSDATE KLLHYAQTHA QGGKKVVQTD EWRNSSVEER LEYALVKGIE KYVVEDTEEA RLNKEKYSRP LHIIEGPLMN GMKTVGDLFG AGKMFLPQVI KSARVMKKAV GHLIPFMEQE REEMRAMSNS TEEEDPYHGT IVLATVKGDV HDIGKNIVGV VLGCNNFRVI DLGVMTPCDK ILRSALENKA DIIGLSGLIT PSLDEMIFVA KEMERLEIKI PLLIGGATTS KTHTAVKIAP RYSAPVIHVL DASKSVVVCS QLLDENVKDD FFEEIQEEYE DIRQDHYDSL KERKYLSLQQ ARNKGFSFDW LNDCRPVKPQ FLGTRVFEDY DLQKLVKYID WKPFFDVWQL RGRYPNRGFP KIFNDKTVGD EAKKVYNEAQ NLLRILIAEK KLTAKGLVGF WPARSVQDDI YLYDTDDDVE SSEPVAKFYG LRQQAEKDSS STDPYYCLSD FISPLKYGIP DYLGLFAVAC FGVDELCKEY EKQCDDYNII MIKALADRLA EAFAEELHER VRKEFWAYSE NEQLEFSDLR RIRYNGIRPA PGYPCQPDHT EKITMWKFAD IEEATGIQLT ESLAMLPASA VSGLYFSNPG SQYFAVGKIL KDQVEDYALR KNMSVAEIEK WLAPILGYDP E // ID G1KT34_ANOCA Unreviewed; 312 AA. AC G1KT34; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 04-MAR-2015, entry version 26. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSACAP00000016516}; DE Flags: Fragment; GN Name=LOC100558455 {ECO:0000313|Ensembl:ENSACAP00000016516}; OS Anolis carolinensis (Green anole) (American chameleon). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; OC Toxicofera; Iguania; Iguanidae; Polychrotinae; Anolis. OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000016516, ECO:0000313|Proteomes:UP000001646}; RN [1] {ECO:0000313|Ensembl:ENSACAP00000016516, ECO:0000313|Proteomes:UP000001646} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG The Genome Sequencing Platform; RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J., RA Lander E.S., Lindblad-Toh K.; RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard)."; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSACAP00000016516} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSACAP00000016516}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSACAT00000016842; ENSACAP00000016516; ENSACAG00000016768. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; G1KT34; -. DR OMA; WGVTKGT; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR Proteomes; UP000001646; Chromosome 2. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001646}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000001646}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 122 122 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 204 204 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 205 205 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSACAP00000016516}. SQ SEQUENCE 312 AA; 34525 MW; 4800AA87E387653B CRC64; GQKVNEAACN IAKEVAEEGD ALVAGGVSQT PSYLSSKSEA EIKSIFRKQL NIFMKQKVDF LIAEYFEHVE EAVWAVETLK ESGLPIAASL CIGPEGDMHG ISPGECAVRL VKAGASIVGV NCHFDPTTCL KTVKLMKEGL AAAKLKAHLM SQPLAFHTPD CGKQGFIDLP EFPFALEPRI LTRWDIHKYA REAYNLGIRY IGGCCGFEPY HIRAIAEELA PERGFLPHGS EKHGSWGSDL SMHTKPWVRA RARKEYWENL LPASGRPYCP SLSKPDDWGV TKGDAELIQQ KEATSEQQLK ELFNKQKLKS KV // ID G1L359_AILME Unreviewed; 1266 AA. AC G1L359; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSAMEP00000001319}; DE Flags: Fragment; GN Name=MTR {ECO:0000313|Ensembl:ENSAMEP00000001319}; OS Ailuropoda melanoleuca (Giant panda). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; OC Ailuropoda. OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000001319, ECO:0000313|Proteomes:UP000008912}; RN [1] {ECO:0000313|Ensembl:ENSAMEP00000001319} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20010809; DOI=10.1038/nature08696; RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., RA Li B., Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., RA Jian M., Li J., Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., RA Ryder O.A., Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., RA Guo X., Wang B., Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., RA Wang G., Yu C., Nie W., Wang J., Wu Z., Liang H., Min J., Wu Q., RA Cheng S., Ruan J., Wang M., Shi Z., Wen M., Liu B., Ren X., Zheng H., RA Dong D., Cook K., Shan G., Zhang H., Kosiol C., Xie X., Lu Z., RA Zheng H., Li Y., Steiner C.C., Lam T.T., Lin S., Zhang Q., Li G., RA Tian J., Gong T., Liu H., Zhang D., Fang L., Ye C., Zhang J., Hu W., RA Xu A., Ren Y., Zhang G., Bruford M.W., Li Q., Ma L., Guo Y., An N., RA Hu Y., Zheng Y., Shi Y., Li Z., Liu Q., Chen Y., Zhao J., Qu N., RA Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X., Vinar T., Wang Y., RA Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y., Wang X., RA Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L., RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., RA Wang J., Wang J.; RT "The sequence and de novo assembly of the giant panda genome."; RL Nature 463:311-317(2010). RN [2] {ECO:0000313|Ensembl:ENSAMEP00000001319} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 1}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSAMEP00000001319}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACTA01099952; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACTA01107952; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACTA01115952; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACTA01123952; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACTA01131952; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSAMET00000001371; ENSAMEP00000001319; ENSAMEG00000001206. DR GeneTree; ENSGT00420000029824; -. DR InParanoid; G1L359; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG7TF786; -. DR TreeFam; TF312829; -. DR Proteomes; UP000008912; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:Ensembl. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008912}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008912}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 258 258 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 783 783 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSAMEP00000001319}. SQ SEQUENCE 1266 AA; 141122 MW; D59315EDFAA8BE27 CRC64; ILQQYSVPHA GVKKSLQDEI EAILRERIMV LDGGMGTMIQ RHKLSEEDFR GHEFQDHARP LKGNNDILSI TQPSVIYQIH KDYLLAGADI IETNTFSSTN IAQADYGLEH LAYRMNKCSA GLARKAAEEV SFQTGIKRFV AGALGPTNKT LSVSPSVEKP DYRNITFDEL VEAYQEQAKG LLDGGADILL IETIFDTANA KAALFALQTL FEEEYSPRPI FISGTIIDKS GRTLSGQMGE AFVISVSHAD PLCIGLNCAL GAAEMRPFIE TIGKCTTAYV LCYPNAGLPN TFGDYDETPH MMATQLKDFA MDGLVNIVGG CCGTTPDHIR EIAKAVRNCK PRVPPATVFE EHMLLSGLEP FRIGPYTNFV NIGERCNVAG SRRFAKLIMA GNYEEALSVA KVQVEMGAQV LDINMDDGML DGSSAMTRFC NFIASEPDIA KVPLCIDSSN FAVIEAGLKC CQGKCIVNSI SLKEGEEDFL EKARKIKKFG AAVVVMAFDE EGQATETDTK ISVCMRAYRL LVKKLGFNPN DIIFDPNILT IGTGMEEHNL YAVNFIRATK IIKETLPGAR VSGGLSNLSF SFRGMEAIRE AMHGVFLYHA IKFGMDMGIV NAGNLPVYDD IHKELLQLCE DLIWNKDPEA TEKLLRYAQT HGKGGKKVIQ TDEWRNGPIE ERLEYALVKG IEKYIIEDTE EARLNQEKYP RPLNIIEGPL MNGMKVVGDL FGAGKMFLPQ VIKSARVMKK AVGHLIPFME KEREENKMHA GTEEKEDPYQ GTIVLATVKG DVHDIGKNIV GVVLGCNNFR VIDLGVMTPC DKILKAALDH KAEIIDIIGL SGLITPSLDE MIFVAKEMER LAIKIPLLIG GATTSRTHTA VKIAPRYSAP VIHVLDASKS VVVCSQLLDE NLKDEFFEEI LEEYEDIRQD HYESLKERRY LTLSQARKNG FHIDWLSEPP PVKPTFLGTR VFEDYDLRKL VAYIDWKPFF DVWQLRGKYP NRSFPKIFKD KTVGEEARKV YDDAQNMLEV LISQKKLRAR GVVGFWPAQS VEDDIHLYAE GATPQAAEPI ATFHGLRQQA EKDSASTDPY HCLSDFIAPL HSGVRDYLGL FAVACFGVEE LSKAYEQECD DYSSIMVKAL GDRLAEAFAE ELHERVRREL WAYCSCEQLD VADLRRLRYE GIRPAPGYPS QPDHSEKLTM WKLADVERCT GIRLTESLAM APASAVSGLY FSNLKSKYFA VGKISKDQIE DYAVRKNMSV AEVEKWLGPI LGYDIE // ID G1LGI1_AILME Unreviewed; 407 AA. AC G1LGI1; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSAMEP00000006021}; GN Name=BHMT {ECO:0000313|Ensembl:ENSAMEP00000006021}; OS Ailuropoda melanoleuca (Giant panda). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; OC Ailuropoda. OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000006021, ECO:0000313|Proteomes:UP000008912}; RN [1] {ECO:0000313|Ensembl:ENSAMEP00000006021} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20010809; DOI=10.1038/nature08696; RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., RA Li B., Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., RA Jian M., Li J., Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., RA Ryder O.A., Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., RA Guo X., Wang B., Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., RA Wang G., Yu C., Nie W., Wang J., Wu Z., Liang H., Min J., Wu Q., RA Cheng S., Ruan J., Wang M., Shi Z., Wen M., Liu B., Ren X., Zheng H., RA Dong D., Cook K., Shan G., Zhang H., Kosiol C., Xie X., Lu Z., RA Zheng H., Li Y., Steiner C.C., Lam T.T., Lin S., Zhang Q., Li G., RA Tian J., Gong T., Liu H., Zhang D., Fang L., Ye C., Zhang J., Hu W., RA Xu A., Ren Y., Zhang G., Bruford M.W., Li Q., Ma L., Guo Y., An N., RA Hu Y., Zheng Y., Shi Y., Li Z., Liu Q., Chen Y., Zhao J., Qu N., RA Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X., Vinar T., Wang Y., RA Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y., Wang X., RA Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L., RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., RA Wang J., Wang J.; RT "The sequence and de novo assembly of the giant panda genome."; RL Nature 463:311-317(2010). RN [2] {ECO:0000313|Ensembl:ENSAMEP00000006021} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSAMEP00000006021}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACTA01042075; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACTA01050075; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_002920330.1; XM_002920284.2. DR Ensembl; ENSAMET00000006270; ENSAMEP00000006021; ENSAMEG00000005696. DR GeneID; 100465664; -. DR KEGG; aml:100465664; -. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; G1LGI1; -. DR KO; K00544; -. DR OMA; WGVTKGT; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000008912; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006577; P:amino-acid betaine metabolic process; IEA:Ensembl. DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008912}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Reference proteome {ECO:0000313|Proteomes:UP000008912}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 217 217 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 407 AA; 45008 MW; 2AC6B42BFAA889B7 CRC64; MAPVGGKKAK RGILERLNAG EVVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAVRQLH REFLRAGSNV MQTFTFYASE DKLENRGNYV AEKISGQKVN EAACDIARQV ADEGDALVAG GVSQTPSYLS CKSETEVKKV FQQQLEVFMK KNVDFLIAEY FEHVEEAVWA VETLKTSGKP VAATMCIGPE GDLHGVSPGE CAVRLVKAGA SIVGVNCHFD PTISLQTVKL MKEGLEAARL KGHLMSQPLA YHTPDCSKQG FIDLPEFPFG LEPRVATRWD IQKYAREAYN LGVRYIGGCC GFEPYHIRAI AEELAPERGF LPPASDKHGS WGSGLDMHTK PWIRARARKE YWENLRIASG RPYNPSMSKP DAWGVTKGTA ELMQQKEATT EQQLKELFEK QKFISAQ // ID G1LGK1_AILME Unreviewed; 365 AA. AC G1LGK1; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSAMEP00000006041}; GN Name=BHMT2 {ECO:0000313|Ensembl:ENSAMEP00000006041}; OS Ailuropoda melanoleuca (Giant panda). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; OC Ailuropoda. OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000006041, ECO:0000313|Proteomes:UP000008912}; RN [1] {ECO:0000313|Ensembl:ENSAMEP00000006041} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20010809; DOI=10.1038/nature08696; RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., RA Li B., Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., RA Jian M., Li J., Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., RA Ryder O.A., Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., RA Guo X., Wang B., Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., RA Wang G., Yu C., Nie W., Wang J., Wu Z., Liang H., Min J., Wu Q., RA Cheng S., Ruan J., Wang M., Shi Z., Wen M., Liu B., Ren X., Zheng H., RA Dong D., Cook K., Shan G., Zhang H., Kosiol C., Xie X., Lu Z., RA Zheng H., Li Y., Steiner C.C., Lam T.T., Lin S., Zhang Q., Li G., RA Tian J., Gong T., Liu H., Zhang D., Fang L., Ye C., Zhang J., Hu W., RA Xu A., Ren Y., Zhang G., Bruford M.W., Li Q., Ma L., Guo Y., An N., RA Hu Y., Zheng Y., Shi Y., Li Z., Liu Q., Chen Y., Zhao J., Qu N., RA Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X., Vinar T., Wang Y., RA Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y., Wang X., RA Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L., RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., RA Wang J., Wang J.; RT "The sequence and de novo assembly of the giant panda genome."; RL Nature 463:311-317(2010). RN [2] {ECO:0000313|Ensembl:ENSAMEP00000006041} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSAMEP00000006041}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACTA01050075; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSAMET00000006290; ENSAMEP00000006041; ENSAMEG00000005719. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; G1LGK1; -. DR OMA; PEGDMHD; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000008912; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0061627; F:S-methylmethionine-homocysteine S-methyltransferase activity; IEA:Ensembl. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl. DR GO; GO:0046500; P:S-adenosylmethionine metabolic process; IEA:Ensembl. DR GO; GO:0033477; P:S-methylmethionine metabolic process; IEA:Ensembl. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008912}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Reference proteome {ECO:0000313|Proteomes:UP000008912}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 208 208 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 365 AA; 40077 MW; 54A803B17EDDC475 CRC64; MAPAGGPGAK KGILERLESG EVVVGDGSFL LTLEKRGYVK AGLWTPEAVV DHPDAVRQLH TEFLRAGSNV MQTFTFSASE DNMESKWEAV NEAACDLARE VAGKGDALVA GGICQTSLYR HHKDEVRVKK LFQLQLEVFI KKNMDFLIAE YFEHAEEAVW AVEVLKESGK PVAATMCIGP DGDMHGVTPG ECAVKLVKAG AAIVGVNCRF GPSTSLKTMR LMKEGLRAAG LKAHLIVQSL GFHTPDCGKG GFVDLPEYPF GLEPRVATRW DIQKYAREAY NLGVRYIGGC CGFEPYHIRA IAEELAPERG FLPPASDKHG SWGSSLNMHT KPWIRARHRA RREYWENLLP ASGRPFCPSL SRPDN // ID G1NAL4_MELGA Unreviewed; 394 AA. AC G1NAL4; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 04-MAR-2015, entry version 24. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMGAP00000009574}; DE Flags: Fragment; OS Meleagris gallopavo (Common turkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; OC Phasianidae; Meleagridinae; Meleagris. OX NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000009574, ECO:0000313|Proteomes:UP000001645}; RN [1] {ECO:0000313|Ensembl:ENSMGAP00000009574, ECO:0000313|Proteomes:UP000001645} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20838655; RA Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A., RA Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K., RA Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C., RA Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A., RA Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., RA de Jong P., Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., RA Lee M.K., Lee T., Mane S., Marcais G., Marz M., McElroy A.P., RA Modise T., Nefedov M., Notredame C., Paton I.R., Payne W.S., RA Pertea G., Prickett D., Puiu D., Qioa D., Raineri E., Ruffier M., RA Salzberg S.L., Schatz M.C., Scheuring C., Schmidt C.J., Schroeder S., RA Searle S.M., Smith E.J., Smith J., Sonstegard T.S., Stadler P.F., RA Tafer H., Tu Z.J., Van Tassell C.P., Vilella A.J., Williams K.P., RA Yorke J.A., Zhang L., Zhang H.B., Zhang X., Zhang Y., Reed K.M.; RT "Multi-platform next-generation sequencing of the domestic turkey RT (Meleagris gallopavo): genome assembly and analysis."; RL PLoS Biol. 8:E1000475-E1000475(2010). RN [2] {ECO:0000313|Ensembl:ENSMGAP00000009574} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSMGAP00000009574}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSMGAT00000010402; ENSMGAP00000009574; ENSMGAG00000009256. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; G1NAL4; -. DR OMA; WGVTKGT; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR Proteomes; UP000001645; Chromosome Z. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001645}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000001645}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 208 208 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSMGAP00000009574}. SQ SEQUENCE 394 AA; 43814 MW; 580D307913C0470C CRC64; QGILERLDAG EIVIGDGGFV FALEKRGYVK AGPWTPEATV EHPEAVTEYC GYNNICLGSN EIQTDTLLIR PFFLSKCGQE TPEWVYCQKV NEAACDIARE VASEGDAVVA GGVSQTPSYL SCKDKAEVKA VFRKQLDIFM KKNVDFLIAE YFEHVEEAVW AVEVLKESGK PVAATMCIGP EGDMHGVPPG QCAVQLVKAG ASIVGVNCHF DPDTALETXA ISIQSLKCHC LMAYLHLGCK RSHSPKTLER GTIYSQNFPE GLEPRIITRW DVQKYARKAY DLGIRYIGGC CGFEPYHIRA IAEELAPERG FLPEASEKHG SWGNSLSMHT KPWVRARARK EYWENLKPAS GRPYCPSMSK PDGWGVTKGA RELMQQKEAT TEQQLKELFQ KQKF // ID G1NGP9_MELGA Unreviewed; 1259 AA. AC G1NGP9; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 2. DT 27-MAY-2015, entry version 29. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMGAP00000012282}; DE Flags: Fragment; GN Name=MTR {ECO:0000313|Ensembl:ENSMGAP00000012282}; OS Meleagris gallopavo (Common turkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; OC Phasianidae; Meleagridinae; Meleagris. OX NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000012282, ECO:0000313|Proteomes:UP000001645}; RN [1] {ECO:0000313|Ensembl:ENSMGAP00000012282, ECO:0000313|Proteomes:UP000001645} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20838655; RA Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A., RA Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K., RA Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C., RA Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A., RA Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., RA de Jong P., Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., RA Lee M.K., Lee T., Mane S., Marcais G., Marz M., McElroy A.P., RA Modise T., Nefedov M., Notredame C., Paton I.R., Payne W.S., RA Pertea G., Prickett D., Puiu D., Qioa D., Raineri E., Ruffier M., RA Salzberg S.L., Schatz M.C., Scheuring C., Schmidt C.J., Schroeder S., RA Searle S.M., Smith E.J., Smith J., Sonstegard T.S., Stadler P.F., RA Tafer H., Tu Z.J., Van Tassell C.P., Vilella A.J., Williams K.P., RA Yorke J.A., Zhang L., Zhang H.B., Zhang X., Zhang Y., Reed K.M.; RT "Multi-platform next-generation sequencing of the domestic turkey RT (Meleagris gallopavo): genome assembly and analysis."; RL PLoS Biol. 8:E1000475-E1000475(2010). RN [2] {ECO:0000313|Ensembl:ENSMGAP00000012282} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 1}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSMGAP00000012282}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSMGAT00000013171; ENSMGAP00000012282; ENSMGAG00000011700. DR GeneTree; ENSGT00420000029824; -. DR InParanoid; G1NGP9; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG7TF786; -. DR TreeFam; TF312829; -. DR Proteomes; UP000001645; Chromosome 2. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:Ensembl. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001645}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001645}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 774 774 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSMGAP00000012282}. SQ SEQUENCE 1259 AA; 140303 MW; 13DAA726CC4060B7 CRC64; AANNRESVED EIESVLRERI MILDGGMGTM IQQYALSEED FRGHEFKDHS KPLKGNNDLL SITQPDIICD IHKEYLLAGA DIIETNTFSS TRVAQADYAL EHLAYRLNRI SAQVARKAAD DVTAQTGIKR YVAGSMGPTN RTLSVSPSVE RPDYRNITFD ELVEAYTEQA KGLLDGGVDV MLVETIFDTA NAKAALFALH KLFEEEYAPR PIFVSGTIVD KSGRTLSGQT GEAFVISVSH SKPLCIGLNC ALGAVEMRPF IETIGKCTTA YVICYPNAGL PNTFGGYDET PEVTAKHIKN FALDGLVNIV GGCCGTTPAH IRKIAEAVKL CKPRVPPSLC QGYMLLSGLE PFRIGPYTNF VNIGERCNVA GSRKFAKLIM AGNYEEALTV AKSQVEMGAQ ILDINMDDGM LDGPSAMTRF CNLISSEPDI AKVPLCIDSS NFSVIEAGLK CCQGKCIVNS ISLKEGEEDF LEKAKKIKLY GAAVVVMAFD EVGQATETET KIAICSRAYH LLVEKVHFNP NDIIFDPNIL TIGTGMEEHN LYAINFINAT KTIKETLPGV RISGGLSNLS FSFRGMDAIR EAMHGVFLYH AIRCGMDMGI VNAGNLPVYD DIHKELLQLC ENLIWNKDPD ATEKLLRYAQ NHAQGGKKVI QTDEWRNSTV EERLEYALVK GIEKYVTADT EEARLNQEKY PRPLNIIEGP LMNGMKIVGD LFGAGKMFLP QVIKSARVMK KAVSHLIPYM EKEREERRAK QGSSEEEDPY NGTIVLATVK GDVHDIGKNI VGVVLGCNNF RVIDLGVMTP CDKILRAAVE NKADIIGLSG LITPSLDEMI FVAKEMERLA IKIPLLIGGA TTSKTHTAVK IAPRYSAPVI HVLDASKSVV VCSQLLDESV KDDFFEEILE EYEEIRQEHY ESLKERRYLS LQQARRKGFH NDWLSDHKPV KPKFIGTKVF EDYDLKRLVE YIDWKPFFDV WQLRGKYPNR GFPKVFNDKT VGKLALKCYC VKQHLLMLSH EKILINQKKL QARGVLGFWP ARSVQDDIYL YAVEEAVGSS EPIAKFCGLR QQAEKDSACT DPYYCLSDFI APLDSGICDY LGLFAVACFG VDELCDDFRR QDDEYNIIMV KALGDRLAEA FAEELHERVR REFWAYCSDE QLDLSDLRKI KYKGIRPAPG YPSQPDHTEK LTMWKLANIE ETTGIGLTES LAMTPASAVS GLYFSSPKSK YFAVGKICKD QVEDYALRKK LSVAEVEKWL GPILGYDTE // ID G1P1K4_MYOLU Unreviewed; 1226 AA. AC G1P1K4; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMLUP00000003700}; DE Flags: Fragment; GN Name=MTR {ECO:0000313|Ensembl:ENSMLUP00000003700}; OS Myotis lucifugus (Little brown bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000003700, ECO:0000313|Proteomes:UP000001074}; RN [1] {ECO:0000313|Ensembl:ENSMLUP00000003700} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., RA Lindblad-Toh K.; RT "The genome sequence of Myotis lucifugus (Bat)."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000001074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [3] {ECO:0000313|Ensembl:ENSMLUP00000003700} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 1}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSMLUP00000003700}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAPE02047092; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSMLUT00000004061; ENSMLUP00000003700; ENSMLUG00000004053. DR GeneTree; ENSGT00420000029824; -. DR InParanoid; G1P1K4; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG7TF786; -. DR TreeFam; TF312829; -. DR Proteomes; UP000001074; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:Ensembl. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001074}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001074}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 221 221 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 746 746 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSMLUP00000003700}. SQ SEQUENCE 1226 AA; 135430 MW; E10D39251CD37D72 CRC64; TMIQRHKLSE EDFGQEFKDH ALPLKGNNDI LSITQPDVIY QIHKDYLLAG ADIIETNTFS STNVAQADYG LEHLVYRMNK CSAAVARKAA EEVTLQTGIK RFVAGALGPT NKTLSVSPSV ERPDFRNITF DELVEAYKEQ AQGLLDGGVD ILLVETIFDT ANAKAALFAL QNLFEETYAP RPIFISGTIV DKSGRTLSGQ TGEAFVISVS HADPLCIGLN CALGAAEMRP FIETIGKCTT AYVLCYPNAG LPNTFGDYEE TPSMMAVHLK GFAMDGLINI VGGCCGTTPD HIREIAEAVK NYKPRVPPAT VFEGHMLLSG LEPFRIGPYT NFVNIGERCN VAGSRNFAQL IMAGNYEAAL SVAKAQVEMG AQVLDINMDD GMLDGPSAMA RFCKLIASEP DIAKVPLCID SSNFAVIEAG LKCCQGKCIV NSISLKGGEA DFLEKAGLVK KFGAAVVVMA FDEEGQATET DTKIQVCTRA YHLLVGKLGF NPNDIIFDPN ILTIGTGMEE HSLYAVNFIH ATKVIKQTLP GAKISGGLSN LSFSFRGMDA IREAMHGVFL YHAIKFGMDM AIVNAGNLPV YDDIHKDLLQ LCEDLIWNKD PEATEKLLRY AQTHGKGGKK VVQTDEWRSG PVEERLEYAL VKGIEKHIIE DTEEARLNQD KYPRALNIIE GPLMNGMKVV GDLFGAGKMF LPQVIKSARV MKKAVGHLIP FMEKERKEAQ VLTGSVEEED PYQGTIVLAT VKGDVHDIGK NIVGVVLGCN NFRVIDLGVM TPCDKILKAA LDHKADIIGL SGLITPSLDE MIFVAKEMER LAIKIPLLIG GATTSRTHTA VKIAPRYSAP VIHVLDASKS VVVCSQLLDE NLKDEYFEEI TEEYEDIRQD HYESLKERRY LTLSQARKHS FHIDWLAEPP PVEPSFLGTR VFEDYDLQAL VGYIDWKPFF DVWQLRGKYP NRGFPKIFDD KTVGEEARRL YDDAQNMLRA LIGEKKLQAR GVVGFWPAQS EQDDIHLYPP GSEPRSAQPI ATFYGLRQQA EKDSASTDPY LCLADFIAPL HSGLRDYLGL FAVACFGVEE LSRAYEEQGD DYSSIMVKAL GDRLAEAFAE ELHERVRREL WAYCGSEQLD VADLRRLRYG GIRPAPGYPS QPDHTEKLTM WKLADIEQCT GIRLTESLAM APASAVSGLY FSNLKSKYFA VGKISKDQVE DYALRKNMSV AEVEKWLGPI LGYDTD // ID G1PD18_MYOLU Unreviewed; 365 AA. AC G1PD18; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMLUP00000008337}; DE Flags: Fragment; GN Name=BHMT2 {ECO:0000313|Ensembl:ENSMLUP00000008337}; OS Myotis lucifugus (Little brown bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000008337, ECO:0000313|Proteomes:UP000001074}; RN [1] {ECO:0000313|Ensembl:ENSMLUP00000008337} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., RA Lindblad-Toh K.; RT "The genome sequence of Myotis lucifugus (Bat)."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000001074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [3] {ECO:0000313|Ensembl:ENSMLUP00000008337} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSMLUP00000008337}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAPE02000644; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSMLUT00000009149; ENSMLUP00000008337; ENSMLUG00000009152. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; G1PD18; -. DR OMA; PEGDMHD; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR Proteomes; UP000001074; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0061627; F:S-methylmethionine-homocysteine S-methyltransferase activity; IEA:Ensembl. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl. DR GO; GO:0046500; P:S-adenosylmethionine metabolic process; IEA:Ensembl. DR GO; GO:0033477; P:S-methylmethionine metabolic process; IEA:Ensembl. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001074}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000001074}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 208 208 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSMLUP00000008337}. SQ SEQUENCE 365 AA; 40210 MW; 99B2163A3EF70242 CRC64; KLEALSPQTK YGILERLESG EVVVGDGGFL VTLEKRGYVK AGLWTPEVVV EHPEAVGQLH MEFLRAGANV MQTFTFSASE EKLESKWKDV NAAACDLARE VADKGDALVA GGICQTAIYK QDADEARVKR LFRLQVEVFA RKNVDFLIAE YFEHAEEAVW AVEVLKESGK PVAATMCIGP EGDKNDITPG ECAVKLVKAG ASIVGVNCRF GPGISLKTMK LMKEGLQAAG LKAHLMVQSL GFHTPDCGKG GFVDLPEYPF GLEPRTATRW DIQKYAREAY NLGVRYIGGC CGFEPYHIRA IAEELAPERG FWPAASDKHG IWGTGLNMHT KPWIRARHRA RREYWENLLP ASGRPFCPSL SKPDS // ID G1PD30_MYOLU Unreviewed; 406 AA. AC G1PD30; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMLUP00000008351}; GN Name=BHMT {ECO:0000313|Ensembl:ENSMLUP00000008351}; OS Myotis lucifugus (Little brown bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000008351, ECO:0000313|Proteomes:UP000001074}; RN [1] {ECO:0000313|Ensembl:ENSMLUP00000008351} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., RA Lindblad-Toh K.; RT "The genome sequence of Myotis lucifugus (Bat)."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000001074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [3] {ECO:0000313|Ensembl:ENSMLUP00000008351} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSMLUP00000008351}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAPE02000644; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_006081344.1; XM_006081282.1. DR Ensembl; ENSMLUT00000009163; ENSMLUP00000008351; ENSMLUG00000009164. DR GeneID; 102425902; -. DR CTD; 635; -. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; G1PD30; -. DR OMA; WGVTKGT; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000001074; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006577; P:amino-acid betaine metabolic process; IEA:Ensembl. DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001074}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Reference proteome {ECO:0000313|Proteomes:UP000001074}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 217 217 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 406 AA; 44811 MW; C75C424416E95049 CRC64; MAPIGGKKAK KGILERLNSG EVVIGDGGFV FSLEKRGYVK AGPWTPEAAV EHPEAVRQLH REFLRAGSNV MQTFTFYASE DKLENRGNYV AEKISGQKVN EAACDIARQV ADEGDALVAG GVSQTPSYLS CKSETEVKKV FQQQLEVFMK KNVDFLIAEY FEHVEEAVWA VEALKASGKP VAATMCIGPE GDLHGVTPGE CAVRLVKAGA SIVGVNCHFD PTISLQTVKL MKEGLQAAGL KAHLMSQPLA YHTPDCGKQG FIDLPEFPFG LEPRVATRWD IQKYAREAYN LGVRFIGGCC GFEPYHIRAI AEELAPERGF LPPASEKHGS WGSGLDMHTK PWIRARARKE YWENLRIASG RPYNPSMSKP DAWGVTKGTS MLMQQKEATT EQQLRELFEK QKYKSA // ID G1QTS1_NOMLE Unreviewed; 1264 AA. AC G1QTS1; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSNLEP00000004339}; GN Name=MTR {ECO:0000313|Ensembl:ENSNLEP00000004339}; OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates OS leucogenys). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hylobatidae; Nomascus. OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000004339}; RN [1] {ECO:0000313|Ensembl:ENSNLEP00000004339} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. RN [2] {ECO:0000313|Ensembl:ENSNLEP00000004339} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG Gibbon Genome Sequencing Consortium; RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 1}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSNLEP00000004339}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADFV01037041; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ADFV01037042; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ADFV01037043; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ADFV01037044; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ADFV01037045; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ADFV01037046; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ADFV01037047; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ADFV01037048; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSNLET00000004565; ENSNLEP00000004339; ENSNLEG00000003551. DR GeneTree; ENSGT00420000029824; -. DR InParanoid; G1QTS1; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG7TF786; -. DR TreeFam; TF312829; -. DR Proteomes; UP000001073; Unplaced. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001073}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001073}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 260 260 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 785 785 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1264 AA; 140362 MW; 4EF2DDEF8F798147 CRC64; MSPALQDLSQ PAGLKKTLRD EIDAILRKRI MVLDGGMGTM IQRQKLNEEH FRGQEFKDHA RPLKGNNDIL SITRPDVIYQ IHKEYLLAGA DIIETNTFSS TSIAQADYGL EHLAYQMNKC SAGVARKAAE EITLQTGIKR FVAGALGPTN KTLSVSPSVE RPDYRNITFD ELVEAYREQA KGLLDGGVDI LLIETIFDTA NAKAALFALQ NLFEEKYAPR PIFISGTIVD KSGRTLSGQT GEGFVVSVSH GEPLCIGLNC ALGAAEMRPF IEIIGKCTTA YVLCYPNAGL PNTFGDYDET PSVMAKHLKD FAMDGLVNIV GGCCGSTPDH IREIAEAVKN CKPRVPPATV FEGHMLLSGL EPFRIGPYTN FVNIGERCNV AGSRKFAKLI MAGNYEEALC VAKVQVEMGA QVLDVNMDDG MLDGPSAMTR FCNLIASEPD IAKVPLCIDS SNFAVIDAGL KCCQGKCIVN SISLKEGEDD FLEKARKIKK YGAAVVVMAF DEEGQATETD TKIRVCTRAY HLLVKKLDFN PNDIIFDPNI LTIGTGMEEH NLYAINFIHA TKVIKETLPG ARISGGLSNL SFSFRGMEAI REAMHGVFLY HAIKSGMDMG IVNAGNLPVY DDIHKELLQL CEDLIWNKDP EATEKLLRYA QTQGTGGKKV IQTDEWRNGP VEERLEYALV KGIEKHIIED TEEARLNQEK YPRPLNIIEG PLMNGMKIVG DLFGAGKMFL PQVIKSARVM KKAVGHLIPF MEKEREETRV LNGTVEEEDP YQGTIVLATV KGDVHDIGKN IVGVVLGCNN FRVIDLGVMT PCDKILKAAL DHKADIIGLS GLITPSLDEM IFVAKEMERL AIKIPLLIGG ATTSKTHTAV KIAPRYSAPV IHVLDASKSV VVCSQLLDEN LKDEYFEEIM EEYEDIRQDH YESLKERRYL PLSQAXXXXH QHQPYFSPVV RPMFIGTQVF EDYDLQKLVD YIDWKPFFDV WQLRGKYPNR GFPKIFNDKT VGGEAKKVYD DAHNMLNTLI SQKKLRARGV VGFWPAQSIQ DDIHLYAEGA VPQAAEPIAT FYGLRQQAEK DSASTEPYYC LSDFIAPLHS GIRDYLGLFA VACFGVEELS KAYEDDGDDY SSIMVKALGD RLAEAFAEEL HERVRRELWA YCGSEQLDVA DLRRLRYKGI RPAPGYPSQP DHTEKLTMWR LADIEQSTGI RLTESLAMAP ASAVSGLYFS NLKSTYFAVG KISKDQVEDY ALRKNISVAE VEKWLGPILG YDTD // ID G1RQR9_NOMLE Unreviewed; 363 AA. AC G1RQR9; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSNLEP00000015583}; GN Name=BHMT2 {ECO:0000313|Ensembl:ENSNLEP00000015583}; OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates OS leucogenys). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hylobatidae; Nomascus. OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000015583, ECO:0000313|Proteomes:UP000001073}; RN [1] {ECO:0000313|Ensembl:ENSNLEP00000015583} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG Gibbon Genome Sequencing Consortium; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSNLEP00000015583} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSNLEP00000015583}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADFV01197661; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ADFV01197662; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_003261561.1; XM_003261513.1. DR Ensembl; ENSNLET00000016376; ENSNLEP00000015583; ENSNLEG00000012819. DR GeneID; 100588253; -. DR KEGG; nle:100588253; -. DR CTD; 23743; -. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; G1RQR9; -. DR OMA; PEGDMHD; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000001073; Unplaced. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0061627; F:S-methylmethionine-homocysteine S-methyltransferase activity; IEA:Ensembl. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl. DR GO; GO:0046500; P:S-adenosylmethionine metabolic process; IEA:Ensembl. DR GO; GO:0033477; P:S-methylmethionine metabolic process; IEA:Ensembl. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001073}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Reference proteome {ECO:0000313|Proteomes:UP000001073}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 208 208 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 363 AA; 40315 MW; 53A5652C25B356FE CRC64; MAPAGRPGAK KGILERLESG EVVIGDGSFL ITLEKRGYVK AGLWTPEAVI EHPDAVRQLH MEFLRAGSNV MQTFTFSASE DNMESKWEDV NAAACDLARE VAGKGDALVA GGICQTSIYK YHKDEARIKK LFRQQLEVFA WKNVDFLIAE YFEHVEEAVW AVEVLKESDR PVAVTMCIGP EGDMHDITPG ECAVRLVKAG ASIVGVNCRF GPETSLKTME LMKEGLEQAG LKAHLMLQPL GFHTPDCGKE GFVDLPEYPF GLESRVATRW DIQKYAREAY NLGVRYIGGC CGFEPYHIRA IAEELAPERG FLPPASEKHG SWGSGLDMHT KPWIRARARR EYWENLLPAS GRPFCPSLSK PDV // ID G1RQT1_NOMLE Unreviewed; 406 AA. AC G1RQT1; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSNLEP00000015595}; GN Name=BHMT {ECO:0000313|Ensembl:ENSNLEP00000015595}; OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates OS leucogenys). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hylobatidae; Nomascus. OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000015595, ECO:0000313|Proteomes:UP000001073}; RN [1] {ECO:0000313|Ensembl:ENSNLEP00000015595} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG Gibbon Genome Sequencing Consortium; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSNLEP00000015595} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSNLEP00000015595}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADFV01197665; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ADFV01197666; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ADFV01197667; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_003261563.1; XM_003261515.2. DR Ensembl; ENSNLET00000016388; ENSNLEP00000015595; ENSNLEG00000012840. DR GeneID; 100588814; -. DR KEGG; nle:100588814; -. DR CTD; 635; -. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; G1RQT1; -. DR KO; K00544; -. DR OMA; WGVTKGT; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000001073; Unplaced. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006577; P:amino-acid betaine metabolic process; IEA:Ensembl. DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001073}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Reference proteome {ECO:0000313|Proteomes:UP000001073}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 217 217 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 406 AA; 45058 MW; 8C13623291350D7A CRC64; MPPVGGKKAK KGILERLNAG EIVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAVRQLH REFLRAGSNV MQTFTFYASE DKLENRGNYV LEKISGQKVN EAACDIARQV ADEGDALVAG GVSQTPSYLS CKSETEVKKI FLQQLEVFMK KNVDFLIAEY FEHVEEAVWA VETLIASGKP VAATMCIGPE GDLHGVPPGE CAVRLVKAGA SIIGVNCHFD PTISLQTVKL MKEGLEAARL KAHLMSQPLA YHTPDCNKQG FIDLPEFPFG LERIVTTRWD IQKYAREAYN LGVRYIGGCC GFEPYHIRAI AEELAPERGF LPPASEKHGS WGSGLDMHTK PWVRARARKE YWENLRIASG RPYNPSMSKP DGWGVTKGTA ELMQQKEATT EQQLKELFEK QKFKSQ // ID G1SMM6_RABIT Unreviewed; 404 AA. AC G1SMM6; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSOCUP00000004187}; GN Name=BHMT {ECO:0000313|Ensembl:ENSOCUP00000004187}; OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; OC Oryctolagus. OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000004187, ECO:0000313|Proteomes:UP000001811}; RN [1] {ECO:0000313|Ensembl:ENSOCUP00000004187} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000004187}; RG The Genome Sequencing Platform; RA Di Palma F., Heiman D., Young S., Gnerre S., Johnson J., Lander E.S., RA Lindblad-Toh K.; RT "Genome Sequence of Oryctolagus cuniculus (European rabbit)."; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000001811} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thorbecke {ECO:0000313|Proteomes:UP000001811}; RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [3] {ECO:0000313|Ensembl:ENSOCUP00000004187} RP IDENTIFICATION. RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000004187}; RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSOCUP00000004187}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSOCUT00000004840; ENSOCUP00000004187; ENSOCUG00000004842. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; G1SMM6; -. DR OMA; WGVTKGT; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000001811; Unplaced. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006577; P:amino-acid betaine metabolic process; IEA:Ensembl. DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001811}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Reference proteome {ECO:0000313|Proteomes:UP000001811}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 217 217 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 298 298 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 404 AA; 44325 MW; EBCF859626CFF25D CRC64; MAPVEGKKAK RGILERLNAG EVVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAVRQLH REFLRAGSNV MQTFTFYASE DKLENRGNYV AEKLSGQKVN EAACDIARQV ADEGDALVAG GVSQTPSYLS CKSEAEVKSI FQQQLAIFMK KNVDFLIAEY FEHVEEAVWA VETLKTSGKP VAATMCIGPE GDLHGVPPGE CAVRLVKAGA SIVGVNCHFD PMMSLQTVKL MKEGLAAARL HAYLMSQPLA YHTPDCSKQG FIDLPEFPFG PEPQGGPRWA SKSGRESYNL GVRYIGGCCG FPYHIRGIAE ELAPEGFLPA ASEKHGSWGS GLDMHTKPWI RARARREYWE NLRIASGRPY SPALSKPDAW GVTKGTAELM QQKEATTEQQ LRELFHKQKI QSAK // ID G1SXW3_RABIT Unreviewed; 1268 AA. AC G1SXW3; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSOCUP00000008420}; DE Flags: Fragment; GN Name=MTR {ECO:0000313|Ensembl:ENSOCUP00000008420}; OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; OC Oryctolagus. OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000008420, ECO:0000313|Proteomes:UP000001811}; RN [1] {ECO:0000313|Ensembl:ENSOCUP00000008420} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000008420}; RG The Genome Sequencing Platform; RA Di Palma F., Heiman D., Young S., Gnerre S., Johnson J., Lander E.S., RA Lindblad-Toh K.; RT "Genome Sequence of Oryctolagus cuniculus (European rabbit)."; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000001811} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thorbecke {ECO:0000313|Proteomes:UP000001811}; RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [3] {ECO:0000313|Ensembl:ENSOCUP00000008420} RP IDENTIFICATION. RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000008420}; RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 1}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSOCUP00000008420}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAGW02026464; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAGW02026465; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAGW02026466; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAGW02026467; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAGW02026468; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSOCUT00000009773; ENSOCUP00000008420; ENSOCUG00000009762. DR GeneTree; ENSGT00420000029824; -. DR InParanoid; G1SXW3; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG7TF786; -. DR TreeFam; TF312829; -. DR Proteomes; UP000001811; Chromosome 16. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:Ensembl. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001811}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001811}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 260 260 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 788 788 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSOCUP00000008420}. SQ SEQUENCE 1268 AA; 141170 MW; 2A9E659FE914B1EE CRC64; LSPSVSMLNL PADMKKTPQH EIEAILQKRI MVLDGGMGTM IQQYKLTEEH FRDQEFKDHA RPLKGNNDIL SITQPDIIYQ IHKEYLLAGA DIIETNTFSS TRIAQADYGL EHLAYRMNKC SAGVARKAAE EMTLQTGIKR FVAGALGPTN KTLSVSPSVE RPDYRNITFD ELVEAYQEQA RGLLDGGVDI LLIETIFDTA NAKAALFALQ QLFEEKYTPR PIFISGTIVD KSGRTLSGQT GEAFVISVSH ADPLCIGLNC ALGAAEMRPF IETIGKCTTS YIICYPNAGL PNTFGDYDET PSIMAAHLKN FAMDGLVNIV GGCCGSTPAH IRLREIAEAV KNCKPRIPPA TVFEGYMLLS GLEPFRIGPY TNFVNIGERC NVAGSRKFAK LIMAGNYEEA LSIAKLQVEM GAQVLDINMD DGMLDGPSAM TRFCNLIASE PDIAKVPLCI DSSNFAVIEA GLKCSQGKCI VNSISLKEGE DDFLEKARKI KKFGAAVVVM AFDEEGQATE TDVKIRVCTR AYHLLVKKLG FNPNDIIFDP NILTIGTGME EHNLYAINFI NATKVIKETL PGVRISGGLS NLSFSFRGME AIREAMHGVF LYHAIKENLD FHLFKRGRLF ICKTIHIYKP LTLCEEIIWS GPAKATAGLF GFIQTQGKGG KKVIQTDEWR NSPIEERLEY ALVKGIEKYI IEDTEEARLN QEKYPRPLNI IEGPLMNGMK VVGDLFGAGK MFLPQVIKSA RVMKKAVGHL IPFMEQEREA NRGLNDAAEE EDPYQGTIVL ATVKGDVHDI GKNIVGVVLG CNNFRVIDLG VMTPCDKILK AALDHKADII GLSGLITPSL DEMIFVAKEM ERLAIKIPLL IGGATTSRTH TAVKIAPRYS APVIHVLDAS KSVVVCSQLL DENLKDDYFE EIMEEYEDIR QDHYESLKER RYLPLSQARK NAFQIDWLSE PHPVKPTFIG TQVFEDYDLQ KLVDYIDWKP FFDVWQLRGK YPNRGFPKIF NDKTVGEEAR KVYDDAQNML NTLISQKKLQ GRGIVGFWPA QSVQDDVHLY AEDAVPQAAE PIATFYGLRQ QAEKDSASTD PYHCLADFIA PLHSGIRDYL GLFAVACFGV EELSKAYEDN GDDYSSIMVK ALGDRLAEAF AEELHERVRR ELWAYCGSEQ LDVADLRRLR YEGIRPAPGY PSQPDHTEKL TMWRLANIEE STGIKLTESL AMTPASAVSG LYFSNLKSKY FAVGKISKDQ IEDYALRKNM SVAEVEKWLG PILGYDTD // ID G1UPH3_9DELT Unreviewed; 798 AA. AC G1UPH3; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGW52523.1}; GN ORFNames=HMPREF1022_00496 {ECO:0000313|EMBL:EGW52523.1}; OS Desulfovibrio sp. 6_1_46AFAA. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=665942 {ECO:0000313|EMBL:EGW52523.1, ECO:0000313|Proteomes:UP000006424}; RN [1] {ECO:0000313|EMBL:EGW52523.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=6_1_46AFAA {ECO:0000313|EMBL:EGW52523.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGW52523.1}. 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; ACWM01000014; EGW52523.1; -; Genomic_DNA. DR EnsemblBacteria; EGW52523; EGW52523; HMPREF1022_00496. DR Proteomes; UP000006424; Unassembled WGS sequence. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006424}. SQ SEQUENCE 798 AA; 84319 MW; 01CF27DCF7DCC7A1 CRC64; MTFRQALGLG RPLLLDGAMG TMLQASGLPV GMSPEQFCME SPQVLRGIHK AYLDAGVDLL TTCTFGGNPY KLPKELDVFA FNKRMAEVAR EAAHDAGRPV FVAGNVGPSG QFAKPLGPVE PRELIAGFAA QIRGLVAGGA DLIFVETQFD LAEARAAVVA ARRECDLPVM VSMTFEQGVS LTGSSPAIFA ETMQNLGVDV VGTNCSLGPD QMLPVVRELL ETCACPVMAE PNAGLPELRG NVTVFPLGPE EFAQKTAAFA GLGARILGGC CGTTPRHLAA LAQAVRGMDY SPSEAARRDG ICLTSRSQLV RIGAGEALVI IGERINPTGK KVLTQELQEG RFDAALQLAD QQVEAGAGVL DVNVGASLVD ETSLLPELAQ RLIGRLTLPL SLDSSNAEAI AKALPYCPGS FLVNSISGEA DRMDVLGPLC RDYGAPFILL PLQGAKLPVQ ASERIRIVEN LLERAAGLGI PRRLVMVDIL ALAVSSKAEG GRQCLEMARW CRSQGLPTTL GLSNTSFGLP ARELLNATFL CMAAGAGLTS CIANPSATRL REAVDAMRVL GAHDPHAESF IASYAEWKPA GGVTLRQGDK AGAAKTLGEA VLTGDKENVL PLLEAELEAG ADPFALVRDT LIPAITEVGA RYERREYFLP QLIRAAETMQ TAFSHLKPRL EANRGPEERP VIVMATVEGD IHDIGKNIVA LLLGNHGFDV VDAGKDVPAE AIVACALEHN ARIIGLSALM TTTMVRMEDT IRLIRERDLP IKVMVGGAAV TQAFADAIGA DAYCPDAVCA VRAAKTFV // ID G1V3G0_9DELT Unreviewed; 257 AA. AC G1V3G0; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 07-JAN-2015, entry version 20. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGW45227.1}; DE Flags: Fragment; GN ORFNames=HMPREF0178_02057 {ECO:0000313|EMBL:EGW45227.1}; OS Bilophila sp. 4_1_30. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Bilophila. OX NCBI_TaxID=693988 {ECO:0000313|EMBL:EGW45227.1}; RN [1] {ECO:0000313|EMBL:EGW45227.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=4_1_30 {ECO:0000313|EMBL:EGW45227.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGW45227.1}. 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; ADCO01000180; EGW45227.1; -; Genomic_DNA. DR RefSeq; WP_009733332.1; NZ_JH114232.1. DR EnsemblBacteria; EGW45227; EGW45227; HMPREF0178_02057. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; FT NON_TER 257 257 {ECO:0000313|EMBL:EGW45227.1}. SQ SEQUENCE 257 AA; 27326 MW; 255A8FD93BE4CC17 CRC64; MADFRSALAS GRTLLLDGGM GTMLQARGLP AGEHPEQFCL DRPDVLRGIH ADYLAAGADI ILTCTFGGSR LKLPAGIDVT PFNRTMARIA RAAVDAAGRE AFVAGDMGPC GQFVRPLGDL HPLELYEALR EQARGLVEGG VDLFLIETQF DLAEVRIAVA AIRAESDLPI MVSMTFEQGT SLTGTTPEIF AETMQNLGVD ALGLNCGLGP EQMAPLMERF LACSSVPVLA EPNAGLPELV DGKTVFRLPP EPFAEKT // ID G1VAR9_9BACT Unreviewed; 915 AA. AC G1VAR9; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 01-APR-2015, entry version 24. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGW48364.1}; GN ORFNames=HMPREF0666_00502 {ECO:0000313|EMBL:EGW48364.1}; OS Prevotella sp. C561. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=563031 {ECO:0000313|EMBL:EGW48364.1}; RN [1] {ECO:0000313|EMBL:EGW48364.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C561 {ECO:0000313|EMBL:EGW48364.1}; 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., 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 Prevotella sp. C561."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGW48364.1}. 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; ADCT01000036; EGW48364.1; -; Genomic_DNA. DR RefSeq; WP_009010693.1; NZ_JH114140.1. DR EnsemblBacteria; EGW48364; EGW48364; HMPREF0666_00502. DR OrthoDB; EOG6091CH; -. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 240 240 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 915 AA; 100924 MW; A5B6F89C0593BBAB CRC64; MKLRDNIKDR ILILDGAMGT MIQGYHLTEQ DFRGNLELLQ MLNYQGNNDM LNLSRPDIIE DIHRRYLEVG ADIISTNTFS AQRVSQADYH MESFSRDIAY AGAKLARKCA DEYSTTDKPR YVAGSIGPTN KTCSMSPDVS DPAKRDLAYD ALFDAYSEQV AAMIEGGIDA VLIETIFDTL NAKVAIDASL SEMKKAGVDL PIMLSVTITD LSGRTLSGQT LDAFLASVSS YPIFSVGLNC SFGAEQMRPY LKELAAKAPY YISIHPNAGL PNSMGEYDET PEIMVPQMAS FVDEGLVNII GGCCGTTEEF IAGYVKVVEG KKPHIPVDAP KEMILSGLEQ FRLTPEISFV NVGERCNVAG SRKFLRLVKE KNYEEALTIA RKQVDDGALV LDINMDDGLL EAKDEMAHFV NMISSEPEIA RVPLMIDSSD WEVVVSALKC VQGKAIVNSI SLKEGEEVFI RHAKDVLRFG AAVVVMCFDE EGQATSYERR IEIAERAYKI LTEKVGFPPQ DIIFDPNILA ICTGMKEHNS YAVDFIRATE WIKKNLPGAH VSGGVSNLSF SFRGNNYIRE AMHAVFLYHA IQVGMDFGIV NPATKVTYAD IPEDHLKIIE DVVLDRVEGA DELLIELANK ILEEKEAQKN GGATQEVEQE AWRNEALEDR LKYALRKGIS TYLNEDIHEA LEKYPHAVNI IEGPLMQGMN EVGDLFGAGK MFLPQVVKTA RTMKDAVAIL QPYIEKEKVD GKAIAGKVLL ATVKGDVHDI GKNIVGVVMA CNNYEVIDLG VMVPADQIIK KAKEENVDLI GLSGLITPSL QEMVNSVVAF KEAGLNIPVM IGGATTSQLH VALKIAPLYD APVVWVKDAS VNPSIAAALL NDKERERFCK DLDATYEKLR AGYKEEQQKV LSLSKARENK LNLFE // ID G1VT53_9FIRM Unreviewed; 786 AA. AC G1VT53; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGX73358.1}; GN ORFNames=HMPREF9022_03184 {ECO:0000313|EMBL:EGX73358.1}; OS Erysipelotrichaceae bacterium 2_2_44A. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae. OX NCBI_TaxID=457422 {ECO:0000313|EMBL:EGX73358.1}; RN [1] {ECO:0000313|EMBL:EGX73358.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=2_2_44A {ECO:0000313|EMBL:EGX73358.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGX73358.1}. 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; ADCZ01000030; EGX73358.1; -; Genomic_DNA. DR RefSeq; WP_002607615.1; NZ_JH126434.1. DR EnsemblBacteria; EGX73358; EGX73358; HMPREF9022_03184. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; SQ SEQUENCE 786 AA; 85124 MW; 276163967E5F0921 CRC64; METEDRILFL DGAMGTQLQA NGLPAGASPE IFMMEHGNII EEIHAAYIDS GSDIIYTNTF GANAKKLTKT RYTVEEIVTT AVQLAKSAAK RKPGVRVALD IGPIGELLEP NGYLPFDDAY DLFAEQVIVG EKAGADLIVF ETMSDLYEVK AAILAAKEHT RLPVFVTMSF EADHRTFTGC TTASFALCAE GLGADAIGIN CSLGPDQILP IAEELAAMSN LPLIIKANAG LPDPVTNTYS INASGYAQML TAFTKLPVTY VGGCCGTTPQ FIRELKKTLP ETIDLSLRKQ RSGSYACTPT KCLHIQDVHV IGERINPTGN KRMKAALLEH RMDEILAIAM EEVAGGADIL DVNVGLPGID EKAMMVEVIG ELQSVIDLPL QIDSTDPDVI EAALRAVNGV AIVNSVNGEA GVMERILPSV KKYGANVVGL TMDEGGIPQS ARERLVIGTR IVETAERYGI ARDRVFLDCL TLTVSAQQSG ARETLQALTD IRSQLGVHTV LGVSNISFGL PSRITLNQNF LTMAMQAGLS MPIMNPNQTA MMDAVRSYRV LYGIDIDSQE YIRIYAQQKK AEMKPASASS QANIEDSIMH GLKEETRHQC CELLKMKEPL QIVNEHLIPA LDAVGSRYEK KEIYLPQLIN AATASQCAFE EIRKHMQSSG LESISKGKII LATVKGDVHD IGKNIVKVVL ENYGYQVFDL GKDVAVEAVV ETAIKEQVRL IGLSALMTTT LKSMEDTITA LHESGHDCKI MVGGAVVSPE YAKQIHADYY AKDAKESADI AREVLG // ID G1VT54_9FIRM Unreviewed; 316 AA. AC G1VT54; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGX73359.1}; GN ORFNames=HMPREF9022_03185 {ECO:0000313|EMBL:EGX73359.1}; OS Erysipelotrichaceae bacterium 2_2_44A. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae. OX NCBI_TaxID=457422 {ECO:0000313|EMBL:EGX73359.1}; RN [1] {ECO:0000313|EMBL:EGX73359.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=2_2_44A {ECO:0000313|EMBL:EGX73359.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGX73359.1}. 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; ADCZ01000030; EGX73359.1; -; Genomic_DNA. DR RefSeq; WP_002607614.1; NZ_JH126434.1. DR EnsemblBacteria; EGX73359; EGX73359; HMPREF9022_03185. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 316 AA; 35601 MW; 10B0ECDC439989FB CRC64; MITELLKEQG YFLFDGAFGT YYAQKYEDDQ EPCELANLNH PERVAAIHQE YIEAGADAIK TNTFSANEQH LECSWDMIQR ILQEGYHIAR DAAQGRARVF ADIGPIMEQK NVSVAAQYQR IADVFLEEGA DCFLFETFLN THELRLVTSY IKERCPHACI VVSFAVTADG YSRQGIAMNR LLQDCLEDDD VDACGLNCVC GPMHMKRLLD SIDRTIKPIL IMPNAGYPTI LANRTYFRDS SSYFAGEMKQ IWQKGAKLLG GCCGTTPVYI QKLKEALMVQ DGVQKTTQPS QALKKSYRRT AIRCAESCRS ISPSLR // ID G1W9J4_9BACT Unreviewed; 921 AA. AC G1W9J4; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGV34316.1}; GN ORFNames=HMPREF9431_00495 {ECO:0000313|EMBL:EGV34316.1}; OS Prevotella oulorum F0390. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=702438 {ECO:0000313|EMBL:EGV34316.1}; RN [1] {ECO:0000313|EMBL:EGV34316.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0390 {ECO:0000313|EMBL:EGV34316.1}; 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., 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., 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 Prevotella oulorum F0390."; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGV34316.1}. 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; ADGI01000017; EGV34316.1; -; Genomic_DNA. DR RefSeq; WP_004379483.1; NZ_JH114215.1. DR EnsemblBacteria; EGV34316; EGV34316; HMPREF9431_00495. DR OrthoDB; EOG6091CH; -. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 242 242 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 921 AA; 101372 MW; 2897738435365E93 CRC64; MKKLQDVIQD RILILDGALG TMFQTYALSE EDYRGTLFQN CPQKQLKGNH DLLNLTRPDV VLDVHRRYLK AGADIIETNT FSAQRISQAD YGLEADSYKI ALEGARLAKT AAMEFATEEK PRFVAGSIGP TNKTCSMSPD VNSPATRNLT YDELYEAYAE EIRGLLNGGV DAFLIETIFD TLNAKVAIDA AIAIMAEYKR ELPIMISATI SDLAGRTLSG QTLEGFLGSL SGYPIFSVGL NCSFGARQMK PFLASLAHKA PYYISVYPNA GLPNSLGQYD ESADSMAQQI EEYLDEGLVN IVGGCCGTTD EFIAKFSQLA KGRKPHRINA KSDAMWLSGL ELLELTPDIR FVNVGERCNV AGSRKFLRLI ENKQYDEALA IARKQVADGA MVIDVNMDDG LLDAKSEMVN FLNLVASDPD VSRVPIMIDS SKWDVILAGL KCIQGKSIVN SISLKNGEEV FLREARDVKR YGAAVVVMCF DEQGQATSYE RKIEIAARSY RLLTEKVGIN PQDIIFDPNI LSIATGIEEH NNYAVDFIKA VGWIKKNLPG AHVSGGVSNL SFSFRGNNDI REAMHAVFLY HAIQQGMDFG IVNPATKMVY ADLPKDWLTT IEDVVLNKDA EASERLIDLA NRVKAEQEQR KNGARAVAEQ HEAWRETDVA QRLAYALRKG ISDYLEVDLA EARQQYPHAV DIIEGPLMAG MNEVGELFGT GKMFLPQVVK TARTMKQAVA ILQPFIEAEK AEGNYVAGKI LLATVKGDVH DIGKNIVGVV MACNNYEVID LGVMVPAEQI VAEAIAHRVD MIGLSGLITP SLEEMVHVAQ EMEKAGLHIP IMIGGATTSQ LHVALKIAPA YSGPVVWMKD ASQNALVAAH LLNDEARERL KHELNAKYDE LRQRFEQRQA KTISLEEARA NKLNLFPTPN A // ID G1WIU6_9ACTN Unreviewed; 840 AA. AC G1WIU6; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGX70754.1}; GN ORFNames=HMPREF9452_01259 {ECO:0000313|EMBL:EGX70754.1}; OS Collinsella tanakaei YIT 12063. OC Bacteria; Actinobacteria; Coriobacteridae; Coriobacteriales; OC Coriobacterineae; Coriobacteriaceae; Collinsella. OX NCBI_TaxID=742742 {ECO:0000313|EMBL:EGX70754.1}; RN [1] {ECO:0000313|EMBL:EGX70754.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=YIT 12063 {ECO:0000313|EMBL:EGX70754.1}; 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., 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 Collinsella tanakaei YIT 12063."; 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. {ECO:0000313|EMBL:EGX70754.1}. 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; ADLS01000016; EGX70754.1; -; Genomic_DNA. DR RefSeq; WP_009141294.1; NZ_JH126469.1. DR EnsemblBacteria; EGX70754; EGX70754; HMPREF9452_01259. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; SQ SEQUENCE 840 AA; 88820 MW; 233917816AFE4B99 CRC64; MTIVQSTQAY TPRTLDTLRI ADDNLRAALE GRRHLLFDGG MGTMLQAAGL KAGALPELLC LTNPDAITRV HAAYVAGGSE VVTTNTFGAN ALKLHGEATV EEVFNAAVAC ARAAGARYVA GDIGPLGTLL RPLGTMGFDE AYDYFAQEAR AAQAAGCDLI IIETMTDLAE IKAAVLAAKE NCDLPIFATM TFEADGRTFL GTSPDIAAIT LDALGADVVG INCSLGPAEL RPFARTMLAV TAKPVMVQAN AGLPHVEDGC TVFDIDPQSY AAAVANMVED GVGIIGGCCG TNPDYIRLLA DIIADRAPQQ RPAPASFTVT GAQRLVELPQ DSHRVAVIGE RINPTGKKRL QAALREGNLD YVVGQGISQQ EQGADVLDVN VGLPGIDEPR MIARAVEALQ GATLLPLQID STNADAIEAG VRAYAGKPII NSVNGKQEVL DAVLPIAAHY GCNVIGLTLD EDGIPATASE RVAIARRIID EAARYGISRE RILIDCLVMT ASTNQAQVTE ILRAVTLCRQ ELGVHCTLGV SNVSFGLPAR ELLNATFLAA AFGAGLDAPI MNPGSQRYMD AVYSYRVLNA EDLGSAQFIE CYAGWNDPYK VPVNVASTPT VPSSTAPATS PNTAPSPASA TSAQGNGELH HLVLSGRKAD VPALVRDLLA EHDAMDVIDR MLIPALDEVG DKFDRGEFFL PQLMASAEAA RAGFDTIRDL MPAGNVADKG KIALATVKGD IHDIGKNIVK MLLENYGYRV YDLGRDVDPQ VVLDAVRQHD IPLVGLSALM TTTVTNMEET IALLRREAPG VRVFVGGAVL TPEYARQIGA DFYAKDAAES ARIAERVFAK // ID G1WKA4_9ACTN Unreviewed; 320 AA. AC G1WKA4; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGX69433.1}; GN ORFNames=HMPREF9452_01724 {ECO:0000313|EMBL:EGX69433.1}; OS Collinsella tanakaei YIT 12063. OC Bacteria; Actinobacteria; Coriobacteridae; Coriobacteriales; OC Coriobacterineae; Coriobacteriaceae; Collinsella. OX NCBI_TaxID=742742 {ECO:0000313|EMBL:EGX69433.1}; RN [1] {ECO:0000313|EMBL:EGX69433.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=YIT 12063 {ECO:0000313|EMBL:EGX69433.1}; 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., 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 Collinsella tanakaei YIT 12063."; 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. {ECO:0000313|EMBL:EGX69433.1}. 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; ADLS01000023; EGX69433.1; -; Genomic_DNA. DR RefSeq; WP_009141758.1; NZ_JH126472.1. DR EnsemblBacteria; EGX69433; EGX69433; HMPREF9452_01724. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 320 AA; 33174 MW; 07F1ABF170B36432 CRC64; MAAQDYYNRD AAKELMDRLA AGPLVAQGPT GSLLADEAGT ADVPAAFWNI AEPQALTRMH ALYQMAGADV LITNTFQASA PCLKRDSILQ DYRSVNRAGA DCALTCSRIT GVPAKLVLGS VGPCGIAWED ADKEEGEEGT KADKEAESAV HKLAREAYRN QATILLESGV AGVLLETFCS LHDLEPAVTG AVEAAHGMPV LASFAIDDAC HLLGDGAAIE QACEAARDLG AQAVGVNCCS VCAATQAVPR MVRAVDLPVM VRPNAGAPTV DQDGCPHWDE DVEGVARASV QWVADGARLV GTCCGFTPIA TCAISGALHG // ID G1WMG2_9FIRM Unreviewed; 801 AA. AC G1WMG2; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGX67719.1}; GN ORFNames=HMPREF9457_00313 {ECO:0000313|EMBL:EGX67719.1}; OS Dorea formicigenerans 4_6_53AFAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Dorea. OX NCBI_TaxID=742765 {ECO:0000313|EMBL:EGX67719.1}; RN [1] {ECO:0000313|EMBL:EGX67719.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=4_6_53AFAA {ECO:0000313|EMBL:EGX67719.1}; 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. {ECO:0000313|EMBL:EGX67719.1}. 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; ADLU01000009; EGX67719.1; -; Genomic_DNA. DR RefSeq; WP_005336605.1; NZ_JH126487.1. DR EnsemblBacteria; EGX67719; EGX67719; HMPREF9457_00313. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; SQ SEQUENCE 801 AA; 87489 MW; C08588840081C7E4 CRC64; MILDRLGKEL IYFDGGTGTL LQERGLKPGE LPETWSLERA DDMIDIARQY YEAGSDIVLS NTFGANALKF HDSRHKLDEI VKAAIENVRK GAKLGVKDGR ETYVGLDIGP TGKLLKPMGD LDFEDAYQAF AEVARLGEEA GADLIHIETM SDTYEVKTAV LAAKENTSLP VFATMIFDDK GKLLTGGDVP SVVAMLEGLR VDALGINCGM GPEQMMPILD EILQYASVPV IVKPNAGLPK QKDGEVYYDV EPEEFGRFMA EILKRGASLI GGCCGTTPAH IRAMVEATKD QRDITDRPGK EFMNRTIVSS YGRAVELGGK PMIIGERINP TGKKKFKQAL KDHDIDYILR EAISQQDAGA HILDVNVGLP DIDEPALMRE VVQELQSVTS LPLQIDTVDI SALEAAMRIY NGKPMVNSVN GKKSSMDAVF PLIQKYGGVV VGLTLDEDGI PATAEGRVKV AGKIIEEAKK YGIDKKDIVI DVLCMTISSE PTGAITTLEA LRQVREKYGV CAVLGVSNIS FGLPYRPAVN SNFYTMAMQS GLSAGIINPL SEDMMRSYYS FCALMNYDEN CEKYIEQYGS QKVQAVTPAT KAEMTLKTAI EKGLKEEAHH ITAELVKDKA PLDIINEELI PALDQVGKGF EKGTVFLPQL LMSADAAKIA FAVLKDELAR SGESEQAKDK VILATVKGDI HDIGKNIVKV LLENYSFDVI DLGKDVPPEE IVETAIKEDV RLVGLSALMT TTVVSMEETI RQLRKKKPEC KVMVGGAVLN QDYSDMIGAD FYGKDAMQSV YYAQQLFGGE K // ID G1XM96_ARTOA Unreviewed; 342 AA. AC G1XM96; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 07-JAN-2015, entry version 16. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGX45749.1}; GN ORFNames=AOL_s00140g65 {ECO:0000313|EMBL:EGX45749.1}; 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 {ECO:0000313|EMBL:EGX45749.1, ECO:0000313|Proteomes:UP000008784}; RN [1] {ECO:0000313|EMBL:EGX45749.1, ECO:0000313|Proteomes:UP000008784} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491 RC {ECO:0000313|Proteomes:UP000008784}; 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. {ECO:0000313|EMBL:EGX45749.1}. 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; ADOT01000227; EGX45749.1; -; Genomic_DNA. DR InParanoid; G1XM96; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000008784; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008784}; KW Reference proteome {ECO:0000313|Proteomes:UP000008784}. SQ SEQUENCE 342 AA; 37968 MW; 7EA29D559A7EE06B CRC64; MSTPIIILDG ALGTLLCDTT SPEASASPLW SSIDLLHNPS RLADVHAQYI KAGAGCIETA TYQLCRETLL RSGVSDEDQM RKICHAAMQL AVDATKDLKP TGNNNNNASV ALSLGPFGMC LHPSQEYSGA YPPPYNTDSA DAVDALEKWH RDRLQAFQKA SNDAFEEIDI LAFETVPYKR VDEIIAIRRV IDSEEFRGRK AWISMVYTEV PKEEVIGRIT RKVFEDIPFG STQRGIGINC TKLENVREIV RVYSKTIIDI GIRKEDVFLV LYPDGGLTYD VNTKTWSDEN GMAEVEKWCR LLQKIVEEAV NDGCWGSIII GGCCKTTPEH ISELSKTFAA IQ // ID G2ANR2_ECOLX Unreviewed; 1227 AA. AC G2ANR2; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGW84689.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGW84689.1}; GN Name=metH {ECO:0000313|EMBL:EGW84689.1}; GN ORFNames=ECSTECDG1313_5237 {ECO:0000313|EMBL:EGW84689.1}; OS Escherichia coli STEC_DG131-3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=754086 {ECO:0000313|EMBL:EGW84689.1}; RN [1] {ECO:0000313|EMBL:EGW84689.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=STEC_DG131-3 {ECO:0000313|EMBL:EGW84689.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGW84689.1}. 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; AFDV01000066; EGW84689.1; -; Genomic_DNA. DR RefSeq; WP_000096010.1; NZ_AFDV01000066.1. DR ProteinModelPortal; G2ANR2; -. DR SMR; G2ANR2; 651-1227. DR EnsemblBacteria; EGW84689; EGW84689; ECSTECDG1313_5237. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGW84689.1}; KW Transferase {ECO:0000313|EMBL:EGW84689.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135969 MW; 31A0CAA1E9127CD9 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID G2B2U7_ECOLX Unreviewed; 1223 AA. AC G2B2U7; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 01-APR-2015, entry version 19. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGW89026.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGW89026.1}; GN Name=metH {ECO:0000313|EMBL:EGW89026.1}; GN ORFNames=ECSTECEH250_4795 {ECO:0000313|EMBL:EGW89026.1}; OS Escherichia coli STEC_EH250. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=754087 {ECO:0000313|EMBL:EGW89026.1}; RN [1] {ECO:0000313|EMBL:EGW89026.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=STEC_EH250 {ECO:0000313|EMBL:EGW89026.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGW89026.1}. 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; AFDW01000038; EGW89026.1; -; Genomic_DNA. DR EnsemblBacteria; EGW89026; EGW89026; ECSTECEH250_4795. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGW89026.1}; KW Transferase {ECO:0000313|EMBL:EGW89026.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 243 243 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 755 755 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1223 AA; 135596 MW; A0C63D8D74F42CC8 CRC64; MEQLRAQLNE RILVLDGGMG TMIQSYRLNE ADFRGERFAD WPCDLKGNND LLVLSKPEVI AAIHNAYFEA GADIIETNTF NSTTIAMADY QMESLSAEIN FAAAKLARAC ADEWTARTPE KPRYVAGVLG PTNRTASISP DVNDPAFRNI TFDGLVAAYR ESTKALVEGG ADLILIETVF DTLNAKAAVF AVKTEFEALG VELPIMISGT ITDASGRTLS GQTTEAFYNS LRHAEALTFG LNCALGPDEL RQYVQELSRI AECYVTAHPN AGLPNAFGEY DLDADTMAKQ IREWAQAGFL NIVGGCCGTT PQHIAAMSRA VEGLAPRKLP EIPVACRLSG LEPLNIGEDS LFVNVGERTN VTGSAKFKRL IKEEKYSEAL DVARQQVENG AQIIDINMDE GMLDAEAAMV RFLNLIAGEP DIARVPIMID SSKWDVIEKG LKCIQGKGIV NSISMKEGVD AFIHHAKLLR RYGAAVVVMA FDEQGQADTR ARKIEICRRA YKILTEEVGF PPEDIIFDPN IFAVATGIEE HNNYAQDFIG ACEDIKRELP HALISGGVSN VSFSFRGNDP VREAIHAVFL YYAIRNGMDM GIVNAGQLAI YDDLPAELRD AVEDVILNRR DDGTERLLEL AEKYRGSKTD DTANAQQAEW RSWEVNKRLE YSLVKGITEF IEQDTEEARQ QATRPIEVIE GPLMDGMNVV GDLFGEGKMF LPQVVKSARV MKQAVAYLEP FIEASKEQGK TNGKMVIATV KGDVHDIGKN IVGVVLQCNN YEIVDLGVMV PAEKILRTAK EVNADLIGLS GLITPSLDEM VNVAKEMERQ GFTIPLLIGG ATTSKAHTAV KIEQNYSGPT VYVQNASRTV GVVAALLSDT QRDDFVARTR KEYETVRIQH GRKKPRTPPV TLEAARDNDF AFDWQAYTPP VAHRLGVQEV EASIETLRNY IDWTPFFMTW SLAGKYPRIL EDEVVGVEAQ RLFKDANDML DKLSAEKTLN PRGVVGLFPA NRVGDDIEIY RDETRTHVIN VSHHLRQQTE KTGFANYCLA DFVAPKLSGK ADYIGAFAVT GGLEEDALAD AFEAQHDDYN KIMVKALADR LAEAFAEYLH ERVRKVYWGY APNENLSNEE LIRENYQGIR PAPGYPACPE HTEKATIWEL LEVEKHTGMK LTESFAMWPG ASVSGWYFSH PDSKYYAVAQ IQRDQVEDYA RRKGMSVTEV ERWLAPNLGY DAD // ID G2DDA5_9GAMM Unreviewed; 669 AA. AC G2DDA5; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGV51423.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGV51423.1}; GN Name=metH' {ECO:0000313|EMBL:EGV51423.1}; GN ORFNames=Rifp1Sym_bk00260 {ECO:0000313|EMBL:EGV51423.1}; OS endosymbiont of Riftia pachyptila (vent Ph05). OC Bacteria; Proteobacteria; Gammaproteobacteria; OC sulfur-oxidizing symbionts. OX NCBI_TaxID=1048808 {ECO:0000313|EMBL:EGV51423.1}; RN [1] {ECO:0000313|EMBL:EGV51423.1} 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGV51423.1}. 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; AFOC01000038; EGV51423.1; -; Genomic_DNA. DR RefSeq; WP_005961397.1; NZ_AFOC01000038.1. DR EnsemblBacteria; EGV51423; EGV51423; Rifp1Sym_bk00260. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGV51423.1}; KW Transferase {ECO:0000313|EMBL:EGV51423.1}. SQ SEQUENCE 669 AA; 73024 MW; 09056189EDFF7897 CRC64; MAGPIMDNIT PELESILCER ILILDGAMGT MIQRHKLTEE DYRGERFTDW PSDLKGNNDL LVLSQPELIR NIHEEYMEAG ADILETNTFG ANRISMADYD MQELAYEMNV AGARLCREAA DKYATPEKPR YVAGVLGPTN RTASISPDVN DPGARNISFD ELVEAYAEAT RGLIEGGVDI LLIETIFDTL NAKAAVAACE QVFDQDQLRL PIMVSGTITD ASGRTLSGQT TEAFYNSLRH ARPISIGLNC ALGPELMRQY VEEISRVAEC YVNVHPNAGL PNEFGEYDLG PEAMGQQIAE WAEAGFLNII GGCCGTTPAH IKAIAEAVAD QAPRKLPEIR PECRLSGLEP LNIGPDSLFV NVGERANVTG SAKFKRLILN EEYEEALDVC RAQVENGAQV VDVNMDEAML DGVAAMQRFL NLCAGEPDIS KVPVMIDSSK WEIIEAGLKC VQGKPIVNSI SMKEGIDKFK QQAKLCRRYG AAVIVMAFDE EGQADTQARK VEICTRAYQI LTEEVGFPAE DIIFDPNIFA VATGIPEHDN YGVDFIEATR EIKAACPHAL ISGGVSNVSF SFRGNNPVRE AIHAVFLYHA IQAGMDMGIV NAAQLAVYDD LPAELRNAVE DVVLNKDPEA GDRLVEIAPN YAGDVVGGNR WRIWSGAAGR STNGWSTPW // ID G2DYV6_9GAMM Unreviewed; 1252 AA. AC G2DYV6; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGV32465.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGV32465.1}; GN ORFNames=ThidrDRAFT_1315 {ECO:0000313|EMBL:EGV32465.1}; OS Thiorhodococcus drewsii AZ1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Thiorhodococcus. OX NCBI_TaxID=765913 {ECO:0000313|EMBL:EGV32465.1}; RN [1] {ECO:0000313|EMBL:EGV32465.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AZ1 {ECO:0000313|EMBL:EGV32465.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGV32465.1}. 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; AFWT01000007; EGV32465.1; -; Genomic_DNA. DR RefSeq; WP_007040029.1; NZ_AFWT01000007.1. DR EnsemblBacteria; EGV32465; EGV32465; ThidrDRAFT_1315. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGV32465.1}; KW Transferase {ECO:0000313|EMBL:EGV32465.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1252 AA; 137214 MW; 3359493B563F24C6 CRC64; MTYSTALIRE RLERSILILD GAMGTMIQRH GLTEADYRGE RFVDWPSDLK GNNDLLALTR PDVIEGIHRQ YLEAGADIIE TNSFNATSVA MADYGMEALA YEINVAAARL ARQAADAIGT EDKPRFVAGV LGPTNRTASI SPDVNDPGYR NIDFDTLVTA YADSTRGLIE GGADIILIET IFDTLNAKAA VFAVRKVFDE DGVELPIMIS GTITDQSGRT LTGQTTEAFY NSLRHADPLS IGLNCALGPS ELRQYVEELA RIAECRVSTH PNAGLPNELG GYDLGPEEMA TEIAEWARSG FLNIIGGCCG TTPDHIRAIA AAVEGMAPRP LPDIAPACRL SGLEPFNIGA ETLFVNVGER TNVTGSARFK RLIKEEDYDT ALSVAQEQVE NGAQVIDVNM DEGLLDAVAA MQRFLNLVAA EPDIAKVPVM IDSSKWEVIE TGLKCVQGKP IVNSISLKEG KEKFLHQAHL CRRYGAAVIV MAFDEVGQAD TQARKIEICT RAYKILTEQV GFPAEDIIFD PNIFAVATGI EEHNNYAVDF IEAVREIKRT LPHAKISGGV SNVSFSFRGN NPVREAIHAV FLYHAIHAGM DMGIVNAGQL AIYDDLPEDL REAVEDVILN RRDDGTERLL DIAPNYQGGG AVEARPEEQE WRSWPVEERL KHSLVKGITD YIDQDTEEAR LELGRPLLVI EGPLMAGMNH VGDLFGAGKM FLPQVVKSAR VMKKAVAYLF PYLEAEKAAS GEAAKNNGRI LMATVKGDVH DIGKNIVGVV LQCNSYEVID IGVMVPADTI LQRAREENVD IIGLSGLITP SLDEMVHVAK EMERSGMAMP LMIGGATTSK LHTAIKISPQ REAPVIYVPD ASRAVGVASN LLSDDLRPAY LASIREDYAR VRAEREGKST VRKFMPITAA RANRVPIDWS SYVPPRPALL DEGFSDSGPW SLQLEPVGGG VVATIANFPL DDLVGCIDWL PFFHAWELAH KRFPDILDDD VIGEEARKLY ADAQSFLERL VSERWLEARA VFGFFPANAV GDDDIALYTD ASRGETLAML HHLRQQMPRD ASRNQPNFCL SDFIAPTGQD DWIAAFAVTA GVGIDAHLAR FEADHDDYSA IMLKSLADRL AEAFAERLHQ LVRTRYWGYA ADEALSNEEL IAEKYQGIRP APGYAACPDH TEKGILWELL EPDRRVGISL TENFAMLPTA AVSGCYFSHP DARYFGVGKI QKDQVEDYAA RKGMTLAEAE RWLAPVLGYD PA // ID G2FIT3_9GAMM Unreviewed; 1234 AA. AC G2FIT3; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGW53268.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGW53268.1}; GN Name=metH {ECO:0000313|EMBL:EGW53268.1}; GN ORFNames=TevJSym_bg00040 {ECO:0000313|EMBL:EGW53268.1}; OS endosymbiont of Tevnia jerichonana (vent Tica). OC Bacteria; Proteobacteria; Gammaproteobacteria; OC sulfur-oxidizing symbionts. OX NCBI_TaxID=1049564 {ECO:0000313|EMBL:EGW53268.1}; RN [1] {ECO:0000313|EMBL:EGW53268.1} 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGW53268.1}. 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; AFZB01000033; EGW53268.1; -; Genomic_DNA. DR RefSeq; WP_006475566.1; NZ_AFZB01000033.1. DR EnsemblBacteria; EGW53268; EGW53268; TevJSym_bg00040. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGW53268.1}; KW Transferase {ECO:0000313|EMBL:EGW53268.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1234 AA; 136285 MW; D5F649C9B4E4EA60 CRC64; MDNITPELES ILCERILILD GAMGTMIQRH KLTEEDYRGE RFTDWPSDLK GNNDLLVLSQ PELIRNIHEE YMEAGADILE TNTFGANRIS MADYDMQELA YEMNVAGARL CREAADKYAT PEKPRYVAGV LGPTNRTASI SPDVNDPGAR NISFDELVEA YAEATRGLIE GGVDILLIET IFDTLNAKAA VAACEQVFDQ DQLRLPIMIS GTITDASGRT LSGQTTEAFY NSLRHARPIS IGLNCALGPE LMRQYVEEIS RVAECYVNVH PNAGLPNEFG EYDLGPEAMG QQIAEWAEAG FLNIIGGCCG TTPAHIKAIA EAVADQAPRK LPEIRPECRL SGLEPLNIGP DSLFVNVGER ANVTGSAKFK RLILNEEYEE ALDVCRAQVE NGAQVVDVNM DEAMLDGVAA MQRFLNLCAG EPDISKVPVM IDSSKWEIIE AGLKCVQGKP IVNSISMKEG IDKFKQQAKL CRRYGAAVIV MAFDEEGQAD TQARKVEICT RAYQILTEEV GFPAEDIIFD PNIFAVATGI PEHDNYGVDF IEATREIKAA CPHALISGGV SNVSFSFRGN NPVREAIHAV FLYHAIQAGM DMGIVNAAQL AVYDDLPAEL RDAVEDVVLN KDPEAGDRLV EIAPNYAGDV VGGNKVEDLE WRSWPVNKRL EHALVKGITE YIDTDTEEAR LAVDKSLEVI EGPLMDGMNV VGDLFGAGKM FLPQVVKSAR VMKKSVAYLE PFLEAEKAEC GVQAQGKILM ATVKGDVHDI GKNIVGVVLQ CNNYEVIDIG VMVPADTILK QAQEHQVDII GLSGLITPSL DEMVHVAKEM KRLRMSQPLM IGGATTSIAH TAVKIEPEYD HPVVYVPDAS RAVGVASNLL SKDLRDDYIA DLRRSYEDVR ERRASKNEAR NLVPIEAARA NPVAIDWDNF VACEPNKLGV NVMDDIQLEL LIDYIDWTFF FHAWQLKGRY PQILEDREKG EEAKKLLADA REMLHKIITE KWLTAKAVIG LFPANAVGDD VEVYGLQPAA GEQRRPISTL HFLRKQGKQP KGKANTCLAD FIAPKASGHS DYIGGFACTA GIGINDKIVE FEKDHDDYSA IMLKALADRL AEALAEWLHE RVRRHYWGYA ANEKLSNEER VAEKYTGIRP AMGYPASPDH TEKDMLWELL DVEKNTGIWL TEAKAMVPTA AVSGLYFSHP DSHYFAVGKI NRDQVVSYAA RIDMELQEVE RWLAPNLAYE PESN // ID G2FNI8_9FIRM Unreviewed; 431 AA. AC G2FNI8; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 07-JAN-2015, entry version 14. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EGW40791.1}; GN ORFNames=DOT_1259 {ECO:0000313|EMBL:EGW40791.1}; OS Desulfosporosinus sp. OT. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfosporosinus. OX NCBI_TaxID=913865 {ECO:0000313|EMBL:EGW40791.1}; RN [1] {ECO:0000313|EMBL:EGW40791.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=OT {ECO:0000313|EMBL:EGW40791.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGW40791.1}. 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; AGAF01000061; EGW40791.1; -; Genomic_DNA. DR RefSeq; WP_009615289.1; NZ_AGAF01000061.1. DR EnsemblBacteria; EGW40791; EGW40791; DOT_1259. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGW40791.1}; KW Transferase {ECO:0000313|EMBL:EGW40791.1}. SQ SEQUENCE 431 AA; 46913 MW; 758194CCCACC525B CRC64; MKSFLSFIQE RVLLYDGSKG VMLQRRGLTG AEASESWNLS NPEEVKNLYN QYKVAGSDVI QTNTFPGNRV TLGKHSLGDK TYQLNFAGVK LAKEITGDST YVAASVGPTG ELLEPSGNLS FDKAYSIYTE PLKAIEDAGA DLVNFETFSD LNELRAAILA AKETTKLPII ASVTFNANSR TLFGNSAEVC AIVCQSLGVA IVGANCSGGP DSLIEPIKKM YSVASIPLCV KANAGMPVLD DDGKVIYHQK PEQFSSYTKE FIENGVRLIG GCCGTTPEFI SAIKKELAEL ETPELELKFM PTIASAYNHL VLSPDKKYSV KKLSPEAVTI LINGNLSTLV RESKSEDVDY LLLDFGNIDV SFDVWSFASE FGLLIKKPVM IKSESPEILY KFLRYYPGKA GVVLSDNSLL SLSQLQHYGA LIVNDALVPY L // ID G2FWJ8_9FIRM Unreviewed; 1213 AA. AC G2FWJ8; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 01-APR-2015, entry version 20. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGW37981.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGW37981.1}; GN Name=metH {ECO:0000313|EMBL:EGW37981.1}; GN ORFNames=DOT_4102 {ECO:0000313|EMBL:EGW37981.1}; OS Desulfosporosinus sp. OT. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfosporosinus. OX NCBI_TaxID=913865 {ECO:0000313|EMBL:EGW37981.1}; RN [1] {ECO:0000313|EMBL:EGW37981.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=OT {ECO:0000313|EMBL:EGW37981.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGW37981.1}. 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; AGAF01000179; EGW37981.1; -; Genomic_DNA. DR RefSeq; WP_009621692.1; NZ_AGAF01000179.1. DR EnsemblBacteria; EGW37981; EGW37981; DOT_4102. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGW37981.1}; KW Transferase {ECO:0000313|EMBL:EGW37981.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 242 242 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 754 754 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1213 AA; 135254 MW; 3583B8440CE14EBA CRC64; MKYTIENCLK ERILVLDGAM GTCIQGYNLS EQEFIGSCSC QRSQKGNNDL LNITHPEIIR AIHKTYLEAG ADIIETNTFN ANKISQKDYG MEDKVYELNL QGAKLAREQA DIFTNAGPSK PRFVAGSVGP TNRTASLSPD VENPGVRNIS FDELVLAYEE QIQGLVDGRV DVLFIETIFD ALNARAAVFA AGNVFEDKGV TLPIFISGTI ADKSGRILSG QTLEAFAHTM KGDEIIGIGL NCSFGAKDLI PFIKYLSKSQ DRYVTFHPNA GLPNSLGVYE ERPEETAALV KELAEEGHLN IVGACCGSTP AHIKAISEAV KGIHPRQIPA LETETVYCGL EAFKVKKENN FVNIGERTNV SGSAKFARLI REKNYEEALF IAKEQVENGA QIIDLNFDDA LLDAHSEMDT FLKLLASEPE ISRVPVMIDS SKFEVLEAGL KAIQGKAVVN SISLKGGEEE FIRQATLIKR YGAGIVVMAF DEQGQADTFD KRITVCKRAY DLLVKTVKFP PTDIIFDPNI LAIATGIEEH NNYAVDFINT VTWIKRNLPF VKVSGGVSNL SFSFRGNNAI REAMHSVFLY HAIAAGMDMA IVNPSMIQIY DEIDKVLLER VEDVVLNKSP DSAEKLLDFA ELYKASGGDQ AENKLVWREK DCKERLIHAL VKGIAEYIEE DVEEVRRQYD KAEKVIEGPL MDGMKVVGEL FGEGKMFLPQ VVKSARVMKK AVGCLLPYIE AEKKSGGSSS AGKVVMATVK GDVHDIGKNI VAVILACNNF EVIDLGVMAS CEVILQTAKK ENADIIALSG LITPSLDEMS HVAEEMERQG FDIPLMIGGA TTSKTHTALK IAPNYSRGVV YSVDASKSVE VAKKLVDKNE RRRYLTQVEE EYQTIRETYG KVERKLMPLN EAREKKFKID WNKETIKVPN LIGTQYLKNF PLSELRNYID WSYFFIAWDM GMVYPKIMED PKYSEEAKKL FDDANEMLDL LEREEILTAN AVWGIFPANS LGDDIELYHK GSVTTFNMLR QQTFSKDNVY RCLADYIAPK ESGITDYLGG FIVTAGIGAK EYAEKLSEQG NDYGAIMVKL LADRLAEAFA ELLHFQVRKD YWGYSPDEEL EIQALLKGSY RGIRPAFGYP SLRDHAEKTK LFQLLEGEYH TGISLTEHYM MNPVASVCGL YFGSQVARYF DIHRIDKDQA ADYAKRNQKE HKELEKMIST ILN // ID G2GBR0_9ACTO Unreviewed; 1161 AA. AC G2GBR0; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=5-methyltetrahydrofolate:homocysteine S-methyltransferase {ECO:0000313|EMBL:EGX59083.1}; GN ORFNames=SZN_14671 {ECO:0000313|EMBL:EGX59083.1}; OS Streptomyces zinciresistens K42. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=700597 {ECO:0000313|EMBL:EGX59083.1}; RN [1] {ECO:0000313|EMBL:EGX59083.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=K42 {ECO:0000313|EMBL:EGX59083.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGX59083.1}. 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; AGBF01000038; EGX59083.1; -; Genomic_DNA. DR RefSeq; WP_007495610.1; NZ_AGBF01000038.1. DR EnsemblBacteria; EGX59083; EGX59083; SZN_14671. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGX59083.1}; KW Transferase {ECO:0000313|EMBL:EGX59083.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 223 223 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 737 737 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1161 AA; 126556 MW; E25BF1173007344E CRC64; MSALREALAT RVVVADGAMG TMLQAQDPTL EDFENLEGCN EILNVTRPDI VRSVHDAYFS VGVDCVETNT FGANHTAAAE YDIADRVHEL SETGARIARE AADEHTARDG RPRWVLGSIG PGTKLPTLGH VGYAVIRDGY QANAEGLLAG GADALIVETT QDLLQTKASV LGARRALEAT GADVPLVVSM AFETTGTMLL GSEIGAALTA LEPLGIDMIG LNCSTGPAEM SEHLRYLNRH SRIPLLCMPN AGLPILTKDG AHFPLGPEGL ADAQENFVRD YGLSLIGGCC GTTPEHLRQV VERVRGLTPT ERSPRPEPGA ASLYQTVAFR QDTSYLAIGE RTNANGSKKF REAMLAARWD DCVEIAREQI REGAHMLDLC VDYVGRDGVA DMQELAGRFA TASTLPIVLD STEVGVIRAG LEKLGGRAVI NSVNYEDGDG PESRFAQVTA LAREHGAALI ALTIDEEGQA RTPEKKVEIA ERLIEDLTGT WGIHESDILI DTLTFTICTG QEESRGDGVA TIEAIRELKR RHPDVQTTLG LSNISFGLNP AARILLNSVF LDECVKAGLD SAIVHASKIL PIARFSEEEV QTALDLIHDR RREGYDPLQK LMQLFEGATA KSLKAGKAEE LAALPLEERL KRRIIDGERN GLEADLDTAL QDRPALDIVN ETLLDGMKVV GELFGSGQMQ LPFVLQSAEV MKAAVAHLEP HMEKSADGEG GAGKGTIVLA TVRGDVHDIG KNLVDIILSN NGYNVVNLGI KQPVSAILEA AEEHRADVIG MSGLLVKSTV IMKENLEELN SRGMAADYPV ILGGAALTRA YVEQDLHEIY EGEVRYARDA FEGLRLMDAL VGVKRGVPGA RLPELKQRRV RAATAAAVLD ERPEEGHVRS DVAVDNPVPE PPFRGTRVIK GIQLKEYASW LDEGALFKGQ WGLKETRSGE GPSYRELVES EGRPRLRGLL DRLQTENLLE AAVVYGYFPC VSKDDDLVIL DEHGNERTRF TFPRQRRGRR LCLADFFRPQ ESGETDVVGL QVVTVGSRIG EETARLFESN SYRDYLELHG LSVQLAEALA EYWHARVRSE LGFAGEDPAG IEDMFALKYR GARFSLGYGA CPNLEDRSKI ADLLRPERIG VQLSEEFQLH PEQSTDAIVI HHPEAKYFNA R // ID G2GKY8_9ACTO Unreviewed; 304 AA. AC G2GKY8; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 12. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:EGX55838.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EGX55838.1}; GN Name=mmuM {ECO:0000313|EMBL:EGX55838.1}; GN ORFNames=SZN_30909 {ECO:0000313|EMBL:EGX55838.1}; OS Streptomyces zinciresistens K42. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=700597 {ECO:0000313|EMBL:EGX55838.1}; RN [1] {ECO:0000313|EMBL:EGX55838.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=K42 {ECO:0000313|EMBL:EGX55838.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGX55838.1}. 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; AGBF01000190; EGX55838.1; -; Genomic_DNA. DR RefSeq; WP_007502528.1; NZ_AGBF01000190.1. DR EnsemblBacteria; EGX55838; EGX55838; SZN_30909. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGX55838.1}; KW Transferase {ECO:0000313|EMBL:EGX55838.1}. SQ SEQUENCE 304 AA; 31752 MW; BC3CEC0E5227483C CRC64; MTSASSLAEA LATGTVVLDG GMSNQLEAAG HDLSDALWSA RLLAESPEAI TRAHLAYFEA GADVAITASY QATFEGFARR GIGRERAAEL LALSVESARE AARRARTGGI ARALWVAASA GPYGAMLADG SEYRGRYGLS VAELERFHRP RLEVLAAAGP DALALETVPD SDEAEALLRA VRGLGVPVWL SYSVAGGRTR AGQPLEEAFA LAADADEVIA VGVNCCAPRD VEGAVATAAR VTGRPVVAYP NSGESWDAEA RTWHGRPAFS PDQVRTWRAA GARLIGGCCR VPPRTIEAVA RALA // ID G2GSP9_STRSL Unreviewed; 316 AA. AC G2GSP9; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 12. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:EGX30406.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EGX30406.1}; GN Name=mmuM {ECO:0000313|EMBL:EGX30406.1}; GN ORFNames=SSALIVM18_07006 {ECO:0000313|EMBL:EGX30406.1}; OS Streptococcus salivarius M18. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1074494 {ECO:0000313|EMBL:EGX30406.1}; RN [1] {ECO:0000313|EMBL:EGX30406.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M18 {ECO:0000313|EMBL:EGX30406.1}; RA Heng N.C.K., Haji-Ishak N.S., Kalyan A., Wong A.Y.C., Lovric M., RA Bridson J.M., Artamonova J., Stanton J.-A.L., Wescombe P.A., RA Burton J.P., Cullinan M.P., Tagg J.R.; RT "Genome sequence of the bacteriocin-producing oral probiotic RT Streptococcus salivarius strain M18."; 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. {ECO:0000313|EMBL:EGX30406.1}. 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; AGBV01000004; EGX30406.1; -; Genomic_DNA. DR RefSeq; WP_004182955.1; NZ_AGBV01000004.1. DR EnsemblBacteria; EGX30406; EGX30406; SSALIVM18_07006. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGX30406.1}; KW Transferase {ECO:0000313|EMBL:EGX30406.1}. SQ SEQUENCE 316 AA; 34707 MW; 619EDA6AEBEEB2CA CRC64; MAIFKDYLEN KSPLILHGAL GTEMESLGYD ISGKLWSAKY LLEKPEVIQK IHETYVAAGA DLITTSSYQA TLPGLIDAGL TKEEAEQIIT LTVQLAKDAR DKVWATLDDS EKANRPYPLI SGDVGPYAAY LANGSEYTGD YGQITIEALK EFHRPRIQIL LDQGVDLLAL ETIPNHLEAQ VLIELLAEEF PEAEAYISFT VQEPGTISDG TSLDEIAQLV GQSDQILALG INCSSPLLYN QALAILKNAG KALITYPNSG EVYDGSTQTW KPKDKDALTL VEHSKDWHTQ FGVKILGGCC RTRPNDIKAL YAEFRT // ID G2H463_9DELT Unreviewed; 626 AA. AC G2H463; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 29-OCT-2014, entry version 17. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EGY27189.1}; DE Flags: Fragment; GN ORFNames=DA2_0528 {ECO:0000313|EMBL:EGY27189.1}; OS Desulfovibrio sp. A2. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=298701 {ECO:0000313|EMBL:EGY27189.1}; RN [1] {ECO:0000313|EMBL:EGY27189.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A2 {ECO:0000313|EMBL:EGY27189.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGY27189.1}. 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; AGFG01000013; EGY27189.1; -; Genomic_DNA. DR RefSeq; WP_007521971.1; NZ_AGFG01000013.1. DR EnsemblBacteria; EGY27189; EGY27189; DA2_0528. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGY27189.1}; KW Transferase {ECO:0000313|EMBL:EGY27189.1}. FT NON_TER 626 626 {ECO:0000313|EMBL:EGY27189.1}. SQ SEQUENCE 626 AA; 64736 MW; D9F7A4A153EC07B4 CRC64; MPDFRQALRS GRRLVFDGGM GTMLQSRGLP PGVSPELFCL ARPDVLVGIH ADYLRAGADV LTTNTFGGCV YKLGTGPGTP DVVEFNRAMA RAAREAVASS GREAFVAGSV GPSGHFMRPL GDLDPAELVA AFRAQIRGLV QGGVDLILAE TQFDLAEARA IVLAVRAECD LPVGVSMTFE NGVSLTGTRP EVFVQSMLNM GVDLVGTNCS AGPEQMVEVA DELLAISEVP VLVEPNAGLP ELVDGKTVFR LGPDDFARHT ARFAAAGARL LGGCCGTTPD HIAALRGALD ALSGGLIPDP ARRDGIVLTT RAQAVHIGAG SPIRIIGERI NPTGKKQLIA ELQAGEFAQA LRFADEQVEA GAPVLDVNVG APMVDEAVLL PALVERLVAR HALPLSLDSS NADAIAGALP FHPGSPLVNS ISGEPGRMEH LGPLCRDHGA PFILLPLKGR KLPVTAAERI AIIEELLQQA DGLRIPRRLV MVDVLALAVS SKAEAARHCL DTIRWCAAQG LPTTIGLSNI SFGLPARELL NSTFLAMAAG PGLSSCIAHP GNARIREAVA ASGVLLGLDA NAEAFIEGYS GWTPGNGEAG AVQTGGAGGA SGASGVKAKA ATLEEAVIRG DREGAL // ID G2HRX7_9PROT Unreviewed; 1158 AA. AC G2HRX7; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 01-APR-2015, entry version 24. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:BAK72093.1}; GN ORFNames=ABLL_0218 {ECO:0000313|EMBL:BAK72093.1}; OS Arcobacter sp. L. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Arcobacter. OX NCBI_TaxID=944547 {ECO:0000313|EMBL:BAK72093.1, ECO:0000313|Proteomes:UP000001290}; RN [1] {ECO:0000313|EMBL:BAK72093.1, ECO:0000313|Proteomes:UP000001290} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP012048; BAK72093.1; -; Genomic_DNA. DR RefSeq; WP_014472934.1; NC_017192.1. DR RefSeq; YP_005552410.1; NC_017192.1. DR EnsemblBacteria; BAK72093; BAK72093; ABLL_0218. DR KEGG; arc:ABLL_0218; -. DR KO; K00548; -. DR BioCyc; ASP944547:GL86-219-MONOMER; -. DR Proteomes; UP000001290; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001290}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAK72093.1}; KW Transferase {ECO:0000313|EMBL:BAK72093.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 223 223 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 727 727 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1158 AA; 129326 MW; 1DF43CBC3C54D937 CRC64; MKELIENLIS KKVLIIDGAM GTQLQIADIK KEEWLFEDLD LEGCNELLNL TAPHILETIH DNYAKAGADL ICTNTFGSMP WVLDEYNIGH MSYELSKLGA SLVKKSCEKY STPEKPRFCV ASIGPGTKLP SLGHIKYDEM YEGYKIMAKG LVDGGTDIFL LETCQDPLQI KAALHALNDV APQIPIMVSV TIELSGTMLI GTDAMTIAAI MAPFNILSLG FNCGTGPVQV HKHIKTLSQV CKFPISVHSN AGLPQNRGGK TYYPMQPEEF TAHQKEFLKI NGVSFLGGCC GTTPEHIEAL AIAVDGMVPL KPCGFLKASL ASLFNTVPLK QEPAPLLIGE RSNATGSKAF RELLKENDYE GTLSVGQQQV RAGAHVIDVS VGFAGRDERF DMDEVVSLYS QKISLPLMPD STQILALEAA LKQIGGRCII NSVNLEDGEE KFDAVCKLAK KFGAALVCLV IDEIGMAKSV ERKLEVAERI YDLCVNRHGF DSADLVFDML TFTIGSGDDE YRNAGIDTLE AIREFQIRHP EVGTTLGLSN ISFGLAANAR IYLNSIYLDH CVKAGLTSAI VNVKHILPLN KISDEDRKAC DDLIFNNQEN GDPLFKFIEH FSNVGAQEEQ SDEEYQKLEP IEKVKKLLLD GDKDRLLPLV EELRHTVQPE IIVNEWLIDG MKIIGELFGS GQMQLPFVLQ SAETMKATVD ALNPYLPKQE KASETTLILG TVKGDVHDVG KNLVDIILSN NGFKVVNIGI KAGLDTFVEK LQEHNAHAIG MSGLLVKSTA VMKENLEELQ KMGIKVPVLL GGAALTKNFI DEYCRPYYDG PIFYCRDAFD GVVSMQRIEK GDENNTALAA DLIQIHDTSN RVEEEVVEIP PYEEIPMPQR GKFVFPPIWE RITKTGNKLD KELIFKWINH RVLFRQRWGY KRGKQDSETF LKYEREVVEP TYEALKAELV DKDIFDPIAI YAYYPCISHD NKLYIFDRKY LFNSLEESKN VPPLDEAIKV LEFPRQKRKP FRCIADFFAN DRLDVVAFTL ASAGLKISDY ERSLYDKGEF SKYYQVHGLG VELAEALAEV LHKQIRLDLD IVPKEGHTLN DVQMKQYVGC RYSPGYAACP DLAMNRDIFD LLNPEEFGIE LSETFQMHPE QTTCAIVVTN PEANYYNI // ID G2I0I4_KOMMN Unreviewed; 1181 AA. AC G2I0I4; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:BAK84442.1}; GN OrderedLocusNames=GLX_20300 {ECO:0000313|EMBL:BAK84442.1}; OS Komagataeibacter medellinensis (strain NBRC 3288 / BCRC 11682 / LMG OS 1693 / Kondo 51) (Gluconacetobacter medellinensis). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Komagataeibacter. OX NCBI_TaxID=634177 {ECO:0000313|Proteomes:UP000009044}; RN [1] {ECO:0000313|Proteomes:UP000009044} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 3288 / BCRC 11682 / LMG 1693 RC {ECO:0000313|Proteomes:UP000009044}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP012159; BAK84442.1; -; Genomic_DNA. DR RefSeq; WP_014105959.1; NC_016027.1. DR RefSeq; YP_004868812.1; NC_016027.1. DR EnsemblBacteria; BAK84442; BAK84442; GLX_20300. DR KEGG; gxy:GLX_20300; -. DR KO; K00548; -. DR BioCyc; GXYL634177:GHBT-2081-MONOMER; -. DR Proteomes; UP000009044; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000009044}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 237 237 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 749 749 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1181 AA; 129902 MW; 5181DBC3F39FAFA3 CRC64; MPYPLSADFR ITMTTRPHLL DALRDQVLLC DGGMGSRVQL LDLEVERDYW GQENCTEILN LSRPELVREI HRGYFEAGAD MVETNSFGGS PITLAEFGLA DRAREINRTA GHLAREAAET FSDGRHRYVV GSIGPGTKLP SLGNIDYDTL EAGLAEQCRG LIEGGVDCFL IETCQDTLQI KAAVNGAKIA RAELGVDTPI FVQVTVETTG TLLVGPDIAA AATVINALDV PLMGLNCATG PQEMAEHVRW LSENWPGLIS VQPNAGLPEL VNGTTHYPLT PAEMASWVER FITEDGLNLI GGCCGTSTPH TQALDLMLRK RAEGTGRIRP APVPRKPVWI PSVASLYSQV PLRQENSYFS IGERCNANGS KKWRQLQEAG DWDGCVALGR EQVAEGSNAL DICTAFVGRD EMKEMNAVVT RFTSSVNAPL VIDSTETPVI EAALKLHGGK PIINSINFED GEAIATDRML LARKFGASVI ALTIDEVGMA KTAEDKLRIA TRLVEFACEK HGLPQSDLMI DPLTFTIGTG TEDDRKLGEW TLEGIRQIRE RFPDIQIVLG LSNISFGLNP AARAVLNSVF LDHAVRAGMT AAIVHVSKIR PLHLIPADEV KVAEDLIFDR RAEGYDPLQR ILEIFADRKA ADAVKKARAE TAPERLKDRI VDGDRKGLEE DLAEAMRDMA PLDIINTVLL DGMKVVGELF GAGKMQLPFV LQSAETMKAA VAWLEPHMER TEGQARGTMV LATVKGDVHD IGKNLVDIIL TNNGYRVINL GIKVPVADMI AAAREHKADA IGMSGLLVKS TVIMRENLEE MNRQGVDVPV MLGGAALTRN YVEEDCTAAY GEDGRVAYAR DAFDGLSLMD KVAQGEFDTY LAAIASRRAG KATRTSRTQD IEAAETRGFG PVDKAAARTR REKLTADEPV LVPPFWGPRV LEATPEAVLP FLNERSLYQF QWGFRKQGRS LDDFMVWARK ELRPVLRHML ALCTEHDILH PKASYGYWKA AGEGNDLVLF GEDGVNEVAR FTLPRQPRAD GACIADFVRD IDDARRDVIG LQVVTVGQDA SDRAREWFEA DRYKDYLYLH GLSVEMAEAM AEYTHKRIRA EMGFAAEDDR DMAKLLQQGY RGSRYSFGYP ACPRLEEQEP ILKLLDAEKI GVSLTDGFQL HPEQSTSALV ILNPHAKYFS I // ID G2IUE6_PSEUL Unreviewed; 1242 AA. AC G2IUE6; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 01-APR-2015, entry version 24. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:BAK74903.1}; GN OrderedLocusNames=NH8B_0054 {ECO:0000313|EMBL:BAK74903.1}; OS Pseudogulbenkiania sp. (strain NH8B). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Chromobacteriaceae; Pseudogulbenkiania. OX NCBI_TaxID=748280 {ECO:0000313|Proteomes:UP000001274}; RN [1] {ECO:0000313|Proteomes:UP000001274} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NH8B {ECO:0000313|Proteomes:UP000001274}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP012224; BAK74903.1; -; Genomic_DNA. DR RefSeq; WP_014085523.1; NC_016002.1. DR RefSeq; YP_004845317.1; NC_016002.1. DR EnsemblBacteria; BAK74903; BAK74903; NH8B_0054. DR KEGG; pse:NH8B_0054; -. DR KO; K00548; -. DR BioCyc; PSP748280:GHJ9-54-MONOMER; -. DR Proteomes; UP000001274; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001274}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001274}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 253 253 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 316 316 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 771 771 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1242 AA; 136053 MW; A692924AB74AE22B CRC64; MFAMTIATNP TLYDHLSRRI LILDGGMGTM IQRHQLTEQD YRGERFADWR CDVKGNNDLL VLTQPGIIGG IHQAYLDAGA DIVETNTFNA TSIAMADYEM EALVWEINHA AARLVKELCV AETAKNPAKP RYCAGVLGPT NRTCSISPDV NDPGYRNVTF DALVESYTEA IDGLVKGGAD LLLVETIFDT LNAKAAVFAI HKYFDERPEA ARLPIMVSGT ITDQSGRTLT GQTTEAFYNS LSHADAISFG LNCALGPDLL RPYVEEMARI SSTFVSVHAN AGLPNAFGGY DLSPADMAVN VREWAESGLI NIVGGCCGTT PEHIAAICLA VQDLPPRALP ALEPKCRLSG LEPFNIGDAD LFVNVGERTN VTGSKAFARL ILNGDYATAL DVARQQVENG AQIIDINMDE GMLDAHAAMV RFLNLIAAEP DIARVPIMID SSKWEVIEAG LKCIQGKGIV NSISMKEGVD KFVEQARLIR HYGAAVIVMA FDEAGQADTY ARKVEICEKS YRILVDEVGF PPEDIIFDPN IFAVATGIEE HARYGLDFIE ATGWIKQNLP HAKISGGVSN VSFSFRGNNK VREAIHAVFL YHAIKRGMTM GIVNAGALEV YDEVDPVLRE RIEDVVLMQG DDSMAATEAL ITLAESFRGD AKEAKGEDLA WRSQPVEKRL EHALIKGITT YIVEDTEEVR LKCERPIHVI EGPLMDGMNV VGDLFGAGKM FLPQVVKSAR VMKAAVAHLE PFIEEEKIAM GLQDAPAKGV IIMATVKGDV HDIGKNIVGV VLRCNNYKVI DLGVMVPCQK ILDAAIEHKA DIIGLSGLIT PSLEEMSHVA KEMQRQGFTI PLLIGGATTS RVHTAVKIAP NYHGPVIYVP DASRAVGVCS NLLSDTLRDV FVEEVAADYA KARAIFEGRG EAKLLPIAEA REQRHQIDWA NYTPPKPSWL GVRRFEHYDL AEIARCIDWT PFFQSWELAG RYPAILSDEV VGESARALWA DAQAMLKQII DEKWLTANAV IGLFPAASVG HDDIEIYHPD SGERLMTWVG LRQQIVKTDK DGNRNPDWCL ADFIAPKDSG VEDYIGAFAV TGGLGIDPHV ARFEAANDDY SAILLKALAD RFAEAFAELM HQRVRTEFWG YAPHEQLDNE ALIDEQYQGI RPAPGYPACP DHTVKKELFE LLDAPAIGMI LTEGYAMLPT AAVSGFYFSH PDSRYFGVGK VSRDQVESYA QRRGVSVEQA QRDLASNLGY NA // ID G2J2J8_PSEUL Unreviewed; 321 AA. AC G2J2J8; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 01-APR-2015, entry version 16. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:BAK76374.1}; GN OrderedLocusNames=NH8B_1552 {ECO:0000313|EMBL:BAK76374.1}; OS Pseudogulbenkiania sp. (strain NH8B). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Chromobacteriaceae; Pseudogulbenkiania. OX NCBI_TaxID=748280 {ECO:0000313|Proteomes:UP000001274}; RN [1] {ECO:0000313|Proteomes:UP000001274} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NH8B {ECO:0000313|Proteomes:UP000001274}; 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 ----------------------------------------------------------------------- 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; BAK76374.1; -; Genomic_DNA. DR RefSeq; WP_014086744.1; NC_016002.1. DR RefSeq; YP_004846788.1; NC_016002.1. DR EnsemblBacteria; BAK76374; BAK76374; NH8B_1552. DR KEGG; pse:NH8B_1552; -. DR KO; K00547; -. DR BioCyc; PSP748280:GHJ9-1551-MONOMER; -. DR Proteomes; UP000001274; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001274}; KW Methyltransferase {ECO:0000313|EMBL:BAK76374.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001274}; KW Transferase {ECO:0000313|EMBL:BAK76374.1}. SQ SEQUENCE 321 AA; 34480 MW; 8BB1281F80654B62 CRC64; MTSPTTDPVA AILADYPVLI LDGALATELQ QRGCDLNDPL WSARVLIEEP ELIRQVHEDY FAAGADVATT ASYQATFEGF ARRGYDAEAA AGLMRRAVTL AVEARDAFWS DPAHRQGRPK PLVAASVGPY GAMLADGSEY RGDYGLGEQQ LMDFHRPRLK VLLEAGADLL ACETIPCQVE ARALARLLAE EFPSARAWIS FSCKDGAHTC QGETLADAVA ELNEVGQVVA VGVNCTAPEF IPALVAAAHG ATTKPLLVYP NSGEHYDPEH KCWHGHADAN RFAEAARGWH QAGARLIGGC CRTTPQDIRA VAEWARPPAG H // ID G2JFY3_ACIBA Unreviewed; 292 AA. AC G2JFY3; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AEP05485.1}; GN ORFNames=ABZJ_01025 {ECO:0000313|EMBL:AEP05485.1}; OS Acinetobacter baumannii MDR-ZJ06. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=497978 {ECO:0000313|EMBL:AEP05485.1, ECO:0000313|Proteomes:UP000009290}; RN [1] {ECO:0000313|EMBL:AEP05485.1, ECO:0000313|Proteomes:UP000009290} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MDR-ZJ06 {ECO:0000313|EMBL:AEP05485.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; AEP05485.1; -; Genomic_DNA. DR RefSeq; WP_000696105.1; NC_017171.1. DR RefSeq; YP_005524981.1; NC_017171.1. DR EnsemblBacteria; AEP05485; AEP05485; ABZJ_01025. DR KEGG; abz:ABZJ_01025; -. DR BioCyc; ABAU497978:GL7S-1061-MONOMER; -. DR Proteomes; UP000009290; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009290}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 202 202 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 275 275 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 276 276 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 292 AA; 32062 MW; 98A1B5614908D18A CRC64; MKILDGGLGR ELARRGAPFR QPEWSALALI EAPETVKEVH LDFINAGAEV ITTNNYAVVP FHIGQERFET DGVRLIKVAI EQAKNAVKES GKNVKIAGCL PPLFGSYRAD LFQPEQAKNL AEPIINTLAP EVDFWLAETQ SCLKEVETVH ALLPQDGKDY WVSFTLQDEI KQEQALLRSG ENMQQVADFI KQSNAKAVLF NCCQPEVILQ AINEIKALIP VSVQIGAYAN AFPPQDESAT ANDGLDEIRK DLDAPAYLAF AKQWQQAGAS LVGGCCGIGP EHIAELSQFF KE // ID G2JG32_ACIBA Unreviewed; 1228 AA. AC G2JG32; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AEP05534.1}; GN ORFNames=ABZJ_01074 {ECO:0000313|EMBL:AEP05534.1}; OS Acinetobacter baumannii MDR-ZJ06. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=497978 {ECO:0000313|EMBL:AEP05534.1, ECO:0000313|Proteomes:UP000009290}; RN [1] {ECO:0000313|EMBL:AEP05534.1, ECO:0000313|Proteomes:UP000009290} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MDR-ZJ06 {ECO:0000313|EMBL:AEP05534.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP001937; AEP05534.1; -; Genomic_DNA. DR RefSeq; WP_000105333.1; NC_017171.1. DR RefSeq; YP_005525030.1; NC_017171.1. DR EnsemblBacteria; AEP05534; AEP05534; ABZJ_01074. DR KEGG; abz:ABZJ_01074; -. DR KO; K00548; -. DR BioCyc; ABAU497978:GL7S-1110-MONOMER; -. DR Proteomes; UP000009290; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000009290}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1228 AA; 135845 MW; B37AFE2D26412013 CRC64; MSTLATLKAL LAKRILIIDG AMGTMIQRHK LEEADYRGER FADWAHDLKG NNDLLVLTQP QIIQGIHEAY LDAGADIIET NSFNGTRVSM SDYHMEDLVP EINREAARLA KAACEKYSTP DKPRFVAGVL GPTSRTCSIS PDVNNPAFRN ISFDELKENY IEATHALIEG GADIILIETV FDTLNCKAAI FAVKEVFKQI GRELPIMISG TITDASGRTL TGQTAEAFWN SVRHGDLLSI GFNCALGADA MRPHVKTISD VADTFVSAHP NAGLPNAFGE YDETPEQTAA FLKEFAESGL INITGGCCGT TPDHIRAIAN AVKDIAPRQV PETVPACRLS GLEPFNIYDD SLFVNVGERT NVTGSKKFLR LIREENFAEA LEVAQQQVEA GAQIIDINMD EGMLDSQNAM VHFLNLVASE PDISRVPIMI DSSKWEIIEA GLKCVQGKPV VNSISLKEGY DEFVEKARLC RQYGAAIIVM AFDEVGQADT AERKREICKR SYDILVNEVG FPAEDIIFDP NVFAVATGIE EHNNYAVDFI EATGWIKQNL PHAMISGGVS NVSFSFRGNE PVREAIHSVF LYHAIKQGMT MGIVNAGQMA IYDDIPTELK EAVEDVILNQ NQGESGQVAT EKLLEVAEKY RGQGGATKEA ENLEWRNESV EKRLEYALVK GITTYIDQDT EEARLKSKRP LDVIEGPLMD GMNVVGDLFG SGKMFLPQVV KSARVMKQAV AWLNPYIEAE KTEGQSKGKV LMATVKGDVH DIGKNIVGVV LGCNGYDIVD LGVMVPCEKI LQTAIDEKCD IIGLSGLITP SLDEMVFVAK EMQRKGFNIP LLIGGATTSK AHTAVKIDPQ YQNDAVIYVA DASRAVGVAT TLLSKEMRGA FIEEHRAEYA KIRERLANKQ PKAAKLTYKE SVENGFKIDE SYVPPKPNLL GTQVLKNYPL ATLVDYFDWT PFFISWSLTG KFPKILEDEV VGEAATDLYN QAQAMLKDII DNNRFDARAV FGMFPAQRTD ADTVSVFDEA GQNVTHTFEH LRQQSDKVTG KPNLSLADYI RADREQQDYL GGFTVSIFGA EELANEYKAK GDDYSAILVQ SLADRFAEAF AEHLHERIRK EFWGYKADEQ LSNEELIKEK YVGIRPAPGY PACPEHSEKA VLFDWLGSTD KIGTKLTEHF AMMPPSSVSG FYYSHPQSEY FNVGKISQDQ LEDYAKRKGW TLDEAKRWLA PNLDDSIV // ID G2KV25_LACSM Unreviewed; 320 AA. AC G2KV25; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AEN98914.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:AEN98914.1}; GN Name=mmuM {ECO:0000313|EMBL:AEN98914.1}; GN OrderedLocusNames=LSA_04660 {ECO:0000313|EMBL:AEN98914.1}; OS Lactobacillus sanfranciscensis (strain TMW 1.1304). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=714313 {ECO:0000313|EMBL:AEN98914.1, ECO:0000313|Proteomes:UP000001285}; RN [1] {ECO:0000313|EMBL:AEN98914.1, ECO:0000313|Proteomes:UP000001285} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TMW 1.1304 {ECO:0000313|EMBL:AEN98914.1, RC ECO:0000313|Proteomes:UP000001285}; RX PubMed=21995419; DOI=10.1186/1475-2859-10-S1-S6; RA Vogel R.F., Pavlovic M., Ehrmann M.A., Wiezer A., Liesegang H., RA Offschanka S., Voget S., Angelov A., Bocker G., Liebl W.; RT "Genomic analysis reveals Lactobacillus sanfranciscensis as stable RT element in traditional sourdoughs."; RL Microb. Cell Fact. 10:S6-S6(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; CP002461; AEN98914.1; -; Genomic_DNA. DR RefSeq; WP_014081772.1; NC_015978.1. DR RefSeq; YP_004840846.1; NC_015978.1. DR EnsemblBacteria; AEN98914; AEN98914; LSA_04660. DR KEGG; lsn:LSA_04660; -. DR KO; K00547; -. DR BioCyc; LSAN714313:GIWZ-495-MONOMER; -. DR Proteomes; UP000001285; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001285}; KW Methyltransferase {ECO:0000313|EMBL:AEN98914.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001285}; KW Transferase {ECO:0000313|EMBL:AEN98914.1}. SQ SEQUENCE 320 AA; 35409 MW; C6DD002A7A80CD01 CRC64; MFFMKLKLDM IKSEKSKMTK TSVEKRLQEK LVLDGAMGTE LEKLGVKTND LLWSANALIN NQKSIYQVHA DYFKAGADIA ITDTYQANIA AFAKVGINHD QALDLIKKGV ELAKQARDDF NPAGLVAGCV GPYGAYLANG AEYTGTYDLS FAEYQKFHQE KIKTLINAGS DLISVDTMPN FAEIKSVVKI INDLPNKIPY WISLSVKDEN TLSDGTPLRD VIIWLGKQSG ISGIGVNCTK IENITPIVSL MHHLTDLPIV VYPNPGDIYD PQTKTWTSVP HTDTFEQEVP RWLAEGANII GGCCRTIPQD IEQITEIIKN // ID G2LHT4_CHLTF Unreviewed; 620 AA. AC G2LHT4; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 23. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=Cabther_A0222 {ECO:0000313|EMBL:AEP10994.1}; OS Chloracidobacterium thermophilum (strain B). OC Bacteria; Acidobacteria; Acidobacteria subdivision 4; OC Chloracidobacterium. OX NCBI_TaxID=981222 {ECO:0000313|EMBL:AEP10994.1, ECO:0000313|Proteomes:UP000006791}; RN [1] {ECO:0000313|EMBL:AEP10994.1, ECO:0000313|Proteomes:UP000006791} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B {ECO:0000313|EMBL:AEP10994.1, RC ECO:0000313|Proteomes:UP000006791}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; AEP10994.1; -; Genomic_DNA. DR RefSeq; WP_014098732.1; NC_016024.1. DR RefSeq; YP_004861510.1; NC_016024.1. DR EnsemblBacteria; AEP10994; AEP10994; Cabther_A0222. DR KEGG; ctm:Cabther_A0222; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR BioCyc; CTHE981222:GHDQ-222-MONOMER; -. DR Proteomes; UP000006791; Chromosome 1. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006791}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:AEP10994.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000006791}; KW Transferase {ECO:0000313|EMBL:AEP10994.1}. SQ SEQUENCE 620 AA; 67572 MW; 39D7548437C4ACC6 CRC64; MKVLKPFREL LAADGIHVFD GAMGTLLYAK GVYVNRCYDE ISLSNPALVQ EVHREYVKAG AEIVQTNTFG ANRPKLEMHG FQDRVQEINY KAAKLAREAV GPQVYVAGSI GPLGIRIEPW GPTSFDEAKA FFREQAEALL DGGVDLIVLE TFTDLTEIRQ ALAAVRELSA DMVVVAQMTV GEDGATGYGT APEIFTKRLD EWGADVIGLN CSVGPKPMLE AIERMAAVTE KPLSAQPNAG LPQDLQGRKI YLCSPEYMAK YARRLIQSGV RFIGGCCGTT PEHIKTLKAA VRALSPAKRI EPVIQVLETK CPDVRITPPE EKSRFARKIV QGEFVTSVEI VPPRGCDPTK MLEGVRLLKA AGVDAVNVPD GPRAQSRMGA IATSLIIEQQ VGIETVTHYC CRDRNLLGMT SDLLGAAALG LRNILLITGD PPKMGPYPDA TAVFDIDSIG LTNMVKRLNL GLDLGGNAIG QPTSYFIGVG VNPCAVDLDY EIRRFEYKVE AGAEFAITQP IFDIGMFRAF LKRIEHCRIP IIAGIWPLTS YRNAEFLSNE VPGVVVAPEI LERMRRANTS PEAGQQEGLA IAREMLSEVR DLVQGVQVSA PFGRVAYALE VFEVLRETVG // ID G2LJW7_CHLTF Unreviewed; 1234 AA. AC G2LJW7; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:AEP13134.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEP13134.1}; GN OrderedLocusNames=Cabther_B0129 {ECO:0000313|EMBL:AEP13134.1}; OS Chloracidobacterium thermophilum (strain B). OC Bacteria; Acidobacteria; Acidobacteria subdivision 4; OC Chloracidobacterium. OX NCBI_TaxID=981222 {ECO:0000313|EMBL:AEP13134.1, ECO:0000313|Proteomes:UP000006791}; RN [1] {ECO:0000313|EMBL:AEP13134.1, ECO:0000313|Proteomes:UP000006791} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B {ECO:0000313|EMBL:AEP13134.1, RC ECO:0000313|Proteomes:UP000006791}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002515; AEP13134.1; -; Genomic_DNA. DR RefSeq; WP_014100872.1; NC_016025.1. DR RefSeq; YP_004863651.1; NC_016025.1. DR EnsemblBacteria; AEP13134; AEP13134; Cabther_B0129. DR KEGG; ctm:Cabther_B0129; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; CTHE981222:GHDQ-2402-MONOMER; -. DR Proteomes; UP000006791; Chromosome 2. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006791}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEP13134.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006791}; KW Transferase {ECO:0000313|EMBL:AEP13134.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 765 765 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1234 AA; 134983 MW; B1271FE175FDE330 CRC64; MSSPTTALLE QALRERILVL DGAMGTMIQS HKLQEADYRG ERFASHTHDL KGNNDLLCLT RPDIVEAIHR AYLEAGADII ETNSFNAQRI SQADYGLEDL SYEMNLAAAQ CARRAVEAFL REDSSRPRFV AGALGPTNKT ASISPDVNDP GARGTTFDEL VAAYAEQAEG LLDGGVDLLL PETTFDTLNL KAALFAIEEV FERRGQRVPV MASVTVADAS GRTLSGQTVE AFLISVEHAP LLALGMNCGF GAAEMRPHVE ELAEKSPFYL ICYPNAGLPN VFGGFDQTPD IMGELLRDFA RHGWLNIVGG CCGTTPKHIA AIAAAVAGMP PRIPPKPSRY TRLSGLEALV IRPETNFVNI GERTNVTGSA KFAELIRAER YEDALTIARQ QVANGAQMID VNMDEAMLDS VRAMTCFLNL VVADPDIARV PIVIDSSKFH VIEAGLKCVQ GKCVVNSISL KEGEAVFIEQ ARRIRRYGAA VVVMAFDEIG QADTAARKIE ICTRAYRILT EQVGFPPEDI IFDPNILAIA TGIEEHANYA VDFIEATRVI KQTLPGCKVS GGVSNLSFSF RGNNVVREAM HSVFLYHAIR AGMDMGIVNA GQLAVYDEIP PDLLELVEDV VLNRHPDATE RLIAFAESVK GAGKAAVKDE AWRQTSVEER LKHALIKGNA DYIETDVEEA LQKYGAPLAV IEGPLMDGMN VVGDLFGAGK MFLPQVVKSA RVMKKAVAVL LPYLEAEKKA AANGQTANGS GRRKVLLATV KGDVHDIGKN IVGVVLGCNN YEVIDLGVMQ PCDVILAKAR EHNVDVIGLS GLITPSLDEM VHVAKTMTEA GFTVPLLIGG ATTSKLHTAV KIAPAYSGTT VHVLDASRAV GVVGALTSHE QRQDFIAQNA AEQAALREEH QSRLDRKHLL PLAEARARRP QLRFDAETVA VPEQLGVMTF DDVTLDALVP YIDWSPFFHT WELRGRYPKI FDDPTIGERA RELFDDAQRL LERIITERRL HPRGVFGLFP ANAVGDDIEL YTDETRTEVL TRFHTLRQQV ERTDGKPNIA LADFIAPKDT GRLDYIGGFV VTAGLGLDEL CAAFDADHDD YHSIMAKALA DRLAEAFAEL AHKRVRDLWG YGRHETLTRE DLIRERYRGI RPAPGYPASP DHTEKRTLFA LLGAEENAGV RLTESCAMWP ASSVSGLYFA HPDAHYFAVG LLGRDQIEDY AARKGWTVAE AERWLRPNLG YDPA // ID G2LY49_9XANT Unreviewed; 321 AA. AC G2LY49; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:AEO41662.1}; GN Name=mmuM {ECO:0000313|EMBL:AEO41662.1}; GN ORFNames=XACM_1378 {ECO:0000313|EMBL:AEO41662.1}; OS Xanthomonas axonopodis pv. citrumelo F1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=981368 {ECO:0000313|EMBL:AEO41662.1, ECO:0000313|Proteomes:UP000001276}; RN [1] {ECO:0000313|EMBL:AEO41662.1, ECO:0000313|Proteomes:UP000001276} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F1 {ECO:0000313|EMBL:AEO41662.1}; 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 ----------------------------------------------------------------------- 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; AEO41662.1; -; Genomic_DNA. DR RefSeq; WP_008578257.1; NC_016010.1. DR RefSeq; YP_004850960.1; NC_016010.1. DR EnsemblBacteria; AEO41662; AEO41662; XACM_1378. DR KEGG; xax:XACM_1378; -. DR KO; K00547; -. DR BioCyc; XALF981368:GH9H-1378-MONOMER; -. DR Proteomes; UP000001276; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001276}; KW Methyltransferase {ECO:0000313|EMBL:AEO41662.1}; KW Transferase {ECO:0000313|EMBL:AEO41662.1}. SQ SEQUENCE 321 AA; 34071 MW; 8992C28D3DFDFC20 CRC64; MTILPRQPRA NAPFSQALQH DGYVVLDGAL ATELEQRGCD LNDALWSARV LMEQPELIYQ VHRDYFAAGA QCAITASYQA TPLGFAARGL DAAQAQALIA RSVALAAQAR ADHLTLHPYA APLWVAGSVG PYGAYLADGS EYRGDYVLPI EQLMDFHRPR IAALAEAGVD LLACETLPSA SEIVALRQLL QHEFPQLHAW FSFTLRDAAH LSDGTPLAQV VPALDACAQV IAVGINCIAL DQASAALHSL AALTALPLVV YPNSGEHYDA SDKRWHAGHG AALTLADQHA HWLAAGARLI GGCCRTAPRD IAALAAARAL G // ID G2LZY5_9XANT Unreviewed; 376 AA. AC G2LZY5; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyl transferase {ECO:0000313|EMBL:AEO41813.1}; GN Name=metH {ECO:0000313|EMBL:AEO41813.1}; GN ORFNames=XACM_1531 {ECO:0000313|EMBL:AEO41813.1}; OS Xanthomonas axonopodis pv. citrumelo F1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=981368 {ECO:0000313|EMBL:AEO41813.1, ECO:0000313|Proteomes:UP000001276}; RN [1] {ECO:0000313|EMBL:AEO41813.1, ECO:0000313|Proteomes:UP000001276} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F1 {ECO:0000313|EMBL:AEO41813.1}; 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 ----------------------------------------------------------------------- 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; AEO41813.1; -; Genomic_DNA. DR RefSeq; WP_014089821.1; NC_016010.1. DR RefSeq; YP_004851111.1; NC_016010.1. DR EnsemblBacteria; AEO41813; AEO41813; XACM_1531. DR KEGG; xax:XACM_1531; -. DR KO; K00548; -. DR BioCyc; XALF981368:GH9H-1531-MONOMER; -. DR Proteomes; UP000001276; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001276}; KW Transferase {ECO:0000313|EMBL:AEO41813.1}. SQ SEQUENCE 376 AA; 40058 MW; B603EB2235DCD418 CRC64; MTPAALHSPV AHALPWLRPE RAAKLTAALA ERILIIDGAM GTMIQRHDLQ EPDYRGTRFA EGYDSAHVHG PGCDHAHVPQ GHDLKGNNDL LLLTRPQIIA GIHRAYLDAG ADLLETNTFN ATSVSQADYH LEHLVYELNK AGAQVARACC DEVEALTPHK PRFVIGVLGP TSRTASISPD VNDPGYRNTS FDALRETYRE AIEGLIDGGA DTLMVETIFD TLNAKAALYA IEEVFEARGG RLPVMVSGTI TDASGRTLSG QTAEAFYASV AHGRPLSIGL NCALGAKDLR PHVETLAQIA DAYVSAHPNA GLPNAFGEYD ETPEEMASTL REFAQAGLLN LVGGCCGTSP DHIRAIAEAV ADLPPRQLPG APELAA // ID G2MWP6_9THEO Unreviewed; 807 AA. AC G2MWP6; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 01-APR-2015, entry version 21. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AEM79158.1}; GN ORFNames=Thewi_1765 {ECO:0000313|EMBL:AEM79158.1}; OS Thermoanaerobacter wiegelii Rt8.B1. OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Thermoanaerobacter. OX NCBI_TaxID=697303 {ECO:0000313|EMBL:AEM79158.1, ECO:0000313|Proteomes:UP000008276}; RN [1] {ECO:0000313|EMBL:AEM79158.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Rt8.B1 {ECO:0000313|EMBL:AEM79158.1}; 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 ----------------------------------------------------------------------- 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; AEM79158.1; -; Genomic_DNA. DR RefSeq; WP_014063140.1; NC_015958.1. DR RefSeq; YP_004820442.1; NC_015958.1. DR EnsemblBacteria; AEM79158; AEM79158; Thewi_1765. DR GeneID; 11083374; -. DR KEGG; twi:Thewi_1765; -. DR KO; K00548; -. DR BioCyc; TWIE697303:GH3A-1815-MONOMER; -. DR Proteomes; UP000008276; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008276}; KW Methyltransferase {ECO:0000313|EMBL:AEM79158.1}; KW Transferase {ECO:0000313|EMBL:AEM79158.1}. SQ SEQUENCE 807 AA; 88090 MW; F164831C68949307 CRC64; MLDIFKELSN RVIVFDGAMG TQLQERGLKT GECPEYMNIT HPEVVFDIHR SYIEAGADVI ETNTFGANRI KLAKYGLENE VFNIVTQAVK IAKRAARDKP VALSIGPTGE LLTPYGDMTF DEAYDVFKEV VIAAERAGAD IVLIETMSDM LEAKAAILAA KENSNMKVIC TMTFQEDGRT LMGSDPITVV VSLQGLGLDA IGVNCSTGPD KMVSVVEKIS QVARIPIIAQ PNAGMPVIRD GKTVYDLKPE EFASFFPLLV EKGASIVGGC CGTTPHYIKL VKKAVKDLKP KVKVNKFTAV ASNTKTVFIG ENYLLRVIGE CINPTGKKKL SEAFLAGDVS LAVEEAIKQQ KCGAEILDVN VGVPGVNEEE LLPKVVSEIQ NVVDIPLQID STNIKAVEKA IRILRGRPII NSVSAKEESL KEVLPIVKKY GACVVGLTVG DKGLPKDRHE RIENAKKIIK KAEEYGIPKE DILIDCIVLT VSSEQEAAIE TLEAIKLAKE ELGVNTVVGL SNVSFGLPER RLINSTFLAM AASYGLTTAI INPCDEAMMD TLRASMVLLN KDKGSVNYLN IYGKKQKEEI KEKEQQKIQE EDLKSKLYIQ ILEGKKSGVE DIVKNILEEE VQPLSIVDNI IIPALKEVGD RYEKGIYFLP QLLSSAEVVQ SAFKIIKEKL PKGSVSKGKI ILATVEGDVH DIGKNIVKVL LENYGYDVID LGKDVKGEVI LEEVKRTGAP LVGLSALMTT TLFNMEKIIK LLKANTDVKI MVGGAVLTEE YAYKIGADYY GKTAQDAVKI ADKFFLKNAL LCKTCGI // ID G2NAI4_STREK Unreviewed; 1170 AA. AC G2NAI4; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEN09012.1}; GN ORFNames=SACTE_1087 {ECO:0000313|EMBL:AEN09012.1}; OS Streptomyces sp. (strain SirexAA-E / ActE). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=862751 {ECO:0000313|EMBL:AEN09012.1, ECO:0000313|Proteomes:UP000001397}; RN [1] {ECO:0000313|EMBL:AEN09012.1, ECO:0000313|Proteomes:UP000001397} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SirexAA-E {ECO:0000313|EMBL:AEN09012.1}; RX PubMed=24710170; RA Takasuka T.E., Acheson J.F., Bianchetti C.M., Prom B.M., RA Bergeman L.F., Book A.J., Currie C.R., Fox B.G.; RT "Biochemical Properties and Atomic Resolution Structure of a RT Proteolytically Processed beta-Mannanase from Cellulolytic RT Streptomyces sp. SirexAA-E."; RL PLoS ONE 9:E94166-E94166(2014). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002993; AEN09012.1; -; Genomic_DNA. DR RefSeq; WP_014045001.1; NC_015953.1. DR RefSeq; YP_004801552.1; NC_015953.1. DR EnsemblBacteria; AEN09012; AEN09012; SACTE_1087. DR KEGG; ssx:SACTE_1087; -. DR KO; K00548; -. DR BioCyc; SSP862751:GHMW-1098-MONOMER; -. DR Proteomes; UP000001397; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001397}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001397}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 237 237 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 747 747 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1170 AA; 127608 MW; 89CB8A2875A7BC43 CRC64; MASLPTPSAD SRNRAAALRE ALATRVVVAD GAMGTMLQAQ DPTLDDFQNL EGCNEILNVT RPDIVRSVHE EYFAVGVDCV ETNTFGANFA ALGEYDIPER VFELSESGAR IAREVADEFT ASTGQQRWVL GSMGPGTKLP TLGHAPYVKL RDAYQQNAEG MIAGGADALL VETTQDLLQT KASVIGARRA LEATGADLPV ICSVTVETTG TMLLGSEIGA ALTALEPLGI DMIGLNCATG PAEMSEHLRY LARHSRVPLS CMPNAGLPVL GKDGAHYPLS PEELADAQET FVADYGLSLV GGCCGTTPEH LRQVVERVRG LAPTAREPRP EPGAASLYQS VPFRQDTSYL AIGERTNANG SKKFREAMLE ARWDDCVEMA RDQIREGAHM LDLCVDYVGR DGVADMEELA GRFATASTLP LVLDSTELPV LRAGLEKLGG RAVLNSVNYE DGDGPESRFA KVSALAAEHG AALIALTIDE EGQARTAEHK VAIAERLIED LTGNWGIHES DILIDCLTFT ICTGQEESRK DGIATIEAIR ELKKRHPDVQ TTLGLSNISF GLNPAARVVL NSVFLDECVK AGLDSAIVHA SKILPIARLE EEQVKVALDL VYDRRAEGYD PLQKLMELFE GVNMKSMKAG KAEELLALPL DERLQRRIID GEKNGLEADL DEALLTRPAL EIVNDTLLAG MKVVGELFGS GQMQLPFVLQ SAEVMKGAVA HLEPHMEKTD DEGKGTIVLA TVRGDVHDIG KNLVDIILSN NGYTVVNLGI KQPVSAILDA AEEHKADVIG MSGLLVKSTV IMKENLEELN QRKMAADYPV ILGGAALTRA YVEQDLHEVY EGEVRYARDA FEGLRLMDAL IAVKRGVPGA TLPELKQRRV PKRDTPLVEE ARPEEGVRSD VSVTNPVPEP PFWGTRVVKG IQLKEYASWL DEGALFKGQW GLKQARAGDG PTYEELVETE GRPHLRGWLD KLQTENLLEA AVVYGYFPCV SKGDDLILLH EDGSERTRFT FPRQRRGRRL CLADFFRPEE SGERDVVGLQ VVTVGSKIGG ETAKLFEANS YRDYLELHGL SVQLAEALAE YWHARVRSEL GFAGEDPSDV EDMFALKYRG ARFSLGYGAC PDLEDRAKIA ALLEPERIGV QLSEEFQLHP EQSTDAIVIH HPEAKYFNAR // ID G2NFY2_STREK Unreviewed; 308 AA. AC G2NFY2; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AEN12928.1}; GN ORFNames=SACTE_5110 {ECO:0000313|EMBL:AEN12928.1}; OS Streptomyces sp. (strain SirexAA-E / ActE). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=862751 {ECO:0000313|EMBL:AEN12928.1, ECO:0000313|Proteomes:UP000001397}; RN [1] {ECO:0000313|EMBL:AEN12928.1, ECO:0000313|Proteomes:UP000001397} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SirexAA-E {ECO:0000313|EMBL:AEN12928.1}; RX PubMed=24710170; RA Takasuka T.E., Acheson J.F., Bianchetti C.M., Prom B.M., RA Bergeman L.F., Book A.J., Currie C.R., Fox B.G.; RT "Biochemical Properties and Atomic Resolution Structure of a RT Proteolytically Processed beta-Mannanase from Cellulolytic RT Streptomyces sp. SirexAA-E."; RL PLoS ONE 9:E94166-E94166(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; CP002993; AEN12928.1; -; Genomic_DNA. DR RefSeq; WP_014048878.1; NC_015953.1. DR RefSeq; YP_004805468.1; NC_015953.1. DR EnsemblBacteria; AEN12928; AEN12928; SACTE_5110. DR KEGG; ssx:SACTE_5110; -. DR KO; K00547; -. DR BioCyc; SSP862751:GHMW-5192-MONOMER; -. DR Proteomes; UP000001397; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001397}; KW Methyltransferase {ECO:0000313|EMBL:AEN12928.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001397}; KW Transferase {ECO:0000313|EMBL:AEN12928.1}. SQ SEQUENCE 308 AA; 31714 MW; 8D67013333A94A45 CRC64; MRADRIPART LPGVLAAGET LVLDGGLSNQ LRAQGCDLSD ALWSARLLAD APQQIEAAHA AYVRAGAQVL ITASYQATFD GFERRGIGRE GAAELMAGSV ELARRAAGRS GREVWVAASV GPYGAMLADG SEYRGRYGLT VRELERFHRP RIEALAEAAP DALALETVPD TDEAEAMLGA VRGCGLPVWL SYTVAGERTR AGQPLADAFA LAAGEDQVVA VGVNCCDPAD ADRAVEVAAA VTGKPVVVYP NSGEIWDAAA RGWAGQGTFD AARAGGWRRA GARLVGGCCR VGPSGISGLA AALASSGP // ID G2P2I1_STRVO Unreviewed; 329 AA. AC G2P2I1; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 29-APR-2015, entry version 20. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AEM81953.1}; GN ORFNames=Strvi_2226 {ECO:0000313|EMBL:AEM81953.1}; OS Streptomyces violaceusniger Tu 4113. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=653045 {ECO:0000313|EMBL:AEM81953.1, ECO:0000313|Proteomes:UP000008703}; RN [1] {ECO:0000313|EMBL:AEM81953.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tu 4113 {ECO:0000313|EMBL:AEM81953.1}; 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 ----------------------------------------------------------------------- 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; AEM81953.1; -; Genomic_DNA. DR RefSeq; WP_014055458.1; NC_015957.1. DR RefSeq; YP_004812233.1; NC_015957.1. DR EnsemblBacteria; AEM81953; AEM81953; Strvi_2226. DR KEGG; svl:Strvi_2226; -. DR KO; K00547; -. DR BioCyc; SVIO653045:GHK6-2012-MONOMER; -. DR Proteomes; UP000008703; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008703}; KW Methyltransferase {ECO:0000313|EMBL:AEM81953.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008703}; KW Transferase {ECO:0000313|EMBL:AEM81953.1}. SQ SEQUENCE 329 AA; 34496 MW; 9700DF505569913B CRC64; MSVTRTPLAT ALERGPLVLD GGLSNQLEAQ GCDLSDELWS ARLLADDPGQ IEAAHTAYAR AGARVLITSS YQATYEGFAH RGVGHEQATA LLRRSVELAR TGAERAATER ATARDQAAGD RAVGGDRAAD DRAAEPVWVA ASVGPYGAML ADGSEYRGRY GLSVAELVRF HRPRIEALAA AGPDVLALET VPDADEAAAL LSAVEGCGVP VWLSYSIAGE TTRAGQPLRE AFALAAGVDQ VIAVGVNCCE PGDADRAVEI AADITGKPVV VYPNSGEEWD ATARSWRGRA TFDPGRVKAW RDAGARLIGG CCRVGPERIA ELAAVVRNH // ID G2P695_STRVO Unreviewed; 1168 AA. AC G2P695; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 29-APR-2015, entry version 25. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEM86045.1}; GN ORFNames=Strvi_6663 {ECO:0000313|EMBL:AEM86045.1}; OS Streptomyces violaceusniger Tu 4113. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=653045 {ECO:0000313|EMBL:AEM86045.1, ECO:0000313|Proteomes:UP000008703}; RN [1] {ECO:0000313|EMBL:AEM86045.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tu 4113 {ECO:0000313|EMBL:AEM86045.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002994; AEM86045.1; -; Genomic_DNA. DR RefSeq; WP_014059522.1; NC_015957.1. DR RefSeq; YP_004816325.1; NC_015957.1. DR EnsemblBacteria; AEM86045; AEM86045; Strvi_6663. DR KEGG; svl:Strvi_6663; -. DR KO; K00548; -. DR BioCyc; SVIO653045:GHK6-6460-MONOMER; -. DR Proteomes; UP000008703; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008703}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008703}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 235 235 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 301 301 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 302 302 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 745 745 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1168 AA; 127326 MW; 5F44C4414A285292 CRC64; MASHTPSSTS AARAEALREA LATRVVVADG AMGTMLQAQD PSLDDFQQLE GCNEILNVTR PDIVRSVHAE YYAAGVDCVE TNTFGANHAA LGEYDIPDRV HELSEAGARI AREVADEFAA DGRQRWVLGS MGPGTKLPTL GHAPYVTLRD AYQANAEGMI AGGADALLVE TTQDLLQTKA AVLGARRALD ATGVSLPLIC SVTVETTGTM LLGSEIGAAL TALEPLGIDM IGLNCATGPA EMSEHLRHLA RHSRIPLSCM PNAGLPVLGK DGAHYPLSPG ELADAQETFV REYGLSLVGG CCGTTPEHLR QVVERVREMT PTERSPRPEP GAASLYQTVP FRQDTSYLAI GERTNANGSK KFRDAMLEAR WDDCVEIARE QIREGAHLLD LCVDYVGRDG VADMEELAGR FATASTLPLV LDSTEVDVIR AGLEKLGGRA VINSVNYEDG DGPESRFAKV TRLAQEHGAA LIALTIDEEG QARTPEHKVE IAERLIADLT GNWGIHESDI LIDTLTFTIC TGQEESRKDG IATIEAIREL KRRHPDVQTT LGLSNISFGL NPAARIVLNS VFLDECVKAG LDSAIVHASK ILPIARFEEE QVKTALDLIY DRRAEGYDPL QKLMGLFEGA TAKSLKAGKA EELAALPLDE RLKRRIIDGE RNGLEADLDE ALQERPALQI VNETLLDGMK VVGELFGSGQ MQLPFVLQSA EVMKTAVAHL EPHMEKSDDE GKGTIVLATV RGDVHDIGKN LVDIILSNNG YNVVNLGIKQ PVSAILEAAE EHRADVIGMS GLLVKSTVIM KENLEELNQR KLAAQFPVIL GGAALTRAYV EQDLHEIYEG EVRYARDAFE GLRLMDALIA VKRGVPGAAL PELRQRRVPQ RAAQVREPEP DEGPARSDVS TDNPLPTPPF WGTRVVKGIQ QADYASWLDE GALFKGQWGL KQARTGDGPG YEELVENEGR PRLRGWLDRL HTGNLLEAAV VYGYFPCVSK GDDLVLLNED GSERTRFTFP RQRRGRRLCL ADFFRPEESG ETDVVGLQVV TVGSKIGEAT AELFAADSYR DYLELHGLSV QLAEALAEYW HARVRGELGF AGEDPSEMED MFALKYRGAR FSLGYGACPD LEDRAKIADL LQPERIGVKL SEEFQLHPEQ STDAIVIHHP EAKYFNAR // ID G2PKI6_MURRD Unreviewed; 333 AA. AC G2PKI6; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEM71005.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEM71005.1}; GN OrderedLocusNames=Murru_1966 {ECO:0000313|EMBL:AEM71005.1}; OS Muricauda ruestringensis (strain DSM 13258 / LMG 19739 / B1). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Muricauda. OX NCBI_TaxID=886377 {ECO:0000313|EMBL:AEM71005.1, ECO:0000313|Proteomes:UP000008908}; RN [1] {ECO:0000313|Proteomes:UP000008908} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13258 / LMG 19739 / B1 {ECO:0000313|Proteomes:UP000008908}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; AEM71005.1; -; Genomic_DNA. DR RefSeq; WP_014033286.1; NC_015945.1. DR RefSeq; YP_004788427.1; NC_015945.1. DR EnsemblBacteria; AEM71005; AEM71005; Murru_1966. DR KEGG; mrs:Murru_1966; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR BioCyc; MRUE886377:GI6V-1992-MONOMER; -. DR Proteomes; UP000008908; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008908}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:AEM71005.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008908}; KW Transferase {ECO:0000313|EMBL:AEM71005.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 243 243 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 333 AA; 36556 MW; 60F2C57703F1AECA CRC64; MEKIEDILQK RILVLDGAMG TMLQRYKFEE EDFRGERFKD WPSDLQGNND LLSLTRPEAV KDIHRMFLEA GADIIETNTF SGTTIAMADY GMEELVYELN YESAKIAKQV AEEFTKKDPD KPRFVAGSIG PTNKTASMSP DVNDPGYRAV SFDELRIAYK QQVEALLDGG SDVLLVETIF DTLNAKAALF AIEEVKDERN IEIPVMVSGT ITDASGRTLS GQTAEAFLIS VSHIPILSIG FNCALGAKQL VPHLEVISAK SEFATSAHPN AGLPNAFGEY DETPEQMAAQ IKEYVEKGLV NIVGGCCGTT PEHIKAIADV VKDYKPRKLL TPA // ID G2PVM9_9FIRM Unreviewed; 604 AA. AC G2PVM9; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 22. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=Calla_2065 {ECO:0000313|EMBL:AEM74629.1}; OS Caldicellulosiruptor lactoaceticus 6A. OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacterales Family III. Incertae Sedis; OC Caldicellulosiruptor. OX NCBI_TaxID=632516 {ECO:0000313|EMBL:AEM74629.1, ECO:0000313|Proteomes:UP000009257}; RN [1] {ECO:0000313|EMBL:AEM74629.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=6A {ECO:0000313|EMBL:AEM74629.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; AEM74629.1; -; Genomic_DNA. DR RefSeq; WP_014043131.1; NC_015949.1. DR RefSeq; YP_004799606.1; NC_015949.1. DR EnsemblBacteria; AEM74629; AEM74629; Calla_2065. DR KEGG; clc:Calla_2065; -. DR KO; K00547; -. DR BioCyc; CLAC632516:GHP3-2111-MONOMER; -. DR Proteomes; UP000009257; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009257}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:AEM74629.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:AEM74629.1}. SQ SEQUENCE 604 AA; 67246 MW; 7C7655CDC2057360 CRC64; MKKNFREFLK EQSTVIFDGA MGTELLNRGF SLDFPLEWAN VTRPELVKQI HTDYILAGAS SIETNTFGAN ECKLKVFGFE NEVERINRSA VRIAKETADD KVYVIGSVGP LGKPVGSGFE IDDRRAKEVY KRQLYFLLDE GVDAIIFETA ASTHEVQIAI EALKELNDEI PYIIQFSFTK DLSTIYGEDI YRVIEFLKST DADIVGLNCG NGPQKTLEAL KIFSQNLKGP FSVQPNAGYP QLVQGRLVYS TSAKYFASFV PEYIKLGAKV VGGCCGTTPE HIKAIKEKIK EFLPSIEVEV VERREEQKAV LKDTPSELSQ KLGKKFIFTV EISPPKGIEL EKTKEGVKLL KEAGADTVNI ADSPMARVRI SPIALAHILK EELGMESILH FTCRDRNLIS LQSELLGAAA LGVKNVLALT GDPPSIGDHP QAKPVFDVNS EGLVLILSRL NNGTDYMGNP IGKATNFTIG VALNLNADDL VKEIEKLKHK IENGAHFIET QPIYEPETLE RFFEKVDFKL PPILGGILPL RSSRHAEFLH NEVPGITIPD KIRERMRSSK EPAKEGVEIA CEIVEKIKHM VSGIYIMPPF EKYEMAAEII KMFK // ID G2PVN0_9FIRM Unreviewed; 411 AA. AC G2PVN0; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 29-APR-2015, entry version 24. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AEM74630.1}; GN ORFNames=Calla_2066 {ECO:0000313|EMBL:AEM74630.1}; OS Caldicellulosiruptor lactoaceticus 6A. OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacterales Family III. Incertae Sedis; OC Caldicellulosiruptor. OX NCBI_TaxID=632516 {ECO:0000313|EMBL:AEM74630.1, ECO:0000313|Proteomes:UP000009257}; RN [1] {ECO:0000313|EMBL:AEM74630.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=6A {ECO:0000313|EMBL:AEM74630.1}; 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 ----------------------------------------------------------------------- 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; AEM74630.1; -; Genomic_DNA. DR RefSeq; WP_014043132.1; NC_015949.1. DR RefSeq; YP_004799607.1; NC_015949.1. DR EnsemblBacteria; AEM74630; AEM74630; Calla_2066. DR KEGG; clc:Calla_2066; -. DR KO; K00548; -. DR BioCyc; CLAC632516:GHP3-2112-MONOMER; -. DR Proteomes; UP000009257; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009257}; KW Methyltransferase {ECO:0000313|EMBL:AEM74630.1}; KW Transferase {ECO:0000313|EMBL:AEM74630.1}. SQ SEQUENCE 411 AA; 45789 MW; 2D25623786215F71 CRC64; MLKDELYRRV LIFDGAMGTQ LIQNGLKEDE CPDLWSVTRQ DVVASIHRQY FEAGSDCVET NTFGANREKL KKYGLENEVE NINKCAVKLA KEVAKEYSGY VGLSVGPTGR LFTPSGDLSF DEAERIFYEQ ILSGIQAGAD FVSIETMSDI KEAKAAFFAY KKAKEEAKRD IPCLVSLTFE QNKRLLMGTP PEVAAYYFSV IGCDIVGANC SGGAMQLLEV IKQMQGFSFV PLSVKPNAGL PKVVDGKTVY ESCIPEFVNL ADEFVENGVR LYGGCCGTNP EYIRAISKVL KGKEALFESS TQKRFITSIY SLLDISQKFS VYEFKLTNDF SAEAVFELAG LEEDAIFVDI NENVEPELLK EFLIESQDFS KKPYVFNIKT KSHADVIERY YFGVYGVVGN IHGKSAVKVQ I // ID G2RVE2_BACME Unreviewed; 311 AA. AC G2RVE2; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Homocysteine S-methyltransferase ybgG {ECO:0000313|EMBL:AEN91274.1}; GN Name=mmuM {ECO:0000313|EMBL:AEN91274.1}; GN ORFNames=BMWSH_4395 {ECO:0000313|EMBL:AEN91274.1}; OS Bacillus megaterium WSH-002. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1006007 {ECO:0000313|EMBL:AEN91274.1, ECO:0000313|Proteomes:UP000001283}; RN [1] {ECO:0000313|EMBL:AEN91274.1, ECO:0000313|Proteomes:UP000001283} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WSH-002 {ECO:0000313|EMBL:AEN91274.1}; 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; AEN91274.1; -; Genomic_DNA. DR RefSeq; WP_014461447.1; NC_017138.1. DR RefSeq; YP_005496583.1; NC_017138.1. DR EnsemblBacteria; AEN91274; AEN91274; BMWSH_4395. DR KEGG; bmh:BMWSH_4395; -. DR KO; K00547; -. DR BioCyc; BMEG1006007:GL8N-4486-MONOMER; -. DR Proteomes; UP000001283; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001283}; KW Methyltransferase {ECO:0000313|EMBL:AEN91274.1}; KW Transferase {ECO:0000313|EMBL:AEN91274.1}. SQ SEQUENCE 311 AA; 34429 MW; A91893038D7FFF42 CRC64; MNPIQQILHT FPVIVLDGAM ATELERYGCD LNDSLWSAKV LMEQPELIKR VHQDYFAAGA DCAITASYQS TFEGFAKRGL SEAEARELIQ ASVKIAAEAR DEFWQQEENR LNRPKPIVAA SVGPYGAFLA NGSEYTGQYD VTEEELMEFH RPRMKALIEA GADVLACETI PNVMEARAIA RLLEEFEGAY AWITFSAKDD LHISSGTLIS ECARYLNSYE QIAALGVNCT PPQYISSLIK EIKSQTDKPV IVYPNSGEHY DAESKTWNGT SAGETYGCSA HSWYEAGAQL IGGCCRTTPD DIKGITKWAR K // ID G2RX33_BACME Unreviewed; 612 AA. AC G2RX33; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 25. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN Name=yitJ {ECO:0000313|EMBL:AEN90820.1}; GN ORFNames=BMWSH_3939 {ECO:0000313|EMBL:AEN90820.1}; OS Bacillus megaterium WSH-002. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1006007 {ECO:0000313|EMBL:AEN90820.1, ECO:0000313|Proteomes:UP000001283}; RN [1] {ECO:0000313|EMBL:AEN90820.1, ECO:0000313|Proteomes:UP000001283} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WSH-002 {ECO:0000313|EMBL:AEN90820.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; AEN90820.1; -; Genomic_DNA. DR RefSeq; WP_014461038.1; NC_017138.1. DR RefSeq; YP_005496129.1; NC_017138.1. DR EnsemblBacteria; AEN90820; AEN90820; BMWSH_3939. DR KEGG; bmh:BMWSH_3939; -. DR KO; K00547; -. DR BioCyc; BMEG1006007:GL8N-4023-MONOMER; -. DR Proteomes; UP000001283; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001283}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:AEN90820.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:AEN90820.1}. SQ SEQUENCE 612 AA; 68127 MW; 0F196C10700D175B CRC64; MGLLEDLKSK ILIGDGATGT LLYSHGIDSC FEELNITKPE EVSRIHRAYV EAGANVIQTN TYAANYQKLA RYGLEDSVKD INVAGVKLAK QAAKDQAYVV GTLGGIRSFQ KNAISLEEVK RSIREQMFWL LNEGVDGLLF ETYYDFEELK TVLTLARKET DKPIITHVSL HDIGVLQDGR PLADALKELE DLGADVVGLN CRLGPYHMIQ SLEEVPLPDR AFLSAYPNAS LPAYVEGKLE YETNEDYFVE SARLFREQGV RLIGGCCGTT PAHVRAMSSA LKDLPPITSK VVKMRPAVTV QEREQQDKPH MHEIVKKRRS VIVELDPPKQ LGPTKFLEGA KALDKVGVDA ITLADNSLAS PRISNLAMAT LMQQETKARP LIHITCRDRN LIGLQSHLMG LHTLGMNQVL AITGDPSKVG DFPGATSVYD LSSFDLISLI AQFNEGLSYS GKPLGQKTNF SIAAAFNPNV RHLDRAVQRL EKKIDCGAHY FITQPLYSTK QIEEVYEATK HLTTPVYIGI MPLTSARNAR FIHHEVPGIK LSEDILERMD ATGNDRIRGE VEGLAIAKNL IDTAYELFDG IYLITPFMRY EMTEILTRYI HDKQLVTSER KI // ID G2RX34_BACME Unreviewed; 1147 AA. AC G2RX34; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 30. DE SubName: Full=Methionine synthase I cobalamin-binding domain-like protein {ECO:0000313|EMBL:AEN90821.1}; GN Name=metH {ECO:0000313|EMBL:AEN90821.1}; GN ORFNames=BMWSH_3940 {ECO:0000313|EMBL:AEN90821.1}; OS Bacillus megaterium WSH-002. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1006007 {ECO:0000313|EMBL:AEN90821.1, ECO:0000313|Proteomes:UP000001283}; RN [1] {ECO:0000313|EMBL:AEN90821.1, ECO:0000313|Proteomes:UP000001283} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WSH-002 {ECO:0000313|EMBL:AEN90821.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP003017; AEN90821.1; -; Genomic_DNA. DR RefSeq; WP_014461039.1; NC_017138.1. DR RefSeq; YP_005496130.1; NC_017138.1. DR EnsemblBacteria; AEN90821; AEN90821; BMWSH_3940. DR KEGG; bmh:BMWSH_3940; -. DR KO; K00548; -. DR BioCyc; BMEG1006007:GL8N-4024-MONOMER; -. DR Proteomes; UP000001283; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001283}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 226 226 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 724 724 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1147 AA; 126565 MW; 6D0BF318D90C9B7E CRC64; MSSLIEQQLK KRILVIDGAM GTMIQDADLT AEDFGGEEYE GCNEYLTRTA PHVIQRIHEE YFAAGADIIE TNTFGSTSTV LDEYDLGHLA YELNIEAVKL ACAARDKYST PEWPRFVAGA IGPTTKTLSV TGGITFPELV ESYEEQARGL LDGGVDLLLV ETCQDMLNVK AAFLGITAAF EKLKTEVPIM ISGTIEPMGT TLAGQDIESF YLSLEHMKPL SVGLNCATGP EFMTDHIRSL SDLATSAVSC YPNAGLPDEE GNYHESPELL AQKIKGFADK GWLNFVGGCC GTTPAHIKAL AEAVKEVAPR SLDRSEHNHA VTGIEPLVYD DSMRPLFVGE RTNVIGSRKF KRLIAEGKIE EASEIARAQV KNGAHVIDIC LADPDREEME DMEEFIQEVV KKVKVPLVID STDEKVIEKA LTYSQGKVII NSINLEDGEE RFDAILPLVK KFGAALVVGT IDETGMAVTA ERKVEIAKRS HDLLVEKHGF NPKDIIFDPL VFPVGTGDEQ YIGSAEETVK GIKMIKEALP DCLTILGVSN VSFGLPPVGR EVLNAVYLYH CTQAGLDYAI VNTEKLERYA SIPEAEIELA NALLFNTTDE TLSTFTDFYR DKKKEAKVEI STLTLEERLA MYIVEGTKEG LLPDLEQALA QYDDPLDIIN GPLMEGMAEV GRLFNDNQLI VAEVLQSAEV MKASVAFLEP HMEATENDSG KGKVILATVK GDVHDIGKNL VDIILSNNGF KVIDLGIKVT PQQLIEAVKD EKPDIIGLSG LLVKSAQQMV LTAQDLTQSS IDVPIMVGGA ALSRKFTDFK IAPEYEGAVL YAKDAMDGLA LANKLQNKEE VIQLLADLKT RQEKKVTVRE RQPQTAQAAT AVLERSAIST DAPVFVPADL KRHVVKHYDL AQVLPYINWQ MLLGHHLGLK GKVNKLLAEK DERAVQLKET VDDLLELALK ENLIKPAVIY QFFPAQADGN DLIIYDPADE KTEIERFTFP RQAKGQFLCL SDFAKPKEKE MDYVCFFSVT AGTGIRERAA KFKENGEFLK SHVFQALALE LAEGLAERVH QQIRDRWGFP DSPDFTMAER FSAKYQGQRF SFGYPACPDL EDQAKLFKLI KPEDIGIQLT DGFMMEPEAS VTALVFAHPE AKYFNVL // ID G2S934_ENTAL Unreviewed; 310 AA. AC G2S934; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AEN63601.1}; GN OrderedLocusNames=Entas_0853 {ECO:0000313|EMBL:AEN63601.1}; OS Enterobacter asburiae (strain LF7a). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex. OX NCBI_TaxID=640513 {ECO:0000313|EMBL:AEN63601.1, ECO:0000313|Proteomes:UP000008527}; RN [1] {ECO:0000313|Proteomes:UP000008527} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LF7a {ECO:0000313|Proteomes:UP000008527}; 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 ----------------------------------------------------------------------- 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; AEN63601.1; -; Genomic_DNA. DR RefSeq; WP_014069047.1; NC_015968.1. DR RefSeq; YP_004827386.1; NC_015968.1. DR EnsemblBacteria; AEN63601; AEN63601; Entas_0853. DR KEGG; eas:Entas_0853; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR BioCyc; EASB640513:GKDM-879-MONOMER; -. DR Proteomes; UP000008527; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008527}; KW Methyltransferase {ECO:0000313|EMBL:AEN63601.1}; KW Transferase {ECO:0000313|EMBL:AEN63601.1}. SQ SEQUENCE 310 AA; 33527 MW; 1CA8DC2E9BA33A82 CRC64; MSQNNPLSAI LETQPFVILD GAMATELEAR GCNLADSLWS AKVLVENPEL IREVHLDYFR AGAQVAITAS YQATPAGFAA RGLDDAQSRA LIGKSVELAR KAREAYLAEN PHAGTLLVAG SVGPYGAYLA DGSEYRGDYV RSAEEFTAFH RPRVEALLDA GADLLACETL PSFAESKALA ALLSEYPRAR AWFSFTLRDS EHLSDGTPLR EVIAELVRYP QIVALGINCI ALENTTAALH YLQSLTSLPL VVYPNSGEHY DAVTKTWHHH GEACEALAGY LPQWLAAGAK LIGGCCRTTP KDIAELNARR // ID G2SA31_ENTAL Unreviewed; 1227 AA. AC G2SA31; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEN62999.1}; GN OrderedLocusNames=Entas_0244 {ECO:0000313|EMBL:AEN62999.1}; OS Enterobacter asburiae (strain LF7a). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex. OX NCBI_TaxID=640513 {ECO:0000313|EMBL:AEN62999.1, ECO:0000313|Proteomes:UP000008527}; RN [1] {ECO:0000313|Proteomes:UP000008527} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LF7a {ECO:0000313|Proteomes:UP000008527}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP003026; AEN62999.1; -; Genomic_DNA. DR RefSeq; WP_014068474.1; NC_015968.1. DR RefSeq; YP_004826784.1; NC_015968.1. DR EnsemblBacteria; AEN62999; AEN62999; Entas_0244. DR KEGG; eas:Entas_0244; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; EASB640513:GKDM-254-MONOMER; -. DR Proteomes; UP000008527; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008527}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135697 MW; FC9A018EFFF62342 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQGY RLSEDDFRGE RFADWPCDLK GNNDLLVLSK PQVIADIHNA YFEAGADIVE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPDKPRYVA GVLGPTNRTA SISPDVNDPA FRNISFDQLV AAYRESTKAL VEGGSDLILI ETVFDTLNAK AAIYAVKEEF EALGVDLPIM ISGTITDASG RTLSGQTTEA FYNSLHHAEA LSFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAAQIREWAE SGFLNIVGGC CGTTPEHIAA MSNAVAGLPP RKLPELPVAC RLSGLEPLTI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VESGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGIDIFIHHA KLVRRYGAAV VVMAFDEVGQ ADTRERKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDATER MLDLAEKYRG SKSDEAVNVQ QAEWRSWDVR KRLEYSLVKG ITEFIELDTE EARLQSARPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EKGSSNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIIDL GVMVPADKIL KTAREVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVSSL LSATQHDDFV ARTRKEYETV RVQHARKKPR TPPVTLQAAR DNDLAFDWSS YTPPVAHRLG VQDVTASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG EEAQRLFKDA NEMLDMLSAE KTLNPRGVVG LFPANRVGDD VEIYRDETRT HVLAVSRHLR QQTEKVGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA IADRLAEAFA EYLHERVRKV HWGYAANENL SNEELIRENY QGIRPAPGYP ACPEHTEKGT IWELLDVETH TGMKLTESFA MWPGASVSGW YFSHPDSKYF AVAQLQRDQI EDYAQRKGMS VSEVERWLAP NLGYDAD // ID G2SGW1_RHOMR Unreviewed; 1236 AA. AC G2SGW1; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 29-APR-2015, entry version 23. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEN74325.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEN74325.1}; GN ORFNames=Rhom172_2432 {ECO:0000313|EMBL:AEN74325.1}; OS Rhodothermus marinus SG0.5JP17-172. OC Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis; OC Rhodothermaceae; Rhodothermus. OX NCBI_TaxID=762570 {ECO:0000313|EMBL:AEN74325.1, ECO:0000313|Proteomes:UP000001280}; RN [1] {ECO:0000313|EMBL:AEN74325.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SG0.5JP17-172 {ECO:0000313|EMBL:AEN74325.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP003029; AEN74325.1; -; Genomic_DNA. DR RefSeq; WP_014067892.1; NC_015966.1. DR RefSeq; YP_004826162.1; NC_015966.1. DR EnsemblBacteria; AEN74325; AEN74325; Rhom172_2432. DR KEGG; rmg:Rhom172_2432; -. DR KO; K00548; -. DR BioCyc; RMAR762570:GJAN-2479-MONOMER; -. DR Proteomes; UP000001280; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001280}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEN74325.1}; KW Transferase {ECO:0000313|EMBL:AEN74325.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1236 AA; 138405 MW; 9CE379293516F80F CRC64; MRDTHPLARL LQERILILDG AMGTMIQRHR LSEEDFRGAR FADHPHPLRG NNDLLVLTQP ELIRDIHRAY LEAGADLIET NTFNANAISQ ADYGLEHLVY ELNVAAARLA REAADEFTRR TPERPRFVAG AIGPTNKTLS ISPDVNNPAY RAVTFDEMVA VYREQVRGLL DGGVDVLLVE TVFDTLNCKA ALFAIQEEFR ARARAVPVMV SGTIVDQSGR TLSGQTPEAF WISIAHMPHL LSVGLNCALG SGQMRPFIEE LARVATVFTS LYPNAGLPDE LGQYRETPEY MAAQLADYAR EGWLNLAGGC CGTTPEHIRA IAEALEGIPP RRIPEVPRTL RLSGLEPLVF RPDLNFVNIG ERTNVTGSRR FARLIREGRY EEALDVAREQ VENGAQMIDV NMDEGLLDGV QAMTTFLNLI ATEPEIARVP VVIDSSKWEV IEAGLKCLQG KGVVNSLSLK DGEEVFKERA RRVRQYGAAV IVMAFDEQGQ ADTLERRIEI CRRAYRILTE EVGFPPEDII FDPNIYAVAT GIPEHNRYAI DFLEATRWIK TNLPYARVSG GISNLSFSFR GNEPVRRAMH TVFLYHAVQA GMDMGIVNPG QLGIYEEIDP ELRERIEDVL FDRRPDATER LIALAQTLTQ SAADAAESET LAWRQAPVEE RLRHALVKGI TEFIEEDVEE ARQKYGSPLA VIEGPLMDGM NVVGDLFGAG KMFLPQVVKS ARVMKKAVAY LVPFLEAEKQ KLGDTRPRAR ILLATVKGDV HDIGKNIVGV VLQCNGFEVI DLGVMVPADR ILEEARRHRV DLIGLSGLIT PSLDEMVHVA RELERAGFDT PLLIGGATTS KVHTALKIDP CYHAPVVHVL DASRAVPVAS ALVDPDRRDA FAEEIRQEYE AIRRRHGRRT DEQLLTIEEA RANRFTCDWS AVPIMRPNRP GLTVFRNYPL AEIRRYIDWT PFFQAWELRG KYPRILDDPK KGPEARRLFA DANQLLDEII AHGWLQAHGV VGLFPANSQG DDVLVFADEA RRKVRAVLHF LRQQTPKRTG QPNRSLADYV APVESGRADY IGAFAVTAGH GLEELVARFE RAHDDYQAIL AKALADRLAE AFAELLHERV RRELWGYAPD ERLTNEELIA ERYRGIRPAP GYPACPDHTE KWTLWELLEA ERHTGIRLTE HLAMHPAASV CGYYLAHPEA SYFNVGHLGM DQIEDYARRK GMTVEEVERW LAPRLAYDPA ARADAA // ID G2SXJ6_ROSHA Unreviewed; 831 AA. AC G2SXJ6; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 29-APR-2015, entry version 20. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AEN97353.1}; GN OrderedLocusNames=RHOM_11225 {ECO:0000313|EMBL:AEN97353.1}; OS Roseburia hominis (strain DSM 16839 / NCIMB 14029 / A2-183). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Roseburia. OX NCBI_TaxID=585394 {ECO:0000313|EMBL:AEN97353.1, ECO:0000313|Proteomes:UP000008178}; RN [1] {ECO:0000313|Proteomes:UP000008178} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16839 / NCIMB 14029 / A2-183 RC {ECO:0000313|Proteomes:UP000008178}; 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 ----------------------------------------------------------------------- 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; AEN97353.1; -; Genomic_DNA. DR RefSeq; WP_014080364.1; NC_015977.1. DR RefSeq; YP_004839285.1; NC_015977.1. DR EnsemblBacteria; AEN97353; AEN97353; RHOM_11225. DR KEGG; rho:RHOM_11225; -. DR KO; K00548; -. DR BioCyc; RHOM585394:GHYQ-2274-MONOMER; -. DR Proteomes; UP000008178; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008178}; KW Methyltransferase {ECO:0000313|EMBL:AEN97353.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008178}; KW Transferase {ECO:0000313|EMBL:AEN97353.1}. SQ SEQUENCE 831 AA; 89811 MW; 7F3ECFE72445B983 CRC64; MTREEFATLV GSRPVILDGA TGTNLQKAGM PVGVCPEQWI LENPGVLIEL QERYVEAGTD ILFAPTFTAS RIKLEEYGLE DSLVQMNREL VALSKRAAGG RAYVAGDLTM TGRQLYPLGD LMFEDLVEVY KEQAKVICEA GADLFVVETM MSLQECRAAV IAIREVCDLP IMVSLTYNED GRTLYGTDPA TAVIVLQSLG ADAVGLNCST GPEAMIDPVQ QMAEYATIPL LAKPNAGMPE LCDGVTVYRT TPEEFASVGA KLVEAGAAII GGCCGTTPEH ICALKQAVGS MPVHMPLTKK RRMLASERMH VEIRLDGKFM VIGERINPTG KKKLQAELKE GSLSMVRTMA TEQEENGAQI LDINMGMNGI DEKQMMLDAI YEVTSTVDLP LCIDSSHVDI IEAALRIYPG RALVNSISLE KEKIEYLLPI AKKYGAMFIL LPLSDEGLPK DSAEKHGIIR EILRRAEAIG MGKEDIVVDG LVATIGANPK AALECFETFS FCKNEMELPT VCGLSNISFG LPERSYVNTA FLTMAIGNGL TMAIANPSQE LLMNAAFASD MLLNKEESGI RYIGRMNYLS EKHEGMEHVW VPVGTAKGAA VKGTAAGQAG NAGGAKDSGN ANEARSAVFT AVLKGNKNHI LDEVKHALDT GEKPDDIING HLIPAINEVG ELFDKQKYFL PQLISSANTM KVAIEYLEPM LARSDKEPKA TLVVATVEGD IHDIGKNLVV LMLKNYGYHV IDLGKDVPAD LIVDTAMKEN ARVIGLSALM TTTMMRMKDV VELVKERGCT AKVVIGGAAI TESFAEEIGA DGYSKDAAEC VKLVDRLLEE E // ID G2TR31_BACCO Unreviewed; 1154 AA. AC G2TR31; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 29-APR-2015, entry version 27. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEP00107.1}; GN ORFNames=Bcoa_0889 {ECO:0000313|EMBL:AEP00107.1}; OS Bacillus coagulans 36D1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=345219 {ECO:0000313|EMBL:AEP00107.1, ECO:0000313|Proteomes:UP000009283}; RN [1] {ECO:0000313|EMBL:AEP00107.1, ECO:0000313|Proteomes:UP000009283} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=36D1 {ECO:0000313|EMBL:AEP00107.1}; 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). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP003056; AEP00107.1; -; Genomic_DNA. DR RefSeq; WP_014096249.1; NC_016023.1. DR RefSeq; YP_004858887.1; NC_016023.1. DR ProteinModelPortal; G2TR31; -. DR EnsemblBacteria; AEP00107; AEP00107; Bcoa_0889. DR GeneID; 11174473; -. DR KEGG; bag:Bcoa_0889; -. DR KO; K00548; -. DR BioCyc; BCOA345219:GH5A-885-MONOMER; -. DR Proteomes; UP000009283; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000009283}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000009283}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 724 724 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1154 AA; 126335 MW; 3FAC7B074C582774 CRC64; MGQTLFEQQL ANRILILDGA MGTMIQQQHL TAADFGGEAY EGCNEYLNLT APDLIRSIHE AYLEAGADII ETNTFGATSI VLNEYGLGHF AEKINIEAAR IAKQAAKKFS TPERPRFVAG SMGPTTKTLS VTGGTTFDAL KTAYQEQACG LIKGGVDVLL LETSQDLLNV KAAFLGITDA FNETGKKLPL LISGTIEPMG TTLAGQNIEA FYISVEHMQP AAVGLNCATG PEFMADSIRT LAGLAKTAVS CYPNAGLPDE EGHYHETPES LAVKMKGFAE KGWLNIAGGC CGTTPAHIKA LNEALAGLPP RQPAKQEHHA VSGIEPFIYD DPSTRPIFVG ERTNVIGSRK FRRLIAEGKW EEASEIARTQ VKNGAQIIDI CLADPDRDEI SDMENFISIA VKKVKVPFMI DSTDENVIEK AFTYCQGKSI VNSINLENGT ERFEKVVPLL KKYGGAVVVG TIDEEGMAVT AERKLEIARR SYDLLVDTYG LNPRDLIFDP LVFPAGTGDK QYFGAAKETV EGIRLIKEAM PECQTILGVS NVSFGLPPAG REVLNSVFLY HCTKAGLDYA IVNTEKLERF ASIPEENVKM AEKLLFETSD EALAAFTEYY RGKVQEKKAP KSTMTLAERL ANYVVEGTKE GLIPDLEQAL KEYPDPLAII NGPLMDGMAE VGRLFNDNQL IVAEVLQSAE VMKASVAFLE PFMEKNETST KGKVLLATVK GDVHDIGKNL VDIILSNNGY KVVDLGIKVA PADLIHAVRK EKPDVIGLSG LLVKSAQQMV VTAQDLREAG IRQPILVGGA ALSRKFTVNK IAPQYEGLVL YAKDAMEGLT LANKLQDESE RSSLETELAN QRSGGTRVAA VNAGGAPVAT LPRRSSVSPD ALVYQPADLK RHVLRNYPLA HIEPYVNMQM LLGHHLGLKG RVEKLLAEGD ERALKLKQQV DELREWVMKE KLLQPSAVYQ FFPAQSDGNT LIVYEPAGEP GTLDLKSLSV LERFTFPRQA KPPYLCLADY VRSVDSGVVD YVCMFAVVAG KNIRHHARYL KEAGEYFKSH ALQALALETA EGFAERLHEL IRGQWGFPDP ADFTMQQRFA AKYQGQRYSF GYPACPNLED QAKLFKLLQP QKIGLHLTEG YMMEPEAAVT ALVFSHPEAR YFAV // ID G2TR32_BACCO Unreviewed; 629 AA. AC G2TR32; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 29-APR-2015, entry version 25. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=Bcoa_0890 {ECO:0000313|EMBL:AEP00108.1}; OS Bacillus coagulans 36D1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=345219 {ECO:0000313|EMBL:AEP00108.1, ECO:0000313|Proteomes:UP000009283}; RN [1] {ECO:0000313|EMBL:AEP00108.1, ECO:0000313|Proteomes:UP000009283} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=36D1 {ECO:0000313|EMBL:AEP00108.1}; 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). CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; AEP00108.1; -; Genomic_DNA. DR RefSeq; WP_014096250.1; NC_016023.1. DR RefSeq; YP_004858888.1; NC_016023.1. DR ProteinModelPortal; G2TR32; -. DR EnsemblBacteria; AEP00108; AEP00108; Bcoa_0890. DR KEGG; bag:Bcoa_0890; -. DR KO; K00547; -. DR BioCyc; BCOA345219:GH5A-886-MONOMER; -. DR Proteomes; UP000009283; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009283}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:AEP00108.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000009283}; KW Transferase {ECO:0000313|EMBL:AEP00108.1}. SQ SEQUENCE 629 AA; 69290 MW; F4121182ABAF3C8F CRC64; MPPFLGGFFH IIQRECKNLN LLETLKNRIL VADGAMGTLL YAYGADTCYE SFNLTHPEDI HAIHRAYIEA GASVIQTNTY SANYIKLAQY GLEEKVKDIN KAAVQIAKEA ANRDTFILGT VGGIRGQRKT EATLAEIKRT FREQIFHLLN EGVDALLLET YFDAEELYTV VDIAKKEADV PVIAQFSLIE PGVLQNGTPV RDAFKELENR GADVTGLNCR LGPHHMIQAF EEIPIPKRAF LSAYPNASLL DYEEGRFTFT NNADYFKTCA EKLVEQGVRL IGGCCGTTPA HIKAIADGVQ GLLPVTEKTV RPPKIEIAAA PAQHEPPLHE IVKKRRSVIV ELDTPKTLNT ARFFEGAKAL HDAGIDALTM ADNSLASPRI SNTAIASILK EKHGIRPLVH ITCRDRNLIG LQSHLMGLAA LGIDQVLAIT GDPTKIGDFP GATSVYDLSS MELIAMIKQF NDGISHSGKS LHRKTNFSVA AAFNPNVRNL DKTVGRLERK IRHGADYFIT QPVFSTEKIE QIHEATKHLD APIYLGIMPL TSYRNAVFLH NEVPGIKLTD EILAAMEKTN GDPAKAREES LAISRTLIDA ALGYFNGIYL ITPLERYELT VECTRYIHEK TAVQGAGIV // ID G2WID8_YEASK Unreviewed; 324 AA. AC G2WID8; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 07-JAN-2015, entry version 15. DE SubName: Full=K7_Mht1p {ECO:0000313|EMBL:GAA24831.1}; GN Name=K7_MHT1 {ECO:0000313|EMBL:GAA24831.1}; GN ORFNames=SYK7_044871 {ECO:0000313|EMBL:GAA24831.1}; 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 {ECO:0000313|Proteomes:UP000001608}; RN [1] {ECO:0000313|Proteomes:UP000001608} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Kyokai no. 7 / NBRC 101557 {ECO:0000313|Proteomes:UP000001608}; 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; DG000048; GAA24831.1; -; Genomic_DNA. DR OrthoDB; EOG7X9GHR; -. DR Proteomes; UP000001608; Chromosome XII. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001608}. SQ SEQUENCE 324 AA; 36746 MW; A77194694A3F1901 CRC64; MKRIPIKELI VEHPGKVLIL DGGQGTELEN RGININSPVW SAAPFTSESF WEPSSQERKV VEEMYRDFMI AGANILMTIT YQANFQSISE NTSIKTLAAY KRFLDKIVSF TREFIGEERY LIGSIGPWAA HVSCEYTGDY GPHPENIDYY GFFKPQLENF NQNRDIDLIG FETIPNFHEL KAILSWDEDI ISKPFYIGLS VDDNSLLRDG TTLEEISVHI KGLGNKINKN LLLMGVNCVS FNQSALILKM LHEHLPGMPL LVYPNSGEIY NPKEKTWHRQ TNKLDDWETT VKKFVDNGAR IIGGCCRTSP KDIAEIASAV DKYS // ID G2WL32_YEASK Unreviewed; 105 AA. AC G2WL32; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 07-JAN-2015, entry version 15. DE SubName: Full=K7_Ymr321cp {ECO:0000313|EMBL:GAA25775.1}; GN Name=K7_YMR321C {ECO:0000313|EMBL:GAA25775.1}; GN ORFNames=SYK7_056851 {ECO:0000313|EMBL:GAA25775.1}; 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 {ECO:0000313|Proteomes:UP000001608}; RN [1] {ECO:0000313|Proteomes:UP000001608} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Kyokai no. 7 / NBRC 101557 {ECO:0000313|Proteomes:UP000001608}; 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; DG000049; GAA25775.1; -; Genomic_DNA. DR OrthoDB; EOG7X9GHR; -. DR Proteomes; UP000001608; Chromosome XIII. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001608}. SQ SEQUENCE 105 AA; 11657 MW; FECF61C0B27ACB7F CRC64; MMDLGDKINP NFSFLGIDCV SFNQSPDILE SLHQALPNMA LLAYPNSGEV YDTEKKIWLP NSDKLNSWDT VVKQYISSGA RIIGGCCRTS PKDIQEISAA VKKYT // ID G2WNR3_YEASK Unreviewed; 325 AA. AC G2WNR3; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=K7_Sam4p {ECO:0000313|EMBL:GAA26706.1}; GN Name=K7_SAM4 {ECO:0000313|EMBL:GAA26706.1}; GN ORFNames=SYK7_068191 {ECO:0000313|EMBL:GAA26706.1}; 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 {ECO:0000313|Proteomes:UP000001608}; RN [1] {ECO:0000313|Proteomes:UP000001608} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Kyokai no. 7 / NBRC 101557 {ECO:0000313|Proteomes:UP000001608}; 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; GAA26706.1; -; Genomic_DNA. DR ProteinModelPortal; G2WNR3; -. DR OrthoDB; EOG7X9GHR; -. DR Proteomes; UP000001608; Chromosome XVI. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001608}. SQ SEQUENCE 325 AA; 36678 MW; 4CC68E458A051B5D CRC64; MARLPLKQFL ADNPKKVLVL DGGQGTELEN RGIKVANPVW STIPFISESF WSDESSANRK IVKEMFNDFL HAGAEILMTT TYQTSYKSVS ENTPIRTLSE YNNLLNRIVD FSRNCIGEDK YLIGCIGPWG AHICREFTGD YGAEPENIDF YQYFKPQLEN FNKNDKLDLI GFETIPNIHE LKAILSWDES VLSRPFYIGL SVHEHGVLRD GTTMEEIAQV IKDLGDKINP NFSFLGINCV SFNQSPDILE SLHQALPNMA LLAYPNSGEV YDTEKKIWLP NSDKLNSWDT VVKQYISSGA RIIGGCCRTS PKDIQEISAA VKKYT // ID G2WXF0_VERDV Unreviewed; 355 AA. AC G2WXF0; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 01-APR-2015, entry version 16. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGY21405.1}; GN ORFNames=VDAG_02929 {ECO:0000313|EMBL:EGY21405.1}; OS Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137) OS (Verticillium wilt). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Hypocreomycetidae; Glomerellales; OC Plectosphaerellaceae; mitosporic Plectosphaerellaceae; Verticillium. OX NCBI_TaxID=498257 {ECO:0000313|Proteomes:UP000001611}; RN [1] {ECO:0000313|Proteomes:UP000001611} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VdLs.17 / ATCC MYA-4575 / FGSC 10137 RC {ECO:0000313|Proteomes:UP000001611}; RX PubMed=21829347; DOI=10.1371/journal.ppat.1002137; RA Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E., RA Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J., RA Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., RA Santhanam P., Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., RA Inderbitzin P., Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., RA Galagan J., Cuomo C.A., Dobinson K.F., Ma L.-J.; RT "Comparative genomics yields insights into niche adaptation of plant RT vascular wilt pathogens."; RL PLoS Pathog. 7:E1002137-E1002137(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; DS572698; EGY21405.1; -; Genomic_DNA. DR RefSeq; XP_009651877.1; XM_009653582.1. DR EnsemblFungi; EGY21405; EGY21405; VDAG_02929. DR GeneID; 20704392; -. DR KEGG; vda:VDAG_02929; -. DR InParanoid; G2WXF0; -. DR KO; K00547; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000001611; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001611}; KW Methyltransferase {ECO:0000313|EMBL:EGY21405.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001611}; KW Transferase {ECO:0000313|EMBL:EGY21405.1}. SQ SEQUENCE 355 AA; 38221 MW; 3FFDECCF967667BF CRC64; MSSSPSNEVL ILDGGLGTSL GDKYGVRFDK STPLWSSHML VSDQDTLLAC QKDFGDVPVD IILTATYQFS IHGFANTRTA HFPDGIDRTK IASYARDAIA IAHSAGKANG GQVALSVGPY GACMIPGQEY TGKYDPEHDT PEDLAAWHLE RFRIFEEAGG FSSPVSYVAV ETMPRLDEIV AARKALDDLG AKAANTPFWI ACVFPGEEMA LPDGASISSA VDAMLNPAVA RSQPWGIGIN CTKVWKLKEL IARFEAAVAD QVQAGHVNEA PALVLYPDGT DGEVYNTTTQ TWELPAGGKV QGAPWEEQLA EIVRDANTRG KWKQIVVGGC CKASHAHLAR LRDYVLNGNE QAKNE // ID G2XMY6_BOTF4 Unreviewed; 369 AA. AC G2XMY6; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 07-JAN-2015, entry version 15. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CCD42242.1}; GN ORFNames=BofuT4_P013700.1 {ECO:0000313|EMBL:CCD42242.1}; OS Botryotinia fuckeliana (strain T4) (Noble rot fungus) (Botrytis OS cinerea). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes; OC Helotiales; Sclerotiniaceae; Botrytis. OX NCBI_TaxID=999810 {ECO:0000313|EMBL:CCD42242.1, ECO:0000313|Proteomes:UP000008177}; RN [1] {ECO:0000313|Proteomes:UP000008177} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T4 {ECO:0000313|Proteomes:UP000008177}; 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; FQ790245; CCD42242.1; -; Genomic_DNA. DR InParanoid; G2XMY6; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000008177; Unassigned contigs. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008177}; KW Reference proteome {ECO:0000313|Proteomes:UP000008177}. SQ SEQUENCE 369 AA; 40267 MW; 937CEA24787C2665 CRC64; MSPGCKIHLL DGGLGTTLGD SHQVQFTEKE PLWSSQLLIP THPHGPKTLL ATQKSFVDAG ADILLTATYQ TSYEGFGGSG YAVHSHSSSN SGKADGDKEE VNGIMRSAVD IASDAFSTKK DSNGKIALSL GAYGAIMTPG QEYTGKYDDD HKSSEQLSSW HHERISVFSR DPKCWERVDY VAFETIPLLE EIEGVRKSMG EVENSNGGTA GSKPFWITCV FPGEGNCLPG GSSVQQIMQA MLGNKGGSPV PFGIGLNCTK VGKVESLILE FEQEVKALIE KGDVSEWPSL VVYPDGTIKG EVYNTSTKVW EIREPPGKED LQWDEAVLEI VRRARDRGLW KDIIVGGCCK TTPREIGKLR ERIDRLDKE // ID G2Z4B2_FLABF Unreviewed; 325 AA. AC G2Z4B2; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=FL-15, complete genome {ECO:0000313|EMBL:CCB70605.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CCB70605.1}; GN OrderedLocusNames=FBFL15_2608 {ECO:0000313|EMBL:CCB70605.1}; OS Flavobacterium branchiophilum (strain FL-15). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=1034807 {ECO:0000313|Proteomes:UP000009186}; RN [1] {ECO:0000313|Proteomes:UP000009186} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FL-15 {ECO:0000313|Proteomes:UP000009186}; RX PubMed=21926215; DOI=10.1128/AEM.05625-11; RG 1:IP; RG Microbial Evolutionary Genomics,F-75015 Paris; RG France 2:CNRS; RG URA2171; RG F-75015 Paris,France 3:Unite de Virologie et Immunologie Mol.; RG INRA,78352 Jouy en Josas Cedex; RG France. 4:Unite de Mathemathique; RG Informatique et Genome,INRA; RG 78352 Jouy en Josas Cedex; RG France. 5:CEA/Genoscope; RG Evry; RG France; RA Touchon M., Barbier P., Bernardet J.F., Loux V., Vacherie B., RA Barbe V., Rocha E.P., Duchaud E.; RT "Complete Genome Sequence of the Fish Pathogen Flavobacterium RT branchiophilum."; RL Appl. Environ. Microbiol. 77:7656-7662(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; FQ859183; CCB70605.1; -; Genomic_DNA. DR RefSeq; WP_014085058.1; NC_016001.1. DR RefSeq; YP_004844842.1; NC_016001.1. DR EnsemblBacteria; CCB70605; CCB70605; FBFL15_2608. DR KEGG; fbr:FBFL15_2608; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR BioCyc; FBRA1034807:GHGD-2608-MONOMER; -. DR Proteomes; UP000009186; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009186}; KW Methyltransferase {ECO:0000313|EMBL:CCB70605.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000009186}; KW Transferase {ECO:0000313|EMBL:CCB70605.1}. SQ SEQUENCE 325 AA; 35810 MW; 8DA5C7C42F7EE0C8 CRC64; MSKIQNALKE RILVLDGAMG TMLQRNNFSE EDFRGDRFKN FPHPLKGNND LLSITQPEAV KQVHRLYFQA GADIVETNTF SGTTIGMADY HLEDLVYELN FQSAKIAREV ADEFTDRPRF VAGSIGPTNR TASMSPDVND PGYRAVTFDD LRVAYKQQVE ALIDGGCDVL LVETIFDTLN AKAALFAIEE VKEERNLDIP VMVSGTITDA SGRTLSGQTV EAFLISISHI PLLSVGFNCA LGADQLKPYL KRLAMNTQLN ISAHPNAGLP NAFGHYDQTP EEMQALIKEY LQDNLVNIIG GCCGTTPEHI KAIADAAKEF KPRKV // ID G2ZAT7_LISIP Unreviewed; 617 AA. AC G2ZAT7; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 25. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=LIV_1653 {ECO:0000313|EMBL:CBW86140.1}; OS Listeria ivanovii (strain ATCC BAA-678 / PAM 55). OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=881621 {ECO:0000313|EMBL:CBW86140.1, ECO:0000313|Proteomes:UP000001286}; RN [1] {ECO:0000313|EMBL:CBW86140.1, ECO:0000313|Proteomes:UP000001286} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-678 / PAM 55 {ECO:0000313|Proteomes:UP000001286}; RX PubMed=22072644; DOI=10.1128/JB.06120-11; RA Buchrieser C., Rusniok C., Garrido P., Hain T., Scortti M., RA Lampidis R., Karst U., Chakraborty T., Cossart P., Kreft J., RA Vazquez-Boland J.A., Goebel W., Glaser P.; RT "Complete Genome Sequence of the Animal Pathogen Listeria ivanovii, RT Which Provides Insights into Host Specificities and Evolution of the RT Genus Listeria."; RL J. Bacteriol. 193:6787-6788(2011). CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR687253; CBW86140.1; -; Genomic_DNA. DR RefSeq; WP_014093038.1; NC_016011.1. DR RefSeq; YP_004855403.1; NC_016011.1. DR EnsemblBacteria; CBW86140; CBW86140; LIV_1653. DR KEGG; liv:LIV_1653; -. DR KO; K00547; -. DR Proteomes; UP000001286; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001286}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 617 AA; 68509 MW; D5D02B66C4EA5D49 CRC64; MNLRKDLSEK VLIADGGMGT LLYSYGVDRS FEELNLSHPE DIVSIHKAYI GAGADIIQTN TYGANYIKLA RYGLEDEVKR INQAAIRLAK EAARGTGTYI FGTIGGINGA VDARLPAAPL EEIKRSFREQ LYCFLLDGVD AILLETYYDL EELKTVLKIL RETTDLPVVA NVSMHEPGLL QNGQKLSDAL EELIALGADV VGVNCRLGPY HMARALETVP LYEHAYLAVY PNASLPEVQE GKVIYQSDTD YFEHYGEVFR QEGARIIGGC CGTTPDHIKA LRNGLKTTKP VLEKEVRPLL ELVPEEVVDE DSGVRLLDKV KEGLTILVEL DPPRTFDTSK FFEGAKALDE AGVDAITISD NSLATPRISN MALASILKHE YGIKPLIHLT TRDHNLVGMH SHVMGFHKLG LHDVLAITGD PTKVGDFPGA SSVFDLRSVE LVQLIKKFND GISYTGKSLK EKARFHVGAA FNPNVLNLEK AVRLIERKVE YGADYIITQP IYDVNKAVLL KEALQKANIN VPLFIGVMPL LSSRNAEFLH NEVPGIRLTD EVRERMRDAE EQGRANEKGM EIARELIDSI CAYFQGIYII TPFLRYDLSI ELAKYVQTKQ QVQVANK // ID G2ZN18_9RALS Unreviewed; 346 AA. AC G2ZN18; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase protein {ECO:0000313|EMBL:CCA80437.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CCA80437.1}; GN Name=metHa {ECO:0000313|EMBL:CCA80437.1}; GN ORFNames=BDB_100117 {ECO:0000313|EMBL:CCA80437.1}; OS blood disease bacterium R229. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=741978 {ECO:0000313|EMBL:CCA80437.1}; RN [1] {ECO:0000313|EMBL:CCA80437.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=R229 {ECO:0000313|EMBL:CCA80437.1}; 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] {ECO:0000313|EMBL:CCA80437.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=R229 {ECO:0000313|EMBL:CCA80437.1}; 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; FR854066; CCA80437.1; -; Genomic_DNA. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:CCA80437.1}; KW Transferase {ECO:0000313|EMBL:CCA80437.1}. SQ SEQUENCE 346 AA; 37612 MW; 59D80E465AFD821F CRC64; MTAPLPYTRA ANLPALLRER ILILDGAMGT MIQRYKLTEA QYRGERFTDH PVDVKGNNEL LLLTRPEVIR EIHEQYLAAG ADLIETNTFG ATTVAQEDYK MADLAYEMNV VAARLAREAC DKYSTPDKPR FVAGAFGPTP KTASISPDVN DPGARNINFD QLRDAYYDQG KALLEGGADV FLVETIFDTL NAKAALFAID QLFEDTGERV PVMISGTVTD ASGRILSGQT VEAFWNSLRH ARPITFGLNC ALGAALMRPY IAELAKICDT AVSCYPNAGL PNPMSDTGFD ETPDVTSSLV DEFAAAGLVN LVGGCCGTTP EHIKAIAERV AQRKPRAWPG QYREAA // ID G3A3W8_9RALS Unreviewed; 346 AA. AC G3A3W8; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase protein {ECO:0000313|EMBL:CCA88581.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CCA88581.1}; GN Name=metHa {ECO:0000313|EMBL:CCA88581.1}; GN ORFNames=RALSY_30329 {ECO:0000313|EMBL:CCA88581.1}; OS Ralstonia syzygii R24. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=907261 {ECO:0000313|EMBL:CCA88581.1}; RN [1] {ECO:0000313|EMBL:CCA88581.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=R24 {ECO:0000313|EMBL:CCA88581.1}; 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] {ECO:0000313|EMBL:CCA88581.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=R24 {ECO:0000313|EMBL:CCA88581.1}; 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; CCA88581.1; -; Genomic_DNA. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:CCA88581.1}; KW Transferase {ECO:0000313|EMBL:CCA88581.1}. SQ SEQUENCE 346 AA; 37582 MW; 59D7AF535AF99CAF CRC64; MTAPLPYTRA ANLPALLRER ILILDGAMGT MIQRYKLTEA QYRGERFADH PVDVKGNNEL LLLTRPEVIR EIHEQYLAAG ADLIETNTFG ATTVAQEDYK MADLAYEMNV VAARLAREAC DKYSTPDKPR FVAGAFGPTP KTASISPDVN DPGARNINFD QLRDAYYDQG KALLEGGADV FLVETIFDTL NAKAALFAID QLFEDTGERV PVMISGTVTD ASGRILSGQT VEAFWNSLRH ARPITFGLNC ALGAALMRPY IAELAKICDT AVSCYPNAGL PNPMSDTGFD ETPDVTSSLV DEFAAAGLVN LVGGCCGTTP EHIKAIAERV AQRKPRAWPG QYREAA // ID G3ATF3_SPAPN Unreviewed; 274 AA. AC G3ATF3; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 07-JAN-2015, entry version 16. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EGW30916.1}; DE Flags: Fragment; GN ORFNames=SPAPADRAFT_62824 {ECO:0000313|EMBL:EGW30916.1}; OS Spathaspora passalidarum (strain NRRL Y-27907 / 11-Y1). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Spathaspora. OX NCBI_TaxID=619300 {ECO:0000313|Proteomes:UP000000709}; RN [1] {ECO:0000313|EMBL:EGW30916.1, ECO:0000313|Proteomes:UP000000709} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL Y-27907 / 11-Y1 {ECO:0000313|Proteomes:UP000000709}; 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; GL996504; EGW30916.1; -; Genomic_DNA. DR RefSeq; XP_007376949.1; XM_007376887.1. DR GeneID; 18874483; -. DR KEGG; spaa:SPAPADRAFT_62824; -. DR InParanoid; G3ATF3; -. DR KO; K00547; -. DR OMA; WESAINI; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000000709; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000709}; KW Reference proteome {ECO:0000313|Proteomes:UP000000709}. FT NON_TER 274 274 {ECO:0000313|EMBL:EGW30916.1}. SQ SEQUENCE 274 AA; 30816 MW; 044396C8A26AB3CF CRC64; MKDIREIIHS KRLVMDGALG TQLEPFIPKT PLWSGFAVLA KPEILAQVHR EYIISGADII ATATYQLSQN LLRQHTDLTD GQIEGIWESA INIALEAIDN RDVLVMGSIG PYSASLGSGA EYSNNIDVSN EFLQAYHIPL FQYFSDNAKV DLIGLETVST LQEFVVFHEF NHTKPYYISI ISNDGDNLPD GTSLSELVSY IDSHSDEWFI GLGINCTEYT LISKMVERIH LPVILNPNLG YIVEGDNARP KEKNDYEWIR GVTNWLQNDN VRIV // ID G3BB61_CANTC Unreviewed; 296 AA. AC G3BB61; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 07-JAN-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGV62147.1}; GN ORFNames=CANTEDRAFT_136088 {ECO:0000313|EMBL:EGV62147.1}; 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; Debaryomycetaceae; Yamadazyma; OC Yamadazyma/Candida clade. OX NCBI_TaxID=590646 {ECO:0000313|Proteomes:UP000000707}; RN [1] {ECO:0000313|EMBL:EGV62147.1, ECO:0000313|Proteomes:UP000000707} 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 {ECO:0000313|Proteomes:UP000000707}; 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; GL996527; EGV62147.1; -; Genomic_DNA. DR RefSeq; XP_006688317.1; XM_006688254.1. DR GeneID; 18249935; -. DR KEGG; cten:CANTEDRAFT_136088; -. DR KO; K00547; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000000707; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000707}; KW Methyltransferase {ECO:0000313|EMBL:EGV62147.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000707}; KW Transferase {ECO:0000313|EMBL:EGV62147.1}. SQ SEQUENCE 296 AA; 31739 MW; 39818122D7A8C536 CRC64; MYVLDGALGI ELDKLTPIRG TPLWAGHAVE ESPDIVRQVH SRYIQAGCDI VSTATYQMSY QALRQTDHDD AGTTAAWKAA VDVVVQARDG AGVDRKILIA GTIGPYGCFV NDGSEYTGNY TDSPTAEWLA AHHRPLVEFL EKNGDVDVIA FETVPSAVEL EAIVALDVQK PYWVSLCVNS SMDLVACAAV LRRCNSSLVA VGVNCVEYSK VSGYLEALSA VGVPLIAYPN YGYIYSQEDG YADLSDLGAW ETAVAEWMKF DMWAIGGCCG TGAEEVSVVR EAASRCQSAG FTPGIV // ID G3H309_CRIGR Unreviewed; 407 AA. AC G3H309; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 04-MAR-2015, entry version 21. DE SubName: Full=Betaine--homocysteine S-methyltransferase 1 {ECO:0000313|EMBL:EGW04217.1}; GN ORFNames=I79_004614 {ECO:0000313|EMBL:EGW04217.1}; OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Cricetidae; Cricetinae; Cricetulus. OX NCBI_TaxID=10029 {ECO:0000313|Proteomes:UP000001075}; RN [1] {ECO:0000313|Proteomes:UP000001075} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21804562; DOI=10.1038/nbt.1932; RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., RA Xie M., Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., RA Koh W., Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., RA Quake S.R., Famili I., Palsson B.O., Wang J.; RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell RT line."; RL Nat. Biotechnol. 29:735-741(2011). CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH000121; EGW04217.1; -; Genomic_DNA. DR RefSeq; XP_003498744.1; XM_003498696.1. DR RefSeq; XP_007634364.1; XM_007636174.1. DR GeneID; 100754488; -. DR KEGG; cge:100754488; -. DR CTD; 635; -. DR InParanoid; G3H309; -. DR KO; K00544; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000001075; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR000082; SEA_dom. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50024; SEA; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001075}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000313|EMBL:EGW04217.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001075}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000313|EMBL:EGW04217.1}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 217 217 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 407 AA; 45065 MW; 54F68725748230E0 CRC64; MAPVAGKKAK KGILERLNAG EVVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAVRQLH REFLRAGSNV MQTFTFYASE DKLENRGNYV AEKISGQKVN EAACDIARQV ADEGDALVAG GVSQTPSYLS CKSEMEVKKI FQQQLEVFMK KNVDFLIAEY FEHVEEAVWA VEALKTSGKP IAATMCIGPE GDLHGVSPGE CAVRLVKAGA SIVGVNCHFD PATSLQTVKL MKEGLEGARL KAYLMTQPLA YHTPDCSKQG FIDLPEFPFG LEPRVATRWD IQKYAREAYN LGVRYIGGCC GFEPYHIRAI AEELAPERGF LPPASEKHGS WGSGLDMHTK PWIRARARKE YWQNLRIASG RPYNPSMSKP DAWGVTKGTS ELMQQKEATT EQQLKELFEK QKFKSAQ // ID G3HWD4_CRIGR Unreviewed; 1253 AA. AC G3HWD4; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 01-APR-2015, entry version 25. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGW01906.1}; GN ORFNames=I79_015290 {ECO:0000313|EMBL:EGW01906.1}; OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Cricetidae; Cricetinae; Cricetulus. OX NCBI_TaxID=10029 {ECO:0000313|Proteomes:UP000001075}; RN [1] {ECO:0000313|Proteomes:UP000001075} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21804562; DOI=10.1038/nbt.1932; RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., RA Xie M., Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., RA Koh W., Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., RA Quake S.R., Famili I., Palsson B.O., Wang J.; RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell RT line."; RL Nat. Biotechnol. 29:735-741(2011). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; JH000829; EGW01906.1; -; Genomic_DNA. DR RefSeq; XP_007646365.1; XM_007648175.1. DR GeneID; 100763416; -. DR KEGG; cge:100763416; -. DR CTD; 4548; -. DR InParanoid; G3HWD4; -. DR KO; K00548; -. DR Proteomes; UP000001075; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001075}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001075}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 773 773 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1253 AA; 139229 MW; 641000535AB6C805 CRC64; MKKTLQDEIE AILRKRIMVL DGGMGTMIQQ YKLSEESFQG QEFKDHTRPL KGNNDILSIT QPDIICQIHK EYLLAGADII ETNTFSSTSI AQADYGLEHL AYRMNKCSAD VARRAAEEIT LQTGIKRFVA GALGPTNKTL SVSPSVERPD YRNITFDELV EAYQEQAKGL LDGGVDILLI ETIFDTANAK AALFALQKLF EEKYAPPRPI FISGTIVDKS GRTLSGQTGE AFVISVSHSD PLCIGLNCAL GAAEMRPFIE TIGKCTTAYV LCYPNAGLPN TFGDYDETPS MMANHLKDFA MDGLVNIVGG CCGSTPDHIR EIAEAVKNCK PRVPPASVFE GHMLLSGLEP FRIGPYTNFV NIGERCNVAG SKKFAKLIMA GNYDEALSIA KVQVEMGAQV LDINMDDGML DGPSAMTRFC NFIASEPDIA KVPLCIDSSN FAVVEAGLKC CQGKCIVNSI SLKEGAEDFL EKARKIKKFG AAVVVMAFDE EGQATETDVK ISVCTRAYHL LVEKLGFNPN DIIFDPNILT IGTGMEEHNL YAINFIHATR IIKETLPGVR ISGGLSNLSF SFRGMEAIRE AMHGVFLYHA IKFGMDMGIV NAGNLPVYDD IQKDLLQLCE DLIWNKDSEA TEKLLRYAQT HGKGGKKVIQ TDEWRNGSIE ERLEYALVKG IEKYVVEDTE EARLNQEKYP RPLNIIEGPL MNGMKVVGDL FGAGKMFLPQ VIKSARVMKK AVGHLIPFME KEREEARVLN GSVEEEDPYQ GTIVLATVKG DVHDIGKNIV GVVLGCNNFR VIDLGVMTPC DKILQAALDH KADIIGLSGL ITPSLDEMIF VAKEMERLAI KIPLLIGGAT TSRTHTAVKI APRYSAPVIH VLDASKSVVV CSQLLDENLK DDYIEEILEE YEDIRQDHYE SLKERKYLPL SQARKNGFHI DWLSEPHPVK PTFIGTQVFE DYNLQKLVDY IDWKPFFDVW QLRGKYPNRG FPKIFNDKTV GKEARKVYDD AQNMLNILIS QKKLQARGVV GFWPAQSVQD DIHLYAEDVV PQASEPIATF YGLRQQAEKD SSSTDPYHCL SDFIAPLHSG VRDYLGLFAV ACFGVEELSK AYEDDGDDYS SIMVKALGDR LAEAFAEELH ERVRRELWAY CSSELLGVTD LRKLRYEGIR PAPGYPSQPD HTEKLTMWRL ANIEQATGIR LTESLAMAPA SAVSGLYFSN VKSKYFAVGK VSKDQIEDYA LRKNMLVAEV ERWLGPILGY DTD // ID G3ITR9_9GAMM Unreviewed; 1226 AA. AC G3ITR9; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGW22590.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGW22590.1}; GN ORFNames=Mettu_1405 {ECO:0000313|EMBL:EGW22590.1}; OS Methylobacter tundripaludum SV96. OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales; OC Methylococcaceae; Methylobacter. OX NCBI_TaxID=697282 {ECO:0000313|EMBL:EGW22590.1}; RN [1] {ECO:0000313|EMBL:EGW22590.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SV96 {ECO:0000313|EMBL:EGW22590.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; JH109152; EGW22590.1; -; Genomic_DNA. DR RefSeq; WP_006890561.1; NZ_JH109152.1. DR EnsemblBacteria; EGW22590; EGW22590; Mettu_1405. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGW22590.1}; KW Transferase {ECO:0000313|EMBL:EGW22590.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 246 246 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1226 AA; 135972 MW; 3658BED60A9A6FB9 CRC64; MSKTELLKQQ LSQRILFLDG AMGTMIQSYK LEEKDYRGER FAQWEVDLKG NNDLLSLTQP DIIKAIHSAY FEVGSDIVET NTFNATSIAM ADYKMESLAY EMNVAAARVA REAADEYTQK TPEKPRFVAG VLGPTNRTAS MSPDVNDPGF RNIFFDDLVL AYTEATQGLI DGGADIILIE TVFDTLNAKA AIFAVEQYFE KIGYKLPVMI SGTITDASGR TLSGQTVAAF WNSLKHVEPI SFGFNCALGA TELRQYIAEL SSIADTHISA HPNAGLPNEF GEYDETPEAM AEELADWAKN GYLNIIGGCC GTSPANIKAI VEAVQQYSPR MVPEIPKQCR LSGLEPLNIG PDSLFVNVGE RTNVTGSAAF KRLVIEGDFE AALDVAEQQV ENGAQIIDIN MDEGMLESKE AMVRFLMLIA SEPDIAKVPI MLDSSKWEIL EAGLKCIQGK GVVNSISLKE GEAAFIEHAK LVRRYGAAVI VMAFDEEGQA DTKARKVEIC QRAYKILTEQ VGFPPEDIIF DPNIFAVATG IDEHNNYGLD FIEATQEIKR TLPYALISGG VSNVSFSFRG NNPVREAIHA VFLYHAIQAG MDMGIVNAGQ LAIYEDIPRD LRDAVEDVIL NRHDGSGTDK LLELADKYRG DGSSSAGKEQ DLEWRSWPVT KRLEHALVKG ITDYIDEDTE QARLEAERPL HVIEGALMDG MNVVGDLFGA GKMFLPQVVK SARVMKKAVA YLMPFMEADK AAGERQTNGK ILMATVKGDV HDIGKNIVGV VLQCNNYDVI DMGVMVPAEN ILQTARLENV DIIGLSGLIT PSLDEMVHVA KEMQRQGFTI PLMIGGATTS RAHTAVKIAP NYDGPIVYVT DASRGVGVAS NLLSADLKDE FVNSVREEYE EVRERHKGRE AKTKQHPLED ARRNKFNWGN YEPVKPSFLG IKVIDHFPLD TLVWYIDWSP FFQTWEMAGS YPKILDDKVI GVEARKLFQD AQDMLKKIIS EEWVTARAVV GFFPANSDGD DVVVYTDDTR SQKKETLHHL RQQNVKAPGR PNYCLSDFIA PVDSGKADYI GAFAVTTGIG IEQKLQEFEQ DNDDYSSIML KALADRLAEA FAEYMHQVVR KEYWGYAKDE AHEADQLINE AYQGIRPAPG YPACPDHTEK GKLFELLNVT EHTTIELTES YAMYPASAVS GWYFSHPESQ YFNVGKIDKD QLQDYAIRKG IAEEVAERWL AAHLHH // ID G3NRP8_GASAC Unreviewed; 401 AA. AC G3NRP8; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGACP00000008015}; OS Gasterosteus aculeatus (Three-spined stickleback). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae; OC Gasterosteus. OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000008015, ECO:0000313|Proteomes:UP000007635}; RN [1] {ECO:0000313|Ensembl:ENSGACP00000008015} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGACP00000008015} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSGACP00000008015}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSGACT00000008034; ENSGACP00000008015; ENSGACG00000006029. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; G3NRP8; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000007635; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007635}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Reference proteome {ECO:0000313|Proteomes:UP000007635}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 210 210 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 292 292 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 401 AA; 44334 MW; 74680B9C80E4DBA0 CRC64; MAPVKKGIIE RLNSGEVVIG DGGFVFALEK RGYVKAGPWT PEATVTHPEA VRQLHREFLR SGSNVMQTFT FYASDDKLEN RGQNLRITGA QINEAACDLA REVASEGDAM VAGGVCQTPS YLSCKSETDV KAIFKKQLDV FMKKNVDFLI AEYFEHVEEA VWAVEVLKTS GKPVAASMCI GPEGDMHGVS PGDCAVRLVK AGAQIVGVNC HFDPMTCVKA VKMMKEGVEK ARLKAHYMVQ PLAYHTPDCN CQGFIDLPEF PFALEPRILT RWDMHEYARE SYKAGIRFIG GCCGFEPYHI RAIAEELAPE RGIVAPASEK HGMWGAGLEM HTKPWVRARA RRDYWENIAP ASGRPKCPSM STPEGWGVTK GHADLLQHKE ATSSQEMKHV LEMQKKSKSS T // ID G3NRQ4_GASAC Unreviewed; 391 AA. AC G3NRQ4; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGACP00000008021}; OS Gasterosteus aculeatus (Three-spined stickleback). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae; OC Gasterosteus. OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000008021, ECO:0000313|Proteomes:UP000007635}; RN [1] {ECO:0000313|Ensembl:ENSGACP00000008021} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGACP00000008021} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSGACP00000008021}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSGACT00000008040; ENSGACP00000008021; ENSGACG00000006029. DR GeneTree; ENSGT00390000003122; -. DR OMA; RGQALKI; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000007635; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007635}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Reference proteome {ECO:0000313|Proteomes:UP000007635}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 210 210 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 292 292 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 391 AA; 43309 MW; 99BAC514A1484B16 CRC64; MAPVKKGIIE RLNSGEVVIG DGGFVFALEK RGYVKAGPWT PEATVTHPEA VRQLHREFLR SGSNVMQTFT FYASDDKLEN RGQNLRITGA QINEAACDLA REVASEGDAM VAGGVCQTPS YLSCKSETDV KAIFKKQLDV FMKKNVDFLI AEYFEHVEEA VWAVEVLKTS GKPVAASMCI GPEGDMHGVS PGDCAVRLVK AGAQIVGVNC HFDPMTCVKA VKMMKEGVEK ARLKAHYMVQ PLAYHTPDCN CQGFIDLPEF PFALEPRILT RWDMHEYARE SYKAGIRFIG GCCGFEPYHI RAIAEELAPE RGIVAPASEK HGMWGAGLEM HTKPWVRARA RRDYWENLKP ASGRPLCPSM SAPDSWGVTK GHKDLVQQKE ATSQDQLKQL F // ID G3NRU1_GASAC Unreviewed; 397 AA. AC G3NRU1; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGACP00000008058}; OS Gasterosteus aculeatus (Three-spined stickleback). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae; OC Gasterosteus. OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000008058, ECO:0000313|Proteomes:UP000007635}; RN [1] {ECO:0000313|Ensembl:ENSGACP00000008058} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGACP00000008058} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSGACP00000008058}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSGACT00000008077; ENSGACP00000008058; ENSGACG00000006029. DR GeneTree; ENSGT00390000003122; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000007635; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007635}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Reference proteome {ECO:0000313|Proteomes:UP000007635}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 210 210 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 292 292 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 397 AA; 43716 MW; 4C697DD1BD9A7BA4 CRC64; MAPSKKGILE RLDAGEVVIG DGGFVFALEK RGYVKAGPWT PEAAAEHPEA VRQLHREFLR AGANVMQTFT FYASDDKLEN RGNKLTFTGA QINEAACDLA REVANEGDAL VAGGVCQTPS YLSCKSETEV KAILKKQLDV FTKKNVDFLI AEYFEHVEEA VWAVEVLKET GKPVAASMCI GPEGDMHGVS PAECAVRLVK AGAQIVGVNC HFDPMTCVKA VKMMKEGVEK AGLKAHYMVQ PLAYHTPDCN CQGFIDLPEF PFGLEPRILS RWDMHKYARE AFNAGIHFIG GCCGFEPYHI RAVAEELAVE RGVLPAASEK HGNWGAGLEM HTKPWVRARA RRDYWENLKP ASGRPLCPSM SAPDSWGVTK GHKDLVQQKE ATSQDQLKQL FDRSKSH // ID G3P6A1_GASAC Unreviewed; 370 AA. AC G3P6A1; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGACP00000013124}; DE Flags: Fragment; OS Gasterosteus aculeatus (Three-spined stickleback). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae; OC Gasterosteus. OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000013124, ECO:0000313|Proteomes:UP000007635}; RN [1] {ECO:0000313|Ensembl:ENSGACP00000013124} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGACP00000013124} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSGACP00000013124}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSGACT00000013149; ENSGACP00000013124; ENSGACG00000009937. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; G3P6A1; -. DR OMA; VGINCHL; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR Proteomes; UP000007635; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007635}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000007635}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 214 214 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 296 296 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 297 297 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSGACP00000013124}. SQ SEQUENCE 370 AA; 40729 MW; 600A925526208549 CRC64; IVPCNICKGI LERLNAGEVV VGDGGYVMQL ERRGYVKAGH WTPEAAVEHP EAVRQLHREF LRAGANVIQT FTFYCSEDKL EISGNVPNIT GAQINEAACD LAREVANEGE ALVAGCVSKT PCYVDTHNET EVKAIFKKQM DDFLKKEIDF FIAEFFEHVE EAAWAVEVLK TGGKPVGATL CISPEGDMHG VPPGECAVRL VRAGVGADIV GINCHLDPLT CVRTVKLMKA GLEKAGLKAH LMIQPLGFHT PECNHSGYLT LPEFPFALET RAMTRWDVHQ YAREAYNAGI RYIGGCCGFE AYHIRAIAEE LAAERGFLPP ASEKHGLWGA ALEMHTKPWV RARSRREYWE KLLPASGRPK CPSMATPADE // ID G3PKG5_GASAC Unreviewed; 323 AA. AC G3PKG5; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGACP00000018095}; OS Gasterosteus aculeatus (Three-spined stickleback). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae; OC Gasterosteus. OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000018095, ECO:0000313|Proteomes:UP000007635}; RN [1] {ECO:0000313|Ensembl:ENSGACP00000018095} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGACP00000018095} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSGACP00000018095}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSGACT00000018130; ENSGACP00000018095; ENSGACG00000013681. DR GeneTree; ENSGT00510000049619; -. DR InParanoid; G3PKG5; -. DR OMA; SYIGKWR; -. DR OrthoDB; EOG7GQXW0; -. DR TreeFam; TF313927; -. DR Proteomes; UP000007635; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007635}; KW Reference proteome {ECO:0000313|Proteomes:UP000007635}. SQ SEQUENCE 323 AA; 34423 MW; 2A9838351A94C7CE CRC64; MGSSARLRLY MEDNGPLILD GGLASELEAQ GAKLQGDPLW SSRLLHTDPQ AIREAHYRFL LGGADVISTA TYQASIPGFV KHLDVTPEGA RELLMSGVRL ARDTVDRFVS DARPSVAASV GPYGAVLLDG SEYTGAYAER MSVEDLKAWH RPQIDALAAA GADLVALETV PSIKEAAALL ELLREFPDTR AWLSFSCKDG RRISDGSAFA DAVRLAASST AQLVAVGVNC CSPELVEPLL DSAGSLLGPD LSWVVYPNSG GDWDTEKGWV TSEEQSASIL KLSPTWRKQG ADLIGGCCCI TPAHIAELRR RLKGSDSSPG TKI // ID G3PRI7_GASAC Unreviewed; 1266 AA. AC G3PRI7; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGACP00000020223}; DE Flags: Fragment; GN Name=MTR {ECO:0000313|Ensembl:ENSGACP00000020223}; OS Gasterosteus aculeatus (Three-spined stickleback). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae; OC Gasterosteus. OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000020223, ECO:0000313|Proteomes:UP000007635}; RN [1] {ECO:0000313|Ensembl:ENSGACP00000020223} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGACP00000020223} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 1}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSGACP00000020223}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSGACT00000020262; ENSGACP00000020223; ENSGACG00000015329. DR GeneTree; ENSGT00420000029824; -. DR InParanoid; G3PRI7; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG7TF786; -. DR TreeFam; TF312829; -. DR Proteomes; UP000007635; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007635}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007635}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 258 258 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 783 783 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSGACP00000020223}. SQ SEQUENCE 1266 AA; 139938 MW; CFE213FC4A12D8C4 CRC64; LINVISLSVP GCRCPLESEL RAVLQQRIMV LDGGMGTMIQ QHKLEEEDFR SEEFKDHPLP LKGNNDLLSL TQPNIIYNIH KDYLLAGADV IETNTFSSTS VAQADYGLEH MAYRLNRASA ELARRAADEV TRQTGCKRYV AGAVGPTNKT LSVSPSVERP DFRNITFDEL VESYSEQVRG LLDGGADILL VETIFDTANA KAALFAIDLL FQKSYERKPI FISGTIVDRS GRTLSGQTGE AFVVSVSHMN PLCIGLNCAL GAIEMRPFIE AIGKSTTAFI ICYPNAGLPN TFGGYDETPE VTASNLKEFA TDGLVNIVGG CCGTTPGHIR AIAEGVKHCQ PRVPAADIYQ DYMLLSGLEP FRIGPYTNFV NIGERCNVAG SRKFAKLIMA GNYEEALSIA KAQVEMGAQV LDINMDEGML EGPSAMARFC NLIASEPDIA RVPLCIDSSN FSVIEAGLKC CQGKCIVNSI SLKEGEEEFL HRAATVKRYG AAVVVMAFDE EGQAADTDRK VEICTRAYQL LVNKVGFDPN DIIFDPNILT IGTGMEEHND YAIYFIRATK VIKEKLPKAR VSGGLSNLSF SFRGMEAIRE AMHGAFLYHA IKDGMDMGIV NAGNLPVYDD IDKELLSLCE NLIWNKDAEA TEKLLAYAQN HVKGAKKVVQ TDEWREGDVE ERLEYALIKG IDKYVVEDVE ECKAQVERYT RPLHIIEGPL MNGMKVVGDL FGAGKMFLPQ VIKSARVMKK AVGYLIPFME KEREEMMALS GSTEEMDPYQ GTIVLATVKG DVHDIGKNIV GVVLGCNNFR VIDLGVMVPC DRILREAITH KADIIGLSGL ITPSLDEMIY VAKEMERLGM TTPLLIGGAT TSKMHTAVKI APRYTSPAIH VLDASRSVVV CSQLLDEAMR DEYFEDLKEE YEEIRQEHYD SLKDRRYLSL SQARAKALHI DWLSPPPPVR PQFLGTRVFE CYDLHSLLAF IDWKPFFDVW QLRGKYPNRG YPKIFKDKTV GAEARRVFDE AQQMLNQMID SGSLTGRGLV GFWRAQSDGD DVRVYEGDAA VHPDTEPIAT FHGLRQQQAE KDSSSSEPYL CVSDFVAPAD SGVTDYVGVF AVGVFGAEEL SQQFLAKGDD YSSIMVKALA DRLAEAFAEE LHARVRKELW GYSTDEALQA SDLHRIRYQG IRPAAGYPSQ PDHTEKSTMW SLAGIQEKTV GIYLTESLAM MPAASVSGLY FSHPQASYFA VGKITKEQVE DYAARKGLGV EEAERWLAPI LGYDSE // ID G3PT87_GASAC Unreviewed; 399 AA. AC G3PT87; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGACP00000020823}; OS Gasterosteus aculeatus (Three-spined stickleback). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae; OC Gasterosteus. OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000020823, ECO:0000313|Proteomes:UP000007635}; RN [1] {ECO:0000313|Ensembl:ENSGACP00000020823} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGACP00000020823} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSGACP00000020823}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSGACT00000020863; ENSGACP00000020823; ENSGACG00000015778. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; G3PT87; -. DR OMA; KAHYMSQ; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000007635; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007635}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Reference proteome {ECO:0000313|Proteomes:UP000007635}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 211 211 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 399 AA; 43682 MW; A48DEA1D32C2FD33 CRC64; MAPGAGKGIL ARLDAGEVVI GDGGFVFALE KRGYVKAGPW TPEAAAEHPE AVRQLHREFL RAGSDVMQTF TFYASDDKLE NRGHTQRFTG QQINEAACDL AREVADEGGA LVAGGVSQTP AYLSCKSEDD VKAIFKKQID VFVQKNVDFL IAEYFEHVEE AEWAVQVLKS TGKPVAATLC IGPEGDLNGV RPGDCAVRLV KAGAHVVGVN CHFDPETCVK TVKMMKEAVE KAGLKAHYMS QPLAYHTPDC NCQGFIDLPE FPFGLEPRVL TRWDMQKYAR EAYKAGIRYI GGCCGFEAYH VRALAEELAP ERGGLPAGSE KHGTWGAGLE MHTKPWVRAR ARRDYWENLK PASGRPLCPS MATPDAWGVT KGHADLMQQK EATSQDQLKA LFDKANKNQ // ID G3QL14_GORGO Unreviewed; 363 AA. AC G3QL14; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGGOP00000003155}; GN Name=BHMT2 {ECO:0000313|Ensembl:ENSGGOP00000003155}; OS Gorilla gorilla gorilla (Western lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000003155, ECO:0000313|Proteomes:UP000001519}; RN [1] {ECO:0000313|Ensembl:ENSGGOP00000003155, ECO:0000313|Proteomes:UP000001519} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Scally A.; RT "Insights into the evolution of the great apes provided by the gorilla RT genome."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGGOP00000003155} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSGGOP00000003155}. 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_004058700.1; XM_004058652.1. DR Ensembl; ENSGGOT00000003227; ENSGGOP00000003155; ENSGGOG00000003210. DR GeneID; 101139189; -. DR KEGG; ggo:101139189; -. DR CTD; 23743; -. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; G3QL14; -. DR OMA; PEGDMHD; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000001519; Chromosome 17. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0061627; F:S-methylmethionine-homocysteine S-methyltransferase activity; IEA:Ensembl. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl. DR GO; GO:0046500; P:S-adenosylmethionine metabolic process; IEA:Ensembl. DR GO; GO:0033477; P:S-methylmethionine metabolic process; IEA:Ensembl. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001519}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Reference proteome {ECO:0000313|Proteomes:UP000001519}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 208 208 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 363 AA; 40366 MW; 0FC2FFE3DB61193D CRC64; MAPAGRPGAK KGILERLESG EVVIGDGSFL ITLEKRGYVK AGLWTPEAVI EHPDAVRQLH MEFLRAGSNV MQTFTFSASE DNMESKWEDV NAAACDLARE VAGKGDALVA GGICQTSIYK YHKDEARIKK LFRQQLEVFA WKNVDFLIAE YFEHVEEAVW AVEVLKESDR PVAVTMCIGP EGDMHDITPG ECAVRLVKAG ASIVGVNCRF GPDTSLKTME LMKEGLEWAG LKAHLMVQPL GFHTPDCGKE GFVDLPEYPF GLESRVATRW DIQKYAREAY SLGVRYIGGC CGFEPYHIRA IAEELAPERG FLPPASEKHG SWGSGLDMHT KPWIRARARR EYWENLLPAS GRPFCPSLSK PDF // ID G3QX64_GORGO Unreviewed; 406 AA. AC G3QX64; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGGOP00000007397}; GN Name=BHMT {ECO:0000313|Ensembl:ENSGGOP00000007397}; OS Gorilla gorilla gorilla (Western lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000007397, ECO:0000313|Proteomes:UP000001519}; RN [1] {ECO:0000313|Ensembl:ENSGGOP00000007397, ECO:0000313|Proteomes:UP000001519} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Scally A.; RT "Insights into the evolution of the great apes provided by the gorilla RT genome."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGGOP00000007397} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSGGOP00000007397}. 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_004058699.1; XM_004058651.1. DR Ensembl; ENSGGOT00000007593; ENSGGOP00000007397; ENSGGOG00000007558. DR GeneID; 101138811; -. DR KEGG; ggo:101138811; -. DR CTD; 635; -. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; G3QX64; -. DR KO; K00544; -. DR OMA; WGVTKGT; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000001519; Chromosome 17. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006577; P:amino-acid betaine metabolic process; IEA:Ensembl. DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001519}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Reference proteome {ECO:0000313|Proteomes:UP000001519}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 217 217 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 406 AA; 44984 MW; 9C6C180023428FDA CRC64; MPPVGGKKAK KGILERLNAG EIVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAVRQLH REFLRAGSNV MQTFTFYASE DKLENRGNYV LEKISGQKVN EAACDVARQV ADEGDALVAG GVSQTPSYLS CKSETEVKKV FLQQLEVFMK KNVDFLIAEY FEHVEEAVWA VETLIASGKP VAATMCIGPE GDLHGVPPGE CAVRLVKAGA SIIGVNCHFD PTISLKTVKL MKEGLEAARL KAHLMSQPLA YHTPDCNKQG FIDLPEFPFG LEPRVATRWD IQKYAREAYN LGVRYIGGCC GFEPYHIRAI AEELAPERGF LPPASEKHGS WGSGLDMHTK PWVRARARKE YWENLRIASG RPYNPSMSKP DGWGVTKGTA ELMQQKEATT EQQLKELFEK QKFKSQ // ID G3RJ67_GORGO Unreviewed; 1265 AA. AC G3RJ67; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 01-APR-2015, entry version 25. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGGOP00000015745}; DE Flags: Fragment; GN Name=MTR {ECO:0000313|Ensembl:ENSGGOP00000015745}; OS Gorilla gorilla gorilla (Western lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000015745, ECO:0000313|Proteomes:UP000001519}; RN [1] {ECO:0000313|Ensembl:ENSGGOP00000015745, ECO:0000313|Proteomes:UP000001519} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Scally A.; RT "Insights into the evolution of the great apes provided by the gorilla RT genome."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGGOP00000015745} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 1}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSGGOP00000015745}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSGGOT00000016196; ENSGGOP00000015745; ENSGGOG00000016123. DR GeneTree; ENSGT00420000029824; -. DR InParanoid; G3RJ67; -. DR Proteomes; UP000001519; Chromosome 1. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001519}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001519}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 260 260 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 785 785 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSGGOP00000015745}. SQ SEQUENCE 1265 AA; 140693 MW; 8AA534D23494B1A6 CRC64; LSPTFSPHFP RKGLKKTLRD EIDAILQKRI MVLDGGMGTM IQREKLNEEH FRGQEFKDHA RPLKGNNDIL SITQPDVIYQ IHKEYLLAGA DIIETNTFSS TSIAQADYGL EHLAYRMNMC SAGVARKAAE EVTLQTGIKR FVAGALGPTN KTLSVSPSVE RPDYRNITFD ELVEAYQEQA KGLLDGGVDI LLIETIFDTA NAKAALFALQ NLFEEKYAPR PIFISGTIVD KSGRTLSGQT GEGFVISVSH GEPLCIGLNC ALGAAEMRPF IEIIGKCTTA YVLCYPNAGL PNTFGDYDET PSMMAKHLKD FAMDGLVNIV GGCCGSTPDH IREIAEAVKN CKPRVPPATA FEGHMLLSGL EPFRIGPYTN FVNIGERCNV AGSRKFAKLI MAGNYEEALC VAKVQVEMGA QVLDINMDDG MLDGPSAMTR FCNLIASEPD IAKVPLCIDS SNFAVIEAGL KCCQGKCIVN SISLKEGEDD FLEKARKIKK YGAAMVVMAF DEEGQATETD TKVRVCTRAY HLLVKKLGFN PNDIIFDPNI LTIGTGMEEH NLYAINFIHA TKVIKETLPG ARISGGLSNL SFSFRGMEAI REAMHGVFLY HAIKSGMDMG IVNAGNLPVY DDIHKELLQL CEDLIWNKDP EATEKLLRYA QTQGTGGKKV IQTDEWRNGP VEERLEYALV KGIEKHIIED TEEARLNQKK YPRPLNIIEG PLMNGMKIVG DLFGAGKMFL PQVIKSARVM KKAVGHLIPF MEKEREETRV LNGTVEEEDP YQGTIVLATV KGDVHDIGKN IVGVVLGCNN FRVIDLGVMT PCDKILKAAL DHKADIIGLS GLITPSLDEM IFVAKEMERL AIRIPLLIGG ATTSKTHTAV KIAPRYSAPV IHVLDASKSV VVCSQLLDEN LKDEYFEEIM EEYEDIRQDH YESLKERRYL PLSQARKSGF QMDWLSEPHP VKPTFIGTQV FEDYDLQKLV DYIDWKPFFD VWQLRGKYPN RGFPKIFNDK TVGGEARKVY DDAHNMLNTL ISRKKLRARG VVGFWPAQSI QDDIHLYAEA AVPQAAEPIA TFYGLRQQAE KDSASTEPYY CLSDFIAPLH SGIRDYLGLF AVACFGVEEL SKTYEDDGDD YSSIMVKALG DRLAEAFAEE LHERVRRELW AYCGSEQLDV ADLRRLRYKG IRPAPGYPSQ PDHTEKLTMW RLADIEHSTG IRLTESLAMA PASAVSGLYF SNLKSKYFAV GKISKDQVED YALRKNISVA EVEKWLGPIL GYDTD // ID G3RTZ4_GORGO Unreviewed; 1265 AA. AC G3RTZ4; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 31. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGGOP00000019271}; GN Name=MTR {ECO:0000313|Ensembl:ENSGGOP00000019271}; OS Gorilla gorilla gorilla (Western lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000019271, ECO:0000313|Proteomes:UP000001519}; RN [1] {ECO:0000313|Ensembl:ENSGGOP00000019271, ECO:0000313|Proteomes:UP000001519} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Scally A.; RT "Insights into the evolution of the great apes provided by the gorilla RT genome."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGGOP00000019271} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 1}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSGGOP00000019271}. 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_004028696.1; XM_004028647.1. DR Ensembl; ENSGGOT00000025525; ENSGGOP00000019271; ENSGGOG00000016123. DR GeneID; 101148736; -. DR KEGG; ggo:101148736; -. DR CTD; 4548; -. DR GeneTree; ENSGT00420000029824; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG7TF786; -. DR TreeFam; TF312829; -. DR Proteomes; UP000001519; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:Ensembl. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001519}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001519}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 260 260 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 785 785 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1265 AA; 140595 MW; C1D868A8683BB2DF CRC64; MSPALQDLSQ PEGLKKTLRD EIDAILQKRI MVLDGGMGTM IQREKLNEEH FRGQEFKDHA RPLKGNNDIL SITQPDVIYQ IHKEYLLAGA DIIETNTFSS TSIAQADYGL EHLAYRMNMC SAGVARKAAE EVTLQTGIKR FVAGALGPTN KTLSVSPSVE RPDYRNITFD ELVEAYQEQA KGLLDGGVDI LLIETIFDTA NAKAALFALQ NLFEEKYAPR PIFISGTIVD KSGRTLSGQT GEGFVISVSH GEPLCIGLNC ALGAAEMRPF IEIIGKCTTA YVLCYPNAGL PNTFGDYDET PSMMAKHLKD FAMDGLVNIV GGCCGSTPDH IREIAEAVKN CKPRVPPATA FEGHMLLSGL EPFRIGPYTN FVNIGERCNV AGSRKFAKLI MAGNYEEALC VAKVQVEMGA QVLDINMDDG MLDGPSAMTR FCNLIASEPD IAKVPLCIDS SNFAVIEAGL KCCQGKCIVN SISLKEGEDD FLEKARKIKK YGAAMVVMAF DEEGQATETD TKVRVCTRAY HLLVKKLGFN PNDIIFDPNI LTIGTGMEEH NLYAINFIHA TKVIKETLPG ARISGGLSNL SFSFRGMEAI REAMHGVFLY HAIKSGMDMG IVNAGNLPVY DDIHKELLQL CEDLIWNKDP EATEKLLRYA QTQGTGGKKV IQTDEWRNGP VEERLEYALV KGIEKHIIED TEEARLNQKK YPRPLNIIEG PLMNGMKIVG DLFGAGKMFL PQVIKSARVM KKAVGHLIPF MEKEREETRV LNGTVEEEDP YQGTIVLATV KGDVHDIGKN IVGVVLGCNN FRVIDLGVMT PCDKILKAAL DHKADIIGLS GLITPSLDEM IFVAKEMERL AIRIPLLIGG ATTSKTHTAV KIAPRYSAPV IHVLDASKSV VVCSQLLDEN LKDEYFEEIM EEYEDIRQDH YESLKERRYL PLSQARKSGF QMDWLSEPHP VKPTFIGTQV FEDYDLQKLV DYIDWKPFFD VWQLRGKYPN RGFPKIFNDK TVGGEARKVY DDAHNMLNTL ISRKKLRARG VVGFWPAQSI QDDIHLYAEA AVPQAAEPIA TFYGLRQQAE KDSASTEPYY CLSDFIAPLH SGIRDYLGLF AVACFGVEEL SKTYEDDGDD YSSIMVKALG DRLAEAFAEE LHERVRRELW AYCGSEQLDV ADLRRLRYKG IRPAPGYPSQ PDHTEKLTMW RLADIEHSTG IRLTESLAMA PASAVSGLYF SNLKSKYFAV GKISKDQVED YALRKNISVA EVEKWLGPIL GYDTD // ID G3SYC9_LOXAF Unreviewed; 1251 AA. AC G3SYC9; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSLAFP00000005484}; DE Flags: Fragment; GN Name=MTR {ECO:0000313|Ensembl:ENSLAFP00000005484}; OS Loxodonta africana (African elephant). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta. OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000005484}; RN [1] {ECO:0000313|Ensembl:ENSLAFP00000005484} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000005484}; RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., RA Lindblad-Toh K.; RT "The Genome Sequence of Loxodonta africana (African elephant)."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSLAFP00000005484} RP IDENTIFICATION. RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000005484}; RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 1}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSLAFP00000005484}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSLAFT00000006536; ENSLAFP00000005484; ENSLAFG00000006529. DR GeneTree; ENSGT00420000029824; -. DR InParanoid; G3SYC9; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG7TF786; -. DR TreeFam; TF312829; -. DR Proteomes; UP000007646; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:Ensembl. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007646}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007646}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 246 246 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 771 771 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSLAFP00000005484}. SQ SEQUENCE 1251 AA; 139340 MW; 1D5D07B98B2ED962 CRC64; VKKTLQDEIE AILQERIMVL DGGMGTMIQR YKLNEEYFRG QEFKDHARPL KGNNDILSIT QPDIIYQIHK EYLLAGADII ETNTFSSTSV AQADYGLEDL AYRMNKSSAA LAKKAAEEVT FQTGIKRFVA GALGPTNKTL SVSPSVERPD YRNIRFDELV EAYQEQAKGL LDGGVDILLI ETIFDTANAK AALFALQKLF EEKYAPRPIF ISGTIVDKSG RTLSGQTGEF VISVSHADPL CIGLNCALGA TEMRPFIETI GKCTTAYVLC YPNAGLPNTF GDYDETPQMM AVHLKDFAVD GLVNIVGGCC GTTPDHIREI AEGVKNCKPR VPPATVFEGH MLLSGLEPFR IGPYTNFVNI GERCNVAGSR KFAKLIMAGN YDEGLSVAKE QVEMGAQVLD INMDDGMLDG PSAMTRFCNF IASEPDIAKV PLCIDSSNFA VIEAGLKCCQ GKCIVNSISL KEGEDDFLEK ARKIKKFGAA VVVMAFDEEG QATETDTKIR VCTRAYHLLV KKLGFNPYDI IFDPNILTIG TGMEEHNLYA VNFIQATKVI KETLPGAKIS GGLSNLSFSF RGMEAIREAM HGVFLYHAIK CGMDMGIVNA GNLPLYDDIH KELLQLCEDL IWNRDPEATE KLLRYAQTHG TQGKKVIQTD EWRSGPIEER LEYALVKGIE KHIVEDTEEA RLNQDKYPRP LNIIEGPLMN GMKVVGDLFG AGKMFLPQVI KSARVMKKAV GHLIPFMEKE REETRELTGA VEEEDPYHGT IVLATVKGDV HDIGKNIVGV VLGCNNFRVI DLGVMTPCDK ILKAALDNKA DIIGLSGLIT PSLDEMIFVA KEMERLAIKI PLLIGGATTS RTHTAVKIAP RYSAPVIHVL DASKSVVVCS QLLDENLKDE YFEEIMEEYE DIRQDHYESL KERRYLPLSQ ARKNGLHIDW LSEPHPVKPT FMGTRVFEDY DLWKLVDYID WKPFFDVWQL RGKYPNRGFP KIFNDKTVGE EARKVYGDAQ NMLKALISQK KLQARGMVGF WPAQSVQDDI HVYAEDAVPQ AAEPMATFYG LRQQAEKDSA STDPYHCLSD FIAPLDSGVR DYLGLFAVAC FGVEELSRAY EEECDDYSSI MVKALGDRLA EAFAEELHER VRKELWAYCG SEQLDMVGLR RLRYEGIRPA PGYPSQPDHT EKLTMWTLAN IEPSTGIRLT ESLAMAPASA VSGLYFSNLK SKYFAVGKIS KDQVEDYALR KNMSVAEIEK WLGPILGYDT D // ID G3TK29_LOXAF Unreviewed; 363 AA. AC G3TK29; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSLAFP00000015143}; DE Flags: Fragment; GN Name=BHMT2 {ECO:0000313|Ensembl:ENSLAFP00000015143}; OS Loxodonta africana (African elephant). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta. OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000015143, ECO:0000313|Proteomes:UP000007646}; RN [1] {ECO:0000313|Ensembl:ENSLAFP00000015143} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000015143}; RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., RA Lindblad-Toh K.; RT "The Genome Sequence of Loxodonta africana (African elephant)."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSLAFP00000015143} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSLAFP00000015143}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSLAFT00000018070; ENSLAFP00000015143; ENSLAFG00000018070. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; G3TK29; -. DR OMA; PEGDMHD; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR Proteomes; UP000007646; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0061627; F:S-methylmethionine-homocysteine S-methyltransferase activity; IEA:Ensembl. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl. DR GO; GO:0046500; P:S-adenosylmethionine metabolic process; IEA:Ensembl. DR GO; GO:0033477; P:S-methylmethionine metabolic process; IEA:Ensembl. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007646}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000007646}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 208 208 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSLAFP00000015143}. SQ SEQUENCE 363 AA; 40122 MW; E1799996F2CDEDE7 CRC64; QVPGLTKRFS QGILERLESG EVVIGDGSFL ITLEKRGYVK AGRWTPEAVV EHPNAVRQLH MEFLRAGSNV MQTFTFSASE DNMESKWEDI NAAACDLARE VAGKGDALVA GGICQTSVYQ HHKDEARIKK IFRLQLEVFA RKNVDFVIAE YFEHAEEAVW AVEVLKEAGK PVAATMCIGP EGDMHDVTPG ECAVKLVMAG ASIVGVNCRF GPRISLKTMK LMKEGLQAAG LKAHLMVQSL GFHTPDCGKG GFVDLPEYPF GLEPRVATRW DIQKYAREAY DLGVRYIGGC CGFEPYHIRA IAEELAPERG FLPPASEKHG NWGCGLDMHT KPWIRARARR EHWENLLPAS GRPFCPSLSK PDA // ID G3TK32_LOXAF Unreviewed; 407 AA. AC G3TK32; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSLAFP00000015148}; GN Name=BHMT {ECO:0000313|Ensembl:ENSLAFP00000015148}; OS Loxodonta africana (African elephant). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta. OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000015148}; RN [1] {ECO:0000313|Ensembl:ENSLAFP00000015148} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000015148}; RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., RA Lindblad-Toh K.; RT "The Genome Sequence of Loxodonta africana (African elephant)."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSLAFP00000015148} RP IDENTIFICATION. RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000015148}; RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSLAFP00000015148}. 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_003408021.1; XM_003407973.2. DR Ensembl; ENSLAFT00000018074; ENSLAFP00000015148; ENSLAFG00000018074. DR GeneID; 100672133; -. DR CTD; 635; -. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; G3TK32; -. DR OMA; WGVTKGT; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000007646; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006577; P:amino-acid betaine metabolic process; IEA:Ensembl. DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007646}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Reference proteome {ECO:0000313|Proteomes:UP000007646}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 217 217 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 407 AA; 44966 MW; 358716307B1205E2 CRC64; MAPVGGKRAK KGILERLNAG EVVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAVRQLH REFLRAGSNV MQTFTFYASE DKLENWGNYV AEKISGQKVN EAACDIARQV ADEGDALVAG GVSQTPSYLS CKSETEVKKI FQQQLEVFMK KNVDFLIAEY FEHVEEAVWA VEALKVSGKP VAATMCIGPD GDLHGVAPGE CAVRLVKAGA SIIGVNCHFD PTTSLKTVKL MKEGLEAAKL KAYLMAQPLA YHTPDCGKQG FIDLPEFPFG LEPRVTTRWD IQKYAREAYN LGVRYIGGCC GFEPYHIRAI AEELAPERGF LPPASEKHGS WGSGLDMHTK PWIRARARRE YWENLRIASG RPYNPSMSKP DAWGVTKGTA ELMQQKEATT DQQLKELIEK QKFKSAP // ID G3UP40_MELGA Unreviewed; 1250 AA. AC G3UP40; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 01-APR-2015, entry version 24. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMGAP00000017328}; DE Flags: Fragment; GN Name=MTR {ECO:0000313|Ensembl:ENSMGAP00000017328}; OS Meleagris gallopavo (Common turkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; OC Phasianidae; Meleagridinae; Meleagris. OX NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000017328, ECO:0000313|Proteomes:UP000001645}; RN [1] {ECO:0000313|Ensembl:ENSMGAP00000017328, ECO:0000313|Proteomes:UP000001645} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20838655; RA Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A., RA Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K., RA Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C., RA Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A., RA Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., RA de Jong P., Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., RA Lee M.K., Lee T., Mane S., Marcais G., Marz M., McElroy A.P., RA Modise T., Nefedov M., Notredame C., Paton I.R., Payne W.S., RA Pertea G., Prickett D., Puiu D., Qioa D., Raineri E., Ruffier M., RA Salzberg S.L., Schatz M.C., Scheuring C., Schmidt C.J., Schroeder S., RA Searle S.M., Smith E.J., Smith J., Sonstegard T.S., Stadler P.F., RA Tafer H., Tu Z.J., Van Tassell C.P., Vilella A.J., Williams K.P., RA Yorke J.A., Zhang L., Zhang H.B., Zhang X., Zhang Y., Reed K.M.; RT "Multi-platform next-generation sequencing of the domestic turkey RT (Meleagris gallopavo): genome assembly and analysis."; RL PLoS Biol. 8:E1000475-E1000475(2010). RN [2] {ECO:0000313|Ensembl:ENSMGAP00000017328} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 1}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSMGAP00000017328}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSMGAT00000019781; ENSMGAP00000017328; ENSMGAG00000011700. DR GeneTree; ENSGT00420000029824; -. DR Proteomes; UP000001645; Chromosome 2. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001645}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001645}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 249 249 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 777 777 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSMGAP00000017328}. SQ SEQUENCE 1250 AA; 139210 MW; 516C596DBCCF7753 CRC64; ANNRESVEDE IESVLRERIM ILDGGMGTMI QQYALSEEDF RGHEFKDHSK PLKGNNDLLS ITQPDIICDI HKEYLLAGAD IIETNTFSST RVAQADYALE HLAYRLNRIS AQVARKAADD VTAQTGIKRY VAGSMGPTNR TLSVSPSVER PDYRNITFDE LVEAYTEQAK GLLDGGVDVM LVETIFDTAN AKAALFALHK LFEEEYAPRP IFVSGTIVDK SGRTLSGQTG EAFVISVSHS KPLCIGLNCA LGAVEMRPFI ETIGKCTTAY VICYPNAGLP NTFGGYDETP EVTAKHIKNF ALDGLVNIVG GCCGTTPAHI RKIAEAVKLC KPRVPPSLCQ GYMLLSGLEP FRIGPYTNFV NIGERCNVAG SRKFAKLIMA GNYEEALTVA KSQVEMGAQI LDINMDDGML DGPSAMTRFC NLISSEPDIA KVPLCIDSSN FSVIEAGLKC CQGKCIVNSI SLKEGEEDFL EKAKKIKLYG AAVVVMAFDE VGQATETETK IAICSRAYHL LVEKVHFNPN DIIFDPNILT IGTGMEEHNL YAINFINATK TIKETLPGVR ISGGLSNLSF SFRGMDAIRE AMHGVFLYHA IRCGMDMGIV NAGNLPVYDD IHKELLQLCE NLIWNKDPDA TEKLLRYAQN HAQGGKKVIQ TDEWRNSTVE ERLEYALVKG IEKYVTADTE EARLNQEKYP RPLNIIEGPL MNGMKIVGDL FGAGKMFLPQ VIKSARVMKK AVSHLIPYME KEREERRAKQ GSSEEEARRI DPYNGTIVLA TVKGDVHDIG KNIVGVVLGC NNFRVIDLGV MTPCDKILRA AVENKADIIG LSGLITPSLD EMIFVAKEME RLAIKIPLLI GGATTSKTHT AVKIAPRYSA PVIHVLDASK SVVVCSQLLD ESVKDDFFEE ILEEYEEIRQ EHYESLKERR YLSLQQARRK GFHNDWLSDH KPVKPKFIGT KVFEDYDLKR LVEYIDWKPF FDVWQLRGKY PNRGFPKVFN DKTVGNIQIT CSTGCECLXK ILINQKKLQA RARSVQDDIY LYAVEEAVGS SEPIAKFCGL RQQAEKDSAC TDPYYCLSDF IAPLDSGICD YLGLFAVACF GVDELCDDFR RQDDEYNIIM VKALGDRLAE AFAEELHERV RREFWAYCSD EQLDLSDLRK IKYKGIRPAP GYPSQPDHTE KLTMWKLANI EETTGIGLTE SLAMTPASAV SGLYFSSPKS KYFAVGKICK DQVEDYALRK KLSVAEVEKW LGPILGYDTE // ID G3V8A4_RAT Unreviewed; 1253 AA. AC G3V8A4; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase, isoform CRA_b {ECO:0000313|EMBL:EDM06981.1}; DE SubName: Full=Methionine synthase {ECO:0000313|Ensembl:ENSRNOP00000023973}; GN Name=Mtr {ECO:0000313|EMBL:EDM06981.1, GN ECO:0000313|Ensembl:ENSRNOP00000023973, ECO:0000313|RGD:621283}; GN ORFNames=rCG_30554 {ECO:0000313|EMBL:EDM06981.1}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000023973, ECO:0000313|Proteomes:UP000002494}; RN [1] {ECO:0000313|Ensembl:ENSRNOP00000023973, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000023973, RC ECO:0000313|Proteomes:UP000002494}; RX PubMed=15057822; DOI=10.1038/nature02426; RG Rat Genome Sequencing Project Consortium; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., RA Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., RA Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., RA Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., RA Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., RA Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., RA Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., RA Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., RA Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., RA D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., RA Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., RA Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., RA Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., RA Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., RA Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., RA Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., RA Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., RA Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., RA Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., RA Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., RA Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., RA Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., RA Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., RA Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., RA Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., RA Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., RA Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., RA Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., RA Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., RA Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., RA Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., RA Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., RA Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., RA Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., RA Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into RT mammalian evolution."; RL Nature 428:493-521(2004). RN [2] {ECO:0000313|EMBL:EDM06981.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BN {ECO:0000313|EMBL:EDM06981.1}; RX PubMed=15632090; DOI=10.1101/gr.2889405; RA Florea L., Di Francesco V., Miller J., Turner R., Yao A., Harris M., RA Walenz B., Mobarry C., Merkulov G.V., Charlab R., Dew I., Deng Z., RA Istrail S., Li P., Sutton G.; RT "Gene and alternative splicing annotation with AIR."; RL Genome Res. 15:54-66(2005). RN [3] {ECO:0000313|EMBL:EDM06981.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BN {ECO:0000313|EMBL:EDM06981.1}; RA Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H., RA Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M., RA Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L., RA Lu F., Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C., RA Sutton G.G., Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|Ensembl:ENSRNOP00000023973} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000023973}; RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. RN [5] {ECO:0000213|PubMed:22673903} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., RA Lundby C., Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 RT different rat organs and tissues."; RL Nat. Commun. 3:876-876(2012). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AABR06092570; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AABR06092571; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AABR06092572; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AABR06092573; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH474071; EDM06981.1; -; Genomic_DNA. DR UniGene; Rn.205061; -. DR Ensembl; ENSRNOT00000023974; ENSRNOP00000023973; ENSRNOG00000017593. DR RGD; 621283; Mtr. DR GeneTree; ENSGT00420000029824; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG7TF786; -. DR TreeFam; TF312829; -. DR Reactome; REACT_271861; Methylation. DR Reactome; REACT_285927; Cobalamin (Cbl, vitamin B12) transport and metabolism. DR Reactome; REACT_289986; Sulfur amino acid metabolism. DR NextBio; 35584117; -. DR Proteomes; UP000002494; Chromosome 17. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:Ensembl. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 1: Evidence at protein level; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002494}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EDM06981.1}; KW Proteomics identification {ECO:0000213|PeptideAtlas:G3V8A4}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}; KW Transferase {ECO:0000313|EMBL:EDM06981.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 773 773 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1253 AA; 139191 MW; CFBD40BB66EBD75E CRC64; MKKTLQDEIE AILRKRIMVL DGGMGTMIQR YKLSEENFQG QEFKDHSRPL KGNNDILSIT QPDVIYQIHK EYLLAGADII ETNTFSSTSI AQADYGLEHL AYRMNKCSAD VARKAAEEIT LQTGVKRFVA GSLGPTNKTL SVSPSVERPD YRNITFDELV EAYQEQAKGL LDGGVDILLI ETIFDTANAK AALFALQKLF EENYASPRPI FISGTIVDKS GRTLSGQTGE AFVTSVSHSD PLCIGLNCAL GAAEMRPFIE TIGKCTTAYV LCYPNAGLPN TFGDYDETPA MMAMHLKDFA VDGLVNVVGG CCGSTPDHIR EIAEAVKNCK PRVPPDSVFE GHMLLSGLEP FRIGPYTNFV NIGERCNVAG SKKFAKLIMA GNYEEALSVA KVQVEMGAQV LDINMDDGML DGPSAMTKFC NFIASEPDIA KVPLCIDSSN FAVIEAGLKC CQGKCIVNSI SLKEGEEDFL EKARKIKKFG AAVVVMAFDE EGQATETDVK VSVCTRAYHL LVEKVGFNPN DIIFDPNILT IGTGMEEHNL YAINFIHATR VIKETLPGVR ISGGLSNLSF AFRGMDAIRE AMHGVFLYHA IKFGMDMGIV NAGSLPVYDD IHKDLLQLCE DLIWNRDAEA TEKLLRYAQT HGKGGKKVIQ TDEWRNGSIE ERLEYALVKG IEKHIVEDTE EARLNREKYP RPLNIIEGPL MNGMKVVGDL FGAGKMFLPQ VIKSARVMKK AVGHLIPFME KEREEARVLN GSVEEEDPYQ GTIVLATVKG DVHDIGKNIV GVVLGCNNFR VIDLGVMTPC DKILQAALDH KADIIGLSGL ITPSLDEMIF VAKEMERLAI KIPLLIGGAT TSRTHTAVKI APRYSAPVIH VLDASKSVVV CSQLLDENLK DDYFEEILEE YEDIRQDHYE SLKERKYLPL SQARKHSFHI DWLSEPHPVK PTFIGTQVFE DYNLQKLVDY IDWKPFFDVW QLRGKYPNRG FPKIFNDKAV GEEARKVYED AQNMLNILIS RKKLRARGVV GFWPAQSVQD DIHLYAEGAV PQAAEPIATF YGLRQQAEKD SSSTDPYHCL SDFVAPLHSG VRDYLGLFAV ACFGVEELSK AYEDDGDDYS SIMVKALGDR LAEAFAEELH ERVRRELWAY CGSEQLGVTD LRKLRYEGIR PAPGYPSQPD HTEKLTMWRL ANIEQATGIR LTESLAMAPA SAVSGLYFSN VKSKYFAVGK ISKDQIEDYA LRKNMSVAEV EKWLGPILGY DTD // ID G3VJM1_SARHA Unreviewed; 1265 AA. AC G3VJM1; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSSHAP00000003376}; GN Name=MTR {ECO:0000313|Ensembl:ENSSHAP00000003376}; OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus. OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000003376, ECO:0000313|Proteomes:UP000007648}; RN [1] {ECO:0000313|Ensembl:ENSSHAP00000003376} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21709235; DOI=10.1073/pnas.1102838108; RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., RA Miller J., Walenz B., Knight J., Qi J., Zhao F., Wang Q., RA Bedoya-Reina O.C., Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., RA Woodbridge P., Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., RA Helgen K.M., Lesk A.M., Pringle T.H., Patterson N., Zhang Y., RA Kreiss A., Woods G.M., Jones M.E., Schuster S.C.; RT "Genetic diversity and population structure of the endangered RT marsupial Sarcophilus harrisii (Tasmanian devil)."; RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011). RN [2] {ECO:0000313|Ensembl:ENSSHAP00000003376} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 1}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSSHAP00000003376}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEFK01160007; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEFK01160008; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEFK01160009; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEFK01160010; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEFK01160011; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEFK01160012; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEFK01160013; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEFK01160014; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEFK01160015; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSSHAT00000003412; ENSSHAP00000003376; ENSSHAG00000002966. DR GeneTree; ENSGT00420000029824; -. DR InParanoid; G3VJM1; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG7TF786; -. DR TreeFam; TF312829; -. DR Proteomes; UP000007648; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:Ensembl. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007648}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007648}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 259 259 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 784 784 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1265 AA; 140976 MW; 8F2FD75BA0171E7B CRC64; MPPTLEEPRP PAGKRILKND IEAILKEKIM VLDGGMGTMI QRYTLSEEDF RGQDLKNHAK PLKGNNDLLS ITQPDIICKI HKEYLMAGAD IIETNTFSST WVAQADYGLE HLAYRLNKCS AEVARKAADD VTSQTGIKRF VAGSMGPTNK TLSVSPSVER PDYRNITFDE LVEAYQEQAR GLLDGGVDIL LVETIFDTAN AKAALFALQK LFEEEYDRRP IFVSGTIVDK SGRTLSGQTG EAFVISVSHA EPLCLGLNCA LGALEMRPFI ETIGKCTTAY VLCYPNAGLP NTFGEYDETP EMTAMHIKNF ALDGLVNVVG GCCGTTPDHI REIAEAVKNC KPRVPPASIF DGYMLLSGLE PFRIGPYTNF VNIGERCNVA GSKKFAKLIM AGNYEEALSV AKTQVEMGAQ ILDINMDDGM LDGPSAMTRF CNFIASEPDI AKVPLCIDSS NFAVIEAGLK CCQGKCIVNS ISLKEGEDDF LAKAKKIKMY GAAVVVMAFD EVGQATETSN KIEICTRAYH LLVKKVRFNP NDIIFDPNIL TIGTGMEEHN LYAVNFINAT KTIKETLPGA KISGGLSNLS FSFRGMEAIR EAMHGVFLYH AIKFGMDMGI VNAGNLPVYD DIHKELLQLC EDLIWNKDPD ATEKLLRYAQ TQAKGGKKTI QTDEWRNGPI EERLEYALVK GIEKYIVEDT EEARMNKEKY PRPLNIIEGP LMNGMKVVGD LFGAGKMFLP QVIKSARVMK KAVGYLIPFM EKERAEKRAL TGNVEEEDPY QGTIVLATVK GDVHDIGKNI VGVVLGCNNF RVIDLGVMTP CDKILRAAID NKADIIGLSG LITPSLDEMI FVAKEMERLD IKIPLLIGGA TTSRTHTAVK IAPRYSAPVI HVLDASKSVV VCSQLLDENL KEDFFEEIIE EYEDIRQDHY ESLKERRYLT LDQARKKGFH IDWLSESAPV KPRFIGTQVF EDYDLQRLAD YIDWKPFFDV WQLRGRYPNR GFPKIFNDKT LIGEEAKKLY DDAQNMLKVL ISEKKLQARG LVGFWPAQSV QDDIHLYAED AVPQSAEPIA TFYGLRQQAE KDSASTDPYY CLSDFIAPLE SGVRDYLGFF AVACFGVDEL SKSYEEQCDI YSSIMVKALG DRLAEAFAEE LHERVRKELW AYSDSEQLDV ADLRRIRYGG IRPAPGYPSQ PDHTEKLTMW KLGHIEETTG IRLTESLAMA PASSVSGLYF ANLKSKYFSV GKISKDQIED YALRKNMSVD EVERWLGPIL GYDAD // ID G3WPY2_SARHA Unreviewed; 408 AA. AC G3WPY2; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSSHAP00000017487}; GN Name=BHMT {ECO:0000313|Ensembl:ENSSHAP00000017487}; OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus. OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000017487, ECO:0000313|Proteomes:UP000007648}; RN [1] {ECO:0000313|Ensembl:ENSSHAP00000017487} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21709235; DOI=10.1073/pnas.1102838108; RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., RA Miller J., Walenz B., Knight J., Qi J., Zhao F., Wang Q., RA Bedoya-Reina O.C., Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., RA Woodbridge P., Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., RA Helgen K.M., Lesk A.M., Pringle T.H., Patterson N., Zhang Y., RA Kreiss A., Woods G.M., Jones M.E., Schuster S.C.; RT "Genetic diversity and population structure of the endangered RT marsupial Sarcophilus harrisii (Tasmanian devil)."; RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011). RN [2] {ECO:0000313|Ensembl:ENSSHAP00000017487} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSSHAP00000017487}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEFK01050637; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSSHAT00000017632; ENSSHAP00000017487; ENSSHAG00000014860. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; G3WPY2; -. DR OMA; WGVTKGT; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR Proteomes; UP000007648; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006577; P:amino-acid betaine metabolic process; IEA:Ensembl. DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007648}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000007648}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 219 219 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 301 301 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 302 302 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 408 AA; 44980 MW; 83B32262EE7C04E6 CRC64; MVPSGGKKVK RGILQRLDAG EVVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAVRQLH REFLRAGSNV MQTFTFYASE DKLENRGNYV AEKISGQKVN EAACDIALEV AAEGDALVAG GVSQTPSYLS CKSETEVKKI FRQQLEVFIK KKVDFLIAEY FEHVEEAVWA VEALKESGKP VAATMCIGPE GDLHGVSPGE CAVRLVKAAL GASIVGVNCH FDPTISLKTV KLMKEGLEAA RLKAHLMAQP LAYHTPDCGK QGFIDLPEFP FGLEPRVATR WDIQKYAREA YNLGVRYIGG CCGFEPYHIR AIAEELAPQR GFLPDASEKH GSWGSGLNMH TKPWVRARAR KEYWESLSLA SGRPYCPSMS RPDAWGVTKG TAELMQQKEA TTDQQLKELF QKQKFKSS // ID G3WQB2_SARHA Unreviewed; 363 AA. AC G3WQB2; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSSHAP00000017617}; GN Name=BHMT2 {ECO:0000313|Ensembl:ENSSHAP00000017617}; OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus. OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000017617, ECO:0000313|Proteomes:UP000007648}; RN [1] {ECO:0000313|Ensembl:ENSSHAP00000017617} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21709235; DOI=10.1073/pnas.1102838108; RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., RA Miller J., Walenz B., Knight J., Qi J., Zhao F., Wang Q., RA Bedoya-Reina O.C., Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., RA Woodbridge P., Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., RA Helgen K.M., Lesk A.M., Pringle T.H., Patterson N., Zhang Y., RA Kreiss A., Woods G.M., Jones M.E., Schuster S.C.; RT "Genetic diversity and population structure of the endangered RT marsupial Sarcophilus harrisii (Tasmanian devil)."; RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011). RN [2] {ECO:0000313|Ensembl:ENSSHAP00000017617} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSSHAP00000017617}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEFK01050640; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEFK01050641; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSSHAT00000017762; ENSSHAP00000017617; ENSSHAG00000014959. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; G3WQB2; -. DR OMA; PEGDMHD; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000007648; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0061627; F:S-methylmethionine-homocysteine S-methyltransferase activity; IEA:Ensembl. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl. DR GO; GO:0046500; P:S-adenosylmethionine metabolic process; IEA:Ensembl. DR GO; GO:0033477; P:S-methylmethionine metabolic process; IEA:Ensembl. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007648}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Reference proteome {ECO:0000313|Proteomes:UP000007648}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 208 208 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 363 AA; 40322 MW; 6AA725BE1BED2511 CRC64; MARVVGERVK KGILERLNSG EVVIGDGSFV FTLEKRGYVK AGLWTPEASV EYPEAVRQLH MEYLRAGSNV MQTFTFFGGK DKLESKWKDV NEASCDLARE VAEKGNALVA GGISQTSLYK SHKNKLEIKE IFQQQLEIFT RKNVDFLIAE YFEYCEEAVW AVEVLKESGK PVATTMCIGP EGDMHNLTPG ECAIRLVKAG ASIVGVNCRF GPTISLATVK LMKEGLEASG LKAHLMVQSL GFHTPDCGKG GFVDLPQYPF GLEPRVATRW DIQKYAREAY NLGVRYIGGC CGFEPYHIRA IAEELAPERG FLPDASEKHD SWGSGLSMHT KPWVRARAQK EYWKNLLPAS GRPYFPSLSK PDG // ID G3XX38_ASPNA Unreviewed; 353 AA. AC G3XX38; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHA24908.1}; GN ORFNames=ASPNIDRAFT_210376 {ECO:0000313|EMBL:EHA24908.1}; 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 {ECO:0000313|EMBL:EHA24908.1, ECO:0000313|Proteomes:UP000009038}; RN [1] {ECO:0000313|EMBL:EHA24908.1, ECO:0000313|Proteomes:UP000009038} 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 {ECO:0000313|Proteomes:UP000009038}; RX PubMed=21543515; DOI=10.1101/gr.112169.110; RA Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J., 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., 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., 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., van Peij N.N., RA 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. {ECO:0000313|EMBL:EHA24908.1}. 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; ACJE01000008; EHA24908.1; -; Genomic_DNA. DR ProteinModelPortal; G3XX38; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000009038; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009038}; KW Reference proteome {ECO:0000313|Proteomes:UP000009038}. SQ SEQUENCE 353 AA; 38706 MW; A8683A4387D7B785 CRC64; MAKTPILILD GGLGTSLQDH YNITFSSSTT PLWSSHLMIS DPSTLLSCQR DFTTTAAVDV LLTATYQVSP EGFQRTKTPS HPTGIPRESI AGYLRTALDV AGQAVQNTSA SVALSLGPYG ACMIPGQEYS GKYDGEHDTE EKLWRWHTDR LGLFNDEAME GMRLGERVKY IAMETVPRID EVRAVRRAVG SSRFCEGIPF WVACVFPIED KDTLPDGSTV DEVVEAALLP IEGGATPWGI GINCTKLHKL PRLVKLFGDA VERLLRDGRI QERPALVLYP DGTQGEVYNT ATQTWEKVQD KSGAADSRPW EVQLAQVVND ASATGQFSSI LVGGCCKASF NDIKRLREQL RPQ // ID G4BC48_AGGAP Unreviewed; 1229 AA. AC G4BC48; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EGY31841.1}; GN ORFNames=ATCC33389_0287 {ECO:0000313|EMBL:EGY31841.1}; OS Aggregatibacter aphrophilus ATCC 33389. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Aggregatibacter. OX NCBI_TaxID=985008 {ECO:0000313|EMBL:EGY31841.1}; RN [1] {ECO:0000313|EMBL:EGY31841.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33389 {ECO:0000313|EMBL:EGY31841.1}; RA Kittichotirat W., Bumgarner R.E., Checn C.; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGY31841.1}. 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; AEWB01000006; EGY31841.1; -; Genomic_DNA. DR RefSeq; WP_005703049.1; NZ_AEWB01000006.1. DR EnsemblBacteria; EGY31841; EGY31841; ATCC33389_0287. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 757 757 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1229 AA; 136497 MW; F2C2CB56927B7F44 CRC64; MKNTTELLKK SLAERILILD GAMGTMIQKY KLTETDFRGE RFAKSAIDLR GNNDLLTLTQ PLLISAIHEK YLEAGADIIE TNTFSSTTIA QADYDLQSIA YELNFAGAKL ARLAADKYST PKKPRFVAGI LGPTNRTASI SPNVNDPGFR NVTFMELVDA YSEASRGLIK GGADLIMIET IFDTLNAKAA IFAIETVFEE LGVELPIMIS GTITDASGRT LSGQTTEAFY NSLRHAKPLT FGLNCALGPK ELRQYVEQLS KISETYVSVH PNAGLPNAFS GYDLGAEDMA AQLKEWAESG FVNIIGGCCG TTPEHIKAFA EAVKNIPPRK LPQIKTAMRL SGLEPLNIDD ESLFVNVGER NNVTGSAKFK RLIKEDKFAE AIEIAIDQVE NGAQVIDVNM DEALLDGKKC MTRFLNIMAT EPDAAKVPVM IDSSKWEVIE AGLQSVQGKP IVNSISLKEG EELFIEHAKL VRKYGAAMVV MAFDEVGQAD TEDRKVEICT RAYNILVNQV GFPPEDIIFD PNIFAIGTGI EEHNNYGVDF INATGRIKRS LPHAKISGGV SNVSFSFRGN NIMREAIHAV FLYYAIKQGM DMGIVNAGQL AIYDDLDPEL RNVIEDAVLN RTPDGTERLL DIAEKYRNQG NDESVVDSVA EWRTWPVEER LKHALVKGIT THIIEDTEEA RQKLPTPLEV IEGPLMAGMD VVGDLFGNGK MFLPQVVKSA RVMKQSVAYL EPFINVTKQK GSSNGKVVIA TVKGDVHDIG KNIVSVVMQC NNFEVIDLGV MVPADKIIQT AIDEKADIIA LSGLITPSLD EMEYFLGEMT RLGLNLPVMI GGATTSKEHT AIKLYPKYKQ HGVFYTSNAS RAVTVCATLM NPEGRAALWE QFKKDYEKIQ QSFANRKPLR KQLSIEEART NRFDGFSGEW ADYVPPTPKQ TGIVEFKNVP IAELRKFIDW SPFFRVWGLM GGYPDAFDHP ESGQEAHRVW NDAQAMLDAF EQNHKLNPSG ILGIFPAERV DDDVVLFADE ERTQAIGTAY GLRQQTERGK NSKSQFNFAL SDFIADRESG KKDWMGMFAV CAGIKEMELV EGYKAAGDDY NAILLQAVGD RLAEAMAEYL HFELRTRIWG YTQEEFDNQG LINENYVGIR PAPGYPSCPE HTEKALIWDL LGVEQRIGMK LTESYAMWPA ASVCGWYFTH PASNYFTLGR IDEDQAQDYA KRKGWDEREM LKWLGVVMK // ID G4CAL8_SALIN Unreviewed; 1301 AA. AC G4CAL8; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 01-APR-2015, entry version 24. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHB39163.1}; GN ORFNames=SEENIN0B_04457 {ECO:0000313|EMBL:EHB39163.1}; OS Salmonella enterica subsp. enterica serovar Infantis str. SARB27. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=596155 {ECO:0000313|EMBL:EHB39163.1, ECO:0000313|Proteomes:UP000004564}; RN [1] {ECO:0000313|EMBL:EHB39163.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SARB27 {ECO:0000313|EMBL:EHB39163.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHB39163.1}. 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; AFYI01000007; EHB39163.1; -; Genomic_DNA. DR EnsemblBacteria; EHB39163; EHB39163; SEENIN0B_04457. DR Proteomes; UP000004564; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000004564}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 384 384 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 385 385 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 833 833 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1301 AA; 143970 MW; 13EFBB5E4F93CE01 CRC64; MTSQDARWRF AYQAYALGAA KVICRLDKAL APPSDKATEV GGKLNMSHVA RCSLFRQHAL CQYGSLRGAL SGASVSSKVE QLRAQLNERI LVLDGGMGTM IQSYRLHEED FRGERFADWP CDLKGNNDLL VLSKPEVIAA IHNAYFEAGA DIIETNTFNS TTIAMADYRM ESLSAAINYA AAKLARACAD EWTARTPEKP RFVAGVLGPT NRTASISPDV NDPAFRNITF DQLVAAYRES TKALVEGGVD LILIETVFDT LNAKAAVFAV KEEFEALGVD LPIMISGTIT DASGRTLSGQ TTEAFYNSLR HAEALTFGLN CALGPDELRQ YVQELSRIAE CYVTAHPNAG LPNAFGEYDL DADTMAKQIR EWAEAGFLNI VGGCCGTTPE HIAAMSRAVA GLPPRQLPDI PVACRLSGLE PLNIGDDSLF VNVGERTNVT GSAKFKRLIK EEKYSEALDV ARQQVESGAQ IIDINMDEGM LDAEAAMVRF LSLIAGEPDI ARVPIMIDSS KWEVIEKGLK CIQGKGIVNS ISMKEGVEAF IHHAKLLRRY GAAVVVMAFD EQGQADTRER KIEICRRAYK ILTEEVGFPP EDIIFDPNIF AVATGIEEHN NYAQDFIGAC EDIKRELPHA LISGGVSNVS FSFRGNDPVR EAIHAVFLYY AIRNGMDMGI VNAGQLAIYD DLPAELRDAV EDVILNRRDD GTERLLDLAE KYRGSKTDEA ANAQQAEWRS WDVKKRLEYS LVKGITEFIE QDTEEARQQA SRPIEVIEGP LMDGMNVVGD LFGEGKMFLP QVVKSARVMK QAVAYLEPFI EASKEKGSSN GKMVIATVKG DVHDIGKNIV GVVLQCNNYE IVDLGVMVPA EKILRTAREV NADLIGLSGL ITPSLDEMVN VAKEMERQGF TIPLLIGGAT TSKAHTAVKI EQNYSGPTVY VQNASRTVGV VAALLSDTQR DDFVARTRKE YETVRIQHAR KKPRTPPVTL EAARDNDLAF DWERYTPPVA HRLGVQEVEA SIETLRNYID WTPFFMTWSL AGKYPRILED EVVGVEAQRL FKDANDMLDK LSAEKLLNPR GVVGLFPANR VGDDIEIYRD ETRTHVLTVS HHLRQQTEKV GFANYCLADF VAPKLSGKAD YIGAFAVTGG LEEDALADAY EAQHDDYNKI MVKAIADRLA EAFAEYLHER VRKVYWGYAP NESLSNDELI RENYQGIRPA PGYPACPEHT EKGTIWQLLD VEKHTGMKLT ESFAMWPGAS VSGWYFSHPE SKYFAVAQIQ RDQVTDYAFR KGMSVENVER WLAPNLGYDA D // ID G4CZ83_9ACTO Unreviewed; 1161 AA. AC G4CZ83; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|EMBL:EGY76802.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGY76802.1}; GN Name=metH {ECO:0000313|EMBL:EGY76802.1}; GN ORFNames=HMPREF9153_1755 {ECO:0000313|EMBL:EGY76802.1}; OS Propionibacterium avidum ATCC 25577. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=997355 {ECO:0000313|EMBL:EGY76802.1, ECO:0000313|Proteomes:UP000005332}; RN [1] {ECO:0000313|EMBL:EGY76802.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 25577 {ECO:0000313|EMBL:EGY76802.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGY76802.1}. 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; AGBA01000015; EGY76802.1; -; Genomic_DNA. DR RefSeq; WP_004811283.1; NZ_JH165054.1. DR EnsemblBacteria; EGY76802; EGY76802; HMPREF9153_1755. DR Proteomes; UP000005332; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000005332}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGY76802.1}; KW Transferase {ECO:0000313|EMBL:EGY76802.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 219 219 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 729 729 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1161 AA; 126597 MW; 58A4AB10AF11195D CRC64; MTLRTALSRH VLVIDGAMGT MLQSSDLTID DFQGLEGCNE ILNVTRPDVI SRIHDAYLDS GADIIETNTF GVNLPALTEY GIAPRAVELA SAATKLAREA ADKRTDKPRY VVGSIGPGTK LPTLRQIGFA AIRDVYQQVI EAMIDAGADG VQIETCQDLL QARAAIIGAH RAATARKVDL PILVDFTVET TGIMLMGSES GAALTVLESL GVDAIGLNCA TGPAEMAEHL RTLSRGAQVP IMCMPNAGLP EITGEGARYP LGPDDLAPVL DDYVDRYGLS VVGGCCGTTP DHIHAIAERV SGRPVPEREI HHVDAVASLY NDVPLSQDTA YLAIGERTNA NGSKAFREAM LAQNWDECVD IARAQTRDGA HLLDLCVDYV GRDGVADMSE LSARLATACT LPIILDSTEP DVLAAGLEHL PGRCIINSVN FEDGDGPGSR YQRVMPMVVE NGAGVVALTI DEEGQARTAE WKVRVASRLI DDLVDNWGMD IGDILVDCLT FPIGTGQEET RRDGLETINA IAEIKKRYPG VRTTLGVSNI SFGLNPAARI VLNSVFLHEA VKAGLDSAIV HTAKILPIDR IPEEQREVAL DLVHDRRHDG YDPLNRFLEL FEGVTAASMR AEREAELAAM PLFERLKQRI IDGNAKGLED DLDEAMESKA ALDIVNEDLL AGMQVVGDLF GSGKMQLPFV LQSAEVMKMA VAHLEPHMDK SDTSGKGTLV LATVKGDVHD IGKNLVDIIV SNNGYHVVNL GIKQPVTAII EAAETHRADV IGMSGLLVKS TMVMKDNLLE LNQTGLASKY PVMLGGAALT RTFVEEDLND LFEGEVRYAR DAFEGLRLMD SVMAVKKGVP GAELPKPRRR RIKVKQAAVE TDDMTSDDNA PRADVARPVP GSVEIPTPPF WGSRVSTGIP LADVLVWLDE RATFMGRWGL KGSRSDGSWD RMVNEVARPR LRLLLDRIRQ ENLAQFGVVD GYWPCFSQGH DLIILDPEDT SREVTRFTFP RQSSGRKLCL VDFFRDVDEA GEYGPDVIGF QLVTMGKAVS AATQRLFEAN SYREYLELHG LSVQLTEALA EMWHARVRHE LRIDDDGTSV TDAIDHQTYR GCRYSFGYAA CPNLDDRAKV VKLLNPARIG VELSEEFQLH PEQSTDAFVV HHPEANYFNA K // ID G4D3N8_9FIRM Unreviewed; 317 AA. AC G4D3N8; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 27-MAY-2015, entry version 12. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGY79859.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EGY79859.1}; GN Name=mmuM {ECO:0000313|EMBL:EGY79859.1}; GN ORFNames=HMPREF9129_1018 {ECO:0000313|EMBL:EGY79859.1}; OS Peptoniphilus indolicus ATCC 29427. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptoniphilaceae; OC Peptoniphilus. OX NCBI_TaxID=997350 {ECO:0000313|EMBL:EGY79859.1}; RN [1] {ECO:0000313|EMBL:EGY79859.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29427 {ECO:0000313|EMBL:EGY79859.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGY79859.1}. 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; AGBB01000093; EGY79859.1; -; Genomic_DNA. DR RefSeq; WP_004820935.1; NZ_JH165061.1. DR EnsemblBacteria; EGY79859; EGY79859; HMPREF9129_1018. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EGY79859.1}; KW Transferase {ECO:0000313|EMBL:EGY79859.1}. SQ SEQUENCE 317 AA; 35263 MW; 6C7A82F907E29317 CRC64; MKKSIDELIS LKKILVLDGA LATELERAGK NINDSLWSTK ILIEDSEAIK KVHLSYLEAG CDIILTSSYQ TTIKGLMKRG YTKDEAIEII KKSFRIANEA KEEYLLKNSV EVEPIIGASI GPYGAFLSDG SEYTGNYEVL DSEMRDFHYE KIKILKDEGV ELFACETIPS FREALVIQKI CEELEVEYYI SFSAKDEYSI SDGTSIRECA GNLNGKYLKG IGINCTAPEF LESLIREIKS VYNGNIVVYP NSGEIFDPVS KTWSGNGQCV FDLAENWIRA GANIIGGCCK TTPQDIKKLA DSIKNKKIKN LLTSIAL // ID G4E615_9GAMM Unreviewed; 1256 AA. AC G4E615; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGZ45638.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGZ45638.1}; GN ORFNames=ThisiDRAFT_1744 {ECO:0000313|EMBL:EGZ45638.1}; OS Thiorhodospira sibirica ATCC 700588. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Thiorhodospira. OX NCBI_TaxID=765914 {ECO:0000313|EMBL:EGZ45638.1}; RN [1] {ECO:0000313|EMBL:EGZ45638.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 700588 {ECO:0000313|EMBL:EGZ45638.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EGZ45638.1}. 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; AGFD01000032; EGZ45638.1; -; Genomic_DNA. DR RefSeq; WP_006787760.1; NZ_AGFD01000032.1. DR EnsemblBacteria; EGZ45638; EGZ45638; ThisiDRAFT_1744. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGZ45638.1}; KW Transferase {ECO:0000313|EMBL:EGZ45638.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 249 249 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1256 AA; 139737 MW; 7623029D5013D8F5 CRC64; MDLPDRLQLF KEHAARRILL LDGAMGTMIQ RYSLSEADYR GERFADWPCD LKGNNDLLVL SRPEIIREIH AKYLEAGADI IETNSFNATR ISMADYAMED LVVELNREAA RLARAVADEW TAHNPHQPRF VAGVLGPTSR TASISPDVND PGFRNVYFDD LVAIYQQAAT ALVEGGADIL MIETVFDTLN AKAAVFALEG LFVQWGRRVP VMISGTITDA SGRTLSGQTT EAFWNSLRHA RPLAFGLNCA LGPLELRPYV EELSRISDCM VSAHPNAGLP NAFGGYDLSP EQMATEIADW AREGFLNIVG GCCGTTPEHI RAIRDAVVIH APRTIPVRPP ACRLAGLEPL NIYHNNLFVN VGERTNVTGS ARFKRLIKDG DYATALEVAA SQVTNGAQII DINMDEGMLD TQAAMERFLN LVAAEPDISR VPIMIDSSKW EVIEAGLKRI QGKGIVNSIS LKEGEAQFIA QAQLLRRYGA AVVVMAFDEQ GQADTRERKI EICSRAYRIL TEQADFPAED IIFDPNIFAV ATGIEEHNRY AVDFIEATAA IRKTLPHALI SGGVSNISFA FRGNDAVREA IHAVFLYHAI RAGLSMGIVN AGQLAVYDEI QPQLRSAVED VILNRHPEAT ERLLELAQQY RSSGTETRTE DLSWRDWPVA KRLEHALVKG VDTYVVADTE AARLEAGHPI QVIEGPLMDG MNVVGDLFGA GKMFLPQVVK SARVMKKAVA HLIPYIEADR SQGAQKQGRI LMATVKGDVH DIGKNIVGVV LQCNNFEVID LGVMVPAQKI LDQAKAQQVD IIGLSGLITP SLDEMVHLAS EMQRLGFEIP LLIGGATTSR AHTAVKIAPH YQGPCVWVKD ASRAVGVAQS LLSPELRGAY QEKIRSEYVQ VREQYEQRQR EQSWLSLAVA RERAWSLDWS SYQPTRPRLL SPENAANIAP EAVCWTHPEA PESALLRFED YPLAELLPYI DWTPFFQSWQ LHGRYPEILQ HPDMGVAAST LFQDAQTMLE QIIHEGWLQA RVVLGFFAAQ RVDHDDIALY KDPARQQEWL RLHHLRQQTQ RKAEAPNLCL SDFIAPQDTG HADYLGAFAV TAGIGIEAHV QRFEQAHDDY RALLLKSLAD RLAEALAERI HERVRREFWG YVPDEDLSNE ALIAEEYQGI RPAPGYPACP EHTEKATLWR LLMADEQAQI SLTEHYAMHP AASVSGWYFA HPQARYFTVG KLNRDQVHSY AQRKGMSLSE AERWLAPNLG YDPEDS // ID G4EXZ4_BACIU Unreviewed; 612 AA. AC G4EXZ4; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 27-MAY-2015, entry version 18. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=BSSC8_32240 {ECO:0000313|EMBL:EHA30127.1}; OS Bacillus subtilis subsp. subtilis str. SC-8. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1089443 {ECO:0000313|EMBL:EHA30127.1}; RN [1] {ECO:0000313|EMBL:EHA30127.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SC-8 {ECO:0000313|EMBL:EHA30127.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHA30127.1}. 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; AGFW01000009; EHA30127.1; -; Genomic_DNA. DR RefSeq; WP_003233035.1; NZ_AGFW01000009.1. DR EnsemblBacteria; EHA30127; EHA30127; BSSC8_32240. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EHA30127.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EHA30127.1}. SQ SEQUENCE 612 AA; 67984 MW; FBA1B99B9F5F3A7A CRC64; MGLLEDLQRQ VLIGDGAMGT LLYSYGIDRC FEELNISKPE EIQRIHKAYV EAGANIIQTN TYGANYIKLS RHGLEDDIKK MNQEAVKIAR ASAGDAYVLG TMGGIRTFNK NAYSLDEIKR SFREQLYLLL HEEPDGLLLE TYYDLEEARE VLKIARKETD LPIMLNVSMH EQGVLQDGTP LSDALRSIAD LGADIVGINC RLGPYHMIEA LSEVPIFDDV FLSVYPNSSL PSLEEGRLVY ETDDTYFQNS ALEFRKQGAR IIGGCCGTTP NHIRAMAEAV GGLAPITEKE VKTRAKEFIS VHHERTEPGL DEIAAKKRSI IVELDPPKKL SFDKFLSAAA ELKEAGIDAL TLADNSLATP RISNVACGAL VKQQLDMRSL VHITCRDRNI IGLQSHLMGL DTLGLNDVLA ITGDPSKIGD FPGATSVYDL TSFDLIRLIK QFNEGLSLSG KPLGKKTNFS VAAAFNPNVR HLDKAVKRLE KKIDCGADYF VSQPVYSEQQ LVDIHNETKH LKTPIYIGIM PLTSSRNAEF IHNEIPGIKL SDTIREKMAH AGEDKEKQKT EGLAIARSLL DTACELFNGI YLITPFLRSD LTAELTSYIQ QKDEQRQNIF LH // ID G4F0G2_BACIU Unreviewed; 296 AA. AC G4F0G2; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 01-OCT-2014, entry version 12. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:EHA28819.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EHA28819.1}; GN ORFNames=BSSC8_40920 {ECO:0000313|EMBL:EHA28819.1}; OS Bacillus subtilis subsp. subtilis str. SC-8. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1089443 {ECO:0000313|EMBL:EHA28819.1}; RN [1] {ECO:0000313|EMBL:EHA28819.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SC-8 {ECO:0000313|EMBL:EHA28819.1}; 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. {ECO:0000313|EMBL:EHA28819.1}. 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; AGFW01000016; EHA28819.1; -; Genomic_DNA. DR EnsemblBacteria; EHA28819; EHA28819; BSSC8_40920. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHA28819.1}; KW Transferase {ECO:0000313|EMBL:EHA28819.1}. SQ SEQUENCE 296 AA; 32648 MW; 09428A3E9DC37F7E CRC64; MATELERKGC DLNDSLWSAK ILMEEPELIK QVHTDYFAAG ADCAITASYQ STFEGFAARG LSEAEARRLI ELSVSIAAEA RDEFWSLKEN RLNRPKPIIA ASIGPYGAYL ADGSEYRGNY AISEDELIEF HRPRMKALIE AGADVLACET IPCLTEAKAI VRLLKEFPET YAWISFSAKD GLHISDGTPA SDCASWLDEH RQIAALGINC TPLQHIPSLI EELKKNTSKP IIVYPNSGEQ YDPETKTWNG AACAESYGAS ARTWHEKGAR LIGGCCRTKP EDIQEIAAWA RSLKTT // ID G4F6N4_9GAMM Unreviewed; 1231 AA. AC G4F6N4; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 01-APR-2015, entry version 19. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EHA15632.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHA15632.1}; GN Name=metH {ECO:0000313|EMBL:EHA15632.1}; GN ORFNames=HAL1_10247 {ECO:0000313|EMBL:EHA15632.1}; OS Halomonas sp. HAL1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=550984 {ECO:0000313|EMBL:EHA15632.1}; RN [1] {ECO:0000313|EMBL:EHA15632.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HAL1 {ECO:0000313|EMBL:EHA15632.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHA15632.1}. 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; AGIB01000045; EHA15632.1; -; Genomic_DNA. DR RefSeq; WP_008957948.1; NZ_AGIB01000045.1. DR EnsemblBacteria; EHA15632; EHA15632; HAL1_10247. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHA15632.1}; KW Transferase {ECO:0000313|EMBL:EHA15632.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1231 AA; 136200 MW; 2AE2417CE2404DCC CRC64; MADSALTATL TQRLAERILI LDGGMGTMLQ NAQLSEEDFR GERFSDWPSD LKGNNDLLAL TCPDVVTRIH RDYLEAGADI IETNTFNSTQ LSQSDYGMEA LVVELNRESA RLAREVCDAV AAETGVPRYV AGVLGPTSRT ASLSPDVNDP AKRNVTFDEL RENYYEAAEA LIAGGADLIM IETIFDTLNA KAAIYALEEL FDDRGERLPV MISGTITDAS GRTLSGQTTE AFWNSVRHAQ PLSVGLNCAL GAEELRPYLE ELSTKADTFV SAHPNAGLPN EFGEYDQTPE EMSEIVSEFA SSGLVNIIGG CCGSTPEHIR AIADSVRDMA PRSIPERSRA CRLSGLEPFN IESDALFVNV GERTNVTGSA RFKRLIVEED FTTALEVALE QVESGAQVID INMDEGMLES KEAMERFLNL IAGEPDIARV PIMIDSSKWE IIEAGLKCVQ GKAVVNSISL KEGEDAFREQ ATKCRRYGAA IVVMAFDEEG QADTFARKTE ICQRAYRLLV DEIGFPAEDI IFDPNIFAIG TGIEEHNNYA VDFIEATQWI RDNLPHAMVS GGVSNVSFSF RGNNPVREAI HSAFLYHAIR AGLTMGIVNA GQLAVYDDLP AELRDAVEDV VLNRRSDGTE RLLDIADKYK GDGSGAPKKE DLEWRSWPVN KRIQHALVKG ITVYIEDDTE EARAQAERPI EVIEGPLMDG MNVVGDLFGD GKMFLPQVVK SARVMKQAVA YLIPYIEAEK SEETKAKGKI VMATVKGDVH DIGKNIVGVV LQCNNYEVID LGVMVAADKI LQAAKDHNAD IIGLSGLITP SLDEMVHVAK EMQRRGMDLP LLIGGATTSK AHTAVKIEPQ YEHPVIYVTD ASRAVGVAGR LLAPNQKAAY VAEIREEYEK VRERNAKRRP KAADLDYTQA RKRRFRTDWN AHTPAEPNML GLKTFDDYDL EELIERIDWT PFFMSWQLAG KYPKILDDKV VGEAARNLFD DAKVMLRKLV EEKRVQARGV IGLWPANSVD DDVIEVYADE SRSEVIERLF HIRQQTTKGR DGICYSLADF IAPKESGKAD WIGGFAVTTG HGVHELSKAY EAAGDDYNAI MVQALTDRLA EAFAERMHER VRKEFWGYVP DETLDNDALI AEKYQGIRPA PGYPACPDHT EKASLFRLLD ATENTGLALT ENFAMWPAAA VSGWYFAHPQ SKYFSTGKIT RDQVEAIAAR KQMPLVEMER WLSPVLSYDP S // ID G4FK79_9SYNE Unreviewed; 1206 AA. AC G4FK79; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 01-APR-2015, entry version 21. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHA63389.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHA63389.1}; GN ORFNames=Syn8016DRAFT_0430 {ECO:0000313|EMBL:EHA63389.1}; OS Synechococcus sp. WH 8016. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechococcus. OX NCBI_TaxID=166318 {ECO:0000313|EMBL:EHA63389.1}; RN [1] {ECO:0000313|EMBL:EHA63389.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=WH 8016 {ECO:0000313|EMBL:EHA63389.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHA63389.1}. 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; AGIK01000001; EHA63389.1; -; Genomic_DNA. DR RefSeq; WP_006852571.1; NZ_AGIK01000001.1. DR EnsemblBacteria; EHA63389; EHA63389; Syn8016DRAFT_0430. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHA63389.1}; KW Transferase {ECO:0000313|EMBL:EHA63389.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 238 238 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1206 AA; 132266 MW; C42A0F93A3D10958 CRC64; MQAVTETPTL NASRFLKRLH DPSRPVLVFD GATGTSLQQM DLSADDFGGE ALEGCNENLV VTRPDAVQSV HRQFLDAGCD VIETDTFGAA SVVLAEYGLE DKTFELNKRA AELAKEVAME YSTDEKPRFV AGSMGPTTKL PTLGHISFDL LRDSYQEQAE GLIAGDVDLL IIETCQDVLQ IKAALQGIEQ AFETSGERRP LMVSVTMETT GTMLVGSDIA AVVAILEPFP IDVLGLNCAT GPEQMKEHMR YLTDNAPFVV SCIPNAGLPE NVGGVAHYRL TPVELKMQLM HFVEDLGVQV IGGCCGTTPA HIAALSEISS ELSAAPRNVR SYHHERKALS YEAAASSIYG ATPYLQDNSF LIIGERLNAS GSKKVRELLN EEDWDGLVAV ARGQVKENAH ILDVNVDYVG RDGERDMREL VNRVVTNVNL PLMLDSTEWQ KMEAGLKVAG GKCILNSTNY EDGDERFFKV LEIAKRYGAG VVIGTIDEDG MARTADQKVA IAKRAYRDAV EYGIPAREIF YDALALPIST GIEEDRRNGA ETIEAIRRIR EDLPQVHVVL GVSNVSFGLS PAARITLNSV FLHDCCEAGM DAAIVSPAKI LPLIKISEEH QKVCRDLIND RRGFEGDVCT YDPLTVLTTL FEGVSAKAAR ESGPSLSDLA VEERLKQHII DGERIGLEDA LKEGLENYPP LDIVNTFLLD GMKVVGELFG SGQMQLPFVL QSAETMKSAV AFLEPFMEKE EGERSAKAKF LIATVKGDVH DIGKNLVDII LTNNGYEVIN LGIKQDVNAI ITAQQEHQAD CIAMSGLLVK STAFMKDNLQ AFNEAGINVP VVLGGAALTP RFVNKDCSDV YDGKVIYGRD AFTDLRFMDA LVAAKSKDRW DDRAGFLDGT PEGLSIGGDA ESTDPSDASP ESPSKEAETA DLKLPVSFER SDAVPEETAV ITPFLGASVL QGEAEIPVDE VIAFLDRQAL FAGQWQMRKA KNQSREEYEQ DLADKAEPIL QKWLARAKED QLLHPAVAYG YFPCGRDGNS VVVFKPEGGA ELGRFDVPRQ RSGNRYCIAD FFRDLKEGQP CDVLPMQAVT MGEEASRFSQ ELFRKDAYSD YLFFHGLAVQ MAEALAEWTH ARIRRECGFS DPKGMPLRDI LAQRYRGSRY SFGYPACPNV ADSRQQLEWL QADRIGLTMD ESDQLHPEQS TTALVALHSN ARYFSA // ID G4HER2_9BACL Unreviewed; 623 AA. AC G4HER2; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 27-MAY-2015, entry version 18. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=PaelaDRAFT_2473 {ECO:0000313|EMBL:EHB65331.1}; OS Paenibacillus lactis 154. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=743719 {ECO:0000313|EMBL:EHB65331.1}; RN [1] {ECO:0000313|EMBL:EHB65331.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=154 {ECO:0000313|EMBL:EHB65331.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGIP01000004; EHB65331.1; -; Genomic_DNA. DR RefSeq; WP_007129645.1; NZ_AGIP01000004.1. DR EnsemblBacteria; EHB65331; EHB65331; PaelaDRAFT_2473. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EHB65331.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EHB65331.1}. SQ SEQUENCE 623 AA; 68096 MW; 20585D26DD7738E5 CRC64; MKPDLRQAWE NQVLIGDGAI GTYLYQLGFP VGISYEELNL TSPEVIGNVH RQYVDAGAQL IETNTFSANY DKLSKYGLES KVGEINRAGV RIAREAAGRD GYVVGAVGSI RAGRRSNIST GELKRYFEEQ LSVLLSEGVD GILLETFYDV EEIQLALQQV RKLTDLPVIC QFAVENIART LDGFSMQDAY RILSQEGADV IGFNCRTGPN GIMRALETLS GVMNLPASVY PNAGIADYVD GEFRYGASPE YFGQMAVPFA DLGARIIGGC CGTTPAHIAE IASALSGYVP SPLPEVEPAE INRIVIQEPA EGNQPERSSE PSLVDLVKER HTVIVELDPP RDLDITKFMK GAEALKNAGA DALTLADNSL AVTRMSNMAL GHLVQARIGL RPLIHIACRD RNLIGTQSHM MGFDALGIDH VLAVTGDPAR FGDLPGSSSV YDMTSFEIIR MIKQLNEGIA FSGKPLKQKA KFVVGAAFNP NVRHLDKAVA RLEKKIASGA DYVMTQPVYD PELIVRLREA TAHLDIPIFI GIMPLASGRN AEYLHNEVPG IQLSDEVRSR MAGLEGEAGR AMGVQIGKEL LDVATKHFNG IYLMTPFMFY EMSVQLMEYV WEISGRRLSP LFH // ID G4HFP3_9BACL Unreviewed; 1146 AA. AC G4HFP3; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHB64560.1}; GN ORFNames=PaelaDRAFT_2804 {ECO:0000313|EMBL:EHB64560.1}; OS Paenibacillus lactis 154. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=743719 {ECO:0000313|EMBL:EHB64560.1}; RN [1] {ECO:0000313|EMBL:EHB64560.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=154 {ECO:0000313|EMBL:EHB64560.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AGIP01000005; EHB64560.1; -; Genomic_DNA. DR RefSeq; WP_007129974.1; NZ_AGIP01000005.1. DR EnsemblBacteria; EHB64560; EHB64560; PaelaDRAFT_2804. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 722 722 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1146 AA; 126134 MW; 99584812E5C5A351 CRC64; MNKPSLQEVL KERILILDGA MGTMIQREDL TADDFGGAEL EGCNETLVIY RPDVIQNIHE QYLAAGADLI ETNTFGATSV VLAEYDIPQL AREINLEAAR LARAAADKYS TPEQPRYVVG AMGPTTKTLS VTGGVTFAEL IASYEEQAIA LIEGKVDALL LETSQDTLNV KAGSIGIRQA FEKTGITLPI MISGTIEPMG TTLAGQNIEA FYISLEHLNP ISIGLNCATG PEFMRDHIRS LSEMSRSAIS CYPNAGLPDE NGQYHESPES LAQKMAAFAE KGWLNIAGGC CGTTPEHISA LKDAMSRFNP RPLTGTHLPA LSGIEPVYIE QDNRPYMVGE RTNVLGSRKF KRLIVEGKYE EASEIARAQV KNGAHIIDIC VQDPDREEAE DMVKFLELVA KKVKVPLMID TTDPAVIDIA LQYSQGKAII NSINLEDGEE KFEKVIPLVH KYGAAVVVGT IDEKGQAITR EDKLKVAKRS YDLLVHKYGV SPEDIIFDTL VFPVGTGDEQ YIGSAKETIE GIRLIKEAMP KVHTILGISN VSFGLPEAGR EVLNSVYLYE CTKAGLDYAI VNTEKLERYA SIPEEERKLA EDLIYRTNDE TLAAFVAAFR DKKVEKKEKV SNLSLEERLA SYVVEGSKEG LIPDLNEALK KYGPLDIING PLMAGMTEVG RLFNNNELIV AEVLQSAEVM KASVAHLEPF MEKNETSVKG KIMLATVKGD VHDIGKNLVE IILSNNGYEI VNLGIKVPPE QIIEAYRREK PDAIGLSGLL VKSAQQMVLT AQDLKNAGID VPIMVGGAAL TRKFTKTRIR PEYDGMVLYA KDAMEGLDLA NKLSDPQQRA EMAKDIEAEM EADAAAPQAV KVMPKLSQGL RSKISTEAPV YIPPDMERHV LRNYPISHIL PYINMQMLLG HHLGLKGSVE QLLKANDPKA VSLKETVDGI LNEAIRSGII QAHAMYRFFP AQGRGNDIII YDPSDHSKIL HTFTFPRQQV EPYLCLADFL KPVDSGIMDY VGFLVVTAGH GVGKLSSQWK DKGDYLRSHA LQAVALETAE GLAERVHHMM RDTWGFPDPA DMTMKQRLGA RYQGIRVSFG YPACPDLEDQ EPLFRLMQPE DIGVALTEGF MMEPEASVSA MVFSHPEAHY FNVDKA // ID G4I1E9_MYCRH Unreviewed; 304 AA. AC G4I1E9; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 29-OCT-2014, entry version 11. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EHB53937.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EHB53937.1}; GN ORFNames=MycrhDRAFT_4400 {ECO:0000313|EMBL:EHB53937.1}; OS Mycobacterium rhodesiae JS60. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=931627 {ECO:0000313|EMBL:EHB53937.1}; RN [1] {ECO:0000313|EMBL:EHB53937.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=JS60 {ECO:0000313|EMBL:EHB53937.1}; 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGIQ01000003; EHB53937.1; -; Genomic_DNA. DR EnsemblBacteria; EHB53937; EHB53937; MycrhDRAFT_4400. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHB53937.1}; KW Transferase {ECO:0000313|EMBL:EHB53937.1}. SQ SEQUENCE 304 AA; 31813 MW; 115D7CB5411B6FCA CRC64; MVFAVPHNTV LIADGGLATE LEARGHDLSD DLWSARLLVD SPDEIVAVHE AFYRAGADIA TTASYQASFD GFAERGFARR EAEQLLVRSV ELARTARDNV DAGGWVAASV GPYGAALANG EEYQGRYGLS VAQLADWHRP RLEVLVSAQP DVLALETVPD IDEAEALAGL VREFGLPAWL SYTIAGGHTR AGQPLEQAFA VAADVPAIVA VGVNCSAPAD VLGAIAVARR VSGKPVIVYP NSGEQWNGPR RTWTGTGAFD ANAATQWAAA GANIIGGCCR VSPADIAAIR RSGPTVSGTP EPCR // ID G4I2Q1_MYCRH Unreviewed; 1249 AA. AC G4I2Q1; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 01-APR-2015, entry version 18. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHB53499.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHB53499.1}; GN ORFNames=MycrhDRAFT_3962 {ECO:0000313|EMBL:EHB53499.1}; OS Mycobacterium rhodesiae JS60. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=931627 {ECO:0000313|EMBL:EHB53499.1}; RN [1] {ECO:0000313|EMBL:EHB53499.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=JS60 {ECO:0000313|EMBL:EHB53499.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AGIQ01000003; EHB53499.1; -; Genomic_DNA. DR EnsemblBacteria; EHB53499; EHB53499; MycrhDRAFT_3962. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHB53499.1}; KW Transferase {ECO:0000313|EMBL:EHB53499.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 258 258 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 778 778 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1249 AA; 137055 MW; 3959B6C5401F3002 CRC64; MSSPELNTFV PNIRPDCTEA LTAVLGRRIM VIDGAMGTAI QRDRPDEAGY RGERFRDWPS DLVGNNDLLT LTQPHIIFGI HREYLEAGAD ILETNTFNAN AVSLSDYGME EFSYELNYAG AALARKACDE FSTPERPRYV AGALGPTTRT ASISPDVNDP GARNVSYDQL VAAYLTAANG LVDGGADLLI VETIFDTLNA KAAIFAIETL FEERGRRWPV IISGTITDAS GRTLSGQVTE AFWNSIRHAK PIAVGLNCAL GAPEMRPYLA EMSRIADIFV SCYPNAGLPN AFGEYDESPK RQAGYVADFV EAGLVNMVGG CCGTTPAHIA EIAKVVEGKP PRDVPQIEVA TRLSGLEPLN ITADSLFVNI GERTNITGSA RFRNLIKAQD YDTALSVALQ QVEVGAQVID INMDEGMIDG VAAMDRFTKL IAAEPDISRV PVMIDSSKWE VIEAGLKSVQ GKPIVNSISM KEGEEKFIRE ARLCRKFGAA VVVMAFDEQG QADNLERRKE ICGRAYRILT EQVGFPAEDI IFDPNCFALA TGIEEHATYG IDFIEACAWI KANLPGVHIS GGISNVSFSF RGNNPVREAI HAVFLFHAIK AGLDMGIVNA GALVPYDSID PELRDRIEDV VLNRREDAAE RLLEIAERFN KSDGPEDSQV AEWRSLPVHE RITHALVKGI DAHVDADTEE LRSEIAAAGG RPIEVIEGPL MDGMNVVGDL FGSGKMFLPQ VVKSARVMKK AVAYLLPFIE AEKEENGTVG SKDTNGTIIM ATVKGDVHDI GKNIVGVVLQ CNNFEVIDLG VMVPAQKILD AAKEHDADII GLSGLITPSL DEMSNFAVEM ERQGLEIPLL IGGATTSRAH TAVKISPRRS GPVVWVKDAS RSVPVAAALL DDKQRPALLE ATEKDYASLR ERHAQKNERP MLTLEKARAN RTPIAWDGYR PPVPAQGLGV REFRDYDLAE LREFIDWQPF FNAWEMKGRF PDILNNPASG EAARKLYDDA QEMLDTLIKE KWLTANGVIG FFPANAVGDD IEVYTDESRT EVCTTLRNLR QQGEHRDGIP NRSLGDFVAP KDTGLADYVG AFAVTAGLGS SEKIAEFKAD HDDYGAILLE SLADRLAEAF AERMHQRVRK EFWGYQPDEQ LDNDALIGEK YVGIRPAPGY PACPEHTEKA TLWTLMDVEE RTGIELTESM AMWPGAAVSG WYFSHPQSQY FVVGRLAQDQ VADYARRKGW TLQEAERWLA PNLGYNPED // ID G4L033_OSCVS Unreviewed; 319 AA. AC G4L033; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 29-APR-2015, entry version 16. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:BAL01414.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:BAL01414.1}; GN Name=mmuM {ECO:0000313|EMBL:BAL01414.1}; GN OrderedLocusNames=OBV_42150 {ECO:0000313|EMBL:BAL01414.1}; OS Oscillibacter valericigenes (strain DSM 18026 / NBRC 101213 / OS Sjm18-20). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Oscillospiraceae; OC Oscillibacter. OX NCBI_TaxID=693746 {ECO:0000313|EMBL:BAL01414.1, ECO:0000313|Proteomes:UP000005219}; RN [1] {ECO:0000313|Proteomes:UP000005219} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18026 / NBRC 101213 / Sjm18-20 RC {ECO:0000313|Proteomes:UP000005219}; 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 ----------------------------------------------------------------------- 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; BAL01414.1; -; Genomic_DNA. DR RefSeq; WP_014120001.1; NC_016048.1. DR RefSeq; YP_004883919.1; NC_016048.1. DR EnsemblBacteria; BAL01414; BAL01414; OBV_42150. DR KEGG; ova:OBV_42150; -. DR KO; K00547; -. DR BioCyc; OVAL693746:GJWX-4276-MONOMER; -. DR Proteomes; UP000005219; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005219}; KW Methyltransferase {ECO:0000313|EMBL:BAL01414.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005219}; KW Transferase {ECO:0000313|EMBL:BAL01414.1}. SQ SEQUENCE 319 AA; 35860 MW; 773ADA4D35281FD4 CRC64; MNSIDEIWKQ KDLVILDGAM ATELERKGLD LNDSLWSARV LAEHPEVIQA VHRDYFVSGA DCSTSASYQA TIPGFMASGY TRREAEELIA RSMTLLLKAR DEWWEEEKTS GRLYPLAAAA VGPYGAYLAN GSEYTGNYSC TEKEYRAFHM PRLQILKDSG AEIFALETMP RLDEALACAG MLEELDCDYW VSFTFRSPRQ ISDGTSVEEI AATLKGFPHL KAVGVNCTPP AFVEGVIRNF RALTSLPICV YPNRGEIYDA VTKTWNGSAD GKTYGDWAQE WYRAGARVIG GCCRTRPEDI RAISDWYENT HRFRRINVK // ID G4M912_9BURK Unreviewed; 358 AA. AC G4M912; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:CCD37641.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CCD37641.1}; GN ORFNames=BKIR_c2_4616 {ECO:0000313|EMBL:CCD37641.1}; OS Candidatus Burkholderia kirkii UZHbot1. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=1055526 {ECO:0000313|EMBL:CCD37641.1}; RN [1] {ECO:0000313|EMBL:CCD37641.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UZHbot1 {ECO:0000313|EMBL:CCD37641.1}; RA Carlier A.; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CCD37641.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UZHbot1 {ECO:0000313|EMBL:CCD37641.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCD37641.1}. 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; CAFE01000117; CCD37641.1; -; Genomic_DNA. DR RefSeq; WP_006998886.1; NZ_HE603793.1. DR EnsemblBacteria; CCD37641; CCD37641; BKIR_c2_4616. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:CCD37641.1}; KW Transferase {ECO:0000313|EMBL:CCD37641.1}. SQ SEQUENCE 358 AA; 38732 MW; 08352469FAEDFF14 CRC64; MQTSSVMTQN AIPNPVRAYT RGAALPALLQ KRILILDGAM GTMIQRYKLD EAAYRGERFK DYDRDIKGNN ELLSITQPQV IREIHEQYLA AGADIIETNT FGATRVAQAD YGMEELAAEM NIESAKLARQ ACDKYATPDK PRFVVGAIGP TPKTASISPD VNDPGALNVT FDELRDAYYE QAKALLDAGC DLFLVETIFD TLNAKAALFA LDQLFEDTGE LVPIMISGTV TDASGRILSG QTVEAFWNSL RHAKPLTFGL NCALGAALMR PYIAELAKLC DTYVSCYPNA GLPNPMSDTG FDETPNLTSG LLKEFATAGL VNIAGGCCGT TPQHIAEIAK ALAEVKPRTF PSQYRDAA // ID G4NF85_MAGO7 Unreviewed; 380 AA. AC G4NF85; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 07-JAN-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EHA47233.1}; GN ORFNames=MGG_04215 {ECO:0000313|EMBL:EHA47233.1}; 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 {ECO:0000313|EMBL:EHA47233.1, ECO:0000313|Proteomes:UP000009058}; RN [1] {ECO:0000313|EMBL:EHA47233.1, ECO:0000313|Proteomes:UP000009058} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958 RC {ECO:0000313|Proteomes:UP000009058}; 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; CM001236; EHA47233.1; -; Genomic_DNA. DR RefSeq; XP_003719600.1; XM_003719552.1. DR EnsemblFungi; MGG_04215T0; MGG_04215T0; MGG_04215. DR GeneID; 2677441; -. DR KEGG; mgr:MGG_04215; -. DR InParanoid; G4NF85; -. DR KO; K00547; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000009058; Chromosome 6. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009058}; KW Methyltransferase {ECO:0000313|EMBL:EHA47233.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000009058}; KW Transferase {ECO:0000313|EMBL:EHA47233.1}. SQ SEQUENCE 380 AA; 40343 MW; E5FCA8FC794A23E0 CRC64; MSDIKILDGG LGTTLEDRFG VVFTHAKPLW SSDLLVSDQE TLQACQREFA AAGADVLLTA TYQVSVEAFA RTKTPEHPDG IAPSSAMLPY LRGAVEIAEK AAAAAAAAAA AAAAAPRNET SAPSPQPAEL ALACGPYGAA MTPGQEYTGA YDAAHSTPDA LSRWHLDRLA LYAAAGEDVP GRCAYVAFET VPNLAEVWAV RDAITRLRQD ASCSRFPSRF WICCVFPHED ERLADGSSVD QVVEAMLAAR GGGENGGAKE SLALPWGIGI NCTKIYKLEG LIKSFERSIS GLKAKGVITN VPALVLYPDG TNGEVYNTTT QKWEAPQVVQ GAGPKTPWDA QLTQIVNDTK SRGVFTSFLV GGCCKANPQN IKDLRNRLKE // ID G4NTM5_BACPT Unreviewed; 296 AA. AC G4NTM5; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 01-APR-2015, entry version 20. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AEP85155.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:AEP85155.1}; GN Name=mmuM {ECO:0000313|EMBL:AEP85155.1}; GN OrderedLocusNames=GYO_0439 {ECO:0000313|EMBL:AEP85155.1}; OS Bacillus subtilis subsp. spizizenii (strain TU-B-10). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1052585 {ECO:0000313|EMBL:AEP85155.1, ECO:0000313|Proteomes:UP000002651}; RN [1] {ECO:0000313|EMBL:AEP85155.1, ECO:0000313|Proteomes:UP000002651} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TU-B-10 {ECO:0000313|EMBL:AEP85155.1, RC ECO:0000313|Proteomes:UP000002651}; 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; AEP85155.1; -; Genomic_DNA. DR RefSeq; WP_014112510.1; NC_016047.1. DR RefSeq; YP_004875787.1; NC_016047.1. DR EnsemblBacteria; AEP85155; AEP85155; GYO_0439. DR KEGG; bst:GYO_0439; -. DR KO; K00547; -. DR BioCyc; BSUB1052585:GJWW-440-MONOMER; -. DR Proteomes; UP000002651; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002651}; KW Methyltransferase {ECO:0000313|EMBL:AEP85155.1}; KW Transferase {ECO:0000313|EMBL:AEP85155.1}. SQ SEQUENCE 296 AA; 32621 MW; 79C32CC5653B733A CRC64; MATELERKGC DLNDSLWSAK ILMEEPDLIK QVHTDYFAAG ADCAITASYQ STFEGFAARG LSEAKARRLI EMSVSIAAEA RDEFWALEEN RLNRPKPIIA ASIGPYGAYL ADGSEYRGHY GISEDELVEF HRPRMKALIE AGADVLACET IPCLTEAKAI VRLLKEFPET YAWISFSAKD GLHISDGTPA AGCASWLDEH RQIAALGINC TPLQHIPSLI EELKKHTSKP IIAYPNSGEQ YDPETKTWNG AACAEPYGQS ARMWHEKGAK LIGGCCRTKP EDIKEIAAWA RSLKTT // ID G4Q2I1_ACIIR Unreviewed; 320 AA. AC G4Q2I1; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:AEQ22637.1}; GN Name=mmuM {ECO:0000313|EMBL:AEQ22637.1}; GN OrderedLocusNames=Acin_1415 {ECO:0000313|EMBL:AEQ22637.1}; OS Acidaminococcus intestini (strain RyC-MR95). OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; OC Acidaminococcaceae; Acidaminococcus. OX NCBI_TaxID=568816 {ECO:0000313|EMBL:AEQ22637.1, ECO:0000313|Proteomes:UP000007093}; RN [1] {ECO:0000313|EMBL:AEQ22637.1, ECO:0000313|Proteomes:UP000007093} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RyC-MR95 {ECO:0000313|EMBL:AEQ22637.1, RC ECO:0000313|Proteomes:UP000007093}; 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; AEQ22637.1; -; Genomic_DNA. DR RefSeq; WP_009015456.1; NC_016077.1. DR RefSeq; YP_004896777.1; NC_016077.1. DR EnsemblBacteria; AEQ22637; AEQ22637; Acin_1415. DR KEGG; ain:Acin_1415; -. DR KO; K00547; -. DR BioCyc; AINT568816:GHMB-1412-MONOMER; -. DR Proteomes; UP000007093; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007093}; KW Methyltransferase {ECO:0000313|EMBL:AEQ22637.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007093}; KW Transferase {ECO:0000313|EMBL:AEQ22637.1}. SQ SEQUENCE 320 AA; 35221 MW; F0F65017E0682BA8 CRC64; MRQTLAKILE KKQICVIDGS MGTALEHLGA NLNNSLWTAR VLLDQPELVK KVHLDYFHAG ADAGITCSYQ ATIPGLMANG LSEKEAEDLI VRSVKVFQEA RNEWWEKEGK AADRAYPMCL AGIGPYGAYL ADGSEYKGHY GIPDAALHDF HQRRAELLWE AGADVLLFET QPSLGEAKIE AAIAERLGAD YWISFSCKDG LHINEGDLIR DCAAAFRSGY PRLRALGVNC TKPEYLESLI KELGKETDLP IVVYPNSGET YDPVTKTWNG KGDGHSFKDY ARTYMEAGAR AVGGCCTTVS EHIVAVAKAR EEFLDRQSKA // ID G4Q6D8_ACIIR Unreviewed; 803 AA. AC G4Q6D8; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AEQ23428.1}; GN Name=metH {ECO:0000313|EMBL:AEQ23428.1}; GN OrderedLocusNames=Acin_2232 {ECO:0000313|EMBL:AEQ23428.1}; OS Acidaminococcus intestini (strain RyC-MR95). OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; OC Acidaminococcaceae; Acidaminococcus. OX NCBI_TaxID=568816 {ECO:0000313|EMBL:AEQ23428.1, ECO:0000313|Proteomes:UP000007093}; RN [1] {ECO:0000313|EMBL:AEQ23428.1, ECO:0000313|Proteomes:UP000007093} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RyC-MR95 {ECO:0000313|EMBL:AEQ23428.1, RC ECO:0000313|Proteomes:UP000007093}; 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; AEQ23428.1; -; Genomic_DNA. DR RefSeq; WP_009015182.1; NC_016077.1. DR RefSeq; YP_004897568.1; NC_016077.1. DR EnsemblBacteria; AEQ23428; AEQ23428; Acin_2232. DR KEGG; ain:Acin_2232; -. DR KO; K00548; -. DR BioCyc; AINT568816:GHMB-2233-MONOMER; -. DR Proteomes; UP000007093; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007093}; KW Methyltransferase {ECO:0000313|EMBL:AEQ23428.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007093}; KW Transferase {ECO:0000313|EMBL:AEQ23428.1}. SQ SEQUENCE 803 AA; 84973 MW; 6C52B4725D3AC03C CRC64; MEIRERLEKE RLFFDGGMGT MLQSAGLMPG ELPELWNLSH ADVIQGVHEA YIRAGAQIIK TNTFGCNGLK FGKAHGTPAV STLVTAAVKL AQKAFQACGE KGCVALDLGP TGKLLQPYGD LPFEEAVSLY AEAVEAGKKA GADLVLIETM SDTYEAKAAI LAVKEHSNLP FVVTFTFDEE GKLLSGADVE TAMIVASSLG ASAVGFNCGL GPKEISRLVP RALAATDLPL VVNPNAGLPV THDGVTQFEV GSEEFAATML EFAPQTALLG GCCGTTPQHI KALVESCAEL PPPEKRNGAP ECITGYGAPV CFDRMPVIIG ERINPTGKKR LKEALKAGDM DYVCQLALEQ IDKGAQVLDV NVGVPGIDEP ALLEKAMRTL QSITPLPLQI DTSDLKAMER ALRLYNGRPL LNSVNGKTSS LSSVLPLAKK YGAMLVGLCL DDDGIAESLE GRLKSARRVI DGAKKAGLSE KALLLDPLAM TISTGGQNAQ IALSIIAALK KAGLKTVMGV SNISFGLPHR DAVNSAFFAS AMQLGLSAGI INPNSAPMME TYLAYGALSG YDTSCKAYVS YFADLPTEKR EPHVPAAKDS GEQGRYGLDE AIEKGLISPA ETAVAALLDE GRDALSIINE YMIPALNRVG DAFEKKTLFL PQLLMSADAA KAGFEIIKKA MFQKGADRGK GDPVIVATVK GDIHDIGKNI VKVLLENYGY DVIDLGKDVP PEAIVEKTLE RDVKLVGLSA LMTTTLGSMA ETIRQLREKA PGCRVIVGGA VMTKEYAEEL GADAYAGNAV AAVSYANALF RKK // ID G4QLU3_GLANF Unreviewed; 353 AA. AC G4QLU3; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:AEP30433.1}; GN OrderedLocusNames=GNIT_2336 {ECO:0000313|EMBL:AEP30433.1}; OS Glaciecola nitratireducens (strain JCM 12485 / KCTC 12276 / FR1064). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Glaciecola. OX NCBI_TaxID=1085623 {ECO:0000313|EMBL:AEP30433.1, ECO:0000313|Proteomes:UP000009282}; RN [1] {ECO:0000313|EMBL:AEP30433.1, ECO:0000313|Proteomes:UP000009282} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 12485 / KCTC 12276 / FR1064 RC {ECO:0000313|Proteomes:UP000009282}; RX PubMed=22123761; DOI=10.1128/JB.06296-11; RA Bian F., Qin Q.L., Xie B.B., Shu Y.L., Zhang X.Y., Yu Y., Chen B., RA Chen X.L., Zhou B.C., Zhang Y.Z.; RT "Complete genome sequence of seawater bacterium Glaciecola RT nitratireducens FR1064T."; RL J. Bacteriol. 193:7006-7007(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; CP003060; AEP30433.1; -; Genomic_DNA. DR RefSeq; WP_014109306.1; NC_016041.1. DR RefSeq; YP_004872426.1; NC_016041.1. DR EnsemblBacteria; AEP30433; AEP30433; GNIT_2336. DR KEGG; gni:GNIT_2336; -. DR BioCyc; GNIT1085623:GJU2-2336-MONOMER; -. DR Proteomes; UP000009282; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009282}; KW Reference proteome {ECO:0000313|Proteomes:UP000009282}. SQ SEQUENCE 353 AA; 38816 MW; 186672D986F2428B CRC64; MSKTTNNLDL LTSIARERIL ILDGAMGTMI QKCQLDEAEY RGEQYKNWHC DVKGNNDLLS ITQPDIIRNI HREYLAAGAD IIETNTFNAT SISMSDYDMQ DESRQINLSA AKLAREAADE YSAKTPDKPR FVAGVIGPTS RTASISPDVN DPGKRNVHFD ELVEAYKEST HALIEGKVDI ILVETIFDTL NAKAAVYAVE EVFEELGIIL PVMISGTITD ASGRTLSGQT SEAFYYSMRH VNPFSVGLNC ALGPDLLRQY VAEIARIAQC NVSAHPNAGL PNEFGEYDME AEELSEHLKE WGQSGLVNIL GGCCGSTPEH IRQVAQAVSG LPPRQIPDIE VKMRLSGLEP FVH // ID G4R7K6_PELHB Unreviewed; 1259 AA. AC G4R7K6; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 29-APR-2015, entry version 25. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AEQ52307.1}; GN OrderedLocusNames=KKY_2298 {ECO:0000313|EMBL:AEQ52307.1}; OS Pelagibacterium halotolerans (strain JCM 15775 / CGMCC 1.7692 / B2). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Hyphomicrobiaceae; Pelagibacterium. OX NCBI_TaxID=1082931 {ECO:0000313|EMBL:AEQ52307.1, ECO:0000313|Proteomes:UP000008850}; RN [1] {ECO:0000313|EMBL:AEQ52307.1, ECO:0000313|Proteomes:UP000008850} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 15775 / CGMCC 1.7692 / B2 RC {ECO:0000313|Proteomes:UP000008850}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP003075; AEQ52307.1; -; Genomic_DNA. DR RefSeq; WP_014131456.1; NC_016078.1. DR RefSeq; YP_004900057.1; NC_016078.1. DR EnsemblBacteria; AEQ52307; AEQ52307; KKY_2298. DR KEGG; phl:KKY_2298; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; PHAL1082931:GJXT-2293-MONOMER; -. DR Proteomes; UP000008850; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008850}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEQ52307.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008850}; KW Transferase {ECO:0000313|EMBL:AEQ52307.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 273 273 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 336 336 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 337 337 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 785 785 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1259 AA; 138168 MW; E6E9400821C359AE CRC64; MGGMGEGGAI AVDALQPGSA PVRTAKEGEE ILAALTAAAR ERILILDGAM GTMIQLEKLS EENFRGERFA DWPKPLQGNN DLLVITEPKI IEDIHFAYAM AGADLLETNT FSGTTIAQAD YGMEALAYEL NVAGAQAAKR AAIRAEAEDG KRRFVAGAVG PTNRTASISP DVNNPGFRAV SFDQLRIAYG EQIEGLIDGG SDLILIETIF DTLNAKAAVF AAEEVFEKKG IRLPVMISGT ITDLSGRTLS GQTPTAFWYS LRHAKPFTIG LNCALGANAM RAHLGEISDI ADTLVCAYPN AGLPNEFGEY DESPEFMASQ IEGFARDGFL NIVGGCCGST PEHIAAIAQA VSKYPPRAVP QIEPRLRLSG LEPFTLTDDI PFVNVGERTN VTGSARFKKL ITAGDYATAL DVARDQVENG AQIIDINMDE GLIDSQQVMV EYLNLVASEP DIARVPVMID SSKWEVIEAG LKCVQGKAIV NSISMKEGED KFREHARLCR LYGAAVVVMA FDEDGQADTK ERKVEICTRA YRILVDEVGF PPEDIIFDPN IFAVATGIEE HDNYGVDFIE ATKEITETLP HVHISGGVSN LSFSFRGNEP VREAMHAVFL YHAIKVGMDM GIVNAGQLAV YESIDPELRE ACEDVVLNRR SDSTERMLDL AERYKGQGGK EAKAKDLSWR EKPVGERISH ALVNGITEYI EADTEEARQS FARPLHVIEG PLMDGMNIVG ELFGAGKMFL PQVVKSARVM KQAVAYLLPF MEAEADGQRQ SAGKILMATV KGDVHDIGKN IVGVVLACNN YEIIDLGVMV PTQKILDTAR EQKVDVIGLS GLITPSLDEM VHVAAEMERE GFDIPLMIGG ATTSRVHTAV KINPRYNRGS TIYVKDASLA VNVVSKLLSK EAANDYVKTI RQEYETVAEK HRKGEADKKR ISLAAARDNA FKPDWSTYTP KAPSFLGTKT FQDWDLGELA KYIDWTPFFQ AWEFKGVYPK ILEDERQGEA ARQLFADAKV MLKRIIDENW FTPKAVVGFW PANRVGDDVQ LFTDESRSNE LAKFFTLRQQ LGKSGDKANL ALADFMAEPG TPDYIGGFCV TAGFEEIAIA DKFDEENDNY SSILVKALAD RFAEAFAERL HEMVRTELWG YAEESYAPEE LIGEPYQGIR PAPGYPAQPD HTEKTTLFEL LDVEAEIGVK LTESYAMWPG SSVSGLYFAH PDSYYFGVAK VERDQVEDYA RRKGMAIEDV ERWLGPVLNY IPGSEKAAG // ID G4RFX2_PELHB Unreviewed; 313 AA. AC G4RFX2; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Putative homocysteine S-methyltransferase {ECO:0000313|EMBL:AEQ51015.1}; GN OrderedLocusNames=KKY_980 {ECO:0000313|EMBL:AEQ51015.1}; OS Pelagibacterium halotolerans (strain JCM 15775 / CGMCC 1.7692 / B2). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Hyphomicrobiaceae; Pelagibacterium. OX NCBI_TaxID=1082931 {ECO:0000313|EMBL:AEQ51015.1, ECO:0000313|Proteomes:UP000008850}; RN [1] {ECO:0000313|EMBL:AEQ51015.1, ECO:0000313|Proteomes:UP000008850} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 15775 / CGMCC 1.7692 / B2 RC {ECO:0000313|Proteomes:UP000008850}; 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; AEQ51015.1; -; Genomic_DNA. DR RefSeq; WP_014130164.1; NC_016078.1. DR RefSeq; YP_004898765.1; NC_016078.1. DR EnsemblBacteria; AEQ51015; AEQ51015; KKY_980. DR KEGG; phl:KKY_980; -. DR OMA; CCGTDHR; -. DR BioCyc; PHAL1082931:GJXT-977-MONOMER; -. DR Proteomes; UP000008850; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008850}; KW Methyltransferase {ECO:0000313|EMBL:AEQ51015.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008850}; KW Transferase {ECO:0000313|EMBL:AEQ51015.1}. SQ SEQUENCE 313 AA; 33451 MW; B9132D1E2E23C82F CRC64; MSKYRQALPQ ADGRLFLSDG GMETALIFLQ GVDLPQFAAF VLLESESGRA ELVRYYEKFL PIARDRGVGF LLDTATWRAS LDWGRSLGFD ADRLTAVNIA AVELIAGLRG RWETPTTPIV LNGAIGPRGD GYKAGRMDVA EARDYHAFQV GIFAGTQVDM VSAITMNTVN EAVGIALAAK AADVPCVVSF TVETDGKLVD GTTLRAAIEA TEEATGASPA YYMVNCAHPT HFEQALERDE AWVGRIRGIR ANASAKSHSE LDDSDTLDIG DIVGLSGHYK ALTSAFPSMR VLGGCCGTDH RHLAAIGEAV APN // ID G4SZ71_META2 Unreviewed; 1223 AA. AC G4SZ71; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 27-MAY-2015, entry version 31. DE SubName: Full=Methionine synthase (5-methyltetrahydrofolate--homocysteine methyltransferase) (Methionine synthase, vitamin-B12 dependent) (MS) {ECO:0000313|EMBL:CCE22221.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CCE22221.1}; GN Name=metH {ECO:0000313|EMBL:CCE22221.1}; GN OrderedLocusNames=MEALZ_0523 {ECO:0000313|EMBL:CCE22221.1}; 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 {ECO:0000313|Proteomes:UP000008315}; RN [1] {ECO:0000313|Proteomes:UP000008315} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z RC {ECO:0000313|Proteomes:UP000008315}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; FO082060; CCE22221.1; -; Genomic_DNA. DR RefSeq; WP_014147029.1; NC_016112.1. DR RefSeq; YP_004915820.1; NC_016112.1. DR GeneID; 11362578; -. DR KEGG; mah:MEALZ_0523; -. DR KO; K00548; -. DR Proteomes; UP000008315; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008315}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CCE22221.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008315}; KW Transferase {ECO:0000313|EMBL:CCE22221.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 246 246 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1223 AA; 136630 MW; 4894BFD20B91F439 CRC64; MSKLENFKKR LSQSILFLDG AMGTMIQSYK LEEKDYRGKR FSDWTVDLKG NNDLLSLTQP DIIKAIHCAY LDVGCDIIET NTFNATQIAM ADYQMESLAY EINLESARIA RQAADEYSQK TPEKPRFVAG ILGPTNRTAS MSPDVNDPGF RNIDFDTLVD AYTEAMRGLI DGGVDIILIE TVFDTLNAKA AIFAVDQYFE AIGYKLPVMI SGTITDASGR TLSGQTVAAF WNSLSHIEPI SFGFNCALGA KELRQHIEEL SSIADTHVSA HPNAGLPNEF GEYDESPEDM ALELADWAAN GYLNIIGGCC GTSPEHIKAI VEAVKQYPPR VVPVIEKQCR LAGLEPMNIG SDSLFVNVGE RTNVTGSAKF KRLVVEGDFE TALEVAKDQV ENGAQIIDIN MDEGMLESKE AMVRFLSLIA AEPDIAKVPI MLDSSKWDII EAGLKCIQGK GIVNSISLKE GEEAFIQHAK LIRRYGAAAI VMAFDEQGQA DTRDRKVEIC SRAYRILTEQ LNFPAEDIIF DPNIFAIATG IDEHNNYGMD FIEATREIKR TLPHALISGG VSNVSFSFRG NNPVREAIHA VFLYHAIKAG MDMGIVNAGQ LAIYEDIPLE LRDAVEDVVL NRNDHATERL LELAEKYRGD GSTAAKPEEL EWRSWPVTKR LEHALVKGIA DFIDEDTEQA RQEAEKPLHV IEGALMDGMN VVGDLFGAGK MFLPQVVKSA RVMKKAVAYL MPFMEAEQDG EMQTNGKILM ATVKGDVHDI GKNIVGVVLQ CNNFQVIDLG VMVPAEKILQ TARDEKVDII GLSGLITPSL DEMVHMAKEM ERQGFDIPLM IGGATTSRAH TAVKIEPNYH GPVVYVADAS RSVGVASHLV SDDSKEAFTQ KIKEEYKEVR ERHQGRKAKT KQHSIEQARR NKFNWTDFEP VKPTFLGNKV IDRFPLDTLV WYIDWTPFFH TWELAGKYPN IFEDRVVGEE ARKLFDDAQV MLKKIINEEW LQARAVIGFY PANSDGDDII LYKDDSRLEK REILHHLRQQ SVKAPGRPNY CLSDFIAPID SGKIDYLGGF AVTTGIGIEA KLEEFEKDHD DYSSIMLKAL ADRLAEAFAE YMHEAVRKDF WGYAKDEQYR NDELISESYQ GIRPAPGYPA CPDHTEKSKL FELLNVTATT GIELTESYAM YPASAVSGWY FSHPEAQYFN VGKIDHDQLE DYARRKGIAK EVAERWLSAH LHH // ID G4T982_PIRID Unreviewed; 218 AA. AC G4T982; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 07-JAN-2015, entry version 18. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CCA67856.1}; GN ORFNames=PIIN_01680 {ECO:0000313|EMBL:CCA67856.1}; OS Piriformospora indica (strain DSM 11827). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; OC Agaricomycetes; Sebacinales; Sebacinales group B; Piriformospora. OX NCBI_TaxID=1109443 {ECO:0000313|EMBL:CCA67856.1, ECO:0000313|Proteomes:UP000007148}; RN [1] {ECO:0000313|EMBL:CCA67856.1, ECO:0000313|Proteomes:UP000007148} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11827 {ECO:0000313|EMBL:CCA67856.1, RC ECO:0000313|Proteomes:UP000007148}; RX PubMed=22022265; DOI=10.1371/journal.ppat.1002290; RA Zuccaro A., Lahrmann U., Gueldener U., Langen G., Pfiffi S., RA Biedenkopf D., Wong P., Samans B., Grimm C., Basiewicz M., Murat C., RA Martin F., Kogel K.-H.; RT "Endophytic life strategies decoded by genome and transcriptome RT analyses of the mutualistic root symbiont Piriformospora indica."; RL PLoS Pathog. 7:E1002290-E1002290(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. {ECO:0000313|EMBL:CCA67856.1}. 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; CAFZ01000021; CCA67856.1; -; Genomic_DNA. DR InParanoid; G4T982; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000007148; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007148}; KW Reference proteome {ECO:0000313|Proteomes:UP000007148}. SQ SEQUENCE 218 AA; 23838 MW; 1CFD9FED9B88CD62 CRC64; MDGAMASELE RYGVEMPKDA TPNLWSSNAL LSDIESVKRV HASYLHAGAK VLSTCTYQLT LQAAGSEQKA RILMKRAINA LHEATRAYNM VNERLLSLGP AATIHPSGAE YSGEYRGPFD PKSATSTAAL TDFHLSRLRL VEREDWDKLD GILFETVPLV TELDAIRAAV GHFQIESPTF SKPIYISMVF PNGRLPEWPQ SVSVVDGMAS IPSCAGSR // ID G4U958_NEUT9 Unreviewed; 361 AA. AC G4U958; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 07-JAN-2015, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EGZ76831.1}; GN ORFNames=NEUTE2DRAFT_99036 {ECO:0000313|EMBL:EGZ76831.1}; OS Neurospora tetrasperma (strain FGSC 2509 / P0656). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae; OC Neurospora. OX NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ76831.1, ECO:0000313|Proteomes:UP000008513}; RN [1] {ECO:0000313|EMBL:EGZ76831.1, ECO:0000313|Proteomes:UP000008513} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513}; 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; GL890999; EGZ76831.1; -; Genomic_DNA. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000008513; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008513}; KW Methyltransferase {ECO:0000313|EMBL:EGZ76831.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008513}; KW Transferase {ECO:0000313|EMBL:EGZ76831.1}. SQ SEQUENCE 361 AA; 39754 MW; 70D5C9E9FE83FC27 CRC64; MATPIPVHIL DGGMGTTLED MHDITFSFET PLWSSHLLVS GEEDKLSDCH EAFKQAGANI ISTATYQISI NGFAATKSPK SGTLDVEREG IDKEEIPRFL SRAVVLAANA AGTEGKVALS LGPYGATMIP STEYSGRYDP EHQDVQALEK WHKERLDLFK DVDPKQVNYI AFETVPRLDE IVAIRNLLSA DHIPTSLRGR PVWISSPYPN DDGKLPDGST VEEVVKAVLT HREGLETPWG IGINCTKVEK LDSLVKKYED AIQTCIKNGE QMAWPSLVLY PDGTNGEVYN TATKTWELSP GHKQSEAPWE TVLANVVEAA RQRGTWKSIV VGGCCKASPE HIRRLRRTLQ DYGHMSTSLA A // ID G4VBH2_SCHMA Unreviewed; 360 AA. AC G4VBH2; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 07-JAN-2015, entry version 16. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:CCD77246.1}; GN ORFNames=Smp_210320 {ECO:0000313|EMBL:CCD77246.1}; OS Schistosoma mansoni (Blood fluke). OC Eukaryota; Metazoa; Platyhelminthes; Trematoda; Digenea; Strigeidida; OC Schistosomatoidea; Schistosomatidae; Schistosoma. OX NCBI_TaxID=6183 {ECO:0000313|Proteomes:UP000008854}; RN [1] {ECO:0000313|Proteomes:UP000008854} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Puerto Rican {ECO:0000313|Proteomes:UP000008854}; RX PubMed=22253936; DOI=10.1371/journal.pntd.0001455; RA Protasio A.V., Tsai I.J., Babbage A., Nichol S., Hunt M., Aslett M.A., RA De Silva N., Velarde G.S., Anderson T.J., Clark R.C., Davidson C., RA Dillon G.P., Holroyd N.E., LoVerde P.T., Lloyd C., McQuillan J., RA Oliveira G., Otto T.D., Parker-Manuel S.J., Quail M.A., Wilson R.A., RA Zerlotini A., Dunne D.W., Berriman M.; RT "A systematically improved high quality genome and transcriptome of RT the human blood fluke Schistosoma mansoni."; RL PLoS Negl. Trop. Dis. 6:E1455-E1455(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; HE601625; CCD77246.1; -; Genomic_DNA. DR EnsemblMetazoa; Smp_210320.1; Smp_210320.1:pep; Smp_210320. DR InParanoid; G4VBH2; -. DR Proteomes; UP000008854; Chromosome 2. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008854}; KW Reference proteome {ECO:0000313|Proteomes:UP000008854}. SQ SEQUENCE 360 AA; 39852 MW; 78ABEEB7EE551F2E CRC64; MCKVNSELVS QWLTEIRVLD GGFGTESQKL SNLQIDGHLA WSSRLLMDDP ELVVKIHKSF LRAGCDVIST NTYQAAPSTL GKALGISIGE AKNLMHTAVH LAQRAREEEN NSVTASEFQR KLPVLIAGSL GPYGACAADG SEYTGSYANE VSFNELVEFH LSRAKILLES GVDFIAWETV PLLKEVSSIC EVMRRLPSAY CWISVSSPDG EKTSGGDLLA SVACEVAKCE QVFGVGVNCN IPHDCIGKGL ANLNSQTCKE SENTSSKLIL FYANDGQLWI PNDGDKKRGH FVNYSQYNHD SWFQNTIQWA KRRETSDDEH LHYSVNDKPP LAQWVGGCCN VRPECIRRLA KWMKPDEFIS // ID G4Z6R3_PHYSP Unreviewed; 333 AA. AC G4Z6R3; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 01-APR-2015, entry version 17. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EGZ20329.1}; GN ORFNames=PHYSODRAFT_488060 {ECO:0000313|EMBL:EGZ20329.1}; OS Phytophthora sojae (strain P6497) (Soybean stem and root rot agent) OS (Phytophthora megasperma f. sp. glycines). OC Eukaryota; Stramenopiles; Oomycetes; Peronosporales; Phytophthora. OX NCBI_TaxID=1094619 {ECO:0000313|Proteomes:UP000002640}; RN [1] {ECO:0000313|EMBL:EGZ20329.1, ECO:0000313|Proteomes:UP000002640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P6497 {ECO:0000313|EMBL:EGZ20329.1}; RX PubMed=16946064; DOI=10.1126/science.1128796; RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H.Y., Aerts A., RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J., RA Damasceno C.M.B., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L., RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., RA Huang W., Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., RA Lee M.-K., McDonald W.H., Medina M., Meijer H.J.G., Nordberg E.K., RA Maclean D.J., Ospina-Giraldo M.D., Morris P.F., Phuntumart V., RA Putnam N.H., Rash S., Rose J.K.C., Sakihama Y., Salamov A.A., RA Savidor A., Scheuring C.F., Smith B.M., Sobral B.W.S., Terry A., RA Torto-Alalibo T.A., Win J., Xu Z., Zhang H., Grigoriev I.V., RA Rokhsar D.S., Boore J.L.; RT "Phytophthora genome sequences uncover evolutionary origins and RT mechanisms of pathogenesis."; RL Science 313:1261-1266(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; JH159153; EGZ20329.1; -; Genomic_DNA. DR RefSeq; XP_009523046.1; XM_009524751.1. DR GeneID; 20656231; -. DR KEGG; psoj:PHYSODRAFT_488060; -. DR InParanoid; G4Z6R3; -. DR Proteomes; UP000002640; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002640}; KW Reference proteome {ECO:0000313|Proteomes:UP000002640}. SQ SEQUENCE 333 AA; 36324 MW; A1399319A751593D CRC64; MSSSSSALTG LQQLLADKSR VVVLDGGFAT ELEKDPRVDL SASSLWSASL LLEKNAHLQS VVVDAHKTYF LAGADVATTA SYQASVDGFK REGVTAIEDV EKLFAKSIDL GVQARDAAWS ELDQTKRIKP LVGASIGCYG AALADGSEYR GDYGMTKEEL VAWHKHRFAY FTNYAPADFL ICETIPCLVE VEAFVDLLNE FPTAHAIVAV ACRNGTELNS GEPIARMTEV LSKLKNPSQL LAIGINCTPP QHVESLLRKL DAAAWPKAVY PNSGEGWDGV NKKWLPADST GGPSSWEEFL PKWYDAGARI FGGCCRTSPD DIRAIREFFE RRQ // ID G4Z7L1_PHYSP Unreviewed; 1195 AA. AC G4Z7L1; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Putative methyltetrahydrofolate-homocysteine S-methyltransferase {ECO:0000313|EMBL:EGZ21051.1}; GN ORFNames=PHYSODRAFT_313428 {ECO:0000313|EMBL:EGZ21051.1}; OS Phytophthora sojae (strain P6497) (Soybean stem and root rot agent) OS (Phytophthora megasperma f. sp. glycines). OC Eukaryota; Stramenopiles; Oomycetes; Peronosporales; Phytophthora. OX NCBI_TaxID=1094619 {ECO:0000313|Proteomes:UP000002640}; RN [1] {ECO:0000313|EMBL:EGZ21051.1, ECO:0000313|Proteomes:UP000002640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P6497 {ECO:0000313|EMBL:EGZ21051.1}; RX PubMed=16946064; DOI=10.1126/science.1128796; RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H.Y., Aerts A., RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J., RA Damasceno C.M.B., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L., RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., RA Huang W., Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., RA Lee M.-K., McDonald W.H., Medina M., Meijer H.J.G., Nordberg E.K., RA Maclean D.J., Ospina-Giraldo M.D., Morris P.F., Phuntumart V., RA Putnam N.H., Rash S., Rose J.K.C., Sakihama Y., Salamov A.A., RA Savidor A., Scheuring C.F., Smith B.M., Sobral B.W.S., Terry A., RA Torto-Alalibo T.A., Win J., Xu Z., Zhang H., Grigoriev I.V., RA Rokhsar D.S., Boore J.L.; RT "Phytophthora genome sequences uncover evolutionary origins and RT mechanisms of pathogenesis."; RL Science 313:1261-1266(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; JH159153; EGZ21051.1; -; Genomic_DNA. DR RefSeq; XP_009523768.1; XM_009525473.1. DR GeneID; 20643602; -. DR KEGG; psoj:PHYSODRAFT_313428; -. DR InParanoid; G4Z7L1; -. DR KO; K00548; -. DR Proteomes; UP000002640; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002640}; KW Methyltransferase {ECO:0000313|EMBL:EGZ21051.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002640}; KW Transferase {ECO:0000313|EMBL:EGZ21051.1}. SQ SEQUENCE 1195 AA; 132849 MW; A5FC6B382496F72D CRC64; MRSDVTAAEV ALLQRPFVRG ESDIFAYLTA LMKQRTLIFD GGMGTMIQTH KFTEEDFRGE RFQDSPCLVK GNNDLLSITQ PQVIKDIHKQ YMQIGRAQLI GTNTFSGTTI AQADYQMEHL VYELNYESAR LAREAADEVT ALDPLRPRFV AGSIGPTNRT LSISPNVEDP GFRNVTFDEL VDAYYTQVEG LVDGGSDILL VETIFDTLNA KAAVFAINKY QEATGKKLPL FISGTIVDMS GRTLSGQTTE AFYVSLRHSK PFCIGLNCAL GANQMKPFLQ RLSNVAECFV SVYANAGLPN AMGGYDDTPA MMAEYCEEFS KDRLINMMGG CCGTTPQHIE AIAIMAAKYE PRPLPELKEP FMWLSGLEDM IVTKERFSFL NVGERCNISG SLRFKRLIMK GDYGTAMDVA RQQVEDGAMV IDVNVDDGML DGVAAMERFL KIAVTEPDVA KVPFMVDSSK FHIVEAGLKC VQGKCIVNSI SLKVGKELFM EHARIVKSHG AAVVVMAFDE EGQAATEAEK VRICKRSYDI LVNEVGFPPE DIIFDPNILT VATGMEEHNN YGVDFINACR VIKEQNPYCG GAVAGGGNKQ EWRTKPIGER LTHALVKGIS EFIDQDVEEM RKVAEKPLDV IEGPLMDGMN VVGQLFGSGK MFLPQVIKSA RVMKKAVAYL LPFMEEEKNQ RRLANTANGI ANEEEDEDSQ YAGKVLIATV KGDVHDIGKN IVGVVLGCNN YKIIDLGVMV PCEDILAAAK EHNVDVIGLS GLITPSLDEM VYVAREMNKA GLKIPLIVGG ATTSKMHAAV KIAPHYSTPE HPVMHVLDAS RSVVVVGNLL RQDEERDEFV EEVMEEYEEM REDYYASLDD IKLISFGDAK AKSYQIDYVA KPPFEKINRV GLHVIEDLPL EDLVPFIDWN PFFQTWELRG RYPNRGYPKI FDDETVGAEA RKVFDEAQKL LQEIMDKKLL RVRGVSGIFP AYREGEDVIV CDPKNPEQEI SKFCMLRQQA EKETSDPYMS LADFIAPKGV GGQDYVGGFA VGVFGVEEMA AKFEADHDDF NKIMSQAIGD RLAEAFAEYI HREMRVKDWG YAADEVLDKE DLLKVKYDGI RPAPGYPSQP DHTEKRALWD LLRADELIGL SLTDSYMMLP GSAVSALCFA HPDSQYFAVG KIGKDQVVEY AKRKGQTLEE TERWLAPILG YDRSA // ID G4ZCR4_PHYSP Unreviewed; 317 AA. AC G4ZCR4; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 01-APR-2015, entry version 17. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EGZ17796.1}; GN ORFNames=PHYSODRAFT_498363 {ECO:0000313|EMBL:EGZ17796.1}; OS Phytophthora sojae (strain P6497) (Soybean stem and root rot agent) OS (Phytophthora megasperma f. sp. glycines). OC Eukaryota; Stramenopiles; Oomycetes; Peronosporales; Phytophthora. OX NCBI_TaxID=1094619 {ECO:0000313|Proteomes:UP000002640}; RN [1] {ECO:0000313|EMBL:EGZ17796.1, ECO:0000313|Proteomes:UP000002640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P6497 {ECO:0000313|EMBL:EGZ17796.1}; RX PubMed=16946064; DOI=10.1126/science.1128796; RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H.Y., Aerts A., RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J., RA Damasceno C.M.B., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L., RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., RA Huang W., Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., RA Lee M.-K., McDonald W.H., Medina M., Meijer H.J.G., Nordberg E.K., RA Maclean D.J., Ospina-Giraldo M.D., Morris P.F., Phuntumart V., RA Putnam N.H., Rash S., Rose J.K.C., Sakihama Y., Salamov A.A., RA Savidor A., Scheuring C.F., Smith B.M., Sobral B.W.S., Terry A., RA Torto-Alalibo T.A., Win J., Xu Z., Zhang H., Grigoriev I.V., RA Rokhsar D.S., Boore J.L.; RT "Phytophthora genome sequences uncover evolutionary origins and RT mechanisms of pathogenesis."; RL Science 313:1261-1266(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; JH159154; EGZ17796.1; -; Genomic_DNA. DR RefSeq; XP_009526854.1; XM_009528559.1. DR GeneID; 20657553; -. DR KEGG; psoj:PHYSODRAFT_498363; -. DR InParanoid; G4ZCR4; -. DR Proteomes; UP000002640; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002640}; KW Reference proteome {ECO:0000313|Proteomes:UP000002640}. SQ SEQUENCE 317 AA; 34926 MW; E7D44E39F1168A55 CRC64; MLRRVSTAAQ RSTKMPLLDG GTGEELFARG LPDDRRIWSA TALVHGQHHA LLREVHTSFL AVGADCITCN NYGVTPGVGF SDEEIVRLTA IVGRVAREAC DQWMESATDM TRQKAKVCGS LPPLLKSYRA DKVPEHEEGV RLYAMIAKAL KPFVDCYLAE TLSSVQEAKM ALLGVQQTWR RIRSGESVCD AARELLDFTA AMSGSELQAI LFNCSQPEAI CKALRELHDD EHTRGSLIYR GVRLGAYANR LTVIPDDWAL AESSEPQAMR TDLAVERYSD FVSQWVELGA GVVGGCCGIG PEYIAHIHKM LCDQGRR // ID G4ZCR5_PHYSP Unreviewed; 320 AA. AC G4ZCR5; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 01-APR-2015, entry version 17. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EGZ17797.1}; GN ORFNames=PHYSODRAFT_300746 {ECO:0000313|EMBL:EGZ17797.1}; OS Phytophthora sojae (strain P6497) (Soybean stem and root rot agent) OS (Phytophthora megasperma f. sp. glycines). OC Eukaryota; Stramenopiles; Oomycetes; Peronosporales; Phytophthora. OX NCBI_TaxID=1094619 {ECO:0000313|Proteomes:UP000002640}; RN [1] {ECO:0000313|EMBL:EGZ17797.1, ECO:0000313|Proteomes:UP000002640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P6497 {ECO:0000313|EMBL:EGZ17797.1}; RX PubMed=16946064; DOI=10.1126/science.1128796; RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H.Y., Aerts A., RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J., RA Damasceno C.M.B., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L., RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., RA Huang W., Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., RA Lee M.-K., McDonald W.H., Medina M., Meijer H.J.G., Nordberg E.K., RA Maclean D.J., Ospina-Giraldo M.D., Morris P.F., Phuntumart V., RA Putnam N.H., Rash S., Rose J.K.C., Sakihama Y., Salamov A.A., RA Savidor A., Scheuring C.F., Smith B.M., Sobral B.W.S., Terry A., RA Torto-Alalibo T.A., Win J., Xu Z., Zhang H., Grigoriev I.V., RA Rokhsar D.S., Boore J.L.; RT "Phytophthora genome sequences uncover evolutionary origins and RT mechanisms of pathogenesis."; RL Science 313:1261-1266(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; JH159154; EGZ17797.1; -; Genomic_DNA. DR RefSeq; XP_009526855.1; XM_009528560.1. DR GeneID; 20641895; -. DR KEGG; psoj:PHYSODRAFT_300746; -. DR InParanoid; G4ZCR5; -. DR Proteomes; UP000002640; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002640}; KW Reference proteome {ECO:0000313|Proteomes:UP000002640}. SQ SEQUENCE 320 AA; 35045 MW; A208A4E4D566811A CRC64; MEGKKVDIIA GGIMHELFRR GLPNDRNMLA ASALVAPAHH HMVVQAHEDF LKAGATMIIT NNYYVTPGVG FTPDEIREYS QLAGELAVSA RSRSNREDRT KICGSLPPLM HSLRSDRTVE RQKGLDTYLL IGEALLPSVD VFVAETMSSL AEAKMAFEGV QPLQKPVMVS FALNSTGQLR SGEDVVESVH SLVEFCTRHM ELLPGEAQGK DNLLCGILFN CSQPEDIAKA IKQLKETPEL MDTLKKHEIR IGGYGDHISP MSKAGAMEES LVPGALQSMM DMEIYSKFAM RWIDDGASIV GGCCGIPPDY LQRIAEVLSL // ID G5APN0_HETGA Unreviewed; 1260 AA. AC G5APN0; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 01-APR-2015, entry version 21. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHA98990.1}; GN ORFNames=GW7_07866 {ECO:0000313|EMBL:EHA98990.1}; OS Heterocephalus glaber (Naked mole rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; OC Hystricognathi; Bathyergidae; Heterocephalus. OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHA98990.1, ECO:0000313|Proteomes:UP000006813}; RN [1] {ECO:0000313|EMBL:EHA98990.1, ECO:0000313|Proteomes:UP000006813} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993625; DOI=10.1038/nature10533; RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L., RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X., RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A., RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., RA Bronson R.T., Buffenstein R., Wang B., Han C., Li Q., Chen L., RA Zhao W., Sunyaev S.R., Park T.J., Zhang G., Wang J., Gladyshev V.N.; RT "Genome sequencing reveals insights into physiology and longevity of RT the naked mole rat."; RL Nature 479:223-227(2011). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; JH166388; EHA98990.1; -; Genomic_DNA. DR InParanoid; G5APN0; -. DR Proteomes; UP000006813; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006813}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006813}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 780 780 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1260 AA; 140235 MW; 3EFE949A8A846EC1 CRC64; MKKTLQDEIE AILQKRIMVL DGGMGTMIQR YKLSEESFQG QEFKDHARPL KGNNDILSIT QPDIIYQIHQ DYLLAGADIV ETNTFSSTSI AQADYGLEHL AYRMNKCSAD VARKAAEEIT LQTGIKRFVA GALGPTNKTL SVSPSVERPD YRNITFDELV EAYQEQAKGL LDGGVDILLI ETIFDTANAK AALFALKKLF EENYTPRPVF ISGTIVDKSG RTLSGQTGEA FVISVSHGDP LCIGLNCALG ATEMRPFIET IGKCTTAYVL CYPNAGLPNT FGDYDETPSM MAMHLKDFAM DGLVNIVGGC CGTTPDHIRE IAEAVKNCKP RVPPASVFEG HMLLSGLEPF RIGPYTNFVN IGERCNVAGS KKFAKLIMAG NYEEALSVAK VQVEMGAQVL DVNMDDGMLD GPSAMTRFCN LIASEPDIAK VPLCIDSSNF AVIEAGLKCC QGKCIVNSIS LKEGEEDFLE KARKIKKFGA AVVVMAFDEE GQATETDVKI SVCTRAYHLL VKKVGFNPND IIFDPNILTI GTGMEEHNWY AVNFIHATKV IKETLPGVRI SGGLSNLSFS FRGMEAIREA MHGVFLYHAI KFGMDMGIVN AGNLPVYDDI QKELLKLCED LIWNKDPEAT EKLLRYAQTH GKGGKKVIQT DEWRNGPIEE RLEYALVKGI EKYIIEDTEE ARLNQEKYPR PLNIIEGPLM NGMKVVGDLF GGGKMFLPQV IKSARVMKKA VGHLIPFMEK EREANRLITG TVEEEASAWL TFQDPYQGTI VLATVKGDVH DIGKNIVGVV LGCNNFRVID LGVMTPCDKI LKAALDHKAD IIGLSGLITP SLDEMIFVAK EMERLAIKIP LLIGGATTSR THTAVKIAPR YSAPVIHVLD ASKSVVVCSQ LLDENLKDEY FEEIMEEYED IRQDHYESLK ERKYVSLSQA RKNGFHIDWL SEPPPVKPTF IGTRVFEDYD LQKLVHYIDW KPFFDVWQLR GKYPNRGFPK IFNDKTVGEE ARKLYDDAQN MLNILVSQKK LQARGVVGFW PAQSVQDDIR LYAEDVVPQA TEPIATFYGL RQQAEKDSAS TDPYHCLSDF IAPLHSGVRD YLGLFAVACF GVEKLSKAYE DDGDDYSSIM VKALGDRLAE AFAEELHERV RRELWAYCDS EQLGIADLRR LRYEGIRPAP GYPSQPDHTE KLTMWRLASI EQCTGIRLTE SLAMAPASAV SGLYFSNLNS RYFAVGKISK DQIEDYALRK NMSVAEVEKW LGPILGYDTN // ID G5ASU0_HETGA Unreviewed; 407 AA. AC G5ASU0; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 04-MAR-2015, entry version 16. DE SubName: Full=Betaine--homocysteine S-methyltransferase 1 {ECO:0000313|EMBL:EHB00101.1}; GN ORFNames=GW7_06605 {ECO:0000313|EMBL:EHB00101.1}; OS Heterocephalus glaber (Naked mole rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; OC Hystricognathi; Bathyergidae; Heterocephalus. OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB00101.1, ECO:0000313|Proteomes:UP000006813}; RN [1] {ECO:0000313|EMBL:EHB00101.1, ECO:0000313|Proteomes:UP000006813} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993625; DOI=10.1038/nature10533; RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L., RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X., RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A., RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., RA Bronson R.T., Buffenstein R., Wang B., Han C., Li Q., Chen L., RA Zhao W., Sunyaev S.R., Park T.J., Zhang G., Wang J., Gladyshev V.N.; RT "Genome sequencing reveals insights into physiology and longevity of RT the naked mole rat."; RL Nature 479:223-227(2011). CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH166815; EHB00101.1; -; Genomic_DNA. DR InParanoid; G5ASU0; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000006813; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006813}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000313|EMBL:EHB00101.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006813}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000313|EMBL:EHB00101.1}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 217 217 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 407 AA; 44955 MW; CFB05A8DE256DF16 CRC64; MAPIEGKKAR KGILERLNAG EVVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAVRQLH REFLRAGSNV MQTFTFYASE DKLENRGNYV AEKISGEKVN EAACDIARQV ADEGNALVAG GVSQTPSYLS CKSETEVKKI FQQQLEVFVK KNVDFLIAEY FEHVEEAVWA VEALKVSGKP VAVTMCIGPE GDLHGVSPGE CAVRLVRAGA SIVGVNCHFD PTTSLQTVKL MKEGLAAAGL KAHLMSQPLA YHTPDCGKQG FIDLPEFPFG LEPRVATRWD IQKYAREAYN LGVRYIGGCC GFEPYHIRAI AEELAPERGF LPPASEKHGG WGSGLDMHTK PWIRARARKE YWQSLRIASG RPYNPSLSKP DAWGVTKGTA ELMQQKEATT EQQLRELFEK QEFRSTQ // ID G5ASU1_HETGA Unreviewed; 363 AA. AC G5ASU1; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 04-MAR-2015, entry version 16. DE SubName: Full=Betaine--homocysteine S-methyltransferase 2 {ECO:0000313|EMBL:EHB00102.1}; GN ORFNames=GW7_06606 {ECO:0000313|EMBL:EHB00102.1}; OS Heterocephalus glaber (Naked mole rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; OC Hystricognathi; Bathyergidae; Heterocephalus. OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB00102.1, ECO:0000313|Proteomes:UP000006813}; RN [1] {ECO:0000313|EMBL:EHB00102.1, ECO:0000313|Proteomes:UP000006813} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993625; DOI=10.1038/nature10533; RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L., RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X., RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A., RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., RA Bronson R.T., Buffenstein R., Wang B., Han C., Li Q., Chen L., RA Zhao W., Sunyaev S.R., Park T.J., Zhang G., Wang J., Gladyshev V.N.; RT "Genome sequencing reveals insights into physiology and longevity of RT the naked mole rat."; RL Nature 479:223-227(2011). CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH166815; EHB00102.1; -; Genomic_DNA. DR RefSeq; XP_004880062.1; XM_004880005.1. DR GeneID; 101720782; -. DR KEGG; hgl:101720782; -. DR CTD; 23743; -. DR InParanoid; G5ASU1; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000006813; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006813}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000313|EMBL:EHB00102.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006813}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000313|EMBL:EHB00102.1}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 208 208 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 363 AA; 40057 MW; EDEC2B3EB4BE3B8A CRC64; MAPAGGSGPK RGILQRLDQG EVVIGDGSFL ITLEKRGYVK AGLWTPEAVV EHPDAVRQLH MEFLRAGSNV MQTFTFSASE DNMDSKWEEV NAAACDLARE VAGKGDALVA GGVCQSSMYK YHRDEARIKK LFRLQLEVFA RKNVDFLIAE YFEHVEEAVW AVEVLKELSK PVAVTMCIGP EGDMHGVTPG GCAVQLAKAG ADIIGVNCRF GPRTSLQTLL LMKQGLRAAG LSPHLMVQPL GFHTPDCGKG GFVDLPEYPF GLEPRVATRW DIQKYAREAY NLGVRYIGGC CGFEPYHIRA ISEELAPERG FLPPASEKHE SWGSALNMHT KPWIRARARR EYWENLLPAS GRPFCPSLSR PDV // ID G5D7D0_9PASE Unreviewed; 203 AA. AC G5D7D0; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 01-APR-2015, entry version 14. DE SubName: Full=Betaine-homocysteine methyltransferase-like protein {ECO:0000313|EMBL:AEP96153.1}; DE Flags: Fragment; OS Euplectes orix (red bishop). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; OC Ploceidae; Euplectes. OX NCBI_TaxID=229098 {ECO:0000313|EMBL:AEP96153.1}; RN [1] {ECO:0000313|EMBL:AEP96153.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=21951614; RA Pointer M.A., Prager M., Andersson S., Mundy N.I.; RT "A novel method for screening a vertebrate transcriptome for genes RT involved in carotenoid binding and metabolism."; RL Mol. Ecol. Resour. 12:149-159(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; JN580913; AEP96153.1; -; mRNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Methyltransferase {ECO:0000313|EMBL:AEP96153.1}; KW Transferase {ECO:0000313|EMBL:AEP96153.1}. FT NON_TER 1 1 {ECO:0000313|EMBL:AEP96153.1}. FT NON_TER 203 203 {ECO:0000313|EMBL:AEP96153.1}. SQ SEQUENCE 203 AA; 22017 MW; 86AACCAD00F4D8DF CRC64; ILERLDAGEI VIGDGGFVFA LEKRGYVKAG PWTPEATVEH PEAVRQLHRE FLRAGSNVLQ TFTFYASEDK LENRGNYVAE KISCQKVNEA ACDIAREVAN EGDALVAGGV SQTPSYLSCK DKTEVKAAFQ KQLEVFMKKN VDFLIAEYFE HVEEAVWAVE VLKESGKPVA ATMCIGPEGD MHGVPPGQCA VQLVKAGASI VGV // ID G5E2H8_9PIPI Unreviewed; 331 AA. AC G5E2H8; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Putative betaine--homocysteine s-methyltransferase 1 {ECO:0000313|EMBL:AEQ17123.1}; DE Flags: Fragment; OS Pipa carvalhoi (Carvalho's Surinam toad). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Pipinae; Pipa. OX NCBI_TaxID=191480 {ECO:0000313|EMBL:AEQ17123.1}; RN [1] {ECO:0000313|EMBL:AEQ17123.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Liver {ECO:0000313|EMBL:AEQ17123.1}; RA Chain F.J.J., Evans B.J., Dushoff J.; RT "The odds of duplicate gene persistence after polyploidization."; 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; JP287592; AEQ17123.1; -; mRNA. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 2. DR SUPFAM; SSF82282; SSF82282; 1. PE 2: Evidence at transcript level; KW Methyltransferase {ECO:0000313|EMBL:AEQ17123.1}; KW Transferase {ECO:0000313|EMBL:AEQ17123.1}. FT NON_TER 1 1 {ECO:0000313|EMBL:AEQ17123.1}. FT NON_TER 331 331 {ECO:0000313|EMBL:AEQ17123.1}. SQ SEQUENCE 331 AA; 36546 MW; 50D591982E7D0673 CRC64; AKKGLLERLD AGEVVIGDGG FVFALEKRGY VKAGPWTPEA AVEHPEAVRQ LHRKFLRAGA NGVSQTPSYL SCKSELDVKA IFRKQLEVFI KKNVFLIAEY FEHVEEAVWA VEVLKEAGKP VAATLCIGPE DLNGVTPGEC AVRLAKAGAA VVGVNCHFDP MTCVEVRLMK EGLQTAKVKA HLMTQPLAYH TPDCGKQGFD LPEFPFALEP RVVTRWDIHQ YAREAYKLGV RYIGGCCGFE PYHTRAIAEE LAPERGFLPQ GSEKHGSWGS GLEMHTKPWV RARARQEYWE KLPPASGRPY CPSMSKPDAW GVTKGDAALM QQKEATTEGQ L // ID G5F7R5_9CLOT Unreviewed; 829 AA. AC G5F7R5; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 01-OCT-2014, entry version 15. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHF07571.1}; GN ORFNames=HMPREF1020_00511 {ECO:0000313|EMBL:EHF07571.1}; OS Clostridium sp. 7_3_54FAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=665940 {ECO:0000313|EMBL:EHF07571.1}; RN [1] {ECO:0000313|EMBL:EHF07571.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=7_3_54FAA {ECO:0000313|EMBL:EHF07571.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHF07571.1}. 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; ACWK01000007; EHF07571.1; -; Genomic_DNA. DR RefSeq; WP_009295952.1; NZ_JH376512.1. DR EnsemblBacteria; EHF07571; EHF07571; HMPREF1020_00511. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; SQ SEQUENCE 829 AA; 88743 MW; 796FCD548CFF6067 CRC64; MAILEELREK ILLFDGGTGS LLQEAGLKPG ELPETWNISH PDIVVKLHSD YLEAGCDIIK TNTFGANRFK YNSGTQYSLK EIVTAAMDNA KCAVKKAGRG YIALDIGPTG KLLKPMGQLD FEEAVSVFRE VAETGAEQGA DLILIETMSD TYELKAAVLA AKEISSLPVF ATVIFDEKGK MLTGGTPQTA IALLEGLGVD AVGMNCGLGP VQMKPLAAEF IKYASVPVIV NPNAGLPRSE GGRTVYDIGP DEFEQAMEEI LDMGISVAGG CCGTTPGHIR RLNRLRAGRR QKLPQEKQST VITSYAAAVE IGDDPVIIGE RINPTGKSKF KQALRDHDLE FILREGISQQ ERGAHVLDVN VGLPEIDEPS MMAEVIRELQ GITELPLQID TSNTEAMARA MRVYNGKPLL NSVNGKQEVM DAVFPLVKRY GAVVVALTLD ESGIPETADG RIAIAEKIYR EAAKYGIGKK DILIDALCMT ISSDRLGALT TLETVKRVRQ EMGGRTILGV SNISFGLPVR ENINANFFTL ALYNGLNAAI INPGSEAMMC SYHSFRALAA LDENCGSYIE AYKNAAASSA AGSGSPAPGT SGNRLGSDTA GRKAEAAPGS GNGRGNNPAW DGEEERLALS VEKGLREQAA QSAKQLLAEK EPLDVINTCM IPALDHVGKG FEAGTVFLPQ LLMSAEAAKA AFDVIKEKMA ESGQAREKKG KIILATVKGD IHDIGKNIVR VLLENYSYDV LDLGKDVAPE QIVREAVKQH VPLVGLSALM TTTVPAMEET IQRLRQEAPW TKIMVGGAVL TPEYAKTIGA DAYCSDAMAS VSYAQKIIG // ID G5G9A8_9BACT Unreviewed; 910 AA. AC G5G9A8; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHG24684.1}; GN ORFNames=HMPREF9332_00159 {ECO:0000313|EMBL:EHG24684.1}; OS Alloprevotella rava F0323. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Alloprevotella. OX NCBI_TaxID=679199 {ECO:0000313|EMBL:EHG24684.1}; RN [1] {ECO:0000313|EMBL:EHG24684.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0323 {ECO:0000313|EMBL:EHG24684.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHG24684.1}. 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; ACZK01000005; EHG24684.1; -; Genomic_DNA. DR RefSeq; WP_009346570.1; NZ_JH376827.1. DR EnsemblBacteria; EHG24684; EHG24684; HMPREF9332_00159. DR OrthoDB; EOG6091CH; -. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 240 240 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 752 752 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 910 AA; 100043 MW; CDDEDDDEBB57A09B CRC64; MGLKEAVKDR ILILDGALGT MIQKYGLSEM DFRGKRFEYL PGQQRGNNDL LVLSRPDVIR EIHTRYLEAG ADIIETCTFN SQSISLADYH CESLVKEINF VAAQLARTCA DKFSTPEKPR FVTGSVGPTN KTCSLSPDVN DPALRALQFD ELAAAYQEQI EALLEGGVDA ILIETVFDTL NAKAAVVAAQ AAMSTVGREV PIMLSVTVAD KGGRTLSGQT LEAFLASFST MPIFSVGLNC SFGAKDMKPF LENLAAKAPY YISVYPNAGL PNSLGEYDET PEHMASEIAE FLDENLINIV GGCCGTTDKF IAEYSKLLKG RTPHQPVAAP TCLWLSGLES CEVRPERNFT NIGERCNVAG SRKFLRLVSE KNYDEAIGIA RKQVEDGAQV IDINFDDGLL ETKEEMVHFL NLLASEPDVA RVPFMIDSSK WDVILAALKC VQGKSIVNSI SLKEGEETFL SHARDIQKYG AAVVVMAFDE TGQATSFERK IEICKRAYNL LTQKLHFNPN DIIFDPNVLS ICTGISEHDS YGFDFIRAVA WIRENLPGAH VSGGISNLSF SFRGNNYLRE AMHTVFLYHA IQNGLDMGIV NPSSTITYSD IPKDLLEVIE SVILNTRDAS EELISLAQQM TDQQKNKVEH SQKTEEWRDF PLEKRLSYSL RKGIDSNLEE DLSEALGKYA HAVDIIEGPL MDGMNEVGDL FGAGKMFLPQ VVKTARTMKK AVSILQPHIE AEKKDGNSAG KVLMATVKGD VHDIGKNIVG AVLSCNNYAI EDLGVMVAPE DIAEKALGIE ADVVGLSGLI TPSLDEMTKT VVMMKERGIE IPVLLGGATT SRLHTALKIA PNYDGPVIWV KDASQMVIAM SKFSNPATAY NYIAENYKQQ EILRDKHNIK TTQDVDFKTA KSDKLNLFNK // ID G5GES0_9FIRM Unreviewed; 606 AA. AC G5GES0; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HMPREF9333_00058 {ECO:0000313|EMBL:EHI56611.1}; OS Johnsonella ignava ATCC 51276. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Johnsonella. OX NCBI_TaxID=679200 {ECO:0000313|EMBL:EHI56611.1}; RN [1] {ECO:0000313|EMBL:EHI56611.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 51276 {ECO:0000313|EMBL:EHI56611.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHI56611.1}. 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; ACZL01000003; EHI56611.1; -; Genomic_DNA. DR RefSeq; WP_005538973.1; NZ_JH378829.1. DR EnsemblBacteria; EHI56611; EHI56611; HMPREF9333_00058. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 606 AA; 67522 MW; EA3752884DA6A6AA CRC64; MINIRDFLKR RVLLFDGAMG TYYARISGDM SLGCEQANIK RPDIIRNIHR EYIDAGAMAI KTNTFGLSYF DTSHEEIQKR NELISAGYDI ATEAAQDKAY VFADIGPAAG ASESETADIY ISQAEIFLKK GALNYIFETL SGSEGILKAA EFIKNLKPSA FIIVSFAVLP DGYTRDGRYY KDLIEKMQKS SVIDAVGINC ISGAGQMYEL VREFDLLRIF ESGKYLSVMP NAGYPVIRGN QSVFDGNDAY FASKLKQIYS YGVRIIGGCC GTTPEYIKKV AQDLSGEAPK SVFVEKIKPE SHKSIKKYTN VFLDRLKTWK DTSKKVIAVE LDPPKDGDAQ LFLQNAKRLK DIGIDILTIS DCPIARARMD SSLLSCKIKR ELSMEVLPHL TCRDRNINAT KALLLGLYSE GVHNVLAVTG DPVPTAERSE VNAVYQFNSR KLASYITSLN KDIFNDSIKI FTALNINSKN FSAELKRAQL KIECGSVGFL TQPAYSQESF ENLKMARCKL DALILGGVIP LISKRNAVFM HNEVNGISIP EDIIDSFENL TPDECKKHAI KLCLDVAARM YEDVDGYYII TPFQKIDIIE KIISGIRQGV NDYGLR // ID G5GES1_9FIRM Unreviewed; 849 AA. AC G5GES1; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHI56612.1}; GN ORFNames=HMPREF9333_00059 {ECO:0000313|EMBL:EHI56612.1}; OS Johnsonella ignava ATCC 51276. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Johnsonella. OX NCBI_TaxID=679200 {ECO:0000313|EMBL:EHI56612.1}; RN [1] {ECO:0000313|EMBL:EHI56612.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 51276 {ECO:0000313|EMBL:EHI56612.1}; 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. {ECO:0000313|EMBL:EHI56612.1}. 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; ACZL01000003; EHI56612.1; -; Genomic_DNA. DR RefSeq; WP_005538974.1; NZ_JH378829.1. DR EnsemblBacteria; EHI56612; EHI56612; HMPREF9333_00059. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; SQ SEQUENCE 849 AA; 91650 MW; 25441E5F56FBE1E8 CRC64; MEDSAGNIIN PLISKGIIKP GKISILDGGM GTMLLAAGMK AGEHPEVFAF NNPGIVEDIH KKYIEAGSDI IYSCTFGANE KKLKGCGITT LQAVLSAVKT AKKAASLKEG VKVALDVGPI GELLEPLGTL SFDEAYNIYK EVMSIGEEAG ADLIVVETFT DLYDAKAALL AAKENTSLPV VVTMSFESGG RTFTGTTIPS MATVLTGLGA DAIGFNCSLG PKEILKFAEE LVQWTDLPVV IKPNAGLPDP VTGKYNLNAS DYASDMLAFK KFGVSMMGGC CGTDPEYINK LRLSLKCERD ARNAADIKTA GMDSSDSDLN SSISINDRDY DENILENYKS TRKIRYGVCS SSKMVELNKV RVIGERLNPT GKPRFAQALL EHDMDYISRM AIEQEESGAQ ILDVNVGVPG ADEPSLMIET VKAIQGITSL PLQIDSSNPA AIEAGLRAFN GKAIINSVNA DDERLDLILP IAKKYGAAVI GLSLSERGVP QTAQERFDNA VYILKKAIEY GLKKEDVFID CLTLTVSAQQ EQAVQTLNAL RKVKSELGLH CVLGVSNISF GLPERSHITE SFLVQAMCCG LDLPIINPNV SSLMDAVYSY KVLSGEDENC SDYIMRFSAN KESKEISGDI KCDVHADMTI EEAVLKGLKV QTREIAAKLL ESMSENDLIN NKLIPALDIV GDKYEKQIIF LPQLINSANA ACEAFELIKE RLAKSNTQGV SKGKIVLATV KGDIHDIGKN IVKIILENYG YRIIDLGRDV PIENVVKAVI EEKVNLVGLS ALMTTTLPSM KETIEAVKAV SPECKIWVGG AVLTPDYAME IGADYYAKDA RASVDIAKLS FPETIEDNL // ID G5GPH7_9FIRM Unreviewed; 594 AA. AC G5GPH7; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HMPREF9334_01158 {ECO:0000313|EMBL:EHG20865.1}; OS Selenomonas infelix ATCC 43532. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Selenomonas. OX NCBI_TaxID=679201 {ECO:0000313|EMBL:EHG20865.1}; RN [1] {ECO:0000313|EMBL:EHG20865.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43532 {ECO:0000313|EMBL:EHG20865.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHG20865.1}. 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; ACZM01000013; EHG20865.1; -; Genomic_DNA. DR RefSeq; WP_006692606.1; NZ_JH376799.1. DR EnsemblBacteria; EHG20865; EHG20865; HMPREF9334_01158. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 594 AA; 64426 MW; B46C0AC7B926EDC0 CRC64; MAQERMDIRE YLKKEPLVFD GGMGTYYAQK THTRGKGVEL ANIETPLVVE NIHTEYLNAG AHAIKTNTFA ANRIVYQGEE ALVQGIIRTG WKLAARAAEP FGAYVFADIG PVSGLPPTDI IEEYRFLSDT FLTAGARHFL FETNSSADGL VETAAHIKQE CPGAFILTSF SAFPGGYTRD GFFVEELVRQ VAESGYIDAV GFNCVSGVQS MKELVHLLGT CPLPFSLMPN AGHPIVVDGR TFYESAPDYF GEELADLVHD GISIVGGCCG TTPEHIRALS RALADSGRVS EDRVEQAEHA ALGPSRSAFF EALKTGGTPI AVELDPPEVG NADKFMAGAR ELMEAGVHAI TIADNPIARA RMDAGMLAGR VQRSLGLEPI PHMTCRDRNL NAIKSTLLGL SAEGIHNMIA ITGDPVPTAE RDEVKSVYQF NSRKLMSFIK SLGERGDVVP FHVFGALNVN AKHFPSQLGL AKKKLEAGMT GFFTQPVLSS RAKENLRTAR DTLPGALILG GIMPVVSERN ARFMESEITG IHVEERIINA YHGLSREEAE ELAVQLSLEI AKDITPYIDG YYIITPFART ALVARIVKGL KGTI // ID G5GPH8_9FIRM Unreviewed; 802 AA. AC G5GPH8; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHG20866.1}; GN ORFNames=HMPREF9334_01159 {ECO:0000313|EMBL:EHG20866.1}; OS Selenomonas infelix ATCC 43532. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Selenomonas. OX NCBI_TaxID=679201 {ECO:0000313|EMBL:EHG20866.1}; RN [1] {ECO:0000313|EMBL:EHG20866.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43532 {ECO:0000313|EMBL:EHG20866.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHG20866.1}. 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; ACZM01000013; EHG20866.1; -; Genomic_DNA. DR RefSeq; WP_006692607.1; NZ_JH376799.1. DR EnsemblBacteria; EHG20866; EHG20866; HMPREF9334_01159. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; SQ SEQUENCE 802 AA; 85785 MW; 0AEFD993727EC33A CRC64; MNQITILDGG MGTELQARGL APGERPELFG MDHPEVIEEV HRNYIAAGSR VIYSNTFGAN GHKLVGTGKT VAEVIAANVA TARRAAENSG AAGVRVALDI GPIGELVEPL GTLSFEAAYE LFREMVVAGE EAGADLVIFE TLTDLYEVKA AVLAAKEHTK LPIWVTMTFE QNGRTFLGAA VPSVAVTLDA LGVAALGVNC SLGPVELVPI VDELMEWTDL PIIVKPNAGL PDPRTGAYEM TAEDFGREMT VFAQRGALIM GGCCGTTPDF IRALTAAVAE GAADRPARKK RKGVASPGRV AEYGKLNVIG ERINPTGKKR LQQALLEEDY GYIKKLAISQ QEAGAQVLDI NVGAQGVDEE KIIPYVVKAV QSVVDLPLQI DSANPKVIEA ALRVTNGRVI INSVSGERER MDAIFPLAKH YGAAVLGLAM DEKGLPETAA QRVNIAERIV AEAEKYGLER EDIIIDCLTL TVSAQQVQAM ETLRAVREVH ERLGLHCALG VSNISFGLPA RGHMTENFLI QAMHVGLDFP IINPNTKGVM DAVVSFRAVS GEDVDCAAYI ERFAPEQAEM RRRKELGITG DEAAGAVQTS AAESADAVDP LMDAIIRGLS DDAERITRKL LTEMAPMDII QEKVIPALDI VGDRYEQEII FLPQLINAAN AATAGLELIK VRLAEAGQGV SKGKIILATV EGDIHDIGKN IVKVVLENYG YQIIDLGRDV PIQRVVEVAI EKKVGLIGLS ALMTTTVTAM KKTIEALHEA GHPCETIVGG AVLTEDYAKE IGADHYAGDA RSMVEIARRV LG // ID G5GUW2_FUSNP Unreviewed; 1081 AA. AC G5GUW2; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 2. DT 27-MAY-2015, entry version 21. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHG19128.2}; GN ORFNames=HMPREF9369_00705 {ECO:0000313|EMBL:EHG19128.2}; OS Fusobacterium nucleatum subsp. polymorphum F0401. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=693991 {ECO:0000313|EMBL:EHG19128.2}; RN [1] {ECO:0000313|EMBL:EHG19128.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0401 {ECO:0000313|EMBL:EHG19128.2}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHG19128.2}. CC ----------------------------------------------------------------------- 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; EHG19128.2; -; Genomic_DNA. DR RefSeq; WP_008702444.1; NZ_ADDB02000001.1. DR EnsemblBacteria; EHG19128; EHG19128; HMPREF9369_00705. DR GeneID; 23370356; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 723 723 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1081 AA; 120755 MW; B361E4114A49EE8A CRC64; MFEIEKELKE RILVLDGAMG TVLQKYELSA EDFNGAKGCY EILNETRPDI IFEVHKKYIE AGADIIETNS FNCNSISLKD YHLEDKVYDL AKKSAEIARD AVKESGKKVY IFGSVGPTNK SLSFPVGDIP FKRAVSFDEM KEVIKVQVAG LIDGGVDGIL LETIFDGLTA KAALLATEEV FEEKNIKLPI SISATVNKQG KLLTGQSMES LIVALDRDSV TSFGFNCSFG AKDLVPLVLK IKELTTKFVT LHANAGLPNQ NGDYVETAQK MKNDLLPLIE NQAINILGGC CGTSYDHIKA IAELVKGQKP RVLPEKNLLE TCLSGNEIYN FKDKFTCVGE RNNISGSKLF RTMIEEHNYL KALDVARQQI DAGAKVLDIN VDDAILDSVE EMKNFLRVLQ NDSFIAKVPI MIDSSDFAVI EEGLKNTAGK AIVNSISLKE GEENFLRKAK ITRKYGASII VMAFDENGQG VSAERKIEIC QRAYNLLKSI GVKNSDIVFD PNILSVGTGQ EADRYHAREF LKTIDYIHKN LKGCGIVGGL SNLSFAFRGN NILRAAFHHI FLEEAIPRGF NFAILNPKEK APQWTDEERE KIKSFIFGDS ANIEDLLSLN LVKRKEDAQI FAETPEDRIR KALIQGGSES LQEVIEELLK KYKALEILEN ILMSAMQEIG RLFEQGELYL PQLIRSASVM NNCVNILTPY LEKVDRTSSK GKILMATVDG DVHDIGKNIV KTVLECNGYE VIDLGVMVPR EKIVEVAKNN NVDIVTLSGL ISPSLKEMER VADSFQKVGM QIPILIAGAA TSKLHTGLKV LPNYDYSLHV TDAMDTITVV SQLLSTKRKD FLEAKQNQLR KIAKRYIENN DQTGEKKILP EVKKTVSYIP KVLGKQFLSL PVEILKDDLK WDIAFYALRV KNTPEEEKTL NDLKKIYEKL IEEKVEFKAA YGYFRCKKTE TFLEMEGMTF EVSPNIAQYI EKEDYLGAFV VSVKSEIFKD DKYLGLLETL LCNVIAEAAS EYMERRVSKD IVPTFLRPAV GYPILPDHSL KKVVFDLIDG EKTGAKLSPA FAMSPLSSVC GFYLCNDNAK Y // ID G5GZA8_9FIRM Unreviewed; 597 AA. AC G5GZA8; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HMPREF9432_00005 {ECO:0000313|EMBL:EHG26149.1}; OS Selenomonas noxia F0398. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Selenomonas. OX NCBI_TaxID=702437 {ECO:0000313|EMBL:EHG26149.1}; RN [1] {ECO:0000313|EMBL:EHG26149.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0398 {ECO:0000313|EMBL:EHG26149.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHG26149.1}. 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; ADGH01000002; EHG26149.1; -; Genomic_DNA. DR RefSeq; WP_006695613.1; NZ_JH376857.1. DR EnsemblBacteria; EHG26149; EHG26149; HMPREF9432_00005. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 597 AA; 64571 MW; BB98C4F05717A1B3 CRC64; MAQNSADIRE HIKKEPLVFD GGMGTYYAQK THTHGKGVEL ANIETPAVVG AIHTEYLQAG AQAIKTNTFA ANRIVYQGDE SLVRRIIRAG WEIAARAAEP FGAYVFADIG PVTGLPHTDI IAEYRFLADT FLACGATHFL FETNASIEGL IETAAHVKRV CPHAFILASF SALPGGYTRD GRFAEDLIHE AAESGSIDAV GFNCVNGVRQ MRELVHHLGM TSLPLSLMPN AGHPIVVDGR TFYESAPEYF GTSLAAIVRD GISIVGGCCG TTPEHIRALC AALADGTGEI DEEGEETRVQ PMEVPLSPFF DALKSGGKPI AVELDPPETG NADKFLVGVR ELQAAGISAI TIADNPIARA RMDAAMLAGR VHRELGIEPI PHMTCRDRNL NAIKSILLGL SAEGVHNMIA ITGDPIPTAE RDEVKSVYQF NSRKLASFVM SLGSRGDIVP FHVFGALNVN AKHFPSQLGL ARKKMEAGMT GFFTQPVLSE RAKENLQTAR DMLPGAFILG GIMPVVSERN ARFMESEIVG IHVEERIISA YRGLDRTAAE ELAVRLSLAI AKDIEPYIDG YYIITPFSRT ALIARIVEGI KERGEIR // ID G5GZA9_9FIRM Unreviewed; 802 AA. AC G5GZA9; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHG26150.1}; GN ORFNames=HMPREF9432_00006 {ECO:0000313|EMBL:EHG26150.1}; OS Selenomonas noxia F0398. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Selenomonas. OX NCBI_TaxID=702437 {ECO:0000313|EMBL:EHG26150.1}; RN [1] {ECO:0000313|EMBL:EHG26150.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0398 {ECO:0000313|EMBL:EHG26150.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHG26150.1}. 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; ADGH01000002; EHG26150.1; -; Genomic_DNA. DR RefSeq; WP_006695614.1; NZ_JH376857.1. DR EnsemblBacteria; EHG26150; EHG26150; HMPREF9432_00006. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; SQ SEQUENCE 802 AA; 86064 MW; 9098148D13FF1DC6 CRC64; MKDIIILDGG MGTELQARGL APGERPELFG IEHPEVVEEI HRNYIAAGSR VIYSNTFGAN GHKLAGTGKT VAEVIGANVQ IARRAAEHSG VEGVRVALDV GPIGELVEPL GTLSFEAAYE LFREMAVAGE EAGADLIIFE TLTDLYEAKA AVLAAKEHTK LPVWVTMTFE QNGRTFLGAA VPSVAVTLDA LGVAAIGVNC SLGPVELLPI VDELMEWTDL PVIVKPNAGL PDPRTGAYEL TAEEFGREMA EFARRGAVIM GGCCGTNPEF IRALAASVAS GAAERPERRK RKGIASPGRV AEYGKLNVIG ERINPTGKKR LQQALLEEDY GYIKKLAISQ QEAGAQVLDI NVGAQGVDEE KIIPYVVKAV QSVVDLPLQI DSANPKVIAA ALRVTNGRVI INSVSGERER MDAIFPLAKH YGAAVLGLAM DEKGLPETAA DRITVAERIV AEAERYGIER EDIIIDCLTL TVSAQQNQAM ETLRAVREVH ERLGLHCALG VSNISFGLPA RVHMTENFLI QAMHVGLDFP IVNPNTKEIM DAVISFRAVS GEDVDCAAYI ARFAPEQAEI RRRKELGITG SESPDAIQTA AADSADAVDP LMDAIIRGLS DDAERITRKL LTEKAPMEII QEKVIPALDI VGDRYEKEII FLPQLINAAN AATAGLELIK ARLAEEGQGV SKGKIILATV EGDIHDIGKN IVKVVLENYG YQIIDLGRDV PVTRVVEVAI EKQVGLIGLS ALMTTTVTAM KRTIDALHEA GHECETVVGG AVLTEDYARE IGADHYAGDA RSIVEIARRV LG // ID G5H4K5_9FIRM Unreviewed; 311 AA. AC G5H4K5; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHG23576.1}; GN ORFNames=HMPREF9432_01852 {ECO:0000313|EMBL:EHG23576.1}; OS Selenomonas noxia F0398. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Selenomonas. OX NCBI_TaxID=702437 {ECO:0000313|EMBL:EHG23576.1}; RN [1] {ECO:0000313|EMBL:EHG23576.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0398 {ECO:0000313|EMBL:EHG23576.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHG23576.1}. 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; ADGH01000018; EHG23576.1; -; Genomic_DNA. DR RefSeq; WP_006697035.1; NZ_JH376861.1. DR EnsemblBacteria; EHG23576; EHG23576; HMPREF9432_01852. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 311 AA; 34019 MW; 15375CB107E4D294 CRC64; MNVIEERLAV QDVIVLDGAF ATELEARGFS VNDALWSAKA LFERPDLVRD VHLDYLRAGA DVVTSASYQA TAEGFQKRGF TAEEAEALLQ KSVRLAQEAR DMYMAERPAE EPEPLVAASI GPYGAYLADG SEYRGDYDAD EDVLTAFHAE RLAVLAAARP DLLACETLPC LVEARALVRA LREKEIRIPA WFSFSCRDAA HISDGTPIAA CAHWLNSVPE AAAIGLNCTS PQYVEELIRT IRRETEKPVV VYPNSGESYD ASDKTWHGAA EDFAAATRRW RAAGARLIGG CCRTAPRDIA AISAWAKKRA E // ID G5H874_9BACT Unreviewed; 1244 AA. AC G5H874; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHB92269.1}; GN ORFNames=HMPREF9450_01134 {ECO:0000313|EMBL:EHB92269.1}; OS Alistipes indistinctus YIT 12060. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Rikenellaceae; OC Alistipes. OX NCBI_TaxID=742725 {ECO:0000313|EMBL:EHB92269.1}; RN [1] {ECO:0000313|EMBL:EHB92269.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=YIT 12060 {ECO:0000313|EMBL:EHB92269.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHB92269.1}. 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; ADLD01000011; EHB92269.1; -; Genomic_DNA. DR RefSeq; WP_009133940.1; NZ_JH370371.1. DR EnsemblBacteria; EHB92269; EHB92269; HMPREF9450_01134. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; SQ SEQUENCE 1244 AA; 133147 MW; 19099E47F15A8323 CRC64; MLKFSLLSEL SRRILVLDGG LGTMVQAYGL GEQDYRGDMF RDWPVPLKGC NETLALTRPD VLTEIHEAYL QAGADIISTD SFNANALSLS DQMLDFYVYD ICRAAASLAR AAADRFTLSN PSKPRFVAGS VGPGNRSASI SPDVNRPGAR AVTFDELKQA YYDQVRGLVD GGADLILIET FFDTLNAKAA IFAVGELSRE RKTRIPVMVS GTLTDVSGRT LSGQTVEAFY TSVHHGDVIS VGLNCGLGAE KMRPYIERLA AVAACAVSAH PNAGLPDKEG HYDETPEMMA ETVEQYLSAG LLNIVGGCCG TTPVHIAAIA AVAARTTPRT IPEPDGNLLL SGLEPLRIAS GPEPLTVGLQ ADATVSPEFA VAIRDKRYET AANAMRAAIE TGSPLAAVCV DDAMGAGPAA IRDLLNIAMA TPETARVPVA ILSSDWKTLE AGMQCVQGKP LIGPLSLADG DEEFVRRVSL AARYGAAVLV ALADEEGDAR SYRRKTSVAA RVAGLLERTG FPSCDVAVDP GVCPVPASGI GEEDTSGMPS DFFDACRGIR QQYPQWKLCG RIGVVSDRYR PDPGVCRALN GVWLSRAAEA GLDLAFADED ALRSVEEIPE ELLGLCEKAI AGSDAASVAA LTDYVLGHNP EAERLRSLFR DLKDRTAVTV PGEGSGQDGG TETGGAGDSI GYAKETATGL TPLWLEPLAG LGELYRAGTI PFALLERGIS VVTGALPDGV AACSRGWGRV LMATVGDDGY DPGRAALKTL LLVSGCRVED MGLVREPRRI IERCLNLPET GAAMTGKTAG STDKSPETTV PGVVGDTNRF DAVLLRGVSA RGVGQIAFLL AVAQKQGLQI PFLVGGPAAS ALQTAVGLAP QYGAGAVLYG GEPVATWRAL RRIASPEKDM FLIDVQMEQM ALREEYADRA KNKPFRTLSE ARAHALKPDF GTVRLPAKTG REVFADYDLK RLVPLINWSY FFGLAGLPGR YPDLLDDPVK GVQARQLYDD ARQLLDEVTE SGVLHARGIV ALYPARRDGD DIVLYEDTAC TRELHRLPQL RNQQTSQAVN LSLADFVAPV DGDAPDCVGL YALTLGDGLA TWITRCREEG SESRAKLAEL LAGRLCEAFA EELHRYARIH LWGIEQEGQL STEELLAGDY PGIRPAFGIP SCPDRSYRET VFRLLGVPAA IGMRLNENFD MEPAPAACGL IFASAEARNF SVGQIDAEQL ETYARRRNMP VELLRKLIRQ YIQS // ID G5HD15_9FIRM Unreviewed; 821 AA. AC G5HD15; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHF00719.1}; GN ORFNames=HMPREF9469_00477 {ECO:0000313|EMBL:EHF00719.1}; OS [Clostridium] citroniae WAL-17108. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=742733 {ECO:0000313|EMBL:EHF00719.1}; RN [1] {ECO:0000313|EMBL:EHF00719.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=WAL-17108 {ECO:0000313|EMBL:EHF00719.1}; 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. {ECO:0000313|EMBL:EHF00719.1}. 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; ADLJ01000003; EHF00719.1; -; Genomic_DNA. DR RefSeq; WP_007858795.1; NZ_JH376420.1. DR EnsemblBacteria; EHF00719; EHF00719; HMPREF9469_00477. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; SQ SEQUENCE 821 AA; 87957 MW; 082B6701817B3686 CRC64; MRLLEEMKVR RLFCDGGMGS MLQARGLQAG EMPEMWNLTH PEIVRDIHRQ YLKAGADIME TNTFGANGLK YKDNLEEIIT AAVGHAKAAV EEAGHGYVAL DVGPTGKLLK PLGDLDFEDA VSLYKEVVAY GVKAGADLVF IATMSDSYEL KAAVLAAKEA GVDPVTGENI PVFTSVTFDE KGKLLTGGNV ESTVALLEGL RVDALGINCG LGPEQMKGIL KDILEVTSLP VMVNPNAGLP RSENGKTVYD INEDQFAQVM REIVDMGAAV VGGCCGTTPD HIRETVKLCK DIPVRWPEKK RRTVISSYAQ AVVVDRKTVI IGERINPTGK SKFKQALRDH NLEYILREGV SQQDNGADVL DVNVGLPEID EPSMMEEVVK ELQSIIDLPL QIDTSNIEAM ERAMRVYNGK PLINSVNGKA EVMSQVFPLV AKYGGVVVGL CLDEGGIPET AEGRIAVGRK IIDTAADYGI GPEDIILDGL CMTVSSDSRG ALTTLETLRR IRDELGGKSV LGVSNISFGL PQREIINGAF FTMAMEAGLN AAIINPNSEA MMRAFYSFNA LMDRDPQCGR YISIYSGQAS GLGRTIGKNG AGQAAGNGGQ ASGASSALSG GEDAGALLTS AIERGLKDAA HQAVGVLLEK RDALDIINDH MIPALDRVGK GFEKGTVFLP QLLMSAEAAK AAFEVIKTRM DQSGQVQEKK GTVILATVKG DIHDIGKNIV KVLLENYGYD VMDLGKDVPP ERIVEEAVKG KVPLVGLSAL MTTTVPSMEE TIQKLRATAP NVKVMVGGAV LTKEYAQTIG ADMYCRDAMA SVNYAESIFV R // ID G5HDU5_9FIRM Unreviewed; 343 AA. AC G5HDU5; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHF00579.1}; GN ORFNames=HMPREF9469_00757 {ECO:0000313|EMBL:EHF00579.1}; OS [Clostridium] citroniae WAL-17108. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=742733 {ECO:0000313|EMBL:EHF00579.1}; RN [1] {ECO:0000313|EMBL:EHF00579.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=WAL-17108 {ECO:0000313|EMBL:EHF00579.1}; 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. {ECO:0000313|EMBL:EHF00579.1}. 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; ADLJ01000004; EHF00579.1; -; Genomic_DNA. DR RefSeq; WP_007859316.1; NZ_JH376420.1. DR EnsemblBacteria; EHF00579; EHF00579; HMPREF9469_00757. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 343 AA; 38875 MW; 4A490A9DDAEB049F CRC64; MTTTQRREKF KKTFAKVPIM MLQGSVGERI KRNFTHQDPT PPLKLAGLYY TENGHRGLDA VFHDYIQIAQ KYDLPMILHP YSKFTTPSMG KGTYWEDRDV SADNLNHCRS IVDGYPAIRD QIFIGTTMGF TGDPYNPFSG LDEEEAYLYY TDHAKKLETS MIDHVRNGLT PSLPDAAGCA RALSETSIPY FITFLIRKDG KLMDGTWLSE AIDYIDAKTG DHPPMFYQVN CVHPRNVMSA LDKRRNRTNA VRERFLGLEG NGSPLSPEEL DNSPVVYSSP ADEWADEMMK LHKDYGLKLL GGCCGTDHDH MEQLAIRVRQ VYDEQMAEQK AEPVTEPAAE TTE // ID G5II48_9FIRM Unreviewed; 841 AA. AC G5II48; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHI58864.1}; GN ORFNames=HMPREF9473_03176 {ECO:0000313|EMBL:EHI58864.1}; OS [Clostridium] hathewayi WAL-18680. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=742737 {ECO:0000313|EMBL:EHI58864.1}; RN [1] {ECO:0000313|EMBL:EHI58864.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=WAL-18680 {ECO:0000313|EMBL:EHI58864.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHI58864.1}. 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; ADLN01000083; EHI58864.1; -; Genomic_DNA. DR RefSeq; WP_006781155.1; NZ_JH379027.1. DR EnsemblBacteria; EHI58864; EHI58864; HMPREF9473_03176. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; SQ SEQUENCE 841 AA; 88963 MW; DE20AA2A2F2582C9 CRC64; MGILEAIRER IVFFDGGMGS LLQARGLGPG ELPETWNILH PEVLREVHRD YLNAGCDVLT TNTFGANGLK YRSACPGLAH VSHTSDYTVK EIVTAAVENA KAAVEEAGRG YIALDLGPTG KLLKPLGDLG FEEAYELYKE VVLAGAAAGA DFVHIETMSD GYETKAAILA AKENCQLPVT ATMTFDAKGK LLTGGDVYSA VALLEGLGVD ALGINCGLGP IQMKGILAEM LTAASIPVIV NPNAGLPRSE GGKTVYDIDA DEFAAVMEEI VRMGANAVGG CCGTTPEHIQ KVVNRCAGLP QKYPEKKHRC VISSFAHAVE IGREPVLIGE RINPTGKSKF KQALREHNLD YILREGVVQQ DNGAHVLDVN VGLPEIDEPS MMEEVVRELQ SIVDLPLQID TSDVNAMERA MRIYNGKPLI NSVNGKEESM RAVFPLVKKY GGVVVALALD ESGIPETADG RIAIAKKIYE RAAEYGIEPE DILIDSLCLT VSSDSKGALT TLETVRRVRE ELGGGTILGV SNISFGLPQR EIINAAFFTM ALQNGLSAAI INPNSEAMMR AYYSFRALAD MDAQCGDYIR IYGGQTAGLG ATLPKGGSAM GGAGGVAGGQ GASSGAGTGT GGPEGGAGQG AGGMMSLGDS ILKGLKDGAQ KAVTSLLETK DALTIINEEM IPALDTVGKG FEKGTIFLPQ LLMSAEAAKS AFEIIKERMA KSGQVQEKKG KIILATVKGD IHDIGKNIVK VLLENYSYDV IDLGKDVPPE LVVETAVAQK APLVGLSALM TTTVPSMEET IRRLRVDAPW VKVMVGGAVL TEDYAKTIGA DQYCKDAMAS VNYAESLNFT F // ID G5INQ2_9FIRM Unreviewed; 314 AA. AC G5INQ2; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHI56926.1}; GN ORFNames=HMPREF9473_05130 {ECO:0000313|EMBL:EHI56926.1}; OS [Clostridium] hathewayi WAL-18680. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=742737 {ECO:0000313|EMBL:EHI56926.1}; RN [1] {ECO:0000313|EMBL:EHI56926.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=WAL-18680 {ECO:0000313|EMBL:EHI56926.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHI56926.1}. 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; ADLN01000128; EHI56926.1; -; Genomic_DNA. DR RefSeq; WP_006783118.1; NZ_JH379031.1. DR EnsemblBacteria; EHI56926; EHI56926; HMPREF9473_05130. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 314 AA; 35183 MW; C89FE00AE11FD766 CRC64; MSFYDCIRNH NAILMEGALG ERLKREYHLT FDEQVAMANL IDTVEGRSAL NAIWQEYMQI ARTYHLPFLA TTPTRRANRE RMTLGGYDTA LIRRNVQFLR RLQEASDIEM YVGGLMGCKG DAYTGADALS EQEAEIFHGW QAGLFRDVDV DFLYAGIMPT LPEAAGMARA MAQTGVPYII SFTIQKDGRL IDGTTIHDAI AYIDSLDTCV NGVWQPPVCY MTNCVHPVIL QKALLQPFNR SELVQSRFLG IQANTSPLSY AELDGSKDLK CSEPEAFAND MAALKDISRI KIYGGCCGTD NRHMEEVAKR LSRK // ID G5J3V1_CROWT Unreviewed; 1192 AA. AC G5J3V1; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 01-APR-2015, entry version 19. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EHJ13134.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHJ13134.1}; GN ORFNames=CWATWH0003_2174 {ECO:0000313|EMBL:EHJ13134.1}; OS Crocosphaera watsonii WH 0003. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Crocosphaera. OX NCBI_TaxID=423471 {ECO:0000313|EMBL:EHJ13134.1}; RN [1] {ECO:0000313|EMBL:EHJ13134.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=WH 0003 {ECO:0000313|EMBL:EHJ13134.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHJ13134.1}. 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; AESD01000331; EHJ13134.1; -; Genomic_DNA. DR EnsemblBacteria; EHJ13134; EHJ13134; CWATWH0003_2174. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHJ13134.1}; KW Transferase {ECO:0000313|EMBL:EHJ13134.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 206 206 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 272 272 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 273 273 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 732 732 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1192 AA; 131949 MW; 5EBF9BAAD6490570 CRC64; MGTNIQSQNL TAEDFGGPEY EGCNEYLVIT KPEAVARVHR NFLKAGADVV ETDSFGSSPL VLAEYDLADR AYELSRKSAE LARRCADEFT TPEKPRFVAG SIGPGTKLPT LGHITYDELR SSFMVQAEGL FDGGADLFIV ETCQDVLQIK AALSAFEAVF AKKGSRLPLM VSVTMEIQGT MLVGTDISGV LAILEPFPID ILGLNCATGP NLMTSHIQYL SENSPFPISC IPNAGLPENV GGQAVYKMTP EEYTTAMTGF IAEHGVQIVG GCCGTRPAHI KALAEAVEHT QIKERSVRKN AVGELREPIS YTPAAASIYS AQTYEQDNSF LIVGERLNAS GSKKVRTLLN EDDWDGLLAI AKSQVKEGAH MLDVNVDYVG RDGERDMREL VSRLVTNTTL PLMLDSTEWT KMEAGLKVAG GKCLLNSTNY EDGEERFFKV LELAKEYGAG VVIGCIDEEG MARTAQKKFE IAKRAYEDAL KFGIPPHEIF YDTLALPIST GIEEDRENAK ATIESIKMIR EHLPGVHFML GVSNISFGLS PATRITLNSV FLNEAMKAGM DGSIVSAAKI LPLSKIEEEH QQVCRDLIYD NRQFEGDICT YDPLTKLTEI FAGVSAKDAR SGPSLADLPI DQRLKQHIID GERIGLDDAL KIGLDAGYKA LDIVNTFLLD GMKVVGELFG SGQMQLPFVL QSAETMKSAV AFLEPYMEKI EGEDEDRGKG KFLIATVKGD VHDIGKNLVD IILTNNGYKV VNLGIKQAIE AIVEAYEQHQ PDCIAMSGLL VKSTAFMKDN LSAFNAKGIT VPVILGGAAL TPKFVYGDCQ ETYNGQVIYG KDAFADLTFM DRLMPAKEQE SWVDTEGFTG EFAQFNQKGR KAIEDSEREA NGDASKSDGE VNGNGKKSDE PIVIDTKRSE DVAIDIERPT PPFWGTKILQ SGDLDLEELF WYMDLQALFA GQWQFRKPKG QSREEYDWFL ASKVNPILEE WKEKIRTERW LEPTLVYGYF PCAAIDNSVH VYEPSVIEQG LTPKTATPFV TWTFPRQKSG RRLCISDFIL PLEYNEFDVF PMQAVTMGEI ATEKAQELYK DNKYTDYLYF HGMAVQLAEG LAEWSHARIR RELGYGDLEP DNIRDILAQR YQGSRYSFGY PACPTVMDQV PQLQLLGCDR IGLSIDESEQ LYPEQSTTAF VSYHPVARYF SA // ID G5JBL1_CROWT Unreviewed; 1193 AA. AC G5JBL1; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EHJ10432.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHJ10432.1}; GN ORFNames=CWATWH0003_4826 {ECO:0000313|EMBL:EHJ10432.1}; OS Crocosphaera watsonii WH 0003. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Crocosphaera. OX NCBI_TaxID=423471 {ECO:0000313|EMBL:EHJ10432.1}; RN [1] {ECO:0000313|EMBL:EHJ10432.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=WH 0003 {ECO:0000313|EMBL:EHJ10432.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHJ10432.1}. 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; AESD01000721; EHJ10432.1; -; Genomic_DNA. DR RefSeq; WP_007312639.1; NZ_AESD01000721.1. DR EnsemblBacteria; EHJ10432; EHJ10432; CWATWH0003_4826. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHJ10432.1}; KW Transferase {ECO:0000313|EMBL:EHJ10432.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 228 228 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 739 739 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1193 AA; 132915 MW; CEA92C755332FFD1 CRC64; MNSTFLNHLK SPKRPVLVFD GATGTSLQSQ NLTAEDFGGP EYEGCNEYLV HTKPSAVEQV HQGFLEAGAD VIETDTFGGT SIVLAEYDLA DQAYYLNKRA TEIAKKMATE YSTPEKPRFV AGSMGPGTKL PTLGHIDFDT LRDAYAEQAE GLYDGGADLF IIETCQDVLQ IKSALNAVEE VFEKKGKRLP LMVSITMETM GTMLVGTEIS AALSILEPYN IDILGLNCAT GPEQMKEHIK YLSEHSPFII SCIPNAGLPE NVGGQAHYRL TPIELKMALM HFIEDLGVQV IGGCCGTRPD HIQSLSELSQ ELTPKERHPH YEPCAASIYS TQPYIQDNSF LIIGERLNAS GSKKCRTLLD AEDWDSLVSL AKTQVKEGAH VLDVNVDYVG RDGVRDMNQL ASRLVNNVTL PLMLDSTEWQ KMESGLKVAG GKCILNSTNY EDGEERFLKV LELAKKYGAG VVVGTIDEDG MGRTADKKFE IAKRAYDAAI EYGISPHEIF FDPLALPIST GIEEDRENGK ATVDSIRRIR EELPGCHILL GISNISFGLN PAARQVLNSI FLYECMQVGL DGAIVSASKI LPLAKIEEEH QKVCHDLIYD LREFDGEICT YDPLTKLTEL FAGKTTKKDA SQTAKLPIEE RLKQHIIDGE RLGLEDALGL ALKQYPPLDI INVFLLDGMK VVGELFGSGQ MQLPFVLQSA QTMKAAVAYL EPLMDKEDGE SNDSGKGKFV IATVKGDVHD IGKNLVDIIL SNNGYKVINL GIKQPVENII QAYEEHNPDC IAMSGLLVKS TAFMKDNLEV FNERGVEIPV ILGGAALTPK FVYEDCQNTY KGKVVYGKDA FSDLHFMDKL MPAKAAENWD NLQGFSGDFN GENSLFQEER GEKAAEKVAE KNGKSAEPET PTVIDTKRSE AVEILEPATP PFWGTKILKP DEFDLNELFW YLDLQALIAG QWQFRKPKTQ SKEEYEAFLA EKVYPILEEW KAKVITDNLL HPTVIYGYFP CQSQENSLLI YDPEIVQNAN NTIPEDLEPI WKIDFPRQKS GRRLCIADFF APKESGKIDV FPMQAVTVGE VATEYAQKLF AANDYTNYLY YHGMAVQTAE ALAEWTHTRV RKELGFSDKE PDNIREMLKQ HYQGSRYSFG YPACPNIQDQ YKQLEVMGCD RINMYMDESE QIYPEQSTTA IITYHPVAKY FSA // ID G5JL17_9STAP Unreviewed; 613 AA. AC G5JL17; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 17. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=SS7213T_10904 {ECO:0000313|EMBL:EHJ07104.1}; OS Staphylococcus simiae CCM 7213. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=911238 {ECO:0000313|EMBL:EHJ07104.1}; RN [1] {ECO:0000313|EMBL:EHJ07104.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCM 7213 {ECO:0000313|EMBL:EHJ07104.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHJ07104.1}. 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; AEUN01000498; EHJ07104.1; -; Genomic_DNA. DR RefSeq; WP_002464867.1; NZ_AEUN01000498.1. DR EnsemblBacteria; EHJ07104; EHJ07104; SS7213T_10904. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EHJ07104.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EHJ07104.1}. SQ SEQUENCE 613 AA; 67867 MW; DF04BC5A8DF4C377 CRC64; MSQFLTQLKD NILVADGAMG TILYSEGIDT CPEAYNLSHP DKIEHIHRSY IAAGADVIQT NTYGANFEKL KNFGLEHKVK EIHQAAVRIA KKAATDHTFI LGTVGGFRGI KQDDLSLQTI LYHSEIQIDT LVEEGVDALL FETYYDLEEL THVIKHTRQK YEIPIIAQLT ASNTNYLVNG TDINSALKSI VDCGANIVGL NCHHGPHHMQ ESFTHIELPD QAFLSCYPNA SLLDIENSEI KYSDNAQYFG TVAQQLVNEG VRLIGGCCGT TPEHIKFIKS SVANLKPINS KKVVPITTSI HFNQSSTHTK QNLTSKVRER PTVIVELDTP KHLDTTKFFD NIAKLDKANI DAVTLADNSL ATVRVSNIAA ASLIKQYYNI EPLVHITCRD RNLIGLQSHL LGLSLIGVNE ILAITGDPSK VGHLPGATNV YDVNSKGLTE LALRFNQGIN TDGDALKKCT HFNIAGAFNP NVRKLDGAVK RLEKKVDSGM SYFITQPVYS KEKIIEIYHA TKHLDTPFFI GIMPIASYKN ALFLHNEVPG IKMSDDILAQ FEAVKDDKAK TRQLSLTLSK ALIDTVHQYF NGLYIITPFQ NVEDSLELAA YSKSITTHKE AIL // ID G5JNE7_STRCG Unreviewed; 315 AA. AC G5JNE7; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 11. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EHI73926.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EHI73926.1}; GN Name=mmuM {ECO:0000313|EMBL:EHI73926.1}; GN ORFNames=STRCR_1401 {ECO:0000313|EMBL:EHI73926.1}; OS Streptococcus criceti HS-6. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=873449 {ECO:0000313|EMBL:EHI73926.1}; RN [1] {ECO:0000313|EMBL:EHI73926.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HS-6 {ECO:0000313|EMBL:EHI73926.1}; RA Stanhope M.J., Durkin A.S., Hostetler J., Kim M., Radune D., Singh I., RA Town C.D.; 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. {ECO:0000313|EMBL:EHI73926.1}. 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; AEUV02000002; EHI73926.1; -; Genomic_DNA. DR RefSeq; WP_004226509.1; NZ_AEUV02000002.1. DR EnsemblBacteria; EHI73926; EHI73926; STRCR_1401. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHI73926.1}; KW Transferase {ECO:0000313|EMBL:EHI73926.1}. SQ SEQUENCE 315 AA; 34429 MW; 94CDE78077697046 CRC64; MGRFKDLLTS QDNLILHGAL GTELEYRGYD VSGKLWSAKY LLEDPQAIQD IHETYLRAGS DIVTTASYQA TLPGLEEYGL SEEEAKAVIA STVSIAKAAR DQVWSELAGE EQAKRPYPLI SGDIGPYAAY LADGSEYTGA YGSVTKKELM DFHRPRIAIL QDQGVDLLAL ETIPNLLEVQ ALVDLLASEF PGMEAYMSFT SQDGLSISDG TPIAEVAPLV DDSRQILALG LNCSSPSVYP SFLQGLRNYS QKPLVTYPNS GEVYDGASQT WTKDPDHSHT LLENTLEWQK LGAKVVGGCC RTRPSDIQIL SSRLR // ID G5JRI2_STRCG Unreviewed; 616 AA. AC G5JRI2; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 17. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=STRCR_1990 {ECO:0000313|EMBL:EHI75284.1}; OS Streptococcus criceti HS-6. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=873449 {ECO:0000313|EMBL:EHI75284.1}; RN [1] {ECO:0000313|EMBL:EHI75284.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HS-6 {ECO:0000313|EMBL:EHI75284.1}; RA Stanhope M.J., Durkin A.S., Hostetler J., Kim M., Radune D., Singh I., RA Town C.D.; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHI75284.1}. 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; AEUV02000002; EHI75284.1; -; Genomic_DNA. DR RefSeq; WP_004229563.1; NZ_AEUV02000002.1. DR EnsemblBacteria; EHI75284; EHI75284; STRCR_1990. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EHI75284.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EHI75284.1}. SQ SEQUENCE 616 AA; 68303 MW; CB0E4023B124DE00 CRC64; MSKLLDKLKT DILVADGAMG TLLYADGLES CHDYYNISHP ERISAIHKAY IDAGADIIQT NTYGAKRHRL KSFGHDNDVK LINQKAVEIA RQAAGESVFV LGTIGASRGL RQCDLSLADI VEETVEQAQA LLETGQLDGL LLETYYDREE LEAVVKAIRP LTDLPLITNM ALHEAGITED GRPLVEALSH LVMLGADIVG LNCHLGPYHM IQSFKQVPLF AQSYLSAYPN ASLLSFASDN EKGQYRFSQN ADYFEYCARL FVEEGVRLIG GCCGTTPDHI RAIKRGIKNL KPVERKTITP LITEEELIDE ISKKETLADK AKKEVTIIAE IDPPKTLAIE KFIEGIKALD KKNIAAITLA DNSLAKTRIC NLSLASLLKN EVTTPFLLHV ACRDHNMIGL QSRLLGMDVL GFNQLLAITG DPTKIGDFPG ATSVYDATSF KLLSLIKQLN HGKGYSGASL KRTTHFTTAA AFNPNVHHLE KSSRLIERKI KAGADYFITQ PIFSEEIIHQ LGHLTEAYDQ PFFIGIMPIT SYNNAVFLHN EVPGIHLPEV FLEKLETVKD DKKACQAIAL AESKKLIDCA LEYFNGIYLI TPFLRYDLTL DLIDYIQKKK TLMSPK // ID G5JTZ7_9STRE Unreviewed; 618 AA. AC G5JTZ7; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 17. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=STRMA_0537 {ECO:0000313|EMBL:EHJ52454.1}; OS Streptococcus macacae NCTC 11558. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=764298 {ECO:0000313|EMBL:EHJ52454.1}; RN [1] {ECO:0000313|EMBL:EHJ52454.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NCTC 11558 {ECO:0000313|EMBL:EHJ52454.1}; RX PubMed=24625962; DOI=10.1093/gbe/evu048; RA Richards V.P., Palmer S.R., Pavinski Bitar P.D., Qin X., RA Weinstock G.M., Highlander S.K., Town C.D., Burne R.A., Stanhope M.J.; RT "Phylogenomics and the dynamic genome evolution of the genus RT Streptococcus."; RL Genome Biol. Evol. 6:741-753(2014). CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHJ52454.1}. 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; AEUW02000001; EHJ52454.1; -; Genomic_DNA. DR RefSeq; WP_003080482.1; NZ_AEUW02000001.1. DR EnsemblBacteria; EHJ52454; EHJ52454; STRMA_0537. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EHJ52454.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EHJ52454.1}. SQ SEQUENCE 618 AA; 68553 MW; D4C8185FD569451E CRC64; MSRLLERLKT DILVADGAMG TLLYADGLEA CHEYYNISHP EKIISIHRAY IAAGADVIQT NTYAAKRHRL KGFGYDHKVE EINREAVALA RQAAGDDLFV LGTIGASRGL KQCDLTLDEI VSETVEQAKI LLETRQIDGL LLETYYDLDE LIAALKALRP LTDLPIITNM ALYEAGITES GRPLVEAFSH LVMLGADIVG LNCHLGPYHM IQSFKQVPLF AQSYLSAYPN ASLLSFSNDD EKGHYSFSQN ADYFERCAKL FVEEGVRLIG GCCGTTPDHI KALKRGIRGL KPIEKKVTLP PADPEEPIFE TEKKESLVDK VKREVTIIAE IDPPKTLAID KFVEGVKALD KKEIAAITLA DNSLARTRIC NLSMASLMKE EVETPFLLHI ACRDHNMIGL QSRLLGMDIL GFDHVLAITG DPSKIGDFPG ATSVYDATSF KLLNLIKQLN QGKGYSGASL KKATHFTVAA AFNPNVKNLS RTSRLIDKKV AAGADYFITQ PVFNAKTIVG LKEVTQNYEQ PFFIGIMPIT SYNNAVFLHN EVPGIELSEE FLARLEKVKD DKEICQELAL AESKRLIDSA LESFNGIYLI TPFMRYDLTA DLIDYIHEKS MTIQEKRA // ID G5JU52_9STRE Unreviewed; 323 AA. AC G5JU52; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 11. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EHJ53031.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EHJ53031.1}; GN Name=mmuM {ECO:0000313|EMBL:EHJ53031.1}; GN ORFNames=STRMA_0592 {ECO:0000313|EMBL:EHJ53031.1}; OS Streptococcus macacae NCTC 11558. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=764298 {ECO:0000313|EMBL:EHJ53031.1}; RN [1] {ECO:0000313|EMBL:EHJ53031.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NCTC 11558 {ECO:0000313|EMBL:EHJ53031.1}; RX PubMed=24625962; DOI=10.1093/gbe/evu048; RA Richards V.P., Palmer S.R., Pavinski Bitar P.D., Qin X., RA Weinstock G.M., Highlander S.K., Town C.D., Burne R.A., Stanhope M.J.; RT "Phylogenomics and the dynamic genome evolution of the genus RT Streptococcus."; RL Genome Biol. Evol. 6:741-753(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. {ECO:0000313|EMBL:EHJ53031.1}. 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; AEUW02000001; EHJ53031.1; -; Genomic_DNA. DR RefSeq; WP_003081788.1; NZ_AEUW02000001.1. DR EnsemblBacteria; EHJ53031; EHJ53031; STRMA_0592. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHJ53031.1}; KW Transferase {ECO:0000313|EMBL:EHJ53031.1}. SQ SEQUENCE 323 AA; 35637 MW; 9CBB1E21389577A3 CRC64; MGRFKELLSQ ENYLILHGAL GTELEFLGYD VSGKLWSAKY LLKDPQLIQD IHETYLKAGS DIITSSSYQA SVLGLCDYGL DYEEALNVIA LTVQLAKKAR ENVWSTLTEK EKKARPYPLI SGDVGPYAAY LADGSEYSGN YGSISKETLK DFHRPRLAVL VDEECDLLAL ETIPNYLEVQ ALSELLQEEF PAVEAYISFT AQTKDSISDG TAIEKVAQLV DRSPQILALG INCSSPLIYK SLLQKIAAIT EKPLVTYPNS GEIYDGKHQN WTKAAASSGS LLENTLTWYK LGAKILGGCC RTRPADIKNL NQGLQRAIKK RVG // ID G5K349_9STRE Unreviewed; 622 AA. AC G5K349; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 17. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=STRIC_1217 {ECO:0000313|EMBL:EHI69449.1}; OS Streptococcus ictaluri 707-05. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=764299 {ECO:0000313|EMBL:EHI69449.1}; RN [1] {ECO:0000313|EMBL:EHI69449.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=707-05 {ECO:0000313|EMBL:EHI69449.1}; RX PubMed=24625962; DOI=10.1093/gbe/evu048; RA Richards V.P., Palmer S.R., Pavinski Bitar P.D., Qin X., RA Weinstock G.M., Highlander S.K., Town C.D., Burne R.A., Stanhope M.J.; RT "Phylogenomics and the dynamic genome evolution of the genus RT Streptococcus."; RL Genome Biol. Evol. 6:741-753(2014). CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHI69449.1}. 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; AEUX02000006; EHI69449.1; -; Genomic_DNA. DR RefSeq; WP_008088859.1; NZ_AEUX02000006.1. DR EnsemblBacteria; EHI69449; EHI69449; STRIC_1217. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EHI69449.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EHI69449.1}. SQ SEQUENCE 622 AA; 68856 MW; 3171D301C8C85598 CRC64; MAKLLERLQE GILIADGAMG TLLYRNGLDN CYEAYNFQKP EDIKTIHKAY IKAGADIIQT NTYGAKRHKL KGYGLEDHFE EINIAGARIA REAAGSEIFV LGTIGASRGI RQCDLSLDEI VSETVEQTKV LLSTQLLDGL LFETYYDTEE IFAVLEAIRP LTDLPIITNI SLQEVGLTAR GQSITEVFSH LVLLGADLIG LNCHQGPYHM IQSLKQVPLF AHSYLSVYPN ASLLALDTGD EFDYQFSSNA EYFGQSVVAM VNEGARLIGG CCGTTPDHIK AVKRAVRGLS PITKKQIKPI VSSAEIIPED QDGERLVDKV KRDITVIAEL DPPKTLDISS FKKGIRALDA TSLDAITLAD NSLAKTRICN VSLAAMMKEE IDTPFLLHLT CRDHNLIGLQ SRLLGMDILG INHILAITGD PSKLGDFPGA TSVYDVNSFK LIELIKDLNK GQSYSGTSLK KATHFTIGAA FNPNIKNLSR SGRLIEKKIE AGADYFLTQP IFKAELIPEL YQLTKSYEQP FFVGIMPITS YNNAVFLHNE VRGIDLSEEF LQALEAVKDD KEQCQAIALA ESKRLIDEAL NYFNGIYLIT PFMRYDLTVE LINYVEKMKQ KRISDSLISN AI // ID G5KY50_STRSU Unreviewed; 315 AA. AC G5KY50; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 11. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EHC03458.1}; GN Name=mmuM {ECO:0000313|EMBL:EHC03458.1}; GN ORFNames=SSUR61_0051 {ECO:0000313|EMBL:EHC03458.1}; OS Streptococcus suis R61. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=996306 {ECO:0000313|EMBL:EHC03458.1}; RN [1] {ECO:0000313|EMBL:EHC03458.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=R61 {ECO:0000313|EMBL:EHC03458.1}; RA Hu P., Yang M., Jin M., Xiao J.; RT "Deep-sequencing identification of multiple resistance mechanism for RT the high antibiotic-resistance strain Streptococcus suis R61."; 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. {ECO:0000313|EMBL:EHC03458.1}. 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; AEYY01000012; EHC03458.1; -; Genomic_DNA. DR RefSeq; WP_002940351.1; NZ_AEYY01000012.1. DR EnsemblBacteria; EHC03458; EHC03458; SSUR61_0051. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHC03458.1}; KW Transferase {ECO:0000313|EMBL:EHC03458.1}. SQ SEQUENCE 315 AA; 34697 MW; AAC3BF1E65FEBBC4 CRC64; MGRFKELLEN QEFVILHGAL GTELEFRGYD VSGKLWSAKY LLENPQLIKD IHKDYIRAGA DLVTTSTYQA TFEGLAEVGL SQAEAEELIR LTVDLAKEAR EEVWVALSEA EKVQRTYPLI SGDVGPYAAY LANGAEYTGD YGNISLEELK AFHRRRMELL LEQGAELLAL ETIPNVLEAQ ALVELLAEDF PEAEAYISFT SQDGQSISDG TSIEKIAELV NSSEQILAVG LNCTAPSLYP AFLSQLREKT DKPFVTYPNS GEVYDGATQT WKEKADDSHS LLDNTLVWHK LGAKVVGGCC RTRPADIADL VAGLK // ID G5LHC8_SALET Unreviewed; 555 AA. AC G5LHC8; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|EMBL:EHC29095.1}; DE Flags: Fragment; GN ORFNames=LTSEADE_5721 {ECO:0000313|EMBL:EHC29095.1}; OS Salmonella enterica subsp. enterica serovar Adelaide str. A4-669. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=913063 {ECO:0000313|EMBL:EHC29095.1}; RN [1] {ECO:0000313|EMBL:EHC29095.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A4-669 {ECO:0000313|EMBL:EHC29095.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHC29095.1}. 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; AFCI01001903; EHC29095.1; -; Genomic_DNA. DR EnsemblBacteria; EHC29095; EHC29095; LTSEADE_5721. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHC29095.1}; KW Transferase {ECO:0000313|EMBL:EHC29095.1}. FT NON_TER 1 1 {ECO:0000313|EMBL:EHC29095.1}. SQ SEQUENCE 555 AA; 60315 MW; 208298BBFEF36C24 CRC64; APPSGKATEV DGKLNMSHVA RCSLFRQHAL CQYGSLRGAL SGASVSSKVE QLRAQLNERI LVLDGGMGTM IQSYRLHEED FRGERFADWP CDLKGNNDLL VLSKPEVIAA IHNAYFEAGA DIIETNTFNS TTIAMADYRM ESLSAEINYA AAKLARACAD EWTARTPEKP RFVAGVLGPT NRTASISPDV NDPAFRNITF DQLVAAYRES TKALVEGGVD LILIETVFDT LNAKAAVFAV KEEFEALGVD LPIMISGTIT DASGRTLSGQ TTEAFYNSLR HAEALTFGLN CALGPDELRQ YVQELSRIAE CYVTAHPNAG LPNAFGEYDL DADTMAKQIR EWAEAGFLNI VGGCCGTTPE HIAAMSRAVA GLPPRQLPDI PVACRLSGLE PLNIGDDSLF VNVGERTNVT GSAKFKRLIK EEKYSEALDV ARQQVESGAQ IIDINDINMD EGMLLIDINM DEGMLDAEAA MVRFLSLIAG EPDIARVPIM IDSSKWEVIE KGLKCIQGKG IVNSISMKEG VEAFIHHAKL LRRYGAAVVV MAFDEQGQAD TRARN // ID G5LWR4_SALET Unreviewed; 328 AA. AC G5LWR4; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|EMBL:EHC29297.1}; DE Flags: Fragment; GN ORFNames=LTSEALA_5820 {ECO:0000313|EMBL:EHC29297.1}; OS Salmonella enterica subsp. enterica serovar Alachua str. R6-377. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=913241 {ECO:0000313|EMBL:EHC29297.1}; RN [1] {ECO:0000313|EMBL:EHC29297.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=R6-377 {ECO:0000313|EMBL:EHC29297.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHC29297.1}. 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; AFCJ01002471; EHC29297.1; -; Genomic_DNA. DR EnsemblBacteria; EHC29297; EHC29297; LTSEALA_5820. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EHC29297.1}; KW Transferase {ECO:0000313|EMBL:EHC29297.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT NON_TER 328 328 {ECO:0000313|EMBL:EHC29297.1}. SQ SEQUENCE 328 AA; 35833 MW; 0EC0F250D5916210 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLHEEDFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYRMESLS AEINYAAAKL ARACADEWTA RTPEKPRFVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKEEF EALGVDLPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPEHIAA MISIWMRG // ID G5MBL8_SALET Unreviewed; 387 AA. AC G5MBL8; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|EMBL:EHC29100.1}; DE Flags: Fragment; GN ORFNames=SeGA_5658 {ECO:0000313|EMBL:EHC29100.1}; OS Salmonella enterica subsp. enterica serovar Gaminara str. A4-567. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=913071 {ECO:0000313|EMBL:EHC29100.1}; RN [1] {ECO:0000313|EMBL:EHC29100.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A4-567 {ECO:0000313|EMBL:EHC29100.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHC29100.1}. 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; AFCL01001859; EHC29100.1; -; Genomic_DNA. DR EnsemblBacteria; EHC29100; EHC29100; SeGA_5658. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHC29100.1}; KW Transferase {ECO:0000313|EMBL:EHC29100.1}. FT NON_TER 387 387 {ECO:0000313|EMBL:EHC29100.1}. SQ SEQUENCE 387 AA; 42165 MW; CAC3E31B3060DD97 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLHEEDFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYRMESLS AEINYAAAKL ARACADEWTA RTPEKPRFVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGVDLILI ETVFDTLNAK AAVFAVKEEF EALGVDLPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPEHIAA MSRAVVGLPP RQLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVA // ID G5P1X3_SALET Unreviewed; 1137 AA. AC G5P1X3; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 01-APR-2015, entry version 18. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|EMBL:EHC56496.1}; DE Flags: Fragment; GN ORFNames=LTSEJOH_5914 {ECO:0000313|EMBL:EHC56496.1}; OS Salmonella enterica subsp. enterica serovar Johannesburg str. S5-703. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=913077 {ECO:0000313|EMBL:EHC56496.1}; RN [1] {ECO:0000313|EMBL:EHC56496.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=S5-703 {ECO:0000313|EMBL:EHC56496.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHC56496.1}. 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; AFCP01001988; EHC56496.1; -; Genomic_DNA. DR EnsemblBacteria; EHC56496; EHC56496; LTSEJOH_5914. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHC56496.1}; KW Transferase {ECO:0000313|EMBL:EHC56496.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. FT NON_TER 1137 1137 {ECO:0000313|EMBL:EHC56496.1}. SQ SEQUENCE 1137 AA; 125922 MW; 08A13CA06DBEEC68 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLHEEDFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYRMESLS AEINYEAAKL ARACADEWTA RTPEKPRFVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKEEF EALGVDLPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPEHIAA MSRAVVGLPP RQLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VESGAQIIDI NMDEGMLDAE AAMVRFLSLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVEAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRERKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLDLAEKYRG SKTDEAANAQ QAEWRSWDVK KRLEYSLVKG ITEFIEQDTE EARQQASRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EKGSSNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAREVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHARKKPR TPPVTLEAAR DNDLAFDWER YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KLLNPRGVVG LFPANRVGDD IEIYRDETRT HVLTVSHHLR QQTEKVGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAYEAQH DDYNKIMVKA IADRLAEAFA EYLHERVRKV YWGYAPNESL SNDELIRENY QGIRPAP // ID G5PVS6_SALET Unreviewed; 401 AA. AC G5PVS6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|EMBL:EHC64924.1}; GN ORFNames=LTSEMIS_5471 {ECO:0000313|EMBL:EHC64924.1}; OS Salmonella enterica subsp. enterica serovar Mississippi str. A4-633. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=913080 {ECO:0000313|EMBL:EHC64924.1}; RN [1] {ECO:0000313|EMBL:EHC64924.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A4-633 {ECO:0000313|EMBL:EHC64924.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHC64924.1}. 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; AFCR01001582; EHC64924.1; -; Genomic_DNA. DR RefSeq; WP_001639476.1; NZ_AFCR01001582.1. DR EnsemblBacteria; EHC64924; EHC64924; LTSEMIS_5471. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHC64924.1}; KW Transferase {ECO:0000313|EMBL:EHC64924.1}. SQ SEQUENCE 401 AA; 43600 MW; C2561E554B92C9F8 CRC64; MSSKVEQLHA QLSERILVLD GGMGTMIQSY RLHEEDFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYRMESLS AEINYAAAKL ARACADEWTA RTPEKPRFVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKEEF EALGVDLPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPEHIAA MSRAVAGLPP RQLPDIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VESGAQIIDI L // ID G5QBC7_SALMO Unreviewed; 1145 AA. AC G5QBC7; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|EMBL:EHC72449.1}; DE Flags: Fragment; GN ORFNames=LTSEMON_5842 {ECO:0000313|EMBL:EHC72449.1}; OS Salmonella enterica subsp. enterica serovar Montevideo str. S5-403. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=913242 {ECO:0000313|EMBL:EHC72449.1}; RN [1] {ECO:0000313|EMBL:EHC72449.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=S5-403 {ECO:0000313|EMBL:EHC72449.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHC72449.1}. 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; AFCS01001288; EHC72449.1; -; Genomic_DNA. DR RefSeq; WP_000095977.1; NZ_AFCS01001288.1. DR EnsemblBacteria; EHC72449; EHC72449; LTSEMON_5842. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHC72449.1}; KW Transferase {ECO:0000313|EMBL:EHC72449.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. FT NON_TER 1145 1145 {ECO:0000313|EMBL:EHC72449.1}. SQ SEQUENCE 1145 AA; 126665 MW; 85079B70A34A0DE6 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLHEEDFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYRMESLS AEINYAAAKL ARACADEWTA RTPEKPRFVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGVDLILI ETVFDTLNAK AAVFAVKEEF EALGVDLPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPEHIAA MSRAVAGLPP RQLPDIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VESGAQIIDI NMDEGMLDAE AAMVRFLSLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVEAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRERKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLDLAEKYRG SKTDEAANAQ QAEWRSWDVK KRLEYSLVKG ITEFIEQDTE EARQQASRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EKGSSNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAREVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHARKKPR TPPVTLEAAR DNDLAFDWER YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KLLNPRGVVG LFPANRVGDD IEIYRDETRT HVLTVSHHLR QQTEKVGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAYEAQH DDYNKIMVKA IADRLAEAFA EYLHERVRKV YWGYAPNESL SNDELIRENY QGIRPAPPGY PACPE // ID G5QSP7_SALRU Unreviewed; 1137 AA. AC G5QSP7; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 01-APR-2015, entry version 19. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|EMBL:EHC77945.1}; DE Flags: Fragment; GN ORFNames=LTSERUB_6248 {ECO:0000313|EMBL:EHC77945.1}; OS Salmonella enterica subsp. enterica serovar Rubislaw str. A4-653. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=913081 {ECO:0000313|EMBL:EHC77945.1}; RN [1] {ECO:0000313|EMBL:EHC77945.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A4-653 {ECO:0000313|EMBL:EHC77945.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHC77945.1}. 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; AFCT01002244; EHC77945.1; -; Genomic_DNA. DR EnsemblBacteria; EHC77945; EHC77945; LTSERUB_6248. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHC77945.1}; KW Transferase {ECO:0000313|EMBL:EHC77945.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. FT NON_TER 1137 1137 {ECO:0000313|EMBL:EHC77945.1}. SQ SEQUENCE 1137 AA; 125906 MW; 83E0D32F34291B49 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLHEEDFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYRMESLS AEINYEAAKL ARACADEWTA RTPEKPRFVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKEEF EALGVDLPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPEHIAA MSRAVVGLPP RQLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VESGAQIIDI NMDEGMLDAE AAMVRFLSLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVEAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRERKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLDLAEKYRG SKTDEAANAQ QAEWRSWDVK KRLEYSLVKG ITEFIEQDTE EARQQAARPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EKGSSNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAREVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHARKKPR TPPVTLEAAR DNDLAFDWER YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KLLNPRGVVG LFPANRVGDD IEIYRDETRT HVLTVSHHLR QQTEKVGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAYEAQH DDYNKIMVKA IADRLAEAFA EYLHERVRKV YWGYAPNESL SNDELIRENY QGIRPAP // ID G5R8I5_SALSE Unreviewed; 443 AA. AC G5R8I5; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|EMBL:EHC79407.1}; DE Flags: Fragment; GN ORFNames=LTSESEN_6111 {ECO:0000313|EMBL:EHC79407.1}; OS Salmonella enterica subsp. enterica serovar Senftenberg str. A4-543. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=913082 {ECO:0000313|EMBL:EHC79407.1}; RN [1] {ECO:0000313|EMBL:EHC79407.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A4-543 {ECO:0000313|EMBL:EHC79407.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHC79407.1}. 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; AFCU01001936; EHC79407.1; -; Genomic_DNA. DR EnsemblBacteria; EHC79407; EHC79407; LTSESEN_6111. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHC79407.1}; KW Transferase {ECO:0000313|EMBL:EHC79407.1}. FT NON_TER 1 1 {ECO:0000313|EMBL:EHC79407.1}. SQ SEQUENCE 443 AA; 48024 MW; 12128608EA2F3595 CRC64; LAPPSGKATE VGGKLNMSHV ARCSLFRQHA LCQYGSLRGA LSGASVSSKV EQLRAQLNER ILVLDGGMGT MIQSYRLHEE DFRGERFADW PCDLKGNNDL LVLSKPEVIA AIHNAYFEAG ADIIETNTFN STTIAMADYR MESLSAEINY AAAKLARACA NEWTARTPEK PRFVAGVLGP TNRTASISPD VNDPAFRNIT FDQLVAAYRE STKALVEGGV DLILIETVFD TLNAKAAVFA VKEEFEVLGV DLPIMISGTI TDASGRTLSG QTTEAFYNSL RHAEALTFGL NCALGPDELR QYVQELSRIA ECYVTAHPNA GLPNAFGEYD LDADTMAKQI REWAEAGFLN IVGGCCGTTP EHIAAMSRAV AGLPPRQLPD IPVACRLSGL EPLNIGDDSL FVNVGERTNV TGSAKFKRLI KEEKYSEALD VARQQVESGY QYG // ID G5RNM3_SALET Unreviewed; 1137 AA. AC G5RNM3; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EHC85250.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHC85250.1}; DE Flags: Fragment; GN ORFNames=LTSEUGA_5632 {ECO:0000313|EMBL:EHC85250.1}; OS Salmonella enterica subsp. enterica serovar Uganda str. R8-3404. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=913083 {ECO:0000313|EMBL:EHC85250.1}; RN [1] {ECO:0000313|EMBL:EHC85250.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=R8-3404 {ECO:0000313|EMBL:EHC85250.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHC85250.1}. 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; AFCV01001414; EHC85250.1; -; Genomic_DNA. DR RefSeq; WP_001654093.1; NZ_AFCV01001414.1. DR EnsemblBacteria; EHC85250; EHC85250; LTSEUGA_5632. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHC85250.1}; KW Transferase {ECO:0000313|EMBL:EHC85250.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. FT NON_TER 1137 1137 {ECO:0000313|EMBL:EHC85250.1}. SQ SEQUENCE 1137 AA; 125789 MW; B212D2844E4A5B6D CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLHEEDFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARVAADEWTA RTPNKPRYVA GVLGPTNRTA SISPDVNDPA YRNITFDQLV AAYRESTKAL VEGGSDLILI ETVFDTLNAK AAVFAVKEEF EALGVDLPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPEHIAA MSRAVAGLPP RQLPDIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VESGAQIIDI NMDEGMLDAE AAMVRFLSLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVEAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRERKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLDLAEKYRG SKTDEAANAQ QAEWRSWDVK KRLEYSLVKG ITEFIEQDTE EARQQAARPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EKGSSNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAREVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHARKKPR TPPVTLEAAR DNDLAFDWER YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KLLNPRGVVG LFPANRIGDD IEIYRDETRT HVLTVSHHLR QQTEKVGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA IADRLAEAFA EYLHERVRKV YWGYAPNESL SNDELIRENY QGIRPAP // ID G5S3X3_SALET Unreviewed; 1135 AA. AC G5S3X3; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 01-APR-2015, entry version 18. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|EMBL:EHC97515.1}; DE Flags: Fragment; GN ORFNames=LTSEURB_6103 {ECO:0000313|EMBL:EHC97515.1}; OS Salmonella enterica subsp. enterica serovar Urbana str. R8-2977. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=913084 {ECO:0000313|EMBL:EHC97515.1}; RN [1] {ECO:0000313|EMBL:EHC97515.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=R8-2977 {ECO:0000313|EMBL:EHC97515.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHC97515.1}. 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; AFCW01002235; EHC97515.1; -; Genomic_DNA. DR EnsemblBacteria; EHC97515; EHC97515; LTSEURB_6103. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHC97515.1}; KW Transferase {ECO:0000313|EMBL:EHC97515.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. FT NON_TER 1135 1135 {ECO:0000313|EMBL:EHC97515.1}. SQ SEQUENCE 1135 AA; 125754 MW; 5CA06DBEEC685EA3 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLHEEDFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYRMESLS AEINYEAAKL ARACADEWTA RTPEKPRFVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKEEF EALGVDLPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPEHIAA MSRAVVGLPP RQLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VESGAQIIDI NMDEGMLDAE AAMVRFLSLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVEAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRERKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLDLAEKYRG SKTDEAANAQ QAEWRSWDVK KRLEYSLVKG ITEFIEQDTE EARQQASRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EKGSSNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAREVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHARKKPR TPPVTLEAAR DNDLAFDWER YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KLLNPRGVVG LFPANRVGDD IEIYRDETRT HVLTVSHHLR QQTEKVGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAYEAQH DDYNKIMVKA IADRLAEAFA EYLHERVRKV YWGYAPNESL SNDELIRENY QGIRP // ID G5SJP1_SALET Unreviewed; 394 AA. AC G5SJP1; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|EMBL:EHC97752.1}; DE Flags: Fragment; GN ORFNames=LTSEWAN_5986 {ECO:0000313|EMBL:EHC97752.1}; OS Salmonella enterica subsp. enterica serovar Wandsworth str. A4-580. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=913086 {ECO:0000313|EMBL:EHC97752.1}; RN [1] {ECO:0000313|EMBL:EHC97752.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A4-580 {ECO:0000313|EMBL:EHC97752.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHC97752.1}. 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; AFCX01001954; EHC97752.1; -; Genomic_DNA. DR EnsemblBacteria; EHC97752; EHC97752; LTSEWAN_5986. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHC97752.1}; KW Transferase {ECO:0000313|EMBL:EHC97752.1}. FT NON_TER 394 394 {ECO:0000313|EMBL:EHC97752.1}. SQ SEQUENCE 394 AA; 42907 MW; D7BE7F7E926CE2A4 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLHEEDFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYRMESLS AEINYAAAKL ARACADEWTA RTPEKPRFVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGVDLILI ETVFDTLNAK AAVFAVKEEF EALGVDLPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPEHIAA MSRAVAGLPP RQLPDIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VESG // ID G5SRA1_9BACT Unreviewed; 920 AA. AC G5SRA1; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EHH00160.1}; GN ORFNames=HMPREF9441_01891 {ECO:0000313|EMBL:EHH00160.1}; OS Paraprevotella clara YIT 11840. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Paraprevotella. OX NCBI_TaxID=762968 {ECO:0000313|EMBL:EHH00160.1}; RN [1] {ECO:0000313|EMBL:EHH00160.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=YIT 11840 {ECO:0000313|EMBL:EHH00160.1}; 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 (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHH00160.1}. 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; AFFY01000023; EHH00160.1; -; Genomic_DNA. DR RefSeq; WP_008620083.1; NZ_JH376598.1. DR EnsemblBacteria; EHH00160; EHH00160; HMPREF9441_01891. DR OrthoDB; EOG6091CH; -. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHH00160.1}; KW Transferase {ECO:0000313|EMBL:EHH00160.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 242 242 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 764 764 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 920 AA; 100990 MW; BA25A5FC58E504B7 CRC64; MRLEEIVKER ILILDGAMGT MIQRYGLTEA DFRGERFRDV PGLMAGNNDL LSLTRPDVIR DIHRKYLAAG ADIIETNTFS SQRVSMADYH VEDYCREINL AACRIARELA DEFTARNPEK PRFVAGSVGP TNKTCSMSPD VNNPAYRALT FDELVAAYRE QMEALLEGGV DALLIETIFD TLNAKAAIYA AEASMQTVGR RVPLMLSVTV SDKSGRTLSG QTMEAFLTSV AHADIFSLGL NCSFGAHDLI PFLQILAHRS PYYISVYPNA GLPNSMGEYD QTPDQMAEEM KFFVDEGWVN IIGGCCGTTD EYIARFPALV KQGRPHVPAG KAEALCLSGL EQFELTPEVR FVNVGERCNV AGSRKFLRLV KEKNYEEALE IARKQVEDGA LVIDINMDDG LLDARQEMVT FLNLLASEPE ISRVPVMIDS SKWDVITAGL KCVQGKSIVN SISLKEGEEV FLTHAREVKR LGAAVIVMAF DEKGQADTYE RKIEVCARAY RLLVDEVGFN PHDIIFDPNV LAIATGMEEH DNYAVDFIRA AGWIRRNLPG AHVSGGVSNL SFSFRGNNYI REAMHAVFLY HACREGMDMG IVNPATSVMY GDIPSDILTV IEDVVLNRRP DAAERLIELA DKLKAEAEAA KAGQPGADGG GMSAKDAWRS SSVEERLQHA LVKGIDSYLQ EDLEEAAQSY PHAVDIIEGP LMAGMNTVGE LFGAGKMFLP QVVKTARTMK KAVGILQPRI EAEKKEGAAR AGLVLVATVK GDVHDIGKNI VSVVMACNNY EIVDLGVMTP AEEIVAKAKE LHPDIIGLSG LITPSLEEMV HVVGELKRAG LSIPVMIGGA TTSRLHTALK IAPVYDGPVI WMKDASQNAL TAARFLNPDT EGEAFRELRE EQERLRESAG TRRVETVSIE EARQKKLNLF // ID G5ZXE7_9PROT Unreviewed; 302 AA. AC G5ZXE7; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Homocysteine/selenocysteine methylase (S-methylmethionine-dependent) {ECO:0000313|EMBL:EHI49128.1}; GN ORFNames=HIMB100_00006950 {ECO:0000313|EMBL:EHI49128.1}; OS SAR116 cluster alpha proteobacterium HIMB100. OC Bacteria; Proteobacteria; Alphaproteobacteria; SAR116 cluster. OX NCBI_TaxID=909943 {ECO:0000313|EMBL:EHI49128.1}; RN [1] {ECO:0000313|EMBL:EHI49128.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HIMB100 {ECO:0000313|EMBL:EHI49128.1}; RX PubMed=22675578; RA Grote J., Bayindirli C., Bergauer K., Carpintero de Moraes P., RA Chen H., D'Ambrosio L., Edwards B., Fernandez-Gomez B., Hamisi M., RA Logares R., Nguyen D., Rii Y.M., Saeck E., Schutte C., Widner B., RA Church M.J., Steward G.F., Karl D.M., Delong E.F., Eppley J.M., RA Schuster S.C., Kyrpides N.C., Rappe M.S.; RT "Draft genome sequence of strain HIMB100, a cultured representative of RT the SAR116 clade of marine Alphaproteobacteria."; RL Stand. Genomic Sci. 5:269-278(2011). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHI49128.1}. 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; AFXB01000006; EHI49128.1; -; Genomic_DNA. DR RefSeq; WP_009604310.1; NZ_AFXB01000006.1. DR EnsemblBacteria; EHI49128; EHI49128; HIMB100_00006950. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EHI49128.1}; KW Transferase {ECO:0000313|EMBL:EHI49128.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 204 204 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 275 275 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 276 276 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 302 AA; 31792 MW; CE58EB3C4B8ECF2F CRC64; MADLSFLDGG LGQEIQNRAS AQPHPLWSVK VMYDEPELVS AVHRDFITAG ARVITANTYT ASPPRLRRDG DLRQIADIHN TALALARAEM DKAGDPDLQL AGCLPPLVGS YVAEVSMDFG DSLTDYRQLV ALQSGKVDLF LIETISNIAE AKAALTAVKE ADMPGFVGLT ICDDHSNRLR SGEALSDALD QLLPLGPDGL MVNCSLPEAV SKAMSVLAGL PIPFGGYANG FTSIDALKPG GTVASLSART DLGPEAYADF ACSWVEAGAT IIGGCCEVGP AHIAHLAQRL RDDGHRLTGL PV // ID G6A0K2_9PROT Unreviewed; 334 AA. AC G6A0K2; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 01-OCT-2014, entry version 18. DE SubName: Full=Cobalamin-dependent methionine synthase I {ECO:0000313|EMBL:EHI48237.1}; GN ORFNames=HIMB100_00018170 {ECO:0000313|EMBL:EHI48237.1}; OS SAR116 cluster alpha proteobacterium HIMB100. OC Bacteria; Proteobacteria; Alphaproteobacteria; SAR116 cluster. OX NCBI_TaxID=909943 {ECO:0000313|EMBL:EHI48237.1}; RN [1] {ECO:0000313|EMBL:EHI48237.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HIMB100 {ECO:0000313|EMBL:EHI48237.1}; RX PubMed=22675578; RA Grote J., Bayindirli C., Bergauer K., Carpintero de Moraes P., RA Chen H., D'Ambrosio L., Edwards B., Fernandez-Gomez B., Hamisi M., RA Logares R., Nguyen D., Rii Y.M., Saeck E., Schutte C., Widner B., RA Church M.J., Steward G.F., Karl D.M., Delong E.F., Eppley J.M., RA Schuster S.C., Kyrpides N.C., Rappe M.S.; RT "Draft genome sequence of strain HIMB100, a cultured representative of RT the SAR116 clade of marine Alphaproteobacteria."; RL Stand. Genomic Sci. 5:269-278(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. {ECO:0000313|EMBL:EHI48237.1}. 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; AFXB01000010; EHI48237.1; -; Genomic_DNA. DR RefSeq; WP_009605493.1; NZ_AFXB01000010.1. DR EnsemblBacteria; EHI48237; EHI48237; HIMB100_00018170. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 334 AA; 35074 MW; 1511623AF38CEE54 CRC64; MKTSFADLCA SRDWLLADGA TGTNLFRAGL ETGYPPELWN VEHPDRVTGL HSAFIDAGAD ILLTNSFGGT AHRLKLHQAE TRVAELNEAA ARLARAVADA ADKPVLVAGS MGPTGELFEP LGALTPDEAE QAFAEQAIAL AAGGADLLWI ETMSSLEEIE AAVKGARHAD LPVAATMTFD TAGRTMMGIT PAAYADVAAN LGLDAFGANC GIGPAELLDS IHGFVEHKAE LLMVAKGNCG IPAYVDGEIH YHGTPELMAD YAVLARDSGV KIIGGCCGTS PEHVKAMAHA LRTTPPAGSA TRQDVAAKLG EAWSNVPEKP TSEQAERRRR RRRG // ID G6AEF9_9BACT Unreviewed; 916 AA. AC G6AEF9; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHG17158.1}; GN ORFNames=HMPREF9138_00486 {ECO:0000313|EMBL:EHG17158.1}; OS Prevotella histicola F0411. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=857291 {ECO:0000313|EMBL:EHG17158.1}; RN [1] {ECO:0000313|EMBL:EHG17158.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0411 {ECO:0000313|EMBL:EHG17158.1}; 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., Mathney J.M.J., RA Dewhirst F.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 Prevotella histicola F0411."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHG17158.1}. 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; AFXP01000003; EHG17158.1; -; Genomic_DNA. DR RefSeq; WP_008822404.1; NZ_JH376762.1. DR EnsemblBacteria; EHG17158; EHG17158; HMPREF9138_00486. DR OrthoDB; EOG6091CH; -. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 240 240 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 916 AA; 101074 MW; 2CDFBDC02653D8AD CRC64; MSIRDSIKER ILILDGAMGT MIQGYNLTEK DFRGRLELLQ MLNYQGNNDM LNLTRPDVIE DIHRRYLKAG ADIITTNTFS SQRVSQADYH LESSARDMAL EGAKIARKCA DEFSTADKPR FVAGSIGPTN KTCSMSPDVS DPAKRDLTYD SLFESYSEQV AAMIEGGIDV ILIETIFDTL NAKVAVDASI SEMCKAGVDL PVMLSVTITD LSGRTLSGQT LDAFLASVSS YPIFSIGLNC SFGAEQMRPY LKELSAKAPY YISIYPNAGL PNSMGLYDET ADTMVPQMAT YIDDKLVNII GGCCGTTDDF IAGYAKIVKG KSPHIPVEWP KEIILSGLEQ FRLSPEITFV NVGERCNVAG SRKFLRLIKE KNYEEALTIA RKQVDDGALV LDINMDDGLL EAKEEMVHFL NMVSSEPEIA RVPLMIDSSD WSVVVAALKC VQGKSIVNSI SLKEGEDSFI QHAKDVLRYG AAVVVMCFDE EGQATSFERR IEIASRAYKI LTEKVGFPAQ DIIFDPNILA ICTGMKEHNS YALDFIRAAE WIKKNLPGAH VSGGVSNLSF SFRGNNYIRE AMHAVFLYHA IQAGMDFGIV NPATKVTYAD IPEDHLKIIE DVVLDRVEGS DELLIDLANK ILEQKDEQVE DGVNHSSSDQ EAWRSESLEE RLVYALRKGI STYLNEDIHE ALQKYSRAVD VIEGPLMRGM NEVGDLFGAG KMFLPQVVKT ARTMKDAVAI LQPYIEKEKV GGKAIAGKVL LATVKGDVHD IGKNIVGVVM ACNNYEVIDM GVMVPADKII KKAKEEKVDL IGLSGLITPS LQEMVNDVVA FKEAGLKIPV MIGGATTSQL HVALKIAPLY DSPVVWIKDA SVNPSIAAVL LNKRERDNFC KELNKTYECL RAGYKEQQLK ILSLDKAREN KLNLFE // ID G6B1T9_9BACT Unreviewed; 921 AA. AC G6B1T9; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EHJ35942.1}; GN ORFNames=HMPREF0673_02867 {ECO:0000313|EMBL:EHJ35942.1}; OS Prevotella stercorea DSM 18206. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=1002367 {ECO:0000313|EMBL:EHJ35942.1}; RN [1] {ECO:0000313|EMBL:EHJ35942.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 18206 {ECO:0000313|EMBL:EHJ35942.1}; 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 (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHJ35942.1}. 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; AFZZ01000251; EHJ35942.1; -; Genomic_DNA. DR RefSeq; WP_007903103.1; NZ_JH379471.1. DR EnsemblBacteria; EHJ35942; EHJ35942; HMPREF0673_02867. DR OrthoDB; EOG6091CH; -. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHJ35942.1}; KW Transferase {ECO:0000313|EMBL:EHJ35942.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 242 242 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 764 764 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 921 AA; 101146 MW; 2690E775215E3407 CRC64; MKKTLNEVVK DRIMILDGAM GTMIQQYALT EEDFRGYRYR KTPGLMKGNN DMLNITRPDV VSDIHRKYLE AGADIITTNT FSSQRISQAD YHLEEAAREM AFAGARLARK AADEFATDER PRFVAGSVGP TNKTCSMSPD VSNPAAREID YLTLYDVYLE QIEALVEGGA DIILIETVFD TLNAKAAIDA TMEAERRSGK TLPIMLSITV SDLAGRTLSG QTLEAVLASV SSYPLFSIGL NCSFGAPQMK PFLKELARKS PYYISAYPNA GLPNSMGEYD ETAESMAPQM QEYVDEGLVN IIGGCCGTTE KFIAEYAKIV EGKQPHTPQP KSQTMWLSGL ELLDVTPDIR FVNVGERCNV AGSRKFLRLI NEKNYDEAVS IARKQVADGA LVIDINMDDG LLDAREEMRT FLNIIASEPD IAKVPVMIDS SKWDVITAGL QCVQGKAIVN SISLKEGEEV FLSHARDVMR YGAAVVVMCF DEKGQATTYE RRIEIAERAY RLLTEKVGMN PLDIIFDPNV LAIATGMSEH DNYALDFIRA TEWIRTNLPG AHISGGVSNL SFSFRGNNYI REAMHAVFLY HAIGKGMDFG IVNPATKVAY GDIPADQLEI LEDVVLNRRP DASERLVDLA EKIKLQQEAL KNGAAAGVAT ASAAQPEWRK ADVAERLSTA LVKGVADYME DDLQEALTVY PKAVDIIEGP LMAGMNKVGE LFGCGKMFLP QVVKTARTMK KAVAILQPYI EADKKEGTTT AGKVLMATVK GDVHDIGKNI VDVVMSCNNY EVIDLGVMVP AEQIVKKAVA ENVDMIGLSG LITPSLEEMV NVATEMEHAG LDLPIMVGGA TTSEMHVALK IAPVYSGIVV WVKDAAQNPL VAQRLMNAAD RKKFKAELDE RYARLRKEYA AHQQKLSSLD EARKNKLNLF E // ID G6B9E2_PEPDI Unreviewed; 811 AA. AC G6B9E2; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 01-OCT-2014, entry version 16. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EHJ28875.1}; GN ORFNames=HMPREF1122_02468 {ECO:0000313|EMBL:EHJ28875.1}; OS Peptoclostridium difficile 002-P50-2011. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Peptoclostridium. OX NCBI_TaxID=997827 {ECO:0000313|EMBL:EHJ28875.1}; RN [1] {ECO:0000313|EMBL:EHJ28875.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=002-P50-2011 {ECO:0000313|EMBL:EHJ28875.1}; 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 (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. {ECO:0000313|EMBL:EHJ28875.1}. 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; AGAA01000045; EHJ28875.1; -; Genomic_DNA. DR EnsemblBacteria; EHJ28875; EHJ28875; HMPREF1122_02468. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHJ28875.1}; KW Transferase {ECO:0000313|EMBL:EHJ28875.1}. SQ SEQUENCE 811 AA; 88761 MW; 9D55CD245538C4CF CRC64; MKIVKTIETV HIEKERTLVE IRQYLKNNIL IFDGAMGTML QQKGLKLGEN PEVFGLQNPD KLIEIHTAYL EAGSNVILTN TFGCNELKLD SKYTVEEVID NAVLVARKAI ENVDNTKPRY VALDIGPIGE MLEPMGTLSF DKAYEIFKRQ VLQGVKSGVD VIVIETMMDL YEAKVAVLAA KENSDLPIFC TMTFDEGGRS FTGCMPECMV ATIEGLGVDA IGVNCSLGPK QLLPIVEKIA SRATVPVMVQ ANAGLPNIVD GEAIYDVDAK EFFEGVKKFV EVGATIIGGC CGTNPSFIKE ISENINSVTK GCIEKIDECV VCSPSKFVEV QSPTVVGERL NPTGRKSLQE ALKNENVDYA INLGLEQVNA GAQILGVNVG LPEIDEKKLM PKLIREIQAV VDTPLQVDSS NVEALEQGLR YYNGRTIVNS VNGKEESLES ILPIVKKYGS CVVGLTLDEK GIPKKAEERF EIAKRIVNRA VSYGIKPKDI FIDCLSLTVS AQQEEAIETI KAITMVKTLG VKTILGVSNI SFGLPNRKAL NASFLTLALG AGLDLAIINP NEYSMMEAIN SFKILNNTDK GCINYINQYS NINNSKKSDS STKIDKDLPL DILVERGLKD EAKNITLNLL KEKDENYILD EILIPALDKV GKRYDSGDIF LPQLIQSAET VKVSLNTIKE TLLSKSSNNV SKGKIIVATV KGDIHDIGKN IVKIMLENYG YEVIDLGKDV PIEEVVEVAK KRNIKLVGLS ALMTTTVQSM KDTIQALRDN EINAKVFVGG AVLTEEYAEE MGADYYSKDA KSAVEIAKLN F // ID G6BIY8_PEPDI Unreviewed; 811 AA. AC G6BIY8; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 01-OCT-2014, entry version 16. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EHJ28758.1}; GN ORFNames=HMPREF1123_01974 {ECO:0000313|EMBL:EHJ28758.1}; OS Peptoclostridium difficile 050-P50-2011. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Peptoclostridium. OX NCBI_TaxID=997828 {ECO:0000313|EMBL:EHJ28758.1}; RN [1] {ECO:0000313|EMBL:EHJ28758.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=050-P50-2011 {ECO:0000313|EMBL:EHJ28758.1}; 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 (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. {ECO:0000313|EMBL:EHJ28758.1}. 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; AGAB01000047; EHJ28758.1; -; Genomic_DNA. DR EnsemblBacteria; EHJ28758; EHJ28758; HMPREF1123_01974. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHJ28758.1}; KW Transferase {ECO:0000313|EMBL:EHJ28758.1}. SQ SEQUENCE 811 AA; 88761 MW; 9D55CD245538C4CF CRC64; MKIVKTIETV HIEKERTLVE IRQYLKNNIL IFDGAMGTML QQKGLKLGEN PEVFGLQNPD KLIEIHTAYL EAGSNVILTN TFGCNELKLD SKYTVEEVID NAVLVARKAI ENVDNTKPRY VALDIGPIGE MLEPMGTLSF DKAYEIFKRQ VLQGVKSGVD VIVIETMMDL YEAKVAVLAA KENSDLPIFC TMTFDEGGRS FTGCMPECMV ATIEGLGVDA IGVNCSLGPK QLLPIVEKIA SRATVPVMVQ ANAGLPNIVD GEAIYDVDAK EFFEGVKKFV EVGATIIGGC CGTNPSFIKE ISENINSVTK GCIEKIDECV VCSPSKFVEV QSPTVVGERL NPTGRKSLQE ALKNENVDYA INLGLEQVNA GAQILGVNVG LPEIDEKKLM PKLIREIQAV VDTPLQVDSS NVEALEQGLR YYNGRTIVNS VNGKEESLES ILPIVKKYGS CVVGLTLDEK GIPKKAEERF EIAKRIVNRA VSYGIKPKDI FIDCLSLTVS AQQEEAIETI KAITMVKTLG VKTILGVSNI SFGLPNRKAL NASFLTLALG AGLDLAIINP NEYSMMEAIN SFKILNNTDK GCINYINQYS NINNSKKSDS STKIDKDLPL DILVERGLKD EAKNITLNLL KEKDENYILD EILIPALDKV GKRYDSGDIF LPQLIQSAET VKVSLNTIKE TLLSKSSNNV SKGKIIVATV KGDIHDIGKN IVKIMLENYG YEVIDLGKDV PIEEVVEVAK KRNIKLVGLS ALMTTTVQSM KDTIQALRDN EINAKVFVGG AVLTEEYAEE MGADYYSKDA KSAVEIAKLN F // ID G6C3S6_9FUSO Unreviewed; 578 AA. AC G6C3S6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHI78442.1}; GN ORFNames=HMPREF9093_01219 {ECO:0000313|EMBL:EHI78442.1}; OS Fusobacterium sp. oral taxon 370 str. F0437. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=861452 {ECO:0000313|EMBL:EHI78442.1}; RN [1] {ECO:0000313|EMBL:EHI78442.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0437 {ECO:0000313|EMBL:EHI78442.1}; 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 (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. {ECO:0000313|EMBL:EHI78442.1}. 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; AGAD01000141; EHI78442.1; -; Genomic_DNA. DR EnsemblBacteria; EHI78442; EHI78442; HMPREF9093_01219. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; SQ SEQUENCE 578 AA; 64122 MW; 166BBFF83020230E CRC64; MRKIMFEFEK ELRERILVLD GAMGTVLQKY ELTPEDFNGA KGCYEILNET RPDIIFEVHK KYIEAGADII ETNSFNCNAI SLKDYHLEDK VYDLAKKSAE IARDAVKQSG KKVYVFGAIG PTNKSLSFPV GDVPFKRAVS FDEMKEVIKV QVAGLIDGGV DGILLETIFD GLTAKAALLA TEEVFEEKNV KLPISISATV NRQGKLLTGQ SMESLIVALD RNSVTSFGFN CSFGAKDLVP LVIKIKELTT KFVSLHANAG LPNQNGDYVE TAQKMRDDLL PLIENQAINI LGGCCGTSYD HIRAITELVK GQKPRVLPEE NLLETCLSGN EIYNFKDKFT CVGERNNISG SKLFRTMIEE HNYLKALEVA RQQIDAGAKV LDINVDDGIL DSVEEMKNFL RVLQNDSFIA KIPIMIDSSD FAVIEEGLKN TSGKAIVNSI SLKEGTEEFL RKAKIIRNFG ASIVVMAFDE KGQGVSAERK IEISQRAYDL LKSIGVKNSD IVFDPNILSV GTGQEADRYH AREFIKTIDY IHENLKGCGV VGGLSNLSFA FRGNNVLRAA FHHIFLEEVC QEDLILLF // ID G6DMX5_DANPL Unreviewed; 341 AA. AC G6DMX5; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 07-JAN-2015, entry version 14. DE SubName: Full=Putative homocysteine S-methyltransferase isoform 1 {ECO:0000313|EMBL:EHJ65150.1}; GN ORFNames=KGM_03024 {ECO:0000313|EMBL:EHJ65150.1}; OS Danaus plexippus (Monarch butterfly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; OC Papilionoidea; Nymphalidae; Danainae; Danaini; Danaina; Danaus; OC Danaus. OX NCBI_TaxID=13037 {ECO:0000313|EMBL:EHJ65150.1, ECO:0000313|Proteomes:UP000007151}; RN [1] {ECO:0000313|EMBL:EHJ65150.1, ECO:0000313|Proteomes:UP000007151} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F-2 {ECO:0000313|EMBL:EHJ65150.1}; RX PubMed=22118469; DOI=10.1016/j.cell.2011.09.052; RA Zhan S., Merlin C., Boore J.L., Reppert S.M.; RT "The monarch butterfly genome yields insights into long-distance RT migration."; RL Cell 147:1171-1185(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. {ECO:0000313|EMBL:EHJ65150.1}. 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; AGBW01011031; EHJ65150.1; -; Genomic_DNA. DR EnsemblMetazoa; EHJ65150; EHJ65150; KGM_03024. DR InParanoid; G6DMX5; -. DR OMA; GEAIRNW; -. DR Proteomes; UP000007151; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007151}; KW Methyltransferase {ECO:0000313|EMBL:EHJ65150.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007151}; KW Transferase {ECO:0000313|EMBL:EHJ65150.1}. SQ SEQUENCE 341 AA; 38625 MW; B929448AED2A46E9 CRC64; MTPTNEDGVE PPHIVVLDGG FSTQLSCHVG HVIDGDPLWS ARFLHTHPNE VVNTHLDFLR AGANFIITNT YQASVEGFVE HLDLTPEQGY ELITRAVELA KQARTLYLEE YENYIQHDHV PLVVGSVGPY GAHLHDGSEY DGSYADTTSA QTMREWHRPR IQALIEAGVD LLALETIPCQ EEAEMLCDLL REFPNMKAWL SFSCKDNQSI AHGESFQKVA KKCWESNSDQ LVAVGVNCCA PSFVTSLLKG INDDRPHDPI PLIVYPNSGE KYNPQIGWID RDKCEPVEVF IQEWLDLGVR YVGGCCRTYA ADVSRIRNQV HCWRDRWRFQ HKFTSNTQNN N // ID G6DQ07_DANPL Unreviewed; 695 AA. AC G6DQ07; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 07-JAN-2015, entry version 16. DE SubName: Full=Putative translin-associated factor X interacting protein 1 isoform 4 {ECO:0000313|EMBL:EHJ64431.1}; GN ORFNames=KGM_02084 {ECO:0000313|EMBL:EHJ64431.1}; OS Danaus plexippus (Monarch butterfly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; OC Papilionoidea; Nymphalidae; Danainae; Danaini; Danaina; Danaus; OC Danaus. OX NCBI_TaxID=13037 {ECO:0000313|EMBL:EHJ64431.1, ECO:0000313|Proteomes:UP000007151}; RN [1] {ECO:0000313|EMBL:EHJ64431.1, ECO:0000313|Proteomes:UP000007151} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F-2 {ECO:0000313|EMBL:EHJ64431.1}; RX PubMed=22118469; DOI=10.1016/j.cell.2011.09.052; RA Zhan S., Merlin C., Boore J.L., Reppert S.M.; RT "The monarch butterfly genome yields insights into long-distance RT migration."; RL Cell 147:1171-1185(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. {ECO:0000313|EMBL:EHJ64431.1}. 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; AGBW01011947; EHJ64431.1; -; Genomic_DNA. DR EnsemblMetazoa; EHJ64431; EHJ64431; KGM_02084. DR InParanoid; G6DQ07; -. DR Proteomes; UP000007151; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007151}; KW Reference proteome {ECO:0000313|Proteomes:UP000007151}. SQ SEQUENCE 695 AA; 81131 MW; 2DB9AB4E70883E0F CRC64; MEKWHRPRIE ALIDAGVDIL ALETMPCGKE AEMLASMIKN YAQIPAWITF SCKDDRSLVD GEDFQTVAQR CWEINPEQLI GIGVNCCSPK VVGNLFKDIS KGIEPPLSLV TYPNSGEKYT EEGWGERDCD SLDTYVHDWL DLNVKFVGGC CRTYAEDIAQ IRKKKVFGIS MRKKQTDNKV KMLLQENNNL KEENLKLSLK ISRLKREIGK IKDDKFSDYL CLMRERDARY TLYFENVALH LKLRELDGTS RCYSVDDSYG DPVILKIALE KCREQLSAAQ NNLKRMKEEY SETIPRREHD LLDAKCYELT KEVNTLKTEY DIVQNSYKRV LAQKKSLEEE LREVKERCSE LERSGTPRPC WELCGDFISG GRDRWWQLAN GLSSRDMLRV LLKELGPAAE SEHLEYFDGL GTDPAIPPYL RHEGRVRNLR LSRREVRVLV NDIWISRATH RDLPLQDYVT RYFEERYQQP SVRAEWSYNM CAGLEQMMDE PSVKLFWGAL LGQLSEDVYW RLRDAWHTLR DRLYTHNGGQ ETLSIEELEK VTRTTFPLKN EVDIKNLMEV VKKQLKLKIN VVEVNLDKLF FENEEGFDRS ELARELYRQR QLAQDKYIRE VIAELGRRNL NKTISVDCLK RAFAIVDPAI DHIRMERYIR WAFSDQSSEL SAICPLPLRT IVSRLASGDI ERIGPRHKGF RRSYK // ID G6ECD5_9SPHN Unreviewed; 353 AA. AC G6ECD5; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EHJ61070.1}; GN ORFNames=NSU_2006 {ECO:0000313|EMBL:EHJ61070.1}; OS Novosphingobium pentaromativorans US6-1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Novosphingobium. OX NCBI_TaxID=1088721 {ECO:0000313|EMBL:EHJ61070.1, ECO:0000313|Proteomes:UP000004030}; RN [1] {ECO:0000313|EMBL:EHJ61070.1, ECO:0000313|Proteomes:UP000004030} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=US6-1 {ECO:0000313|EMBL:EHJ61070.1}; 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. {ECO:0000313|EMBL:EHJ61070.1}. 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; AGFM01000028; EHJ61070.1; -; Genomic_DNA. DR RefSeq; WP_007012921.1; NZ_AGFM01000028.1. DR EnsemblBacteria; AIT80087; AIT80087; JI59_10055. DR EnsemblBacteria; EHJ61070; EHJ61070; NSU_2006. DR Proteomes; UP000004030; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000004030}; KW Methyltransferase {ECO:0000313|EMBL:EHJ61070.1}; KW Transferase {ECO:0000313|EMBL:EHJ61070.1}. SQ SEQUENCE 353 AA; 37860 MW; 14E6927CCA045292 CRC64; MSPRETFLAE AAKRILITDG AFGTEIQNWK LAEADYAGNL GLSHEQKGNN DILALSKPEV PEAIHRAYFE AGADIAETNT FSANRISQAD YGAEHLVREI NVESARLARK VADEFQAKDA ANGISRPRFV AGAIGPTNKT LSLSPDVNDP GYREIDWDTL VDVYKEQAAA LIEGGADFIL IETVFDTLNA KAGIMAVKQL EAELGREVPI MLSMTLTDLS GRNLSGHTVE AFWHAVRHAR PITIGLNCSF GATQLRPHVK TLSEIADTLI MIYPNAGLPN ELGAYDEMPD TTAGFVGEWA VAGQVNVLGG CCGSTPAHIA AIAQQVKGVA PRKVPSLEPV TRLAGLEPFI MAA // ID G6ETV4_LACDE Unreviewed; 310 AA. AC G6ETV4; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EHE90113.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EHE90113.1}; GN ORFNames=LDBUL1632_00650 {ECO:0000313|EMBL:EHE90113.1}; OS Lactobacillus delbrueckii subsp. bulgaricus CNCM I-1632. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1042399 {ECO:0000313|EMBL:EHE90113.1}; RN [1] {ECO:0000313|EMBL:EHE90113.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CNCM I-1632 {ECO:0000313|EMBL:EHE90113.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHE90113.1}. 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; AGFO01000012; EHE90113.1; -; Genomic_DNA. DR RefSeq; WP_003619413.1; NZ_AGFO01000012.1. DR ProteinModelPortal; G6ETV4; -. DR EnsemblBacteria; EHE90113; EHE90113; LDBUL1632_00650. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHE90113.1}; KW Transferase {ECO:0000313|EMBL:EHE90113.1}. SQ SEQUENCE 310 AA; 33197 MW; A4327A0B0F1501F9 CRC64; MADLPTLLAQ GPVTLDGSMS TPLEAWGEDT NSDLWTAKAL ADNPDLVYRV HQEYFKAGAR VTITDSYQAS LPAFMKHGLS EDAARALIRE SAAVAIKARD DFEKATGIHN FVAGSVGPYG AYLADGSEYR GDYALSHEEY VDFHAPRIEE LVAGGVDCLA VETQPKLSEV RAILDYLKAK YPDLPVYVSF SLKDPATISE GLPLTEAVEE VSAYAQVFAA GANCFKLAWT VDVVKNLRAS KLPIVVYPNS GAEYDPSVKK WVYPPEAADF GQAGAAWLAA GAKLVGGCCT TMPEDIAGLA AAVKKVYTAF // ID G6EU01_LACDE Unreviewed; 69 AA. AC G6EU01; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 01-OCT-2014, entry version 10. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EHE90160.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EHE90160.1}; GN ORFNames=LDBUL1632_00697 {ECO:0000313|EMBL:EHE90160.1}; OS Lactobacillus delbrueckii subsp. bulgaricus CNCM I-1632. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1042399 {ECO:0000313|EMBL:EHE90160.1}; RN [1] {ECO:0000313|EMBL:EHE90160.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CNCM I-1632 {ECO:0000313|EMBL:EHE90160.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHE90160.1}. 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; AGFO01000012; EHE90160.1; -; Genomic_DNA. DR EnsemblBacteria; EHE90160; EHE90160; LDBUL1632_00697. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHE90160.1}; KW Transferase {ECO:0000313|EMBL:EHE90160.1}. SQ SEQUENCE 69 AA; 8009 MW; CC14B46F6424CF3B CRC64; MKEIGKYTFK PLVVYPNLGA SYDPKIKQWR EFKEKFDFNK LTKKCYQEGA RLIGGCCTTG PTEIKQMIV // ID G6EU02_LACDE Unreviewed; 187 AA. AC G6EU02; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 01-OCT-2014, entry version 10. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EHE90161.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EHE90161.1}; GN ORFNames=LDBUL1632_00698 {ECO:0000313|EMBL:EHE90161.1}; OS Lactobacillus delbrueckii subsp. bulgaricus CNCM I-1632. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1042399 {ECO:0000313|EMBL:EHE90161.1}; RN [1] {ECO:0000313|EMBL:EHE90161.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CNCM I-1632 {ECO:0000313|EMBL:EHE90161.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHE90161.1}. 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; AGFO01000012; EHE90161.1; -; Genomic_DNA. DR EnsemblBacteria; EHE90161; EHE90161; LDBUL1632_00698. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHE90161.1}; KW Transferase {ECO:0000313|EMBL:EHE90161.1}. SQ SEQUENCE 187 AA; 21238 MW; 6BC6D6FC6CDEC099 CRC64; MSDELERQGV KTNNKLWTAT ALINELDKVY QAHWDYFTAG AELVITDTYQ ANVQVFTQAG YSEQEAEKFI RDAVKVAKKA RDDYEQKTGK HNYVAGTVGS YGAYLADGNE YRGDYELSEL EYLAFHLPRL RQILAEKPDL IALETQPKLD EPLAVLNWLK ENASDYPIYV SFTLKDATHI SDGTTLE // ID G6F1B2_9PROT Unreviewed; 1164 AA. AC G6F1B2; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=5-methyltetrahydrofolate-S-homocysteine methyltransferase {ECO:0000313|EMBL:EHD13906.1}; GN ORFNames=CIN_12650 {ECO:0000313|EMBL:EHD13906.1}; OS Commensalibacter intestini A911. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae. OX NCBI_TaxID=1088868 {ECO:0000313|EMBL:EHD13906.1}; RN [1] {ECO:0000313|EMBL:EHD13906.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A911 {ECO:0000313|EMBL:EHD13906.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHD13906.1}. 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; AGFR01000007; EHD13906.1; -; Genomic_DNA. DR RefSeq; WP_008854255.1; NZ_AGFR01000007.1. DR EnsemblBacteria; EHD13906; EHD13906; CIN_12650. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHD13906.1}; KW Transferase {ECO:0000313|EMBL:EHD13906.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 225 225 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 292 292 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 738 738 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1164 AA; 129414 MW; 4D820641231F896F CRC64; MSEHNKLLEK LQQQILLCDG GMGSIVQMLD LDIQKDFWGK ENCTEVLNLS RPDLVRDIHR QYFEAGADMV ETNSFGGSIT TLSEFDLQDQ TREINKRAAE IAHEAADLFK DGKERFVVGS IGPGTRLPSL GNIAYDPLEA SITEQCRGLI DGGVNCFLIE TCQDPLQIKA AVNAAKIAQK EANIFLPIFV QVTIETTGTL LVGSDIAAAA TVIDALDVQM MGMNCGTGPR EMGEAIKWLS QYWPRLISMQ PNAGLPELLD GKTHYPLSPE EMGHWMARYI EEQKINMIGG CCGTNPKHIA AMDQVLRERS KNEGTPDRPK AIPRTHIAMP AVASLFSSTP LRQENSLFSI GERCNANGSK KWRDLQAEQD WDGCVTVGRE QLKEGSNALD VCMAFVGRDE IAEMGEIIPR FTSSINAPLV IDSTGSDVIE ACLKLHGGKP IINSINFEDG EEIAAERMVL AKKFGAAVVA LTIDEVGMAK TPEDKLRIAT RLVEFACDRY GLPQSDLMID PLTFTIATGV EDDRKLGLWT LEGIKAIHDK FPDIQIVLGL SNISFGLNPA ARAVLNSVFL YHAQQAGMTS AIVHVSKIRP MHLIDKEEIK VIEDLIFDRR TKDYDPLKKV LEIFADRKAS QAVARPVATT IEEQLHDRIV DGNRKGLEDD LNKAMEKYEP LEIINTLLLS GMKTVGELFG SGKMQLPFVL QSAETMKASV SFLEPFMEKT SDDAKGTMVL ATVKGDVHDI GKNLVDIILS NNGFNVVNLG IKVPVADMIT AAKEHKADAI GMSGLLVKST VIMRENLEEM AEQGLNVPVL LGGAALTRAY VEEDCSEAYS KNNGLVAYAR DAFDGLTLME KIAEGNLEGY VAAQKVQNKR PKRPAKKEKV EAPPLTKEEA TQRRQEMAPK EDVHTPPFWG VKKLESKMKA ILPFLNERSL YQLQWGMKKQ GKTLEEFLEH AKTELRPTLH KLIDLCEKEN ILQPQALYGY WKAAACGEDL ILFDEDGQTE LCRFALPRQP GANRFCITDF IRDINDPVRD VVGLQVVTVG QSASDVARVW FEENRYQDYL YLHGLSVEMT EAMAEYTHQR MRSELGYIGE DDTDMNQLLM QGYRGSRYSF GYPACPNLED QKHILKLLKA EQLGITISDE WQLHPEQSTS ALVIFHPKAK YFIV // ID G6F3T4_LACDE Unreviewed; 106 AA. AC G6F3T4; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 01-OCT-2014, entry version 10. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EHE91489.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EHE91489.1}; GN ORFNames=LDBUL1519_00070 {ECO:0000313|EMBL:EHE91489.1}; OS Lactobacillus delbrueckii subsp. bulgaricus CNCM I-1519. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1042400 {ECO:0000313|EMBL:EHE91489.1}; RN [1] {ECO:0000313|EMBL:EHE91489.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CNCM I-1519 {ECO:0000313|EMBL:EHE91489.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHE91489.1}. 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; AGHW01000002; EHE91489.1; -; Genomic_DNA. DR EnsemblBacteria; EHE91489; EHE91489; LDBUL1519_00070. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHE91489.1}; KW Transferase {ECO:0000313|EMBL:EHE91489.1}. SQ SEQUENCE 106 AA; 11951 MW; 4D99F17442200DF4 CRC64; MIMNKKTGKH NYVAGTVGSY GAYLADGNEY RGDYELSELE YLAFHLPRLR QILAEKPDLI ALETQPKLDE PLAVLNWLKE NASDYPVYVS FTLKDATHIS DGTTLE // ID G6F3Y6_LACDE Unreviewed; 310 AA. AC G6F3Y6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 11. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EHE91541.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EHE91541.1}; GN ORFNames=LDBUL1519_00122 {ECO:0000313|EMBL:EHE91541.1}; OS Lactobacillus delbrueckii subsp. bulgaricus CNCM I-1519. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1042400 {ECO:0000313|EMBL:EHE91541.1}; RN [1] {ECO:0000313|EMBL:EHE91541.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CNCM I-1519 {ECO:0000313|EMBL:EHE91541.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHE91541.1}. 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; AGHW01000002; EHE91541.1; -; Genomic_DNA. DR RefSeq; WP_003622356.1; NZ_AGHW01000002.1. DR EnsemblBacteria; EHE91541; EHE91541; LDBUL1519_00122. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHE91541.1}; KW Transferase {ECO:0000313|EMBL:EHE91541.1}. SQ SEQUENCE 310 AA; 33227 MW; FCD1F99C13683BAB CRC64; MADLPTLLAQ GPVTLDGSMS TPLEAWGEDT NSDLWTAKAL ADNPDLVYRV HQEYFKAGAR VTITDSYQAS LPAFMKHGLS EDAARALIRE SAAVAIKARD DFEKETGIHN FAAGSVGPYG AYLADGSEYR GDYALSHEEY VDFHAPRIEE LVAGGVDCLA VETQPKLSEV RAILDYLKAK YPDLPVYVSF SLKDPATISE GLPLTEAVEE VSAYAQVFAA GANCFKLAWT VDVVKNLRAS KLPIVVYPNS GAEYDPSVKK WVYPPEAADF GQAGAAWLAA GAKLVGGCCT TMPEDIAGLA AAVKKVYTAF // ID G6FPR4_9CYAN Unreviewed; 1179 AA. AC G6FPR4; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 01-APR-2015, entry version 20. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHC18864.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHC18864.1}; GN ORFNames=FJSC11DRAFT_0844 {ECO:0000313|EMBL:EHC18864.1}; OS Fischerella sp. JSC-11. OC Bacteria; Cyanobacteria; Stigonematales; Fischerella. OX NCBI_TaxID=741277 {ECO:0000313|EMBL:EHC18864.1}; RN [1] {ECO:0000313|EMBL:EHC18864.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=JSC-11 {ECO:0000313|EMBL:EHC18864.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHC18864.1}. 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; AGIZ01000002; EHC18864.1; -; Genomic_DNA. DR RefSeq; WP_009455044.1; NZ_AGIZ01000002.1. DR EnsemblBacteria; EHC18864; EHC18864; FJSC11DRAFT_0844. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHC18864.1}; KW Transferase {ECO:0000313|EMBL:EHC18864.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 228 228 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 737 737 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1179 AA; 131599 MW; FD1B4C3FE578DF67 CRC64; MTHPFLERLH SPERPVIVFD GAMGTNLQRQ NLVAEDFGGP EYEGCNEYLV HTKPEAVAKV HRDFLAAGAD VIETDTFGGT SIVLAEYGLA DKAYYLNKTA AQLAKRVAAE FSTPEKPRFV AGSMGPTTKL PTLGHIDFDT MKDAFAQQAE ALWDGGVDLF IVETCQDVLQ IKAALNGIEE VFAKKGDRRP LMVSVTMETM GTMLVGTEIN AVLTILEPYP IDILGLNCAT GPDLMKPHIK YLSEHSPFVV SCIPNAGLPE NVGGKAHYRL TPMELRMSLM HFVEDLGVQV IGGCCGTRPE HIQQLAEIAK ELKPKVREPK LEPAAASIYS IQPYEQDNSF LIIGERINAS GSKKCRELLN AEDWDGLVSM ARAQVKEGAH ILDINVDYVG RDGVRDMHEL VSRIVNNVTL PLMLDSTEWE KMEAGLKVAG GKCLLNSTNY EDGEPRFLKV LELAKKYGAG VVIGTIDEEG MARTADKKFQ IAQRAYRQAL EYGIPAHEIF FDTLALPIST GIEEDRENAK ATIEAIRRIR QELPGCHVVL GVSNISFGLS PAARIVLNSM FLHEAMAAGM DAAIVSANKI LPLAKIEEKH QQVCRQLIYD ERKFEGDVCV YDPLAELTKM FEGVTTKRDK GVDENLPIEE RLKRHIIDGE RIGLDIALAE ALKKYPALDI INIFLLDGMK VVGELFGSGQ MQLPFVLQSA ETMKAAVAYL EPFMEKSAAG DNAKGTFIIA TVKGDVHDIG KNLVDIILSN NGYRVINLGI KQSVESIIEA YEKHKADCIA MSGLLVKSTA FMKENLEVFN EKGITVPVIL GGAALTPKFV YEDCQNTYKG KVVYGKDAFS DLHFMDKLMP AKAAGKWDDL KGFLDEFAQA PQNGHKEPVV REEVEVKAAV EATEVDTRRS EAVAVDIPRP TPPFWGTRLL QPSDISWEEV FWYLDLQALI AGQWQFRKPK EQSKEEYQAF LHEKVYPILE KWKQRIVAEN LLQPQVIYGY FPCQAEGNSL YVYDWNRQDA EDAEVRATFE FPRQKSLRRL CIADFFAPKE SGVIDVFPMQ AVTVGEVATV YAQKLFADNQ YTDYLYFHGL AVQMAEALAE WTHARIRREL GFAAEEPDNI RDVLAQRYRG SRYSFGYPAC PNIQDQYKQL ELLGAKRINL YMDESEQLYP EQSTTAIICY HPVAKYFSA // ID G6XH24_9PROT Unreviewed; 1168 AA. AC G6XH24; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=5-methyltetrahydrofolate-S-homocysteine methyltransferase {ECO:0000313|EMBL:EHH69482.1}; GN ORFNames=GMO_07890 {ECO:0000313|EMBL:EHH69482.1}; OS Gluconobacter morbifer G707. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Gluconobacter. OX NCBI_TaxID=1088869 {ECO:0000313|EMBL:EHH69482.1}; RN [1] {ECO:0000313|EMBL:EHH69482.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=G707 {ECO:0000313|EMBL:EHH69482.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHH69482.1}. 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; AGQV01000001; EHH69482.1; -; Genomic_DNA. DR RefSeq; WP_008850939.1; NZ_AGQV01000001.1. DR EnsemblBacteria; EHH69482; EHH69482; GMO_07890. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHH69482.1}; KW Transferase {ECO:0000313|EMBL:EHH69482.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 225 225 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 292 292 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 735 735 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1168 AA; 129122 MW; 0778D4E1BEF2DE16 CRC64; MSKRPHLLDA LTDQVLLCDG GMGSRVQMLD LEVDRDYWGQ ENCTEILNLS RPELVREIHR GYFEAGADMV ETNTFGGSTV TLAEFDLQDR AREINRIAAT LAREAAETFS DDRHRYVIGS IGPGTKLPTL GNIDYDTLEA GIAEQCRGLV EGGVDAFLIE TCQDTLQIKA AVNAAKLARQ ELRSDAPIFV QVTVETTGTL LVGPDIAAAA TTVQALDVPS LGLNCATGPQ EMGEHVRWLS ENWPGLISMQ PNAGLPELVD GKTVYPLSPT EMAIWMERFI QEDGLNLIGG CCGTSTPHIQ ALDDMLRRLG DEKYRPAPVK RSTIWMPSVS SLYTQVPLRQ ENSYFSIGER CNANGSKKWR ELQEAGDWDG CVGIGREQAA EGSNALDICT AFVGRNETAE MTEVITRFTS SVNAPLVIDS TETPVIEAAL KLHGGKPVIN SINFEDGEEH AHDRMKLARK FGAAMIALTI DEVGMAKEPQ DKLRIAERLV DFACNQYGLP QSDLMIDPLT FTIATGVEDD RKLGQWTLEG IRLIREKFPE IQIILGLSNI SFGLNPAARA VLNSVFLDHA VKAGMTGAIV HVSKIRPLHL IAPEEVKVAE DLIFDRRTED YDPLQKLLEL FAGRKAADAV KKRRAETPAE RLKDRIVDGD RKGIEEDLEA AMQEMPPLDI INNVLLDGMK VVGELFGSGK MQLPFVLQSA ETMKTAVAWL EPHMERVEGQ HRGTMVLATV KGDVHDIGKN LVDIILTNNG YQVINLGIKV PLADMIAAAK KHTAHAIGMS GLLVKSTVIM RENLEEMQRQ GINLPVILGG AALTRNYVEE ECAASYGGGT PGRVAYARDA FDGLALMDRV AQNEFDGYLA AIQSRRAGKP SRRKERAPET AETRGFGVVD RDAARARRER ISGSLPPVTP PFWGSRVIEA PPNAVLPFLN ERSLYQFQWG FRKQGRSLEE FMEYAKQELR PVLKRMLALS AEQNIIRPQA SYGYWKAAGD GNDLVLFHED GQTEAARFTL PRQPKDDGEC IADFVRDIGD EVRDVIGLQV VTVGQKASDL AREWFEANRY QDYLYLHGLS VEMAEAMAEY THKRIRAELG FAAEDSRDME KLLSQGYRGS RYSFGYPACP KLENQEPILK LLDAERIGVS LSDGYQLHPE QSTSALVILN PQAKYFTV // ID G6XRN5_RHIRD Unreviewed; 1257 AA. AC G6XRN5; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EHH07581.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHH07581.1}; GN Name=metH {ECO:0000313|EMBL:EHH07581.1}; GN ORFNames=ATCR1_06931 {ECO:0000313|EMBL:EHH07581.1}; OS Agrobacterium tumefaciens CCNWGS0286. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium; OC Agrobacterium tumefaciens complex. OX NCBI_TaxID=1082932 {ECO:0000313|EMBL:EHH07581.1}; RN [1] {ECO:0000313|EMBL:EHH07581.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCNWGS0286 {ECO:0000313|EMBL:EHH07581.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHH07581.1}. 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; AGSM01000003; EHH07581.1; -; Genomic_DNA. DR RefSeq; WP_004430640.1; NZ_AGSM01000003.1. DR EnsemblBacteria; EHH07581; EHH07581; ATCR1_06931. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHH07581.1}; KW Transferase {ECO:0000313|EMBL:EHH07581.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 260 260 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 776 776 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1257 AA; 138745 MW; 73F3E6121E671AEC CRC64; MFDDLFGPEG AKRDGAEIFK ALREAASERI LILDGAMGTQ IQGLGFDEDH FRGDRFIGCA CHQKGNNDLL ILTQPDAIEE IHYRYAMAGA DILETNTFSS TRIAQADYEM ENAVYDLNRE GAQIVRRAAQ RAEREDGRRR FVAGAIGPTN RTASISPDVN NPGYRAVTFD DLRIAYGEQI DGLIDGGADI ILIETIFDTL NAKAAIFACE ERFEAKGIRL PVMISGTITD LSGRTLSGQT PSAFWNSVRH ANPFTIGLNC ALGADAMRPH LQELSDVADT FVCAYPNAGL PNEFGQYDET PEMMARQVEG FVRDGLVNIV GGCCGSTPEH IRAIAEAVKD YKPRPIPEHK PFMSLSGLEP FVLTKDIPFV NVGERTNVTG SAKFRKLITA GDYTAALAVA RDQVENGAQI IDINMDEGLI DSEKAMVEFL NLIAAEPDIA RVPVMIDSSK FEIIEAGLKC VQGKPIVNSI SLKEGEEKFL QQARLVHNYG AAVVVMAFDE VGQADTYQRK VEICSRAYKL LTEKAGLSPE DIIFDPNVFA VATGIEEHNN YGVDFIEATK TIRETMPLTH ISGGVSNLSF SFRGNEPVRE AMHAVFLYHA IQVGMDMGIV NAGQLAVYDN IDAELREACE DVVLNRRDDA TERLLEVAER FRGTGAKDTK VQDLSWRELP VEKRLEHALV NGITDFIEAD TEEARQKAER PLHVIEGPLM AGMNVVGDLF GSGKMFLPQV VKSARVMKQA VAVLLPYMEE EKRLNGGSER SAAGKVLMAT VKGDVHDIGK NIVGVVLACN NYEIIDLGVM VPTTKILETA IAEKVDVIGL SGLITPSLDE MVHVAAEMER QGFDIPLLIG GATTSRVHTA VKIHPRYEQG QAIYVTDASR AVGVVSALLS AEQKPAYIDG IRSEYAKVAE AHARNEREKL RLPLSRAREN AHKIDWSSYS AVKPQFFGTK VFETYDLEEL SRYIDWTPFF QTWELKGRFP AILEDEKQGE AARQLYSDAQ AMLKKIIEEN WFRPRAVIGF WPANAVGDDI RLFTDESRKE ELATFFTLRQ QLSKRDGRPN VALSDFVAPV DSGVADYVGG FVVTAGIEEV AIAERFERAN DDYSSILVKA LADRFAEAFA ERMHERVRKE FWGYAPDEAF AGDELIGEAY AGIRPAPGYP AQPDHTEKKT LFALLDATNA AGVELTESYA MWPGSSVSGL YIGHPESYYF GVAKVERDQV LDYARRKDMP VEEVERWLGP VLNYVPTNAA EEIDSAA // ID G6Y0M7_RHIRD Unreviewed; 303 AA. AC G6Y0M7; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=S-methyltransferase {ECO:0000313|EMBL:EHH03051.1}; GN ORFNames=ATCR1_22384 {ECO:0000313|EMBL:EHH03051.1}; OS Agrobacterium tumefaciens CCNWGS0286. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium; OC Agrobacterium tumefaciens complex. OX NCBI_TaxID=1082932 {ECO:0000313|EMBL:EHH03051.1}; RN [1] {ECO:0000313|EMBL:EHH03051.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCNWGS0286 {ECO:0000313|EMBL:EHH03051.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHH03051.1}. 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; AGSM01000019; EHH03051.1; -; Genomic_DNA. DR RefSeq; WP_003509454.1; NZ_AGSM01000019.1. DR EnsemblBacteria; EHH03051; EHH03051; ATCR1_22384. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EHH03051.1}; KW Transferase {ECO:0000313|EMBL:EHH03051.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 303 AA; 31744 MW; D1346A86116FD8CC CRC64; MSTIRILDGG MSRELQRLGA VLKQPEWSAL ALIDAPEIVR QVHQEFIEAG ADVVTTNSYA LVPFHIGEER FQKDGASLIA LSGKLAREAA DASGRKVLVA GSLPPIFGSY EPQNFDAGRV QAYLMVLVDN LAPHVDVWLG ETLSLIAEGE AVREAVAATG KPFWISFTLN DDAAATGGEP ALRSGETVKA AAEWAAQSGA AALLFNCSKP EVMKAAVETA AAVFAEKGVS LEIGVYANAF EGEQGDSAAN EGLHDTRADL TDDVYSRFAC SWADAGATMI GGCCGIGAAH IHKVATALRR AAA // ID G6YAD2_9RHIZ Unreviewed; 312 AA. AC G6YAD2; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 12. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EHH11287.1}; GN ORFNames=MEA186_14522 {ECO:0000313|EMBL:EHH11287.1}; OS Mesorhizobium amorphae CCNWGS0123. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=1082933 {ECO:0000313|EMBL:EHH11287.1}; RN [1] {ECO:0000313|EMBL:EHH11287.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCNWGS0123 {ECO:0000313|EMBL:EHH11287.1}; 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGSN01000110; EHH11287.1; -; Genomic_DNA. DR RefSeq; WP_006202427.1; NZ_AGSN01000110.1. DR EnsemblBacteria; EHH11287; EHH11287; MEA186_14522. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHH11287.1}; KW Transferase {ECO:0000313|EMBL:EHH11287.1}. SQ SEQUENCE 312 AA; 33285 MW; 704AEC56F20B1CB8 CRC64; MTMAKINLRE LSEAVLLTDG GLETSLVFLD GLDLPSFAAF PLLGEEEGRE RLGRYFRQYL DIADKYGVGF VLDTPTWRAN PDWGEKLCYS KKALSGIDQQ AVSWARALAA PYAARGMIVL VNGVVGPRGD GYRVETVMTP AEAEAYHGDQ IKAFRDAGAD MISAVTMTYS QEAAGIACAA MGAGLPSVIS FTVETDGRLP SGESLKDAIE TVDDETDGAP AYFMINCAHP SHFEAVLAGD GGWLGRIRGV RANASAKSHA ELDAATELDP GDPVDLGRRY RAMRDRFGHI GVLGGCCGTD ARHIAAICDA CL // ID G6YCM1_9RHIZ Unreviewed; 299 AA. AC G6YCM1; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EHH10343.1}; GN ORFNames=MEA186_18532 {ECO:0000313|EMBL:EHH10343.1}; OS Mesorhizobium amorphae CCNWGS0123. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=1082933 {ECO:0000313|EMBL:EHH10343.1}; RN [1] {ECO:0000313|EMBL:EHH10343.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCNWGS0123 {ECO:0000313|EMBL:EHH10343.1}; 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGSN01000128; EHH10343.1; -; Genomic_DNA. DR RefSeq; WP_006203297.1; NZ_AGSN01000128.1. DR EnsemblBacteria; EHH10343; EHH10343; MEA186_18532. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 299 AA; 31592 MW; 00D9081B0444ECB5 CRC64; MKKVVLTDGG MGQELVRRSK SEPTPLWSAR VLIDEPDLVR DLHAEFIRAG ACVITINTYS ATPERLVREG AEDLFKQLQK RGIELARQAC EQAGEATIAG CLSPLFGSYA PALTISYQET LDTYRRIVAE QADGVDLFLC ETMASTDEAR AAVTAASESG KPVWVSWTLA DHGAPRLRSG EAIAAASGAL DGMPLAARLI NCCRPEAVSA ALPELIALGG PVGAYANGFT SVEALKHGGT VEVLHARHDL DPEAYADQAI GWVEAGASIV GGCCEVGPAH IAALHDRLEQ AGYQISGVQ // ID G6YCS3_9RHIZ Unreviewed; 338 AA. AC G6YCS3; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=Methionine synthase I {ECO:0000313|EMBL:EHH10395.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHH10395.1}; GN ORFNames=MEA186_18792 {ECO:0000313|EMBL:EHH10395.1}; OS Mesorhizobium amorphae CCNWGS0123. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=1082933 {ECO:0000313|EMBL:EHH10395.1}; RN [1] {ECO:0000313|EMBL:EHH10395.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCNWGS0123 {ECO:0000313|EMBL:EHH10395.1}; 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGSN01000128; EHH10395.1; -; Genomic_DNA. DR RefSeq; WP_006203355.1; NZ_AGSN01000128.1. DR EnsemblBacteria; EHH10395; EHH10395; MEA186_18792. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHH10395.1}; KW Transferase {ECO:0000313|EMBL:EHH10395.1}. SQ SEQUENCE 338 AA; 35336 MW; F7B17A07E429272A CRC64; MTNPIEALLA EKGVLLADGA TGTNLFAMGL EAGEAPELLN ETAPATITSL HQNFVDAGAD IILTNSFGGT RHRLKLHHAQ DRVHALNKRA AEIACAVADK AGRKVIVAGS VGPTGELLVP LGAMTYDEAV DAFAEQIEGL KDGGAEVAWI ETMSAPDEIR AAAEAAIRVG LPYTYTGSFD TAGRTMMGLL PKDIHGVVDG LSTAPLGVGA NCGVGASDIL ASLLDMTDAK PEATVIVKGN CGIPEFRGTE IHYSGTPELM ADYVRLAVDA GARIVGGCCG TSFQHLAAMR KALDAHTKEG RPTVETIVER IGPMRNKVAT ANTAETSEAR RERRRGRA // ID G6YR83_9ALTE Unreviewed; 1232 AA. AC G6YR83; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EHJ05254.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHJ05254.1}; GN Name=metH {ECO:0000313|EMBL:EHJ05254.1}; GN ORFNames=KYE_06868 {ECO:0000313|EMBL:EHJ05254.1}; OS Marinobacter manganoxydans MnI7-9. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Marinobacter. OX NCBI_TaxID=1094979 {ECO:0000313|EMBL:EHJ05254.1}; RN [1] {ECO:0000313|EMBL:EHJ05254.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MnI7-9 {ECO:0000313|EMBL:EHJ05254.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AGTR01000026; EHJ05254.1; -; Genomic_DNA. DR RefSeq; WP_008171685.1; NZ_AGTR01000026.1. DR EnsemblBacteria; EHJ05254; EHJ05254; KYE_06868. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHJ05254.1}; KW Transferase {ECO:0000313|EMBL:EHJ05254.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1232 AA; 136900 MW; 7AE91704C969BFE0 CRC64; MTDRTTRLDQ LHKALQERIV ILDGGMGTMI QNLKLDEKAF RGDRFADYER EVQGNNDLLN LTQPALLRNI HADYLDAGAD IIETNTFNST QLSQADYGLE AIARELNVAA AELARQIADE YTAKNPEKPR FVAGAVGPTS RTASISPDVN NPGYRNVDFQ TLVDNYYEAV GGLVEGGCDL ILIETIFDTL NAKAAIYATQ QYFEDSGITL PIMISGTITD ASGRTLSGQT TEAFWNSVAH AKPISVGLNC ALGADALRPY VEELSAKAET YVSAHPNAGL PNEFGEYDQT PEEMAEIIEG FARDGFLNII GGCCGSRPDH IEAIAQAVSK YPPRKIPERP KALRLSGLEP FTGDDNVLFI NVGERTNVTG SKRFLRLIKE EQYEEALSVA RDQVENGAQI IDINMDEGML ESKEVMVTFL NLVASEPDIS RVPIMIDSSK WDVIEAGLRC IQGKAVVNSI SLKEGEEEFV KRARDCMRYG AAVVVMAFDE QGQADTYERK TEICKRSYDV LTGIGFNPAD IIFDPNIFAI ATGIEEHNNY AVDFINATRW IRENLPHASI SGGVSNVSFS FRGNDVVREA IHSVFLYHAI KAGMNMGIVN PGQLVIYDEI DPELKELVED VVLNRRDDST DRLLEIAERY KGKGGKTQEE DLAWREWPVE KRLEHALVKG ITTYIVDDTE ACRQRATHPI EVIEGPLMDG MNVVGDLFGD GKMFLPQVVK SARVMKQAVA HLIPYIEAEK TEDQKAKGKI LMATVKGDVH DIGKNIVGVV LQCNNYEVID LGVMVPCDKI LAAAKEHDVD LIGLSGLITP SLDEMVHVAR EMQRLDFNIP LMIGGATTSK AHTAVKIEPQ YKNDIALYVS DASRCVNVAS QLLSKNAKPE FVEAARTEYD EIRERRKNRG DRTKLVSLKE ARDRAPDISF EGYQPPKPAF TGIRVFEEYD LNELVDYIDW TPFFMSWDIS GKYPAIFDDP KRGEAARHLF DDAQKILHRM IDEKRVSARG VIGFWPANRR GDDVVLYTDE SCTEELTTLH HLRQQDEKAP GKPMMALSDF VAPEGSGTVD YVGGFAVTTG IGAEEFSVEF KDANDDYNAI MVKALADRLA EAFAERMHER VRQEFWGYAA DEKLANDDLI KERYRGIRPA PGYPACPDHT EKATLFNLLE ATDTAGIELT EHFAMFPTAA VSGWYFAHPE SKYFAVGKIG ADQVEDYAER KGISKAEAER WLAPSLAYDP AE // ID G6YSB4_9ALTE Unreviewed; 301 AA. AC G6YSB4; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EHJ04858.1}; GN ORFNames=KYE_08773 {ECO:0000313|EMBL:EHJ04858.1}; OS Marinobacter manganoxydans MnI7-9. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Marinobacter. OX NCBI_TaxID=1094979 {ECO:0000313|EMBL:EHJ04858.1}; RN [1] {ECO:0000313|EMBL:EHJ04858.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MnI7-9 {ECO:0000313|EMBL:EHJ04858.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGTR01000032; EHJ04858.1; -; Genomic_DNA. DR RefSeq; WP_008172376.1; NZ_AGTR01000032.1. DR EnsemblBacteria; EHJ04858; EHJ04858; KYE_08773. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EHJ04858.1}; KW Transferase {ECO:0000313|EMBL:EHJ04858.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 200 200 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 271 271 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 272 272 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 301 AA; 32034 MW; 770463E25A5FFD2F CRC64; MKSVALLDGG LGQEIYRRAM NVTSLLWSVA VMREQPDVVT DVHADFIRAG ARTLTLNTYA ATPTRLAREG LGDEIGAIHQ RAFEVLERAI ALTGADVDIA GCLPPLVGSY RSQPDRTFED LKSEFDILVK LQSGADVFLI ETMTNSLEAK AACAAANESG KPFGVAFRLE ADGKLRSGET LAEAVEAVRA SGPTAIMLNC CDPEVISQAM PELAGLYPCT GGYANAFKTV EPMAGGALVD ELEARQDVSP GVYGLQVKQW LDDGAGVVGG CCEITPEHIS HLADVLTGEY NLIRFSELAR G // ID G7CMJ8_MYCTH Unreviewed; 1191 AA. AC G7CMJ8; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase MetH {ECO:0000313|EMBL:EHI10818.1}; GN ORFNames=KEK_21223 {ECO:0000313|EMBL:EHI10818.1}; OS Mycobacterium thermoresistibile ATCC 19527. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=1078020 {ECO:0000313|EMBL:EHI10818.1}; RN [1] {ECO:0000313|EMBL:EHI10818.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 19527 {ECO:0000313|EMBL:EHI10818.1}; RG Tuberculosis Structural Genomics Consortium; RA Ioerger T.R.; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHI10818.1}. 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; AGVE01000052; EHI10818.1; -; Genomic_DNA. DR RefSeq; WP_003927704.1; NZ_AGVE01000052.1. DR EnsemblBacteria; EHI10818; EHI10818; KEK_21223. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHI10818.1}; KW Transferase {ECO:0000313|EMBL:EHI10818.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 231 231 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 297 297 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 298 298 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 742 742 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1191 AA; 130296 MW; 2DCD8D7F01BB88A2 CRC64; MTPVDTAVYD TDLLETLSRR VMVGDGAMGT QLQAADLTLD DFNGLEGCNE ILNETRPDVI AEIHRNYLAA GADAVETNTF GCNLSNLGDY DIADKIRSLS EQGTAIARRV ADEMSTPDHR RYVLAAMGPG TKLPTLGHTE FGVIRDAYIE AALGMLDGGA DAILIETCQD LLQLKAAVLG ARRAMARAGR HIPIITHVTV ETTGTMLLGS EIGAALTAIE PLGVDVIGLN CATGPAEMSE HLRYLSRHSR LPVSVMPNAG LPVLGPDGAV YPLRPDELAE ALAGFVSEFG LSLVGGCCGT TPEHIRQVVD AVSGVQRAGR QISYEPGLSS LYTSTPFAQD ASVLMIGERT NANGSKAFRE AMIAEDYQRC LDIAKEQTRD GAHLLDLCVD YVGRDGVADM KALASRLATA STLPIMLDST ETDVLRAGLE HLGGRCAVNS VNYEDGAGPE SRFHKTMELV AEHGAAVVAL TIDEEGQART AEHKVAIAER LIEDITTNWG VEKSSILVDC LTFTICTGQE ESRRDGIETI EAIRELKKRH PDVQTTLGLS NISFGLNPAA RQVLNSVFLH ECREAGLDSA IVHASKILPM NRIDEKQREV ALDLIYDRRR EGYDPLQELM TMFEGVSTAD SKESRAAELA KLPVLERLAQ RIVDGERNGL EADLDEAMTI KPPLEIINEH LLAGMKVVGE LFGAGQMQLP FVLQSAEVMK AAVAHLEPHM EKSEDDSGKG RIVLATVKGD VHDIGKNLVD IILTNNGYEV VNLGIKQPIS TILEVAEDKN ADVVGMSGLL VKSTVVMKEN LEEMNARGVA ERFPVLLGGA ALTRGYVEDD LSEIYEGEVY YARDAFEGLR LMDRIMSEKR GGGPDPDSPE AIAAREKEAE RKARRARSKR IAAERKAKEE PVEVPARSDV AADVEVPVPP FWGTRIVKGV AVADYAGTLD ERALFLGQWG LRGARGGDGP SYEELVETEG RPRLRYWLDR LATEGILAHA AVVYGYFPAV SQGDDVIVLT EPEPDADERF RFTFPRQQRG RFLCIADFIR SRELAAKTGQ VDVLPFQLVT MGQPIADFAN ELFASNAYRD YLEVHGIGVQ LTEAFAEYWH RRIREELRFG DRAMAAEDPE SVEEYFKLGY RGARFSFGYG ACPDLEDRKK MMELLEPERI GVVLSEELQL HPEQSTDAFV LHHPEAKYFN V // ID G7DGW8_BRAJP Unreviewed; 318 AA. AC G7DGW8; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 29-APR-2015, entry version 22. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:BAL05791.1}; GN ORFNames=BJ6T_04930 {ECO:0000313|EMBL:BAL05791.1}; OS Bradyrhizobium japonicum USDA 6. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=1037409 {ECO:0000313|EMBL:BAL05791.1, ECO:0000313|Proteomes:UP000005663}; RN [1] {ECO:0000313|EMBL:BAL05791.1, ECO:0000313|Proteomes:UP000005663} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=USDA 6 {ECO:0000313|EMBL:BAL05791.1}; 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; BAL05791.1; -; Genomic_DNA. DR RefSeq; WP_014490691.1; NZ_AXAV01000007.1. DR RefSeq; YP_005605379.1; NC_017249.1. DR EnsemblBacteria; BAL05791; BAL05791; BJ6T_04930. DR KEGG; bju:BJ6T_04930; -. DR BioCyc; BJAP1037409:GL9L-493-MONOMER; -. DR Proteomes; UP000005663; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005663}. SQ SEQUENCE 318 AA; 34451 MW; BC2805E188E09FB7 CRC64; MAKYRDNLPQ RHGGIFLTDG GMETTLIFHK GLELPHFAAF VLLDSEAGRS HLKQYYEAYL AIARQHGLGF VLDGPTWRAN PDWGAKLGYD MDALTAVNMR AIRFLEELRG PWETSGLPCV INGAIGPRGD GYKAGNMDAT EAMDYHSSQI ASFAEAGADM VTAFTLNSVN EAIGVVRAAK MHAIPVAISF TVETDGCLVR GETLREAIET VDHVTERACE YFLINCAHPT HFESALQAGE PWVERIHGVR ANASAKSHAE LDESEVLDSG DPADLGRRYV ALRRAFPRMQ LLGGCCGTDH RHAAAICAAC VPPQAAGA // ID G7DK43_BRAJP Unreviewed; 1284 AA. AC G7DK43; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:BAL13672.1}; GN ORFNames=BJ6T_84290 {ECO:0000313|EMBL:BAL13672.1}; OS Bradyrhizobium japonicum USDA 6. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=1037409 {ECO:0000313|EMBL:BAL13672.1, ECO:0000313|Proteomes:UP000005663}; RN [1] {ECO:0000313|EMBL:BAL13672.1, ECO:0000313|Proteomes:UP000005663} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=USDA 6 {ECO:0000313|EMBL:BAL13672.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP012206; BAL13672.1; -; Genomic_DNA. DR RefSeq; WP_014498249.1; NZ_AXAV01000025.1. DR RefSeq; YP_005613260.1; NC_017249.1. DR EnsemblBacteria; BAL13672; BAL13672; BJ6T_84290. DR KEGG; bju:BJ6T_84290; -. DR KO; K00548; -. DR BioCyc; BJAP1037409:GL9L-8426-MONOMER; -. DR Proteomes; UP000005663; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000005663}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 770 770 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1284 AA; 140030 MW; 939233FAE8C31863 CRC64; MTVSTSPKRT ALLNAARERI LVLDGAMGTM IQNLQFDEAA FRGERFKDFH RDLRGNNDLL ILTQPQAIED IHAAYLRAGA DIVATNTFST TSIAQADYDL TDIVYEMARE GARLAGNAAR RVEAEDGKPR FVAGAIGPTN RTASISPDVS NPGYRAVTFD DLRKSYGEQI NGMLDGGVDL LLVETIFDTL NAKAALYAIA EITEARGIDV PVMVSGTITD KSGRLLSGQM PEAFWNSVRH AKPVTIGFNC ALGAEDLRAH IADIGRVADT LVCAYPNAGL PNEFGQYDET PEYMARLVGE FARDGLVNIV GGCCGTTPDH IAAIAAAVAP HKPRIVPEIE PRLRLSGLEP FILTDAIPFV NVGERTNVTG SARFRKLITA GDYTAALQVA RDQVENGAQI IDVNMDEGLL DSEAAMVTFL NLVAAEPDIA RVPVMVDSSK FSVIESGLKC VQGKPVVNSI SMKEGEEKFI HEAKIARRHG AAVVVMAFDE VGQADTFARK TEICKRAYDI LVDRVGFPPE DIIFDPNIFA IATGIEEHNN YGVDFIEATR WIRQNLPGAH ISGGVSNLSF SFRGNEPVRE AMHSVFLYHA IKAGMDMGIV NAGQMIVYDD IDAELRQVCE DVILNRDPGA SERLLALAEK FRGNKTQTKE ADLAWREWPV EKRLSHSLVH GITEFIDVDT EEARKASKRP LDVIEGPLMA GMNVVGDLFG DGKMFLPQVV KSARVMKQAV AWLMPFMEEE KARNLANGIG TEGSSSAGKI VLATVKGDVH DIGKNIVGIV LQCNNFEVID LGVMVPAAKI VETVKAEKAD IVGLSGLITP SLDEMAFFAG ELQREGLKLP LLIGGATTSR VHTAVKIDPS YRAGPVVHVN DASRAVGVAS SLLSPEKREA YAAEVRAEYA KISDAHLRAQ ADKKRLKLAA ARANRVPVDF AANKPVKPTF LGIRSFDDYD LAELVPYIDW TPFFQTWELA GRFPAILDDS KVGEVARSLY DDARKMLDLI VKEKWFRARA TVGFWPANAE GDDIVLYADE SRTRQIATLH TLRQQLEKRE GRFNAALADF VAPAGSGVPD YVGGFVVTAG IGEDVVADRF KMANDDYSSI LCKALADRLA EAFAERMHAR VRREFWAYAP DEALSSEDLI LEKYQGIRPA PGYPAQPDHT EKATLFELLD AEATAGVKLT ESFAMWPGSS VSGLYFANPE SYYFGVGKIE RDQVEDYAAR KGMTVAETER WLAPVLNYIP SQQTDKAFAA TPANDETSKD LASHPPGCTC AVHLVWQKKR AGAG // ID G7EAG9_MIXOS Unreviewed; 352 AA. AC G7EAG9; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 29-APR-2015, entry version 15. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:GAA99829.1}; GN Name=Mo06532 {ECO:0000313|EMBL:GAA99829.1}; GN ORFNames=E5Q_06532 {ECO:0000313|EMBL:GAA99829.1}, GN L969DRAFT_43183 {ECO:0000313|EMBL:KEI42319.1}; 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 {ECO:0000313|EMBL:GAA99829.1, ECO:0000313|Proteomes:UP000009131}; RN [1] {ECO:0000313|Proteomes:UP000009131} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS 9802 / IAM 14324 / JCM 22182 / KY 12970 RC {ECO:0000313|Proteomes:UP000009131}; 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). RN [2] {ECO:0000313|EMBL:GAA99829.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=IAM 14324 {ECO:0000313|EMBL:GAA99829.1}; RX PubMed=22724063; DOI=10.1098/rsob.120043; RA Nishida H., Kondo S., Matsumoto T., Suzuki Y., Yoshikawa H., RA Taylor T.D., Sugiyama J.; RT "Characteristics of nucleosomes and linker DNA regions on the genome RT of the basidiomycete Mixia osmundae revealed by mono- and dinucleosome RT mapping."; RL Open Biol. 2:120043-120043(2012). RN [3] {ECO:0000313|EMBL:KEI42319.1, ECO:0000313|Proteomes:UP000027399} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS 9802 / IAM 14324 / JCM 22182 / KY 12970 RC {ECO:0000313|Proteomes:UP000027399}, and RC IAM 14324 {ECO:0000313|EMBL:KEI42319.1}; RX PubMed=24372469; DOI=10.1111/nph.12653; RA Toome M., Ohm R.A., Riley R.W., James T.Y., Lazarus K.L., RA Henrissat B., Albu S., Boyd A., Chow J., Clum A., Heller G., RA Lipzen A., Nolan M., Sandor L., Zvenigorodsky N., Grigoriev I.V., RA Spatafora J.W., Aime M.C.; RT "Genome sequencing provides insight into the reproductive biology, RT nutritional mode and ploidy of the fern pathogen Mixia osmundae."; RL New Phytol. 202:554-564(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; BABT02000240; GAA99829.1; -; Genomic_DNA. DR EMBL; KL411542; KEI42319.1; -; Genomic_DNA. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000009131; Unassembled WGS sequence. DR Proteomes; UP000027399; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 2. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009131}; KW Reference proteome {ECO:0000313|Proteomes:UP000009131}. SQ SEQUENCE 352 AA; 37793 MW; A139458F3DF5CC7C CRC64; MTTLLEAALG SRTGPLLLDG GMSTTLEDEL GASTDHPLWS SHLLSDAKGR QQIQKVHQMF HDAGSDIIQT NTYQMDESLC EANGLSATEL VSNAIALARS VKGSPLVALS LGPYGALTSP GSEYSGHYTG PYGPFESSLP DSRVDPSSTL PPASDAECYE DALTDFHTKR LRTFLASEKP DLLAFETVPL LTEVRAIRRA VRLCQTELPY WISFVLPDGI CPQSTHPTID AKRCTLEALT LAALQGEQPP VAIGINCTHP SLIASNVIRM ARTVSSHKLS IPWLVLYPDG GLTYDTVTKS WHAREAQQSD RSWADALLDA ASTGDRAFAG YILGGCCKST PSYIAALRSI SG // ID G7EF70_9GAMM Unreviewed; 357 AA. AC G7EF70; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:GAA59542.1}; GN ORFNames=P20652_1405 {ECO:0000313|EMBL:GAA59542.1}; OS Pseudoalteromonas sp. BSi20652. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=388384 {ECO:0000313|EMBL:GAA59542.1}; RN [1] {ECO:0000313|EMBL:GAA59542.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BSi20652 {ECO:0000313|EMBL:GAA59542.1}; 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] {ECO:0000313|EMBL:GAA59542.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BSi20652 {ECO:0000313|EMBL:GAA59542.1}; 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. {ECO:0000313|EMBL:GAA59542.1}. 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; BADT01000085; GAA59542.1; -; Genomic_DNA. DR RefSeq; WP_008167901.1; NZ_BADT01000085.1. DR EnsemblBacteria; GAA59542; GAA59542; P20652_1405. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:GAA59542.1}; KW Transferase {ECO:0000313|EMBL:GAA59542.1}. SQ SEQUENCE 357 AA; 38970 MW; 499EFA32752E1247 CRC64; MPNNAPTNNK QAEISAALKE RILILDGAMG TMIQDHKLEE EDYRGERFKD WHVLIKGNND LLSLTKPDLI TDIHRGFLSA GADIIETNTF NSTTISMEDY DMASLSREIN LESAKLARAI CDEFTAKTPE KPRYVAGVLG PTSKTCSISP DVNDPGYRNV TFDKLVTAYI ESTLALMEGG ADLILIETIF DTLNAKAASF GVEEAFEQAG RKLPVMISGT ITDASGRTLS GQTTEAFYNS IRHIKPISIG LNCALGPDLL RQYVEELSRV CETFTSVHPN AGLPNEFGEY DLEADDMATE IIDWGKSGFI NIVGGCCGTT PAHIRAFAKG LAGVKPRQLP ELEVRMRLSG LEACNLN // ID G7ESY9_9GAMM Unreviewed; 356 AA. AC G7ESY9; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=B12-dependent homocysteine-N5-methyltetrahydrofolate transmethylase {ECO:0000313|EMBL:GAA64012.1}; GN ORFNames=P20311_1804 {ECO:0000313|EMBL:GAA64012.1}; OS Pseudoalteromonas sp. BSi20311. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=383911 {ECO:0000313|EMBL:GAA64012.1, ECO:0000313|Proteomes:UP000005146}; RN [1] {ECO:0000313|EMBL:GAA64012.1, ECO:0000313|Proteomes:UP000005146} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BSi20311 {ECO:0000313|EMBL:GAA64012.1}; 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BADU01000078; GAA64012.1; -; Genomic_DNA. DR RefSeq; WP_008111932.1; NZ_BADU01000078.1. DR EnsemblBacteria; GAA64012; GAA64012; P20311_1804. DR Proteomes; UP000005146; Unassembled WGS sequence. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005146}; KW Methyltransferase {ECO:0000313|EMBL:GAA64012.1}; KW Transferase {ECO:0000313|EMBL:GAA64012.1}. SQ SEQUENCE 356 AA; 38945 MW; FB1FCB3619B66E32 CRC64; MPNNPQNNKH QELSAALKQR ILILDGAMGT MIQAHKLEEQ DYRGERFKDW HVLIKGNNDL LSLTKPEIIT DIHRSFLAAG ADIIETNTFN STTISMEDYD MASISREVNL ESAKLARAVC DEFSAKTPEK PRYVAGVLGP TSKTCSLSPD VNDPGYRNIT FDKLVTAYVE STLALMEGGV DIILIETIFD TLNAKAASFA VEEAFEQAGR TLPVMISGTI TDASGRTLSG QTTEAFYNSI RHIKPLSIGL NCALGPDLLR QYVEELSRVC ETFVSVHPNA GLPNEFGEYD LEADDMAKEI IDWGKSGFIN IVGGCCGTTP AHIRAFAKGL EGAAPRKLPE LEVRMRLSGL EACNLN // ID G7EU78_9GAMM Unreviewed; 300 AA. AC G7EU78; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:GAA64451.1}; GN ORFNames=P20311_2247 {ECO:0000313|EMBL:GAA64451.1}; OS Pseudoalteromonas sp. BSi20311. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=383911 {ECO:0000313|EMBL:GAA64451.1, ECO:0000313|Proteomes:UP000005146}; RN [1] {ECO:0000313|EMBL:GAA64451.1, ECO:0000313|Proteomes:UP000005146} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BSi20311 {ECO:0000313|EMBL:GAA64451.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BADU01000095; GAA64451.1; -; Genomic_DNA. DR RefSeq; WP_008112796.1; NZ_BADU01000095.1. DR EnsemblBacteria; GAA64451; GAA64451; P20311_2247. DR Proteomes; UP000005146; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005146}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:GAA64451.1}; KW Transferase {ECO:0000313|EMBL:GAA64451.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 204 204 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 279 279 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 280 280 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 300 AA; 32632 MW; E6BD9C8A4A2A914A CRC64; MSKLTILDGG MGRELKRMGA PFSQPLWSAQ ALIEAPQCVT QAHQAFINAG AEIITVNSYA CVPFHLGETL YQAQGATLAQ QAAVIAKEAA QKTKQNVLVA GSLPPAFGSY RADFFQSERA FTILDTLYKA QDEYIDIWIG ETISSIEEAH VMASVLNNSK KPCYYAFTLS DEVSEQATLR SGELVSDATL ALLEHNIAGI FFNCSIPEVI EQALRDTNRV LKQQNKHLNL GAFANSFTPI ASDYKANEGS QGYRDLSPAE YVAFAKQWHN LGATIIGGCC GIGPEFIAAL VKWKSDIKAL // ID G7F0J7_9GAMM Unreviewed; 357 AA. AC G7F0J7; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:GAA66670.1}; GN ORFNames=P20429_0782 {ECO:0000313|EMBL:GAA66670.1}; OS Pseudoalteromonas sp. BSi20429. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=1097676 {ECO:0000313|EMBL:GAA66670.1}; RN [1] {ECO:0000313|EMBL:GAA66670.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BSi20429 {ECO:0000313|EMBL:GAA66670.1}; 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] {ECO:0000313|EMBL:GAA66670.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BSi20429 {ECO:0000313|EMBL:GAA66670.1}; 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BADV01000022; GAA66670.1; -; Genomic_DNA. DR RefSeq; WP_007581206.1; NZ_BADV01000022.1. DR EnsemblBacteria; GAA66670; GAA66670; P20429_0782. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:GAA66670.1}; KW Transferase {ECO:0000313|EMBL:GAA66670.1}. SQ SEQUENCE 357 AA; 38885 MW; 187BB5CB19FE1152 CRC64; MPNNAPTNNK QAEISAALKE RILILDGAMG TMIQDHKLEE EDYRGERFKD WHVLIKGNND LLSLTKPDLI TDIHRGFLSA GADIIETNTF NSTTISMEDY DMASLSREIN LESAKLARAI CDEFTAKTPE KPRYVAGVLG PTSKTCSISP DVNDPGYRNV TFDKLVTAYI ESTLALMEGG ADLILIETIF DTLNAKAASF GVEEAFEQAG RTLPVMISGT ITDASGRTLS GQTTEAFYNS IRHIKPISIG LNCALGPDLL RQYVEELSRV CETFTSVHPN AGLPNEFGEY DLEAGDMATE IIDWGKSGFI NIVGGCCGTT PAHIRAFAKG LAGVKPRQLP ELEVRMRLSG LEACNLN // ID G7FY00_9GAMM Unreviewed; 357 AA. AC G7FY00; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:GAA78023.1}; GN ORFNames=P20495_0513 {ECO:0000313|EMBL:GAA78023.1}; OS Pseudoalteromonas sp. BSi20495. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=386429 {ECO:0000313|EMBL:GAA78023.1}; RN [1] {ECO:0000313|EMBL:GAA78023.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BSi20495 {ECO:0000313|EMBL:GAA78023.1}; 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] {ECO:0000313|EMBL:GAA78023.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BSi20495 {ECO:0000313|EMBL:GAA78023.1}; 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BADY01000016; GAA78023.1; -; Genomic_DNA. DR RefSeq; WP_008133982.1; NZ_BADY01000016.1. DR EnsemblBacteria; GAA78023; GAA78023; P20495_0513. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:GAA78023.1}; KW Transferase {ECO:0000313|EMBL:GAA78023.1}. SQ SEQUENCE 357 AA; 39007 MW; A598D0F3E9158E50 CRC64; MPNNAPTNNK QAEISAALKE RILILDGAMG TMIQDHKLEE EDYRAERFKD WHVLIKGNND LLSLTKPDLI TDIHRGFLSA GADIIETNTF NSTTISMEDY DMANLSREIN LESAKLARAI CDEFTAKTPE KPRYVAGVLG PTSKTCSISP DVNDPGYRNV TFDKLVTAYI ESTLALMEGG ADLILIETIF DTLNAKAASF GVEEAFEQAG RKLPVMISGT ITDASGRTLS GQTTEAFYNS IRHIKPISIG LNCALGPDLL RQYVEELSRV CETFTSVHPN AGLPNEFGEY DLEAPEMATE IIDWGKSGFI NIVGGCCGTT PAHIRAFAKG LAGVKPRQLP ELEVRMRLSG LEACNLN // ID G7GE79_9GAMM Unreviewed; 1228 AA. AC G7GE79; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 01-APR-2015, entry version 21. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:GAB01904.1}; GN Name=metH {ECO:0000313|EMBL:GAB01904.1}; GN ORFNames=ACT4_023_00800 {ECO:0000313|EMBL:GAB01904.1}; OS Acinetobacter sp. NBRC 100985. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=1071390 {ECO:0000313|EMBL:GAB01904.1}; RN [1] {ECO:0000313|EMBL:GAB01904.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NBRC 100985 {ECO:0000313|EMBL:GAB01904.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; BAEB01000023; GAB01904.1; -; Genomic_DNA. DR RefSeq; WP_007481585.1; NZ_BAEB01000023.1. DR EnsemblBacteria; GAB01904; GAB01904; ACT4_023_00800. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1228 AA; 135394 MW; 5A26D049B424D895 CRC64; MSTLATLQSL LAQRILIIDG AMGTMIQRHK LEEEDYRGDR FADWASDLKG NNDLLVLTQP QIIQGIHEAY LDAGADIIET NSFNGTRVSM SDYHMEDLVP EINREAARLA RAACDKYSTP DKPRFVAGVL GPTSRTCSIS PNVNDPAYRN ITFDELKENY IEAAHALIEG GADIILIETV FDTLNCKAAI FAVKEVFKQI GYELPLMISG TITDASGRTL TGQTAEAFWN SVRHGDLLSI GFNCALGADA MRPHVKTIAD VADTFVSAHP NAGLPNAFGE YDETPEQTAA FIKEFAESGL INITGGCCGT TPDHIRAIYN AVKDIPPRQV PETIPACRLS GLEPFNIDEN SLFVNVGERT NVTGSKKFLR LIREENFAEA LEVAQQQVEA GAQIIDINMD EGMLDSQNAM VHFLNLVASE PDISRVPIMI DSSKWEIIEA GLKCVQGKPV VNSISLKEGY DEFVEKARLC RQYGAAIIVM AFDETGQADT AARKREICKR SYDVLVNDVG FPAEDIIFDP NVFAVATGIE EHNNYGVDFI EATGWIKQNL PHAMISGGVS NVSFSFRGNE PVREAIHSVF LYYAIKQGMT MGIVNAGQMA IYDDIPKELK DAVEDVILNQ NQGESGNDAT EKLLEVAEKF RGHGGAAKEA ENLEWRNESV EKRLEYALVK GITTYIDEDT EEARLKAKRP LDVIEGALMD GMNVVGDLFG SGKMFLPQVV KSARVMKQAV AWLNPYIEAE KTGSQSKGKV LMATVKGDVH DIGKNIVGVV LGCNGYDIVD LGVMVPCEKI LQTAIDEKCD IIGLSGLITP SLDEMVFVAK EMQRKGFDIP LLIGGATTSK AHTAVKIDPQ YQNDAVIYVA DASRAVGVAT TLLSKEMRGN FIAEHRAEYA KIRERLANKQ PKAAKLSYAE SIENGFKVDD NYVPPIPNTL GTQVITNYPL ATLVEYFDWT PFFISWSLAG KFPKILTDEV VGEAATDLYN QAQEMLKDII ENHRFDARAV FGLYPAQRTA ADTVSVFDAT GQNVTHTFEH IRQQSDKVTG KPNLSLADFI STSKDNTDYL GGFTVSIFGA EELADEYKAK GDDYSAILIQ SLADRFAEAF AEHLHERIRK EFWGYKADET LSNEELIKEK YVGIRPAPGY PACPEHSEKA VLFDWLGSEA KIGTKLTEHF AMMPPSSVSG FYYSHPQSEY FNVGKISQDQ LEDYAKRKGW TLDEAKRWLA PNLDDSIG // ID G7GJG6_9ACTO Unreviewed; 1192 AA. AC G7GJG6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:GAB03741.1}; GN Name=metH {ECO:0000313|EMBL:GAB03741.1}; GN ORFNames=GOAMR_04_00580 {ECO:0000313|EMBL:GAB03741.1}; OS Gordonia amarae NBRC 15530. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Gordoniaceae; Gordonia. OX NCBI_TaxID=1075090 {ECO:0000313|EMBL:GAB03741.1}; RN [1] {ECO:0000313|EMBL:GAB03741.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NBRC 15530 {ECO:0000313|EMBL:GAB03741.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; BAED01000004; GAB03741.1; -; Genomic_DNA. DR RefSeq; WP_005181765.1; NZ_BAED01000004.1. DR EnsemblBacteria; GAB03741; GAB03741; GOAMR_04_00580. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 238 238 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 748 748 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1192 AA; 129358 MW; 99651A54AB9FD37B CRC64; MSYRKSHATE QAGYDSSFLS AMSRRVLIGD GAMGTMLQAA DLTLDDFNGL EGCNEILNDT RPDVLAGIHR AYFEAGADAV ETNTFGCNLS NLGDYDIADR IRELSYKGTA IARGVADEMG VSADGTPRFV LGSIGPGTKL PSLGHTTFEI IRNAYFECVA GMLDGGADAI LVETSQDLLQ VKAAVIAARR AMAELGRSIP IISHVTVETT GTMLLGSEIG AALTAIEPLG VDMIGLNCAT GPAEMSEHLR YLSKHSRIPV SVMPNAGLPV LGPNGAEYPL APDELAEALS GFVSGFGLAF VGGCCGTTPE HIRQVAEAVA QVTPAVRAPD HQSETSSLYT AVPFDQDASF LVIGERTNSN GSKAFREAMI AGDYQKCLDA AKDQTRDGAH MLDLNVDYVG RDGAADMTAL ATRFATSSTL PIMIDSTEPD VIQAGLEALG GRCAVNSVNY EDGDGPDSRF ARIMRLVVEH GAAVVALTID EEGQARTADH KVRIAERLIA EITGEWGLSE EDIIIDALTF PISTGQEEVR RDGIETIEAI RRLKEAHPEI HFTLGISNIS FGLNPAARQV LNSVFLHECV QAGLDTAIVH ASKILPMARI PDEQRTVALD LVYNRRTDDY DPLQKLMELF EGVSAASARE SRAAELAKLP LFERLERRIV DGERNGLEAD LDEAMTTVPP LKIINETLLS GMKTVGELFG SGQMQLPFVL QSAEVMKTAV AHLEPHMEST GDSGKGRIVL ATVKGDVHDI GKNLVDIILS NNGYEVVNIG IKQPISTILE VAEDKKADVI GMSGLLVKST VVMKENLEEI NSRGLADTYP VLLGGAALTR AYVENDLTDT YDGDVHYARD AFEGLRLMDD IMATKRGEGP DPDSPEAIAA AKKAADRKAR HERSKKIAAK RKAAEVPVEV PARSDVVSDN QIPTPPFWGT RIIKGVPVAD YLQLLDERAL FLGQWGLRGT RGGDGPSYED LVESEGRPRL RHWIDRLSTE NILQHAAVVY GYFPAVSEGD AVHVLTEPRP DAPVRYTFEF PRQQRSRFLC IADFIASRES AVAAGHVDVL PFQLVTMGQP IADFANKLFA EDAYRDYLEV HGIGVQLTEA LAEYWHQRVR SELSFGGEDP ENPQGFFDLE YRGARFSFGY GACPDLDDRA KMIDLLEPER IGVTLSEELQ LHPEQSTDAF VLHHPEAKYF NT // ID G7H0J4_9ACTO Unreviewed; 1193 AA. AC G7H0J4; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:GAB09369.1}; GN Name=metH {ECO:0000313|EMBL:GAB09369.1}; GN ORFNames=GOARA_036_01010 {ECO:0000313|EMBL:GAB09369.1}; OS Gordonia araii NBRC 100433. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Gordoniaceae; Gordonia. OX NCBI_TaxID=1073574 {ECO:0000313|EMBL:GAB09369.1}; RN [1] {ECO:0000313|EMBL:GAB09369.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NBRC 100433 {ECO:0000313|EMBL:GAB09369.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; BAEE01000036; GAB09369.1; -; Genomic_DNA. DR RefSeq; WP_007321445.1; NZ_BAEE01000036.1. DR EnsemblBacteria; GAB09369; GAB09369; GOARA_036_01010. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 235 235 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 301 301 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 302 302 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 745 745 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1193 AA; 129587 MW; 243881349BE818B6 CRC64; MDPSSPTASN YDSTLLSAMS ERVLIGDGAM GTMLQAADLT LDDFLGLEGC NEILNETRPD VLAHIHRAYF EAGADLVETN TFGCNQSNLG DYDIADRITD LAYRGTAIAR GVADEMGKTA YGTDRFVVGS IGPGTKLPSL GHTTFGVLRD AYQQCAVGML DGGADAILIE TAQDLLQVKA AVVASRRAME ARGRHIPILV HVTVETTGTM LLGSEIGAAL TALEPLGIDV IGLNCATGPA EMSEHLRYLS RHARIPVSVM PNAGLPVLGP NGAEYPLTAE ELAVALRDFV TDYGLSMVGG CCGTTPEHIR QVAEAVAAVE RAPREQQHES ATSSLYTSVP FAQDASFLVI GERTNSNGSK AFREAMIAED YQHCLDVAKE QTRDGAHMLD LNVDYVGRDG AQDMTALATR FATSSTLPIM IDSTEPEVIR AGLEALGGRC AVNSVNFEDG DGPGSRYQRI MELVVEHGAA VVALTIDEEG QARTADDKVR IAERLIADLT STWGLTDEDI IVDALTFPIS TGQEEVRRDG IETIEAIRRL KAAHPSLHFT LGISNISFGL NPAARQVLNS VFLHECVQVG LDTAIVHASK ILPMARIPEE QRETALDLVY DRRRDGYDPL QKLMELFEGV SAASARESRA AELAALPLFE RLERRIVDGE RAGLEADLDE AMTQVPPLQI INETLLSGMK TVGELFGSGQ MQLPFVLQSA EVMKSAVAHL EPHMEATGDS GKGRIVLATV KGDVHDIGKN LVDIILSNNG YEVVNLGIKQ PINTILEAAR DKNADVIGMS GLLVKSTVVM KENLEEMNSR GAAQYPVLLG GAALTRAYVE NDLTETYEGE VHYARDAFEG LRLMDDIMAT KRGEGPAPDS PEAIEAAQKA AERKARHARS KAIAAKRKAA EEPVEVPARS DVATDNEIPV PPFWGNRIVK GIPVAEYREM LDERALFLGQ WGLRGTRGGD GPSYEELVET EGRPRLRYWI DRLATEGILA HAAVVYGYFP AVSEGNTVHV LTEPDPAAPV LLSMDFPRQQ RPRFLCVADF IASREAAIES GRPDVLPMQL VTMGTPIADF ANTLFAENAY RDYLEVHGIS VQLTEALAEY WHQRVRSELT FAEGSMAEED PDDPQGFFDL EYRGARYSFG YGACPNLEDR AHIVDLLESE RIGVTLSEEL QLHPEQSTDA FVLHHPEAKY FNT // ID G7HDD3_9BURK Unreviewed; 355 AA. AC G7HDD3; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:CCE48021.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CCE48021.1}; DE SubName: Full=MetH2 protein {ECO:0000313|EMBL:CDN61505.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CDN61505.1}; GN Name=metH2 {ECO:0000313|EMBL:CDN61505.1}; GN ORFNames=I35_1852 {ECO:0000313|EMBL:CCE48021.1}, GN I35_2982 {ECO:0000313|EMBL:CDN61505.1}; OS Burkholderia cenocepacia H111. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=1055524 {ECO:0000313|EMBL:CCE48021.1}; RN [1] {ECO:0000313|EMBL:CCE48021.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=H111 {ECO:0000313|EMBL:CCE48021.1}; 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] {ECO:0000313|EMBL:CDN61505.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=H111 {ECO:0000313|EMBL:CDN61505.1}; RX PubMed=24723723; DOI=10.1128/genomeA.00298-14; RA Carlier A., Agnoli K., Pessi G., Suppiger A., Jenul C., Schmid N., RA Tummler B., Pinto-Carbo M., Eberl L.; RT "Genome Sequence of Burkholderia cenocepacia H111, a Cystic Fibrosis RT Airway Isolate."; RL Genome Announc. 2:e00298-e00214(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; CAFQ01000019; CCE48021.1; -; Genomic_DNA. DR EMBL; HG938370; CDN61505.1; -; Genomic_DNA. DR RefSeq; WP_006495429.1; NZ_HG934864.1. DR EnsemblBacteria; CCE48021; CCE48021; I35_1852. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:CCE48021.1}; KW Transferase {ECO:0000313|EMBL:CCE48021.1}. SQ SEQUENCE 355 AA; 38167 MW; 9C620C99AE424719 CRC64; MSATPLAAST PLDARYTRGA ALPALLKSRI LILDGAMGTM IQRYKLDEAA YRGERFKDFP RDIKGNNELL SLTQPQIIRE IHDQYFAAGA DIVETNTFGA TTVAQADYGM EDLVVEMNVA SAKLARESAA KYATPDKPRF VAGAIGPTPK TASISPDVND PGARNVTFDE LRTAYYQQAK ALLDGGVDLF LVETIFDTLN AKAALFALDE LFEDTGERLP IMISGTVTDA SGRILSGQTV EAFWNSLRHA KPLTFGLNCA LGAALMRPYI AELAKLCDTY VSCYPNAGLP NPMSDTGFDE TPDVTSGLLK EFAQAGLVNL AGGCCGTTPE HIAEIAKALA GVKPRRWPNQ YSDNA // ID G7K1K6_MEDTR Unreviewed; 326 AA. AC G7K1K6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Homocysteine S-methyltransferase-like protein {ECO:0000313|EMBL:AES97600.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:AES97600}; GN OrderedLocusNames=MTR_5g056640 {ECO:0000313|EMBL:AES97600.1}; 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 {ECO:0000313|EMBL:AES97600.1, ECO:0000313|Proteomes:UP000002051}; RN [1] {ECO:0000313|EMBL:AES97600.1, ECO:0000313|EnsemblPlants:AES97600, ECO:0000313|Proteomes:UP000002051} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A17 {ECO:0000313|EMBL:AES97600.1}, and RC cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES97600, RC ECO:0000313|Proteomes:UP000002051}; RX PubMed=22089132; DOI=10.1038/nature10625; RA Young N.D., Debelle F., Oldroyd G.E.D., Geurts R., Cannon S.B., RA Udvardi M.K., Benedito V.A., Mayer K.F.X., 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.T., Tang H., Rombauts S., Zhao P.X., Zhou P., RA Barbe V., Bardou P., Bechner M., Bellec A., Berger A., Berges H., RA Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R., RA Deshpande S., Dai X., Doyle J.J., Dudez A.-M., Farmer A.D., RA Fouteau S., Franken C., Gibelin C., Gish J., Goldstein S., RA Gonzalez A.J., Green P.J., Hallab A., Hartog M., Hua A., RA Humphray S.J., Jeong D.-H., Jing Y., Jocker A., Kenton S.M., RA Kim D.-J., Klee K., Lai H., Lang C., Lin S., Macmil S.L., RA Magdelenat G., Matthews L., McCorrison J., Monaghan E.L., Mun J.-H., RA Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R., RA Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., RA Sallet E., Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., RA Schiex T., Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., RA Singer S.R., Sinharoy S., Sterck L., Viollet A., Wang B.-B., Wang K., RA Wang M., Wang X., Warfsmann J., Weissenbach J., White D.D., RA White J.D., Wiley G.B., Wincker P., Xing Y., Yang L., Yao Z., Ying F., RA Zhai J., Zhou L., Zuber A., Denarie J., Dixon R.A., May G.D., RA 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). RN [2] {ECO:0000313|EMBL:AES97600.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A17; RX PubMed=24767513; DOI=10.1186/1471-2164-15-312; RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S., RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F., RA Schwartz D.C., Town C.D.; RT "An improved genome release (version Mt4.0) for the model legume RT Medicago truncatula."; RL BMC Genomics 15:312-312(2014). RN [3] {ECO:0000313|EnsemblPlants:AES97600} RP IDENTIFICATION. RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES97600}; RG EnsemblPlants; RL Submitted (APR-2015) 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; CM001221; AES97600.1; -; Genomic_DNA. DR RefSeq; XP_003614642.1; XM_003614594.1. DR EnsemblPlants; AES97600; AES97600; MTR_5g056640. DR GeneID; 11422561; -. DR KEGG; mtr:MTR_5g056640; -. DR KO; K00547; -. DR OMA; GEAIRNW; -. DR Proteomes; UP000002051; Chromosome 5. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002051}; KW Methyltransferase {ECO:0000313|EMBL:AES97600.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002051}; KW Transferase {ECO:0000313|EMBL:AES97600.1}. SQ SEQUENCE 326 AA; 36004 MW; B96AEFA03887BBFF CRC64; MKGEKKSLLQ DLIENSGGCV VTDGGFATQL EKHGAFINDP LWSAICLIKQ PHLIKKVHME YLEAGADILV TSSYQATIPG FLSKGLSIEE GESLLQRSVK LAVEARDSFW SSAKRNPGNK YRRALVAASI GSYGAYLADG SEYRGLYGPD VSLVKLKDFH RRRLQVLVEA GPDLLAFETI PNKLEAQACV ELLEEINVQI PSWICFTSVD GENAPSGESF QYCLEVINKS NKVEAVGINC APPHFMESLI PKFKQLTNKA IVVYPNSGEV WDGIAKKWLP SKCFHDDDFG FYATRWRELG AKIIGGCCRT TPSTIQIISN ALRENI // ID G7LUZ1_9ENTR Unreviewed; 321 AA. AC G7LUZ1; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 07-JAN-2015, entry version 12. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EHD20937.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EHD20937.1}; GN ORFNames=BrE312_1529 {ECO:0000313|EMBL:EHD20937.1}; OS Brenneria sp. EniD312. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Brenneria. OX NCBI_TaxID=598467 {ECO:0000313|EMBL:EHD20937.1, ECO:0000313|Proteomes:UP000002759}; RN [1] {ECO:0000313|EMBL:EHD20937.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=EniD312 {ECO:0000313|EMBL:EHD20937.1}; 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 ----------------------------------------------------------------------- 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; EHD20937.1; -; Genomic_DNA. DR RefSeq; WP_009112243.1; NZ_CM001230.1. DR EnsemblBacteria; EHD20937; EHD20937; BrE312_1529. DR Proteomes; UP000002759; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002759}; KW Methyltransferase {ECO:0000313|EMBL:EHD20937.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002759}; KW Transferase {ECO:0000313|EMBL:EHD20937.1}. SQ SEQUENCE 321 AA; 34750 MW; 94AAAACF063345E2 CRC64; MLRNNPVAEM LATAPAIVLD GALATELEAR GCDLNDPLWS AKVLVENPAL IYQVHLDYFH AGAQCAITAS YQATPLRFKS RGFSERQSQA LIEKSVRLAV QARDDFRKTH SQVGKLLIAG SIGPYGAYLA DGSEYRGDYL LPQSEMMDFH RVRMATLLDA GVDILACETL PSFPEIKALA ELLTEFPQAS AWFSFTLRDS AHLSDGTPLR EVLTLLNAYP QVVAVGINCI ALNKVTAALA QLSAETSLPL VVYPNSGEHY DAVAKTWGDG DGHTCSLAEY LPQWRAAGAK LIGGCCRTTP ADIAAIARFC QPQGKDNDDG Y // ID G7LVM3_9ENTR Unreviewed; 1231 AA. AC G7LVM3; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 01-APR-2015, entry version 21. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHD19931.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHD19931.1}; GN ORFNames=BrE312_0479 {ECO:0000313|EMBL:EHD19931.1}; OS Brenneria sp. EniD312. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Brenneria. OX NCBI_TaxID=598467 {ECO:0000313|EMBL:EHD19931.1, ECO:0000313|Proteomes:UP000002759}; RN [1] {ECO:0000313|EMBL:EHD19931.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=EniD312 {ECO:0000313|EMBL:EHD19931.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CM001230; EHD19931.1; -; Genomic_DNA. DR RefSeq; WP_009111240.1; NZ_CM001230.1. DR EnsemblBacteria; EHD19931; EHD19931; BrE312_0479. DR Proteomes; UP000002759; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002759}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHD19931.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002759}; KW Transferase {ECO:0000313|EMBL:EHD19931.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 251 251 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 315 315 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 763 763 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1231 AA; 135967 MW; DEA4BA7B1C98011E CRC64; MGFFVINRLD ELRRQLAQRI MVLDGGMGTM IQSYHLQEED YRGERFADWP SDVKGNNDLL VLTRPQVISA IHDAYLEAGA DILETNTFNS TTIAMADYGM ESLSAEINTA AARLARACAD RWTALTPDKP RFVAGVLGPT NRTASISPDV NDPAFRNISF DQLVAAYRES TRALIEGGVD LIMIETIFDT LNAKAAVFAV ETEFEALGVE LPVMISGTIT DASGRTLSGQ TTEAFYNALR HARPLSFGLN CALGPEELRQ YVAELSRIAE CYVSAHPNAG LPNAFGEYDL DAADMARHIG EWARAGFLNI VGGCCGSTPA HIAAVAKVVD GVAPRKLPQI PAACRLAGLE PLNIDADTLF VNVGERTNVT GSARFKRLIK EEKYNEALDV ARQQVESGAQ IIDINMDEGM LDAQAAMTRF LSLIAGEPDI ARVPIMIDSS KWEVIEQGLK CIQGKGIVNS ISMKEGVEAF VHHARLVRRY GAAVVVMAFD ETGQADSRAR KIEICRRAYR ILTQEVGFPA EDIIFDPNIF AVATGIEEHN NYAVDFIEAC ADIKAQLPHA MISGGVSNVS FSFRGNDMVR EAIHAVFLYH AIRNGMDMGI VNAGQLAIYD DLPAELRDAV EDVILNRRDD ATERLLDLAE KYRGSKSEDE STKPQAEWRG WPVNKRLEYS LVKGITEFIE PDTEEARRQA QRPIEVIEGP LMDGMNVVGD LFGAGKMFLP QVVKSARVMK QAVAYLEPYI EASKAKGSTA GKILLATVKG DVHDIGKNIV GVVLQCNNYE IIDLGVMVPT DKILKTAREE QVDIIGLSGL ITPSLDEMVN VAKEMERQGF TLPLMIGGAT TSKAHTAVKI EQNYSGPTVY VQNASRTVGV VSALLSPTQY ADFVARTRKE YETVRIQHGR KKPRTPPVTL EAARNNAFSP DWASYTPPVA HRLGVQQVTA SVDTLRHYID WTPFFMTWSL AGKYPRILED DVVGEEAKRL FADANAMLDE LSASGSLNPR GVVGLFPANR VGDDVEIYSD ERRDKVLLVS HHLRQQTEKT DFPNYCLADF VAPQSSGKPD YLGAFAVTGG LEEDTLAERW DAKHDDYNKI MVKALSDRLA EAFAEYLHER VRKVYWGYAA NENLSNDELI RESYQGIRPA PGYPACPDHT EKAEIWQLLE VEKRAGMKLT DSYAMWPGAS VSGWYFSHPE SKYFAVAQIQ RDQVEDYAKR KGISVSEIER WLAPNLGYDA D // ID G7M5A1_9CLOT Unreviewed; 1213 AA. AC G7M5A1; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 01-APR-2015, entry version 21. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHI99704.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHI99704.1}; GN ORFNames=CDLVIII_3122 {ECO:0000313|EMBL:EHI99704.1}; OS Clostridium sp. DL-VIII. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=641107 {ECO:0000313|EMBL:EHI99704.1, ECO:0000313|Proteomes:UP000005106}; RN [1] {ECO:0000313|EMBL:EHI99704.1, ECO:0000313|Proteomes:UP000005106} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DL-VIII {ECO:0000313|EMBL:EHI99704.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CM001240; EHI99704.1; -; Genomic_DNA. DR RefSeq; WP_009170366.1; NZ_CM001240.1. DR EnsemblBacteria; EHI99704; EHI99704; CDLVIII_3122. DR Proteomes; UP000005106; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000005106}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHI99704.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005106}; KW Transferase {ECO:0000313|EMBL:EHI99704.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 242 242 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 754 754 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1213 AA; 135328 MW; 659916D7896F110C CRC64; MNLQIKELLE KRILVLDGAM GTCIQNYKLE EKDYRGNLNI SCNQKGNNDI LNLTNPNIIR EIHEAYLESG ADIIETNTFN STSISQKDYE MEDKIYELNF EGAKIAKEAA DKFTAENPDK PRFVAGSLGP TNKTASLSPD VENPGYRNIS FDELKEAYKD QVLGLIDGGV DLILIETIFD ALNARAALMG AKSAFLEKGK ELPVIISGTI ADKSGRILSG QTLEAFVNTM VDESIIAIGL NCSFGAKDLI PFVKYLSKTQ NRFISMYPNA GLPNSFGEYD EKPEDTAALI KGLAEDGCLN IVGGCCGTTP DHIKAISEAI KDIPPRKIPD VEKETVYCGL EALRANKENN FINIGERTNV AGSAKFARLI REKNYEEALS IAKDQVQNGA QVVDINFDDA LLEAKEEMDN FLKLLAGEPE ISKVPVMIDS SKFEVLVTGL KALQGKPIVN SISLKVGEEE FKRQAKVIKD FGAAAVVMAF DENGQADSYE KKISICKRAY DILVNEVKFP PENIVFDPNI LTIATGIEEH NNYAVDFINA TKWIKENLPY AKVSGGVSNL SFAFRGNNVI REAMHSVFLY HAIKAGMDMG IVNPGMIQIY DEIDEALLEK VEAVIFNKSE NAAEELLEFA ATYNKAESKA EESKEAWRNE NVKERLKTAL VKGIDKYIKE DVEEVRTEYS KSLEVIEGPL MDGMNEVGKL FGDGKMFLPQ VVKSARVMKK AVEVLMPYLE EEKSSSGSVS AGKIVFATVK GDVHDIGKNI VSVVLSCNNF EVIDLGVMVP TEVILETAKN ENADIIALSG LITPSLEEMA TVAEEMEKQG FKIPLMVGGA TTSRAHTAIK IAPKYSGGVI HTTDASKAVE AAKYLLNKDK KAEYLKALEA EYEKIRELFN KVPRKFIPLD YARKNNLKIE WDKEQIDKPK MLGIKKFIDF PIGKLRKYID WSFFFIGWDM GMPYPQILED PKYGEEAKKL LADAEKMLDK IESENILKAN AAFGIFEANS VGDNIEVYNN SEVTTFNLLR QQEEKKDNTY LCLSDYIAPK NSEIKDYIGA FITTGGVGAK EYADKLKASG DDYSATMVIL LADRLAEALA EYIHEKVRKE FWAYSKEENL LMEDIFKGNY RGIRPAIGYP SLRDHSEKVK LFNLLDKEVE LKVELTDSYM MSPTASTCGL YFGNKNAKYF DINKIDEDQF EDYVKRNGRD KGELRKLMYT LID // ID G7M5N2_9CLOT Unreviewed; 593 AA. AC G7M5N2; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 07-JAN-2015, entry version 17. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=CDLVIII_3589 {ECO:0000313|EMBL:EHJ00147.1}; OS Clostridium sp. DL-VIII. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=641107 {ECO:0000313|EMBL:EHJ00147.1, ECO:0000313|Proteomes:UP000005106}; RN [1] {ECO:0000313|EMBL:EHJ00147.1, ECO:0000313|Proteomes:UP000005106} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DL-VIII {ECO:0000313|EMBL:EHJ00147.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; EHJ00147.1; -; Genomic_DNA. DR RefSeq; WP_009170807.1; NZ_CM001240.1. DR EnsemblBacteria; EHJ00147; EHJ00147; CDLVIII_3589. DR Proteomes; UP000005106; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005106}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EHJ00147.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000005106}; KW Transferase {ECO:0000313|EMBL:EHJ00147.1}. SQ SEQUENCE 593 AA; 66675 MW; 8068A273F244DA30 CRC64; MIKDYLQNNI LIFDGAMGTY YSELTGNDIS YCEFANLDDG DTIKKIHKEY INAGAKLIRT NTFSANTHDL GVSYETLKNI IKCGIDIAKE VTRNTSVFIG ASIGPIKEDN IDESQEDILK EYKYIVDCFL DNNINIFVFE TFSNYNYLKE ISEYIKGKDS KSFILTQFAV KPDGFTRDGI SASKLIKKVK EIKTIDSYGF NCGSGPTHVA EFIRTIDIEN DIVSAIPNAG YPEIIHERTV YPNNPVYFAN KVNAMTTLGV SIIGGCCGTN PNYIKELVSL IKNNSNEINS YSKKEEIKEY KEKTENAFKN KLDKNEFTIA IELSAPINTD ISKLMAGAKI CKENNIDLVT IPDSPMSKVR ADPTIIASKI KREIGIEVMP HICCRDRNTN AIRSSLIGSH IENIRNILAI TGDPISDANK IETKSVFNLN SFRLMKLIND MNEDLFKEDN IYIGGALNLN VLNKDVEFNR MLKKIDNGAK FFLTQPIYED DAIEFLSKIK AKTNVKILAG LLPIVSYRNA VFLNNELPGV KIPERYMKMF SENMSKEEAQ EIGVKIAVEI GNKLKGVSDG LYFITPFNRV NMLIDIVKQL QLS // ID G7MD30_9CLOT Unreviewed; 815 AA. AC G7MD30; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 04-MAR-2015, entry version 15. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHI98914.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHI98914.1}; GN ORFNames=CDLVIII_2252 {ECO:0000313|EMBL:EHI98914.1}; OS Clostridium sp. DL-VIII. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=641107 {ECO:0000313|EMBL:EHI98914.1, ECO:0000313|Proteomes:UP000005106}; RN [1] {ECO:0000313|EMBL:EHI98914.1, ECO:0000313|Proteomes:UP000005106} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DL-VIII {ECO:0000313|EMBL:EHI98914.1}; 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; EHI98914.1; -; Genomic_DNA. DR EnsemblBacteria; EHI98914; EHI98914; CDLVIII_2252. DR Proteomes; UP000005106; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005106}; KW Methyltransferase {ECO:0000313|EMBL:EHI98914.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005106}; KW Transferase {ECO:0000313|EMBL:EHI98914.1}. SQ SEQUENCE 815 AA; 89355 MW; 52C8D5227960F318 CRC64; MRIAALEERE KTVGLKEYIK DNILIFDGAM GTMLQKKGLK LGENPELLNI KEPYIIEEIH KEYINSGANV ITTNTFGANE LKLKLCNLEV EDAVDAAVKI AKRAKGDSNT YIALDIGPIG ELLEPMGTLG FDRAYEIFKR QVIQGTKSGV DIILIETMTD LYELKAAILA AKENSDLPVF CTMTFEENLR TFTGCSPEAM VLVLEGLGVD ALGVNCSLGP KQLKPVIEEI CSIAHIPVMV QPNAGLPTLS IGNETRYDVT KEEFADTLCG FIDSGVRIIG GCCGTTPEYI KELSNTVKEK KIIPITREHY AAICTPSKVV RIDGVRIIGE RINPTGKKIF KEALKNGDLD YILSQAVSQI EAGAHILDVN VGLPEIDEPS MMHKVIKEIQ GIIDTPLQID SSDHKAIETG LRYYNGKPIL NSVNGEDAVL DKILPLVKKY GASVVGLTLD ERGIPAKAEE RFEIAKKIIN KAAEYGIKKE DVFIDCLVLT VSAQQEEVQE TLKAVRMVKE KLGVKTVLGV SNISFGLPNR ELINETFLAL ALANGLDLPI INPNAKGMTR VIDSYNVLYN YDKGAESYIN NYANVEVLTE VTAKGTTKNN LSANSNANTD HDLKYIVIKG LKEEAKQATI ELLKSKKELE IVNEYLIPAL DEVGSKYEKG ELFLPQLIQS AETVKNAFSI LKTEIAKSNT KSISKGKIIV ATVKGDIHDI GKNIVKVILE NYGYEMIDLG KDVPIKTVVE EAKNHEVSLI GLSALMTTTL KSMEETIKAL REDGYNGKIF VGGAVLTKDT AERIGADFYA KDAKESVEIA RKVLL // ID G7MFM9_MACMU Unreviewed; 1265 AA. AC G7MFM9; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 04-FEB-2015, entry version 21. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AFE78363.1}; GN Name=MTR {ECO:0000313|EMBL:AFE78363.1}; GN ORFNames=EGK_02100 {ECO:0000313|EMBL:EHH15926.1}; OS Macaca mulatta (Rhesus macaque). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9544 {ECO:0000313|EMBL:EHH15926.1}; RN [1] {ECO:0000313|EMBL:EHH15926.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CR-5 {ECO:0000313|EMBL:EHH15926.1}; RX PubMed=22002653; DOI=10.1038/nbt.1992; RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., RA Li Q., Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., RA Huang Z., Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., RA Huang Y., Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., RA Li B., Liu X., Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., RA Li Y., Wang W., Katze M.G., Su B., Nielsen R., Yang H., Wang J., RA Wang X., Wang J.; RT "Genome sequencing and comparison of two nonhuman primate animal RT models, the cynomolgus and Chinese rhesus macaques."; RL Nat. Biotechnol. 29:1019-1023(2011). RN [2] {ECO:0000313|EMBL:AFE78363.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Caudate {ECO:0000313|EMBL:AFE78363.1}, and RC Thymus {ECO:0000313|EMBL:AFH32479.1}; RX PubMed=25319552; DOI=10.1186/1745-6150-9-20; RA Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X., RA Pandey S., Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P., RA Tharp G.K., Marcais G., Roberts M., Ferguson B., Fox H.S., RA Treangen T., Salzberg S.L., Yorke J.A., Norgren R.B.Jr.; RT "A new rhesus macaque assembly and annotation for next-generation RT sequencing analyses."; RL Biol. Direct 9:20-20(2014). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; JU334610; AFE78363.1; -; mRNA. DR EMBL; JU475675; AFH32479.1; -; mRNA. DR EMBL; CM001253; EHH15926.1; -; Genomic_DNA. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 2: Evidence at transcript level; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 260 260 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 785 785 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1265 AA; 140704 MW; 899B4B515D684F9B CRC64; MSPALQDLSQ PAGLKKTPRD EIDAILQKRI MVLDGGMGTM IQRQKLNEEH FRGQEFKDHA RPLKGNNDIL SITQPDVIYQ IHKEYLLAGA DIIETNTFSS TSIAQADYGL EHLAYRMNKC SAGVARKAAE EITLQTGIKR FVAGALGPTN KTLSVSPSVE RPDYRNIKFD ELVEAYQEQA KGLLDGGVDI LLIETIFDTA NAKAAVFALQ NLFEEKYAPR PIFISGTIVD KSGRTLSGQT GEAFVISLSH AEPLCIGLNC ALGAAEMRPF IEMIGKCTTA YVLCYPNAGL PNTFGDYDET PSTMAKHLKD FAMDGLVNIV GGCCGSTPDH IREIAEAVKN CKPRVPLATV FEGHMLLSGL EPFRIGQYTN FVNIGERCNV AGSRKFAKLI MAGNYEEALG VARVQVEMGA QVLDINMDDG MLDGPSAMTR FCNLIASEPD IAKVPLCIDS SNFAVIEAGL KCCQGKCIVN SISLKEGEDD FLEKARKIKK FGAAMVVMAF DEEGQATETD TKIRVCTRAY HLLVKKLGFN PNDIIFDPNI LTIGTGMEEH NLYAINFIHA TKVIKETLPG ARISGGLSNL SFSFRGMEAI REAMHGVFLY HAIKSGMDMG IVNAGNLPVY DDIHKELLQL CEDLIWNKDP EATEKLLRYA QTQGTGGKKV IQTDEWRNGP VEERLEYALV KGIEKHIIED TEEARLNQER YPRPLNIIEG PLMNGMKIVG DLFGAGKMFL PQVIKSARVM KKAVGHLIPF MEKEREETRV LNGTTEEEDP YQGTIVLATV KGDVHDIGKN IVGVVLGCNN FRVIDLGVMT PCDKILKAAL DHKADIIGLS GLITPSLDEM IFVAKEMERL AIKIPLLIGG ATTSRTHTAV KIAPRYSAPV IHVLDASKSV VVCSQLLDEN LKDEYFEEIM EEYEDIRQDH YESLKERRYL PLSQARKSGF QMDWLSEPHP VKPTFIGTQV FEDYDLQKLV DYIDWKPFFD VWQLRGKYPN RGFPKIFNDK TVGEEAKKVY DDAQNMLNTL INQKKLQARG VVGFWPAQSI QDDIHLYTES AVPQAAEPIA TFYGLRQQAE KDSASTEPYY CLSDFIAPLH SGIRDYLGLF AVACFGVEEL SKAYEDDGDD YSSIMVKALG DRLAEAFAEE LHERVRRELW AYCGSEQLDV ADLRRLRYEG IRPAPGYPSQ PDHTEKLTMW RLADIEQSTG IRLTESLAMA PASAVSGLYF SNLKSKYFAV GKISRDQVED YALRKNMAVA EVEKWLGPIL GYDTD // ID G7MUU6_MACMU Unreviewed; 406 AA. AC G7MUU6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 04-MAR-2015, entry version 13. DE SubName: Full=Betaine--homocysteine S-methyltransferase 1 {ECO:0000313|EMBL:EHH26612.1}; GN ORFNames=EGK_16628 {ECO:0000313|EMBL:EHH26612.1}; OS Macaca mulatta (Rhesus macaque). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9544 {ECO:0000313|EMBL:EHH26612.1}; RN [1] {ECO:0000313|EMBL:EHH26612.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CR-5 {ECO:0000313|EMBL:EHH26612.1}; RX PubMed=22002653; DOI=10.1038/nbt.1992; RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., RA Li Q., Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., RA Huang Z., Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., RA Huang Y., Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., RA Li B., Liu X., Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., RA Li Y., Wang W., Katze M.G., Su B., Nielsen R., Yang H., Wang J., RA Wang X., Wang J.; RT "Genome sequencing and comparison of two nonhuman primate animal RT models, the cynomolgus and Chinese rhesus macaques."; RL Nat. Biotechnol. 29:1019-1023(2011). CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001258; EHH26612.1; -; Genomic_DNA. DR UniPathway; UPA00051; UER00083. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000313|EMBL:EHH26612.1}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000313|EMBL:EHH26612.1}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 217 217 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 406 AA; 45012 MW; 947B513239BB9F16 CRC64; MPPVGGKKAK KGILERLNAG EIVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAVRQLH REFLRAGSNV MQTFTFYASE DKLENRGNYV LEKISGQKVN EAACDIARQV ADEGDALVAG GVSQTPSYLS CKSETEVKKV FLQQLEVFMK KNVDFLIAEY FEHVEEAVWA VETLIASGKP VAATMCIGPE GDLHGVPPGE CAVRLVKAGA SIIGVNCHFD PTISLQTVKL MKEALEAARL KAHLMSQPLA YHTPDCNKQG FIDLPEFPFG LEPRVATRWD IQKYAREAYN LGVRYIGGCC GFEPYHIRAI AEELAPERGF LPPASEKHGS WGSGLDMHTK PWVRARARKE YWENLRIASG RPYNPSMSKP DGWGVTKGTA ELMQQKEATT EQQLKELFEK QKFKSQ // ID G7NWN4_MACFA Unreviewed; 1264 AA. AC G7NWN4; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 01-APR-2015, entry version 21. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EHH50901.1}; DE Flags: Fragment; GN ORFNames=EGM_01800 {ECO:0000313|EMBL:EHH50901.1}; OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9541 {ECO:0000313|Proteomes:UP000009130}; RN [1] {ECO:0000313|EMBL:EHH50901.1, ECO:0000313|Proteomes:UP000009130} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CE-4 {ECO:0000313|EMBL:EHH50901.1}; RX PubMed=22002653; DOI=10.1038/nbt.1992; RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., RA Li Q., Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., RA Huang Z., Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., RA Huang Y., Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., RA Li B., Liu X., Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., RA Li Y., Wang W., Katze M.G., Su B., Nielsen R., Yang H., Wang J., RA Wang X., Wang J.; RT "Genome sequencing and comparison of two nonhuman primate animal RT models, the cynomolgus and Chinese rhesus macaques."; RL Nat. Biotechnol. 29:1019-1023(2011). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CM001276; EHH50901.1; -; Genomic_DNA. DR Proteomes; UP000009130; Chromosome 1. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000009130}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000009130}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 260 260 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 785 785 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. FT NON_TER 1264 1264 {ECO:0000313|EMBL:EHH50901.1}. SQ SEQUENCE 1264 AA; 140619 MW; 70F0B68B319D48F4 CRC64; MSPALQDLSQ PAGLKKTPRD EIDAILQKRI MVLDGGMGTM IQRQKLNEEH FRGQEFKDHA RPLKGNNDIL SITQPDVIYQ IHKEYLLAGA DIIETNTFSS TSIAQADYGL EHLAYRMNKC SAGVARKAAE EITLQTGIKR FVAGALGPTN KTLSVSPSVE RPDYRNIKFD ELVEAYQEQA KGLLDGGVDI LLIETIFDTA NAKAAVFALQ NLFEEKYAPR PIFISGTIVD KSGRTLSGQT GEAFVISLSH AEPLCIGLNC ALGAAEMRPF IEMIGKCTTA YVLCYPNAGL PNTFGDYDET PSMMAKHLKD FAMDGLVNIV GGCCGSTPDH IREIAEAVKN CKPRVPLATV FEGHMLLSGL EPFRIGQYTN FVNIGERCNV AGSRKFAKLI MAGNYEEALG VARVQVEMGA QVLDINMDDG MLDGPSAMTR FCNLIASEPD IAKVPLCIDS SNFAVIEAGL KCCQGKCIVN SISLKEGEDD FLEKARKIKK FGAAMVVMAF DEEGQATETD TKIRVCTRAY HLLVKKLGFN PNDIIFDPNI LTIGTGMEEH NLYAINFIHA TKVIKETLPG ARISGGLSNL SFSFRGMEAI REAMHGVFLY HAIKSGMDMG IVNAGNLPVY DDIHKELLQL CEDLIWNKDP EATEKLLRYA QTQGTGGKKV IQTDEWRNGP VEERLEYALV KGIEKHIIED TEEARLNQER YPRPLNIIEG PLMNGMKIVG DLFGAGKMFL PQVIKSARVM KKAVGHLIPF MEKEREETRV LNGTTEEEDP YQGTIVLATV KGDVHDIGKN IVGVVLGCNN FRVIDLGVMT PCDKILKAAL DHKADIIGLS GLITPSLDEM IFVAKEMERL AIKIPLLIGG ATTSRTHTAV KIAPRYSAPV IHVLDASKSV VVCSQLLDEN LKDEYFEEIM EEYEDIRQDH YESLKERRYL PLSQARKSGF QMDWLSEPHP VKPTFIGTQV FEDYDLQKLV DYIDWKPFFD VWQLRGKYPN RGFPKIFNDK TVGEEAKKVY DDAQNMLNTL INQKKLQARG VVGFWPAQSI QDDIHLYTES AVPQAAEPIA TFYGLRQQAE KDSASTEPYY CLSDFIAPLH SGIRDYLGLF AVACFGVEEL SKAYEDDGDD YSSIMVKALG DRLAEAFAEE LHERVRRELW AYCGSEQLDV ADLRRLRYEG IRPAPGYPSQ PDHTEKLTMW RLADIEQSTG IRLTESLAMA PASAVSGLYF SNLKSKYFAV GKISRDQVED YALRKNMAVA EVEKWLGPIL GYDT // ID G7P7T9_MACFA Unreviewed; 363 AA. AC G7P7T9; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 04-MAR-2015, entry version 17. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EHH54360.1}; GN ORFNames=EGM_15183 {ECO:0000313|EMBL:EHH54360.1}; OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9541 {ECO:0000313|Proteomes:UP000009130}; RN [1] {ECO:0000313|EMBL:EHH54360.1, ECO:0000313|Proteomes:UP000009130} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CE-4 {ECO:0000313|EMBL:EHH54360.1}; RX PubMed=22002653; DOI=10.1038/nbt.1992; RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., RA Li Q., Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., RA Huang Z., Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., RA Huang Y., Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., RA Li B., Liu X., Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., RA Li Y., Wang W., Katze M.G., Su B., Nielsen R., Yang H., Wang J., RA Wang X., Wang J.; RT "Genome sequencing and comparison of two nonhuman primate animal RT models, the cynomolgus and Chinese rhesus macaques."; RL Nat. Biotechnol. 29:1019-1023(2011). CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001281; EHH54360.1; -; Genomic_DNA. DR ProteinModelPortal; G7P7T9; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000009130; Chromosome 6. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009130}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Reference proteome {ECO:0000313|Proteomes:UP000009130}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 208 208 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 363 AA; 40333 MW; CE911F88B30FA4FD CRC64; MAPAGRPGAK KGILERLESG EVVIGDGSFL ITLEKRGYVK AGLWTPEAVI EHPDAVRQLH MEFLRAGSNV MQTFTFSASE DNMESKWEDV NAAACDLARE VAGKGDALVA GGICQTSIYK YHKDETRIKK LFRQQLEVFA WKKVDFLIAE YFEHVEEAVW AVEVLKESDR PVAVTMCIGP EGDMHDTTPG ECAVRLVKAG ASIVGVNCRF GPETSLKTME LMKEGLERAG LKAHLMVQPL GFHTPDCGKE GFVDLPEYPF GLESRVATRW DIQKYAREAY NLGVRYIGGC CGFEPYHIRA IAEELAPERG FLPPASEKHG SWGSGLDMHT KPWIRARARR EYWENLLPAS GRPFCPSLSK PDA // ID G7P7U0_MACFA Unreviewed; 406 AA. AC G7P7U0; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 04-MAR-2015, entry version 14. DE SubName: Full=Betaine--homocysteine S-methyltransferase 1 {ECO:0000313|EMBL:EHH54361.1}; GN ORFNames=EGM_15184 {ECO:0000313|EMBL:EHH54361.1}; OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9541 {ECO:0000313|Proteomes:UP000009130}; RN [1] {ECO:0000313|EMBL:EHH54361.1, ECO:0000313|Proteomes:UP000009130} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CE-4 {ECO:0000313|EMBL:EHH54361.1}; RX PubMed=22002653; DOI=10.1038/nbt.1992; RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., RA Li Q., Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., RA Huang Z., Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., RA Huang Y., Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., RA Li B., Liu X., Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., RA Li Y., Wang W., Katze M.G., Su B., Nielsen R., Yang H., Wang J., RA Wang X., Wang J.; RT "Genome sequencing and comparison of two nonhuman primate animal RT models, the cynomolgus and Chinese rhesus macaques."; RL Nat. Biotechnol. 29:1019-1023(2011). CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001281; EHH54361.1; -; Genomic_DNA. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000009130; Chromosome 6. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009130}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000313|EMBL:EHH54361.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000009130}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000313|EMBL:EHH54361.1}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 217 217 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 406 AA; 44998 MW; 691275A4E1A3FDE6 CRC64; MPPVGGKKAK KGILERLNAG EIVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAVRQLH REFLRAGSNV MQTFTFYASE DKLENRGNYV LEKISGQKVN EAACDIARQV ADEGDALVAG GVSQTPSYLS CKSETEVKKV FLQQLEVFMK KNVDFLIAEY FEHVEEAVWA VETLIASGKP VAATMCIGPE GDLHGVPPGE CAVRLVKAGA SIIGVNCHFD PTISLQTVKL MKEGLEAARL KAHLMSQPLA YHTPDCNKQG FIDLPEFPFG LEPRVATRWD IQKYAREAYN LGVRYIGGCC GFEPYHIRAI AEELAPERGF LPPASEKHGS WGSGLDMHTK PWVRARARKE YWENLRIASG RPYNPSMSKP DGWGVTKGTA ELMQQKEATT EQQLKELFEK QKFKSQ // ID G7Q4K8_9DELT Unreviewed; 806 AA. AC G7Q4K8; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 07-JAN-2015, entry version 14. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHJ47231.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHJ47231.1}; GN ORFNames=DFW101_1221 {ECO:0000313|EMBL:EHJ47231.1}; OS Desulfovibrio sp. FW1012B. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=644968 {ECO:0000313|EMBL:EHJ47231.1, ECO:0000313|Proteomes:UP000004662}; RN [1] {ECO:0000313|EMBL:EHJ47231.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FW1012B {ECO:0000313|EMBL:EHJ47231.1}; 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 ----------------------------------------------------------------------- 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; EHJ47231.1; -; Genomic_DNA. DR RefSeq; WP_009180642.1; NZ_CM001368.1. DR EnsemblBacteria; EHJ47231; EHJ47231; DFW101_1221. DR Proteomes; UP000004662; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000004662}; KW Methyltransferase {ECO:0000313|EMBL:EHJ47231.1}; KW Transferase {ECO:0000313|EMBL:EHJ47231.1}. SQ SEQUENCE 806 AA; 83319 MW; 6BADED6E9E0FA88F CRC64; MGDFRQALGD GEILVFDGAM GTLLQGRGLA AGQSPELFGL AHPEAIVATH REYIEAGSRV ITSNTFGGTR YKLPPGTDVT ALSRDMARLA RQAAGQGVFV AGSVGPTGQF VAPLGKASLA ELVAAFATQI KGLAEGGCDL IVGETHFDLA EAKALVLAAR QVCSLPVAVC MTFEGAVSLT GSGPEVFADA MENLGVDLVG VNCGAGPDDM RLVAEVFSRR LSTPFFVKPN AGMPRLEGGR TVFPMGPEEF AEKTARFADL GAKALSGCCG TTPAHIKALA GALAGRTHTR PEAVDRPVLA VTSRALTVTL GGKSPCAVIG ERINPTGKAG LAAELAAGEF AQALAFAEEQ VAAGAAILDV NVGAPMVDET VVLPGLAVEL TKRQQTPLCL DSNNADALVA ALYASPATPL VNSISGEPGR MERLGPICRD HGAPFILLPL KGRKLPVTAA ERLAIIEELL VQADGLGIPR RLILVDALAL TVSSKPEAAL ACLETIRHCR ERWGLPTVLG LSNISFGLPA RELVNAAFFA MCLGAGLSAA IANPNVPRLM ETSGACEVLL ARDPQAGRFI GRFAGWTPAA PSGAAPTAAS AGGAGEEGAS PLRQAVVRGR RAELDGLIDA ALAEGRAAAD ILSEDLIPGI MDVGERYERK EFFLPQLLVA AEAMRAGFTR LEPLLAETAG AAKARIVMAT VEGDIHDIGK NIVCLMLKNH GFEVIDLGKD VPAATIVAEA EARDADVIGL SALMTTTMVR MEDTVRLVRE RGLRAKVMVG GAVVTEAFAK SIGAHARAAD AVDAVRQAKA LLGANA // ID G7SEN0_STRSU Unreviewed; 315 AA. AC G7SEN0; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 01-APR-2015, entry version 20. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AER20257.1}; GN Name=mmuM {ECO:0000313|EMBL:AER20257.1}; GN ORFNames=SSUD12_1994 {ECO:0000313|EMBL:AER20257.1}; OS Streptococcus suis D12. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1004952 {ECO:0000313|EMBL:AER20257.1, ECO:0000313|Proteomes:UP000008845}; RN [1] {ECO:0000313|EMBL:AER20257.1, ECO:0000313|Proteomes:UP000008845} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=D12 {ECO:0000313|EMBL:AER20257.1}; 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002644; AER20257.1; -; Genomic_DNA. DR RefSeq; WP_014638733.1; NC_017621.1. DR RefSeq; YP_006083505.1; NC_017621.1. DR EnsemblBacteria; AER20257; AER20257; SSUD12_1994. DR KEGG; ssk:SSUD12_1994; -. DR KO; K00547; -. DR BioCyc; SSUI1004952:GLLJ-2008-MONOMER; -. DR Proteomes; UP000008845; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008845}; KW Methyltransferase {ECO:0000313|EMBL:AER20257.1}; KW Transferase {ECO:0000313|EMBL:AER20257.1}. SQ SEQUENCE 315 AA; 34854 MW; 799DA279E19705ED CRC64; MGRFKELLEQ KEYVILHGAL GTELEFRGHD VSGKLWSAKY LLENPQYIKD IHKDYIRAGA DLVTTSTYQA TFEGLAEVGL SQAEAEELIR LTVDLAKEAR DEVWAELSEA EKVQRTYPLI SGDVGPYAAY LANGAEYTGD YGNISLSELK DFHRRRIELL LEQEAELLAL ETIPNVLEAQ ALVELLAEDF PEAEAYISFT SQDGQSISDG TSIEKIAELV NSSEQILAVG LNCTAPSLYP AFLSQLREKT DKPFVTYPNS GEVYDGATQT WKEKADDSHS LLDNTLEWHE LGAKVVGGCC RTRPADIADL VAGLK // ID G7T9U6_XANOB Unreviewed; 172 AA. AC G7T9U6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEQ95946.1}; GN ORFNames=XOC_1784 {ECO:0000313|EMBL:AEQ95946.1}; OS Xanthomonas oryzae pv. oryzicola (strain BLS256). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=383407 {ECO:0000313|EMBL:AEQ95946.1, ECO:0000313|Proteomes:UP000008851}; RN [1] {ECO:0000313|EMBL:AEQ95946.1, ECO:0000313|Proteomes:UP000008851} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BLS256 {ECO:0000313|EMBL:AEQ95946.1, RC ECO:0000313|Proteomes:UP000008851}; 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 ----------------------------------------------------------------------- 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; AEQ95946.1; -; Genomic_DNA. DR RefSeq; WP_014502791.1; NC_017267.1. DR RefSeq; YP_005628114.1; NC_017267.1. DR EnsemblBacteria; AEQ95946; AEQ95946; XOC_1784. DR KEGG; xor:XOC_1784; -. DR KO; K00548; -. DR BioCyc; XORY383407:GLMS-1710-MONOMER; -. DR Proteomes; UP000008851; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008851}. SQ SEQUENCE 172 AA; 17986 MW; B61686D855406803 CRC64; MIDGGADTLM VETICDTLNA KAALYAIKEV FEARGGRLPV MISGTITDAS GRTLSGQTAE AFYASVAHGR PLSVGLNCAL GAKDLRPHVE TLSQIADAYV SAHPNAGLPN AFGEYDETSE EMAETLREFA ESGLLNLVGG CCGTSPDHIR AIAEAVADLP PRQRPGAQKL AE // ID G7T9U7_XANOB Unreviewed; 51 AA. AC G7T9U7; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEQ95947.1}; GN ORFNames=XOC_1785 {ECO:0000313|EMBL:AEQ95947.1}; OS Xanthomonas oryzae pv. oryzicola (strain BLS256). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=383407 {ECO:0000313|EMBL:AEQ95947.1, ECO:0000313|Proteomes:UP000008851}; RN [1] {ECO:0000313|EMBL:AEQ95947.1, ECO:0000313|Proteomes:UP000008851} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BLS256 {ECO:0000313|EMBL:AEQ95947.1, RC ECO:0000313|Proteomes:UP000008851}; 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 ----------------------------------------------------------------------- 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; AEQ95947.1; -; Genomic_DNA. DR RefSeq; WP_014502792.1; NC_017267.1. DR RefSeq; YP_005628115.1; NC_017267.1. DR EnsemblBacteria; AEQ95947; AEQ95947; XOC_1785. DR KEGG; xor:XOC_1785; -. DR BioCyc; XORY383407:GLMS-1711-MONOMER; -. DR Proteomes; UP000008851; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008851}. SQ SEQUENCE 51 AA; 5316 MW; 00A7E611C17FA81E CRC64; MYELNKAGAQ VARACCDAVE ALTPQKPRFV IGVLGPTSRT ASISPDVNDP G // ID G7T9U8_XANOB Unreviewed; 134 AA. AC G7T9U8; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 29-APR-2015, entry version 21. DE SubName: Full=Methionine synthase (5-methyltetrahydrofolate--homocysteine methyltransferase) vitamin-B12 dependent {ECO:0000313|EMBL:AEQ95948.1}; GN ORFNames=XOC_1786 {ECO:0000313|EMBL:AEQ95948.1}; OS Xanthomonas oryzae pv. oryzicola (strain BLS256). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=383407 {ECO:0000313|EMBL:AEQ95948.1, ECO:0000313|Proteomes:UP000008851}; RN [1] {ECO:0000313|EMBL:AEQ95948.1, ECO:0000313|Proteomes:UP000008851} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BLS256 {ECO:0000313|EMBL:AEQ95948.1, RC ECO:0000313|Proteomes:UP000008851}; 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 ----------------------------------------------------------------------- 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; AEQ95948.1; -; Genomic_DNA. DR RefSeq; WP_014502793.1; NC_017267.1. DR RefSeq; YP_005628116.1; NC_017267.1. DR EnsemblBacteria; AEQ95948; AEQ95948; XOC_1786. DR KEGG; xor:XOC_1786; -. DR KO; K00548; -. DR BioCyc; XORY383407:GLMS-1712-MONOMER; -. DR Proteomes; UP000008851; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008851}; KW Methyltransferase {ECO:0000313|EMBL:AEQ95948.1}; KW Transferase {ECO:0000313|EMBL:AEQ95948.1}. SQ SEQUENCE 134 AA; 14777 MW; 4B640814D0BDB908 CRC64; MTHARIPHSE SPIPFALPWL HPERAAKLTA ALAERILIID GAMGTMIQRH DLKKPDYRGT RFADGYDSAH VHGRGCDHAH APESHDLKGN NDLLLLSRPE IIAGIHRAYL DAGADLLETN TFNATSVSQA DYHL // ID G7TA16_XANOB Unreviewed; 321 AA. AC G7TA16; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AEQ97201.1}; GN ORFNames=XOC_3103 {ECO:0000313|EMBL:AEQ97201.1}; OS Xanthomonas oryzae pv. oryzicola (strain BLS256). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=383407 {ECO:0000313|EMBL:AEQ97201.1, ECO:0000313|Proteomes:UP000008851}; RN [1] {ECO:0000313|EMBL:AEQ97201.1, ECO:0000313|Proteomes:UP000008851} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BLS256 {ECO:0000313|EMBL:AEQ97201.1, RC ECO:0000313|Proteomes:UP000008851}; 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 ----------------------------------------------------------------------- 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; AEQ97201.1; -; Genomic_DNA. DR RefSeq; WP_014503948.1; NC_017267.1. DR RefSeq; YP_005629369.1; NC_017267.1. DR EnsemblBacteria; AEQ97201; AEQ97201; XOC_3103. DR KEGG; xor:XOC_3103; -. DR KO; K00547; -. DR BioCyc; XORY383407:GLMS-3002-MONOMER; -. DR Proteomes; UP000008851; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008851}; KW Methyltransferase {ECO:0000313|EMBL:AEQ97201.1}; KW Transferase {ECO:0000313|EMBL:AEQ97201.1}. SQ SEQUENCE 321 AA; 34283 MW; 5035A6F1E9458E9E CRC64; MTTASRQPRA DAPFSQVLQH DGCVLLDGAL ATELEHRGCD LNDALWSARV LIEQPELIYQ VHRDYFAAGA QCAITASYQA TPLGFAARGL DVAQSQALIA RSVELAVQAR ADHLHVQPQA APLWVAGSVG PYGAYLADGS EYRGDYILPI AQLMDFHRPR IAALADAGVD VLACETLPSA SEIVALRQLL QNEFPQLHAW FSFTLRDAAH LSDGTPLAQV VPALDACRQV IAVGINCIAL DQVTAALHSL SVLTALPLVV YPNSGEHYDA SDKRWHAGHA SALTLADQHA HWLAAGARLI GGCCRTTPRD IAALAAARLA D // ID G7V6S1_THELD Unreviewed; 821 AA. AC G7V6S1; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 01-APR-2015, entry version 21. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AER66030.1}; GN OrderedLocusNames=Tlie_0291 {ECO:0000313|EMBL:AER66030.1}; OS Thermovirga lienii (strain ATCC BAA-1197 / DSM 17291 / Cas60314). OC Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae; OC Thermovirga. OX NCBI_TaxID=580340 {ECO:0000313|EMBL:AER66030.1, ECO:0000313|Proteomes:UP000005868}; RN [1] {ECO:0000313|Proteomes:UP000005868} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1197 / DSM 17291 / Cas60314 RC {ECO:0000313|Proteomes:UP000005868}; 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 ----------------------------------------------------------------------- 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; AER66030.1; -; Genomic_DNA. DR RefSeq; WP_014162452.1; NC_016148.1. DR RefSeq; YP_004932127.1; NC_016148.1. DR EnsemblBacteria; AER66030; AER66030; Tlie_0291. DR KEGG; tli:Tlie_0291; -. DR KO; K00548; -. DR BioCyc; TLIE580340:GH7T-291-MONOMER; -. DR Proteomes; UP000005868; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005868}; KW Methyltransferase {ECO:0000313|EMBL:AER66030.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005868}; KW Transferase {ECO:0000313|EMBL:AER66030.1}. SQ SEQUENCE 821 AA; 87535 MW; C01316CDD13CF880 CRC64; MDRMKFWQWM EAKSRVILMD GGMGTLLAEK GWKPPMLPEE MNVYSPDVVA SIHEAYLASG ADIIETNSFG GSTRKLAHRG LQGKARDINK EAARIAKGCA GDKALVAGSV GPLGELLEPF GSLSFEEAYE AFYEQIAGLA EGGADFILIE TMMDIREAKA AVAAAKDAAQ GLAFVVSFTF DHHGKTVTGT PPEVAAAWAY AVGAAGVGAN CGVGPGEYVE TVKKLWEYSR LPVFVYANAG LPGDENFWDP RAFAEKSKEL ALAGASVIGG CCGTTPEHIR EMKEALAGVL SLPPSSRKET FLASRSKLVA AGCGGPLLVV GERINVSRKS ALKEQVANGD FTLLKEEAKL QEQAGAEVID VNVGLPGVDQ VALMSEAISV VEATVTSPVS IDSDKIEVLE AGLKRASGVP LINSVTAKQG HLEKGLELAS RYGAVLTVLP MDEKGLPHTI EERRAVIDSI VERARKTGFP MENLIIDGLT LAVGADEKAP RVTLQALEYI SQLGCLSILG VSNVSHGLPS RHLVNRTFLA MAMASGLGAA IIDPTAPGIF ETILASNLLR GSDPKALNYI QAQDKLKERA LVEPGRDSAP KKEERKKEIE EPTEEKNQGP YFPLMEAIIE GDEKAAQLHV RDLIDEKGVK PMDVISCGII PALEEVGKLY EVGEFFLPQL LASAQAAQVS CDFARERMEP SDRGENKATV VLATVEGDLH DLGKNIVGTV LRSYGYQVID LGRNVPAQKI LEAASESNAH IVGLSALMTT TMEEMARTVK LLKEKLPHLP VIVGGASVNE SFAKKIGSDG TAPDAIGAVR LVSRLTERGD E // ID G7VRV5_PAETH Unreviewed; 1146 AA. AC G7VRV5; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=Methionine synthase I, cobalamin-binding domain protein {ECO:0000313|EMBL:AET60762.1}; GN OrderedLocusNames=HPL003_20120 {ECO:0000313|EMBL:AET60762.1}; OS Paenibacillus terrae (strain HPL-003). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=985665 {ECO:0000313|EMBL:AET60762.1, ECO:0000313|Proteomes:UP000005876}; RN [1] {ECO:0000313|Proteomes:UP000005876} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HPL-003 {ECO:0000313|Proteomes:UP000005876}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP003107; AET60762.1; -; Genomic_DNA. DR RefSeq; WP_014281460.1; NC_016641.1. DR RefSeq; YP_005076985.1; NC_016641.1. DR EnsemblBacteria; AET60762; AET60762; HPL003_20120. DR KEGG; pta:HPL003_20120; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; PTER985665:GHT3-4084-MONOMER; -. DR Proteomes; UP000005876; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000005876}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 722 722 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1146 AA; 126381 MW; 73E333296559447A CRC64; MDKVSLQDAL QRRILILDGA MGTMIQQEDL SPDDFGGEEL EGCNEMLVLT RPDVIQGIHE AYLEAGSDLI ETNTFGATSV VLADYDIPER AREINLVAAK LARNAADKYS TADKPRFVVG AMGPTTKTLS VTGGVTFAEL IESYEEQALA LIEGGVDALL LETSQDTLNV KAGSIGIRQA FEKTGIELPI MISGTIEPMG TTLAGQNIES FCISLEHLHP VSIGLNCATG PEFMRDHIRS LSDMSSAAIS CYPNAGLPDE NGQYHESPDS LARKMAAFAE KGWLNIAGGC CGTTPEHIRV MSESMAQFEP RPLEGHHPPA VSGIEPVYIE QENRPYMVGE RTNVLGSRKF KRLIVEGKYE EASEIARAQV KSGAHVIDIC VQDPDRDEMT DMEAFLKLVV NKVKVPLVID TTDIQVIDTA LQYSQGKAII NSINLEDGEE KFEKMAPLIH KYGAAVVVGT IDERGQAISR EDKLEVAKRS YDLLVNRYGL APEDLIFDTL VFPVGTGDEQ YIGSAKETIE GIRIIKEALP GVHTILGISN VSFGLPEAGR EVLNSVYLYE CTKAGLDYAI VNTEKLERYA SIPEHERKLA EDLIYKTNDD TLSAFVAAFR NKKVEKKEKV SNLSLEERLA SYVVEGSKEG LIPDLEQALA KYSSLEIING PLMKGMEEVG RLFNNNELIV AEVLQSAEVM KASVAYLEPY MEKNESSVKG KILLATVKGD VHDIGKNLVE IILSNNGYHI VNLGIKVPPE RIIEAYREEK ADAIGLSGLL VKSAQQMVLT AQDLKNANID IPIMVGGAAL TRKFTKNRIR PEYDGMVVYA KDAMDGLDIA NKLMNPESRK KMAEEMEAER EAEAATVVEA KPLPKLTRAV RSKIAQDLPV YIPPDTDRHV LRNYPLNYIL PYVNMQMLMG HHLGLKGNVE QLLASGNPKA TQLKETVDSI MFEAVTDGII QAHAVYRFFP AQSQGDQILI YDPSDVSKVL HTFTFPRQQV EPYLCLADYL KSVESGVMDY VGFMVVTAGH GIQQLSTQWK EKGDYLRSHA LQSVALEVAE GLAERLHHII RDSWGFPDSA DMTMKQRHGA RYQGIRVSFG YPACPDLEDQ GPLFQLLKPE DIGVELTEGF MMEPEASVSA MVFSHPQAQY FNVEKV // ID G7VVB7_PAETH Unreviewed; 630 AA. AC G7VVB7; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 21. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=HPL003_24490 {ECO:0000313|EMBL:AET61614.1}; OS Paenibacillus terrae (strain HPL-003). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=985665 {ECO:0000313|EMBL:AET61614.1, ECO:0000313|Proteomes:UP000005876}; RN [1] {ECO:0000313|Proteomes:UP000005876} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HPL-003 {ECO:0000313|Proteomes:UP000005876}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; AET61614.1; -; Genomic_DNA. DR RefSeq; WP_014282303.1; NC_016641.1. DR RefSeq; YP_005077837.1; NC_016641.1. DR EnsemblBacteria; AET61614; AET61614; HPL003_24490. DR KEGG; pta:HPL003_24490; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR BioCyc; PTER985665:GHT3-4936-MONOMER; -. DR Proteomes; UP000005876; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005876}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:AET61614.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:AET61614.1}. SQ SEQUENCE 630 AA; 68557 MW; D95D80D962F0DD49 CRC64; MKPDLRTVLE REIIVGDGAM GTFLYQLGFP VNTSYEELNI TSPDVISDVH RQYLQAGARL LETNTFSAND YKLARFGLES KVEEINRAGV RIARAAAGPE HYVVGAVGSI CGGKRLNISK VELARNYDQQ IDALLSEGVD GILCETFYSL DEVRIALRGV RKYSNIPVIC QFAVDQVGRT QDGFSVEEAF TVLRNEGADI LGFNCHSGPQ GIMSVMEQLD GPLSVPLSVY PNAGLADYVD GHYVYGASPE YFGECAASFV ELGTRIIGGC CGTTPEHIAA ISKALNGLQP PPLAPREILT DAPVIVAEPE QIAREGERGN GINASEPNIV ELVKERHTVI VELDPPRDLD ITRFMQGAQA LKAAGADALT LADNSLAVTR MSNMALGHLV SLETGLRPLI HIACRDRNLI GTQSHMMGFD ALGIDHVLAV TGDPARFGDL PGASSVYDMT SFEIIRMIKQ LNDGIAFSGK PLKQKANFVV GAAFNPNVKH LGKAVQRLEK KIASGADYIM TQPVYDHELI IAMAEQTRHL EVPIFIGIMP LASGRNAEYL HNEVPGIQLS DEVRARMSGL EGEEGRAMGV TIAKELLDTA MEHFNGIYLM TPFMFYEMTA ELTSYVWQKS GSVQAPLFRL // ID G7W3K1_PAETH Unreviewed; 326 AA. AC G7W3K1; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 29-APR-2015, entry version 18. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:AET58088.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:AET58088.1}; GN Name=mmuM {ECO:0000313|EMBL:AET58088.1}; GN OrderedLocusNames=HPL003_06625 {ECO:0000313|EMBL:AET58088.1}; OS Paenibacillus terrae (strain HPL-003). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=985665 {ECO:0000313|EMBL:AET58088.1, ECO:0000313|Proteomes:UP000005876}; RN [1] {ECO:0000313|Proteomes:UP000005876} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HPL-003 {ECO:0000313|Proteomes:UP000005876}; 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; AET58088.1; -; Genomic_DNA. DR RefSeq; WP_014278837.1; NC_016641.1. DR RefSeq; YP_005074311.1; NC_016641.1. DR EnsemblBacteria; AET58088; AET58088; HPL003_06625. DR KEGG; pta:HPL003_06625; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR BioCyc; PTER985665:GHT3-1351-MONOMER; -. DR Proteomes; UP000005876; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005876}; KW Methyltransferase {ECO:0000313|EMBL:AET58088.1}; KW Transferase {ECO:0000313|EMBL:AET58088.1}. SQ SEQUENCE 326 AA; 36204 MW; 24CB96B87E638B98 CRC64; MNPIQHILDK YPVIVLDGAM ATELERHGHD LNDSLWSAKI LHEHPESIKR VHREYFEAGA DCAITASYQA TVEGYVQRGL NENEALELIQ SSVRIAVQAR DEFWADITSG AKQQHRPKPL VAASVGPYGA FLADGSEYRG DYTLSEEQLV EFHRPRMKAL IEAGADILAC ETIPCLVEAK AIARLLKEFP GTYAWISFSA KDGQHISNGE SAAECAEWLD EHEQVAAVGI NCTLPQYIPS LIQEMRSHTD KPVVVYPNLG EEYDPVTKTW HGTSCTETFG QSARKWYEAG ARLIGGCCRT QPQDIKEVVA WSRDVYTETR LGGGCP // ID G7W9L4_DESOD Unreviewed; 434 AA. AC G7W9L4; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 29-APR-2015, entry version 20. DE SubName: Full=Cobalamin-dependent methionine synthase I {ECO:0000313|EMBL:AET69931.1}; GN OrderedLocusNames=Desor_4523 {ECO:0000313|EMBL:AET69931.1}; 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 {ECO:0000313|EMBL:AET69931.1, ECO:0000313|Proteomes:UP000006346}; RN [1] {ECO:0000313|Proteomes:UP000006346} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19365 / DSM 765 / NCIMB 8382 / VKM B-1628 RC {ECO:0000313|Proteomes:UP000006346}; 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. RN [2] {ECO:0000313|EMBL:AET69931.1, ECO:0000313|Proteomes:UP000006346} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19365 / DSM 765 / NCIMB 8382 / VKM B-1628 RC {ECO:0000313|Proteomes:UP000006346}; RX PubMed=23105050; DOI=10.1128/JB.01392-12; RA Pester M., Brambilla E., Alazard D., Rattei T., Weinmaier T., Han J., RA Lucas S., Lapidus A., Cheng J.F., Goodwin L., Pitluck S., Peters L., RA Ovchinnikova G., Teshima H., Detter J.C., Han C.S., Tapia R., RA Land M.L., Hauser L., Kyrpides N.C., Ivanova N.N., Pagani I., RA Huntmann M., Wei C.L., Davenport K.W., Daligault H., Chain P.S., RA Chen A., Mavromatis K., Markowitz V., Szeto E., Mikhailova N., RA Pati A., Wagner M., Woyke T., Ollivier B., Klenk H.P., Spring S., RA Loy A.; RT "Complete Genome Sequences of Desulfosporosinus orientis DSM765T, RT Desulfosporosinus youngiae DSM17734T, Desulfosporosinus meridiei RT DSM13257T, and Desulfosporosinus acidiphilus DSM22704T."; RL J. Bacteriol. 194:6300-6301(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; CP003108; AET69931.1; -; Genomic_DNA. DR RefSeq; WP_014186738.1; NC_016584.1. DR RefSeq; YP_004972446.1; NC_016584.1. DR EnsemblBacteria; AET69931; AET69931; Desor_4523. DR KEGG; dor:Desor_4523; -. DR KO; K00548; -. DR BioCyc; DORI768706:GHQZ-4514-MONOMER; -. DR Proteomes; UP000006346; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006346}; KW Reference proteome {ECO:0000313|Proteomes:UP000006346}. SQ SEQUENCE 434 AA; 47415 MW; 974B22FF97C0AFFC CRC64; MSGFLSSILE KVLLYDGSKG VMLQMKGLKG SEAAESWNLS KPEEVKSLYR AYKEAGSDVI QTNTFPGNRI TLEKHSLGDK TYQLNFAGVK LAQEVAGEDT YVAASVGPTG RMFEPAGDLT FDKAYDIFKE QLRAIDDAGA DIVNFETFTD LNEMRAAILA AKETTGLPVI ASLTFNENCR TLSGNSAEAC AIVCQSLGAA VVGANCSGGP DSLMEPIRKM YAVASIPLAV KANAGLPELV KGETVYKQKP EQFSSYTKEF VENGVRLIGG CCGTTPEFIK ALKEELSKLQ APDLQVRSTS GIASPFNHLD MVNSQEYSVK TLSLKEDSMV EMLKNGDFYG LLLNYKSETM DALLMDFGDK DLAFDVWGLV TNISFLIKKP LIIKSESTEL VDKFLRYYPG RVGVVISEDM KLSLSQLKHY GCLFLNENLE PMAI // ID G7WAX8_DESOD Unreviewed; 311 AA. AC G7WAX8; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Homocysteine/selenocysteine methylase (S-methylmethionine-dependent) {ECO:0000313|EMBL:AET67479.1}; GN OrderedLocusNames=Desor_1846 {ECO:0000313|EMBL:AET67479.1}; 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 {ECO:0000313|EMBL:AET67479.1, ECO:0000313|Proteomes:UP000006346}; RN [1] {ECO:0000313|Proteomes:UP000006346} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19365 / DSM 765 / NCIMB 8382 / VKM B-1628 RC {ECO:0000313|Proteomes:UP000006346}; 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. RN [2] {ECO:0000313|EMBL:AET67479.1, ECO:0000313|Proteomes:UP000006346} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19365 / DSM 765 / NCIMB 8382 / VKM B-1628 RC {ECO:0000313|Proteomes:UP000006346}; RX PubMed=23105050; DOI=10.1128/JB.01392-12; RA Pester M., Brambilla E., Alazard D., Rattei T., Weinmaier T., Han J., RA Lucas S., Lapidus A., Cheng J.F., Goodwin L., Pitluck S., Peters L., RA Ovchinnikova G., Teshima H., Detter J.C., Han C.S., Tapia R., RA Land M.L., Hauser L., Kyrpides N.C., Ivanova N.N., Pagani I., RA Huntmann M., Wei C.L., Davenport K.W., Daligault H., Chain P.S., RA Chen A., Mavromatis K., Markowitz V., Szeto E., Mikhailova N., RA Pati A., Wagner M., Woyke T., Ollivier B., Klenk H.P., Spring S., RA Loy A.; RT "Complete Genome Sequences of Desulfosporosinus orientis DSM765T, RT Desulfosporosinus youngiae DSM17734T, Desulfosporosinus meridiei RT DSM13257T, and Desulfosporosinus acidiphilus DSM22704T."; RL J. Bacteriol. 194:6300-6301(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; CP003108; AET67479.1; -; Genomic_DNA. DR RefSeq; WP_014184296.1; NC_016584.1. DR RefSeq; YP_004969994.1; NC_016584.1. DR EnsemblBacteria; AET67479; AET67479; Desor_1846. DR KEGG; dor:Desor_1846; -. DR BioCyc; DORI768706:GHQZ-1842-MONOMER; -. DR Proteomes; UP000006346; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006346}; KW Methyltransferase {ECO:0000313|EMBL:AET67479.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006346}; KW Transferase {ECO:0000313|EMBL:AET67479.1}. SQ SEQUENCE 311 AA; 34983 MW; 0DD5E018A179F401 CRC64; MDFESCYNKF PIILMEGAVG ERLKREYQIP NDEVVALASH IYNEESKKAL EEIFNQYISI SMKHNFPIML TTPTRRANKE RVFQSKYNKN IICDNVSFLH KLKNKFPSHV YIGGLMGCRG DAYKADSILS VKEALEFHSW QASLFAETKV DFLYAGIMPA LSEAIGMAMT MENTSLPYII SFMIKENGQL IDGTTIHEAI AAIDSSTKRK PLCYMTNCVH PTVVFKALSQ IDNTTTLVQE RFKGIQANTS SLPPELLDIS SELKTSDANS FAAGMLELYK NYKLKIFGGC CGTDNTHMNE TAQRLGVVNY E // ID G7XZ18_ASPKW Unreviewed; 354 AA. AC G7XZ18; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 07-JAN-2015, entry version 14. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:GAA92203.1}; GN ORFNames=AKAW_10317 {ECO:0000313|EMBL:GAA92203.1}; 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 {ECO:0000313|EMBL:GAA92203.1, ECO:0000313|Proteomes:UP000006812}; RN [1] {ECO:0000313|Proteomes:UP000006812} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 4308 {ECO:0000313|Proteomes:UP000006812}; 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; DF126489; GAA92203.1; -; Genomic_DNA. DR InParanoid; G7XZ18; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000006812; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006812}; KW Methyltransferase {ECO:0000313|EMBL:GAA92203.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006812}; KW Transferase {ECO:0000313|EMBL:GAA92203.1}. SQ SEQUENCE 354 AA; 38911 MW; DB7F848FA941D447 CRC64; MAKTPILILD GGLGTSLQDH YNITFSSDTT PLWSSHLMIS DPKTLLSCQR DFTTTAAVDV LLTATYQVSP EGFQRTKTPS HPSGIPRASI AGYLRTALDV AEQAVQDTSA SVALSLGPYG ACMIPGQEYS GKYDGEHDDE EKLWRWHTDR LGLFDDEAME GKGLRERVKY IAMETVPRID EVRAVRRAVW SSKGFCEGVP FWVACVFPVE DKDTLPDGST VDEVVEAMLL PIEGGATPWG IGINCTKLHK LPKLVGLFGD AVGRLLREGR IQERPALVLY PDGTQGEVYN TATQTWEKVQ DKSGTADSRP WEVQLSQVVN DAAATGRFSS ILVGGCCKAS FNDIKRLREQ LRQE // ID G7Z3X0_AZOL4 Unreviewed; 1163 AA. AC G7Z3X0; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=B12-dependent homocysteine-N5-methyltetrahydrofolate transmethylase {ECO:0000313|EMBL:CBS86112.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CBS86112.1}; GN Name=metH {ECO:0000313|EMBL:CBS86112.1}; GN OrderedLocusNames=AZOLI_0758 {ECO:0000313|EMBL:CBS86112.1}; OS Azospirillum lipoferum (strain 4B). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Azospirillum. OX NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS86112.1, ECO:0000313|Proteomes:UP000005667}; RN [1] {ECO:0000313|Proteomes:UP000005667} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4B {ECO:0000313|Proteomes:UP000005667}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; FQ311868; CBS86112.1; -; Genomic_DNA. DR RefSeq; WP_014247150.1; NC_016622.1. DR RefSeq; YP_005038358.1; NC_016622.1. DR EnsemblBacteria; CBS86112; CBS86112; AZOLI_0758. DR KEGG; ali:AZOLI_0758; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; ALIP862719:GJAA-704-MONOMER; -. DR Proteomes; UP000005667; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000005667}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CBS86112.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005667}; KW Transferase {ECO:0000313|EMBL:CBS86112.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 733 733 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1163 AA; 127736 MW; 5A939E8E332D5826 CRC64; MPHILDTLRD RVLLCDGGFG SRIQALDLDV EKDYWGHENC TDILPLSRPD IVRDIHRGYF EAGADMVETD TFGASPVTLG EFGISEKAFE INQRAVELAR EAAESFRDGQ PRFVIGSIGP GTKLPSLGHI AYQPAEDSFY VQAAGLIAGG ADAILVETCQ DPLQIKAAVN GIKRARAEAN SDTPVFVQVT VETTGTLLVG TDIAAAATVI QALDVPLMGL NCATGPLEMS EHVRWLSQNW PGLISVQPNA GLPELVDGKT HYPLLANDFA HWLERFVSED GVNLVGGCCG TNVPHIAAAN QMLRKLAPAG SHRPAPKGRT VHWVPAVASL YSQVTLRQEN AFFAIGERCN ANGSKKWREL QEKNDWDGCV EMAREQVKEG SHSLDVCTAF VGRDEVAEMN AVISRFAGSV TAPLVIDSTE YKVLEQALAL YGGKAILNSI NFEDGEEPAR KRLELAKKFG AAVIALTIDE EGMAKTPDRK LAIAKRLYDL AVNEYGLAPS DLLFDPLTFT IATGNEDDRK LAIWTLEGIE AIAREMPGCQ IILGLSNVSF GLNAAARHVL NSVFLDHAVK KGMTGAIVHV SKILPLHQIP EKEVKTAEDL IFDRRAEGYD PLQAFIALFE GRKAADAKKK ARAENVEDRL KERIVDGDRT GLEDDLAEAM KTHPPLEIIN TYLLDGMKVV GELFGAGKMQ LPFVLQSAET MKAAVAWLEP HMEKIEGQQK GTLVLATVKG DVHDIGKNLV DIILTNNGYK VINLGIKQPV TAIIQAAKEH KADAVGMSGL LVKSTVVMRE NLEEMTREGL EVPVLLGGAA LTRAYVEGDC VASYGSGRVA YAGDAFDGLT LMDKVVEGSF DQQLAIQQAK RAGKATNRRR VLGQATSAAT GPVDKDAVRA RRHRLAEGVP VPTPPFWGPK LIDHVPLKTL VTYLNERMLY QLQWGYRKDG KSFEEFKEWA KKELRPVLDR ILQIAAKEEI LRPTAVYGYW KAAADGNDVI LFEEDGTTEA ARFTMPRQGK EDGECIADFL RDVTDPERDV LGLQVVTMGQ HCAEVAREWF AENRYQDYLY LHGLSVEMTE AMAEYVHARI RAELGYGAED SRDKEKLLQQ SYRGSRYSFG YPACPNLKDQ EQLLKLLDAG RIGIEMSDED QLHPEQSTSA IVLHHPRAKY FSV // ID G7ZRB3_STAAU Unreviewed; 613 AA. AC G7ZRB3; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 26. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=SAMSHR1132_03300 {ECO:0000313|EMBL:CCE58183.1}; OS Staphylococcus aureus subsp. aureus MSHR1132. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=985002 {ECO:0000313|EMBL:CCE58183.1, ECO:0000313|Proteomes:UP000005887}; RN [1] {ECO:0000313|EMBL:CCE58183.1, ECO:0000313|Proteomes:UP000005887} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MSHR1132 {ECO:0000313|EMBL:CCE58183.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; CCE58183.1; -; Genomic_DNA. DR RefSeq; WP_000077332.1; NC_016941.1. DR RefSeq; YP_005324852.1; NC_016941.1. DR EnsemblBacteria; CCE58183; CCE58183; SAMSHR1132_03300. DR KEGG; suh:SAMSHR1132_03300; -. DR KO; K00547; -. DR BioCyc; SAUR985002:GLKP-331-MONOMER; -. DR Proteomes; UP000005887; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005887}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862, KW ECO:0000313|EMBL:CCE58183.1}. SQ SEQUENCE 613 AA; 68504 MW; 96A6C489668D072A CRC64; MSQFLTQLKD NVLVADGAIG TILYSEGLDT CPEAYNLSHP DKVERIHRSY IEAGADVIQT NTYGANFEKL KRFGLEDKVK DIHQAAVRIA KKASNKDTFI LGTVGGFRGI KQEDISLQTI LYHTEIQIDT LVEEGVDALL FETYYDLEEL TNVITRTRKK YDIPIIAQLT ASNTNYLVNG QAINEGLKQL VQCGANIVGL NCHHGPHHMQ ESFTHIELPE QAYLSCYPNA SLLDIENSEF KYSDNAQYFG QVAQNLIREG IRLIGGCCGT TPEHIKFIKE SIQSLKPVND KKVIPIPTKA LFNPSQHKVR QSLTSKVQER PTVIIELDTP KHLDTDRFFE NIAKLDKANV DAVTLADNSL ATVRISNIAA ASLIKQYYNI EPLVHITCRD RNLIGLQSHL LGLSLIGVNE ILAITGDPSK VGHLPGATNV YDVNSKGLTE LALRFNQGIN TDGDALKKRT HFNIAGAFNP NVRKLDGAVK RLEKKIESGM SYFITQPVYS KEKIIEIYHA TKHLNKPFFI GIMPIASYKN ALFLHNEVPG IKMSDEILQQ FEAVKDDKAK TRELSLKLSK DLIDTVHEYF NGLYIITPFQ NVEDSLELAA YSKSITAHKE AIL // ID G8AMD6_AZOBR Unreviewed; 609 AA. AC G8AMD6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Main chromosome complete genome {ECO:0000313|EMBL:CCC98398.1}; GN ORFNames=AZOBR_140128 {ECO:0000313|EMBL:CCC98398.1}; OS Azospirillum brasilense Sp245. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Azospirillum. OX NCBI_TaxID=1064539 {ECO:0000313|EMBL:CCC98398.1, ECO:0000313|Proteomes:UP000007319}; RN [1] {ECO:0000313|Proteomes:UP000007319} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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; HE577327; CCC98398.1; -; Genomic_DNA. DR RefSeq; WP_014240621.1; NC_016617.1. DR RefSeq; YP_005031790.1; NC_016617.1. DR EnsemblBacteria; CCC98398; CCC98398; AZOBR_140128. DR KEGG; abs:AZOBR_140128; -. DR KO; K00548; -. DR Proteomes; UP000007319; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007319}; KW Reference proteome {ECO:0000313|Proteomes:UP000007319}. SQ SEQUENCE 609 AA; 66566 MW; D4F413650F379C4A CRC64; MPHILDTLRD RVLLCDGGFG SRIQALDLDV EKDYWGHENC TDILPLSRPD IVREIHRGYF EAGADMVETD TFGASPVTLG EFGISEKAFE INQRAVELAR EAAETFTDGQ PRFVIGSVGP GTKLPSLGHI PYQDLEDSFF VQAAGLIAGG ADAILVETCQ DPLQIKAAVN GIKRARAEAG SDTPVFVQVT VETTGTLLVG TDIAAAATVI QALDVPLMGL NCATGPLEMS EHVKWLTQNW PGTRLRAAER RPAGTGRRQD ALPAARRRLR PLAGALRDRG RGEPRRRLLW HQRSAHRGGQ PDAAQAGPGR VAPPEPEGPH GPLGACGRLA LLAGHAAPGE RFLRHRRALQ RQRLQEVARA SGEERLGRLR RDGARAGEGR FAHAGRLHRL RRPRRGGGDE GRRAALRRLG HRPAGHRLHR IHRSGEGAGA LRRQGDHQLH QLRGRRGAGP QAPRARQEVR RGGDRSDHRR GGHGEDAGAQ ARRRQAPLRP RGQRVWPAGP RPAVRPADLH HRHRQRGRPQ AGHLDAGGHR GDQPRDARLP DHPGPVQRLL RPERGGPPRA ELGLPRPCGE ARHDRRHRAC VEDHAAAPDP GKGGQDRRGP DLRPPRGRV // ID G8AMD7_AZOBR Unreviewed; 918 AA. AC G8AMD7; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 29-APR-2015, entry version 23. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CCC98399.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CCC98399.1}; GN Name=metH {ECO:0000313|EMBL:CCC98399.1}; GN ORFNames=AZOBR_140129 {ECO:0000313|EMBL:CCC98399.1}; OS Azospirillum brasilense Sp245. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Azospirillum. OX NCBI_TaxID=1064539 {ECO:0000313|EMBL:CCC98399.1, ECO:0000313|Proteomes:UP000007319}; RN [1] {ECO:0000313|Proteomes:UP000007319} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; HE577327; CCC98399.1; -; Genomic_DNA. DR RefSeq; WP_014240622.1; NC_016617.1. DR RefSeq; YP_005031791.1; NC_016617.1. DR EnsemblBacteria; CCC98399; CCC98399; AZOBR_140129. DR KEGG; abs:AZOBR_140129; -. DR KO; K00548; -. DR Proteomes; UP000007319; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007319}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CCC98399.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007319}; KW Transferase {ECO:0000313|EMBL:CCC98399.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 43 43 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 44 44 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 488 488 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 918 AA; 101412 MW; 32D8441C1E45098A CRC64; MQPNAGLPEL VDGKTHYPLR ADDFAHWLER FVTEDGVNLV GGCCGTNVPH IAAANQMLRK LAPAGSHRPN PKGRTVHWVP AVASLYSQVT LRQENAFFAI GERCNANGSK KWRELQEKND WDGCVEMARE QVKEGSHTLD VCTAFVGRDE VAEMKAVVQR FAGSVTAPLV IDSTEYIVLE KALALYGGKA IINSINFEDG EEPARKRLAL AKKFGAAVIA LTIDEEGMAK TPERKLAVAK RLYDLAVNEF GLPAHDLLFD PLTFTIATGN EDDRKLAIWT LEGIEAISRE MPGCQIILGL SNVSFGLNAA ARHVLNSVFL DHAVKRGMTG AIVHVSKIMP LHLIPEKEVK TAEDLIFDRR AEGYDPLQAF IALFEGRKAA DAKKKARAET VEERLKERIV DGDRTGLEDD LAEAMKTHPP LEIINTYLLD GMKVVGELFG AGKMQLPFVL QSAETMKAAV AWLEPHMEKL DGQQKGTMVL ATVKGDVHDI GKNLVDIILT NNGYKVVNLG IKQPVGAIIQ AAKEHKADAV GMSGLLVKST VVMRENLEEM TREGLEVPVL LGGAALTRAY VETDCVASYG SGRVAYAGDA FDGLTLMDQV VGGSFDQQLA IQQAKRAGRA VNRRRVLGQA TSATIGPVDK DAARARRARL AEGVPVPTPP FWGPKVIEHV PLKTLVTYLN ERMLYQLQWG YRKDGKSFEE FKEWAKKELR PVLDRILQIA AKEEILRPQA VYGYWKAAAD GDDVILFAEN GTSEVARFSL PRQAKEDGEC IADFLRDVND GERDVLGLQI VTMGQHCAEV AREWFAENRY QDYLYLHGLS VEMTEAMAEY VHARIRAELG YGAEDSRDKE KLLQQAYRGS RYSFGYPACP NLADQEQLLK LLDAGRIGVE MSDEHQLHPE QSTSAIVLHH PRAKYFSV // ID G8BWD7_TETPH Unreviewed; 331 AA. AC G8BWD7; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 29-APR-2015, entry version 16. DE SubName: Full=TPHA0G03760 protein {ECO:0000313|EMBL:CCE64215.1}; GN Name=TPHA0G03760 {ECO:0000313|EMBL:CCE64215.1}; GN OrderedLocusNames=TPHA_0G03760 {ECO:0000313|EMBL:CCE64215.1}; 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 {ECO:0000313|EMBL:CCE64215.1, ECO:0000313|Proteomes:UP000005666}; RN [1] {ECO:0000313|EMBL:CCE64215.1, ECO:0000313|Proteomes:UP000005666} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5 RC {ECO:0000313|Proteomes:UP000005666}; 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; HE612862; CCE64215.1; -; Genomic_DNA. DR RefSeq; XP_003686649.1; XM_003686601.1. DR GeneID; 11535796; -. DR KEGG; tpf:TPHA_0G03760; -. DR KO; K00547; -. DR OrthoDB; EOG7X9GHR; -. DR Proteomes; UP000005666; Chromosome 7. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005666}; KW Reference proteome {ECO:0000313|Proteomes:UP000005666}. SQ SEQUENCE 331 AA; 37699 MW; FE65E8BBB7EF605B CRC64; MARQCIKNYL QENPNKVLVM DGGQGTELEN RGIKVANPVW STIPFISESF WSDQSSEDRK IVKEMFNDFI NAGAEILMTT TYQTSFKSVS ENTPIKNTKH YNELLNRIID FSRDCIGEER YLIGCIGSWG AHICAEFHGD YGEHPENIDF YEYFKPQLDN FFNNNKLDLI GFETVPNIHE LKAILSWDEK ILSKPFYIGL SVHENGLLRD GTSMQEVANL IKGFGEKLNP NLTLLGINCV SYNHSNDIIK SIHKELPNLP LIAYPNSGEI YDTTKKIWLP NKNPIFTWDD IVKGYIEAGV RIIGGCCRTT PNDIKAVTIA VKERAKKYID M // ID G8BXA5_TETPH Unreviewed; 323 AA. AC G8BXA5; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 29-APR-2015, entry version 16. DE SubName: Full=TPHA0I00260 protein {ECO:0000313|EMBL:CCE64533.1}; GN Name=TPHA0I00260 {ECO:0000313|EMBL:CCE64533.1}; GN OrderedLocusNames=TPHA_0I00260 {ECO:0000313|EMBL:CCE64533.1}; 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 {ECO:0000313|EMBL:CCE64533.1, ECO:0000313|Proteomes:UP000005666}; RN [1] {ECO:0000313|EMBL:CCE64533.1, ECO:0000313|Proteomes:UP000005666} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5 RC {ECO:0000313|Proteomes:UP000005666}; 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; HE612864; CCE64533.1; -; Genomic_DNA. DR RefSeq; XP_003686967.1; XM_003686919.1. DR GeneID; 11534333; -. DR KEGG; tpf:TPHA_0I00260; -. DR KO; K00547; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000005666; Chromosome 9. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005666}; KW Reference proteome {ECO:0000313|Proteomes:UP000005666}. SQ SEQUENCE 323 AA; 36772 MW; 27FD428A699054FE CRC64; MRVPFRKFID EHPNEILVLD GGQGTELENR GVNINSPLWS TISFVNDKFW DENIENTERK CIREMFNDFK DAGANVFSTL TYQTSFSSVS ENTDIKSLQE YHELLRKITG FCRRCISDDD YLLGCIGAYA ASIGAEYDGN YGLFAGKIDY LKYFKPQLDE FNNDMNIDII GFETIPNKHE LEAILSWDED IINRPFFIAL SLSDKNGLRD GTSFEEMGRL FAKYKGRNKN LVYVGGNCIS YAYSIDNIRK LHDIVPHLNL IAYPNSGEIY DQKSKQWSST SAIKISWEEV VNEYADAGVK IIGGCCRTTP DDIKQIKKAV DAL // ID G8JSB9_ERECY Unreviewed; 326 AA. AC G8JSB9; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 07-JAN-2015, entry version 18. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AET39641.1}; GN OrderedLocusNames=Ecym_4612 {ECO:0000313|EMBL:AET39641.1}; 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 {ECO:0000313|EMBL:AET39641.1, ECO:0000313|Proteomes:UP000006790}; RN [1] {ECO:0000313|Proteomes:UP000006790} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS 270.75 / DBVPG 7215 / KCTC 17166 / NRRL Y-17582 RC {ECO:0000313|Proteomes:UP000006790}; 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; CP002500; AET39641.1; -; Genomic_DNA. DR RefSeq; XP_003646458.1; XM_003646410.1. DR GeneID; 11472848; -. DR KEGG; erc:Ecym_4612; -. DR InParanoid; G8JSB9; -. DR KO; K00547; -. DR OrthoDB; EOG7X9GHR; -. DR Proteomes; UP000006790; Chromosome 4. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006790}; KW Reference proteome {ECO:0000313|Proteomes:UP000006790}. SQ SEQUENCE 326 AA; 36926 MW; 70FB66C74E720715 CRC64; MVRASVKQLL QSNPDQILIM DGGQGTELEN RGINVANPVW STIPFINDSF WSDRSSRDRQ IVAGMFEEYI AAGANLLMTI TYQSSFKSVS ENTDIKTLEE YNQLLDRIVA FSRTCIGADN YLVGCIGSWG AHICAEFSGD YGEHPERIPY LDYFRPQLNN FNLQEDIDVI GFETIPNIHE LTAILSWDES IIKKPFYIGM SVHEHGTLRD GTTMSQVAQL FRSLGKKLNP NFLALGINCC SFRYSHMILE SLHEELPYIP LIAYPNSGEL YDTVKKIWLK NENCIVTWDE IVKSYLQSGA RIIGGCCRTT PNDIRQIVTA VKKYKP // ID G8LHG7_ENTCL Unreviewed; 1232 AA. AC G8LHG7; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 29-APR-2015, entry version 27. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEW71677.1}; GN Name=metH {ECO:0000313|EMBL:AEW71677.1}; GN ORFNames=EcWSU1_00237 {ECO:0000313|EMBL:AEW71677.1}; OS Enterobacter cloacae EcWSU1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex. OX NCBI_TaxID=1045856 {ECO:0000313|EMBL:AEW71677.1, ECO:0000313|Proteomes:UP000007838}; RN [1] {ECO:0000313|EMBL:AEW71677.1, ECO:0000313|Proteomes:UP000007838} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EcWSU1 {ECO:0000313|EMBL:AEW71677.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002886; AEW71677.1; -; Genomic_DNA. DR RefSeq; WP_014168179.1; NC_016514.1. DR RefSeq; YP_004950098.1; NC_016514.1. DR EnsemblBacteria; AEW71677; AEW71677; EcWSU1_00237. DR KEGG; eec:EcWSU1_00237; -. DR KO; K00548; -. DR BioCyc; ECLO1045856:GHCE-246-MONOMER; -. DR Proteomes; UP000007838; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007838}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 252 252 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 315 315 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 316 316 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 764 764 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1232 AA; 135913 MW; 9D7DA076B10F0125 CRC64; MSGASVSSKV EQLRAQLNKR ILVLDGGMGT MIQSYRLSED DFRGERFADW PCDLKGNNDL LVLSKPQVIS AIHNAYFEAG ADIVETNTFN STTIAMADYQ MESLSAEINL AAAKLARACA DEWTARTPDK PRYVAGVLGP TNRTASISPD VNDPAFRNIS FDQLVAAYRE STKALVEGGS DLILIETVFD TLNAKAAIYA VKEEFEALGV DLPIMISGTI TDASGRTLSG QTTEAFYNSL RHAEALSFGL NCALGPDELR QYVQELSRIA ECYVTAHPNA GLPNAFGEYD LDADTMAAQI REWAESGFLN IVGGCCGTTP EHIAAMSNAV AGLPPRQLPT LPVACRLAGL EPLTIGDDSL FVNVGERTNV TGSAKFKRLI KEEKYSEALD VARQQVESGA QIIDINMDEG MLDAEAAMVR FLNLIAGEPD IARVPIMIDS SKWEVIEKGL KCIQGKGIVN SISMKEGVDT FIHHAKMVRR YGAALVVMAF DEMGQADTRA RKIEICRRAY KILTEEVGFP PEDIIFDPNI FAVATGIEEH NNYAQDFIGA CEDIKRELPH ALISGGVSNV SFSFRGNDPV REAIHAVFLY YAIRNGMDMG IVNAGQLAIY DDLPAELRDA VEDVILNRRD DATERMLDLA EKYRGSKSDA SVNIQQAEWR AWDVKKRLEY SLVKGITEFI EQDTEEARQQ STRPIEVIEG PLMDGMNVVG DLFGEGKMFL PQVVKSARVM KQAVAYLEPF IEASKEKGSS NGKMVIATVK GDVHDIGKNI VGVVLQCNNY EIIDLGVMVP ADKILKTARE VNADLIGLSG LITPSLDEMV NVAKEMERQG FTIPLLIGGA TTSKAHTAVK IEQNYSGPTV YVQNASRTVG VVSALLSATQ RDDFVARTRK EYETVRIQHG RKKPRTPPVT LQAARDNDLA FDWASYTPPV AHRLGVQDVT ASIETLRNYI DWTPFFMTWS LAGKYPRILE DEVVGEEAKR LFNDANEMLD QLSAHKSLNP RGVVGLFPAN RVGDDIEIYR DETRTHVLAV SRHLRQQTEK VGFANYCLAD FVAPKLSGKA DYIGAFAVTG GLEEDALAEA FDAQHDDYNK IMVKAIADRL AEAFAEYLHE RVRKVHWGYA ANENLSNEEL IRENYQGIRP APGYPACPEH TEKGTIWTLL DVEAHTGMKL TESFAMWPGA SVSGWYFSHP DSKYFAVAQL QRDQIEDYAL RKGMSVSEVE RWLAPNLGYD AD // ID G8LP61_ENTCL Unreviewed; 310 AA. AC G8LP61; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AEW72321.1}; GN Name=mmuM {ECO:0000313|EMBL:AEW72321.1}; GN ORFNames=EcWSU1_00881 {ECO:0000313|EMBL:AEW72321.1}; OS Enterobacter cloacae EcWSU1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex. OX NCBI_TaxID=1045856 {ECO:0000313|EMBL:AEW72321.1, ECO:0000313|Proteomes:UP000007838}; RN [1] {ECO:0000313|EMBL:AEW72321.1, ECO:0000313|Proteomes:UP000007838} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EcWSU1 {ECO:0000313|EMBL:AEW72321.1}; 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 ----------------------------------------------------------------------- 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; AEW72321.1; -; Genomic_DNA. DR RefSeq; WP_014168799.1; NC_016514.1. DR RefSeq; YP_004950742.1; NC_016514.1. DR EnsemblBacteria; AEW72321; AEW72321; EcWSU1_00881. DR KEGG; eec:EcWSU1_00881; -. DR KO; K00547; -. DR BioCyc; ECLO1045856:GHCE-910-MONOMER; -. DR Proteomes; UP000007838; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007838}; KW Methyltransferase {ECO:0000313|EMBL:AEW72321.1}; KW Transferase {ECO:0000313|EMBL:AEW72321.1}. SQ SEQUENCE 310 AA; 33473 MW; 3DE69D802793F008 CRC64; MSQNNPLTAI LEKQPFVVLD GAMATELEAR GCNLADSLWS AKVLVENPDL IRDVHLDYYR AGAQVAITAS YQATPAGFAA RGLDEAQSRA LIGKSVELAR KAREAYLAEN PHAGTLLVAG SVGPYGAYLA DGSEYRGDYV RSAEAFTDFH RPRVEALLDA GADLLACETL PSFAEIKALA ALLAEYPRAR GWFSFTLRDS EHLSDGTPLR EVISALERYP QIVALGINCI ALENTTAALK HLHSLTALPL VVYPNSGEHY DAVTKTWHHH GEACETLAGY LPQWLAAGAK LIGGCCRTTP TDIAELKAQR // ID G8LVZ9_CLOCD Unreviewed; 802 AA. AC G8LVZ9; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Homocysteine S-methyltransferase/B12 binding domain/Pterin binding enzyme {ECO:0000313|EMBL:AEV68603.1}; GN OrderedLocusNames=Clocl_2004 {ECO:0000313|EMBL:AEV68603.1}; OS Clostridium clariflavum (strain DSM 19732 / NBRC 101661 / EBR45). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminiclostridium. OX NCBI_TaxID=720554 {ECO:0000313|EMBL:AEV68603.1, ECO:0000313|Proteomes:UP000005435}; RN [1] {ECO:0000313|Proteomes:UP000005435} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19732 / NBRC 101661 / EBR45 RC {ECO:0000313|Proteomes:UP000005435}; 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 ----------------------------------------------------------------------- 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; AEV68603.1; -; Genomic_DNA. DR RefSeq; WP_014255183.1; NC_016627.1. DR RefSeq; YP_005046527.1; NC_016627.1. DR EnsemblBacteria; AEV68603; AEV68603; Clocl_2004. DR KEGG; ccl:Clocl_2004; -. DR KO; K00548; -. DR BioCyc; CCLA720554:GI2T-2001-MONOMER; -. DR Proteomes; UP000005435; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005435}; KW Methyltransferase {ECO:0000313|EMBL:AEV68603.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005435}; KW Transferase {ECO:0000313|EMBL:AEV68603.1}. SQ SEQUENCE 802 AA; 87118 MW; A79092EE384E71AA CRC64; MNRQQFLEFL KENIMILDGA TGTELQKRGM PKGVCPEKWV IENPDVILDV QREYVSAGSN AVYTCTFGAN RIKLEAFGLQ DKVVEMNAEL ARLSKKAVGD KAFVAGDLAP TGKFIKPFGD MDFETCVEVY KEQVKGLLEG GVDFFVIETM MDIQEARAAL IAVKESCDLP VCVSMTFEES GKTLMGTDPL TALITLQSLG ADAVGCNCST GPKAMIEIIR AMKPYALVPL LAKPNAGLPK LVDGKTVFDM GVEEYGTYVE ELVKSGVNLL GGCCGTSPLY IAEIKKNLKG LKPLKIEPEK VSAITSARST VFLGTNQPTV VVGERINPTG KKKLQEELKE GKTSLVTDLA LEQVEKGAKV LDVNVGMPGI DEKETMVKIV ELLVSMVSTP LCLDSSSPEV LEAALRIYPG RALINSISAE KAKLEKLLPV AAKYGAMFIL LPLSDEGVPA TAEERYTIIN EVYERAKKYG YEKKDIVIDG LVMTVASDQK AALETLKVID WSTNTFGCNT ILGLSNVSFG LPERSWVNSA FLAMAMGKGL TMAILNPSSD TLMSIKMAGD VLTGKDKNSL KYIEYFGGST KEKPVQTKKA EQSVTERIYG AVVGGDRENI KLHIETALKE GYEASYLVDN CLIPAINHVG DLYDKKEYFL PQLIQSAETM KEAFGLVEPL LKKDETAEKA KARIVIATVK GDIHDIGKNI VALMLRNYGF EVYDLGKDVP AEEIINAAKE KKAEIIGLSA LMTTTMMEMK TVIELAKKEG LKAKFMVGGA VVTESFAKEI GADGYSEDAY SAVKLANKLL EA // ID G8MAK5_9BURK Unreviewed; 356 AA. AC G8MAK5; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AET87974.1}; GN ORFNames=BYI23_A001360 {ECO:0000313|EMBL:AET87974.1}; OS Burkholderia sp. YI23. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=1097668 {ECO:0000313|EMBL:AET87974.1, ECO:0000313|Proteomes:UP000006801}; RN [1] {ECO:0000313|EMBL:AET87974.1, ECO:0000313|Proteomes:UP000006801} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YI23 {ECO:0000313|EMBL:AET87974.1}; 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 ----------------------------------------------------------------------- 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; AET87974.1; -; Genomic_DNA. DR RefSeq; WP_014190214.1; NC_016589.1. DR RefSeq; YP_004975951.1; NC_016589.1. DR EnsemblBacteria; AET87974; AET87974; BYI23_A001360. DR KEGG; byi:BYI23_A001360; -. DR KO; K00548; -. DR BioCyc; BSP1097668:GKEO-138-MONOMER; -. DR Proteomes; UP000006801; Chromosome 1. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006801}; KW Methyltransferase {ECO:0000313|EMBL:AET87974.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006801}; KW Transferase {ECO:0000313|EMBL:AET87974.1}. SQ SEQUENCE 356 AA; 38392 MW; A3CB1CEDB4278794 CRC64; MSVMTENAIP KAPARAYTRG AALPALLQKR ILILDGAMGT MIQRYKLDEA AYRGERFKDY GRDIKGNNEL LSITQPQVIR EIHEQYLAAG ADILETNTFG ATRVAQADYG MEDLAAEMNI ESAKLAREAC DKYSTPDKPR FVAGAIGPTP KTASISPDVN DPGARNVTFD ELREAYYEQA KALLDAGCDL FLVETIFDTL NAKAALFALD QLFDDTGELV PIMISGTVTD ASGRILSGQT VEAFWNSLRH AKPLTFGLNC ALGAALMRPY IAELAKLCDT YVSCYPNAGL PNPMSDTGFD ETPDVTSGLL KEFATAGLVN IAGGCCGTTP EHIAEIAKAL AEVKPRAFPS QYRDAA // ID G8MIG5_9BURK Unreviewed; 321 AA. AC G8MIG5; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 01-APR-2015, entry version 16. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AET93373.1}; GN ORFNames=BYI23_C012270 {ECO:0000313|EMBL:AET93373.1}; OS Burkholderia sp. YI23. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=1097668 {ECO:0000313|EMBL:AET93373.1, ECO:0000313|Proteomes:UP000006801}; RN [1] {ECO:0000313|EMBL:AET93373.1, ECO:0000313|Proteomes:UP000006801} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YI23 {ECO:0000313|EMBL:AET93373.1}; 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003089; AET93373.1; -; Genomic_DNA. DR RefSeq; WP_014194011.1; NC_016590.1. DR RefSeq; YP_004979811.1; NC_016590.1. DR EnsemblBacteria; AET93373; AET93373; BYI23_C012270. DR KEGG; byi:BYI23_C012270; -. DR BioCyc; BSP1097668:GKEO-7268-MONOMER; -. DR Proteomes; UP000006801; Chromosome 3. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006801}; KW Methyltransferase {ECO:0000313|EMBL:AET93373.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006801}; KW Transferase {ECO:0000313|EMBL:AET93373.1}. SQ SEQUENCE 321 AA; 35089 MW; 725E906B54884BEA CRC64; MSQYRTHLPQ LDDALFMTDG GIETTLIFHE GIELPCFAAF DLLKDEAGTA RLEAYFRRYA SLAQSEGVGL VLEAPTWRAS ADWGRKLGYS DAALAEANRR AIGLLVRVRD AFETPGTPIV ISGCLGPRGD GYRIDSRMTR DEARAYHQPQ IDTLASTEAD LIAAFTMTYP EEGIGVIDAA RARSMPVAIS FTLETDGRLP SGDALRDVIE RADEQTDAYA AYYMINCAHP SHFDTVLGEG GAWRERIHGV RANASRRSHA ELDESVDLDD GNPDELGAQY RALNAFLPRM NVVGGCCGTD HRHVGAICHA MKGARNPYAH A // ID G8N715_GEOTH Unreviewed; 1136 AA. AC G8N715; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 01-APR-2015, entry version 24. DE SubName: Full=Methionine synthase I containing methyltransferase and cobalamin-binding domains {ECO:0000313|EMBL:AEV18121.1}; GN ORFNames=GTCCBUS3UF5_7980 {ECO:0000313|EMBL:AEV18121.1}; OS Geobacillus thermoleovorans CCB_US3_UF5. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus; OC Geobacillus thermoleovorans group. OX NCBI_TaxID=1111068 {ECO:0000313|EMBL:AEV18121.1, ECO:0000313|Proteomes:UP000005636}; RN [1] {ECO:0000313|EMBL:AEV18121.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCB_US3_UF5 {ECO:0000313|EMBL:AEV18121.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP003125; AEV18121.1; -; Genomic_DNA. DR RefSeq; WP_014195052.1; NC_016593.1. DR RefSeq; YP_004981221.1; NC_016593.1. DR EnsemblBacteria; AEV18121; AEV18121; GTCCBUS3UF5_7980. DR KEGG; gte:GTCCBUS3UF5_7980; -. DR KO; K00548; -. DR BioCyc; GTHE1111068:GJY8-861-MONOMER; -. DR Proteomes; UP000005636; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000005636}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEV18121.1}; KW Transferase {ECO:0000313|EMBL:AEV18121.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 724 724 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1136 AA; 125448 MW; D8E95F5D3096F322 CRC64; MANVTLEQQL QRKILVIDGA MGTMIQSANL SAADFGGEAY EGCNEYLTLT APHVIRRIHE AYLEAGADII ETNTFGATRI VLDEYGLGHL ALELNIEAAK LAKQTAESFS TPDWPRFVAG SMGPTTKTLS VTGGATFEEL VAAYEEQARG LLLGGVDLLL LETCQDTLNV KAGFLGISKA FEAVGRRVPL MISGTIEPMG TTLAGQAIDA FFISVRHMKP IAVGLNCATG PEFMTDHLRT LASLADTAVS CYPNAGLPDE EGHYHETPNM LAEKIRRFAE KGWINIVGGC CGTTPDHIRA IAEAVRDLPP RAIPSSFDVH AVSGIEALIY DETMRPLFVG ERTNVIGSRK FKRLIAEGKY EEAAEIARAQ VKNGAHVIDI CLADPDRDEL HDMEQFVREV VKKVKVPLVI DSTDERVIER ALTYSQGKAI INSINLEDGE ERFANVVPLL HRYGAAVVVG TIDEQGMAVT AERKLEIALR SYDLLVNRYG VPERDIIFDP LVFPVGTGDE QYIGAAKETI EGIRLIKERL PHCLTMLGIS NVSFGLPPAG REVLNSVFLY HCTQAGLDYA IVNTEKLERF ASIPEEEVRM AEALLFDTND ETLNAFIEFY RSKITAAKPA QTNLSLEERL ARYVIEGSKD GLIPDLEKAL ETYSDPLSII NGPLMAGMDE VGRLFNNNQL IVAEVLQSAE VMKAAVAFLE PYMEKKEGST KGKVILATVK GDVHDIGKNL VDIILSNNGY EVIDLGIKVA PQQLIEAVRE HQPDIIGLSG LLVKSAQQMV VTAQDLRQAG ISTPILVGGA ALTRKFTENK IAPEYDGVVL YAKDAMDGLA LANQIQQGEI DYKKKETAES EPTRQTTVVT AVKSTVSTDV PVYIPADLER HVLKNVPLDH VLPYVNWQMV LGHHLGLKGK VKRLLEEKDE KALALKAVVD ELLAEAKERR WIQPAGVYRF FPAQSDGNRV YIYDPTDGKT VLEMFDFPRQ PRAPYLCLAD YLKSKESGEM DYVGLFAVTA GHGVRELAQH WKEEGEFLKS HAIQALALEI AEGFAERIHQ IMRDRWGFPD DPDFTMEERF AAKYQGQRYS FGYPACPNLE DQEKLFRLLH PEDIGIRLTD GYMMEPEASV SAIVFAHPEA RYFNVL // ID G8N716_GEOTH Unreviewed; 615 AA. AC G8N716; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 24. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=GTCCBUS3UF5_7990 {ECO:0000313|EMBL:AEV18122.1}; OS Geobacillus thermoleovorans CCB_US3_UF5. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus; OC Geobacillus thermoleovorans group. OX NCBI_TaxID=1111068 {ECO:0000313|EMBL:AEV18122.1, ECO:0000313|Proteomes:UP000005636}; RN [1] {ECO:0000313|EMBL:AEV18122.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCB_US3_UF5 {ECO:0000313|EMBL:AEV18122.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; AEV18122.1; -; Genomic_DNA. DR RefSeq; WP_014195053.1; NC_016593.1. DR RefSeq; YP_004981222.1; NC_016593.1. DR EnsemblBacteria; AEV18122; AEV18122; GTCCBUS3UF5_7990. DR KEGG; gte:GTCCBUS3UF5_7990; -. DR KO; K00547; -. DR BioCyc; GTHE1111068:GJY8-862-MONOMER; -. DR Proteomes; UP000005636; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005636}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 615 AA; 67298 MW; 47DC434BB385E5FD CRC64; MGLLDKLKER ILIADGAMGT LLYSHGIDRC FEELNLSNPD EIVHIHEAYI AAGADVIQTN TYGANYVKLA RYGLEDEVPA INRAAVRLAR QAANGRAYVL GTIGGLRTLN KSVVTLEEVK RTFREQLFVL LAEGVDGVLL ETYYDLEELE TVLAIARKET DLPIIAHVSL HEVGVLQDGT PLADALARLE ALGADVVGLN CRLGPYHMLR SLEEVPLPKQ AFLSAYPNAS LPDYRDGRLV YETNAEYFEE TAKAFRDQGV RLIGGCCGTT PKHIAAMAKA LSDRTPVTEK TVKRRAVSVS VQADRPAPSP LPELARTRRS VIVELDPPKK LGIDKFLAGA KALHDAGIDA LTLADNSLAT PRISNAAVAT IIKEQLGIRP LVHITCRDRN LIGLQSHLMG LHTLGITDVL AITGDPSKIG DFPGATSVYD LSSFDLIRLI RQFNEGLSYS GKPLGQKTNF SIGAAFNPNV RHLDKAVERM EKKIQCGAHY FLTQPIYSEE KIVEVHEATK HLDTPIYIGI MPLVSARNAD FLHHEVPGIT LSDEIRARMA ACGGDPVQAA KEGIAIAKSL IDAAFDLFNG IYLITPFLRY DMTVELVRYI HEKEAAAKER KVVHG // ID G8NCY4_9DEIN Unreviewed; 1183 AA. AC G8NCY4; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 01-APR-2015, entry version 23. DE SubName: Full=5-methyltetrahydrofolate homocysteine S-methyltransferase {ECO:0000313|EMBL:AEV16125.1}; GN ORFNames=TCCBUS3UF1_10800 {ECO:0000313|EMBL:AEV16125.1}; OS Thermus sp. CCB_US3_UF1. OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; OC Thermus. OX NCBI_TaxID=1111069 {ECO:0000313|EMBL:AEV16125.1, ECO:0000313|Proteomes:UP000005635}; RN [1] {ECO:0000313|EMBL:AEV16125.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCB_US3_UF1 {ECO:0000313|EMBL:AEV16125.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP003126; AEV16125.1; -; Genomic_DNA. DR RefSeq; WP_014515484.1; NC_017278.1. DR RefSeq; YP_005654199.1; NC_017278.1. DR EnsemblBacteria; AEV16125; AEV16125; TCCBUS3UF1_10800. DR KEGG; thc:TCCBUS3UF1_10800; -. DR KO; K00548; -. DR BioCyc; TSP1111069:GLMD-1090-MONOMER; -. DR Proteomes; UP000005635; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000005635}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEV16125.1}; KW Transferase {ECO:0000313|EMBL:AEV16125.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 256 256 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1183 AA; 130780 MW; 4519BBB9B2753E73 CRC64; MVEVHTCSPG CRHHLGGAGF GEAPLVRLGY NKEARARKFP YLKALLERPL VFDGAMGTEL QKRDLSPEDY GGEAHFGCPE VLNRTRPEVV REVHRAYLEA GAEVIETNTF GALRHVLAEY GLEGEAEELA YLGARIAKEA AEPYGAFVAG ALGPGTKLIS LGQISWEELF AAYKEAVRGL LRGGVDLILL ETAQDILQVR CAVLAAREAM AEVGREVPLQ VQVTLEATGT MLVGTDEQAA LAALESLPVD VVGMNCATGP DLMDSKIRYF AKNSTRFVAC LPNAGLPRNE GGRVVYDLTP EELAQWHRKF VLEYGVNAVG GCCGTTPQHI RRVAEAVKGL PVQARPQAFP PQVASLYQAV ALRQEASLFL VGERLNATGS KRFREMLFAR DLEGILALAR EQVEEGAHAL DLSVAWTGRD ELEDLKWLLP HLATAVTVPF MVDSTSAEAM ELALKHLPGR VLLNSANLEE GLARFDRVAS LAKAHGAALV VLTIDEKGMA KTREEKVRVA LSMYERLTEH HGFRPEDLLL DLLTFPITQG DEESRPLAKE TLLALEELRE RLPGVGFILG VSNVSFGLKP RPRRVLNSVF LDEARKKGLT AAIVDAGKIL PMDAIPEEAY ALALDLIYDR RREGYDPLFA FMAYFEAHQG DFAAKEDAFA ALPLWERLKR RVVEGRKGGL EADLDQALKE GHGPLDLING PLLQGMKEVG ELFAAGRMQL PFVLQAAEVM KRAVAHLEPH MERKGEGRGR MVLATVKGDV HDIGKNLVDI ILSNNGYQVV NLGIKVPIEE ILKAVEEHKP HAVGMSGLLV KSTLVMKENL EYMRERGYTL PVILGGAALT RSFVEEELRR IYPNVYYAED AFEGLRLMEA LTGGAPLPAP AQGIPRPKEA PRVAVRSKPV GEPPFVPRPP FFGVRVEEGL DLATLAHYVN KLALFRGQWG YRRQGMSREA WQALVEREAE PVFRRLLEEA IREGWLRPRV LYGFFPAARE GEEVLVFSPD TGEVLERFPF PRQRGGGLSL VDYFRPRFAP PLGEEAAWLP AYGAGARDVL GVQLVTMGEE ASQKARALFA AGAYQDYLFV HGFAVEMTEA LAEYWHKRMR QMWGIAGKDA PDIRRLFQQG YQGARYSFGY PACPDLSHQA KLDRLMGFHR VGVRLTESYQ LDPEHATSAL VVHHPEARYF NVD // ID G8NTX8_GRAMM Unreviewed; 366 AA. AC G8NTX8; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEU37534.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEU37534.1}; GN OrderedLocusNames=AciX8_3233 {ECO:0000313|EMBL:AEU37534.1}; OS Granulicella mallensis (strain ATCC BAA-1857 / DSM 23137 / MP5ACTX8). OC Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae; OC Granulicella. OX NCBI_TaxID=682795 {ECO:0000313|EMBL:AEU37534.1, ECO:0000313|Proteomes:UP000007113}; RN [1] {ECO:0000313|EMBL:AEU37534.1, ECO:0000313|Proteomes:UP000007113} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1857 / DSM 23137 / MP5ACTX8 RC {ECO:0000313|Proteomes:UP000007113}; 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; AEU37534.1; -; Genomic_DNA. DR RefSeq; WP_014266408.1; NC_016631.1. DR RefSeq; YP_005058564.1; NC_016631.1. DR EnsemblBacteria; AEU37534; AEU37534; AciX8_3233. DR KEGG; gma:AciX8_3233; -. DR KO; K00548; -. DR BioCyc; GMAL682795:GHBV-3275-MONOMER; -. DR Proteomes; UP000007113; Chromosome. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007113}; KW Methyltransferase {ECO:0000313|EMBL:AEU37534.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007113}; KW Transferase {ECO:0000313|EMBL:AEU37534.1}. SQ SEQUENCE 366 AA; 39782 MW; 49B35BA40D2040B9 CRC64; MTKAHQHPLE KILESRIAII DGAMGTTIRT YGMTEADIRG ERFKDSKKDL LNNGDLFSLT QPKMICDIHR RFLEAGADII ETNTFGATGI TQSEFFVDDP REHGGRKDPE FYQKIIEDKF LNDLAWEINE QSARQCREWA DRTANETGRQ RFVAGAIGPL TVSLSNSPDA DDSGFRVVTF DQVKAAYVQQ VRALIAGGSD LLLVETIFDS LNAKAALVAI REVFDQDGLT SNNKELPVMI SAAVGRGGET LISAQTTEAF WNAVQHVKPL SVGLNCSLGP DLMYPFLEEL SEKADVAISC YPNAGLPNPL SETGFDLGPQ DMARYLGDFA RGGLINIAGG CCGNTPEHIA AIAKALDGKA PRELGA // ID G8NVM1_GRAMM Unreviewed; 627 AA. AC G8NVM1; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 20. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=AciX8_3395 {ECO:0000313|EMBL:AEU37693.1}; OS Granulicella mallensis (strain ATCC BAA-1857 / DSM 23137 / MP5ACTX8). OC Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae; OC Granulicella. OX NCBI_TaxID=682795 {ECO:0000313|EMBL:AEU37693.1, ECO:0000313|Proteomes:UP000007113}; RN [1] {ECO:0000313|EMBL:AEU37693.1, ECO:0000313|Proteomes:UP000007113} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1857 / DSM 23137 / MP5ACTX8 RC {ECO:0000313|Proteomes:UP000007113}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; AEU37693.1; -; Genomic_DNA. DR RefSeq; WP_014266567.1; NC_016631.1. DR RefSeq; YP_005058723.1; NC_016631.1. DR ProteinModelPortal; G8NVM1; -. DR EnsemblBacteria; AEU37693; AEU37693; AciX8_3395. DR KEGG; gma:AciX8_3395; -. DR KO; K00547; -. DR BioCyc; GMAL682795:GHBV-3439-MONOMER; -. DR Proteomes; UP000007113; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007113}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:AEU37693.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862, KW ECO:0000313|EMBL:AEU37693.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007113}; KW Transferase {ECO:0000313|EMBL:AEU37693.1}. SQ SEQUENCE 627 AA; 67201 MW; 117459682327717B CRC64; MAVGIDRLFA GGTVLCDGAM GTMLYSCGVF INRCYDELNL SQPEMVRSVH QQYLQAGAEV IETNTFGANS FRLERFALRE KVREFNLAGA AIARQSVDAI REKQGTEAFV AGAVGPLGVR LEPLGKLSLE EAREAFAEQI SALAEGGVDL IIIETMMSID EAEQAVLAAR QVAPHLKVAV MVTVDEDGNC LDGTSPEVAA ERLTAVGADA IGCNCSSGPA TVLTVIERMR EATALPLLAM PNAGMPRNVE GRNIYLTSPE YMASFVRKAV RAGASWVGGC CGTTPAHIRA MRGSLRAMDA QESGERATEH TPHIVHASES EHRVEPRPLG ERSQIGRMIA DGEFVTMVEI VPPKGFDCSK ELAGALLMKK RGVHVINVPD SPRASARMGA QSLCVQIQQQ VGIETILHYT CRDRNVLSMQ SDLLGASSIG LKNILCLTGD PPKMGNYPDA TAVFDVDAIG LVNIVHGLNQ GLDIGRNPIG GSTGFTISVA ANPGVPDIEH EVRRFAYKVE AGAEFCITQP VFDLRLLEDF LRRIEGFRIP VIAGIWPLTS LRNAEFMKND LRVAMPDEIF VRMAAAGGKE EALAEGLKIA QEMLASVRGS VQGVQVSAPF GKYTAAAEVL GLTEEIA // ID G8PUV3_PSEUV Unreviewed; 1248 AA. AC G8PUV3; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 01-APR-2015, entry version 25. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:AEV38816.1}; GN OrderedLocusNames=PSE_4314 {ECO:0000313|EMBL:AEV38816.1}; OS Pseudovibrio sp. (strain FO-BEG1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Pseudovibrio. OX NCBI_TaxID=911045 {ECO:0000313|EMBL:AEV38816.1, ECO:0000313|Proteomes:UP000005634}; RN [1] {ECO:0000313|Proteomes:UP000005634} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FO-BEG1 {ECO:0000313|Proteomes:UP000005634}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP003147; AEV38816.1; -; Genomic_DNA. DR RefSeq; WP_014286646.1; NC_016642.1. DR RefSeq; YP_005082838.1; NC_016642.1. DR EnsemblBacteria; AEV38816; AEV38816; PSE_4314. DR KEGG; psf:PSE_4314; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; PSP911045:GJTQ-4372-MONOMER; -. DR Proteomes; UP000005634; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000005634}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005634}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 255 255 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 318 318 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 319 319 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 770 770 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1248 AA; 137146 MW; F9CB232DA9BAA970 CRC64; MSLQVKKTGS DIFAALEAAA KERILVLDGA MGTMIQNLQF SEEQFRGERF KSWNQDLKGN NDLLILTQPD AIRDIHLQYL KAGADIIETN TFSSTSIAQA DYAMESIVYE LNKEGARLCC EAVEQMKEID PSRRRFVAGG LGPTNRTASI SPDVNNPGFR AVSFDDLKDS YAEATRGLID GGCDLILVET IFDTLNAKAA LFAIDEVFEE KGVKLPVMIS GTITDLSGRT LSGQTPEAFW NSVRHAAPFT VGLNCALGAK EMRAHVDEIS RVADTLVCAY PNAGLPNEFG EYDESPEYMA GLLKEFAEAG LVNVVGGCCG TTPEHIKAVA DAVEGLPPRA LPEVPRLMRL SGLEPFTFTK DVNFVNVGER TNVTGSARFR KLIKNDDYTT ALDVARSQVE NGAQIIDINM DEGLLDSEEA MVTFLNLIAA EPDIAKVPVM IDSSKWTVIE AGLKCVQGKA VVNSISLKEG EENFIAQAKL IRRYGAAVVV MAFDETGQAD TLQRKIEICK RSYDVLVDKV GFGPEDIIFD PNIFAVATGI EEHDNYGVDF IEATRWISEN LPYAHISGGV SNLSFSFRGN EPVREAMHSV FLYHAIQAGM DMGIVNAGQL AVYDDLPAEL RELCEDVVLN RRSDSTDRLL DAAEKFKGAG GKKREVDLTW REGTVEKRLE HSLVHGITDF IVEDTEEARQ KADRPLHVIE GPLMDGMNVV GDLFGAGKMF LPQVVKSARV MKAAVAYLMP YLEQEKKELG LDESSSNGKI LMATVKGDVH DIGKNIVGVV LQCNNFEVID LGVMVPTAKI IDEAKKHNVD IIGLSGLITP SLDEMCHVAS EMEREGLDIP LLIGGATTSR VHTAVKIHPN YSKGQAIYVT DAGRAVGVAS RLMAEGGREE IYENTRLEYV DVAEKHAAAR NKKVRASIET ARANRFKPDF ETHKPTKPKF LGTKTFTDFS LEELVDYIDW TPFFATWEIK GAYPAVLTDD RYGPAAQALY NDAREMLKEI VDGKLLQANA VVGFWPCAQD GDDLVLYTDE SRTEELKRLY TLRQQMDRSS SDRGNVALAD FVAPVESGIP DYVGGFAVTA GIGEDVLAKR YADAGDDYNK ILSQAIADRL AEALAERMHQ LVRTELWAYA PDETLSNADL IAEGYDGIRP APGYPAQPDH TEKGTLWELL DAEAQTGISL TESYAMWPGS AVSGLYFSHP DSHYFGVGKI ERDQVQDYAV RKGWDLETAE RWLAPILNYN PMAREAAE // ID G8Q6L5_PSEFL Unreviewed; 1236 AA. AC G8Q6L5; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=MetH {ECO:0000313|EMBL:AEV63244.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:AEV63244.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEV63244.1}; GN Name=metH {ECO:0000313|EMBL:AEV63244.1}; GN ORFNames=PSF113_3245 {ECO:0000313|EMBL:AEV63244.1}; OS Pseudomonas fluorescens F113. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1114970 {ECO:0000313|EMBL:AEV63244.1, ECO:0000313|Proteomes:UP000005437}; RN [1] {ECO:0000313|EMBL:AEV63244.1, ECO:0000313|Proteomes:UP000005437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F113 {ECO:0000313|EMBL:AEV63244.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP003150; AEV63244.1; -; Genomic_DNA. DR RefSeq; WP_014338672.1; NC_016830.1. DR RefSeq; YP_005208639.1; NC_016830.1. DR EnsemblBacteria; AEV63244; AEV63244; PSF113_3245. DR GeneID; 11831337; -. DR KEGG; pfe:PSF113_3245; -. DR KO; K00548; -. DR BioCyc; PFLU1114970:GJXA-3264-MONOMER; -. DR Proteomes; UP000005437; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000005437}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEV63244.1}; KW Transferase {ECO:0000313|EMBL:AEV63244.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1236 AA; 135472 MW; DE6234EBB4F1412D CRC64; MSDRSARLYL LQQALKERIL ILDGGMGTMI QSYKLEEQDY RGKRFADWPS DVKGNNDLLV LSRPDVIGAI EKAYLDAGAD ILETNTFNAT QVSQADYGMQ SLAYELNLEG ARLARKVADA KTLETPDKPR FVAGVLGPTS RTCSLSPDVN NPGYRNVTFD ELVENYTEAT KGLIEGGADL ILIETIFDTL NAKAAIFAVQ GVYEELGVEL PIMISGTITD ASGRTLSGQT TEAFWNSVAH AKPISVGLNC ALGASELRPY LEELSNKAST HVSAHPNAGL PNEFGEYDEL PAETAKVIEE FAQSGFLNIV GGCCGTTPAH IEAIAKAVAG YAPRPIPEIP RACRLSGLEP FTIDRSSLFV NVGERTNITG SAKFARLIRE DNYTEALEVA LQQVEAGAQV IDINMDEGML DSKKAMVTFL NLIAGEPDIS RVPIMIDSSK WEVIEAGLKC IQGKGIVNSI SMKEGVEQFI HHAKLCKRYG AAVVVMAFDE AGQADTEARK KEICKRSYDI LVNEVGFPPE DIIFDPNIFA VATGIEEHNN YAVDFINACA YIRDELPYAL TSGGVSNVSF SFRGNNPVRE AIHSVFLLYA IRAGLTMGIV NAGQLEIYDQ IPVELRDAVE DVILNRTPEG TDALLAIADK YKGDGSVKEA ETEEWRGWEV NKRLEHALVK GITTHIVEDT EQSRLSFARP IEVIEGPLMA GMNIVGDLFG AGKMFLPQVV KSARVMKQAV AHLIPFIEAE KGDKPEAKGK ILMATVKGDV HDIGKNIVGV VLGCNGYDIV DLGVMVPAEK ILQVAKEQKC DIIGLSGLIT PSLDEMVHVA REMQRQDFHL PLMIGGATTS KAHTAVKIEP KYSNDAVIYV TDASRAVGVA TQLLSKELKP AFVEKTRLDY IDVRERTSNR SARTERLSYP AAVAKKPQFD WSSYQPVKPT FTGAKVLDNI DLNVLAEYID WTPFFISWDL AGKYPRILTD EVVGEAATAL YADARAMLRK LIDEKLISAR AVFGFWPANQ VHDDDLEVYG DDGKPLARLH HLRQQIIKTD GKPNFSLADF VAPKDSGVTD YVGGFITTAG IGAEEVAKAY QEAGDDYNSI MVKALADRLA EACAEWLHQQ VRKDYWGYAQ DESLDNDALI KEQYTGIRPA PGYPACPDHT EKATLFRLLD PEASELKAGR SGVFLTEHYA MFPAAAVSGW YFAHPQAQYF AVGKIDKDQV QSYTARKGQD LSVTERWLSP NLGYDN // ID G8Q833_PSEFL Unreviewed; 299 AA. AC G8Q833; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AEV65818.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:AEV65818.1}; GN ORFNames=PSF113_5844 {ECO:0000313|EMBL:AEV65818.1}; OS Pseudomonas fluorescens F113. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1114970 {ECO:0000313|EMBL:AEV65818.1, ECO:0000313|Proteomes:UP000005437}; RN [1] {ECO:0000313|EMBL:AEV65818.1, ECO:0000313|Proteomes:UP000005437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F113 {ECO:0000313|EMBL:AEV65818.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; AEV65818.1; -; Genomic_DNA. DR RefSeq; WP_014340927.1; NC_016830.1. DR RefSeq; YP_005211213.1; NC_016830.1. DR EnsemblBacteria; AEV65818; AEV65818; PSF113_5844. DR GeneID; 11833966; -. DR KEGG; pfe:PSF113_5844; -. DR BioCyc; PFLU1114970:GJXA-5884-MONOMER; -. DR Proteomes; UP000005437; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005437}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:AEV65818.1}; KW Transferase {ECO:0000313|EMBL:AEV65818.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 207 207 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 299 AA; 31449 MW; E54B1806B100AEAE CRC64; MGSATTVILD GGMGRELQRR GAPFRQPEWS ALALSEAPQA VEAVHAAYIA SGANVITSNS YAVVPFHIGE ARFAEEGQAL AALAGELAQR AVHASGKAVR VAGSLPPLFG SYRPDLFDAS RASELLAPLV NGLAPHVDLW LAETQSSTVE ARAIHAGLPK DGKPFWLSFT LKDEDTDEVP RLRSGEPVAD AAAVAAELGV EVLLFNCSQP EVIGAAIDAA RDTFARLGVK IHIGAYANAF PPQPKEATAN DGLDPLREDL DPPGYLQWAA DWQKRGASHL GGCCGIGPEH IAVLAQKLV // ID G8QHN5_AZOSU Unreviewed; 1226 AA. AC G8QHN5; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AEV25186.1}; GN OrderedLocusNames=Dsui_0779 {ECO:0000313|EMBL:AEV25186.1}; 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 {ECO:0000313|EMBL:AEV25186.1, ECO:0000313|Proteomes:UP000005633}; RN [1] {ECO:0000313|EMBL:AEV25186.1, ECO:0000313|Proteomes:UP000005633} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-33 / DSM 13638 / PS RC {ECO:0000313|Proteomes:UP000005633}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP003153; AEV25186.1; -; Genomic_DNA. DR RefSeq; WP_014235887.1; NC_016616.1. DR RefSeq; YP_005027027.1; NC_016616.1. DR EnsemblBacteria; AEV25186; AEV25186; Dsui_0779. DR KEGG; dsu:Dsui_0779; -. DR KO; K00548; -. DR BioCyc; AORY640081:GHAS-779-MONOMER; -. DR Proteomes; UP000005633; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000005633}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEV25186.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005633}; KW Transferase {ECO:0000313|EMBL:AEV25186.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 763 763 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1226 AA; 133222 MW; 39B4C41588E872CA CRC64; MQPDRSSELS ALLQQRLLIL DGAMGTMIQR HGLTEKDYRG TRFADHAHDL KGNNDLLLLT RPEVIRGIHA EYLAAGADIL ETNTFNATKV SQADYKLEAI VYELNVAGAR LAREVCDEFT AKNPAKPRFV AGVLGPTSRT ASISPDVNDP GYRNVTFDEL VENYLEAIRG LTDGGADILL VETVFDTLNA KAALFAIETF FDKVGRRWPV MISGTITDAS GRTLSGQTAE AFWNSLNHIR PLSFGLNCAL GAKELRQYVE ELSRVCDCFV SAHPNAGLPN AFGGYDETPE QLAEEIADWA RHGFVNIVGG CCGTSPDHIA AIAKMVAGIA PRAIPAIEPQ LRLSGLEPFN VGPDSLYVNV GERTNVTGSK AFARMILEGR YDDALAVARQ QVENGAQVID INMDEAMLDS VAAMEKFLKL IASEPDISRV PIMLDSSKWE VIETGLKCIQ GKGIVNSISM KEGEAKFLEQ AKLARRYGAA VIVMAFDEKG QADTYARKTE ICKRAYDLLV GIGFPAQDII FDPNIFAIAT GIEEHDNYAV DFINATRWIR ENLPHAQISG GVSNVSFSFR GNDPVREAIH TVFLYHAIQA GMTMGIVNAG MLGVYDDLEP ELRQKVEDVV LNRHPGAGEA LVEFAQTVKE GKAKDTGPDL TWRTLPVEKR LEHALVKGIT EFVVADTEEV RAALAAAGKP PLAVIEGPLM NGMNTVGDLF GAGKMFLPQV VKSARVMKQA VAHLIPYIEE EKARTGASSK GKIVIATVKG DVHDIGKNIV GVVLGCNGYD VVDLGVMVPT EKILHAAKEH GAQAIGLSGL ITPSLEEMSH VASEMQRQGF NVPLLIGGAT TSRAHTAIKI APNYQAPVVY VPDASRAVGV VTSLLSEGQR ESYAAEVAAD YANIRQQHAG KKGSAMVTLA EARANRLPWD ATLVPTVPQK LGLQVLQDID LATLAKYIDW GPFFQTWDLA GRFPAILDDA VVGETARGVY ADAQAMLKQI IEEKWLRAGA VFGLWPANAV GDDIVFYADE QRSAPVLTWH GIRQQHKRPE DKANLCLSDY VAPKESGIAD YAGAFAVTAG LGIEQKLAEF EAAHDDYKSI MLKSLADRLA EACAEWLHQK VRKEDWGYAA DEQLSNEQLI KEEYRGIRPA PGYPACPDHT AKGGLFQLLQ PEANIGMGLT ESYAMTPAAA VSGFFLAHPQ AQYFAIQKIG QDQLEDWASR AGFTLEQAKR WLAPNL // ID G8QYQ3_SPHPG Unreviewed; 1180 AA. AC G8QYQ3; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AEV29680.1}; GN OrderedLocusNames=SpiGrapes_1886 {ECO:0000313|EMBL:AEV29680.1}; OS Sphaerochaeta pleomorpha (strain ATCC BAA-1885 / DSM 22778 / Grapes). OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; OC Sphaerochaeta. OX NCBI_TaxID=158190 {ECO:0000313|EMBL:AEV29680.1, ECO:0000313|Proteomes:UP000005632}; RN [1] {ECO:0000313|EMBL:AEV29680.1, ECO:0000313|Proteomes:UP000005632} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1885 / DSM 22778 / Grapes RC {ECO:0000313|Proteomes:UP000005632}; 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., Munk A.C., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., RA Ritalahtilisa K., Loeffler F., Woyke T.; RT "Complete sequence of Spirochaeta sp. grapes."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP003155; AEV29680.1; -; Genomic_DNA. DR RefSeq; WP_014270523.1; NC_016633.1. DR RefSeq; YP_005062690.1; NC_016633.1. DR EnsemblBacteria; AEV29680; AEV29680; SpiGrapes_1886. DR KEGG; sgp:SpiGrapes_1886; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; SPLE158190:GHFO-1886-MONOMER; -. DR Proteomes; UP000005632; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000005632}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEV29680.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005632}; KW Transferase {ECO:0000313|EMBL:AEV29680.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 240 240 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 755 755 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1180 AA; 128825 MW; ECC30EC647C6F4FD CRC64; MDRQQYLLKL LSERVLVLDG AMGTMIQNQG LRDEDFYLED IKAVGCNELL SLTRGDVIFD IHTQYLQAGS DIITTNTFCA NSFNLEEYGL SSEVETLNRA ACEIAREAAA DFERTQEKYA FIAGTLGPTN RSLAFSSDVD DPSFRKSDFK GFEEMYLQQA GVLLDGGVDL LLIETVFDTL AAKAAIRSCF KAMEEKERKV PVMVSVTFSD LSGRTLSGQT LEAFVSSLAP FPIFSLGLNC STGPEQMVPL IEKLSAISPF FVSAHPNAGF PDKEGHYTLT PRQLADQMAP VLGKGCLNIV GGCCGTTPEH IQALKEATNR AKVHVKNERP PVLVLSGLER LEVRDGSFLV IGERTNVAGS KKFARLIKEE NWEEALSVAR NQIAQGAQVI DICMDASMLD APKAMVAFLR QVASDPSVSK VPVMIDSSDW EVIEIALGEI QGKGIVNSIS LKEGEEKFLS HARLIASYGC AMVVMLFDEK GQADHYERKI AIAKRSYDLL VQAGIKPEDI IFDANVLSIA TGIDEHDLYA KDFIRASLWI KENLPFAHTS GGISNLSFSF RGNDVLRNAM HAMFLAFAKL DMAIINPGAD RNLDSIPPHA RAIIGKALLP EDTKAAQARQ NLIDLALSGE LTKPTQTKEK TKEEAWKSLG PEERLAEAIF HGENTFLQTD LASLDSMDPI QLVEGPLMYG MKKVGKLFGE GKLFLPQVVR SARTMKLAVD ILEPRITAYL TDVNNKIGFQ KKKIAVMATV KGDVHDIGKN IVNLILTCNN FEVIDLGVMV PPQKILASAL EHKADLVGLS GLITPSLKEM ASVVSLFEAN GCTIPLFVGG ATTSELHTAV KLAPLYSSAV IQTKDASSMA LAAQKVVGAQ KGEYLAELSK RYELLRNDTF FARYPRTAVS LPSVGYTQAL SLVQQKALGT PAKNYGIFTI DHFALDELLP LVNWKMYSTS WKVPVGTSES EKLISDALEM LADPQIIRLL ESGCKAVCGL FPATSDRMTV SAGTGKFHFL RNESTGLCLA DYVAKESDTV GLFVVSSSLS IGEYLKELKE KGDDYRALSL QLICDRLVEV LAEKTERFLA DRWGSKNLGF IRPAPGYPAW SDHSEKKGIF DLLGATDAIG VRLTENFAMD PSSSICAMVF GGDDPRYFSV GNVSQEQLDQ YAKAKGLSAP DLATILQGME // ID G8R382_OWEHD Unreviewed; 346 AA. AC G8R382; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Cobalamin-dependent methionine synthase I {ECO:0000313|EMBL:AEV34107.1}; GN OrderedLocusNames=Oweho_3155 {ECO:0000313|EMBL:AEV34107.1}; OS Owenweeksia hongkongensis (strain DSM 17368 / JCM 12287 / NRRL OS B-23963). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Cryomorphaceae; Owenweeksia. OX NCBI_TaxID=926562 {ECO:0000313|EMBL:AEV34107.1, ECO:0000313|Proteomes:UP000005631}; RN [1] {ECO:0000313|EMBL:AEV34107.1, ECO:0000313|Proteomes:UP000005631} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17368 / JCM 12287 / NRRL B-23963 RC {ECO:0000313|Proteomes:UP000005631}; 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; AEV34107.1; -; Genomic_DNA. DR RefSeq; WP_014203454.1; NC_016599.1. DR RefSeq; YP_004990752.1; NC_016599.1. DR EnsemblBacteria; AEV34107; AEV34107; Oweho_3155. DR KEGG; oho:Oweho_3155; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR BioCyc; OHON926562:GHWV-3154-MONOMER; -. DR Proteomes; UP000005631; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005631}; KW Reference proteome {ECO:0000313|Proteomes:UP000005631}. SQ SEQUENCE 346 AA; 37752 MW; 18FDC87325B596F9 CRC64; MTKSLLADEA KKRILVLDGA MGTMIQGYKL TEADYRGERF KDYPSDLKGN NDLLSLTQPD IIKAIHAKYF EAGADLIETN TFNSTRISMA DYDMEDLVPE INLKAAQIAR EVADEFTAKE PHKPRFVIGS MGPTNKTASL SPDVNNPGYR AIDYDTLVRD YKEQALALIE GGVDALMVET VFDTLNAKAA LYGIMELYDE IGKELPIMVS GTITDASGRT LSGQTTEAFL ISIEHAPLLS VGLNCALGAD QLRPYLQILS RESPFMVSAH PNAGLPNAFG EYDETPEKMA AQIKEYLDMG LINIIGGCCG TGPEHISAIA KLAGEYEPRS VKSIQSTVDS PQEIDR // ID G8RLU6_MYCRN Unreviewed; 313 AA. AC G8RLU6; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Homocysteine/selenocysteine methylase (S-methylmethionine-dependent) {ECO:0000313|EMBL:AEV74919.1}; GN OrderedLocusNames=MycrhN_4425 {ECO:0000313|EMBL:AEV74919.1}; OS Mycobacterium rhodesiae (strain NBB3). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=710685 {ECO:0000313|EMBL:AEV74919.1, ECO:0000313|Proteomes:UP000005442}; RN [1] {ECO:0000313|EMBL:AEV74919.1, ECO:0000313|Proteomes:UP000005442} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBB3 {ECO:0000313|EMBL:AEV74919.1, RC ECO:0000313|Proteomes:UP000005442}; 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 ----------------------------------------------------------------------- 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; AEV74919.1; -; Genomic_DNA. DR RefSeq; WP_014212667.1; NC_016604.1. DR RefSeq; YP_005002134.1; NC_016604.1. DR EnsemblBacteria; AEV74919; AEV74919; MycrhN_4425. DR KEGG; mrh:MycrhN_4425; -. DR BioCyc; MRHO710685:GI37-4418-MONOMER; -. DR Proteomes; UP000005442; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005442}; KW Methyltransferase {ECO:0000313|EMBL:AEV74919.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005442}; KW Transferase {ECO:0000313|EMBL:AEV74919.1}. SQ SEQUENCE 313 AA; 33309 MW; B6226D51C1AB3554 CRC64; MTRERLPELT GDDLFVADGG LETELIFHHG IDLPAFAAFP LLDHPSTRDL LRRYYDGYLA VARRHGAGFV VSTPTWRANP DWAAQLGYSP ERLDAVNRAA VQLAEEVRAA AAADGLTAVV SGCMGPRGDG YDPSDAMTVE DAERYHAVQI ATFADTTADQ VAAMTITNAP EAIGIVRAAA AADIPAVISF TVETDGRLPT GQPLHDAIDQ VDAETGGSAA YFMVNCAHPT HFSDALEHDG PWRQRLVGLR ANASSKSHAE LDESTELDEG DPEDLGARHA ALRDRLPNVT VLGGCCGTDA RHVAAICAAW SAQ // ID G8RWV5_MYCRN Unreviewed; 1254 AA. AC G8RWV5; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AEV75603.1}; GN OrderedLocusNames=MycrhN_5125 {ECO:0000313|EMBL:AEV75603.1}; OS Mycobacterium rhodesiae (strain NBB3). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=710685 {ECO:0000313|EMBL:AEV75603.1, ECO:0000313|Proteomes:UP000005442}; RN [1] {ECO:0000313|EMBL:AEV75603.1, ECO:0000313|Proteomes:UP000005442} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBB3 {ECO:0000313|EMBL:AEV75603.1, RC ECO:0000313|Proteomes:UP000005442}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP003169; AEV75603.1; -; Genomic_DNA. DR RefSeq; WP_014213345.1; NC_016604.1. DR RefSeq; YP_005002818.1; NC_016604.1. DR EnsemblBacteria; AEV75603; AEV75603; MycrhN_5125. DR KEGG; mrh:MycrhN_5125; -. DR KO; K00548; -. DR BioCyc; MRHO710685:GI37-5118-MONOMER; -. DR Proteomes; UP000005442; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000005442}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEV75603.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005442}; KW Transferase {ECO:0000313|EMBL:AEV75603.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 263 263 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 326 326 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 327 327 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 783 783 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1254 AA; 137619 MW; AC1DB16CCE93052C CRC64; MTAVESTVSE SNAFAPNIRP DCSDDLTAAL RQRILVIDGA MGTAIQRDRP DEAGYRGERF ADWPSDLVGN NDLLTLTQPH IIEGIHREYL EAGADILETN TFNANAVSLS DYGMAELSYE LNYAGAALAR KACDEFSTPD QPRYVAGALG PTTRTASISP DVNDPGARNV SYDQLVAAYF DSARGLVDGG ADLLIVETIF DTLNAKAAIF AIETLFEERG RRWPVIISGT ITDASGRTLS GQVTEAFWNS IRHAKPIAVG LNCALGAPEM RPYLAEMSRI ADTFVSCYPN AGLPNAFGEY DESPKRQAGY VADFAEAGLV NMVGGCCGTT PAHIAEIAKV VEGMPPREVP EVEVATRLSG LEPLNITEDS LFVNIGERTN ITGSARFRNL IKAEDYDTAL SVALQQVEVG AQVIDINMDE GMIDGVAAMD RFTKLIASEP DISRVPEMID SSKWEVIEAG LKNVQGKPIV NSISMKEGED KFIREARLCR KYGAAVVVMA FDEQGQADNL ERRKEICGRA YRVLTEEVGF PPEDIIFDPN CFALATGIEE HATYGIDFIE ACAWIKENLP GVHISGGISN VSFSFRGNNP VREAIHAVFL FHAIKAGLDM GIVNAGALVP YDSIDPELRD RIEDVVLNRR EDAAERLLEI AERFNRKENS EDPQAAEWRS LPVRERITHA LVKGIDAHVD DDTEELRAEI AGAGGRPIEV IEGPLMDGMN VVGDLFGSGK MFLPQVVKSA RVMKKAVAYL LPFIEKEKEE NGTADSKDTN GTIVMATVKG DVHDIGKNIV GVVLQCNNFE VIDLGVMVPA QKILDAAKEH DADIIGLSGL ITPSLDEMAN FAVEMERAGL EIPLLIGGAT TSRAHTAVKI SPRRSGPVVW VKDASRSVPV AAALLDDKQR PALLEATEKD YASLRERHAQ KNERPMLTLE KARANRTPIE WDGYAPPVPA HGLGVREFLD YDMSELREFI DWQPFFNAWE MKGRFPDILN NPASGEAARK LYDDAQQMLD TAIKEKWLTA NGVIGFFPAN VVGDDIEVYT DDSRSEVLTT LHNLRQQGEH RDGIPNRSLG DFVAPKDTGL ADYVGAFAVT TGLGSQEKIT EFKAALDDYS AILLESLADR LAEAFAERMH QRVRKEFWGY QPEEQLDNDA LIGEKYVGIR PAPGYPACPE HTEKATLWKL LDVKERTGIE LTESMAMWPG AAVSGWYFSH PQSQYFVVGR LAQDQVADYA KRKGWTLAEA ERWLAPNLGY NPED // ID G8SEG0_ACTS5 Unreviewed; 1199 AA. AC G8SEG0; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 29-APR-2015, entry version 24. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|EMBL:AEV82844.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEV82844.1}; GN Name=metH {ECO:0000313|EMBL:AEV82844.1}; GN OrderedLocusNames=ACPL_1947 {ECO:0000313|EMBL:AEV82844.1}; OS Actinoplanes sp. (strain ATCC 31044 / CBS 674.73 / SE50/110). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micromonosporineae; Micromonosporaceae; Actinoplanes. OX NCBI_TaxID=134676 {ECO:0000313|EMBL:AEV82844.1, ECO:0000313|Proteomes:UP000005440}; RN [1] {ECO:0000313|Proteomes:UP000005440} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 31044 / CBS 674.73 / SE50/110 RC {ECO:0000313|Proteomes:UP000005440}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP003170; AEV82844.1; -; Genomic_DNA. DR RefSeq; WP_014688916.1; NC_017803.1. DR RefSeq; YP_006264912.1; NC_017803.1. DR EnsemblBacteria; AEV82844; AEV82844; ACPL_1947. DR KEGG; ase:ACPL_1947; -. DR KO; K00548; -. DR OMA; QPFFNAW; -. DR BioCyc; ASP134676:GL7H-1869-MONOMER; -. DR Proteomes; UP000005440; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000005440}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEV82844.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005440}; KW Transferase {ECO:0000313|EMBL:AEV82844.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 243 243 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 752 752 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1199 AA; 129424 MW; 7840DEBCC7B30336 CRC64; MTQSVATLRE LLAERVLVLD GAAGTMLQGA RLSPADYRAD LIPADHEQDV TGDPDLLNLT SPDVILDIHR QYLAAGADII TTNTFTATTI AQADYGLEHL VRDMNVRAAR LARQAADEAE AADGRPRFVA GDVGPLNVTL SLSPKVDDPA YRAVTFDQVK TAYAEQIAAL AEGGVDLLMI ETVFDTLNAK AAIAAAREVA PDLPLWVSVT IVDLSGRTLS GQTVEAFWRS IERARPLVVG LNCALGAAEA RPHVAELARL SDTFVAAHPN AGLPNAFGGY DQTPAETGAL IGEFAASGLV NIVGGCCGTT PPHIAEVARA VAGAAPRVVA PPAPTTRFSG LEPFAIGPDT GFVMIGERTN VTGSARFRRL VEADDYQAAV DVALDQVRGG ANLLDVNMDA DLLDSERAMT TFLNLIATEP EVARIPIMID SSKWNVLEAG LKCVQGKAVV NSISLKEGPD LFLRQARRIR DFGAGVVVMA FDEQGQADTT ERKVEICGRA YDLLVEDGFD PTDIIFDPNV LAVATGIAEH NGYAKAFIDA LPLIKQRCPG ARTSGGISNL SFAFRGNDVV REAMHSAFLF HAVRAGLDMG IVNAGQLAVY QDIPADLLEL VEDVLFDRRP DATDRLVTFA STVTGSGAKR EVDLSWRDAP VEQRLSHALV HGIVDFIEAD TEEARLKLPR PLDVIEGPLM DGMGVVGDLF GAGKMFLPQV VKSARVMKRS VAYLLPYMEK DKTESSRGQG RVVLATVKGD VHDIGKNIVG VVLGCNNYEV IDLGVMVPAA KILETAIAEG ADAIGLSGLI TPSLDEMVAV GAEMQRRGMT LPLLIGGATT SKQHTAVRIA PAYDGATVHV LDASRVVGVV SDLLDPERSA KLDEANRAEQ ERLREQHEKR HAQPLLTLAQ ARANRERVDF TGLPTPTFTG VREVQPTIAE LREMIDWQFL FLAWELKGKY PAILNEPVAR ELFDDATAML DQIIADGSFQ ARGLYGFWPA HAEGDDILLD NGHGFPMLRQ QTEKPAGRAN RCLADYIAPA GDHLGGFAVA IHGAEKLAAR YEAEHDDYRA IMVKALADRL AEAFAEYLHL KARREWFEPD AQPKLEDLHA ERFRGIRPAL GYPACPDHSE KKDLFQLLDT GRIGVALTES YAMTPAAAVS GLIFAHPDAK YFTVGRLGKD QIEDYAARRG VPVGEVERWL RPNLAYPID // ID G8T7I9_NIAKG Unreviewed; 346 AA. AC G8T7I9; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEW02244.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEW02244.1}; GN OrderedLocusNames=Niako_6018 {ECO:0000313|EMBL:AEW02244.1}; OS Niastella koreensis (strain DSM 17620 / KACC 11465 / GR20-10). OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Chitinophagaceae; Niastella. OX NCBI_TaxID=700598 {ECO:0000313|EMBL:AEW02244.1, ECO:0000313|Proteomes:UP000005438}; RN [1] {ECO:0000313|EMBL:AEW02244.1, ECO:0000313|Proteomes:UP000005438} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17620 / KACC 11465 / GR20-10 RC {ECO:0000313|Proteomes:UP000005438}; 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; AEW02244.1; -; Genomic_DNA. DR RefSeq; WP_014222154.1; NC_016609.1. DR RefSeq; YP_005011647.1; NC_016609.1. DR EnsemblBacteria; AEW02244; AEW02244; Niako_6018. DR KEGG; nko:Niako_6018; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR BioCyc; NKOR700598:GHC3-6082-MONOMER; -. DR Proteomes; UP000005438; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005438}; KW Methyltransferase {ECO:0000313|EMBL:AEW02244.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005438}; KW Transferase {ECO:0000313|EMBL:AEW02244.1}. SQ SEQUENCE 346 AA; 37697 MW; 1B11FB2507D1EF31 CRC64; MKTIQQSLKE RILIIDGAMG TMIQRHKLEE ADYRGERFKD WASDLKGNND LLVLTQPDII KGIHKLYLAA GADIIETNTF NAQVISLADY HMESLAYELN VAAAKIAKEA VEEFFSSPTG GGREGASGRD RAYVAGAIGP LNKTLSLSPD VNNPGYRALT FDEAVSAYYE QVKGLVDGGV DLLLIETIFD TLNAKAAIYA IKKYFADVNK PEVPIMISGT ITDASGRTLS GQTLEAFYTS VMHAKPLSIG LNCALGASEM RPHIEELSQI ASCFTSAYPN AGLPNAMGEY DEQPEQTAHF LEEWAREGFV NIVGGCCGTT PDHIKHIADH VRNFKPRPLP VLETAL // ID G8TSS6_SULAD Unreviewed; 623 AA. AC G8TSS6; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 23. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=Sulac_0951 {ECO:0000313|EMBL:AEW04453.1}; 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 {ECO:0000313|EMBL:AEW04453.1, ECO:0000313|Proteomes:UP000005439}; RN [1] {ECO:0000313|Proteomes:UP000005439} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700253 / DSM 10332 / NAL RC {ECO:0000313|Proteomes:UP000005439}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; AEW04453.1; -; Genomic_DNA. DR RefSeq; WP_013987811.1; NC_016884.1. DR RefSeq; YP_005256125.1; NC_016884.1. DR EnsemblBacteria; AEW04453; AEW04453; Sulac_0951. DR KEGG; sap:Sulac_0951; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR BioCyc; SACI679936:GHYT-976-MONOMER; -. DR Proteomes; UP000005439; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005439}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:AEW04453.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862, KW ECO:0000313|EMBL:AEW04453.1}; KW Transferase {ECO:0000313|EMBL:AEW04453.1}. SQ SEQUENCE 623 AA; 66617 MW; FD75FDFDF7DC4761 CRC64; MKPLAEALSH GLWLADGAIG TWFLSQGVEP HQLPLLPLDH PDLVIRCHLE YLQAGAQIIE THSFSANRSK LAAMGWDGSV GELNRRAAQL ARHARDIFGE PAYVLGSLGP LAVPVDSPIV PGLDRAEAET VYREAVAGLL AGGVDGFLVE TMSDLATVEA AVSAIRAESD LPIVVSFAFS PLGTTLYGIT PEAAVEAVMT LPGGPPAAIG ANCGSGPSPL LDAVIRMAEK ARTYQLPVVA YPNAGEPALR DGHVHYPASP DYMATIAPAL KAAGCAVIGG CCGTTPSHIR AIRQNMQGDL HPQLTARPGW SLTEDVVPKS PDPEWSRPPR LVHELLAQQF VLSVELDPPR GPNLTRLVDA ARQLEEEQVD VINVADSPMA RVRLGALATA RLIQERTRLA TILHFTTRDR NLMGLQSDLL GAFALGLTNI LCLTGDPPGL GDYAHATAVY DLDSIGLTKV LAGFNQGLDA LGQPLGSPTV FSIGVGVNPT ADPLEKEIER FRQKVAAGAH YAMSQPIYAP EQFYRFLDAL GGPLPIPLIL GIMPLVSYRQ ALYLHNEVPG ITIPPEVLSR FESVQDGVHV GIELALELIQ ALRAGIHGIY LVPSFNRVEP LVPLIREIRR LTR // ID G8UNZ5_TANFA Unreviewed; 1229 AA. AC G8UNZ5; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AEW21186.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEW21186.1}; GN Name=metH {ECO:0000313|EMBL:AEW21186.1}; GN OrderedLocusNames=BFO_0838 {ECO:0000313|EMBL:AEW21186.1}; OS Tannerella forsythia (strain ATCC 43037 / JCM 10827 / FDC 338) OS (Bacteroides forsythus). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Tannerella. OX NCBI_TaxID=203275 {ECO:0000313|EMBL:AEW21186.1, ECO:0000313|Proteomes:UP000005436}; RN [1] {ECO:0000313|Proteomes:UP000005436} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43037 / JCM 10827 / FDC 338 RC {ECO:0000313|Proteomes:UP000005436}; RA Dewhirst F., Tanner A., Izard J., Brinkac L., Durkin A.S., RA Hostetler J., Shetty J., Torralba M., Gill S., Nelson K.; RT "Complete sequence of Tannerella forsythia ATCC 43037."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP003191; AEW21186.1; -; Genomic_DNA. DR RefSeq; WP_014224271.1; NC_016610.1. DR RefSeq; YP_005013766.1; NC_016610.1. DR EnsemblBacteria; AEW21186; AEW21186; BFO_0838. DR KEGG; tfo:BFO_0838; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; TFOR203275:GHRQ-837-MONOMER; -. DR Proteomes; UP000005436; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000005436}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEW21186.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005436}; KW Transferase {ECO:0000313|EMBL:AEW21186.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1229 AA; 136572 MW; CD261D34ADFAEADB CRC64; MTKKTIQQLL DERILILDGG MGTMIQGFKL TEADYRGEQF ANFTGALKGN NDLLNITRPE VIRSIHRQYL DAGVDIFTTN TFNANAISMD DYGMASLVRE MNLAAGRLTR QLADDYMNEH PERSIFVAGS LGPTNKTASM SPDVSDPAFR AVSYMDLFRA YHEQVEALID GGVDLILFET TFDTLNVKAG LEAALDVMRT PNRERPIMLS LTLSGQGGRT FSGQTLAAFL ASVQHIPLMS IGLNCSFGAA DMKPYLKELG DIAPYFISAY PNAGLPNQFG RYDETPEKMA AQIKDFIDEG LVNIVGGCCG TTPEHIAQYS ELILHARPHM PVPPPDALWL SGLELLEVKP ENNFLNIGER CNVAGSRKFL RLIKEKNYEE ALTIARKQVE DGAQVLDINM DDGLLDAVEE MKTFLNLIAS EPDISRVPVM IDSSKWQVIE EGLMCVQGKS IVNSISLKEG EEEFLIRAAR IRQLGAATVV MAFDEQGQAD VFERKIEVCE RAYRLLTEKI GFPPQDIIFD PNVLAIATGM PEHNGYGLDF IRSVEWIKKH LPGAKVSGGV SNLSFSFRGN NYVREAMHSV FLYHAIREGM DMGIVNPSAS VTYEDIEPSF RNLLEDVILA RRPEAAEELI AYAQSHIEQA SGEQEKTHDA WRDRSLDERL EYALLKGIGD FLETDLKEAL QRYGQAVAII DGPLMNGMNR VGKLFGAGKM FLPQVVKTAR TMKKAVAILQ PAIEAQKTSS GAAKAGKVVF ATVKGDVHDI GKNIVSIVLT CNNYEVIDLG VMVPAEKIIE TVRNEKPDLL CLSGLITPSL EEMVHVTDEM QKAGFSTPIM IGGATTSKLH TALKIAPHYD HPVIHVVDAS QNPLIAAKLL NPATHDAYVS ELTDEYERLR QAKSNEEVKP LLPYAEAQKL KLQTDWANYT PAEPKKKGLQ LLAIPVAEIV PYINWVFLFT AWRITGRYDD LMQLHDCPAC RAAWLEKRPE AERAKAKEAL KLYNDAQALL KRLIAGNACC KALYEIFPSA SEGDNIRIAD TVIPVLRQQL PNDKGQCLSL ADYVMPASEG RNDYVGVFAV TAGDCMEELR ARYEQEEDSY HLMLLQTLSD RLAEASAEYL HTKVRREYWG YVPDEELSVD EMFRAHYRGI RPAVGYPSLP DQGLIFSLDR LIGVDRIGIA ITENGALSPT SSVAGFYFAH PESRYFMIGR IGEDQLTDYT ARRGETVEHI RKFLGKVTE // ID G8X6P8_FLACA Unreviewed; 329 AA. AC G8X6P8; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AEW85633.1}; GN OrderedLocusNames=FCOL_03965 {ECO:0000313|EMBL:AEW85633.1}; OS Flavobacterium columnare (strain ATCC 49512 / CIP 103533 / TG 44/87). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=1041826 {ECO:0000313|EMBL:AEW85633.1, ECO:0000313|Proteomes:UP000005638}; RN [1] {ECO:0000313|Proteomes:UP000005638} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49512 / CIP 103533 / TG 44/87 RC {ECO:0000313|Proteomes:UP000005638}; 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; AEW85633.1; -; Genomic_DNA. DR RefSeq; WP_014164914.1; NC_016510.2. DR RefSeq; YP_004941426.1; NC_016510.2. DR EnsemblBacteria; AEW85633; AEW85633; FCOL_03965. DR KEGG; fco:FCOL_03965; -. DR KO; K00548; -. DR BioCyc; FCOL1041826:GHZN-809-MONOMER; -. DR Proteomes; UP000005638; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005638}; KW Methyltransferase {ECO:0000313|EMBL:AEW85633.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005638}; KW Transferase {ECO:0000313|EMBL:AEW85633.1}. SQ SEQUENCE 329 AA; 36378 MW; 3E44327C44920AB9 CRC64; MSKIHSEIKN RILVLDGAMG TMLQRYKFEE EDFRGDRFKD FPHPLKGNND LLSLTQPEAV KEVHRLYFQA GADIVETNTF SGTTIGMADY HMEDLVYELN YQSAKIACEV ADEFTDKPRF VAGSIGPTNR TASMSPDVND PGYRAVTFDD LRIAYKQQVE ALLDGGCDLL LVETIFDTLN AKAALFAIEE VKEERNIEVP IMVSGTITDA SGRTLSGQTV EAFLISISHI PLLSVGFNCA LGADLLKPYL KTLAHNTSFN VSAHPNAGLP NAFGEYDESP EQTQAFIKEY LEENLVNIIG GCCGTTPEHI KLMAEIAKNY KPRTPQVVD // ID G8YCN2_PICSO Unreviewed; 334 AA. AC G8YCN2; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 07-JAN-2015, entry version 21. DE SubName: Full=Piso0_002454 protein {ECO:0000313|EMBL:CCE82713.1}; GN Name=Piso0_002454 {ECO:0000313|EMBL:CCE82713.1}; GN ORFNames=GNLVRS01_PISO0J12351g {ECO:0000313|EMBL:CCE82713.1}; 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 {ECO:0000313|EMBL:CCE82713.1, ECO:0000313|Proteomes:UP000005222}; RN [1] {ECO:0000313|Proteomes:UP000005222} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC 10061 / NRRL RC Y-12695 {ECO:0000313|Proteomes:UP000005222}; RX DOI=10.1534/g3.111.001032; 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., RA Schacherer J., Seret M.-L., Talla E., Samson G., Jubin C., Poulain J., RA Vacherie B., Barbe V., Pelletier E., Sherman D.J., Westhof E., RA Weissenbach J., Baret P.V., Wincker P., Gaillardin C., Dujon B., RA Souciet J.-L.; RT "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps RT of genome resolution following polyploidization."; RL G3 (Bethesda) 2:299-311(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; FO082050; CCE82713.1; -; Genomic_DNA. DR RefSeq; XP_004199050.1; XM_004199002.1. DR GeneID; 14522159; -. DR InParanoid; G8YCN2; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000005222; Chromosome J. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005222}; KW Reference proteome {ECO:0000313|Proteomes:UP000005222}. SQ SEQUENCE 334 AA; 38135 MW; 7F14585521F88C07 CRC64; MKQMLGEILG DKHLVLDGAL GTELESIIPS TSKSQPRDDP LWSTRVLINE PKLVEEVHYR YLMSGSNIIT TCTYQASLCG LLKYGDHFSK EDALGLWQKS VDVGKSAARR YYKECSRAQR VLIAGSIGPY GAYLADGSEY SGNYGDFSNK QLEQFHFDLM KFLILNKDVD LIGVETLPSL REFKVLFKLF LKLSNKYNSN KKIYFSFDFK NEHVLCDGSS MENVFFFINK HLAKSQSLAN NILAIGCNCI DYKLVTSILE QFKYLNTFEV PTIVYPNFGF TYNKGTDRYK AHKDLDKWKR LANEWLDYNV KLIGGCCSTG PQEIKIISDL LKER // ID G8YF33_PICSO Unreviewed; 334 AA. AC G8YF33; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 07-JAN-2015, entry version 17. DE SubName: Full=Piso0_002454 protein {ECO:0000313|EMBL:CCE81782.1}; GN Name=Piso0_002454 {ECO:0000313|EMBL:CCE81782.1}; GN ORFNames=GNLVRS01_PISO0I10524g {ECO:0000313|EMBL:CCE81782.1}; 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 {ECO:0000313|EMBL:CCE81782.1, ECO:0000313|Proteomes:UP000005222}; RN [1] {ECO:0000313|Proteomes:UP000005222} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC 10061 / NRRL RC Y-12695 {ECO:0000313|Proteomes:UP000005222}; RX DOI=10.1534/g3.111.001032; 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., RA Schacherer J., Seret M.-L., Talla E., Samson G., Jubin C., Poulain J., RA Vacherie B., Barbe V., Pelletier E., Sherman D.J., Westhof E., RA Weissenbach J., Baret P.V., Wincker P., Gaillardin C., Dujon B., RA Souciet J.-L.; RT "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps RT of genome resolution following polyploidization."; RL G3 (Bethesda) 2:299-311(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; FO082051; CCE81782.1; -; Genomic_DNA. DR RefSeq; XP_004199901.1; XM_004199853.1. DR GeneID; 14523055; -. DR Proteomes; UP000005222; Chromosome I. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005222}; KW Reference proteome {ECO:0000313|Proteomes:UP000005222}. SQ SEQUENCE 334 AA; 37992 MW; F6E547BE134B48EB CRC64; MKEVLSEIPG NQQLVLDGAL GTELESIIPP TSKSQPKNDP LWSTRVLIND PKLVEEVHYR YLMSGSNIIT TCTYQASLNG LLKYGDQFSK EDALGLWQKS VDVAKSAARR YYKEHSQTQK VLIAGSIGPY GAYLADGSEY TGNYGDFSNE HLEKFHFDLM KFLILNKDVD LIGVETVPSL REFKVLFKLF LKLSEKYNST KKIYFSFNFK NEHELCDGSS MEKVFFFLNK HLAKTPVLAK SVLAIGCNCV DYKLVTSILD QFKYLNTFEI PAIVYPNFGF AYNKDTGNYE AHKDLDNWKR LANEWLDYNV KIIGGCCSTG PQEIKIISDL LKQR // ID G8ZUH3_TORDC Unreviewed; 328 AA. AC G8ZUH3; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 29-APR-2015, entry version 18. DE SubName: Full=TDEL0E00240 protein {ECO:0000313|EMBL:CCE92267.1}; GN Name=TDEL0E00240 {ECO:0000313|EMBL:CCE92267.1}; GN ORFNames=TDEL_0E00240 {ECO:0000313|EMBL:CCE92267.1}; 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 {ECO:0000313|Proteomes:UP000005627}; RN [1] {ECO:0000313|EMBL:CCE92267.1, ECO:0000313|Proteomes:UP000005627} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10662 / CBS 1146 / NBRC 0425 / NCYC 2629 / NRRL Y-866 RC {ECO:0000313|Proteomes:UP000005627}; 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; CCE92267.1; -; Genomic_DNA. DR RefSeq; XP_003681478.1; XM_003681430.1. DR GeneID; 11503660; -. DR KEGG; tdl:TDEL_0E00240; -. DR InParanoid; G8ZUH3; -. DR KO; K00547; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000005627; Chromosome 5. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005627}; KW Reference proteome {ECO:0000313|Proteomes:UP000005627}. SQ SEQUENCE 328 AA; 37014 MW; 9387E223A213B672 CRC64; MGRVPLRKVL TDSRKILVLD GGQGTEMENR GIEVANPVWS SIPFVSESFW TDEWSKERKI VEEIYKDFMS SGSDMLMTVT YQASFKAIAE NTELQTLSEY NSLLDRIVAF SRRCIGDERY LVGSVGPWAA YNASEYTGDY GLHADSIDYY GYYKPQLDNF NKQEEIDMIG IETVPNFHEL KAILSWDEKK IAKPFYVSLT THDSGVLRDG TAMEDIAQYI KCLGNNLNPN FMLLGINCVS FNDSRDILEL LHNALPEMLL LAYPNSGEVY EPKKKIWLAN KCKTTSWDSV VKSFINSGAR IIGGCCRTSP QDIADVSIAV KKYSMTAE // ID G8ZW18_TORDC Unreviewed; 328 AA. AC G8ZW18; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 29-APR-2015, entry version 18. DE SubName: Full=TDEL0E05690 protein {ECO:0000313|EMBL:CCE92812.1}; GN Name=TDEL0E05690 {ECO:0000313|EMBL:CCE92812.1}; GN ORFNames=TDEL_0E05690 {ECO:0000313|EMBL:CCE92812.1}; 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 {ECO:0000313|Proteomes:UP000005627}; RN [1] {ECO:0000313|EMBL:CCE92812.1, ECO:0000313|Proteomes:UP000005627} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10662 / CBS 1146 / NBRC 0425 / NCYC 2629 / NRRL Y-866 RC {ECO:0000313|Proteomes:UP000005627}; 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; CCE92812.1; -; Genomic_DNA. DR RefSeq; XP_003682023.1; XM_003681975.1. DR GeneID; 11501011; -. DR KEGG; tdl:TDEL_0E05690; -. DR InParanoid; G8ZW18; -. DR KO; K00547; -. DR OrthoDB; EOG7X9GHR; -. DR Proteomes; UP000005627; Chromosome 5. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005627}; KW Reference proteome {ECO:0000313|Proteomes:UP000005627}. SQ SEQUENCE 328 AA; 37003 MW; 43BC323710634D02 CRC64; MVRIPIKKLV IESKEILVLD GGQGTELENR GIEVANPVWS TIPFLSESFW TDSSSKERKI VESVFDDFKK SGSNILMTIT YQTSFTSIVE NTQFKTLAEY NTLLDRIVKF SRSCIGDERY LIGSVGPWGA HVCCEFTGNY GLHPESIDYY EYFKPQLDNF NGQDEIDLIG FETVPNFHEL KAILSWDETK IAKPFYIGLS VHNNGVLRDG TTMEEIGEYI KGLGEKISSN FLLLGVNCVS FNDSSDMVKS IHKALPDMPL LAYPNSGEVY DTEKKIWFDN KDKLDSWDSV VRSYIDNGAR IIGGCCRTSP RDIAEVSAAV KKYNKVQE // ID G9A1J2_RHIFH Unreviewed; 1256 AA. AC G9A1J2; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=5-methyltetrahydrofolate-homocysteinemethyltransf erase {ECO:0000313|EMBL:CCE97572.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CCE97572.1}; GN Name=metH {ECO:0000313|EMBL:CCE97572.1}; GN OrderedLocusNames=SFHH103_03080 {ECO:0000313|EMBL:CCE97572.1}; OS Rhizobium fredii (strain HH103) (Sinorhizobium fredii). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=1117943 {ECO:0000313|EMBL:CCE97572.1, ECO:0000313|Proteomes:UP000007735}; RN [1] {ECO:0000313|EMBL:CCE97572.1, ECO:0000313|Proteomes:UP000007735} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HH103 {ECO:0000313|EMBL:CCE97572.1, RC ECO:0000313|Proteomes:UP000007735}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; HE616890; CCE97572.1; -; Genomic_DNA. DR RefSeq; WP_014329977.1; NC_016812.1. DR RefSeq; YP_005190397.1; NC_016812.1. DR EnsemblBacteria; CCE97572; CCE97572; SFHH103_03080. DR KEGG; sfh:SFHH103_03080; -. DR KO; K00548; -. DR BioCyc; SFRE1117943:GJT5-3125-MONOMER; -. DR Proteomes; UP000007735; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007735}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CCE97572.1}; KW Transferase {ECO:0000313|EMBL:CCE97572.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 261 261 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 325 325 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 778 778 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1256 AA; 137721 MW; 183D0B574FA3EBAA CRC64; MSAASLFGDL SPRPDGSEIF RALRQAASER ILIMDGAMGT EIQQLGFVED HFRGERFGGC ACHQQGNNDL LTLTQPKAIE EIHYRYALAG ADILETNTFS STRIAQADYG MEDTVYDLNR DGARLARRAA KRAEAEDGRR RFVAGALGPT NRTASISPDV NNPGYRAVSF DDLRLAYAEQ LRGLIDGGAD IILIETIFDT LNAKAAIFAT QEVFAEKKIH LPVMISGTIT DLSGRTLSGQ TPTAFWYSVR HAAPFTIGLN CALGANAMRA HIDELSTVAD TLVCAYPNAG LPNEFGRYDE SPEAMAAQIE AFARDGLVNI VGGCCGSTPA HIRAIAEAVG KYPPRQIPEI ERRMRLSGLE PFTLTDEIPF VNVGERTNVT GSAKFRKLIT TGDYAAALDV ARDQVANGAQ IIDINMDEGL IDSTGAMVEF LNLVASEPDI ACVPVMIDSS KWEVIEAGLK CVQGKALVNS ISLKEGEEAF LHHARLVRAY GAAVVVMAFD EKGQADSKTR KVEICRRAYR LLTEEVGFPP EDIIFDPNIF AVATGIEEHN NYGVDFIEAT HEIIATLPHV HVSGGVSNLS FSFRGNEPVR EAMHAVFLYH AIQAGMDMGI VNAGQLAVYD AIDTELREAC EDVVLNRSPD ATERLLEIAE RYRGQGGSQG KEKDLAWREW PVAKRLEHAL VNGITEFIEA DTEEARLAAE RPLHVIEGPL MAGMNVVGDL FGAGKMFLPQ VVKSARVMKQ AVAVLLPHME AERLANGGAG TRESAGKILM ATVKGDVHDI GKNIVGVVLA CNNYEIIDLG VMVPSAKILE MARQEKVDAI GLSGLITPSL DEMVHVASEL EREGFDIPLL IGGATTSRVH TAVKINPRYS LGQTVYVTDA SRAVGVVSSL LSPEARDGYK EMIRAEYLKV ADAHARNEAE KRRLPLSQAR ANAPKLDWDA HQPKAPSFLG TRVFESWDLA ELARYIDWTP FFQTWELKGV YPRILDDEHQ GPAARQLFAD AQAMLDKIIA EKWFAPTAVV GFWPAGSVAD DIRLFTDEAR ERELATLFTL RQQLAKRDGR PNVALADFVA PIDSGRPDYL GGFVVTAGIE EVAIAERFER ANDDYSSILV KALADRFAEA FAERMHEYVR KELWGYAADE SFTPQELIAE PYAGIRPAPG YPAQPDHTEK ETLFRLLDAE AAIGVSLTES YAMWPGSSVS GLYIGHPDAY YFGVAKIERD QVEDYATRKR MNVREVERWL SPILNYVPMP ETEAAE // ID G9A2Q4_RHIFH Unreviewed; 322 AA. AC G9A2Q4; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 29-APR-2015, entry version 17. DE SubName: Full=Homocysteine S-methyltransferase 2 S-methylmethionine:homocysteine methyltransferase 2 SMM:Hcy S-methyltransferase 2 AtHMT-2 {ECO:0000313|EMBL:CCE95178.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:CCE95178.1}; GN OrderedLocusNames=SFHH103_00679 {ECO:0000313|EMBL:CCE95178.1}; OS Rhizobium fredii (strain HH103) (Sinorhizobium fredii). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=1117943 {ECO:0000313|EMBL:CCE95178.1, ECO:0000313|Proteomes:UP000007735}; RN [1] {ECO:0000313|EMBL:CCE95178.1, ECO:0000313|Proteomes:UP000007735} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HH103 {ECO:0000313|EMBL:CCE95178.1, RC ECO:0000313|Proteomes:UP000007735}; 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; CCE95178.1; -; Genomic_DNA. DR RefSeq; WP_014327690.1; NC_016812.1. DR RefSeq; YP_005188003.1; NC_016812.1. DR EnsemblBacteria; CCE95178; CCE95178; SFHH103_00679. DR KEGG; sfh:SFHH103_00679; -. DR BioCyc; SFRE1117943:GJT5-686-MONOMER; -. DR Proteomes; UP000007735; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007735}; KW Methyltransferase {ECO:0000313|EMBL:CCE95178.1}; KW Transferase {ECO:0000313|EMBL:CCE95178.1}. SQ SEQUENCE 322 AA; 35462 MW; EE51439EC364AE22 CRC64; MEHEFAKYRH DLPLLQGGTF LSDGGMETAL IFHEGVELPH FASFVLLSSM EGRRQLLHYY TSYLEIARCR DTGFVLDTAT WRANADWGEK LGYDAEDLDQ VNRDAVYLLT ELRAQYERPQ VPIVFNGVIG PRGDGYKAGM MNAAEAEDYH AAQVAAFAGS EADMVTAVTM TNVDEAIGVA RAARKHGMPC AISFTVETDG RLVTGRSLQE AVETVDAETE GYPHYYMVNC AHPSHFESSL DQDQAWVRRI GGIRANASTK SHAELDESET LDIGDISDLA RRYRSLTGRL PHLRVLGGCC GTDHRHIAAI CEACLPQAAM SA // ID G9A7M8_RHIFH Unreviewed; 338 AA. AC G9A7M8; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Methionine synthase I {ECO:0000313|EMBL:CCE96258.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CCE96258.1}; GN OrderedLocusNames=SFHH103_01761 {ECO:0000313|EMBL:CCE96258.1}; OS Rhizobium fredii (strain HH103) (Sinorhizobium fredii). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=1117943 {ECO:0000313|EMBL:CCE96258.1, ECO:0000313|Proteomes:UP000007735}; RN [1] {ECO:0000313|EMBL:CCE96258.1, ECO:0000313|Proteomes:UP000007735} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HH103 {ECO:0000313|EMBL:CCE96258.1, RC ECO:0000313|Proteomes:UP000007735}; 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; CCE96258.1; -; Genomic_DNA. DR RefSeq; WP_014328721.1; NC_016812.1. DR RefSeq; YP_005189083.1; NC_016812.1. DR EnsemblBacteria; CCE96258; CCE96258; SFHH103_01761. DR KEGG; sfh:SFHH103_01761; -. DR KO; K00548; -. DR BioCyc; SFRE1117943:GJT5-1790-MONOMER; -. DR Proteomes; UP000007735; Chromosome. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007735}; KW Methyltransferase {ECO:0000313|EMBL:CCE96258.1}; KW Transferase {ECO:0000313|EMBL:CCE96258.1}. SQ SEQUENCE 338 AA; 35109 MW; 153EBBF022F98F97 CRC64; MSIAANALSD LLAQKGVLLA DGATGTSLFA MGLEAGEAPE LWNETKPENI TKLHQDFVDA GADIILTNSF GGTRHRLKLH QAEDRVHALN KRAAEIARAV ADKAARKVIT AGSVGPTGEL LIPLGALSYD AAVSAFVEQI EGLKAGGAEV AWIETMSSPD EIRAAAEAAT KVGLPYVYTG SFDTAGKTMM GLHPKDLHAV AAEIGEGPVA VGANCGVGAS DILSSLLDMT AANPEGTVVV KGNCGIPEFR GSEIHYSGTP PLMAEYARLA VDAGAKIIGG CCGTTCNHLA AMRLALDNHT KGERPTLEVI IEKIGPLRNK TANEGATAPA RERRSRRA // ID G9AIH7_RHIFH Unreviewed; 302 AA. AC G9AIH7; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Predicted MHT1, Homocysteine/selenocysteine methylase {ECO:0000313|EMBL:CCF00859.1}; DE EC=2.1.1.5 {ECO:0000313|EMBL:CCF00859.1}; GN Name=mHT1 {ECO:0000313|EMBL:CCF00859.1}; GN OrderedLocusNames=SFHH103_06400 {ECO:0000313|EMBL:CCF00859.1}; OS Rhizobium fredii (strain HH103) (Sinorhizobium fredii). OG Plasmid pSfHH103e {ECO:0000313|EMBL:CCF00859.1, OG ECO:0000313|Proteomes:UP000007735}. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=1117943 {ECO:0000313|EMBL:CCF00859.1, ECO:0000313|Proteomes:UP000007735}; RN [1] {ECO:0000313|EMBL:CCF00859.1, ECO:0000313|Proteomes:UP000007735} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HH103 {ECO:0000313|EMBL:CCF00859.1, RC ECO:0000313|Proteomes:UP000007735}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; CCF00859.1; -; Genomic_DNA. DR RefSeq; WP_014332498.1; NC_016815.1. DR RefSeq; YP_005192998.1; NC_016815.1. DR EnsemblBacteria; CCF00859; CCF00859; SFHH103_06400. DR KEGG; sfh:SFHH103_06400; -. DR BioCyc; SFRE1117943:GJT5-5554-MONOMER; -. DR Proteomes; UP000007735; Plasmid pSfHH103e. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007735}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:CCF00859.1}; KW Plasmid {ECO:0000313|EMBL:CCF00859.1}; KW Transferase {ECO:0000313|EMBL:CCF00859.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 209 209 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 302 AA; 32390 MW; 90BF7A4FE3EA2E12 CRC64; MNQLRILDGG MSRELIRLGA ELRQPEWSAL ALMESPEIVG QVHREFIDAG ADVITTNSYA LVPFHIGEAR FRSEGRSLIG LAGKLAREAA DQRVDRKVLV AGSLPPIFGS YEPERFDPLR VQDYLKVLVE GLAPYVDVWL GETLSLIAEG DAVRAAVAAT GKPFWVSFTL ADDAEALEQD EPKLRSGESV AAAAAWAAAA GAEALLFNCS RPEVMARAVA AAAATFRERK ANVGIGVYAN AFEAEETEGA ANETLHHTRT DLTADRYSRF ACDWVEAGAS IVGGCCGIGA RHIHNLGQAL RG // ID G9ECR2_9GAMM Unreviewed; 124 AA. AC G9ECR2; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EHJ94547.1}; GN ORFNames=KUC_1506 {ECO:0000313|EMBL:EHJ94547.1}; OS Halomonas boliviensis LC1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=1072583 {ECO:0000313|EMBL:EHJ94547.1}; RN [1] {ECO:0000313|EMBL:EHJ94547.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=LC1 {ECO:0000313|EMBL:EHJ94547.1}; 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; JH393257; EHJ94547.1; -; Genomic_DNA. DR RefSeq; WP_007112483.1; NZ_JH393257.1. DR EnsemblBacteria; EHJ94547; EHJ94547; KUC_1506. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 124 AA; 12648 MW; 429B06279CB1E667 CRC64; MDDSDGTRLR SGESLANAAR EVAALGAERI MVNCSAPEAV TTAMGELATL SVPFGGYANG FISVAPLQPG STVDKLASRT DLDPAAYAEH AIKWFGQGAT AIGGCCEVGP AHIAALAKRL SERG // ID G9EDM1_9GAMM Unreviewed; 319 AA. AC G9EDM1; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 11. DE SubName: Full=Homocysteine S-methyltransferase ybgG {ECO:0000313|EMBL:EHJ92496.1}; GN ORFNames=KUC_2452 {ECO:0000313|EMBL:EHJ92496.1}; OS Halomonas boliviensis LC1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=1072583 {ECO:0000313|EMBL:EHJ92496.1}; RN [1] {ECO:0000313|EMBL:EHJ92496.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=LC1 {ECO:0000313|EMBL:EHJ92496.1}; 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; JH393258; EHJ92496.1; -; Genomic_DNA. DR RefSeq; WP_007113405.1; NZ_JH393258.1. DR EnsemblBacteria; EHJ92496; EHJ92496; KUC_2452. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHJ92496.1}; KW Transferase {ECO:0000313|EMBL:EHJ92496.1}. SQ SEQUENCE 319 AA; 33832 MW; BDBA450F3EE21C31 CRC64; MTELNPIKAL LAQVPFMVID GALATELEAL GCDLNDALWS ARLLAQAPEK IRQVHQAYFE AGADCAITAS YQATVPGFMQ AGLTAEEARA LIQLSVTLAQ QARDAVWQPG QTDRPKPLIA ASVGPYGAYL ADGSEYRGGY DLDRAGLVAF HRERFELLLA AGADLLAAET LPSLEEALAI TDLLAEHPGA QAWITFSAKD GQHISDGTPI AKCAAALANC PGVAAIGVNC TALAHIESLI KEIRRECDLP IVVYPNSGEV YDPVTKTWHS ATCDHTAADL SGLAQGVEHW LAAGASGFGG CCRTSPEDIQ ALAQWRRSR // ID G9EGS2_9GAMM Unreviewed; 1231 AA. AC G9EGS2; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHJ91766.1}; GN ORFNames=KUC_3323 {ECO:0000313|EMBL:EHJ91766.1}; OS Halomonas boliviensis LC1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=1072583 {ECO:0000313|EMBL:EHJ91766.1}; RN [1] {ECO:0000313|EMBL:EHJ91766.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=LC1 {ECO:0000313|EMBL:EHJ91766.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; JH393259; EHJ91766.1; -; Genomic_DNA. DR RefSeq; WP_007114255.1; NZ_JH393259.1. DR EnsemblBacteria; EHJ91766; EHJ91766; KUC_3323. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1231 AA; 136230 MW; EF874EA064BBC566 CRC64; MADSALIATL TQRLAERILI LDGGMGTMLQ NAQLSEEDFR GERFSDWPSD LKGNNDLLAL TCPDVVTRIH RDYLEAGADI IETNTFNSTQ LSQSDYGMES LVVELNRESA RLAREVCDAV AAETGVPRYV AGVLGPTSRT ASLSPDVNDP AKRNVTFDEL RENYYEAAEA LIAGGADLIM IETIFDTLNA KAAIYALEEL FDDRGERLPV MISGTITDAS GRTLSGQTTE AFWNSVRHAQ PLSVGLNCAL GAEELRPYLE ELATKADTFV SAHPNAGLPN EFGEYDQTPE EMSEIVSEFA ASGLVNIIGG CCGSTPEHIR AIADSVRDMA PRVIPERSRA CRLSGLEPFN IEADSLFVNV GERTNVTGSA RFKRLIVEED FTTALEVALE QVESGAQVID INMDEGMLES KEAMERFLNL IAGEPDIARV PIMIDSSKWE IIEAGLKCVQ GKAVVNSISL KEGEAAFREQ ATKCRRFGAA IVVMAFDEDG QADTFARKTE ICQRAYRLLV DEIGFPAEDI IFDPNIFAIA TGIEEHNNYA VDFIEATQWI RDNLPHAMIS GGVSNVSFSF RGNNPVREAI HSAFLYHAIR AGLTMGIVNA GQLAVYDDLP AELRDAVEDV VLNRRSDGTE RLLDIADKYK GDGSGAAKKE DLEWRSWPVN KRIEHALVKG ITVYIEDDTE QARAEAERPI EVIEGPLMDG MNVVGDLFGD GKMFLPQVVK SARVMKQAVA YLIPYIEAEK SEETKAKGKI VMATVKGDVH DIGKNIVGVV LQCNNYEVID LGVMVPADKI LQAAKEHNAD IIGLSGLITP SLDEMVHVAK EMQRRGMDLP LLIGGATTSK AHTAVKIEPQ YEHPVIYVTD ASRAVGVAGK LLTPALKTPY IAEIREEYEK VRERNAKRRP KAADLDYTQA RKRRFRTDWN AHTPAEPNML GLRTFDDYDL EELIERIDWT PFFMSWQLAG KYPKILDDNV VGEAARNLFE DAKVMLRKLV EEKRVQARGV IGLWPANSVD DDVIEVYADE SRSEVVERLH HIRQQTTKGR DGICYSLADF IAPKESGKAD WIGGFAVTTG HGVDQLSKAY EAAGDDYNAI MVQALTDRLA EAFAERMHER VRKEFWGYVP EETLDNDALI AEKYQGIRPA PGYPACPDHT EKATLFRLLD ATENTGLALT ENFAMWPAAA VSGWYFAHPQ SKYFSTGKIT RDQVEAIAAR KQMPLEEMER WLSPVLSYDP S // ID G9EY58_CLOSG Unreviewed; 792 AA. AC G9EY58; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EHN15968.1}; GN ORFNames=IYC_05934 {ECO:0000313|EMBL:EHN15968.1}; OS Clostridium sporogenes PA 3679. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1075091 {ECO:0000313|EMBL:EHN15968.1, ECO:0000313|Proteomes:UP000005747}; RN [1] {ECO:0000313|Proteomes:UP000005747} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=22374960; DOI=10.1128/JB.06765-11; RA Bradbury M., Greenfield P., Midgley D., Li D., Tran-Dinh N., RA Vriesekoop F., Brown J.L.; RT "Draft Genome Sequence of Clostridium sporogenes PA 3679, the Common RT Nontoxigenic Surrogate for Proteolytic Clostridium botulinum."; RL J. Bacteriol. 194:1631-1632(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; JH470502; EHN15968.1; -; Genomic_DNA. DR RefSeq; WP_003491383.1; NZ_JH470502.1. DR EnsemblBacteria; EHN15968; EHN15968; IYC_05934. DR Proteomes; UP000005747; Unassembled WGS sequence. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005747}; KW Methyltransferase {ECO:0000313|EMBL:EHN15968.1}; KW Transferase {ECO:0000313|EMBL:EHN15968.1}. SQ SEQUENCE 792 AA; 87565 MW; 93073D9FCAFAC61F CRC64; MNIKDYIKEN IIVFDGAMGT MLQKLGLKIS DLPEELNVLE SEKIINIHRK YVDAGAKVIT TNTFGANEIK LKQSEFSVER IIDKAIDNVK KARGNKEIFI ALDIGPIGQL LEPMGTLKFE EAYEIFKGQV IQGEKSGADI ILIETMTDLY EAKAAILAAK ENTNLPVFCT MTFEKNKRTF TGCTPVSMVI TLEGLGVDAL GVNCSLGPNE LEDIVDEIIK YSSVPIMVQP NAGLPTVKDG KTIYNIKPKE FAAFQRSIVE KGVRIVGGCC GTTDEFIREI VYSLKDVQVK KLKEKNICGV CSSTKAVLID GVKIIGERIN PTGKKLFKEA LRNNDIDYIL KEAIGQVESG ADILDVNVGL PEIDEEETMK KVIKEIQSII DAPLQIDSNN PKVIEKALRV YNGKAIVNSV NGEDKVLDNL LPLIKKYGAA VVALTLDDKG IPKKAEERLK IAEKIVNKAL DYGMKREDVF IDCLVLTASA QQEDVRETLK AVTLVKEKLK VKTILGVSNI SFGLPNRELI NKTFLAMSLQ SGLDLPILNP NNKEMINIIN AFKVLNNQDI GAANYIEMYA NETSNSKEVK TQKSNLNLKE IVIKGIKEEA YSKTKELLKD RAELSIINEE LIPALDEVGE KYEKGIIFLP QLIQSAETVK KAFAAIKEKL REDNSPKINK GKILMATVKG DIHDIGKNIV KVILENYGFD IIDLGKDVEV ERIVEEVKKN NIKLVGLSAL MTTTVNSMKD TIKALKDSGI DCKTFVGGAV LNEEYAEMIN ADFYAKDAKE AVDIAKRFFG GF // ID G9KBS8_MUSPF Unreviewed; 84 AA. AC G9KBS8; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|EMBL:AES02353.1}; DE Flags: Fragment; OS Mustela putorius furo (European domestic ferret) (Mustela furo). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; OC Mustelinae; Mustela. OX NCBI_TaxID=9669 {ECO:0000313|EMBL:AES02353.1}; RN [1] {ECO:0000313|EMBL:AES02353.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Lungs {ECO:0000313|EMBL:AES02353.1}; RX PubMed=23236062; DOI=10.1128/JVI.02476-12; RA Leon A.J., Banner D., Xu L., Ran L., Peng Z., Yi K., Chen C., Xu F., RA Huang J., Zhao Z., Lin Z., Huang S.H., Fang Y., Kelvin A.A., RA Ross T.M., Farooqui A., Kelvin D.J.; RT "Sequencing, annotation, and characterization of the influenza ferret RT infectome."; RL J. Virol. 87:1957-1966(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; JP013755; AES02353.1; -; mRNA. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0008705; F:methionine synthase activity; IEA:Ensembl. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Methyltransferase {ECO:0000313|EMBL:AES02353.1}; KW Transferase {ECO:0000313|EMBL:AES02353.1}. FT NON_TER 1 1 {ECO:0000313|EMBL:AES02353.1}. FT NON_TER 84 84 {ECO:0000313|EMBL:AES02353.1}. SQ SEQUENCE 84 AA; 9398 MW; 1C1EDE01695C41BD CRC64; KLSEEDFRGH EFQDHARSLK GNNDILSITQ PNVIYQIHKD YLLAGADIIE TNTFSSTSIA QADYGLEHLA YQMNRCSAGV ARKA // ID G9KBS9_MUSPF Unreviewed; 96 AA. AC G9KBS9; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|EMBL:AES02354.1}; DE Flags: Fragment; OS Mustela putorius furo (European domestic ferret) (Mustela furo). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; OC Mustelinae; Mustela. OX NCBI_TaxID=9669 {ECO:0000313|EMBL:AES02354.1}; RN [1] {ECO:0000313|EMBL:AES02354.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Lungs {ECO:0000313|EMBL:AES02354.1}; RX PubMed=23236062; DOI=10.1128/JVI.02476-12; RA Leon A.J., Banner D., Xu L., Ran L., Peng Z., Yi K., Chen C., Xu F., RA Huang J., Zhao Z., Lin Z., Huang S.H., Fang Y., Kelvin A.A., RA Ross T.M., Farooqui A., Kelvin D.J.; RT "Sequencing, annotation, and characterization of the influenza ferret RT infectome."; RL J. Virol. 87:1957-1966(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; JP013756; AES02354.1; -; mRNA. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0008705; F:methionine synthase activity; IEA:Ensembl. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Methyltransferase {ECO:0000313|EMBL:AES02354.1}; KW Transferase {ECO:0000313|EMBL:AES02354.1}. FT NON_TER 1 1 {ECO:0000313|EMBL:AES02354.1}. FT NON_TER 96 96 {ECO:0000313|EMBL:AES02354.1}. SQ SEQUENCE 96 AA; 10352 MW; AF3FCEC41E4A65DD CRC64; QTLFEEEYPP RPIFISGTII DKSGRTLSGQ TGEAFVISVS HADPLCIGLN CALGAAEMRP FIETIGKCTT AYVLCYPNAG LPNTFGDYDE TPDMMA // ID G9N2U7_HYPVG Unreviewed; 348 AA. AC G9N2U7; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 07-JAN-2015, entry version 17. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHK19006.1}; GN ORFNames=TRIVIDRAFT_44209 {ECO:0000313|EMBL:EHK19006.1}; 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 {ECO:0000313|EMBL:EHK19006.1, ECO:0000313|Proteomes:UP000007115}; RN [1] {ECO:0000313|EMBL:EHK19006.1, ECO:0000313|Proteomes:UP000007115} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Gv29-8 {ECO:0000313|EMBL:EHK19006.1, RC ECO:0000313|Proteomes:UP000007115}; 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. {ECO:0000313|EMBL:EHK19006.1}. 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; ABDF02000085; EHK19006.1; -; Genomic_DNA. DR EnsemblFungi; EHK19006; EHK19006; TRIVIDRAFT_44209. DR InParanoid; G9N2U7; -. DR OMA; SSVEGFM; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000007115; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007115}; KW Reference proteome {ECO:0000313|Proteomes:UP000007115}. SQ SEQUENCE 348 AA; 38276 MW; 91387747396EF97B CRC64; MTNTRSPVPV SFLDGGLGTS LEQNYSIAFG PDTPLWSSHL LISDPSTLLR CQKDFGDVPV DMILTATYQV SLHGFAGTKT AEFSDGIAPE QVPRFLETAV HIAEQAKQPS SAVALSIGPY GACMIPSQEY SGKYDAAYDS GDALFAWHRE RMEVFASIKD VRQRVRYIAL ETVPRLDEVI AMRRAMSAVP GLSSGVPFWI SCLFPNEDEK IPDGSSPEAV IRAMLDPSIA PAVPWGVGIN CTKVWKLESL LRRYEAGVSQ LLQEGLVEKW PALVLYPDGT NGEVYNTTTK TWELPQGTEQ KDRIPWETQL AEVIRAAEAR GKWSHIIVGG CCRARPSDIQ KLRSCLTT // ID G9NT47_HYPAI Unreviewed; 342 AA. AC G9NT47; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 07-JAN-2015, entry version 15. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHK45896.1}; GN ORFNames=TRIATDRAFT_292149 {ECO:0000313|EMBL:EHK45896.1}; 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 {ECO:0000313|EMBL:EHK45896.1, ECO:0000313|Proteomes:UP000005426}; RN [1] {ECO:0000313|EMBL:EHK45896.1, ECO:0000313|Proteomes:UP000005426} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 20476 / IMI 206040 {ECO:0000313|Proteomes:UP000005426}; 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. {ECO:0000313|EMBL:EHK45896.1}. 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; ABDG02000023; EHK45896.1; -; Genomic_DNA. DR OMA; WESAINI; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000005426; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005426}; KW Reference proteome {ECO:0000313|Proteomes:UP000005426}. SQ SEQUENCE 342 AA; 37550 MW; FC7868FE83B05461 CRC64; MPKIKILDGG LGTSLEQNHN IIFSSDTPLW SSHLLISDPS TLLQCQKDFG DVPVDVILTA TYQVSLHGFA NTKTADFPNG IDASQVPQFL ETAVKIAEDA KQPACAIALS VGPYGACMVP SQEYSGRYDA AHDSGDALLA WHRERLEVFG LIKDVKQRVQ YIALETVPRL DEVISMRRAL SAVPGLFPDL PFWISCLFPN EDESIPDGSS PEDVIRAMLD PSLAAAVPWG VGINCTKVWK LDSLLRRYEA AIKSLLQEGV ITDWPALVLY PDGTNGEVYN TTTKQWELPE GAEREDGIPW EKQLTEVVRA TEERGKWSQI IVGGCCMASP SDIKRLHGCI NA // ID G9PMT8_9ACTO Unreviewed; 325 AA. AC G9PMT8; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHM94087.1}; GN ORFNames=HMPREF0975_01709 {ECO:0000313|EMBL:EHM94087.1}; OS Actinomyces sp. oral taxon 849 str. F0330. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Actinomycineae; Actinomycetaceae; Actinomyces. OX NCBI_TaxID=653386 {ECO:0000313|EMBL:EHM94087.1}; RN [1] {ECO:0000313|EMBL:EHM94087.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0330 {ECO:0000313|EMBL:EHM94087.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHM94087.1}. 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; ACTB01000095; EHM94087.1; -; Genomic_DNA. DR RefSeq; WP_009233694.1; NZ_JH470352.1. DR EnsemblBacteria; EHM94087; EHM94087; HMPREF0975_01709. DR OrthoDB; EOG6C019S; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 325 AA; 34112 MW; 2F7E4B7748585C10 CRC64; MRTSSASTTS LERNPVRLSD LLSRGPVVLD GAMGTELDSR GVDTHDPLWS ALALTTAPEA VRQVHTDYLK AGARVITTNT YQATLPALLR AGHDAHRARE VIAAGARLAG EAARRFEAEH PEAQLLIAGG LGPYGAYLAD GSEYTGVYDV GALDAPVFRD VHLPRIEMLA GEGIDLFALE TLPRLDEAQA LVGAVEDLAA ESECWVSFQV RPDGAHLADG TPLAEAAAWA ADQETVVAVG VNCVAPDVVA RALPVLREAT TKPLVAYPNS GDLYDPATKT WKAGEEGDGL AALAPSWGAS GVRLIGGCCR TRPAQIRELA HALSA // ID G9PTR9_9BACT Unreviewed; 784 AA. AC G9PTR9; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 01-OCT-2014, entry version 17. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHL69362.1}; GN ORFNames=HMPREF1006_01962 {ECO:0000313|EMBL:EHL69362.1}; OS Synergistes sp. 3_1_syn1. OC Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae; OC Synergistes. OX NCBI_TaxID=457415 {ECO:0000313|EMBL:EHL69362.1}; RN [1] {ECO:0000313|EMBL:EHL69362.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_syn1 {ECO:0000313|EMBL:EHL69362.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHL69362.1}. 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; ACUH01000015; EHL69362.1; -; Genomic_DNA. DR RefSeq; WP_008709571.1; NZ_JH414692.1. DR EnsemblBacteria; EHL69362; EHL69362; HMPREF1006_01962. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; SQ SEQUENCE 784 AA; 83057 MW; B96FFB9EB4CEBEDB CRC64; MIELDKILLF DGAMGTMLQR RGLELGTVPE ALNVTAPEAI ESIHREYLAA GADVILANTF GANRFKAEKA GMELAKMVAA GVKTARKAIG GAPGRYAALD IGPCGRVLQP AGDLPFDEAV EVFAEVIRAG TEAGADFILL ETFTDLYELK AAVIAAKENS PLPVFATMSF EANGTTFFGA SVESMVMTLE ALGVSALGVN CSLGPRQLVP IVRRILAATR LPVLVQPNAG LPVMEDGVTR YDITPEEFAS SIREFVAEGV RFVGGCCGTT PEYIRLTKST IAGMAPAAIE TAPRYGICSP SKVVGFDRVT VIGERLNPTG KKALQAALRA HDMDFVLREA IREEEQGAEV LDVNMGLPDI DEPAMLSEAV REIQAVTDLP LQLDSASPAA LERAARIYNG KPLLNSVNGK KESLDTVLPI AKKYGCAVLG LTLDEKGIPK DAEARLAIAR RIVKAAEAAG LRREDIFIDC LMMTVSAQPD QAHETMKAIS LVKKELGVKT VLGVSNVSFG LPARPIINRT MLAMALASGL DAPIMNPGDA GMTETVAAAR VLLEQDADSK EYVEKYGGAA PAQAAPVKDE APQIGYAISR GLKDEAAKAA AALLAEQPPL AVVEKEIIPA LDTVGKDYES GRIFLPQLIK SAEAAKAAFE VLRAELIKAS GDTQKGKKIV IATVHGDIHD IGKNIVKVIL ENYNFDVTDL GKDVPPRQVI AAVKETGAKL VGLSALMTTT VASMRETIEL LRRECPGVKV IVGGAVLTEG LAAYAGADRY AKDAMETVRH ADSL // ID G9Q1R3_9BACI Unreviewed; 610 AA. AC G9Q1R3; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 20. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HMPREF1014_00605 {ECO:0000313|EMBL:EHL77122.1}; OS Bacillus sp. 7_6_55CFAA_CT2. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=665957 {ECO:0000313|EMBL:EHL77122.1}; RN [1] {ECO:0000313|EMBL:EHL77122.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=7_6_55CFAA_CT2 {ECO:0000313|EMBL:EHL77122.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHL77122.1}. 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; ACWE01000009; EHL77122.1; -; Genomic_DNA. DR RefSeq; WP_000770358.1; NZ_JH414708.1. DR EnsemblBacteria; EHL77122; EHL77122; HMPREF1014_00605. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 610 AA; 67188 MW; 940A599A984B27B3 CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNVSDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTK INRAAVKLAK ASVTDKNAIL GTIGGMKHIG AVTTTDMERE FILLEQAGAL LEEQVDGLLL ETFYDEFELL HAVQVLRKQT NIPIVAQLAL HEAGTTQNGN DVNEILKQLL DYGANVVGLN CQLGPLHMTE AFKMISIPQN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPKFIEQGI RLLGGCCGTT PEHIQSMKRA VANITPVIEK ETIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRVSNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIK LIEEVYEATK HLEQPIFIGI MPLVSKRNAD FLHFEVPGIT LPEEIRERMD GHETKEAAIE EGIRISQELV DAAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID G9Q1R4_9BACI Unreviewed; 1132 AA. AC G9Q1R4; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHL77123.1}; GN ORFNames=HMPREF1014_00606 {ECO:0000313|EMBL:EHL77123.1}; OS Bacillus sp. 7_6_55CFAA_CT2. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=665957 {ECO:0000313|EMBL:EHL77123.1}; RN [1] {ECO:0000313|EMBL:EHL77123.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=7_6_55CFAA_CT2 {ECO:0000313|EMBL:EHL77123.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHL77123.1}. 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; ACWE01000009; EHL77123.1; -; Genomic_DNA. DR RefSeq; WP_000649687.1; NZ_JH414708.1. DR EnsemblBacteria; EHL77123; EHL77123; HMPREF1014_00606. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 125999 MW; 082FD74DF7F25F46 CRC64; MKCIEEKLKN SILILDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYELSHLDE ELNEKAALLA KQAVKESGNE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGE VDVLLVETSQ DMRNVKAAYI GIQAAFEELK KTVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWVN IIGGCCGTTP EHIKEMKSAL ASLKPRDHHE REGHGISGLE ALQYDESMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMENF LAEVTKVLKV PIMIDSTDEN VMEQALTYIQ GKAVINSINL EDGEERFKKV TPLLQKYGAA IVVGTIDEDG MAVSAERKIE IAKRSYELLT KKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIHLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPEE EKRLADALLF ETTKETLEEF TNFYRVAKKK DIVVQETLTL DERLANYIVE GTKQGLHEDL SLALEEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILA NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAANIDVPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV KKEEKKVEIP AVIEPLPKAE VIVPDSTKRI VLRDIPAFHL APFLNRQMLL GHHLGLKGNV KKLLKEGNKR AHELNDLIDE LLQEGQSWLK PKAVYQFFPA QSDGQNIVIY DPKDHTRVIE RFTFPRQGKA PYRTLGDYLR PIGDEMDYVA FLSVTVGEGI RDIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID G9QDI5_9BACI Unreviewed; 325 AA. AC G9QDI5; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHL68244.1}; GN ORFNames=HMPREF1014_04727 {ECO:0000313|EMBL:EHL68244.1}; OS Bacillus sp. 7_6_55CFAA_CT2. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=665957 {ECO:0000313|EMBL:EHL68244.1}; RN [1] {ECO:0000313|EMBL:EHL68244.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=7_6_55CFAA_CT2 {ECO:0000313|EMBL:EHL68244.1}; 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. {ECO:0000313|EMBL:EHL68244.1}. 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; ACWE01000079; EHL68244.1; -; Genomic_DNA. DR RefSeq; WP_000066231.1; NZ_JH414712.1. DR EnsemblBacteria; EHL68244; EHL68244; HMPREF1014_04727. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 325 AA; 36304 MW; 837737A663156D24 CRC64; MSNKINPIDA ILSQHSIMLL DGALATELEG HGCNLDDPLW SARVLLENPE LIYQVHSDYF RSGADCAITA SYQATISGFS ARGIQEQEAL ELIKKTVLLA RRARDDFWKE NIQTNRPKPL VVASVGPYGA YLADGSEYVG NYGVTDKTLA DFHRSRMSAL IEAGADLLAF ETIPSLQEAR VLDTLLREFP ETYAWLSFSL KNEKEISEGM KLVECARVFE KSEQIVAIGI NCAPVTVVTG AIQELRANTK KPIIVYPNSG ETYNPETKTW HGHEKCNALD ILSEEWYQAG ARLIGGCCRT TPYHIEEISN KWRSSEFFYS NEAKQ // ID G9QKJ3_9BACI Unreviewed; 620 AA. AC G9QKJ3; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 20. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HMPREF1015_01682 {ECO:0000313|EMBL:EHL78323.1}; OS Bacillus smithii 7_3_47FAA. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=665952 {ECO:0000313|EMBL:EHL78323.1}; RN [1] {ECO:0000313|EMBL:EHL78323.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=7_3_47FAA {ECO:0000313|EMBL:EHL78323.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHL78323.1}. 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; ACWF01000081; EHL78323.1; -; Genomic_DNA. DR RefSeq; WP_003353848.1; NZ_JH414751.1. DR EnsemblBacteria; EHL78323; EHL78323; HMPREF1015_01682. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 620 AA; 68853 MW; 63F35FAE99C5C366 CRC64; MGFLDRLKTE ILTADGAMGT LLYSYGIDYC YEELNITKPE IISKIHEEYI LAGADVIQTN TYSANAVKLR RYGLEENVKQ INKAAVRLAK KAAADHGTFV FGTIGGIRGF RKDTCSLADI KEAFLEQAES LLNENPDGLL LETYYDFEEL TTVLKIARKL TNIPIIAQVS MHEPGVLQNG LSLNEALHRL EDHGADLVGV NCRLGPYHMI QALEKATLPK KAYLSAYPNA SLLDVKDGRV IYESEAEYFG RAAVKLRNQG VRLIGGCCGT TPKHIEAVKK ALSGLSPIHQ KSVKPEKPII VKEPPAPLDP PLHELAKKKR TIIVELDTPK HLDTFQYFKG TQVLKEVGID ALTMADNSLA SPRISNMAMA ALVKANQHIR PLVHITCRDR NLIGLQSHLM GLHTLGIHDI LVITGDPTKV GDFPGATSVY DVSSLELISL IKQLNNGISF SGKPLKQKTH FSVSAAFNPN VRVLEKAVKR MERKIECGAD SFITQPVFTK EKIKEIYEAT KHLNVPIFIG IMPLTSLKNA EFLHNEVPGI KLSDEIIERM RAFDGDKEKS QQTGIEIAKE LIDTALRYFN GIYLITPFLR YEMTADLARY IREQDAKKGE TVHAEITTSN // ID G9QKJ4_9BACI Unreviewed; 1150 AA. AC G9QKJ4; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHL78324.1}; GN ORFNames=HMPREF1015_01683 {ECO:0000313|EMBL:EHL78324.1}; OS Bacillus smithii 7_3_47FAA. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=665952 {ECO:0000313|EMBL:EHL78324.1}; RN [1] {ECO:0000313|EMBL:EHL78324.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=7_3_47FAA {ECO:0000313|EMBL:EHL78324.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHL78324.1}. 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; ACWF01000081; EHL78324.1; -; Genomic_DNA. DR RefSeq; WP_003353849.1; NZ_JH414751.1. DR EnsemblBacteria; EHL78324; EHL78324; HMPREF1015_01683. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 229 229 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 292 292 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 727 727 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1150 AA; 127725 MW; 8E03486FE8BAFA0F CRC64; MPKLQHPIEH ELEKRILIID GAMGTMIQQA GLTSNDFGGE QYDGCNEFLN ITAPHVVEWI HRSYLEAGAD VIETNSFGGT PLVLNEYNLG DRAYEINRRA AEIAKKAAAE FSTPEKPRFV AGAMGPTTKT LSVTGGIDFE SLSKHFEIQA RGLIDGGCDL LLLETSQDML NVKAGFLGIQ RAFKATGKTL PLMISGTIEP MGTTLAGQNI EAFYLSLEHM NPLSVGLNCA TGPEFMTDHI RSLSGLAQSF VSCYPNAGLP DEEGKYHETP ESLSKKIAGF AEKGWLNLVG GCCGTTPEHI RAISEAVKPY PPRKRPNQPH GHAVSGIEPL IYDDSMRPLF IGERTNVIGS RKFKRLIIEG KYEEASEIAR AQVKGGAHVI DICLANPDRD ELSDMENFIK EVVKKVKVPL VIDSTDEKVI EKALTYSQGK AIINSINLED GEERFEKVVP LIKKYGAAVV VGTIDEKGMA VTRERKLEIA ERSYDLLVHK WGLQPEDLIF DPLVFPVGTG DEQYIGSAQE TIEGIRLIKE KLPRCLTVLG ISNVSFGLPP VGREVLNAVF LYHCTQAGLD YAIVNTEKLE RYASIPEDER HLAEKLLFET NDDTLAAFTA FYRDKKKEHK VQELPKTVEE RLRYYIVEGT KEGLIPDLQK ALEIFETPLD IINGPLMDGM AEVGRLFNDN QLIVAEVLQS AEVMKAAVAF LEPFMEKSDN DSGKGKVLLA TVKGDVHDIG KNLVDIILSN NGFKVIDLGI KVAPSELIQA VQKEQPDIVG LSGLLVKSAQ QMVMTVQDMK QAGINVPVLV GGAALSRRFT ETKISPEYEG PVLYAKDAME GLSLANRLQN EEEKQDLLLE LEAQQVKRAE TERKKTSIQS AAVAVMEKTS KTVRQDVPVF VPRDTKKHLF VDYPIAYLKP YINLQTLIGH HLGLKGKVDK MLAQGDEKAT ALMEMIDDFL FSGILKPKGM YQFFPAQSDG NDVIIYDPAD QKTVIERFSF PRQKKEPYLC LADYLKPKES GLMDYVGLFV VSAGFGVRDK ANEWKAKGKF LASHALQATA LELAEAFAER LHQEMRDFWG FPDPTDFTMR DRFAAKYQGQ RYSFGYPACP NLEDQKKLFR LLQPEEIGIH LTDGYMMEPE ASVSAIVFAH PDARYFNVES // ID G9R148_9FIRM Unreviewed; 784 AA. AC G9R148; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHM91891.1}; GN ORFNames=HMPREF1021_01829 {ECO:0000313|EMBL:EHM91891.1}; OS Coprobacillus sp. 3_3_56FAA. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae; Coprobacillus. OX NCBI_TaxID=665941 {ECO:0000313|EMBL:EHM91891.1, ECO:0000313|Proteomes:UP000004267}; RN [1] {ECO:0000313|EMBL:EHM91891.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_3_56FAA {ECO:0000313|EMBL:EHM91891.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHM91891.1}. 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; ACWL01000042; EHM91891.1; -; Genomic_DNA. DR RefSeq; WP_003536636.1; NZ_JH470425.1. DR ProteinModelPortal; G9R148; -. DR EnsemblBacteria; EHM91891; EHM91891; HMPREF1021_01829. DR Proteomes; UP000004267; Unassembled WGS sequence. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000004267}. SQ SEQUENCE 784 AA; 85452 MW; E5134BF302724244 CRC64; MLQERLKNDI LVFDGAMGTQ LQDAGLKAGD IPECLNITDP KLIQTIHLNY LNAGADFITT NTFGANPLKM AEAPYSYEEI INAAIDNATI ARKTADRQND SYIVLDIGPI GQLLEPMGTL TFDEAYEIIK KQVIIAKDKV DAVLLETMTD IYEVKAGILA VKENSDLPVF VTMTYENNLR TLSGCDPLTM VNVLEGLNVD VLGVNCSLGP IELTPIIDQI LAAATIPVLL QPNAGLPCLV EGKTCYNMDK ETFVQESLKH VKNGVAIIGG CCGTTPDFIA SLKNNLPVRK KITPKRATRV SSGTKTVEFG HHVVVCGERL NPTGKKKLKL ALKEERYDEL VVEAIKQDQA GAHVLDVNVG LPGINEVATM KHVIKLLQEV ISLPLQIDSS VPGAIEQACR YYNGKPLINS VNGKDETMDA IFPIVKKYGG VVIGLTLDEN GIPPLAKDRY KIAKKIINKA ASYGITKENI IIDCLVLTVS AQQKEVMETV KAVAMVKELG VHTVLGVSNV SFGLPNRPLL NKTFLAMAMS AGLDLPIINP MDQELMATID AFNVLYNYDH DAAVYIERRA NQETITKKDT STFTLNDIVL HGLKDEVTNA TKELLKTTPG LEIINNILIP ALDTVGKQYE KNIIFLPQLI QSAETSKIAF GIIKDTFKDT AATKGPIIMA TVHGDIHDIG KNIVKVVLES YGYKVIDLGK DVPPETVVEA FHKHHPKAIG LSALMTTTVV SMAKTIELLK QIDNICPIFV GGAVLTADYA KEINADYYSK DAMEAVELLN KIIK // ID G9RXZ5_9FIRM Unreviewed; 784 AA. AC G9RXZ5; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 01-OCT-2014, entry version 14. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHL65103.1}; GN ORFNames=HMPREF1032_01146 {ECO:0000313|EMBL:EHL65103.1}; OS Subdoligranulum sp. 4_3_54A2FAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Subdoligranulum. OX NCBI_TaxID=665956 {ECO:0000313|EMBL:EHL65103.1}; RN [1] {ECO:0000313|EMBL:EHL65103.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=4_3_54A2FAA {ECO:0000313|EMBL:EHL65103.1}; 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 Subdoligranulum sp. 4_3_54A2FAA."; 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. {ECO:0000313|EMBL:EHL65103.1}. 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; ACWW01000089; EHL65103.1; -; Genomic_DNA. DR RefSeq; WP_009325602.1; NZ_JH414706.1. DR EnsemblBacteria; EHL65103; EHL65103; HMPREF1032_01146. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; SQ SEQUENCE 784 AA; 83270 MW; D3006BE815EC63DE CRC64; MNKIFDGKRY WLLDGAMGTM LQKSGLKLGE RPDLLSITHP DVVERINRAY VEAGSDLICA NTFGSNAKKL AGCGYTVEEV VAAGIGTAKR AAAGTAARVM LDVGPIGELL EPAGALKFEE AYEIYKEVVL AGWRAGADLV KFATMTDLYE IKAAVLAAKE NTPLPVLVSM TFEENGRTFT GCTVESFAIT AEGLGVDGVG INCSLGPAEI YPMAQRLCAA TSLSVFIKPN AGLPDPATGR YSIGPKEFCD ELERFKALGI SAVGGCCGTT PEYLALLAKT FKQDTPVHRE PVRRSAVCTP TRTVEIDTVR VIGERINPTG KKRFKEALRD GDMDYILSQA VEQAGAGADI LDVNVGLPEI DEQEMMIRAV KAVQSVCDLP LQLDSTRADV LEAGLRVYNG KPIVNSVNGE QAVLDRLLPI CKKYGAAVVG LTLDENGIPA LAEQRFALAQ KIVAAAEAAG IPREDVYIDC LTLTASAQQE AVRETLKAVR MVKERLGVKT VLGVSNISFG LPCREQVNTS FLTLAMAHGL DLPIINPNAE AMMAAVASFK VLYNIDRDSR EYLARYAGQA AVQPAAQQTV TLYDAVLQGL KAAAAQAART ALQAKSPEEL VNEVLIPALD TVGAGFEKGV LFLPQLLQSA GAAQAAFEVV KDAIAASGKK SGGKGKIIVA TVKGDIHDIG KNIVKTLLEN YGYDVLDLGR DVPAETVVKA AQEHGVRLVG LSALMTTTLG SMEETICALR RAGLSCQVMV GGAVLTPEYA MHIGADYYAK DAKQSVDIAR EVLG // ID G9S0R1_9PORP Unreviewed; 1227 AA. AC G9S0R1; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHL88904.1}; GN ORFNames=HMPREF1033_00347 {ECO:0000313|EMBL:EHL88904.1}; OS Tannerella sp. 6_1_58FAA_CT1. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Tannerella. OX NCBI_TaxID=665949 {ECO:0000313|EMBL:EHL88904.1, ECO:0000313|Proteomes:UP000004488}; RN [1] {ECO:0000313|EMBL:EHL88904.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=6_1_58FAA_CT1 {ECO:0000313|EMBL:EHL88904.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHL88904.1}. 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; ACWX01000007; EHL88904.1; -; Genomic_DNA. DR RefSeq; WP_009316699.1; NZ_JH414766.1. DR EnsemblBacteria; EHL88904; EHL88904; HMPREF1033_00347. DR Proteomes; UP000004488; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000004488}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 240 240 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 754 754 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136467 MW; 9DB81E2815EDAFB2 CRC64; MTIQDALKQR ILILDGAMGT MIQRYNLSES DYRGELFTNH PEELKGNNDI LCLTQPQIIS EIHEAYLQAG SDIIETNTFN ATSVSMNDYG MQNHIREINI KAAQLARKAA DKYTTEDKPR FVAGSIGPTN KTTSMSPDVN NPAFRSLSYD NLVFSYLEQI KALLSGGVDA LLVETVFDTL NAKAALFAAT AAMEETGIHV PIMVSATVSD SGGRTLSGQT LEAFLASIQH APILTLGLNC SFGARDMKPF LKQLSEIAPY YISAYPNAGL PNRFGEYDET PEAMANQMRE FVEERLVNII GGCCGTTPAH IKLYNELIDG KQPHIPIDKP NVLWLSGLER LEIKPENNFI NVGERCNVAG SRKFLRLISE KNYEEALGIA RKQVEDGAQI IDINMDDAML DAKSEMITFL NLIASEPEIS KVPIMIDSSK WEVIESGLKC VQGKSIVNSI SLKEGETIFL EHARMIKKLG AAMVVMAFDE NGQADSFDRK IEICERAYKL LTQKAGIDPN DIIFDPNVLA VATGIDEHLN YGIDFIKATA WIKKNLPGAK VSGGISNLSF SFRGNNYIRE AMHAAFLFHA VNAGMDMGIV NPGTSVTYTD IPKEVLSVIE DVILNRKPDA TEKLIILAEE LKNRQNGKTV EKKDIRDEMT LDERLEYALI KGISENLETD LSEAMRIYGK AVKVIDGPLM KGMNTVGELF GAGKMFLPQV VKTARTMKQA VAILKPFIEA DKADKSSPEK AGKFLLATVK GDVHDIGKNI VGVVLACNNY EVIDLGVMVP TEKIIKTAIE EKVDIVCLSG LITPSLEEMC HVAEEMEKAG MTIPLMIGGA TTSKIHTAVK IAPRYSGPVI HVKDASQNPL IAAQLANSET RKIFLEQLKK EQEKLRESIQ EKILLTPLSN ARNHKIKIGW GNYNPVKPLL TGQVQELHFS IKEIRPYINW IFFFNAWKLG GKFASIAFIN GCDHCKASWL TQFPEQERAK AAEAMQLYKE ASRMLNKLIE DQTETDILVG IFEANSQNES IYIQKEGVSH IIPCLRQQVQ KKGSEACYYS LSDFIMPADT QKTDYIGVFT VTAGKEIENR IEYYKQQDDN YNALLLQSLA DRIAEAATEL LHYRVRKEIW GYSPNETATV ESLLKEHYQG IRPAIGYPSL PDQSLAFDID KLLGFDRIDV SLTENGAMKP NSTVSGIMIA HPQSAYFHIG QIDMEQRAEY CKKRNFSIED SYKWLSV // ID G9WDB1_SALET Unreviewed; 1145 AA. AC G9WDB1; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|EMBL:EHJ79770.1}; DE Flags: Fragment; GN ORFNames=LTSEBAI_5515 {ECO:0000313|EMBL:EHJ79770.1}; OS Salmonella enterica subsp. enterica serovar Baildon str. R6-199. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=913069 {ECO:0000313|EMBL:EHJ79770.1}; RN [1] {ECO:0000313|EMBL:EHJ79770.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=R6-199 {ECO:0000313|EMBL:EHJ79770.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHJ79770.1}. 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; AFCK01001604; EHJ79770.1; -; Genomic_DNA. DR RefSeq; WP_001600556.1; NZ_AFCK01001604.1. DR EnsemblBacteria; EHJ79770; EHJ79770; LTSEBAI_5515. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHJ79770.1}; KW Transferase {ECO:0000313|EMBL:EHJ79770.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. FT NON_TER 1145 1145 {ECO:0000313|EMBL:EHJ79770.1}. SQ SEQUENCE 1145 AA; 126594 MW; A6428B2E79CCF84E CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLHEEDFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYRMESLS AEINYAAAKL ARACADEWTA RTPEKPRFVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGVDLILI ETVFDTLNAK AAVFAVKEEF EALGVDLPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MATQIREWAE AGFLNVVGGC CGTTPEHIAA MSRAVDGLPP RKLPEIPVSC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VESGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVEAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRERKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDEAASAQ QAEWRSWDVK KRLEYSLVKG ITEFIEQDTE EARQQAARPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EKGSSNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAREVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHARKKPR TPPVTLEAAR DNDLAFDWER YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KLLNPRGVVG LFPANRIGDD IEIYRDETRT HVLTVSHHLR QQTEKVGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAYEAQH DDYNKIMVKA IADRLAEAFA EYLHERVRKV YWGYAPNESL SNDELIRENY QGIRPAPAGL SCLPG // ID G9X3F8_9FIRM Unreviewed; 796 AA. AC G9X3F8; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 01-OCT-2014, entry version 17. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHL09923.1}; GN ORFNames=HMPREF9629_00915 {ECO:0000313|EMBL:EHL09923.1}; OS Peptostreptococcaceae bacterium ACC19a. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae. OX NCBI_TaxID=796937 {ECO:0000313|EMBL:EHL09923.1}; RN [1] {ECO:0000313|EMBL:EHL09923.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ACC19a {ECO:0000313|EMBL:EHL09923.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHL09923.1}. 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; AFZE01000058; EHL09923.1; -; Genomic_DNA. DR RefSeq; WP_009525150.1; NZ_JH414550.1. DR EnsemblBacteria; EHL09923; EHL09923; HMPREF9629_00915. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; SQ SEQUENCE 796 AA; 88045 MW; 4B2DA0B67F1D5626 CRC64; MFKIKFRDLL RKELIILDGA MGSVLQQKGM QAGELPEILN ITNPELIQDI NGAYYKSGAN VTYTNTFGAN RLKFEGSSYD FKEIIKAAVK NAQIARENVK NDREKFVALD IGPLGKLLKP IGDLEFEDAV DIFKEMIEAG VEAGADLIAI ETMSDTYELK AAVIAAKEVC DLPIIATVAF SDDKRLLNGA DAKSVIALLE GLRVDVLGFN CGLDPRNIDD LVEEFISYSS TPIAIKPNAG IPENVNGVIK FNLEPDGFGK IVGDFVEKGV MLVGGCCGTT PEHIKKLYEY TKDKKICKQT FKNHTLISSY TKCVVCDRPI IIGERINPTG KKLLKQALMN KDFSYILKEA VIQEENRAEI LDLNVGMNDI DEEEMMIKTI KAVQEISTLP LQIDSAKINV IEQGLRIYNG KAMLNSVNGK KESMEKIFPL VKKYGAVVVA LTLDENGIPE NAEGRYKIAE KIVKTAKEYG IDKKDIVVDP LCMTISSDKN AANETLKALD LIKKNLGVKT TLGVSNISFG LPQRELINHT FFSMALKTGL DFGIINPLAE DMIRAYDAHM VLAGLDENAL NYISKYSQAK KETQTPIKNQ MTLCESIKKG LKEDSFMIAK SMLSDKQPLD IINEELIPAL DEVGLGFEKG TVFLPQLMMS ADAASRAFDA LKEKLISLED KSKEKDKIIL ATVKGDIHDI GKNIVKVLLE NYGYDVYDLG KDVDYNTILD AIVKENVKLV GLSALMTTTV DNMQKTIELI KEKTPKTQIM VGGAVLTKDY SMKIGADRYC KDAMESVRYA KEVFGR // ID G9XA76_9FIRM Unreviewed; 796 AA. AC G9XA76; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 01-OCT-2014, entry version 17. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHL20090.1}; GN ORFNames=HMPREF9628_00901 {ECO:0000313|EMBL:EHL20090.1}; OS Peptostreptococcaceae bacterium CM5. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae. OX NCBI_TaxID=796940 {ECO:0000313|EMBL:EHL20090.1}; RN [1] {ECO:0000313|EMBL:EHL20090.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CM5 {ECO:0000313|EMBL:EHL20090.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHL20090.1}. 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; AFZG01000002; EHL20090.1; -; Genomic_DNA. DR RefSeq; WP_009529000.1; NZ_JH414601.1. DR EnsemblBacteria; EHL20090; EHL20090; HMPREF9628_00901. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; SQ SEQUENCE 796 AA; 88194 MW; 902C111BAFFFE7B9 CRC64; MFKIKFRDLL RKELIILDGA MGSVLQQKGM QAGELPEILN ITNPELIQDI NEAYYKSGAN VTYTNTFGAN RLKFEGSSYD FKEIIKAAVK NAQIARENVK NDREKFVALD IGPLGKLLKP IGDLEFEDAV DIFKEMIEAG VEAGADLIAI ETMSDTYELK AAVIAAKEVC DLPIIATVAF SDDKRLLNGA DAKSVIALLE GLRVDVLGFN CGLDPRNIDD LVEEFISYSS TPIAIKPNAG IPENVNGVIK FNLEPDGFGK IVGDFVEKGV MLVGGCCGTT PEHIKKLYEY TKDKKICKQT FKNHTLISSY TKCVVCDRPI IIGERINPTG KKLLKQALMN KDFSYILKEA VIQEENKAEI LDLNVGMNDI DEEEMMIKTI RAVQEISTLP LQIDSAKINV IEQGLRIYNG KAMLNSVNGK KESMEKIFPL VKKYGAVVVA LTLDENGIPE NAQGRYKIAE KIVKTAKEYG IDKKDIVVDP LCMTISSDKN AANETLKALY LIKKNLGVKT TLGVSNISFG LPQRELINHT FFSMALKTGL DFGIINPLAE DMIRAYDVHM VLVGLDENAL NYISKYSQAK KETQTPIKNQ MTLCESIKKG LKEDSFMIAK SMLSDKQPLD IINEELIPAL DEVGLGFEKG TVFLPQLMMS ADAASRAFDA LKEKLISLED KSKEKDKIIL ATVKGDIHDI GKNIVKVLLE NYGYDVYDLG KDVDYDTILD AIVKENAKLV GLSALMTTTV DNMQKTIELI KEKTPKTQIM VGGAVLTKDY SMKIGADRYC KDAMESVRYA KEVFGR // ID G9XHC5_DESHA Unreviewed; 285 AA. AC G9XHC5; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EHL08927.1}; GN ORFNames=HMPREF0322_00348 {ECO:0000313|EMBL:EHL08927.1}; OS Desulfitobacterium hafniense DP7. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfitobacterium. OX NCBI_TaxID=537010 {ECO:0000313|EMBL:EHL08927.1}; RN [1] {ECO:0000313|EMBL:EHL08927.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DP7 {ECO:0000313|EMBL:EHL08927.1}; 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 (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHL08927.1}. 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; AFZX01000010; EHL08927.1; -; Genomic_DNA. DR RefSeq; WP_005808414.1; NZ_JH414441.1. DR EnsemblBacteria; EHL08927; EHL08927; HMPREF0322_00348. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EHL08927.1}; KW Transferase {ECO:0000313|EMBL:EHL08927.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 200 200 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 265 265 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 266 266 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 285 AA; 30775 MW; 87C7DCCDF71FCEC7 CRC64; MILDKDSYVI FDGAMGTMLQ KYDLAPGQPP EVLNITRPEV IEEVHRKYIK AGSNIITTNT FGAIETKLNG TGYSVEEVVQ SAIAIARRAA GKNLVALDVG PTGELIEPLG DLSFEEVYDL YACQIKAAAL TGNVDLVLIE TFFDLTEAHA AIRAAKDHSS LPVICTFTFQ QKGRTLMGKD IKTVVASLEE YGVDAVGVNC SLGPGEMLSI VETMVSSTQL PILVQPNAGL PKLIGDRTVY DVEPEEFARY IQVMANLGVK WFGGCCGTTP EFISAIKESL GLKHN // ID G9YB20_HAFAL Unreviewed; 1205 AA. AC G9YB20; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 01-APR-2015, entry version 18. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EHM39632.1}; GN ORFNames=HMPREF0454_03783 {ECO:0000313|EMBL:EHM39632.1}; OS Hafnia alvei ATCC 51873. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Hafnia. OX NCBI_TaxID=1002364 {ECO:0000313|EMBL:EHM39632.1}; RN [1] {ECO:0000313|EMBL:EHM39632.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 51873 {ECO:0000313|EMBL:EHM39632.1}; 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 (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHM39632.1}. 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; AGCI01000091; EHM39632.1; -; Genomic_DNA. DR EnsemblBacteria; EHM39632; EHM39632; HMPREF0454_03783. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHM39632.1}; KW Transferase {ECO:0000313|EMBL:EHM39632.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 225 225 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 737 737 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1205 AA; 133278 MW; 1C02E1C69A47000D CRC64; MGTMIQGYRL TEEDFRGDRF ADWQSDLKGN NDLLVLTKPD IISAIHYDYL EAGADILETN TFNSTRIAMA DYHMESLSAE INYEAARLAR ACADEWTART PNKPRYVAGV LGPTNRTASI SPDVNDPAFR NISFDQLVEA YRESTRALVE GGVDLIMIET IFDTLNAKAA IYAVETEFEA MGVELPVMIS GTITDASGRT LSGQTTEAFY NSLRHVKPLT FGLNCALGPD ELRQYVAELS RIAECFVTAH PNAGLPNAFG EYDLGPKEMA EHIAEWAQAG FLNIVGGCCG TTPAHIAAIS RAVDGVKPRV LPDIPVACRL AGLEPLTIDA NTLFVNVGER TNVTGSAKFK RLIKEDKYAE ALEVALQQVE SGAQIIDINM DEGMLDAEAA MVRFLNLIAG EPDIARVPIM IDSSKWEVIE KGLKCIQGKG IVNSISMKEG EDKFIEHARK VRRYGAAMVV MAFDEVGQAD TRARKIEICR RAYKLLTETV GFPPEDIIFD PNIFAVATGI EEHNNYAVDF IEACADIKAE LPHALISGGV SNVSFSFRGN DPVREAIHAV FLYYAIRNGM DMGIVNAGQL AIYDDLPMDL RDAVEDVILN RREDGTERLL DLAEKYRGSK SDDDSNKPQA EWRTWPVKKR LEYSLVKGIT EFIEADTEEA RLEAERPIEV IEGPLMDGMN VVGDLFGDGK MFLPQVVKSA RVMKQAVAYL EPFIEASKEK GTSAGKVLLA TVKGDVHDIG KNIVGVVLQC NNYEIIDLGV MVPCDKILKT AREQNVDIIG LSGLITPSLD EMVYVAKEME RQGFDLPLLI GGATTSKAHT AVKIEQNYSG PTTYVSNASR TVGVVAALLS PTQKPDFVAR TRKEYETVRI QHGRKKPRTP PVSLEAAREN ATSLDWSDYT PPVPHRLGVH QVTASIDTLR NYIDWTPFFM TWSLAGKYPR ILEDEVVGEE AKRVFADANA MLDDLASSGK LNPRGVYGIF PANRVGDDVE IYSNEFRDEV LVTGHHLRQQ TEKTDFANYC LADFVAPKSS GKSDYIGAFA VTGGLEEDAL ADAYEAQHDD YNKIMVKALS DRLAEAFAEY LHEKVRKVYW GYAANENLSN EELIRENYQG IRPAPGYPAC PEHTEKAAIW TLLDAENTVG MKLTESYAMW PGASVSGWYF SHPESKYFAV AQIQRDQVED YAQRKGMPVA EVERWLAPNL GYDAD // ID G9YI84_9FIRM Unreviewed; 842 AA. AC G9YI84; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EHM39894.1}; GN ORFNames=HMPREF0080_01369 {ECO:0000313|EMBL:EHM39894.1}; OS Anaeroglobus geminatus F0357. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Anaeroglobus. OX NCBI_TaxID=861450 {ECO:0000313|EMBL:EHM39894.1}; RN [1] {ECO:0000313|EMBL:EHM39894.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0357 {ECO:0000313|EMBL:EHM39894.1}; 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 (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. {ECO:0000313|EMBL:EHM39894.1}. 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; AGCJ01000058; EHM39894.1; -; Genomic_DNA. DR RefSeq; WP_006790344.1; NZ_JH417599.1. DR EnsemblBacteria; EHM39894; EHM39894; HMPREF0080_01369. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHM39894.1}; KW Transferase {ECO:0000313|EMBL:EHM39894.1}. SQ SEQUENCE 842 AA; 90411 MW; 9B110885960C8307 CRC64; MKKKLLDRLG KEWLFFDGGT GSILQAEGLQ PGELPETWNL IHPDKIISLH EHYLEAGCHI FNTNTFGANR LKFPDTIDEI VTAAVRLAKK ARRRAGRDDA YIALDIGPTG KLLKPMGDLP FEDAVSIFAE IVRIGAREGA DLVLIETMND SYEAKAAVLA AKENCDLPVL LTCVFDEKGK MLTGGTPESI VAVMEGLGID GIGINCSLGP KEMLPTVKRL TAAASVPVLV NPNAGLPESI DGETVYTIGP DEFATCMKEI ARLGASAVGG CCGTTPEHIK KVIAAVSPLP FMPVKPKHRT VISSFSRTVT IGRDTAPVII GERINPTGKK RFKQALLDHD IDYIVGQGLE QEEAGAHVLD VNVGSPETDE VELIQEVVGK LQSILPLPLQ IDTSNPEAME KALRMYNGKA LINSVNGKEE TMKAVFPLVK KYGGVVVALA LDEDGIPPTA DGRVAIAGKI YDKAAFYGIA KENIIIDGLC MTVSADPASA LVTLETVRRI HDELGGNTIL GVSNISFGLP ARELINSYFF AMALQSGLTS AIINPNNTAM MQAYRTYCVL TDKDPNFTEF IGAYRDYKTP DKRVDEAVSA YKKKILRALD FDLGEIKAVT VKPVASKTIE PSPTADGRKE STGKGSKLMD AIERGLANPA AEATRNALLT RDALAIINED LVPALDNVGH GFEKGTIFLP QLLMAAEAAK AAFSVVKESM KDIAQDVKGK VILATVKGDI HDIGKNIVKV LLENYGYKVV DLGRDVSPEL IVETAVKDDV KLVGLSALMT TTVVNMEETI NQLHAKKPDC KIVVGGAVMT KQYADSIGAD CYGKDAMSTV RYADELVAAG LL // ID G9YLB3_9FIRM Unreviewed; 786 AA. AC G9YLB3; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EHM54778.1}; GN ORFNames=HMPREF0372_00278 {ECO:0000313|EMBL:EHM54778.1}; OS Flavonifractor plautii ATCC 29863. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Flavonifractor. OX NCBI_TaxID=411475 {ECO:0000313|EMBL:EHM54778.1}; RN [1] {ECO:0000313|EMBL:EHM54778.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29863 {ECO:0000313|EMBL:EHM54778.1}; 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 (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. {ECO:0000313|EMBL:EHM54778.1}. 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; AGCK01000024; EHM54778.1; -; Genomic_DNA. DR RefSeq; WP_007488231.1; NZ_JH417639.1. DR EnsemblBacteria; EHM54778; EHM54778; HMPREF0372_00278. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHM54778.1}; KW Transferase {ECO:0000313|EMBL:EHM54778.1}. SQ SEQUENCE 786 AA; 83601 MW; 034A18544FAD65BB CRC64; MGIEIPQNKF LILDGAMGTV LQQRGLSPQG RPELLNLTEP ELLDSVYKEY IAAGSQVIYA NTFGANGLKL AKTGHSVEEV VGAAIAVAKK AAAGTGTLVA LDVGPLGELL EPMGTLSFER AYDLFREMAE AGAKAGADLI VVETMTDLYE AKAALLAAKE AAHLPVFVTM SFDAGGRTFT GCTVASMART LEGLGADAIG LNCSLGPDLL APLLKELCEN TRLPVIAKPN AGLPDPVDGH YDMGPEDFAQ ALLTCVEAGI SIVGGCCGTS PEYIRRLTAV LEGKKPVSRH YNNTGLVCTP VTPIRLNGVR VIGERINPTG KKRFQQALLE NDLDYILDVG VQQEDAGADI LDVNVGFPGV NEVVMLPRVV KKLQSAIAVP LQLDSSNPDA LEAGLRVYNG KAAVNSVNGE PEVLERVLPI VKKYGASVVG LTLDKNGIPK TAEERVAIAC RILQAALDHG IPREDVWIDC LTLTVSAQQE QAAETLKAVR TIREELGLQV VLGVSNISFG LPNRKLITQN FLIQAMHAGL TLPIINPNQT EMMDAVAAYR VLSGEDRECR AYVARFAAES PVVQAAPKAD ALTLGDAVIR GLKADAGKLA AKALETEDEL SLVENHLIPA LDKVGEDYDK GTAFLPQLLS AAQAAQAVFE VIRSSIAAKG GVPVKKGKLI VATVQGDIHD IGKNIVKTVL GNYGYEVLDL GRDVPPETIL RTVQEQGVRL VGLSALMTTT LPAMEKTIRL LHTMEEPPVI FVGGAVVTPE YAKQMNADYY AKDAHQSVEI TRKVMG // ID G9YLB4_9FIRM Unreviewed; 592 AA. AC G9YLB4; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 16. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HMPREF0372_00279 {ECO:0000313|EMBL:EHM54779.1}; OS Flavonifractor plautii ATCC 29863. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Flavonifractor. OX NCBI_TaxID=411475 {ECO:0000313|EMBL:EHM54779.1}; RN [1] {ECO:0000313|EMBL:EHM54779.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29863 {ECO:0000313|EMBL:EHM54779.1}; 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 (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHM54779.1}. 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; AGCK01000024; EHM54779.1; -; Genomic_DNA. DR RefSeq; WP_007488232.1; NZ_JH417639.1. DR EnsemblBacteria; EHM54779; EHM54779; HMPREF0372_00279. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EHM54779.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EHM54779.1}. SQ SEQUENCE 592 AA; 64539 MW; E79199CBF287CFF5 CRC64; MMDIRTYLSQ GKPLLFDGAM GTYFAAHPGR AEERCERANL TRPEEILRIH RAYLQAGCRA IKTNTFAISG DLSDGNDETA CDIVNAACHL ARQAAQPYGA YVFADLGPAP RDHSRAPADL YQTQAQWFLE QGVTHFLVET LSGDEGLPEL AGWLKEKNPD AFLMVSFAVD HSGMTSAGRL GSELYRFASE LAGVDAVGFN CVSGPRHLLK YIQTLELSDK PLTVMPNAGY PTVLGRRTVF GGQPDYFAGQ IAQIVQAGAS IVGGCCGTTP EHIAQTAQAL KEPLPKCTVS APKKLLKPAA NASNSLWEKL EAGKRVIAVE LDPPVDDDSA GFWEGVQALR GSGADAVTIA DCPIGRPRAD SSLLACKIKR DIGIEPLPHM TCRDRNLNAT KALLLGLSME GVHNVLVVTG DPIPTEDRNE VKSVFNFNSR KLARFVHMLN ENTLRTPFRI YGALNLNARN FDVELRRAQE KEACGVSGFL TQPVLSAEAL DNLKLAHKTL RGKILGGIFP VVSHRNACFL NNEISGMRVC DEIIHLYEGK DRDAAEALAV TVSTAIAKEI FPYTDGYYLM TPFRRVALME HIIQNIQQSC IS // ID G9YUK5_9FIRM Unreviewed; 415 AA. AC G9YUK5; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EHM42031.1}; GN ORFNames=HMPREF0372_03219 {ECO:0000313|EMBL:EHM42031.1}; OS Flavonifractor plautii ATCC 29863. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Flavonifractor. OX NCBI_TaxID=411475 {ECO:0000313|EMBL:EHM42031.1}; RN [1] {ECO:0000313|EMBL:EHM42031.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 29863 {ECO:0000313|EMBL:EHM42031.1}; 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 (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. {ECO:0000313|EMBL:EHM42031.1}. 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; AGCK01000259; EHM42031.1; -; Genomic_DNA. DR RefSeq; WP_007493652.1; NZ_JH417820.1. DR EnsemblBacteria; EHM42031; EHM42031; HMPREF0372_03219. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHM42031.1}; KW Transferase {ECO:0000313|EMBL:EHM42031.1}. SQ SEQUENCE 415 AA; 44510 MW; 3F8BCF7752511ACC CRC64; MDTIPPLSLP ILLDGATGSE LYKRGMPAGA CTEQWVLGHP EALLELQRGY VAAGSQVLIA PTFGANRVRL EQHGIFGQVA DYNRRLVELS RQAAGGRALV AGDMAPTGLF IAPFGESSFE ELVAIYTEQA AALAAAGVDL FLIETTMTMP EARAAVLACK SVSDRPVWVT FTCDENGRTL SGTDVLAALI VMQGMGVDAF GLNCSSGPAE MLEQMRRLTP YTTVPLIAKP NAGLPETVEG QAVYHCPPEE FASYAAGFAA AGVRIFGGCC GTTAEHVAAL RAAVEAVDFS AFVPPRRDPD VIPCASEKEA RFITPDIDVG ETIECTSDLL EDILEAEENA PQGALKIAIY DEDDLYTFAE NQYAVKDALC LWTDVPELLE QALRLYQGRA FWDGTGELEA AFLQEMARKY GLVLL // ID G9YY32_9ENTR Unreviewed; 1227 AA. AC G9YY32; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EHM51703.1}; GN ORFNames=HMPREF0880_00121 {ECO:0000313|EMBL:EHM51703.1}; OS Yokenella regensburgei ATCC 43003. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yokenella. OX NCBI_TaxID=1002368 {ECO:0000313|EMBL:EHM51703.1, ECO:0000313|Proteomes:UP000003044}; RN [1] {ECO:0000313|EMBL:EHM51703.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43003 {ECO:0000313|EMBL:EHM51703.1}; 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 (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHM51703.1}. 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; AGCL01000005; EHM51703.1; -; Genomic_DNA. DR RefSeq; WP_006816654.1; NZ_JH417862.1. DR EnsemblBacteria; EHM51703; EHM51703; HMPREF0880_00121. DR Proteomes; UP000003044; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000003044}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHM51703.1}; KW Transferase {ECO:0000313|EMBL:EHM51703.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136252 MW; 11D7D05BB7CC6856 CRC64; MSNKVEQLHQ QLKERILVLD GGMGTMIQSY RLEEQDFRGE RFTDWPCDLK GNNDLLAITQ PETIAAIHYA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINYEAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNVTFDQLV EAYRESTRAL VEGGSDLILI ETVFDTLNAK AAIFAVKEEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHADA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAAQIREWAE AGFLNIVGGC CGTTPEHIAA MSRAVEGLTP RALPDLPVAC RLAGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY NEALDVARQQ VESGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVEAFIHHA KKVRRYGAAV VVMAFDEVGQ ADTRKRKIEI CRRAYQILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDSTER MLELAEKYRG SKADDGANAQ QAEWRSWDVK KRLEYSLVKG ITEFIELDTE EARQQAARPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPYIEASK EKGSSNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIIDL GVMVPAEKIL KTAREVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQHDDFV ARTRKEYDTV RIQHARKKPR TPPVTLEAAR ENDFAFDWSS YTPPVAHRLG VQEVSASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG EEAKRLFHDA NEMLDKLSAE QLLTPRGVVG LFPANRVGDD IEIYRDETRT HVLTVSHHLR QQTEKNGFAN YCLSDFVAPK LSGKADYIGA FAVTGGLEED ALAEAYEAQH DDYNKIMVKA IADRLAEAFA EYLHERVRKV YWGYAANENL SNEELIRENY QGIRPAPGYP ACPEHTEKGT IWQLLDVETH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMN VAEVERWLAP NLGYDAD // ID G9ZCJ3_9GAMM Unreviewed; 289 AA. AC G9ZCJ3; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHM55725.1}; GN ORFNames=HMPREF9080_00471 {ECO:0000313|EMBL:EHM55725.1}; OS Cardiobacterium valvarum F0432. OC Bacteria; Proteobacteria; Gammaproteobacteria; Cardiobacteriales; OC Cardiobacteriaceae; Cardiobacterium. OX NCBI_TaxID=797473 {ECO:0000313|EMBL:EHM55725.1}; RN [1] {ECO:0000313|EMBL:EHM55725.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0432 {ECO:0000313|EMBL:EHM55725.1}; 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 (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. {ECO:0000313|EMBL:EHM55725.1}. 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; AGCM01000023; EHM55725.1; -; Genomic_DNA. DR RefSeq; WP_006984497.1; NZ_JH417893.1. DR EnsemblBacteria; EHM55725; EHM55725; HMPREF9080_00471. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; SQ SEQUENCE 289 AA; 30951 MW; 6BE74222B3F43329 CRC64; MPHPLLIHDG GTGRELLRRG APFAQPQWSV LALMQRPSAV ADVHRAYIEA GTDIIITNSY ALVPFHLGED DFRAQGDKLA ASPENWRSRL SGTAAKNCAS PPHCHHHLAP AAPTCLTPRR PRPSPARLLT GRLPMPTCGW PEPKAAPPKS VPCMRWRRTI APSGPPSPLT TSTLPSRHAC TVVKASPTLL PPSLTSAPMP CSSIAATPKS WRTPSWWPAP RWMRQVAPCA SASMPTHSAP TTPAKPPCLP ITAWMTSAPT SAPPPTSPLP KPGVTAKPSP SNRNIRKKS // ID G9ZNF3_9LACO Unreviewed; 325 AA. AC G9ZNF3; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Putative homocysteine S-methyltransferase {ECO:0000313|EMBL:EHL98934.1}; GN ORFNames=HMPREF9103_01256 {ECO:0000313|EMBL:EHL98934.1}; OS Lactobacillus parafarraginis F0439. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=797515 {ECO:0000313|EMBL:EHL98934.1}; RN [1] {ECO:0000313|EMBL:EHL98934.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0439 {ECO:0000313|EMBL:EHL98934.1}; 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-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. {ECO:0000313|EMBL:EHL98934.1}. 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; AGEY01000054; EHL98934.1; -; Genomic_DNA. DR RefSeq; WP_008212205.1; NZ_JH414951.1. DR EnsemblBacteria; EHL98934; EHL98934; HMPREF9103_01256. DR OrthoDB; EOG6C019S; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHL98934.1}; KW Transferase {ECO:0000313|EMBL:EHL98934.1}. SQ SEQUENCE 325 AA; 35345 MW; 57A5A6ABC523EA4B CRC64; MREDNMANLI NENLKKKAAL VLDGAMATEL EKRGVHTDNA LWSATALISN PEAVKAVHKS YFEAGADIAI TDTYQANVNG FEQAGYSEGQ SEKLITEAVR LARAARDEFY FELPADQRAN RAPYPIVAGS VGPYGAYLAD GSEYTGDYLL TTTEFQEFHA PRMELMAKAG VDMFAFETQP NFDEAKALAS MMKTRFPNMF AWLSFSVSDP EHLCDGTPLA EAVAYFNGNP QISAIGVNCT SMNNIEATIK TIAPNTDKPI IVYPNNGDIY DPKTKTWEPN PQAATFADLT PKWLAAGAKI IGGCCRTTPG DIEQVADAVN AKNLS // ID H0A3M2_9PROT Unreviewed; 1166 AA. AC H0A3M2; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 01-APR-2015, entry version 21. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EHL98892.1}; GN ORFNames=HMPREF9946_03415 {ECO:0000313|EMBL:EHL98892.1}; OS Acetobacteraceae bacterium AT-5844. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; unclassified Acetobacteraceae. OX NCBI_TaxID=1054213 {ECO:0000313|EMBL:EHL98892.1}; RN [1] {ECO:0000313|EMBL:EHL98892.1} 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHL98892.1}. 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; AGEZ01000104; EHL98892.1; -; Genomic_DNA. DR RefSeq; WP_007437780.1; NZ_JH599980.1. DR EnsemblBacteria; EHL98892; EHL98892; HMPREF9946_03415. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHL98892.1}; KW Transferase {ECO:0000313|EMBL:EHL98892.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 224 224 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 735 735 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1166 AA; 128690 MW; 8E5F9B0D7ED3F467 CRC64; MARPHLLDAL RDRVLLCDGG MGSRVQALTL EIEKDFWGKE NCTEVLNLSR PELVREIHRG YYEAGSDMVL TNSFGGSPIT LEEFELGDRA FEINKLSVEL AREAADSFAD GRDRWVVGDI GPGTKLPSLG HIDYDTLEAA LTEQCRGLIA GGADALLTET NQDTLFIKAA VNAAKIAKAE AKSDIPIFVQ VTVETTGTLL VGSDIAAAAT AIHALDVPLI GLNCATGPQE MAEHVRWLSQ NWPGLLSCQP NAGLPELVDG KTHYPLGAEE MASWMQRFVE EDGLNLIGGC CGTSIPHIQG LDAMLRRISG NQSRPVPAQR QSYWVPSVAS LYGQVSLRQE NSYFSIGERC NANGSKAWRE RQAAHDWDAC VSIGREQVGE GSNSLDVCTA FVGRDEKAEM DEVIRRFTGS VNAPLVIDST ETPVIESALK LHGGKPIINS INFEDGEGHA TDRMVLAKKF GAAVIALTID EVGMAKTPED KLRIAERLVD FACNKHGLPQ SDLLIDPLTF TIATGNEDDR KLGLWTLEGI RMIREKFPDI QIILGLSNIS FGLNPAARHV LNSVFLDHAV KAGMTGAIVH VSKIKPLHSI PPEEVKVAED LIFDRREEGY DPLQKLLEMF AGRKAADAAK KVKADTVEGR LKDRIVDGDR KGLDEELADA LAKGIKPLDI INGILLEGMK VVGELFGAGK MQLPFVLQSA ETMKAAVAYL EPHMEKIEGQ EKGTIVLATV RGDVHDIGKN LVDIILTNNG YRVINLGIKV PLNEMIAAVQ EHKANAIGMS GLLVKSTVVM KENLEEMSRQ GLEVPVLLGG AALTRNFVED DCVNAYTSGR VAYARDAFDG LHLMDRVMGS DFDGYLATLQ QKRSGKSRNT TRVLGQADPR GFAPVDLNYA QERRRRQTAN EPVPTPPFWG SRIVQSDPKA VVPFINERSL YQFQWGFRKQ GRSLEDFIGW AKQELRPVLR RMLELSEREN ILKPQAIYGY WKCAGQGNDV ILFEEDGITE ACRFTLPRQP KQDGECIADF IRDIDDGPEK RDVIGLQVVT VGQKASDMAR DWFEANRYQD YLYLHGLSVE MAEAMAEYVH KRIRAELGYA AEDDRDLEKM LAQGYRGGRY SFGYPACPRL EDQAPLLKLL DSERIGVSIS DEWQLHPEQS TSAIVLHHPR AKYFSV // ID H0A4D7_9PROT Unreviewed; 317 AA. AC H0A4D7; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 01-OCT-2014, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EHL98162.1}; GN ORFNames=HMPREF9946_03684 {ECO:0000313|EMBL:EHL98162.1}; OS Acetobacteraceae bacterium AT-5844. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; unclassified Acetobacteraceae. OX NCBI_TaxID=1054213 {ECO:0000313|EMBL:EHL98162.1}; RN [1] {ECO:0000313|EMBL:EHL98162.1} 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHL98162.1}. 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; AGEZ01000128; EHL98162.1; -; Genomic_DNA. DR RefSeq; WP_007438045.1; NZ_JH599999.1. DR EnsemblBacteria; EHL98162; EHL98162; HMPREF9946_03684. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHL98162.1}; KW Transferase {ECO:0000313|EMBL:EHL98162.1}. SQ SEQUENCE 317 AA; 34493 MW; AEB272A652C187EF CRC64; MRPDTTPLPA QTEAVFLTDG GLETSLIFEQ GIELPQFAAF PLLASPEGRE SLRTYFEPFL ALAHQHQVGF LLDTPTWRAN PEWGTKLGFS PSALDDIQHR AVAWARELRR PFHSPDTPVP INGAVGPRGD GYRVEQRMTV EEARQYHLPQ LKALQEGGAD MATAVTMNYP EEAIGIALAA RDIRMPVAIS FTVETEGQLA SGDELPAAIA AVEAASGGWP LYYMINCAHP THFMKVVQAG GEWTKRLRGI RANASALSHA ELDAAEELDA GDPQALGQDY RELRSILPHF SVMGGCCGTG QRHLRAICEA CLPARTA // ID H0BEC5_9ACTO Unreviewed; 309 AA. AC H0BEC5; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 01-OCT-2014, entry version 11. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:EHM27989.1}; GN ORFNames=SPW_3612 {ECO:0000313|EMBL:EHM27989.1}; OS Streptomyces sp. W007. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1055352 {ECO:0000313|EMBL:EHM27989.1}; RN [1] {ECO:0000313|EMBL:EHM27989.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=W007 {ECO:0000313|EMBL:EHM27989.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHM27989.1}. 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; AGSW01000129; EHM27989.1; -; Genomic_DNA. DR RefSeq; WP_007452268.1; NZ_AGSW01000129.1. DR EnsemblBacteria; EHM27989; EHM27989; SPW_3612. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHM27989.1}; KW Transferase {ECO:0000313|EMBL:EHM27989.1}. SQ SEQUENCE 309 AA; 32146 MW; 6C10E9D668A65700 CRC64; MSTGSTLADA LDAGPVLLDG GLSNQLEAQG CDLSDALWSA RLLADAPEQI EAAHLAYLRA GARVLITASY QATFEGFGRY GLDRAGTEAL LARSVELARG AAEAARRAGP GRETWVAASV GPYGAMLADG SEYRGRYGLS VRELEHFHRP RVAALAAAGP DALALETVPD LDEAEALVRV AEETGVPYWL SYSVAGGRTR AGQPLEEAFA VAAGRDSVLA VGVNCCDPEE AQGAVEQAVA VTGRPAVVYP NSGEGWDAAA RGWTGRGTFD PGRVRAWTRA GARLVGGCCR VGPDLITELD GRLESQGPP // ID H0BK15_9ACTO Unreviewed; 1147 AA. AC H0BK15; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 01-APR-2015, entry version 19. DE SubName: Full=Putative 5-methyltetrahydrofolate:homocysteine S-methyltransferase {ECO:0000313|EMBL:EHM25985.1}; GN ORFNames=SPW_5603 {ECO:0000313|EMBL:EHM25985.1}; OS Streptomyces sp. W007. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1055352 {ECO:0000313|EMBL:EHM25985.1}; RN [1] {ECO:0000313|EMBL:EHM25985.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=W007 {ECO:0000313|EMBL:EHM25985.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHM25985.1}. 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; AGSW01000198; EHM25985.1; -; Genomic_DNA. DR EnsemblBacteria; EHM25985; EHM25985; SPW_5603. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHM25985.1}; KW Transferase {ECO:0000313|EMBL:EHM25985.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 212 212 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 278 278 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 279 279 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 722 722 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1147 AA; 125135 MW; 22ABCAB789DDAFB5 CRC64; MVVADGAMGT MLQAQDPTLE DFENLEGCNE ILSVTRPDIV RSVHEEYFAV GVDCVETNTF GANHSAANEY DIADRIFELS ESGARIAREV ADEFTLSTGQ QRWVLGSMGP GTKLPTLGHA PYVTLRDSYQ QNAEGLIAGG ADALMVETTQ DLLQTKASII GARRAMEATG ASVPLICSVT VETTGTMLLG SEIGAALTAL EPLGIDMIGL NCATGPAEMS EHLRYLARHS RIPLSCMPNA GLPVLGKNGA HYPLGPAELA DAQENFVQEY GLSLVGGCCG TTPEHLRQVV ERVRGLTPTS RDPRPEPGAA SLYQTVPFRQ DTSYLAIGER TNANGSKKFR EAMLGARWDD CVEMARDQIR EGAHMLDLCV DYVGRDGVAD MAELAGRFAT ASTLPIVLDS TELPVLRAGL EKLGGRAVLN SVNYEDGDGP ESRFAQVSAL ASEHGAALIA LTIDEEGQAR TIEHKVAIAE RLIEDLTTNW GIHESDILID TLTFTICTGQ EESRGDGIAT IGAIRELKKR HPDVQTTLGL SNISFGLNPA ARVVLNSVFL DECVKAGLDS AIVHASKILP IARLEEDQVK VALDLIYDRR AEGYDPLQKL MELFEGVNMK SMKAGRAEEL MALPLDERLQ RRIIDGEKNG LEADLDEALQ DTPALDIVNN ILLEGMKVVG ELFGSGQMQL PFVLQSAEVM KGAVAHLEPH MEKTDDDGKG TIVLATVRGD VHDIGKNLVD IILSNNGYNV VNLGIKQPVS AILEAAEEHR ADVIGMSGLL VKSTVIMKEN LQELNQRNMA ADYPVILGGA ALTRAYVEQD LHEIYEGEVR YARDAFEGLR LMDALIAVKR GVPGATLPEL KQRRVPKKNI DTAVLEVEEP EGSVRSDVSI TNPVPEPPFR GTRVIKGIPL KDYASWLDEG ALFKGQWGLK QARTGDGPTY EELVETEGRP HLRGWLDHLQ SNNLLEAAVV YGYFPCVSKG EDVILLHEDG SERTRFTFPR QRRGRRLCLA DFFRPEESGE TDVIGLQIVT VGSRIGEATA ELFAANSYRD YLELHGLSVQ LAEALAEYWH ARVRSELGFA GEDPADVEDM FALKYRGARF SLGYGACPDL EDRAKIADLL QPERIGVHLS EEFQLHPEQS TDAIVIHHPE AKYFNAR // ID H0BWU7_9BURK Unreviewed; 354 AA. AC H0BWU7; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHL23003.1}; GN ORFNames=KYG_09210 {ECO:0000313|EMBL:EHL23003.1}; OS Acidovorax sp. NO-1. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Acidovorax. OX NCBI_TaxID=512030 {ECO:0000313|EMBL:EHL23003.1}; RN [1] {ECO:0000313|EMBL:EHL23003.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NO-1 {ECO:0000313|EMBL:EHL23003.1}; 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGTS01000075; EHL23003.1; -; Genomic_DNA. DR RefSeq; WP_008904537.1; NZ_AGTS01000075.1. DR EnsemblBacteria; EHL23003; EHL23003; KYG_09210. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 354 AA; 38470 MW; 4290A395D52B191C CRC64; MQALHYTRAA QLPDILAQRI VILDGAMGTM IQRFKLGEAQ YRGEGYNGPD GAGDRFKDFP RDVKGNNELL SITRPDVIRD IHERYLAAGA DLIETNTFGA TTIAQEDYKM AHLAREMNLK SAQLARAACD KYSTPDKPRF VAGALGPTPK TASISPDVND PGARNVDFEQ LRAAYYEQTE ALVEGGADVL LVETIFDTLN AKAALFAIDE FFDKSGERLP LIISGTVTDA SGRILSGQTV TAFWHSVRHS RPLAIGLNCA LGATLMRPYI QELNRVAEDT FISCYPNAGL PNPMSDTGFD ETPEITSRLV HEFAAEGLVN ILGGCCGTTP DHIGAIAKAV ENVPTRKMFY PAEA // ID H0DJS0_9STAP Unreviewed; 613 AA. AC H0DJS0; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 17. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=SEVCU012_1027 {ECO:0000313|EMBL:EHM67152.1}; OS Staphylococcus pettenkoferi VCU012. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=904314 {ECO:0000313|EMBL:EHM67152.1}; RN [1] {ECO:0000313|EMBL:EHM67152.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=VCU012 {ECO:0000313|EMBL:EHM67152.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHM67152.1}. 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; AGUA01000094; EHM67152.1; -; Genomic_DNA. DR RefSeq; WP_002472770.1; NZ_AGUA01000094.1. DR EnsemblBacteria; EHM67152; EHM67152; SEVCU012_1027. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EHM67152.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EHM67152.1}. SQ SEQUENCE 613 AA; 68427 MW; B53212EEED3AC2AD CRC64; MDKLLHKLQT QVLVGDGAMG TILFTEGLDT CPEAYNLTHP EKIEAIHRSY IEAGADVIQT NTYGANFEKL KAFGLEHKVK HIHQAAVAIA QRAAQPETII LGTVGGFRSV TQEDLSLSTI LYHTELQIET LIQSGVDALL FETYYDLEEL TAVVKLAREM TDRPIIAQLT ASNTHYLKDS TEINRAIQHV VKCGANMVGL NCHHCPHHMQ QSFSHIDLPQ DAYLSCYPNA SLLDIENQEI RYSDNAAYFG KMAQKLINEG VRLIGGCCGT TPEHVRYIKQ AVKDLSPVTR KNVIPIKKRE TNQAIPTHKK NLTSIVKQRP SIIVELDTPK HLDTSTFFDN VQQLDQLGID AITLADNSLA TVRISNIAAA SIIKQQYKLE PLVHIACRDR NLIGLQSHLL GLSLLDITEI LTITGDPARI GNLPGATNVY DVNSRGLTEM ALRFNQGINT DGAELKQRTH FNIAGAFDPN VRRLDHAVKR AEQKIKHGTH YFITQPVYSS DKIQEIYEAT KHLETPFYIG IMPITSYNNA LFLHNEVPGI TLSEDILEQF EAVKDDAAQT KALSLKISKA LIETVHRYFN GLYLITPFQR VDLTIELAHY SQTITSTKQE ALL // ID H0E7J4_9ACTN Unreviewed; 1210 AA. AC H0E7J4; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 01-APR-2015, entry version 21. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EHN10365.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHN10365.1}; GN ORFNames=PAI11_27960 {ECO:0000313|EMBL:EHN10365.1}; OS Patulibacter medicamentivorans. OC Bacteria; Actinobacteria; Rubrobacteridae; Solirubrobacterales; OC Patulibacteraceae; Patulibacter. OX NCBI_TaxID=1097667 {ECO:0000313|EMBL:EHN10365.1}; RN [1] {ECO:0000313|EMBL:EHN10365.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=I11 {ECO:0000313|EMBL:EHN10365.1}; RX PubMed=23212173; DOI=10.1007/s10532-012-9610-5; RA Almeida B., Kjeldal H., Lolas I., Knudsen A.D., Carvalho G., RA Nielsen K.L., Barreto Crespo M.T., Stensballe A., Nielsen J.L.; RT "Quantitative proteomic analysis of ibuprofen-degrading Patulibacter RT sp. strain I11."; RL Biodegradation 24:615-630(2013). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHN10365.1}. 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; AGUD01000225; EHN10365.1; -; Genomic_DNA. DR RefSeq; WP_007576300.1; NZ_AGUD01000225.1. DR EnsemblBacteria; EHN10365; EHN10365; PAI11_27960. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHN10365.1}; KW Transferase {ECO:0000313|EMBL:EHN10365.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 225 225 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 292 292 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 735 735 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1210 AA; 131798 MW; 14E86D869971EE7B CRC64; MAERDYLAAV REGVVVFDGS MGALLEEKNL SLEEDYRLPG RAHEVLVLNR PDVIEELHTT MLDAGAVVLE TDSFQASRLK LDEWGLADHT LEINVRAAEI ARKAAGPDRF VAGSIGPTGF LPSSDDPTLG NILFPELVTV FEEQSRGLIQ GGADLLIIET AQDILEVKAA IFGAREAFKA TGRRVPLQIS VSLLPNGGKM LLGTDVAAVV TTLEALKVDV IGLNCSTGPE DMRDAIRYLG ENASVPVHCI PNAGIPQQGV NGETVFPEKP QPLADALGEF VDDYGVAIVG GCCGTTPEHI SAIAERVARK PAGRTANAGT VDRRIQVSSM IGAADLVQEP RPTIVGERVN SQGSRKAKEL LLADDYDSLV TIAEGQVEGG AHVLDVCVAL TERSDEAEQM RQVVKKISLT QPAPIQIDST EPDVIKVALE QIPGRAIVNS VNLEAGRDKM DVVVPLALEH GAAVIALTID EIGMGKTVER KLEIAERIKQ IACDEHGLEP EALIFDLLTF TLTTGDEEWR DSAVQTIEAI RAIGDRLPGV KTSLGVSNVS FGVGLAARSV LNSVFLYHCV EAGLDLAMVN PAHIIPMGEI DPTERQLAED LVWNRREDAL ELFINHFESK GPGEETAEKA DPTAEMEPEE ALHFRILKRK KDGVEADIDR AVEKLGAVPV LNDVLLPAMK EVGDKFGAGE LILPFVLQSA EVMKKAVKQL ENYLERTADY TKGTVVLATV FGDVHDIGKS LVNTILSNNG YTVVDLGKQV PVGTILEAAK EHDATAIGLS ALLVSTSKQM PLAVQELHRE GLKYPVLVGG AAINRNFSYR ALHPNGLDDD TVYEGGVFYC KDAFEGLGVM DRMVDDEAHP QMLEEIKAGA IKLRDAAKED ENLPPVTDTS VRSPVATDAP VPEPPFWGVQ EVPVDMDELY HHLDTHVLFK LHWGGKGIKG DAWRKLVEGD PTDEDAGEGF RHKLERMWRE QTYLHPRALI GFFPCYADGN EIVVLDPEDR TTEINRFVTP RQQKGDRMAT SDFFRPGVKQ EDGTVVAPEQ LDVIAVQALT VGDEVTQLMA KLEAEGEYAE QLFVHGLGVQ TAEGLSEWLH WKVRNWFGIP VTQGRRLSWG YPAIPDQSEH EKVKELLDIS RIGLDLTDGY SPTPEQSTLA MIVHHPQAVY YGMRNGRFLQ DGSPDDVIKD SERDPTRIEA DFLESEVDDA EAVEAEGAAA // ID H0F318_9BURK Unreviewed; 1261 AA. AC H0F318; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EHK67314.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHK67314.1}; GN Name=metH {ECO:0000313|EMBL:EHK67314.1}; GN ORFNames=KYC_05786 {ECO:0000313|EMBL:EHK67314.1}; OS Achromobacter arsenitoxydans SY8. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Achromobacter. OX NCBI_TaxID=477184 {ECO:0000313|EMBL:EHK67314.1}; RN [1] {ECO:0000313|EMBL:EHK67314.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SY8 {ECO:0000313|EMBL:EHK67314.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHK67314.1}. 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; AGUF01000027; EHK67314.1; -; Genomic_DNA. DR RefSeq; WP_008159817.1; NZ_AGUF01000027.1. DR EnsemblBacteria; EHK67314; EHK67314; KYC_05786. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHK67314.1}; KW Transferase {ECO:0000313|EMBL:EHK67314.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 260 260 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 325 325 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 326 326 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 793 793 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1261 AA; 139181 MW; 650514A9B295BC70 CRC64; MDLIVSYPRL PYPPEAYTQG GEFARLLGKR ILILDGAMGT MIQRYKLGEA DFRGERFKDH GKDVKGNNEL LSLVRPDVIS EIHRQYLEAG ADVIETNTFG ATTIAQGDYD LPELAYELNL VSAKLAREAC DAYSTPDKPR FVAGALGPQP KTASISPDVN DPGARNVTFD ELRVAYIEQL NGLLDGGIDI VLIETIFDTL NAKAAIFATE EVFEQRGIRL PVMISGTVTD ASGRILSGQT VEAFWNSVRH ARPVTIGLNC ALGAALMRPY VAELSKICDT YVCVYPNAGL PNPMAETGFD ETPADTSALL EEFARAGLVN MSGGCCGTTP DHIRAIAEKV TALTPRVVPD IPVKTRLSGL EALNIDEDTL YVNVGERTNV TGSKMFARLI REEKYDEALA VARQQVENGA QIIDINMDEA MLDSVACMHR FLNLIASEPD IARVPVMIDS SKWDVIETGL KCVQGKAVVN SISMKEGLEP FRHHARLCRR YGAAVVVMAF DEQGQADTLE RRKEICGRAY KILVEEEGFP PEDIIFDPNV FAVATGIDEH NHYAVDFIEG TRWIRENLPY ARISGGVSNV SFSFRGNEPM REAIHTVFLY YAVKEGMTMG IVNAGQLGVY ADLDPKLRDL VEDVVLDRAN PVGKTEADDE RTPTERLVQF ADTVKGTGAK KEEDLAWRNA EVEQRLSHAL VHGITAFIVE DTEEVRQKIA ARGGRPIEVI EGPLMDGMNV VGDLFGEGKM FLPQVVKSAR VMKQAVAHLI PFIEEEKRQI AAAGGDVRAK GKIVIATVKG DVHDIGKNIV SVVLQCNNFE VVNMGVMVPC AQILEKAKEE NADIVGLSGL ITPSLEEMAY VASEMQRDEY FRSRKVPLMI GGATTSRVHT AVKIAPNYEG PVIYVPDASR SVGVATSLMS DQSEAYLAEL TQEYEDVRRR HANRKAAPIL PLAEARASRP AIDWDSYTPP RPKFIGRRTF KSYDLAEIAK YVDWGPFFQT WSLFGPFPAI LEDKVVGEQA RKVYADGQAM MKRIVEGRWL SANGVVGFYP ANSVNDEDIE VYKDETRSEV LFTYRNLRQQ GAKREGVSNK SLSDFIAPKS SGKLDYIGMF AVTAGLGIEK KEAEFEKALD DYSSIMLKSL ADRLAEAFAE CLHARVRQDL WGYAPDEALS NDDMIAEKYV GIRPAPGYPA CPEHVVKTDM FRVLDGEDIG MMLTDSYAMY PASSVSGFYF SHPQSQYFNV GIIGEDQLED YARRSGRSIE DLKRTLAPNL G // ID H0FZ62_RHIML Unreviewed; 1256 AA. AC H0FZ62; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EHK77742.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHK77742.1}; GN Name=metH {ECO:0000313|EMBL:EHK77742.1}; GN ORFNames=SM0020_12480 {ECO:0000313|EMBL:EHK77742.1}; OS Sinorhizobium meliloti CCNWSX0020. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=1107881 {ECO:0000313|EMBL:EHK77742.1}; RN [1] {ECO:0000313|EMBL:EHK77742.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCNWSX0020 {ECO:0000313|EMBL:EHK77742.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AGVV01000019; EHK77742.1; -; Genomic_DNA. DR RefSeq; WP_004435239.1; NZ_AGVV01000019.1. DR EnsemblBacteria; EHK77742; EHK77742; SM0020_12480. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHK77742.1}; KW Transferase {ECO:0000313|EMBL:EHK77742.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 261 261 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 325 325 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 778 778 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1256 AA; 137990 MW; 8A299818EB468E46 CRC64; MSADALFGNV SPKPDGSEVL RQLAQAAAER ILIMDGAMGT EIQQLGFVED HFRGERFGGC ACHQQGNNDL LTLTQPKAIE DIHYHYAIAG ADILETNTFS STRIAQADYG MEDMVYDLNR DGARLARRAA KRAEAEDGRR RFVAGALGPT NRTASISPDV NNPGYRAFSF DDLRLAYAEQ VRGLIDGGAD IILIETIFDT LNAKAAIFAT QEVFAEKGVR LPVMISGTIT DLSGRTLSGQ TPTAFWYSVR HADPFTIGLN CALGANAMRA HIDELSAVAD TLVCAYPNAG LPNEFGRYDE SPEQMAAQVE GFARDGLVNI VGGCCGSTPA HIRAIAEAVA KYPPRRVPEI DRRMRLSGLE PFTLTDEIPF VNVGERTNVT GSAKFRKLIT AGDYAAALDV ARDQVANGAQ IIDVNMDEGL IDSKQVMVEF LNLVASEPDI ARVPVMIDSS KWEVIEAGLK CVQGKALVNS ISLKEGEAAF LHHARLVRAY GAAVVVMAFD EKGQADTKTR KVEICRRAYR LLTEEVGFPP EDIIFDPNIF AVATGIEEHN NYGVDFIEAT HEIIAALPHV HVSGGVSNLS FSFRGNEPVR EAMHAIFLYH AIQAGMDMGI VNAGQLAVYD AIDPELREAC EDVVLNRRAD STERLLEIAE RYRGKGGSQG KEKDLAWREW PVEKRLEHAL VNGITEFIEA DTEEARLAAE RPLHVIEGPL MAGMNVVGDL FGSGKMFLPQ VVKSARVMKQ AVAVLLPHME EEKRANGGGE ARESAGKILM ATVKGDVHDI GKNIVGVVLA CNNYEIIDLG VMVPSAKILE VAREQKVDIV GLSGLITPSL DEMAHVASEL EREGFDVPLL IGGATTSRVH TAVKINPRYS LGQTVYVTDA SRAVGVVSSL LSPEVRDSYK KTVRAEYLKV ADAHARNEAE KRRLPLSQAR ANAFRIDWDA HQPKVPSFLG TRVFEGWDLA ELARYIDWTP FFQTWELKGV FPKILDDERQ GAAARQLFED AQAMVEKIVA EAWFAPKAVI GFWPAASMGD DVRLFADEVR EAELATFFTL RQQMVKRDGR PNVALADFVA PAASGKRDYV GGFVVTAGIE EVAIAERFER ANDDYSSIMV KALADRFAEA FAERMHEYVR KELWGYAPDE AFTPQELIAE PYAGIRPAPG YPAQPDHTEK ETLFRLLDAE AAIGVRLTES YAMWPGSSVS GLYVGHPDSY YFGVAKIERD QVEDYADRKR MSVREVERWL SPILNYVPMP ETEAAE // ID H0G284_RHIML Unreviewed; 337 AA. AC H0G284; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Methionine synthase I {ECO:0000313|EMBL:EHK76575.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHK76575.1}; GN ORFNames=SM0020_17872 {ECO:0000313|EMBL:EHK76575.1}; OS Sinorhizobium meliloti CCNWSX0020. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=1107881 {ECO:0000313|EMBL:EHK76575.1}; RN [1] {ECO:0000313|EMBL:EHK76575.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCNWSX0020 {ECO:0000313|EMBL:EHK76575.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGVV01000035; EHK76575.1; -; Genomic_DNA. DR RefSeq; WP_003530700.1; NZ_AGVV01000035.1. DR ProteinModelPortal; H0G284; -. DR EnsemblBacteria; EHK76575; EHK76575; SM0020_17872. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EHK76575.1}; KW Transferase {ECO:0000313|EMBL:EHK76575.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 215 215 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 281 281 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 282 282 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 337 AA; 35069 MW; 121A703F6038BDD7 CRC64; MSVAAHALSD LLAQKGVLLA DGATGTSLFA MGLEAGEAPE IWNETKPDNI TKLHQDFVDA GADIILTNSF GGTRHRLKLH QAEDRVHQLN KRAAEIARAV ADKAPRKVIT AGSVGPTGEL LIPLGALSYE DAVAAFVEQI EGLKAGGAEV AWIETMSSPD EIRAAAEAAA KVGLPYVYTG SFDTAGKTMM GLHPKDIHGV AADIGEGPVA VGANCGVGAS DILSSLLDMT AASPEATIVV KGNCGIPEFR GSEIHYSGTP PLMAEYARLA VDAGAKIIGG CCGTSCNHLA AMRLAIDNHT RGERPTLETI VEKIGPLRNK SANEGPAAPA RERRRRA // ID H0GJS9_SACCK Unreviewed; 324 AA. AC H0GJS9; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Mht1p {ECO:0000313|EMBL:EHN05765.1}; GN ORFNames=VIN7_3103 {ECO:0000313|EMBL:EHN05765.1}; OS Saccharomyces cerevisiae x Saccharomyces kudriavzevii (strain VIN7) OS (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=1095631 {ECO:0000313|EMBL:EHN05765.1, ECO:0000313|Proteomes:UP000009009}; RN [1] {ECO:0000313|EMBL:EHN05765.1, ECO:0000313|Proteomes:UP000009009} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VIN7 {ECO:0000313|EMBL:EHN05765.1}; 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. 12:88-96(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. {ECO:0000313|EMBL:EHN05765.1}. 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; AGVY01000040; EHN05765.1; -; Genomic_DNA. DR PhylomeDB; H0GJS9; -. DR Proteomes; UP000009009; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009009}. SQ SEQUENCE 324 AA; 36753 MW; A62C3C9DF4D16F14 CRC64; MKRIPIKELI VEHPGKVLIL DGGQGTELEN RGININSPVW SAAPFTSESF WEPSSRERKV VEEMYRDFMI AGANILMTIT YQANFQSISE NTSIKTLAAY KRFLDKIVSF TREFIGEERY LIGSIGPWAA HVSCEYTGDY GPHPENIDYY GFFKPQLENF NQNRDIDLIG FETIPNFHEL KAILSWDEDI ISKPFYIGLS VDDNSLLRDG TTLEEISVHI KGLGNKINKN LLLMGVNCVS FNQSALILKM LHEHLPGMPL LVYPNSGEIY NPKEKTWHRP TNKLDDWETX VKKFVDNGAR IIGGCCRTSP KDIAEIASAV DKYS // ID H0GLL1_SACCK Unreviewed; 207 AA. AC H0GLL1; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Sam4p {ECO:0000313|EMBL:EHN05540.1}; GN ORFNames=VIN7_3954 {ECO:0000313|EMBL:EHN05540.1}; OS Saccharomyces cerevisiae x Saccharomyces kudriavzevii (strain VIN7) OS (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=1095631 {ECO:0000313|EMBL:EHN05540.1, ECO:0000313|Proteomes:UP000009009}; RN [1] {ECO:0000313|EMBL:EHN05540.1, ECO:0000313|Proteomes:UP000009009} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VIN7 {ECO:0000313|EMBL:EHN05540.1}; 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. 12:88-96(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. {ECO:0000313|EMBL:EHN05540.1}. 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; AGVY01000042; EHN05540.1; -; Genomic_DNA. DR PhylomeDB; H0GLL1; -. DR Proteomes; UP000009009; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009009}. SQ SEQUENCE 207 AA; 23579 MW; 700E1A13CBC23AD0 CRC64; MARLPLKQFL ADNPKKVLVL DGGQGTELEN RGIKVANPVW STIPFISESF WSDESSANRK IVKEMFNDFL NAGAEILMTT TYQTSYKSVS ENTPIRTLSE YNNLLNRIVD FSRNCIGEDK YLIGCIGPWG AHICREFTGD YGAEPENIDF YQYFKPQLEN FNKNDKLDLI GFETIPNIHE LKAILSWDES ILSRPFYIGL SVHEHGA // ID H0GXV7_SACCK Unreviewed; 178 AA. AC H0GXV7; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Mht1p {ECO:0000313|EMBL:EHN01330.1}; GN ORFNames=VIN7_8509 {ECO:0000313|EMBL:EHN01330.1}; OS Saccharomyces cerevisiae x Saccharomyces kudriavzevii (strain VIN7) OS (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=1095631 {ECO:0000313|EMBL:EHN01330.1, ECO:0000313|Proteomes:UP000009009}; RN [1] {ECO:0000313|EMBL:EHN01330.1, ECO:0000313|Proteomes:UP000009009} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VIN7 {ECO:0000313|EMBL:EHN01330.1}; 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. 12:88-96(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. {ECO:0000313|EMBL:EHN01330.1}. 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; AGVY01000298; EHN01330.1; -; Genomic_DNA. DR PhylomeDB; H0GXV7; -. DR Proteomes; UP000009009; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009009}. SQ SEQUENCE 178 AA; 20162 MW; 608A26B927E5B605 CRC64; MKRISIEKLI LEYPTRVLVL DGGQGTELEN RGINIGGPVW SATPFTSDSF WEQSSHDREV VEEMYRDFMN AGANVLMTIT YQANFKSISE NTSIQTLSAY NGFLNRIVSF TRRIIGEESY LVGSIGPWAA HVSSEYTGNY GPHPEDIDYY NFFKPQLDSF NENKDIDLIG FETASQFS // ID H0GZS8_SACCK Unreviewed; 325 AA. AC H0GZS8; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Sam4p {ECO:0000313|EMBL:EHN00688.1}; GN ORFNames=VIN7_9365 {ECO:0000313|EMBL:EHN00688.1}; OS Saccharomyces cerevisiae x Saccharomyces kudriavzevii (strain VIN7) OS (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=1095631 {ECO:0000313|EMBL:EHN00688.1, ECO:0000313|Proteomes:UP000009009}; RN [1] {ECO:0000313|EMBL:EHN00688.1, ECO:0000313|Proteomes:UP000009009} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VIN7 {ECO:0000313|EMBL:EHN00688.1}; 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. 12:88-96(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. {ECO:0000313|EMBL:EHN00688.1}. 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; AGVY01000340; EHN00688.1; -; Genomic_DNA. DR PhylomeDB; H0GZS8; -. DR Proteomes; UP000009009; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009009}. SQ SEQUENCE 325 AA; 36471 MW; C1F40B5EB1389CC3 CRC64; MVRLPLKQLL EDDPKKVLVL DGGQGTELEN RGIKVANPVW STIPFISDSF WSDESSANRK IVKEMFNDFL NAGAEILMTT TYQTSYKSVS ENTPIKTLSE YNNLLTRIVD FSRDCIGENK YLIGCIGPWG AHICREFTGD YGPDPESIDF YKYFKPQLDN FNKNDKLDLI GFETIPNVHE LRAILSWDES ILSKPFYIGL SVHEHGVLRD GTTVEEVAKV IKGLGDKINP NFSLLGINCV SFNQSPDILE SLHQALPNMA LLAYPNSGEV YDTEKKIWLP NSDKLNSWDT VVKQYIGSGA RIIGGCCRTS PNDIQEISTA VKKYT // ID H0H1Q1_SACCK Unreviewed; 325 AA. AC H0H1Q1; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Sam4p {ECO:0000313|EMBL:EHN00009.1}; GN ORFNames=VIN7_10206 {ECO:0000313|EMBL:EHN00009.1}; OS Saccharomyces cerevisiae x Saccharomyces kudriavzevii (strain VIN7) OS (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=1095631 {ECO:0000313|EMBL:EHN00009.1, ECO:0000313|Proteomes:UP000009009}; RN [1] {ECO:0000313|EMBL:EHN00009.1, ECO:0000313|Proteomes:UP000009009} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VIN7 {ECO:0000313|EMBL:EHN00009.1}; 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. 12:88-96(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. {ECO:0000313|EMBL:EHN00009.1}. 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; AGVY01000374; EHN00009.1; -; Genomic_DNA. DR PhylomeDB; H0H1Q1; -. DR Proteomes; UP000009009; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009009}. SQ SEQUENCE 325 AA; 36504 MW; 03E40B505FC89221 CRC64; MVRLPLKQLL EDDPKKVLVL DGGQGTELEN RGIKVANPVW STIPFISDSF WSDESSANRK IVKEMFNDFL NAGAEILMTT TYQTSYKSVS ENTPIKTLSE YNNLLTRIVD FSRDCIGENK YLIGCIGPWG AHICREFTGD YGPDPESIDF YKYFKPQLDN FNKNDKLDLI GFETIPNVHE LRAILSWDES ILSKPFYIGL SVHEHGVLRD GTTMEEVAKV IKGLGDKINP NFSLLGINCV SFNQSPDILE SLHQALPDMA LLAYPNSGEV YDTEKKIWLP NSDKLNSWDT VVKQYIGSGA RIIGGCCRTS PNDIQEISTA VKKYT // ID H0H7G1_RHIRD Unreviewed; 1257 AA. AC H0H7G1; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EHJ98610.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHJ98610.1}; GN Name=metH {ECO:0000313|EMBL:EHJ98610.1}; GN ORFNames=AT5A_07955 {ECO:0000313|EMBL:EHJ98610.1}; OS Agrobacterium tumefaciens 5A. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium; OC Agrobacterium tumefaciens complex. OX NCBI_TaxID=1107544 {ECO:0000313|EMBL:EHJ98610.1}; RN [1] {ECO:0000313|EMBL:EHJ98610.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=5A {ECO:0000313|EMBL:EHJ98610.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHJ98610.1}. 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; AGVZ01000003; EHJ98610.1; -; Genomic_DNA. DR RefSeq; WP_003513341.1; NZ_AGVZ01000003.1. DR EnsemblBacteria; EHJ98610; EHJ98610; AT5A_07955. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHJ98610.1}; KW Transferase {ECO:0000313|EMBL:EHJ98610.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 260 260 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 776 776 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1257 AA; 138744 MW; 6565DD7978EEF1FB CRC64; MFDDLFGPEG AKRDGAEILR ALRQAASERI LILDGAMGTQ IQGLGFDEDH FRGDRFIGCA CHQQGNNDLL ILTQPDAIEE IHYRYAMAGA DILETNTFSS TRIAQADYEM ENAVYDLNRE GAQIVRRAAQ RAEREDGRRR FVAGAIGPTN RTASISPDVN NPGYRAVSFD DLRIAYGEQI DGLIDGGADI ILIETIFDTL NAKAAIFACE ERFEAKGIRL PVMISGTITD LSGRTLSGQT PSAFWNSVRH ANPFTIGLNC ALGADAMRPH LQELSDVADT FVCAYPNAGL PNEFGQYDET PEMMARQVQG FARDGLVNIV GGCCGSTPEH IRAIAEAVKD YKPRPIPEHK PFMSLSGLEP FVLTKDIPFV NVGERTNVTG SARFRKLITA GDYTAALAVA RDQVENGAQI IDINMDEGLI DSQKAMVEFL NLIAAEPDIA RVPVMIDSSK FEIIEAGLKC VQGKSIVNSI SLKEGEEKFL QQARLVHNYG AAVVVMAFDE VGQADTYQRK VEICTRAYML LTEKAGLSPE DIIFDPNVFA VATGIEEHNN YGVDFIEATK TIRETMPLTH ISGGVSNLSF SFRGNEPVRE AMHAVFLYHA IQVGMDMGIV NAGQLAVYDN IDAELREACE DVVLNRRDDA TERLLDVAER FRGTGEKQAK VQDLSWRELS VEKRLQHALV NGITEFIEAD TEEARQQAAR PLHVIEGPLM AGMNVVGDLF GSGKMFLPQV VKSARVMKQA VAVLLPYMEE EKRLNGGEQN KAAGKVLMAT VKGDVHDIGK NIVGVVLACN NYEIIDLGVM VPTTKILETA IAEKVDVIGL SGLITPSLDE MVHVAAEMER QGFNIPLLIG GATTSRVHTA VKIHPRYEQG QAIYVTDASR AVGVVSALLS AEQKPAYIDG IRAEYAKVAE AHARNEREKQ RLPLSRAREN AHKIDWSTYS VVKPQFFGTK VFETYDLEEL SRYIDWTPFF QTWELKGRYP AILEDEKQGE AARQLYADAQ AMLKKIIKEK WFRPRAVIGF WPANAVGDDI RLFTDENRSE ELATFFTLRQ QLSKRDGRPN VALSDFVAPV DSGVADYVGG FVVTAGIEEV AIAERFERAN DDYSSILVKA LADRFAEAFA ERMHERVRKE FWGYAPEEAL AGDELIGEAY AGIRPAPGYP AQPDHTEKKT LFSLLDATNA AGVELTESYA MWPGSSVSGL YIGHPESYYF GVAKVERDQV LDYARRKDMP LVEVERWLGP VLNYVPVNGA EEIDSAA // ID H0H864_RHIRD Unreviewed; 304 AA. AC H0H864; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=S-methyltransferase {ECO:0000313|EMBL:EHJ98863.1}; GN ORFNames=AT5A_09220 {ECO:0000313|EMBL:EHJ98863.1}; OS Agrobacterium tumefaciens 5A. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium; OC Agrobacterium tumefaciens complex. OX NCBI_TaxID=1107544 {ECO:0000313|EMBL:EHJ98863.1}; RN [1] {ECO:0000313|EMBL:EHJ98863.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=5A {ECO:0000313|EMBL:EHJ98863.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHJ98863.1}. 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; AGVZ01000003; EHJ98863.1; -; Genomic_DNA. DR RefSeq; WP_003513818.1; NZ_AGVZ01000003.1. DR EnsemblBacteria; EHJ98863; EHJ98863; AT5A_09220. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EHJ98863.1}; KW Transferase {ECO:0000313|EMBL:EHJ98863.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 304 AA; 31931 MW; 71AF2FDE848F29C1 CRC64; MGTIRILDGG MSRELQRLGA ELKQPEWSAL ALINSPDIVR QVHQEFIEAG ADVVTTNSYA LVPFHIGEER FQKDGASLIA LSGRLAREAA DASGRDVLVA GSLPPIFGSY EPQNFDETRV QDYLKVLVDN LGPFVDVWLG ETLSLIAEGE AVREAVAATG KPFWISFTLN DDAAATGGGE PALRSGETVK AAAEWAAQSG AAALLFNCSK PEIMKAAVET ASAVFAEKGV SLEIGVYANA FEGEQGDSAA NEGLHGTRTD LTDDVYSRFA CSWADAGATM IGGCCGIGAA HIHTVATALR RAAA // ID H0HJZ8_9RHIZ Unreviewed; 267 AA. AC H0HJZ8; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 12. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EHK58969.1}; DE Flags: Fragment; GN ORFNames=MAXJ12_02266 {ECO:0000313|EMBL:EHK58969.1}; OS Mesorhizobium alhagi CCNWXJ12-2. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=1107882 {ECO:0000313|EMBL:EHK58969.1}; RN [1] {ECO:0000313|EMBL:EHK58969.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCNWXJ12-2 {ECO:0000313|EMBL:EHK58969.1}; 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHAM01000022; EHK58969.1; -; Genomic_DNA. DR RefSeq; WP_008834110.1; NZ_AHAM01000022.1. DR EnsemblBacteria; EHK58969; EHK58969; MAXJ12_02266. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHK58969.1}; KW Transferase {ECO:0000313|EMBL:EHK58969.1}. FT NON_TER 267 267 {ECO:0000313|EMBL:EHK58969.1}. SQ SEQUENCE 267 AA; 29120 MW; E348407BD005321C CRC64; MAKYRQNLPQ LANRTFLSDG GMETTLIFHE GIDLPHFASF PLIATLEGRQ QLKEYYVRYL TIARQSGTGF ILDTPTWRAN PDWGKLLGYG PEALRAVNED SIALLLELRQ EFETPETPCV ISGAIGPRGD GYKAGRMEAG EAQAYHAAQV ESFARTDADM VAAYTMNTVE EAIGIASAAK AARMPCMVSF TVETDGRLAT GTALGEAIER VDDATGGSPA YYMINCAHPT HFMQALKKGE KWLDRVYGVK ANASAKSHAE LDESTTL // ID H0HJZ9_9RHIZ Unreviewed; 41 AA. AC H0HJZ9; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 12. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EHK58939.1}; DE Flags: Fragment; GN ORFNames=MAXJ12_02271 {ECO:0000313|EMBL:EHK58939.1}; OS Mesorhizobium alhagi CCNWXJ12-2. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=1107882 {ECO:0000313|EMBL:EHK58939.1}; RN [1] {ECO:0000313|EMBL:EHK58939.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCNWXJ12-2 {ECO:0000313|EMBL:EHK58939.1}; 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHAM01000023; EHK58939.1; -; Genomic_DNA. DR RefSeq; WP_008834111.1; NZ_AHAM01000023.1. DR EnsemblBacteria; EHK58939; EHK58939; MAXJ12_02271. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHK58939.1}; KW Transferase {ECO:0000313|EMBL:EHK58939.1}. FT NON_TER 1 1 {ECO:0000313|EMBL:EHK58939.1}. SQ SEQUENCE 41 AA; 4360 MW; E80637276A7685F2 CRC64; LGRRYSGLRA SFPTMRILGG CCGTDHRHIA AICEACVPQA A // ID H0HSY0_9RHIZ Unreviewed; 340 AA. AC H0HSY0; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=Methionine synthase I {ECO:0000313|EMBL:EHK56206.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHK56206.1}; GN ORFNames=MAXJ12_16356 {ECO:0000313|EMBL:EHK56206.1}; OS Mesorhizobium alhagi CCNWXJ12-2. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=1107882 {ECO:0000313|EMBL:EHK56206.1}; RN [1] {ECO:0000313|EMBL:EHK56206.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCNWXJ12-2 {ECO:0000313|EMBL:EHK56206.1}; 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHAM01000133; EHK56206.1; -; Genomic_DNA. DR RefSeq; WP_008836890.1; NZ_AHAM01000133.1. DR EnsemblBacteria; EHK56206; EHK56206; MAXJ12_16356. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHK56206.1}; KW Transferase {ECO:0000313|EMBL:EHK56206.1}. SQ SEQUENCE 340 AA; 35729 MW; BA3EBE9AB4A06826 CRC64; MTNPIDALLA EKGVLLADGA TGTNLFGMGL EAGEAPELWN ETAPEKITAL HQNFVDAGAD IILTNSFGGT RHRLKLHHAQ DRVHELNKRA AEIARSVADR AGRKVIVAGS VGPTGELLQP LGAMTYDEAV DAFAEQIRGL KEGGAEVAWI ETMSAPDEAK AAAQAAIDAG LPYTYTVSFD TAGRSMMGLA PKDIHGVTEG LPEKPVAVGA NCGVGASDIL SSLLDMTGAK PEATVIVKGN CGIPEFRGTE IHYSGTPELM ADYVRLAVDG GAKIVGGCCG TSFQHLAAMR HALDAHRKSA RPTVETIVER IGPMRNKQAS QSGGTGETSD ARRERRRARA // ID H0HX96_9RHIZ Unreviewed; 1265 AA. AC H0HX96; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EHK54693.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHK54693.1}; GN Name=metH {ECO:0000313|EMBL:EHK54693.1}; GN ORFNames=MAXJ12_24077 {ECO:0000313|EMBL:EHK54693.1}; OS Mesorhizobium alhagi CCNWXJ12-2. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=1107882 {ECO:0000313|EMBL:EHK54693.1}; RN [1] {ECO:0000313|EMBL:EHK54693.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCNWXJ12-2 {ECO:0000313|EMBL:EHK54693.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AHAM01000204; EHK54693.1; -; Genomic_DNA. DR RefSeq; WP_008838403.1; NZ_AHAM01000204.1. DR EnsemblBacteria; EHK54693; EHK54693; MAXJ12_24077. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHK54693.1}; KW Transferase {ECO:0000313|EMBL:EHK54693.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 262 262 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 325 325 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 326 326 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 787 787 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1265 AA; 138781 MW; 5B66A8F3A0FDA822 CRC64; MSSVDELFGP VAAKSDGSEL LAALRSAARE RILFLDGAMG TQIQGLGFHE DQFRGDRFLG CSCHQQGNND LLILTQPQAI EDIHYAYAKA GADIIETNTF SSTRIAQADY GMEDMVYELN RDGARLVRRA AIRAQQEDGR RRFVGGALGP TNRTASMSPD VNNPGFRAIT FDELRLAYGE QLRGLIDGGA DIILIETIFD TLNAKAAIFA AEEIFAEKGV WLPVMISGTI TDLSGRTLSG QTPTAFWHSV RHAKPFTVGL NCALGAAAMR PHLAELSGVA DTFICAYPNA GLPNAFGQYD ESPEFMASQV EDFAREGLVN VIGGCCGSTP DHIAAIAEAV SRHKPRSVPK VKTLMRLSGL EPFTLTKDIP FVNVGERTNV TGSAKFRKLI TAADYAAALD VARDQVANGA QIIDVNMDEG LIDSKKAMVE YLNLIAAEPD IARVPVMIDS SKWEVIEAGL KCVQGKPVVN SISMKEGEEA FLHHAKLCRM YGAAVVVMAF DQQGQADTKA RKVEICTRAY KLLTEQAGFA PEDIIFDPNV FAVATGIEEH DNYGVDFIEA TGEITSTLPH VHISGGVSNL SFSFRGNEPV REAMHAVFLY HAIQRGMDMG IVNAGQLAVY DTIEPELREA CEDVVLNRTP KAGATATERM LEIAERFKGT AGQEAKERDL AWRDWPVEKR ISHALVNGIT EFIDADTDEA RLEAERPLHV IEGPLMAGMN VVGDLFGAGK MFLPQVVKSA RVMKQAVAGL LPHMEAEKLA NAANGIDNGE RKTAGKILMA TVKGDVHDIG KNIVGVVLAC NNYEIIDLGV MVPATKILQT AKDEKVDIVG LSGLITPSLD EMVHVASEME REGFDIPLLI GGATTSRVHT AVKIHPRYAR GQAVHVNDAS RAVGVVSALL SKDARNGYIE TVRAEYKKVT EAHHRSEADK LRLPLARARA NAHKIDWANY EPPKPSFFST RVFEDWDLEE LARYIDWTPF FQAWELKGRY PKLLEDEKQG PAARQLFEDA QAMLRKIIDE KWFAPKAVIG FWPANAVGDD IRLFTDETRA QELATFFTLR QQLTKRDGKP NVALSDFVAP VESGKPDYVG GFVVTAGIEE IAIAKRFERA NDDYNSILVK ALADRFAEAL AERLHERVRR EFWGYAPGES LSPDELIGEP YQGIRPAPGY PAQPDHTEKV TLFRLLEAEK NAGVSLTESM AMWPGSSVSG IYLSHLDSYY FGVAKVERDQ VEGYAARKRM PVDEVERWLG PILNYVPANF AEAAE // ID H0IN76_MYCAB Unreviewed; 1256 AA. AC H0IN76; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EHM21250.1}; GN ORFNames=MBOL_19390 {ECO:0000313|EMBL:EHM21250.1}; OS Mycobacterium abscessus subsp. bolletii BD. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium abscessus. OX NCBI_TaxID=1091046 {ECO:0000313|EMBL:EHM21250.1}; RN [1] {ECO:0000313|EMBL:EHM21250.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BD {ECO:0000313|EMBL:EHM21250.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHM21250.1}. 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; AHAS01000008; EHM21250.1; -; Genomic_DNA. DR RefSeq; WP_005075018.1; NZ_AHAS01000008.1. DR EnsemblBacteria; EHM21250; EHM21250; MBOL_19390. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 255 255 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 318 318 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 319 319 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 782 782 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1256 AA; 137550 MW; 92D2A3C4441A2CE7 CRC64; MHVTNLQPNV RPDCTEALTA ALEQRILVID GAMGTAIQRD RPDEAGYRGE RFADWPSDLV GNNDLLTLTQ PHIIEGIHRE YLEAGADILE TNTFNANAVS LSDYGMEELS YELNYAGAAL ARVAADEYST PAKPRYVAGA LGPTTRTASI SPDVNDPGAR NVSYDQLVAA YLEAAHGLVD GGADIILVET IFDSLNAKAA VFAIETLFEQ RGRRWPIIIS GTITDASGRT LSGQVTEAFW NAIRHARPIA VGLNCALGAP EMRPYIAEMS RIADTFVSCY PNAGLPNAFG EYDESPEHQA GYLAEFAEAG LVNLVGGCCG TAPAHIAEIA KVVEGVKPRD VPSIDVATRL SGLEPLNITD DSLFVNIGER TNITGSARFR NLIKAEDYDT ALSVALQQVE VGAQVIDINM DEGMIDGVAA MDRFTKLIAA EPDISRVPVM IDSSKWEVIE AGLKNVQGKP IVNSISMKEG EEKFIREARL CRKYGAAVVV MAFDEKGQAD NLERRKEICG RAYRILTEEV GFPAEDIIFD PNCFALATGI EEHATYGIDF IEACAWIKEN LPGVHISGGI SNVSFSFRGN NPVREAIHAV FLFHAIKAGL DMGIVNAGAL VPYDSIDSEL RDRIEDVVLN RRADAAERLL EIAERFNSTE NSGGGDDRAA QEWRSLPVRE RITHALVKGI DAHVDDDTEE LRAEIAAAGG RPIEVIEGPL MDGMNVVGDL FGSGKMFLPQ VVKSARVMKK AVAYLLPFIE AEKEDNAGTT GDSKSKDTNG TIVMATVKGD VHDIGKNIVG VVLQCNNFEV IDLGVMVPAQ KILDAAKEHD ADIIGLSGLI TPSLDEMANF AVEMEREGLE IPLLIGGATT SRAHTAVKIS PRRKGPVVWV KDASRSVPVA AALLDDKQRP GLLEATEKDY ASLRERHAQK NERPTLTLEK ARANRTPVEW DGYTPPVPAQ GLGVREFLDY DLAEVREYID WQPFFNAWEM KGRFPDILNN PATGEAARKL YDDAQQMLDT LIKEKWLTAN GVIGFFPANA VGPGFEDIEV YTDDTRTEVL TTLHNLRQQG EHRDGIPNRS LGDYIAPKET GLRDYIGAFA VTAGLGSQDK IMEFKADLDD YSAILLESIA DRLAEAFAER MHQRVRTEFW GFQPDEQLDN EALIGEKYRG IRPAPGYPAC PEHTEKVTLF DLLDVTKRTG IELTESMAMW PGAAVSGWYF AHPQSQYFVV GRLAQDQVAD YAKRKGWTLQ EAERWLGPNL GYNPED // ID H0IXD6_9GAMM Unreviewed; 1231 AA. AC H0IXD6; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 01-APR-2015, entry version 19. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EHK62640.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHK62640.1}; GN Name=metH {ECO:0000313|EMBL:EHK62640.1}; GN ORFNames=MOY_00100 {ECO:0000313|EMBL:EHK62640.1}; OS Halomonas sp. GFAJ-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=1118153 {ECO:0000313|EMBL:EHK62640.1}; RN [1] {ECO:0000313|EMBL:EHK62640.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=GFAJ-1 {ECO:0000313|EMBL:EHK62640.1}; RA Phung L.T., Silver S., Trimble W.L., Gilbert J.; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EHK62640.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=GFAJ-1 {ECO:0000313|EMBL:EHK62640.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHK62640.1}. 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; AHBC01000001; EHK62640.1; -; Genomic_DNA. DR RefSeq; WP_009095138.1; NZ_AHBC01000001.1. DR EnsemblBacteria; EHK62640; EHK62640; MOY_00100. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHK62640.1}; KW Transferase {ECO:0000313|EMBL:EHK62640.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1231 AA; 135906 MW; 4FC3BC3F19E1A6E5 CRC64; MAASDLTASL TQRLTQRILI LDGGMGTMLQ NAELSEEDFR GDRFSDWPSD LKGNNDLLAL TCPDVVARIH RDYLEAGADI LETNTFNSTR LSQADYGMEE LVPELNRESA RLAREVCDAV AAETDIPRYV AGVLGPTSRT ASLSPDVNDP AKRNVTFDEL RENYYEAASC LIEGGADLIM IETIFDTLNA KAAIYALEEL FDDLGRRLPV MISGTITDAS GRTLSGQTTE AFWNSVRHAQ PLSVGLNCAL GAEELRPYIE ELSTKANTFV SAHPNAGLPN EFGEYDQTPE EMAAIVSEFA ASGLVNIIGG CCGSTPEHIR AIADAVRPMT PRQVPKRDHA CRLSGLEPFN IQADSLFVNV GERTNVTGSA RFKRLIVEED FTTALEVALE QVENGAQIID INMDEGMLES QEAMVRFLNL IAGEPDIARV PIMIDSSKWD IIEAGLKCVQ GKAVVNSISL KEGEAAFREQ ATKCRRFGAA IVVMAFDEEG QADTFARKTE ICERAYRLLV DDIGFPAEDI IFDPNIFAIA TGIDEHNNYA VDFIEATQWI RDNLPHAMIS GGVSNVSFSF RGNNPVREAI HSVFLYHAIR AGLSMGIVNA GQLAVYDDLP AELRDAVEDV VLNRRSDGTE RLLELADKYK GDGSSAAKKE DLEWRSGPVN KRIEHALVKG VTAFIEEDTE QARAEAARPI EVIEGPLMDG MNVVGDLFGA GKMFLPQVVK SARVMKQAVA YLIPYIEAEK SEETQAKGKI VMATVKGDVH DIGKNIVGVV LQCNNYEVID LGVMVPTEKI LQAAIDHNAD IIGLSGLITP SLDEMVHVAK EMQRRGMSLP LLIGGATTSK AHTAVKIEPQ YEHPVIYVTD ASRAVGVAGK LLAPNLKPAY VAEIREEYEK VRERNAKRRP KAADLDYTQA RKRRFRTDWN TLTPAKPNTL GLITFDDYDL EELVERIDWT PFFMSWQLAG KYPKILEDDI VGEAARNLFA DAKVMLRKLI DEKRVQARGV IGLWPANSVD DDVIEVYADE SRTEVVEHLH HIRQQTTKGR DGICYSLADF IAPKESGKAD WIGGFAVTTG HGVDELSKAY EAAGDDYNAI LVQALTDRLA EAFAERMHER VRKEFWGYVP EESLDNDALI AEKYQGIRPA PGYPACPDHT EKATLFRLLN APENTGLTLT ENFAMWPAAA VSGWYFAHPQ SKYFSTGKIT RDQVEAIAER KQMPLAEMER WLSPVLSYDP S // ID H0J099_9GAMM Unreviewed; 302 AA. AC H0J099; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EHK61615.1}; GN ORFNames=MOY_05255 {ECO:0000313|EMBL:EHK61615.1}; OS Halomonas sp. GFAJ-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=1118153 {ECO:0000313|EMBL:EHK61615.1}; RN [1] {ECO:0000313|EMBL:EHK61615.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=GFAJ-1 {ECO:0000313|EMBL:EHK61615.1}; RA Phung L.T., Silver S., Trimble W.L., Gilbert J.; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EHK61615.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=GFAJ-1 {ECO:0000313|EMBL:EHK61615.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHK61615.1}. 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; AHBC01000021; EHK61615.1; -; Genomic_DNA. DR RefSeq; WP_009097303.1; NZ_AHBC01000021.1. DR EnsemblBacteria; EHK61615; EHK61615; MOY_05255. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EHK61615.1}; KW Transferase {ECO:0000313|EMBL:EHK61615.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 206 206 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 277 277 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 278 278 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 302 AA; 31630 MW; 4AF7BFEDD93E9821 CRC64; MTDSTPSVIL LDGGMGQELR KRSRYPASPL WSAQVMLDEP HLVTAAHRDF IEAGAEVITL NNYSATPQRL ARDGDPALFA TLHGAALAAA RQAQQESGRA VLIAGCLPPL VASYHHEVVP DDETCLDSYR QLVDAQAGVD LFICETMSLA REALAATTAA AERDTRVWTA FTVDDTDGTR LRSGELLADA AEATMSAGAE KILVNCSVPE AITTAMGVLA AANIPFGGFA NGFTSIAALQ PGGTVDTLTA REDLGPQAYA DYALQWVEQG ATVVGGCCEV GPAHIAAIAT RLKNAGYTLT TP // ID H0J6R0_9PSED Unreviewed; 1236 AA. AC H0J6R0; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EHK72594.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHK72594.1}; GN Name=metH {ECO:0000313|EMBL:EHK72594.1}; GN ORFNames=PPL19_00075 {ECO:0000313|EMBL:EHK72594.1}; OS Pseudomonas psychrotolerans L19. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1112217 {ECO:0000313|EMBL:EHK72594.1}; RN [1] {ECO:0000313|EMBL:EHK72594.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=L19 {ECO:0000313|EMBL:EHK72594.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AHBD01000001; EHK72594.1; -; Genomic_DNA. DR RefSeq; WP_007158400.1; NZ_AHBD01000001.1. DR EnsemblBacteria; EHK72594; EHK72594; PPL19_00075. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHK72594.1}; KW Transferase {ECO:0000313|EMBL:EHK72594.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1236 AA; 135122 MW; 4B0B774AB5CD482E CRC64; MTDRSSRLAA LRHALAQRIL ILDGGMGTMI QSYRLDEADY RGERFADWPS DVKGNNDLLL LTQPKIIAEI EKAYLDAGAD ILETNTFNAT RVSQADYGME AITYELNLAG ARVAREVADA KTLETPDRPR FVAGVLGPTS RTCSISPDVN NPGFRNVTFD ELVENYTEAT RGLIEGGADL ILIETIFDTL NAKAAIFAVQ GVFEEVGVEL PIMISGTITD ASGRTLSGQT TEAFWNSVRH ANPISVGLNC ALGAKELRPY VEELATKADT FVSAHPNAGL PNAFGEYDES PAQMAAVVEE FAASGLLNIV GGCCGTTPAH IQAIAEAVAK HPPRQLPEIP KACRLSGLEP FTISRESLFV NVGERTNITG SAKFARLIRE ENYAEALEVA QQQVEAGAQV IDINMDEGML DSKAAMVTFL NLIASEPDIS RVPIMIDSSK WEVIEAGLKC IQGKGIVNSI SMKEGVEAFI HHAKLCKRYG AAVVVMAFDE DGQADTEARK NEICARSYDI LVNQVGFPPE DIIFDPNIFA VATGIEEHNN YAVDFINACA FIHDNLPYAL TSGGVSNVSF SFRGNNPVRE AIHSVFLYHA IQNGLTMGIV NAGQLEIYDE IPAALRERVE DVVLNRTPAG TDALLAIADD YKGGGAVKEA ETEEWRGLPV DKRLEHALVK GITTYIVEDT EECRQQCARP IEVIEGPLMS GMNVVGDLFG SGKMFLPQVV KSARVMKQAV AHLIPFIEAE KGDKPEAKGK ILMATVKGDV HDIGKNIVGV VLGCNGYDIV DLGVMVPAEK ILQTAIAEKC DIIGLSGLIT PSLDEMVHVA KEMQRQGFTL PLMIGGATTS KAHTAVKIEP QYQNDAVVYV TDASRAVGVA TQLLSKELKA GFVERTRADY VEVRERTANR SARTERLTYA KAVANKPAFN WLGYQAPTPS FTGTRVLEDI DLAVLAEYID WTPFFISWDL AGKYPRILTD EVVGEAATAL FHDAQAMLRK LIDEKLIRAR AVFGFWPANQ VRDDDLEVYG EDGQPLATLH HLRQQTIKPE GKPNLSLADF VAPKETGVTD YMGGFIVTAG IGAEELAKDY ERKGDDYNSI MVKALADRLA EACAEWLHER VRKEHWGYAA DETLDNEALI REQYKGIRPA PGYPACPDHT EKAALFKLLD PEARFNEAGR SGVFLTEHYA MFPAAAVSGW YFAHPEAQYF AVGKIDRDQV DSYTERKGQE LAVTERWLAP NLGYDN // ID H0JAW0_9PSED Unreviewed; 300 AA. AC H0JAW0; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 12. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EHK71727.1}; GN ORFNames=PPL19_08586 {ECO:0000313|EMBL:EHK71727.1}; OS Pseudomonas psychrotolerans L19. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1112217 {ECO:0000313|EMBL:EHK71727.1}; RN [1] {ECO:0000313|EMBL:EHK71727.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=L19 {ECO:0000313|EMBL:EHK71727.1}; 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHBD01000003; EHK71727.1; -; Genomic_DNA. DR RefSeq; WP_007160084.1; NZ_AHBD01000003.1. DR EnsemblBacteria; EHK71727; EHK71727; PPL19_08586. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHK71727.1}; KW Transferase {ECO:0000313|EMBL:EHK71727.1}. SQ SEQUENCE 300 AA; 31801 MW; 59E7EDA0EC58B09D CRC64; MANMNLVLLD GGMGRELQRR GAPFRQPEWS ALALSEAPEQ VEAVHRAYIE AGAQVITSNS YAVVPFHIGE ARFAAEGEAL AARAGQLARQ AVVASGQPVR VAGSLPPLFG SYRPDLFEPA RVDEVLQPLI RGLAPHVDLW LAETQSSLAE VRAIAAGLPR DGKPLWLSFT LKDEDVDETP RLRSGEPVAE AAQLAVELGA GALLFNCSQP EVMAAALDTA RATFAAAGIE IPFGAYANAF PPQPEEATAN DGLDPLRPDL DPPGYLSFAQ DWQARGASLI GGCCGIGPEH IAVLNQRLRG // ID H0JZR4_9PSEU Unreviewed; 323 AA. AC H0JZR4; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 01-OCT-2014, entry version 10. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:EHK89207.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EHK89207.1}; GN Name=mmuM {ECO:0000313|EMBL:EHK89207.1}; GN ORFNames=SZMC14600_01247 {ECO:0000313|EMBL:EHK89207.1}; OS Saccharomonospora azurea SZMC 14600. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Pseudonocardineae; Pseudonocardiaceae; Saccharomonospora. OX NCBI_TaxID=1114959 {ECO:0000313|EMBL:EHK89207.1}; RN [1] {ECO:0000313|EMBL:EHK89207.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SZMC 14600 {ECO:0000313|EMBL:EHK89207.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHK89207.1}. 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; AHBX01000043; EHK89207.1; -; Genomic_DNA. DR EnsemblBacteria; EHK89207; EHK89207; SZMC14600_01247. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHK89207.1}; KW Transferase {ECO:0000313|EMBL:EHK89207.1}. SQ SEQUENCE 323 AA; 34004 MW; 5BFE28E5739768AE CRC64; MELFGAGAWV SDGGLATELE ARGHDLSDAL WSARLLLDAP EEIVAAHRAF FDAGAVIATT ASYQASFEGF AERGIDRATA TRLLRRSVDL ARQARDDVSG DGRPRFVAAS VGPYGAALAD GSEYRGAYGL TVARLRDWHR PRLEVLAEAR PDLLAIETVP DVVEAEALVE ALAGIGVPAW LSFTVADGRT RAGQPLTEAF AVAAGSPDVA AVGVNCCAPS EVSPALACAK AVTGKPVVVY PNSGEGWDAR RRAWTGATQF SPRLAARWVA EGAHVVGGCC RVRPPTSPSW RAGCDVGRRR STTVSAAAAR RRTGVIARRR TTS // ID H0K3P9_9PSEU Unreviewed; 1184 AA. AC H0K3P9; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 01-APR-2015, entry version 20. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:EHK87796.1}; GN ORFNames=SZMC14600_08419 {ECO:0000313|EMBL:EHK87796.1}; OS Saccharomonospora azurea SZMC 14600. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Pseudonocardineae; Pseudonocardiaceae; Saccharomonospora. OX NCBI_TaxID=1114959 {ECO:0000313|EMBL:EHK87796.1}; RN [1] {ECO:0000313|EMBL:EHK87796.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SZMC 14600 {ECO:0000313|EMBL:EHK87796.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHK87796.1}. 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; AHBX01000078; EHK87796.1; -; Genomic_DNA. DR EnsemblBacteria; EHK87796; EHK87796; SZMC14600_08419. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 225 225 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 292 292 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 735 735 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1184 AA; 130413 MW; 80017D13F29C4FC4 CRC64; MIMDSRFLVE LDRRILVADG GMGTALQEFD LSLDDFDNLE GCNEVLNDTR PDVVSTVHRG FLEAGCDAIE TNTFGTNYGN FGEYGILDRI RELAEKGTTL ARRCADEYAT PEKPRFVLGS MGPGTKLPTL GHAPYHVLRD AYVENALGML DGGVDAVLVE TSQDLLQTKA AIVGAKRAMA QAGRRVPLIA QVTVEQTGTM LVGSEIGAAL TALEPLGIDL IGMNCATGPA EMSEHLRVLA DHASVPISVM PNAGLPELGP KGAVYPLRPD ELAEALATFV RDFGVRLVGG CCGTTAEHVR AVVEAVSSLP PRQREPRIQP ALSSVYQPVP FEQDASILNV GERTNANGSK KFREAMLEER YDDCVEIAKA QTREGAHVLD LCVDYVGRDG TRDMAELASR LATASTLPVM VDSTEPDVVR TGLEHLGGRC AINSVNYEDG TGPDSRYQRV LELAVEHGAA VVVTCIDEEG QARTADWKVR VAERAIEDLT TNWGLSLSSI IIDCLVFPIT TGQEEVRKDA LETIEAIRRL KQRHPGVLTT LGLSNVSFGL NPAARQVLNS VFLHECRQAG LDSAILNSSK IVPMNKIDDE AREVALDLVY DRRREGYDPL QRLMQLFEGK TASSARESRA EELAKLPLLE RLEKRIVEGE STGLEADLEA AMQQKKPIDI INENLLAGMK TVGDLFGSGQ MQLPFVLQSA EVMKTAVAYL EPHMEKTDTD GKGKLLLATV KGDVHDIGKN LVDIIVSNNG YDVVNIGIKQ PINAILEAAE ENRVDAIGMS GLLVKSTVIM KDNLQEMNAR GVATKYPVLL GGAALTRTYV ENDLDEVYQG DVHYAKDAFE GLRLMDRVMA VKRGEATEED EAERAKRAER KARRERSLRI AEKRKAEQGT EPSLDDTTRS DVDLDVDVPT PPFWGSRVVK GIAVADYLAL LDERATFLGQ WGLRGARKGE GPSYEELVES EGRPRLRAWI DDLSTRGVLA HAALVYGYFP CYSDGNDLVV LEKDEPDALE RLRFRFPRQR RDRRLCLADF FRSRQKAEET GQVDVLPVQL VTMGQPIADH ANELFARNAY RDYLEIHGLG VQLTEALAEY WHRRIREELR FSSGTPVAAE DPDDVEEYFK LGYRGARFSF GYGACPDLED RAKIVELLDA ERIGVALSEE FQLHPEQSTD AIVAHHPEAK YFNT // ID H0KCI5_AGGAC Unreviewed; 62 AA. AC H0KCI5; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 12. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EHK91525.1}; GN ORFNames=RHAA1_00791 {ECO:0000313|EMBL:EHK91525.1}; OS Aggregatibacter actinomycetemcomitans RhAA1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Aggregatibacter. OX NCBI_TaxID=1089447 {ECO:0000313|EMBL:EHK91525.1}; RN [1] {ECO:0000313|EMBL:EHK91525.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=RhAA1 {ECO:0000313|EMBL:EHK91525.1}; RX PubMed=22328766; DOI=10.1128/JB.06710-11; RA Karched M., Furgang D., Planet P.J., Desalle R., Fine D.H.; RT "Genome Sequence of Aggregatibacter actinomycetemcomitans RHAA1, RT Isolated from a Rhesus Macaque, an Old World Primate."; RL J. Bacteriol. 194:1275-1276(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; AHGR01000002; EHK91525.1; -; Genomic_DNA. DR RefSeq; WP_005576099.1; NZ_AHGR01000002.1. DR EnsemblBacteria; EHK91525; EHK91525; RHAA1_00791. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHK91525.1}; KW Transferase {ECO:0000313|EMBL:EHK91525.1}. SQ SEQUENCE 62 AA; 7203 MW; 8DD21BED6BDBC5C7 CRC64; MRKAKYVKYY DSRRCLDNIR DDLNPQQYLA WAQKWIGNDA TIVGGCYGIR PEHIAALAET LE // ID H0NEX5_SALET Unreviewed; 1227 AA. AC H0NEX5; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EHN41721.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHN41721.1}; GN Name=metH {ECO:0000313|EMBL:EHN41721.1}; GN ORFNames=SEEPO729_20941 {ECO:0000313|EMBL:EHN41721.1}; OS Salmonella enterica subsp. enterica serovar Pomona str. ATCC 10729. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=941188 {ECO:0000313|EMBL:EHN41721.1}; RN [1] {ECO:0000313|EMBL:EHN41721.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 10729 {ECO:0000313|EMBL:EHN41721.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHN41721.1}. 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; AHIA01000083; EHN41721.1; -; Genomic_DNA. DR RefSeq; WP_000095984.1; NZ_AHIA01000083.1. DR EnsemblBacteria; EHN41721; EHN41721; SEEPO729_20941. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHN41721.1}; KW Transferase {ECO:0000313|EMBL:EHN41721.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136033 MW; 6AB8BD18284D545D CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLHEEDFRGE RFADWPCDLK GNNDLLVLSK PGVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYRMESLS AEINYAAAKL ARACADEWTA RTPEKPRFVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGVDLILI ETVFDTLNAK AAVFAVKEEF EALGVDLPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPEHIAA MSRAVAGLPP RQLPDIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VESGAQIIDI NMDEGMLDAE AAMVRFLSLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVEAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRERKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLDLAEKYRG SKTDEAANAQ QAEWRSWDVK KRLEYSLVKG ITEFIEQDTE EARQQASRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EKGSSNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAREVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHARKKPR TPPVTLEAAR DNDLAFDWER YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KLLNPRGVVG LFPANRVGDD IEIYRDETRT HVLTVSHHLR QQTEKVGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAYEAQH DDYNKIMVKA IADRLAEAFA EYLHERVRKV YWGYAPNESL SNDELIRENY QGIRPAPGYP ACPEHTEKGT IWQLLDVEKH TGMKLTESFA MWPGASVSGW YFSHPESKYF AVAQIQRDQV TDYAFRKGMS VENVERWLAP NLGYDAD // ID H0Q064_9RHOO Unreviewed; 1229 AA. AC H0Q064; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 01-APR-2015, entry version 27. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:BAL26662.1}; GN Name=metH {ECO:0000313|EMBL:BAL26662.1}; GN ORFNames=AZKH_4385 {ECO:0000313|EMBL:BAL26662.1}; OS Azoarcus sp. KH32C. OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Rhodocyclaceae; Azoarcus. OX NCBI_TaxID=748247 {ECO:0000313|EMBL:BAL26662.1, ECO:0000313|Proteomes:UP000007106}; RN [1] {ECO:0000313|EMBL:BAL26662.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=KH32C {ECO:0000313|EMBL:BAL26662.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP012304; BAL26662.1; -; Genomic_DNA. DR RefSeq; WP_015437962.1; NC_020516.1. DR RefSeq; YP_007553638.1; NC_020516.1. DR EnsemblBacteria; BAL26662; BAL26662; AZKH_4385. DR KEGG; aza:AZKH_4385; -. DR KO; K00548; -. DR Proteomes; UP000007106; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007106}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007106}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 765 765 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1229 AA; 132971 MW; 5FC413E8C8642E45 CRC64; MQADRSNEIR DLLARRILIL DGAMGTMIQQ HKLGESDYRG ERFRAHPKDL KGNNDLLVLT RPEVVAGIHR AYLEAGADII ETNTFNGTRV SQAEYGLADV AYEINVAGAR LVRELCDEYT AKDPAKPRYC AGVLGPTSRT LSISPDVNDP GFRNISFDAL VDDYYDSARG LLEGGADLLL IETIFDTLNA KAAVFAVEKL FAEMDRRVPV MISGTITDAS GRTLSGQTAE AFWNSLAHAR PISFGLNCAL GAKELRQYVE DLSNVCDTHV SAHPNAGLPN PLAPTGYDET PEQLATAIRE WAAAGLVNIV GGCCGTTPAH IAAIAEAVAD IAPRKVPEVE KKLRLSGLEP FNVGADSLFV NVGERTNVTG SKAFARMILE GRFDDALAVA RQQVENGAQV IDINMDEAML DSLAAMERFL KLIASEPDIS RVPIMLDSSK WSVMEAGLKC IQGKGVVNSI SMKEGEAEFL RQARLCRQYG AAVIVMAFDE KGQADTYARK TEICKRAYDL LTGIGFPPED IIFDPNIFAI ATGIEEHDNY AVDFINAVAW IKANLPFAKT SGGVSNVSFS FRGNDPVREA IHTVFLYHAI KAGLSMGIVN AGMLGVYDDL DPALREKVED VVLNRNAGAG EALVEFAQGV KEGKAKNAGP DLAWRALSVE ERLSHALVKG ITEFVVADTE EVRAKLEAAG KPPLAVIEGP LMAGMSVVGD LFGAGKMFLP QVVKSARVMK QAVAHLIPFI EAEKLRTGAA SKGRIVMATV KGDVHDIGKN IVGVVLGCNG YEVIDLGVMV PAEKILNAAR EHGAQAIGLS GLITPSLEEM SHVAAEMQRQ GFDVPLLIGG ATTSRAHTAI KIAPHYGQPV VYVPDASRAV GVVTALLSEG GAADFKAQLA ADYDKIRAQH ANKKGVQLVS LEAARANAFR WDSVPGYVPT RPKTLGVQAL AVPLAELLEF IDWAPFFQTW DLAGSFPKIL DDELVGETAR GVFKDGQAML ERIVAEDWLE ARAVFGLFPA NRVGDDIAFY ADESRSEPLM HWHGLRQQHE RPSDKPHYCL SDFVAPKESG VADYAGAFAV TAGIGIEKKL AEFEATHDDY HAIMLKSLAD RLAEACAEWL HWRVRKEFWA YAADESLDNN ALIHEEYRGI RPAPGYPACP DHTAKGGLFA LLDATKNTGM TLTESFAMSP AAAVSGFYLA HPEARYFAIP KIGRDQLEDW AKRTGMTVGE AARWLAPIL // ID H0QHJ4_ARTGO Unreviewed; 1182 AA. AC H0QHJ4; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:GAB12295.1}; GN Name=metH {ECO:0000313|EMBL:GAB12295.1}; GN ORFNames=ARGLB_011_00190 {ECO:0000313|EMBL:GAB12295.1}; OS Arthrobacter globiformis NBRC 12137. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Micrococcaceae; Arthrobacter. OX NCBI_TaxID=1077972 {ECO:0000313|EMBL:GAB12295.1}; RN [1] {ECO:0000313|EMBL:GAB12295.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NBRC 12137 {ECO:0000313|EMBL:GAB12295.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:GAB12295.1}. 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; BAEG01000011; GAB12295.1; -; Genomic_DNA. DR RefSeq; WP_003798233.1; NZ_BAEG01000011.1. DR EnsemblBacteria; GAB12295; GAB12295; ARGLB_011_00190. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 206 206 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 272 272 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 273 273 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 736 736 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1182 AA; 128084 MW; 542429EE115A0B9B CRC64; MGTMLQGRDL SLEKDFLGLE GCNEILNDTR PDVLADIHDA YFATGIDAVE TNTFGANWSN LSDYGIDDRI EELARKGAEI ARERAEAAEK TDERMRWVLG SMGPGTKLPS LGHTSYDYLK QTFALQAEGL IDGGADAFLI ETSQDLLQTK AAVNGCKQAI VSRGVRLPIF VEVTVETTGT MLMGSEIGAA LTALEPLGVD AIGLNCATGP DEMSEHLRHL SKQSSVAIAC MPNAGLPVLG ANGAHYPLSP SELATAHEQF VREFGLGLVG GCCGTTPEHM AAVVERLAPF RASAAVTGGG RGTDGARVPT EREAGIASLY HHVPFDQESS YLAIGERTNA NGSKAFRQAM LEERWDDCVD IAREQVRVGA HLLDVCIDYV GRDGVADIKE VVSRFASAST LPLVIDSTEP PVLQAGLEHI GGRPVVNSVN YEDGDGPDSR FARIMPLVKE HGTAVIALTI DEHGQARTTE GKVAIASRLI DSLVGEWGMR VEDIIVDALT FPIATGQEET RRDAIETIEA IRQITAKYPG IHTTLGVSNV SFGLNPAARI VLNSVFLHEA VQAGLSSGII DAAKIVPLAS LPEEQRQVAL DLVWDRREYD ADGNVTYDPL ARILDLYAGV DSAALKDQRA AELAALPTGE RLQRRIIDGE GKGLEEDLDL ARSEGMTPLG IINDQLLEGM KVVGERFGAG EMQLPFVLQS AEVMKNAVAL LEPHMEKSDA SGKGTMVIAT VRGDVHDIGK NLVDIILTNN GYKVINIGIK QPIADIIAAA EEHDADVIGM SGLLVKSTVV MKENLAELQS RGLAKKWPII LGGAALTRAY VEQDLAEQFE GTVRYAKDAF EGLALMEPLV QVARGAAPDA VGLPPLKKRI HKGGAKLTVT EPEAMPGRSD VAADNPVPSP PFWGTRIVRG VALHDYAALL DERATFMGQW GLKPGRGDDG DSYEELVERE GRPRLRYWLD RILAEGMLDA SVAYGYFPVV SEGEQVVVLH HGEDHDGVLG TAGLLAPDGG SGGPIGTDRL RFDFPRQRRD RHLCLADFVR SRESGQIDVL PIQLVTAGSK IEEVTSELFA GNHYRDYYEL NGLVMQLTEA LAEFWHARIR SELGFAAEEP KDKAGYFKLD YRGARFSLGY PACPDMEDRR KVTELLRPER MGVILSDELM LHPEQSTDAF VFHHPEAKYF KV // ID H0QQM9_ARTGO Unreviewed; 319 AA. AC H0QQM9; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 11. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:GAB15130.1}; GN Name=mmuM {ECO:0000313|EMBL:GAB15130.1}; GN ORFNames=ARGLB_083_00160 {ECO:0000313|EMBL:GAB15130.1}; OS Arthrobacter globiformis NBRC 12137. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Micrococcaceae; Arthrobacter. OX NCBI_TaxID=1077972 {ECO:0000313|EMBL:GAB15130.1}; RN [1] {ECO:0000313|EMBL:GAB15130.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NBRC 12137 {ECO:0000313|EMBL:GAB15130.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAB15130.1}. 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; BAEG01000083; GAB15130.1; -; Genomic_DNA. DR RefSeq; WP_003804386.1; NZ_BAEG01000083.1. DR EnsemblBacteria; GAB15130; GAB15130; ARGLB_083_00160. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:GAB15130.1}; KW Transferase {ECO:0000313|EMBL:GAB15130.1}. SQ SEQUENCE 319 AA; 33813 MW; 64037B56415C6443 CRC64; MPSNTKLSRM LDAGANLTVD GALATELEAH GCHLDDPLWS AKVLLEQPQL VKHVHRDYFR AGAAVAITAS YQATPQGFAR RGIDEEEALE LVALSVRLAD EARSEHLAEN PGAGPLLIAG SVGPYGAYLS DGSEYRGDYF LSRNEFLEFH RPRVAALVDA GADFLACETL PSLPEAEALV ELMKEFDVEG WLSFTLRDGG HISDGTPLAQ VAKLSRAQPS VVAIGVNCVP LELVAPSLGA LRKATDTPLI AYPNSGESYD AVSKTWRPAT AIGGPDGNHA ASLAEGTALW RELGARLIGG CCRTTPEDIA AVAMLTESP // ID H0R674_9ACTO Unreviewed; 1203 AA. AC H0R674; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:GAB20575.1}; GN Name=metH {ECO:0000313|EMBL:GAB20575.1}; GN ORFNames=GOEFS_120_00350 {ECO:0000313|EMBL:GAB20575.1}; OS Gordonia effusa NBRC 100432. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Gordoniaceae; Gordonia. OX NCBI_TaxID=1077974 {ECO:0000313|EMBL:GAB20575.1}; RN [1] {ECO:0000313|EMBL:GAB20575.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NBRC 100432 {ECO:0000313|EMBL:GAB20575.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:GAB20575.1}. 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; BAEH01000120; GAB20575.1; -; Genomic_DNA. DR RefSeq; WP_007319910.1; NZ_BAEH01000120.1. DR EnsemblBacteria; GAB20575; GAB20575; GOEFS_120_00350. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 754 754 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1203 AA; 130542 MW; 835378C237862292 CRC64; MSDRSNAATT IGGQQGAGAY DTTLLEAMSR RVLIGDGAMG TMLQAADLTL DDFLGLEGCN EILNETRPDV LADIHRAYYE AGADIVETNT FGCNLSNLGD YDIADRIREL ARKGTAIARG VADEMGPGPH GDPRYVLGSV GPGTKLPSLG HTTFELIRDA YTECAAGMLE GGADGILIET CQDLLQVKAA VIGSRRAMDL VGRAIPIFVH VTVETTGTML LGSEIGAALT ALEPLGIDVI GLNCATGPAE MSEHLRYLSR HARIPVSVMP NAGLPVLGAN GAEYPLTAPE LATALSGFVS EFGLSMVGGC CGTTPEHISR VAEAVAQAQQ AAREPAHESS TSSLYTPVPF AQDASFLVIG ERTNSNGSKA FRESMISGDY QSCLDIAKDQ TRDGAHMLDL NVDYVGRDGA LDMTALASRF ATASTLPIMI DSTEPQVIQA GLEALGGRCA VNSVNYEDGD APDSRFARIM KLVVEHGAAV VALTIDEEGQ ARTADHKVSI AERLIADITG NWGLLEEDII IDALTFPIST GQEEVRRDGI ETIEAIRRLK AAHPEIHFTL GISNISFGLN PAARQVLNSV FLHECVQAGL DTAIVHASKI LPMARIPEEH RDVALDLIYD RRREGYDPLS KLMELFEGVS AASARESRAA ELAALPLFER LERRIVDGER NGLEDDLDEA MTQVPPLKII NETLLSGMKT VGELFGSGQM QLPFVLQSAE VMKTAVAHLE PHMESTGEDG KGRIVLATVK GDVHDIGKNL VDIILSNNGY EVVNIGIKQP ISTILEVAED KKVDVIGMSG LLVKSTVVMK DNLEEINHRG LAENYPVLLG GAALTRSYVE TDLAETYGGD VHYARDAFEG LRLMDDIMAV KRGGGPDPDS PVALAAKAKA EERKARHARS KRIAEKRRAE QEPIEVPARS DVAADNEVPT PPFWGSRVVR GIPVAEYRQL LDERALFLGQ WGLRGTRGGE GPDYDELVET EGRPRLRYWI DRLSTEGILA HAAVVYGYFP VVSDGDTLHV LTEPKPDAPV RFSFEFPRQQ RSRFLCIADF VRSRDDAIAQ GVVDVLPMQL VTMGQPIADF ANKLFAENAY RDYLEVHGIS VQLTEALAEF WHQRVRSELQ FSGHAMASED PDNPQGFFDL EYRGARYSFG YGACPDLEDR GKLVEMLEAE RIGVTLSEEL QLHPEQSTDA FVLHHPEAKY FNT // ID H0REL1_9ACTO Unreviewed; 1203 AA. AC H0REL1; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:GAB23512.1}; GN Name=metH {ECO:0000313|EMBL:GAB23512.1}; GN ORFNames=GOPIP_054_00770 {ECO:0000313|EMBL:GAB23512.1}; OS Gordonia polyisoprenivorans NBRC 16320 = JCM 10675. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Gordoniaceae; Gordonia. OX NCBI_TaxID=1077976 {ECO:0000313|EMBL:GAB23512.1}; RN [1] {ECO:0000313|EMBL:GAB23512.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NBRC 16320 {ECO:0000313|EMBL:GAB23512.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:GAB23512.1}. 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; BAEI01000054; GAB23512.1; -; Genomic_DNA. DR RefSeq; WP_006370144.1; NZ_BAEI01000054.1. DR EnsemblBacteria; GAB23512; GAB23512; GOPIP_054_00770. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 235 235 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 301 301 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 302 302 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 754 754 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1203 AA; 130786 MW; 62EF381DE45666AA CRC64; MSSHTPNPGN HDTTFLSAMA RRVLVGDGAM GTMLQAADLT LDDFAGLEGC NEILNDTRPD VLEQIHRAYF EAGADAVETN TFGCNLSNLG DYDIADRIRE LSYKGTAIAR GVADEMGPSA DGTARFVLGS IGPGTKLPSL GHTTFGVIRD AYFECVAGML DGGADAVLIE TSQDLLQVKA AVVAARAAMD ELGRRIPIIS HVTVETTGTM LLGSEIGAAL AAIEPLGVDM IGLNCATGPA EMSEHLRYLS RHARIPVSVM PNAGLPQLGP NGAEYPLQPD ELASALSTFV GEFGLAFVGG CCGTTPEHIR QVAAAVAETT KADRAPAHIS ETSSLYSAVP FDQDASFLVI GERTNSNGSK AFREAMLAED YQRCLDIAKE QTRDGAHMLD LNVDYVGRDG AADMTALASR FATSSTLPIM LDSTEPEVIR AGLEALGGRC AVNSVNYEDG DGPESRFSRI MSLVVEHGAA VVALTIDEEG QARTADWKIR VAERLIADIT GNWGLAEEDI ILDTLTFPIS TGQEEVRRDG IETIEAIRRL HEAHPDVHFT LGISNISFGL NPAARQVLNS VFLHECVQAG LDTAIVHASK ILPMNKIPDE QRDVALDLVY DRRGAAGTHS EGREDYDPLQ KLMELFEGVS AASARESRAQ ELARLPLFER LERRIVDGER NGLEADLDEA MTQKPPLEII NETLLSGMKT VGELFGSGQM QLPFVLQSAE VMKTSVAHLE PHMEATGEDG KGRIVLATVK GDVHDIGKNL VDIILSNNGY EVVNIGIKQP ISTILEVAED KRADVIGMSG LLVKSTVVMK ENLEEINARG LADNYPVLLG GAALTRAYVE NDLSDTYEGQ VHYARDAFEG LRLMDEIMAF KRGGGSVPES ADSLAAAKKA AERKARHERS QRIAAKRKAA ETPVEVPARS DVIADNEIPT PPFWGTRIIK GIPVADYLQL LDERALFLGQ WGLRGARGGN GPTYEELVET EGRPRLREWI DRLSTEGILA HAAVVYGYFP AVSDGDVVHI LTEPTPDAPT RFSFTFPRQQ RSRFLCIADF VRSREAALAD GRVDVLPFQL VTMGQPIADF ANELFARDAY RDYLEVHGIS VQLTEALAEY WHQRVRGELA FADRAVDAED PDNAQGFFDL EYRGARFSFG YGACPDLEDR VKMMELLEPE RIGVHLSEEL QLHPEQSTDA FVLHHPEAKY FNT // ID H0S2C6_9BRAD Unreviewed; 1288 AA. AC H0S2C6; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 01-APR-2015, entry version 19. DE SubName: Full=B12-dependent homocysteine-N5-methyltetrahydrofolate transmethylase {ECO:0000313|EMBL:CCD88353.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CCD88353.1}; GN Name=metH {ECO:0000313|EMBL:CCD88353.1}; GN ORFNames=BRAO285_330004 {ECO:0000313|EMBL:CCD88353.1}; OS Bradyrhizobium sp. ORS 285. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=115808 {ECO:0000313|EMBL:CCD88353.1}; RN [1] {ECO:0000313|EMBL:CCD88353.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ORS285 {ECO:0000313|EMBL:CCD88353.1}; RA Rouy Z.; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CCD88353.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ORS285 {ECO:0000313|EMBL:CCD88353.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:CCD88353.1}. 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; CAFH01000229; CCD88353.1; -; Genomic_DNA. DR RefSeq; WP_006613694.1; NZ_CAFH01000229.1. DR EnsemblBacteria; CCD88353; CCD88353; BRAO285_330004. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CCD88353.1}; KW Transferase {ECO:0000313|EMBL:CCD88353.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 767 767 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1288 AA; 139594 MW; 4248490D0D30FE1F CRC64; MSPPVSTART AFLAAARERI LILDGAMGTM IQALQFDEAA FRGDRFKDFH RDLRGNNDLL ILTQPDAIED IHAQYLRAGA DIVATNTFSA TSIAQADYDL SDIIYELNRE GARLARNAAV RVAAEDGKPR FVAGAMGPTN RTASISPDVS NPGYRAVTFD DLRLAYGEQA RGLLDGGADI LLVETIFDTL NAKAALYAIT ELCEERGIDV PVMISGTITD KSGRLLSGQM PEAFWNSVRH AKPLTIGFNC ALGAEDLRAH VADIGRVADT LVCAYPNAGL PNEFGQYDET PAYMARLIGE FASAGLVNIV GGCCGTTPDH IAAIAAAVAP HKPRAVPEIA PRLRLSGLEP FELTPAIPFV NVGERTNVTG SAKFRKLITA GDYTAALQVA RDQVENGAQV IDVNMDEGLL DSEAAMRTFL NLVAAEPDIA RVPVMVDSSK FHVIEAGLKC VQGKPVVNSI SLKEGEEKFI HEAKIARRHG AAVVVMAFDE TGQADTYQRK TEICARAYKI LVETVGFPPE DIIFDPNIFA IATGLEEHNN YGVDFIEATR WIRQNLPHAH ISGGVSNLSF SFRGNEPVRE AMHSVFLYHA IKAGMDMGIV NAGQMIVYDD IDPELRQVCE DVVLNRDPGA SERLLALAEK FRGQGKQTKE ADLAWREWPV DKRLSHALVH GITEFIEQDT EEARAKSARP LDVIEGPLMA GMNVVGDLFG DGKMFLPQVV KSARVMKQAV AYLMPFMEAE KAANKGRGNE RSNAGKIVLA TVKGDVHDIG KNIVGIVLQC NNFEVIDLGV MVPAAKIIET AKAENADIIG LSGLITPSLD EMAYLASEME RQGLNVPLLI GGATTSRVHT AVKIDPNYHG GPVVHVNDAS RAVGVASSLL SPERKDAYAA DIRGEYQKIA AAHLRGQADK KRLSLTDARA NAPKIDFAKA KPVKPTFLGT KTFVDYDLAE LVPYIDWTPF FQTWELAGRF PAILDDAKVG EAARALYDDA LKMLKQIVDE KWFTARAAIG FWPANAVGDD IVLYADDSRT KTVATLHTLR QQLEKREGRF NTALSDFVAP AGSGVPDYVG GFVVTTGLGE DAVADRFKNA NDDYSSILVK ALADRLAEAF AERLHARVRR EFWAYAPDET LSADDLILEK YQGIRPAPGY PAQPDHTEKA TLFELLDAEK NAGVRLTESF AMWPGSSVSG LYFASPESFY FGVGKIERDQ VEDYAARKGM TVAEVERWLA PILNYIPARG GPQADAVARA TASPAPANDA APAELASHPA GCTCAVHLAW RKKAVGAK // ID H0SF17_9BRAD Unreviewed; 1288 AA. AC H0SF17; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 01-APR-2015, entry version 19. DE SubName: Full=B12-dependent homocysteine-N5-methyltetrahydrofolate transmethylase {ECO:0000313|EMBL:CCD92794.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CCD92794.1}; GN Name=metH {ECO:0000313|EMBL:CCD92794.1}; GN ORFNames=BRAO375_2240003 {ECO:0000313|EMBL:CCD92794.1}; OS Bradyrhizobium sp. ORS 375. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=566679 {ECO:0000313|EMBL:CCD92794.1}; RN [1] {ECO:0000313|EMBL:CCD92794.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ORS375 {ECO:0000313|EMBL:CCD92794.1}; RA Rouy Z.; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CCD92794.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ORS375 {ECO:0000313|EMBL:CCD92794.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:CCD92794.1}. 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; CAFI01000140; CCD92794.1; -; Genomic_DNA. DR RefSeq; WP_009027772.1; NZ_CAFI01000140.1. DR EnsemblBacteria; CCD92794; CCD92794; BRAO375_2240003. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CCD92794.1}; KW Transferase {ECO:0000313|EMBL:CCD92794.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 767 767 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1288 AA; 139856 MW; 92525B09772A6CE2 CRC64; MSAPVSTARS AFLAAARDRI LILDGAMGTM IQALQFDEAA FRSERFKDFH RDLRGNNDLL ILTQPEAIEN IHAQYLRAGA DVVATNTFSA TSIAQADYDL SDIIYELNRE GARLARSAAT RVAAEDGKPR FVAGAMGPTN RTASISPDVS NPGYRAVTFD DLRLAYGEQA RGLLDGGADI LLLETIFDTL NAKAALYAIA ELCEERGIDV PVMISGTITD KSGRLLSGQM PEAFWNSVRH AKPLTIGFNC ALGAEDLRAH VADIGRVADT LVCAYPNAGL PNEFGQYDET PAYMARLIGE FASAGLVNIV GGCCGTTPDH IAAIAAAVAP HKPRAVPEIA PRLRLSGLEP FELTPAIPFV NVGERTNVTG SAKFRKLITA GDYTAALQVA RDQVENGAQV IDVNMDEGLL DSETAMRTFL NLVAAEPDIA RVPVMVDSSK FHVIEAGLKC VQGKPVVNSI SLKEGEEKFI HEAKIARRHG AAVVVMAFDE TGQADTYQRK TEICARAYKI LVEQVGFPPE DIIFDPNIFA IATGIEEHNN YGVDFIEATR WIRQNLPHAH VSGGVSNLSF SFRGNEPVRE AMHSVFLYHA IKAGMDMGIV NAGQMIVYDD IDPELRQVCE DVVLNRDPGA SERLLALAEK FRGQGKQTKE ADLAWREWPV DKRLSHALVH GITEFIELDT EEARAKSTRP LDVIEGPLMA GMNVVGDLFG DGKMFLPQVV KSARVMKQAV AYLMPFMEAE KAANKGRANE RSNAGKIVLA TVKGDVHDIG KNIVGIVLQC NNFEVIDLGV MVPAAKIIET AKAENADIIG LSGLITPSLD EMAYLASEME RQGLNVPLLI GGATTSRVHT AVKIDPNYQG GPVVHVNDAS RAVGVASSLL SAERKDAYAA EIRTEYQKIA AAHLRGQADK KRLSLTDARV NAPKIDFAKA KPVKPTFLGT RTFVDYDLAE LVPYIDWTPF FQTWELAGRF PAILDDAKVG EAARALYDDA LKMLKQIVEQ KWFTARAAIG FWPANAVGDD IVLYADDSRT KTVATLHTLR QQLEKREGRF NTALSDFVAP AGSGVPDYVG GFVVTTGLGE DAIADRFKNA NDDYSSILVK ALADRLAEAF AERLHARVRR EFWAYAPDET LSADDLILEK YQGIRPAPGY PAQPDHTEKA TLFELLDAET NAGVRLTESF AMWPGSSVSG LYFASPESFY FGVGKIERDQ VEDYAARKGM TVAEVERWLA PILNYIPARG GQQADTTART VASPAPANDA VPSELASHPV GCTCAVHLAW RKKAVGAK // ID H0SUT6_9BRAD Unreviewed; 1288 AA. AC H0SUT6; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 01-APR-2015, entry version 19. DE SubName: Full=B12-dependent homocysteine-N5-methyltetrahydrofolate transmethylase {ECO:0000313|EMBL:CCD97963.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CCD97963.1}; GN Name=metH {ECO:0000313|EMBL:CCD97963.1}; GN ORFNames=BRAS3809_1510003 {ECO:0000313|EMBL:CCD97963.1}; OS Bradyrhizobium sp. STM 3809. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=551936 {ECO:0000313|EMBL:CCD97963.1}; RN [1] {ECO:0000313|EMBL:CCD97963.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=STM 3809 {ECO:0000313|EMBL:CCD97963.1}; RA Rouy Z.; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CCD97963.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=STM 3809 {ECO:0000313|EMBL:CCD97963.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:CCD97963.1}. 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; CAFJ01000059; CCD97963.1; -; Genomic_DNA. DR RefSeq; WP_008960576.1; NZ_CAFJ01000059.1. DR EnsemblBacteria; CCD97963; CCD97963; BRAS3809_1510003. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CCD97963.1}; KW Transferase {ECO:0000313|EMBL:CCD97963.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 767 767 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1288 AA; 139604 MW; 2855343A774A679E CRC64; MSAPVSTARS AFLAAASQRI LILDGAMGTM IQALQFDEAA FRGERFKDFH RDLRGNNDLL ILTQPDAIED IHAQYLRAGA DIVATNTFSA TSIAQADYDL SDIIYELNRE GARLARNAAT RVAAEDGRPR FVAGAMGPTN RTASISPDVS NPGYRAVTFD DLRLAYGEQA RGLLDGGADI LLVETIFDTL NAKAALYAIA ELCEERGIDV PVMISGTITD KSGRLLSGQM PEAFWNSVRH AKPLTIGFNC ALGAEDLRAH VADIGRVADT LVCAYPNAGL PNEFGQYDET PAYMARLIGE FAASGLVNIV GGCCGTTPDH IAAIAAAVAP HKPRAVPEIA PRLRLSGLEP FELTPAIPFV NVGERTNVTG SAKFRKLITA GDYTAALQVA RDQVENGAQV IDVNMDEGLL DSEAAMRTFL NLVAAEPDIA RVPVMVDSSK FHVIEAGLKC VQGKPVVNSI SLKEGEEKFI HEARIARRHG AAVVVMAFDE TGQADTYKRK TEICARAYKI LVETVGFPPE DIIFDPNIFA IATGIEEHDN YGVDFIEATR WIRQNLPHAH VSGGVSNLSF SFRGNEPVRE AMHSVFLYHA IKAGMDMGIV NAGQMIVYDD IDPELRQVCE DVVLNRDPGA SERLLALAEK FRGQGKQTKE ADLAWREWPV EKRLSHALVH GITEFIDVDT EEARAKSTRP LDVIEGPLMA GMNVVGDLFG DGKMFLPQVV KSARVMKQAV AYLMPFMEAE KAANKGRANE RSNAGKIVLA TVKGDVHDIG KNIVGIVLQC NNFEVIDLGV MVPAAKIIDT AKAENADIIG LSGLITPSLD EMAYLASEME RQGLNVPLLI GGATTSRVHT AVKIDPNYQG GPVVHVNDAS RAVGVASSLL SPERKDAYAA DIRGEYQKIA AAHLRGQADK KRLSLADARA NAPTIDFAKA KPVKPTFLGT KTFVDYDLAE LVPYIDWTPF FQTWELAGRF PAILDDAKVG EAARALYDDA LKMLKQIVDE KWFTARAAIG FWPANADGDD IVLYADDSRT RKIATLHTLR QQLEKREGRF NTALADFVAP VGSGVPDYVG GFVVTTGLGE DAVADRFKNA NDDYSSILVK ALADRLAEAF AERLHARVRR EFWAYAPDET LSADDLILEK YQGIRPAPGY PAQPDHTEKA TLFELLDAEK NAGVRLTESF AMWPGSSVSG LYFASPESFY FGVGKIERDQ VEDYAARKGM TVAEVERWLA PILNYIPARG GQQADAVARA TASPAPANDA APAELASHPV GCTCAVHLAW RKKAVGAK // ID H0TUM3_9BRAD Unreviewed; 1292 AA. AC H0TUM3; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 01-APR-2015, entry version 19. DE SubName: Full=B12-dependent homocysteine-N5-methyltetrahydrofolate transmethylase {ECO:0000313|EMBL:CCE10161.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CCE10161.1}; GN Name=metH {ECO:0000313|EMBL:CCE10161.1}; GN ORFNames=BRAS3843_40019 {ECO:0000313|EMBL:CCE10161.1}; OS Bradyrhizobium sp. STM 3843. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=551947 {ECO:0000313|EMBL:CCE10161.1}; RN [1] {ECO:0000313|EMBL:CCE10161.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=STM 3843 {ECO:0000313|EMBL:CCE10161.1}; RA Rouy Z.; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CCE10161.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=STM 3843 {ECO:0000313|EMBL:CCE10161.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:CCE10161.1}. 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; CAFK01000285; CCE10161.1; -; Genomic_DNA. DR RefSeq; WP_008972672.1; NZ_CAFK01000285.1. DR EnsemblBacteria; CCE10161; CCE10161; BRAS3843_40019. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CCE10161.1}; KW Transferase {ECO:0000313|EMBL:CCE10161.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 767 767 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1292 AA; 139935 MW; 09E8A98BB54FF22E CRC64; MSVSVSPKRT AFLAAARQRI LILDGAMGTM IQALQFDEAS FRGDRFKDFH RDLRGNNDLL ILTQPQAIED IHAQYLRAGA DIVATNTFSA TSIAQADYDL TDIIYELNRE GAKLARNAAQ RVAAEDGKPR FVAGAMGPTN RTASISPDVA NPGYRAVTFD DLRLAYGEQA RGLLDGGADI LLVETIFDTL NAKAALYAIA ELCEERGIDV PVMVSGTITD KSGRLLSGQM PEAFWNSVRH AKPVTIGFNC ALGAEDLRAH IADIGRVADT LVCAYPNAGL PNEFGQYDET PDYMARLIGE FARDGLVNIV GGCCGTTPDH IAAIAAAVAP HKPRAVPEIA PRLRLSGLEP FELTPAIPFV NVGERTNVTG SAKFRKLITA GDYTAALQVA RDQVNNGAQV IDVNMDEGLL DSEAAMRTFL NLVAAEPDIA RVPVMVDSSK FHVIEAGLKC VQGKPVVNSI SLKEGEEKFL QEARIARRHG AAVVVMAFDE TGQADTYARK TEICARAYKI LVEQVGIPPE DIIFDPNIFA IATGLEEHNN YGVDFIEATR WIRQNLPGAH VSGGVSNLSF SFRGNEPVRE AMHSVFLYHA IKAGMDMGIV NAGQMIVYDD IDPELRQVCE DVVLNRDAGA AERLLALAEK FRGQGKQTKE ADLAWREWPV AKRLSHALVH GITEFIEQDT EEARAASTRP LDVIEGPLMA GMNVVGDLFG DGKMFLPQVV KSARVMKQAV AYLMPFMEAE KAANKGASAE RSTAGKIVLA TVKGDVHDIG KNIVGIVLQC NNFEVIDLGV MVPATKIIET AKTEKADIIG LSGLITPSLD EMAYLASEME RQDLNMPLLI GGATTSRVHT AVKIDPNYRN GPVVHVNDAS RAVGVASSLL SPERKAAYAA DVRGEYAKIA EAHLRGQANK KRLTLADARA NATKIDFAKA RPVKPSFLGV KSFADYDLAE LVPYIDWTPF FQTWELAGRF PAILDDAKVG EAARALYDDA LKMLDRIVKE NWFTARATIG FWPANAVGDD IVLYADEARD KLIATLHTLR QQLEKREGRF NTALSDFIAP AASGVPDYIG GFVVTAGIGE DVVADRFKNA NDDYSSILVK ALADRLAEAF AERMHARVRR EFWAYAPDEA LSNAELILEK YQGIRPAPGY PAQPDHTEKA TLFALLDAET NAGVKLTESF AMWPGSSVSG LYFANPESFY FGVGKIERDQ VEDYAARKGM SVAEVERWLA PILNYIPAQA TGDAKQAAAT PARAPAGAVA ANDAEPEGLA SHPPGCTCAV HLAWRKKAVG AK // ID H0UDL1_BRELA Unreviewed; 1149 AA. AC H0UDL1; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 01-APR-2015, entry version 21. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:CCF15555.1}; GN Name=metH {ECO:0000313|EMBL:CCF15555.1}; GN ORFNames=BLGI_3505 {ECO:0000313|EMBL:CCF15555.1}; OS Brevibacillus laterosporus GI-9. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Brevibacillus. OX NCBI_TaxID=1118154 {ECO:0000313|EMBL:CCF15555.1}; RN [1] {ECO:0000313|EMBL:CCF15555.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=GI-9 {ECO:0000313|EMBL:CCF15555.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:CCF15555.1}. 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; CAGD01000018; CCF15555.1; -; Genomic_DNA. DR EnsemblBacteria; CCF15555; CCF15555; BLGI_3505. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 717 717 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1149 AA; 126960 MW; 458DCEADCC73496C CRC64; MQEQLARKIL ILDGAMGTML QQANLTADDF GGEEYEGCNE LLNVTRPDVI RHIHATYFEA GADIVETNTF GATDVVLAEY DIADRDYELN LAAARIAKEV ADEFSTESWP RYVAGSMGPT TKTLSLTGGV TFEQLIHAYY RQTKALMEGG VDLLLVETSQ DTLNVKAGGI GIRQAFQELG YELPIMISGT IEPMGTTLAG QNIEAFYVSI EHLKPITIGL NCATGPEFMR DHLRTLSDLA LCGISCYPNA GLPDENGHYH ESPQGLAMKM KAFAEKGWLN VAGGCCGTTP EHIRALHEAL QGITPRENKK SHATAVSGIE VLYVEDDNRP IFVGERTNVI GSKKFRDLIA AGQFEEGSDI ARAQVKRGAA VIDICLADPD RDEYEDMEKF LPYVSRKVKA PLMIDSTDKK VVELGLKYSQ GKAIINSINL EDGLDRFEEV VPLIHKYGAA VVVGTIDEAG MAITRERKLE VATRSYDLLV NQFGINPQDI IFDALVFPVG TGDEQYIGSA QETIEGIRLI KQHFPLCKQI LGVSNVSFGL PPAGREVLNA VFLYHTTVAG LDYAIVNTEK IERYASISEE ERKLAEDLLF HTNDETLATF TDFYRQKKKE VAKEVSNLTL EERLANYVVE GSKDGLIPDL TLALEKYVPL DIINGPLMKG MEEVGRLFNG NQLIVAEVLQ SAEVMKASVA FLEPHMEKSE STVKGKILLA TVKGDVHDIG KNLVEIILSN NGYEVINLGI KVAPEQLIAA CHQEKPDAIG LSGLLVKSAQ QMVITAQDLR SSGIDVPLMV GGAALTRKFT TNRIAPEYEG IVLFAKDAMD GLNLANKLHD PQARLKLVEE LQAQATVNQA QIEEKASESV VIPQPEMIRS ATSITTPVYV APDLERHVLR NYPINHLRPY VNLRMLLGKH LGIKGNVDKL IESGDKKATE LYEIVDDLLN EAIRSQILQA NGMYQFFPAQ SFGNDILIYD PNDHTKLLER FTFPRQPQAP HLCLADFLRP VETNEMDYVA FLTVTAGKGV RDLAQEWKEK GDYLRSHVLQ AVALELAEAF AERIHHVIRD SWGFPDPADM TMLERFGARY QGIRVSFGYP ACPDLEDQEK LFKLLSPQDI GIQLTEGFMM DPEASVSAMV FAHPEARYFN ATPPVGVEV // ID H0UDL2_BRELA Unreviewed; 621 AA. AC H0UDL2; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 17. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN Name=yitJ {ECO:0000313|EMBL:CCF15556.1}; GN ORFNames=BLGI_3506 {ECO:0000313|EMBL:CCF15556.1}; OS Brevibacillus laterosporus GI-9. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Brevibacillus. OX NCBI_TaxID=1118154 {ECO:0000313|EMBL:CCF15556.1}; RN [1] {ECO:0000313|EMBL:CCF15556.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=GI-9 {ECO:0000313|EMBL:CCF15556.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCF15556.1}. 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; CAGD01000018; CCF15556.1; -; Genomic_DNA. DR RefSeq; WP_003338099.1; NZ_CAGD01000018.1. DR EnsemblBacteria; CCF15556; CCF15556; BLGI_3506. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:CCF15556.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:CCF15556.1}. SQ SEQUENCE 621 AA; 68293 MW; F3E643CE922F4531 CRC64; MGKRDLRAYL TQHVLVGDGA MATQLYEQGV PIGVSYEELC LSNPQIIRNV HTAYYEAGAR LIETNTFGAN RDSLSRYGLE SKVTRMNRAA VTLAREAVGD DAFVVGAMGS IIAGRVRTKQ IDQFKDQFEE QATSLLHAGV DGILLETFLD VDELLLALEV IRPLTELPII AQLATLEVGT TRDGHSLTYA FQQIKDAGAD VIGLNCRLGP AEILRSFEAT VCPDDVFLSA FPNAGRLGMA DGTLSYKSSP DYFAESALRL HEQGVRLIGG CCGTTPEHTR AIAEKLAGRK PLPRVNPPAP IHSERIEVQA VQKRLQPSII EEVKHHPTII VEFDPPKDLH TEDFLQGCCA LHDAGANAIT LADNSLATVR MSNMALGAMM KRLGIEPLLH IACRDRNLIG QQSHLMGLHA LGIDQVLVIT GDPSRFGDLP GASSVYDVSS FDLIRMVKQL NQGYAFSGKQ LKQHAQFIVG AAFNPHVRHL DAAVARLEKK VEAGADYIMT QPVYDAETIV QIYEATKHIR VPIFIGIMPL TSSRNAEFLH NEVPGIKLSP YALEQMKLFT GEAARQEGNR MAKELIDATL QYFNGIYLIT PFNYYQMTVE LTQYIRQQEQ VKAGLKEVSS S // ID H0ULX9_9BACT Unreviewed; 808 AA. AC H0ULX9; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EHM12521.1}; GN ORFNames=JonanDRAFT_0087 {ECO:0000313|EMBL:EHM12521.1}; OS Jonquetella anthropi DSM 22815. OC Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae; OC Jonquetella. OX NCBI_TaxID=885272 {ECO:0000313|EMBL:EHM12521.1, ECO:0000313|Proteomes:UP000003806}; RN [1] {ECO:0000313|EMBL:EHM12521.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 22815 {ECO:0000313|EMBL:EHM12521.1}; 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., 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., Klenk H.-P., Eisen J.A.; RT "The Noncontiguous Finished genome of Jonquetella anthropi DSM RT 22815."; 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; CM001376; EHM12521.1; -; Genomic_DNA. DR RefSeq; WP_008520046.1; NZ_CM001376.1. DR EnsemblBacteria; EHM12521; EHM12521; JonanDRAFT_0087. DR Proteomes; UP000003806; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000003806}; KW Methyltransferase {ECO:0000313|EMBL:EHM12521.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000003806}; KW Transferase {ECO:0000313|EMBL:EHM12521.1}. SQ SEQUENCE 808 AA; 84453 MW; 83B31690D5653101 CRC64; MAVEFTSPSR RLTLGRDRII FDGAMGTALG SRGLRRGSLP EELNLSSPET VAAVHRSFLE AGSDFITTNT FGAFPSRLAH AGLSVGPVVR SACQIARREA ERFGGFVALD IGPSGRLMEP LGDATFDEIY QGVCEVLHAG AAYCDAVLLE TFTDLAEIRA AALAVRENCG LPLLATMSFE PSGRTFSGAS AEACSLVLSG LGASAFGTNC SAGPRALRET VRQICGACPV PVIVQPNAGL PEFSGSSVVY SAGPDEFQSV MGEFARWGVA VLGGCCGTTP DYIRRLSSLR GDVPPRSVPL GPAACSASQV VRFDMFVPVG ERINPTGKPV LADAYASRLP SPLLEDAIKQ TQEGAVMLDV NAGVPGVDEA AALSWAVQTL QEGVTCPLQL DSANPKALEA ALRACVGLPM INSASARPES LEPAIRLAKK YGVSILGLPM DETGVPERAA DRLAVAARIK ERWTAAGLAA EKLLFDPLVM AAAAGPERVS ETLNTLSALK ERLGAKTMAG ISNVSFGLPA RGAVNRTMLA ACLDRGLDAA ILNPGDLGMM DTVAVWNLLS GRDADASGYL AYCAARPEEL EPESRDALPV PEANQDDNED ELGRAVRLGL VQEARRAAAE LCKGVSAMTV VEEYLVPALD RVGDDYEAGR IFLPGLLKAA SAASAAFDEI RQALPAGSGA RDKGPIVLAT VQGDVHDIGK NIAGTVLESY GFRVIDLGKN VPAETVVRTV VENRAPLVGL SALMTATVAS MEDTVAALRR AAPGVKIIVG GAVLSRVLAR SIGADYYAAT AMETVRLAEK AIKLKERE // ID H0UR06_9BACT Unreviewed; 806 AA. AC H0UR06; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EHM10843.1}; GN ORFNames=TheveDRAFT_1725 {ECO:0000313|EMBL:EHM10843.1}; OS Thermanaerovibrio velox DSM 12556. OC Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae; OC Thermanaerovibrio. OX NCBI_TaxID=926567 {ECO:0000313|EMBL:EHM10843.1, ECO:0000313|Proteomes:UP000005730}; RN [1] {ECO:0000313|EMBL:EHM10843.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 12556 {ECO:0000313|EMBL:EHM10843.1}; 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., 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 ----------------------------------------------------------------------- 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; EHM10843.1; -; Genomic_DNA. DR RefSeq; WP_006584337.1; NZ_CM001377.1. DR EnsemblBacteria; EHM10843; EHM10843; TheveDRAFT_1725. DR Proteomes; UP000005730; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005730}; KW Methyltransferase {ECO:0000313|EMBL:EHM10843.1}; KW Transferase {ECO:0000313|EMBL:EHM10843.1}. SQ SEQUENCE 806 AA; 84434 MW; 6295394FA3308D32 CRC64; MEQRRVREFF RGLRSPLVLD GGMGTQLAER GWHPPMLPEE MCLHMPQAVL EVHRGYVASG AAVIETNSFG GSVRKLSLKG LGDRAEELAR RSAELARRAA GDQVLVAGSV GPSGDMLKPL GDMSFQEAVM SFEPQVRGLV EGGADLILVE TMLDLKEAKA AVEAVKRVRE DMPFVVSFTF DRDGRTVSGD SPEAAAIWAE AVGAIGVGAN CGLGPRGYVE VVRRLAGAAS LPVWVYPNAG VPSAGDYLGP QEFAEGCAAL LEAGASVIGG CCGTTPEHVK ALAAMAANRS LAATDAAGGL RLCGRSKVFS FGPGLPLGII GERINVSRKS PIREQVGLYR YGAVKEEARS QALAGASVID VNVGLPEIDQ VRAMREAVWA VESAAPLPIS LDSDDLGVLE AGLREAAGVP LINSVTAKEE QLRLGMRLAM RYGAALTVLL IDHRGILEDG LERARIAERV LEAAREEGFP GSRIVFDPLT LTLGSGEANG LETLRAVREV VALGGLTSLG ISNVSHGLPA RGLLNRSFLA MAMGAGLDMV ICNPLDRELM GIVKACDALR GRDKGLSCFM AFGADWCDVP SGGALGALKA KQPEGGAVGG SKAPDGEVHL SPLAAKVLDG DEEGALGEAR RLIDLEGPLG VISDHLVPAL DEVGRRYETG EFFLPQLIEA AQAASAVCAL AEEELLREGS SASRGTVVLA TVEGDLHDLG KNVVATVLKS HGYRVVDLGK DVKAERIVEA ALREGAQVVG LSALMTSTVP RMKEVIEETH RRGCGFKVIV GGAAVSPWYA RSIGADGMSY DAVGAC // ID H0UYS8_CAVPO Unreviewed; 355 AA. AC H0UYS8; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCPOP00000002304}; DE Flags: Fragment; GN Name=BHMT {ECO:0000313|Ensembl:ENSCPOP00000002304}; OS Cavia porcellus (Guinea pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; OC Hystricognathi; Caviidae; Cavia. OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000002304}; RN [1] {ECO:0000313|Ensembl:ENSCPOP00000002304} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000002304}; RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [2] {ECO:0000313|Ensembl:ENSCPOP00000002304} RP IDENTIFICATION. RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000002304}; RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSCPOP00000002304}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAKN02048579; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSCPOT00000002566; ENSCPOP00000002304; ENSCPOG00000002532. DR GeneTree; ENSGT00390000003122; -. DR Proteomes; UP000005447; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006577; P:amino-acid betaine metabolic process; IEA:Ensembl. DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005447}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000005447}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 182 182 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 264 264 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 265 265 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSCPOP00000002304}. SQ SEQUENCE 355 AA; 39230 MW; A82CB7B9475C7339 CRC64; RGYVKAGPWT PEAAVEHPEA VRQLHREFLR AGSNVMQTFT FYASEDKLEN RGNYVAEKIS GQKVNEAACD IARQVAEEGD ALVAGGVSQT PSYLSCKSES EVKKIFQQQL EVFMKKNVDF LIAEYFEHVE EAVWAVEALK ASGKPVAATM CIGPEGDLHG VSPGECAVRL VRAGASIVGV NCHFDPTTSL QTVKLMKQGL TAARLKAHLM CQPLAYHTPD CGKQGFIDLP EFPFGLEPRV ATRWDIQKYA REAYELGVRY IGGCCGFEPY HIRAIAEELA PERGFLPPAS EKHGGWGSGL DMHTKPWIRA RARKEYWQSL RIASGRPYNP ALSKPDAWGV TKGTTELMQQ KEATT // ID H0V2S0_CAVPO Unreviewed; 363 AA. AC H0V2S0; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCPOP00000003847}; GN Name=BHMT2 {ECO:0000313|Ensembl:ENSCPOP00000003847}; OS Cavia porcellus (Guinea pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; OC Hystricognathi; Caviidae; Cavia. OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000003847}; RN [1] {ECO:0000313|Ensembl:ENSCPOP00000003847} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000003847}; RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [2] {ECO:0000313|Ensembl:ENSCPOP00000003847} RP IDENTIFICATION. RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000003847}; RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSCPOP00000003847}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAKN02048577; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_003464437.1; XM_003464389.2. DR Ensembl; ENSCPOT00000004310; ENSCPOP00000003847; ENSCPOG00000004265. DR GeneID; 100718920; -. DR CTD; 23743; -. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; H0V2S0; -. DR OMA; PEGDMHD; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000005447; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0061627; F:S-methylmethionine-homocysteine S-methyltransferase activity; IEA:Ensembl. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl. DR GO; GO:0046500; P:S-adenosylmethionine metabolic process; IEA:Ensembl. DR GO; GO:0033477; P:S-methylmethionine metabolic process; IEA:Ensembl. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005447}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Reference proteome {ECO:0000313|Proteomes:UP000005447}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 208 208 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 363 AA; 39769 MW; 557309421BA75BEB CRC64; MAPGGGPTAR RGILERLDNG EVVIGDGSFL LTLEKRGYVK AGLWTPEAVV EHPDAVRQLH MEFLRAGSNV MQTFTFSASE DCMESKWEEA NVAACDLARE VAGKGDALVA GGVCQSSVYK DHKDEARIKK LFRLQLKVFT RKNVDFLIAE YFEHVEEAVW AVEVLKESGK PVAVTMCIGP EGDMHGVAPG ACAVELAKAG ADIVGVNCRF GPRTSLQTLH LMKLGLEAAG LSRHLMAQPL GFHTPDCGKG GFLDLPEYPF GLEPRVATRW DIQKYAREAY ELGVRYIGGC CGFEPYHIRA IAEELAPERG FLPPASEKHG SWGSALSMHT KPWIRARASR EYWENLLPAS GRPFCPSLSK PDI // ID H0VSR0_CAVPO Unreviewed; 1267 AA. AC H0VSR0; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCPOP00000013677}; DE Flags: Fragment; GN Name=MTR {ECO:0000313|Ensembl:ENSCPOP00000013677}; OS Cavia porcellus (Guinea pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; OC Hystricognathi; Caviidae; Cavia. OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000013677}; RN [1] {ECO:0000313|Ensembl:ENSCPOP00000013677} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000013677}; RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [2] {ECO:0000313|Ensembl:ENSCPOP00000013677} RP IDENTIFICATION. RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000013677}; RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 1}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSCPOP00000013677}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAKN02021692; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSCPOT00000015318; ENSCPOP00000013677; ENSCPOG00000015171. DR GeneTree; ENSGT00420000029824; -. DR InParanoid; H0VSR0; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG7TF786; -. DR TreeFam; TF312829; -. DR Proteomes; UP000005447; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:Ensembl. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000005447}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005447}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 259 259 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 785 785 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSCPOP00000013677}. SQ SEQUENCE 1267 AA; 140955 MW; 1FD97FBE4FFDE3BB CRC64; TMPGFKFLFK GDMKETLQDE IEAILQKRIM VLDGGMGTMI QQYKLSEESF QGQEFKDHTR PLKGNNDILS ITQPDIIYQI HKDYLLAGAD IIETNTFSST SIAQTDYGLE HLAYRMNKCS ADVARKAAEE ITLHTGIKRF VAGALGPTNK TLSVSPSVER PDYRNITFDE LVEAYQEQAK GLLDGGVDIL LIETIFDTAN AKAALFALKK LFEEGYTPRP VFISGTIVDK SGRTLSGQTG EAFVISVSHG DPLCIGLNCA LGATEMRPFI ETIGKCTTAY VLCYPNAGLP NTFGDYDETP SMMAMHLKDF AMDGLVNIVG GCCGTTPDHI REIAEAVKNC KPRVPPANVF EGHMLLSELA PAFRIGQYTN FVNIGERCNV AGSKKFAKLI MAGNYEEALS VAKVQVEMGA QVLDVNMDDG MLDGPSAMTK FCNFIASEPD IAKVPLCIDS SNFAVIEAGL KCCQGKCIVN SISLKEGEED FLEKARKIKK FGAAVVVMAF DEEGQATETD VKISVCTRAY HLLVKKVGFN PNDIIFDPNI LTIGTGMEEH NWYAINFIHA TKVIKETLPG VRINGGLSNL SFSFRGMEAI REAMHGVFLY HAIKFGMDMG IVNAGNLPVY DDIHKDLLQL CEDLIWNKDP EATEKLLRYA QTQGKGGKKV IQTDEWRNGP IEERLEYALV KGIEKYIIED TEEARLNQEK YPRPLNIIEG PLMNGMKVVG DLFGAGKMFL PQVIKSARVM KKAVGHLIPF MEKEREEKRV INGTVEEEDP YQGTIVLATV KGDVHDIGKN IVGVVLGCNN FRVIDLGVMT PCDKILKAAL DHKAVIDIIG LSGLITPSLD EMIFVAKEME RLAIKIPLLI GGATTSKTHT AVKIAPRYSA PVIHVLDASK SVVVCSQLLD ENLKEEYFEE IMEEYEDIRQ EHYESLKERK YVPLSQARKN GFHIDWLSEP PPVKPTFIGT QVFEDYDLQK LVPYIDWKPF FDVWQLRGKY PNRGFPKIFN DKTVGEEARK VYNDAQNMLN ILISQKKLQA KGVVGFWPAQ SVQDDIHLYA EDVVPQAAEP IATFFGLRQQ AEKDSTSTDP YHCLSDFIAP LHSGVCDYLG LFAVACFGVE KLSKAYEDDG DDYSSIMVKA LGDRLAEAFA EELHERVRKE LWAYSASEQL DVADLRRLRY EGIRPAPGYP SQPDHTEKLT MWRLASIEQC TGIRLTESLA MTPASAVSGL YFSNLNSKYF AVGKISKDQI EDYALRKNMS VAEVEKWLGP ILGYDTN // ID H0WBR4_CAVPO Unreviewed; 404 AA. AC H0WBR4; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCPOP00000020430}; DE Flags: Fragment; GN Name=BHMT {ECO:0000313|Ensembl:ENSCPOP00000020430}; OS Cavia porcellus (Guinea pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; OC Hystricognathi; Caviidae; Cavia. OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000020430}; RN [1] {ECO:0000313|Ensembl:ENSCPOP00000020430} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000020430}; RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [2] {ECO:0000313|Ensembl:ENSCPOP00000020430} RP IDENTIFICATION. RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000020430}; RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSCPOP00000020430}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAKN02048579; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSCPOT00000027817; ENSCPOP00000020430; ENSCPOG00000002532. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; H0WBR4; -. DR OMA; WGVTKGT; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR Proteomes; UP000005447; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006577; P:amino-acid betaine metabolic process; IEA:Ensembl. DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005447}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000005447}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 214 214 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 296 296 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 297 297 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSCPOP00000020430}. SQ SEQUENCE 404 AA; 44774 MW; 7C423581B9A78581 CRC64; LCPCLPLQGI LERLDAGEVV IGDGGFVFAL EKRGYVKAGP WTPEAAVEHP EAVRQLHREF LRAGSNVMQT FTFYASEDKL ENRGNYVAEK ISGQKVNEAA CDIARQVAEE GDALVAGGVS QTPSYLSCKS ESEVKKIFQQ QLEVFMKKNV DFLIAEYFEH VEEAVWAVEA LKASGKPVAA TMCIGPEGDL HGVSPGECAV RLVRAGASIV GVNCHFDPTT SLQTVKLMKQ GLTAARLKAH LMCQPLAYHT PDCGKQGFID LPEFPFGLEP RVATRWDIQK YAREAYELGV RYIGGCCGFE PYHIRAIAEE LAPERGFLPP ASEKHGGWGS GLDMHTKPWI RARARKEYWQ SLRIASGRPY NPALSKPDAW GVTKGTTELM QQKEATTEQQ LRELFEKQKF RSIQ // ID H0WUZ8_OTOGA Unreviewed; 407 AA. AC H0WUZ8; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSOGAP00000006104}; GN Name=BHMT {ECO:0000313|Ensembl:ENSOGAP00000006104}; OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Strepsirrhini; OC Lorisiformes; Galagidae; Otolemur. OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000006104, ECO:0000313|Proteomes:UP000005225}; RN [1] {ECO:0000313|Ensembl:ENSOGAP00000006104} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG The Broad Institute Genome Sequencing Platform; RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B., RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N., RA Walker B.J., Sharpe T., Hall G.; RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby)."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSOGAP00000006104} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSOGAP00000006104}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAQR03040161; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAQR03040162; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_003785988.1; XM_003785940.1. DR Ensembl; ENSOGAT00000006824; ENSOGAP00000006104; ENSOGAG00000006820. DR GeneID; 100945871; -. DR CTD; 635; -. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; H0WUZ8; -. DR OMA; WGVTKGT; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000005225; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006577; P:amino-acid betaine metabolic process; IEA:Ensembl. DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005225}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Reference proteome {ECO:0000313|Proteomes:UP000005225}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 217 217 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 407 AA; 44981 MW; 73A9464D42395C1A CRC64; MAHVGGKRAK RGILERLNAG EVVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAVRQLH REFLRAGSNV MQTFTFYASE DKLENRGNYV LEKISGQKVN EAACDIARQV ADEGDALVAG GVSQTPSYLS CKSETEVKKI FQQQLEVFMK KNVDFLIAEY FEHVEEAVWA VEALKVSGKP VAATMCIGPE GDLHGISPGE CAVRLVKAGA SIVGVNCHFD PTISLQTVKL MKEGLGAAGL KAHLMSQPLA YHTPDCSKQG FIDLPEFPFG LEPRVATRWD IQKYAREAYN LGVRYIGGCC GFEPYHIRAI AEELAPERGF LPPASEKHGS WGSGLDMHTK PWIRARARKE YWENLRIASG RPYNPSMSKP DAWGVTKGTA ELMQQKEATT EQQLKELFEK QKIRSAE // ID H0WYW1_OTOGA Unreviewed; 363 AA. AC H0WYW1; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSOGAP00000007734}; GN Name=BHMT2 {ECO:0000313|Ensembl:ENSOGAP00000007734}; OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Strepsirrhini; OC Lorisiformes; Galagidae; Otolemur. OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000007734, ECO:0000313|Proteomes:UP000005225}; RN [1] {ECO:0000313|Ensembl:ENSOGAP00000007734} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG The Broad Institute Genome Sequencing Platform; RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B., RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N., RA Walker B.J., Sharpe T., Hall G.; RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby)."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSOGAP00000007734} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSOGAP00000007734}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAQR03040160; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_003785987.1; XM_003785939.1. DR Ensembl; ENSOGAT00000008632; ENSOGAP00000007734; ENSOGAG00000008629. DR GeneID; 100945549; -. DR CTD; 23743; -. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; H0WYW1; -. DR OMA; PEGDMHD; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000005225; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0061627; F:S-methylmethionine-homocysteine S-methyltransferase activity; IEA:Ensembl. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl. DR GO; GO:0046500; P:S-adenosylmethionine metabolic process; IEA:Ensembl. DR GO; GO:0033477; P:S-methylmethionine metabolic process; IEA:Ensembl. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005225}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Reference proteome {ECO:0000313|Proteomes:UP000005225}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 208 208 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 363 AA; 39726 MW; 664E25C9E0F66863 CRC64; MAPAGRPGAK KGILERLDGG EVVVGDGSFL ITLEKRGYVK AGLWTPEAVV EHPGAVRQLH MEFLRAGSNV MQTFTFSASE DNMESKWEDV NAAACDLARE VAGEGDALVA GGICQTSLYK YHKDEARIKK LFQQQLEVFT RKDVDFLIAE YFEHVEEAVW AVEVLKESGK PVAATMCIGP EGDMHDVSPG ECAAKLVKAG AAIVGVNCRF GPWTSLKTVG LMKEGLGAAG LKAHLMVQSL GFHTPDCGKG GFVDLPEYPF GLEPRVVTRW DIQKYAREAY NLGVRYIGGC CGFEPYHIRA IAEELAPERG FLPLASEKHG SWGSGLNMHT KPWIRARARR EYWENLLPAS GRPFCPSLSK PDV // ID H0XD77_OTOGA Unreviewed; 1265 AA. AC H0XD77; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSOGAP00000013808}; GN Name=MTR {ECO:0000313|Ensembl:ENSOGAP00000013808}; OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Strepsirrhini; OC Lorisiformes; Galagidae; Otolemur. OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000013808, ECO:0000313|Proteomes:UP000005225}; RN [1] {ECO:0000313|Ensembl:ENSOGAP00000013808} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG The Broad Institute Genome Sequencing Platform; RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B., RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N., RA Walker B.J., Sharpe T., Hall G.; RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby)."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSOGAP00000013808} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 1}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSOGAP00000013808}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAQR03186306; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAQR03186307; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAQR03186308; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAQR03186309; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAQR03186310; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAQR03186311; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAQR03186312; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAQR03186313; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAQR03186314; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAQR03186315; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAQR03186316; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAQR03186317; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAQR03186318; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAQR03186319; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAQR03186320; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAQR03186321; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAQR03186322; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAQR03186323; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAQR03186324; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAQR03186325; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAQR03186326; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSOGAT00000015425; ENSOGAP00000013808; ENSOGAG00000015411. DR GeneTree; ENSGT00420000029824; -. DR InParanoid; H0XD77; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG7TF786; -. DR TreeFam; TF312829; -. DR Proteomes; UP000005225; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:Ensembl. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000005225}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005225}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 260 260 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 785 785 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1265 AA; 140585 MW; 813ED1AA27361B44 CRC64; MSPALSQPSF KAGLKKTLRD EIEAILRRRI MVLDGGMGTM IQRHKLSEEH FQGQEFKDHS RPLKGNNDIL SITQPDIIYQ IHKEYLLAGA DIIETNTFSS TSIAQADYGL EHLAYQMNKC SAGVARKAAE EITLQTGIKR FVAGALGPTN KTLSVSPSVE RPDYRNITFD ELVEAYEEQA KGLLDGGVDI LLIETIFDTA NAKAALFALQ KLFEEKYDPR PIFISGTIVD KSGRTLSGQT GEAFVISVSH ADCLCIGLNC ALGAAEMRPF IETIGKCTTA YVLCYPNAGL PNTFGDYDET PSVMATYLKD FAMDGLVNIV GGCCGSTPDH LREIAKAVKN CKPRVPPATV FEGHMLLSGL EPFKIGPYTN FVNIGERCNV AGSRKFAKLI MAGNYEEALS VAKVQVEMGA QILDINMDDG MLDGPSAMTR FCNLIASEPD IAKVPLCIDS SNFAVIEAGL KCSQGKCIVN SISLKEGEED FLEKAKKIKK YGAAVVVMAF DEEGQATETD TKIEVCTRAY QLLVKNLGFN PNDIIFDPNI LTIGTGMEEH NWYAVNYIHA TKVIKETLPG ARISGGLSNL SFSFRGMEAI REAMHGVFLY HAIKFGMDMG IVNAGNLPVY DDIHKELLQL CEDLIWNKDP EATEKLLRYA QTHGKGGKKV IQTDEWRTGP VEERLEYALV KGIEKHIIED TEEARLNQEK YPRPLNIIEG PLMNGMKVVG DLFGAGKMFL PQVIKSARVM KKAVGHLIPF MEKEREETRV LNGTVEEEDP YQGTIVLATV KGDVHDIGKN IVGVVLGCNN FRVIDLGVMT PCEKILKAAI DHKADIIGLS GLITPSLDEM IFVAKEMERL AIKIPLLIGG ATTSRTHTAV KIAPRYSAPV IHVLDASKSV VVCSQLLDEN LKDEYFEEIM EEYEDIRQDH YESLKEKRYL SLSQARKNGF RIDWLSEPCP VKPTFTGTRV FADYDLQKLV DYIDWKPFFD VWQLRGKYPN RGFPKIFNDK TVGEEARKVY DDAQNMLNTL ISQKKLQARG VVGFWPAQSV QDDIHLYAED AVPQAAEPIA TFHGLRQQAE KDSASTEPYY CLSDFIAPLH SGVRDYLGLF AVACFGVEEL SKAYEDDSDD YSSIMVKALG DRLAEAFAEE LHERVRRELW AYCGSERLDV ADLRRLRYEG IRPAPGYPSQ PDHTEKLSMW QLADIEQATG IRLTESLAMA PASAVSGLYF SNLKSKYFAV GKISKDQIED YALRKNMSVA EVEKWLGPIL GYDTD // ID H0Z020_TAEGU Unreviewed; 393 AA. AC H0Z020; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 01-APR-2015, entry version 25. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSTGUP00000003905}; DE Flags: Fragment; GN Name=BHMT2 {ECO:0000313|Ensembl:ENSTGUP00000003905}; OS Taeniopygia guttata (Zebra finch) (Poephila guttata). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; OC Estrildidae; Estrildinae; Taeniopygia. OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000003905, ECO:0000313|Proteomes:UP000007754}; RN [1] {ECO:0000313|Ensembl:ENSTGUP00000003905, ECO:0000313|Proteomes:UP000007754} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20360741; DOI=10.1038/nature08819; RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W., RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A., RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P., RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., RA London S.E., Li Y., Lin Y.C., George J., Sweedler J., Southey B., RA Gunaratne P., Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., RA Itoh Y., Whitney O., Pfenning A.R., Howard J., Volker M., RA Skinner B.M., Griffin D.K., Ye L., McLaren W.M., Flicek P., RA Quesada V., Velasco G., Lopez-Otin C., Puente X.S., Olender T., RA Lancet D., Smit A.F., Hubley R., Konkel M.K., Walker J.A., RA Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z., Eichler E.E., RA Stapley J., Slate J., Ekblom R., Birkhead T., Burke T., Burt D., RA Scharff C., Adam I., Richard H., Sultan M., Soldatov A., Lehrach H., RA Edwards S.V., Yang S.P., Li X., Graves T., Fulton L., Nelson J., RA Chinwalla A., Hou S., Mardis E.R., Wilson R.K.; RT "The genome of a songbird."; RL Nature 464:757-762(2010). RN [2] {ECO:0000313|Ensembl:ENSTGUP00000003905} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSTGUP00000003905}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABQF01045238; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSTGUT00000003947; ENSTGUP00000003905; ENSTGUG00000003783. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; H0Z020; -. DR OMA; WGVTKGT; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR Reactome; REACT_324201; Sulfur amino acid metabolism. DR Proteomes; UP000007754; Chromosome Z. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007754}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000007754}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 207 207 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSTGUP00000003905}. SQ SEQUENCE 393 AA; 43621 MW; CF5561759D3D1ADB CRC64; QGILERLDAG EIVIGDGGFV FALEKRGYVK AGPWTPEATV EHPEAVRQLH REFLRAGSSV LQTFTFYASE DKLENRGNYV AEKISCQKVN EAACDIAREV ANEGDALVAG GVSQTPSYLS CKDKTEVKAA FQKQLEVFVK KNVDFLIAEY FEHVEEAVWA VEVLKESGKP VAATMCIGPE GDMHGVSPGQ CAVQLVKAGA SIVGVNCHFD PETSIETVRL MKEGLQAAKL KAHLMCQPLA FHTPDCGKQG FIDLPEFPFG LEPRIATRWD IQKYARKAYD LGIRFIGGCC GFEPYHIRAI AEELAPERGF LPEASEKHGS WGDNLSMHTK PWVRARARKE YWENLKPASG RPYCPGMSKP DGWGVTKGAK ELMQQKEATT EQQLKELFHK KKF // ID H0ZJP8_TAEGU Unreviewed; 1250 AA. AC H0ZJP8; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSTGUP00000010817}; DE Flags: Fragment; GN Name=MTR {ECO:0000313|Ensembl:ENSTGUP00000010817}; OS Taeniopygia guttata (Zebra finch) (Poephila guttata). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; OC Estrildidae; Estrildinae; Taeniopygia. OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000010817, ECO:0000313|Proteomes:UP000007754}; RN [1] {ECO:0000313|Ensembl:ENSTGUP00000010817, ECO:0000313|Proteomes:UP000007754} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20360741; DOI=10.1038/nature08819; RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W., RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A., RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P., RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., RA London S.E., Li Y., Lin Y.C., George J., Sweedler J., Southey B., RA Gunaratne P., Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., RA Itoh Y., Whitney O., Pfenning A.R., Howard J., Volker M., RA Skinner B.M., Griffin D.K., Ye L., McLaren W.M., Flicek P., RA Quesada V., Velasco G., Lopez-Otin C., Puente X.S., Olender T., RA Lancet D., Smit A.F., Hubley R., Konkel M.K., Walker J.A., RA Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z., Eichler E.E., RA Stapley J., Slate J., Ekblom R., Birkhead T., Burke T., Burt D., RA Scharff C., Adam I., Richard H., Sultan M., Soldatov A., Lehrach H., RA Edwards S.V., Yang S.P., Li X., Graves T., Fulton L., Nelson J., RA Chinwalla A., Hou S., Mardis E.R., Wilson R.K.; RT "The genome of a songbird."; RL Nature 464:757-762(2010). RN [2] {ECO:0000313|Ensembl:ENSTGUP00000010817} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 1}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSTGUP00000010817}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABQF01014589; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABQF01014590; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABQF01014591; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSTGUT00000010930; ENSTGUP00000010817; ENSTGUG00000010458. DR GeneTree; ENSGT00420000029824; -. DR InParanoid; H0ZJP8; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG7TF786; -. DR TreeFam; TF312829; -. DR Reactome; REACT_324201; Sulfur amino acid metabolism. DR Reactome; REACT_344789; Cobalamin (Cbl, vitamin B12) transport and metabolism. DR Reactome; REACT_352949; Methylation. DR Proteomes; UP000007754; Chromosome 3. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:Ensembl. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007754}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007754}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 246 246 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 770 770 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSTGUP00000010817}. SQ SEQUENCE 1250 AA; 139143 MW; BD502321754B40EB CRC64; QKSVEDEIES ILQERIMVLD GGMGTMIQQH ALTEEDFRGH EFKDHSRPLK GNNDLLSITQ PDIICDIHKE YLLSGADIIE TNTFSSTRVA QADYGLEHLA YRLNRVSAQV ARKAADTVTA ETGIRRYVAG AMGPTNRTLS VSPSVERPDY RNITFDELVE AYTEQAKGLL DGGVDILLVE TIFDTANAKA ALFALQMLFE EEYASRPIFV SGTIVDKSGR TLSGQTGEAF VVSVSHSKPL CIGLNCALGA VEMRPFIETI GKCTTAYIIC YPNAGLPNTF GGYDETPEVT AKHIENFALD GLVNIVGGCC GTTPAHIRKI AEAVKFCKPR VPPSLSEGYM LLSGLEPFRI GPYTNFVNIG ERCNVAGSRK FAKLIMAGNY EEALSVAKLQ VEMGAQILDI NMDDGMLDGP TAMTKFCNLI SSEPDIAKVP LCIDSSNFSV IEAGLKCCQG KCIVNSISLK EGEEDFLEKA RKIKLYGAAV VVMAFDEVGQ ATETETKIAI CSRAYHLLVG KVHFNPNDII FDPNILTIGT GMEEHNLYAI NFINATKTIK ETLPGARISG GLSNLSFSFR GMDAIREAMH GVFLYHAIKY GMDMGIVNAG NLPVYDDIHK ELLQLCENLI WNKDPDATEK LLHYAQNHAQ GGKKVVQTDE WRKGSVEERL EYALIKGIEK YVIADTEEAR LKQEKYPRPL NVIEGPLMNG MKIVGDLFGA GKMFLPQVIK SARVMKKAVG HLIPYMEKER EERRAKQGST EEEARYKGTI VLATVKGDVH DIGKNIVGVV LGCNNFRVID LGVMTPCDKI LRAAVENKAD IIGLSGLITP SLDEMIFVAK EMERLAIKIP LLIGGATTSK THTAVKIAPR YSAPVVHVLD ASKSVVVCSQ LLDDSIKDDF FEEILDEYEE IRQEHYESLK ERRYLSLQQA RRKGFQNNWL SGHIPVKPKF IGTKVFEDYD LRRLVDYIDW KPFFDVWQLR GKYPNRSFPK IFNDKTVGEE AKRVYNDAQD LLKMLINEKK LQARGVVGFW PARSVQDDIH LYAVEEAVGS SEPIAKFYGL RQQAEKDSAC TDPYYCLSDF IAPLDSGICD YLGLFAVACF GVDDLCSEFR KQEDEYNIIM VKALGDRLAE AFAEELHERV RREFWAYSSS EQLDLSGLRK IKYEGIRPAP GYPSQPDHTE KLTMWKLANI EETTGIGLTE SLAMIPASAV SGLYFSSPNS KYFAVGKICR DQVEDYALRK NLSVVEVEKW LEPILGYDAE // ID H1AJ47_9FIRM Unreviewed; 784 AA. AC H1AJ47; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHQ48159.1}; GN ORFNames=HMPREF0978_00865 {ECO:0000313|EMBL:EHQ48159.1}; OS Coprobacillus sp. 8_2_54BFAA. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae; Coprobacillus. OX NCBI_TaxID=469597 {ECO:0000313|EMBL:EHQ48159.1, ECO:0000313|Proteomes:UP000005559}; RN [1] {ECO:0000313|EMBL:EHQ48159.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=8_2_54BFAA {ECO:0000313|EMBL:EHQ48159.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHQ48159.1}. 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; ACTG01000001; EHQ48159.1; -; Genomic_DNA. DR RefSeq; WP_008791466.1; NZ_JH599901.1. DR EnsemblBacteria; EHQ48159; EHQ48159; HMPREF0978_00865. DR Proteomes; UP000005559; Unassembled WGS sequence. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005559}. SQ SEQUENCE 784 AA; 85411 MW; 9655EDEF4823C44D CRC64; MLQERLKNDI LVFDGAMGTQ LQDAGLKAGD IPECLNITDP KLIQTIHLNY LNAGADFITT NTFGANPLKM AEAPYSYEEI INAAIDNATI ARKTADRQND SYIVLDIGPI GQLLEPMGTL TFDEAYEIIK KQVIIAKDKV DAVLLETMTD IYEVKAGILA VKENSDLPVF VTMTYESNLR TLSGCDPLTM VNVLEGLNVD VLGVNCSLGP IELTPVIDQI LAAATIPVLL QPNAGLPCLV EGKTCYNMDK ETFVQESLKH VKNGVAIIGG CCGTTPDFIA SLKNNLPVRK KITPKRATRV SSGTKTVEFG HHVVVCGERL NPTGKKKLKL ALKEERYDEL VVEAIKQDQA GAHVLDVNVG LPGINEVATM KHVIKLLQEV ISLPLQIDSS VPGAIEQACR YYNGKPLINS VNGKDETMDA IFPIVKKYGG VVIGLTLDEN GIPPLAKDRY KIAKKIINKA ASYGITKENI IIDCLVLTVS AQQKEVMETV KAVAMVKELG VHTVLGVSNV SFGLPNRPLL NKTFLAMAMS AGLDLPIINP MDQELMATID AFNVLYNYDH DAAVYIERRA NQETITKKDT STFTLNDIVL HGLKDEVTNA TKELLKTTPG LEIINNILIP ALDTVGKQYE KNIIFLPQLI QSAETSKIAF GIIKDTFKDT AATKGPIIMA TVHGDIHDIG KNIVKVVLES YGYKVIDLGK DVPPETVVEA FHKHHPKAIG LSALMTTTVV SMAKTIELLK QIDNICPIFV GGAVLTADYA KEINADYYSK DAMEAVELLN KIIK // ID H1BEJ8_9FIRM Unreviewed; 786 AA. AC H1BEJ8; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Methylmalonyl-CoA mutase domain-containing protein {ECO:0000313|EMBL:EHO22478.1}; GN ORFNames=HMPREF0981_03631 {ECO:0000313|EMBL:EHO22478.1}; OS Erysipelotrichaceae bacterium 6_1_45. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae. OX NCBI_TaxID=469614 {ECO:0000313|EMBL:EHO22478.1, ECO:0000313|Proteomes:UP000003818}; RN [1] {ECO:0000313|EMBL:EHO22478.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=6_1_45 {ECO:0000313|EMBL:EHO22478.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHO22478.1}. 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; ACTK01000068; EHO22478.1; -; Genomic_DNA. DR RefSeq; WP_008818812.1; NZ_JH590970.1. DR EnsemblBacteria; EHO22478; EHO22478; HMPREF0981_03631. DR Proteomes; UP000003818; Unassembled WGS sequence. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000003818}. SQ SEQUENCE 786 AA; 85411 MW; FE4576F3F7004FE8 CRC64; MEIENKIQFL DGAMGTQLQD KGLPAGASPE LFMMEHGEII EDVHAAYIDS GSDIIYTNTF GANAKKLCKS QYTVEEVITR AVQLAKSAAK RRNGVQVALD IGPIGELLEP NGYLPFEEAY ELYRQQVVAG EQAGADLVIF ETMSDLYEVK AAILAAKEHT QLPVFVTMSF EADHRTFTGC TTASFALCAE GLGADAIGIN CSLGPDQILP IAEELAAMTN LPLIIKANAG LPDPLTNTYS IDAAAYARML LPYTKLPLAY VGGCCGTTPQ FIQELKNTLP TTIAVEKRKR RIGSYACTPT KCLHIQDVHV IGERINPTGN KRMKAALQEH RMDEILAIAM EEVEGGADIL DVNVGLPGID EKEMMVEVIK ELQSVIDLPL QIDSTDPAVI RAALRAVNGV AIVNSVNGEA AVMESILPAV KKYGANVVGL TMDEDGIPAC AQKRLEIGTR IVETAQRYGI AKERVFLDCL TLTVSAQQSG AKETLQALTA IREQLGVHTV LGVSNISFGL PSRILLNQSF LTMAMQAGLS MPIMNPNQAA MMDAVRSYRV LQGIDVDSQE YIRIYAQQKR EGGKPHIESV HINIEESIMR GLKEETRQLC TKLLSEKEPL QIVNEHLIPA LDAVGARYEK KEIYLPQLIN AATASQCAFE EIRRSVQAGG LESISKGKII LATVKGDVHD IGKNIVKVVL ENYGYQVFDL GKDVPVETVV ETAIKEQVRL IGLSALMTTT LKSMEETIQA LHESGHECKI MVGGAVVSAD YAKQIHADYY ARDAKESADI AKEVLG // ID H1BEJ9_9FIRM Unreviewed; 587 AA. AC H1BEJ9; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 19. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HMPREF0981_03632 {ECO:0000313|EMBL:EHO22479.1}; OS Erysipelotrichaceae bacterium 6_1_45. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae. OX NCBI_TaxID=469614 {ECO:0000313|EMBL:EHO22479.1, ECO:0000313|Proteomes:UP000003818}; RN [1] {ECO:0000313|EMBL:EHO22479.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=6_1_45 {ECO:0000313|EMBL:EHO22479.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHO22479.1}. 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; ACTK01000068; EHO22479.1; -; Genomic_DNA. DR RefSeq; WP_008818813.1; NZ_JH590970.1. DR EnsemblBacteria; EHO22479; EHO22479; HMPREF0981_03632. DR Proteomes; UP000003818; Unassembled WGS sequence. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003818}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 587 AA; 66542 MW; F3951C2FB5ACA13A CRC64; MIENYLNTQG YMLFDGAFGT YYAQRYAEDQ KPCEMANLNH PKRVAAIHQE YIEAGADAIK TNTFSANEQH LECSWEMIRR ILQEGYRIAK EAAKDKVKVF ADIGPIMEQK NVSLAQQYQQ IVDVFLAEGA DCFLFETLLN TQELHAVTSY IKEQCPQACI IVSFAVTADG YSRQGIAMSR LLQDCLADEH VDACGLNCVC GPMHMKRLLD SIDRTQKPIL IMPNAGYPTI LANRTYFRDS STYFAKEMRE IWQKGARLLG GCCGTTPVYI QKTREALQEH KIIQKVQQPV QETERIPQED HNPLRRKLQR KQPVIAVEFD PPANCEIERF MNHVEFLKEA GVDAVTIADC PIARARVDSS LIACKLHREL GLDVIPHMTC RDRNINATKA LLFGLQIEGI RNVLVVTGDP IPSEDRQEVK GVFNFNSQIL AGYIRDLNAT MFTSPFMVFG ALNLNAVNFE AELAKAKRKV TQGMEGFLTQ PVHSRQALFN LKRARKELQA YILGGVLPIV SHRNAVYMNN EISGIEVDEE IVAMYEGTTR KEAQKLAVDI SCKTMDEMRP YIDGYYLITP FNRVEIIADM ITYIHKQ // ID H1BIG1_9FIRM Unreviewed; 781 AA. AC H1BIG1; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 01-OCT-2014, entry version 16. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHO86418.1}; GN ORFNames=HMPREF0984_00168 {ECO:0000313|EMBL:EHO86418.1}; OS Eubacterium sp. 3_1_31. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium. OX NCBI_TaxID=457402 {ECO:0000313|EMBL:EHO86418.1}; RN [1] {ECO:0000313|EMBL:EHO86418.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_31 {ECO:0000313|EMBL:EHO86418.1}; 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 Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., RA Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P., RA McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Eubacterium sp. 3_1_31."; 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. {ECO:0000313|EMBL:EHO86418.1}. 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; ACTL01000003; EHO86418.1; -; Genomic_DNA. DR RefSeq; WP_008687042.1; NZ_JH594448.1. DR EnsemblBacteria; EHO86418; EHO86418; HMPREF0984_00168. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; SQ SEQUENCE 781 AA; 85319 MW; 224358DE0A550D96 CRC64; MKDKAMITLL DGAMGTMLQE KGLTPGELPE VFGYHHGDIV TSIHKAYVES GADIIYANTF QANRKKLKKN GFSVQKIITS AIQQAKKAAN VTTRVALDIG PIGELLEPNG YLTFDEAYDI FKEMVMAGQQ AGADLIVFET MSDLMEVKAA ILAAKENSNL PIFVTMSFEK DHRTFTGCCA ASFALLAERL RVDAVGVNCS LGPDELLPIV EEMAAYTNLP LIVKANAGLP DPLTNTYAMQ AHEFANSLQR FTHLPIRYIG GCCGTTPAFI AELKQHAMTG TMVAKKIPSC VCTPTKCVTM DGVRVIGERI NPTGNKRMKQ ALLDHDLDEI AAIAMEQIEA GAEVLDVNVG LPGIDEKQMM VEVIRHLQTL VDVPLQIDST DPAVIEAALR IYNGIAIVNS VNGEISSMQQ ILPLIERYGA NVVGLTLDEQ GIANDASKRY QIAKRILTTA QQYHIEKERV FIDCLTLTVS AQQKSAIETL KTLHMVKEKL QVPTVLGVSN ISFGLPRRLL LNQSFLTMAL SAGLNMPIIN PNHAAMMEAV YSFRVLHGLD VDAQAYIERF AEQKDGEQNK GNEKAGITID MAIQKGLKEE TRALCKKLLE KETPLTIVDA YLIPALDKVG NLYENKQLYL PQLINAASAS QAAFDEIRQQ LQRQGKTTIT KGKILLATVR GDVHDIGKNI VKVVLENYGY QVFDLGKDVP VDIIVKTAVE KQIPLIGLSA LMTTTLAAME ETIQALHACK HPCKIMIGGA VVSQEYADKV QADYYAKDAK ASADIAKEVF G // ID H1BIG2_9FIRM Unreviewed; 586 AA. AC H1BIG2; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 07-JAN-2015, entry version 19. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HMPREF0984_00169 {ECO:0000313|EMBL:EHO86419.1}; OS Eubacterium sp. 3_1_31. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium. OX NCBI_TaxID=457402 {ECO:0000313|EMBL:EHO86419.1}; RN [1] {ECO:0000313|EMBL:EHO86419.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=3_1_31 {ECO:0000313|EMBL:EHO86419.1}; 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 Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., RA Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P., RA McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Eubacterium sp. 3_1_31."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHO86419.1}. 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; ACTL01000003; EHO86419.1; -; Genomic_DNA. DR RefSeq; WP_008687044.1; NZ_JH594448.1. DR EnsemblBacteria; EHO86419; EHO86419; HMPREF0984_00169. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 586 AA; 65972 MW; 677974952B06F57A CRC64; MHPLFMKQKR LLFDGAFGTY YASLYGNEEP CEMANVKAPT RVAAIHEEYL KAGANAIKTN TFAMNEAVLD CSKAKREELL RQGYRIAKRV ATPYQASVFA DIGPCVETRT RSAFTQYKEL VDVFLEEGAD CFLFETLPND HGIHEIAAYL KERCPHVCVL VSFAVTADGY TQQGVPLTKL VKAAHEDENI HGFGLNCICG PMHMRRLLKY FDTKKDTILI MPNAGYPTIL ANHTYFRDNS SYYAQEMEKI SSMGVRILGG CCGSKPSYIQ KIKERLQEEA VLSLPTPAAN DPVLYKDCNP LRKKLQRKEK VICVEFDPPM DCRIERFMND AEYLKEQGID AITIADCPIA RARVDSSLLA CKLHRELGID VIPHMTCRDR NINATKALLF GLNIEDIYNV LVVTGDPIPA ADRQEVKGVF SFNSQLLAGY IRDLNETTFP HPFLIFGALN VNAANFKQEL LKAKQKIQQG VQAFLTQPIH SAKGLQNLQQ AHRELDAWIL GGVMPIVSYR NALYMKNEIA GIEVDDAILS RYEHKNREEA AVLAVTIAKA TIDEMVSFVD GFYLITPFHR VEIMQQIIAH IQQMDD // ID H1BU96_ECOLX Unreviewed; 1227 AA. AC H1BU96; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHP66904.1}; GN ORFNames=HMPREF0986_01080 {ECO:0000313|EMBL:EHP66904.1}; OS Escherichia coli 4_1_47FAA. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1127356 {ECO:0000313|EMBL:EHP66904.1}; RN [1] {ECO:0000313|EMBL:EHP66904.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=4_1_47FAA {ECO:0000313|EMBL:EHP66904.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHP66904.1}. 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; ACTQ01000015; EHP66904.1; -; Genomic_DNA. DR RefSeq; WP_000096059.1; NZ_JH594554.1. DR EnsemblBacteria; EHP66904; EHP66904; HMPREF0986_01080. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136084 MW; E5209AFD0B754571 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE VAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPAEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAE // ID H1C6N3_9FIRM Unreviewed; 786 AA. AC H1C6N3; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=Methylmalonyl-CoA mutase domain-containing protein {ECO:0000313|EMBL:EHO35769.1}; GN ORFNames=HMPREF0995_00111 {ECO:0000313|EMBL:EHO35769.1}; OS Lachnospiraceae bacterium 7_1_58FAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=658087 {ECO:0000313|EMBL:EHO35769.1}; RN [1] {ECO:0000313|EMBL:EHO35769.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=7_1_58FAA {ECO:0000313|EMBL:EHO35769.1}; 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. {ECO:0000313|EMBL:EHO35769.1}. 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; ACTW01000004; EHO35769.1; -; Genomic_DNA. DR RefSeq; WP_009256712.1; NZ_JH590866.1. DR EnsemblBacteria; EHO35769; EHO35769; HMPREF0995_00111. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; SQ SEQUENCE 786 AA; 83626 MW; 9478CEEB6A0A67CF CRC64; MGIEIPQNKF LILDGAMGTV LQQRGLSPQG RPELLNLTEP ELLDSVYKEY IAAGSQVIYA NTFGANGLKL AKTGHSVEEV VGAAIAVAKK AAAGTGTLVA LDVGPLGELL EPMGTLSFER AYDLFREMAE AGAKAGADLI VVETMTDLYE AKAALLAAKE AAHLPVFVTM SFDAGGRTFT GCTVASMART LEGLGADAIG LNCSLGPDLL APLLKELCEN TRLPVIAKPN AGLPDPVDGH YDMGPEDFAQ ALLTCVEAGI SIVGGCCGTS PEYIRRLTAV LEGKKPVSRH YNNTGLVCTP VTPIRLNGVR VIGERINPTG KKRFQQALLE NDLDYILDVG VQQEDAGADI LDVNVGFPGV NEVVMLPRVV KKLQSAIAVP LQLDSSNPDA LEAGLRVYNG KAAVNSVNGE PEVLERVLPI VKKYGASVVG LTLDKNGIPK TAEERVAIAR RILQAALDHG IPREDVWIDC LTLTVSAQQE QAAETLKAVR TIREELGLQV VLGVSNISFG LPNRKLITQN FLIQAMHAGL TLPIINPNQT EMMDAVAAYR VLSGEDRECR AYVARFAAES PAVQAAPKAD ALTLGDAVIR GLKADAGKLA AKALETEDEL SLVENHLIPA LDKVGEDYDK GTAFLPQLLS AAQAAQAVFE VIRSSIAAKG GVPVKKGKLI VATVQGDIHD IGKNIVKTVL GNYGYEVLDL GRDVPPETIL RTVQEQGVRL VGLSALMTTT LPAMEKTIRL LHTMEEPPVI FVGGAVVTPE YAKQMNADYY AKDAHQSVEI TRKVMG // ID H1C6N4_9FIRM Unreviewed; 592 AA. AC H1C6N4; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 19. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HMPREF0995_00112 {ECO:0000313|EMBL:EHO35770.1}; OS Lachnospiraceae bacterium 7_1_58FAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=658087 {ECO:0000313|EMBL:EHO35770.1}; RN [1] {ECO:0000313|EMBL:EHO35770.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=7_1_58FAA {ECO:0000313|EMBL:EHO35770.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHO35770.1}. 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; ACTW01000004; EHO35770.1; -; Genomic_DNA. DR RefSeq; WP_007488232.1; NZ_JH590866.1. DR EnsemblBacteria; EHO35770; EHO35770; HMPREF0995_00112. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 592 AA; 64539 MW; E79199CBF287CFF5 CRC64; MMDIRTYLSQ GKPLLFDGAM GTYFAAHPGR AEERCERANL TRPEEILRIH RAYLQAGCRA IKTNTFAISG DLSDGNDETA CDIVNAACHL ARQAAQPYGA YVFADLGPAP RDHSRAPADL YQTQAQWFLE QGVTHFLVET LSGDEGLPEL AGWLKEKNPD AFLMVSFAVD HSGMTSAGRL GSELYRFASE LAGVDAVGFN CVSGPRHLLK YIQTLELSDK PLTVMPNAGY PTVLGRRTVF GGQPDYFAGQ IAQIVQAGAS IVGGCCGTTP EHIAQTAQAL KEPLPKCTVS APKKLLKPAA NASNSLWEKL EAGKRVIAVE LDPPVDDDSA GFWEGVQALR GSGADAVTIA DCPIGRPRAD SSLLACKIKR DIGIEPLPHM TCRDRNLNAT KALLLGLSME GVHNVLVVTG DPIPTEDRNE VKSVFNFNSR KLARFVHMLN ENTLRTPFRI YGALNLNARN FDVELRRAQE KEACGVSGFL TQPVLSAEAL DNLKLAHKTL RGKILGGIFP VVSHRNACFL NNEISGMRVC DEIIHLYEGK DRDAAEALAV TVSTAIAKEI FPYTDGYYLM TPFRRVALME HIIQNIQQSC IS // ID H1CJX8_9FIRM Unreviewed; 415 AA. AC H1CJX8; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHO26663.1}; GN ORFNames=HMPREF0995_04756 {ECO:0000313|EMBL:EHO26663.1}; OS Lachnospiraceae bacterium 7_1_58FAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=658087 {ECO:0000313|EMBL:EHO26663.1}; RN [1] {ECO:0000313|EMBL:EHO26663.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=7_1_58FAA {ECO:0000313|EMBL:EHO26663.1}; 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. {ECO:0000313|EMBL:EHO26663.1}. 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; ACTW01000096; EHO26663.1; -; Genomic_DNA. DR RefSeq; WP_007493652.1; NZ_JH590886.1. DR EnsemblBacteria; EHO26663; EHO26663; HMPREF0995_04756. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 415 AA; 44510 MW; 3F8BCF7752511ACC CRC64; MDTIPPLSLP ILLDGATGSE LYKRGMPAGA CTEQWVLGHP EALLELQRGY VAAGSQVLIA PTFGANRVRL EQHGIFGQVA DYNRRLVELS RQAAGGRALV AGDMAPTGLF IAPFGESSFE ELVAIYTEQA AALAAAGVDL FLIETTMTMP EARAAVLACK SVSDRPVWVT FTCDENGRTL SGTDVLAALI VMQGMGVDAF GLNCSSGPAE MLEQMRRLTP YTTVPLIAKP NAGLPETVEG QAVYHCPPEE FASYAAGFAA AGVRIFGGCC GTTAEHVAAL RAAVEAVDFS AFVPPRRDPD VIPCASEKEA RFITPDIDVG ETIECTSDLL EDILEAEENA PQGALKIAIY DEDDLYTFAE NQYAVKDALC LWTDVPELLE QALRLYQGRA FWDGTGELEA AFLQEMARKY GLVLL // ID H1D1Y0_9FIRM Unreviewed; 791 AA. AC H1D1Y0; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHO62493.1}; GN ORFNames=HMPREF9453_01618 {ECO:0000313|EMBL:EHO62493.1}; OS Dialister succinatiphilus YIT 11850. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Dialister. OX NCBI_TaxID=742743 {ECO:0000313|EMBL:EHO62493.1}; RN [1] {ECO:0000313|EMBL:EHO62493.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=YIT 11850 {ECO:0000313|EMBL:EHO62493.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHO62493.1}. 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; ADLT01000052; EHO62493.1; -; Genomic_DNA. DR RefSeq; WP_008860112.1; NZ_JH591188.1. DR EnsemblBacteria; EHO62493; EHO62493; HMPREF9453_01618. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; SQ SEQUENCE 791 AA; 84314 MW; 67B4615D9B5062E3 CRC64; MILFDGGMGT MLQKFGLEAG SCPDYYNISH PDVVQQIHRA YMEAGSQFIT TNTFGSSPLK LADYDLSDKV EEIAAAAVRN VRAACGDKVK VAGDMGPTGK FIKPIGDLSF DETCENYYRL AKALAQAGAD CLIIETIIDI QEMKAALIAA KEAASLPVIC QMTYSEDGRT IPGTDPVTAT ILLDAMGADV IGANCSVGPD KLLEAARQMV SVTNKPVIIQ PNAGMPVLEN GETRFPLGPE EFASYAPEFA KIGVSYLGGC CGTTPDHIRK VAEVLKDVPL TLPPKVKPFT ALTSRTKTVF IGDDYAPVKI GERINPTGRK KMREDIQKGS FVSVKKEGLA EVAAGADVLD VNMGVPGIDQ REAMETVISQ LSMLCPVPLS IDSTDPAVLE RALKVYPGRP LINSVNGADD EILEKVLKLA KTYGAAVLCL PLEKGNLPKT ADERIRIASA IIDKALKAGL RKEDLLLDPL VLTIGSSDTG ARETLKTISL YKKEFGLPCV MGTSNVSFGL PARPRINAAF LTMAFACGMN APIINPLDKD IQDAFINARL LLGFDPGARD FIRAAALSEE PKAKSAPSED LPPLERIKAA VKNGEKEESA ALIKTLLDNG ISSETIIKEG LTAAMTEIGD GYGAGKVYLP QVMMAAEAMQ AAFKELKKIL PEMNSSAKGT LVIGTVKGDI HDLGKNIVAA LMENSGYRVI DLGKDVDPEV FVSAVKDHHA DLAGLCSLMT TTLPEMEHTV KALKEETPGV KILVGGAVVT QDYASRIGAP NYCRDGIAAV KIADRLTGKE E // ID H1D392_9FIRM Unreviewed; 287 AA. AC H1D392; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHO61999.1}; DE Flags: Fragment; GN ORFNames=HMPREF9453_02080 {ECO:0000313|EMBL:EHO61999.1}; OS Dialister succinatiphilus YIT 11850. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Dialister. OX NCBI_TaxID=742743 {ECO:0000313|EMBL:EHO61999.1}; RN [1] {ECO:0000313|EMBL:EHO61999.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=YIT 11850 {ECO:0000313|EMBL:EHO61999.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHO61999.1}. 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; ADLT01000079; EHO61999.1; -; Genomic_DNA. DR RefSeq; WP_008860571.1; NZ_JH591190.1. DR EnsemblBacteria; EHO61999; EHO61999; HMPREF9453_02080. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; FT NON_TER 287 287 {ECO:0000313|EMBL:EHO61999.1}. SQ SEQUENCE 287 AA; 31671 MW; 8C30F776E6F8B33C CRC64; MIEDILKKYP FIVLDGAFST ELERQGFSIN DELWSAIALY ERPDLVKAVH RSYFDAGSDI VTSASYQATL EGFEKKGFSR KEGRELLIRS VQLVQEARDE FLAESSPERR PVPLAAASVG PYGAFLADGS EYKGHYGKTR EELADFHRER LHILAEAGPD IFACETIPCL LEALAETDVL SEIKNASAWV SFSCKDGLHT CGDDYIGDCA KALDPIPCVK AIGVNCTAPE YVESLILEIR KYTSKPVVVY PNSGEHYDPS DKTWGGAAAD YADFVKIWQK AGARLIG // ID H1D4Y2_9FUSO Unreviewed; 142 AA. AC H1D4Y2; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHO21658.1}; GN ORFNames=HMPREF9466_00515 {ECO:0000313|EMBL:EHO21658.1}; OS Fusobacterium necrophorum subsp. funduliforme 1_1_36S. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=742814 {ECO:0000313|EMBL:EHO21658.1}; RN [1] {ECO:0000313|EMBL:EHO21658.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_1_36S {ECO:0000313|EMBL:EHO21658.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHO21658.1}. 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; ADLZ01000005; EHO21658.1; -; Genomic_DNA. DR RefSeq; WP_005953053.1; NZ_JH590846.1. DR EnsemblBacteria; EHO21658; EHO21658; HMPREF9466_00515. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 142 AA; 16182 MW; F5DDF29A85375959 CRC64; MLHEELSKRI LILDGAMGTV LQKYSLQSED FCGAVGCYEI LNETRAEIIL EVHKKYIEAG ADIIETNSFN CNAISLKDYQ LENKVYSLAK KSAEIARQAV EESGKKFMFS VLWDLPKKLK FFIRRCPLSG KFIVSRVERG IL // ID H1D4Y3_9FUSO Unreviewed; 160 AA. AC H1D4Y3; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHO21659.1}; GN ORFNames=HMPREF9466_00516 {ECO:0000313|EMBL:EHO21659.1}; OS Fusobacterium necrophorum subsp. funduliforme 1_1_36S. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=742814 {ECO:0000313|EMBL:EHO21659.1}; RN [1] {ECO:0000313|EMBL:EHO21659.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_1_36S {ECO:0000313|EMBL:EHO21659.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHO21659.1}. 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; ADLZ01000005; EHO21659.1; -; Genomic_DNA. DR RefSeq; WP_005953054.1; NZ_JH590846.1. DR EnsemblBacteria; EHO21659; EHO21659; HMPREF9466_00516. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 160 AA; 17977 MW; 0A66B24B0BECACDC CRC64; MFQELREAYY EQILGLVDGE VDGILIETVF DALNAKAAVI AAEEVFAFRK KALWICISAT VNEQGKLFTG QSMESLIFSL DGPSILSFGF NCSFGAKHLV PLIQKIQSCT TKYISLYPNA GLPNQNGDYM ETAEQMIQDL LPVIQNQKSE YVRRLLWNKL // ID H1DHD7_9PORP Unreviewed; 1175 AA. AC H1DHD7; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHP47820.1}; GN ORFNames=HMPREF9449_01673 {ECO:0000313|EMBL:EHP47820.1}; OS Odoribacter laneus YIT 12061. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Odoribacter. OX NCBI_TaxID=742817 {ECO:0000313|EMBL:EHP47820.1}; RN [1] {ECO:0000313|EMBL:EHP47820.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=YIT 12061 {ECO:0000313|EMBL:EHP47820.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHP47820.1}. 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; ADMC01000022; EHP47820.1; -; Genomic_DNA. DR RefSeq; WP_009136821.1; NZ_JH594596.1. DR EnsemblBacteria; EHP47820; EHP47820; HMPREF9449_01673. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 236 236 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 751 751 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1175 AA; 129644 MW; 1E74C3D98A2EF28C CRC64; MLKNLLEERI LILDGAMGTA IQQYQLEEKD FRGEEFVNHP VNLKGNNDIL SLTRPDIISR IHQSYIDAGA DIIETNTFNS NAVSQADYQC SADVYRLNYA GARLAREVAD KAGRPVYVAG SIGPTSKTLS LSPDVNQPAF RAIDFDTLAA TYAQQISGLI DGGVDILLVE TVFDGLNAKA ALYAIDKIQT EKATRLPVMI SATINDKSGR TLTGQSLEAL YTALAHYPLF SFGLNCSFGA KELLPFVEQL HKFLPCNLSL YPNAGLPNEM GEYDESPDYT AAFLKSMAQK GWLNIAGGCC GTTPAHIRAI RKALEGIAPR IPAKPFPSLV VSGLDNIVVD KALSNFVNVG ERTNVAGSAK FAKLIHADAY DEASNIARKQ IEDGASIIDI NMDDAMLDSA KEMATFIRII SNDPDIAKAA LMIDSSDWKT LLAGLKNAQG KCIVNSISLK EGEKEFLRKA AEIKRLGAAV VVMAFDEEGQ AVSYERKIAI CQRAFQLLTE QAGFAPENII FDVNILAIGT GMEEHNNYAV DFIRAVAWTK KHLPGSSTSG GVSNLSFSFR GNNPVREAMH SVFLYHAIAA GLDMAIVNPS LLQVYDDIDP QLLQAVEAVV LNKNPEATEH LIELAEKMKA HKTEEKTIKN ESWRTLSLEE RLIYALVKGI KEYLPEDISA ALQAYASPVE IIEGPLMKGM DKVGQLFGEG KMFLPQVVKS ARIMKEAVAI LQPAIEHSNS LKTSDIRKHK VVLATAKGDV HDIGKNIVHI VLSCNNMEVI DLGVMVDNHR ILEAARQYQA DIIGVSGLIT PSLAEMEDLC RLLEQAQLKI PLLVGGATTS SVHTAVKLAP LYSYGVLHGG DASRTAGLIK RLLQHPENYL QQIKTEQENI RQLYYKAHTS LVSYSEAQAA APQYDPESYL LPKAFGEHNL RARKLDLREL ADRIDWTPFF HFWGFKGKFP EIIYTHEEAD HTYQAALETL GQIIAGNEFE ASVLVKFFNA RSENNEIILE NGYHFPMLRQ QMRNSEYLSL ADFISPDPAF KSTIGIFCLK VSDTHKCTDC PDFNQLIRES LCARLTEALA EWMHEQLSEG LHMIRPAFGY PACPDHSLKK EVFQLLNAPA DIGVELTSSY AIIPTTSLCG MLIAHPQARY FNVTKISSEQ FHTYCQQRGF SPEEGKRLLG PLIDN // ID H1G3C9_9GAMM Unreviewed; 1253 AA. AC H1G3C9; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 01-APR-2015, entry version 18. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EHQ52250.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHQ52250.1}; GN Name=metH {ECO:0000313|EMBL:EHQ52250.1}; GN ORFNames=ECTPHS_06137 {ECO:0000313|EMBL:EHQ52250.1}; OS Ectothiorhodospira sp. PHS-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Ectothiorhodospira. OX NCBI_TaxID=519989 {ECO:0000313|EMBL:EHQ52250.1}; RN [1] {ECO:0000313|EMBL:EHQ52250.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PHS-1 {ECO:0000313|EMBL:EHQ52250.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHQ52250.1}. 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; AGBG01000010; EHQ52250.1; -; Genomic_DNA. DR RefSeq; WP_008931817.1; NZ_AGBG01000010.1. DR EnsemblBacteria; EHQ52250; EHQ52250; ECTPHS_06137. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHQ52250.1}; KW Transferase {ECO:0000313|EMBL:EHQ52250.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1253 AA; 138646 MW; 3D73D6325240F0B3 CRC64; MNSDRLTQLH QEIQRRIMIL DGGMGTMIQG YGLQEADYRG ARFADWPSDI KGNNDLLVLT QPGIIREVHA AYLEAGADIL ETNTFNATRI AMADYGMEDL VPEINREAAR LAREVADEYT RKTPDRPRYV AGILGPTNRT ASISPDVNDP GFRNVWFDEL VAAYREAAEA LLDGGVDILM IETVFDTLNA KAAVFAVEGL FEDRGERWPV MISGTITDAS GRTLTGQTTE AFWNSLRHAR PFSIGLNCAL GPKELRPYVE ELSRIADTHV SAHPNAGLPN EFGGYDETPA QMAEEISEWA GSGLLNIVGG CCGTTPDHIR AIREAVEKHP PRPVPEIAPA CRLSGLEPFN ITADTLFVNV GERTNVTGSA RFKRLIKDGD YETALEVAAE QVESGAQVID VNMDEGMLDA LEAMKRFLCL AAAEPDISRV PVMIDSSKWE VIETGLKCIQ GKGIVNSISL KEGEDIFIRQ ARLLRRYGAA VVVMAFDETG QADTEDRKVE ICRRAYQILT EVVGFPAEDI IFDPNIFAVA TGIEEHNNYG VDFIEATRRI KQTLPHALVS GGVSNVSFSF RGNNPVREAI HAVFLYHAIR AGMDMGIVNA GQLVVYDEIE PDLRERVEDV VLNRRPDGTE RLLEIADRFR DTGGETRKED LAWRSLPVAK RLEHALVKGI DAYVVEDTEE ARLTFDRPIH VIEGPLMDGM NVVGDLFGAG KMFLPQVVKS ARVMKKAVAH LIPYIEAEKS DDSKNNGRIL MATVKGDVHD IGKNIVGVVL QCNNFEVIDL GVMVPAQKIL EAAREHKVDV IGLSGLITPS LEEMTHLAAE LQREGFGTPL MIGGATTSRA HTAVKIAPAY EGVTVWVKDA SRAVGVAQSL VSPELRGPYG EKIRAEYADV RQQHAARRKT QDWLTLAEAR ANRTPVDWSG YTPPRPAVLD ADQAPSVGGP APEILRLHGP DSILLRFDDY PLDRLVDYID WTPFFRAWDL HAAYPRILED EIVGEEATRL FADARPMLRR IIDEGWLRAR AVVGFFPAAR VDADDIQLYR DAAGHEPLMR LHHVRQQTRK PRQAPNMCLS DFIAPQGSGP RDYLGAFAVT AGGGIDEHVA RFEAAHDDYS AIMIKALADR LAEAFAEHLH ERVRREFWGY AAGEALSNED LIKEKYQGIR PAPGYPACPE HTEKGLLWEL IDPVTHAGMT LTDSYAMSPA SSVSGFYFSH PESRYFAVGK LNRDQVEDYA RRKGMPLETA ERWLAPNLGY DPD // ID H1GEA4_LISIO Unreviewed; 617 AA. AC H1GEA4; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HMPREF0557_02347 {ECO:0000313|EMBL:EHN60833.1}; OS Listeria innocua ATCC 33091. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=1002366 {ECO:0000313|EMBL:EHN60833.1, ECO:0000313|Proteomes:UP000003597}; RN [1] {ECO:0000313|EMBL:EHN60833.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 33091 {ECO:0000313|EMBL:EHN60833.1}; 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 (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHN60833.1}. 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; AGCN01000033; EHN60833.1; -; Genomic_DNA. DR RefSeq; WP_003762590.1; NZ_JH556647.1. DR EnsemblBacteria; EHN60833; EHN60833; HMPREF0557_02347. DR Proteomes; UP000003597; Unassembled WGS sequence. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003597}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EHN60833.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EHN60833.1}. SQ SEQUENCE 617 AA; 68709 MW; FECA51509A8F77CD CRC64; MNLRKDLSEK VLIADGAMGT LLYSYGVDRS FEELNLSHPE DIVAIHKAYI GAGADIIQTN TYGANYIKLA RYGLEDEVKR INQAAIRLAK EAARGTGTYI FGTIGGINGA VDARLPAAPL EEIKRSFREQ LYCFLLDGVD AILLETYYDL DELKTVLKIL RETTDLPVVA NVSMHEPGIL QNGKKLPDAL EELIALGADV VGINCRLGPY HMARALETVP LYDKAYLAVY PNASLPEVQE GKVIYQSDTD YFEHYGEVFR QEGARIIGGC CGTTPDHIRA LRKGLESTKP VLEKEVRPIL ELVPEEVEDE ESGERLLDKV KERLTILVEL DPPRTFDTSK FFEGAKALDE AGVDAITISD NSLATPRISN MALASILKHE YGIKPLIHLT TRDHNLVGMH SHVMGFHKLG LHDVLAITGD PTKVGDFPGA SSVFDLRSVE LVQLIKKFND GISYTGKSLK EKARFHVGAA FNPNVLNLEK AVRLIERKVE YGADYIITQP IYDVNKAVLL KEALQKANID VPLFIGVMPL LSSRNAEFLH NEVPGIRLTD EVRERMREAE EHGRANEEGM TIARELVDAI CEHFQGIYII TPFLRYDLSI ELAKYVQNKQ QLQIASK // ID H1H2S9_9FLAO Unreviewed; 1243 AA. AC H1H2S9; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHO15229.1}; GN ORFNames=HMPREF9715_00417 {ECO:0000313|EMBL:EHO15229.1}; OS Myroides odoratimimus CIP 101113. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Myroides. OX NCBI_TaxID=883154 {ECO:0000313|EMBL:EHO15229.1, ECO:0000313|Proteomes:UP000004834}; RN [1] {ECO:0000313|EMBL:EHO15229.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIP 101113 {ECO:0000313|EMBL:EHO15229.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHO15229.1}. 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; AGEE01000003; EHO15229.1; -; Genomic_DNA. DR RefSeq; WP_006262644.1; NZ_JH590837.1. DR EnsemblBacteria; EHO15229; EHO15229; HMPREF9715_00417. DR Proteomes; UP000004834; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000004834}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 249 249 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 769 769 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1243 AA; 138600 MW; 40E6A6B83B6284E2 CRC64; MSTTLIHTDI RSLLKQRTLV LDGAMGTMLQ AYRFSEEDFR GERFADFAHP LKGNNDLLSI TQPDAVKEVH RQYLLAGADI LSTNTFSGTT IAMADYHLED IVYELNYQSA KIAREVADEV EALDPNKPRY VAGAIGPTNK TASLSPDVNN PGYRAITFEE LRIAYKQQAE ALLDGGCDLL LVETIFDTLN AKAALFAIDE IQAERGIDIP IMISGTITDA SGRTLSGQTV EAFLISIAHI PLLSIGFNCA LGAEQLEPYV KQLSQHAAVN ISAHPNAGLP NAFGEYDQTP TEMKELIDSF LSQNLVQIIG GCCGTTPEHI KLIAQAVAEH SKDRQPKQFN LKPVLALSGL EPLYVTAEAN FINIGERTNV TGSRKFLRLI KEEKFDEALA VAREQVEGGA QVIDINMDEG LLDGVHCMTN FLNLIASEPD IAKVPIMIDS SKWEIIEAGL RVVQGKAIVN SISLKEGEEL FIEHAKLIKR YGAASVVMAF DEKGQADSLE RRIEICQRSY DILVNQVNFA PQDIIFDPNI FPVATGMEEH NNNALDFFNA TKWIRENLPY ANVSGGVSNV SFSFRGNNKV REAMHAAFLY HAIQHGMNMG IVNPEMLEVY DEVDKDLMEH VEDVLLNRRD DATERLLDFA ESIKNESAIQ STEIKVEEWR SGSIQDRLTH ALVKGIETYV IEDTEEARLS VPQPIQVIEQ YLMNGMNVVG DLFGAGKMFL PQVVKSARVM KKAVAYLLPF IEESKKQNAE ASVGNAGKIL MATVRGDVHD IGKNIVAVVL ACNNYEIIDL GVMVPPEKII ETAIKEQVDI IGLSGLITPS LDEMVHLAKE LDKVNSNIPI MIGGATTSRV HTAVKIAPEY KNCVVHVHDA SRSVTIANQL LQKEIEATFK DNIREEYDQL RRDYLGRARD KSYITIEQAR ANKVKIEWDA KDIVKPNFIG TKTVTVELDE LLPFIDWAPF FRSWQLYGKF PQILTDEVVG QTATQVYDDA LIMLDKIINE RWFEARGVLG IFPANQVNDD DIEVYNEQGE TLDKLLTLRQ QSLKNIKAPN IALADFVAPK ESGLEDYIGL FAVSTGFGVD EIAKEYEDDL DDYNAIMVKA LADRLVEAFA EYLHHRVRKE IWGYASAERL SNEELIKEAY QGIRPAPGYP ACPDHLEKGT IWKLLQVEER IGVSLTESYA MFPAAAVSGY YFAHPQSRYF GLGKIEQDQL EDYANRRNIS IEEAERWLSP NLAQNNKLTT NES // ID H1HF88_FUSNU Unreviewed; 1081 AA. AC H1HF88; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHO77951.1}; GN ORFNames=HMPREF9942_01139 {ECO:0000313|EMBL:EHO77951.1}; OS Fusobacterium nucleatum subsp. animalis F0419. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=999414 {ECO:0000313|EMBL:EHO77951.1, ECO:0000313|Proteomes:UP000004565}; RN [1] {ECO:0000313|EMBL:EHO77951.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=OT 420 {ECO:0000313|EMBL:EHO77951.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHO77951.1}. 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; AGEH01000012; EHO77951.1; -; Genomic_DNA. DR RefSeq; WP_005909883.1; NZ_JH594451.1. DR EnsemblBacteria; EHO77951; EHO77951; HMPREF9942_01139. DR Proteomes; UP000004565; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000004565}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 723 723 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1081 AA; 120879 MW; D5C69FB38582536D CRC64; MFEIEKELRE RILVLDGAMG TVLQKYELSA EDFNGAKGCY EILNETRPDI IFEVHKKYIE VGADIIETNS FNCNAISLKD YHLEDKVYDL AKKSAEIARD AVKESGKKVY IFGSVGPTNK SLSFPVGDIP FKRAVSFDEM KEVIKVQVAG LIDGGVDGIL LETIFDGLTA KAALLATEEV FEEKNIKLPI SISATVNKQG KLLTGQSMES LIVALDRDSV TSFGFNCSFG AKDLVPLVIK IKELTTKFVT LHANAGLPNQ NGDYVETAQK MKNDLLPLIE NQAINILGGC CGTSYDHIKA IAELVKGQKP RVLPEKNLLE TCLSGNEIYN FKDKFTCVGE RNNISGSKLF RTMIEEHNYL KALDVARQQI DAGAKVLDIN VDDAILDSVE EMKNFLRVLQ NDSFIAKVPI MIDSSDFAVI EEGLKNTAGK AIVNSISLKE GEEKFLRKAK IIRKYGASII VMAFDENGQG VSAERKIEIC QRAYNLLKSI GVKNSDIVFD PNILSVGTGQ EADRYHAREF LKTIDYIHKN LKGCGIVGGL SNLSFAFRGN NILRAAFHHI FLEEAIPRGF NFAILNPKEK APQWTDEERE KIKSFIFGDS TNIEDLLSLN LVKRKEDAQI FAETPENRIR KALIQGGSES LQEVIEELLK KYKALEILEN ILMSAMQEIG RLFEQGELYL PQLIRSASVM NNCVNILTPY LEKVDRTSSK GKILMATVDG DVHDIGKNIV KTVLECNGYE VIDLGVMVPR EKIVEVAKNN NVDIVTLSGL ISPSLKEMER VADSFQKVGM QIPILIAGAA TSKLHTGLKV LPNYDYSLHV TDAMDTITVV SQLLSTKRKD FLEAKQNQLR KIAKRYIENN DQTGEKKVLP EVKKTVSYIP KVLGKQFLSL PVEILKDDLK WDIAFYALRV KNTPEEEKTL NDLKKIYEKL IEEKVEFRAA YGYFRCKKTE TFLEMEGMTF EVSPNIAQYI EKEDYLGAFV VSVKSEIFKD DKYLGLLETL LCNVIAEAAS EYMERRVSKD IVPTFLRPAV GYPILPDHSL KKIVFDLIDG EKTGAKLSPA FAMSPLSSVC GFYLCNDNAK Y // ID H1HM16_9BACT Unreviewed; 921 AA. AC H1HM16; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHO70809.1}; GN ORFNames=HMPREF9944_01210 {ECO:0000313|EMBL:EHO70809.1}; OS Prevotella maculosa OT 289. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=999422 {ECO:0000313|EMBL:EHO70809.1}; RN [1] {ECO:0000313|EMBL:EHO70809.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=OT 289 {ECO:0000313|EMBL:EHO70809.1}; 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 Prevotella maculosa OT 289."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHO70809.1}. 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; AGEK01000023; EHO70809.1; -; Genomic_DNA. DR RefSeq; WP_008565115.1; NZ_JH594502.1. DR EnsemblBacteria; EHO70809; EHO70809; HMPREF9944_01210. DR OrthoDB; EOG6091CH; -. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 242 242 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 764 764 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 921 AA; 101130 MW; DEB9B4C6B0633838 CRC64; MKGLRELVKE RILILDGAMG TMVQSYHLSE SDFRGLRFKQ EDGRQMKGNN DLLCLTRPDV VLDIHRRYLA AGADIIETNT FSAQSISQAD YGLQDICYEL SYEGARLARQ AADELTTEEK PRFVAGAVGP TNKTCSMSPD VSDPAARDLT YDALFAAYEE QIRGLLDGGV DALLIETIFD TLNAKVAIDV AVSLMEQRGL DLPIMLSVTV SDLAGRTLSG QTLEAFLGSI SSYPVFSVGL NCSFGAHQMK PYLKELGKKS PYYISAYPNA GLPNSMGQYD ETAESMSPQI AEFMDEGLVN IVGGCCGTTD EFIRRYTEMA EGKPSRQPIE KPESMWLSGL ELLEVSKEVR FVNVGERCNV AGSKKFLRLI KEKNYEEALT IARKQVTDGA LVIDVNMDDG LLDARTEMVN FLNLIASEPD VAKVPVMIDS SKWDVITAGL KCMQGKCIIN SISLKNGEAE FVCHARDAKR YGAAIVVMCF DETGQATTYE RKIEIAERAY RILVDKVGFN PLDIIFDPNI LSIATGIEEH DNYAVDFIKA TAWIKQHLPG AHISGGVSNL SFSFRGNDYI REAMHAVFLY HAIHEGMDFG IVNPATKVTY ADIPADRLRI IEDVVLNRKP GAAEELIELA GRIKAEAEEA KANGTSVGSS NAEQHEAWRE QPVDKRLAYA LRKGIGNYME EDLAEALRQY PHAVNIIEGP LMDGMNEVGE LFGEGKMFLP QVVKTARTMK QAVAILQPHI EAEKTGDSYK AGKIVLATVK GDVHDIGKNI VGVVMACNNY DVIDLGVMVP AEQIVRKAIA EKADMIGLSG LITPSLEEMV NVAKEMKKAG LDIPIMIGGA TTSQLHVALK IAPVYGGPVV WMKDASQNAL IAAKLLNDAE RQTLTNDLNA KYADLREGYN QEQQKLLSLE EARKNKLDLF S // ID H1HS00_9FIRM Unreviewed; 817 AA. AC H1HS00; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 01-APR-2015, entry version 18. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHO18186.1}; GN ORFNames=HMPREF9623_00370 {ECO:0000313|EMBL:EHO18186.1}; OS Stomatobaculum longum. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Stomatobaculum. OX NCBI_TaxID=796942 {ECO:0000313|EMBL:EHO18186.1}; RN [1] {ECO:0000313|EMBL:EHO18186.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ACC2 {ECO:0000313|EMBL:EHO18186.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHO18186.1}. 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; AGEL01000003; EHO18186.1; -; Genomic_DNA. DR RefSeq; WP_009532204.1; NZ_JH590861.1. DR EnsemblBacteria; EHO18186; EHO18186; HMPREF9623_00370. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; SQ SEQUENCE 817 AA; 88395 MW; 8AFA9C51610D991A CRC64; MEKRSLRACL GKEWLYCDGG TGSLLQEKGL KGGELPERWN LERPEDVIEI AESYFRAGAD IVNTNTFGAN RLHYPDRAEL EQIVRAGVRH VREGLSRSGR TDGFVALDLG PTGRLLKPMG DLEFETCVEI FAEVVRWGKE EGADLVLIET MSDAMEAKAA VLAAKENSDL PVFVTVVFDE KGKTLTGGTV ESVTAMLEGL RIDALGVNCG LGPVQLYPIV KALTEVCSIP IVVNPNAGLP HAKDGKTYYD LSAEEFSDEM KKIASLGVQV LGGCCGTTPE HIRLEIQKTG ELPFCEPVKK HRAVVSSFSQ TVVLGKRPII IGERINPTGK KRFKEALRNG DIEYILEQGI EQEDAGADML DVNVGLPELN EPDMMETVMT RLQGVTALPL QLDTTNLEAL ERGLRLYHGK AMINSVNGKE ESLETVLPLV AKYGGVVVGL ALDEGGIPED AEGRIRVAKK IYARAAAYGI PPEDIIIDGL AMTISTDDNS ANVTLEVLRR VRDELHGHSI LGVSNISFGL PQRELINSFF FALAMKSGLS CAIINPNNEA MMAAYRSYLA LSGFDRQCQG YIAEYAGKAN VFAGKGKVVV TAEGGEKAKI GSAELPEGMQ GSPLIDAIRF GLGEKATEET KRRIAEGEAP LDIVNRELIP ALDVVGKGFE KGTLFLPQLL MSAEAAKAAF EVIKSAMSGT ARKERGSVIL ATVKGDIHDI GKNIVKVLME NYGYKVYDLG RDVPAETIVE TAVAHDVKLI GLSALMTTTV VNMEDAIKLI RERKPDAKVV VGGAVMTKEY ADDIGADCYA KEAMDTVRYA DTLFPEA // ID H1KKL1_METEX Unreviewed; 1250 AA. AC H1KKL1; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHP91951.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHP91951.1}; GN ORFNames=MetexDRAFT_3173 {ECO:0000313|EMBL:EHP91951.1}; OS Methylobacterium extorquens DSM 13060. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=882800 {ECO:0000313|EMBL:EHP91951.1}; RN [1] {ECO:0000313|EMBL:EHP91951.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 13060 {ECO:0000313|EMBL:EHP91951.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHP91951.1}. 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; AGJK01000084; EHP91951.1; -; Genomic_DNA. DR RefSeq; WP_003601080.1; NZ_AGJK01000084.1. DR EnsemblBacteria; EHP91951; EHP91951; MetexDRAFT_3173. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHP91951.1}; KW Transferase {ECO:0000313|EMBL:EHP91951.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 254 254 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 318 318 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 771 771 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1250 AA; 137091 MW; F1A45A89E1BA55FF CRC64; MTAFPPVDGT EIERALRQRA SEKILVLDGA MGTVIQRLKY TEEDFRGERF KDHSHDQKGN NDLLILTQPD AIRQIHLDYF LAGADVCETN TFSGTTIAQA DYGMESIIHE LNAEGARLAR EAAKLAEEQD GRRRFVAGAI GPTNRTLSIS PDVNNPGYRA VTFDGVKQAY VEQVRGLIDG GAELILIETI FDTLNAKAAI AAAWQVFDET GIRLPIQISG TITDLSGRTL SGQTPAAFWN SLRHSSPLTF GLNCALGAKE MRGHIAELSR ICDTLVCAYP NAGLPNEFGL YDESPEAMGK LVGEFAASGL VNMVGGCCGT TPDHIRAIAE AVADKKPREI PEIPRLMRLS GLEPFVLTKE IPFVNVGERT NVTGSAKFRK LITNNDYAAA LDVARDQVAA GAQVIDVNMD EGLLDSEKAM VEFLNLVAAE PDIARVPVMV DSSKFEVIEA GLKCIQGKPI VNSISMKEGE AKFIEAAKIC RSYGAAVVVM AFDEQGQADS YERKVEICTK AYKILTEQVG FPPEDIIFDP NIFAVATGIE EHNPYGVAFI EATRTIRETL PHAHISGGVS NLSFAFRGNE PVREAMHAVF LFHCIKAGMD MGIVNAGQLA VYDEIPAELR ELCEDVVLNR REDSTERLLE AAERFKTGAS AQAKTADLTW REAPVAKRIE HALVNGITEY IVADTEEARK EAARPLHVIE GPLMAGMNVV GDLFGSGKMF LPQVVKSARV MKQAVAYLEP FMEEEKRANG GDGKRQAAGK VLMATVKGDV HDIGKNIVGV VLACNNYEII DLGVMVPAAK ILETAKRENV DIVGLSGLIT PSLDEMVHVA AEMEREGMEM PLLIGGATTS RVHTAVKIHP AYAKGQAVYV TDASRAVGVV SSLISKETRG ATVEKVRAEY AKVADAHRRS EADKQRLPLA KARANAFKVD WSAYKPAKPS FTGTRVYGSY EVADLVPYID WTPFLQTYEF KGRYPAILDD PEQGPAARAL FEDAQVMLKQ IVEERWFNPK AVIGFWPANS VGDDIRLFTG ESRQETLATF HGLRQQLSKR DGRANTCISD FVAPAETGIA DYVGAFVVTA GLEEVRIAER FERANDDYRS ILVKALADRI AEAFAERMHE RVRKEFWGYA PDEAYAPEEL VSEKYDGIRP APGYPAQPDH TEKVQLFDLL KAESRIGVKL TESYAMWPGS SVSGLYLAHP DAHYFGVAKV ERDQVEDYAL RKGMDVSEVE RWLGPILNYD PVRYLKAAAE // ID H1LKB7_9LACO Unreviewed; 282 AA. AC H1LKB7; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EHO47591.1}; GN ORFNames=HMPREF9104_03063 {ECO:0000313|EMBL:EHO47591.1}; OS Lactobacillus kisonensis F0435. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=797516 {ECO:0000313|EMBL:EHO47591.1}; RN [1] {ECO:0000313|EMBL:EHO47591.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0435 {ECO:0000313|EMBL:EHO47591.1}; 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-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. {ECO:0000313|EMBL:EHO47591.1}. 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; AGRJ01000257; EHO47591.1; -; Genomic_DNA. DR RefSeq; WP_008858209.1; NZ_JH591058.1. DR EnsemblBacteria; EHO47591; EHO47591; HMPREF9104_03063. DR OrthoDB; EOG6091CH; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHO47591.1}; KW Transferase {ECO:0000313|EMBL:EHO47591.1}. SQ SEQUENCE 282 AA; 30470 MW; BB542F47F65AFD51 CRC64; MVLNFNQLKS PLLFDGAMGT MLISAVPGIK QPVSLANLTH PELVQQIHQA YVAAGCDIVT TNTFQLHQSD FTPTQVAQVV ATGIQLAKSA HPKWVAYDMG PVNDPREHLT TNQLYERFKQ QALLAEKGQV DFILIETMTN LQEARMAVKA VHENTQLPVA VTFSFQPNGL LPTGEDGEAV TRYLQNLAVD ALGLNCGFGP ASMMQILGAV LMTSRVPVIV QPNTSVPYSD NGNFDQQTQP ATFAAAMGKM LAQGVQLIGS CCGSTPTVTG EVRKLIDQFD LK // ID H1LQJ8_9PAST Unreviewed; 1229 AA. AC H1LQJ8; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EHO46326.1}; GN ORFNames=HMPREF9096_01571 {ECO:0000313|EMBL:EHO46326.1}; OS Haemophilus sp. oral taxon 851 str. F0397. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=762965 {ECO:0000313|EMBL:EHO46326.1}; RN [1] {ECO:0000313|EMBL:EHO46326.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0397 {ECO:0000313|EMBL:EHO46326.1}; 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-2011) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHO46326.1}. 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; AGRK01000030; EHO46326.1; -; Genomic_DNA. DR RefSeq; WP_009500823.1; NZ_JH591082.1. DR EnsemblBacteria; EHO46326; EHO46326; HMPREF9096_01571. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHO46326.1}; KW Transferase {ECO:0000313|EMBL:EHO46326.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 757 757 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1229 AA; 136180 MW; AE949B535BB6F100 CRC64; MVNKTAQLKQ ALENRILILD GAMGTMIQKY KLTEADFRGE KFKESAVDLR GNNDLLTLTQ PLLISAIHEK YLAAGADIIE TNTFSSTTIA QADYDLQSIA YELNFVGAKL ARLAADKYST PEKPRFVAGV LGPTNRTASI SPDVNDPGFR NVTFMELVDA YAQATKGLIE GGADLIMIET IFDTLNAKAA VFAIESVFEE LGMELPIMIS GTITDASGRT LSGQTTEAFY NSLRHAKPLT FGLNCALGPK ELRQYVEQLS KISETYVSVH PNAGLPNAFG GYDLGAEDMA AHLKEWAESG FVNIIGGCCG TTPEHIKAFA EAVENIPPRK LPQIKTAMRL SGLEPLNIDD ESLFVNVGER NNVTGSAKFK RLIKEDKFAE AIEIAIDQVE NGAQVIDVNM DEALLDGKKC MTRFLNIMAT EPDAAKVPVM IDSSKWEVIE AGLQSVQGKP IVNSISLKEG EEKFIHQAKL VRKYGAAVVV MAFDEVGQAD TEERKVEICT RAYNILVNQV GFPPEDIIFD PNIFAIGTGI EEHNNYGVDF INATGRIKRS LPHAKISGGV SNVSFSFRGN NVMREAIHAV FLYHAIKQGM DMGIVNAGQL AIYDDLDPEL RNVIEDAVLN RTPDGTERLL DIAEKYRNQG NDESAVDSVA EWRTWPVEER LKHALVKGIT THIIEDTEEA RQKLPTPLEV IEGPLMAGMD VVGDLFGDGK MFLPQVVKSA RVMKQSVAYL EPFINSTKQK GSSNGKVVIA TVKGDVHDIG KNIVSVVLQC NNFEVIDLGV MVPADKIIQT AIDEKADIIG LSGLITPSLD EMEYFLGEMT RLGLNLPVLI GGATTSKEHT AIKLYPKYKQ HGVFYTSNAS RAVTVCATLM NPEGCAALWE QFKKDYEKIQ QSFANRKPLR KQLSIEDARA NRFDGFSGEW ADYVPPTPNQ TGIVEFKNVP IAELRKFIDW SPFFRIWGLM GGYPDAFDYP EGGEEARKVW NDAQVVLDEL EQNHKLNPSG ILGIFPAERV GDDVVLFSDE ERTQSIGTAY GLRQQTERGK NSKSPFNFCL SDFVADRESG KKDWFGMFAV CAGIEEMDLV EGYKAAGDDY NAILLQAVGD RLAEAMAEYL HFELRTRIWG YTQEEFDNQG LINENYVGIR PAPGYPSCPE HTEKALIWDL LEVEQRIGMK LTESYAMWPA ASVCGWYFTH PASNYFTLGR IDEDQAQDYA KRKGWDEREM MKWLGVAMK // ID H1LV03_9FIRM Unreviewed; 322 AA. AC H1LV03; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EHO52656.1}; GN ORFNames=HMPREF9099_01289 {ECO:0000313|EMBL:EHO52656.1}; OS Lachnospiraceae bacterium oral taxon 082 str. F0431. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=861454 {ECO:0000313|EMBL:EHO52656.1}; RN [1] {ECO:0000313|EMBL:EHO52656.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0431 {ECO:0000313|EMBL:EHO52656.1}; 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-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. {ECO:0000313|EMBL:EHO52656.1}. 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; AGRL01000078; EHO52656.1; -; Genomic_DNA. DR RefSeq; WP_009445731.1; NZ_JH591135.1. DR EnsemblBacteria; EHO52656; EHO52656; HMPREF9099_01289. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHO52656.1}; KW Transferase {ECO:0000313|EMBL:EHO52656.1}. SQ SEQUENCE 322 AA; 35478 MW; E36C68585915A66F CRC64; MDNIREYLKN NVLLFDGAMG TYYDELTDDG IGCELANIKN PELIKGIHNE YIEAGAKAIL TNTFSVGIDV FNGDRSLQKE VVVAGIDIAN EAAKDRAYVF ADIGPIHTGS SELAFEEYKI LIDIFLEKGV KNFLFETRSS TSGMVLSAEY IKEKCSDAFI TASFAVMPDG YSSEGYQYKA LFAEITNSGV FDAVGLNCVS GANHMAKLLK DVDTKGLYLF AKPNAGYPVV RDDRVYYSSL ANYFANQIED ILEMGVNIVG GCCGTTPKHI ELLKKSMSGK LIKPRRAVKS EKNAVQNIRV NRFKEKLDLG QKPIAVELVT HL // ID H1LV04_9FIRM Unreviewed; 788 AA. AC H1LV04; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EHO52657.1}; GN ORFNames=HMPREF9099_01290 {ECO:0000313|EMBL:EHO52657.1}; OS Lachnospiraceae bacterium oral taxon 082 str. F0431. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=861454 {ECO:0000313|EMBL:EHO52657.1}; RN [1] {ECO:0000313|EMBL:EHO52657.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0431 {ECO:0000313|EMBL:EHO52657.1}; 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-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. {ECO:0000313|EMBL:EHO52657.1}. 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; AGRL01000078; EHO52657.1; -; Genomic_DNA. DR RefSeq; WP_009445732.1; NZ_JH591135.1. DR EnsemblBacteria; EHO52657; EHO52657; HMPREF9099_01290. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHO52657.1}; KW Transferase {ECO:0000313|EMBL:EHO52657.1}. SQ SEQUENCE 788 AA; 85787 MW; 2C99DCAF8574B025 CRC64; MHNLLILDGA MGTMLQAAGM KAGEHPEVFG FDNPDIVKNI HLKYIEAGSN IIYANTFGAN AHKLEGCKID VDTAIKTAIQ SAKEAVAESK RDVKVALDIG PIGELLEPLG VLRFEDAYDI YKEMVVAGEK YGADIIVYET FTDLYDVRAG VLAAKENTKL PVWVTMTYET TGRTFTGTKI ESMAVTLEGL GVDAIGFNCS LGPKEIFPLA KKLKEWTTLP IIIKPNAGLP NPSTGEYDLH AADFAKLMAE YKSLGISYAG GCCGTAPDFI KELKSELDAT EAKEGKSVKV KTGICSANEM VELNGVRVVG ERLNPTGKKR FQEALLNHEM EYICKVAIEE EESGADILDI NVGVPGGDEV ALMREAVKAV QSVVNIPLQI DSSNPEAIEA GLRVYNGRAI VNSVNAEDER LDLILPIVKK YGAAVIGLAL NENGLPTTAK QRVDNASHIL ERCLEYGLKK EDVIIDCLTL TVSAQQDQAR ETLEAVRMVT NDLGLHTTLG VSNISFGLPA RSHITENFLI QAMYAGLDLP IVNPNIEGIM NAIYSFKVLS GEDKDSVKYI ERFATVKTET KVVTVSNNGE VTKEMVEDAI LKGLKEETYN NAKKLLETKG ELEIINEYLI PALDTVGDLY EKQVIFLPQL INAANAASSA FELIKERIAN KGEHNVSKGK IVVCTVKGDI HDIGKNIVKV ILENYGYRMI DLGRDVDIKN VVDTVVRENV KLVGLSALMT TTLPAMKKTI EEIRKVSNDC KVWVGGAVLT KEYADEMGAD FYAPDARSSV DIAKTVLG // ID H1QK09_9ACTO Unreviewed; 309 AA. AC H1QK09; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 01-OCT-2014, entry version 11. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:EHN75230.1}; GN ORFNames=SMCF_5294 {ECO:0000313|EMBL:EHN75230.1}; OS Streptomyces coelicoflavus ZG0656. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1120227 {ECO:0000313|EMBL:EHN75230.1}; RN [1] {ECO:0000313|EMBL:EHN75230.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ZG0656 {ECO:0000313|EMBL:EHN75230.1}; 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. {ECO:0000313|EMBL:EHN75230.1}. 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; AHGS01001196; EHN75230.1; -; Genomic_DNA. DR EnsemblBacteria; EHN75230; EHN75230; SMCF_5294. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHN75230.1}; KW Transferase {ECO:0000313|EMBL:EHN75230.1}. SQ SEQUENCE 309 AA; 32260 MW; E9DD7EF3905F2D5A CRC64; MTSDFADALA SGPLVLDGGL SNQLEAAGHD LGDALWSARL LADDPEAITR AHLAYFEAGA DVVITSSYQA TFEGFARRGI GGQRAAELLA LSVESAREAA RRARVGPAGG AGRRLWVAAS AGPYGAMLAD GSEYRGRYGL DVGELERFHR PRLEVLAAAR PDVLALETVP DTVEAVALLR AVRGLGVPAW LSYTVDGDRT RAGQPLEEAF ALAADAEEVV AVGVNCCAPG DVSGAVRTAA RVTGKPVVAY PNSGEVWDAR ARAWRGRSLF APRLVREWRA AGARLVGGCC RVGPDAIRSI ASAPSSDPS // ID H1QNQ9_9ACTO Unreviewed; 1170 AA. AC H1QNQ9; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 01-APR-2015, entry version 20. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHN73927.1}; GN ORFNames=SMCF_6624 {ECO:0000313|EMBL:EHN73927.1}; OS Streptomyces coelicoflavus ZG0656. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1120227 {ECO:0000313|EMBL:EHN73927.1}; RN [1] {ECO:0000313|EMBL:EHN73927.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ZG0656 {ECO:0000313|EMBL:EHN73927.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHN73927.1}. 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; AHGS01001398; EHN73927.1; -; Genomic_DNA. DR EnsemblBacteria; EHN73927; EHN73927; SMCF_6624. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 238 238 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 748 748 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1170 AA; 127963 MW; 66329F7E539E5F19 CRC64; MASSPSTPPA DTRTRVSALR EALATRVVVA DGAMGTMLQA QNPTLEDFQQ LEGCNEVLNL TRPDIVRSVH EEYFAVGVDA VETNTFGANH SALGEYDIPE RVHELSEAGA RVAREVADEF AARDGRQRWV LGSMGPGTKL PTLGHAPYPV LRDAYQRNAE GLVAGGADAL LVETTQDLLQ TKASVLGARR ALDALGLDLP VIVSVTVETT GTMLLGSEIG AALTALEPLG IDMIGLNCAT GPAEMSEHLR YLARHSRVPL SCMPNAGLPV LGKDGAHYPL TAPELADAQE TFVREYGLSL IGGCCGTTPE HLRQVVERVR GTAPTARDPR PEPGAASLYQ TVPFRQDTSY LAIGERTNAN GSKKFREAML EGRWDDCVEM ARDQIREGAH MLDLCVDYVG RDGVADMEEL AGRFATASTL PIVLDSTEVD VIRAGLEKLG GRAVINSVNY EDGAGPESRF ARVTTLAREH GAALIALTID EVGQARTAEK KVEIAERLID DLTGNWGIHE SDILVDCLTF TICTGQEESR KDGLATIEGI RELKRRHPDV QTTLGLSNIS FGLNPAARIL LNSVFLDECV KAGLDSAIVH ASKILPIARF DEEQVTTALD LIYDRRREGY DPLQKLMQLF EGATAKSLKA SKAEELAALP LEERLKHRII DGEKNGLEQD LDAALQERPA LDIVNDTLLD GMKVVGELFG SGQMQLPFVL QSAEVMKTAV AHLEPHMEKT DDDGKGTIVL ATVRGDVHDI GKNLVDIILS NNGYTVVNLG IKQPVSAILE AADEHRADVI GMSGLLVKST VIMKENLEEL NQRKLASDYP VILGGAALTR AYVEQDLHEI YDGEVRYARD AFEGLRLMDA LIGIKRGVPG AKLPELKQRR VRAATVEIEE RPEEGSVRSD VATDNPVPAP PFRGTRVVKG IQLKEYASWL DEGALFKGQW GLKQARTGEG PSYEELVESE GRPRLRGLLD RLQTDNLLEA AVVYGYFPCV SKDDDLIVLD EAGNERTRFT FPRQRRGRRL CLADFFRPEE SGETDVVGFQ VVTVGSRIGE ETARMFEANA YRDYLELHGL SVQLAEALAE YWHARVRSEL GFAGEDPAEM EDMFALKYRG ARFSLGYGAC PDLEDRAKIA ALLEPERIGV HLSEEFQLHP EQSTDAIVIH HPEAKYFNAR // ID H1RIT6_COMTE Unreviewed; 358 AA. AC H1RIT6; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EHN67469.1}; GN ORFNames=CTATCC11996_00370 {ECO:0000313|EMBL:EHN67469.1}; OS Comamonas testosteroni ATCC 11996. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Comamonas. OX NCBI_TaxID=1009852 {ECO:0000313|EMBL:EHN67469.1}; RN [1] {ECO:0000313|EMBL:EHN67469.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 11996 {ECO:0000313|EMBL:EHN67469.1}; 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHIL01000002; EHN67469.1; -; Genomic_DNA. DR RefSeq; WP_003071808.1; NZ_AHIL01000002.1. DR EnsemblBacteria; EHN67469; EHN67469; CTATCC11996_00370. DR GeneID; 8565368; -. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHN67469.1}; KW Transferase {ECO:0000313|EMBL:EHN67469.1}. SQ SEQUENCE 358 AA; 38453 MW; B2BF22F3E2C5C011 CRC64; MSQSHPTPAY TRAQELPATL AKRLVILDGA MGTMIQRFKL GEAQYRGEGY AGAEGAGERF KDFAHDVKGN NELLSLTRPD VIRDIHEKYL AAGADLIETN TFGATTIAQE DYHMADLAYE MNLKSAQLAR AACDKYSTPD HKRYVAGALG PTPKTASISP DVNDPAARNI TFEQLRQAYL EQTLALIEGG ADVILVETIF DTLNAKAALF AVDEAFEQTG ERLPIMISGT VTDASGRILS GQTVTAFWHS VRHSNPLSVG LNCALGATLM RPYVQELAKA APDTFISCYP NAGLPNPMSD TGFDETPEIT SRLVHEFAAE GLVNIVGGCC GTTPDHIGAI AKAVQATATR KLFYPAEA // ID H1SBV9_9BURK Unreviewed; 355 AA. AC H1SBV9; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EHP40016.1}; GN ORFNames=OR16_28404 {ECO:0000313|EMBL:EHP40016.1}; OS Cupriavidus basilensis OR16. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Cupriavidus. OX NCBI_TaxID=1127483 {ECO:0000313|EMBL:EHP40016.1}; RN [1] {ECO:0000313|EMBL:EHP40016.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=OR16 {ECO:0000313|EMBL:EHP40016.1}; 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. {ECO:0000313|EMBL:EHP40016.1}. 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; AHJE01000076; EHP40016.1; -; Genomic_DNA. DR RefSeq; WP_006161305.1; NZ_AHJE01000076.1. DR EnsemblBacteria; EHP40016; EHP40016; OR16_28404. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHP40016.1}; KW Transferase {ECO:0000313|EMBL:EHP40016.1}. SQ SEQUENCE 355 AA; 38216 MW; 0B76E7ACDE39963F CRC64; MSAAPRSASL PPARPYTRAA NLPALLRERI LILDGAMGTM IQRYKLTEAD YRGERFAGHH VDVKGNNELL LLSRPQVISE IHEQYLAAGA DLIETNTFGA TGVAQEDYKM ADLAYEMNVV AARLAREACD KYSTPDKPRF VAGAFGPTPK TASISPDVND PGARNVTFEE LRHSYYEQGK GLLEGGADVF LVETIFDTLN AKAALFAIDQ LFEDTGERLP VMISGTVTDA SGRILSGQTV EAFWNSLRHA RPITFGLNCA LGATLMRPYI AELAKICDAA VSCYPNAGLP NPMSDTGFDE TPEVTSALVE EFAASGLVNL VGGCCGTTPE HIAAIAERVA SKKPRAWPSQ YRAAA // ID H1UGM3_ACEPA Unreviewed; 1171 AA. AC H1UGM3; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 01-APR-2015, entry version 19. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:GAB27804.1}; GN ORFNames=APT_1294 {ECO:0000313|EMBL:GAB27804.1}; OS Acetobacter pasteurianus NBRC 101655. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acetobacter. OX NCBI_TaxID=1006554 {ECO:0000313|EMBL:GAB27804.1}; RN [1] {ECO:0000313|EMBL:GAB27804.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NBRC 101655 {ECO:0000313|EMBL:GAB27804.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:GAB27804.1}. 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; BACF01000012; GAB27804.1; -; Genomic_DNA. DR EnsemblBacteria; GAB27804; GAB27804; APT_1294. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 228 228 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 740 740 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1171 AA; 129220 MW; 3C0DFBEFAB9074A1 CRC64; MVAMSSRLPL LDALRDQVLL CDGGMGSRIQ MLDLDVQRDY WGQENCTEIL TLSRPELIRE IHRGYFEAGA DMVETNTFGG SPITLGEFGL TDKAREINKN SAILAREAAE SFADGRTRYV LGSMGPGTKL PSLGNIDYDS LEAALAEQAR GLIEGGVDAI LIETCQDTLQ IKAAVNGVKI ARKELGTTTP IFVQVTVETT GTLLVGPDIA AAATVIHSLD VDLMGLNCAT GPQEMAEHVK WLSENWPRLI SVQPNAGLPE LVNGQTHYPL TPAEMATWVE RFITEDGLNL IGGCCGTSTP HTEALDAMLR RRAEGTGHLR PAPVPRTSVW VPSVASLYSQ VPLRQENAYF SIGERCNANG SKKWRELQEA HDWDGCVTVG REQIREGSNA LDICTAFVGR NERAEMDEVI KRFTSSVNAP LVIDSTETPV IEAALKLHGG KPIINSINFE DGEGPASDRM ELARKFGAAV VALTIDEEGM ARKPEDKLRI ASRLVEFACE KYGLPQSDLM IDPLTFTIAT GAEDDRKLGQ WTLEGIKMIR DTFPDIQIVL GLSNISFGLN PAARAVLNSV YLDHAVKAGM TAAIVHVSKI RPLHLIAPEE VKVAEDLIFD RRTEDYDPLQ TLLAMFADRK AADAVKRKRA ETAEERLKDR IVDGDRKGLE ADLEEAMQNM APLDIINTVL LDGMKVVGEL FGAGKMQLPF VLQSAETMKA AVAYLEPHME RIDGQQRGTI VLATVKGDVH DIGKNLVDII LTNNGYRVVN LGIKVPVQDM IDAARKEKAD AIGMSGLLVK STVIMRENLE EISRAGLDTP VLLGGAALTR NYVEEDCVAA YAPTGRVAYA RDAFDGLTLM DQISQKKFDD YLAAIQKRRE GKATRTNART PETAETRGFG PVDVAAARAR RERLTADEPP MVPPFWGSRV LEATPEAVLP FLNERALYQF QWGFRKQGRS LDDFLVWARQ ELRPILRRML DLTAKENILK PQAIYGYWKA AGDGNDLVLF EEDGTTEACR FTLPRQPKAD GECIADFVRD ISEPERDVIG LQVVTVGQKA SDIARDWFEE NRYQDYLYLH GLSVEMAEAM AEYTHKRIRA ELGFAGEDAR DMEKLLQQGY RGSRYSFGYP ACPRLEDQHP ILALLDAERI GVSLTDGDQL HPEQSTSALV ILNKHAKYFT I // ID H1URK2_ACEPA Unreviewed; 1187 AA. AC H1URK2; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 01-APR-2015, entry version 20. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:GAB31283.1}; GN ORFNames=APS_1885 {ECO:0000313|EMBL:GAB31283.1}; OS Acetobacter pasteurianus subsp. pasteurianus LMG 1262 = NBRC 106471. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acetobacter. OX NCBI_TaxID=940265 {ECO:0000313|EMBL:GAB31283.1}; RN [1] {ECO:0000313|EMBL:GAB31283.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=IFO 3191 {ECO:0000313|EMBL:GAB31283.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:GAB31283.1}. 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; BACG01000020; GAB31283.1; -; Genomic_DNA. DR EnsemblBacteria; GAB31283; GAB31283; APS_1885. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 756 756 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1187 AA; 130950 MW; E6833897ED61261B CRC64; MLCGVGKAPF PFLLYFMVAM SSRLPLLDAL RDQVLLCDGG MGSRIQMLDL DVQRDYWGQE NCTEILTLSR PELIREIHRG YFEAGADMVE TNTFGGSPIT LGEFGLTDKA REINKNSAIL AHEAAESFAD GRTRYVLGSM GPGTKLPSLG NIDYDSLEAA LAEQARGLIE GGVDAILIET CQDTLQIKAA VNGVKIARKE LGTTTPIFVQ VTVETTGTLL VGPDIAAAAT VIHSLDVDLM GLNCATGPQE MAEHVKWLSE NWPRLISVQP NAGLPELVNG QTHYPLTPAE MATWVERFIT EDGLNLIGGC CGTSTPHTEA LDAMLRRRAE GTGRLRPAPV PRTSVWVPSV ASLYSQVPLR QENAYFSIGE RCNANGSKKW RELQEAHDWD GCVTVGREQI REGSNALDIC TAFVGRNERA EMDEVIKRFT SSVNAPLVID STETPVIEAA LKLHGGKPII NSINFEDGEG PASDRMELAR KFGAAVVALT IDEEGMARKP EDKLRIASRL VDFACKKYGL PQSDLMIDPL TFTIATGAED DRKLGQWTLE GIKMIRDAFP DIQIVLGLSN ISFGLNPAAR AVLNSVYLDH AVKAGMTAAI VHVSKIRPLH LIAPEEVKVA EDLIFDRRTE DYDPLQTLLA MFADRKAADA VKRKRAETAE ERLKDRIVDG DRKGLEADLE EAMQNMAPLD IINTVLLDGM KVVGELFGAG KMQLPFVLQS AETMKAAVAY LEPHMERIDG QQRGTIVLAT VKGDVHDIGK NLVDIILTNN GYRVVNLGIK VPVQDMIDAA RKEKADAIGM SGLLVKSTVI MRENLEEISR AGLDTPVLLG GAALTRNYVE EDCVAAYAPT GRVAYARDAF DGLTLMDQIS QKKFDDYLAA IQKRREGKAT RTNARTPETA ETRGFGPVDV AAARARRERL TADEPPVVPP FWGSRVLEAT PEAVLPFLNE RALYQFQWGF RKQGRSLDDF LVWARQELRP ILRRMLDLTA KEHILKPQAI YGYWKAAGDG NNLVLFEKDG TTEACRFTLP RQPKADGECI ADFVRDISEP ERDVIGLQVV TVGQKASDIA RDWFEENRYQ DYLYLHGLSV EMAEAMAEYT HKRIRAELGF AGEDARDMEK LLQQGYRGSR YSFGYPACPR LEDQHPILAL LDAERIGVSL TDGDQLHPEQ STSALVILNK HAKYFTI // ID H1UYD9_COLHI Unreviewed; 357 AA. AC H1UYD9; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 04-MAR-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:CCF32990.1}; GN ORFNames=CH063_00897 {ECO:0000313|EMBL:CCF32990.1}; OS Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose OS fungus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Hypocreomycetidae; Glomerellales; Glomerellaceae; OC Colletotrichum. OX NCBI_TaxID=759273 {ECO:0000313|Proteomes:UP000007174}; RN [1] {ECO:0000313|Proteomes:UP000007174} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000007174}; 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. {ECO:0000313|EMBL:CCF32990.1}. 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; CACQ02000602; CCF32990.1; -; Genomic_DNA. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000007174; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007174}; KW Methyltransferase {ECO:0000313|EMBL:CCF32990.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007174}; KW Transferase {ECO:0000313|EMBL:CCF32990.1}. SQ SEQUENCE 357 AA; 38616 MW; 37EAE98AFF37AD70 CRC64; MGAAEQQQQP PRVLILDGGL GTSLEDKYNI KFESATTPLW STHLLVDGQD TLLACQKDFG DVPVDIILTA TYQLSIHGFA STRTAKYPQG IDRATIGNFI QDAIRIAHEA GRTQASKTAL SVGPYGACMI PGQEYSGAYD AEHDSLDKLR EWHLERLQLF KDAGAFASPV SYVAVETIPR ADEIKAVRQA LDESGVLATQ ASIPFWIASL FPREDECLPD GSSIKEAVXA MLSPDVATSR PWGIGINCTK VWKLESLVKG YESAVQGLID DGAIAEAPAL ILYPDGTNGE VYNTTTQKWE LPEGSSHPAT SWETQLSQVV ANAQSRGLWK QIVVGGCCKA SHSDISRLRT AVKGLSR // ID H1WGL1_9CYAN Unreviewed; 1181 AA. AC H1WGL1; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 01-APR-2015, entry version 19. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:CCE18693.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CCE18693.1}; GN Name=metH {ECO:0000313|EMBL:CCE18693.1}; GN ORFNames=ARTHRO_430014 {ECO:0000313|EMBL:CCE18693.1}; OS Arthrospira sp. PCC 8005. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Arthrospira. OX NCBI_TaxID=376219 {ECO:0000313|EMBL:CCE18693.1}; RN [1] {ECO:0000313|EMBL:CCE18693.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PCC 8005 {ECO:0000313|EMBL:CCE18693.1}; RA Rouy Z.; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CCE18693.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PCC 8005 {ECO:0000313|EMBL:CCE18693.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CAFN01000368; CCE18693.1; -; Genomic_DNA. DR RefSeq; WP_008054045.1; NZ_CAFN01000368.1. DR EnsemblBacteria; CCE18693; CCE18693; ARTHRO_430014. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CCE18693.1}; KW Transferase {ECO:0000313|EMBL:CCE18693.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 228 228 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 737 737 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1181 AA; 130829 MW; DDE4154F64911345 CRC64; MESLFLQHLH SPQRPVIIFD GAMGTNLQVQ NLTAEDFGGK EYEGCNEYLV HTKPEAVATV HRQFLQAGAD VIETDTFGGT SIVLAEYDLA DQAYQLNKTA ATLAKSVTAE FSSPEKPRFV AGSMGPGTKL PTLGHIDFDT LERAFCQQAE GLFDGGVDLF IVETCQDVLQ IKAALNGIEE VFKMKGERRP IMVSVTMEAF GTMLVGSEIN AALTILEPYK IDILGLNCAT GPDLMKEHIA YLSEHSPFVV SCIPNAGLPE NVGGQAHYKL TPLELKMALM HFIEDLGVQV IGGCCGTRPD HIKALAEIAQ TLTPKPRHPQ ITPSAASIYS TVSYEQENSF LIVGERLNAS GSKKCRDLLN AEDWDGLVAL AKAQVKEGAQ ILDVNVDYVG RNGVRDMHEL VSRLVTNVNL PLMLDSTEWE KMEAGLKVAG GKCLLNSTNY EDGEPRFYKV LELAKKYGAG VVVGTIDEEG MARTATKKFA IAKRAYNDAI AFGIAATEIF FDPLALPIST GIEEDRENGK ATIEAINQMR QELPGCHILL GISNISFGLN PAARQVLNSV FLHETMAVGL DSAIVTANKI LPLAKIEPEH QEVCRHLIYD QRQFDGDVCT YDPLTKLTTL FEGKTTKRDR SGDANLPIEE RLKQHIIDGE RIGLEDALAE ALKKYPPLDI INIFLLDGMK VVGELFGSGQ MQLPFVLQSA QTMKAAVAYL EPFMEKSESG NNAKGTFVIA TVKGDVHDIG KNLVDIILSN NGYKVVNLGI KQPVDNIIAA YREHNADCIA MSGLLVKSTA FMKDNLEVFN QEGITVPVIL GGAALTSKFV YEDCQNTYKG RVIYGKDAFS DLTFMDKLMP AKKSGKWEDF KGFLDEFVED ETITANGDNQ QSAQPDQPEP DTPKVVDTRR SEAVAVDIDR PTPPFWGVKV LEPADMPFDE LFWYLDLQAL TAGQWQFRKP QGQPRSEYNQ FLEAKVYPIL AEWKQRIISE NLLHPRAVYG YFPCQSEGNT LLIYDPEKIK AGEISEPITS FEFPRQRSGR RLCIADFFAP KDSGQMDVFP MHAVTVGQIA TDYAQKLFAA DDYTNYLYFH GMAVQTAEAM AEWLHARIRR ELGFGGEDAD NIRDILKQRY RGSRYSFGYP ACPNMQDQYK QLDLLKAEVI GLYMDESEQL YPEQSTTAII TYHPAAKYFS A // ID H1WPH9_LEUCI Unreviewed; 304 AA. AC H1WPH9; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 12. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:CCF24228.1}; GN Name=mmuM {ECO:0000313|EMBL:CCF24228.1}; GN ORFNames=LEUCOC10_02885 {ECO:0000313|EMBL:CCF24228.1}; OS Leuconostoc citreum LBAE C10. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostocaceae; OC Leuconostoc. OX NCBI_TaxID=1108974 {ECO:0000313|EMBL:CCF24228.1, ECO:0000313|Proteomes:UP000002947}; RN [1] {ECO:0000313|EMBL:CCF24228.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=LBAE C10 {ECO:0000313|EMBL:CCF24228.1}; 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAGE01000005; CCF24228.1; -; Genomic_DNA. DR RefSeq; WP_004900405.1; NZ_CAGE01000005.1. DR EnsemblBacteria; CCF24228; CCF24228; LEUCOC10_02885. DR Proteomes; UP000002947; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002947}; KW Methyltransferase {ECO:0000313|EMBL:CCF24228.1}; KW Transferase {ECO:0000313|EMBL:CCF24228.1}. SQ SEQUENCE 304 AA; 33694 MW; 94EC825788010AB8 CRC64; MTKFSELLLQ GPVILDGGLG SEIDKQHIAV ANNLWSASAL IQAPNLVRDI HQSYFNAGAQ IAIVDTYQAH PQTFVDSGLS ENEAYELIDL AVALARDGLK KSEKSSGIIA GSVGPYGAYL ANGAEYTGDY DLSIQAYQVF HRQRIKRLVH NNVDILALET MPNFKEAQAI ALLLQNEFPE VEAYLSFATE AGDHLWDGTR LAHAVAYFNQ FEQIKAIGIN CTAPDNILPA ITRIKPNTDK KVIVYPNAGE VYNPETKRWV TNNEPINWRR LVPLWQHAGA DIIGGCCRTS PEDIREIHDI LQKQ // ID H1XBS8_9XANT Unreviewed; 321 AA. AC H1XBS8; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 11. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:CCF66658.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:CCF66658.1}; GN Name=mmuM {ECO:0000313|EMBL:CCF66658.1}; GN ORFNames=XAPC_347 {ECO:0000313|EMBL:CCF66658.1}; OS Xanthomonas axonopodis pv. punicae str. LMG 859. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=1085630 {ECO:0000313|EMBL:CCF66658.1}; RN [1] {ECO:0000313|EMBL:CCF66658.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 859 {ECO:0000313|EMBL:CCF66658.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCF66658.1}. 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; CAGJ01000003; CCF66658.1; -; Genomic_DNA. DR RefSeq; WP_005924914.1; NZ_CAGJ01000003.1. DR EnsemblBacteria; CCF66658; CCF66658; XAPC_347. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:CCF66658.1}; KW Transferase {ECO:0000313|EMBL:CCF66658.1}. SQ SEQUENCE 321 AA; 34268 MW; 6A9B94F3707AB5A5 CRC64; MTILPRQPRA NAPFSQALQH DGYVVLDGAL ATELEQRGCD LNDALWSARV LMEQPELIYQ VHRDYFAAGA QCAITASYQA TPLGFAARGL DVAQAQALIA RSVALAMQAR ADHLTLHPHA APLWVAGSVG PYGAYLADGS EYRGDYVLPI EQLMDFHRPR IAALAEAGVD LLACETLPSA SEIVALRQLL RHEFPQLHAW FSFTLRDAAH LSDGTPLAQV VPALDACAQV IAVGINCIAL DQATAALHSL SALTALPLVV YPNSGEHYDA SDKRWHVGRG AALTLADQHA HWLAAGARLI GGCCRTAPRD IAALAAARAA E // ID H1XN58_9XANT Unreviewed; 379 AA. AC H1XN58; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:CCF70638.1}; GN Name=metH {ECO:0000313|EMBL:CCF70638.1}; GN ORFNames=XAPC_4375 {ECO:0000313|EMBL:CCF70638.1}; OS Xanthomonas axonopodis pv. punicae str. LMG 859. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=1085630 {ECO:0000313|EMBL:CCF70638.1}; RN [1] {ECO:0000313|EMBL:CCF70638.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 859 {ECO:0000313|EMBL:CCF70638.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCF70638.1}. 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; CAGJ01000158; CCF70638.1; -; Genomic_DNA. DR RefSeq; WP_005913782.1; NZ_CAGJ01000158.1. DR EnsemblBacteria; CCF70638; CCF70638; XAPC_4375. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:CCF70638.1}; KW Transferase {ECO:0000313|EMBL:CCF70638.1}. SQ SEQUENCE 379 AA; 40588 MW; BC8289DDDAB96336 CRC64; MTHVRIPNPE SPIPFALPWL HPERAAKLTA ALAERILIID GAMGTMIQRH DLQEPDYRGT RFADGYDSAH VHGPGCDHAH VPQGHDLKGN NDLLLLTRPE IIAGIHRAYL EAGADLLETN TFNATSVSQA DYHLEHLVYE LNKAGAQVAR ACCDDVEALT PHKPRFVIGV LGPTSRTASI SPDVNDPGYR NTSFDALRAT YREAIEGLID GGADTLMVET IFDTLNAKAA LYAIEEVFDA RGGRLPVMVS GTITDASGRT LSGQTAEAFY ASVAHGRPLS IGLNCALGAR DLRPHVETLA QIADTYVSAH PNAGLPNAFG EYDETPEEMA QTLREFAQAG LLNLVGGCCG TSPDHIRAIA EAVADLPPRQ LPGAQELAA // ID H1XNC7_9BACT Unreviewed; 296 AA. AC H1XNC7; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EHO42098.1}; GN ORFNames=Calab_2488 {ECO:0000313|EMBL:EHO42098.1}; OS Caldithrix abyssi DSM 13497. OC Bacteria; Caldithrix. OX NCBI_TaxID=880073 {ECO:0000313|EMBL:EHO42098.1, ECO:0000313|Proteomes:UP000004671}; RN [1] {ECO:0000313|EMBL:EHO42098.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 13497 {ECO:0000313|EMBL:EHO42098.1}; 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 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 Brambilla E., Klenk H.-P., Eisen J.A.; RT "The permanent draft genome of Caldithrix abyssi DSM 13497."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001402; EHO42098.1; -; Genomic_DNA. DR RefSeq; WP_006929331.1; NZ_CM001402.1. DR EnsemblBacteria; EHO42098; EHO42098; Calab_2488. DR Proteomes; UP000004671; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000004671}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EHO42098.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000004671}; KW Transferase {ECO:0000313|EMBL:EHO42098.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 211 211 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 276 276 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 277 277 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 296 AA; 32233 MW; CC36C17B58CCE2AB CRC64; MESVLLKRLS AGDILLCDGA MGTELQKRGL KRGECPELMN IEQPQIVQSI YRDYYAAGSD IVETNSFGGT RSRLSHYDLQ DQAYRLNREA ARLAKEVCPE GRFVAGSMGP TGAILEPYGE LSVDEAVDQF KEQAEALAEG GVDIFFIETM ITLEEMGAAI QAVKSVSDLP VAATFTFELG PTGIHTNWGV DVPSAVRFLT EQGVDILGAN CGEGIDVILR TVQEMRKLTD LPILAQPNAG LPEIKNEVIV YHETPEAMRE KIKELLALQI NILGGCCGTS ASHIKMMREL IDGKGQ // ID H1XWI1_9BACT Unreviewed; 1229 AA. AC H1XWI1; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHO41819.1}; GN ORFNames=Calab_2209 {ECO:0000313|EMBL:EHO41819.1}; OS Caldithrix abyssi DSM 13497. OC Bacteria; Caldithrix. OX NCBI_TaxID=880073 {ECO:0000313|EMBL:EHO41819.1, ECO:0000313|Proteomes:UP000004671}; RN [1] {ECO:0000313|EMBL:EHO41819.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 13497 {ECO:0000313|EMBL:EHO41819.1}; 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 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 Brambilla E., Klenk H.-P., Eisen J.A.; RT "The permanent draft genome of Caldithrix abyssi DSM 13497."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CM001402; EHO41819.1; -; Genomic_DNA. DR RefSeq; WP_006928998.1; NZ_CM001402.1. DR EnsemblBacteria; EHO41819; EHO41819; Calab_2209. DR Proteomes; UP000004671; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000004671}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000004671}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1229 AA; 137395 MW; 2D34BCCEF5A339FD CRC64; MQDKEKRIRS QLEKRILVLD GAMGTMIQRY RLGEEDFRGS RFKDWPTDLK GNNDLLSLTQ PDIIREIHAA YLDAGADIIE TNTFNANAIS LADYQMEELV YEMNRASAQL ARQAADAKTA ETPHKPRFVA GSVGPTNRTL SISPKVEDPG YRAVTFDQVV DAYYQQVKGL IEGGVDLILI ETIFDTLNAK AALYAIQNCF DELNTHLPIM ISVTIVDKSG RTLSGQTLEA FWVSIKPYPI FSVGLNCSLG PEEMRPFIEE LSKMADVYVT LYPNAGLPNQ FGEYEATADQ MSVVLKEYAA QGWLNIVGGC CGTTPEHIRA FVEIVEHLPP RKIPEPPIYT QFSGLEALTI LPTSNFINIG ERCNIAGSRK FARLIREGHF EEAVAIARKQ VEDGAQILDV NMDEGLIDSV EAMKRFLNLI AAEPDIARVP VMIDSSRWEV IEAGLKCLQG KSIINSISLK EGEETFLEHA RMARRLGAAV LVMAFDEKGQ ADTLERRIEV CTRAYRLLTE KIHFPPQDII LDPNIFAVGT GMSEHANYAL DYLEAVRYIK AHLPYAKVSG GVSNLSFSFR GNNLIREAMH SAFLYHAIQA GMDMGIVNAG QITVYEDIPK DLLELVEDVL FNRRPDATER LIAFAQQARQ STVKEEKKLA WREKGVEERL HYALIKGITE FIEADTEEAY QKYGDPIKVI EGPLMEGMKT VGDLFGSGKM FLPQVVKSAR VMKKAVAHLT PYLEALKLQS ASTARGKILL ATVKGDVHDI GKNIVGVVLG CNNYEIIDLG VMVPAEKIIE AARALKVDII GLSGLITPSL DEMVHVAKEL DRQGLDLPLL IGGATTSQKH TAVKIAPAYS RGLAVYVPDA SQSVGVVSNL LNRKTRAKFA SALRNDYQKL AENFHKQRSR VRLIPIEEAR RNRLKLSFSP KEITAPQTSG LQILKNYSID LLRERIDWTP FFNAWELRGK YPQILTESEH REEAQKLFND ANRLLDEITR KQWLQANGVL GVFPANAIGD DIEVYGNVER TQLLAVVHTL RQQMQRNGRK PNFALSDFIA PKESGINDYL GFFVVTAGIG LQEVITHLEA DHNDYKIIML KALSDRLAEA FAEHLHERLR KEFWGYARDE NLSNEQIIAE KYRGIRPAPG YPACPDHTEK QTIFKILQAT EKIGVTLTES MAMQPAASVA GYYFAHPKAR YFGVGKIGMD QLTDYAHRKG MSIESLKRWL APILIEEDG // ID H1YAC1_9SPHI Unreviewed; 1238 AA. AC H1YAC1; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHQ26964.1}; GN ORFNames=Mucpa_2853 {ECO:0000313|EMBL:EHQ26964.1}; OS Mucilaginibacter paludis DSM 18603. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Mucilaginibacter. OX NCBI_TaxID=714943 {ECO:0000313|EMBL:EHQ26964.1, ECO:0000313|Proteomes:UP000002774}; RN [1] {ECO:0000313|EMBL:EHQ26964.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 18603 {ECO:0000313|EMBL:EHQ26964.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CM001403; EHQ26964.1; -; Genomic_DNA. DR RefSeq; WP_008507210.1; NZ_CM001403.1. DR EnsemblBacteria; EHQ26964; EHQ26964; Mucpa_2853. DR Proteomes; UP000002774; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002774}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002774}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 252 252 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 315 315 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 316 316 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 772 772 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1238 AA; 136729 MW; A9A057D3342C88B2 CRC64; MDIRQELQKR ILIIDGAMGT MIQRYQLTEA DFRGERFKNH HSDLQGNNDL LNITRPDIIK TIHAEYLEAG ADIIETNTFS TQVISLADYH LEELAYELSY EGARIAREAA DEYTEKTPHK PRFVAGAIGP TNRTASLSPD VNDPGYRAVT FDDLVAAYYT QVRGLVDGGS DVLLIETIFD TLNAKAAIFA IKQYENECKA AGKDYPAFRP TGGIMISGTI TDASGRTLSG QTVEAFWNSI RHANLLSVGL NCALGAKEMR PHIEELSAKA SVYISAYPNA GLPNEFGAYD EAPHETAHLV EDFMAAGLVN IVGGCCGTTP DHISCIAKKT ESFPRRQIPK VETFMRLSGL EAITLTPESN FANVGERTNI TGSPKFSKLI LAEDYEGALV VARQQVEGGA QVIDVNMDEG MIDSEAAMTK FMNLIASEPD IAKLPIMVDS SKWSVIEAGL KCLQGKGIVN SISLKEGEDK FRDSARKIMQ YGAATVVMAF DETGQADSLE RRIEICKRSY DILVNEVGFP AEDIIFDPNI LTVATGLEEH NNYAVDFIEA TRWIKQNLPH AKVSGGVSNI SFSFRGNNTV REAMHSAFLY HAIQAGMDMG IVNAGMLEVY EEIPKPLLEL VEDVLLNRRP DATERLVEYA DTVKSKGKEI VKDEEWRKEP VEKRLSHALV KGIIEYLDAD VEEARQKYPK PLEVIEGPLM DGMNIVGDLF GAGKMFLPQV VKSARVMKKA VAYLLPFIAA EKARVLAAGE GADNERSNAG KILMATVKGD VHDIGKNIVG VVLACNNFEI IDLGVMVPAH KIIEEAKKQN VDIIGLSGLI TPSLDEMVHF AKEMEREGFT IPLIVGGATT SRIHAAVKID PNYSGPAIHV LDASRSVTVC SNLMSKDNRD AYIQGIKDEY AKAREAHLNK KSDKRFVSIG DARKQTIELD LDAIAPKPSF LGTKVIEAYP LEDLVPYIDW TPFFHTWELR GSYPKIFDDK SAGVEAKKLY DDARALLTEI VDNKLLQANG VIGFWPANSV GDDIELYTDE SRSEVLSTIY TLRQQAEKVK GEPYYALSDF VAPKASGAAD YWGGFAVTAG IGCDELVAKY EKDHDDYNSI MAKALADRLA EAFAEKMHEL VRKDYWGYAK EEQLQSEDLI KEKYQGIRPA PGYPACPDHT EKTTLFELLK AEDNAKMYLT ESLAMMPAAS VSGFYFAHPQ ARYFGLGKIG KDQVVDYAER KGADLETTER WLSPNINY // ID H1ZRL5_PLAFE Unreviewed; 401 AA. AC H1ZRL5; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 04-MAR-2015, entry version 15. DE SubName: Full=Betain homocystein methyltransferase {ECO:0000313|EMBL:CBA10403.1}; GN Name=bhmt {ECO:0000313|EMBL:CBA10403.1}; OS Platichthys flesus (European flounder) (Pleuronectes flesus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Carangaria; Pleuronectiformes; Pleuronectoidei; Pleuronectidae; OC Platichthys. OX NCBI_TaxID=8260 {ECO:0000313|EMBL:CBA10403.1}; RN [1] {ECO:0000313|EMBL:CBA10403.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Muscle {ECO:0000313|EMBL:CBA10400.1}; RX PubMed=20621770; DOI=10.1016/j.marenvres.2010.05.002; RA Marchand J., Evrard E., Guinand B., Cachot J., Quiniou L., Laroche J.; RT "Genetic polymorphism and its potential relation to environmental RT stress in five populations of the European flounder Platichthys RT flesus, along the French Atlantic coast."; RL Mar. Environ. Res. 70:201-209(2010). CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN432389; CBA10400.1; -; mRNA. DR EMBL; FN432392; CBA10403.1; -; Genomic_DNA. DR UniPathway; UPA00051; UER00083. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000313|EMBL:CBA10403.1}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000313|EMBL:CBA10403.1}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 210 210 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 292 292 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 401 AA; 43980 MW; 47C3163E8C08F896 CRC64; MAPGKKGIIE RLNAGEVVIG DGGFVFALEK RGYVKAGPWT PEATVTHPEA VRQLHREFLR AGSNVMQAFT FYASDDKLEN RGQTLSITGV QVNEAACDLA REVANEGDAL VAGGVCADPS YLSCKSETEV KGIFKKQLEV FAKKNVDFLI AEYFEHVEEA EWAVQVLKTS GKPVAASLCI GPEGDMHGVS PGECAVRLVK AGAQIVGVNC HFDPMTCVKA VKLMKEGVEK AGLKAHYMVQ PLAFHTPDCN CQGFIDLPEF PFGLEPRILT RWDMHKYARE AYKAGIKFIG GCCGYEPYHI RAVAEELALE RGVMPPGSDK HGMWGAGLEM HTKPWVRARA RRDYWEHLLP ASGRPLCASL STPESWGVTK GHTDLLQHKE ATSTQEMKHV LEKQKKAKSS A // ID H2A6U5_STRMD Unreviewed; 315 AA. AC H2A6U5; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 29-APR-2015, entry version 16. DE SubName: Full=YbgG protein {ECO:0000313|EMBL:CCF02472.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:CCF02472.1}; GN Name=ybgG {ECO:0000313|EMBL:CCF02472.1}; GN OrderedLocusNames=SMA_1181 {ECO:0000313|EMBL:CCF02472.1}; OS Streptococcus macedonicus (strain ACA-DC 198). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1116231 {ECO:0000313|EMBL:CCF02472.1, ECO:0000313|Proteomes:UP000007152}; RN [1] {ECO:0000313|EMBL:CCF02472.1, ECO:0000313|Proteomes:UP000007152} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ACA-DC 198 {ECO:0000313|EMBL:CCF02472.1, RC ECO:0000313|Proteomes:UP000007152}; 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; CCF02472.1; -; Genomic_DNA. DR RefSeq; WP_014294682.1; NC_016749.1. DR RefSeq; YP_005094814.1; NC_016749.1. DR EnsemblBacteria; CCF02472; CCF02472; SMA_1181. DR KEGG; smn:SMA_1181; -. DR KO; K00547; -. DR Proteomes; UP000007152; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007152}; KW Methyltransferase {ECO:0000313|EMBL:CCF02472.1}; KW Transferase {ECO:0000313|EMBL:CCF02472.1}. SQ SEQUENCE 315 AA; 34577 MW; EDA2FF2F499E71F1 CRC64; MGTFKELLAS QDYVILDGAL GTELEKRGYD VSGKLWSAKY LLENPSVIQD LHDVYLRSGA DILTTSSYQA TVQGLEDFGL SEKEALDIIS LTVTLAREAR DNFWNGLSDE AKKKRPYPLI SGDVGPYAAY LADGSEYNGN YQQTQEEYQV FHRPRIQALL SAGSDFLGIE TIPNVAEAKA LLDLLATEFP QTEAYISFTA QDDKHISDGT PIEEVADLCE QSPQILAFGI NCSSPAVISG LLKRIRTVSP KPLVTYPNSG EIYDGATQTW KSIPDNSHTL LENSRAWHQL GAKIVGGCCR TSPKDIACLA QAFRE // ID H2A703_STRMD Unreviewed; 618 AA. AC H2A703; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 29-APR-2015, entry version 23. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=SMA_1241 {ECO:0000313|EMBL:CCF02532.1}; OS Streptococcus macedonicus (strain ACA-DC 198). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1116231 {ECO:0000313|EMBL:CCF02532.1, ECO:0000313|Proteomes:UP000007152}; RN [1] {ECO:0000313|EMBL:CCF02532.1, ECO:0000313|Proteomes:UP000007152} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ACA-DC 198 {ECO:0000313|EMBL:CCF02532.1, RC ECO:0000313|Proteomes:UP000007152}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; CCF02532.1; -; Genomic_DNA. DR RefSeq; WP_014294735.1; NC_016749.1. DR RefSeq; YP_005094869.1; NC_016749.1. DR EnsemblBacteria; CCF02532; CCF02532; SMA_1241. DR KEGG; smn:SMA_1241; -. DR KO; K00547; -. DR Proteomes; UP000007152; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007152}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862, KW ECO:0000313|EMBL:CCF02532.1}. SQ SEQUENCE 618 AA; 68100 MW; 05524928CAC93D53 CRC64; MSRLLERLKT DILVADGAMG TLLYANGLDN CYEAYNLTHP DKISAIHHAY LEAGADIIQT NTYAAKRHRL KGYAYDDQVK EINQAGVKIA REATGDDAFV LGTVGALRGL KQCDLTLDEI IEETLEQVGY LIETNQIDGL LFETYYDEEE IIEVLKAVRP ITDLPIITNI ALHEAGITEN GRPLVEILGK LVMLGADVVG LNCHLGPYHM IKSLKQVPLF AQSYLSVYPN ASLLSFVDDN GSGQYGFSQN ADYFGKSAEL LVAEGARLIG GCCGTTPDHI RAVKRAVKGL KPVERKFVTP MVEEAELIKA AKQSETLVDR VKREVTIIAE LDPPKTLDIA KFTEGVKALD KAGISAITLA DNSLAKTRIC NVSIAALLKN EISTPFLLHL SCRDHNMIGL QSRLLGMDVL GFNHVLAITG DPSKIGDFPG ATSVYDATSF KLLALIKQLN KGQGYSGASI KKETNFTAAA AFNPNVKNLS RCGRLIERKV AAGADYFITQ PVFNTEIIDE LANLTRDYEA PFFVGIMPIT SYNNAIFLHN EVPGIQLSDE FLAKLEAVKD DKETCQKLAL EESKQLIDRA LKHFKGIYLI TPFMRYDLTV ELIDYIHQKV ELKNQRIS // ID H2APM1_KAZAF Unreviewed; 326 AA. AC H2APM1; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 29-APR-2015, entry version 20. DE SubName: Full=KAFR0B00210 protein {ECO:0000313|EMBL:CCF56321.1}; GN Name=KAFR0B00210 {ECO:0000313|EMBL:CCF56321.1}; GN ORFNames=KAFR_0B00210 {ECO:0000313|EMBL:CCF56321.1}; 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 {ECO:0000313|EMBL:CCF56321.1, ECO:0000313|Proteomes:UP000005220}; RN [1] {ECO:0000313|EMBL:CCF56321.1, ECO:0000313|Proteomes:UP000005220} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 / RC NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220}; 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; HE650822; CCF56321.1; -; Genomic_DNA. DR RefSeq; XP_003955456.1; XM_003955407.1. DR GeneID; 13882489; -. DR KEGG; kaf:KAFR_0B00210; -. DR InParanoid; H2APM1; -. DR KO; K00547; -. DR OrthoDB; EOG7X9GHR; -. DR Proteomes; UP000005220; Chromosome 2. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005220}; KW Reference proteome {ECO:0000313|Proteomes:UP000005220}. SQ SEQUENCE 326 AA; 36854 MW; 43D8FA4328190618 CRC64; MPRQPIKEYL EENPKKVLVL DGGQGTELEN RGIHVANPVW STIPFISESF WSNASSKDRE IVKGMFQDFL DAGADILMTI TYQTSFKSVT ENTPIKTLKE YNELLERIVS FSRSCIGDEK YLIGCIGPWG AHVCAEFNGD YGGHPENIDY YAYFKPQLDN FFQNKDLDLI GFETVPNFHE LKAILSWDDT ILSKPFYIGL SVHENGVLRD GTTMNEIGYY IKSLGSKINP NFLLLGINCV SFSDSPDILE SIHKELPDMP LIAYPNSGEI YDTVKKIWLP NHYSDITWND VVNRYIKAGA RIIGGCCRTM PDDIEQVSAA VKKSHK // ID H2AXD7_KAZAF Unreviewed; 326 AA. AC H2AXD7; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 29-APR-2015, entry version 20. DE SubName: Full=KAFR0F04420 protein {ECO:0000313|EMBL:CCF59037.1}; GN Name=KAFR0F04420 {ECO:0000313|EMBL:CCF59037.1}; GN ORFNames=KAFR_0F04420 {ECO:0000313|EMBL:CCF59037.1}; 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 {ECO:0000313|EMBL:CCF59037.1, ECO:0000313|Proteomes:UP000005220}; RN [1] {ECO:0000313|EMBL:CCF59037.1, ECO:0000313|Proteomes:UP000005220} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 / RC NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220}; 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; HE650826; CCF59037.1; -; Genomic_DNA. DR RefSeq; XP_003958172.1; XM_003958123.1. DR GeneID; 13884504; -. DR KEGG; kaf:KAFR_0F04420; -. DR InParanoid; H2AXD7; -. DR KO; K00547; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000005220; Chromosome 6. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005220}; KW Reference proteome {ECO:0000313|Proteomes:UP000005220}. SQ SEQUENCE 326 AA; 36626 MW; 4413DCE4B6D7CEDE CRC64; MGRVPIKEYL LRNSDKILVL DGGQGTELEK RGINISSPVW STLPFINESF WSNSSSNDRK IIKDMYSDFI SAGADVLSTT TYQTSFASIS ENTNIQTLKD YHELLNRITK FTRECIGDSK YLVGSIGTYA AYLSAEYTGD FGDAADTIDY HGYFKPQLDN FNRSTEIDII GFETIPNIHE LRAILSLNKK DLSKPFYISL STNSKAQLRD GTSLKGVVDV IKSFESTLNP NLILLGINCI GLNSSHLTME YLNNHLPQFP LIVYPNSGEK YDPVRKIWLA DEDPAFTWEY IVHRYLDAGA RIVGGCCRTT PSDIRSISEA IKCYTK // ID H2B1X2_KAZAF Unreviewed; 326 AA. AC H2B1X2; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 29-APR-2015, entry version 20. DE SubName: Full=KAFR0L00150 protein {ECO:0000313|EMBL:CCF60622.1}; GN Name=KAFR0L00150 {ECO:0000313|EMBL:CCF60622.1}; GN ORFNames=KAFR_0L00150 {ECO:0000313|EMBL:CCF60622.1}; 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 {ECO:0000313|EMBL:CCF60622.1, ECO:0000313|Proteomes:UP000005220}; RN [1] {ECO:0000313|EMBL:CCF60622.1, ECO:0000313|Proteomes:UP000005220} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 / RC NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220}; 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; HE650832; CCF60622.1; -; Genomic_DNA. DR RefSeq; XP_003959757.1; XM_003959708.1. DR GeneID; 13886830; -. DR KEGG; kaf:KAFR_0L00150; -. DR InParanoid; H2B1X2; -. DR KO; K00547; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000005220; Chromosome 12. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005220}; KW Reference proteome {ECO:0000313|Proteomes:UP000005220}. SQ SEQUENCE 326 AA; 36407 MW; 85A261EA9083C690 CRC64; MVRVPLKKYL KENPEKVLVS DGGQGLELER RGLDIKHRLW STRPFLSKSF WSDPSSNDIR IVKGMFEDFV NAGAEILMTT TYQTSFKAVS ESTELKSLRE YNELLDKIVG FTRACIGDNR YLIGSIGSYG ALVGGEYSGD YGDSPETVDF YSYFKPQLDN FLNNDEIDIV GFETIANFTE LKSLLSWDEK KVSKPFYISL SVHDNGNLRD GTPMHLITDY IKSLATAINP NLTFLGVNCV NYNKATEIID SIHNGLPTMP LSVFPNSGEV FNVEKGIWTA NPEAAASWEA VVKRFISSGV RIVGGCCRTR PHDIEQISKA VKKLSN // ID H2BVT7_9FLAO Unreviewed; 339 AA. AC H2BVT7; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EHQ01820.1}; GN ORFNames=Gilli_1146 {ECO:0000313|EMBL:EHQ01820.1}; OS Gillisia limnaea DSM 15749. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Gillisia. OX NCBI_TaxID=865937 {ECO:0000313|EMBL:EHQ01820.1}; RN [1] {ECO:0000313|EMBL:EHQ01820.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 15749 {ECO:0000313|EMBL:EHQ01820.1}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Held B., Kyrpides N., Mavromatis K., RA Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F., RA Hugenholtz P., Woyke T., Wu D., Tindall B., Pomrenke H., Brambilla E., RA Klenk H.-P., Eisen J.A.; RT "The Improved High-Quality Draft genome of Gillisia limnaea DSM RT 15749."; 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; JH594606; EHQ01820.1; -; Genomic_DNA. DR RefSeq; WP_006988142.1; NZ_JH594606.1. DR EnsemblBacteria; EHQ01820; EHQ01820; Gilli_1146. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHQ01820.1}; KW Transferase {ECO:0000313|EMBL:EHQ01820.1}. SQ SEQUENCE 339 AA; 36954 MW; D6F6DDDDA31F96D3 CRC64; MSKLEEILSK KILILDGAMG TMLQDYKFSE EDFRGSRFAD WPVSLKGNND LLSLTQPEAI AEIHRKYFLA GADIVETNTF SGTTIAMADY KMEELVYELN YESARIAKKV AEELTLENPE KPRFVAGAIG PTNKTASMSP DVNDPGYRAI SFEALKIAYK QQARALIDGG VDVLLVETVF DTLNAKAALF GIDELKEELN TAIPVMISGT ITDASGRTLS GQTAEAFLIS ISHMDLLSVG FNCALGAKQL TPHLEVLSQK SGFYVSAYPN AGLPNAFGEY DESAEEMANQ IKEYLEKGLV NILGGCCGTT PAHIKAMADV AKEYKPRKIA SREPSKILD // ID H2CDD8_9LEPT Unreviewed; 419 AA. AC H2CDD8; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EHQ05442.1}; GN ORFNames=Lepil_0741 {ECO:0000313|EMBL:EHQ05442.1}; OS Leptonema illini DSM 21528. OC Bacteria; Spirochaetes; Spirochaetales; Leptospiraceae; Leptonema. OX NCBI_TaxID=929563 {ECO:0000313|EMBL:EHQ05442.1}; RN [1] {ECO:0000313|EMBL:EHQ05442.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 21528 {ECO:0000313|EMBL:EHQ05442.1}; 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., 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; EHQ05442.1; -; Genomic_DNA. DR RefSeq; WP_002770072.1; NZ_JH597773.1. DR EnsemblBacteria; EHQ05442; EHQ05442; Lepil_0741. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHQ05442.1}; KW Transferase {ECO:0000313|EMBL:EHQ05442.1}. SQ SEQUENCE 419 AA; 45774 MW; D44291DFE08C77F3 CRC64; MHRIEIEADQ RILILDGAMG TMIQQAGPVE DDFRGPLLKG HSIELKGNND LLCLTAADLI LQIHKEYVLA GADILSTNTF GANRISQTDY ETAHLSYEMN RQGAILAREA ARSADKRPVF VAGAMGPTTK LGSLSPDVND PGYRSVGFDE LVEAYQEQIE GLLDGGVDLF LLETVTDTLN AKAAIYALMN TFERRGKSYP VMVSGTITDA SGRILSGQTI EAFLISISHA PLFSVGLNCS LGAKELYPFV HDLHRASTFR VSVHPNAGLP NAFGSYDQSA GEFADLVRSM AEQGWLNIVG GCCGTTPAHI RAAAKALRDV MPRRSRHASH SIEQRATTAA PVVEAVEAWQ PSHEKPTFNL PHLLSMIASI EDEATLRAFK SRFDKERALY HSEQAMLAGA HLIGRFQYLR EEGRLRRSA // ID H2CLR7_9LEPT Unreviewed; 1233 AA. AC H2CLR7; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:EHQ04678.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHQ04678.1}; GN ORFNames=Lepil_4200 {ECO:0000313|EMBL:EHQ04678.1}; OS Leptonema illini DSM 21528. OC Bacteria; Spirochaetes; Spirochaetales; Leptospiraceae; Leptonema. OX NCBI_TaxID=929563 {ECO:0000313|EMBL:EHQ04678.1}; RN [1] {ECO:0000313|EMBL:EHQ04678.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 21528 {ECO:0000313|EMBL:EHQ04678.1}; 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., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; JH597775; EHQ04678.1; -; Genomic_DNA. DR RefSeq; WP_002775938.1; NZ_JH597775.1. DR EnsemblBacteria; EHQ04678; EHQ04678; Lepil_4200. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHQ04678.1}; KW Transferase {ECO:0000313|EMBL:EHQ04678.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 254 254 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 318 318 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 768 768 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1233 AA; 136699 MW; F969DC02DFB0E788 CRC64; MTVTYTKRPR LEDFTVYKEL QKRILVLDGA MGTMIQRHTL TEADFRGERF KDTTQELKGN NDLLSITQPD IIRGIHEAYY AAGSDIVETN TFSSTTIAQA DYGLEPLAYE LNVASARLAR EAADKYSTPD RPRFVAGAIG PTNRTLSLSP DVNDPGYRAV SFDEVVDAYY EQITGLVDGG ADILLVETIF DTLNCKAALF AIQKYFDATG NYRPVMISGT VVDQSGRTLS GQTVSAFWIS VSHVPLLMSV GLNCALGSEQ MRPFVSEMAR IATCAISLYP NAGLPNAFGG YDETPRMMAE VIRDYAAHGW LNIVGGCCGT TPDHIRSMAE LVSDITPRKP AVDDHLLKLS GLEPLVVTAE TNFLNVGERT NVTGSKKFAR LILEGNYDEA LSVAAEQVES GAQVIDVNMD EGMLDSKAAM DRFLKLIAAE PDISKVPIMI DSSKFDVIET GLKCVQGKCI VNSISMKEGV DAFLEQARRV RAYGAAAVVM AFDEKGQADT YERRINICKQ AYDLLVNEVG FPPEDVIFDP NIFAIATGIE EHNNYALDFI QATEWIKKNL PHAKVSGGVS NISFSFRGNE PVRRAMHSVF LYHAIKAGMD MGIVNAGQLD VYDEIEPELR ELCEDVILNR RPDATERLIT KAESLKGQGG EVSAKEEQAW RSAPVEERLK HALVRGIVDF IDEDTEEARQ KYGSPLTVIE GPLMDGMNVV GDLFGSGKMF LPQVVKSARV MKKSVAYLIP YLEEEKRRNQ DGRRNAKILL ATVKGDVHDI GKNIVGVVLA CNNYDVVDLG VMVPREKILD EAVRENADVI GLSGLITPSL EEMAEVAREM ERRGMKVPLL IGGATTSEMH TAVKIDREYS GPVVHVLDAS RSVPVAGQLI SPDTREGYMA KIREQYDMLR ERHASRHEEK ELLSLEEARK NALKLSFDGA NRPVAPKSPG VFDIRPSLEE LRPFIDWTPF FLTWEMRGKY PAIFDDPNLG EEAKKLFADA NTLLDEIITG KLIEARGVYG LFPASTDGDS ILIYKDESRK EVAGRFEGLR QQGKKREGEP NRSLSDLIAP ASSGVPDWMG AFVVTAGIGL EKLVSKFEAD HDDYRSIMAK ALADRLAEAF AEWLHDKVRR EFWGYETGDR LSNEELIREK YSGIRPAPGY PSQPDHTEKR ELFRLLDATQ RAHVQLTESL AMYPAASVSG LYFAHPEAAY FHLGRIGEDQ LEDYAKRKGM TIEEAARWLS PIL // ID H2EIF6_MALDO Unreviewed; 324 AA. AC H2EIF6; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 29-OCT-2014, entry version 13. DE SubName: Full=Homocysteine s-methytransferase {ECO:0000313|EMBL:AEX97078.1}; DE Flags: Fragment; GN Name=HMT {ECO:0000313|EMBL:AEX97078.1}; OS Malus domestica (Apple) (Pyrus malus). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Rosales; Rosaceae; Maloideae; Maleae; OC Malus. OX NCBI_TaxID=3750 {ECO:0000313|EMBL:AEX97078.1}; RN [1] {ECO:0000313|EMBL:AEX97078.1} RP NUCLEOTIDE SEQUENCE. RA Song Y.; RT "Characterization and isolation of differentially expressed bud sport RT genes in apple by suppression subtractive hybridization."; 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; JN941559; AEX97078.1; -; mRNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Transferase {ECO:0000313|EMBL:AEX97078.1}. FT NON_TER 324 324 {ECO:0000313|EMBL:AEX97078.1}. SQ SEQUENCE 324 AA; 35575 MW; EF050CB5D46A14BD CRC64; MGLNKAFTSS LEDAIEKAGG CAVVDGGFAT QLERHGAAIN DPLWSAVCLI NQPDLIKRVH LDYLDAGADI LITSSYQATI PGFLSRGLSI EQGELLLKKS VKLAVEARNS FWDALKVTPD HRYNRALVAA SIGSYGAYLA DGSEYSGCYG PRVDVDKLKD FHRRRFQVLV EAGPDLLAFE TFPNKLEAQA CLELLEEQSV QIPSWICFSS VDGENAPSGE GFTECLEVIN KSNKIHAVGI NCTPPHLIKS LICKFKDLTS KAIIVYPNSG EIWDGKAKRW LPAKCFDEEN FECFATIWRD SGAKHIGRCC RTTPSTVRAI SKVL // ID H2FYG5_OCESG Unreviewed; 1221 AA. AC H2FYG5; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 01-APR-2015, entry version 23. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:AEY00558.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEY00558.1}; GN Name=metH {ECO:0000313|EMBL:AEY00558.1}; GN OrderedLocusNames=GU3_04005 {ECO:0000313|EMBL:AEY00558.1}; OS Oceanimonas sp. (strain GK1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales; OC Aeromonadaceae; Oceanimonas. OX NCBI_TaxID=511062 {ECO:0000313|EMBL:AEY00558.1, ECO:0000313|Proteomes:UP000007742}; RN [1] {ECO:0000313|EMBL:AEY00558.1, ECO:0000313|Proteomes:UP000007742} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GK1 {ECO:0000313|EMBL:AEY00558.1, RC ECO:0000313|Proteomes:UP000007742}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP003171; AEY00558.1; -; Genomic_DNA. DR RefSeq; WP_014291293.1; NC_016745.1. DR RefSeq; YP_005091308.1; NC_016745.1. DR EnsemblBacteria; AEY00558; AEY00558; GU3_04005. DR KEGG; oce:GU3_04005; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; OSP511062:GI6E-837-MONOMER; -. DR Proteomes; UP000007742; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007742}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEY00558.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007742}; KW Transferase {ECO:0000313|EMBL:AEY00558.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 755 755 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1221 AA; 134944 MW; D74550787865C250 CRC64; MFSQLEQALA ERILIIDGGM GTMIQSYRLD EAAYRGERFA DWGSDLKGNN DLLVLTQPEI IAQIHSDYFA AGADIVETNT FNATTIAMAD YHMESLAAEI NLEAAKLARR VADEWTAKEP HKPRFVAGVL GPTNRTASIS PDVNDPGYRN ISFDQLVAAY TEATEALIDG GVDLLMIETI FDTLNAKAAV FAIEGVFEKR GVRLPVMISG TITDASGRTL TGQTTEAFYH SLRHAQPISF GLNCALGPDE LRQYVAELSR ISETYVSAHP NAGLPNAFGE YDLDAAEMAA HIREWAESGF LNLVGGCCGS TPEHIRAIAE AVKGIAPRPL PELPVACRLS GLEPVLITPE SMFVNVGERT NVTGSAKFKR LIKEELYDEA LEVALQQVEN GAQIIDINMD EGMLDAEACM ARFLNLIAGE PDISRVPIMI DSSKWEVIEA GLKCIQGKGI VNSISLKEGE AKFIEQARLV RRYGAAVIVM AFDEVGQADT RERKFEICQR AYRVLVDKVG FPPEDIIFDP NIFAVATGID EHNNYAVDFI EAVKDIKDNL PHAMISGGVS NVSFSFRGNE PVREAIHAVF LYHAIKNGMD MGIVNAGQLA IYEDIEPELK EKVEAVVLNL NDNATEALLE VAERYRNSGG PANDARDLEW RSWPVNKRLE HALVKGLTDF IEEDTEEARQ QAARPLDVIE GPLMDGMNVV GDLFGEGKMF LPQVVKSARV MKRAVAYLNP YIEATKAVGQ SNGKIVMATV KGDVHDIGKN IVGVVLQCNN FEVVDLGVMV PCETILKTAR ETNADMIGLS GLITPSLDEM VHVAKEMQRQ GFKIPLLIGG ATTSKAHTAV KIEQNYDEPV VYVSNASRAV GVVQSLLSET NKPAFVDRLN KEYEVVRDQH ARKKPRTKPV TLAEARANKV DIDWDAYTPP VPVKPGIHEF RDVPIATLRE YIDWTPFFLT WSLAGKYPRI LEDEVVGEEA KRLFADANAM LDKLAAEGEL SCAGVIGLFP ANSVGDDVEI YADESRSRVL HTLRFLRQQT EKKDGFPNYC LADYVAPKGS KPDYIGGFAV TGGIGEDEIV QRYKDAHDDY NAIMASAVAD RLAEAFAEYM HLRVRREFWG YAPDETLSND ELIREKYQGI RPAPGYPACP EHTEKGTLWQ WLDVENRIGM KLTESYAMWP GAAVSGFYFS YPDTRYFAVA RIQEDQLLDY AARKGMTRID AEKWLAPNLN D // ID H2GZY2_CORD7 Unreviewed; 1200 AA. AC H2GZY2; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 29-APR-2015, entry version 25. DE SubName: Full=5-methyltetrahydrofolate-homocysteinemethyltransferase {ECO:0000313|EMBL:AEX67449.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEX67449.1}; GN Name=metH {ECO:0000313|EMBL:AEX67449.1}; GN OrderedLocusNames=CDC7B_1253 {ECO:0000313|EMBL:AEX67449.1}; OS Corynebacterium diphtheriae (strain ATCC 27012 / C7 (beta)). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=698963 {ECO:0000313|EMBL:AEX67449.1, ECO:0000313|Proteomes:UP000007160}; RN [1] {ECO:0000313|EMBL:AEX67449.1, ECO:0000313|Proteomes:UP000007160} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27012 / C7 (beta) {ECO:0000313|Proteomes:UP000007160}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP003210; AEX67449.1; -; Genomic_DNA. DR RefSeq; WP_014319087.1; NC_016801.1. DR RefSeq; YP_005162703.1; NC_016801.1. DR EnsemblBacteria; AEX67449; AEX67449; CDC7B_1253. DR KEGG; cds:CDC7B_1253; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; CDIP698963:GHGE-1288-MONOMER; -. DR Proteomes; UP000007160; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007160}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEX67449.1}; KW Transferase {ECO:0000313|EMBL:AEX67449.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 233 233 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 751 751 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1200 AA; 131400 MW; 2F9B108473AD95EC CRC64; MNTATPQFKT AFLDAMKNRV LIGDGAMGTQ LQGFDLDVDS DFLGLEGCNE ILNHTRPDVV SAIHRAYFEA GADLVETNTF GCNLPNLADY DIADRCKELA FKGVKIAREV ADELGPSADG TPRFVLGSMG PGTKLPSLGH APYEALKNHY TEASLGMIEG GADAILVETA QDLLQVKAAV HGCQTAFETS GIQLPIVCHV TVETTGTMLL GSEIGAALTA IELLNVDMIG LNCATGPDEM SEHLRYLSRN AHIPVSVMPN AGLPVLGKNG AEYPLTEQEL ASALRGFVEE YGLSMVGGCC GTTPTHIREV RKAVLGDSEH QPALQAERNP DVGDAVSSLY TSVNLTQDTG ITMIGERTNA NGSKAFREAM LVGDLEKCVD IAKQQTRDGA HMLDLCVDYV GRDGTADMAQ LASLLATSST LPIMIDSTEP DVIQVGLEHL GGRCAVNSVN FEDGDGPDSR YQRIMRLVKR HGAAVVALTI DEEGQARTAE KKIEIAERLI ADITSTWGLD ESDIIVDTLT FPISTGQEET RRDGIETIEA IRELKKRHPK IHTTLGLSNI SFGLNPAARQ VLNSVFLNEC IEAGLDSAIA HSSKIVPMNR IDEEQRRVAL DLVYDRRSEG YDPLQTFMRL FEGVSAASAS DARAEALAAM PLFKRIAQRI IDGEKAGFED DLDAGMKEKE PLQIINEDLL EGMKTVGDLF GSGQMQLPFV LQSAETMKHA VAYLEQFIEA DEDAGDGNGT IVIATVKGDV HDIGKNLVDI ILSNNGFNVV NIGIKQPIAN ILEAAEKHKA DAIGMSGLLV KSTVIMKENL QEMNQAQKSD YPVILGGAAL TRAYVEDDLT EVYEGNVHYA KDAFESLRLM QEFMAEARGE RLDPQSPEAL AAVKKKAERK ARRERSKQIV AQRKAKEIPI EVPERSEVAA DVPIATPPFW GTRIVKGINL SEYLPLLDER ALFVGRWGLK ATRGGEGPSY EELVETEGRP RLRYWIDRLK AEKILDHAAV VYGYFPAVSE GDTVILLESP DPTSAEVARF NFPRQQRGEF LCVADFIRSR EHAIKTKTVD VFPLQLVTMG QPIADFANVL FADNNYRDYL EVHGVGVQLT EALAEYWHAR IRHELSLSDG SHAGDEDSAD LQEFFNLKYR GARYSFGYGS CPNLEDRETL VDLLDSRRIG VDISEEFQLH PEQSTDAFVL YHPEAKYFNV // ID H2IBC5_VIBSJ Unreviewed; 318 AA. AC H2IBC5; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 29-APR-2015, entry version 17. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AEX21809.1}; GN ORFNames=VEJY3_06585 {ECO:0000313|EMBL:AEX21809.1}; OS Vibrio sp. (strain EJY3). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=1116375 {ECO:0000313|EMBL:AEX21809.1, ECO:0000313|Proteomes:UP000006799}; RN [1] {ECO:0000313|EMBL:AEX21809.1, ECO:0000313|Proteomes:UP000006799} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EJY3 {ECO:0000313|EMBL:AEX21809.1, RC ECO:0000313|Proteomes:UP000006799}; 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; AEX21809.1; -; Genomic_DNA. DR RefSeq; WP_014231687.1; NC_016613.1. DR RefSeq; YP_005022787.1; NC_016613.1. DR EnsemblBacteria; AEX21809; AEX21809; VEJY3_06585. DR KEGG; vej:VEJY3_06585; -. DR BioCyc; VSP1116375:GJV8-1361-MONOMER; -. DR Proteomes; UP000006799; Chromosome 1. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006799}; KW Methyltransferase {ECO:0000313|EMBL:AEX21809.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006799}; KW Transferase {ECO:0000313|EMBL:AEX21809.1}. SQ SEQUENCE 318 AA; 35234 MW; 7ADD6F0EB08CB2B2 CRC64; MAAQKSFPTQ QDGRLYLTEG GTETELMYKY GFDLPQFAMY PLLDNPAAVE KMREMFRSYL DVAAKHKVCA LMGGLDYRAS PDWGALLGYS AQSLADANIQ CIEFLREVAK EYATDIPEVL FQGLIGPRGD AYSTNHKITE NEAEDYHSVQ LETLKKADVD LALAITFNNI PESIGVVRAA QKIGVPLAIS LTLDSSSKLN SGPSLAEAIK TIDRETDNAV EFYLINCSHP VEYEPAIENS DWIHRIRGVR PNASKMEKLA LCKLGHLEDG DPVELGEQCG DLAKRYPHMD IWGGCCGTWD NHLDEITKQV IAAKAKED // ID H2ICZ7_VIBSJ Unreviewed; 1226 AA. AC H2ICZ7; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 29-APR-2015, entry version 23. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:AEX23258.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AEX23258.1}; GN Name=metH {ECO:0000313|EMBL:AEX23258.1}; GN ORFNames=VEJY3_13920 {ECO:0000313|EMBL:AEX23258.1}; OS Vibrio sp. (strain EJY3). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=1116375 {ECO:0000313|EMBL:AEX23258.1, ECO:0000313|Proteomes:UP000006799}; RN [1] {ECO:0000313|EMBL:AEX23258.1, ECO:0000313|Proteomes:UP000006799} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EJY3 {ECO:0000313|EMBL:AEX23258.1, RC ECO:0000313|Proteomes:UP000006799}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP003241; AEX23258.1; -; Genomic_DNA. DR RefSeq; WP_014233124.1; NC_016613.1. DR RefSeq; YP_005024237.1; NC_016613.1. DR EnsemblBacteria; AEX23258; AEX23258; VEJY3_13920. DR KEGG; vej:VEJY3_13920; -. DR KO; K00548; -. DR BioCyc; VSP1116375:GJV8-2851-MONOMER; -. DR Proteomes; UP000006799; Chromosome 1. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006799}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEX23258.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006799}; KW Transferase {ECO:0000313|EMBL:AEX23258.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1226 AA; 136687 MW; C691710FFEDBA662 CRC64; MGTNVRQQIE AQLKQRILLI DGGMGTMIQG YKLEEHDYRG ERFADWHSDL KGNNDLLVLS QPQLIKEIHS AYLEAGADIL ETNTFNATTI AMADYDMESL SEEINFAAAK LAREVADEWT AKTPEKPRYV AGVLGPTNRT CSISPDVNDP GYRNVSFDEL VEAYSESTRA LIKGGSDLIL IETIFDTLNA KACAFAVDSV FEELGIELPV MISGTITDAS GRTLSGQTTE AFYNSLRHVR PISFGLNCAL GPDELRPYVE ELSRISESFV SAHPNAGLPN AFGEYDLSPE DMAKHVKEWA ESGFLNLIGG CCGTTPEHIR QMAEAVNQVT PRQLPELQVA CRLSGLEPLT IEKESLFINV GERTNVTGSA RFKRLIKEEL YDEALDVARQ QVENGAQIID INMDEGMLDA EACMVRFLNL CASEPEISKV PIMVDSSKWE VIEAGLKCIQ GKGIVNSISL KEGKEKFVEQ AKLIRRYGAA VIVMAFDEVG QADTRERKIE ICTNAYRILV DEVGFPPEDI IFDPNIFAVA TGIDEHNNYA VDFIEAVGDI KRDLPHAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK NGMDMGIVNA GQLEIYDNVP EKLREAVEDV VLNRRNDATE RLLDIASEYA DKGVGKEEDA SALEWRTWPV EKRLEHALVK GITEFIVEDT EEARVNASKP LEVIEGPLMD GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AHLEPFIDAE KQVGQTNGKI LLATVKGDVH DIGKNIVGVV LQCNNYEIID LGVMVPCEKI LKVAKEENVD IIGLSGLITP SLDEMVHVAK EMERLDFDLP LLIGGATTSK AHTAVKIEQN YKHPVVYVNN ASRAVGVCTS LLSDERRPDF VEKLNADYER VRDQHNRKKP RTKPVTLQEA RANKVAIDWE AYTPPAPKQS GIHIFDDFDV ATLRKYIDWT PFFMTWSLVG KYPTIFDHEE VGEEAKRLFH DANELLDRVE SEGLMQARGM CGLFPAASVG DDIEVYTDES RTEVAKVLCN LRQQTEKPKG FNYCLSDYVA PKDSGKHDWI GAFAVTGGIG ERELADEYKA KGDDYNAIMI QAVADRLAEA FAEYLHERVR KEIWGYAEDE NLSNDELIRE KYQGIRPAPG YPACPEHTEK GPLWDLLNVE ENIGMSLTSS YAMYPGASVS GWYFSHPDSR YFAIAQIQED QLESYAERKG WDRLEAEKWL GPNING // ID H2IM48_VIBSJ Unreviewed; 302 AA. AC H2IM48; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AEX24525.1}; GN ORFNames=VEJY3_20541 {ECO:0000313|EMBL:AEX24525.1}; OS Vibrio sp. (strain EJY3). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=1116375 {ECO:0000313|EMBL:AEX24525.1, ECO:0000313|Proteomes:UP000006799}; RN [1] {ECO:0000313|EMBL:AEX24525.1, ECO:0000313|Proteomes:UP000006799} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EJY3 {ECO:0000313|EMBL:AEX24525.1, RC ECO:0000313|Proteomes:UP000006799}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; AEX24525.1; -; Genomic_DNA. DR RefSeq; WP_014234369.1; NC_016614.1. DR RefSeq; YP_005025500.1; NC_016614.1. DR EnsemblBacteria; AEX24525; AEX24525; VEJY3_20541. DR KEGG; vej:VEJY3_20541; -. DR BioCyc; VSP1116375:GJV8-4177-MONOMER; -. DR Proteomes; UP000006799; Chromosome 2. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006799}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:AEX24525.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006799}; KW Transferase {ECO:0000313|EMBL:AEX24525.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 208 208 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 302 AA; 32641 MW; 32690752AD038EB7 CRC64; MKTNTMLILD GGMGRELNRR GAPFRQPEWS ALAMIEAPEI VKDVHTDYIQ SGAQVITTNS YALVPFHIGE ARFKEAGQSL AALSGQVAKE AAQGTGAKVA GSLPPLFGSY RPDLYDQEHV RDLATPLILG LSDSVDFWLA ETQSLIAESV AVKALVDELT SEAKPFWVSF TLEDSEPTDE PCLRSGETVQ QAVTTMAQAG VSAILFNCCQ PEIVEEALQV SVRTLEELGL SHIRLGVYAN AFPPQPKDAT ANDGLDEIRD DLSPDAYLIW AEKWRQSGAS IIGGCCGIGP EHIAKLSQHF KG // ID H2IV67_RAHAC Unreviewed; 1233 AA. AC H2IV67; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 29-APR-2015, entry version 23. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AEX53981.1}; GN OrderedLocusNames=Rahaq2_4215 {ECO:0000313|EMBL:AEX53981.1}; 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 {ECO:0000313|EMBL:AEX53981.1, ECO:0000313|Proteomes:UP000009010}; RN [1] {ECO:0000313|Proteomes:UP000009010} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 / RC CIP 78.65 {ECO:0000313|Proteomes:UP000009010}; 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 ----------------------------------------------------------------------- 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; AEX53981.1; -; Genomic_DNA. DR RefSeq; WP_015699018.1; NZ_JMPO01000127.1. DR RefSeq; YP_005202121.1; NC_016818.1. DR EnsemblBacteria; AEX53981; AEX53981; Rahaq2_4215. DR EnsemblBacteria; KFD02789; KFD02789; GRAQ_03211. DR KEGG; raq:Rahaq2_4215; -. DR KO; K00548; -. DR Proteomes; UP000009010; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009010}; KW Methyltransferase {ECO:0000313|EMBL:AEX53981.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000009010}; KW Transferase {ECO:0000313|EMBL:AEX53981.1}. SQ SEQUENCE 1233 AA; 136759 MW; 16FE7F5B7CF7AADF CRC64; MGDEVKVTNR VEALHKQLAQ RILVLDGGMG TMIQSYRLEE EDYRGERFAD WESDLKGNND LLVLSKPEVI VEIHNGYLAA GADILETNTF NSTTIAMADY HMESLSAEIN YEAARLARQC ADEWTARTPD KPRYVAGVLG PTNRTASISP DVNDPAFRNV SFDQLVEAYR ESTRALIEGG ADLIMIETVF DTLNAKAATF AVESEFEAMG IVLPVMVSGT ITDASGRTLS GQTTEAFYNS LRHVKPLTFG LNCALGPDEL RQYVAELSRI AECYVTAHPN AGLPNAFGEY DLEAKEMAEH IAEWARSGFL NIVGGCCGTT PAHIAAMVKA VEGVPPRVLP TIPVACRLAG LEPLTIDPQT LFVNVGERTN VTGSARFKRL IKEEKYSEAL AVARQQVESG AQIIDINMDE GMLDAEAAMV RFLSLIAGEP DIARVPIMID SSKWDVIEKG LKCIQGKGIV NSISMKEGEE AFLHHARMVR RYGAAVVVMA FDETGQADTR ARKIEICRRA YKLLTEKVGF PPEDIIFDPN IFAVATGIDE HNNYAVDFIE ACADIKAQLP HALISGGVSN VSFSFRGNEP VREAIHAVFL YHAIRNGMDM GIVNAGQLAI YDDLPAELRD AVEDVILNRR PDGTERLLEL AEKYRGSKDD GEANKQQAEW RSWEVKKRLE YSLVKGITEF IELDTEECRQ LAARPIEVIE GPLMDGMNVV GDLFGAGKMF LPQVVKSARV MKQAVAYLEP YIEASKEKGQ TNGKILLATV KGDVHDIGKN IVGVVLQCNN YEIIDLGVMV PTDKILKTAI EENVDIIGLS GLITPSLDEM VNVAKEMERR GFTMPLLIGG ATTSKAHTAV KIEQNYSGVT CYVQNASRSV GVVSALLSKD QRDAFIERTR KEYDTVRIQH GRKKPRTPPV SLEVARDNAT VIDWENYTPP VAHRPGIQKV EASIETLRNY IDWTPFFMTW SLAGKYPRIL EDEVVGEEAK RLFKDANDLL DKLSTEKSLN PRGVVGLFPA NSKGDDIEIY SDERRQDVLV VSHHLRQQTE KTDFANYCLA DFVAPKSSGK KDYMGAFAVT GGLEEDALAE AYDKQHDDYN KIMIKALADR LAEAFAEYLH EKVRKVYWGF AANENLSNEE LIRENYQGIR PAPGYPACPE HTEKGQIWKL LDVEANTGMQ LTESFAMWPG AAVSGWYFSH PDSKYFAVAQ IQRDQVEDYA ARKNMPVAEV ERWLAPNLGY DAD // ID H2J1V0_RAHAC Unreviewed; 300 AA. AC H2J1V0; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Homocysteine/selenocysteine methylase (S-methylmethionine-dependent) {ECO:0000313|EMBL:AEX54547.1}; GN OrderedLocusNames=Rahaq2_4828 {ECO:0000313|EMBL:AEX54547.1}; OS Rahnella aquatilis (strain ATCC 33071 / DSM 4594 / JCM 1683 / NBRC OS 105701 / NCIMB 13365 / CIP 78.65). OG Plasmid pRahaq201 {ECO:0000313|EMBL:AEX54547.1, OG ECO:0000313|Proteomes:UP000009010}. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Rahnella. OX NCBI_TaxID=745277 {ECO:0000313|EMBL:AEX54547.1, ECO:0000313|Proteomes:UP000009010}; RN [1] {ECO:0000313|Proteomes:UP000009010} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 / RC CIP 78.65 {ECO:0000313|Proteomes:UP000009010}; 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 plasmid 1 of Rahnella aquatilis CIP 78.65."; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003245; AEX54547.1; -; Genomic_DNA. DR RefSeq; WP_014341833.1; NZ_JMPO01000152.1. DR RefSeq; YP_005220555.1; NC_016835.1. DR EnsemblBacteria; AEX54547; AEX54547; Rahaq2_4828. DR EnsemblBacteria; KFD00042; KFD00042; GRAQ_04626. DR KEGG; raq:Rahaq2_4828; -. DR Proteomes; UP000009010; Plasmid pRahaq201. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009010}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:AEX54547.1}; KW Plasmid {ECO:0000313|EMBL:AEX54547.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000009010}; KW Transferase {ECO:0000313|EMBL:AEX54547.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 207 207 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 300 AA; 31519 MW; FD1C7FE062905591 CRC64; MISNIKILDG GMGRELARMG APFRQPEWSA LALMQAPEFV RAAHDAFIAA GSQVITTNSY AVVPFHVGEE IFAEQGAALI ALSGKLAREA AEAAPAAVQV AGSLPPVLGS YRPDLFEPVA AKKLLQVLVD NLTDSVDVWL AETQSSVAEV EAVRDVLGDD PRPLWLSFTL QDNPDDQGNA LLRSGESVGD AVSAALRVSA AAVLFNCSRP EVMATAVKTA RAALTTQGSQ LDIGVYANAF EPSDNKRGAN EGLSKMRQDT DPAGYLDFAK DWVAQGATLV GGCCGIGPEH IAALKQAFAK // ID H2J4L7_MARPK Unreviewed; 782 AA. AC H2J4L7; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase/B12 binding domain/Pterin binding enzyme {ECO:0000313|EMBL:AEX85959.1}; GN OrderedLocusNames=Marpi_1569 {ECO:0000313|EMBL:AEX85959.1}; OS Marinitoga piezophila (strain DSM 14283 / JCM 11233 / KA3). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Marinitoga. OX NCBI_TaxID=443254 {ECO:0000313|EMBL:AEX85959.1, ECO:0000313|Proteomes:UP000007161}; RN [1] {ECO:0000313|Proteomes:UP000007161} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14283 / JCM 11233 / KA3 RC {ECO:0000313|Proteomes:UP000007161}; 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., Jebbar M., RA Vannier P., Oger P., Cario A., Bartlett D., Noll K.M., Woyke T.; RT "Complete sequence of chromosome of Marinitoga piezophila KA3."; RL Submitted (JAN-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; CP003257; AEX85959.1; -; Genomic_DNA. DR RefSeq; WP_014297030.1; NC_016751.1. DR RefSeq; YP_005097257.1; NC_016751.1. DR EnsemblBacteria; AEX85959; AEX85959; Marpi_1569. DR KEGG; mpz:Marpi_1569; -. DR KO; K00548; -. DR BioCyc; MPIE443254:GI5V-1569-MONOMER; -. DR Proteomes; UP000007161; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007161}; KW Methyltransferase {ECO:0000313|EMBL:AEX85959.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007161}; KW Transferase {ECO:0000313|EMBL:AEX85959.1}. SQ SEQUENCE 782 AA; 87073 MW; 3196D003294F77BE CRC64; MNRKEFSELL NQRVLFLDGA YGTEFFKMGI RGRMPIELLN ITNPDAVYTL QKAYVNAGVD FLLTNTFSAN RLKMQSLKVK ENIKDINFHA VKIAKDAAKN SNVKILGDIS STGILLTPLG ELSFDEAYEV FKEQGEILLN AGIDGFIIET MSDLKELKAA FLALRDLDNN IPIIAHLTFE ENGRTVTGTS VEIFATLFND LDVDVIGMNC TLTPEEMIKV FQTLSKYSKK PISVEPNAGK PKLQPDGSVI YNTTPEKFSV YMEDFVHLGA NIIGGCCGTG PEHIKLMREF IGKTRVRKRE TIKKQFLSSR TILRETEPFL IIGERINASG KKNFQNAIRE YNFDRMVNLA TAQEKEGSHV LDINLGIEKL LDKKHFEKSI IILDKIGSIP LSLDIQQPEF MEVALKEYVG RPLINSSTVE KEKLDTAIRW LKRYGGMLIL LTMKNKIPET AQERFEIAMK GIKYLEENGI SKDRIFVDPL VLPVGAKKDP FVTLETIKLL SEKGIKTSIG LSNLSFGLPS REGINASFLS LAIHNGLSGA ILNSKESSTM NIVFGSLILH GMEVSRDTST STGDELADLI LKKKSRELKE KINLLLKDYT PLQVSQNILA KTMEYIGELY SKGEIYLPQL ILAAETVTPI FEYLNNMLKK EESSSKGTIL VATVEGDVHD IGKKIVATVL KSSGYEVIDI GKDIPGKIIL EKVKELKSDL LGLSAMMTTT VGKIKEVKDL LLENGVEIPI IAGGASMNKE LASKFGVFYA KNANEALKYA KRFINNKKIR EL // ID H2JCA2_9CLOT Unreviewed; 585 AA. AC H2JCA2; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 01-APR-2015, entry version 21. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=Clo1100_0738 {ECO:0000313|EMBL:AEY65009.1}; OS Clostridium sp. BNL1100. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=755731 {ECO:0000313|EMBL:AEY65009.1, ECO:0000313|Proteomes:UP000007324}; RN [1] {ECO:0000313|EMBL:AEY65009.1, ECO:0000313|Proteomes:UP000007324} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BNL1100 {ECO:0000313|EMBL:AEY65009.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; AEY65009.1; -; Genomic_DNA. DR RefSeq; WP_014312394.1; NC_016791.1. DR RefSeq; YP_005146814.1; NC_016791.1. DR EnsemblBacteria; AEY65009; AEY65009; Clo1100_0738. DR KEGG; clb:Clo1100_0738; -. DR KO; K00547; -. DR BioCyc; CSP755731:GJVM-737-MONOMER; -. DR Proteomes; UP000007324; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007324}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 585 AA; 64843 MW; 47E97723956BC318 CRC64; MNIFINRDYF LFDGAMGTYY SSKNKNNTPC EFANISEREN ILNIHLEYIQ AGVNAIKTNT FGANRFSLGC QQSEVDRIIK SGYDIAVQAC SGQEVAVFAD IGPIPDGKGA NPEEEYKKIV DIFMECGAKN FLFETFSSTD ILTGVAAYIR LRLPDAVIIT SFAVYPDGYS KEGLFYIDIM EKMYASGLVD AVGLNCISGP AHMYRLIKKA DIRGKNIIIM PNSGYPGTER GRTVYYDNSE YYAEKLLDIM KLGVKILGGC CGTTPRHIAA AAKLLTSPQP VESNTDISTH MEICDLEYEN ILDRLVKNKK PILVEVDPPF DTNWEYMLRD TLILKQAGAD IITIADSPLA KARAESTIMA AKIQREVAIP VMPHITCRDK NLLGIKASLL GVHIEGIRNV LVITGDPIAN IESSRIKGVF SFNSSNLANY IKSLNSNVFC GQDIKIAGAL NVNAVNFSAE LKKAFTKIEN GISCFLTQAI YTKGAVENLQ KAVEALNVPI FAGFMPIVSY KNAQFINNEV PGIDIDIETI EKFRDRSREE SEKLGMEITM DIVEEIYPHV SGFYLMTPLK RTGVICELIK KIKEI // ID H2JDK8_9CLOT Unreviewed; 434 AA. AC H2JDK8; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 01-APR-2015, entry version 18. DE SubName: Full=Cobalamin-dependent methionine synthase I {ECO:0000313|EMBL:AEY66375.1}; GN ORFNames=Clo1100_2194 {ECO:0000313|EMBL:AEY66375.1}; OS Clostridium sp. BNL1100. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=755731 {ECO:0000313|EMBL:AEY66375.1, ECO:0000313|Proteomes:UP000007324}; RN [1] {ECO:0000313|EMBL:AEY66375.1, ECO:0000313|Proteomes:UP000007324} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BNL1100 {ECO:0000313|EMBL:AEY66375.1}; 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; AEY66375.1; -; Genomic_DNA. DR RefSeq; WP_014313746.1; NC_016791.1. DR RefSeq; YP_005148180.1; NC_016791.1. DR EnsemblBacteria; AEY66375; AEY66375; Clo1100_2194. DR KEGG; clb:Clo1100_2194; -. DR KO; K00548; -. DR BioCyc; CSP755731:GJVM-2192-MONOMER; -. DR Proteomes; UP000007324; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007324}. SQ SEQUENCE 434 AA; 47285 MW; D709F2F367E08B0E CRC64; MSFLNDIEKK VLVFDGSMGI MLQSKGLEVG TCPEEWNVTH PDKVKEIYTA YRNAGANVIQ SNTFQSNLMK LSEYGLQDKH YDINFAGVSL AKEVMGDNGY VAASIGPLGK LLEPFGELTF KQAYNTFKEQ VVAVTAGGAD IISFETFTDV SEMRIALLAA KENCNLPVIC SISYEQNGRT LMGSDPAVCA YILHSLGADM VGTNCSFGPE YMIKVAEIYG KTGLNFSIKP NAGIPQTVDG KLVYDETPEK FAKYAHEFIK NGARLVGGCC GSRPEFIAEI SKVVSECNAV SFPLNVDFIT SSTKVISFVD IKQTEIGWID INKEEILKKD LLAGDVSSIT DTAMDLMEED YGLIAIDVDV AGADELLLSH VVKEAQTYLK QPFVLKSDNP KSLEAALRIY KGRAGVITKA SDCVDELLYK YGAVNVGGFI SNEK // ID H2JNA2_STRHJ Unreviewed; 1155 AA. AC H2JNA2; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 29-APR-2015, entry version 21. DE SubName: Full=5-methyltetrahydrofolate:homocysteine S-methyltransferase {ECO:0000313|EMBL:AEY88370.1}; GN OrderedLocusNames=SHJG_3096 {ECO:0000313|EMBL:AEY88370.1}; OS Streptomyces hygroscopicus subsp. jinggangensis (strain 5008). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1133850 {ECO:0000313|EMBL:AEY88370.1, ECO:0000313|Proteomes:UP000007170}; RN [1] {ECO:0000313|Proteomes:UP000007170} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=5008 {ECO:0000313|Proteomes:UP000007170}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP003275; AEY88370.1; -; Genomic_DNA. DR RefSeq; WP_014671704.1; NC_017765.1. DR RefSeq; YP_006244243.1; NC_017765.1. DR EnsemblBacteria; AEY88370; AEY88370; SHJG_3096. DR KEGG; shy:SHJG_3096; -. DR KO; K00548; -. DR BioCyc; SHYG1133850:GLLU-3099-MONOMER; -. DR Proteomes; UP000007170; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007170}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AEY88370.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007170}; KW Transferase {ECO:0000313|EMBL:AEY88370.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 223 223 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 733 733 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1155 AA; 126604 MW; 71D1D41DE4005D95 CRC64; MSALREALAT RVVVADGAMG TMLQAQEPTL EDFQNLEGCN EVLNITRPDI VRSVHEAYFA VGVDCVETNT FGANHAAMAE YDIADRVHEL SEAGARIARE TADEFSARDG RPRWVLGSIG PGTKLPTLGH IGFTTIRDGF QANAEGLLTG GADALIVETT QDLLQTKASV LGARRAMERL GTEVPLLCSM AFETTGTMLL GSEIGAALTA LEPLGIDMIG LNCSTGPAEM SEHLRYLTRH SRIPLLCMPN AGLPILTKDG AHFPLDAEGL ADAQENFVRD YGLSLVGGCC GTTPEHLRQV VERVRDLTPP ERDPRPEPGA ASLYQSVPFR QDTSYLAIGE RTNANGSKKF REAMLEGRWD DCVEMAREQI REGAHLLDLC VDYVGRDGVA DMEELAGRFA TASTLPIVLD STEVDVIKAG LEKLGGRAVI NSVNYEDGDG PDSRFAKVTR LAREHGAALI ALTIDEEGQA RTPEKKVEIA ERLIADLTGN WGIREEDILI DTLTFTICTG QEESRKDGIA TIEAIRELKR RHPAVQTTLG LSNISFGLNP AARILLNSVF LDECVKAGLD SAIVHASKIL PIARFGEEEV ATALDLIHDR RAEGYDPLQK LMQLFEGATA KSLKAGKAEE LAALPLEERL KRRIIDGERN GLEADLDQAL QDRPALDIVN ETLLDGMKVV GELFGSGQMQ LPFVLQSAEV MKAAVAYLEP HMEKSDAEGK GTIVLATVRG DVHDIGKNLV DIILSNNGYN VVNLGIKQPV SAILEAAEEH RADVIGMSGL LVKSTVIMKE NLEELNQRGL AARFPVILGG AALTRAYVEQ DLHEIYEGEV RYARDAFEGL RLMDALIGVK RGVPGAKLPE LRQRRVRAAA VEVEERPEEG HVRSDVATDN PIPEPPFWGT RVVKGIQLKE YASWLDEGAL FKGQWGLKQA RTGEGPTYEE LVETEGRPRL RGLLDRLQTE NLLEAAVVHG YFPCVSKDDD LIILDEQGNE RTRFTFPRQR RGRRLCLADF FRPEESGETD VVGLQVVTIG SRIGAETAKL FEANAYRDYL ELHGLSVQLA EALAEYWHAR VRAELGFGGE DPAAIEDMFD LKYRGARFSL GYGACPDLED RAKIAELLKP ERIGVHLSEE FQLHPEQSTD AIVIHHPEAK YFNAR // ID H2K7U1_STRHJ Unreviewed; 309 AA. AC H2K7U1; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 29-APR-2015, entry version 17. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:AEY92475.1}; GN OrderedLocusNames=SHJG_7208 {ECO:0000313|EMBL:AEY92475.1}; OS Streptomyces hygroscopicus subsp. jinggangensis (strain 5008). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1133850 {ECO:0000313|EMBL:AEY92475.1, ECO:0000313|Proteomes:UP000007170}; RN [1] {ECO:0000313|Proteomes:UP000007170} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=5008 {ECO:0000313|Proteomes:UP000007170}; 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 ----------------------------------------------------------------------- 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; AEY92475.1; -; Genomic_DNA. DR RefSeq; WP_014675760.1; NC_017765.1. DR RefSeq; YP_006248348.1; NC_017765.1. DR EnsemblBacteria; AEY92475; AEY92475; SHJG_7208. DR KEGG; shy:SHJG_7208; -. DR KO; K00547; -. DR BioCyc; SHYG1133850:GLLU-7274-MONOMER; -. DR Proteomes; UP000007170; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007170}; KW Methyltransferase {ECO:0000313|EMBL:AEY92475.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007170}; KW Transferase {ECO:0000313|EMBL:AEY92475.1}. SQ SEQUENCE 309 AA; 32305 MW; A212E157AB835B61 CRC64; MTMTSHTSPT LADALAAGTV VLDGGMSNQL ESAGHDLSDE LWSARLLAER PEAVTEAHLA YYLAGASVAI TSSYQATFEG FGKRGIGRDE AARLLGLSVE LARDAARKAQ GAGVPRPLWV AASVGPYGAM LADGSEYRGR YGMSVDELER FHRPRMEVLA AAAPDVLALE TVPDADEAAA LLRAVRGLGM PAWLSYTVEG LRTRAGQPLE EAFGLAADAD EVIAVGVNCC APEDVRGAVE IAARVTGKPV VVYPNSGEAW DARARAWRGR TTFGAEQVKA WREAGARLIG GCCRVGPQAI TGIAGALAA // ID H2KVN9_CLOSI Unreviewed; 451 AA. AC H2KVN9; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 07-JAN-2015, entry version 10. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:GAA34816.1}; GN ORFNames=CLF_112792 {ECO:0000313|EMBL:GAA34816.1}; OS Clonorchis sinensis (Chinese liver fluke). OC Eukaryota; Metazoa; Platyhelminthes; Trematoda; Digenea; OC Opisthorchiida; Opisthorchiata; Opisthorchiidae; Clonorchis. OX NCBI_TaxID=79923 {ECO:0000313|Proteomes:UP000008909}; RN [1] {ECO:0000313|Proteomes:UP000008909} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Wang X., Chen W., Huang Y., Sun J., Men J., Liu H., Luo F., Guo L., RA Lv X., Deng C., Zhou C., Fan Y., Li X., Huang L., Hu Y., Liang C., RA Hu X., Xu J., Yu X.; RT "The draft genome of the carcinogenic human liver fluke Clonorchis RT sinensis."; 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; DF144786; GAA34816.1; -; Genomic_DNA. DR InParanoid; H2KVN9; -. DR Proteomes; UP000008909; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008909}; KW Methyltransferase {ECO:0000313|EMBL:GAA34816.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008909}; KW Transferase {ECO:0000313|EMBL:GAA34816.1}. SQ SEQUENCE 451 AA; 50409 MW; B8C8EC04E71D902C CRC64; MTDDRVARWM NEIRVLDGGV GSECQKRSHL PIDGHKAWSC RLLKEDPNLV CEVHKSYLRA GCDVLSTNTY QASPLTLAKA LKISDSEARE LMRHAVRLVR RAIATTNEES FAADTHQWKS RKLPVLVAGS LGPYGACLAD GSEYSGSYAD KMTFDELVEF HYARAKILVD AGVDFLAWET IPILMEVVAI AEVMRRLPQA LAWLSVASSN GQTTVGGDPL HQVAFEIQKC DQIFGIGVNC CIEHDKIGLA LSNLNIGQDG CGPGTDDGYH PPPCSKRPEH LDKLSTKPRK LLVLYANSGE MWSPPPKGLS RRRGHWVWPP NKGPSVWART IAQFSMRRCA DWEKELFNGV AVRRSDPEAV YPKAQWVGGC CRVGPMEIRH LAILMKPDEV QDVFLETSLA IPSIQTPAST VLFRRQSARN KRKLTENYQR RIQPSRAVKS RRSVGYNQEE H // ID H2LAV3_ORYLA Unreviewed; 399 AA. AC H2LAV3; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 29-APR-2015, entry version 19. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSORLP00000003019}; OS Oryzias latipes (Japanese rice fish) (Japanese killifish). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; OC Oryziinae; Oryzias. OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000003019, ECO:0000313|Proteomes:UP000001038}; RN [1] {ECO:0000313|Ensembl:ENSORLP00000003019, ECO:0000313|Proteomes:UP000001038} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000003019, RC ECO:0000313|Proteomes:UP000001038}; RX PubMed=17554307; DOI=10.1038/nature05846; RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., RA Yamada T., Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., RA Shimada A., Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., RA Asakawa S., Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., RA Sugano S., Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., RA Nomoto H., Nogata K., Morishita T., Endo T., Shin-I T., Takeda H., RA Morishita S., Kohara Y.; RT "The medaka draft genome and insights into vertebrate genome RT evolution."; RL Nature 447:714-719(2007). RN [2] {ECO:0000313|Ensembl:ENSORLP00000003019} RP IDENTIFICATION. RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000003019}; RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSORLP00000003019}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSORLT00000003020; ENSORLP00000003019; ENSORLG00000002431. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; H2LAV3; -. DR OMA; KAHYMSQ; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000001038; Chromosome 12. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001038}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Reference proteome {ECO:0000313|Proteomes:UP000001038}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 212 212 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 399 AA; 43889 MW; 64F749C5CCE3691A CRC64; MAPSGTKKNI LERLEAGEVI IGDGGFVVAL EKRGYVKAGP WTPEAAAEHP EAVRQLHREF LRAGSTVMQT FTFYASDDKL ENRGNTQRFT GQQINEAACD LAREVANEGD ALVAGGVSQT PSYMSCESEQ AVKAIFKKQI DVFIRKDVDF LIAEYFEHVE EAEWAVQILK TSGKPVAATL CIGPEGDLNG VSPGDCAVRL VKAGADIVGV NCHFDPETCV KTVKLMKEGV ERAGLKAHYM SQPLALHTPD CNRQGFIDLP EFPFALEPRV LTRWDMHRYA RGAYNAGIRY IGGCCGFEPY HIRAVAEELA PERGFLPPAS EHGSWGAGLE MHTKPWVRAR ARREYWETLK PASGRPFCAA MSKPDCWGIS RGHADLMQTK EATSEAQLKA VFDKAAQSQ // ID H2LDV1_ORYLA Unreviewed; 397 AA. AC H2LDV1; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSORLP00000004115}; GN Name=LOC101157623 {ECO:0000313|Ensembl:ENSORLP00000004115}; OS Oryzias latipes (Japanese rice fish) (Japanese killifish). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; OC Oryziinae; Oryzias. OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000004115, ECO:0000313|Proteomes:UP000001038}; RN [1] {ECO:0000313|Ensembl:ENSORLP00000004115, ECO:0000313|Proteomes:UP000001038} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000004115, RC ECO:0000313|Proteomes:UP000001038}; RX PubMed=17554307; DOI=10.1038/nature05846; RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., RA Yamada T., Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., RA Shimada A., Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., RA Asakawa S., Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., RA Sugano S., Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., RA Nomoto H., Nogata K., Morishita T., Endo T., Shin-I T., Takeda H., RA Morishita S., Kohara Y.; RT "The medaka draft genome and insights into vertebrate genome RT evolution."; RL Nature 447:714-719(2007). RN [2] {ECO:0000313|Ensembl:ENSORLP00000004115} RP IDENTIFICATION. RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000004115}; RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSORLP00000004115}. 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_004072245.1; XM_004072197.2. DR Ensembl; ENSORLT00000004116; ENSORLP00000004115; ENSORLG00000003310. DR GeneID; 101157623; -. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; H2LDV1; -. DR OMA; WGVTKGT; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000001038; Chromosome 9. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001038}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Reference proteome {ECO:0000313|Proteomes:UP000001038}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 210 210 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 292 292 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 397 AA; 44170 MW; 248A551F32A5BC5C CRC64; MAPTKKGILE RLNAGEIVIG DGGFVFALEK RGYVKAGPWT PEAAKEYPEA VRQLHREFLR AGSNVMQTFT FYASDDKLEN RGNKLSYTGA QINEAACDLA REVANEGDAL VAGGVSQTPS YLSCKSEKDV KAIFKKQLDV FVKKNVDFLI AEYFEHVEEA VWAVEMLKET GKPVAATLCI GPQGDMHGVS PQECAVRLVT AGAQIVGINC HFDPETCVKT VKMMKEGVEK AGLKAHYMVQ PLAFHTPDCN CQGFIDLPEF PFGLEPRILT RWDMHKYARE AYNAGIRYIG GCCGFEPYHI RAVAEELATE RGFFPAATEK HGPWGSGLEM HTKPWVRARA RRDYWENLKP SSGRPFCPSL SVPDGWGVTR GHAELMQQKE ATSKDQLKQL FDRSKTQ // ID H2MH00_ORYLA Unreviewed; 1267 AA. AC H2MH00; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 29-APR-2015, entry version 24. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSORLP00000017896}; DE Flags: Fragment; GN Name=MTR {ECO:0000313|Ensembl:ENSORLP00000017896}; OS Oryzias latipes (Japanese rice fish) (Japanese killifish). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; OC Oryziinae; Oryzias. OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000017896, ECO:0000313|Proteomes:UP000001038}; RN [1] {ECO:0000313|Ensembl:ENSORLP00000017896, ECO:0000313|Proteomes:UP000001038} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000017896, RC ECO:0000313|Proteomes:UP000001038}; RX PubMed=17554307; DOI=10.1038/nature05846; RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., RA Yamada T., Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., RA Shimada A., Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., RA Asakawa S., Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., RA Sugano S., Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., RA Nomoto H., Nogata K., Morishita T., Endo T., Shin-I T., Takeda H., RA Morishita S., Kohara Y.; RT "The medaka draft genome and insights into vertebrate genome RT evolution."; RL Nature 447:714-719(2007). RN [2] {ECO:0000313|Ensembl:ENSORLP00000017896} RP IDENTIFICATION. RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000017896}; RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 1}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSORLP00000017896}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSORLT00000017897; ENSORLP00000017896; ENSORLG00000014271. DR GeneTree; ENSGT00420000029824; -. DR InParanoid; H2MH00; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG7TF786; -. DR TreeFam; TF312829; -. DR Proteomes; UP000001038; Chromosome 19. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001038}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001038}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 260 260 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 785 785 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSORLP00000017896}. SQ SEQUENCE 1267 AA; 140264 MW; 03516291C975917B CRC64; ITGGLKPFLL SAGCRPQLEA ELRALLQQRI LVLDGGMGTM IQQQQLDEGD FRGEEFKAHP LPLNGNNDLL SITRPDVIYK IHKEYLLAGA DIVETNTFSS TSIAQADYGL EHMAYLLNRR SAELARKAAD DVTKQTGVKR FVAGALGPTN KTLSVSPSVE RPDFRNITFD ELVEAYSDQA RGLLDGGADI LLVETIFDSA NAKAALFAID LLFEKGYERR PIFISGTIVD RSGRTLSGQT GEAFVVSVSH AKPLCIGLNC ALGATEMRPF IEAIGKNTTA FIICYPNAGL PNTFGGYDET PEVTASHLKD FATDGLVNVV GGCCGTTPSH IRAISEAVKH RQPRVPPTAI YEDYLLLSGL EPFKIGSHTN FVNIGERCNV AGSRKFAKLI LAGHYEEALS IAKAQVEMGA QILDINMDEG MLEGPKAMAR FCNYIASEPD IARVPLCIDS SNFAVIEAGL KCCQGKCIVN SISLKEGEEE FLLRAATVKR YGAALVVMAF DEEGQATETN RKIQICTRAY TLLVNQVGFD PNDIIFDPNI LTIGTGMEEH NNYAVNFIQA TRLIKETLPR ARVSGGLSNL SFSFRGMEAV REAMHGVFLY HAIKDGMDMG IVNAGSLPVY DDIDKELLLL CENLIWNRDA DATEKLLAYA QNIVKGGKKV VQTDEWREVS VEERLEYALV KGIEKYVVED VEECQAQVSR YKRPIHIIEG PLMNGMKMVG DLFGAGKMFL PQVIKSARVM KKAVGHLIPF MEKERLELMA ASGSAEETSP YQGTILLATV KGDVHDIGKN IVGVVLGCNN FRVIDLGVMV PCDQILRAAV AHKADIIGLS GLITPSLDEM IYVAKEMERL GMRVPLLIGG ATTSKRHTAV KIAPRYSCPV IHVLDASRSV VVCSQLLDET MKEDYFEELK EEYEEVRLEH YDSLKDRRYL SLSEARQKAL HLDWSSMPAP VLPQFLGTRV FECYDLHRLL DFIDWKPFFD VWQLRGKYPN RGFPKIFNDK TVGPEARRLF DEAQLMLSDM IDSGTLKGRG LVGFWRAQSD GDDIHLYNHS ERVGVDTRPV ATFHGLRQQA EKDGASSEPY LCLSDFVAPV DSNVADYVGM FAVGIFGAEE LSQQFLAQRD DYSSIMVKAL ADRLAEAFAE ELHARVRKEL WAYSTEEALQ ASDLHRLRYQ GIRPAAGYPS QPDHTEKITM WNLAAVEEKT GIALTESLAM TPAASVSGLY FSNPQASYFA VGKITKEQVE DYARRKEMSV EEVERWLAPI LGYEQED // ID H2MLT6_ORYLA Unreviewed; 315 AA. AC H2MLT6; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 29-APR-2015, entry version 17. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSORLP00000019671}; GN Name=LOC101164391 {ECO:0000313|Ensembl:ENSORLP00000019671}; OS Oryzias latipes (Japanese rice fish) (Japanese killifish). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; OC Oryziinae; Oryzias. OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000019671, ECO:0000313|Proteomes:UP000001038}; RN [1] {ECO:0000313|Ensembl:ENSORLP00000019671, ECO:0000313|Proteomes:UP000001038} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000019671, RC ECO:0000313|Proteomes:UP000001038}; RX PubMed=17554307; DOI=10.1038/nature05846; RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., RA Yamada T., Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., RA Shimada A., Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., RA Asakawa S., Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., RA Sugano S., Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., RA Nomoto H., Nogata K., Morishita T., Endo T., Shin-I T., Takeda H., RA Morishita S., Kohara Y.; RT "The medaka draft genome and insights into vertebrate genome RT evolution."; RL Nature 447:714-719(2007). RN [2] {ECO:0000313|Ensembl:ENSORLP00000019671} RP IDENTIFICATION. RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000019671}; RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSORLP00000019671}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSORLT00000019672; ENSORLP00000019671; ENSORLG00000015709. DR GeneTree; ENSGT00510000049619; -. DR InParanoid; H2MLT6; -. DR OMA; PYVDVWL; -. DR OrthoDB; EOG7GQXW0; -. DR TreeFam; TF313927; -. DR Proteomes; UP000001038; Chromosome 4. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001038}; KW Reference proteome {ECO:0000313|Proteomes:UP000001038}. SQ SEQUENCE 315 AA; 34010 MW; 22161A8512DC0EBC CRC64; MGSSARLRLF INRNRPLILD GGLATELEAH GAQLQGDPLW SARLLHTNPK AIKDAHHRFL LSGADVITTA TYQASVQGFV THLGMSAERA KELLMSGVHL AREVVKNFGS GNTGPLVAGS IGSYGAYLHD TSEYTGTFAE KMTVDELKDW HRPQVEGLLA AGADLLAFET IPSIKEADAV VELLREFPDS SAWLSFSVKD ETRISDGSPF AEAVRVASRS AQLLAVGVNC CSPTVVEPLL DSASSQLSPD MSWVVYPNSG WEYDSQQGWQ ARGESSIWIP ELSRRWVKQG AALIGGCCCI SPAEIAELRK VLKGS // ID H2N3B5_PONAB Unreviewed; 1265 AA. AC H2N3B5; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPPYP00000000082}; GN Name=MTR {ECO:0000313|Ensembl:ENSPPYP00000000082}; OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pongo. OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000000082, ECO:0000313|Proteomes:UP000001595}; RN [1] {ECO:0000313|Ensembl:ENSPPYP00000000082, ECO:0000313|Proteomes:UP000001595} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Wilson R.K., Mardis E.; RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSPPYP00000000082} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 1}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSPPYP00000000082}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABGA01284255; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01284256; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01284257; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01284258; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01284259; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01284260; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01284261; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01284262; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01284263; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01284264; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01284265; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01284266; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01284267; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01284268; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01284269; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01284270; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01379464; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSPPYT00000000090; ENSPPYP00000000082; ENSPPYG00000000083. DR GeneTree; ENSGT00420000029824; -. DR InParanoid; H2N3B5; -. DR OrthoDB; EOG7TF786; -. DR TreeFam; TF312829; -. DR Proteomes; UP000001595; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:Ensembl. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001595}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001595}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 260 260 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 785 785 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1265 AA; 140252 MW; BB6C675F03ECB3B0 CRC64; MSPALQDLSQ PAGLKKTLRD EIDAILRKRI MVLDGGMGTM IQREKLNEEH FRGQEFKDHA RPLKGNNDIL SITQPDVIYQ IHKEYLLAGA DIIETNTFSS TSIAQADYGL EHLAYRMNMC SAGVARKAAE DVTLQTGIKR FVAGALGPTN KTLSVSPSVE RPDYRNITFD ELVEAYQEQA KGLLDGGVDI LLIETIFDTA NAKAALFALQ NLFEEKYAPR PIFISGTIVD KSGRTLSGQT GEGFVISVSH GEPLCIGLNC ALGAAEMRPF IEIIGKCTTA YVLCYPNAGL PNTFGDYDET PSMMAKHLKD FAMDGLVNIV GGCCGSTPDH IREIAEAVKN CKPRVPPATT FEGHMLLSGL EPFRIGPYTN FVNIGERCNV AGSRKFAKLI MAGNYEEALC VAKVQVEMGA QVLDVNMDDG MLDGPSAMTR FCNLIASEPD IAKVPLCIDS SNFAVIEAGL KCCQGKCIVN SISLKEGEDD FLEKAGKIKK YGAAVVVMAF DEEGQATETD TKIRVCTRAY HLLVKKLGFN PNDIIFDPNI LTIGTGMEEH NLYAINFIHA TKVIKETLPG ARISGGLSNL SFSFRGMEAI REAMHGVFLY HAIKSGMDMG IVNAGNLPVY DDIHKELLQL CEDLIWNKDP EATEKLLRYA QTQGTGGKKV IQTDEWRNGS VEERLEYALV KGIEKHIVED TEEARLNQEK YPRPLNIIEG PLMNGMKIVG DLFGAGKMFL PQVIKSARVM KKAVGHLIPF MEKEREETRV LNGTVEEEDP YQGTIVLATV KGDVHDIGKN IVGVVLGCNN FRVIDLGVMT PCDKILKAAL DHKADIIGLS GLITPSLDEM IFVAKEMERL AIKIPLLIGG ATTSKTHTAV KIAPRYSAPV IHVLDASKSV VVCSQLLDEN LKDEYFEEIM EEYEDIRQDH YESLKERRYL PLSQARKSGF QMDWLSEPYP VKPTFIGTQV FEDYDLQKLV DYIDWKPFFD VWQLRGKYPN RGFPKIFNDK TVGGEAKKVY DDAQNMLNTL ISQKKLQARG VVGFWPAQSI QDDIHLYAEG AVPQAAEPIA TFYGLRQQAE KDSASTEPYY CLSDFIAPLH SGIRDYLGLF AVACFGVEEL SKAYEDDGDD YSSIMVKALG DRLAEAFAEE LHERVRRELW AYCGSEQLDV ADLRRLRYKG IRPAPGYPSQ PDHTEKLTMW RLADIEQSTG IRLTESLAMA PASAVSGLYF SNLKSTYFAV GKISKDQVED YALRKNISVA EVEKWLGPIL GYDTD // ID H2PFY6_PONAB Unreviewed; 406 AA. AC H2PFY6; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 04-MAR-2015, entry version 19. DE SubName: Full=Betaine--homocysteine S-methyltransferase 1 {ECO:0000313|Ensembl:ENSPPYP00000017423}; GN Name=BHMT {ECO:0000313|Ensembl:ENSPPYP00000017423}; OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pongo. OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000017423, ECO:0000313|Proteomes:UP000001595}; RN [1] {ECO:0000313|Ensembl:ENSPPYP00000017423, ECO:0000313|Proteomes:UP000001595} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Wilson R.K., Mardis E.; RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSPPYP00000017423} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSPPYP00000017423}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABGA01301850; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01301851; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01301852; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01301853; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01301854; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSPPYT00000018129; ENSPPYP00000017423; ENSPPYG00000015586. DR GeneTree; ENSGT00390000003122; -. DR OrthoDB; EOG79GT7C; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000001595; Chromosome 5. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001595}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Reference proteome {ECO:0000313|Proteomes:UP000001595}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 217 217 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 406 AA; 45263 MW; 7505B1D8915B1CE8 CRC64; MPPVVGKKAK KGILERLNAG EIVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAVRQLH REFLRAGSNV MQTFTFYASE DKLENRGNYV LEKISGRKSM KAACDIARQV ADEGDALVAG GVSQTPSYLS CKSETEVKKV FLQQLEVFMK KNVDFLIAEY FEHVEEAVWA VETLIASGKP VAATMCIGPE GDLHGVPPGE CAVRLVKAGA SIIGVNCHFD PTISLKTVKL MKEGLEAARL KAHLMSQPLA YHTPDCNKQG FIDLPEFPFV YRPRVATRWD IQKYAREAYN MGIRYIGGCC GFEPYHIRAI AEELAPERGF LPPASEKHGS WGSALDMHTK PWVRARARKE YWENLRIASG RPYNPSMSKP DGWGVTKGTA ELMQQKEATT EQQLKELFEK QKFKLQ // ID H2PFY7_PONAB Unreviewed; 408 AA. AC H2PFY7; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Betaine--homocysteine S-methyltransferase 1 {ECO:0000313|Ensembl:ENSPPYP00000017424}; GN Name=BHMT {ECO:0000313|Ensembl:ENSPPYP00000017424}; OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pongo. OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000017424, ECO:0000313|Proteomes:UP000001595}; RN [1] {ECO:0000313|Ensembl:ENSPPYP00000017424, ECO:0000313|Proteomes:UP000001595} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Wilson R.K., Mardis E.; RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSPPYP00000017424} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSPPYP00000017424}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABGA01301850; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01301851; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01301852; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01301853; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01301854; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSPPYT00000018130; ENSPPYP00000017424; ENSPPYG00000015586. DR GeneTree; ENSGT00390000003122; -. DR OMA; WGVTKGT; -. DR TreeFam; TF329202; -. DR Proteomes; UP000001595; Chromosome 5. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006577; P:amino-acid betaine metabolic process; IEA:Ensembl. DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001595}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000001595}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 219 219 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 301 301 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 302 302 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 408 AA; 45441 MW; 7384069FA57D000E CRC64; MPPVVGKKAK KGILERLNAG EIVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAVRQLH REFLRAGSNV MQTFTFYASE DKLENRGNYV LEKISVRGRK SMKAACDIAR QVADEGDALV AGGVSQTPSY LSCKSETEVK KVFLQQLEVF MKKNVDFLIA EYFEHVEEAV WAVETLIASG KPVAATMCIG PEGDLHGVPP GECAVRLVKA GASIIGVNCH FDPTISLKTV KLMKEGLEAA RLKAHLMSQP LAYHTPDCNK QGFIDLPEFP FDLLPRVATR WDIQKYAREA YNMGIRYIGG CCGFEPYHIR AIAEELAPER GFLPPASEKH GSWGSALDMH TKPWVRARAR KEYWENLRIA SGRPYNPSMS KPDGWGVTKG TAELMQQKEA TTEQQLKELF EKQKFKLQ // ID H2QR52_PANTR Unreviewed; 363 AA. AC H2QR52; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Betaine--homocysteine S-methyltransferase 2 {ECO:0000313|EMBL:JAA08019.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPTRP00000029150}; GN Name=BHMT2 {ECO:0000313|EMBL:JAA08019.1, GN ECO:0000313|Ensembl:ENSPTRP00000029150}; OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000029150, ECO:0000313|Proteomes:UP000002277}; RN [1] {ECO:0000313|Ensembl:ENSPTRP00000029150, ECO:0000313|Proteomes:UP000002277} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16136131; DOI=10.1038/nature04072; RG Chimpanzee sequencing and analysis consortium; RT "Initial sequence of the chimpanzee genome and comparison with the RT human genome."; RL Nature 437:69-87(2005). RN [2] {ECO:0000313|Ensembl:ENSPTRP00000029150} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. RN [3] {ECO:0000313|EMBL:JAA08019.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Adipose stromal {ECO:0000313|EMBL:JAA08019.1}, RC Skeletal muscle {ECO:0000313|EMBL:JAA42420.1}, and RC Skin {ECO:0000313|EMBL:JAA22270.1}; RA Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.; RT "De novo assembly of the reference chimpanzee transcriptome from RT NextGen mRNA sequences."; RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AACZ03040915; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; GABC01003319; JAA08019.1; -; mRNA. DR EMBL; GABD01010830; JAA22270.1; -; mRNA. DR EMBL; GABD01010829; JAA22271.1; -; mRNA. DR EMBL; GABE01002319; JAA42420.1; -; mRNA. DR RefSeq; XP_527207.2; XM_527207.4. DR ProteinModelPortal; H2QR52; -. DR Ensembl; ENSPTRT00000031557; ENSPTRP00000029150; ENSPTRG00000017022. DR GeneID; 471829; -. DR KEGG; ptr:471829; -. DR CTD; 23743; -. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; H2QR52; -. DR OMA; PEGDMHD; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000002277; Chromosome 5. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0061627; F:S-methylmethionine-homocysteine S-methyltransferase activity; IEA:Ensembl. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl. DR GO; GO:0046500; P:S-adenosylmethionine metabolic process; IEA:Ensembl. DR GO; GO:0033477; P:S-methylmethionine metabolic process; IEA:Ensembl. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Complete proteome {ECO:0000313|Proteomes:UP000002277}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000313|EMBL:JAA08019.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002277}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000313|EMBL:JAA08019.1}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 208 208 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 363 AA; 40363 MW; 1576BB2C314087D4 CRC64; MAPAGRPGAK KGILERLESG EVVIGDGSFL ITLEKRGYVK AGLWTPEAVI EHPDAVRQLH MEFLRAGSNV MQTFTFSASE DNMESKWEDV NAAACDLARE VAGKGDALVA GGICQTSIYK YHKDEARIKK LFRQQLEVFA WKNVDFLIAE YFEHVEEAVW AVEVLKESDR PVAVTMCIGP EGDMHDITPG ECAVRLVKAG ASIVGVNCRF GPDTSLKTME LMKEGLERAG LKAHLMVQPL GFHTPDCGKE GFVDLPEYPF GLESRVATRW DIQKYAREAY NLGVRYIGGC CGFEPYHIRA IAEELAPERG FLPPASEKHG SWGSGLDMHT KPWIRARARR EYWENLLPAS GRPFCPSLSK PDF // ID H2QR53_PANTR Unreviewed; 406 AA. AC H2QR53; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPTRP00000029151}; GN Name=BHMT {ECO:0000313|Ensembl:ENSPTRP00000029151}; OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000029151, ECO:0000313|Proteomes:UP000002277}; RN [1] {ECO:0000313|Ensembl:ENSPTRP00000029151, ECO:0000313|Proteomes:UP000002277} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16136131; DOI=10.1038/nature04072; RG Chimpanzee sequencing and analysis consortium; RT "Initial sequence of the chimpanzee genome and comparison with the RT human genome."; RL Nature 437:69-87(2005). RN [2] {ECO:0000313|Ensembl:ENSPTRP00000029151} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSPTRP00000029151}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AACZ03040914; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AACZ03040915; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_517686.3; XM_517686.5. DR Ensembl; ENSPTRT00000031558; ENSPTRP00000029151; ENSPTRG00000017023. DR GeneID; 461786; -. DR KEGG; ptr:461786; -. DR CTD; 635; -. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; H2QR53; -. DR KO; K00544; -. DR OMA; WGVTKGT; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000002277; Chromosome 5. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006577; P:amino-acid betaine metabolic process; IEA:Ensembl. DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002277}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Reference proteome {ECO:0000313|Proteomes:UP000002277}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 217 217 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 406 AA; 44979 MW; 47C785B77FF82D50 CRC64; MPPVGGKKAK KGILERLNAG EIVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAVRQLH REFLRAGSNV MQTFTFYASE DKLENRGNYV LEKISGQKVN EAACDIARQV ADEGDALVAG GVSQTPSYLS CKSEIEVKKV FLPQLEVFMK KNVDFLIAEY FEHVEEAVWA VETLIASGKP VAATMCIGPE GDLHGVPPGE CAVRLVKAGA SIIGVNCHFD PTISLKTVKL MKEGLEAARL KAHLMSQPLA YHTPDCNKQG FIDLPEFPFG LEPRVATRWD IQKYAREAYN LGVRYIGGCC GFEPYHIRAI AEELAPERGF LPPASEKHGS WGSGLDMHTK PWVRARARKE YWENLRIASG RPYNPSMSKP DGWGVTKGTA ELMQQKEATT EQQLKELFEK QKFKSQ // ID H2R7Z7_PANTR Unreviewed; 1265 AA. AC H2R7Z7; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|EMBL:JAA09123.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPTRP00000051007}; GN Name=MTR {ECO:0000313|EMBL:JAA09123.1, GN ECO:0000313|Ensembl:ENSPTRP00000051007}; OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000051007, ECO:0000313|Proteomes:UP000002277}; RN [1] {ECO:0000313|Ensembl:ENSPTRP00000051007, ECO:0000313|Proteomes:UP000002277} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16136131; DOI=10.1038/nature04072; RG Chimpanzee sequencing and analysis consortium; RT "Initial sequence of the chimpanzee genome and comparison with the RT human genome."; RL Nature 437:69-87(2005). RN [2] {ECO:0000313|Ensembl:ENSPTRP00000051007} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. RN [3] {ECO:0000313|EMBL:JAA09123.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Adipose stromal {ECO:0000313|EMBL:JAA09123.1}, RC Skeletal muscle {ECO:0000313|EMBL:JAA44620.1}, RC Skin {ECO:0000313|EMBL:JAA32458.1}, and RC Smooth vascular {ECO:0000313|EMBL:JAA20213.1}; RA Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.; RT "De novo assembly of the reference chimpanzee transcriptome from RT NextGen mRNA sequences."; RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AACZ03003123; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AACZ03003124; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AACZ03003125; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; GABC01002215; JAA09123.1; -; mRNA. DR EMBL; GABF01001932; JAA20213.1; -; mRNA. DR EMBL; GABD01000642; JAA32458.1; -; mRNA. DR EMBL; GABE01000119; JAA44620.1; -; mRNA. DR EMBL; GABE01000118; JAA44621.1; -; mRNA. DR EMBL; GABE01000117; JAA44622.1; -; mRNA. DR EMBL; GABE01000116; JAA44623.1; -; mRNA. DR RefSeq; XP_514294.2; XM_514294.5. DR Ensembl; ENSPTRT00000058064; ENSPTRP00000051007; ENSPTRG00000002145. DR GeneID; 457844; -. DR KEGG; ptr:457844; -. DR CTD; 4548; -. DR GeneTree; ENSGT00420000029824; -. DR InParanoid; H2R7Z7; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG7TF786; -. DR TreeFam; TF312829; -. DR Proteomes; UP000002277; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:Ensembl. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 2: Evidence at transcript level; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002277}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:JAA09123.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002277}; KW Transferase {ECO:0000313|EMBL:JAA09123.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 260 260 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 785 785 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1265 AA; 140501 MW; 19613268F2BC84C1 CRC64; MSPALQDLSQ PEGLKKTLRD EIDAILQKRI MVLDGGMGTM IQREKLNEEH FRGQEFKDHA RPLKGNNDIL SITQPDVIYQ IHKEYLLAGA DIIETNTFSS TSIAQADYGL EHLAYRMNMC SAGVARKAAE EVTLQTGIKR FVAGALGPTN KTLSVSPSVE RPDYRNITFD ELVEAYQEQA KGLLDGGVDI LLIETIFDTA NAKAALFALQ NLFEEKYAPR PIFISGTIVD KSGRTLSGQT GEGFVISVSH GEPLCIGLNC ALGAAEMRPF IEIIGKCTTA YVLCYPNAGL PNTFGDYDET PSMMAKHLKD FAMDGLVNIV GGCCGSTPDH IREIAEAVKN CKPRVPPATA FEGHMLLSGL EPFRIGPYTN FVNIGERCNV AGSRKFAKLI MAGNYEEALC VAKVQVEMGA QVLDVNMDDG MLDGPSAMTR FCNLIASEPD IAKVPLCIDS SNFAVIEAGL KCCQGKCIVN SISLKEGEDD FLEKARKIKK YGAAMVVMAF DEEGQATETD TKIRVCTRAY HLLVKKLGFN PNDIIFDPNI LTIGTGMEEH NLYAINFIHA TKVIKETLPG ARISGGLSNL SFSFRGMEAI REAMHGVFLY HAIKSGMDMG IVNAGNLPVY DDIHKELLQL CEDLIWNKDP EATEKLLRYA QTQGTGGKKV IQTDEWRSGP VEERLEYALV KGIEKHIIED TEEARLNQKK YPRPLNIIEG PLMNGMKIVG DLFGAGKMFL PQVIKSARVM KKAVGHLIPF MEKEREETRV LNGTVEEEDP YQGTIVLATV KGDVHDIGKN IVGVVLGCNN FRVIDLGVMT PCDKILKAAL DHKADIIGLS GLITPSLDEM IFVAKEMERL AIRIPLLIGG ATTSKTHTAV KIAPRYSAPV IHVLDASKSV VVCSQLLDEN LKDEYFEEIM EEYEDIRQDH YESLKERRYL PLSQARKSGF QMDWLSEPHP VKPTFIGTQV FEDYDLQKLV DYIDWKPFFD VWQLRGKYPN RGFPKIFNDK TVGGEARKVY DDAHNMLNTL ISQKKLRARG VVGFWPAQSI QDDIHLYAEA AVPQAAEPIA TFYGLRQQAE KDSASTEPYY CLSDFIAPLH SGIRDYLGLF AVACFGVEEL SKAYEDDGDD YSSIMVKALG DRLAEAFAEE LHERVRRELW AYCGSEQLDV ADLRRLRYKG IRPAPGYPSQ PDHTEKLTMW RLADIEQSTG IRLTESLAMA PASAVSGLYF SNLKSKYFAV GKISKDQVED YALRKNISVA EVEKWLGPIL GYDTD // ID H2RFU1_PANTR Unreviewed; 253 AA. AC H2RFU1; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPTRP00000060386}; GN Name=BHMT {ECO:0000313|Ensembl:ENSPTRP00000060386}; OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000060386, ECO:0000313|Proteomes:UP000002277}; RN [1] {ECO:0000313|Ensembl:ENSPTRP00000060386, ECO:0000313|Proteomes:UP000002277} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16136131; DOI=10.1038/nature04072; RG Chimpanzee sequencing and analysis consortium; RT "Initial sequence of the chimpanzee genome and comparison with the RT human genome."; RL Nature 437:69-87(2005). RN [2] {ECO:0000313|Ensembl:ENSPTRP00000060386} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSPTRP00000060386}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AACZ03040914; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AACZ03040915; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; H2RFU1; -. DR SMR; H2RFU1; 8-250. DR Ensembl; ENSPTRT00000074306; ENSPTRP00000060386; ENSPTRG00000017023. DR GeneTree; ENSGT00390000003122; -. DR Proteomes; UP000002277; Chromosome 5. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002277}; KW Reference proteome {ECO:0000313|Proteomes:UP000002277}. SQ SEQUENCE 253 AA; 28206 MW; BD2C7BC33488D7C9 CRC64; MPPVGGKKAK KGILERLNAG EIVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAGASII GVNCHFDPTI SLKTVKLMKE GLEAARLKAH LMSQPLAYHT PDCNKQGFID LPEFPFGLEP RVATRWDIQK YAREAYNLGV RYIGGCCGFE PYHIRAIAEE LAPERGFLPP ASEKHGSWGS GLDMHTKPWV RARARKEYWE NLRIASGRPY NPSMSKPDGW GVTKGTAELM QQKEATTEQQ LKELFEKQKF KSQ // ID H2RIB3_PANTR Unreviewed; 203 AA. AC H2RIB3; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPTRP00000061271}; GN Name=BHMT {ECO:0000313|Ensembl:ENSPTRP00000061271}; OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000061271, ECO:0000313|Proteomes:UP000002277}; RN [1] {ECO:0000313|Ensembl:ENSPTRP00000061271, ECO:0000313|Proteomes:UP000002277} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16136131; DOI=10.1038/nature04072; RG Chimpanzee sequencing and analysis consortium; RT "Initial sequence of the chimpanzee genome and comparison with the RT human genome."; RL Nature 437:69-87(2005). RN [2] {ECO:0000313|Ensembl:ENSPTRP00000061271} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSPTRP00000061271}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AACZ03040914; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AACZ03040915; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; H2RIB3; -. DR SMR; H2RIB3; 10-122. DR Ensembl; ENSPTRT00000075411; ENSPTRP00000061271; ENSPTRG00000017023. DR GeneTree; ENSGT00390000003122; -. DR Proteomes; UP000002277; Chromosome 5. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002277}; KW Reference proteome {ECO:0000313|Proteomes:UP000002277}. SQ SEQUENCE 203 AA; 21738 MW; 19D78198C4D31C70 CRC64; MPPVGGKKAK KGILERLNAG EIVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAGASII GVNCHFDPTI SLKTVKLMKE GLEAARLKAH LMSQPLAYHT PDCNKQGFID LPEFPFGLEP ELPPDGIFKN TPERPTTWGS GTLAGAVDLS PTTSGQLQRS WPQKGAFCHQ LQKNMAAGEV VWTCTPNPGL EQGPGRNTGR IFG // ID H2SC19_TAKRU Unreviewed; 399 AA. AC H2SC19; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSTRUP00000009948}; GN Name=LOC101062063 {ECO:0000313|Ensembl:ENSTRUP00000009948}; OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; OC Takifugu. OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000009948, ECO:0000313|Proteomes:UP000005226}; RN [1] {ECO:0000313|Ensembl:ENSTRUP00000009948} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSTRUP00000009948}; RX PubMed=17554307; DOI=10.1038/nature05846; RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., RA Yamada T., Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., RA Shimada A., Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., RA Asakawa S., Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., RA Sugano S., Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., RA Nomoto H., Nogata K., Morishita T., Endo T., Shin-I T., Takeda H., RA Morishita S., Kohara Y.; RT "The medaka draft genome and insights into vertebrate genome RT evolution."; RL Nature 447:714-719(2007). RN [2] {ECO:0000313|Ensembl:ENSTRUP00000009948} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSTRUP00000009948}. 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_003978166.1; XM_003978117.2. DR PRIDE; H2SC19; -. DR Ensembl; ENSTRUT00000010004; ENSTRUP00000009948; ENSTRUG00000004203. DR GeneID; 101062063; -. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; H2SC19; -. DR OMA; KAHYMSQ; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000005226; Unplaced. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005226}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Reference proteome {ECO:0000313|Proteomes:UP000005226}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 212 212 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 399 AA; 44239 MW; ADBC3C4D92ADCC9D CRC64; MAPAANKKGI LERLDAGEIV IGDGGFVFAL EKRGYVKAGP WTPEATVEYP EAVRQLHREF LRAGSDVMQT FTFYASDDKL ENRGHAQRFT GTQINEAACD LAREVANEGN ALVAGGVSQT PAYLSCKSED EVKAIFKKQL DVFVKKDVDF LIAEYFEHVE EAEWAVQVLK ATGKPVAATL CIGPEGDLNG ISPGECGVRL VKAGAQIVGI NCHFDPETCV KTVKMMKEGV EKAGLKAHYM SQPLAYHTPD CNCQGFIDLP EFPFSLEPRI LTRWDMQKYA REAYNAGIRY IGGCCGFEAY HIRALSEELQ AERGFYPAGS EKHGNWGSGL EIHTKPWVRA RARRDYWEKL KPASGRPFCP SLSEPDSWGI TKGHADLMQK KEATSQEEMK ALFQKADKC // ID H2SPA9_TAKRU Unreviewed; 311 AA. AC H2SPA9; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 07-JAN-2015, entry version 16. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSTRUP00000014246}; DE Flags: Fragment; GN Name=LOC101062046 {ECO:0000313|Ensembl:ENSTRUP00000014246}; OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; OC Takifugu. OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000014246, ECO:0000313|Proteomes:UP000005226}; RN [1] {ECO:0000313|Ensembl:ENSTRUP00000014246} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSTRUP00000014246}; RX PubMed=17554307; DOI=10.1038/nature05846; RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., RA Yamada T., Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., RA Shimada A., Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., RA Asakawa S., Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., RA Sugano S., Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., RA Nomoto H., Nogata K., Morishita T., Endo T., Shin-I T., Takeda H., RA Morishita S., Kohara Y.; RT "The medaka draft genome and insights into vertebrate genome RT evolution."; RL Nature 447:714-719(2007). RN [2] {ECO:0000313|Ensembl:ENSTRUP00000014246} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSTRUP00000014246}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSTRUT00000014311; ENSTRUP00000014246; ENSTRUG00000005847. DR GeneTree; ENSGT00510000049619; -. DR InParanoid; H2SPA9; -. DR OMA; SEWCKDG; -. DR OrthoDB; EOG7GQXW0; -. DR TreeFam; TF313927; -. DR Proteomes; UP000005226; Unplaced. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005226}; KW Reference proteome {ECO:0000313|Proteomes:UP000005226}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSTRUP00000014246}. SQ SEQUENCE 311 AA; 33844 MW; A41CCBF5448FDE36 CRC64; YDDGPLILDG GLATELETQG FHLQGDPLWS ARLLHTNPQA IRDAHGRFLL SGADVISTAT YQASVEGFIR HLHVSSECAK DLIMSAVQLA KEATDETKKS QRCPLVAGSV GPYGAFLHNG SEYTGDYAEQ MSVQELKAWH RPQIECLAAA GADLLAFETI PSIKEAEALV ELLKEFPNTK AWLALSCKDV RSLSDGSPFA DAVQMANRSQ QLIAVGVNCC PPQLVEPLLE SARCLLRPEI SWVVYPNSGE DWDSEQGWHG AETETESSPL IEMSRTWMKQ GAALIGGCCR ISPAHIAKLR HHLKGTCEPP S // ID H2T6W4_TAKRU Unreviewed; 1269 AA. AC H2T6W4; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 01-APR-2015, entry version 23. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSTRUP00000020403}; GN Name=MTR {ECO:0000313|Ensembl:ENSTRUP00000020403}; OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; OC Takifugu. OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000020403, ECO:0000313|Proteomes:UP000005226}; RN [1] {ECO:0000313|Ensembl:ENSTRUP00000020403} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSTRUP00000020403}; RX PubMed=17554307; DOI=10.1038/nature05846; RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., RA Yamada T., Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., RA Shimada A., Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., RA Asakawa S., Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., RA Sugano S., Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., RA Nomoto H., Nogata K., Morishita T., Endo T., Shin-I T., Takeda H., RA Morishita S., Kohara Y.; RT "The medaka draft genome and insights into vertebrate genome RT evolution."; RL Nature 447:714-719(2007). RN [2] {ECO:0000313|Ensembl:ENSTRUP00000020403} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 1}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSTRUP00000020403}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSTRUT00000020488; ENSTRUP00000020403; ENSTRUG00000008159. DR GeneTree; ENSGT00420000029824; -. DR InParanoid; H2T6W4; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG7TF786; -. DR TreeFam; TF312829; -. DR Proteomes; UP000005226; Unplaced. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000005226}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005226}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 264 264 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 327 327 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 328 328 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 787 787 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1269 AA; 140811 MW; 89D76E4F0830FCC3 CRC64; MISTNTSLPN SAGAANPTDC PLETELREIL QQRIVILDGG MGTMIQQQKL EECDFRGDVF KDHPHPLMGN NDLLSLTRPD IVYKIHKDYL LAGADIIETN TFSGTSVAQA DYGLEHMAYR LNRASAELAR KAADDVTSQT GVKRYVAGAL GPTNKTLSVS PSVERPHFRN ITFDALVEAY TEQVRGLMDG GVDILLVETI FDTANAKAAL FAIDLLFEKS YKRKPIFISG TVVDRSGRTL SGQTVEAFVV SVSHANPLCI GLNCALGATE MRPFIEAIGK CTTAFVICYP NAGLPNTFGE YDESPEVTAS NLKEFSIDGL VNVVGGCCGT TPEHIRALCE AVRMCQPRVP PSDVYQDYLM LSGLEPFKIG PYTNFVNIGE RCNVAGSRKF AKLITSGLCE EALSIAKAQV EMGAQILDIN MDEGMLDGVT AMAQFCNLIA SDPDIARVPL CIDSSNFSVI EAGLKCCQGK CIVNSISLKE GETDFLNKAA CVKRYGAAVV VMAFDEQGQA TDTDRKVEIC TRAYQLLLTK VGFKPNDIIF DPNILTIGTG IDEHSEYAIN FIKATELIKG TLPGTRVSGG LSNLSFSFRG MEVIREAMHG VFLYHAIKVG MDMGIVNAGN LPVYDDIDKE LMLLCENLIW SRDSDATENL LAYAQNIVKR GKKIDHTEEW REGSVEERLE YALVKGVDKY VIDDVKECQA QVDHYTRPIH IIEGPLMNGM KIVGDLFGAG KMFLPQVIKS ARVMKKAVGY LIPFMEKERQ EMMSESSQDL DPYMGTIILA TVKGDVHDIG KNIVGVVLSC NNFRVIDLGV MVPCDKILKE AIVHNADIIG LSGLITPSLE EMIYVAKEME RLRMTIPLLI GGATTSKTHT AVKIAPRYAA PVIHVLDASR SVVVIKCSQL LDEMGKEDYF EELKQDYEEV RQEHYDSLKA RHYLPLSKAR EKALHIDWLS VARPIPPQFL GTRAFECYDL NRLLDFIDWK PFFDVWQLRG KYPNRSYPRI FNDKTIGMEA KQVFEDVQRL LKIIISSGSL KAHGLVGFWH AQSSGDDIDV YKEDVSVFRD TKPIATFHCL RQQLEKDSSV SEPYLCLSDF IAPVDSGVPD YIGLFAVGIF GAEELSQQFQ TQGDDYRNIM VKALADRLAE AFAEELHARV RKEFWGYNTT ETLQASDLHH VRYQGIRPAP GYPSQPHTEK TTMWSLAEIQ EKTGIGLTES FAMTPAASVS GLYFSNPQST YFAVGKITKE QVDDYSKRKN MKVEEAERWL APILGYDTE // ID H2V0K6_TAKRU Unreviewed; 400 AA. AC H2V0K6; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 04-MAR-2015, entry version 19. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSTRUP00000042736}; DE Flags: Fragment; GN Name=LOC101061373 {ECO:0000313|Ensembl:ENSTRUP00000042736}; OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; OC Takifugu. OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000042736, ECO:0000313|Proteomes:UP000005226}; RN [1] {ECO:0000313|Ensembl:ENSTRUP00000042736} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSTRUP00000042736}; RX PubMed=17554307; DOI=10.1038/nature05846; RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., RA Yamada T., Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., RA Shimada A., Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., RA Asakawa S., Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., RA Sugano S., Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., RA Nomoto H., Nogata K., Morishita T., Endo T., Shin-I T., Takeda H., RA Morishita S., Kohara Y.; RT "The medaka draft genome and insights into vertebrate genome RT evolution."; RL Nature 447:714-719(2007). RN [2] {ECO:0000313|Ensembl:ENSTRUP00000042736} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSTRUP00000042736}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSTRUT00000042880; ENSTRUP00000042736; ENSTRUG00000016702. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; H2V0K6; -. DR OMA; WGVTKGT; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR Proteomes; UP000005226; Unplaced. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005226}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000005226}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 214 214 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 296 296 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 297 297 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSTRUP00000042736}. SQ SEQUENCE 400 AA; 44157 MW; E0260447E12EC4B7 CRC64; IPPLSKRRAG GILERLNAGQ VVIGDGGFVF ALEKRGYVKA GPWTPEATKE HPEAVRQLHR EFLRAGANVM QTFTFYASDD KLENRGNKLT YTGAQINEAA CDLAREVANE GDALVAGGVS QTPSYLSCKS EKEVKDIFKR QLDVFVKKNV DFLIAEYFEH VEEAVWAVEV LKATGKPVAA SLCIGPKGDM HGVSPAECAV RLVKAGAQIV GVNCHFDPMT CVEAVKMMKE GVEKAGLKAH YMVQPLAFHT PDCNCQGFID LPEFPFGLEP RILTRWDMHK YAREAYNAGI RFIGGCCGFE PYHIRALAEE LSPERGCLPV GSEKHGSWGA GLEMHTKPWV RARARRDYWE NLKPASGRPL CASLSAPDCW GVTKGDTALM QQKEATTKDQ LKQLFDRKSN // ID H2V0K7_TAKRU Unreviewed; 398 AA. AC H2V0K7; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 04-MAR-2015, entry version 18. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSTRUP00000042737}; GN Name=LOC101061373 {ECO:0000313|Ensembl:ENSTRUP00000042737}; OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; OC Takifugu. OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000042737, ECO:0000313|Proteomes:UP000005226}; RN [1] {ECO:0000313|Ensembl:ENSTRUP00000042737} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSTRUP00000042737}; RX PubMed=17554307; DOI=10.1038/nature05846; RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., RA Yamada T., Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., RA Shimada A., Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., RA Asakawa S., Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., RA Sugano S., Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., RA Nomoto H., Nogata K., Morishita T., Endo T., Shin-I T., Takeda H., RA Morishita S., Kohara Y.; RT "The medaka draft genome and insights into vertebrate genome RT evolution."; RL Nature 447:714-719(2007). RN [2] {ECO:0000313|Ensembl:ENSTRUP00000042737} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSTRUP00000042737}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSTRUT00000042881; ENSTRUP00000042737; ENSTRUG00000016702. DR GeneTree; ENSGT00390000003122; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000005226; Unplaced. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005226}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Reference proteome {ECO:0000313|Proteomes:UP000005226}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 210 210 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 292 292 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 398 AA; 43958 MW; 073955BA56BC402D CRC64; MAPGKKGILE RLNAGQVVIG DGGFVFALEK RGYVKAGPWT PEATKEHPEA VRQLHREFLR AGANVMQTFT FYASDDKLEN RGNKLTYTGA QINEAACDLA REVANEGDAL VAGGVSQTPS YLSCKSEKEV KDIFKRQLDV FVKKNVDFLI AEYFEHVEEA VWAVEVLKAT GKPVAASLCI GPKGDMHGVS PAECAVRLVK AGAQIVGVNC HFDPMTCVEA VKMMKEGVEK AGLKAHYMVQ PLAFHTPDCN CQGFIDLPEF PFGLEPRILT RWDMHKYARE AYNAGIRFIG GCCGFEPYHI RALAEELSPE RGCLPVGSEK HGSWGAGLEM HTKPWVRARA RRDYWENLKP ASGRPLCASL SAPDCWGVTK GDTALMQQKE ATTKDQLKQL FDRKSNKH // ID H2V0K8_TAKRU Unreviewed; 400 AA. AC H2V0K8; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 04-MAR-2015, entry version 18. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSTRUP00000042738}; GN Name=LOC101061373 {ECO:0000313|Ensembl:ENSTRUP00000042738}; OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; OC Takifugu. OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000042738, ECO:0000313|Proteomes:UP000005226}; RN [1] {ECO:0000313|Ensembl:ENSTRUP00000042738} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSTRUP00000042738}; RX PubMed=17554307; DOI=10.1038/nature05846; RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., RA Yamada T., Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., RA Shimada A., Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., RA Asakawa S., Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., RA Sugano S., Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., RA Nomoto H., Nogata K., Morishita T., Endo T., Shin-I T., Takeda H., RA Morishita S., Kohara Y.; RT "The medaka draft genome and insights into vertebrate genome RT evolution."; RL Nature 447:714-719(2007). RN [2] {ECO:0000313|Ensembl:ENSTRUP00000042738} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSTRUP00000042738}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSTRUT00000042882; ENSTRUP00000042738; ENSTRUG00000016702. DR GeneTree; ENSGT00390000003122; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000005226; Unplaced. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005226}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Reference proteome {ECO:0000313|Proteomes:UP000005226}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 210 210 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 292 292 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 400 AA; 44220 MW; 1AEFA5FCB2CA56BC CRC64; MAPGKKGILE RLNAGQVVIG DGGFVFALEK RGYVKAGPWT PEATKEHPEA VRQLHREFLR AGANVMQTFT FYASDDKLEN RGNKLTYTGA QINEAACDLA REVANEGDAL VAGGVSQTPS YLSCKSEKEV KDIFKRQLDV FVKKNVDFLI AEYFEHVEEA VWAVEVLKAT GKPVAASLCI GPKGDMHGVS PAECAVRLVK AGAQIVGVNC HFDPMTCVEA VKMMKEGVEK AGLKAHYMVQ PLAFHTPDCN CQGFIDLPEF PFGLEPRILT RWDMHKYARE AYNAGIRFIG GCCGFEPYHI RALAEELSPE RGCLPVGSEK HGSWGAGLEM HTKPWVRARA RRDYWENLKP ASGRPLCASL SAPDCWGVTK GDTALMQQKE ATTKDQLKQL FDRKSKQKKQ // ID H2V0K9_TAKRU Unreviewed; 364 AA. AC H2V0K9; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 04-MAR-2015, entry version 18. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSTRUP00000042739}; GN Name=LOC101061373 {ECO:0000313|Ensembl:ENSTRUP00000042739}; OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; OC Takifugu. OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000042739, ECO:0000313|Proteomes:UP000005226}; RN [1] {ECO:0000313|Ensembl:ENSTRUP00000042739} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSTRUP00000042739}; RX PubMed=17554307; DOI=10.1038/nature05846; RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., RA Yamada T., Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., RA Shimada A., Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., RA Asakawa S., Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., RA Sugano S., Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., RA Nomoto H., Nogata K., Morishita T., Endo T., Shin-I T., Takeda H., RA Morishita S., Kohara Y.; RT "The medaka draft genome and insights into vertebrate genome RT evolution."; RL Nature 447:714-719(2007). RN [2] {ECO:0000313|Ensembl:ENSTRUP00000042739} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSTRUP00000042739}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSTRUT00000042883; ENSTRUP00000042739; ENSTRUG00000016702. DR GeneTree; ENSGT00390000003122; -. DR UniPathway; UPA00051; UER00083. DR Proteomes; UP000005226; Unplaced. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005226}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Reference proteome {ECO:0000313|Proteomes:UP000005226}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 209 209 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 292 292 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 364 AA; 40059 MW; 2E38D9BF687B547E CRC64; MAPGKKHIGK EQGILERLNA GQVVIGDGGF VFALEKRGYV KAGPWTPEAT KEHPEAVRQL HREFLRAGAN VMQTFTFYAS DDKLENRGAQ INEAACDLAR EVANEGDALV AGGVSQTPSY LSCKSEKEVK DIFKRQLDVF VKKNVDFLIA EYFEHVEEAV WAVEVLKATG KPVAASLCIG PKGDMHGVSP AECAVRLVKA GAQIVGVNCH FDPMTCVEAV KMMKEGVEKA GLKAHYMVQP LAFHTPDCNC QGFIDLPEFP FGLEPRILTR WDMHKYAREA YNAGIRFIGG CCGFEPYHIR ALAEELSPER GCLPVGSEKH GSWGAGLEMH TKPWVRARAR RDYWENLKPA SGRPLCASLS APDC // ID H2VHY0_CAEJA Unreviewed; 272 AA. AC H2VHY0; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 2. DT 27-MAY-2015, entry version 18. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:CJA00806}; GN Name=WBGene00120010 {ECO:0000313|EnsemblMetazoa:CJA00806}; OS Caenorhabditis japonica. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=281687 {ECO:0000313|EnsemblMetazoa:CJA00806}; RN [1] {ECO:0000313|EnsemblMetazoa:CJA00806} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DF5081 {ECO:0000313|EnsemblMetazoa:CJA00806}; RG Caenorhabditis japonica Sequencing Consortium; RA Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblMetazoa:CJA00806} RP IDENTIFICATION. RC STRAIN=DF5081 {ECO:0000313|EnsemblMetazoa:CJA00806}; RG EnsemblMetazoa; 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 EnsemblMetazoa; CJA00806; CJA00806; CJA00806. DR InParanoid; H2VHY0; -. DR Proteomes; UP000005237; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005237}; KW Reference proteome {ECO:0000313|Proteomes:UP000005237}. SQ SEQUENCE 272 AA; 30039 MW; 9275016E0FB6CBE6 CRC64; MADVLREFAR DGLVNIIGGC CGTTPDHIRA LYNAVKGVTP RVPPSDPHVG KMLLSGLEPS LVGPETNYVN IGERCNVAGS RRFCNLIKNE NYDAAIDVAR VQVDNGAQIL DVNMDEGLLD GPYAMAKFLR LISSEPDVAK IPVCIDSSDF NVIIAGLEST QGKCVVNSIS LKEGEEKFKD RARIIKRYGA AVVVMAFDEE GQAAETERKF EICERSYRIL TEEVGFNPND IIFDANILTI ATGMEEHANY ELFIEMSKNV KNWLNMSKIL MD // ID H2W962_CAEJA Unreviewed; 329 AA. AC H2W962; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 2. DT 27-MAY-2015, entry version 15. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:CJA12057}; GN Name=WBGene00131261 {ECO:0000313|EnsemblMetazoa:CJA12057}; OS Caenorhabditis japonica. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=281687 {ECO:0000313|EnsemblMetazoa:CJA12057}; RN [1] {ECO:0000313|EnsemblMetazoa:CJA12057} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DF5081 {ECO:0000313|EnsemblMetazoa:CJA12057}; RG Caenorhabditis japonica Sequencing Consortium; RA Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblMetazoa:CJA12057} RP IDENTIFICATION. RC STRAIN=DF5081 {ECO:0000313|EnsemblMetazoa:CJA12057}; RG EnsemblMetazoa; 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 EnsemblMetazoa; CJA12057; CJA12057; CJA12057. DR InParanoid; H2W962; -. DR Proteomes; UP000005237; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005237}; KW Reference proteome {ECO:0000313|Proteomes:UP000005237}. SQ SEQUENCE 329 AA; 37174 MW; 57B226BF9906B2A3 CRC64; MPSKIRLLDG SMSAQLSAFG YNTEDHKPHW TFPANEDLEL MKQVYQSNLS TGADVVTTNT YHFGSVLDTS IAENVQKRVE FERFFEKTCN LMVKLVKEAG SNTEVWGSVG TLATMYHDLS EYNGKYIDLP GSFGYLKRRR LRFHVASRLK TQYMYISSQD TALNYFKTVI AIFQEKTVIR KLVFETIPTE REAMAAVSAL QQFPEMKAVI SFTCDKNGCL RHGEKITNVA KELENNKQIV GIGVNCTDPS NITAALLEIR HCNFQEIFVY PNVGDATFLD NEKDEEDVFK FDLIASWVDS GATVIGGCCG VQNKQLLSLR KIIDKINKH // ID H2WVI9_CAEJA Unreviewed; 153 AA. AC H2WVI9; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 2. DT 27-MAY-2015, entry version 16. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:CJA20903}; GN Name=WBGene00176475 {ECO:0000313|EnsemblMetazoa:CJA20903}; OS Caenorhabditis japonica. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=281687 {ECO:0000313|EnsemblMetazoa:CJA20903}; RN [1] {ECO:0000313|EnsemblMetazoa:CJA20903} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DF5081 {ECO:0000313|EnsemblMetazoa:CJA20903}; RG Caenorhabditis japonica Sequencing Consortium; RA Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblMetazoa:CJA20903} RP IDENTIFICATION. RC STRAIN=DF5081 {ECO:0000313|EnsemblMetazoa:CJA20903}; RG EnsemblMetazoa; 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 EnsemblMetazoa; CJA20903; CJA20903; CJA20903. DR InParanoid; H2WVI9; -. DR Proteomes; UP000005237; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005237}; KW Reference proteome {ECO:0000313|Proteomes:UP000005237}. SQ SEQUENCE 153 AA; 16773 MW; 0C0C7D6A8A6E1BAD CRC64; MTRSSLFEEL AEIAKERIMI IDGAMAFQEL VKAYGDQARS LLQGGVDILL VETVFDSANA KAALFAIRTL FEDDGLPEVP VFLSGTIVDM SGRTLSGQTG EAFLVSTRQG NPMCVGLNCA LGAKDMRQFV ENMSKWSDAL ILCYPNAGWW KRN // ID H2Y1G0_CIOIN Unreviewed; 1269 AA. AC H2Y1G0; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCINP00000035744}; DE Flags: Fragment; GN Name=LOC100179361 {ECO:0000313|Ensembl:ENSCINP00000035744}; OS Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis). OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Enterogona; OC Phlebobranchia; Cionidae; Ciona. OX NCBI_TaxID=7719 {ECO:0000313|Ensembl:ENSCINP00000035744, ECO:0000313|Proteomes:UP000008144}; RN [1] {ECO:0000313|Ensembl:ENSCINP00000035744} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12481130; DOI=10.1126/science.1080049; RA Dehal P., Satou Y., Campbell R.K., Chapman J., Degnan B., RA De Tomaso A., Davidson B., Di Gregorio A., Gelpke M., Goodstein D.M., RA Harafuji N., Hastings K.E., Ho I., Hotta K., Huang W., Kawashima T., RA Lemaire P., Martinez D., Meinertzhagen I.A., Necula S., Nonaka M., RA Putnam N., Rash S., Saiga H., Satake M., Terry A., Yamada L., RA Wang H.G., Awazu S., Azumi K., Boore J., Branno M., Chin-Bow S., RA DeSantis R., Doyle S., Francino P., Keys D.N., Haga S., Hayashi H., RA Hino K., Imai K.S., Inaba K., Kano S., Kobayashi K., Kobayashi M., RA Lee B.I., Makabe K.W., Manohar C., Matassi G., Medina M., RA Mochizuki Y., Mount S., Morishita T., Miura S., Nakayama A., RA Nishizaka S., Nomoto H., Ohta F., Oishi K., Rigoutsos I., Sano M., RA Sasaki A., Sasakura Y., Shoguchi E., Shin-i T., Spagnuolo A., RA Stainier D., Suzuki M.M., Tassy O., Takatori N., Tokuoka M., Yagi K., RA Yoshizaki F., Wada S., Zhang C., Hyatt P.D., Larimer F., Detter C., RA Doggett N., Glavina T., Hawkins T., Richardson P., Lucas S., RA Kohara Y., Levine M., Satoh N., Rokhsar D.S.; RT "The draft genome of Ciona intestinalis: insights into chordate and RT vertebrate origins."; RL Science 298:2157-2167(2002). RN [2] {ECO:0000313|Ensembl:ENSCINP00000035744} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 1}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSCINP00000035744}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EAAA01002024; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSCINT00000034848; ENSCINP00000035744; ENSCING00000023410. DR GeneTree; ENSGT00420000029824; -. DR InParanoid; H2Y1G0; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG7TF786; -. DR TreeFam; TF312829; -. DR Proteomes; UP000008144; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008144}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008144}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 262 262 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 325 325 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 326 326 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 791 791 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSCINP00000035744}. SQ SEQUENCE 1269 AA; 141056 MW; 81AB85CA01512C78 CRC64; LNPTLFSLHF GAGLATYSEI ESTLQKRIMI FDGGMGTMIQ NLRLEEEDFC GDRFKDHSKP LKGNNDLLSL TKPESIYEIH KAYLEAGADF IETNTFSGTS IAQADYALEH VVYELNYESA KIAKRAARDV SNATGVKRYV AGSVGPTNKT LSVSPSVEKP EYRNITFDEL VTSYSEQVRG LLDGGADVLL VETIFDTANA KAGLFAIQVV LDDEKYAPLR GIPIFVSGTI VDKSGRTLSG QTGEAFVVSV SHAKPMCLGL NCALGAVEMR PFIEVIGNFT DRYVICYPNA GLPNTFGGYD ETPQTTAKYL AEFAASGLVN IVGGCCGTTP EHIRAIANAV KIHKPRVPPH DPHKGCLLLS GLEPAIISSL TNFVNIGERC NVAGSRRFAR LIQNGKYESA LDVARSQVEM GAQILDINMD EGMLDGGVVM PKFINLIGSE PDVSKVPLCI DSSNFNIVVA GLKTTQGKCI VNSISLKEGE EDFVEKAKLI LRFGAAVVVM AFDEEGQATS SEDKVRICTR SYRILVDQVG FNPNDIIFDP NILTIGTGME EHNEYAIHFI NATRIIKQTL PGCRISGGLS NLSFSFRGME TIREAMHSVF LFHAITAGMD MGIVNAGNLP VYDDIPADLL KLCEDLIWNK DPDATEKLLK YAQDYGKSGS KSVESEEWRS WEVEERLQHS LVKGIDKYVI EDTKECQQNT VRYPRALNVI EGPLMKGMGV VGDLFGAGKM FLPQVIKSAR VMKKAVGYLI PIMEEEKKLR YKEMEKMGME CVEEDRFAGT VVMATVKGDV HDIGKNIVGV VLGCNNYRVI DLGVMTPCDK ILQTALENKA DIIGLSGLIT PSLSEMIHVA KEMERQDMKI PLLIGGATTS RTHTAVKISP RYNQPTIHVL DASKSVVVIS SLLNDDLRME YLDEIKEEYE EVRMDHYDSL LERKFLSLEQ TRNKKLMIDW TTSGITEPTF LGNKVYHEYH IEKLLQYIDW KPFFDVWQLR GKYPNRGYPK IFKDKTVGEE ALRVFNDAQV MLRKIIDEDL YQMEGVVSFF PANSVGDDIH VYADDVMPRP TTPLAVFYGL RQQAEKEWES VEPYYCLSDF IAPRVSGVRD YIGMFAVSCF GARELCKQYE DNMDDYSSIM AKAVADRLAE AFAEALHELV RTTLWPYSSN EQLEAGDLHK IKYQGIRPAP GYPSQPDHTE KLTMWDVMKV EETIGTKLTG SLAMDPPASV SGLYFANEKA TYFAVGKICE DQVADYASRK GCTKAEIEEW LSPILSYDS // ID H2YDK6_CIOSA Unreviewed; 373 AA. AC H2YDK6; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCSAVP00000003404}; DE Flags: Fragment; OS Ciona savignyi (Pacific transparent sea squirt). OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Enterogona; OC Phlebobranchia; Cionidae; Ciona. OX NCBI_TaxID=51511 {ECO:0000313|Ensembl:ENSCSAVP00000003404, ECO:0000313|Proteomes:UP000007875}; RN [1] {ECO:0000313|Ensembl:ENSCSAVP00000003404} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Birren B., Nusbaum C., Abebe A., Abouelleil A., Adekoya E., RA Ait-zahra M., Allen N., Allen T., An P., Anderson M., Anderson S., RA Arachchi H., Armbruster J., Bachantsang P., Baldwin J., Barry A., RA Bayul T., Blitshsteyn B., Bloom T., Blye J., Boguslavskiy L., RA Borowsky M., Boukhgalter B., Brunache A., Butler J., Calixte N., RA Calvo S., Camarata J., Campo K., Chang J., Cheshatsang Y., Citroen M., RA Collymore A., Considine T., Cook A., Cooke P., Corum B., Cuomo C., RA David R., Dawoe T., Degray S., Dodge S., Dooley K., Dorje P., RA Dorjee K., Dorris L., Duffey N., Dupes A., Elkins T., Engels R., RA Erickson J., Farina A., Faro S., Ferreira P., Fischer H., RA Fitzgerald M., Foley K., Gage D., Galagan J., Gearin G., Gnerre S., RA Gnirke A., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., RA Hagopian D., Hagos B., Hall J., Hatcher B., Heller A., Higgins H., RA Honan T., Horn A., Houde N., Hughes L., Hulme W., Husby E., Iliev I., RA Jaffe D., Jones C., Kamal M., Kamat A., Kamvysselis M., Karlsson E., RA Kells C., Kieu A., Kisner P., Kodira C., Kulbokas E., Labutti K., RA Lama D., Landers T., Leger J., Levine S., Lewis D., Lewis T., RA Lindblad-toh K., Liu X., Lokyitsang T., Lokyitsang Y., Lucien O., RA Lui A., Ma L.J., Mabbitt R., Macdonald J., Maclean C., Major J., RA Manning J., Marabella R., Maru K., Matthews C., Mauceli E., RA Mccarthy M., Mcdonough S., Mcghee T., Meldrim J., Meneus L., RA Mesirov J., Mihalev A., Mihova T., Mikkelsen T., Mlenga V., Moru K., RA Mozes J., Mulrain L., Munson G., Naylor J., Newes C., Nguyen C., RA Nguyen N., Nguyen T., Nicol R., Nielsen C., Nizzari M., Norbu C., RA Norbu N., O'donnell P., Okoawo O., O'leary S., Omotosho B., RA O'neill K., Osman S., Parker S., Perrin D., Phunkhang P., Piqani B., RA Purcell S., Rachupka T., Ramasamy U., Rameau R., Ray V., Raymond C., RA Retta R., Richardson S., Rise C., Rodriguez J., Rogers J., Rogov P., RA Rutman M., Schupbach R., Seaman C., Settipalli S., Sharpe T., RA Sheridan J., Sherpa N., Shi J., Smirnov S., Smith C., Sougnez C., RA Spencer B., Stalker J., Stange-thomann N., Stavropoulos S., RA Stetson K., Stone C., Stone S., Stubbs M., Talamas J., Tchuinga P., RA Tenzing P., Tesfaye S., Theodore J., Thoulutsang Y., Topham K., RA Towey S., Tsamla T., Tsomo N., Vallee D., Vassiliev H., RA Venkataraman V., Vinson J., Vo A., Wade C., Wang S., Wangchuk T., RA Wangdi T., Whittaker C., Wilkinson J., Wu Y., Wyman D., Yadav S., RA Yang S., Yang X., Yeager S., Yee E., Young G., Zainoun J., Zembeck L., RA Zimmer A., Zody M., Lander E.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCSAVP00000003404} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSCSAVP00000003404}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSCSAVT00000003456; ENSCSAVP00000003404; ENSCSAVG00000002026. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; H2YDK6; -. DR OMA; WITKLAT; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR Proteomes; UP000007875; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007875}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000007875}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 220 220 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT NON_TER 1 1 {ECO:0000313|Ensembl: FT ENSCSAVP00000003404}. SQ SEQUENCE 373 AA; 41768 MW; 0A50DE204A0CEA53 CRC64; LNIMSNVRKR KGLLELLVEG PVVGDGSMCM TLEKRGYCRA GPWTPEAVLL YPDAVKQLLR EYMRAGADVL QTPCYASSDG RLKRGNINYT VRHKFHTSEI NEAACKIAHE VALEGNALVC GGITPVLSYL HKKGDLVIRA EFTDQLEIFI QRRDTVDFIL AEFFGHVEEL EICIDVMKRS KMPIACTMRI GPLGDLNGVS VKECAVRMAR TGADLIGLNC MFDLNTTLKT IKRMKKALDD EGLETPLMCQ PLGFMCPEVE NSLYGYARLS EDPFALEPRQ VTRFEVHAFA RAAYDLGVRY IGGCCGMEPH HIRAIAQELS AERGRNPPVQ DMCPPCEWLK KSNITTTQKK TNLEFWMNLK PGCGRPFNPS CNK // ID H2YEI3_CIOSA Unreviewed; 375 AA. AC H2YEI3; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCSAVP00000003731}; DE Flags: Fragment; GN Name=Csa.4075 {ECO:0000313|Ensembl:ENSCSAVP00000003731}; OS Ciona savignyi (Pacific transparent sea squirt). OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Enterogona; OC Phlebobranchia; Cionidae; Ciona. OX NCBI_TaxID=51511 {ECO:0000313|Ensembl:ENSCSAVP00000003731, ECO:0000313|Proteomes:UP000007875}; RN [1] {ECO:0000313|Ensembl:ENSCSAVP00000003731} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Birren B., Nusbaum C., Abebe A., Abouelleil A., Adekoya E., RA Ait-zahra M., Allen N., Allen T., An P., Anderson M., Anderson S., RA Arachchi H., Armbruster J., Bachantsang P., Baldwin J., Barry A., RA Bayul T., Blitshsteyn B., Bloom T., Blye J., Boguslavskiy L., RA Borowsky M., Boukhgalter B., Brunache A., Butler J., Calixte N., RA Calvo S., Camarata J., Campo K., Chang J., Cheshatsang Y., Citroen M., RA Collymore A., Considine T., Cook A., Cooke P., Corum B., Cuomo C., RA David R., Dawoe T., Degray S., Dodge S., Dooley K., Dorje P., RA Dorjee K., Dorris L., Duffey N., Dupes A., Elkins T., Engels R., RA Erickson J., Farina A., Faro S., Ferreira P., Fischer H., RA Fitzgerald M., Foley K., Gage D., Galagan J., Gearin G., Gnerre S., RA Gnirke A., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., RA Hagopian D., Hagos B., Hall J., Hatcher B., Heller A., Higgins H., RA Honan T., Horn A., Houde N., Hughes L., Hulme W., Husby E., Iliev I., RA Jaffe D., Jones C., Kamal M., Kamat A., Kamvysselis M., Karlsson E., RA Kells C., Kieu A., Kisner P., Kodira C., Kulbokas E., Labutti K., RA Lama D., Landers T., Leger J., Levine S., Lewis D., Lewis T., RA Lindblad-toh K., Liu X., Lokyitsang T., Lokyitsang Y., Lucien O., RA Lui A., Ma L.J., Mabbitt R., Macdonald J., Maclean C., Major J., RA Manning J., Marabella R., Maru K., Matthews C., Mauceli E., RA Mccarthy M., Mcdonough S., Mcghee T., Meldrim J., Meneus L., RA Mesirov J., Mihalev A., Mihova T., Mikkelsen T., Mlenga V., Moru K., RA Mozes J., Mulrain L., Munson G., Naylor J., Newes C., Nguyen C., RA Nguyen N., Nguyen T., Nicol R., Nielsen C., Nizzari M., Norbu C., RA Norbu N., O'donnell P., Okoawo O., O'leary S., Omotosho B., RA O'neill K., Osman S., Parker S., Perrin D., Phunkhang P., Piqani B., RA Purcell S., Rachupka T., Ramasamy U., Rameau R., Ray V., Raymond C., RA Retta R., Richardson S., Rise C., Rodriguez J., Rogers J., Rogov P., RA Rutman M., Schupbach R., Seaman C., Settipalli S., Sharpe T., RA Sheridan J., Sherpa N., Shi J., Smirnov S., Smith C., Sougnez C., RA Spencer B., Stalker J., Stange-thomann N., Stavropoulos S., RA Stetson K., Stone C., Stone S., Stubbs M., Talamas J., Tchuinga P., RA Tenzing P., Tesfaye S., Theodore J., Thoulutsang Y., Topham K., RA Towey S., Tsamla T., Tsomo N., Vallee D., Vassiliev H., RA Venkataraman V., Vinson J., Vo A., Wade C., Wang S., Wangchuk T., RA Wangdi T., Whittaker C., Wilkinson J., Wu Y., Wyman D., Yadav S., RA Yang S., Yang X., Yeager S., Yee E., Young G., Zainoun J., Zembeck L., RA Zimmer A., Zody M., Lander E.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCSAVP00000003731} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSCSAVP00000003731}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSCSAVT00000003788; ENSCSAVP00000003731; ENSCSAVG00000002210. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; H2YEI3; -. DR OMA; RGQALKI; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR Proteomes; UP000007875; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007875}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000007875}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 218 218 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT NON_TER 1 1 {ECO:0000313|Ensembl: FT ENSCSAVP00000003731}. SQ SEQUENCE 375 AA; 41758 MW; CA76F2B0F79E454F CRC64; ITMAKGDQCK KGLLELLKEG PVVGDGSMCM TLEKRGYCRA GPWTPEAVLL YPDAVKQLLR EYMRAGADVL QTPCFYCSDG MFKKGSKSGE PISYTTDAIN EAACRIAHEI SKEGKDVLVC GGLSPVLSYF REKNMEKARA EFDSQLDVFI KYKVDFVLAE FFAYIEELEI CIDVMKRSKM PIACTMRIGP LGDSNGVSVE ECAVRMARTG ADLIGINCLY DFDTCLKTLK RMRDALDKEG LKTHLICQPL GWRCPEVEHT LIGYLDLPET PLGSLEPRQV TRFEVHAFAR AAYDLGVRYI GGCCGMEPHH IRAIAQELAP ERKRNPPVED MCPPLGYLQL SGLSNIKKKD NKQYWIEQKP GSGRPFSPAL SSTEG // ID H2Z6R3_CIOSA Unreviewed; 1262 AA. AC H2Z6R3; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCSAVP00000013275}; OS Ciona savignyi (Pacific transparent sea squirt). OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Enterogona; OC Phlebobranchia; Cionidae; Ciona. OX NCBI_TaxID=51511 {ECO:0000313|Ensembl:ENSCSAVP00000013275, ECO:0000313|Proteomes:UP000007875}; RN [1] {ECO:0000313|Ensembl:ENSCSAVP00000013275} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Birren B., Nusbaum C., Abebe A., Abouelleil A., Adekoya E., RA Ait-zahra M., Allen N., Allen T., An P., Anderson M., Anderson S., RA Arachchi H., Armbruster J., Bachantsang P., Baldwin J., Barry A., RA Bayul T., Blitshsteyn B., Bloom T., Blye J., Boguslavskiy L., RA Borowsky M., Boukhgalter B., Brunache A., Butler J., Calixte N., RA Calvo S., Camarata J., Campo K., Chang J., Cheshatsang Y., Citroen M., RA Collymore A., Considine T., Cook A., Cooke P., Corum B., Cuomo C., RA David R., Dawoe T., Degray S., Dodge S., Dooley K., Dorje P., RA Dorjee K., Dorris L., Duffey N., Dupes A., Elkins T., Engels R., RA Erickson J., Farina A., Faro S., Ferreira P., Fischer H., RA Fitzgerald M., Foley K., Gage D., Galagan J., Gearin G., Gnerre S., RA Gnirke A., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., RA Hagopian D., Hagos B., Hall J., Hatcher B., Heller A., Higgins H., RA Honan T., Horn A., Houde N., Hughes L., Hulme W., Husby E., Iliev I., RA Jaffe D., Jones C., Kamal M., Kamat A., Kamvysselis M., Karlsson E., RA Kells C., Kieu A., Kisner P., Kodira C., Kulbokas E., Labutti K., RA Lama D., Landers T., Leger J., Levine S., Lewis D., Lewis T., RA Lindblad-toh K., Liu X., Lokyitsang T., Lokyitsang Y., Lucien O., RA Lui A., Ma L.J., Mabbitt R., Macdonald J., Maclean C., Major J., RA Manning J., Marabella R., Maru K., Matthews C., Mauceli E., RA Mccarthy M., Mcdonough S., Mcghee T., Meldrim J., Meneus L., RA Mesirov J., Mihalev A., Mihova T., Mikkelsen T., Mlenga V., Moru K., RA Mozes J., Mulrain L., Munson G., Naylor J., Newes C., Nguyen C., RA Nguyen N., Nguyen T., Nicol R., Nielsen C., Nizzari M., Norbu C., RA Norbu N., O'donnell P., Okoawo O., O'leary S., Omotosho B., RA O'neill K., Osman S., Parker S., Perrin D., Phunkhang P., Piqani B., RA Purcell S., Rachupka T., Ramasamy U., Rameau R., Ray V., Raymond C., RA Retta R., Richardson S., Rise C., Rodriguez J., Rogers J., Rogov P., RA Rutman M., Schupbach R., Seaman C., Settipalli S., Sharpe T., RA Sheridan J., Sherpa N., Shi J., Smirnov S., Smith C., Sougnez C., RA Spencer B., Stalker J., Stange-thomann N., Stavropoulos S., RA Stetson K., Stone C., Stone S., Stubbs M., Talamas J., Tchuinga P., RA Tenzing P., Tesfaye S., Theodore J., Thoulutsang Y., Topham K., RA Towey S., Tsamla T., Tsomo N., Vallee D., Vassiliev H., RA Venkataraman V., Vinson J., Vo A., Wade C., Wang S., Wangchuk T., RA Wangdi T., Whittaker C., Wilkinson J., Wu Y., Wyman D., Yadav S., RA Yang S., Yang X., Yeager S., Yee E., Young G., Zainoun J., Zembeck L., RA Zimmer A., Zody M., Lander E.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCSAVP00000013275} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 1}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSCSAVP00000013275}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSCSAVT00000013425; ENSCSAVP00000013275; ENSCSAVG00000007792. DR GeneTree; ENSGT00420000029824; -. DR InParanoid; H2Z6R3; -. DR OMA; TWTFPRQ; -. DR OrthoDB; EOG7TF786; -. DR TreeFam; TF312829; -. DR Proteomes; UP000007875; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007875}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007875}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 252 252 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 315 315 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 316 316 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 783 783 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1262 AA; 139592 MW; 48579F0E190D5810 CRC64; MSGHTTAIEI EATLKQRIMV FDGGMGTMIQ NLRLEEQDFR GSQFIDHPKS LKGNNDLLSI TKPDSIYEIH KAYLEAGADF IETNTFSGTS IAQADYALEA FVYQLNFESA RIAKKAAVDV TNATGVKRYV AGSIGPTNKT LSVSPSVERP EYRNITFDEL VVAYSEQTRG LLDGGSDVLL VETIFDTANA KAALFAIQEV LDEEKYSPLR GIPIFVSGTI VDKSGRTLSG QTGEAFVISV SHAKPMCLGL NCALGAVEMR PFIEVIGNFT DAYVICYPNA GLPNTFGGYD ETPATTAKYL AEFAASGLVN IVGGCCGTTP EHIKAIADAV RPHKPRTPPN NPHKGCLLLS GLEPAVISSI TNFVNIGERC NVAGSRRFAR LVQNGKYEAA LDVARSQVEM GAQILDINMD EGMLDGKSVM PKFINLIGSE PDVSKVPLCV DSSNFDIVVA GLKCTQGKCI VNSISLKEGE EDFINKAKLI KRFGAAVVVM AFDEDGQATS SEDKVRICTR SFRVLVDQIG FEPNDIIFDP NILTIGTGME EHNEYAINFI AATRIIKKNL PGCRISGGLS NLSFSFRGME RIREAMHSVF LYHAISAGMD MGIVNAGNLP VYDDIPKDLL KYCEDLIWNK NAEATETLLK YAQEHSGGGN KAVESEEWRS WEVEDRLQHS LVKGIDKYVI EDTKECQENT EKYPRALNVI ERPLMKGMSI VGDLFGAGKM FLPQVIKSAR VMKKAVGYLI PIMEEEKRAR LKEMEINGME CVEEEENRFA GTVVIATVKG DVHDIGKNIV AVVLGCNNYR VIDLGVMTPC EKILQTAVEN NADIIGLSGL ITPSLSEMIH VAKEMERLEM KIPLLIGGAT TSRTHTAVKI SPRYSQPTIH VLDASKSVVV ISSLLNEDVR MEYLEDIREE YEDVRTDHYD SLLERKFLTI ADARSKKLSI DWTSSPITEP KFIGNKVFHD FNIEKLVPYI DWKPFFDVWQ LRGKYPNRGY PKIFKDKTVG EEALRVFNDA QNMLQKIVDD GLYTMEGVVS FYPANSVGDD IHVYAEDVTP RPTTPLAVFY GLRQQAEKEW ESIEPYYCLS DFIAPRVSGV HDYIGLFAVS CCGAQQLCAQ FERNLDDYSS IMAKALADRL AEAFAEAMHE IVRTTLWPYS SSESLEAGDL HKIKYQGIRP APGYPSQPDH TEKLTMWEVM GVSESIGTKL TESLAMDPPA SVSGLYFANE NAKYFAVGKI DEDQVSDYAA RKGCSKSEIE EWLSPILCYD PT // ID H2Z6R4_CIOSA Unreviewed; 1245 AA. AC H2Z6R4; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCSAVP00000013276}; DE Flags: Fragment; OS Ciona savignyi (Pacific transparent sea squirt). OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Enterogona; OC Phlebobranchia; Cionidae; Ciona. OX NCBI_TaxID=51511 {ECO:0000313|Ensembl:ENSCSAVP00000013276, ECO:0000313|Proteomes:UP000007875}; RN [1] {ECO:0000313|Ensembl:ENSCSAVP00000013276} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Birren B., Nusbaum C., Abebe A., Abouelleil A., Adekoya E., RA Ait-zahra M., Allen N., Allen T., An P., Anderson M., Anderson S., RA Arachchi H., Armbruster J., Bachantsang P., Baldwin J., Barry A., RA Bayul T., Blitshsteyn B., Bloom T., Blye J., Boguslavskiy L., RA Borowsky M., Boukhgalter B., Brunache A., Butler J., Calixte N., RA Calvo S., Camarata J., Campo K., Chang J., Cheshatsang Y., Citroen M., RA Collymore A., Considine T., Cook A., Cooke P., Corum B., Cuomo C., RA David R., Dawoe T., Degray S., Dodge S., Dooley K., Dorje P., RA Dorjee K., Dorris L., Duffey N., Dupes A., Elkins T., Engels R., RA Erickson J., Farina A., Faro S., Ferreira P., Fischer H., RA Fitzgerald M., Foley K., Gage D., Galagan J., Gearin G., Gnerre S., RA Gnirke A., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., RA Hagopian D., Hagos B., Hall J., Hatcher B., Heller A., Higgins H., RA Honan T., Horn A., Houde N., Hughes L., Hulme W., Husby E., Iliev I., RA Jaffe D., Jones C., Kamal M., Kamat A., Kamvysselis M., Karlsson E., RA Kells C., Kieu A., Kisner P., Kodira C., Kulbokas E., Labutti K., RA Lama D., Landers T., Leger J., Levine S., Lewis D., Lewis T., RA Lindblad-toh K., Liu X., Lokyitsang T., Lokyitsang Y., Lucien O., RA Lui A., Ma L.J., Mabbitt R., Macdonald J., Maclean C., Major J., RA Manning J., Marabella R., Maru K., Matthews C., Mauceli E., RA Mccarthy M., Mcdonough S., Mcghee T., Meldrim J., Meneus L., RA Mesirov J., Mihalev A., Mihova T., Mikkelsen T., Mlenga V., Moru K., RA Mozes J., Mulrain L., Munson G., Naylor J., Newes C., Nguyen C., RA Nguyen N., Nguyen T., Nicol R., Nielsen C., Nizzari M., Norbu C., RA Norbu N., O'donnell P., Okoawo O., O'leary S., Omotosho B., RA O'neill K., Osman S., Parker S., Perrin D., Phunkhang P., Piqani B., RA Purcell S., Rachupka T., Ramasamy U., Rameau R., Ray V., Raymond C., RA Retta R., Richardson S., Rise C., Rodriguez J., Rogers J., Rogov P., RA Rutman M., Schupbach R., Seaman C., Settipalli S., Sharpe T., RA Sheridan J., Sherpa N., Shi J., Smirnov S., Smith C., Sougnez C., RA Spencer B., Stalker J., Stange-thomann N., Stavropoulos S., RA Stetson K., Stone C., Stone S., Stubbs M., Talamas J., Tchuinga P., RA Tenzing P., Tesfaye S., Theodore J., Thoulutsang Y., Topham K., RA Towey S., Tsamla T., Tsomo N., Vallee D., Vassiliev H., RA Venkataraman V., Vinson J., Vo A., Wade C., Wang S., Wangchuk T., RA Wangdi T., Whittaker C., Wilkinson J., Wu Y., Wyman D., Yadav S., RA Yang S., Yang X., Yeager S., Yee E., Young G., Zainoun J., Zembeck L., RA Zimmer A., Zody M., Lander E.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCSAVP00000013276} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 1}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSCSAVP00000013276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSCSAVT00000013426; ENSCSAVP00000013276; ENSCSAVG00000007792. DR GeneTree; ENSGT00420000029824; -. DR Proteomes; UP000007875; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007875}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007875}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 255 255 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 318 318 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 319 319 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 770 770 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. FT NON_TER 1 1 {ECO:0000313|Ensembl: FT ENSCSAVP00000013276}. SQ SEQUENCE 1245 AA; 137334 MW; C739D79DDC49EEE2 CRC64; VVVSPGHTTA IEIEATLKQR IMVFDGGMGT MIQNLRLEEQ DFRGSQFIDH PKSLKGNNDL LSITKPDSIY EIHKAYLEAG ADFIETNTFS GTSIAQADYA LEAFVYQLNF ESARIAKKAA VDVTNATGVK RYVAGSIGPT NKTLSVSPSV ERPEYRNITF DELVVAYSEQ TRGLLDGGSD VLLVETIFDT ANAKAALFAI QEVLDEEKYS PLRGIPIFVS GTIVDKSGRT LSGQTGEAFV ISVSHAKPMC LGLNCALGAV EMRPFIEVIG NFTDAYVICY PNAGLPNTFG GYDETPATTA KYLAEFAASG LVNIVGGCCG TTPEHIKAIA DAVRPHKPRT PPNNPHKGCL LLSGLEPAVI SSITNFVNIG ERCNVAGSRR FARLVQNGKY EAALDVARSQ VEMGAQILDI NMDEGMLDGK SVMPKFINLI GSEPDVSKVP LCVDSSNFDI VVAGLKCTQG KCIVNSISLK EGEEDFINKA KLIKRFGAAV VVMAFDEDGQ ATSSEDKVRI CTRSFRVLVD QIGFEPNDII FDPNILTIGT GMEEHNEYAI NFIAATRIIK KNLPGCRISG GLSNLSFSFR GMERIREAMH SVFLYHAISA GMDMGIVNAG NLPVYDDIPK DLLKYCEDLI WNKNAEATET LLKYAQEHSG GGNKAVESEE WRSWEVEDRL QHSLVKGIDK YVIEDTKECQ ENTEKYPRAL NVIERPLMKG MSIVGDLFGA GKMFLPQVIK SARVMKKAVG YLIPIMEEEK RASNRFAGTV VIATVKGDVH DIGKNIVAVV LGCNNYRVID LGVMTPCEKI LQTAVENNAD IIGLSGLITP SLSEMIHVAK EMERLGMVIP LLIGGATTSR THTAVKISPR YSQPTIHVLD ASKSVVVISS LLNEDVRMEY LEDIREEYED VRTDHYDSLL ERKFLTIADA RSKKLSIDWT SSPITEPKFI GNKVFHDFNI EKLVPYIDWK PFFDVWQLRG KYPNRGYPKI FKDKTVGEEA LRVFNDAQNM LQKIVDDGLY TMEGVVSFYP ANSVGDDIHV YAEDVTPRPT TPLAVFYGLR QQWESIEPYY CLSDFIAPRV SGVHDYIGLF AVSCCGAQQL CAQFERNLDD YSSIMAKALA DRLAEAFAEA MHEIVRTTLW PYSSSESLEA GDLHKIKYQG IRPAPGYPSQ PDHTEKLTMW EVMGVSESIG TKLTESLAMD PPASVSGLYF ANENAKYFAV GKIDEDQVSD YAARKGCSKS EIEEWLSPIL CYDPT // ID H2Z6R5_CIOSA Unreviewed; 1258 AA. AC H2Z6R5; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCSAVP00000013277}; DE Flags: Fragment; OS Ciona savignyi (Pacific transparent sea squirt). OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Enterogona; OC Phlebobranchia; Cionidae; Ciona. OX NCBI_TaxID=51511 {ECO:0000313|Ensembl:ENSCSAVP00000013277, ECO:0000313|Proteomes:UP000007875}; RN [1] {ECO:0000313|Ensembl:ENSCSAVP00000013277} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Birren B., Nusbaum C., Abebe A., Abouelleil A., Adekoya E., RA Ait-zahra M., Allen N., Allen T., An P., Anderson M., Anderson S., RA Arachchi H., Armbruster J., Bachantsang P., Baldwin J., Barry A., RA Bayul T., Blitshsteyn B., Bloom T., Blye J., Boguslavskiy L., RA Borowsky M., Boukhgalter B., Brunache A., Butler J., Calixte N., RA Calvo S., Camarata J., Campo K., Chang J., Cheshatsang Y., Citroen M., RA Collymore A., Considine T., Cook A., Cooke P., Corum B., Cuomo C., RA David R., Dawoe T., Degray S., Dodge S., Dooley K., Dorje P., RA Dorjee K., Dorris L., Duffey N., Dupes A., Elkins T., Engels R., RA Erickson J., Farina A., Faro S., Ferreira P., Fischer H., RA Fitzgerald M., Foley K., Gage D., Galagan J., Gearin G., Gnerre S., RA Gnirke A., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., RA Hagopian D., Hagos B., Hall J., Hatcher B., Heller A., Higgins H., RA Honan T., Horn A., Houde N., Hughes L., Hulme W., Husby E., Iliev I., RA Jaffe D., Jones C., Kamal M., Kamat A., Kamvysselis M., Karlsson E., RA Kells C., Kieu A., Kisner P., Kodira C., Kulbokas E., Labutti K., RA Lama D., Landers T., Leger J., Levine S., Lewis D., Lewis T., RA Lindblad-toh K., Liu X., Lokyitsang T., Lokyitsang Y., Lucien O., RA Lui A., Ma L.J., Mabbitt R., Macdonald J., Maclean C., Major J., RA Manning J., Marabella R., Maru K., Matthews C., Mauceli E., RA Mccarthy M., Mcdonough S., Mcghee T., Meldrim J., Meneus L., RA Mesirov J., Mihalev A., Mihova T., Mikkelsen T., Mlenga V., Moru K., RA Mozes J., Mulrain L., Munson G., Naylor J., Newes C., Nguyen C., RA Nguyen N., Nguyen T., Nicol R., Nielsen C., Nizzari M., Norbu C., RA Norbu N., O'donnell P., Okoawo O., O'leary S., Omotosho B., RA O'neill K., Osman S., Parker S., Perrin D., Phunkhang P., Piqani B., RA Purcell S., Rachupka T., Ramasamy U., Rameau R., Ray V., Raymond C., RA Retta R., Richardson S., Rise C., Rodriguez J., Rogers J., Rogov P., RA Rutman M., Schupbach R., Seaman C., Settipalli S., Sharpe T., RA Sheridan J., Sherpa N., Shi J., Smirnov S., Smith C., Sougnez C., RA Spencer B., Stalker J., Stange-thomann N., Stavropoulos S., RA Stetson K., Stone C., Stone S., Stubbs M., Talamas J., Tchuinga P., RA Tenzing P., Tesfaye S., Theodore J., Thoulutsang Y., Topham K., RA Towey S., Tsamla T., Tsomo N., Vallee D., Vassiliev H., RA Venkataraman V., Vinson J., Vo A., Wade C., Wang S., Wangchuk T., RA Wangdi T., Whittaker C., Wilkinson J., Wu Y., Wyman D., Yadav S., RA Yang S., Yang X., Yeager S., Yee E., Young G., Zainoun J., Zembeck L., RA Zimmer A., Zody M., Lander E.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCSAVP00000013277} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 1}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSCSAVP00000013277}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSCSAVT00000013427; ENSCSAVP00000013277; ENSCSAVG00000007792. DR GeneTree; ENSGT00420000029824; -. DR Proteomes; UP000007875; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007875}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007875}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 255 255 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 318 318 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 319 319 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 781 781 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. FT NON_TER 1 1 {ECO:0000313|Ensembl: FT ENSCSAVP00000013277}. SQ SEQUENCE 1258 AA; 138941 MW; 4AE8D275D7225D41 CRC64; VVVSPGHTTA IEIEATLKQR IMVFDGGMGT MIQNLRLEEQ DFRGSQFIDH PKSLKGNNDL LSITKPDSIY EIHKAYLEAG ADFIETNTFS GTSIAQADYA LEAFVYQLNF ESARIAKKAA VDVTNATGVK RYVAGSIGPT NKTLSVSPSV ERPEYRNITF DELVVAYSEQ TRGLLDGGSD VLLVETIFDT ANAKAALFAI QEVLDEEKYS PLRGIPIFVS GTIVDKSGRT LSGQTGEAFV ISVSHAKPMC LGLNCALGAV EMRPFIEVIG NFTDAYVICY PNAGLPNTFG GYDETPATTA KYLAEFAASG LVNIVGGCCG TTPEHIKAIA DAVRPHKPRT PPNNPHKGCL LLSGLEPAVI SSITNFVNIG ERCNVAGSRR FARLVQNGKY EAALDVARSQ VEMGAQILDI NMDEGMLDGK SVMPKFINLI GSEPDVSKVP LCVDSSNFDI VVAGLKCTQG KCIVNSISLK EGEEDFINKA KLIKRFGAAV VVMAFDEDGQ ATSSEDKVRI CTRSFRVLVD QIGFEPNDII FDPNILTIGT GMEEHNEYAI NFIAATRIIK KNLPGCRISG GLSNLSFSFR GMERIREAMH SVFLYHAISA GMDMGIVNAG NLPVYDDIPK DLLKYCEDLI WNKNAEATET LLKYAQEHSG GGNKAVESEE WRSWEVEDRL QHSLVKGIDK YVIEDTKECQ ENTEKYPRAL NVIERPLMKG MSIVGDLFGA GKMFLPQVIK SARVMKKAVG YLIPIMEEEK RARLKEMEIN GMECNRFAGT VVIATVKGDV HDIGKNIVAV VLGCNNYRVI DLGVMTPCEK ILQTAVENNA DIIGLSGLIT PSLSEMIHVA KEMERLGMVI PLLIGGATTS RTHTAVKISP RYSQPTIHVL DASKSVVVIS SLLNEDVRME YLEDIREEYE DVRTDHYDSL LERKFLTIAD ARSKKLSIDW TSSPITEPKF IGNKVFHDFN IEKLVPYIDW KPFFDVWQLR GKYPNRGYPK IFKDKTVGEE ALRVFNDAQN MLQKIVDDGL YTMEGVVSFY PANSVGDDIH VYAEDVTPRP TTPLAVFYGL RQQAEKEWES IEPYYCLSDF IAPRVSGVHD YIGLFAVSCC GAQQLCAQFE RNLDDYSSIM AKALADRLAE AFAEAMHEIV RTTLWPYSSS ESLEAGDLHK IKYQGIRPAP GYPSQPDHTE KLTMWEVMGV SESIGTKLTE SLAMDPPASV SGLYFANENA KYFAVGKIDE DQVSDYAARK GCSKSEIEEW LSPILCYD // ID H2Z6R6_CIOSA Unreviewed; 1227 AA. AC H2Z6R6; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCSAVP00000013278}; DE Flags: Fragment; OS Ciona savignyi (Pacific transparent sea squirt). OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Enterogona; OC Phlebobranchia; Cionidae; Ciona. OX NCBI_TaxID=51511 {ECO:0000313|Ensembl:ENSCSAVP00000013278, ECO:0000313|Proteomes:UP000007875}; RN [1] {ECO:0000313|Ensembl:ENSCSAVP00000013278} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Birren B., Nusbaum C., Abebe A., Abouelleil A., Adekoya E., RA Ait-zahra M., Allen N., Allen T., An P., Anderson M., Anderson S., RA Arachchi H., Armbruster J., Bachantsang P., Baldwin J., Barry A., RA Bayul T., Blitshsteyn B., Bloom T., Blye J., Boguslavskiy L., RA Borowsky M., Boukhgalter B., Brunache A., Butler J., Calixte N., RA Calvo S., Camarata J., Campo K., Chang J., Cheshatsang Y., Citroen M., RA Collymore A., Considine T., Cook A., Cooke P., Corum B., Cuomo C., RA David R., Dawoe T., Degray S., Dodge S., Dooley K., Dorje P., RA Dorjee K., Dorris L., Duffey N., Dupes A., Elkins T., Engels R., RA Erickson J., Farina A., Faro S., Ferreira P., Fischer H., RA Fitzgerald M., Foley K., Gage D., Galagan J., Gearin G., Gnerre S., RA Gnirke A., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., RA Hagopian D., Hagos B., Hall J., Hatcher B., Heller A., Higgins H., RA Honan T., Horn A., Houde N., Hughes L., Hulme W., Husby E., Iliev I., RA Jaffe D., Jones C., Kamal M., Kamat A., Kamvysselis M., Karlsson E., RA Kells C., Kieu A., Kisner P., Kodira C., Kulbokas E., Labutti K., RA Lama D., Landers T., Leger J., Levine S., Lewis D., Lewis T., RA Lindblad-toh K., Liu X., Lokyitsang T., Lokyitsang Y., Lucien O., RA Lui A., Ma L.J., Mabbitt R., Macdonald J., Maclean C., Major J., RA Manning J., Marabella R., Maru K., Matthews C., Mauceli E., RA Mccarthy M., Mcdonough S., Mcghee T., Meldrim J., Meneus L., RA Mesirov J., Mihalev A., Mihova T., Mikkelsen T., Mlenga V., Moru K., RA Mozes J., Mulrain L., Munson G., Naylor J., Newes C., Nguyen C., RA Nguyen N., Nguyen T., Nicol R., Nielsen C., Nizzari M., Norbu C., RA Norbu N., O'donnell P., Okoawo O., O'leary S., Omotosho B., RA O'neill K., Osman S., Parker S., Perrin D., Phunkhang P., Piqani B., RA Purcell S., Rachupka T., Ramasamy U., Rameau R., Ray V., Raymond C., RA Retta R., Richardson S., Rise C., Rodriguez J., Rogers J., Rogov P., RA Rutman M., Schupbach R., Seaman C., Settipalli S., Sharpe T., RA Sheridan J., Sherpa N., Shi J., Smirnov S., Smith C., Sougnez C., RA Spencer B., Stalker J., Stange-thomann N., Stavropoulos S., RA Stetson K., Stone C., Stone S., Stubbs M., Talamas J., Tchuinga P., RA Tenzing P., Tesfaye S., Theodore J., Thoulutsang Y., Topham K., RA Towey S., Tsamla T., Tsomo N., Vallee D., Vassiliev H., RA Venkataraman V., Vinson J., Vo A., Wade C., Wang S., Wangchuk T., RA Wangdi T., Whittaker C., Wilkinson J., Wu Y., Wyman D., Yadav S., RA Yang S., Yang X., Yeager S., Yee E., Young G., Zainoun J., Zembeck L., RA Zimmer A., Zody M., Lander E.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCSAVP00000013278} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 1}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSCSAVP00000013278}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSCSAVT00000013428; ENSCSAVP00000013278; ENSCSAVG00000007792. DR GeneTree; ENSGT00420000029824; -. DR Proteomes; UP000007875; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007875}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007875}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 246 246 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 762 762 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. FT NON_TER 1 1 {ECO:0000313|Ensembl: FT ENSCSAVP00000013278}. SQ SEQUENCE 1227 AA; 135524 MW; B4A99BFF8A8F0780 CRC64; TAIEIEATLK QRIMVFDGGM GTMIQNLRLE EQDFRGSQFI DHPKSLKGNN DLLSITKPDS IYEIHKAYLE AGADFIETNT FSGTSIAQAD YALEAFVYQL NFESARIAKK AAVDVTNATV KRYVAGSIGP TNKTLSVSPS VERPEYRNIT FDELVVAYSE QTRGLLDGGS DVLLVETIFD TANAKAALFA IQEVLDEEKY SPLRGIPIFV SGTIVDKSGR TLSGQTGEAF VISVSHAKPM CLGLNCALGA VEMRPFIEVI GNFTDAYVIC YPNAGLPNTF GGYDETPATT AKYLAEFAAS GLVNIVGGCC GTTPEHIKAI ADAVRPHKPR TPPNNPHKGC LLLSGLEPAV ISSITNFVNI GERCNVAGSR RFARLVQNGK YEAALDVARS QVEMGAQILD INMDEGMLDG KSVMPKFINL IGSEPDVSKV PLCVDSSNFD IVVAGLKCTQ GKCIVNSISL KEGEEDFINK AKLIKRFGAA VVVMAFDEDG QATSSEDKVR ICTRSFRVLV DQIGFEPNDI IFDPNILTIG TGMEEHNEYA INFIAATRII KKNLPGCRIS GGLSNLSFSF RGMERIREAM HSVFLYHAIS AGMDMGIVNA GNLPVYDDIP KDLLKYCEDL IWNKNAEATE TLLKYAQEHS GGGNKAVESE EWRSWEVEDR LQHSLVKGID KYVIEDTKEC QENTEKYPRA LNVIERPLMK GMSIVGDLFG AGKMFLPQVI KSARVMKKAV GYLIPIMEEE KRASFNRFAG TVVIATVKGD VHDIGKNIVA VVLGCNNYRV IDLGVMTPCE KILQTAVENN ADIIGLSGLI TPSLSEMIHV AKEMERLEMK IPLLIGGATT SRTHTAVKIS PRYSQPTIHV LDASKSVVVI SSLLNEDVRM EYLEDIREEY EDVRTDHYDS LLERKFLTIA DARSKKLSID WTSSPITEPK FIGNKVFHDF NIEKLVPYID WKPFFDVWQL RGKYPNRGYP KIFKDKTVGE EALRVFNDAQ NMLQKIVDDG LYTMEGVVSF YPANSVGDDI HVYAEDVTPR PTTPLAVFYG LRQQPYYCLS DFIAPRVSGV HDYIGLFAVS CCGAQQLCAQ FERNLDDYSS IMAKALADRL AEAFAEAMHE IVRTTLWPYS SSESLEAGDL HKIKYQGIRP APGYPSQPDH TEKLTMWEVM GVSESIGTKL TESLAMDPPA SVSGLYFANE NAKYFAVGKI DEDQVSDYAA RKGCSKSEIE EWLSPIL // ID H2Z6R7_CIOSA Unreviewed; 381 AA. AC H2Z6R7; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCSAVP00000013279}; DE Flags: Fragment; OS Ciona savignyi (Pacific transparent sea squirt). OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Enterogona; OC Phlebobranchia; Cionidae; Ciona. OX NCBI_TaxID=51511 {ECO:0000313|Ensembl:ENSCSAVP00000013279, ECO:0000313|Proteomes:UP000007875}; RN [1] {ECO:0000313|Ensembl:ENSCSAVP00000013279} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Birren B., Nusbaum C., Abebe A., Abouelleil A., Adekoya E., RA Ait-zahra M., Allen N., Allen T., An P., Anderson M., Anderson S., RA Arachchi H., Armbruster J., Bachantsang P., Baldwin J., Barry A., RA Bayul T., Blitshsteyn B., Bloom T., Blye J., Boguslavskiy L., RA Borowsky M., Boukhgalter B., Brunache A., Butler J., Calixte N., RA Calvo S., Camarata J., Campo K., Chang J., Cheshatsang Y., Citroen M., RA Collymore A., Considine T., Cook A., Cooke P., Corum B., Cuomo C., RA David R., Dawoe T., Degray S., Dodge S., Dooley K., Dorje P., RA Dorjee K., Dorris L., Duffey N., Dupes A., Elkins T., Engels R., RA Erickson J., Farina A., Faro S., Ferreira P., Fischer H., RA Fitzgerald M., Foley K., Gage D., Galagan J., Gearin G., Gnerre S., RA Gnirke A., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., RA Hagopian D., Hagos B., Hall J., Hatcher B., Heller A., Higgins H., RA Honan T., Horn A., Houde N., Hughes L., Hulme W., Husby E., Iliev I., RA Jaffe D., Jones C., Kamal M., Kamat A., Kamvysselis M., Karlsson E., RA Kells C., Kieu A., Kisner P., Kodira C., Kulbokas E., Labutti K., RA Lama D., Landers T., Leger J., Levine S., Lewis D., Lewis T., RA Lindblad-toh K., Liu X., Lokyitsang T., Lokyitsang Y., Lucien O., RA Lui A., Ma L.J., Mabbitt R., Macdonald J., Maclean C., Major J., RA Manning J., Marabella R., Maru K., Matthews C., Mauceli E., RA Mccarthy M., Mcdonough S., Mcghee T., Meldrim J., Meneus L., RA Mesirov J., Mihalev A., Mihova T., Mikkelsen T., Mlenga V., Moru K., RA Mozes J., Mulrain L., Munson G., Naylor J., Newes C., Nguyen C., RA Nguyen N., Nguyen T., Nicol R., Nielsen C., Nizzari M., Norbu C., RA Norbu N., O'donnell P., Okoawo O., O'leary S., Omotosho B., RA O'neill K., Osman S., Parker S., Perrin D., Phunkhang P., Piqani B., RA Purcell S., Rachupka T., Ramasamy U., Rameau R., Ray V., Raymond C., RA Retta R., Richardson S., Rise C., Rodriguez J., Rogers J., Rogov P., RA Rutman M., Schupbach R., Seaman C., Settipalli S., Sharpe T., RA Sheridan J., Sherpa N., Shi J., Smirnov S., Smith C., Sougnez C., RA Spencer B., Stalker J., Stange-thomann N., Stavropoulos S., RA Stetson K., Stone C., Stone S., Stubbs M., Talamas J., Tchuinga P., RA Tenzing P., Tesfaye S., Theodore J., Thoulutsang Y., Topham K., RA Towey S., Tsamla T., Tsomo N., Vallee D., Vassiliev H., RA Venkataraman V., Vinson J., Vo A., Wade C., Wang S., Wangchuk T., RA Wangdi T., Whittaker C., Wilkinson J., Wu Y., Wyman D., Yadav S., RA Yang S., Yang X., Yeager S., Yee E., Young G., Zainoun J., Zembeck L., RA Zimmer A., Zody M., Lander E.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCSAVP00000013279} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSCSAVP00000013279}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSCSAVT00000013429; ENSCSAVP00000013279; ENSCSAVG00000007792. DR GeneTree; ENSGT00420000029824; -. DR Proteomes; UP000007875; Unassembled WGS sequence. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007875}; KW Reference proteome {ECO:0000313|Proteomes:UP000007875}. FT NON_TER 1 1 {ECO:0000313|Ensembl: FT ENSCSAVP00000013279}. SQ SEQUENCE 381 AA; 41087 MW; 6E0AD290A9F04A55 CRC64; TAIEIEATLK QRIMVFDGGM GTMIQNLRLE EQDFRGSQFI DHPKSLKGNN DLLSITKPDS IYEIHKAYLE AGADFIETNT FSGTSIAQAD YALEAFVYQL NFESARIAKK AAVDVTNATG VKRYVAGSIG PTNKTLSVSP SVERPEYRNI TFDELVVAYS EQTRGLLDGG SDVLLVETIF DTANAKAALF AIQEVLDEEK YSPLRGIPIF VSGTIVDKSG RTLSGQTGEA FVISVSHAKP MCLGLNCALG AVEMRPFIEV IGNFTDAYVI CYPNAGLPNT FAKYLAVSIC SFFAASGLVN IVGGCCGTTP EHIKAIADAV RPHKPRTPPN NPHKGCLLLS GLEPAVISSI TNFVNIGERC NVAGSRRFAR LVQNGKYEAA L // ID H2Z6R8_CIOSA Unreviewed; 1160 AA. AC H2Z6R8; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCSAVP00000013280}; DE Flags: Fragment; OS Ciona savignyi (Pacific transparent sea squirt). OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Enterogona; OC Phlebobranchia; Cionidae; Ciona. OX NCBI_TaxID=51511 {ECO:0000313|Ensembl:ENSCSAVP00000013280, ECO:0000313|Proteomes:UP000007875}; RN [1] {ECO:0000313|Ensembl:ENSCSAVP00000013280} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Birren B., Nusbaum C., Abebe A., Abouelleil A., Adekoya E., RA Ait-zahra M., Allen N., Allen T., An P., Anderson M., Anderson S., RA Arachchi H., Armbruster J., Bachantsang P., Baldwin J., Barry A., RA Bayul T., Blitshsteyn B., Bloom T., Blye J., Boguslavskiy L., RA Borowsky M., Boukhgalter B., Brunache A., Butler J., Calixte N., RA Calvo S., Camarata J., Campo K., Chang J., Cheshatsang Y., Citroen M., RA Collymore A., Considine T., Cook A., Cooke P., Corum B., Cuomo C., RA David R., Dawoe T., Degray S., Dodge S., Dooley K., Dorje P., RA Dorjee K., Dorris L., Duffey N., Dupes A., Elkins T., Engels R., RA Erickson J., Farina A., Faro S., Ferreira P., Fischer H., RA Fitzgerald M., Foley K., Gage D., Galagan J., Gearin G., Gnerre S., RA Gnirke A., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., RA Hagopian D., Hagos B., Hall J., Hatcher B., Heller A., Higgins H., RA Honan T., Horn A., Houde N., Hughes L., Hulme W., Husby E., Iliev I., RA Jaffe D., Jones C., Kamal M., Kamat A., Kamvysselis M., Karlsson E., RA Kells C., Kieu A., Kisner P., Kodira C., Kulbokas E., Labutti K., RA Lama D., Landers T., Leger J., Levine S., Lewis D., Lewis T., RA Lindblad-toh K., Liu X., Lokyitsang T., Lokyitsang Y., Lucien O., RA Lui A., Ma L.J., Mabbitt R., Macdonald J., Maclean C., Major J., RA Manning J., Marabella R., Maru K., Matthews C., Mauceli E., RA Mccarthy M., Mcdonough S., Mcghee T., Meldrim J., Meneus L., RA Mesirov J., Mihalev A., Mihova T., Mikkelsen T., Mlenga V., Moru K., RA Mozes J., Mulrain L., Munson G., Naylor J., Newes C., Nguyen C., RA Nguyen N., Nguyen T., Nicol R., Nielsen C., Nizzari M., Norbu C., RA Norbu N., O'donnell P., Okoawo O., O'leary S., Omotosho B., RA O'neill K., Osman S., Parker S., Perrin D., Phunkhang P., Piqani B., RA Purcell S., Rachupka T., Ramasamy U., Rameau R., Ray V., Raymond C., RA Retta R., Richardson S., Rise C., Rodriguez J., Rogers J., Rogov P., RA Rutman M., Schupbach R., Seaman C., Settipalli S., Sharpe T., RA Sheridan J., Sherpa N., Shi J., Smirnov S., Smith C., Sougnez C., RA Spencer B., Stalker J., Stange-thomann N., Stavropoulos S., RA Stetson K., Stone C., Stone S., Stubbs M., Talamas J., Tchuinga P., RA Tenzing P., Tesfaye S., Theodore J., Thoulutsang Y., Topham K., RA Towey S., Tsamla T., Tsomo N., Vallee D., Vassiliev H., RA Venkataraman V., Vinson J., Vo A., Wade C., Wang S., Wangchuk T., RA Wangdi T., Whittaker C., Wilkinson J., Wu Y., Wyman D., Yadav S., RA Yang S., Yang X., Yeager S., Yee E., Young G., Zainoun J., Zembeck L., RA Zimmer A., Zody M., Lander E.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCSAVP00000013280} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 1}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSCSAVP00000013280}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSCSAVT00000013430; ENSCSAVP00000013280; ENSCSAVG00000007792. DR GeneTree; ENSGT00420000029824; -. DR Proteomes; UP000007875; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007875}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007875}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 237 237 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 301 301 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 752 752 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. FT NON_TER 1 1 {ECO:0000313|Ensembl: FT ENSCSAVP00000013280}. SQ SEQUENCE 1160 AA; 127614 MW; FECEF662A58A8F1F CRC64; AIEIEATLKQ RIMVFDGGMG TMIQNLRLEE QDFRGSQFID HPKSLKGNND LLSITKPDSI YEIHKAYLEA GADFIETNTF SGTSIAQADY ALEAFVYQLN FESARIAKKA AVDVTNATVK RYVAGSIGPT NKTLSVSPSK TFDELVVAYS EQTRGLLDGG SDVLLVETIF DTANAKAALF AIQEVLDEEK YSPLRGIPIF VSGTIVDKSG RTLSGQTGEA FVISVSHAKP MCLGLNCALG AVEMRPFIEV IGNFTDAYVI CYPNAGLPNT FGGYDETPAT TAKYLAEFAA SGLVNIVGGC CGTTPEHIKA IADAVRPHKP RTPPNNPHKG CLLLSGLEPA VISSITNFVN IGERCNVAGS RRFARLVQNG KYEAALDVAR SQVEMGAQIL DINMDEGMLD GKSVMPKFIN LIGSEPDVSK VPLCVDSSNF DIVVAGLKCT QGKCIVNSIS LKEGEEDFIN KAKLIKRFGA AVVVMAFDED GQATSSEDKV RICTRSFRVL VDQIGFEPND IIFDPNILTI GTGMEEHNEY AINFIAATRI IKKNLPGCRI SGGLSNLSFS FRGMERIREA MHSVFLYHAI SAGMDMGIVN AGNLPVYDDI PKDLLKYCED LIWNKNAEAT ETLLKYAQEH SGGGNKAVES EEWRSWEVED RLQHSLVKGI DKYVIEDTKE CQENTEKYPR ALNVIERPLM KGMSIVGDLF GAGKMFLPQV IKSARVMKKA VGYLIPIMEE EKRASNRFAG TVVIATVKGD VHDIGKNIVA VVLGCNNYRV IDLGVMTPCE KILQTAVENN ADIIGLSGLI TPSLSEMIHV AKEMERLEMK IPLLIGGATT SRTHTAVKIS PRYSQPTIHV LDASKSVVVV SYDVRTDHYD SLLERKFLTI ADARSKSKRQ PLSIDWTSSP ITEPKFIGNK VFHDFNIEKL VPYIDWKPFF DVWQLRGKYP NRGYPKIFKD KTNMLQKIVD DGLYTMEGVV SFYPANSVGD DIHVYAEDVT PRPTTPLAVF YGLRQQPYYC LSDFIAPRVS GVHDYIGLFA VSCCGAQQLC AQFERNLDDY SSIMAKALAD RLAEAFAEAM HEIVRTTLWP YSSSESLEAG DLHKIKYQGI RPAPGYPSQP DHTEKLTMWE VMGVSESIGT KLTESLAMDP PASVSGLYFA NENAKYFAVG // ID H2ZFT2_CIOSA Unreviewed; 376 AA. AC H2ZFT2; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCSAVP00000016448}; GN Name=Csa.1410 {ECO:0000313|Ensembl:ENSCSAVP00000016448}; OS Ciona savignyi (Pacific transparent sea squirt). OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Enterogona; OC Phlebobranchia; Cionidae; Ciona. OX NCBI_TaxID=51511 {ECO:0000313|Ensembl:ENSCSAVP00000016448, ECO:0000313|Proteomes:UP000007875}; RN [1] {ECO:0000313|Ensembl:ENSCSAVP00000016448} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Birren B., Nusbaum C., Abebe A., Abouelleil A., Adekoya E., RA Ait-zahra M., Allen N., Allen T., An P., Anderson M., Anderson S., RA Arachchi H., Armbruster J., Bachantsang P., Baldwin J., Barry A., RA Bayul T., Blitshsteyn B., Bloom T., Blye J., Boguslavskiy L., RA Borowsky M., Boukhgalter B., Brunache A., Butler J., Calixte N., RA Calvo S., Camarata J., Campo K., Chang J., Cheshatsang Y., Citroen M., RA Collymore A., Considine T., Cook A., Cooke P., Corum B., Cuomo C., RA David R., Dawoe T., Degray S., Dodge S., Dooley K., Dorje P., RA Dorjee K., Dorris L., Duffey N., Dupes A., Elkins T., Engels R., RA Erickson J., Farina A., Faro S., Ferreira P., Fischer H., RA Fitzgerald M., Foley K., Gage D., Galagan J., Gearin G., Gnerre S., RA Gnirke A., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., RA Hagopian D., Hagos B., Hall J., Hatcher B., Heller A., Higgins H., RA Honan T., Horn A., Houde N., Hughes L., Hulme W., Husby E., Iliev I., RA Jaffe D., Jones C., Kamal M., Kamat A., Kamvysselis M., Karlsson E., RA Kells C., Kieu A., Kisner P., Kodira C., Kulbokas E., Labutti K., RA Lama D., Landers T., Leger J., Levine S., Lewis D., Lewis T., RA Lindblad-toh K., Liu X., Lokyitsang T., Lokyitsang Y., Lucien O., RA Lui A., Ma L.J., Mabbitt R., Macdonald J., Maclean C., Major J., RA Manning J., Marabella R., Maru K., Matthews C., Mauceli E., RA Mccarthy M., Mcdonough S., Mcghee T., Meldrim J., Meneus L., RA Mesirov J., Mihalev A., Mihova T., Mikkelsen T., Mlenga V., Moru K., RA Mozes J., Mulrain L., Munson G., Naylor J., Newes C., Nguyen C., RA Nguyen N., Nguyen T., Nicol R., Nielsen C., Nizzari M., Norbu C., RA Norbu N., O'donnell P., Okoawo O., O'leary S., Omotosho B., RA O'neill K., Osman S., Parker S., Perrin D., Phunkhang P., Piqani B., RA Purcell S., Rachupka T., Ramasamy U., Rameau R., Ray V., Raymond C., RA Retta R., Richardson S., Rise C., Rodriguez J., Rogers J., Rogov P., RA Rutman M., Schupbach R., Seaman C., Settipalli S., Sharpe T., RA Sheridan J., Sherpa N., Shi J., Smirnov S., Smith C., Sougnez C., RA Spencer B., Stalker J., Stange-thomann N., Stavropoulos S., RA Stetson K., Stone C., Stone S., Stubbs M., Talamas J., Tchuinga P., RA Tenzing P., Tesfaye S., Theodore J., Thoulutsang Y., Topham K., RA Towey S., Tsamla T., Tsomo N., Vallee D., Vassiliev H., RA Venkataraman V., Vinson J., Vo A., Wade C., Wang S., Wangchuk T., RA Wangdi T., Whittaker C., Wilkinson J., Wu Y., Wyman D., Yadav S., RA Yang S., Yang X., Yeager S., Yee E., Young G., Zainoun J., Zembeck L., RA Zimmer A., Zody M., Lander E.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCSAVP00000016448} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSCSAVP00000016448}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSCSAVT00000016629; ENSCSAVP00000016448; ENSCSAVG00000009672. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; H2ZFT2; -. DR OMA; NINEAAC; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR Proteomes; UP000007875; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007875}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000007875}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 216 216 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 301 301 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 376 AA; 41548 MW; 750873213ECC8A4D CRC64; MDKNAQSKKG LLERLKEGPV VGDGSMCTTL EKRGYCRAGP WTPEAVLLYP DAVKQLLREY MRAGADVLQT PCFYCNDGKL KNVSQSGESI SYSTEAINEA ACRIAHEIAN EGDDMLVCGG LSPVLSYGRE RNMEKARAEF DSQLNVFIKH KVDFVLAEFF GHVEELEICV DVMKRSKMPI ACTMRIGPLG DSNGVSVEEC AVRMARTGAD LIGINCMYDF NTCLKTLKRM QNALDKEGLK TYLMCQPLGW RCPEVENSLI GYADLPETPL ALEPRQATRF EAHAFARAAY DLGVRYIGGC CGMEPHHIRA IAQELSSERK KNPAVDDMCP ALGFLEHSQV TTIHKKVNKA YWMGQKPGSG RPFSPASSFT QGGAYT // ID H2ZJR6_CIOSA Unreviewed; 302 AA. AC H2ZJR6; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCSAVP00000017832}; OS Ciona savignyi (Pacific transparent sea squirt). OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Enterogona; OC Phlebobranchia; Cionidae; Ciona. OX NCBI_TaxID=51511 {ECO:0000313|Ensembl:ENSCSAVP00000017832, ECO:0000313|Proteomes:UP000007875}; RN [1] {ECO:0000313|Ensembl:ENSCSAVP00000017832} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Birren B., Nusbaum C., Abebe A., Abouelleil A., Adekoya E., RA Ait-zahra M., Allen N., Allen T., An P., Anderson M., Anderson S., RA Arachchi H., Armbruster J., Bachantsang P., Baldwin J., Barry A., RA Bayul T., Blitshsteyn B., Bloom T., Blye J., Boguslavskiy L., RA Borowsky M., Boukhgalter B., Brunache A., Butler J., Calixte N., RA Calvo S., Camarata J., Campo K., Chang J., Cheshatsang Y., Citroen M., RA Collymore A., Considine T., Cook A., Cooke P., Corum B., Cuomo C., RA David R., Dawoe T., Degray S., Dodge S., Dooley K., Dorje P., RA Dorjee K., Dorris L., Duffey N., Dupes A., Elkins T., Engels R., RA Erickson J., Farina A., Faro S., Ferreira P., Fischer H., RA Fitzgerald M., Foley K., Gage D., Galagan J., Gearin G., Gnerre S., RA Gnirke A., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., RA Hagopian D., Hagos B., Hall J., Hatcher B., Heller A., Higgins H., RA Honan T., Horn A., Houde N., Hughes L., Hulme W., Husby E., Iliev I., RA Jaffe D., Jones C., Kamal M., Kamat A., Kamvysselis M., Karlsson E., RA Kells C., Kieu A., Kisner P., Kodira C., Kulbokas E., Labutti K., RA Lama D., Landers T., Leger J., Levine S., Lewis D., Lewis T., RA Lindblad-toh K., Liu X., Lokyitsang T., Lokyitsang Y., Lucien O., RA Lui A., Ma L.J., Mabbitt R., Macdonald J., Maclean C., Major J., RA Manning J., Marabella R., Maru K., Matthews C., Mauceli E., RA Mccarthy M., Mcdonough S., Mcghee T., Meldrim J., Meneus L., RA Mesirov J., Mihalev A., Mihova T., Mikkelsen T., Mlenga V., Moru K., RA Mozes J., Mulrain L., Munson G., Naylor J., Newes C., Nguyen C., RA Nguyen N., Nguyen T., Nicol R., Nielsen C., Nizzari M., Norbu C., RA Norbu N., O'donnell P., Okoawo O., O'leary S., Omotosho B., RA O'neill K., Osman S., Parker S., Perrin D., Phunkhang P., Piqani B., RA Purcell S., Rachupka T., Ramasamy U., Rameau R., Ray V., Raymond C., RA Retta R., Richardson S., Rise C., Rodriguez J., Rogers J., Rogov P., RA Rutman M., Schupbach R., Seaman C., Settipalli S., Sharpe T., RA Sheridan J., Sherpa N., Shi J., Smirnov S., Smith C., Sougnez C., RA Spencer B., Stalker J., Stange-thomann N., Stavropoulos S., RA Stetson K., Stone C., Stone S., Stubbs M., Talamas J., Tchuinga P., RA Tenzing P., Tesfaye S., Theodore J., Thoulutsang Y., Topham K., RA Towey S., Tsamla T., Tsomo N., Vallee D., Vassiliev H., RA Venkataraman V., Vinson J., Vo A., Wade C., Wang S., Wangchuk T., RA Wangdi T., Whittaker C., Wilkinson J., Wu Y., Wyman D., Yadav S., RA Yang S., Yang X., Yeager S., Yee E., Young G., Zainoun J., Zembeck L., RA Zimmer A., Zody M., Lander E.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCSAVP00000017832} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSCSAVP00000017832}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSCSAVT00000018026; ENSCSAVP00000017832; ENSCSAVG00000010494. DR GeneTree; ENSGT00510000049619; -. DR InParanoid; H2ZJR6; -. DR OMA; SYIGKWR; -. DR OrthoDB; EOG7GQXW0; -. DR TreeFam; TF313927; -. DR Proteomes; UP000007875; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007875}; KW Reference proteome {ECO:0000313|Proteomes:UP000007875}. SQ SEQUENCE 302 AA; 33392 MW; B06BDDEA37875F8F CRC64; MQDIKILDGG LCTDLFFNGG FDRATVNNDP LWSSRIIYED PNAIKSSHLR FINAGCDVIS TCSYQASVKG YVEHAGLTEE KAEDVIGSSV DVAKQAVKES GRNVLVAGSI SPYGTILHDM SEYTGSYIDT TSEKELCEFH RQNVRILATK EVDFLAFETL PSLKEAVVLA ELLKEYPSLK AWVSFTTKDG VHTSYGEPFT EVFKTLAGYK QVEAVGLNCC SFKCVSSLLS VAKNNMAKHQ KLIIYPNNLD YGPSRTGPLD WLPEVKPWLE SNLIGYIGGC CMTLPNHVAE IKQAVVEWQV QK // ID H2ZQK5_CIOSA Unreviewed; 300 AA. AC H2ZQK5; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCSAVP00000019871}; DE Flags: Fragment; OS Ciona savignyi (Pacific transparent sea squirt). OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Enterogona; OC Phlebobranchia; Cionidae; Ciona. OX NCBI_TaxID=51511 {ECO:0000313|Ensembl:ENSCSAVP00000019871, ECO:0000313|Proteomes:UP000007875}; RN [1] {ECO:0000313|Ensembl:ENSCSAVP00000019871} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Birren B., Nusbaum C., Abebe A., Abouelleil A., Adekoya E., RA Ait-zahra M., Allen N., Allen T., An P., Anderson M., Anderson S., RA Arachchi H., Armbruster J., Bachantsang P., Baldwin J., Barry A., RA Bayul T., Blitshsteyn B., Bloom T., Blye J., Boguslavskiy L., RA Borowsky M., Boukhgalter B., Brunache A., Butler J., Calixte N., RA Calvo S., Camarata J., Campo K., Chang J., Cheshatsang Y., Citroen M., RA Collymore A., Considine T., Cook A., Cooke P., Corum B., Cuomo C., RA David R., Dawoe T., Degray S., Dodge S., Dooley K., Dorje P., RA Dorjee K., Dorris L., Duffey N., Dupes A., Elkins T., Engels R., RA Erickson J., Farina A., Faro S., Ferreira P., Fischer H., RA Fitzgerald M., Foley K., Gage D., Galagan J., Gearin G., Gnerre S., RA Gnirke A., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., RA Hagopian D., Hagos B., Hall J., Hatcher B., Heller A., Higgins H., RA Honan T., Horn A., Houde N., Hughes L., Hulme W., Husby E., Iliev I., RA Jaffe D., Jones C., Kamal M., Kamat A., Kamvysselis M., Karlsson E., RA Kells C., Kieu A., Kisner P., Kodira C., Kulbokas E., Labutti K., RA Lama D., Landers T., Leger J., Levine S., Lewis D., Lewis T., RA Lindblad-toh K., Liu X., Lokyitsang T., Lokyitsang Y., Lucien O., RA Lui A., Ma L.J., Mabbitt R., Macdonald J., Maclean C., Major J., RA Manning J., Marabella R., Maru K., Matthews C., Mauceli E., RA Mccarthy M., Mcdonough S., Mcghee T., Meldrim J., Meneus L., RA Mesirov J., Mihalev A., Mihova T., Mikkelsen T., Mlenga V., Moru K., RA Mozes J., Mulrain L., Munson G., Naylor J., Newes C., Nguyen C., RA Nguyen N., Nguyen T., Nicol R., Nielsen C., Nizzari M., Norbu C., RA Norbu N., O'donnell P., Okoawo O., O'leary S., Omotosho B., RA O'neill K., Osman S., Parker S., Perrin D., Phunkhang P., Piqani B., RA Purcell S., Rachupka T., Ramasamy U., Rameau R., Ray V., Raymond C., RA Retta R., Richardson S., Rise C., Rodriguez J., Rogers J., Rogov P., RA Rutman M., Schupbach R., Seaman C., Settipalli S., Sharpe T., RA Sheridan J., Sherpa N., Shi J., Smirnov S., Smith C., Sougnez C., RA Spencer B., Stalker J., Stange-thomann N., Stavropoulos S., RA Stetson K., Stone C., Stone S., Stubbs M., Talamas J., Tchuinga P., RA Tenzing P., Tesfaye S., Theodore J., Thoulutsang Y., Topham K., RA Towey S., Tsamla T., Tsomo N., Vallee D., Vassiliev H., RA Venkataraman V., Vinson J., Vo A., Wade C., Wang S., Wangchuk T., RA Wangdi T., Whittaker C., Wilkinson J., Wu Y., Wyman D., Yadav S., RA Yang S., Yang X., Yeager S., Yee E., Young G., Zainoun J., Zembeck L., RA Zimmer A., Zody M., Lander E.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCSAVP00000019871} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSCSAVP00000019871}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSCSAVT00000020084; ENSCSAVP00000019871; ENSCSAVG00000011671. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; H2ZQK5; -. DR OMA; KAHYMSQ; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR Proteomes; UP000007875; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007875}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000007875}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 201 201 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT NON_TER 1 1 {ECO:0000313|Ensembl: FT ENSCSAVP00000019871}. SQ SEQUENCE 300 AA; 33010 MW; FEB422DD5AB18584 CRC64; CPAKSSMSGI LHRLSNGPFV GDGSVLLTLE KRGYCRAGAW TPEAVIQYPE AVRQLLREYV RAGADAIQAP CFNFTEGSWK TGADKINEAA CNIAREVATE NGALVYASVG PVADFVRGKN ETDTRQSFQK LLNLYLKNKV DYFYFAHIEE LEICVEVLKK SKLPVACTMR IGPTGDLDGV SVENCAIRMA KTGADIIGIN CLYDPVTALK TMKRIKDAVK DVGLSPYLMC QPLGWMCPEV ENQKMGYLAL PEFPFALDSR SVTRFEFGKF ARKAFEMGVQ YIGGCCGAEP HHIRAIAQEV // ID H3APQ5_LATCH Unreviewed; 301 AA. AC H3APQ5; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSLACP00000011626}; GN Name=LOC102347529 {ECO:0000313|Ensembl:ENSLACP00000011626}; OS Latimeria chalumnae (West Indian ocean coelacanth). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Coelacanthiformes; Coelacanthidae; Latimeria. OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000011626, ECO:0000313|Proteomes:UP000008672}; RN [1] {ECO:0000313|Ensembl:ENSLACP00000011626} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D., RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.; RT "The draft genome of Latimeria chalumnae."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSLACP00000011626} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSLACP00000011626}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFYH01057220; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AFYH01057221; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AFYH01057222; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AFYH01057223; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_005994548.1; XM_005994486.1. DR Ensembl; ENSLACT00000011715; ENSLACP00000011626; ENSLACG00000010232. DR GeneID; 102347529; -. DR GeneTree; ENSGT00510000049619; -. DR InParanoid; H3APQ5; -. DR OMA; HWTFPAN; -. DR OrthoDB; EOG7GQXW0; -. DR TreeFam; TF313927; -. DR Proteomes; UP000008672; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008672}; KW Reference proteome {ECO:0000313|Proteomes:UP000008672}. SQ SEQUENCE 301 AA; 33175 MW; AF7A3391B76268C0 CRC64; MSEVKILDGG FATELEAAGF HLQDDPLWSA RILHTNPQAI KDVHARFLSG GADVISTATY QATVEGFVRH LGVSSEDAVQ LLHLAVTLAK EAVEEFCSQN KERKLLIAGS VGPYGAFLHD GSEYTGSYVD LMSIEEIKAW HRVQIQPLVS AGVDLIAMET IPSQKEGEAL VELLREFPNT VSWLSFSCKD EQHTHHGEKF EEAVKIVNKS RNLVAVGVNC CAPTLISPLL TAANKNKNPD IDWIVYPNSG EEWKRSSGWQ GRKIKNPLTV SALRWKELGA KWIGGCCRTT PSDISELRNI L // ID H3APQ6_LATCH Unreviewed; 277 AA. AC H3APQ6; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSLACP00000011627}; DE Flags: Fragment; GN Name=LOC102347529 {ECO:0000313|Ensembl:ENSLACP00000011627}; OS Latimeria chalumnae (West Indian ocean coelacanth). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Coelacanthiformes; Coelacanthidae; Latimeria. OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000011627, ECO:0000313|Proteomes:UP000008672}; RN [1] {ECO:0000313|Ensembl:ENSLACP00000011627} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D., RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.; RT "The draft genome of Latimeria chalumnae."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSLACP00000011627} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSLACP00000011627}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFYH01057220; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AFYH01057221; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AFYH01057222; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AFYH01057223; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSLACT00000011716; ENSLACP00000011627; ENSLACG00000010232. DR GeneTree; ENSGT00510000049619; -. DR Proteomes; UP000008672; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008672}; KW Reference proteome {ECO:0000313|Proteomes:UP000008672}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSLACP00000011627}. SQ SEQUENCE 277 AA; 30213 MW; CD35EEF94B253706 CRC64; ILDGGFATEL EAAGFHLQDD PLWSARILHT NPQAIKDVHA RFLSGGADVI STATYQATVE GFVRHLGVSS EDAVQLLHLA VTLAKEAVEE FCSQNKVNLV GKGKRTLIVG NWIIVGCTVA QRKLLIAGSV GPYGAFLHDG SEYTGSYVDL MSIEEIKAWH RVQIQPLVSA GVDLIAMETI PSQKEGEALV ELLREFPNTV SWLSFSCKDE QHTHHGEKFE EAVKIVNKSR NLVAVGVNCC APTLISPLLT AANKNKNPDI DWIVYPNSGE EWKRSSG // ID H3B9U9_LATCH Unreviewed; 1252 AA. AC H3B9U9; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSLACP00000018670}; DE Flags: Fragment; GN Name=MTR {ECO:0000313|Ensembl:ENSLACP00000018670}; OS Latimeria chalumnae (West Indian ocean coelacanth). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Coelacanthiformes; Coelacanthidae; Latimeria. OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000018670, ECO:0000313|Proteomes:UP000008672}; RN [1] {ECO:0000313|Ensembl:ENSLACP00000018670} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D., RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.; RT "The draft genome of Latimeria chalumnae."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSLACP00000018670} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 1}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSLACP00000018670}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFYH01020934; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AFYH01020935; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AFYH01020936; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AFYH01020937; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AFYH01020938; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AFYH01020939; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AFYH01020940; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AFYH01020941; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AFYH01020942; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AFYH01020943; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AFYH01020944; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AFYH01020945; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AFYH01020946; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AFYH01020947; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AFYH01020948; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSLACT00000018803; ENSLACP00000018670; ENSLACG00000016440. DR GeneTree; ENSGT00420000029824; -. DR InParanoid; H3B9U9; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG7TF786; -. DR TreeFam; TF312829; -. DR Proteomes; UP000008672; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008672}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008672}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 773 773 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSLACP00000018670}. SQ SEQUENCE 1252 AA; 138656 MW; 189BAD6711850D3C CRC64; AGAKNGLRDE IESVLRERIM VLDGGMGTMI QQRRLEEEDF RGEEFKDHPK SLKGNNDLLS VTCPGIVYSI HKDYLMAGAD IVETNTFSGT RVAQADYGLG HLAYRLNKAS AELAKKAATE VTALTGIKRF VAGAIGPTNR TLSVSPSVER PDYRNITFDE LVEAYEEQTR GLLDGGADVL LVETIFDTAN AKAAVFAIDK LFEEYEPRPI FISGTIVDKS GRTLSGQTGE AFVISMSHAQ PLCIGLNCAL GAAEMRPFIE AIGNCTTSYV ICYPNAGLPN TFGDYDETPE RTAKHLKEFA LDGLVNIVGG CCGTTPAHIR EVAKAVRNCK PRVPPSSVFE GYMLLSGLEP FRIGPYTNFV NIGERCNVAG SRRFAKLIKA GNYEEALSIA KSQVELGAQV LDINMDEGML DGKSAMTRFC NLIASEPDIA KMPLCIDSSN FSVIEAGLKC CQGKCIVNSI SLKEGEQEFL ERTQTIKRFG AAVVVMAFDE EGQATETERK VQVCARAYSL LVEKVGFNPH DIIFDPNILT IGTGMEEHNS YAVNFIRATT NIKETLPGAR VSGGLSNLSF SFRGMEAIRE AMHGVFLYHA IKSGMDMGIV NAGNLPVYDD IDKVLLELCE NLIWNKDPEA TEKLLHYSQT CAKGGKRVIQ TDDWRSKSVE ERLEYALVKG IEKYVVEDTE EARANHEKYP RPLNVIEKPL MNGMKMVGDL FGAGKMFLPQ VIKSARVMKK AVSYLIPFME KEREEMMAKS NCTEEVDPYQ GTIVLATVKG DVHDIGKNIV GVVLGCNNFR VIDLGVMTPC DNILRAAVES KADVIGLSGL ITPSLDEMIY VAKEMERLGM KTPLLIGGAT TSKTHTAVKI APRYSAPVIH VLDASKSVVV CSQLLDENLK DDYFEEISEE YEEVRQDHYE SLQDRRYLSL EVARNKGLHI NWMSHPTPGQ FQGVANQIFY EISLEEQQGS ILWQQVIKPY PIRNLFFVCV CVYKPPPPLG EEAKKVFSDA QNLLNTLIDQ KKLQARGVVG FWPAQGVWDD IHVYAEDLVP RSAEPVAVLH GLRQQAEKDS ASTDPYFCLS DFVAPRDSGV PDYVGLFAVA CFGAEELSRK YEKQCDDYSS IMVKALADRL AEAFAEELHE RVRKEFWGYC IDEQLETADM HKIRYTGIRP APGYPSQPDH TEKLAMWKLA NIEETTGIKL TESLAMAPAA AISGLYFSSP RSTYFAVGKI TKEQVEDYAL RKQMAVTEVE KWLGPILGYD TE // ID H3BF72_LATCH Unreviewed; 276 AA. AC H3BF72; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSLACP00000020543}; DE Flags: Fragment; GN Name=BHMT {ECO:0000313|Ensembl:ENSLACP00000020543}; OS Latimeria chalumnae (West Indian ocean coelacanth). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Coelacanthiformes; Coelacanthidae; Latimeria. OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000020543, ECO:0000313|Proteomes:UP000008672}; RN [1] {ECO:0000313|Ensembl:ENSLACP00000020543} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D., RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.; RT "The draft genome of Latimeria chalumnae."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSLACP00000020543} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSLACP00000020543}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFYH01028121; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AFYH01028122; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AFYH01028123; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AFYH01028124; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AFYH01028125; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSLACT00000020683; ENSLACP00000020543; ENSLACG00000018054. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; H3BF72; -. DR OMA; EVKNIFR; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR Proteomes; UP000008672; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008672}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000008672}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 217 217 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSLACP00000020543}. SQ SEQUENCE 276 AA; 30185 MW; EC6466BEA41FB1D1 CRC64; LHPESPIHLS KGILERLDAG EVVVGDGGFV FALEKRGWVR AGPWTPEATV EHPEAVRQLH REFLRAGANV MQTFTFYASE DKLENRGNYV SQKISSQKVN EAACDLAREI AQEGDALVAG GVCQSPSYLS CKSEVEVKNI FRKQLDVFVK KNVDFLIAEY FEHVEEAEWA VHVLKESGKP IASSLCIGPQ GDLNGVPPGE CAVKLVKAGA SIVGVNCHFD PATCLKTVKL MKEGLQAAGV KAHLMIQPLA FHTPDCSQQG FIDLPEFPFG MFHDND // ID H3CJI2_TETNG Unreviewed; 1141 AA. AC H3CJI2; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSTNIP00000008411}; DE Flags: Fragment; OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon OS nigroviridis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; OC Tetraodon. OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000008411, ECO:0000313|Proteomes:UP000007303}; RN [1] {ECO:0000313|Ensembl:ENSTNIP00000008411} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15496914; DOI=10.1038/nature03025; RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N., RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., RA Nicaud S., Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., RA Dasilva C., Salanoubat M., Levy M., Boudet N., Castellano S., RA Anthouard V., Jubin C., Castelli V., Katinka M., Vacherie B., RA Biemont C., Skalli Z., Cattolico L., Poulain J., De Berardinis V., RA Cruaud C., Duprat S., Brottier P., Coutanceau J.-P., Gouzy J., RA Parra G., Lardier G., Chapple C., McKernan K.J., McEwan P., Bosak S., RA Kellis M., Volff J.-N., Guigo R., Zody M.C., Mesirov J., RA Lindblad-Toh K., Birren B., Nusbaum C., Kahn D., Robinson-Rechavi M., RA Laudet V., Schachter V., Quetier F., Saurin W., Scarpelli C., RA Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.; RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals RT the early vertebrate proto-karyotype."; RL Nature 431:946-957(2004). RN [2] {ECO:0000313|Ensembl:ENSTNIP00000008411} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 1}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSTNIP00000008411}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAAE01012111; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CAAE01013712; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSTNIT00000008578; ENSTNIP00000008411; ENSTNIG00000005701. DR GeneTree; ENSGT00420000029824; -. DR InParanoid; H3CJI2; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG7TF786; -. DR TreeFam; TF312829; -. DR Proteomes; UP000007303; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007303}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007303}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 257 257 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 782 782 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSTNIP00000008411}. SQ SEQUENCE 1141 AA; 127110 MW; 2AD0CBE7AB6E002C CRC64; NPRNVASVEP SECPLEPELR GILERRIMIL DGGMGTMIQQ HKLEECNFRG DEFKDHPQPL MGNNDLLSLT CPDIVYKIHK DYLLAGADII ETNTFSGTSV AQADYGLEHM AYRLNKASAE LARKAADDVT SSTGVKRYVA GALGPTNKTL SVSPSVEKPH FRNITFDALV EAYTEQVKGL LDGGVDILLV ETIFDTANAK AALFAIDLLF EKSYSRKPIF ISGTVVDRSG RTLSGQTVEA FVVSVSHAKP LCIGLNCALG ATEMRPFIEA IGKCTTAFVI CYPNAGNPHL FNQYLSDTVR PTHISFNAKE FSVDGLVNIV GGCCGTTPEH IRALCEAVKM CQPRVAPAEM YKDYMMLSGL EPFKVGPYTN FVNIGERCNV AGSRKFAKLI TSGLYEVRLA SRNHFSRPSM LLFDSDLING CLFFFRSCFY SEKTSEIRKV PLCIDSSNFS VIEAGLKCCQ GKCIVNSISL KEGESDFLDK AASVKRYGAA VVVMAFDEHG QATDTDRKVE ICTRAYQLLL TKVGFKPNDI IFDPNILTIG TGIEEHSEYA INFIKATKLI KETLPGARVS GGLSNLSFSF RGMEVIREAM HGVFLYHAIK SSVQINLMTM QRIKMYRPEQ KKILEKNKCK NWQKGIVVSI ILKEKAVFMS TGGTQILATP LMWRSRCMSA FLLKVYSQGV DKYVVEDVKK CQAQVDRYTR PIHIIEGPLM SGMKIVGDLF GPGKMFLPKV IKSARVMKKA VGYLIPFMEK EREDMMTWSV ALMYEDPYMG TIVLATVKGD VHDIGKNIVG VVLSCNNFRV IDLGVMVPCD KILKEAIIHN AEDIIGLSGL ITPSLDEMIH VAKEMERLRM TIPLLIGGAT TSKTHTAVKI APRYAAPVIH VLDASRSVVV CSQLLDEMGK EDYFEDVKQD YEEVRQEHYD SLKVRPVCSS DRKPKGVTFC TLNDCVIFGL RLVTICLLAK PERRLYKMTS CLWPGQFFST MTQMSEDMHN DICLYDYRSI MVKALADRLA EAFAEELHAR VRKEFWAYST TETLQTSDLH QVRYQGIRPA PGYPSQPDHT EKTTMWSLAG IQEKTGIGLT ESFAMTPAAS VSGLYFSSPQ ATYFAVGKIT KEQVDDYSRR KAMKVEEVER WLAPILGYDA E // ID H3D8E0_TETNG Unreviewed; 314 AA. AC H3D8E0; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSTNIP00000016781}; OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon OS nigroviridis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; OC Tetraodon. OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000016781, ECO:0000313|Proteomes:UP000007303}; RN [1] {ECO:0000313|Ensembl:ENSTNIP00000016781} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15496914; DOI=10.1038/nature03025; RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N., RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., RA Nicaud S., Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., RA Dasilva C., Salanoubat M., Levy M., Boudet N., Castellano S., RA Anthouard V., Jubin C., Castelli V., Katinka M., Vacherie B., RA Biemont C., Skalli Z., Cattolico L., Poulain J., De Berardinis V., RA Cruaud C., Duprat S., Brottier P., Coutanceau J.-P., Gouzy J., RA Parra G., Lardier G., Chapple C., McKernan K.J., McEwan P., Bosak S., RA Kellis M., Volff J.-N., Guigo R., Zody M.C., Mesirov J., RA Lindblad-Toh K., Birren B., Nusbaum C., Kahn D., Robinson-Rechavi M., RA Laudet V., Schachter V., Quetier F., Saurin W., Scarpelli C., RA Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.; RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals RT the early vertebrate proto-karyotype."; RL Nature 431:946-957(2004). RN [2] {ECO:0000313|Ensembl:ENSTNIP00000016781} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSTNIP00000016781}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAAE01014770; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSTNIT00000016995; ENSTNIP00000016781; ENSTNIG00000013779. DR GeneTree; ENSGT00510000049619; -. DR InParanoid; H3D8E0; -. DR OMA; YGRSVTK; -. DR OrthoDB; EOG7GQXW0; -. DR TreeFam; TF313927; -. DR Proteomes; UP000007303; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007303}; KW Reference proteome {ECO:0000313|Proteomes:UP000007303}. SQ SEQUENCE 314 AA; 34009 MW; 8546FC14DA98F6B0 CRC64; MAETNNVKDG GLATDLEAQG VHLQGDPLWS ARLLYTNPQA IRDAHCRFLL SGADVISTAT YQASVEGFMD HLNVSSEGAK ELIMSGVQLA KEAVERLKGR RCPLVAGSLG PYGAFLHNGS EYTGDYAEKM SVQELKAWHR PQVECLAAAE ADVLAFETIP SIKEAEALVE LLKEFPNTKA WLSLSCKDVK RLSDGSLFRD AVQIANRSEQ LIAVGVNCCP PELVEPLLDS ARTLLSPEIS WVVYPNSGES WDPEQGWCTS EAALPALLEM SGTWVKQGAA LIGGCCRISP AHVAKLRRHL KGSRGSPTSE PRPK // ID H3DH20_TETNG Unreviewed; 398 AA. AC H3DH20; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSTNIP00000019814}; DE Flags: Fragment; OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon OS nigroviridis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; OC Tetraodon. OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000019814, ECO:0000313|Proteomes:UP000007303}; RN [1] {ECO:0000313|Ensembl:ENSTNIP00000019814} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15496914; DOI=10.1038/nature03025; RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N., RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., RA Nicaud S., Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., RA Dasilva C., Salanoubat M., Levy M., Boudet N., Castellano S., RA Anthouard V., Jubin C., Castelli V., Katinka M., Vacherie B., RA Biemont C., Skalli Z., Cattolico L., Poulain J., De Berardinis V., RA Cruaud C., Duprat S., Brottier P., Coutanceau J.-P., Gouzy J., RA Parra G., Lardier G., Chapple C., McKernan K.J., McEwan P., Bosak S., RA Kellis M., Volff J.-N., Guigo R., Zody M.C., Mesirov J., RA Lindblad-Toh K., Birren B., Nusbaum C., Kahn D., Robinson-Rechavi M., RA Laudet V., Schachter V., Quetier F., Saurin W., Scarpelli C., RA Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.; RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals RT the early vertebrate proto-karyotype."; RL Nature 431:946-957(2004). RN [2] {ECO:0000313|Ensembl:ENSTNIP00000019814} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSTNIP00000019814}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAAE01015007; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSTNIT00000020044; ENSTNIP00000019814; ENSTNIG00000016705. DR GeneTree; ENSGT00390000003122; -. DR InParanoid; H3DH20; -. DR OMA; WGVTKGT; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR Proteomes; UP000007303; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007303}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000007303}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 211 211 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSTNIP00000019814}. SQ SEQUENCE 398 AA; 44144 MW; C5276EE39653B501 CRC64; QRVGKAQGIL ERLNAGEIVI GDGGFVFALE KRGYVKAGPW TPEATKEHPE AVRQLHREFL RAGANVMQTF TFYASDDKLE NRGNKVTYTG VQINEAACDL AREVANEGDA LVAGGVCQTP SYLSCKSEKE VKDIFKRQLD VFVKKNVDFL IAEYFEHVEE AVWAVEVLKT TGKPVAASLC IGPKGDMHGV SPGECAVRLV KAGAQIVGVN CHFDPMTCVE TVKLMKEGVE KAGLKAHYMV QPLAFHTPDC NCQGFIDLPE FPFGLEPRIL TRWDMHKYAR EAYNAGIRFI GGCCGFEPYH IRALAEELAP ERGFLPVGSD KHGNWGAGLE MHTKPWVRAR ARRDYWEALK PASGRPLCPS LSTPDCWGVT KGDTELMQQK EATSKEQLKQ LFDRSKSH // ID H3DQ69_TETNG Unreviewed; 163 AA. AC H3DQ69; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSTNIP00000022668}; DE Flags: Fragment; OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon OS nigroviridis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; OC Tetraodon. OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000022668, ECO:0000313|Proteomes:UP000007303}; RN [1] {ECO:0000313|Ensembl:ENSTNIP00000022668} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15496914; DOI=10.1038/nature03025; RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N., RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., RA Nicaud S., Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., RA Dasilva C., Salanoubat M., Levy M., Boudet N., Castellano S., RA Anthouard V., Jubin C., Castelli V., Katinka M., Vacherie B., RA Biemont C., Skalli Z., Cattolico L., Poulain J., De Berardinis V., RA Cruaud C., Duprat S., Brottier P., Coutanceau J.-P., Gouzy J., RA Parra G., Lardier G., Chapple C., McKernan K.J., McEwan P., Bosak S., RA Kellis M., Volff J.-N., Guigo R., Zody M.C., Mesirov J., RA Lindblad-Toh K., Birren B., Nusbaum C., Kahn D., Robinson-Rechavi M., RA Laudet V., Schachter V., Quetier F., Saurin W., Scarpelli C., RA Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.; RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals RT the early vertebrate proto-karyotype."; RL Nature 431:946-957(2004). RN [2] {ECO:0000313|Ensembl:ENSTNIP00000022668} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSTNIP00000022668}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAAE01022184; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSTNIT00000022907; ENSTNIP00000022668; ENSTNIG00000019455. DR GeneTree; ENSGT00390000003122; -. DR OrthoDB; EOG79GT7C; -. DR TreeFam; TF329202; -. DR Proteomes; UP000007303; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007303}; KW Reference proteome {ECO:0000313|Proteomes:UP000007303}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSTNIP00000022668}. SQ SEQUENCE 163 AA; 17522 MW; 01FDD416F29F3029 CRC64; XDDKLENRGH TQRFSGAQIN EAACDLAREV ANEGNALVAG GVSQTPAYLS CKSEEEVKAI FKKQLDVFVK KDVDFLIAEY FEHVEEAEWA VHVLKTAGKP VAATLCIGPE GDLNGVSPGE CGVRLVKAGA QIVGINCHFD PETCVKTVKM MKEGVEKAGL KAH // ID H3F1J3_PRIPA Unreviewed; 307 AA. AC H3F1J3; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:PPA15964}; GN Name=WBGene00105518 {ECO:0000313|EnsemblMetazoa:PPA15964}; OS Pristionchus pacificus (Parasitic nematode). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Diplogasterida; OC Neodiplogasteridae; Pristionchus. OX NCBI_TaxID=54126 {ECO:0000313|EnsemblMetazoa:PPA15964}; RN [1] {ECO:0000313|EnsemblMetazoa:PPA15964} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PS312 {ECO:0000313|EnsemblMetazoa:PPA15964}; RA Wilson R.K.; RT "Draft sequence assembly of the Pristionchus pacificus genome."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblMetazoa:PPA15964} RP IDENTIFICATION. RC STRAIN=PS312 {ECO:0000313|EnsemblMetazoa:PPA15964}; RG EnsemblMetazoa; 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 EnsemblMetazoa; PPA15964; PPA15964; PPA15964. DR InParanoid; H3F1J3; -. DR OMA; SYIGKWR; -. DR Proteomes; UP000005239; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005239}; KW Reference proteome {ECO:0000313|Proteomes:UP000005239}. SQ SEQUENCE 307 AA; 34471 MW; BA2A5C1F58040AF9 CRC64; MDSSPPEKDK KKVKKLAFKA YLDDKKAKNE LVFLDGSFST ELEKENVDFE NHIGWTAYAN FEFLDKVQAV YESYINIGCD IITTNTYHHA YETLAPIYGC NATNSAFRAA INTAHIARFA HKNEDNVRIL LSIGSYAITQ RDGSEYTGAY AATVDPQHVR RYYLNQLVFA RPLDYDGVIF ETIPTKIDVE MIINAIREQS AIHDVIVSFS LNKLNLRDGT PLQDAVRMLL NVSQIIGVGV NCTNPADGVD QIKSIVDCGW IDAGKHIFIY PNSGEAWVDG QCVYFNHSFI SNRFETTVTR TSPNMGV // ID H3FSI4_PRIPA Unreviewed; 597 AA. AC H3FSI4; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:PPA25256}; GN Name=WBGene00114810 {ECO:0000313|EnsemblMetazoa:PPA25256}; OS Pristionchus pacificus (Parasitic nematode). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Diplogasterida; OC Neodiplogasteridae; Pristionchus. OX NCBI_TaxID=54126 {ECO:0000313|EnsemblMetazoa:PPA25256}; RN [1] {ECO:0000313|EnsemblMetazoa:PPA25256} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PS312 {ECO:0000313|EnsemblMetazoa:PPA25256}; RA Wilson R.K.; RT "Draft sequence assembly of the Pristionchus pacificus genome."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblMetazoa:PPA25256} RP IDENTIFICATION. RC STRAIN=PS312 {ECO:0000313|EnsemblMetazoa:PPA25256}; RG EnsemblMetazoa; 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 EnsemblMetazoa; PPA25256; PPA25256; PPA25256. DR InParanoid; H3FSI4; -. DR OMA; EINIESA; -. DR Proteomes; UP000005239; Unassembled WGS sequence. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005239}; KW Reference proteome {ECO:0000313|Proteomes:UP000005239}. SQ SEQUENCE 597 AA; 65162 MW; 9B1E2DB0D4725A7A CRC64; MPERRSANFD ILNASFKERI LVFDGGMGTM IQREGLGEND FRNTELEKHE KPLKGNNDLL SITRPDIIQK LQIHKMYLDA GADIIGTNTF SGTTIAQADY GCEHLVKEIN IESARVARAA CVEAERETGR KRFVAGSIGP TNKTLSISPS VEDPGARNVE FQELVEAYGQ QARALLEGGV DILLVETVFD SANAKAALFA LRGIFENEDV VEVPVFLSAT IVDLSGRTLS GQTGEAFLIA TRQGQAMTVG LNCALGAREM RPFVEAMANY TDQFILCYPN AGLPNALGGY DETPEQMADT IGEFARSGLL NMVGGCCGTT PDHISAIAKA VNGVTPRVPP SDPNHGFLKL SGLEPFIVGP HTNFVNIGER CNVAGSRKFC NLIKDNKYEE AISIARSQVE NGAQVIDVNM DDGLLDGPFC MKKFLRMLST EPDVAKVPLC IDSSDFNVII SGLESIQGKC IVNSISLKEG HEAFVQKARL IHRYGAAVVV MAFDEEGQAV EIQNKYDICE RSYRILTEEV GMDPTDIIFD INVLTIATGM DEHAEYGKNF IFACRMIKEN LPGCSISGGV SNLSFAFRGM EKSSSSMQFK QEWIWAL // ID H3G8D7_PHYRM Unreviewed; 1255 AA. AC H3G8D7; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblProtists:Phyra71145}; OS Phytophthora ramorum (Sudden oak death agent). OC Eukaryota; Stramenopiles; Oomycetes; Peronosporales; Phytophthora. OX NCBI_TaxID=164328 {ECO:0000313|EnsemblProtists:Phyra71145}; RN [1] {ECO:0000313|EnsemblProtists:Phyra71145} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pr102 {ECO:0000313|EnsemblProtists:Phyra71145}; RX PubMed=16946064; DOI=10.1126/science.1128796; RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H.Y., Aerts A., RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J., RA Damasceno C.M.B., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L., RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., RA Huang W., Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., RA Lee M.-K., McDonald W.H., Medina M., Meijer H.J.G., Nordberg E.K., RA Maclean D.J., Ospina-Giraldo M.D., Morris P.F., Phuntumart V., RA Putnam N.H., Rash S., Rose J.K.C., Sakihama Y., Salamov A.A., RA Savidor A., Scheuring C.F., Smith B.M., Sobral B.W.S., Terry A., RA Torto-Alalibo T.A., Win J., Xu Z., Zhang H., Grigoriev I.V., RA Rokhsar D.S., Boore J.L.; RT "Phytophthora genome sequences uncover evolutionary origins and RT mechanisms of pathogenesis."; RL Science 313:1261-1266(2006). RN [2] {ECO:0000313|EnsemblProtists:Phyra71145} RP IDENTIFICATION. RC STRAIN=Pr102 {ECO:0000313|EnsemblProtists:Phyra71145}; RG EnsemblProtists; RL Submitted (FEB-2015) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; DS566002; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EnsemblProtists; Phyra71145; Phyra71145; Phyra71145. DR InParanoid; H3G8D7; -. DR Proteomes; UP000005238; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000005238}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005238}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 237 237 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 301 301 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 775 775 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1255 AA; 139526 MW; E466EB1A87C87603 CRC64; MKQRTFIFDG GMGTMIQTHR FTEEDFRGER FADSPCLVKG NNDLLSITQP QVIKDIHKQY MQVGRAQLIG TNTFSGTTIA QADYQMEHLV YELNFESARL AREAADEVTL LDPLLPRFVA GSIGPTNRTL SISPNVEDPG FRNVTFDELV DAYYTQVEGL VDGGSDVLLV ETIFDTLNAK AAVFAINKYQ ETTGRKLPLF ISGTIVDMSG RTLSGQTTEA FYVSLRHSKP FCIGLNCALG ANQMKPFLQR LANVAECFVS VYANAGLPNA MGGYDDTPAM MAEYCEEFSK DRLINMMGGC CGTTPQHIEA IAIMAAKYEP RPLPELKEPF MWLSGLEDMV VTKERFSFLN VGERCNISGS IRFKRLIMKG DYGTAMDVAR QQVEDGAMVI DVNVDDGMLD GVAAMERFLK IAVTEPDVSK VPFMVDSSKF HIVEAGLKCV QGKCIVNSIS LKVGKELFME HARIVKSHGA AVVVMAFDEE GQAATEAEKV RICKRSYDIL VNEVGFPPED IIFDPNILTV ATGMEEHNNY GVDFINACRI IKEQNPYCKI SGGVSNLSFG FRGVNVIREA IHSVFLYHAV QAGMDMGIVN AAMLEVYDDI PKDLLKLVED VVLNRNPDGT EALLDRSLIE KEKADAAKKG GVVASSGNKQ EWRSKPIGER LTHALVKGIS EFIDQDVEEM RKVAEKPLDV IEGPLMDGMN VVGKLFGSGK MFLPQVIKSA RVMKKAVAYL LPYMEEEKNQ RRLANTANGI ANEEEDEDSQ YAGKVLIATV KGDVHDIGKN IVGVVLGCNN YKIIDMGVMV PCEDILAAAK KYNVDVIGLS GLITPSLDEM VYVAREMSKA GLKVPLIVGG ATTSKMHAAV KIAPHYSTPE HPVMHVLDAS RSVVVVGNLL RQDEERDEFV EEVMEEYEEM REDYYASLDD IKLIGFENAK TKSYQIDYTA KPPFQKINRV GLHVIEDLPL EDLVPFIDWN PFFQTWELRG RYPNRGYPKI FDDEAVGAEA RKVFDEAQKL LQEIMDKKLL RVRGVSGIFP AYREGDDVIV CDPKNPEQEI SKFCMLRQQA EKETSDPYIS LADFIAPKGV GGQDYIGGFA VGVFGVEDMA AKFEADHDDF NKIMSQAIGD RLAEAFAEYI HREMRVKDWG YAADEVLNQE DLLKVKYDGI RPAPGYPSQP DHTEKRALWD LLKADELIDL KLTDSYMMLP GSAVSALCFA HPDSQYFAVG KIGKDQVVEY AERKGLTLEE TERWLAPILG YDRSA // ID H3GC99_PHYRM Unreviewed; 330 AA. AC H3GC99; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblProtists:Phyra73021}; OS Phytophthora ramorum (Sudden oak death agent). OC Eukaryota; Stramenopiles; Oomycetes; Peronosporales; Phytophthora. OX NCBI_TaxID=164328 {ECO:0000313|EnsemblProtists:Phyra73021}; RN [1] {ECO:0000313|EnsemblProtists:Phyra73021} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pr102 {ECO:0000313|EnsemblProtists:Phyra73021}; RX PubMed=16946064; DOI=10.1126/science.1128796; RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H.Y., Aerts A., RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J., RA Damasceno C.M.B., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L., RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., RA Huang W., Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., RA Lee M.-K., McDonald W.H., Medina M., Meijer H.J.G., Nordberg E.K., RA Maclean D.J., Ospina-Giraldo M.D., Morris P.F., Phuntumart V., RA Putnam N.H., Rash S., Rose J.K.C., Sakihama Y., Salamov A.A., RA Savidor A., Scheuring C.F., Smith B.M., Sobral B.W.S., Terry A., RA Torto-Alalibo T.A., Win J., Xu Z., Zhang H., Grigoriev I.V., RA Rokhsar D.S., Boore J.L.; RT "Phytophthora genome sequences uncover evolutionary origins and RT mechanisms of pathogenesis."; RL Science 313:1261-1266(2006). RN [2] {ECO:0000313|EnsemblProtists:Phyra73021} RP IDENTIFICATION. RC STRAIN=Pr102 {ECO:0000313|EnsemblProtists:Phyra73021}; RG EnsemblProtists; RL Submitted (FEB-2015) 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; DS565999; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EnsemblProtists; Phyra73021; Phyra73021; Phyra73021. DR InParanoid; H3GC99; -. DR Proteomes; UP000005238; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005238}; KW Reference proteome {ECO:0000313|Proteomes:UP000005238}. SQ SEQUENCE 330 AA; 36034 MW; 75D04E202205698C CRC64; MSPALTGLQQ LLADKSCVVV LDGGFATELE KDPRVDLSAS SLWSGSLLLG KNTHLQEVVV NAHKSYFLAG ADVATTASYQ ASVDGFKREG VTAIEDVEKL FAKSIDLGVQ ARDAAWSELD QSKRIKPLVG ASVGCYGAAL ADGSEYRGDY GKTKEELVAW HTHRFEFFAN YAPADFLICE TIPCLVEVEA FVDLLNEFPA AYAVVAVACH NGTELNSGEP ISRIPEILAK LKNPSQLLAI GINCTPPQHV ESLLRALDCH WPKAVYPNSG EGWDGVNKKW LPADSTGGPS SWEEFLPKWY DAGARFFGGC CRTSPDDIRA IREYFERRLE // ID H3GW73_PHYRM Unreviewed; 320 AA. AC H3GW73; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblProtists:Phyra81704}; OS Phytophthora ramorum (Sudden oak death agent). OC Eukaryota; Stramenopiles; Oomycetes; Peronosporales; Phytophthora. OX NCBI_TaxID=164328 {ECO:0000313|EnsemblProtists:Phyra81704}; RN [1] {ECO:0000313|EnsemblProtists:Phyra81704} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pr102 {ECO:0000313|EnsemblProtists:Phyra81704}; RX PubMed=16946064; DOI=10.1126/science.1128796; RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H.Y., Aerts A., RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J., RA Damasceno C.M.B., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L., RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., RA Huang W., Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., RA Lee M.-K., McDonald W.H., Medina M., Meijer H.J.G., Nordberg E.K., RA Maclean D.J., Ospina-Giraldo M.D., Morris P.F., Phuntumart V., RA Putnam N.H., Rash S., Rose J.K.C., Sakihama Y., Salamov A.A., RA Savidor A., Scheuring C.F., Smith B.M., Sobral B.W.S., Terry A., RA Torto-Alalibo T.A., Win J., Xu Z., Zhang H., Grigoriev I.V., RA Rokhsar D.S., Boore J.L.; RT "Phytophthora genome sequences uncover evolutionary origins and RT mechanisms of pathogenesis."; RL Science 313:1261-1266(2006). RN [2] {ECO:0000313|EnsemblProtists:Phyra81704} RP IDENTIFICATION. RC STRAIN=Pr102 {ECO:0000313|EnsemblProtists:Phyra81704}; RG EnsemblProtists; RL Submitted (FEB-2015) 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; DS566059; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EnsemblProtists; Phyra81704; Phyra81704; Phyra81704. DR InParanoid; H3GW73; -. DR Proteomes; UP000005238; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005238}; KW Reference proteome {ECO:0000313|Proteomes:UP000005238}. SQ SEQUENCE 320 AA; 35144 MW; D6AFB2C21AE2D2D9 CRC64; MESKKVDILA GGVMHELFRR GLPNDRNMLS ASALVSPARH HMVVKAHDDF IKAGATMIVT NNYYVTPGVG FTPDEIREYS GVAGELAAEA RAKTNRQDRV KICGSLPPLM HSFRSDRTID RQKGLDTYLL IGEALLPSVD VFLAETMSSL DEAKMAFEAV QPLQKPVMVS FALNSTGQLR SGESIVESVQ SLVEFCSRRA ELLPGDVEKK DNLLCGILFN CAQPEDIAKA IKQLKENLKL MEQLKKHEIR VGGYGDHISP MSKAGAMEES LVAGALQPVM DMEIYSKFAM RWIDDGASIV GGCCGIPPEY LQRITEILSL // ID H3HA59_PHYRM Unreviewed; 603 AA. AC H3HA59; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblProtists:Phyra87773}; GN Name=fgenesh1_pg.C_scaffold_2657000001 GN {ECO:0000313|EnsemblProtists:Phyra87773}; OS Phytophthora ramorum (Sudden oak death agent). OC Eukaryota; Stramenopiles; Oomycetes; Peronosporales; Phytophthora. OX NCBI_TaxID=164328 {ECO:0000313|EnsemblProtists:Phyra87773}; RN [1] {ECO:0000313|EnsemblProtists:Phyra87773} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pr102 {ECO:0000313|EnsemblProtists:Phyra87773}; RX PubMed=16946064; DOI=10.1126/science.1128796; RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H.Y., Aerts A., RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J., RA Damasceno C.M.B., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L., RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., RA Huang W., Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., RA Lee M.-K., McDonald W.H., Medina M., Meijer H.J.G., Nordberg E.K., RA Maclean D.J., Ospina-Giraldo M.D., Morris P.F., Phuntumart V., RA Putnam N.H., Rash S., Rose J.K.C., Sakihama Y., Salamov A.A., RA Savidor A., Scheuring C.F., Smith B.M., Sobral B.W.S., Terry A., RA Torto-Alalibo T.A., Win J., Xu Z., Zhang H., Grigoriev I.V., RA Rokhsar D.S., Boore J.L.; RT "Phytophthora genome sequences uncover evolutionary origins and RT mechanisms of pathogenesis."; RL Science 313:1261-1266(2006). RN [2] {ECO:0000313|EnsemblProtists:Phyra87773} RP IDENTIFICATION. RC STRAIN=Pr102 {ECO:0000313|EnsemblProtists:Phyra87773}; RG EnsemblProtists; RL Submitted (FEB-2015) 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; DS568346; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EnsemblProtists; Phyra87773; Phyra87773; Phyra87773. DR InParanoid; H3HA59; -. DR Proteomes; UP000005238; Unassembled WGS sequence. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005238}; KW Reference proteome {ECO:0000313|Proteomes:UP000005238}. SQ SEQUENCE 603 AA; 66690 MW; 561F922291EA0882 CRC64; MRSDATAEEV AMLQRPFVRG ETDLFAYLTA LMKQRTFIFD GGMGTMIQTH RFTEEDFRGE RFADSPCLVK GNNDLLSITQ PQVIKDIHKQ YMQVGRAQLI GTNTFSGTTI AQADYQMEHL VYELNFESAR LAREAADEVT LLDPLLPRFV AGSIGPTNRT LSISPNVEDP GFRNVTFDEL VDAYYTQVEG LVDGGSDVLL VETIFDTLNA KAAVFAINKY QETTGRKLPL FISGTIVDMS GRTLSGQTTE AFYVSLRHSK PFCIGLNCAL GANQMKPFLQ RLANVAECFV SVYANAGLPN AMGGYDDTPA MMAEYCEEFS KDRLINMMGG CCGTTPQHIE AIAIMAAKYE PRPLPELKEP FMWLSGLEDM VVTKERFSFL NVGERCNISG SIRFKRLIMK GDYGTAMDVA RQQVEDGAMV IDVNVDDGML DGVAAMERFL KIAVTEPDVS KVPFMVDSSK FHIVEAGLKC VQGKCIVNSI SLKVGKELFM EHARIVKSHG AAVVVMAFDE EGQAATEAEK VRICKRSYDI LVNEVGFPPE DIIFDPNILT VATGMEEHNN YGVDFINACR IIKEQNPYCK ISGGVSNLSF GFRGVNVIRE AIH // ID H3K967_9FIRM Unreviewed; 790 AA. AC H3K967; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHR35546.1}; GN ORFNames=HMPREF9454_01790 {ECO:0000313|EMBL:EHR35546.1}; OS Megamonas funiformis YIT 11815. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Megamonas. OX NCBI_TaxID=742816 {ECO:0000313|EMBL:EHR35546.1}; RN [1] {ECO:0000313|EMBL:EHR35546.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=YIT 11815 {ECO:0000313|EMBL:EHR35546.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHR35546.1}. 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; ADMB01000080; EHR35546.1; -; Genomic_DNA. DR RefSeq; WP_008539273.1; NZ_JH601091.1. DR EnsemblBacteria; EHR35546; EHR35546; HMPREF9454_01790. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; SQ SEQUENCE 790 AA; 84243 MW; B82D86C81CA6300D CRC64; MIHIFDGATG TMLQKSVLKP GMCPELLNIE APEAIQNVHR AYVEAGSNIV ETNTFGASRI KLNEYNLGDK VEAINIAAVK NAKIATAGKA KVAGSMGPTG AFIEPLGELT FDEVYENYYE QAKILADAGV DYILIETCIE IQEMRAALLA AKDACDLPVI CQLSFSEDGR TVTGTDPQSA AIILEAMGAD IIGANCSLGP EQLVPIIKEL ADNCSCPISV QANAGMPHLE NGQTIFPLTP EDMAKWAPKL VEAGATYIGG CCGTTPAHIK AIKEALADVS EPIRKTPNPN LALASRSKTV FIGKDLPTRL IGERINPTGR KKLAEEIKNG SFISVKREAI EQTQAGAQIL DVNMGVAGID QAKAMHKAIT EISQLVNTPL AIDTSDVKAL EAGLKAYPGR ALINSVSAEP DRLKYFIPLA KRYGAAILCL PLSDEGIPKT AKERLALAQK IIAEAKAQGL KDNNFLLDAL VMTIAADKNA CNEVLNTLKL YREHIGAPST MGLSNISFGL PNRPLINSTF FTMCLAMGLD APIMNPYDDS MQNALSASNA LLAKDPNGRD YSLNHSGQNI PVAKAKNAVS SGDIIEDIKS AIISGEKESI AQMVEQALTE GHKTNEITDK ALSAAMNVVG KDFGAKKIFL PQVMLSAEAM REAFIKIKER IPADSVSNKG TIVIATVKGD IHDLGKNIVS ALLENNGFKV IDLGKDIDKE EIIKAAIDNK ADMIGLCSLM TTTITQIDEV IAELNKSEYS TKVMIGGAVV TQEYADNVGA DAYAPDGVEA VEIAKKLINK // ID H3KFM4_9BURK Unreviewed; 318 AA. AC H3KFM4; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 11. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EHY31091.1}; GN ORFNames=HMPREF9440_01543 {ECO:0000313|EMBL:EHY31091.1}; OS Sutterella parvirubra YIT 11816. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Sutterellaceae; Sutterella. OX NCBI_TaxID=762967 {ECO:0000313|EMBL:EHY31091.1}; RN [1] {ECO:0000313|EMBL:EHY31091.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=YIT 11816 {ECO:0000313|EMBL:EHY31091.1}; 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 (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. {ECO:0000313|EMBL:EHY31091.1}. 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; AFBQ01000227; EHY31091.1; -; Genomic_DNA. DR RefSeq; WP_008542561.1; NZ_JH604981.1. DR EnsemblBacteria; EHY31091; EHY31091; HMPREF9440_01543. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHY31091.1}; KW Transferase {ECO:0000313|EMBL:EHY31091.1}. SQ SEQUENCE 318 AA; 33976 MW; FE7AAF163D1FBE02 CRC64; MTTNTTTSPA SRPARPFTAL LAKKESLIID GAMSTALEAL GADLKDDLWT AKVLVNEPEI VERVHEAYAR AGADVAITCS YQATEAGLAK KGLDSEAAFD VIAKSVTLAR EGCRRGGRED AIVAGSVGPY GAYLADGSEY RGDYRLTDAE FEAFHALRMD ALKAAGCDLY ALETQPQFAE IRALVRMTAA RGMTCWVTMT HKAGDPTRLP DGTPLSEVAA WLDGEDCVEA LGLNCVPKAT AAQALDALTG ATSKPVILYP NSGETYDAAT KTWSKADPHA HDWDADVVRW KGQGVRCLGG CCRTLPEDVR VMRKAFLG // ID H3KWV6_ECOLX Unreviewed; 1227 AA. AC H3KWV6; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHU34486.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHU34486.1}; GN Name=metH {ECO:0000313|EMBL:EHU34486.1}; GN ORFNames=ECDEC2B_4863 {ECO:0000313|EMBL:EHU34486.1}; OS Escherichia coli DEC2B. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868139 {ECO:0000313|EMBL:EHU34486.1}; RN [1] {ECO:0000313|EMBL:EHU34486.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC2B {ECO:0000313|EMBL:EHU34486.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHU34486.1}. 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; AFJB01000040; EHU34486.1; -; Genomic_DNA. DR RefSeq; WP_000095940.1; NZ_AFJB01000040.1. DR EnsemblBacteria; EHU34486; EHU34486; ECDEC2B_4863. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHU34486.1}; KW Transferase {ECO:0000313|EMBL:EHU34486.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136052 MW; 0CD8269975292F72 CRC64; MSSKVEQLCA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVISAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPAEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPT ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANTQ QAEWRSWVVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KMLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK VSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAE // ID H3M0L8_KLEOX Unreviewed; 310 AA. AC H3M0L8; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 11. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EHT02938.1}; GN ORFNames=HMPREF9689_00506 {ECO:0000313|EMBL:EHT02938.1}; OS Klebsiella oxytoca 10-5245. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=883120 {ECO:0000313|EMBL:EHT02938.1, ECO:0000313|Proteomes:UP000003205}; RN [1] {ECO:0000313|EMBL:EHT02938.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=10-5245 {ECO:0000313|EMBL:EHT02938.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHT02938.1}. 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; AGDL01000006; EHT02938.1; -; Genomic_DNA. DR RefSeq; WP_004110935.1; NZ_JH603137.1. DR EnsemblBacteria; EHT02938; EHT02938; HMPREF9689_00506. DR Proteomes; UP000003205; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000003205}; KW Methyltransferase {ECO:0000313|EMBL:EHT02938.1}; KW Transferase {ECO:0000313|EMBL:EHT02938.1}. SQ SEQUENCE 310 AA; 33364 MW; 7F3A264538BF0F31 CRC64; MSQNNPLTAL IDAKPFILLD GAMATELEAR GCNLADSLWS AKVLVDNPEL IREVHLDYFR AGAQVAITAS YQATPAGFAA LGLDEAQSKA LIGKSVELAR KAREAYLAEN PQAGALLVAG SVGPYGAFLA DGSEYRGDYV RSDEEFQAFH RPRVEALLDA GADLLACETM PNFAEMKALA ELLTAYPRAR AWFSFTLRDA QHLSDGTPLR EVVAVLANYP QVVALGINCI ALENTTAALA HLHSLTALPL VVYPNSGEHY DAVSKTWHRH GEACATLAEY LPQWLAAGAK LIGGCCRTTP KDIAELNARR // ID H3MDV1_KLEOX Unreviewed; 1227 AA. AC H3MDV1; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHS88864.1}; GN ORFNames=HMPREF9689_05139 {ECO:0000313|EMBL:EHS88864.1}; OS Klebsiella oxytoca 10-5245. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=883120 {ECO:0000313|EMBL:EHS88864.1, ECO:0000313|Proteomes:UP000003205}; RN [1] {ECO:0000313|EMBL:EHS88864.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=10-5245 {ECO:0000313|EMBL:EHS88864.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHS88864.1}. 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; AGDL01000044; EHS88864.1; -; Genomic_DNA. DR RefSeq; WP_004117169.1; NZ_JH603137.1. DR EnsemblBacteria; EHS88864; EHS88864; HMPREF9689_05139. DR Proteomes; UP000003205; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000003205}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135689 MW; 0D4D9681D4E6CDE0 CRC64; MSSKVEQLHQ QLKERILVLD GGMGTMIQSY RLSEQDFRGE RFADWPCDLK GNNDLLVLSK PEVITAIHDA YFAAGADIIE TNTFNSTTIA MADYQMESLS AEINFTAAKL ARASADAWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV EAYRESTKAL VEGGADLILI ETVFDTLNAK AAIFAVKEEF EALGVDLPIM ISGTITDASG RTLSGQTTEA FYNSLRHADA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MATQIREWAE AGFLNIVGGC CGTTPEHIAA MSRAVAGLPP RQLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY NEALDVARQQ VESGAQIIDI NMDEGMLDAE AAMTRFLNLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVEPFIQHA KKVRRYGAAV VVMAFDEVGQ ADTRERKIEI CRRAYTILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLDLAEKYRG SKTDDTANAQ QAEWRSWDVK KRLEYSLVKG ITEFIELDTE EARQQAARPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPYIEASK EKGSSNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPADKIL KTAREVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDSQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDLAFDWAS YTPPVAHRLG VHEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG EEAQRLFKDA NELLDKLSAG KALNPRGVVG LFPANRVGDD IEIYRDETRT HVLTVGHHLR QQTEKVGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAWEAQH DDYNKIMVKA IADRLAEAFA EYLHERVRKV YWGYAANENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKR TGMKLTESFA MWPGASVSGW YFSHPDSKYF AVAQIQRDQV EDYALRKGMS VAEVERWLAP NLGYDAD // ID H3MFN7_KLEOX Unreviewed; 1227 AA. AC H3MFN7; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHT14961.1}; GN ORFNames=HMPREF9690_00040 {ECO:0000313|EMBL:EHT14961.1}; OS Klebsiella oxytoca 10-5246. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=883121 {ECO:0000313|EMBL:EHT14961.1}; RN [1] {ECO:0000313|EMBL:EHT14961.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=10-5246 {ECO:0000313|EMBL:EHT14961.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHT14961.1}. 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; AGDM01000003; EHT14961.1; -; Genomic_DNA. DR RefSeq; WP_004856388.1; NZ_JH603146.1. DR EnsemblBacteria; EHT14961; EHT14961; HMPREF9690_00040. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135770 MW; 447AC69B1D2E15F7 CRC64; MSSKVEQLHQ QLKKRILVLD GGMGTMIQGY RLSEEDFRGE RFADWPCDLK GNNDLLVLSK PEVITAIHDA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFVAAKL ARACADEWTS RTPEKPRYVA GVLGPTNRTA SISPDVNDPA YRNITFDGLV EAYRESTKAL VEGGVDLILI ETVFDTLNAK AAIFAVKEEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHADA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAAQIREWAE SGFLNIVGGC CGTTPEHIAA MTRAVTGLAP RVLPEIPVAC RLAGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY NEALDVARQQ VESGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVEAFVEHA KKVRRYGAAV VVMAFDEIGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPV ELRDAVEDVI LNRHADGTER LLELAEKYRG SKTDDSANAQ QAEWRSWDVK KRLEYSLVKG ITEFIELDTE EARQQAARPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPYIEASK EKGSSNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIIDL GVMVPADKIL KTAREVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVSAL LSDTQHDDFV ARTRREYETV RIQHARKKPR TPPVTLAAAR DNDLAFDWAS YTPPVAHRLG VQSVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG EEAKRLFHDA NEMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVLTVSHHLR QQTEKVGFAN YCLADFVAPK LSGKADYLGA FAVTGGLEED ALAEAFDAQH DDFNKIMVKA IADRLAEAFA EYLHERVRKV YWGYAANENL SNEELIRENY QGIRPAPGYP ACPEHTEKAV IWELLDVEAH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMT PAEVERWLAP NLGYDAD // ID H3MI15_KLEOX Unreviewed; 310 AA. AC H3MI15; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 11. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EHT13218.1}; GN ORFNames=HMPREF9690_00868 {ECO:0000313|EMBL:EHT13218.1}; OS Klebsiella oxytoca 10-5246. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=883121 {ECO:0000313|EMBL:EHT13218.1}; RN [1] {ECO:0000313|EMBL:EHT13218.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=10-5246 {ECO:0000313|EMBL:EHT13218.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHT13218.1}. 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; AGDM01000016; EHT13218.1; -; Genomic_DNA. DR RefSeq; WP_004858411.1; NZ_JH603146.1. DR EnsemblBacteria; EHT13218; EHT13218; HMPREF9690_00868. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHT13218.1}; KW Transferase {ECO:0000313|EMBL:EHT13218.1}. SQ SEQUENCE 310 AA; 33524 MW; B4657B43F9135079 CRC64; MSQNNPLTAI LDAQPFILLD GAMATELEAR GCNLADSLWS AKVLVDNPEL IREVHLDYFR AGAQVAITAS YQATPAGFAA RGLDEAQSKA LIGKSVELAR KAREAYLAEN PQAGTLLVAG SVGPYGAFLA DGSEYRGDYV RSHEEFQAFH RPRVEALLDA GADLLACETM PGFAEIKALA ELLSTYPRAR AWFSFTLRDA QHLSDGTPLR EVISILANYP QIVALGINCI ALEETTAALE HLHSLTALPL VVYPNSGEHY DPVSKTWHHH GEACETLAGY LPRWLAAGAK LIGGCCRTTP KDIAELNAQR // ID H3N5S4_KLEOX Unreviewed; 1227 AA. AC H3N5S4; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHT08936.1}; GN ORFNames=HMPREF9694_03517 {ECO:0000313|EMBL:EHT08936.1}; OS Klebsiella oxytoca 10-5250. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=883125 {ECO:0000313|EMBL:EHT08936.1}; RN [1] {ECO:0000313|EMBL:EHT08936.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=10-5250 {ECO:0000313|EMBL:EHT08936.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHT08936.1}. 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; AGDP01000017; EHT08936.1; -; Genomic_DNA. DR RefSeq; WP_004127713.1; NZ_JH603150.1. DR EnsemblBacteria; EHT08936; EHT08936; HMPREF9694_03517. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135623 MW; FC5553B85E0619FB CRC64; MSSKVEQLHQ QLKARILVLD GGMGTMIQSY RLSEQDFRGA RFADWPCDLK GNNDLLVLSK PEVITAIHDA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFTAAKL ARASADAWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA YRNITFDGLV EAYRESTKAL VEGGADLILI ETVFDTLNAK AAIFAVKEEF EALGVDLPIM ISGTITDASG RTLSGQTTEA FYNSLRHADA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAAQIREWAE AGFLNIVGGC CGTTPEHIAA MSRAVAGLPP RQLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY NEALDVARQQ VESGAQIIDI NMDEGMLDAE AAMTRFLNLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVEPFIQHA KKVRRYGAAV VVMAFDEVGQ ADTRERKIEI CRRAYNILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLDLAEKYRG SKTDDTANAQ QAEWRSWDVK KRLEYSLVKG ITEFIELDTE EARQQAARPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPYIEASK EKGSSNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPADKIL KTAREVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSATQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDLAFDWES YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG EEAQRLFKDA NELLDKLSAG KTLNPRGVVG LFPANRVGDD VEIYRDETRT HVLTVGHHLR QQTEKVGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAYEAQH DDYNKIMVKA IADRLAEAFA EYLHERVRKV YWGYAANENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYF AVAQIQRDQV EDYALRKGMS VAEVERWLAP NLGYDAD // ID H3N7T0_KLEOX Unreviewed; 310 AA. AC H3N7T0; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 11. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EHT07348.1}; GN ORFNames=HMPREF9694_04350 {ECO:0000313|EMBL:EHT07348.1}; OS Klebsiella oxytoca 10-5250. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=883125 {ECO:0000313|EMBL:EHT07348.1}; RN [1] {ECO:0000313|EMBL:EHT07348.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=10-5250 {ECO:0000313|EMBL:EHT07348.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHT07348.1}. 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; AGDP01000021; EHT07348.1; -; Genomic_DNA. DR RefSeq; WP_004129514.1; NZ_JH603150.1. DR EnsemblBacteria; EHT07348; EHT07348; HMPREF9694_04350. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHT07348.1}; KW Transferase {ECO:0000313|EMBL:EHT07348.1}. SQ SEQUENCE 310 AA; 33433 MW; 9434C2B178257706 CRC64; MSQNNPLTAL LDARPFILLD GAMATELEGR GCNLADSLWS AKVLVDNPEL IREVHLDYFR AGAQVAITAS YQATPAGFAA RGLDEAQSKA LIGKSVELAR KAREAYLAEN PQAGALLVAG SVGPYGAYLA DGSEYRGDYL RSHEEFQAFH RPRVEALLDA GADLLACETL PNFAEIKALA ELLTAYPRAR AWFSFTLRDA QHLSDGTPLR EVIGVLANYP QVVALGINCI ALESTTAALA HLHSLTALPL VVYPNSGEHY DPESKTWHHH GEACETLAGY LPQWLAAGAK LIGGCCRTTP KDIAELNARR // ID H3NTW9_9GAMM Unreviewed; 336 AA. AC H3NTW9; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 01-OCT-2014, entry version 16. DE SubName: Full=Cobalamin-dependent methionine synthase I {ECO:0000313|EMBL:EHQ58284.1}; GN ORFNames=OMB55_00020310 {ECO:0000313|EMBL:EHQ58284.1}; OS gamma proteobacterium HIMB55. OC Bacteria; Proteobacteria; Gammaproteobacteria; OMG group; OM60 clade. OX NCBI_TaxID=745014 {ECO:0000313|EMBL:EHQ58284.1}; RN [1] {ECO:0000313|EMBL:EHQ58284.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HIMB55 {ECO:0000313|EMBL:EHQ58284.1}; RX PubMed=22493201; DOI=10.1128/JB.00171-12; RA Huggett M.J., Rappe M.S.; RT "Genome Sequence of Strain HIMB55, a Novel Marine Gammaproteobacterium RT of the OM60/NOR5 Clade."; RL J. Bacteriol. 194:2393-2394(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. {ECO:0000313|EMBL:EHQ58284.1}. 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; AGIF02000001; EHQ58284.1; -; Genomic_DNA. DR RefSeq; WP_009471807.1; NZ_AGIF02000001.1. DR EnsemblBacteria; EHQ58284; EHQ58284; OMB55_00020310. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 336 AA; 35265 MW; 8DEB6B5FC9355BB1 CRC64; MSNPILDVIA RKGWCVTDGA TGSNFFGRGL EAGYPPELWC VERPDEVLWL HREFLKAGAD LILTNSFGAN APRLKLHKSE HRVHEINKAA AQLARQAAAE HADADGNEAV VAGSMGPTGE LFAPMGDLTH ASTAAFFAEQ AEALAEGGAD ALWIETMSST EEVAAAAEAA KKTGLPVAAT LTFDTARRSM MGITPTEYAA FAKEIGLDLI GSNCGIGPAE LMDSTTELLS ADSGLPVIAK GNCGIPQYVD GEIHFHGSPE LMAHYALHAR DAGATVIGGC CGTTPEHLAA MVEALNSTPP RTFDGEAMAE QLGKPWPDLS SRGGEGGGRR SRRRQG // ID H3NUA2_9GAMM Unreviewed; 311 AA. AC H3NUA2; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 01-OCT-2014, entry version 10. DE SubName: Full=Homocysteine/selenocysteine methylase (S-methylmethionine-dependent) {ECO:0000313|EMBL:EHQ57422.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EHQ57422.1}; GN ORFNames=OMB55_00011550 {ECO:0000313|EMBL:EHQ57422.1}; OS gamma proteobacterium HIMB55. OC Bacteria; Proteobacteria; Gammaproteobacteria; OMG group; OM60 clade. OX NCBI_TaxID=745014 {ECO:0000313|EMBL:EHQ57422.1}; RN [1] {ECO:0000313|EMBL:EHQ57422.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HIMB55 {ECO:0000313|EMBL:EHQ57422.1}; RX PubMed=22493201; DOI=10.1128/JB.00171-12; RA Huggett M.J., Rappe M.S.; RT "Genome Sequence of Strain HIMB55, a Novel Marine Gammaproteobacterium RT of the OM60/NOR5 Clade."; RL J. Bacteriol. 194:2393-2394(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. {ECO:0000313|EMBL:EHQ57422.1}. 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; AGIF02000001; EHQ57422.1; -; Genomic_DNA. DR RefSeq; WP_009470945.1; NZ_AGIF02000001.1. DR EnsemblBacteria; EHQ57422; EHQ57422; OMB55_00011550. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHQ57422.1}; KW Transferase {ECO:0000313|EMBL:EHQ57422.1}. SQ SEQUENCE 311 AA; 32910 MW; 74590F8F1B691286 CRC64; MSDGNVSTLK ITLLDGGLGQ ELIKRSSAPP HPLWSTKVML DEPHLVSDIH RDFCDAGARV ICLNTYAVSR HRLKTFAPEH SVKEMLDAAA TTAKSGISAS SATNPVSTVA SLPPLNASYD HTVAPDFDNA YEQYSELVAL QKDSVEGFLL ETMSNIAEAT AGAKAIRDAG VIGAVGFTLS DSDPQKLRSG ELLADAIAAV KPYSPDAIML NCSTPEVVTE GLKTALASGI RCGAYANGFT SVEALVPGST VDRLASRKDL GPDDYLAFVK TWLEMGVEII GGCCEIGPDH IRAIRSYLDE QGIETTEALA P // ID H3NXP7_9GAMM Unreviewed; 1227 AA. AC H3NXP7; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 01-APR-2015, entry version 18. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:EHQ56687.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHQ56687.1}; GN ORFNames=OMB55_00003990 {ECO:0000313|EMBL:EHQ56687.1}; OS gamma proteobacterium HIMB55. OC Bacteria; Proteobacteria; Gammaproteobacteria; OMG group; OM60 clade. OX NCBI_TaxID=745014 {ECO:0000313|EMBL:EHQ56687.1}; RN [1] {ECO:0000313|EMBL:EHQ56687.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HIMB55 {ECO:0000313|EMBL:EHQ56687.1}; RX PubMed=22493201; DOI=10.1128/JB.00171-12; RA Huggett M.J., Rappe M.S.; RT "Genome Sequence of Strain HIMB55, a Novel Marine Gammaproteobacterium RT of the OM60/NOR5 Clade."; RL J. Bacteriol. 194:2393-2394(2012). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHQ56687.1}. 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; AGIF02000001; EHQ56687.1; -; Genomic_DNA. DR RefSeq; WP_009470210.1; NZ_AGIF02000001.1. DR EnsemblBacteria; EHQ56687; EHQ56687; OMB55_00003990. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHQ56687.1}; KW Transferase {ECO:0000313|EMBL:EHQ56687.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 763 763 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135093 MW; C1DAA34BC3DCFEB0 CRC64; MSVWNRSSRI EWLKKSLSER IVLLDGGMGT MIQQAGLSES DYRGDEFAHW SFDLKGNNDL LTLTQPSLIA QIHRQYLAAG SDIIETNTFN TNAPSMGDYG MTDLVARLNK EAAQLARAVC DKAETADVPK LVAGVLGPTN RTASISPKVE DPSFRNITFD ELVDTYSTAT RALMDGGADL ILVETIFDTL NAKAALYAID VVSEELGELI EIMISGTITD ASGRTLSGQT TESFWYSVRH ANPISVGLNC ALGPAELRPF LRELADVADT HVSAHPNAGL PNQFGEYDLT TTEMADIVAE YSASGLVNIV GGCCGTTPDH IAEIAARVKG HQPKPLSVKP RVMRLSGLEP FVADDAKGFI NIGERTNVTG SARFKKLILE DDLETALEVA RQQVENGAQI IDINMDEGLL DSEGAMVRYL NLLASEPDIS RVPIMIDSSK WDVLKAGMKC VQGKGVVNSI SLKEGEASFI EQAREIRRYG FAVVVMAFDE TGQADTRDRK VEICKRSYEI LTREVGFPPE DIIFDPNIFA VATGIEEHDN YAKDFIEACG KIREVCPHSM TSGGLSNVSF SFRGNNPVRE AMHSVFLYHA IRNGLNMAIV NAGQLAIYAD IDPELRDLVE DVVLNRRSDG TDRLVDRAPA FANSGEEVVE SLAEWRSKPV KERLEYALVN GIDQYAVEDT EEARLNSARP LDVIEGPLMD GMNTVGDLFG AGKMFLPQVV KSARVMKKAV AHLVPFIEAE KAESGESSEQ GTIIMATVKG DVHDIGKNIV GVVLQCNNYK VIDLGVMVPT QAIWDAAKEH NADIIGLSGL ITPSLDEMVT VAAEMERQGF DIPLLIGGAT TSPAHTSLKI EPSYSGDTVY VKDASRAVGV AAKLLGEQKE AFSAELKRDH EAKRASYAHK KTAPMLSFEE AVARRDKLEF TPEVIQKPAQ LGVHVLDDYP LAVLVDTIDW MPFFNAWEFS GRFPDILNDP IKGVEAKKLF NDAQAMLERI IDENWLQARA MYGLFPAYSR DNQIVILDPQ SYEPLETTHW LRQQKPMPDG KPQLCLSDFI APESESVRDY IGAFAVTAGH GIDAHVKRFE EAHDDYSAIM LKALADRLAE SFAEHLHRRV RTEFWGYAAD ETLDNNQLIR EQYRGIRPAP GYPACPDHRE KETLFRLLDV EKNTGIALTE SMAMTPTASV SGFYFGHPDA RYFNLGKITN DQLIAYSEAR SEPLAEAQRW LAPVLAD // ID H3RGQ2_PANSE Unreviewed; 311 AA. AC H3RGQ2; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 10. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EHT99430.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EHT99430.1}; GN Name=mmuM {ECO:0000313|EMBL:EHT99430.1}; GN ORFNames=CKS_1468 {ECO:0000313|EMBL:EHT99430.1}; OS Pantoea stewartii subsp. stewartii DC283. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Pantoea. OX NCBI_TaxID=660596 {ECO:0000313|EMBL:EHT99430.1}; RN [1] {ECO:0000313|EMBL:EHT99430.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DC283 {ECO:0000313|EMBL:EHT99430.1}; 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] {ECO:0000313|EMBL:EHT99430.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DC283 {ECO:0000313|EMBL:EHT99430.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHT99430.1}. 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; AHIE01000026; EHT99430.1; -; Genomic_DNA. DR RefSeq; WP_006120676.1; NZ_AHIE01000026.1. DR EnsemblBacteria; EHT99430; EHT99430; CKS_1468. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHT99430.1}; KW Transferase {ECO:0000313|EMBL:EHT99430.1}. SQ SEQUENCE 311 AA; 33742 MW; 80C23A82389337EF CRC64; MSRNPVSHAL QQTAPLILDG ALATELEARG CDLTDALWSA KVLMENPELI YQVHYDYFAA GARCAITASY QATPQGFAAR GLNEQQSLAL IAQSVELAQR ARADYLATQT DDRILLVAGS VGPYGAFLAD GSEYRGDYTL PEAEMMAFHR PRIAALLAAG VDVLACETLP SFAEAQTLVN LLREFPDSCA WFSFTLRDAE HLSDGTPLRD VAAYLNAQPQ VIAVGINCIA LDSVTPALQQ LQRLTEKPLV VYPNSGEQYD TNSKSWHSAP SGCTLHDKFA EWQQAGARLI GGCCRTSPRD IAAIARHCQP Q // ID H3SBQ7_9BACL Unreviewed; 1145 AA. AC H3SBQ7; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHQ63421.1}; GN ORFNames=PDENDC454_04716 {ECO:0000313|EMBL:EHQ63421.1}; OS Paenibacillus dendritiformis C454. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1131935 {ECO:0000313|EMBL:EHQ63421.1}; RN [1] {ECO:0000313|EMBL:EHQ63421.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C454 {ECO:0000313|EMBL:EHQ63421.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHQ63421.1}. 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; AHKH01000008; EHQ63421.1; -; Genomic_DNA. DR RefSeq; WP_006675457.1; NZ_AHKH01000008.1. DR EnsemblBacteria; EHQ63421; EHQ63421; PDENDC454_04716. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 722 722 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1145 AA; 127385 MW; E9EC470122EB723F CRC64; MKKPTLEERL QERILILDGA MGTMIQQADL LPEDFGGEHL DGCNEMLVLT RPDVISRIHE QYLEAGADIL ETNTFGATGI VLAEYDLQDR ARELNLAAAK LAVEAAQKFS TPEWPRYVAG AMGPTTKTLS VTGGVTFEQL VESYYEQALA LIEAGVDALL LETSQDTLNV KAGSIAIQRA RETTGQKLPL MISGTIEPMG TTLAGQNIES FYISLEHLNP VSIGLNCATG PEFMRDHLRS LSAISRAAIS CYPNAGLPDE NGHYHESPES LARKIATFAE QGWLNIAGGC CGTTPEHIRV LKEELDKYEP RRQAGSHPPA VSGIETVYIE NESRPYMVGE RTNVLGSRKF KRLIREGKIE EAAEVARAQV KSGAHVIDVC LQDPDRDEAE DMRVFLQEVV KKVKVPLVID TTDPEVLELA LTYTQGKAII NSVNLEDGLE KFENVVPLVH RYGASLVVGT IDERGQAITR EDKLAVAKRS YDILVNDFGI EPENIIFDPL VFPVGTGDEQ YIGSAKETIE GIRLIKEAMP RCQSILGVSN ISFGLPEAGR EVLNSVFLYE CTKAGLDYAI VNTEKLERYA SIPEHERKLS EALLYETNDE TLAEFVAAFR NRTVEKKVKT NDLPLEERLA SYIVEGTKEG LIPDLTLALE KYPPLDIING PLMKGMEEVG RLFNNNELIV AEVLQSAEVM KASVAFLEPH MEKNESAVKG KILLATVKGD VHDIGKNLVE IILSNNGYEI INLGIKVPPE QLIEAYRKEK PDAIGLSGLL VKSAQQMVVT AQDLRSAGID VPIMVGGAAL TRKFTKNRII PEYDGLVLYA KDAMEGLDLA NKLMNAEERQ LLVDELRAHK ERLAKEEEVE QKLPKLTRAV RSAIKEAPVH LPPDLDRHVL RNIAVPQVIP YVNMQMLLGH HLGMRGSVEQ RLKERDPKTV ELKETVDRIL REEAESGVLQ ANAMYRFFPA QSEGDSIHIY NPERQDEVLH TFTFPRQQVE PYMCLADFLR SKESGVMDYV GFLVVTAGKG VRERSDEFKQ QGEYLRSHAL QSVALELAEG LAERIHHMMR EVWGIPDPAE MTMKERFGAR YQGIRVSFGY PACPNLEDQE PLFRLMQPED IGVHLTEGFM MEPEASVTAM VFAHPQGTYF NVDKA // ID H3SQ01_9BACL Unreviewed; 633 AA. AC H3SQ01; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 16. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=PDENDC454_28310 {ECO:0000313|EMBL:EHQ58844.1}; OS Paenibacillus dendritiformis C454. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1131935 {ECO:0000313|EMBL:EHQ58844.1}; RN [1] {ECO:0000313|EMBL:EHQ58844.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C454 {ECO:0000313|EMBL:EHQ58844.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHQ58844.1}. 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; AHKH01000196; EHQ58844.1; -; Genomic_DNA. DR RefSeq; WP_006680125.1; NZ_AHKH01000196.1. DR EnsemblBacteria; EHQ58844; EHQ58844; PDENDC454_28310. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EHQ58844.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EHQ58844.1}. SQ SEQUENCE 633 AA; 69359 MW; 2953C7B49837F922 CRC64; MKDLRQVLQG EIIVGDGAMG TYLYQLGYPV GISYESLNIS EPERIRDIHR EYVSAGARLL ETNTFTANRE KLSKHGMEKQ VKAINRAAAR LAREAAGGQA YVVGALGSIR AGKRENIETD QVKRDYTEQL SALLEEGVDG IMFETFYDME EMKLAVQIVR ALDDRIPIIC QFAVEESHRT KDGLRLLDAF RLLREEGADV VGLNCRMGPN GLMRAMEDLT GRLALPMSAF PNAGLPDYVD GRYNFVATAD YMAESAVRFA ELGARIIGGC CGTTPEHIQA IAQALANAPA PALPTLAEEE AQVQAVPPLE IGERGTAPAS GQGKAASGPS LVDTVRQRHT VIVELDPPRD LDIAKFMLGA QALKDAGADA LTLADNSLAV TRMSNMALGY LALDKIGIRP LIHIACRDRN LIGTQSHMMG LDALGIDHVL AVTGDPARFG DLPDSSSVYD LTSFEIIRMI KQLNAGLAFS GKALKQRANF VVGAAFNPNV KHLNKAIERL ERKIEAGADY IMTQPVYDAS LIERIAEGTK HLNVPVFLGI MPLASGRNAE YLHNEVPGIH LSDEVRERMK GLEGESGRRE GVAIAKELLD VAMKHFNGIY FMTPFMFYEM TAELTEHVWQ KAERLTDPLY RHT // ID H3ZH50_9ALTE Unreviewed; 355 AA. AC H3ZH50; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EHR40190.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHR40190.1}; GN Name=metH {ECO:0000313|EMBL:EHR40190.1}; GN ORFNames=AJE_13500 {ECO:0000313|EMBL:EHR40190.1}; OS Alishewanella jeotgali KCTC 22429. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Alishewanella. OX NCBI_TaxID=1129374 {ECO:0000313|EMBL:EHR40190.1}; RN [1] {ECO:0000313|EMBL:EHR40190.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=KCTC 22429 {ECO:0000313|EMBL:EHR40190.1}; 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. {ECO:0000313|EMBL:EHR40190.1}. 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; AHTH01000045; EHR40190.1; -; Genomic_DNA. DR RefSeq; WP_008951320.1; NZ_AHTH01000045.1. DR EnsemblBacteria; EHR40190; EHR40190; AJE_13500. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHR40190.1}; KW Transferase {ECO:0000313|EMBL:EHR40190.1}. SQ SEQUENCE 355 AA; 38567 MW; 1293125D35155BBC CRC64; MTELRLTPQQ LRQLLASRIL VLDGAMGTMI QQHRLDEAGY RGAEFADWPS DLKGNNDLLV LTQPELIADI HRQYLLAGAD IIETNTFNAT TIAMHDYQMA HLSERINREA AALARRVCDE VTAQQPDKPR FVAGVLGPTN RTASISPDVN DPGFRNVSFD ELVLAYKEST RALIAGGADI IMLETIFDTL NAKAAAFAVL EVFEELQLEL PVMISGTITD ASGRTLSGQT TEAFYYSLAH VKPVTFGLNC ALGPDLLRPY VETLATISEA YVSVHPNAGL PNEFGEYDLG AEAMAAEIAD WAKQGFLNIV GGCCGTTPEH IKAIAEAVKD APPRQPKAAD HSFHLAGLEA FAVEW // ID H4F043_9RHIZ Unreviewed; 303 AA. AC H4F043; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EHS53933.1}; GN ORFNames=PDO_3876 {ECO:0000313|EMBL:EHS53933.1}; OS Rhizobium sp. PDO1-076. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=1125979 {ECO:0000313|EMBL:EHS53933.1}; RN [1] {ECO:0000313|EMBL:EHS53933.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PDO-076 {ECO:0000313|EMBL:EHS53933.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHS53933.1}. 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; AHZC01000013; EHS53933.1; -; Genomic_DNA. DR RefSeq; WP_007596792.1; NZ_AHZC01000013.1. DR EnsemblBacteria; EHS53933; EHS53933; PDO_3876. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EHS53933.1}; KW Transferase {ECO:0000313|EMBL:EHS53933.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 303 AA; 32352 MW; 08A5FEEB412A6490 CRC64; MKDILILDGG VSRELLRLGA ELKQPEWSAL ALMNSPEIVR RVHDEFIVAG ADVVTTNSYA LVPFHIGEQA FERDGASLAA LSGKLAREAA DAAGRKVLVA GSLPPIFGSY EPENFDPARV QHYLRVLVAN LAPYVDVWLG ETLSLIAEGE AVRQAIKVSP KPLWISFTLA DDAAQMAGGE AKLRSGETVR AAAEWAASSG AEGLLFNCAR PEVMKTAVET ASVVFRKNDS VVKIGVYANA FESDTDDQAA NQGLHDTRED LTGDVYSRFA CEWADAGASM IGGCCGIGAH HIHMLADTLR KAG // ID H4F108_9RHIZ Unreviewed; 318 AA. AC H4F108; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 01-OCT-2014, entry version 10. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EHS53620.1}; GN ORFNames=PDO_4114 {ECO:0000313|EMBL:EHS53620.1}; OS Rhizobium sp. PDO1-076. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=1125979 {ECO:0000313|EMBL:EHS53620.1}; RN [1] {ECO:0000313|EMBL:EHS53620.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PDO-076 {ECO:0000313|EMBL:EHS53620.1}; 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. {ECO:0000313|EMBL:EHS53620.1}. 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; AHZC01000032; EHS53620.1; -; Genomic_DNA. DR RefSeq; WP_007597475.1; NZ_AHZC01000032.1. DR EnsemblBacteria; EHS53620; EHS53620; PDO_4114. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHS53620.1}; KW Transferase {ECO:0000313|EMBL:EHS53620.1}. SQ SEQUENCE 318 AA; 34527 MW; 572DA2A856FBAD5E CRC64; MAKYRQQLPQ LEGGDFLTDG GMETTFVFHR GMELPHFAAF PLLDSDDGRS ELLSYIEPYI LLAQQRGVGF ILDTPTWRAN ADWGQKLGYD RKALHALNLR AVDFAAACRN RWETRATPVV ISGIIGPRGD AYKNGQTSVT EAHDYHADQV ASFAQSAADM VSAMTINTVE EASGIALAAA GHGIPCVMSF TVETDGHLLN GTSLQEAIER TDEATNGGPV YYMVNCAHPT HFEQALAADA PWVQRIYGLR ANASAKSHAE LDESETLDIG DPADLGRRYR ALRRNFPGFR ILGGCCGTDH RHIEAICEAC TPSAGLAA // ID H4F1A2_9RHIZ Unreviewed; 338 AA. AC H4F1A2; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 01-OCT-2014, entry version 14. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EHS53524.1}; GN ORFNames=PDO_4142 {ECO:0000313|EMBL:EHS53524.1}; OS Rhizobium sp. PDO1-076. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=1125979 {ECO:0000313|EMBL:EHS53524.1}; RN [1] {ECO:0000313|EMBL:EHS53524.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PDO-076 {ECO:0000313|EMBL:EHS53524.1}; 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. {ECO:0000313|EMBL:EHS53524.1}. 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; AHZC01000035; EHS53524.1; -; Genomic_DNA. DR RefSeq; WP_007597759.1; NZ_AHZC01000035.1. DR EnsemblBacteria; EHS53524; EHS53524; PDO_4142. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHS53524.1}; KW Transferase {ECO:0000313|EMBL:EHS53524.1}. SQ SEQUENCE 338 AA; 35241 MW; 361C4C59166D4659 CRC64; MASLSNPLSD LLAEKGVLLA DGATGTNLFA QGLEAGEAPE LWNEAQPEKI VKLHQDFVDA GADIILTNSF GGTRHRLKLH HAQDRVHELN RKAAEIARAV ADKAPRKVIV AGSVGPTGEL LVPLGAMTYD EAVAAFVEQM EGLKAGGADV AWIETMSSPE EIRAAAEAAV KVGLPYTFTG SFDTAGKTMM GLDPKDIHGV AGDIGAGPLA VGANCGVGAS DILASLLDMT AANPDATVIV KGNCGIPEFR GTEIFYSGTP PLMADYARLA RDSGARIIGG CCGTSCGHLA AMRAAIDDYT PGPRPTLEVI VERIGPLRNK TATESSSQES GRRNRRRG // ID H4F9F6_9RHIZ Unreviewed; 1251 AA. AC H4F9F6; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 01-APR-2015, entry version 20. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHS50576.1}; GN ORFNames=PDO_2398 {ECO:0000313|EMBL:EHS50576.1}; OS Rhizobium sp. PDO1-076. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=1125979 {ECO:0000313|EMBL:EHS50576.1}; RN [1] {ECO:0000313|EMBL:EHS50576.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PDO-076 {ECO:0000313|EMBL:EHS50576.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHS50576.1}. 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; AHZC01000366; EHS50576.1; -; Genomic_DNA. DR RefSeq; WP_007605003.1; NZ_AHZC01000366.1. DR EnsemblBacteria; EHS50576; EHS50576; PDO_2398. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 260 260 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 777 777 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1251 AA; 137052 MW; F3E48A8909A00A03 CRC64; MLDSLFGRQG ANRDGAEILS ALQQAARERI LILDGAMGTE IQGLGLNEDD FRGERFIGCA CHQQGNNDLL ILTQPQAIED IHFRYAMAGA DIIETNTFSS TSIAQADYQM EGAVYDLNKE GAQAVRRAIL RAEREDGKRR FVAGAIGPTN RTASISPDVN NPGYRAVSFD DLRLAYGEQI DGLIDGGADL ILIETIFDTL NAKAAIFACE ERFAAKGIRL PVMISGTITD LSGRTLSGQT PSAFWNSISH ARPFAVGLNC ALGADAMRPH LQELSSVADT FISAYPNAGL PNEFGKYDQD PEEMAALVAG FADEGIVNVV GGCCGSTPEH IRAISEAVAG KAPRVPAEHR PFMSLSGLEP FVLTKDIPFV NVGERTNVTG SAKFRKLITA GDYSAALVVA RDQVENGAQI IDINMDEGLI DSEKAMVEFL NVIAAEPDIA RVPVMIDSSK FQIIESGLKC VQGKSVVNSI SLKEGEENFI AQGRLIRNYG AAVVVMAFDE QGQADTYERK VEICSRAYKI LTEEAGFPPE DIIFDPNIFA VATGIEEHNN YGVDFIEATR TIRERMPLVH ISGGVSNLSF SFRGNEPVRE AMHAVFLYHA IQAGMDMGIV NAGQLAVYES IDADLREACE DVVLNRRSDG TERLLEIAER YRGTGEKQAR VQDMSWREQP VEKRLEHALV NGITEFIDAD TEEARLRAAR PLHVIEGPLM AGMNVVGDLF GAGKMFLPQV VKSARVMKQA VAVLLPYMEE EKRANGGTGE RQAAGKVLMA TVKGDVHDIG KNIVGVVLAC NNYEIIDLGV MVPATKILQT AIEQKVDIIG LSGLITPSLD EMVHMAAEMQ RQGFNIPLLI GGATTSRVHT AVKIHPQYQA GQAVYVTDAS RAVGVVSSLL SNETRDGTIE TLRGEYAKVA DAHARAEAEK QRLPLARARA NAVKVDWSQY KPVKPSFTGT KIFEDYDLAE LAKYIDWTPF FQTWELKGRY PAILEDEKQG EAARALYADA QAMLDKIIAE NWFRPRAVIG FWPANAVDDD IRLFVDDSRT EERATFFTLR QQLSKRDGRP NVALSDFVAP LDTGVEDYVG GFVVTAGIEE VAIAERFERA NDDYSSILVK ALADRFAEAF AERMHERVRR EFWGYAADEA FTPDQLVAED YGGIRPAPGY PAQPDHTEKA TLFSLLDATE ATGVTLTESY AMWPGSSVSG IYIGHPDSYY FGVAKVERDQ VEDYAGRKGM EVREVERWLG PVLNYVPKAP E // ID H4GHR4_9LACO Unreviewed; 307 AA. AC H4GHR4; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 10. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EHS87544.1}; GN ORFNames=PS3_13004 {ECO:0000313|EMBL:EHS87544.1}; OS Lactobacillus gastricus PS3. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1144300 {ECO:0000313|EMBL:EHS87544.1}; RN [1] {ECO:0000313|EMBL:EHS87544.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PS3 {ECO:0000313|EMBL:EHS87544.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHS87544.1}. 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; AICN01000004; EHS87544.1; -; Genomic_DNA. DR RefSeq; WP_007121598.1; NZ_AICN01000004.1. DR EnsemblBacteria; EHS87544; EHS87544; PS3_13004. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHS87544.1}; KW Transferase {ECO:0000313|EMBL:EHS87544.1}. SQ SEQUENCE 307 AA; 33089 MW; 56620001A821F489 CRC64; MELAELLKET PIVIDGSMST PLEIWGAQTD SDLWTAAALI NHPDLVKRVH QAYFEAGARI TITDSYQTNV AAFEKHGYGE QAARRLIRLS AQLAQTARDE YEKATGVHNL VAGSIGPYGA YLADGSEYRG DYELSLADYQ DFHAPRLEEL LAAGVDCLAI ETQPKLAEVT AILAWLHDHQ ISVPVWVSFS LQDPQTISEG TALTQAVEAI QDDLNVLAVG VNCMPVTMAT PAVETIAKVA SVPIIVYPNS GAQYDPITKT WQTTTGQTSF AQAAVDWVQA GAGIIGGCCT TMPKDIQEIK LAIAKES // ID H4I495_ECOLX Unreviewed; 1227 AA. AC H4I495; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHU03455.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHU03455.1}; GN Name=metH {ECO:0000313|EMBL:EHU03455.1}; GN ORFNames=ECDEC1A_4608 {ECO:0000313|EMBL:EHU03455.1}; OS Escherichia coli DEC1A. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868133 {ECO:0000313|EMBL:EHU03455.1}; RN [1] {ECO:0000313|EMBL:EHU03455.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC1A {ECO:0000313|EMBL:EHU03455.1}; 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] {ECO:0000313|EMBL:EHU03455.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC1A {ECO:0000313|EMBL:EHU03455.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHU03455.1}. 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; AIEV01000061; EHU03455.1; -; Genomic_DNA. DR RefSeq; WP_000095940.1; NZ_AIEV01000061.1. DR EnsemblBacteria; EHU03455; EHU03455; ECDEC1A_4608. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHU03455.1}; KW Transferase {ECO:0000313|EMBL:EHU03455.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136052 MW; 0CD8269975292F72 CRC64; MSSKVEQLCA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVISAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPAEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPT ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANTQ QAEWRSWVVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KMLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK VSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAE // ID H4IJA2_ECOLX Unreviewed; 1227 AA. AC H4IJA2; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHU05733.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHU05733.1}; GN Name=metH {ECO:0000313|EMBL:EHU05733.1}; GN ORFNames=ECDEC1B_4823 {ECO:0000313|EMBL:EHU05733.1}; OS Escherichia coli DEC1B. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868134 {ECO:0000313|EMBL:EHU05733.1}; RN [1] {ECO:0000313|EMBL:EHU05733.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC1B {ECO:0000313|EMBL:EHU05733.1}; 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] {ECO:0000313|EMBL:EHU05733.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC1B {ECO:0000313|EMBL:EHU05733.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHU05733.1}. 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; AIEW01000065; EHU05733.1; -; Genomic_DNA. DR RefSeq; WP_000095940.1; NZ_AIEW01000065.1. DR EnsemblBacteria; EHU05733; EHU05733; ECDEC1B_4823. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHU05733.1}; KW Transferase {ECO:0000313|EMBL:EHU05733.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136052 MW; 0CD8269975292F72 CRC64; MSSKVEQLCA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVISAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPAEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPT ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANTQ QAEWRSWVVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KMLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK VSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAE // ID H4J086_ECOLX Unreviewed; 1227 AA. AC H4J086; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHU03485.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHU03485.1}; GN Name=metH {ECO:0000313|EMBL:EHU03485.1}; GN ORFNames=ECDEC1C_4902 {ECO:0000313|EMBL:EHU03485.1}; OS Escherichia coli DEC1C. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868135 {ECO:0000313|EMBL:EHU03485.1}; RN [1] {ECO:0000313|EMBL:EHU03485.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC1C {ECO:0000313|EMBL:EHU03485.1}; 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] {ECO:0000313|EMBL:EHU03485.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC1C {ECO:0000313|EMBL:EHU03485.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHU03485.1}. 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; AIEX01000076; EHU03485.1; -; Genomic_DNA. DR RefSeq; WP_000095940.1; NZ_AIEX01000076.1. DR EnsemblBacteria; EHU03485; EHU03485; ECDEC1C_4902. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHU03485.1}; KW Transferase {ECO:0000313|EMBL:EHU03485.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136052 MW; 0CD8269975292F72 CRC64; MSSKVEQLCA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVISAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPAEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPT ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANTQ QAEWRSWVVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KMLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK VSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAE // ID H4JGB5_ECOLX Unreviewed; 1227 AA. AC H4JGB5; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHU17152.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHU17152.1}; GN Name=metH {ECO:0000313|EMBL:EHU17152.1}; GN ORFNames=ECDEC1D_5158 {ECO:0000313|EMBL:EHU17152.1}; OS Escherichia coli DEC1D. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868136 {ECO:0000313|EMBL:EHU17152.1}; RN [1] {ECO:0000313|EMBL:EHU17152.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC1D {ECO:0000313|EMBL:EHU17152.1}; 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] {ECO:0000313|EMBL:EHU17152.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC1D {ECO:0000313|EMBL:EHU17152.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHU17152.1}. 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; AIEY01000066; EHU17152.1; -; Genomic_DNA. DR RefSeq; WP_000095940.1; NZ_AIEY01000066.1. DR EnsemblBacteria; EHU17152; EHU17152; ECDEC1D_5158. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHU17152.1}; KW Transferase {ECO:0000313|EMBL:EHU17152.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136052 MW; 0CD8269975292F72 CRC64; MSSKVEQLCA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVISAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPAEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPT ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANTQ QAEWRSWVVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KMLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK VSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAE // ID H4JVA4_ECOLX Unreviewed; 1227 AA. AC H4JVA4; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHU20154.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHU20154.1}; GN Name=metH {ECO:0000313|EMBL:EHU20154.1}; GN ORFNames=ECDEC1E_4956 {ECO:0000313|EMBL:EHU20154.1}; OS Escherichia coli DEC1E. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868137 {ECO:0000313|EMBL:EHU20154.1}; RN [1] {ECO:0000313|EMBL:EHU20154.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC1E {ECO:0000313|EMBL:EHU20154.1}; 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] {ECO:0000313|EMBL:EHU20154.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC1E {ECO:0000313|EMBL:EHU20154.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHU20154.1}. 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; AIEZ01000037; EHU20154.1; -; Genomic_DNA. DR RefSeq; WP_000095940.1; NZ_AIEZ01000037.1. DR EnsemblBacteria; EHU20154; EHU20154; ECDEC1E_4956. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHU20154.1}; KW Transferase {ECO:0000313|EMBL:EHU20154.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136052 MW; 0CD8269975292F72 CRC64; MSSKVEQLCA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVISAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPAEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPT ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANTQ QAEWRSWVVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KMLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK VSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAE // ID H4KAM2_ECOLX Unreviewed; 1227 AA. AC H4KAM2; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHU21744.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHU21744.1}; GN Name=metH {ECO:0000313|EMBL:EHU21744.1}; GN ORFNames=ECDEC2A_4813 {ECO:0000313|EMBL:EHU21744.1}; OS Escherichia coli DEC2A. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868138 {ECO:0000313|EMBL:EHU21744.1}; RN [1] {ECO:0000313|EMBL:EHU21744.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC2A {ECO:0000313|EMBL:EHU21744.1}; 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] {ECO:0000313|EMBL:EHU21744.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC2A {ECO:0000313|EMBL:EHU21744.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHU21744.1}. 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; AIFA01000071; EHU21744.1; -; Genomic_DNA. DR RefSeq; WP_000095940.1; NZ_AIFA01000071.1. DR EnsemblBacteria; EHU21744; EHU21744; ECDEC2A_4813. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHU21744.1}; KW Transferase {ECO:0000313|EMBL:EHU21744.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136052 MW; 0CD8269975292F72 CRC64; MSSKVEQLCA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVISAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPAEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPT ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANTQ QAEWRSWVVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KMLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK VSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAE // ID H4KQ69_ECOLX Unreviewed; 1227 AA. AC H4KQ69; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHU35867.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHU35867.1}; GN Name=metH {ECO:0000313|EMBL:EHU35867.1}; GN ORFNames=ECDEC2C_4874 {ECO:0000313|EMBL:EHU35867.1}; OS Escherichia coli DEC2C. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868140 {ECO:0000313|EMBL:EHU35867.1}; RN [1] {ECO:0000313|EMBL:EHU35867.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC2C {ECO:0000313|EMBL:EHU35867.1}; 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] {ECO:0000313|EMBL:EHU35867.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC2C {ECO:0000313|EMBL:EHU35867.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHU35867.1}. 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; AIFB01000072; EHU35867.1; -; Genomic_DNA. DR RefSeq; WP_000095940.1; NZ_AIFB01000072.1. DR EnsemblBacteria; EHU35867; EHU35867; ECDEC2C_4874. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHU35867.1}; KW Transferase {ECO:0000313|EMBL:EHU35867.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136052 MW; 0CD8269975292F72 CRC64; MSSKVEQLCA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVISAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPAEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPT ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANTQ QAEWRSWVVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KMLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK VSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAE // ID H4KYU7_ECOLX Unreviewed; 1227 AA. AC H4KYU7; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHU45830.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHU45830.1}; GN Name=metH {ECO:0000313|EMBL:EHU45830.1}; GN ORFNames=ECDEC2D_2199 {ECO:0000313|EMBL:EHU45830.1}; OS Escherichia coli DEC2D. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868141 {ECO:0000313|EMBL:EHU45830.1}; RN [1] {ECO:0000313|EMBL:EHU45830.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC2D {ECO:0000313|EMBL:EHU45830.1}; 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] {ECO:0000313|EMBL:EHU45830.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC2D {ECO:0000313|EMBL:EHU45830.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHU45830.1}. 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; AIFC01000020; EHU45830.1; -; Genomic_DNA. DR RefSeq; WP_000095940.1; NZ_AIFC01000020.1. DR EnsemblBacteria; EHU45830; EHU45830; ECDEC2D_2199. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHU45830.1}; KW Transferase {ECO:0000313|EMBL:EHU45830.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136052 MW; 0CD8269975292F72 CRC64; MSSKVEQLCA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVISAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPAEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPT ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANTQ QAEWRSWVVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KMLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK VSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAE // ID H4LKC7_ECOLX Unreviewed; 1227 AA. AC H4LKC7; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHU49594.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHU49594.1}; GN Name=metH {ECO:0000313|EMBL:EHU49594.1}; GN ORFNames=ECDEC2E_4850 {ECO:0000313|EMBL:EHU49594.1}; OS Escherichia coli DEC2E. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868142 {ECO:0000313|EMBL:EHU49594.1}; RN [1] {ECO:0000313|EMBL:EHU49594.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC2E {ECO:0000313|EMBL:EHU49594.1}; 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] {ECO:0000313|EMBL:EHU49594.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC2E {ECO:0000313|EMBL:EHU49594.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHU49594.1}. 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; AIFD01000054; EHU49594.1; -; Genomic_DNA. DR RefSeq; WP_000095940.1; NZ_AIFD01000054.1. DR EnsemblBacteria; EHU49594; EHU49594; ECDEC2E_4850. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHU49594.1}; KW Transferase {ECO:0000313|EMBL:EHU49594.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136052 MW; 0CD8269975292F72 CRC64; MSSKVEQLCA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVISAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPAEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPT ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANTQ QAEWRSWVVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KMLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK VSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAE // ID H4UCA3_ECOLX Unreviewed; 1227 AA. AC H4UCA3; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHV41519.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHV41519.1}; GN Name=metH {ECO:0000313|EMBL:EHV41519.1}; GN ORFNames=ECDEC5E_5026 {ECO:0000313|EMBL:EHV41519.1}; OS Escherichia coli DEC5E. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868159 {ECO:0000313|EMBL:EHV41519.1}; RN [1] {ECO:0000313|EMBL:EHV41519.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC5E {ECO:0000313|EMBL:EHV41519.1}; 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] {ECO:0000313|EMBL:EHV41519.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC5E {ECO:0000313|EMBL:EHV41519.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHV41519.1}. 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; AIFU01000027; EHV41519.1; -; Genomic_DNA. DR RefSeq; WP_000096047.1; NZ_AIFU01000027.1. DR ProteinModelPortal; H4UCA3; -. DR SMR; H4UCA3; 651-1227. DR EnsemblBacteria; EHV41519; EHV41519; ECDEC5E_5026. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHV41519.1}; KW Transferase {ECO:0000313|EMBL:EHV41519.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136040 MW; 8FB5738E12303E7E CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID H4US52_ECOLX Unreviewed; 1227 AA. AC H4US52; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHV51314.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHV51314.1}; GN Name=metH {ECO:0000313|EMBL:EHV51314.1}; GN ORFNames=ECDEC6A_4848 {ECO:0000313|EMBL:EHV51314.1}; OS Escherichia coli DEC6A. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868160 {ECO:0000313|EMBL:EHV51314.1}; RN [1] {ECO:0000313|EMBL:EHV51314.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC6A {ECO:0000313|EMBL:EHV51314.1}; 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] {ECO:0000313|EMBL:EHV51314.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC6A {ECO:0000313|EMBL:EHV51314.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHV51314.1}. 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; AIFV01000039; EHV51314.1; -; Genomic_DNA. DR RefSeq; WP_000096011.1; NZ_AIFV01000039.1. DR ProteinModelPortal; H4US52; -. DR SMR; H4US52; 6-639, 651-1227. DR PRIDE; H4US52; -. DR EnsemblBacteria; EHV51314; EHV51314; ECDEC6A_4848. DR OMA; DYNSIMV; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHV51314.1}; KW Transferase {ECO:0000313|EMBL:EHV51314.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135997 MW; 91F0CAA1E9127D9A CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAD // ID H4V8S8_ECOLX Unreviewed; 1227 AA. AC H4V8S8; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHV50784.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHV50784.1}; GN Name=metH {ECO:0000313|EMBL:EHV50784.1}; GN ORFNames=ECDEC6B_5128 {ECO:0000313|EMBL:EHV50784.1}; OS Escherichia coli DEC6B. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868161 {ECO:0000313|EMBL:EHV50784.1}; RN [1] {ECO:0000313|EMBL:EHV50784.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC6B {ECO:0000313|EMBL:EHV50784.1}; 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] {ECO:0000313|EMBL:EHV50784.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC6B {ECO:0000313|EMBL:EHV50784.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHV50784.1}. 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; AIFW01000048; EHV50784.1; -; Genomic_DNA. DR RefSeq; WP_000096011.1; NZ_AIFW01000048.1. DR ProteinModelPortal; H4V8S8; -. DR SMR; H4V8S8; 6-639, 651-1227. DR PRIDE; H4V8S8; -. DR EnsemblBacteria; EHV50784; EHV50784; ECDEC6B_5128. DR OMA; DYNSIMV; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHV50784.1}; KW Transferase {ECO:0000313|EMBL:EHV50784.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135997 MW; 91F0CAA1E9127D9A CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAD // ID H4Z4A3_ECOLX Unreviewed; 1227 AA. AC H4Z4A3; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHW04390.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHW04390.1}; GN Name=metH {ECO:0000313|EMBL:EHW04390.1}; GN ORFNames=ECDEC8A_4909 {ECO:0000313|EMBL:EHW04390.1}; OS Escherichia coli DEC8A. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868170 {ECO:0000313|EMBL:EHW04390.1}; RN [1] {ECO:0000313|EMBL:EHW04390.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC8A {ECO:0000313|EMBL:EHW04390.1}; 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] {ECO:0000313|EMBL:EHW04390.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC8A {ECO:0000313|EMBL:EHW04390.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHW04390.1}. 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; AIGF01000053; EHW04390.1; -; Genomic_DNA. DR RefSeq; WP_000096053.1; NZ_AIGF01000053.1. DR EnsemblBacteria; EHW04390; EHW04390; ECDEC8A_4909. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHW04390.1}; KW Transferase {ECO:0000313|EMBL:EHW04390.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136040 MW; D1A76336C7330E3D CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID H5A521_ECOLX Unreviewed; 1227 AA. AC H5A521; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHW09790.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHW09790.1}; GN Name=metH {ECO:0000313|EMBL:EHW09790.1}; GN ORFNames=ECDEC8C_5859 {ECO:0000313|EMBL:EHW09790.1}; OS Escherichia coli DEC8C. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868172 {ECO:0000313|EMBL:EHW09790.1}; RN [1] {ECO:0000313|EMBL:EHW09790.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC8C {ECO:0000313|EMBL:EHW09790.1}; 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] {ECO:0000313|EMBL:EHW09790.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC8C {ECO:0000313|EMBL:EHW09790.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHW09790.1}. 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; AIGH01000074; EHW09790.1; -; Genomic_DNA. DR RefSeq; WP_000096053.1; NZ_AIGH01000074.1. DR EnsemblBacteria; EHW09790; EHW09790; ECDEC8C_5859. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHW09790.1}; KW Transferase {ECO:0000313|EMBL:EHW09790.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136040 MW; D1A76336C7330E3D CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID H5EA70_ECOLX Unreviewed; 1227 AA. AC H5EA70; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHW62371.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHW62371.1}; GN Name=metH {ECO:0000313|EMBL:EHW62371.1}; GN ORFNames=ECDEC10B_5556 {ECO:0000313|EMBL:EHW62371.1}; OS Escherichia coli DEC10B. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868181 {ECO:0000313|EMBL:EHW62371.1}; RN [1] {ECO:0000313|EMBL:EHW62371.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC10B {ECO:0000313|EMBL:EHW62371.1}; 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] {ECO:0000313|EMBL:EHW62371.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC10B {ECO:0000313|EMBL:EHW62371.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHW62371.1}. 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; AIGQ01000075; EHW62371.1; -; Genomic_DNA. DR RefSeq; WP_000096053.1; NZ_AIGQ01000075.1. DR EnsemblBacteria; EHW62371; EHW62371; ECDEC10B_5556. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHW62371.1}; KW Transferase {ECO:0000313|EMBL:EHW62371.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136040 MW; D1A76336C7330E3D CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID H5G540_ECOLX Unreviewed; 1227 AA. AC H5G540; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHW85245.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHW85245.1}; GN Name=metH {ECO:0000313|EMBL:EHW85245.1}; GN ORFNames=ECDEC10F_5709 {ECO:0000313|EMBL:EHW85245.1}; OS Escherichia coli DEC10F. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868185 {ECO:0000313|EMBL:EHW85245.1}; RN [1] {ECO:0000313|EMBL:EHW85245.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC10F {ECO:0000313|EMBL:EHW85245.1}; 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] {ECO:0000313|EMBL:EHW85245.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC10F {ECO:0000313|EMBL:EHW85245.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHW85245.1}. 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; AIGU01000072; EHW85245.1; -; Genomic_DNA. DR RefSeq; WP_000096053.1; NZ_AIGU01000072.1. DR EnsemblBacteria; EHW85245; EHW85245; ECDEC10F_5709. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHW85245.1}; KW Transferase {ECO:0000313|EMBL:EHW85245.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136040 MW; D1A76336C7330E3D CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID H5IS16_ECOLX Unreviewed; 1227 AA. AC H5IS16; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHX24124.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHX24124.1}; GN Name=metH {ECO:0000313|EMBL:EHX24124.1}; GN ORFNames=ECDEC12A_4910 {ECO:0000313|EMBL:EHX24124.1}; OS Escherichia coli DEC12A. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868191 {ECO:0000313|EMBL:EHX24124.1}; RN [1] {ECO:0000313|EMBL:EHX24124.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC12A {ECO:0000313|EMBL:EHX24124.1}; 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] {ECO:0000313|EMBL:EHX24124.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC12A {ECO:0000313|EMBL:EHX24124.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHX24124.1}. 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; AIHA01000044; EHX24124.1; -; Genomic_DNA. DR RefSeq; WP_000096075.1; NZ_AIHA01000044.1. DR EnsemblBacteria; EHX24124; EHX24124; ECDEC12A_4910. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHX24124.1}; KW Transferase {ECO:0000313|EMBL:EHX24124.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136010 MW; 7D51E73DFC090607 CRC64; MSSKVEQLRA QLNQRILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENAAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAD // ID H5J9L9_ECOLX Unreviewed; 1227 AA. AC H5J9L9; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHX21521.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHX21521.1}; GN Name=metH {ECO:0000313|EMBL:EHX21521.1}; GN ORFNames=ECDEC12B_5369 {ECO:0000313|EMBL:EHX21521.1}; OS Escherichia coli DEC12B. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868192 {ECO:0000313|EMBL:EHX21521.1}; RN [1] {ECO:0000313|EMBL:EHX21521.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC12B {ECO:0000313|EMBL:EHX21521.1}; 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] {ECO:0000313|EMBL:EHX21521.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC12B {ECO:0000313|EMBL:EHX21521.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHX21521.1}. 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; AIHB01000073; EHX21521.1; -; Genomic_DNA. DR RefSeq; WP_000096075.1; NZ_AIHB01000073.1. DR EnsemblBacteria; EHX21521; EHX21521; ECDEC12B_5369. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHX21521.1}; KW Transferase {ECO:0000313|EMBL:EHX21521.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136010 MW; 7D51E73DFC090607 CRC64; MSSKVEQLRA QLNQRILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENAAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAD // ID H5JBW6_ECOLX Unreviewed; 1227 AA. AC H5JBW6; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHX39165.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHX39165.1}; GN Name=metH {ECO:0000313|EMBL:EHX39165.1}; GN ORFNames=ECDEC12C_5761 {ECO:0000313|EMBL:EHX39165.1}; OS Escherichia coli DEC12C. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868193 {ECO:0000313|EMBL:EHX39165.1}; RN [1] {ECO:0000313|EMBL:EHX39165.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC12C {ECO:0000313|EMBL:EHX39165.1}; 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] {ECO:0000313|EMBL:EHX39165.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC12C {ECO:0000313|EMBL:EHX39165.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHX39165.1}. 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; AIHC01000029; EHX39165.1; -; Genomic_DNA. DR RefSeq; WP_000096075.1; NZ_AIHC01000029.1. DR EnsemblBacteria; EHX39165; EHX39165; ECDEC12C_5761. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHX39165.1}; KW Transferase {ECO:0000313|EMBL:EHX39165.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136010 MW; 7D51E73DFC090607 CRC64; MSSKVEQLRA QLNQRILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENAAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAD // ID H5K6T0_ECOLX Unreviewed; 1227 AA. AC H5K6T0; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHX39244.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHX39244.1}; GN Name=metH {ECO:0000313|EMBL:EHX39244.1}; GN ORFNames=ECDEC12D_5042 {ECO:0000313|EMBL:EHX39244.1}; OS Escherichia coli DEC12D. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=868194 {ECO:0000313|EMBL:EHX39244.1}; RN [1] {ECO:0000313|EMBL:EHX39244.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC12D {ECO:0000313|EMBL:EHX39244.1}; 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] {ECO:0000313|EMBL:EHX39244.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DEC12D {ECO:0000313|EMBL:EHX39244.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHX39244.1}. 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; AIHD01000078; EHX39244.1; -; Genomic_DNA. DR RefSeq; WP_000096075.1; NZ_AIHD01000078.1. DR EnsemblBacteria; EHX39244; EHX39244; ECDEC12D_5042. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHX39244.1}; KW Transferase {ECO:0000313|EMBL:EHX39244.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136010 MW; 7D51E73DFC090607 CRC64; MSSKVEQLRA QLNQRILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENAAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAD // ID H5SHG0_9GAMM Unreviewed; 1215 AA. AC H5SHG0; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 01-APR-2015, entry version 18. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:BAL55596.1}; GN ORFNames=HGMM_F29A09C15 {ECO:0000313|EMBL:BAL55596.1}; OS uncultured gamma proteobacterium. OC Bacteria; Proteobacteria; Gammaproteobacteria; environmental samples. OX NCBI_TaxID=86473 {ECO:0000313|EMBL:BAL55596.1}; RN [1] {ECO:0000313|EMBL:BAL55596.1} 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] {ECO:0000313|EMBL:BAL55596.1} 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP011721; BAL55596.1; -; Genomic_DNA. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAL55596.1}; KW Transferase {ECO:0000313|EMBL:BAL55596.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 241 241 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 750 750 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1215 AA; 133743 MW; 8C2994FBE99D29B5 CRC64; MPSIRQILAE RILILDGAMG TLIQAHGLSE ADYRGKQFKD WPRELKGNND LLSLTQPEIV SEIHRRYLEA GADLIETNTF NANRISLADY GMEDLARELN FAAARLARQA ADAFSTETKP RFVAGVLGPT NRTASISPEV SDPGFRNVSF QDLVVAYTEA VAGLIEGGVD LILIETVFDT LNAKAAVFAV KQYLARHGLE RPLLISGTIT DASGRTLSGQ TPEAFWNSLR HAEPLAFGFN CALGPKELRQ YVEEISAYVD TFVSAHPNAG LPNAFGGYDE TPETMAEEIG AWAKEGWLNI VGGCCGTTPD HIRAIAEAVA GAPPRRVPKP KVMTRLAGLE PLNIGPDSLF VNIGERTNVT GSAHFRRLIQ EGRYDAALEI ARQQVANGAQ MIDVNLDEGM LDSKAAMVRF LNLVAAEPDI ARVPVMIDSS KWEVIEAGLQ CLQGKGVINS ISLKEGEETF LAHARLARLY GAAVVVMAFD EQGQADTKER KVEICTRAYR LLREKLDFPP EDIIFDPNVF AVATGIPEHR RYGLDFLEAV AEIKNTLPYA LTSGGISNVS FAFRGNDAVR EAIHAVFLYH AIRAGLDMGI VNAGQLGIYE EVPWELREAI EDVLLCRRED ADERLLQLAA SYRGAGEAKV QELEWRSWPV EKRLEHALVQ GIADYIEEDT EEARKLLGSP LAVIEGPLMA GMNVVGDLFG AGKMFLPQVV KSARVMKKAV AHLEPYLKAE RQEGKSAGKV LLATVKGDVH DIGKNIVGVV LQCNGFEVVD LGVMVPADKI LHAAREQQVD IVGLSGLITP SLDEMVHVAK EMARQGLDIP LLIGGATTSR VHTAVKIAPH YAAPVVYVPD ASRAVGVVGS LLSAELRGPF LANLAREYEE VRARHAKRQE SAKLLAIEAA RANRLRTDWA SYLPPVPRKP GIHVFDAYPL ETLVRYIDWS PFFQAWELVG SYPKILDDPV VGKEARRLLA DAEKLLEQLV AEKWLTAQGV FGLFSAASRG DDIVVKAHGR EWVLHHLRQQ QQKPQGQPNY CLADFVAPED SGVPDFIGAF AVTCGIGIEA QLERFAREHD DYRAILLEAL ADRLAEAFAE HLHERVRREF WGYAPYEDLS NEELIAEKYR GIRPAPGYPA CPDHTEKRAL FSLLGVEETT SIRLTESFAM HPGASVSGWY FSHPKAGYFN VGRIGRDQVE DYARRKGWRL SEAEQWLAPN LAYAP // ID H5SL32_9CHLR Unreviewed; 623 AA. AC H5SL32; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 07-JAN-2015, entry version 14. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HGMM_F01E07C31 {ECO:0000313|EMBL:BAL52559.1}, GN HGMM_F44F02C09 {ECO:0000313|EMBL:BAL56868.1}; OS uncultured Chloroflexi bacterium. OC Bacteria; Chloroflexi; environmental samples. OX NCBI_TaxID=166587 {ECO:0000313|EMBL:BAL56868.1}; RN [1] {ECO:0000313|EMBL:BAL56868.1} 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] {ECO:0000313|EMBL:BAL56868.1} 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011631; BAL52559.1; -; Genomic_DNA. DR EMBL; AP011760; BAL56868.1; -; Genomic_DNA. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:BAL56868.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:BAL56868.1}. SQ SEQUENCE 623 AA; 68113 MW; B19EB2C393C396FA CRC64; MSSHPFLDLL DQLEAPLLAD GAMGTMLHAH GISFDRCFDA LNLEQPQLVL DIHRQYVQAG ARLLLTNTFG ANRYKLERHG LANQLIEINQ AGVALARRAA QEGREQVFVA GDVGPLGVRV APYGRVRVEQ ARLAFAEQIQ VLAQAGADVI VIETMSDLNE ALLAIEAVRQ SCDLPLIVSL TFTRDDRTLL GDDPASAARR LSEAGVDVIG INCSSGPAQV LRILKQMRAV APQARFWVKP NAGWPEQVGG RIMYPASPAY FGEYSMAFCQ AGARVVGGCC GTTPAHIAAM HEALSRLPQQ CTAPQIEWTP PREEITPIEV PPSQLAQKLA DGRFVISVEM EPPRGLATEK LVAAASLLQE AGADVINVSD TPMARMRMSA WAVCEVIQRQ VGIETTLHFP TRGRNLLRVQ GDLLAAHALG IRNIFVVMGD PTAIGDYPEA TDNYDLVPSG LIKLIKQGFN LGVDHSGTSI GQPTRFFVGG ALNLTAAEPE QEIKNLRRKI KAGADFFITQ PIYRPEDGER FLEEYEKRHG ALEKPILIGI LPLVSLRHAR FLHHEVPGIS IPQEVQDRLE RAGDHAAQVG VELAIELIEK LKSWAQGIYL MPQFKRFDLI AEIIEAVKTT VKA // ID H5SL33_9CHLR Unreviewed; 1179 AA. AC H5SL33; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 01-APR-2015, entry version 20. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:BAL56869.1}; GN ORFNames=HGMM_F44F02C10 {ECO:0000313|EMBL:BAL56869.1}; OS uncultured Chloroflexi bacterium. OC Bacteria; Chloroflexi; environmental samples. OX NCBI_TaxID=166587 {ECO:0000313|EMBL:BAL56869.1}; RN [1] {ECO:0000313|EMBL:BAL56869.1} 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] {ECO:0000313|EMBL:BAL56869.1} 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP011760; BAL56869.1; -; Genomic_DNA. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 236 236 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 302 302 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 756 756 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1179 AA; 130825 MW; 64C5ED2E9EC456C9 CRC64; MTRKYTNRRY LDALETRVLI YDGAMGTNLQ KMNLRAEHFG GARYFGCNDY LVLTYPQAVE TVHRSFLEVG VDVIETNTFR SNRITLAEYG LADKVIEINR AAASLARRLA DEYAARSGQP RFVAGSIGPS GKLPSADDPE LSNITFDELA DVFREQAIGL IQGGVDVLLI ETSQDILEVK AAIHGILRAF EETGIWLPIQ AQVTLDTTGR MLLGTDIQAA LTILEGLPID VIGMNCSTGP EHMREPIRIL GEQSRLPVSC IPNAGLPLNV DGQAVYPLEP EPFAAALVEF VEKHHINVVG GCCGTTPAHL KLLVEKLHGR PRPPRPILSL PRLASAIQAV PMRQTPPPML IGERCNAQGS RKFKQLLLAE DYDGILELAR EQVNNGAHAL DISTALTERP DEAELMRKVV KKLSMGVEVP LVIDTTEVEV LEVALKTAPG RCLINSTHLE SGRTKADRVF RLAKEHNAAV ICLTIDEQGM AKTRERKLEV AKRIYELAVH EHGLPPESLV FDALTFTLAT GDPEFANSAI ETLEGIRLIK QNLPGVLTSL GVSNLSFGLA PHARPVLNSV MLYHAVEAGL DMAIINPAHV TAYADIPAEA RELAEDLIFN RRPDALQRYI EYFEKTRPQT SETAADPTSG MTAPQRLYWR IVHRHKEGVE ADIDEIIAEA LSQDTSDRPL GERRHAAAVH ILNNVLLPAM KEVGDKFGAG ELILPFVLQS AEVMKRAVAH LETYLEKKEG VSKGRIVLAT VYGDVHDIGK NLVKTILVNN GYEVIDLGKQ VPAEKIIQTA VETQATAIGL SALLVSTSRQ MPLIVNELHR RGLQFPVLIG GAAINRRFGR RILFTESGQP YLPGVFYCKD AFEGLETMDA LIDPQQRERL LERILREAEM ELGRATATPS TAARPRSAIV PKPLTPLPQK WGPRIVRQMP LEIVFQHLSK NELFRLSWGA KNTHGEEWEH LHAEFEERLA RMQKEALRYG WLKPQGVYGY WPCQSEGDDL IIYDPATLQS SSPEEIMRFT FPRQPDQEHL CLADYFASVD SGQFDVVAFQ VVTVGPMATE HFEQLQAEGN YTEAYFFHGL AVQTTEATAE YLHRHIRREL GLADGQGKRY SWGYPAIPDL ADHRKVFDLL PAESALGMSL TAAYQLVPEQ STAAIIVHHP QAKYYSVGES RVEQLLKNR // ID H5T7P7_9ALTE Unreviewed; 359 AA. AC H5T7P7; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Betaine-homocysteine S-methyltransferase {ECO:0000313|EMBL:GAB54324.1}; DE EC=2.1.1.5 {ECO:0000313|EMBL:GAB54324.1}; GN ORFNames=GPUN_0170 {ECO:0000313|EMBL:GAB54324.1}; OS Glaciecola punicea DSM 14233 = ACAM 611. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Glaciecola. OX NCBI_TaxID=1121923 {ECO:0000313|EMBL:GAB54324.1}; RN [1] {ECO:0000313|EMBL:GAB54324.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ACAM 611 {ECO:0000313|EMBL:GAB54324.1}; 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] {ECO:0000313|EMBL:GAB54324.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ACAM 611 {ECO:0000313|EMBL:GAB54324.1}; RA Qin Q.L., Xie B.B., Shu Y.L., Zhang Y.Z.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:GAB54324.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ACAM 611 {ECO:0000313|EMBL:GAB54324.1}; RX PubMed=25009843; RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J., RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.; RT "Comparative genomics of the marine bacterial genus Glaciecola reveals RT the high degree of genomic diversity and genomic characteristic for RT cold adaptation."; RL Environ. Microbiol. 16:1642-1653(2014). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAB54324.1}. 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; BAET01000002; GAB54324.1; -; Genomic_DNA. DR RefSeq; WP_006002430.1; NZ_BAET01000002.1. DR EnsemblBacteria; GAB54324; GAB54324; GPUN_0170. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:GAB54324.1}; KW Transferase {ECO:0000313|EMBL:GAB54324.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 219 219 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 359 AA; 39739 MW; BF4DC71EB2A37238 CRC64; MEACQKSYRS FVLVELAGHI NKGPVICAEG FLFELERRGY LTAGEFVPEV ALEHPEVLES LHRDFQRAGS DIVEAFTYNG HREKMRVIGK EELLEPLNRA ALKIARKVAD SKPGNLMAGN ISNTNIWHPT DTNKQQEVRS MFEEMVGWAV EEGVDIIIGE TFYYAEEAYT ALEVAKASGL PVIITLAPMA SNQMQDGVSV VETCVELEKR GADVVGLNCF RGPQTMLPYL KEIRAAVSCH VAALPIPYRT NEKEPTFFNL SDHDSCTCPA PHGRAFPTAL DPLYCNRYEI GQFAKDAYAL GINYLGVCCG ASPMLLRQMA EAVGITTEAS RFSENMSNHF MYGSNERLPE NIKALGDKA // ID H5TCE4_9ALTE Unreviewed; 1244 AA. AC H5TCE4; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:GAB55971.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:GAB55971.1}; GN Name=metH {ECO:0000313|EMBL:GAB55971.1}; GN ORFNames=GPUN_1855 {ECO:0000313|EMBL:GAB55971.1}; OS Glaciecola punicea DSM 14233 = ACAM 611. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Glaciecola. OX NCBI_TaxID=1121923 {ECO:0000313|EMBL:GAB55971.1}; RN [1] {ECO:0000313|EMBL:GAB55971.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ACAM 611 {ECO:0000313|EMBL:GAB55971.1}; 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] {ECO:0000313|EMBL:GAB55971.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ACAM 611 {ECO:0000313|EMBL:GAB55971.1}; RA Qin Q.L., Xie B.B., Shu Y.L., Zhang Y.Z.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:GAB55971.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ACAM 611 {ECO:0000313|EMBL:GAB55971.1}; RX PubMed=25009843; RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J., RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.; RT "Comparative genomics of the marine bacterial genus Glaciecola reveals RT the high degree of genomic diversity and genomic characteristic for RT cold adaptation."; RL Environ. Microbiol. 16:1642-1653(2014). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:GAB55971.1}. 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; BAET01000019; GAB55971.1; -; Genomic_DNA. DR RefSeq; WP_006005610.1; NZ_BAET01000019.1. DR EnsemblBacteria; GAB55971; GAB55971; GPUN_1855. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:GAB55971.1}; KW Transferase {ECO:0000313|EMBL:GAB55971.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 251 251 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 315 315 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 762 762 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1244 AA; 137176 MW; 8B272528BA328E78 CRC64; MAKPQQFPSS LLEQQLAKRI LLLDGAMGTM IQAYDFSEED YRGERFANWS CDVKGNNDLL VLSQPHIIST IHREYLAAGA DILETNTFNA TRIAMADYEM ENLSREINVQ AAKIARKVAD EYTALNPDKP RFVAGVLGPT NRTCSISPDV NDPAFRNVTF DELKDAYIES ILALLEGGAD IIMIETIFDT LNAKAAVFAV EQVFSDLGKR YPVMISGTIT DASGRTLSGQ TTEAFYNSLA HAKPISFGLN CALGPKELRQ YVEELSRISS CAVSAHPNAG LPNAFGGYDL DAQEMNEHIK EWAQSGLLNI VGGCCGTTPE HIRVMAEVLA NIPPRIIKDI KVACRLSGLE ALTIDAKSLF VNVGERTNVT GSALFKKLIV EELYDDALSV ALQQVENGAQ IIDINMDEGM LDSKTAMQRF LNMIAGEPDI AKVPIMIDSS KWDILEAGLK CVQGKGIVNS ISLKEGEDNF REQAELIRRY GAAVIVMAFD EVGQADTRVR KFQICQRAYN ILVDELNFPP QDIIFDPNIF AVATGIEEHN NYAVDFIEAV ADIKKNLPHA MISGGVSNVS FSFRGNNAVR EAIHAVFLYY AIKNGMDMGI VNAGQLAILK DVPADLRKAV EHVVQNSDDG ATERLLDVAA KYSSTGGAKS SVLDLSWREL STHKRLEHAL VKGINAFIIE DTEAARLEAK IPLHVIEGPL MDGMNIVGDL FGEGQMFLPQ VVKSARVMKQ AVAHLQPFIE EGKTEITDNG KVLMATVKGD VHDIGKNIVG VVLQCNNFAI TDLGVMVACE KILTTARELK VDVIGLSGLI TPSLDEMVHI AKEMQRQGFT IPLLIGGATT SKAHTAVKIQ PHYKHGVVYV PNASRSVSVV QTLLNSGKAE FLANIDKEYE KVRARHYAKG PRSTLVSLEK ARANAVPLSF DKYVPVKPQK LGVTVLNDVP LDIVREYIDW TPFFMTWQLS GKYPRILEHE LIGEVATDLF NDANKMLDEI IGNKSICGKA VFGLFPANRV GDDIEVYLDE SRTKVNKKLC QLRQQSKKPT GQFNRCLSDY IAHKNDGIED YIGAFAVSAG FGGDALVAQY DKENDTYNSI LCKAVTDRLA EALAEYLHQQ IRMVYWGYTK DEKLDNTALI RESYQGIRPA PGYPACPEHT EKGVLWELLD VENNIGMTLT SSFAMWPGAA VSGWYFAHPE SKYFAVAKLT QDQVHDYAKR KNMHVKEAER WLAANLDYEP EQAETVVQAE LAVV // ID H5TEY9_9ALTE Unreviewed; 314 AA. AC H5TEY9; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:GAB56916.1}; GN ORFNames=GPUN_2802 {ECO:0000313|EMBL:GAB56916.1}; OS Glaciecola punicea DSM 14233 = ACAM 611. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Glaciecola. OX NCBI_TaxID=1121923 {ECO:0000313|EMBL:GAB56916.1}; RN [1] {ECO:0000313|EMBL:GAB56916.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ACAM 611 {ECO:0000313|EMBL:GAB56916.1}; 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] {ECO:0000313|EMBL:GAB56916.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ACAM 611 {ECO:0000313|EMBL:GAB56916.1}; RA Qin Q.L., Xie B.B., Shu Y.L., Zhang Y.Z.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:GAB56916.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ACAM 611 {ECO:0000313|EMBL:GAB56916.1}; RX PubMed=25009843; RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J., RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.; RT "Comparative genomics of the marine bacterial genus Glaciecola reveals RT the high degree of genomic diversity and genomic characteristic for RT cold adaptation."; RL Environ. Microbiol. 16:1642-1653(2014). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAB56916.1}. 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; BAET01000033; GAB56916.1; -; Genomic_DNA. DR RefSeq; WP_006007567.1; NZ_BAET01000033.1. DR EnsemblBacteria; GAB56916; GAB56916; GPUN_2802. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 204 204 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 292 292 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 314 AA; 33626 MW; 6125517B53E0693F CRC64; MTKITLLDGG MGQELLRRSS RLATRLWSAD IMHNEPSLVR DLHRDFILAG ARVITLNNYT ATPERLTREN VPEQLESLHS AAIRAATQAV EIAQCDGVKI AGCLPPLVAS YQPEVILTYP EALASYRRLV QLQYNACDVF LCETMASIAE ASAACTAGVE SGKPVWVALT VSDSHFGLLR SGESLTKAVA VLSSLGAHAI LLNCSQPEAI SACWPDLSWA AKTTVNASGQ KASLPSHTLE IGAYANGFVS IDSLHPGVTV DVLEARMDLN PQEYAEVAMQ WVTNGASIIG GCCEIGPAHI QVLHDSLCEK GYLV // ID H5THE4_9ACTO Unreviewed; 1203 AA. AC H5THE4; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:GAB32902.1}; GN Name=metH {ECO:0000313|EMBL:GAB32902.1}; GN ORFNames=GOOTI_033_00110 {ECO:0000313|EMBL:GAB32902.1}; OS Gordonia otitidis NBRC 100426. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Gordoniaceae; Gordonia. OX NCBI_TaxID=1108044 {ECO:0000313|EMBL:GAB32902.1}; RN [1] {ECO:0000313|EMBL:GAB32902.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NBRC 100426 {ECO:0000313|EMBL:GAB32902.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:GAB32902.1}. 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; BAFB01000033; GAB32902.1; -; Genomic_DNA. DR RefSeq; WP_007237163.1; NZ_BAFB01000033.1. DR EnsemblBacteria; GAB32902; GAB32902; GOOTI_033_00110. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 235 235 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 301 301 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 302 302 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 754 754 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1203 AA; 131423 MW; EB40F7BBDD99EB5C CRC64; MSDPTRTDSD FDTTFLTDMS RRVLIGDGAM GTMLQAADLT LDDFNNLEGC NEILNDTRPD VLADIHRAYF EAGADAVETN TFGCNLSNLG DYDIADRIRE LSFKGTSIAR GVADEMGPSS DGTGRYVLGS IGPGTKLPSL RHTTFDVIRD AYFECVAGML DGGADAILVE TSQDLLQVKA AVVAAKRAMA ELGRRIPIIS HVTVETTGTM LLGSEIGAAL TAIEPLGVDM IGLNCATGPA EMSEHLRYLS RHARIPVSVM PNAGLPELGP NGAVYPLQPH ELAESLATFV GEFGLSFVGG CCGTTPDHIR EVAAAVSEVT KARRTPQHES ETSSLYTAVP FDQDASFLVI GERTNSNGSK AFREAMIAED YQRCLDIAKD QTRDGAHMLD LNVDYVGRDG SADMTALASR FATSSTLPIM LDSTEPEVIR AGLETLGGRC AVNSVNYEDG DGPDSRFARI MRLVVEHGAA VVALTIDEEG QARTADWKVR VAERLIADIT GNWGLSEEDI ILDTLTFPIS TGQEEVRKDG IETIEAIRRL HESHPDVHFT LGISNISFGL NPAARQVLNS VFLHECVQAG LDTAIVHASK ILPMARIPEE QREVALDLVY DRRRPRGTNG EDDPGYDPLQ KLMELFEGVS AASARESRAA ELAKLPLFER LERRIVDGER NGLEADLDEA MTQKPPLEII NETLLSGMKT VGELFGSGQM QLPFVLQSAE VMKTAVAHLE PHMEATGEDG KGRIVLATVK GDVHDIGKNL VDIILSNNGY EVVNIGIKQP ISTILEVAED KRADVIGMSG LLVKSTVVMK ENLEEINARG LADNYPVLLG GAALTRSYVE NDLSDTYEGD VHYARDAFEG LRLMDDIMAL KRGGGSVPES ADSIAAAQKA AERKARHERS KRIAAKRKAA ETPVEIPARS DVAADNDVPT PPFWGTRIIK GVPVADYRQL LDERALFLGQ WGLRGARGGN GPSYEELVET EGRPRLRYWI DRLSTEGILQ HAAVVYGYFP AVSEGDTVHV LTEPRPDVPV RHSFSFPRQQ RPKFLCIADF IRSREDAITT GQVDVLPFQL VTMGQPIADF ANKLFADDAY RDYLEVHGIG VQLTEALAEY WHQRVRSELM VGDRSLGTED PDAAQGFFDL EYRGARFSFG YGACPNLEDR ATMMELLEPE RIGVELSEEL QLHPEQSTDA FVLHHPEAKY FNV // ID H5TWG4_9ACTO Unreviewed; 1194 AA. AC H5TWG4; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:GAB37822.1}; GN Name=metH {ECO:0000313|EMBL:GAB37822.1}; GN ORFNames=GOSPT_022_01670 {ECO:0000313|EMBL:GAB37822.1}; OS Gordonia sputi NBRC 100414. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Gordoniaceae; Gordonia. OX NCBI_TaxID=1089453 {ECO:0000313|EMBL:GAB37822.1}; RN [1] {ECO:0000313|EMBL:GAB37822.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NBRC 100414 {ECO:0000313|EMBL:GAB37822.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:GAB37822.1}. 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; BAFC01000022; GAB37822.1; -; Genomic_DNA. DR RefSeq; WP_005202919.1; NZ_BAFC01000022.1. DR EnsemblBacteria; GAB37822; GAB37822; GOSPT_022_01670. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 235 235 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 301 301 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 302 302 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 745 745 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1194 AA; 130021 MW; 9BE7E4A4AED466F8 CRC64; MSNPSRTATD LDTTFLTDMS RRVLIGDGAM GTMLQAADLT LDDFNNLEGC NEILNDTRPD VLADIHRAYF EAGADAVETN TFGCNLSNLG DYDIADRIRE LSFKGTSIAR GVADEMGPSS DGTGRYVLGS IGPGTKLPSL GHTTFEAIRD AYFECVAGML DGGADAILVE TSQDLLQVKA AVLAAKRAMA QLGRRIPIIS HVTVETTGTM LLGSEIGAAL TAIEPLGVDM IGLNCATGPA EMSEHLRYLS RHATIPVSVM PNAGLPELGP NGAVYPLQPD ELASSLATFV GEFGLSFVGG CCGTTPDHIR EVAAAVADVT KAQRNPQHES ETSSLYTAVP FDQDASFLVI GERTNSNGSK AFREAMLAED YQKCLDIAKD QTRDGAHMLD LNVDYVGRDG AADMTALAGR FATSSTLPIM LDSTEPEVIR AGLEALGGRC AVNSVNYEDG DGPDSRFARI MRLAVEHGAA VVALTIDEEG QARTADWKVR VAERLIADIT GNWGLAEEDI ILDTLTFPIS TGQEEVRKDG IETIEAIRRL HEAHPEVHFT LGISNISFGL NPAARQVLNS VFLHECVQAG LDTAIVHASK ILPMARIPDE QRDVALDLIY DRRRDGYDPL QKLMELFEGV SAASARETRA AELNRLPLFE RLERRIVDGE RNGLEADLDE AMTQKPPLEI INETLLSGMK TVGELFGSGQ MQLPFVLQSA EVMKTAVAHL EPHMEATGED GKGRIVLATV KGDVHDIGKN LVDIILSNNG YEVVNIGIKQ PISTILEVAE DKRADVIGMS GLLVKSTVVM KENLEEINAR GLADNYPVLL GGAALTRSYV ENDLSEAYEG DVHYARDAFE GLRLMDDIMA LKRGGGSVPE SADSIAAAQK AAERKARHER SKRIAAKRKA AETPIEVPAR SDVAADNDVP TPPFWGTRII KGVPVAEYRQ LLDERALFLG QWGLRGARGG DGPSYEELVE TEGRPRLRYW IDRLSTEGIL QHASVVYGYF PAVSEGDTVH VLTEPRPDAP VRYSFSFPRQ QRPKFLCIAD FIRSRDDAVA TGQVDVLPFQ LVTMGQPIAD FANKLFADDA YRDYLEVHGI GVQLTEALAE YWHQRVRSEL TVGDKSFGSE DPDAAQGFFD LEYRGARFSF GYGACPNLED RVTMMKLLEP ERIGVELSEE LQLHPEQSTD AFVLHHPEAK YFNV // ID H5U9F7_9ACTO Unreviewed; 1196 AA. AC H5U9F7; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:GAB42365.1}; GN Name=metH {ECO:0000313|EMBL:GAB42365.1}; GN ORFNames=GOTRE_014_00600 {ECO:0000313|EMBL:GAB42365.1}; OS Gordonia terrae NBRC 100016. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Gordoniaceae; Gordonia. OX NCBI_TaxID=1089454 {ECO:0000313|EMBL:GAB42365.1}; RN [1] {ECO:0000313|EMBL:GAB42365.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NBRC 100016 {ECO:0000313|EMBL:GAB42365.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:GAB42365.1}. 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; BAFD01000014; GAB42365.1; -; Genomic_DNA. DR RefSeq; WP_004019088.1; NZ_BAFD01000014.1. DR EnsemblBacteria; GAB42365; GAB42365; GOTRE_014_00600. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 237 237 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 747 747 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1196 AA; 130409 MW; F2A631E3AF28362E CRC64; MSPDFSGTDP RDFDTTFLSS MSRRVLIGDG AMGTMLQAAD LTLDDFRGLE GCNEILNDTR PDVLEGIHRA YFEAGADAVE TNTFGCNLSN LGDYDIADRI RELSYKGTAI ARGVADEMGP SADGTARFVL GSIGPGTKLP SLGHTTYAAI RDAYLECVIG MLEGGADAVL IETSQDLLQV KSAVVAAHRA MERVGRRIPI ISHVTVETTG TMLLGSEIGA ALTALEPLGI DLIGLNCATG PAEMSEHLRY LSKHARIPVS VMPNAGLPVL GANGAEYPLT PEELAQAMAQ FVGEFGLEFV GGCCGTTPEH IRQVAAAVAE VTPATRTPEH ESETSSLYSA VPFDQDASFL VIGERTNTNG SKAFREAMIA EDYQKCLDIA KDQTRDGAHM LDLNVDYVGR DGAADMTALA SRFATSSTLP IMLDSTEPEV IRAGLESLGG RCAVNSVNYE DGDGPDSRFT KIMQLVVEHG AAVVALTIDE EGQARTADWK VRVAERLIAD ITGNWGLAEE DIILDTLTFP ISTGQEEVRR DGIETIEAIR RLHEAHPDVH FTLGISNISF GLNPAARQVL NSVFLHECVQ AGLDTAIVHA SKILPMARIP EEHREVALDL VYDRRREGYD PLQKLMELFE GVSAASARES RAQELAKLPL FERLERRIVD GERNGLTDDL DEAMTQVPPL SIINDTLLSG MKTVGELFGS GQMQLPFVLQ SAEVMKTAVA HLEPHMEATG EDGKGRIVLA TVKGDVHDIG KNLVDIILSN NGYEVVNIGI KQPIATILDV AADKRADVIG MSGLLVKSTV VMKENLEEIN SRGLADEYPV LLGGAALTRS YVENDLSETY EGDVHYARDA FEGLRLMDDI MATKRGGGPD PDSAEAKAAA EKAAERKARH DRSKRIAAKR KAAEEPVEVP ARSDVAADNE IPTPPFWGSR IVKGVPIADY MQLLDERALF LGQWGLRGAR GGDGPSYEEL VETEGRPRLR YWIDRLSTEN ILQHAAVVYG YFPAVSDGDT VHVLTEPEPD APVRFSFTFP RQQRSRFLCI ADFIRSRDDA KAAGKVDVLP FQLVTMGQPI ADFANTLFAE DAYRDYLEVH GIGVQLTEAL AEYWHQRVRS ELTFGDRTMD SEDPENAQGF FDLEYRGARF SFGYGACPDL EDRAKMIELL EPGRIGVELS EELQLHPEQS TDAFVLHHPE AKYFNT // ID H5UTH1_9MICO Unreviewed; 1195 AA. AC H5UTH1; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:GAB49029.1}; GN Name=metH {ECO:0000313|EMBL:GAB49029.1}; GN ORFNames=MOPEL_096_00360 {ECO:0000313|EMBL:GAB49029.1}; OS Mobilicoccus pelagius NBRC 104925. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Dermatophilaceae; Mobilicoccus. OX NCBI_TaxID=1089455 {ECO:0000313|EMBL:GAB49029.1}; RN [1] {ECO:0000313|EMBL:GAB49029.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NBRC 104925 {ECO:0000313|EMBL:GAB49029.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:GAB49029.1}. 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; BAFE01000073; GAB49029.1; -; Genomic_DNA. DR RefSeq; WP_009482927.1; NZ_BAFE01000073.1. DR EnsemblBacteria; GAB49029; GAB49029; MOPEL_096_00360. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 226 226 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 292 292 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 753 753 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1195 AA; 130003 MW; 48EFB86F678BFE7B CRC64; MSSRSDQFRT LLSERVIVAD GAMGTMLQAA DPSMEDFENL EGCNEILNVT RPDIVRSVHE EYLTVGVDAV ETNTFGANWA NLAEYDIADR IEELAEAGAR IAREACDAHA TQDKPRFVLG SMGPGTKLPS LLHAPYAQLR DAYQECARGL VRGGADALLV ETCQDLLQAK AAIVGSRRAL AELGEDVPII CSVTVETTGT MLMGTEIGAA LVALEPLGID MISLNCATGP AEMSEHLRHL SQNARIAVGC MPNAGLPELG KDGAVYPLGP DDLAKAHRRF VEDYGLSLVG GCCGTTPAHL AAVVEAVGGM PVTPRDPRPE PAVSSLYTAV PFRQDASFLS IGERTNANGS KAFREAMLAA DWEQCVEIAK NQTREGAHLL DVCADYVGRD GAEDMSEIVS RFATSSTLPL VLDSTEPGVV EAGLERMGGR AVINSVNYED GDGPDSRFTR MMRLAKEHGA AVVALTIDEN GQARTADGKV EIATRLVEAI TNDWGMRVED IVVDALTFPI ATGQEETRRD GLETLEAIRR ITEAYPDIQT TLGVSNVSFG LKPAARVVLN SVFLDECVKA GLSSAIVNAA KILPIARIDE GQYKVALDLV YDRREWAGEP GESECTYDPL QVMLEMFEGV DSASLKESRL EELNSLPVGE RLAQRIIDGE RQGLDADLDE AVAGGTPALQ IINDHLLEGM KVVGERFGAG TMQLPFVLQS AETMKAAVAH LEPVIEEQVA ASGGTGRQAK AKVLLATVKG DVHDIGKNLV DIILSNNGYD VVNIGIKKTV NEIIEAAEEN DVDVVGMSGL LVKSTVVMKD NLEEFNKRGL AAKWPVMLGG AALTRVYVED DLASMYEGHV RYARDAFEGL RLMDAIAAAK RDGSDLAEAL PPLKKRRVAR SSAAEEGAEF TDTTRSDVAR LAEVPTPPFW GTRIVKGIAL ADYAAYLDER ATFLGQWGLK PTRGGDGPDY EELVETEGRP RLRMWLDRIK TEDIMEPAVV YGYFPCYSEG NDLVVLWHEG GTHTVDGREV EHHEGDIRER FTFPRQRRDR RLDLADFFRS KEEYEKTGVP DVVPFQLVTM GAKVSDVTAG LYAKNAYRDY LELHGLSVQL TEALAEMWHA RVRDELGIGD PDSLGLGEIL DVKFRGCRYS FGYPACPELG DRATMVRLLE PERIGVELSE ELQLHPEQST DAMVVHHPEA SYFKV // ID H5UUW3_9MICO Unreviewed; 319 AA. AC H5UUW3; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 9. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:GAB49521.1}; GN Name=mmuM {ECO:0000313|EMBL:GAB49521.1}; GN ORFNames=MOPEL_130_01280 {ECO:0000313|EMBL:GAB49521.1}; OS Mobilicoccus pelagius NBRC 104925. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Dermatophilaceae; Mobilicoccus. OX NCBI_TaxID=1089455 {ECO:0000313|EMBL:GAB49521.1}; RN [1] {ECO:0000313|EMBL:GAB49521.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NBRC 104925 {ECO:0000313|EMBL:GAB49521.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAB49521.1}. 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; BAFE01000089; GAB49521.1; -; Genomic_DNA. DR RefSeq; WP_009483364.1; NZ_BAFE01000089.1. DR EnsemblBacteria; GAB49521; GAB49521; MOPEL_130_01280. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:GAB49521.1}; KW Transferase {ECO:0000313|EMBL:GAB49521.1}. SQ SEQUENCE 319 AA; 32893 MW; 12148EC77C6F2256 CRC64; MGRTVGSMTS RPVDLLGGEV WVADGGLATQ LEAMGHDLID ALWSARLLHD DPEAIVEAHL HFLRAGARIV TTASYQATDE GFAAAGMDAD ETTQFLRRSV DLAREAVDRH VADGGTRALV AASVGPYGAM LADGSEYRGR YGLTVADLRE FHARRVDVLA GEVADGGADL LALETIPDVD EVVALTDLLG AAGVPGWVSC TVEAGRTRAG QPLADAVAAA ADTGEVVAIG ANCCAPRDVE AVLDAVATAG RGRPAVVYPN SGEGWDARAR TWTGTGTDLA ALAPGWVEAG ARIVGGCCRV GPDRIAALAR AVTKSTRVN // ID H5V105_ESCHE Unreviewed; 311 AA. AC H5V105; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 9. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:GAB51663.1}; GN Name=mmuM {ECO:0000313|EMBL:GAB51663.1}; GN ORFNames=EH105704_03_01680 {ECO:0000313|EMBL:GAB51663.1}; OS Escherichia hermannii NBRC 105704. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1115512 {ECO:0000313|EMBL:GAB51663.1}; RN [1] {ECO:0000313|EMBL:GAB51663.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NBRC 105704 {ECO:0000313|EMBL:GAB51663.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAB51663.1}. 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; BAFF01000003; GAB51663.1; -; Genomic_DNA. DR RefSeq; WP_002435019.1; NZ_BAFF01000003.1. DR EnsemblBacteria; GAB51663; GAB51663; EH105704_03_01680. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:GAB51663.1}; KW Transferase {ECO:0000313|EMBL:GAB51663.1}. SQ SEQUENCE 311 AA; 33197 MW; 9FD6A2635FC87576 CRC64; MPLNNPLLPL LAQSPFIVLD GALATELEAR GCDLNDTLWS AKVLLENPES VYQVHLDYFR AGAQCAVTAS YQATPAGFAA RGMNEAQATA LIKQSVELAQ RARTDFLAER PDSGALLIAG SVGPYGAYLA DGSEYRGDYT LSQAAYCDFH RPRMAALVEA GVDLLACETL PSFAETRALV ALLAECPDTT AWFSFTLHDS HHLSDGTPLE DVVALLDGHD QVLAIGVNCI APEQATAALQ TLHGMTTLPL VVYPNSGETY DAQTKCWTAG GQTCDSLDGY LDDWLCAGAR LIGGCCRTTP ADIALLAQRQ R // ID H5V782_ESCHE Unreviewed; 1227 AA. AC H5V782; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:GAB53840.1}; GN Name=metH {ECO:0000313|EMBL:GAB53840.1}; GN ORFNames=EH105704_21_00410 {ECO:0000313|EMBL:GAB53840.1}; OS Escherichia hermannii NBRC 105704. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1115512 {ECO:0000313|EMBL:GAB53840.1}; RN [1] {ECO:0000313|EMBL:GAB53840.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NBRC 105704 {ECO:0000313|EMBL:GAB53840.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:GAB53840.1}. 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; BAFF01000021; GAB53840.1; -; Genomic_DNA. DR RefSeq; WP_002438417.1; NZ_BAFF01000021.1. DR EnsemblBacteria; GAB53840; GAB53840; EH105704_21_00410. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135617 MW; 76FCB8D216B04F77 CRC64; MSLIVEKLQQ QLSKRILILD GGMGTMIQSY RLEEADYRGE RFADWPSDLK GNNDLLVLTK PEIIAAIHYA YFEAGADIIE TNTFNATTIA MADYHMESLS AEINYEAAKL ARACADEWTA RTPDKPRYVA GVLGPTNRTA SISPNVNDPA FRNVTFNQLV EAYRESTRAL VEGGADLILI ETVFDTLNAK AAVFAVKSEF EALGVDLPIM ISGTITDASG RTLSGQTTEA FYNSLRHADA LSFGLNCALG PDELRQYVAE LSRIAHCYVT AHPNAGLPNA FGEYDLDADV MAAQIGEWAQ AGFLNIVGGC CGTTPAHIAA MSKAVEGVAP RKLPDIPVAC RLSGLEPLNI GADSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALEVALQQ VESGAQIIDI NMDEGMLDAE VAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLQCIQG KGIVNSISMK EGVDTFIHHA KLVRRYGAAM VVMAFDEVGQ ADTRERKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHAMISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRREDGTER LLELAEKYRG SKGDDAANAQ QAEWRTWDVA KRLEYSLVKG ITEFIEEDTE QARLEAARPI DVIEGPLMAG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA WLEPFINASK EQGKSNGKIV LATVKGDVHD IGKNIVGVVL QCNNYEIIDL GVMVPTDKIL KTAREVNADI IGLSGLITPS LDEMVNVAKE MERQGFTLPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVSSL LSDTLRDDFV ARTRKEYETV RVQHGRKKPR TPPVTLQAAR ENDLAFDWES YTPPVAHRLG VQEVTASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG EEAKRLFKDA NEMLDQLSAE KSLNPRGVVG LFPANRVGDD IEVYRDETRT HVLAVSHHLR QQTEKVGFAN YCLADFVAPK LSGKADYLGA FAVTGGLEED ALAEAFDAQH DDYNKIMVKA VADRLAEAFA EYLHERVRKV YWGYAANENL SNEELIRENY QGIRPAPGYP ACPEHTEKAA IWQLLDVENR IGMKLTESYA MWPGASVSGW YFSHPDSKYF AVAQLQRDQI EDYARRKGMS VSEVERWLAP NLGYDAD // ID H5WCB6_RALSL Unreviewed; 346 AA. AC H5WCB6; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase protein {ECO:0000313|EMBL:CCF97437.1}; GN Name=metHa {ECO:0000313|EMBL:CCF97437.1}; GN ORFNames=RSK60_2070018 {ECO:0000313|EMBL:CCF97437.1}; OS Ralstonia solanacearum K60-1. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=1091042 {ECO:0000313|EMBL:CCF97437.1}; RN [1] {ECO:0000313|EMBL:CCF97437.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=K60 {ECO:0000313|EMBL:CCF97437.1}; RA LABGeM C.E.A.; RT "Ralstonia solanacearum K60, WGS."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CCF97437.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=K60 {ECO:0000313|EMBL:CCF97437.1}; 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. {ECO:0000313|EMBL:CCF97437.1}. 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; CAGT01000121; CCF97437.1; -; Genomic_DNA. DR RefSeq; WP_003270017.1; NZ_CAGT01000121.1. DR EnsemblBacteria; CCF97437; CCF97437; RSK60_2070018. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:CCF97437.1}; KW Transferase {ECO:0000313|EMBL:CCF97437.1}. SQ SEQUENCE 346 AA; 37450 MW; B155394ED0AB0606 CRC64; MTAPLPYTRA ANLPALLRQR ILILDGAMGT MIQRYKLTEA QYRGERFAGH PVDVKGNNEL LLLTAPEVIR EIHEQYLAAG ADLIETNTFG ATTVAQEDYK MAELAYEMNV VAARLAREAC DKYSTPDKPR FVAGAFGPTP KTASISPDVN DPGARNINFD QLRDAYYEQG KALLEGGADV FLVETIFDTL NAKAALFAID QLFEDLGERV PVMISGTVTD ASGRILSGQT VEAFWNSLRH AKPITFGLNC ALGAALMRPY IAELAKICDT AVSCYPNAGL PNPMSDTGFD ETPDVTSSLV DEFAAAGLVN LVGGCCGTTP EHIKAIAERV AQRKPRAWPG QYREAA // ID H5WUF9_9BURK Unreviewed; 353 AA. AC H5WUF9; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Cobalamin-dependent methionine synthase I {ECO:0000313|EMBL:EHR69178.1}; GN ORFNames=BurJ1DRAFT_0281 {ECO:0000313|EMBL:EHR69178.1}; OS Burkholderiales bacterium JOSHI_001. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales. OX NCBI_TaxID=864051 {ECO:0000313|EMBL:EHR69178.1, ECO:0000313|Proteomes:UP000004674}; RN [1] {ECO:0000313|EMBL:EHR69178.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=JOSHI_001 {ECO:0000313|EMBL:EHR69178.1}; 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., Lu M., Detter J.C., Han C., RA Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., RA Smith J., Lewis G., Woyke T.; RT "Noncontiguous Finished sequence of Burkholderiales bacterium RT JOSHI_001."; 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; CM001438; EHR69178.1; -; Genomic_DNA. DR RefSeq; WP_009548324.1; NZ_CM001438.1. DR EnsemblBacteria; EHR69178; EHR69178; BurJ1DRAFT_0281. DR Proteomes; UP000004674; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000004674}; KW Reference proteome {ECO:0000313|Proteomes:UP000004674}. SQ SEQUENCE 353 AA; 37697 MW; 6054A13F1459116B CRC64; MNAQSQSPKF TRGAQLPEVL AQRIAVIDGA MGTMVQRYKL GEADFRSERF ADHPKDLKGN NDLLVLTRPD VIREIHRQYL AAGADIIETN TFGATSIAQE DYALGHIAHE MNVAAARIAR LEADAAATPD KPRFVAGALG PTPRTASISP DVNDPGARNV SFDQLRDAYR EQAAGLLEGG CDLFLVETIF DTLNAKAAIF ALDELMEDTG ERLPVIVSGT VTDASGRILS GQTVHAFWHS VRHARPIAVG LNCALGAALM RPYIEELSKV AADTWISCYP NAGLPNPMSD TGFDETPAVT GALVAEFAEA GFLNIAGGCC GTTPDHIAEI ARRVGKYRPR GKADPLFSGL LAA // ID H5WZU0_9PSEU Unreviewed; 1182 AA. AC H5WZU0; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EHR51877.1}; GN ORFNames=SacmaDRAFT_3664 {ECO:0000313|EMBL:EHR51877.1}; OS Saccharomonospora marina XMU15. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Pseudonocardineae; Pseudonocardiaceae; Saccharomonospora. OX NCBI_TaxID=882083 {ECO:0000313|EMBL:EHR51877.1, ECO:0000313|Proteomes:UP000004926}; RN [1] {ECO:0000313|EMBL:EHR51877.1, ECO:0000313|Proteomes:UP000004926} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=XMU15 {ECO:0000313|EMBL:EHR51877.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CM001439; EHR51877.1; -; Genomic_DNA. DR RefSeq; WP_009155259.1; NZ_CM001439.1. DR EnsemblBacteria; EHR51877; EHR51877; SacmaDRAFT_3664. DR Proteomes; UP000004926; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000004926}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHR51877.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000004926}; KW Transferase {ECO:0000313|EMBL:EHR51877.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 223 223 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 733 733 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1182 AA; 130034 MW; C949B6F56D6DAA48 CRC64; MESRFLAELQ RRVLVADGGM GTALQEHDLT LDDFAQLEGC NEILNETRPD VVASVYRGFL EAGSDAIETN TFGTNLANFA EYDIVDRIRE LAEKGTSLAR QCADEYSTPD RPRFVLGSIG PGTKLPTLGH ITFAELRDAY VDNALGLLDG GADVVLVETS QDLLQTKAAI IGAKRAMQRA GRTVPVIAQV TVEQTGTMLV GSEIAAALTA LEPLGIDLIG MNCATGPAEM SEHLRVLSDH ARVPISVMPN AGLPELGPNG AVYPLRPDEL AEALAGFVTE FGARLVGGCC GTTAEHVRAV REAVADLSPK VRTPEIVPSV SSVYQSVPFR QDASILNVGE RTNANGSKAF RDAMLEQRWD DCVEIAKSQT REGAHMLDLC VDYVGRDGTA DMSELASRLA TASTLPIMVD STEAEVVRAG LERFGGRCAI NSVNYEDGTE PGGRYDEVMR LAVEHGAAVV ITCIDEEGQA RTAEWKLRVA ERAIEDLTTN WGMDKSSIII DTLVFPITTG QEEVRKDALE TINAIRELKR RHPDVQTTLG LSNVSFGLNP AARQVLNSVF LNECREAGLD SAIVNSSKIL PMNKIDDEPK QVALDLVYDR RAQDYDPLQK LMSLFEGKTA SSTRASRAEE LAKLPLLERL EKRIIEGELN GLEDDLEAAM REKDPLAIIN ENLLAGMKVV GELFGSGQMQ LPFVLQSAEV MKTAVAYLEP YMEKDDSGGK GKLLLATVKG DVHDIGKNLV DIIVSNNGYD VVNIGIKQPI NAILDAADEH KVDAIGMSGL LVKSTVIMKD NLKEMNARGV ADKYPVLLGG AALTRTYVEN DLDEVYDGDV RYAKDAFEGL RLMDHVMAVK RGEAVEEDAE EKARRQERKE RRKRSLRIAE KRKAEQGEEP STDDTTRSDV DADVPVPTPP FWGSKVIKGI ATADYLALLD ERATFFGQWG LRGAKKGEGP SYEELVETEG RPRLRAWMDE LSTAGILRHA AIVYGYFPCY SEGNDLVVLD KDEPDALERL RFTFPRQRRD RRLCLADFFR PKEKAEQTGQ VDVLPLQLVT MGQPIADYAN ELFAKDAYRD YLEIHGLGVQ LTEALAEYWH RRVRQELLFP SGSAVAEEDP DDVREFFKLG YRGARFSLGY GACPDLEDRA KIVELLEPGR IGVELSEEFQ LHPEQSTDAI VAHHPEAKYF NT // ID H5X1S7_9PSEU Unreviewed; 611 AA. AC H5X1S7; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 25. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=SacmaDRAFT_2699 {ECO:0000313|EMBL:EHR50940.1}; OS Saccharomonospora marina XMU15. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Pseudonocardineae; Pseudonocardiaceae; Saccharomonospora. OX NCBI_TaxID=882083 {ECO:0000313|EMBL:EHR50940.1, ECO:0000313|Proteomes:UP000004926}; RN [1] {ECO:0000313|EMBL:EHR50940.1, ECO:0000313|Proteomes:UP000004926} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=XMU15 {ECO:0000313|EMBL:EHR50940.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {ECO:0000256|RuleBase:RU004255}. CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; EHR50940.1; -; Genomic_DNA. DR RefSeq; WP_009154325.1; NZ_CM001439.1. DR EnsemblBacteria; EHR50940; EHR50940; SacmaDRAFT_2699. DR UniPathway; UPA00193; -. DR Proteomes; UP000004926; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004255}; KW Complete proteome {ECO:0000313|Proteomes:UP000004926}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000004926}. SQ SEQUENCE 611 AA; 63577 MW; 60CFC8E55CFD7C36 CRC64; MSDFAEAVRE RLLVCDGAMG TMLHAAGNSL DRSLPELNLS NPELVSTVHE SYVDAGADIL LTNTFGASRP RLAEHGFSGD PGEINRAGVR LARQAARQAG RPIFVGGSVA PAVSAGRRTQ VGAADRAAAV REQVLALADA GVDLLVLETF GYLDELAEAV VTASAATGLP ILAQATFTAE GHTPGGQTPH EVVTALAELD VAALGVNCTV GPQRMLAVVE QLRRHTTLPL SAQPNAGLPR RVHGRRFEYS LDHDYFARYA RRCAERGVSI VGGCCGTTPG HVRAIAAAVS ELDGRRTSRG RAAKVAVAAP AEQGGLARRL ADGDFVVAAE IAPPQGGVAE EAAELAADLR QRGAELILVS GAGGARAQLN STSLALHLQS QVGTETIATV TTWDKTIMSL QADLLGAHAF GARTVVCETG NPPLRGDYPN ADGIWEVDSV GLVELVAGLN DGRDCDGLSL ATKTSFHIGA RCNPGAEDVD AEIARTRAKI AAGAQFLITR PVYELTTLRW MVAELSDEGV PIIVAVSPLS GFAEAEFLAY EVPDVTVPIS TLSTLAQRER AGDDGRGVGL RLASELVEQA RSLADGVLVV VRDHDADAAA RLLAAATSPP G // ID H5X8S0_9PSEU Unreviewed; 315 AA. AC H5X8S0; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine/selenocysteine methylase (S-methylmethionine-dependent) {ECO:0000313|EMBL:EHR51439.1}; GN ORFNames=SacmaDRAFT_3214 {ECO:0000313|EMBL:EHR51439.1}; OS Saccharomonospora marina XMU15. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Pseudonocardineae; Pseudonocardiaceae; Saccharomonospora. OX NCBI_TaxID=882083 {ECO:0000313|EMBL:EHR51439.1, ECO:0000313|Proteomes:UP000004926}; RN [1] {ECO:0000313|EMBL:EHR51439.1, ECO:0000313|Proteomes:UP000004926} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=XMU15 {ECO:0000313|EMBL:EHR51439.1}; 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 ----------------------------------------------------------------------- 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; EHR51439.1; -; Genomic_DNA. DR RefSeq; WP_009154823.1; NZ_CM001439.1. DR EnsemblBacteria; EHR51439; EHR51439; SacmaDRAFT_3214. DR Proteomes; UP000004926; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000004926}; KW Methyltransferase {ECO:0000313|EMBL:EHR51439.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000004926}; KW Transferase {ECO:0000313|EMBL:EHR51439.1}. SQ SEQUENCE 315 AA; 33242 MW; 858DB7F152E1D393 CRC64; MSEAGDARSG QLGREFTYAD DVWERQRIVL DGGVATELEA RGHDLSDALW SARLLADAPE EVVSAHRAFF RAGANVATTA SYQASFTGFA ARGIGPGQAA ALLRRSVELA KRARDQVSDD VPRWVAASVG PYGAVLADGS EYRGRYGVSR QKLAAFHRPR LDVLAEAEPD LLALETVPDV EEAEALLDAL ESVGMPAWLS YTVDGGRTRA GQPLEEAFAV VAGRPDIVAV GVNCCAPEEV ADAVAIAGET TGKPVLAYPN SGQGWDPEVG RWTGTSRFRA DEAASWYARG VTAVGGCCRV PPADIAALSR VARSG // ID H5XDS4_9PSEU Unreviewed; 1182 AA. AC H5XDS4; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EHR62404.1}; GN ORFNames=SaccyDRAFT_3576 {ECO:0000313|EMBL:EHR62404.1}; OS Saccharomonospora cyanea NA-134. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Pseudonocardineae; Pseudonocardiaceae; Saccharomonospora. OX NCBI_TaxID=882082 {ECO:0000313|EMBL:EHR62404.1, ECO:0000313|Proteomes:UP000002791}; RN [1] {ECO:0000313|EMBL:EHR62404.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NA-134 {ECO:0000313|EMBL:EHR62404.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CM001440; EHR62404.1; -; Genomic_DNA. DR RefSeq; WP_005458183.1; NZ_CM001440.1. DR EnsemblBacteria; EHR62404; EHR62404; SaccyDRAFT_3576. DR Proteomes; UP000002791; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002791}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHR62404.1}; KW Transferase {ECO:0000313|EMBL:EHR62404.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 223 223 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 733 733 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1182 AA; 130067 MW; 2C7EEAEE3A62E82E CRC64; MDSRFLVELD RRILVADGGM GTALQAFDLS LDDFAQLEGC NEILNDTRPD VVSAVHRSFL EAGCDAVETN TFGTNYGNFG EYGILDRIRE LAEKGTVLAR QCADEYSTPE RPRFVLGSVG PGTKLPTLGH APYSVLRDAY VENTLGMLDG GVDAVLVETS QDLLQTKAAV VGAKRAMARA GRRVPIIAQV TVEQTGTMLV GSEIGAALTA LEPLGIDVIG MNCATGPAEM SEHLRVLSEQ ARVPISVMPN AGLPELGPNG AVYPLRPDEL AEALATFAKD FGARLVGGCC GTTPEHLRAV VEAVSSLSPA QRRSRHLPSV SSVYQSVPFE QDASILNVGE RTNANGSKKF REAMLDERYD DCVEIAKAQT REGAHVLDLC VDYVGRDGTR DMAELASRLA TASTLPIMVD STEPDVVRTG LEHFGGRCAI NSVNYEDGTG PESRYQRVME LAVEHGAAVV VTCIDEEGQA RTADWKLRVA ERAIEDLTTN WGLTTSSIII DCLVFPITTG QEEVRRDALE TIEAIRELKK RHPDVLTTLG LSNVSFGLNP AARQVLNSVF LHECREAGLD SAILNSSKIL PMNKIDDEAR QVALDLVYDR RRDGYDPLRR LMELFEGKTA SSARASRAEE LARLPLFERL EKRIVEGEVN GLEADLDAAM REKNPIDIIN ENLLAGMKVV GELFGSGQMQ LPFVLQSAEV MKTAVAHLEP HMEKTDSGGK GKLLLATVKG DVHDIGKNLV DIIVSNNGYD VVNIGIKQPI NAILEAAEEH RVDAIGMSGL LVKSTVVMKD NLQEMNSRGV ARKYPVLLGG AALTRTYVEN DLDEVYEGDV RYAKDAFEGL KLMDRVMAVK RGEAPEEDEA ERAKKAERKA RRERSLRIAE KRRAEQGPEP SLHDTARSDV DPDVPVPTPP FWGSKVVKGI AVADYLSMLD ERATFLGQWG LRGARKGEGP SYEELVETEG RPRLRAWIDE LSTRGVLAHA ALVYGYFPCY SDGNDLVVVD KDEPDAAERL RFSFPRQRRD RRLCLADFFR SREKAEQTGQ VDVLPLQLVT MGQPIADHAN ELFARNAYRD YLEVHGLGVQ LTEALAEYWH RRIRQELRFS SGTPVAAEDP DDVRQFFKLG YRGARFSFGY GACPDLEDRA KIVELLDAER IGVTLSEEFQ LHPEQSTDAI VAHHPEAKYF NT // ID H5XN82_9PSEU Unreviewed; 343 AA. AC H5XN82; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Homocysteine/selenocysteine methylase (S-methylmethionine-dependent) {ECO:0000313|EMBL:EHR63715.1}; GN ORFNames=SaccyDRAFT_4919 {ECO:0000313|EMBL:EHR63715.1}; OS Saccharomonospora cyanea NA-134. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Pseudonocardineae; Pseudonocardiaceae; Saccharomonospora. OX NCBI_TaxID=882082 {ECO:0000313|EMBL:EHR63715.1, ECO:0000313|Proteomes:UP000002791}; RN [1] {ECO:0000313|EMBL:EHR63715.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NA-134 {ECO:0000313|EMBL:EHR63715.1}; 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 ----------------------------------------------------------------------- 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; EHR63715.1; -; Genomic_DNA. DR RefSeq; WP_005460194.1; NZ_CM001440.1. DR EnsemblBacteria; EHR63715; EHR63715; SaccyDRAFT_4919. DR Proteomes; UP000002791; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002791}; KW Methyltransferase {ECO:0000313|EMBL:EHR63715.1}; KW Transferase {ECO:0000313|EMBL:EHR63715.1}. SQ SEQUENCE 343 AA; 35887 MW; EA02FFE2C0C1E8B9 CRC64; MKRLPTVLRL HLGLGRVAYP NCGHAYAKCG HGGVRAGAPT VVAVELFDGG PVVSDGGLAT ELEARGHDLT DALWSARLLL DAPGEIVAAH RAFYEAGAVV ATTASYQASF PGFAERGLDR GEVATLLHRS VALARQAGDE VSGDGRRRFV AASVGPYGAA LADGSEYRGD YGLTVAQLRD WHLPRLETLA EAEPDLLAVE TIPDVVEAEA LVGALAGLDV PAWLAYTVDG DRTRAGQPLA EAFAVAAAAD EVVAVGVNCC APADVTPAIA CARAVTDKPV VVYPNSGESW DARQRTWTGP SRYSPELARQ WVAEGARVVG GCCRVRPSDI ADISDIAELA RTL // ID H5XXK5_9FIRM Unreviewed; 427 AA. AC H5XXK5; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Cobalamin-dependent methionine synthase I {ECO:0000313|EMBL:EHQ91211.1}; GN ORFNames=DesyoDRAFT_4255 {ECO:0000313|EMBL:EHQ91211.1}; OS Desulfosporosinus youngiae DSM 17734. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfosporosinus. OX NCBI_TaxID=768710 {ECO:0000313|EMBL:EHQ91211.1, ECO:0000313|Proteomes:UP000005104}; RN [1] {ECO:0000313|EMBL:EHQ91211.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17734 {ECO:0000313|EMBL:EHQ91211.1}; 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 ----------------------------------------------------------------------- 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; EHQ91211.1; -; Genomic_DNA. DR RefSeq; WP_007786036.1; NZ_CM001441.1. DR EnsemblBacteria; EHQ91211; EHQ91211; DesyoDRAFT_4255. DR Proteomes; UP000005104; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005104}. SQ SEQUENCE 427 AA; 46433 MW; 6020F077A7A17F89 CRC64; MKRFLSSVRE RVLLYDGSKG VMLQKRGLTG NEAAEAWNLS KPDEVKNLYN LYKQAGSDVI QTNTFPGNKV TLEKHGLGDK TYPINFAGVK LAKEVAGETT YVAASVGPTG MILEPAGDLS FDQAYTVFKE QLRAIEDAGA DLVNFETFTD LNELRAAILA AKETTSLPII ASVTFNENSR TMSGNSAEVC AIVCESLGAE VVGANCSGGP DSLIEPIKKM RSVVSIPLSV KANAGMPELV NGEAVYGQKP EQFSSYTKEF IENGVRLIGG CCGTTPEFIR AVKKELEGIK APDLELKSSS ALASAFNHLL FANDKEYSAA ELSLKDDKAV NMLKKGDFYQ LLQDYRTAAM DYLLIDFGDM TESFDVLGFS NTISFAIKKP LILKSESVEL LTKFLRYYPG RAGVILTEKT KGSLPQLRHY GALILNS // ID H5YE59_9BRAD Unreviewed; 1287 AA. AC H5YE59; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 01-APR-2015, entry version 20. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EHR00628.1}; GN ORFNames=Bra471DRAFT_01202 {ECO:0000313|EMBL:EHR00628.1}; OS Bradyrhizobium sp. WSM471. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=319017 {ECO:0000313|EMBL:EHR00628.1, ECO:0000313|Proteomes:UP000005774}; RN [1] {ECO:0000313|EMBL:EHR00628.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=WSM471 {ECO:0000313|EMBL:EHR00628.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CM001442; EHR00628.1; -; Genomic_DNA. DR RefSeq; WP_007605343.1; NZ_CM001442.1. DR EnsemblBacteria; EHR00628; EHR00628; Bra471DRAFT_01202. DR Proteomes; UP000005774; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000005774}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHR00628.1}; KW Transferase {ECO:0000313|EMBL:EHR00628.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 770 770 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1287 AA; 140358 MW; 56CB371E1E36DF7F CRC64; MTVSTSPKRT ALLDAARERI LVLDGAMGTM IQNLQFDEAA FRGERFKSFH RDLRGNNDLL ILTQPQAIED IHAAYLRAGA DIVATNTFST TSIAQADYDL ADIVYEMARE GARLAGNAAR RVEAEDGKPR FVAGAIGPTN RTASISPDVS NPGYRAVTFD DLRKSYGEQI NGMLDGGVDL LLVETIFDTL NAKAALYAIA EITEERGIDM PVMVSGTITD KSGRLLSGQL PEAFWHSVQH ARPVTIGFNC ALGAKDLRAH IADIGRVADT LVCAYPNAGL PNEFGQYDET PEYMARLVGE FARDGLVNIV GGCCGTTPDH IAAIAAAVAP HKPRIVPEIE PRLRLSGLEP FILTDAIPFV NVGERTNVTG SARFRKLVTA GDYTAALQVA RDQVENGAQI IDVNMDEGLL DSEAAMVTFL NLVAAEPDIA RVPVMVDSSK FSVIEAGLKC VQGKPVVNSI SMKEGEDKFI HEAKVARRHG AAVVVMAFDE VGQADTFARK TEICKRAYDI LVNRVGFPPE DIIFDPNIFA IATGIEEHNN YGVDFIEATR WIRKNLPGAH ISGGVSNLSF SFRGNEPVRE AMHSVFLYHA IKAGMDMGIV NAGQMIVYDD IDPELRQVCE DVILNRDPGA SERLLALAER FRGNKTQTKE ADLAWREWPV AKRLSHALVH GITEFIEQDT EEARKASKRP LDVIEGPLMA GMNVVGDLFG DGKMFLPQVV KSARVMKQAV AWLMPFMEEE KARNLANGIG TEGSSSAGKI VLATVKGDVH DIGKNIVGIV LQCNNYEVID LGVMVPAAKI VETVKAEKAD IVGLSGLITP SLDEMAFFAG ELQREGLKLP LLIGGATTSR VHTAVKIDPS YRAGPVVHVN DASRAVGVAS ALLSPERREA YAAEVRAEYA KISDAHMRAQ ADKKRLKLAT ARANRVPVDF AANKPVKPTF LGTRSFDDYD LAELVPYIDW TPFFQTWELA GRFPAILNDV KVGEVARSLY DDARKMLDLI VKEKWFRARA TVGFWPANAQ GDDIVLYADE SRTRTIATLH TLRQQLEKRE GRFNAALADF VAPAGTGVPD YVGGFVVTAG IGEDVVADRF KMANDDYSSI LCKALADRLA EAFAERMHAR VRREFWAYAP DETLSTDDLI LEKYQGIRPA PGYPAQPDHT EKATLFELLD AENTAGVKLT ESFAMWPGSS VSGLYLANPE SYYFGVGKIE RDQVEDYAAR KGMSLAEAER WLAPILNYIP ARESASDKAA FAATPANDET SKELASHPPG CTCAVHLVWQ KKRAGAG // ID H6BDD0_LOLPR Unreviewed; 191 AA. AC H6BDD0; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 29-OCT-2014, entry version 8. DE SubName: Full=Homocysteine S-methyltransferase-3 {ECO:0000313|EMBL:AFA36476.1}; DE Flags: Fragment; OS Lolium perenne (Perennial ryegrass). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; OC Pooideae; Poeae; Loliinae; Lolium. OX NCBI_TaxID=4522 {ECO:0000313|EMBL:AFA36476.1}; RN [1] {ECO:0000313|EMBL:AFA36476.1} RP NUCLEOTIDE SEQUENCE. RA Li H., Hu T., Fu J.; RT "Identification of genes involved in salinity tolerance in Lolium RT perenne."; 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; JF747347; AFA36476.1; -; mRNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Methyltransferase {ECO:0000313|EMBL:AFA36476.1}; KW Transferase {ECO:0000313|EMBL:AFA36476.1}. FT NON_TER 1 1 {ECO:0000313|EMBL:AFA36476.1}. FT NON_TER 191 191 {ECO:0000313|EMBL:AFA36476.1}. SQ SEQUENCE 191 AA; 20986 MW; A141C5D2C32C35AA CRC64; SGDYGEAGTL EFLKDFHRRR LQVLAEARPD LIAFETIPNK LEAQAYVELL EECNISIPSW FSFNSKDGVH VVSGDSLIEC AKVANSCAKV GAIGINCTPP RFIHSLILTI RKVTDKPILI YPNSGERYDA EKKEWVESTG VSDGDFVSYV SEWCKDGAAL IGGCCRTTPN TIRAITRTLN QFCPAPQLSV A // ID H6BTW8_EXODN Unreviewed; 333 AA. AC H6BTW8; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 04-FEB-2015, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EHY55545.1}; GN ORFNames=HMPREF1120_03677 {ECO:0000313|EMBL:EHY55545.1}; 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 {ECO:0000313|EMBL:EHY55545.1, ECO:0000313|Proteomes:UP000007304}; RN [1] {ECO:0000313|Proteomes:UP000007304} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 34100 / CBS 525.76 / NIH/UT8656 RC {ECO:0000313|Proteomes:UP000007304}; 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; JH226132; EHY55545.1; -; Genomic_DNA. DR RefSeq; XP_009156006.1; XM_009157758.1. DR GeneID; 20308316; -. DR InParanoid; H6BTW8; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000007304; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007304}; KW Methyltransferase {ECO:0000313|EMBL:EHY55545.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007304}; KW Transferase {ECO:0000313|EMBL:EHY55545.1}. SQ SEQUENCE 333 AA; 37209 MW; 9F6CC0077B7EE65B CRC64; MARDLLGRNI LLLDGGLGTT LEDEHGVRFS VKTPLWSSHL LVENPSLLRV VQRDFANAGA DIILTATYQA SFEGFRNTKT QNDVGIAADD AKKYMLSAVS IARDAFNGRS GLVALSLGAY GATMVPSTEY SGEYGPMNED DLFKFHMDRI SIFTCDKPVW ADIDLVAFET LPRLDEVRVA RKVMRTITDK DYWISCVFPN NDDRLPDGTE VEDLVRTMLH GERRPFAIGL NCTKVHKVPG LIRRFEEAAQ SLSIKLPRLV IYPDGAGTKV YDTQLQQWVG EDQDAKAWDQ QIFEIVSDVQ TRGAWEGVIV GGCCKTTPEH IQKLGKRLDV LQR // ID H6CJN3_9BACL Unreviewed; 1123 AA. AC H6CJN3; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 01-APR-2015, entry version 22. DE SubName: Full=Methionine synthase 1 {ECO:0000313|EMBL:EHS57301.1}; GN ORFNames=WG8_2670 {ECO:0000313|EMBL:EHS57301.1}; OS Paenibacillus sp. Aloe-11. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1050222 {ECO:0000313|EMBL:EHS57301.1}; RN [1] {ECO:0000313|EMBL:EHS57301.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Aloe-11 {ECO:0000313|EMBL:EHS57301.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; JH601055; EHS57301.1; -; Genomic_DNA. DR RefSeq; WP_007430659.1; NZ_JH601055.1. DR EnsemblBacteria; EHS57301; EHS57301; WG8_2670. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 204 204 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 267 267 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 268 268 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 699 699 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1123 AA; 123933 MW; BA9850BA59BEF643 CRC64; MIQQEDLSPD DFGGEELEGC NEMLVLTRPD VIQGIHEAYL EAGADLIETN TFGATSVVLA DYDIPERARE INLAAAKLAR NAVDKFNTAD KPRFVVGAMG PTTKTLSVTG GVTFAELIES YQEQALALIE GGVDALLLET SQDTLNVKAG SIGIRQAFEQ TGIELPLMIS GTIEPMGTTL AGQNIESFCI SLEHLHPVSI GLNCATGPEF MRDHIRSLSE MSSAAISCYP NAGLPDENGQ YHESPESLAR KMAAFAEKGW LNIAGGCCGT TPEHIRVMSE QMAQFEPRPL AGHHPPAVSG IEPVYIEQDN RPYMVGERTN VLGSRKFKRL IVEGKYEEAS EIARAQVKSG AHVIDICVQD PDRDEMTDME AFLKLVVNKV KVPLVIDTTD IKVVDKALQY SQGKAIINSI NLEDGEEKFE KMAPLIHKYG AAVVVGTIDE RGQAISREDK LEVAKRSYDL LVNRYGLAAE DLIFDTLVFP VGTGDEQYIG SAKETIEGIR IIKEALPGVH TILGISNVSF GLPEAGREVL NSVYLYECTK AGLDYAIVNT EKLERYASIP EHERKLAEDL IYKTNDDTLS AFVAAFRNKK VEKKEKVSNL SLEERLASYV VEGSKEGLIP DLEQALAKYS SLEIINGPLM KGMEEVGRLF NNNELIVAEV LQSAEVMKAS VAYLEPFMEK NESSVKGKIL LATVKGDVHD IGKNLVEIIL SNNGYQIVNL GIKVPPERII EAYREEKADL IGLSGLLVKS AQQMVLTAQD LKNANIDIPI MVGGAALTRK FTKNRIRPEY DGLVAYAKDA MDGLDIANKL MDPESRKKMA EEMEAEREAE AATVVETKQL PKLTRAVRSK IAQDLPVYIP PDTDRHVLRN YPLNYILPYV NMQMLMGHHL GLKGNVEKLL AEGDPKATQL KDTVDSIMFE AVTDGIIQAH AMYRFFPAQS QGDQILIYDP SDVSKVLHTF TFPRQQVEPY LCLADFLKSV ESGVMDYVGF MVVTAGHGIQ QLSTQWREQG DYLRSHALQA VALEVAEGLA ERLHHIIRDS WGFPDPADMT MKQRHGARYQ GIRVSFGYPA CPDLEDQGPL FQLLKPEDIG VELTEGFMME PEASVSAMVF SHPQAQYFNV EKV // ID H6CK56_9BACL Unreviewed; 630 AA. AC H6CK56; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 07-JAN-2015, entry version 15. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=WG8_3019 {ECO:0000313|EMBL:EHS56749.1}; OS Paenibacillus sp. Aloe-11. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1050222 {ECO:0000313|EMBL:EHS56749.1}; RN [1] {ECO:0000313|EMBL:EHS56749.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Aloe-11 {ECO:0000313|EMBL:EHS56749.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH601056; EHS56749.1; -; Genomic_DNA. DR RefSeq; WP_007431007.1; NZ_JH601056.1. DR EnsemblBacteria; EHS56749; EHS56749; WG8_3019. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EHS56749.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EHS56749.1}. SQ SEQUENCE 630 AA; 68643 MW; 7603414CD9725033 CRC64; MKPDLRTVLN RELIVGDGAM GTYLYQLGFP VNTSYEELNM TSPDVIADVH SQYLNAGARL LETNTFSAND YKLARFGLES RVEEINRAGV RIARAAAGPE HYVVGAVGSI CGGKRLNISK LELARNYDQQ IDALLSEGVD GILCETFYSL DEMRIALHGV RKYSDIPVIC QFAVDQVGRT QDGFLVAEAF SVLRDEGADI LGFNCHSGPQ GIMSVMEQLK GPLSVPLSVY PNAGLADYVD GHYVYGATPE YFGECAASFV DLGTRLIGGC CGTTPDHIAA ISKALSGLQP PPLAPREVLL KESIHVAEPE PTVDGRERGN GRYASKPNIV ETVKERHTVI VELDPPRDLD ITRFMQGAHA LKKAGADALT LADNSLAVTR MSNMALGHLV SIETGLRPLI HIACRDRNLI GTQSHMMGFD ALGIDHVLAV TGDPARFGDL PGASSVYDMT SFEIIRMIKQ LNDGVAFSGK PLKQKANFVV GAAFNPNVKH LGKAVQRLEK KIASGADYIM TQPVYDRELI AAIAEETRHL EVPIFIGIMP LASGRNAEYL HNEVPGIQLS DEVRARMSGL EGPEGRAMGV SIAKELLDTA MEHFNGIYLM TPFMFYEMTA ELTSYVWQKS GRVQAPLFRL // ID H6CS36_9BACL Unreviewed; 315 AA. AC H6CS36; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 07-JAN-2015, entry version 10. DE SubName: Full=Homocysteine S-methyltransferase (S-methylmethionine:homocysteine methyltransferase) {ECO:0000313|EMBL:EHS54759.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EHS54759.1}; GN ORFNames=WG8_5115 {ECO:0000313|EMBL:EHS54759.1}; OS Paenibacillus sp. Aloe-11. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1050222 {ECO:0000313|EMBL:EHS54759.1}; RN [1] {ECO:0000313|EMBL:EHS54759.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Aloe-11 {ECO:0000313|EMBL:EHS54759.1}; 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; JH601082; EHS54759.1; -; Genomic_DNA. DR RefSeq; WP_007433091.1; NZ_JH601082.1. DR EnsemblBacteria; EHS54759; EHS54759; WG8_5115. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EHS54759.1}; KW Transferase {ECO:0000313|EMBL:EHS54759.1}. SQ SEQUENCE 315 AA; 34959 MW; 101DF9F282DBCB21 CRC64; MNPIQHILDE YPLIVLDGAM ATELERQGHD LNDSLWSAKI LHEHPEAIKR VHKDYFEAGA DCAITASYQA TVEGYVQRGL SENEALELIQ SSVRIAVQAR DEFWAEAANA ANQQHRPKPL VAASVGPYGA FLADGSEYRG DYELSEEQLV EFHRPRMKAL IEAGADILAC ETIPCLVEAK AIARLLKEFP GTYAWISFSA KDGQHISNGE TAAACAEWLN DHEQVAAVGL NCTLPKFIPS LIQEMRSHTD KPVVVYPNLG EEYDPVTKTW HGHTCAETFG QSARQWYEAG ARLIGGCCRT QPQDIKEIVA WSREV // ID H6L831_SAPGL Unreviewed; 1225 AA. AC H6L831; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 26. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:AFC25359.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AFC25359.1}; GN Name=metH {ECO:0000313|EMBL:AFC25359.1}; GN OrderedLocusNames=SGRA_2631 {ECO:0000313|EMBL:AFC25359.1}; OS Saprospira grandis (strain Lewin). OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Saprospiraceae; Saprospira. OX NCBI_TaxID=984262 {ECO:0000313|EMBL:AFC25359.1, ECO:0000313|Proteomes:UP000007519}; RN [1] {ECO:0000313|EMBL:AFC25359.1, ECO:0000313|Proteomes:UP000007519} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Lewin {ECO:0000313|EMBL:AFC25359.1, RC ECO:0000313|Proteomes:UP000007519}; RX PubMed=22675601; DOI=10.4056/sigs.2445005; RA Saw J., Yuryev A., Kanbe M., Hou S., Young A., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002831; AFC25359.1; -; Genomic_DNA. DR RefSeq; WP_015692970.1; NC_016940.1. DR RefSeq; YP_005322943.1; NC_016940.1. DR EnsemblBacteria; AFC25359; AFC25359; SGRA_2631. DR KEGG; sgn:SGRA_2631; -. DR KO; K00548; -. DR BioCyc; SGRA984262:GLJW-2661-MONOMER; -. DR Proteomes; UP000007519; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007519}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AFC25359.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007519}; KW Transferase {ECO:0000313|EMBL:AFC25359.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 243 243 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 754 754 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1225 AA; 135202 MW; A0800F6588BA6395 CRC64; MQRLHERIEQ QILVIDGAMG TMLQQYKLQE ADYRGERFAD FHRDLKGNND LLSITQPHLV TEVHKAYLDA GADIIETNTF NATAISQEDY DMQELVYELN YASAQCARAA VDAFNAENPE KFRFVAGAMG PTNRTASLSP DVNNPGYRAI NFEQLRAAYY EQAKALAEGG ADLFLVETVF DTLNCKAALF AIDQYCEEVG IAYPVMVSGT ITDASGRTLS GQTVEAFWLS VSHANLFSVG LNCALGAAEM RPHIEALSNI AHCYISAYPN AGLPNEMGEY DQTAQEMGLL IEDFAQSGFI NIVGGCCGTS PAHIRRMAEV VAQLPVRKKP APMQLSAYSG LEPLIVRPGF NFINVGERTN VTGSRKFARL IKNGNYEEAL SVAQQQVEGG AQIIDVNMDE GMLDSVEAMS YFLNLIASEP DIARLPIMID SSKWEVIEAG LRCVQGKAIV NSISLKEGKA AFVQQAKLVR RYGAAAVVMA FDEVGQADTM ERKVEICSRA YKILTEEVGF PPQDIIFDPN IFAIGTGIEE HNNYGVDFIE ATKEIKRRMP LVKISGGVSN LSFSFRGNNI VREAIHSAFL YHAVQAGMDM GIVNAGMIEV YEDIPKELLE LVEDLLFNRR PDATERLTDY AEQLKGQGGK KRQEDLSWRE VPVEDRLAHA LVKGITKFVI EDTEEARQQY SSPLEVIEGP LMSGMNIVGD LFGAGKMFLP QVVKSARVMK QAVAHLTPFI EAEKSAGQSA KGKILLATVK GDVHDIGKNI VGVVLACNNF EIIDMGVMVP ANEILKKAQE EQVDILGLSG LITPSLDEMV YVAKEMQRLG MQMPLLIGGA TTSKTHTAVK IAPQYSGPTV HVLDASRAVT VAASLLAEKE ENRAAYMEQV LAEQERIRVQ RAKRTSAKRY LSLKKARENK LALDWSKIEP VVPNKMGITV LDQLDLAVLR DYIDWTPFFS SWQLAGKFPA ILEDEVVGQE AKSLYADAQQ MLDQIIAENW LQAKAVCGLF AANSIDDDDI LVYPNGPEAE PMRLHHLRQQ RQKAAGKPNY CLSDFLAPKA SGKTDYMGAF AVTAGIGIEE HVARFEAAHD DYNAILLKAL ADRLAEAAAE YLHAEVRRNY WGYAADEALD NQALIAETYQ GIRPAPGYPA CPEHTEKRSL FALLEVEERI GIRLTESCAM YPAAAVSGWY FGQEEARYFG LGNIEKDQVE SYAARKGMTV EEAERWLMPV LNYDI // ID H6LG76_ACEWD Unreviewed; 793 AA. AC H6LG76; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Methionine synthase MetH {ECO:0000313|EMBL:AFA49552.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AFA49552.1}; GN Name=metH {ECO:0000313|EMBL:AFA49552.1}; GN OrderedLocusNames=Awo_c28010 {ECO:0000313|EMBL:AFA49552.1}; 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 {ECO:0000313|EMBL:AFA49552.1, ECO:0000313|Proteomes:UP000007177}; RN [1] {ECO:0000313|Proteomes:UP000007177} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 RC {ECO:0000313|Proteomes:UP000007177}; 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; AFA49552.1; -; Genomic_DNA. DR RefSeq; WP_014357150.1; NC_016894.1. DR RefSeq; YP_005270441.1; NC_016894.1. DR EnsemblBacteria; AFA49552; AFA49552; Awo_c28010. DR KEGG; awo:Awo_c28010; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR BioCyc; AWOO931626:GI4Q-2799-MONOMER; -. DR Proteomes; UP000007177; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR023467; MeTrfase_MtrH/MtxH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR ProDom; PD009948; MtrH_MeTrfase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007177}; KW Methyltransferase {ECO:0000313|EMBL:AFA49552.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007177}; KW Transferase {ECO:0000313|EMBL:AFA49552.1}. SQ SEQUENCE 793 AA; 85279 MW; EAB7D94733B0BCB3 CRC64; MNIKELLKKK RLYLDGAMGS LLQDKLDEIG PVPEVLNLTQ PELIKEIHQQ YINAGANIIL ANTFGVNGYK LKNTTYSVDQ LVTAGVKNAK SLKPDYVALD VGPLGTLIGA LGEVSFEQAL DYFKEVVEAG DEAGADLIVI ETMTDICEAR AALIAAKEVS DLPVIVSMTY EDNKRTLTGS DALTVVNILE ALGADAIGIN CSTGPDGMVP IIEDLIEYAS VPIMVEPNAG LPQMVDGKTV YNISIDEFTQ YMVQIAEMGA LILGGCCGTT PSYIKKMIAA TKDLPLYAVN EKWYTAVSSS TKTIILGDDI HIIGECINPT TNPILKASLR QGDLTVVSQL AVEQKKDGAH VLDINLGLPD IDELKMMTEA VDTVSRLVDC PLQIDSSNPE VIEAVLRGYP GKAIINSVNG KKSAMAKIFP IAQKYGALVL GLTMDETGIP SLAEDRFAIA KKIMAVGESY GISQKNILID ALVLTASAQQ AEVRETLKTL AQLREALGVP TVLGVSNISF GLPNRELLNR TFLGMALEAG LTTPIMNPGD KEMMDTINAF RALWGLDGQC IAYANRYKES SFGESKSAAD KKLLGLKEII EEGLSDQAAA ATRLLLETRE PLDIVNNEIV PALDAVGDAF ETGECFLPHL IFAAETAQKA FEVIKETMQQ TGQAQVAKGT IILATVEGDV HDIGKNILKV ILENYGYAIL DLGKDVKAET IIQSIKAEQI QLVGLSALMT TTVKNMEKII KEIKTNCPQT TIMVGGAVLN PEYAETIGAD YYGKDAREGA GIAQKVFQSI RLV // ID H6N2I6_GORPV Unreviewed; 1203 AA. AC H6N2I6; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=Methionine synthase MetH {ECO:0000313|EMBL:AFA73411.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AFA73411.1}; GN Name=metH {ECO:0000313|EMBL:AFA73411.1}; GN OrderedLocusNames=GPOL_c23820 {ECO:0000313|EMBL:AFA73411.1}; OS Gordonia polyisoprenivorans (strain DSM 44266 / VH2). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Gordoniaceae; Gordonia. OX NCBI_TaxID=1112204 {ECO:0000313|EMBL:AFA73411.1, ECO:0000313|Proteomes:UP000009154}; RN [1] {ECO:0000313|EMBL:AFA73411.1, ECO:0000313|Proteomes:UP000009154} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44266 / VH2 {ECO:0000313|Proteomes:UP000009154}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP003119; AFA73411.1; -; Genomic_DNA. DR RefSeq; WP_014360015.1; NC_016906.1. DR RefSeq; YP_005282777.1; NC_016906.1. DR EnsemblBacteria; AFA73411; AFA73411; GPOL_c23820. DR KEGG; gpo:GPOL_c23820; -. DR KO; K00548; -. DR BioCyc; GPOL1112204:GJWY-2378-MONOMER; -. DR Proteomes; UP000009154; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000009154}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AFA73411.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000009154}; KW Transferase {ECO:0000313|EMBL:AFA73411.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 235 235 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 301 301 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 302 302 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 754 754 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1203 AA; 130805 MW; 67414BF278258C98 CRC64; MSSHTPNPGN HDTTFLSAMA RRVLVGDGAM GTMLQAADLT LDDFAGLEGC NEILNDTRPD VLEQIHRAYF EAGADAVETN TFGCNLSNLG DYDIADRIRE LSYKGTAIAR GVADEMGPSA DGTARFVLGS IGPGTKLPSL GHTTFGVIRD AYFECVAGML DGGADAVLIE TSQDLLQVKA AVVAARAAMD ELGRRIPIIS HVTVETTGTM LLGSEIGAAL AAIEPLGVDM IGLNCATGPA EMSEHLRYLS RHARIPVSVM PNAGLPQLGP NGAEYPLQPD ELASALSTFV GEFGLAFVGG CCGTTPEHIR QVAAAVAETT KADRAPAHIS ETSSLYSAVP FDQDASFLVI GERTNSNGSK AFREAMLAED YQRCLDIAKE QTRDGAHMLD LNVDYVGRDG AADMTALASR FATSSTLPIM LDSTEPEVIR AGLEALGGRC AVNSVNYEDG DGPESRFSRI MSLVVEHGAA VVALTIDEEG QARTADWKIR VAERLIADIT GNWGLAEEDI ILDTLTFPIS TGQEEVRRDG IETIEAIRRL HEAHPDVHFT LGISNISFGL NPAARQVLNS VFLHECVQAG LDTAIVHASK ILPMNKIPDE QRDVALDLVY DRRGAAGTRS EGREDYDPLQ KLMELFEGVS AASARESRAQ ELARLPLFER LERRIVDGER NGLEADLDEA MTQKPPLEII NETLLSGMKT VGELFGSGQM QLPFVLQSAE VMKTSVAHLE PHMEATGEDG KGRIVLATVK GDVHDIGKNL VDIILSNNGY EVVNIGIKQP ISTILEVAED KRADVIGMSG LLVKSTVVMK ENLEEINARG LADNYPVLLG GAALTRAYVE NDLSDTYEGQ VHYARDAFEG LRLMDEIMAF KRGGGSVPES ADSLAAAKKA AERKARHERS QRIAAKRKAA ETPVEVPARS DVIADNEIPT PPFWGTRIIK GIPVADYLQL LDERALFLGQ WGLRGARGGN GPTYEELVET EGRPRLREWI DRLSTEGILA HAAVVYGYFP AVSDGDVVHI LTEPTPDAPT RFSFTFPRQQ RSRFLCIADF VRSREAALAD GRVDVLPFQL VTMGQPIADF ANELFARDAY RDYLEVHGIS VQLTEALAEY WHQRVRGELA FADRAVDAED PDNAQGFFDL EYRGARFSFG YGACPDLEDR VKMMELLEPE RIGVHLSEEL QLHPEQSTDA FVLHHPEAKY FNT // ID H6ND56_9BACL Unreviewed; 1144 AA. AC H6ND56; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 01-APR-2015, entry version 25. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AFC30017.1}; GN ORFNames=PM3016_3162 {ECO:0000313|EMBL:AFC30017.1}; OS Paenibacillus mucilaginosus 3016. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1116391 {ECO:0000313|EMBL:AFC30017.1, ECO:0000313|Proteomes:UP000007523}; RN [1] {ECO:0000313|EMBL:AFC30017.1, ECO:0000313|Proteomes:UP000007523} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3016 {ECO:0000313|EMBL:AFC30017.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP003235; AFC30017.1; -; Genomic_DNA. DR RefSeq; WP_014370104.1; NC_016935.1. DR RefSeq; YP_005313166.1; NC_016935.1. DR EnsemblBacteria; AFC30017; AFC30017; PM3016_3162. DR KEGG; pmq:PM3016_3162; -. DR KO; K00548; -. DR BioCyc; PMUC1116391:GLI5-3241-MONOMER; -. DR Proteomes; UP000007523; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007523}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007523}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 722 722 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1144 AA; 126198 MW; BAFF9B8A4E5C23E2 CRC64; MSKPSLQEQL KKKIMILDGA MGTMIQQENL TEADFGSEDL DGCNEILVVT RPDVIQKIHE AYFAAGADMV ETNTFGATSV VLAEYDLQDR ARELNLAAAK LAIEAANKYS TPEWPRYVIG AMGPTTKTLS VTGGVTFDEL VESYQEQAEA LIEAGVDALL LETSQDTLNV KAGSIGIRSA FDKLGVKLPL MISGTIEPMG TTLAGQNIES FYVSLEHLNP VSFGLNCATG PEFMRDHIRT LSEIAGTAVS CYPNAGLPDE NGKYHESPES LALKLAGFAE QGWLNIAGGC CGTTPDHIRA MAETLGKFEP RKQAGVHPPA ISGIETVYVE PDNRPIMVGE RTNISGSRKF KRLIKEGKFE EASEIARTQV KNGAHIIDIN LQDTDIDEAY AINEFLPQVV KKVKVPLMID STYDHIIELG LKYSQGKAIV NSINLEDGES KFEAIVPLLH KYGAAVVMIL IDERGQAVSR QAKMEVADRA YELLTKKYGM KPQDIIFDPN MFPVGSGDPQ YIGSAVETIE GIRMIKEKYP ETMTILGLSN ISFGLPDAGR EVLNSVYLYH CTKAGLDYAI VNTEKLERYA SIPEEERALA EELIFNTNDD TLAKFVAYFR VKKVEKKEKI SNLTLEERLA SYVVEGTKEG LIPDLEEALK KYAPLDIING PLMKGMEEVG RLFNNNELIV AEVLQSAEVM KASVAHLEQY MEKADSAVKG KIILATVKGD VHDIGKNLVE IILSNNGYKI VNLGIKVPPE QLIEAYRKEK PDAIGLSGLL VKSAQQMVVT AQDMKNAGID VPILVGGAAL TRKFTKTRIA PEYDGMVLYA KDAMDGLDIA NKLSDPEQRQ VLIRELRESM DSDVKEAGRK EESMPALTRV MTSTVDRTVP VQVPPDLKRR VLRDYPISHL VPYVNMQMLL GHHLGLKGKV ENLIAEKDPK ALQLKETVDG ILAEAQQAGI IKAQGMYRFF PAQSDGNDVL IYDPEDTGRV VQKFTFPRQE KEPYLCLADY LKPVSSGEMD YVGFLVVTAG HGVSELSAQW REKGDYLRSH ALQAAALELA EGFAERVHQM MRDQWGFPDP AEMTMAERFG AKYRGQRFSF GYPACPNLDD QQQLFALLHP EDIGVTLTEG SMMEPEASVS AIVFAHPQAR YFNA // ID H6NQX3_9BACL Unreviewed; 627 AA. AC H6NQX3; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 01-APR-2015, entry version 21. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=PM3016_5253 {ECO:0000313|EMBL:AFC31966.1}; OS Paenibacillus mucilaginosus 3016. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1116391 {ECO:0000313|EMBL:AFC31966.1, ECO:0000313|Proteomes:UP000007523}; RN [1] {ECO:0000313|EMBL:AFC31966.1, ECO:0000313|Proteomes:UP000007523} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3016 {ECO:0000313|EMBL:AFC31966.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; AFC31966.1; -; Genomic_DNA. DR RefSeq; WP_013919591.1; NC_016935.1. DR RefSeq; YP_005315115.1; NC_016935.1. DR EnsemblBacteria; AFC31966; AFC31966; PM3016_5253. DR KEGG; pmq:PM3016_5253; -. DR KO; K00547; -. DR BioCyc; PMUC1116391:GLI5-5284-MONOMER; -. DR Proteomes; UP000007523; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007523}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:AFC31966.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000007523}; KW Transferase {ECO:0000313|EMBL:AFC31966.1}. SQ SEQUENCE 627 AA; 68018 MW; 9047563C5163022C CRC64; MKPGLREALR SQVLVGDGAM GTYLYQMGFP IGISYEELNL LKPDVIMDVH RRYYEAGARL IETNTFSANR EKLSKFGLEG EVEAINRAGV ELARRAVGED AYVVGAVGSI RAGKRKNVRT NKVREDLREQ ISILCDTKVD GLLLESFLDL DEMLIALKEV RRISDLPVIC QFATEGAGVT QDGVPLKEAF AKLLEAGADV VGLNCRSGPN GLLRSLEGAA AAEADHPPYS VFPNAGLADY VDGRYSFPAT PQYFGETARR FADLGTRIIG GCCGTTPEHI AAVAGALAGY VPNPEAAKRA AAAPAAEVAE RAAAGAGAEV PTEPSIVDLV RQRHTVIVEL DPPKDLDIGK FMEGTEALKK AGVDALTMAD NSLAVTRMSN LALGSIVKER TGIRPLIHIA CRDRNLIGTQ SHMMGLHALG IDHVLAVTGD PARFGDLPGS SSVYDLTSFE IIRMIKQLNE GIAFSGKPLK KQANFIIGAA FNPNVKYLDK AVQRLERKVE AGADYIMTQP VYNAELIEQV YEATKHLSVP IFIGIMPLAS GNNAEYLHNE VPGIQLSDDV RKRMSGLRGE EGRAMGVQIG RELLDAAMRR FNGIYLMTPF LAYEMTVQLT EYVWEKAGRR HLSPLPK // ID H6P901_STRIC Unreviewed; 314 AA. AC H6P901; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 29-APR-2015, entry version 18. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:AEZ62405.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:AEZ62405.1}; GN Name=mmuM {ECO:0000313|EMBL:AEZ62405.1}; GN OrderedLocusNames=Sinf_1083 {ECO:0000313|EMBL:AEZ62405.1}; OS Streptococcus infantarius (strain CJ18). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1069533 {ECO:0000313|EMBL:AEZ62405.1, ECO:0000313|Proteomes:UP000008191}; RN [1] {ECO:0000313|EMBL:AEZ62405.1, ECO:0000313|Proteomes:UP000008191} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CJ18 {ECO:0000313|EMBL:AEZ62405.1, RC ECO:0000313|Proteomes:UP000008191}; 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 ----------------------------------------------------------------------- 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; AEZ62405.1; -; Genomic_DNA. DR RefSeq; WP_014334847.1; NC_016826.1. DR RefSeq; YP_005203876.1; NC_016826.1. DR EnsemblBacteria; AEZ62405; AEZ62405; Sinf_1083. DR KEGG; sif:Sinf_1083; -. DR KO; K00547; -. DR BioCyc; SINF1069533:GLL3-1160-MONOMER; -. DR Proteomes; UP000008191; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008191}; KW Methyltransferase {ECO:0000313|EMBL:AEZ62405.1}; KW Transferase {ECO:0000313|EMBL:AEZ62405.1}. SQ SEQUENCE 314 AA; 34711 MW; 44F0F9B89309BE27 CRC64; MGKLKELLES TDYLILDGAL GTELENRGHD VSGKLWSAKY LLENPQIIQE LHEDYLRSGA DIVTTSSYQA TVQGLEDYGL SEKEALDTIA LTVELAKNAR QNFWQSLSDD EKKKRVYPLI AGDVGPYAAY LADGSEYTGD YQLSKESFKD FHRSRIQTLL AAGSDFLAIE TIPNMTEATA LVELLADEFP DTEAYMSFTA QDSQSISDGT LMTEVAKLCD SSKQILAFGI NCSRPAIISD LLKASRTISQ KPLVTYPNSG EIYDGATQTW KSLPDNSHTL CENSQVWHKL SAKIVGGCCR TRPEDIKLLA DKLK // ID H6P950_STRIC Unreviewed; 618 AA. AC H6P950; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 22. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=Sinf_1133 {ECO:0000313|EMBL:AEZ62454.1}; OS Streptococcus infantarius (strain CJ18). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1069533 {ECO:0000313|EMBL:AEZ62454.1, ECO:0000313|Proteomes:UP000008191}; RN [1] {ECO:0000313|EMBL:AEZ62454.1, ECO:0000313|Proteomes:UP000008191} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CJ18 {ECO:0000313|EMBL:AEZ62454.1, RC ECO:0000313|Proteomes:UP000008191}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; AEZ62454.1; -; Genomic_DNA. DR RefSeq; WP_014334886.1; NC_016826.1. DR RefSeq; YP_005203925.1; NC_016826.1. DR EnsemblBacteria; AEZ62454; AEZ62454; Sinf_1133. DR KEGG; sif:Sinf_1133; -. DR KO; K00547; -. DR BioCyc; SINF1069533:GLL3-1210-MONOMER; -. DR Proteomes; UP000008191; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008191}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:AEZ62454.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:AEZ62454.1}. SQ SEQUENCE 618 AA; 67987 MW; 2496839B391C25F9 CRC64; MSGLLERLKT DILVADGAMG TLLYANGLDN CYEAYNLTHP EKVLAIHKAY IDAGADVIQT NTYAAKRHRL GGYGYGDKIK EINQAGVKIA RQAAGEDTLV LGTVGALRGL KQCELSLDEI IKETLEQVGY LLETKEIDGL LFETYYDEEE IIEILKAVRP LTKLPIITNI SIHEAGITEN GRPLVEIFGK LVMLGADVVG LNCHLGPYHM IQSLKQVPLF AQSYLSVYPN ASLLSFVDDN GSGQYGFSQN ADYFGKSAEL LVAEGARLIG GCCGTTPDHI RAVKRAIKAL KPVSRKFVTP MVEEAELIKA VKQSETIVDK VKRKVTIIAE LDPPKTLDIR KFTKGVKALD EAGVSAITLA DNSLAKTRIC NVSIASLLKN EISTPFLLHL SCRDHNMIGL QSRLLGMDVL GFHQVLAITG DPSKIGDFPG ATSVYDATSF KLLELIKQLN KGIGYSGASI KKETTFTAAA AFNPNVKNLS RCGRLIERKI AAGADCFITQ PIFNSEIIEN LAKLTRDYET PFFVGIMPIT SYNNAIFLHN EVPGIQLSDN FLAKLKAVKD DKEKCQQLAL EESKQLIDHA LKFFNGIYLI TPFMRYDLTV ELVEYIHQKV EQSHQIIS // ID H6QZH4_NOCCG Unreviewed; 1198 AA. AC H6QZH4; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CCF64133.1}; GN Name=metH {ECO:0000313|EMBL:CCF64133.1}; GN OrderedLocusNames=NOCYR_3368 {ECO:0000313|EMBL:CCF64133.1}; OS Nocardia cyriacigeorgica (strain GUH-2). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Nocardiaceae; Nocardia. OX NCBI_TaxID=1127134 {ECO:0000313|EMBL:CCF64133.1, ECO:0000313|Proteomes:UP000008190}; RN [1] {ECO:0000313|EMBL:CCF64133.1, ECO:0000313|Proteomes:UP000008190} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GUH-2 {ECO:0000313|EMBL:CCF64133.1, RC ECO:0000313|Proteomes:UP000008190}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; FO082843; CCF64133.1; -; Genomic_DNA. DR RefSeq; WP_014351589.1; NC_016887.1. DR EnsemblBacteria; CCF64133; CCF64133; NOCYR_3368. DR KEGG; ncy:NOCYR_3368; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; NCYR1127134:GLHX-3354-MONOMER; -. DR Proteomes; UP000008190; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008190}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008190}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 233 233 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 749 749 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1198 AA; 130415 MW; CCA83B661884C94E CRC64; MSASSSTAFD TTLLDTLARR VVIGDGAMGT MLQAADLTLD DFRGLEGCNE ILNDTRPDVL RGIHRAYFEA GADAVETNTF GCNLPNLADY DIADRIRELS EKGTRLAREV ADEMGPGADG SARFVLGSMG PGTKLPTLGH APYAALRDAY AEAALGMLDG GADAILIETC QDLLQVKAAV TGSRRAMERA GRRIPIITHV TVETTGTMLV GSEIGAALTA LEPLGIDMIG LNCATGPDEM SEHLRHLSRH ARIPVSVMPN AGLPVLGAKG AEYPLTPEEL AVALSGFVSE FGLALVGGCC GTTPEHIRQV TEAVREVEPT LPPIEQRRDP VHEPAVSSMY TAVPFAQDAS VMMIGERTNA NGSKAFREAM LAGDWQKCLD IAKDQTRDGA HMLDLCIDYV GRDGTADMSE LASRLATAST LPIMLDSTEP PVLQAGLEHL GGRCAVNSVN YEDGDGPDSR YQQIMRLVAE HGAAVVALTI DEEGQARTAE KKVEIAERLI ADITGTWGLD ESDIIIDTLT FTLGTGQEES RRDGLETIEA IRELKRRHPR VQTTLGLSNI SFGLNPAARQ VLNSVFMHEC VQAGLDSAIV HASKILPISR IPEEQRETAL DLVYDRRRDG YDPLQKLMQL FEGVSASSSK ASRAEELAAL PLFERLERRI VDGEKAGMEA DLDAAMTEVP PLRIINETLL AGMKTVGELF GSGQMQLPFV LQSAEVMKAA VAYLEPHMEA TDDSGKGRIV LATVKGDVHD IGKNLVDIIL SNNGYEVVNL GIKQPISTIM DAAVDKKADV IGMSGLLVKS TVVMKENLEE LNAKGMAGQF PVLLGGAALT RSYVENDLTE VYEGDVHYAR DAFEGLRLMD DIMSRKRGGG PDPDSPEAIA EREKAAERKA RHERSKRIAA ERKAAEAPVV VPERSDVAAD LPVPVPPFWG TRVIKGLALH EYSGLLDERA LFLGQWGLRG QRGGDGPSYE ELVETEGRPR LRAWLDRLST EGVLQHAAVV YGYFPAVSEG DDVIVLTEPD PGAPERYRFT FPRQQRDRFL CIADFIRSRE RAAETGQVDV LPFQLVTMGQ PIADFANELF AADNYRDYLE VHGIGVQLTE ALAEYWHRRV REELVLEGHS VAESDPDDVQ EYFKLGYRGA RYSFGYGACP ELEDRAKLVD LLDSERIGVT LSEELQLHPE QSTDAFVLLH PEAKYFNA // ID H6RDT7_9BACT Unreviewed; 335 AA. AC H6RDT7; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:CCF99198.1}; GN ORFNames=VIS_S3ASA20019 {ECO:0000313|EMBL:CCF99198.1}; OS uncultured Flavobacteriia bacterium. OC Bacteria; Bacteroidetes; Flavobacteriia; environmental samples. OX NCBI_TaxID=212695 {ECO:0000313|EMBL:CCF99198.1}; RN [1] {ECO:0000313|EMBL:CCF99198.1} 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] {ECO:0000313|EMBL:CCF99198.1} 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; FO117573; CCF99198.1; -; Genomic_DNA. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 335 AA; 36918 MW; E825033917D85DBC CRC64; MSKLQDALQK RILILDGAMG TMLQRYKFTE DDFRGLRFKD WLDSVQGNND LLSLTQPRAI AEIHAKYFDA GADIVETNTF SGTTIAMADY RMEELVYELN YESAKIARRV ADEFTAKEPQ KPRFVAGAMG PTNKTASMSP DVNDPGYRAI TFDELRKAYK QQAEALLDGG VDILLVETIF DTLNAKAALF AIEEIKEERA MDIPVMVSGT ITDASGRTLS GQTAEAFLIS ISHLELLSVG FNCALGAEQL TPYLEVVSNR SECGISAYPN AGLPNAFGEY DQTPQEMADQ VKEYLEKGLI NIIGGCCGTT PEHIKAIAEV AKNFKPRKIR ELSSN // ID H6RJR0_BLASD Unreviewed; 1266 AA. AC H6RJR0; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CCG03563.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CCG03563.1}; GN Name=metH {ECO:0000313|EMBL:CCG03563.1}; GN OrderedLocusNames=BLASA_2688 {ECO:0000313|EMBL:CCG03563.1}; OS Blastococcus saxobsidens (strain DD2). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Frankineae; Geodermatophilaceae; Blastococcus. OX NCBI_TaxID=1146883 {ECO:0000313|EMBL:CCG03563.1, ECO:0000313|Proteomes:UP000007517}; RN [1] {ECO:0000313|Proteomes:UP000007517} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DD2 {ECO:0000313|Proteomes:UP000007517}; RA Genoscope.; RT "Complete genome sequence of Blastococcus saxobsidens strain DD2."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; FO117623; CCG03563.1; -; Genomic_DNA. DR RefSeq; WP_014376446.1; NC_016943.1. DR RefSeq; YP_005329594.1; NC_016943.1. DR EnsemblBacteria; CCG03563; CCG03563; BLASA_2688. DR KEGG; bsd:BLASA_2688; -. DR KO; K00548; -. DR OMA; QPFFNAW; -. DR BioCyc; BSAX1146883:GL9E-2598-MONOMER; -. DR Proteomes; UP000007517; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007517}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CCG03563.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007517}; KW Transferase {ECO:0000313|EMBL:CCG03563.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 254 254 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 318 318 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 771 771 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1266 AA; 138514 MW; F2913BAE30A14549 CRC64; MSESPTLRPD VTAQLTDLLR QRILVLDGAM GTAIQRDRPD EAGYRGERFA DWPSDVQGNN DLLSITQPQI IAAIHREYLE AGADLIETNT FNATTISLSD YGMGDLAYEL NVASARLARR EADAMAARTP GKPRFVVGAI GPTSRTASIS PDVNDPGARN VSFDDLVAAY LEQANGLVDG GSDALLVETI FDTLNAKAAI FALETLFEER GRRWPVLISG TITDASGRTL SGQVTEAFWH SVRHVHPLLV GLNCALGAKE MRPYVAEISR VADTFVSCYP NAGLPNAFGE YDEAPDETAA IVGEFAESGF VNMVGGCCGT TPAHIAAIAR AVEEQAPRTP AEVRPALRLS GLEPLTVTEE SLFVNVGERT NITGSARFRN LIKAGDYPTA LTVARQQVEA GAQVIDINMD EGMIDGVEAM DRFTKLIAAE PDISRVPVMV DSSKWEVMEA GLKNIQGKAI VNSISLKEGE EKFVHHARLC RKYGAAVVVM AFDEAGQGDT LERRTQICRR AYDILVEQVG FPIEDIIFDP NIFAVATGIE EHANYGLDFI EATRWIKQNL PGALVSGGVS NVSFSFRGNN PVREAIHSVF LYHAIAAGLD MAIVNAGQLE VYSEVPELLR ERIEDVILNR RPDSTERLLE IAGDFAGDGS VKEVATEEWR SLPVGERITH ALVKGIDEFA ESDTEELRAE IAARGGRPIE VIEGPLMDGM NVVGDLFGAG KMFLPQVVKS ARVMKKAVAY LIPYIEAEKQ PGDAERTNGK VVMATAKGDV HDIGKNIVGV VLQCNNYDVV DLGVMVPPQK ILDAAKAEGA DVIGLSGLIT PSLDEMVTLA TEMERQGFEV PLLIGGATTS RAHTAVKIAQ KYHGPVIWVK DASRSVPVVA ALLSDEQRPK LLAETDADYA ALRERHAARQ DSRKLLPIAA ARAAATPIDW SDYLPPRPRM LLQQALDTCS GAGCDHLRHT ATQFGKTFPD YPLEELRGYI DWQPFFNAWE MRGRFPDILH NPTTGEAARR LYEDAQAMLD RIVEERWLRA SGVFGLFPAN QVEGDDIEVY TDESRTGVRT VLHQLRQQTE GREGSPRKSL ADFVAPKETG LRDYVGAFAV TAGLGSTERV TAFKKDNDDY SAIMLEALAD RLAEAFAERL HERVRREFWG YAADETLDNQ ALIAEKYTGI RPAPGYPACP EHTEKRTIWD LLDVEAATGI ELTESMAMWP GAAVSGLYFS HPQSRYFVLG RVGRDQVEDY AGRKGWSVGE AERWLSPNLG YRTEDE // ID H6RVP0_BLASD Unreviewed; 302 AA. AC H6RVP0; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=MmuM protein {ECO:0000313|EMBL:CCG03315.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:CCG03315.1}; GN Name=mmuM {ECO:0000313|EMBL:CCG03315.1}; GN OrderedLocusNames=BLASA_2413 {ECO:0000313|EMBL:CCG03315.1}; OS Blastococcus saxobsidens (strain DD2). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Frankineae; Geodermatophilaceae; Blastococcus. OX NCBI_TaxID=1146883 {ECO:0000313|EMBL:CCG03315.1, ECO:0000313|Proteomes:UP000007517}; RN [1] {ECO:0000313|Proteomes:UP000007517} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DD2 {ECO:0000313|Proteomes:UP000007517}; 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; CCG03315.1; -; Genomic_DNA. DR RefSeq; WP_014376198.1; NC_016943.1. DR RefSeq; YP_005329346.1; NC_016943.1. DR EnsemblBacteria; CCG03315; CCG03315; BLASA_2413. DR KEGG; bsd:BLASA_2413; -. DR KO; K00547; -. DR OMA; YGRSVTK; -. DR BioCyc; BSAX1146883:GL9E-2346-MONOMER; -. DR Proteomes; UP000007517; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007517}; KW Methyltransferase {ECO:0000313|EMBL:CCG03315.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007517}; KW Transferase {ECO:0000313|EMBL:CCG03315.1}. SQ SEQUENCE 302 AA; 30240 MW; 1150A3F725647B0C CRC64; MIGGMPSLAD ALATGPVVLD GGLSTELESR GHDVSSALWS ARLLRDDPAA IVSAHAAFAA AGAQVATTAS YQATVEGFAA VGVDADVARR LIASSVALAR DGQGTGWVAG SVGPYGAMLA DGSEYTGGYV AEMDVAALCA FHRPRMELLA QAGADVLACE TVPAAAEAEA LLLAAQELGV PVWLSLTTVV DAAGVARTRR GELAADVFAM AADVAEVVAV GVNCTAPDAV RPAVLAAGTS GKPVVAYPNS GETWDAGARR WAGPPGVAAD DAVAWTTAGA RLVGGCCRVR PADIAAITMM IR // ID H6SN06_RHOPH Unreviewed; 1230 AA. AC H6SN06; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Rhodospirillum photometricum DSM 122 draft genome sequence {ECO:0000313|EMBL:CCG06882.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CCG06882.1}; GN ORFNames=RSPPHO_00256 {ECO:0000313|EMBL:CCG06882.1}; OS Rhodospirillum photometricum DSM 122. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Rhodospirillum. OX NCBI_TaxID=1150469 {ECO:0000313|EMBL:CCG06882.1}; RN [1] {ECO:0000313|EMBL:CCG06882.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 122 {ECO:0000313|EMBL:CCG06882.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; HE663493; CCG06882.1; -; Genomic_DNA. DR RefSeq; WP_014413522.1; NC_017059.1. DR RefSeq; YP_005415852.1; NC_017059.1. DR EnsemblBacteria; CCG06882; CCG06882; RSPPHO_00256. DR KEGG; rpm:RSPPHO_00256; -. DR KO; K00548; -. DR BioCyc; RPHO1150469:GLJ6-328-MONOMER; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CCG06882.1}; KW Transferase {ECO:0000313|EMBL:CCG06882.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 265 265 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 331 331 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 332 332 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 776 776 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1230 AA; 135167 MW; EE119BE7365CE4AD CRC64; MPLADGRWRA RLPLLYPQPA GSGPSHLPRP WGASPSRPRE PRSMSRFLDA LRERVLLCDG GMGSLVQAMD LSVEKDFLGR ENCTEALTLA RPDVVRGLHA RYFEAGADCV ETNTFGGSIL TLAEFDLQDR TREINRRSVE LAREAAEGFS DGRERFVLGS VGPGTRLPSL GHVDYDTLKD SLTEQCLGLI EGGADAILIE TCQDPLQFKA AINAAKKARI HHGTDTPILL QVTVETTGTL LVGADIAAAA TVAHALGVDS LGLNCATGPR EMSEHVRWLA ENWPGFISLQ PNAGLPELVD GKAHYPLTPA ELADWHKRFI LEDGVNLVGG CCGTTPPHIQ AVDAMLRTLA QETGRPDRPA PVRRTVHWVP SVASLYGAVP LRQENAFLSI GERCNANGSK KFRTLQDAED WDGIVGMARE QGREGSHTLD VCTAFVGRNE TRDMTEVITR LRGSVHMPLV IDSTETKVLA AALKLYGGKA ILNSINFEDG EETAAQRLEL AREFGAAVIA LTIDEEGMAK DADSKLRIAR RLYEFAVTEH GLAPEDLLFD PLTFTICTGN EDDRRLGLET LNAIRQIREQ MPGCQIILGL SNISFGLKPA ARCVLNSVFL DEAVKAGMTG AIVHVSKILP LHKIPEAEVQ AALNLIHDRR EAGDPLHAFI RLFEDRVEAK AEARADAPVD ERLRQRIIDG DRLGLEADLE EARALMPPLE IINTILLDGM RVVGELFGAG KMQLPFVLQS AETMKAAVSH LEPHMEKIEG QERGIMVLAT VKGDVHDIGK NLVDIILSNN GYKVVNIGIK QPLPAILDAA RTHKADAIGL SGLLVKSTVI MKDNLEEMAR DGWDVPVVLG GAALTRAFVE EDCVRAYGNH GRVAYARDAF DGLDLMAKVM EGSFDRHLAA IQEKRQAKPS RRAREAAEAL DAVALAAAND LTADQAQAAK PRRLDRPVDA EEISLRRAEL ARQTEIHTPP FWGARLVEGI SLKTLVPFIN EATLFQFQWG FRKGSRTRDE WKVWAETELR PILFDMLQRC AQDAILEPKA VYGFWKAASD GDAIVLYDED GRREVARFAL PRQAKAGGLC LADFVRDVSA GPQDRDVVAL QAVTVGARAS DVARAWFAEN KYKDYLYLHG VSVEVAEALA EYMHKRIRAE LGFGAEDARD TEELFKQAYR GSRYSFGYPA CPHLEDQRHL LDLLGAERIG LDLSEEFELV PEQSTSALVL FHPQAKYFRV // ID H6SSE0_RHOPH Unreviewed; 296 AA. AC H6SSE0; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Rhodospirillum photometricum DSM 122 draft genome sequence {ECO:0000313|EMBL:CCG07819.1}; GN ORFNames=RSPPHO_01193 {ECO:0000313|EMBL:CCG07819.1}; OS Rhodospirillum photometricum DSM 122. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Rhodospirillum. OX NCBI_TaxID=1150469 {ECO:0000313|EMBL:CCG07819.1}; RN [1] {ECO:0000313|EMBL:CCG07819.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 122 {ECO:0000313|EMBL:CCG07819.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; CCG07819.1; -; Genomic_DNA. DR RefSeq; WP_014414458.1; NC_017059.1. DR RefSeq; YP_005416789.1; NC_017059.1. DR EnsemblBacteria; CCG07819; CCG07819; RSPPHO_01193. DR KEGG; rpm:RSPPHO_01193; -. DR BioCyc; RPHO1150469:GLJ6-1295-MONOMER; -. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 204 204 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 280 280 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 281 281 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 296 AA; 31250 MW; 142B900F059B9872 CRC64; MATVRVLDGG MGRELKRRGA PFRQPEWSAL ALLEGPGFVT LAHQAFLEAG ASILTTNSYA VVPFHLGQER FEARGTELAA LAGRLAREVA DRASPAAIVA GSLPPALGSY RPDLFDEAAS IAIHQKLIEG LAPFVDVWLA ETQSSIAEVR AARTALGNDP KPLWLSFTLD DEPVAGPVLR SGEPVAVAVE EALALGARAV LFNCSQPEVM GAAVTTAREE ARKAGVSLDL GVYANAFPPT PKDAKANETL DELRPDLDPA RYAAWAQAWV DQGATIIGGC CGITPEHINA LARALK // ID H7CWE9_CLOPF Unreviewed; 279 AA. AC H7CWE9; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EIA17102.1}; GN ORFNames=HA1_08892 {ECO:0000313|EMBL:EIA17102.1}; OS Clostridium perfringens F262. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=883064 {ECO:0000313|EMBL:EIA17102.1, ECO:0000313|Proteomes:UP000005358}; RN [1] {ECO:0000313|EMBL:EIA17102.1, ECO:0000313|Proteomes:UP000005358} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F262 {ECO:0000313|EMBL:EIA17102.1}; 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. {ECO:0000313|EMBL:EIA17102.1}. 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; AFES01000023; EIA17102.1; -; Genomic_DNA. DR RefSeq; WP_003481554.1; NZ_CM001477.1. DR EnsemblBacteria; EIA17102; EIA17102; HA1_08892. DR Proteomes; UP000005358; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005358}. SQ SEQUENCE 279 AA; 30967 MW; EA737850251E34A4 CRC64; MKNLNLKNGV IIADGAMGTR IMELGVNLKE TPSELLNIKK PELIEKIHRE YIESGANLIL SNTFMCNIIN AKRNNYNLEE VIEAGISIAK KACGDHGLVA LDIGPLSYYI EENDSSFKEI VYENTERIIN ASKDKFDLVI FETLGSLKEG EFAVKKAKTL TDKKVICSFT LAYKKDIPNF IKNMVSTLEP LGVDALGINC TGYEEILIAL DILKENTNLP IMIKANLGIP KKVGEELVYD KTLEEFKNLS KRALEKGVNI IGGCCGTTPE YIRAICNLK // ID H7EFE9_SALHO Unreviewed; 1227 AA. AC H7EFE9; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EHY67160.1}; GN ORFNames=SEHO0A_04280 {ECO:0000313|EMBL:EHY67160.1}; OS Salmonella enterica subsp. houtenae str. ATCC BAA-1581. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=523831 {ECO:0000313|EMBL:EHY67160.1, ECO:0000313|Proteomes:UP000004436}; RN [1] {ECO:0000313|EMBL:EHY67160.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-1581 {ECO:0000313|EMBL:EHY67160.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHY67160.1}. 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; AGRM01000005; EHY67160.1; -; Genomic_DNA. DR RefSeq; WP_000096077.1; NZ_CM001471.1. DR EnsemblBacteria; EHY67160; EHY67160; SEHO0A_04280. DR Proteomes; UP000004436; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000004436}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136114 MW; 2553AEC5C0AFFFD9 CRC64; MSSKVEQLRT QLNERILVLD GGMGTMIQSY RLHEENFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYRMESLS AEINYAAAKL ARACADEWTA RTPEKPRFVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VDGGADLILI ETVFDTLNAK AAVFAVKETF EALGVDLPIM ISGTITDASG RTLSGQTTEA FYNSLRHAGA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKHIREWAQ AGFLNIVGGC CGTTPEHIAA MSRAVEHLPP RKLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VESGAQIIDI NMDEGMLDAE AAMVRFLSLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVETFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRERKIEI CRRAYHILTK EVGFPPEDII FDPNIFAVAT GIDEHNNYAQ DFIGACEDIK RELPYALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLSLAEKYRG SKTDEAANAQ QAEWRSWDVK KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EKGSSNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIIDL GVMVPADKIL KTAREVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHARKKPR TPPVTLEAAR DNDLAFDWER YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG EEAKRLFKDA NDMLDKLSAE KLLNPRGVVG LFPANRVGDD IEIYRDETRT HVLTVSRHLR QQTEKVGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAYEAQH DDYNKIMVKA IADRLAEAFA EYLHERVRKV YWGYAPGESL SNEELIRENY QGIRPAPGYP ACPEHTEKGT IWQLLDVEKH TGMKLTESFA MWPGASVSGW YFSHPESKYF AVAQIQCDQV TDYAFRKGMS VEDVERWLAP NLGYDAD // ID H7ELC2_9SPIO Unreviewed; 888 AA. AC H7ELC2; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Cobalamin B12-binding domain protein {ECO:0000313|EMBL:EIC01654.1}; GN ORFNames=TresaDRAFT_2043 {ECO:0000313|EMBL:EIC01654.1}; OS Treponema saccharophilum DSM 2985. OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema. OX NCBI_TaxID=907348 {ECO:0000313|EMBL:EIC01654.1}; RN [1] {ECO:0000313|EMBL:EIC01654.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 2985 {ECO:0000313|EMBL:EIC01654.1}; 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., 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. {ECO:0000313|EMBL:EIC01654.1}. 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; AGRW01000048; EIC01654.1; -; Genomic_DNA. DR RefSeq; WP_002704689.1; NZ_AGRW01000048.1. DR EnsemblBacteria; EIC01654; EIC01654; TresaDRAFT_2043. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; SQ SEQUENCE 888 AA; 94986 MW; 349739DABAD0AD0A CRC64; MEKRKPAFRE FLKERIQAGK PVYFDGGMGT MIQASGVTDY AIPEDLSVTN PDVIKEIHKK YIRAGAHVLT GNTFGINPLK IGDARFSLEE YLKAEFDVMK AAISEEKADG EPRYAAWDSG QIGRLLEPMG DMTFDEAYEA YKIAATTAEK YGAELAILET MSDLHELKAA ILAVKENTKL PIVATTTFQD NLRTLTGADV LTCVTYLEAL RVDVLGFNCG GSLPDGEELT RQFCRYSHTP VLVQPNAGIP TVVNGKAVFP ARAGEFAQSQ LRNRFSGALL LGGCCGTTPD HISAMIGAVE SGKAAEDSGK RAEFKNIAEI GAKKTAEPRN STDSTSAQQE SGDNSASCRS VDTFICSYNS TVQIGGKAGP QIVGERINPT GKKKVKAALQ AHDMNFVLDE AESQINAGAQ ILDVNVGLPG IDEAQTMVDA VKTIQAAFNV PLQLDSSEAP VLEKGLRYYN GKPLVNSVNG KREVMDKVFP LVAHYGGAVV ALCIDEDGIA PTAEGRCAVA RKIIAEAAKY GIPVRDIVID TLTLTVSSQQ KEALETCRAI EILKKEFGAQ GLQFILGVSN ISFGLPRRDI VNSRFFMAAL YSGLTACIIN PLSEPMMETY HGYRALAGFD ENCLGYIEKY TGTTAPVYGI SAEQARSLSG TEAGGTSNAK TPENSSAVLP ADLTEEEKTL IDTICKGFKD ASPDATRKLL DGGKKPVEII DRCIVPALDL VGKDFESGRK FLPQLLLSAD TVSAAFAVIK ETLASSGAAA EEKGKIVIAT VHGDIHDIGK NIVKAMLENY GYTVIDLGKN VPAETVVKTV VENEIRLVGL SALMTTTVAS MEETIKLLRE ETAKLGRDVK IIAGGAVLTA DYAAKIGADY FGKDAMATVA VAKEVFGK // ID H7EQ85_PSEST Unreviewed; 1230 AA. AC H7EQ85; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EHY75909.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EHY75909.1}; GN Name=metH {ECO:0000313|EMBL:EHY75909.1}; GN ORFNames=PstZobell_00542 {ECO:0000313|EMBL:EHY75909.1}; OS Pseudomonas stutzeri ATCC 14405 = CCUG 16156. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=32042 {ECO:0000313|EMBL:EHY75909.1}; RN [1] {ECO:0000313|EMBL:EHY75909.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCUG 16156 {ECO:0000313|EMBL:EHY75909.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EHY75909.1}. 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; AGSL01000010; EHY75909.1; -; Genomic_DNA. DR RefSeq; WP_003279782.1; NZ_AGSL01000010.1. DR EnsemblBacteria; EHY75909; EHY75909; PstZobell_00542. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHY75909.1}; KW Transferase {ECO:0000313|EMBL:EHY75909.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1230 AA; 134827 MW; 009D2AD5D172BE4A CRC64; MSTRSSRLQA LQQALKERIL ILDGGMGTMI QSYKLEEEDY RGARFADWPQ DVKGNNDLLL LSRPDVIQAI EKAYLDAGAD ILETNTFNAT QVSQADYGME SLVYELNVEG ARLAREVADA KTAETPDRPR FVAGVLGPTS RTCSISPDVN NPGYRNVTFD LLVENYVEAT RGLIEGGADL ILIETIFDTL NAKAAIFAVQ QVFEDEGVEL PIMISGTITD ASGRTLSGQT TEAFWNSVRH AKPISVGLNC ALGAKDLRPY LEELSSKADT FVSAHPNAGL PNAFGEYDES PAEMAAVVEE FAVSGFLNII GGCCGTTPAH IQAIAEAVSK YPPRVIPDIP KACRLSGLEP FTIDRSSLFV NVGERTNITG SAKFARLIRE ENYTEALEVA LQQVEAGAQV IDINMDEGML DSKAAMVTFL NLIAGEPDIS RVPIMIDSSK WEVIEAGLKC IQGKGIVNSI SMKEGVEQFK HHAHLCKRYG AAVVVMAFDE AGQADTAARK REICQRSYDI LVNEVGFPPE DIIFDPNIFA IATGIEEHNN YAVDFIEACA FIRDNLPYAL TSGGVSNVSF SFRGNNPVRE AIHSVFLFHA IKAGLTMGIV NAGQLEIYDE IPKELRDAVE DVVLNRSANG TEGLLELADK YKGDGSVKEA ETEEWRGLPV GKRLEHALVK GITAFIVEDT EEYRQQCARP IEVIEGPLMS GMNVVGDLFG AGKMFLPQVV KSARVMKQAV AHLIPFIEAE KGDKPEAKGK ILMATVKGDV HDIGKNIVGV VLGCNGYDVV DMGVMVPAEK ILQTAIAEKC DIIGLSGLIT PSLDEMVHVA KEMQRQGFSL PLMIGGATTS KAHTAVKIDP QYHNDAVVYV TDASRAVGVA TTLLSKELKP AFVEKTREEY AMIRERTANR SARTERLSYA QAVANKPQFD WASYTPVKPS FTGRQLLEDI DLRTLAEYID WTPFFIAWDL AGKYPRILED EVVGEAATAL FSDAQAMLNK LIDEKLIRAR AVFGFWPANQ VQDDDLEVYG DNGEKLATLH HLRQQIIKPD AKPNLSLADF VAPKDCGIAD YVGGFICTAG IGAEELAKAY QDKGDDYNSI MVKALADRLA EACAEWLHQQ VRKQYWGYAK DEQLSNDELI REQYKGIRPA PGYPACPDHT EKGTLFQLLD ADGISQVTLT EHYAMLPTAA VSGWYFAHPE AQYFAVGKID KDQVESYSQR KGEDIAVSER WLMPNLGYDA // ID H7F7I4_9LIST Unreviewed; 614 AA. AC H7F7I4; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 27-MAY-2015, entry version 17. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=KKC_11401 {ECO:0000313|EMBL:EIA19623.1}; OS Listeria fleischmannii subsp. coloradonensis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=1081736 {ECO:0000313|EMBL:EIA19623.1}; RN [1] {ECO:0000313|EMBL:EIA19623.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TTU M1-001 {ECO:0000313|EMBL:EIA19623.1}; RX PubMed=23524352; DOI=10.1099/ijs.0.048587-0; RA den Bakker H.C., Manuel C.S., Fortes E.D., Wiedmann M., RA Nightingale K.K.; RT "Genome sequencing identifies Listeria fleischmannii subsp. RT coloradonensis subsp. nov., isolated from a ranch."; RL Int. J. Syst. Evol. Microbiol. 63:3257-3268(2013). CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIA19623.1}. 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; AGUG01000141; EIA19623.1; -; Genomic_DNA. DR RefSeq; WP_007547097.1; NZ_AGUG01000141.1. DR EnsemblBacteria; EIA19623; EIA19623; KKC_11401. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EIA19623.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EIA19623.1}. SQ SEQUENCE 614 AA; 68429 MW; 133750A91B435E07 CRC64; MNLRKDLSEK VLIADGAMGT LLYSYGVDRA FEELSLTHPE DVLNIHKAYI EAGADIIQTN TYGANYIKLK RYGLEDEIKR INQAAIRLAK RATSGTGTYI FGTMGGINGA SDSKVEQAPL DEIKRSFREQ LYCFLLEGVD AILLETFYDP NELKTVLQIV RENTDLPVIA NVSMHEPGLL QNGEKLPDVL QEIADLGADV VGVNCRLGPY HMARALETVP LLDNAYLAAY PNASLPEMQE GKIIYQAETD YFQEYGEIFR KQGARIIGGC CGTTPEHIRA FRAGLRSTKP IKTKEVRPII ELVPEEPSPL EGVRLLDKVR EECTVLVELD PPRTFDTEQF FEGAKALHAA GADAITISDN SLATPRISNM AIASILKHEY DIKPLIHLTT RDHNLVGMHS HIMGFHKLGL HDVLAVTGDP TKVGDFPGAS SVFDLRSVEL IQLIKKFNDG ISYTGKSLKE KARFHVAAAF NPNVLNVEKA VRLIERKVEY GADYIITQPI YDTQKARVLN EALKEAQISV PVFVGVMPLL SSRNAEFLHN EVPGIRLTNE VRERMREAEK AGRGNEEGML ISKEIIDSIS EHFNGVYIIT PFLRYDLSLE LLQYAKSKEQ VHVI // ID H7FPL8_9FLAO Unreviewed; 333 AA. AC H7FPL8; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EIA09698.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EIA09698.1}; GN ORFNames=HJ01_01116 {ECO:0000313|EMBL:EIA09698.1}; OS Flavobacterium frigoris PS1. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=1086011 {ECO:0000313|EMBL:EIA09698.1}; RN [1] {ECO:0000313|EMBL:EIA09698.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PS1 {ECO:0000313|EMBL:EIA09698.1}; RA Raymond J., Kim H.J.; RT "Flavobacterium frigoris PS1, a freeze-tolerant bacterium from RT Antarctic sea ice."; 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. {ECO:0000313|EMBL:EIA09698.1}. 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; AHKF01000014; EIA09698.1; -; Genomic_DNA. DR RefSeq; WP_007137293.1; NZ_AHKF01000014.1. DR EnsemblBacteria; EIA09698; EIA09698; HJ01_01116. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EIA09698.1}; KW Transferase {ECO:0000313|EMBL:EIA09698.1}. SQ SEQUENCE 333 AA; 36327 MW; 3D6C7ED9BE7642AF CRC64; MSSIHEAIKK NILILDGAMG TMLQRYNFSE EDFRGERFKD FPHSLKGNND LLSLTQPQAI KAVHAAYFEA GADIVETNTF SGTTIGMADY HLEDIVYELN YESAKLAREV ADEFTAKNPD KPRFVAGSIG PTNRTASMSP DVNDPGYRAV TFDDLRIAYK QQVEALIDGG SDLLLVETIF DTLNAKAALF AIEEVKDERN IDIPIMVSGT ITDASGRTLS GQTVEAFLVS VSHIPLLSVG FNCALGADLL KPYLQTLSQN TSFNVSAHPN AGLPNAFGEY DETPAEMQSQ IKTYLDDNLV NIIGGCCGTT PEHIKLIADI AKDYKPRVST ATM // ID H7FYY0_9LACO Unreviewed; 307 AA. AC H7FYY0; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 27-MAY-2015, entry version 12. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:EIA32730.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EIA32730.1}; GN Name=mmuM {ECO:0000313|EMBL:EIA32730.1}; GN ORFNames=SMXD51_01893 {ECO:0000313|EMBL:EIA32730.1}; OS Lactobacillus salivarius SMXD51. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1108963 {ECO:0000313|EMBL:EIA32730.1}; RN [1] {ECO:0000313|EMBL:EIA32730.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SMXD51 {ECO:0000313|EMBL:EIA32730.1}; RX PubMed=22582370; DOI=10.1128/JB.00344-12; RA Kergourlay G., Messaoudi S., Dousset X., Prevost H.; RT "Genome Sequence of Lactobacillus salivarius SMXD51, a Potential RT Probiotic Strain Isolated from Chicken Cecum, Showing Anti- RT Campylobacter Activity."; RL J. Bacteriol. 194:3008-3009(2012). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIA32730.1}. 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; AICL01000003; EIA32730.1; -; Genomic_DNA. DR RefSeq; WP_003709360.1; NZ_AICL01000003.1. DR EnsemblBacteria; EIA32730; EIA32730; SMXD51_01893. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EIA32730.1}; KW Transferase {ECO:0000313|EMBL:EIA32730.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 223 223 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 307 AA; 34414 MW; E0E8887EF1911759 CRC64; MDFTEFLTNN PVVLDGAMST PLEKLGADTN NDLWTAKALI DNEELVYEVH KMYFEAGADL IITDTYQANV QAFEKVGYSE KEARNLIKKA VKIAQKARDD YENRTGKHNY IAGTIGPYGA YLANGSEYRG DYELSAEEYQ QFHLPRIEEL VNAGVDILAI ETQPKLDEVL AILELLKEKY PQQKVYVSYT LSDDDTISDG TPLPRAIHAL EDYSQVIAVG INCVKLELVE PALKNMKEIT DKHLIVYPNS SAVYDPKSKT WSQPKTSATF EELIPNWYEA GARIIGGCCT TGPKEIKAVA DFIKRNK // ID H8DLX9_9ENTR Unreviewed; 311 AA. AC H8DLX9; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 01-OCT-2014, entry version 9. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:EIB97862.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EIB97862.1}; GN Name=mmuM {ECO:0000313|EMBL:EIB97862.1}; GN ORFNames=S7A_05075 {ECO:0000313|EMBL:EIB97862.1}; OS Pantoea sp. Sc1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Pantoea. OX NCBI_TaxID=593105 {ECO:0000313|EMBL:EIB97862.1}; RN [1] {ECO:0000313|EMBL:EIB97862.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Sc1 {ECO:0000313|EMBL:EIB97862.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIB97862.1}. 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; AJFP01000001; EIB97862.1; -; Genomic_DNA. DR RefSeq; WP_009088564.1; NZ_AJFP01000001.1. DR EnsemblBacteria; EIB97862; EIB97862; S7A_05075. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EIB97862.1}; KW Transferase {ECO:0000313|EMBL:EIB97862.1}. SQ SEQUENCE 311 AA; 33382 MW; 1FDA5454B767EDB2 CRC64; MSYNPVAQAL TESPLLILDG ALATELEARG CQLADALWSA KVLMEDPELI YQVHYDYFVA GARCAITASY QATPQGFATR GLSEDESLAL IARSVELTQR ARHDYLAVRP DAKTLLVAGS VGPYGAFLAD GSEYRGDYAL PEAEMMAFHR PRVQALLAAG ADLLACETLP SFAEAQALVK LLAEFPDARA WFSFTLRDAG HISDGTPLAE VVSWLNQQPQ VVALGVNCVA LESVTPALQQ LQTLTDKPLV VYPNSGEQYD AGSKTWHSAP SGCTLHDKLA EWQQAGARLI GGCCRTSPGD IAAIARTCQP Q // ID H8DN94_9ENTR Unreviewed; 1227 AA. AC H8DN94; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 01-APR-2015, entry version 17. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EIC00332.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EIC00332.1}; GN Name=metH {ECO:0000313|EMBL:EIC00332.1}; GN ORFNames=S7A_17520 {ECO:0000313|EMBL:EIC00332.1}; OS Pantoea sp. Sc1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Pantoea. OX NCBI_TaxID=593105 {ECO:0000313|EMBL:EIC00332.1}; RN [1] {ECO:0000313|EMBL:EIC00332.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Sc1 {ECO:0000313|EMBL:EIC00332.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EIC00332.1}. 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; AJFP01000001; EIC00332.1; -; Genomic_DNA. DR RefSeq; WP_009092638.1; NZ_AJFP01000001.1. DR EnsemblBacteria; EIC00332; EIC00332; S7A_17520. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EIC00332.1}; KW Transferase {ECO:0000313|EMBL:EIC00332.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135136 MW; 1671F6D648CD37BC CRC64; MSTKIDALYQ QLAQRIMVLD GAMGTLIQRY RLEEADFRGS RFAEWPCDLK GNNDLLVLSQ PAVIREIHDA YLAAGADILE TNTFNATSIA MADYRMESLS AEINREAARL ARSCADAWTA KTPDRPRFVA GVLGPTNRTC SISPDVNDPA FRNVTFSQLV DAYRESTRAL VEGGVDLIMI ETVFDTLNAK AAVYAVQSEM EALGVTLPLM ISGTITDASG RTLSGQTTEA FYNALRHAEP LSFGLNCALG PDELRQYVAE LSRIAEGYVS AHPNAGLPNA FGEYDLDAEV MARQMGEWAR AGFLNIIGGC CGTTPQHIAA MAAAVEGVAP RKPPAIPVAC RLSGLEPLNI SAESLFVNVG ERTNVTGSAK FKRLIKEEKY HEALDVALQQ VQSGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP VMIDSSKWAV IEKGLQCIQG KGIVNSISMK EGEAAFIHYA RQVRRYGAAM VVMAFDEVGQ ADTRARKIAI CRRAYQILTQ EVGFPPEDII FDPNIFAVAT GIEEHNNYAM DFIGACEDIR RELPHAMISG GVSNVSFSFR GNEPVREAIH AVFLYHAIRN GMGMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRREEGTER LLALAETYRG GKSDGAEEKQ LAEWRGWAVA KRLEYSLVKG ITEFIEQDTE EARQQVSRPI EVIEGPLMAG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EAGRSNGKIV LATVKGDVHD IGKNIVGVVL QCNNYEIIDL GVMVPGEKIL KTAREVDADI IGLSGLITPS LDEMVNMAKE MERQGFTLPL LIGGATTSKA HTAVKIEQHY SGPTVYVQNA SRTVGVVSSL LSDTLKADFI ARTRREYETV RIQHARKKPR TPPVSLQAAR DNASLIAWEN YTPPVPHRPG VSQVEASIDT LRHYIDWTPF FMTWSLAGKY PRILEDEVVG EEAQRLFADA SAMLDRLSEQ SLLTPRGVVG IFPANRVGDD IHLYSDERRD EVLCVSHHLR QQTEKADFAN YCLADFVAPK STGKADYLGA FAVTGGLEED ALAAAYDLQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV IWGFAPNENL SNDELIRERY QGIRPAPGYP ACPDHTEKAA IWTLLGVEEQ IGMTLTESYA MWPGAAVAGW YFSHPDSRYF AVAQIQRDQV EDYAARKAMS VSEVERWLAP HLGYDEE // ID H8E3X7_9MICO Unreviewed; 1243 AA. AC H8E3X7; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EIC08464.1}; GN ORFNames=OR221_1557 {ECO:0000313|EMBL:EIC08464.1}; OS Microbacterium laevaniformans OR221. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Microbacteriaceae; Microbacterium. OX NCBI_TaxID=1160710 {ECO:0000313|EMBL:EIC08464.1}; RN [1] {ECO:0000313|EMBL:EIC08464.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=OR221 {ECO:0000313|EMBL:EIC08464.1}; RX PubMed=22628508; DOI=10.1128/JB.00474-12; RA Brown S.D., Palumbo A.V., Panikov N., Ariyawansa T., Klingeman D.M., RA Johnson C.M., Land M.L., Utturkar S.M., Epstein S.S.; RT "Draft Genome Sequence for Microbacterium laevaniformans Strain OR221, RT a Bacterium Tolerant to Metals, Nitrate, and Low pH."; RL J. Bacteriol. 194:3279-3280(2012). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EIC08464.1}. 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; AJGR01000118; EIC08464.1; -; Genomic_DNA. DR RefSeq; WP_005049815.1; NZ_AJGR01000118.1. DR EnsemblBacteria; EIC08464; EIC08464; OR221_1557. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 246 246 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 797 797 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1243 AA; 133781 MW; B33B4ED0F7850F39 CRC64; MTASIAAARF ALDIDGVPRT ARAQALLDTL SERVVIADGA MGTMLQRHDL QIDTDFHGLE GCNEILNVTR PDVVGAIHDA YFAVGVDAVE TNTFGANWSN LSDYGIDDRI TELAAAGARI ARERAEAAEA VDGRMRWVLG SMGPGTKLPS LGHTTYAHLK ETFALQAEGL IDGGADAFLV ETSQDLLQTK AAINGCKQAI VARGIRLPIF VEVTVETTGA MLMGSEIGAA LTALEPLGVD AIGLNCATGP AEMSEHLRHL SKHSSVTIAC MPNAGLPVLT ADGAHYPLTP AELATAHEQF VREFGIGLIG GCCGTTPEHL AAVVERVGHL PVATRTPDRE TPPGHRDTES APVSRRENGV SLASAIETEP GVASLYQHVP FRQDASYLAI GERTNANGSK AFREAMLEGR WEDCVEIARG QIRVGAHLLD VCVDYVGRDG VDDIREVVSR FASASTLPLV IDSTEPAVIQ AGLELIGGRP VVNSVNYEDG DGPASRFGRI MPLVKEHGTA VIALTIDEQG QARTAEDKLR IASRLVDELV GAWGMRVEDI IVDCLTFPIA TGQEETRRDG IETIEAIRGL VAKYPGINTT LGVSNVSFGL NPAARSVLNS VFLHEATQAG LTSGIIDAAK IVPLASLPDE QRKVALDLVW DRREWDADGT LTYDPLATML DLFAGVDTAA LRDQRAAELA ALPVGERLER RIIDGELKGL EADLDLARAG DADAAPLSPL QIINDHLLEG MKVVGERFGS GQMQLPFVLQ SAEVMKTAVA LLEPNMEKTD EAGKGTIVLA TVRGDVHDIG KNLVDIILTN NGYTVINLGI KQPIADIIAA AEEHDADVIG MSGLLVKSTV VMKENLEELM ARGLGTRWPV ILGGAALTRA YVEQDLAELF DGEVRYAKDA FEGLALMEPL VRIARGEAPD AVGLPPLKKR IHAAGSRLTL TEPEAMPARS DVASDNPVPA PPFWGTRIVR GIALADYAAF LDERATFMGQ WGLKPGRGEG GLSYEQLVEA EGRPRLRYWL DRILAERMLD ASVAYGYFPV VSEGDDIVVL HHGDDPTGLL GRAGLLAPDG GSGGPLGADR LRFHFPRQRR DRHLNLADFV RSRASGQIDV LPVQLVTAGA AIDAVTAKMF AEDRYRDYYE LNGLVMQLTE ALAEFWHARI RAELGFAAED PADTAGLFTL DYRGARFSLG YPACPDMEDR RKVVELLRPE RMGVELSEEL QLHPEQSTDA FVFHHPEATY FSV // ID H8FDK3_XANCI Unreviewed; 379 AA. AC H8FDK3; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:CCG36440.1}; GN Name=metH {ECO:0000313|EMBL:CCG36440.1}; GN ORFNames=XMIN_1412 {ECO:0000313|EMBL:CCG36440.1}; OS Xanthomonas citri pv. mangiferaeindicae LMG 941. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=1156940 {ECO:0000313|EMBL:CCG36440.1}; RN [1] {ECO:0000313|EMBL:CCG36440.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 941 {ECO:0000313|EMBL:CCG36440.1}; 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] {ECO:0000313|EMBL:CCG36440.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 941 {ECO:0000313|EMBL:CCG36440.1}; RA Patil P.; 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. {ECO:0000313|EMBL:CCG36440.1}. 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; CAHO01000013; CCG36440.1; -; Genomic_DNA. DR RefSeq; WP_003484666.1; NZ_CAHO01000013.1. DR EnsemblBacteria; CCG36440; CCG36440; XMIN_1412. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:CCG36440.1}; KW Transferase {ECO:0000313|EMBL:CCG36440.1}. SQ SEQUENCE 379 AA; 40651 MW; F241FB2DBFEE7358 CRC64; MTHVRIPNPE SPIRFALPWL HPERAAKLTA ALAERILIID GAMGTMIQRH DLQEPDYRGT RFADGYDSAH VHGPGCDHAH VTQGHDLKGN NDLLLLTRPE IIAGIHRAYL EAGADLLETN TFNATSVSQA DYHLEHLVYE LNKAGAQVAR ACCDDVEALT PHKPRFVIGV LGPTSRTASI SPDVNDPGYR NTSFDALRAT YREAIEGLID GGADTLMVET IFDTLNAKAA LYAIEEVFDA RGGRLPVMVS GTITDASGRT LSGQTAEAFY ASVAHGRPLS IGLNCALGAR DLRPHVETLA QLADTYVSAH PNAGLPNAFG EYDETPEEMA QTLREFAQAG LLNLVGGCCG TSPDHIRAIA EAVADLPPRQ LPGAQELAA // ID H8FEM1_XANCI Unreviewed; 321 AA. AC H8FEM1; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 27-MAY-2015, entry version 9. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:CCG36808.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:CCG36808.1}; GN Name=mmuM {ECO:0000313|EMBL:CCG36808.1}; GN ORFNames=XMIN_1782 {ECO:0000313|EMBL:CCG36808.1}; OS Xanthomonas citri pv. mangiferaeindicae LMG 941. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=1156940 {ECO:0000313|EMBL:CCG36808.1}; RN [1] {ECO:0000313|EMBL:CCG36808.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 941 {ECO:0000313|EMBL:CCG36808.1}; 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] {ECO:0000313|EMBL:CCG36808.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 941 {ECO:0000313|EMBL:CCG36808.1}; RA Patil P.; 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. {ECO:0000313|EMBL:CCG36808.1}. 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; CAHO01000017; CCG36808.1; -; Genomic_DNA. DR RefSeq; WP_003485415.1; NZ_CAHO01000017.1. DR EnsemblBacteria; CCG36808; CCG36808; XMIN_1782. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:CCG36808.1}; KW Transferase {ECO:0000313|EMBL:CCG36808.1}. SQ SEQUENCE 321 AA; 34298 MW; 695495FC23F0A1A5 CRC64; MTILPRQPRA NAPFSQALQH DGYVVLDGAL ATELEQRGCD LNDALWSARV LMEQPELIYQ VHRDYFAAGA QCAITASYQA TPLGFAARGL DVAQAQALIA RSVALAMQAR ADHLTLHPHA APLWVAGSVG PYGAYLADGS EYRGDYVLPI EQLMDFHRPR IAALAEAGVD LLACETLPSA SEIVALRQLL QHEFPQLHAW FSFTLRDAAH LSDGTPLAQV VPALDACAQV IAVGINCIAL DQATAALHSL SALTALPLVV YPNSGEHYDA SDKRWHVSRG AALTLADQHA HWLAAGARLI GGCCRTAPRD IAALAVARAA E // ID H8FSY8_PHAMO Unreviewed; 1155 AA. AC H8FSY8; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:CCG41476.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CCG41476.1}; GN Name=metH {ECO:0000313|EMBL:CCG41476.1}; GN ORFNames=PHAMO_280010 {ECO:0000313|EMBL:CCG41476.1}; OS Phaeospirillum molischianum DSM 120. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Phaeospirillum. OX NCBI_TaxID=1150626 {ECO:0000313|EMBL:CCG41476.1}; RN [1] {ECO:0000313|EMBL:CCG41476.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 120 {ECO:0000313|EMBL:CCG41476.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:CCG41476.1}. 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; CAHP01000021; CCG41476.1; -; Genomic_DNA. DR RefSeq; WP_002728624.1; NZ_CAHP01000021.1. DR EnsemblBacteria; CCG41476; CCG41476; PHAMO_280010. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CCG41476.1}; KW Transferase {ECO:0000313|EMBL:CCG41476.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 287 287 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 727 727 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1155 AA; 125797 MW; D3DD5FD2FFE786BC CRC64; MSSILDHLSQ AVLLCDGGTG ALVQAMNLSV DKDFLGLENC TEILVESRPD VIRGIHARYF SAGADMVEAN TFGASPITLA EFGIADRAFD LNKRAIELAH EAAEQFADGR RRYVLGAIGP GTKLPSLGHI GYDPLEAAYL IQARGMIAGN VDAFLIETCQ DPLQIKAAVN GCKRALAETG GTAPIFVQVT VETTGTLLVG ADIAAAATVI QSLGVPLIGM NCAAGPQEMA EHFKWLVDNW PGFLSIQPNA GLPELIDGRT HYPLLPDELA VWHERFVGMG ANLVGGCCGT TPDHIGATDA MLRRIGAGSR PAPVKRLVHW VPSVASLYTQ VPLRQENAFL SIGERCNANG SKKFRDLQDA EDWDGITATA REQVKEGSHT LDVCTAFVGR DEIRDMTEVV SRLRGAVTTP LVIDSTELPV LEAGLKLYGG KAILNSINFE NGEEDAAARL KLARTFGSAV VALTIDEAGM AKDAESKLRI ARRLYDFAVN QHGLPASDLL FDPLTFTICT GVIDDRKLAI ETLDAIERIA AEMPDCGIIL GLSNVSFGLK PAARQVLNSV FIDLAIKRGM TGAIVHVSKI LPLHTLPTNE VQAAEDLILD RDPEALSRFI ALFGDRTVAE VKKERAATPE ERLKQRIIDG DRTGLDDDLL AAIEAGWQPL DIINQLLLDG MKVVGELFGS GKMQLPFVLQ SAETMKAAVA FLEPRMEKAD GQQKATIVLA TVKGDVHDIG KNLVDIILTN NGYRVVNLGI KQPVAEIIKA AREHKADAVG MSGLLVKSTV IMRENLEEMS REGLDLPVLL GGAALTRKYV EEACHEAYDS GRVAYARDAF DGLNLMAKVV ESTFDNHVKA RLDAPHRPGP ALPKSGEMLP ATRPVDWEAI TLRQTELHRD ITPATPPFWG ARVIESVPLQ NLIPFLNETT LYQFHWGYRK QGRTIDEFRA WAHKELRPVA LSMLKRCADE KILLPQAVYG YWKAASEGDN VVLFAEDGIT EVARFAFPRQ AKEGGLSIAD FFRPTSDPIR DVIGLQAVTV GRNASDTARQ WFEADKYQDY LYLHGLSVEI AEALAEYVHK RVRAELGFAA LDAAETDQLL KQGYRGSRFS FGYPACPNIE DQSMILSLLG AERIGISLSD EFQLEPEQST SAIVSLHPQA KYFVL // ID H8G7A0_9PSEU Unreviewed; 1182 AA. AC H8G7A0; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EHY88339.1}; GN ORFNames=SacazDRAFT_01409 {ECO:0000313|EMBL:EHY88339.1}; OS Saccharomonospora azurea NA-128. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Pseudonocardineae; Pseudonocardiaceae; Saccharomonospora. OX NCBI_TaxID=882081 {ECO:0000313|EMBL:EHY88339.1, ECO:0000313|Proteomes:UP000004705}; RN [1] {ECO:0000313|EMBL:EHY88339.1, ECO:0000313|Proteomes:UP000004705} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NA-128 {ECO:0000313|EMBL:EHY88339.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CM001466; EHY88339.1; -; Genomic_DNA. DR RefSeq; WP_005439979.1; NZ_CM001466.1. DR EnsemblBacteria; EHY88339; EHY88339; SacazDRAFT_01409. DR Proteomes; UP000004705; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000004705}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EHY88339.1}; KW Transferase {ECO:0000313|EMBL:EHY88339.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 223 223 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 733 733 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1182 AA; 130168 MW; 849D0F58EB9E963B CRC64; MDSRFLVELD RRILVADGGM GTALQEFDLS LDDFDNLEGC NEVLNDTRPD VVSTVHRGFL EAGCDAIETN TFGTNYGNFG EYGILDRIRE LAEKGTTLAR RCADEYATPE KPRFVLGSMG PGTKLPTLGH APYHVLRDAY VENALGMLDG GVDAVLVETS QDLLQTKAAI VGAKRAMAQA GRRVPLIAQV TVEQTGTMLV GSEIGAALTA LEPLGIDLIG MNCATGPAEM SEHLRVLADH ASVPISVMPN AGLPELGPKG AVYPLRPDEL AEALATFVRD FGVRLVGGCC GTTAEHVRAV VEAVSSLPPR QREPRIQPAL SSVYQPVPFE QDASILNVGE RTNANGSKKF REAMLEERYD DCVEIAKAQT REGAHVLDLC VDYVGRDGTR DMAELASRLA TASTLPVMVD STEPDVVRTG LEHLGGRCAI NSVNYEDGTG PDSRYQRVLE LAVEHGAAVV VTCIDEEGQA RTADWKVRVA ERAIEDLTTN WGLSLSSIII DCLVFPITTG QEEVRKDALE TIEAIRRLKQ RHPGVLTTLG LSNVSFGLNP AARQVLNSVF LHECRQAGLD SAILNSSKIV PMNKIDDEAR EVALDLVYDR RREGYDPLQR LMQLFEGKTA SSARESRAEE LAKLPLLERL EKRIVEGEST GLEADLEAAM QQKKPIDIIN ENLLAGMKTV GDLFGSGQMQ LPFVLQSAEV MKTAVAYLEP HMEKTDTDGK GKLLLATVKG DVHDIGKNLV DIIVSNNGYD VVNIGIKQPI NAILEAAEEN RVDAIGMSGL LVKSTVIMKD NLQEMNARGV ATKYPVLLGG AALTRTYVEN DLDEVYQGDV HYAKDAFEGL RLMDRVMAVK RGEATEEDEA ERAKRAERKA RRERSLRIAE KRKAEQGTEP SLDDTTRSDV DLDVDVPTPP FWGSRVVKGI AVADYLALLD ERATFLGQWG LRGARKGEGP SYEELVESEG RPRLRAWIDD LSTRGVLAHA ALVYGYFPCY SDGNDLVVLE KDEPDALERL RFRFPRQRRD RRLCLADFFR SRQKAEETGQ VDVLPVQLVT MGQPIADHAN ELFARNAYRD YLEIHGLGVQ LTEALAEYWH RRIREELRFS SGTPVAAEDP DDVEEYFKLG YRGARFSFGY GACPDLEDRA KIVELLDAER IGVALSEEFQ LHPEQSTDAI VAHHPEAKYF NT // ID H8G861_9PSEU Unreviewed; 300 AA. AC H8G861; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine/selenocysteine methylase (S-methylmethionine-dependent) {ECO:0000313|EMBL:EHY89413.1}; GN ORFNames=SacazDRAFT_02516 {ECO:0000313|EMBL:EHY89413.1}; OS Saccharomonospora azurea NA-128. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Pseudonocardineae; Pseudonocardiaceae; Saccharomonospora. OX NCBI_TaxID=882081 {ECO:0000313|EMBL:EHY89413.1, ECO:0000313|Proteomes:UP000004705}; RN [1] {ECO:0000313|EMBL:EHY89413.1, ECO:0000313|Proteomes:UP000004705} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NA-128 {ECO:0000313|EMBL:EHY89413.1}; 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 ----------------------------------------------------------------------- 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; EHY89413.1; -; Genomic_DNA. DR RefSeq; WP_005442014.1; NZ_CM001466.1. DR EnsemblBacteria; EHY89413; EHY89413; SacazDRAFT_02516. DR Proteomes; UP000004705; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000004705}; KW Methyltransferase {ECO:0000313|EMBL:EHY89413.1}; KW Transferase {ECO:0000313|EMBL:EHY89413.1}. SQ SEQUENCE 300 AA; 31554 MW; 09E85EFBA792064F CRC64; MLRLEGVELF GAGAWVNDGG LATELEARGH DLSDALWSAR LLLDAPEEIV AAHRAFFDAG AVIATTASYQ ASFEGFAERG IDRATATRLL RRSVDLARQA RDDVSGDGRP RFVAASVGPY GAALADGSEY RGAYGLTVAR LRDWHRPRLE VLAEARPDLL AIETVPDVVE AEALVEALAG IGVPAWLSFT VADGRTRAGQ PLAEAFAVAA GSPDVAAVGV NCCAPSDVSP ALACAKAVTG KPVVVYPNSG EGWDARRRAW TGATQFSPRL AARWVAEGAH VVGGCCRVRP ADIAELARRL // ID H8GNL7_METAL Unreviewed; 1224 AA. AC H8GNL7; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EIC29610.1}; GN ORFNames=Metal_1844 {ECO:0000313|EMBL:EIC29610.1}; OS Methylomicrobium album BG8. OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales; OC Methylococcaceae; Methylomicrobium. OX NCBI_TaxID=686340 {ECO:0000313|EMBL:EIC29610.1, ECO:0000313|Proteomes:UP000005090}; RN [1] {ECO:0000313|EMBL:EIC29610.1, ECO:0000313|Proteomes:UP000005090} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BG8 {ECO:0000313|EMBL:EIC29610.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CM001475; EIC29610.1; -; Genomic_DNA. DR RefSeq; WP_005371599.1; NZ_CM001475.1. DR EnsemblBacteria; EIC29610; EIC29610; Metal_1844. DR Proteomes; UP000005090; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000005090}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EIC29610.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005090}; KW Transferase {ECO:0000313|EMBL:EIC29610.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 246 246 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1224 AA; 135008 MW; 02E247209BCFF224 CRC64; MDKTPDLKQL LSQKILFLDG AMGTMIQSYK LEEKDYRGAR FADWDIDLKG NNDLLSLTQP AIIKAIHCAY LEAGADIIET NTFNSTRVAM ADYRMEALVY EINVESARLA RQACDDYTQL TPDKPRFVAG VLGPTNRTAS MSPDVNDPGF RNISFDELVE AYTEATRGLI DGGADIILIE TVFDTLNAKA AAFAVDAYFE RIGHKLPVMI SGTITDASGR TLSGQTVAAF WHSLKHIEPI SFGFNCALGA KELRQHIDEL STIADTHVSA HPNAGLPNEF GEYDESPEMM AQEIADWAKQ GFLNIIGGCC GTTPAHIKAI VEAVSPYPPR AIPDIPKACR LSGLEATAIG PDSLFVNVGE RTNVTGSAVF KRLIVAGDYE AALDVARQQV ENGAQVIDIN MDEGMLESKE AMVRFLMLLA AEPDIAKVPI MLDSSKWEIL EAGLKCIQGK GIVNSISLKE GEAKFIEHAK LVRRYGAAVI VMAFDEVGQA DTQARKVEIC TRAYRILTEQ LGFPPEDIIF DPNIFAIATG IEEHNNYGLD FIEATHEIKA TLPHALISGG VSNVSFSFRG NNPVREAIHA VFLYHAIQAG MDMGIVNAGQ LAIYEDIPAE LREAVEDVVL NRHPHATEKL LEIAERYRGD GSSGAVKPEE LEWRSWPVNK RLEHALVKGI ADFIDEDTEA ARLQADKPLH VIEGPLMDGM NVVGDLFGAG KMFLPQVVKS ARVMKKAVAY LMPFMEDDQA EERQSNGKIL MATVKGDVHD IGKNIVGVVL QCNNYEVIDL GVMVPAETIL QTARKEKVDI IGLSGLITPS LDEMVHLAKE MQRQGFTIPL LIGGATTSRA HTAVKIEPNY EGATVYVPDA SRGVGVAGSL LSADLKAGYT EAVRAEYREV RERHKGKEAK TQQHPIEAAR RNRAAWNGHI PIKPSFLGIR AIDRFPLETL VWYIDWSPFF QTWELAGRYP KILDDSVVGL EARKLFDDAQ VMLHKIINEA WLTARAVIGF FPANSDGDDV IVYADESRAK VRAVLHHLRQ QNVKAPGRPN YCLSDFIAPK EQGIADYIGA FAVTAGVGIE AKLAEFERDH DDYSAIMLKA LADRLAEALA EYMHQAVRTD YWGYAKDEKL SNEQLIEEAY RGIRPAPGYP ACPDHTEKAR LFELLNVTES TGITLTESYA MYPAAAVSGW YFAHPEAQYF NVGKINRDQL QDYAKRKGIA EEVAERWLSA HLNH // ID H8GYK6_DEIGI Unreviewed; 1194 AA. AC H8GYK6; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AFD26053.1}; GN Name=metH {ECO:0000313|EMBL:AFD26053.1}; GN OrderedLocusNames=DGo_CA2126 {ECO:0000313|EMBL:AFD26053.1}; OS Deinococcus gobiensis (strain DSM 21396 / JCM 16679 / CGMCC 1.7299 / OS I-0). OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; OC Deinococcaceae; Deinococcus. OX NCBI_TaxID=745776 {ECO:0000313|EMBL:AFD26053.1, ECO:0000313|Proteomes:UP000007575}; RN [1] {ECO:0000313|EMBL:AFD26053.1, ECO:0000313|Proteomes:UP000007575} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 21396 / JCM 16679 / CGMCC 1.7299 / I-0 RC {ECO:0000313|Proteomes:UP000007575}; RX PubMed=22470573; DOI=10.1371/journal.pone.0034458; RA Yuan M., Chen M., Zhang W., Lu W., Wang J., Yang M., Zhao P., Tang R., RA Li X., Hao Y., Zhou Z., Zhan Y., Yu H., Teng C., Yan Y., Ping S., RA Wang Y., Lin M.; RT "Genome sequence and transcriptome analysis of the radioresistant RT bacterium Deinococcus gobiensis: insights into the extreme RT environmental adaptations."; RL PLoS ONE 7:E34458-E34458(2012). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002191; AFD26053.1; -; Genomic_DNA. DR RefSeq; WP_014685536.1; NC_017790.1. DR RefSeq; YP_006261511.1; NC_017790.1. DR EnsemblBacteria; AFD26053; AFD26053; DGo_CA2126. DR KEGG; dgo:DGo_CA2126; -. DR KO; K00548; -. DR BioCyc; DGOB745776:GLCE-2184-MONOMER; -. DR Proteomes; UP000007575; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007575}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AFD26053.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007575}; KW Transferase {ECO:0000313|EMBL:AFD26053.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 199 199 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 262 262 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 263 263 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 708 708 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1194 AA; 129654 MW; ED5111FA10D0E2D1 CRC64; MYRGNFDLLQ LTRPDVIRQV HRDYFAAGAD IASTNTFNST TISQADYGTE ALAFAMNEAG ARLAREVADE FTARDGKPRW VAGSVGPTNR TATLSPDVER PEFRNVTYDD LVEAYTSAVR GLMAGGADLI LLETVFDTLN AKAALFACDE AFAAEGRRLP VMLSGTITDA SGRTLSGQTP EAFAVSTEHA HLFSLGLNCA LGADLLRPHL RAIAANTGAL VSVHPNAGLP NAFGEYDETP EHTASVLADF AREGLVNIVG GCCGTTPEHI RAIADAMSAL PPRTAPERTP YLRLSGLEAF TLTPETNFVN VGERTNVTGS PKFAQAILAG DYDAGLKIAR QQVTNGAQVV DINFDEGMLD GEAAMVKFLN LLAGEPDISR VPLMLDSSKW EILEAGLKRV QGKAIVNSIS LKDGEEKFLE RARRLRRYGA AAVVMAFDER GQADNLQRRQ EITARAYKLL TEQADFPPQD IIFDPNVLTV ATGIEEHDRY ALDFIEATRW IKANLPGALV SGGISNVSFS FRGNNHVREA MHAVFLYHAI RAGLDMGIVN AGMLAVYADI EPELRDAVED VILARRPDAT ERLLTLADQY KGIKREAAAQ SAWREQPVAQ RLTHALVQGI TDHVEADAEE AYRELGSPLA VIEGPLMDGM NVVGDLFGAG QMFLPQVVKS ARVMKRAVAY LTPYMEAEQQ ESGGKGKVLL ATVKGDVHDI GKNIVGVVLA CNGYQVTDLG VMVPTEKVLD EAQRIGADVI GLSGLITPSL DEMVGVAREM TRRGMTQPLL IGGATTSRAH TAVKIDPAYE GTVVHVLDAS RAVTTTSDLL ADEAGYRERI RGEYDALRER HGGRQVRLIS IAEARERAPQ LAAPTPPAPR QPGRQVIEQP IAGLLDYIDW TPFFIAWEMK GIYPNILTDP LRGEEARKLF ADAQALLRRV VDEGLMQARG VIGLWPAHRE GDDIVLEPLA QAETLDHRTH EIAAGRERLP HRTRLHTLRQ QREQGTPNVA LADYVAEGAD HIGAFAVAIH GAEELARAFE AAHDDYNSIL VKAVADRLAE AFAEKLHRDV RRNHWGYAPD ETLDNADLIR ERYDGIRPAP GYPAQPDHTE KRTLFALLDA GEVGLSLTDS CAMLPAAAVS GLYFAHPEAR YFAVGRIGKD QVEDYAARKG WALEEAERWL GPLLAYDPAA APPPAEVSVS GGAA // ID H8IQA2_MYCIA Unreviewed; 314 AA. AC H8IQA2; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 01-APR-2015, entry version 16. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:AFC43014.1}; GN OrderedLocusNames=OCU_17950 {ECO:0000313|EMBL:AFC43014.1}; 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 {ECO:0000313|EMBL:AFC43014.1, ECO:0000313|Proteomes:UP000008004}; RN [1] {ECO:0000313|EMBL:AFC43014.1, ECO:0000313|Proteomes:UP000008004} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13950 / DSM 43223 / JCM 6384 / NCTC 13025 / 3600 RC {ECO:0000313|Proteomes:UP000008004}; 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 ----------------------------------------------------------------------- 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; AFC43014.1; -; Genomic_DNA. DR RefSeq; WP_014379673.1; NC_016946.1. DR RefSeq; YP_005337335.1; NC_016946.1. DR EnsemblBacteria; AFC43014; AFC43014; OCU_17950. DR KEGG; mia:OCU_17950; -. DR KO; K00547; -. DR BioCyc; MINT487521:GLGN-1824-MONOMER; -. DR Proteomes; UP000008004; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008004}; KW Methyltransferase {ECO:0000313|EMBL:AFC43014.1}; KW Transferase {ECO:0000313|EMBL:AFC43014.1}. SQ SEQUENCE 314 AA; 32627 MW; F09C879F90B1B92F CRC64; MGLAVGLRWP SGTVVLDGGL ATELEARGHD LSDRLWSARL LADAPREIVA VHAAYFRAGA TIATTASYQA SFEGFAARGL DRRETDLLLR RSVELAKAAR DEAGAAGLLV AASVGPYGAA LADGSEYRGR YGLSVGALAR WHRPRLETLA DAGADVLACE TVPDVDEAEA LVDVVRSVGM PAWLSYTIDG ARTRAGQPLT EAFAVAAGVD EIVAVGVNCC APDDVLPAIA SASEIGKPVI VYPNSGERWD GRAWVGPRTF ATGLAAQWVS AGARIVGGCC RVGPVDIAEL APLRRACNQG EKSALGSRGD CNTS // ID H8IWR2_MYCIA Unreviewed; 1264 AA. AC H8IWR2; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:AFC43588.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AFC43588.1}; GN OrderedLocusNames=OCU_23690 {ECO:0000313|EMBL:AFC43588.1}; 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 {ECO:0000313|EMBL:AFC43588.1, ECO:0000313|Proteomes:UP000008004}; RN [1] {ECO:0000313|EMBL:AFC43588.1, ECO:0000313|Proteomes:UP000008004} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13950 / DSM 43223 / JCM 6384 / NCTC 13025 / 3600 RC {ECO:0000313|Proteomes:UP000008004}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP003322; AFC43588.1; -; Genomic_DNA. DR RefSeq; WP_014380026.1; NC_016946.1. DR RefSeq; YP_005337909.1; NC_016946.1. DR EnsemblBacteria; AFC43588; AFC43588; OCU_23690. DR GeneID; 11909109; -. DR KEGG; mia:OCU_23690; -. DR KO; K00548; -. DR BioCyc; MINT487521:GLGN-2402-MONOMER; -. DR Proteomes; UP000008004; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008004}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AFC43588.1}; KW Transferase {ECO:0000313|EMBL:AFC43588.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 270 270 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 333 333 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 334 334 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 790 790 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1264 AA; 138701 MW; B04755EB216C7A40 CRC64; MHMTAVETKT SATNTSASDA FAPNIRPDCT DELTAALRQR IMVIDGAMGT AIQRDRPDEA GYRGDRFTEW PTALQGNNDL LNLTQPQIIE GIHREYLEAG ADILETNTFN ANAISLSDYD MADLAYELNY AGAALARKAA DEYSTPEKPR YVAGAIGPTT RTASISPDVN DPGARNVSYD QLVAAYLEAA NGLVDGGADL LIIETIFDSL NAKAAVFAVE TLFEDRGRRW PVIISGTITD ASGRTLSGQV TEAFWNAIRH AKPIAVGLNC ALGAPEMRPY IAEMSRIADT FVSCYPNAGL PNAFGEYDET PERQAGYIAD FAEAGLVNLV GGCCGTAPPH IAEIAKVVEG NPPREVPKIE VATRLSGLEP LNITDDSLFV NIGERTNITG SARFRNLIKA EDYDTALSVA LQQVEVGAQV IDINMDEGMI DGVAAMDRFT KLIAAEPDIS RVPVMIDSSK WEVIEAGLKN VQGKPIVNSI SMKEGEEKFI REARLCRKYG AAVVVMAFDE QGQADNLERR KEICGRAYRI LTEEVGFPPE DIIFDPNCFA LATGIEEHAT YGIDFIEACA WIKENLPGVH ISGGISNVSF SFRGNNPVRE AIHAVFLFHA IKAGLDMGIV NAGALVPYDS IDPELRDRIE DVVLNRREDA AERLLEIAER FNKSEKSEDP AAAEWRSLPV RERITHALVK GIDAHVDDDT EELRAEIAAA GGRPIEVIEG PLMDGMNVVG DLFGSGKMFL PQVVKSARVM KKAVAYLLPF IEKEKEQNGT AAAKDTNGTI VMATVKGDVH DIGKNIVGVV LQCNNFEVID LGVMVPAEKI LAAAREHDAD IIGLSGLITP SLDEMSNFAV EMEREGLEIP LLIGGATTSR AHTAVKISPR RSGPVVWVKD ASRSVPVAAA LLDDKQRPGL LEATEKDYAS LRERHAQKNE RPMLTLEKAR ANRTPIEWDG YTPPVPAQGL GVREFKEYDL AELREYIDWQ PFFNAWEMKG RFPDILNNPA TGEAARKLYD DAQEMLDTLI KEKWLTANAV IGFFPANAVG SGIEDIEVYT DDTRTEVLTT LHHLRQQGEH REGIPNRSLS DYIAPKDTGL ADYIGAFAVT AGLGSGEKIA EFKAALDDYS AILLESLADR LAEAFAERMH QRVRKEFWGF KPDEHLDNDA LIAEKYQGIR PAPGYPACPE HTEKATLWKL MDVHERTGIE LTESMAMWPG AAVSGWYFSH PQSQYFVVGR MAQDQVADYA RRKGWTLKEG ERWLSSNLAY NPED // ID H8KWP1_SOLCM Unreviewed; 1231 AA. AC H8KWP1; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 29-APR-2015, entry version 23. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AFD08220.1}; GN OrderedLocusNames=Solca_3209 {ECO:0000313|EMBL:AFD08220.1}; 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 {ECO:0000313|EMBL:AFD08220.1, ECO:0000313|Proteomes:UP000007590}; RN [1] {ECO:0000313|Proteomes:UP000007590} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29591 / DSM 3403 / NBRC 15130 / NCIMB 12057 / USAM 9D RC {ECO:0000313|Proteomes:UP000007590}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP003349; AFD08220.1; -; Genomic_DNA. DR RefSeq; WP_014681444.1; NC_017770.1. DR RefSeq; YP_006257396.1; NC_017770.1. DR EnsemblBacteria; AFD08220; AFD08220; Solca_3209. DR KEGG; scn:Solca_3209; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; SCAN929556:GLKC-3209-MONOMER; -. DR Proteomes; UP000007590; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007590}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AFD08220.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007590}; KW Transferase {ECO:0000313|EMBL:AFD08220.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 242 242 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 764 764 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1231 AA; 137095 MW; 23A19F0F6BCBB348 CRC64; MDIRNILTKR ILVLDGAMGT MIQRYKLQED DFRGKRFKDH PTDLKGNNDL LSITRPDVIK AIHREYLEAG ADIIETNTFS GTTIAMADYQ MEHLAYELNY ESAKIAKEVT AEFNAKYPEK PRFVAGAIGP TNRTASLSPD VNDPGFRAIT FDQLVEAYTE QVHGLVSGGA DIILVETIFD TLNAKAALFA IDQYFEVNKI KLPIMVSGTI TDASGRTLSG QTAEAFLISL SNFDLLSIGF NCALGAKDMR PYLEEISEKA PFFVGAYPNA GLPNQFGEYD ETPDQMLDQI RDFLKSGFIN IVGGCCGTTP DHIRAIADEV AKYAPRKKAE PQPFLRLSGL EPIVITPETN FVNVGERTNI TGSPKFSKLI LSGDYEGALA VARQQVEGGA QVIDVNMDEG MLDSEAAMVK FLNLIASEPD IAKLPIMIDS SKWSVIEAGL KCLQGKGIVN SISLKEGEEK FKEHARKIKR YGAATVVMAF DEKGQADTYE RRIEICERSY KLLVNEIGFA PQDIIFDPNI LTVATGLDEH NNYAVDFIET ARWIKQNLPL AKVSGGVSNI SFSFRGNNTV REAMHSAFLY HAIKAGLDMG IVNAGMLEVY EEIPKDLLVL VEDVLLNRKP DATEHLVAFA ETVKAKGKTI VKDEEWRKEG VEKRLSHSLV KGIIEYLEED VEEARQKYDR PLQVIEGPLM DGMNVVGDLF GSGKMFLPQV VKSARVMKKA VAYLLPFIEA EKEKLAHADP SSVIEGGREG AGKILLATVK GDVHDIGKNI VGVVLACNNY QIIDLGVMVS CQQILETARK ENVDIIGLSG LITPSLDEMV HVAKEMEREG FNIPLLIGGA TTSRVHTAVK ISPNYNGPVV HVLDASRSVP VAGNLLNDQK DNFMAGITKE YDQLRDFHLN KKSTKTFVSI EEARNRRLKL NWESYQPVKP SFTGAKVLDN YDLAELAEYI DWTPFFHTWE LYGSYPKIFN DEVVGTEAKK LFADAQVLLK RIVDEKLLTA RAVIGFWPAN SVGHDDIELY TDDSRSEKLT TIHTLRQQLE KAQNIPYFAL ADFIAPKETG ITDYWGGFAV TTGIGLDKLV EEFESQHDDY NSIMAKALAD RLAEAFAERM HERVRKEYWG YVADEHFSNE ELIEERYKGI RPAPGYPACP DHTEKTTLFE ILDAEANTGI FLTESLAMYP TAAVSGFYFS HPESKYFGLG KIQKDQVEDY ATRKKMTVAE VERWMAPNLA Y // ID H8L0W3_FRAAD Unreviewed; 358 AA. AC H8L0W3; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Cobalamin-dependent methionine synthase I {ECO:0000313|EMBL:AFC86283.1}; GN OrderedLocusNames=Fraau_1890 {ECO:0000313|EMBL:AFC86283.1}; 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 {ECO:0000313|EMBL:AFC86283.1, ECO:0000313|Proteomes:UP000005234}; RN [1] {ECO:0000313|Proteomes:UP000005234} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33424 / DSM 6220 / NBRC 3245 / NCIMB 13370 RC {ECO:0000313|Proteomes:UP000005234}; 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; AFC86283.1; -; Genomic_DNA. DR RefSeq; WP_014403288.1; NC_017033.1. DR RefSeq; YP_005377965.1; NC_017033.1. DR EnsemblBacteria; AFC86283; AFC86283; Fraau_1890. DR KEGG; fau:Fraau_1890; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR BioCyc; FAUR767434:GLDK-1890-MONOMER; -. DR Proteomes; UP000005234; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005234}; KW Reference proteome {ECO:0000313|Proteomes:UP000005234}. SQ SEQUENCE 358 AA; 38285 MW; 18703F6A35CC91B1 CRC64; MPALPWLHPA RVDRLQHALA HRILILDGGM GTMLQGHQLD EDGYRGERFS AGHDSCGGPG HDHACDLKGN NDLLSLTQPD IIRGIHEAYL EAGADLVETN TFNATRISQA DYHLEHLVPE LNRRGAELAR QACDSWTART PDKPRFVIGV LGPTSRTASI SPDVNDPGFR NVTYQELVDN YTEATLALIE GGADLIMVET IFDTLNAKAA LFALEESFRQ VGGRLPVMIS GTITDRSGRT LSGQTAEAFY YSVSHIAPLS VGLNCALGAE DLRPHVQTLA RVADCLISSH PNAGLPNAFG EYDETPEHMA GVIGGFARDG LLNLVGGCCG TTPAHIRAIA EAVAAFPPRR PAAADTAA // ID H8MHE8_CORCM Unreviewed; 326 AA. AC H8MHE8; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Homocysteine S-methyltransferase domain-containing protein {ECO:0000313|EMBL:AFE09444.1}; GN Name=mmuM {ECO:0000313|EMBL:AFE09444.1}; GN OrderedLocusNames=COCOR_00727 {ECO:0000313|EMBL:AFE09444.1}; 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 {ECO:0000313|EMBL:AFE09444.1, ECO:0000313|Proteomes:UP000007587}; RN [1] {ECO:0000313|Proteomes:UP000007587} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25202 / DSM 2259 / NBRC 100086 / M2 RC {ECO:0000313|Proteomes:UP000007587}; 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; AFE09444.1; -; Genomic_DNA. DR RefSeq; WP_014393578.1; NC_017030.1. DR RefSeq; YP_005366733.1; NC_017030.1. DR EnsemblBacteria; AFE09444; AFE09444; COCOR_00727. DR KEGG; ccx:COCOR_00727; -. DR BioCyc; CCOR1144275:GLBO-729-MONOMER; -. DR Proteomes; UP000007587; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007587}; KW Methyltransferase {ECO:0000313|EMBL:AFE09444.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007587}; KW Transferase {ECO:0000313|EMBL:AFE09444.1}. SQ SEQUENCE 326 AA; 34317 MW; EBD34CAB043BEC6A CRC64; MSGLANHASF LRALHEAPRV LTEGSVVERL RRHPAGLLDP HVANAGLLFN PEGREALAGI YRDYRDIGLR HGLPTLLLTP TWRANAERLA RAGLAGRDVF GEAVGLLAGL RDEVGGRGEG VFIGGLVGCR GDAYRPEEAL PREEAAAFHA PHVEALARAG VDFLVAQALP ALSEAEGLAL AMAGTRAPFL LSFILRPTGT LLDGTPLAEA VARIDALPGA RPAAYMVNCV HPSIFREGLS RQLAASPALG ARVVGLQANT SRLSPEELEG RAELDSETPD AFAREMARVH AECGTRLLGG CCGTDERHIA ALASALTEGA PGERRP // ID H8MHK1_CORCM Unreviewed; 1171 AA. AC H8MHK1; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 29-APR-2015, entry version 22. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AFE09399.1}; GN Name=metH {ECO:0000313|EMBL:AFE09399.1}; GN OrderedLocusNames=COCOR_01995 {ECO:0000313|EMBL:AFE09399.1}; 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 {ECO:0000313|EMBL:AFE09399.1, ECO:0000313|Proteomes:UP000007587}; RN [1] {ECO:0000313|Proteomes:UP000007587} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25202 / DSM 2259 / NBRC 100086 / M2 RC {ECO:0000313|Proteomes:UP000007587}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP003389; AFE09399.1; -; Genomic_DNA. DR RefSeq; WP_014394834.1; NC_017030.1. DR RefSeq; YP_005367992.1; NC_017030.1. DR EnsemblBacteria; AFE09399; AFE09399; COCOR_01995. DR KEGG; ccx:COCOR_01995; -. DR KO; K00548; -. DR BioCyc; CCOR1144275:GLBO-1997-MONOMER; -. DR Proteomes; UP000007587; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007587}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AFE09399.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007587}; KW Transferase {ECO:0000313|EMBL:AFE09399.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 739 739 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1171 AA; 127132 MW; BC68B51994F0020C CRC64; MTSHIAHPLP LPPGEHGQRV EALKAAMRER ILVLDGAMGT LLQGHQLVAA DFGGAEYEGC NEHLVLTRPD VIEGIHAKYF AAGADVTETD SFGGTPVVLA EFELGHKAME INIAASRLAL NAAKAAEAKD GRMRWVAGSI GPTTKAISVT GGITFEELVD NFAVQAEGLA VGGSDYLLVE TAQDTRNVKA ALLGIDRAFK KLGWKLPVAV SGTIEPMGTM LAGQSVESLA TSLEHTDLLY LGLNCATGPD FMTDHIRSLS SMSPFPVSCV PNAGLPDENG QYLESPEMIS RSLRRFCDNG WINVVGGCCG THAGHIEALA AMVKGLKPRT ETPKPRSSLS GVDYLEVTDE QRPIIVGERT NVIGSKKFKE LIVAGAFDDA SEIARAQVRR AAQVIDICLA NPDRDELEDM RHFLEVVVKK VRVPLMIDST DEKVIAMALT YCQGKAIINS VNLEDGEERF EKVVPLAKAF GAALVVGCID EVGMAVTRDR KLAVAERSYD LLTQKYGMRP EDLYFDPLVF PCASGDAQYT GSGVETIEGV RLIKQRFPQC RTVLGISNVS FGLPTAGREV LNSVFLYHCV QAGLDMALVN SEKLERYPSL PEEERKLSED LIYNRGQDPV TPFAAHFRER KPARAQVSSL PLNERLQRYI IEGTRDGLTA DLDLAMKEMS PLDIINGPLM KGMDEVGRLF GANELIVAEV LQSAESMKAA VSHLEPHMSQ TQTASRGKIV LATVKGDVHD IGKNLVEIIL ANNGFQVVNL GIKVPPEQLV LAVKEHRPDI LGLSGLLVKS AHQMVATAED LKRAGVETPI LVGGAALSRN FVDRNIAPAY GGGTVAYAQD AMNGLELAKQ IVEPGAHAKL RDDLAARRLK LAQEAKDRPA PAAPVRRSRS TEVPVLTTVP PAPDFARHVL TNTPLDHIWK FINPVMLYGR HLGLRTSSRA LGTPAEADLA KTEEGRKALA LKEAVEELKT LLRGGVMHAR SVFQFFKAAS DGDRVLLFDG TTGEPVTSFD FPRQDKDNGL CLADYVRPLE NGKPVDALSL FVTTAGAGIR ELSEGFKAKG EFLKMHAVQA LALETAEGYA ELLHTQLRSM WGFPDRADMT MLERFRAEYT GKRYSFGYPA CPRLEDQTKL FAALKPEEIG VQLTDGCMME PEASVSAIVF HHPNATYFSV T // ID H8NQR2_RAHAQ Unreviewed; 1227 AA. AC H8NQR2; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:AFE60387.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AFE60387.1}; GN Name=metH {ECO:0000313|EMBL:AFE60387.1}; GN ORFNames=Q7S_20890 {ECO:0000313|EMBL:AFE60387.1}; OS Rahnella aquatilis HX2. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Rahnella. OX NCBI_TaxID=1151116 {ECO:0000313|EMBL:AFE60387.1, ECO:0000313|Proteomes:UP000007594}; RN [1] {ECO:0000313|EMBL:AFE60387.1, ECO:0000313|Proteomes:UP000007594} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HX2 {ECO:0000313|EMBL:AFE60387.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP003403; AFE60387.1; -; Genomic_DNA. DR RefSeq; WP_015690561.1; NC_017047.1. DR RefSeq; YP_005403954.1; NC_017047.1. DR EnsemblBacteria; AFE60387; AFE60387; Q7S_20890. DR KEGG; raa:Q7S_20890; -. DR KO; K00548; -. DR BioCyc; RAQU1151116:GLJ4-4186-MONOMER; -. DR Proteomes; UP000007594; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007594}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AFE60387.1}; KW Transferase {ECO:0000313|EMBL:AFE60387.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136151 MW; 85F68560E0B0D7C2 CRC64; MTNRVEALHK QLAQRILVLD GGMGTMIQSY RLEEEDYRGE RFADWESDLK GNNDLLVLSK PDVIVEIHNG YLAAGADILE TNTFNSTTIA MADYHMESLS AEINYEAARL ARQCADAWTA RTPDKPRYVA GVLGPTNRTA SISPDVNDPA FRNVSFDQLV EAYRESTRAL IEGGADLIMI ETVFDTLNAK AATFAVESEF EAMGIVLPVM VSGTITDASG RTLSGQTTEA FYNSLRHVKP LTFGLNCALG PDELRQYVAE LSRIAECYVT AHPNAGLPNA FGEYDLEAKE MAEHIAEWAR SGFLNIVGGC CGTTPAHIAA MVKAVEGVPP RALPTIPVAC RLAGLEPLTI DPQTLFVNVG ERTNVTGSAR FKRLIKEEKY AEALAVARQQ VESGAQIIDI NMDEGMLDAE AAMVRFLSLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGEEAFLHHA RMVRRYGAAV VVMAFDETGQ ADTRARKIEI CRRAYKLLTE KVGFPPEDII FDPNIFAVAT GIDEHNNYAV DFIEACADIK AQLPHALISG GVSNVSFSFR GNEPVREAIH AVFLYHAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKDDGEANKQ QAEWRSWDVK KRLEYSLVKG ITEFIELDTE ECRQLAARPI EVIEGPLMDG MNVVGDLFGA GKMFLPQVVK SARVMKQAVA YLEPYIEASK EKGQTNGKIL LATVKGDVHD IGKNIVGVVL QCNNYEIIDL GVMVPTDKIL KTAIEENVDI IGLSGLITPS LDEMVNVAKE MERRGFTMPL LIGGATTSKA HTAVKIEKNY SGVTCYVQNA SRSVGVVSAL LSKDQRDAFI ERTRKEYDTV RIQHGRKKPR TPPVSLEVAR DNATFIDWEA YTPPVVHRLG IQKVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG EEAKRLFKDA NDLLDKLCAE KLLNPRGVVG LFPANRKGDD IEIYSDERRE DVLVVSHHLR QQTEKTDFAN YCLADFVAPK SSGKKDYMGA FAVTGGLEED ALAEAYDKQH DDYNKIMIKA LADRLAEAFA EYLHEKVRKV YWGFAANENL SNEELIRENY QGIRPAPGYP ACPEHTEKGQ IWKLLDVEAN TGMQLTESFA MWPGAAVSGW YFSHPDSKYF AVAQIQRDQV EDYAARKNMP VAEVERWLAP NLGYDAD // ID H8P0C2_RAHAQ Unreviewed; 300 AA. AC H8P0C2; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AFE61124.1}; GN ORFNames=Q7S_24871 {ECO:0000313|EMBL:AFE61124.1}; OS Rahnella aquatilis HX2. OG Plasmid PRA1 {ECO:0000313|EMBL:AFE61124.1, OG ECO:0000313|Proteomes:UP000007594}. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Rahnella. OX NCBI_TaxID=1151116 {ECO:0000313|EMBL:AFE61124.1, ECO:0000313|Proteomes:UP000007594}; RN [1] {ECO:0000313|EMBL:AFE61124.1, ECO:0000313|Proteomes:UP000007594} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HX2 {ECO:0000313|EMBL:AFE61124.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003404; AFE61124.1; -; Genomic_DNA. DR RefSeq; WP_014416664.1; NC_017060.1. DR RefSeq; YP_005419228.1; NC_017060.1. DR EnsemblBacteria; AFE61124; AFE61124; Q7S_24871. DR KEGG; raa:Q7S_24871; -. DR BioCyc; RAQU1151116:GLJ4-4950-MONOMER; -. DR Proteomes; UP000007594; Plasmid PRA1. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007594}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:AFE61124.1}; KW Plasmid {ECO:0000313|EMBL:AFE61124.1}; KW Transferase {ECO:0000313|EMBL:AFE61124.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 207 207 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 300 AA; 31630 MW; 7965B7F614F93856 CRC64; MFSNVKILDG GMGRELARMG APFRQPEWSA LALMEAPEFV RAAHDAFIAA GSQVITTNSY AVVPFHISED VFVEQGAALI ALSGKLAREA ADAAPADVLV AGSLPPVLGS YRPDLFEPVA AKKLLQVLVN NLTDSVDVWL AETQSSVAEV EAVREVLGDD PRPLWLSFTL QDNLDENGNA LLRSGESVDD AVNGALRISA GAVLFNCSRP EVMATAVKTA RAALTAQGSA LDIGVYANAF EPSDNQRGAN EGLSKMRQDT DPAGYLDFAK DWVAQGATMV GGCCGIGPEH IAALKQAFAK // ID H8WEK1_MARHY Unreviewed; 1232 AA. AC H8WEK1; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 29-APR-2015, entry version 22. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CCG95239.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CCG95239.1}; GN Name=metH {ECO:0000313|EMBL:CCG95239.1}; GN ORFNames=MARHY1762 {ECO:0000313|EMBL:CCG95239.1}; OS Marinobacter hydrocarbonoclasticus ATCC 49840. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Marinobacter. OX NCBI_TaxID=1163748 {ECO:0000313|EMBL:CCG95239.1, ECO:0000313|Proteomes:UP000007884}; RN [1] {ECO:0000313|EMBL:CCG95239.1, ECO:0000313|Proteomes:UP000007884} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49840 {ECO:0000313|EMBL:CCG95239.1}; 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). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; FO203363; CCG95239.1; -; Genomic_DNA. DR RefSeq; WP_014421408.1; NC_017067.1. DR RefSeq; YP_005429662.1; NC_017067.1. DR EnsemblBacteria; CCG95239; CCG95239; MARHY1762. DR KEGG; mhc:MARHY1762; -. DR KO; K00548; -. DR BioCyc; MHYD1163748:GLG7-1766-MONOMER; -. DR Proteomes; UP000007884; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007884}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CCG95239.1}; KW Transferase {ECO:0000313|EMBL:CCG95239.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1232 AA; 136980 MW; 28A3FA9323BEC742 CRC64; MTDRNTRLEQ LHQALKERIV ILDGGMGTMI QNQKLDEAAF RGDRFKDYER EVQGNNDLLN LTQPALLRNI HAEYLDAGAD IIETNTFNST KLSQADYGLE SLARELNVAA AKLAREIADE FTARNPQKPR FVAGAVGPTS RTASISPDVN NPGYRNVDFQ TLVDNYYEAV SGLVEGGSDL ILIETVFDTL NAKAAIYATQ QFFIDSGIEL PIMISGTITD ASGRTLSGQT TEAFYNSVAH AKPISVGLNC ALGADALRPY VEELSNKAET YVSAHPNAGL PNEFGEYDQT PEEMAEIIEG FAKDGFLNII GGCCGSRPDH IEAIARAVAK YPPRQIPDRP KALRLSGLEP FTGDENTLFI NVGERTNVTG SKRFLRLIKE EQYEEALSVA RDQVENGAQI IDINMDEGML DSREVMVTFL NLVASEPDIS RVPIMIDSSK WDVIEAGLRC IQGKAVVNSI SLKEGEEEFI KRARDCMRYG AAVVVMAFDE DGQADTFERK TEICKRSYDV LTGIGFNPAD IIFDPNIFAI ATGIEEHNNY AVDFINATRW IREHCPHASI SGGVSNVSFS FRGNDAVREA IHSVFLYHAV KAGMNMGIVN PGQLVIYDEI EPDLKELVED VVLNRRDDST DRLLEAAEKF KGKGGQAKEE DLAWREWPVE KRLEHALVKG ITSYIIDDTE ACRQNASHPI EVIEGPLMAG MNVVGDLFGD GKMFLPQVVK SARVMKQAVA HLIPYIEAEK TEDQQAKGKI LMATVKGDVH DIGKNIVGVV LQCNNYEVID LGVMVPCEKI LETARKENVD MIGLSGLITP SLDEMVHVAR EMQRLDFNIP LMIGGATTSK AHTAVKIEPQ YKNDIALYVS DASRCVNVAS QLLSKTAKPA FVEAARTEYD EIRERRKNRG DRTKLVSLKE ARARAPEIDF ENYQPPKPAF TGVRVFEDYD LKELVDYIDW TPFFISWDIA GKYPAIFDDP KRGEAARTLF DDAQKLLKQM IADQRISARG VVGFWPANRR GDDIVVYTDE SRTEELTTLH HLRQQDEKAP GKPMMALSDF VAPESLHLGD YVGGFAVTTG IGVDELTAEF KNAHDDYSAI MVQALADRLA EAFAERMHER VRKEFWGYAT DEQMANEDLI KERYRGIRPA PGYPACPDHT EKATLFKLLD ATANTSLQLT EHFAMYPTAA VSGWYFAHPD AKYFAVGKIG VDQVEDYAER KGLTKAEAER WLMPSLAYDP AE // ID H8XQI7_FLAIG Unreviewed; 339 AA. AC H8XQI7; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Flavobacterium indicum GPTSA100-9 complete genome {ECO:0000313|EMBL:CCG52481.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CCG52481.1}; GN OrderedLocusNames=KQS_02445 {ECO:0000313|EMBL:CCG52481.1}; OS Flavobacterium indicum (strain DSM 17447 / CIP 109464 / GPTSA100-9). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=1094466 {ECO:0000313|EMBL:CCG52481.1, ECO:0000313|Proteomes:UP000007599}; RN [1] {ECO:0000313|Proteomes:UP000007599} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17447 / CIP 109464 / GPTSA100-9 RC {ECO:0000313|Proteomes:UP000007599}; RA Barbier P., Houel A., Loux V., Poulain J., Bernardet J.-F., RA Touchon M., Duchaud E.; RT "Complete genome sequence of Flavobacterium indicum GPTSA100-9T, RT isolated from warm spring water."; 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; HE774682; CCG52481.1; -; Genomic_DNA. DR RefSeq; WP_014387625.1; NC_017025.1. DR RefSeq; YP_005356538.1; NC_017025.1. DR EnsemblBacteria; CCG52481; CCG52481; KQS_02445. DR KEGG; fin:KQS_02445; -. DR KO; K00548; -. DR BioCyc; FIND1094466:GLDB-489-MONOMER; -. DR Proteomes; UP000007599; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007599}; KW Methyltransferase {ECO:0000313|EMBL:CCG52481.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007599}; KW Transferase {ECO:0000313|EMBL:CCG52481.1}. SQ SEQUENCE 339 AA; 37492 MW; 38B948D8892CBA40 CRC64; MKSSYRVIKI MSKIQEELKK RILVLDGAMG TMLQRNKFEE ADFRGNRFAD FPHPLKGNND LLSITQPEAV KAVHRAYFAA GADIVETNTF SGTTIGMADY HMEDLVYELN YQSAKIAREV ADEFTDKPRF VAGSIGPTNR TASMSPDVND PGYRAVTFDE LKLAYKQQVE ALIDGGSDLL LVETIFDTLN AKAALFAIEE VKEERKIDIP VMVSGTITDA SGRTLSGQTV EAFLISIEHI PLLSVGFNCA LGADQLKPYL KRLSQNTSLN ISAHPNAGLP NAFGQYDQTP EEMQQLIREY LQENLVNIIG GCCGTTPEHI KLIAEVAKEF KPRKLLVVS // ID H8Z7S6_9GAMM Unreviewed; 1256 AA. AC H8Z7S6; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 01-APR-2015, entry version 17. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EIC19929.1}; DE Flags: Precursor; GN ORFNames=Thi970DRAFT_03536 {ECO:0000313|EMBL:EIC19929.1}; OS Thiorhodovibrio sp. 970. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Thiorhodovibrio. OX NCBI_TaxID=631362 {ECO:0000313|EMBL:EIC19929.1}; RN [1] {ECO:0000313|EMBL:EIC19929.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=970 {ECO:0000313|EMBL:EIC19929.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; JH603170; EIC19929.1; -; Genomic_DNA. DR RefSeq; WP_009150332.1; NZ_JH603170.1. DR EnsemblBacteria; EIC19929; EIC19929; Thi970DRAFT_03536. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EIC19929.1}; KW Signal {ECO:0000313|EMBL:EIC19929.1}; KW Transferase {ECO:0000313|EMBL:EIC19929.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT SIGNAL 1 24 Potential. {ECO:0000313|EMBL:EIC19929.1}. FT CHAIN 25 1256 Potential. {ECO:0000313|EMBL:EIC19929.1}. FT /FTId=PRO_5000880392. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1256 AA; 138014 MW; 6F5BA72AFE81C71D CRC64; MTDNSRLLQE RLARSILILD GAMGTMIQRH KLDEAAYRGE RFKDWPSDLK GNNDLLVLTQ PEIIKGIHSE YLAAGADIIE TNTFNGTRIA MADYGMEELV YEINLAAAKL ARQAADEAST PEKPRFVAGI LGPTNRTASI SPDVNDPGFR NVDFDTLVSA YAEATRALIE GGVDILLIET IFDTLNAKAA AFGVWQVFDQ DGVERPILLS GTITDQSGRT LTGQTTEAFY NSLRHAQPLS IGLNCALGPS ELRPYVEELS RIAECQISAH PNAGLPNELG GYDLGPEDMA KEVSEWARSG FLNIIGGCCG TTPDHIRAMA EAVAGMAPRQ APTISPACRL SGLEPCNITE DSFFVNVGER TNVTGSARFK RLIKEGDYDT ALSVAVEQVE NGAQVIDVNM DEGLLDAVAA MKRFLNLTAA EPDIARVPVM IDSSKWEVIE TGLKCVQGKA IVNSISMKEG EDKFIEQARL CRRYGAAVIV MAFDEVGQAD TQARKVEICT RAYKLLTEQV GFPAEDIIFD PNIFAVATGI EEHNNYAVDF IEATREIKRT LPHALVSGGV SNVSFSFRGN NPVREAIHCV FLYHAVKAGM DMGIVNAGQL AIYDDLPEEL REAVEDVIQN RRPDATERLL DIAPKYQGDG STAEKAEDQE WRSWPVEKRL EHSLVKGITD FIDEDTEAAR AAADKPLEVI EGPLMAGMNV VGDLFGEGKM FLPQVVKSAR VMKKAVAYLF PYLEAEKEAS GMAGTSYGKF LIATVKGDVH DIGKNIVAVV LQCNGYEVVD LGVMVPTETI LKRAREEQVD MIGLSGLITP SLDEMVHVAK EMERQGFDIP LLIGGATTSK LHTAVKIAPQ RKHPVVYVVD ASRAVGVVSN LLSKTQRDGY VAQIAADYER LRVEREAKSG TRKSMPIGDA RANKVGIDWA GYQPPRPQIL EPRFDTGSLD QPDWKLTVER QGDGVILTID DYPLADLVNF IDWSPFFNAW ELAGKYPAIL NDKVVGQEAR KLFEDAKPFL ETLVKENWLT ARAVCGFFPA QSVNDDDIAL FSDEARSTPL ATLRMLRQQM FRAAGKNQPN LCLTDFIAPA DSGAQDWIGG FAVTAGVGID EHIARFEADH DDYNSIMLKA LADRLAEAFA ERLHQIVRTQ LWGHAPDEQL DNSALIAEKY QGIRPAPGYA ACPDHTEKGT LWELLKPDER IGLTLTESYA MLPTAAVSGW YFSHPESRYF GVGRIQKDQV EDYAQRKGMT LEQAERWLAP VLGYDP // ID H8ZVM8_9LAMI Unreviewed; 74 AA. AC H8ZVM8; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 29-OCT-2014, entry version 9. DE SubName: Full=Selenocysteine methyltransferase {ECO:0000313|EMBL:AFD50203.1}; DE Flags: Fragment; GN Name=SMT {ECO:0000313|EMBL:AFD50203.1}; OS Micromeria varia. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; OC Mentheae; Micromeria. OX NCBI_TaxID=306401 {ECO:0000313|EMBL:AFD50203.1}; RN [1] {ECO:0000313|EMBL:AFD50203.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Obasi005Lanz {ECO:0000313|EMBL:AFD50203.1}; RA Curto M.A., Puppo P., Ferreira D., Nogueira M., Meimberg H.; RT "Development of phylogenetic markers from single-copy nuclear genes RT for multi locus, species level analyses in the mint family RT (Lamiaceae)."; RL Mol. Phylogenet. Evol. 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; JN587567; AFD50203.1; -; Genomic_DNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:AFD50203.1}; KW Transferase {ECO:0000313|EMBL:AFD50203.1}. FT NON_TER 1 1 {ECO:0000313|EMBL:AFD50203.1}. FT NON_TER 74 74 {ECO:0000313|EMBL:AFD50203.1}. SQ SEQUENCE 74 AA; 8261 MW; 779CC4D1FB278CB4 CRC64; VHLDYLEAGA DIILTASYQA TIQGFQNKGY SMEESESMLR KSVELAREAR ELYYTSCREA SAAKDIPHDK VSSS // ID H8ZVM9_9LAMI Unreviewed; 74 AA. AC H8ZVM9; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 29-OCT-2014, entry version 9. DE SubName: Full=Selenocysteine methyltransferase {ECO:0000313|EMBL:AFD50204.1}; DE Flags: Fragment; GN Name=SMT {ECO:0000313|EMBL:AFD50204.1}; OS Micromeria varia. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; OC Mentheae; Micromeria. OX NCBI_TaxID=306401 {ECO:0000313|EMBL:AFD50204.1}; RN [1] {ECO:0000313|EMBL:AFD50204.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Obasi005Mhys {ECO:0000313|EMBL:AFD50204.1}; RA Curto M.A., Puppo P., Ferreira D., Nogueira M., Meimberg H.; RT "Development of phylogenetic markers from single-copy nuclear genes RT for multi locus, species level analyses in the mint family RT (Lamiaceae)."; RL Mol. Phylogenet. Evol. 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; JN587568; AFD50204.1; -; Genomic_DNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:AFD50204.1}; KW Transferase {ECO:0000313|EMBL:AFD50204.1}. FT NON_TER 1 1 {ECO:0000313|EMBL:AFD50204.1}. FT NON_TER 74 74 {ECO:0000313|EMBL:AFD50204.1}. SQ SEQUENCE 74 AA; 8291 MW; 779CC4C1FA278CB4 CRC64; VHLDYLEAGA DIILTASYQA TIQGFQNKGY SMEESESMLR KSVELAREAR ELYYTSCREA SATKDIPHDK VSSS // ID H8ZVN0_9LAMI Unreviewed; 74 AA. AC H8ZVN0; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 29-OCT-2014, entry version 9. DE SubName: Full=Selenocysteine methyltransferase {ECO:0000313|EMBL:AFD50205.1}; DE Flags: Fragment; GN Name=SMT {ECO:0000313|EMBL:AFD50205.1}; OS Micromeria tenuis. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; OC Mentheae; Micromeria. OX NCBI_TaxID=412921 {ECO:0000313|EMBL:AFD50205.1}; RN [1] {ECO:0000313|EMBL:AFD50205.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Obasi005Mten {ECO:0000313|EMBL:AFD50205.1}; RA Curto M.A., Puppo P., Ferreira D., Nogueira M., Meimberg H.; RT "Development of phylogenetic markers from single-copy nuclear genes RT for multi locus, species level analyses in the mint family RT (Lamiaceae)."; RL Mol. Phylogenet. Evol. 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; JN587569; AFD50205.1; -; Genomic_DNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:AFD50205.1}; KW Transferase {ECO:0000313|EMBL:AFD50205.1}. FT NON_TER 1 1 {ECO:0000313|EMBL:AFD50205.1}. FT NON_TER 74 74 {ECO:0000313|EMBL:AFD50205.1}. SQ SEQUENCE 74 AA; 8291 MW; 779CC4C1FA278CB4 CRC64; VHLDYLEAGA DIILTASYQA TIQGFQNKGY SMEESESMLR KSVELAREAR ELYYTSCREA SATKDIPHDK VSSS // ID H8ZVN1_9LAMI Unreviewed; 74 AA. AC H8ZVN1; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 29-OCT-2014, entry version 9. DE SubName: Full=Selenocysteine methyltransferase {ECO:0000313|EMBL:AFD50206.1}; DE Flags: Fragment; GN Name=SMT {ECO:0000313|EMBL:AFD50206.1}; OS Micromeria varia. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; OC Mentheae; Micromeria. OX NCBI_TaxID=306401 {ECO:0000313|EMBL:AFD50206.1}; RN [1] {ECO:0000313|EMBL:AFD50206.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Obasi005Mvthy {ECO:0000313|EMBL:AFD50206.1}; RA Curto M.A., Puppo P., Ferreira D., Nogueira M., Meimberg H.; RT "Development of phylogenetic markers from single-copy nuclear genes RT for multi locus, species level analyses in the mint family RT (Lamiaceae)."; RL Mol. Phylogenet. Evol. 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; JN587570; AFD50206.1; -; Genomic_DNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:AFD50206.1}; KW Transferase {ECO:0000313|EMBL:AFD50206.1}. FT NON_TER 1 1 {ECO:0000313|EMBL:AFD50206.1}. FT NON_TER 74 74 {ECO:0000313|EMBL:AFD50206.1}. SQ SEQUENCE 74 AA; 8317 MW; 779CC4C1FA3F2FB4 CRC64; VHLDYLEAGA DIILTASYQA TIQGFQNKGY SMEESESMLR KSVELAREAR ELYYTSCREA LATKDIPHDK VSSS // ID H8ZVN2_9LAMI Unreviewed; 73 AA. AC H8ZVN2; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 29-OCT-2014, entry version 9. DE SubName: Full=Selenocysteine methyltransferase {ECO:0000313|EMBL:AFD50207.1}; DE Flags: Fragment; GN Name=SMT {ECO:0000313|EMBL:AFD50207.1}; OS Micromeria lanata. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; OC Mentheae; Micromeria. OX NCBI_TaxID=412919 {ECO:0000313|EMBL:AFD50207.1}; RN [1] {ECO:0000313|EMBL:AFD50207.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Obasi005lanGC {ECO:0000313|EMBL:AFD50207.1}; RA Curto M.A., Puppo P., Ferreira D., Nogueira M., Meimberg H.; RT "Development of phylogenetic markers from single-copy nuclear genes RT for multi locus, species level analyses in the mint family RT (Lamiaceae)."; RL Mol. Phylogenet. Evol. 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; JN587571; AFD50207.1; -; Genomic_DNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:AFD50207.1}; KW Transferase {ECO:0000313|EMBL:AFD50207.1}. FT NON_TER 1 1 {ECO:0000313|EMBL:AFD50207.1}. FT NON_TER 73 73 {ECO:0000313|EMBL:AFD50207.1}. SQ SEQUENCE 73 AA; 8204 MW; 9CC4C1FA278CB403 CRC64; VHLDYLEAGA DIILTASYQA TIQGFQNKGY SMEESESMLR KSVELAREAR ELYYTSCREA SATKDIPHDK VSS // ID H8ZVN3_9LAMI Unreviewed; 73 AA. AC H8ZVN3; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 29-OCT-2014, entry version 9. DE SubName: Full=Selenocysteine methyltransferase {ECO:0000313|EMBL:AFD50208.1}; DE Flags: Fragment; GN Name=SMT {ECO:0000313|EMBL:AFD50208.1}; OS Micromeria varia. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; OC Mentheae; Micromeria. OX NCBI_TaxID=306401 {ECO:0000313|EMBL:AFD50208.1}; RN [1] {ECO:0000313|EMBL:AFD50208.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Obasi005variaEH {ECO:0000313|EMBL:AFD50208.1}; RA Curto M.A., Puppo P., Ferreira D., Nogueira M., Meimberg H.; RT "Development of phylogenetic markers from single-copy nuclear genes RT for multi locus, species level analyses in the mint family RT (Lamiaceae)."; RL Mol. Phylogenet. Evol. 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; JN587572; AFD50208.1; -; Genomic_DNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:AFD50208.1}; KW Transferase {ECO:0000313|EMBL:AFD50208.1}. FT NON_TER 1 1 {ECO:0000313|EMBL:AFD50208.1}. FT NON_TER 73 73 {ECO:0000313|EMBL:AFD50208.1}. SQ SEQUENCE 73 AA; 8204 MW; 9CC4C1FA278CB403 CRC64; VHLDYLEAGA DIILTASYQA TIQGFQNKGY SMEESESMLR KSVELAREAR ELYYTSCREA SATKDIPHDK VSS // ID H8ZVN5_ORIVU Unreviewed; 69 AA. AC H8ZVN5; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 29-OCT-2014, entry version 9. DE SubName: Full=Selenocysteine methyltransferase {ECO:0000313|EMBL:AFD50210.1}; DE Flags: Fragment; GN Name=SMT {ECO:0000313|EMBL:AFD50210.1}; OS Origanum vulgare (Wild marjoram). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; OC Mentheae; Origanum. OX NCBI_TaxID=39352 {ECO:0000313|EMBL:AFD50210.1}; RN [1] {ECO:0000313|EMBL:AFD50210.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Obasi005LNIV008 {ECO:0000313|EMBL:AFD50210.1}; RA Curto M.A., Puppo P., Ferreira D., Nogueira M., Meimberg H.; RT "Development of phylogenetic markers from single-copy nuclear genes RT for multi locus, species level analyses in the mint family RT (Lamiaceae)."; RL Mol. Phylogenet. Evol. 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; JN587574; AFD50210.1; -; Genomic_DNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:AFD50210.1}; KW Transferase {ECO:0000313|EMBL:AFD50210.1}. FT NON_TER 1 1 {ECO:0000313|EMBL:AFD50210.1}. FT NON_TER 69 69 {ECO:0000313|EMBL:AFD50210.1}. SQ SEQUENCE 69 AA; 7785 MW; 40C282452371107C CRC64; VHLDYLEAGA DIILTATIQG FQNKGYSLEE SESMLRKSVE LAREARDLYY TRCCEASRAK DIPNDKISS // ID H8ZVN6_LAVAN Unreviewed; 71 AA. AC H8ZVN6; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 29-OCT-2014, entry version 9. DE SubName: Full=Selenocysteine methyltransferase {ECO:0000313|EMBL:AFD50211.1}; DE Flags: Fragment; GN Name=SMT {ECO:0000313|EMBL:AFD50211.1}; OS Lavandula angustifolia (Lavender). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; OC Lavanduleae; Lavandula. OX NCBI_TaxID=39329 {ECO:0000313|EMBL:AFD50211.1}; RN [1] {ECO:0000313|EMBL:AFD50211.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Obasi005LNIV002 {ECO:0000313|EMBL:AFD50211.1}; RA Curto M.A., Puppo P., Ferreira D., Nogueira M., Meimberg H.; RT "Development of phylogenetic markers from single-copy nuclear genes RT for multi locus, species level analyses in the mint family RT (Lamiaceae)."; RL Mol. Phylogenet. Evol. 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; JN587575; AFD50211.1; -; Genomic_DNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:AFD50211.1}; KW Transferase {ECO:0000313|EMBL:AFD50211.1}. FT NON_TER 1 1 {ECO:0000313|EMBL:AFD50211.1}. FT NON_TER 71 71 {ECO:0000313|EMBL:AFD50211.1}. SQ SEQUENCE 71 AA; 8066 MW; 47505517FB8D8275 CRC64; VHLDYLEAGA XIIITAXYQA TIQGFQNKGY SLEESESMLR KSVELACEAR ELYYTRCREA STKDTPHDKI S // ID H8ZVN7_OCIBA Unreviewed; 72 AA. AC H8ZVN7; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 29-OCT-2014, entry version 9. DE SubName: Full=Selenocysteine methyltransferase {ECO:0000313|EMBL:AFD50212.1}; DE Flags: Fragment; GN Name=SMT {ECO:0000313|EMBL:AFD50212.1}; OS Ocimum basilicum (Sweet basil). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; OC Ocimeae; Ocimum. OX NCBI_TaxID=39350 {ECO:0000313|EMBL:AFD50212.1}; RN [1] {ECO:0000313|EMBL:AFD50212.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Obasi005LNIV018 {ECO:0000313|EMBL:AFD50212.1}; RA Curto M.A., Puppo P., Ferreira D., Nogueira M., Meimberg H.; RT "Development of phylogenetic markers from single-copy nuclear genes RT for multi locus, species level analyses in the mint family RT (Lamiaceae)."; RL Mol. Phylogenet. Evol. 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; JN587576; AFD50212.1; -; Genomic_DNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:AFD50212.1}; KW Transferase {ECO:0000313|EMBL:AFD50212.1}. FT NON_TER 1 1 {ECO:0000313|EMBL:AFD50212.1}. FT NON_TER 72 72 {ECO:0000313|EMBL:AFD50212.1}. SQ SEQUENCE 72 AA; 8143 MW; AF27376E59852A30 CRC64; VHLDYLEAGA NIILTASYQA TIQXFQNKGY PLEVSENMLR KSVEIALEAR ELYYARCHEX SAEDTPDDKI SS // ID H9J3W9_BOMMO Unreviewed; 325 AA. AC H9J3W9; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 27-MAY-2015, entry version 17. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:BGIBMGA004208-TA}; GN Name=LOC692944 {ECO:0000313|EnsemblMetazoa:BGIBMGA004208-TA}; OS Bombyx mori (Silk moth). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; OC Bombycoidea; Bombycidae; Bombycinae; Bombyx. OX NCBI_TaxID=7091 {ECO:0000313|EnsemblMetazoa:BGIBMGA004208-TA, ECO:0000313|Proteomes:UP000005204}; RN [1] {ECO:0000313|EnsemblMetazoa:BGIBMGA004208-TA} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=p50T {ECO:0000313|EnsemblMetazoa:BGIBMGA004208-TA}; RX PubMed=19121390; DOI=10.1016/j.ibmb.2008.11.004; RG International Silkworm Genome Consortium; RT "The genome of a lepidopteran model insect, the silkworm Bombyx RT mori."; RL Insect Biochem. Mol. Biol. 38:1036-1045(2008). RN [2] {ECO:0000313|EnsemblMetazoa:BGIBMGA004208-TA} RP IDENTIFICATION. RC STRAIN=p50T (Dazao) {ECO:0000313|EnsemblMetazoa:BGIBMGA004208-TA}; RG EnsemblMetazoa; RL Submitted (DEC-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; DQ311365; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EnsemblMetazoa; BGIBMGA004208-RA; BGIBMGA004208-TA; BGIBMGA004208. DR InParanoid; H9J3W9; -. DR OMA; SEWCKDG; -. DR OrthoDB; EOG7GQXW0; -. DR Proteomes; UP000005204; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005204}; KW Reference proteome {ECO:0000313|Proteomes:UP000005204}. SQ SEQUENCE 325 AA; 36595 MW; 0774EC9910E3A398 CRC64; MSNFEVSSKT VFVLDGGFST QLTCHAGHTA DGDPLWSARF LKTHPQDVIN THLDFLRAGS DIIETNTYQA SVDGFVKHLN LTVEESYELI KSAVEFARTA RDLYLQECQE SNLSGRKPLI AGSVGPYGAY LHDTSEYTGN YADNTTKETI KNWHRTRIQA LVEAGVDILA FETIPCQKEA EALVEILKEY PNMKAWLSFS CKNETSLAHG ENFQNVAKKC WKSNPDQLIA IGVNCCSPKI VTELFKDINN DQETSIQFIT YPNSGETYDH KLGWTESDKC ESLHNFVAEW LDLGVRYIGG CCRTNDVDIS RIRIETDLWL KKNSL // ID H9J8R6_BOMMO Unreviewed; 249 AA. AC H9J8R6; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:BGIBMGA005908-TA}; OS Bombyx mori (Silk moth). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; OC Bombycoidea; Bombycidae; Bombycinae; Bombyx. OX NCBI_TaxID=7091 {ECO:0000313|EnsemblMetazoa:BGIBMGA005908-TA, ECO:0000313|Proteomes:UP000005204}; RN [1] {ECO:0000313|EnsemblMetazoa:BGIBMGA005908-TA} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=p50T {ECO:0000313|EnsemblMetazoa:BGIBMGA005908-TA}; RX PubMed=19121390; DOI=10.1016/j.ibmb.2008.11.004; RG International Silkworm Genome Consortium; RT "The genome of a lepidopteran model insect, the silkworm Bombyx RT mori."; RL Insect Biochem. Mol. Biol. 38:1036-1045(2008). RN [2] {ECO:0000313|EnsemblMetazoa:BGIBMGA005908-TA} RP IDENTIFICATION. RC STRAIN=p50T (Dazao) {ECO:0000313|EnsemblMetazoa:BGIBMGA005908-TA}; RG EnsemblMetazoa; RL Submitted (AUG-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 EnsemblMetazoa; BGIBMGA005908-RA; BGIBMGA005908-TA; BGIBMGA005908. DR InParanoid; H9J8R6; -. DR OMA; ARFIHTH; -. DR OrthoDB; EOG7GQXW0; -. DR Proteomes; UP000005204; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 2. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005204}; KW Reference proteome {ECO:0000313|Proteomes:UP000005204}. SQ SEQUENCE 249 AA; 28319 MW; 22F4B02EFCAD3DA4 CRC64; MTPPSSENTE APHIVVLDGG FSTQLSCHVG HVIDGDPLWS ARFIHTHPNE VVNTHLDFLR AGADLIITNT YQASVEGFVE HLGVTKEQGY ELIARAVQLA KQARTLYLEE YRDYVQNDDI PLIVGSVGPY GAHLHDGSEY DGSYADTTSI ETMREWHRPR IQALVEAGVD LLALETIPCQ EEAETFWIDR DKCEPVEIYI QEWLDLGVRY VGGCCRTYAA DVSRIQNQVH RWRDRYRFQT KYQSNNGLH // ID H9UC42_FERPD Unreviewed; 784 AA. AC H9UC42; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 29-APR-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase/B12 binding domain/Pterin binding enzyme {ECO:0000313|EMBL:AFG35085.1}; GN OrderedLocusNames=Ferpe_0975 {ECO:0000313|EMBL:AFG35085.1}; OS Fervidobacterium pennivorans (strain DSM 9078 / Ven5). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; OC Fervidobacterium. OX NCBI_TaxID=771875 {ECO:0000313|EMBL:AFG35085.1, ECO:0000313|Proteomes:UP000007384}; RN [1] {ECO:0000313|Proteomes:UP000007384} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 9078 / Ven5 {ECO:0000313|Proteomes:UP000007384}; 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., Noll K.M., RA Woyke T.; RT "Complete sequence of Fervidobacterium pennivorans DSM 9078."; 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; CP003260; AFG35085.1; -; Genomic_DNA. DR RefSeq; WP_014451526.1; NC_017095.1. DR RefSeq; YP_005471204.1; NC_017095.1. DR EnsemblBacteria; AFG35085; AFG35085; Ferpe_0975. DR KEGG; fpe:Ferpe_0975; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR BioCyc; FPEN771875:GLDA-975-MONOMER; -. DR Proteomes; UP000007384; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007384}; KW Methyltransferase {ECO:0000313|EMBL:AFG35085.1}; KW Transferase {ECO:0000313|EMBL:AFG35085.1}. SQ SEQUENCE 784 AA; 86644 MW; 4FB3514783FFB3A2 CRC64; MEPLTRQKFS ELLSQRVMFL DGAYGTELFK RGYIKNREPI ELLNITNAKA VLSLQSDYVC AGVDFLLTNT FSANRHKLMK LGYDEYFKEI NQSAVKIAKE ATKVANKQVF VLGDISSVGE MIEPLGELKS KYVYNIFKEQ VEVLVDVGVD GIIIETMSDI KEAKLAYLAA RDVAPEIPVL VSMTFEENGV TVTGTSLEVY VALFNDLDVD AIGINCTLTP EKMVPLVKKL VALSKKPVFV EPNAGKPTLS ADGKLTYKTT PEEFTIYIED YVELGANIVG GCCGTGPEHI KYMVQHIGLK RPKARKVEEL NVVTSRVHMF NVAPFLVVGE RINASARKKL HNEIREFNFE NVLKLAKSQE QEGAQVIDVN FGIESVLSEE HFSKAIVELD KIVSIPISFD IQYNEFLESA LMEYPGRPLI NSSKATKEEL DKKIRLLKRY GGLLIVLAMG KEIPKTAEER YTLGKMAVEY LESQGIDRSR IFVDPLVLPI GANQDYNVTL ETIKKLSSDG IKTMIGLSNF SFGMPNRDEL NASFLALAMH SGLSGAILNT SEDATMKILR GMIRILGKES ARISEEVKSS ELVHLLLRGN LNDAEKHVLS FLDTLTPIEI IQTILAKAME EIGNLYAENK IYLPHLILAA ETSKPIFNKL LSMVAEKDSA RLGRILLATV EGDIHDIGKK IVATVLESAG FEVIDIGKDV PASVILEKVK ELKPDIVGLS AMMTTTVIQV GHVVKTLRDN GIEIPVIAGG ASMNGELAKR FGSYYAKDAQ EAVKLCKQIL TNNQ // ID H9UGF0_SPIAZ Unreviewed; 1312 AA. AC H9UGF0; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AFG36593.1}; GN OrderedLocusNames=Spiaf_0490 {ECO:0000313|EMBL:AFG36593.1}; OS Spirochaeta africana (strain ATCC 700263 / DSM 8902 / Z-7692). OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Spirochaeta. OX NCBI_TaxID=889378 {ECO:0000313|EMBL:AFG36593.1, ECO:0000313|Proteomes:UP000007383}; RN [1] {ECO:0000313|Proteomes:UP000007383} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 700263 / DSM 8902 / Z-7692 RC {ECO:0000313|Proteomes:UP000007383}; RX PubMed=23991249; DOI=10.4056/sigs.3607108; RA Liolos K., Abt B., Scheuner C., Teshima H., Held B., Lapidus A., RA Nolan M., Lucas S., Deshpande S., Cheng J.F., Tapia R., Goodwin L.A., RA Pitluck S., Pagani I., Ivanova N., Mavromatis K., Mikhailova N., RA Huntemann M., Pati A., Chen A., Palaniappan K., Land M., Rohde M., RA Tindall B.J., Detter J.C., Goker M., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Woyke T., Klenk H.P., Kyrpides N.C.; RT "Complete genome sequence of the halophilic bacterium Spirochaeta RT africana type strain (Z-7692(T)) from the alkaline Lake Magadi in the RT East African Rift."; RL Stand. Genomic Sci. 8:165-176(2013). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP003282; AFG36593.1; -; Genomic_DNA. DR RefSeq; WP_014454590.1; NC_017098.1. DR RefSeq; YP_005474300.1; NC_017098.1. DR EnsemblBacteria; AFG36593; AFG36593; Spiaf_0490. DR KEGG; sfc:Spiaf_0490; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; SAFR889378:GLKD-489-MONOMER; -. DR Proteomes; UP000007383; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007383}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AFG36593.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007383}; KW Transferase {ECO:0000313|EMBL:AFG36593.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 348 348 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 349 349 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 798 798 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1312 AA; 143745 MW; 5E548C7C4EBAF4A7 CRC64; MKGTKKTLIR GNVPADTAVR LRALEALIQE RIVYLDGAMG TMIQNCKLQE ADFRADYGGL LTDHPKPLQG NNDLLLLTRP DIIREIHTEF LDAGADILET NTFNSTSVSQ ADYGTEHLVY ELNRAGAALA RECAAAADAR EAGTIAGADA SAAAADQSPA PPPTHFVAGV LGPTSKTLSL SPDVNDPGFR AITFPELAES YREAVGGLID GGADLILIET IFDTLNAKAA IYACKQEFHA RGYELPIMIS GTITDASGRT LSGQTVEAFY NSICHAEPFS VGLNCALGAD LLKRYVSDLS RVADQPVSTH PNAGLPNEFG EYDHSPEFMA RIMGEFAAEG IVNIIGGCCG TTPEHLRQIV AATGGHAPRA IPEHKQQLSL SGLEPLVNTP DLGFINVGER TNVTGSRKFL RLIRDKQYEE ALEVARDQVE GGAQIIDINM DEAMLESADE MRTFLNLVGA EPDISRIPIM VDSSKWSVIE AGLQCIQGKG VVNSISMKEG EAEFLEHARL VRLYGAAAIV MAFDEKGQAD TLERRVEICR RAYKLLTEKL DFPPEDIIFD LNIFAIGTGI EEHRNYAVDF IEAARIIRRE MPLVSISGGV SNVSFSFRGN NAVREAIHTV FLYHAVKAGM NMGIVNPGQL EVYDDIQPEL LEHVEDLVMN RREDATERLL ELAESIQSGG KSRVKDLSWR EQPVGKRLEH ALVKGITAWV EEDTEEARQQ LPQALEVIEG PLMDGMNVVG DLFGSGKMFL PQVVKSARVM KMAVAYLLPY IEAEKKAGGG EQQAKGKILM ATVKGDVHDI GKNIVGVVLG CNNYEIVDLG VMVECEDILA AAREHKVDVI GLSGLITPSL DEMVHVASEM ERQGFELPLM IGGATTSKIH TAVKIDPAYH APIAHVKDAS LAVNIVSRMI GDRENIGREL KAEYQRMREK RAATTSTKEY ITIQEARDQR FLPGMTIPQP EGTEVAMAQV ASAPASAAAA PASANAADAA TPAVAPGKPG WEGYVPPTPN LIGRKHFIDY PLEHIRKYID WAFFFYSWQL RGKFPDILDD PEMGEEARKL YADANAMLDR MISEKRIRAD GSIFILPANS TEDDDIRIYD ETGKQQIGVW NTLRQQKQKT ETPYYLSLSD FTAPESSGIR DYIGGFAVTA GHGADDFAKT FEDAGDDYSA ILVKILADRM AEAFAECLHE DVRREHWGYA PDEDLSIEDL LAIRYQGIRP APGYPPCPNH EDKAGLFELL DTTPHTGIEL TQSWMMTPPA SVSGYIFAHP ESHYFGVGTL MRDQVQDWAR RKNLPLATAE KWLAPKLAYD PE // ID H9UNV6_ECOLX Unreviewed; 310 AA. AC H9UNV6; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AFG39199.1}; GN Name=mmuM {ECO:0000313|EMBL:AFG39199.1}; GN ORFNames=P12B_c0315 {ECO:0000313|EMBL:AFG39199.1}; OS Escherichia coli P12b. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=910348 {ECO:0000313|EMBL:AFG39199.1, ECO:0000313|Proteomes:UP000007385}; RN [1] {ECO:0000313|EMBL:AFG39199.1, ECO:0000313|Proteomes:UP000007385} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P12b {ECO:0000313|EMBL:AFG39199.1}; 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 ----------------------------------------------------------------------- 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; AFG39199.1; -; Genomic_DNA. DR RefSeq; WP_000081352.1; NC_017663.1. DR RefSeq; YP_006167369.1; NC_017663.1. DR ProteinModelPortal; H9UNV6; -. DR SMR; H9UNV6; 11-307. DR EnsemblBacteria; AFG39199; AFG39199; P12B_c0315. DR KEGG; elp:P12B_c0315; -. DR KO; K00547; -. DR BioCyc; ECOL910348:GI9X-323-MONOMER; -. DR Proteomes; UP000007385; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007385}; KW Methyltransferase {ECO:0000313|EMBL:AFG39199.1}; KW Transferase {ECO:0000313|EMBL:AFG39199.1}. SQ SEQUENCE 310 AA; 33423 MW; 8381CFF475E5FB7A CRC64; MSQNNPLRAL LDKQDILLLD GAMATELEAR GCNLADSLWS AKVLVENPEL IREVHLDYYR AGAQCAITAS YQATPAGFAA RGLDEAQSKA LIGKSVELAR KAREAYLAEN PQAGTLLVAG SVGPYGAYLA DGSEYRGDYH CSVEAFQAFH RPRVEALLDA GADLLACETL PNFSEIEALA ELLTAYPRAR AWFSFTLRDS EHLSDGTPLR DVVALLAGYP QVVALGINCI ALENTTAALQ HLHGLTVLPL VVYPNSGEHY DAVSKTWHHH GEHCAQLADY LPQWQAAGAR LIGGCCRTTP ADIAALKARS // ID H9UZJ6_ECOLX Unreviewed; 1205 AA. AC H9UZJ6; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AFG42939.1}; GN Name=metH {ECO:0000313|EMBL:AFG42939.1}; GN ORFNames=P12B_c4126 {ECO:0000313|EMBL:AFG42939.1}; OS Escherichia coli P12b. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=910348 {ECO:0000313|EMBL:AFG42939.1, ECO:0000313|Proteomes:UP000007385}; RN [1] {ECO:0000313|EMBL:AFG42939.1, ECO:0000313|Proteomes:UP000007385} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P12b {ECO:0000313|EMBL:AFG42939.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002291; AFG42939.1; -; Genomic_DNA. DR RefSeq; WP_014641226.1; NC_017663.1. DR RefSeq; YP_006171109.1; NC_017663.1. DR EnsemblBacteria; AFG42939; AFG42939; P12B_c4126. DR KEGG; elp:P12B_c4126; -. DR KO; K00548; -. DR BioCyc; ECOL910348:GI9X-4222-MONOMER; -. DR Proteomes; UP000007385; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007385}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 225 225 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 737 737 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1205 AA; 133604 MW; 994D13C5D52C836E CRC64; MGTMIQSYRL NEADFRGERF ADWPCDLKGN NDLLVLSKPE VIAAIHNAYF EAGADIIETN TFNSTTIAMA DYQMESLSAE INFAAAKLAR ACADEWTART PEKPRYVAGV LGPTNRTASI SPDVNDPAFR NITFDGLVAA YRESTKALVE GGADLILIET VFDTLNAKAA VFAVKTEFEA LGVELPIMIS GTITDASGRT LSGQTTEAFY NSLRHAEALT FGLNCALGPD ELRQYVQELS RIAECYVTAH PNAGLPNAFG EYDLDADTMA KQIREWAQAG FLNIVGGCCG TTPQHIAAMS RAVEGLAPRK LPEIPVACRL SGLEPLNIGE DSLFVNVGER TNVTGSAKFK RLIKEEKYSE ALDVARQQVE NGAQIIDINM DEGMLDAEAA MVRFLNLIAG EPDIARVPIM IDSSKWDVIE KGLKCIQGKG IVNSISMKEG VDAFIHHAKL LRRYGAAVVV MAFDEQGQAD TRARKIEICR RAYKILTEEV GFPPEDIIFD PNIFAVATGI EEHNNYAQDF IGACEDIKRE LPHALISGGV SNVSFSFRGN DPVREAIHAV FLYYAIRNGM DMGIVNAGQL AIYDDLPAEL RDAVEDVILN RRDDGTERLL ELAEKYRGSK TDDTANAQQA EWRSWEVNKR LEYSLVKGIT EFIEQDTEEA RQQATRPIEV IEGPLMDGMN VVGDLFGEGK MFLPQVVKSA RVMKQAVAYL EPFIEASKEQ GKTNGKMVIA TVKGDVHDIG KNIVGVVLQC NNYEIVDLGV MVPAEKILRT AKEVNADLIG LSGLITPSLD EMVNVAKEME RQGFTIPLLI GGATTSKAHT AVKIEQNYSG PTVYVQNASR TVGVVAALLS DTQRDDFVAR TRKEYETVRI QHGRKKPRTP PVTLEAARDN DFAFDWQAYT PPVAHRLGVQ EVEASIETLR NYIDWTPFFM TWSLAGKYPR ILEDEVVGVE AQRLFKDAND MLDKLSAEKT LNPRGVVGLF PANRVGDDIE IYRDETRTHV INVSHHLRQQ TEKTGFANYC LADFVAPKLS GKADYIGAFA VTGGLEEDAL ADAFEAQHDD YNKIMVKALA DRLAEAFAEY LHERVRKVYW GYAPNENLSN EELIRENYQG IRPAPGYPAC PEHTEKATIW ELLEVEKHTG MKLTESFAMW PGASVSGWYF SHPDSKYYAV AQIQRDQVED YARRKCMSVT EVERWLAPNL GYDAD // ID H9ZSM3_THETH Unreviewed; 1185 AA. AC H9ZSM3; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 01-APR-2015, entry version 22. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AFH39333.1}; GN ORFNames=TtJL18_1453 {ECO:0000313|EMBL:AFH39333.1}; OS Thermus thermophilus JL-18. OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; OC Thermus. OX NCBI_TaxID=798128 {ECO:0000313|EMBL:AFH39333.1, ECO:0000313|Proteomes:UP000007388}; RN [1] {ECO:0000313|EMBL:AFH39333.1, ECO:0000313|Proteomes:UP000007388} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JL-18 {ECO:0000313|EMBL:AFH39333.1}; RX PubMed=23405355; DOI=10.1128/genomeA.00106-12; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP003252; AFH39333.1; -; Genomic_DNA. DR RefSeq; WP_014629938.1; NC_017587.1. DR RefSeq; YP_006059119.1; NC_017587.1. DR EnsemblBacteria; AFH39333; AFH39333; TtJL18_1453. DR KEGG; ttl:TtJL18_1453; -. DR KO; K00548; -. DR BioCyc; TTHE798128:GLMF-1452-MONOMER; -. DR Proteomes; UP000007388; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007388}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AFH39333.1}; KW Transferase {ECO:0000313|EMBL:AFH39333.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 256 256 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1185 AA; 131059 MW; 18C01140CCCC61CB CRC64; MVEVHACSPG CRHHLGGAGW GDAPLVRLGY NKEARAKKFP YLKALLERPL VFDGAMGTEL QKRDLTPEDY GGEAYFGCPE VLNRTRPEVV REIHLAYLEA GAEVIETNTF GTLRHVLAEY GLEEEAEELA FLGARIAREA ADPHGAFVAG ALGPGTKLVS LGQISWDALY RAYKEAARGL LRGGVDLILL ETAQDILQVR CAVLAVREAM AEVGREVPLQ VQVTFEATGT MLVGTDEQAA LAALESLPID VVGMNCATGP DLMDSKVRYF AEHSTRFVSC LPNAGLPRNE GGRVVYDLTP EELAKWHLKF VAEYGVNAVG GCCGTGPEHI RKVAEAVKGL PARPRPKSFP PQVASLYQAV PLKQEASLFL VGERLNATGS KRFREMLFAR DLEGILALAR EQVEEGAHAL DLSVAWTGRD ELEDLRWLLP SLTTAVTVPV MVDSTSPEAM ELALKHLPGR VLLNSANLED GLERFDQVAS LAKAHGAALV VLAIDEKGMA KTWEEKVRVA LRMYERLTEH HGLRPEDLLF DLLTFPITQG DEESRPLAKE TLLAMEELRE RLPGVGFILG VSNVSFGLKP RARRVLNSVF LDEARKRGLT AAIVDAGKIL PISQIPEEAY ALALDLIYDR RKEGFDPLLA FMAYFEAHKE DPGKREDAFL ALPLLERLKR RVVEGRKQGL EADLEEALKA GHKPLDLING PLLAGMKEVG DLFGAGKMQL PFVLQAAEVM KRAVAYLEPH MEKKGEGKGT LVLATVKGDV HDIGKNLVDI ILSNNGYRVV NLGIKVPIEE ILKAVEAHKP HAVGMSGLLV KSTLVMKENL EYMRDRGYTL PVILGGAALT RSYVEELRAI YPNVYYAEDA FEGLRLMEEL TGHAPPELTR KAPARPKREA PKVAPRARPV GEAPAVPRPP FFGVRVEEGL DLATIAHYVN KLALYRGQWG YSRKGLSREA WQALVEREAE PVFQRLLKEA MAEGWLEPKV LYGFFPVARE GEELLVFSPE TGEVLERFRF PRQKGGGLSL VDYFRPRFAA PLGDEADWMP KEAFRAGARD VLGVQLVTMG EAPSRKAQAL FQSGAYQDYL FVHGFSVEMT EALAEYWHKR MRQMWGIAHK DATEIQKLFQ QGYQGARYSF GYPACPDLAD QAKLDRLMGF HRVGVRLTEN FQLEPEHATS ALVVHHPEAC YFSVD // ID HMT_BACSU Reviewed; 315 AA. AC O31463; Q7DL43; DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 27-MAY-2015, entry version 75. DE RecName: Full=Homocysteine S-methyltransferase YbgG; DE EC=2.1.1.10; DE AltName: Full=S-methylmethionine:homocysteine methyltransferase; GN Name=ybgG; OrderedLocusNames=BSU02410; 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=9455481; DOI=10.1093/dnares/4.5.329; RA Haga K., Liu H., Takahashi H., Yoshikawa H.; RT "Sequence analysis of a 45-kb segment in the 19 degrees-23 degrees RT region of the Bacillus subtilis chromosome containing glpT and mpr RT loci."; RL DNA Res. 4:329-333(1997). 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 DISRUPTION PHENOTYPE. RC STRAIN=168 / PY79; RX PubMed=11267663; DOI=10.1016/S0167-4781(01)00182-8; RA Yazgan A., Oezcengiz G., Marahiel M.A.; RT "Tn10 insertional mutations of Bacillus subtilis that block the RT biosynthesis of bacilysin."; RL Biochim. Biophys. Acta 1518:87-94(2001). CC -!- CATALYTIC ACTIVITY: S-methyl-L-methionine + L-homocysteine = 2 L- CC methionine. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00333}; CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show reduced CC bacilysin biosynthetic activity. {ECO:0000269|PubMed:11267663}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB006424; BAA33139.1; -; Genomic_DNA. DR EMBL; AL009126; CAB12035.1; -; Genomic_DNA. DR PIR; B69751; B69751. DR RefSeq; NP_388123.1; NC_000964.3. DR RefSeq; WP_003246467.1; NZ_JNCM01000030.1. DR ProteinModelPortal; O31463; -. DR SMR; O31463; 3-314. DR STRING; 224308.BSU02410; -. DR PaxDb; O31463; -. DR EnsemblBacteria; CAB12035; CAB12035; BSU02410. DR GeneID; 938412; -. DR KEGG; bsu:BSU02410; -. DR PATRIC; 18972031; VBIBacSub10457_0244. DR GenoList; BSU02410; -. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR InParanoid; O31463; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR PhylomeDB; O31463; -. DR BioCyc; BSUB:BSU02410-MONOMER; -. DR Proteomes; UP000001570; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Metal-binding; KW Methionine biosynthesis; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase; Zinc. FT CHAIN 1 315 Homocysteine S-methyltransferase YbgG. FT /FTId=PRO_0000379124. FT DOMAIN 2 309 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 229 229 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 294 294 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 295 295 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. SQ SEQUENCE 315 AA; 34736 MW; 01B6F2DD00180D67 CRC64; MNPIQHILDT YPLIVLDGAM ATELERKGCN LNDSLWSAKI LMEEPELIKQ VHTDYFAAGA DCAITASYQS TFEGFAARGL SEAEARRLIE LSVSIAAEAR DEFWSLEENR LNRPKPIIAA SIGPYGAYLA DGSEYRGNYA ISEDELIEFH RPRMKALIEA GADVLACETI PCLTEAKAIV RLLKEFPETY AWISFSAKDG LHISDGTPAA DCASWLDEHR QIAALGINCT PLQHIPSLIE ELKKNTSKPI IVYPNSGEQY DPETKTWNGA ACAESYGASA RTWHEKGARL IGGCCRTKPE NIQEIAAWAR SLKTT // ID HMT1_ARATH Reviewed; 326 AA. AC Q9SDL7; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 29-APR-2015, entry version 84. DE RecName: Full=Homocysteine S-methyltransferase 1; DE EC=2.1.1.10; DE AltName: Full=S-methylmethionine:homocysteine methyltransferase 1; DE Short=AtHMT-1; DE Short=SMM:Hcy S-methyltransferase 1; GN Name=HMT-1; OrderedLocusNames=At3g25900; ORFNames=MPE11.5, MPE11.6; 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 [GENOMIC DNA], ENZYME ACTIVITY, ENZYME REGULATION, RP AND SUBUNIT. RX PubMed=10747987; DOI=10.1074/jbc.M001116200; RA Ranocha P., Bourgis F., Ziemak M.J., Rhodes D., Gage D.A., RA Hanson A.D.; RT "Characterization and functional expression of cDNAs encoding RT methionine-sensitive and -insensitive homocysteine S- RT methyltransferases from Arabidopsis."; RL J. Biol. Chem. 275:15962-15968(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=10819329; DOI=10.1093/dnares/7.2.131; RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC RT clones."; RL DNA Res. 7:131-135(2000). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. RN [4] 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 [5] RP PROBABLE FUNCTION OF SMM CYCLE, BIOPHYSICOCHEMICAL PROPERTIES, AND RP TISSUE SPECIFICITY. RX PubMed=11309147; DOI=10.1046/j.1365-313x.2001.00988.x; RA Ranocha P., McNeil S.D., Ziemak M.J., Li C., Tarczynski M.C., RA Hanson A.D.; RT "The S-methylmethionine cycle in angiosperms: ubiquity, antiquity and RT activity."; RL Plant J. 25:575-584(2001). CC -!- FUNCTION: Catalyzes methyl transfer from S-methylmethionine (SMM) CC to adenosyl-L-homocysteine (AdoMet). SMM degradation (by HMT-1, CC HMT-2 and HMT-3) and biosynthesis (by MMT1) constitute the SMM CC cycle in plants, which is probably required to achieve short term CC control of AdoMet level. CC -!- CATALYTIC ACTIVITY: S-methyl-L-methionine + L-homocysteine = 2 L- CC methionine. {ECO:0000269|PubMed:10747987}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00333}; CC -!- ENZYME REGULATION: Strongly inhibited by methionine. CC {ECO:0000269|PubMed:10747987}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=29 uM for S-methylmethionine {ECO:0000269|PubMed:11309147}; CC KM=1950 uM for (S,S)-AdoMet {ECO:0000269|PubMed:11309147}; CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10747987}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=1; CC Comment=A number of isoforms are produced. According to EST CC sequences.; CC Name=1; CC IsoId=Q9SDL7-1; Sequence=Displayed; CC -!- TISSUE SPECIFICITY: Expressed predominantly in roots. Expressed in CC rosette leaves, cauline leaves and developing seeds. CC {ECO:0000269|PubMed:11309147}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF219222; AAF23821.1; -; Genomic_DNA. DR EMBL; AB023041; BAB01052.1; -; Genomic_DNA. DR EMBL; CP002686; AEE77087.1; -; Genomic_DNA. DR EMBL; AY065163; AAL38339.1; -; mRNA. DR EMBL; AY081604; AAM10166.1; -; mRNA. DR PIR; T51941; T51941. DR RefSeq; NP_189219.1; NM_113493.4. [Q9SDL7-1] DR UniGene; At.23868; -. DR ProteinModelPortal; Q9SDL7; -. DR SMR; Q9SDL7; 22-326. DR BioGrid; 7517; 1. DR IntAct; Q9SDL7; 1. DR PaxDb; Q9SDL7; -. DR PRIDE; Q9SDL7; -. DR EnsemblPlants; AT3G25900.1; AT3G25900.1; AT3G25900. [Q9SDL7-1] DR GeneID; 822186; -. DR KEGG; ath:AT3G25900; -. DR TAIR; AT3G25900; -. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; AINDPLW; -. DR PhylomeDB; Q9SDL7; -. DR BioCyc; ARA:AT3G25900-MONOMER; -. DR BioCyc; ARA:GQT-1769-MONOMER; -. DR BioCyc; ARA:GQT-1770-MONOMER; -. DR BRENDA; 2.1.1.10; 399. DR SABIO-RK; Q9SDL7; -. DR PRO; PR:Q9SDL7; -. DR Proteomes; UP000006548; Chromosome 3. DR ExpressionAtlas; Q9SDL7; baseline and differential. DR Genevestigator; Q9SDL7; -. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IDA:TAIR. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IDA:TAIR. DR GO; GO:0033528; P:S-methylmethionine cycle; IBA:GO_Central. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 1: Evidence at protein level; KW Alternative splicing; Amino-acid biosynthesis; Complete proteome; KW Metal-binding; Methionine biosynthesis; Methyltransferase; KW Reference proteome; S-adenosyl-L-methionine; Transferase; Zinc. FT CHAIN 1 326 Homocysteine S-methyltransferase 1. FT /FTId=PRO_0000114611. FT DOMAIN 9 323 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 241 241 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 308 308 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 309 309 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. SQ SEQUENCE 326 AA; 35980 MW; EBE5F904FDA8DC99 CRC64; MVLEKKSALL EDLIKKCGGC AVVDGGFATQ LEIHGAAIND PLWSAVSLIK NPELIKRVHM EYLEAGADIV VTSSYQATIP GFLSRGLSIE ESESLLQKSV ELAVEARDRF WEKVSKVSGH SYNRALVAAS IGSYGAYLAD GSEYSGHYGE NVSLDKLKDF HRRRLQVLVE AGPDLLAFET IPNKLEAQAC VELLEEEKVQ IPAWICFTSV DGEKAPSGES FEECLEPLNK SNNIYAVGIN CAPPQFIENL IRKFAKLTKK AIVVYPNSGE VWDGKAKQWL PSQCFGDDEF EMFATKWRDL GAKLIGGCCR TTPSTINAIS RDLKRR // ID HMT1_BRAOT Reviewed; 326 AA. AC A4ZGQ8; DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2007, sequence version 1. DT 01-APR-2015, entry version 24. DE RecName: Full=Homocysteine S-methyltransferase 1; DE Short=BoHMT1; DE EC=2.1.1.10; GN Name=HMT1; OS Brassica oleracea var. italica (Broccoli). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Brassiceae; OC Brassica. OX NCBI_TaxID=36774; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, RP BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, TISSUE SPECIFICITY, RP AND INDUCTION BY SELENATE. RC STRAIN=cv. Green comet; RX PubMed=17391716; DOI=10.1016/j.phytochem.2007.02.007; RA Lyi S.M., Zhou X., Kochian L.V., Li L.; RT "Biochemical and molecular characterization of the homocysteine S- RT methyltransferase from broccoli (Brassica oleracea var. italica)."; RL Phytochemistry 68:1112-1119(2007). CC -!- FUNCTION: Catalyzes methyl transfer from S-methylmethionine to CC homocysteine. The highest preference is for DL-homocysteine >> DL- CC cysteine. Has no selenocysteine methyltransferase activity. CC {ECO:0000269|PubMed:17391716}. CC -!- CATALYTIC ACTIVITY: S-methyl-L-methionine + L-homocysteine = 2 L- CC methionine. {ECO:0000269|PubMed:17391716}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00333}; CC -!- ENZYME REGULATION: Inhibited by L-methionine. CC {ECO:0000269|PubMed:17391716}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=72 uM for DL-homocysteine {ECO:0000269|PubMed:17391716}; CC pH dependence: CC Optimum pH is 7.2. {ECO:0000269|PubMed:17391716}; CC -!- TISSUE SPECIFICITY: Expressed in roots, young leaves, florets and CC flowers. Not detected in old leaves. CC {ECO:0000269|PubMed:17391716}. CC -!- INDUCTION: Not induced by selenate or selenite. Up-regulated by CC sulfate. Not affected by the status of methionine, s- CC methylmethionine or homocysteine, or by cadmium. CC {ECO:0000269|PubMed:17391716}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DQ679980; ABG74913.1; -; mRNA. DR BioCyc; MetaCyc:MONOMER-15250; -. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR GO; GO:0032259; P:methylation; IDA:UniProtKB. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 1: Evidence at protein level; KW Metal-binding; Methyltransferase; Transferase; Zinc. FT CHAIN 1 326 Homocysteine S-methyltransferase 1. FT /FTId=PRO_0000409376. FT DOMAIN 9 323 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 241 241 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 308 308 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 309 309 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. SQ SEQUENCE 326 AA; 35817 MW; E7B32300AE2FB4A2 CRC64; MGLEKKSALL EDLIEKCGGC AVVDGGFATQ LEIHGAAIND PLWSAVSLIK DPELIKRVHM EYLEAGADVV VTSSYQATIP GFLSRGLSME ESESLLQKSV KLAVEARDRF WDKVSKTSGH SYNRALVAAS IGSYGAYLAD GSEYSGSYGE DVSLDKLKDF HRRRIQVLVE ASPDLLAFET IPNKLEAQAC VELLEEENVQ IPAWICFTSV DGENAPSGES FQECLETLNK SNNICAVGIN CAPPQFMDNL IRKFSKLTQK AIVVYPNSGE VWDGKAKKWL PSQCFGDAEF EMFATKWRDL GAKLIGGCCR TTPSTIKAIS RDLKRR // ID HMT1_MAIZE Reviewed; 323 AA. AC Q9FUN0; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAY-2015, entry version 62. DE RecName: Full=Homocysteine S-methyltransferase 1; DE EC=2.1.1.10; DE AltName: Full=S-methylmethionine:homocysteine methyltransferase 1; DE Short=SMM:Hcy S-methyltransferase 1; DE AltName: Full=ZmHMT-1; GN Name=HMT-1; 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 [MRNA]. RX PubMed=11309147; DOI=10.1046/j.1365-313x.2001.00988.x; RA Ranocha P., McNeil S.D., Ziemak M.J., Li C., Tarczynski M.C., RA Hanson A.D.; RT "The S-methylmethionine cycle in angiosperms: ubiquity, antiquity and RT activity."; RL Plant J. 25:575-584(2001). CC -!- FUNCTION: Catalyzes methyl transfer from S-methylmethionine (SMM) CC to adenosyl-L-homocysteine (AdoMet). SMM degradation (by HMT-1, CC HMT-2, HMT-3 and HMT-4) and biosynthesis (by MMT1) constitute the CC SMM cycle in plants, which is probably required to achieve short CC term control of AdoMet level (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: S-methyl-L-methionine + L-homocysteine = 2 L- CC methionine. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00333}; CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF297044; AAG22537.1; -; mRNA. DR RefSeq; NP_001105011.1; NM_001111541.1. DR UniGene; Zm.13424; -. DR ProteinModelPortal; Q9FUN0; -. DR EnsemblPlants; GRMZM6G310687_T01; GRMZM6G310687_P02; GRMZM6G310687. DR GeneID; 541873; -. DR KEGG; zma:541873; -. DR Gramene; Q9FUN0; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR Proteomes; UP000007305; Chromosome 9. DR ExpressionAtlas; Q9FUN0; baseline and differential. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Amino-acid biosynthesis; Complete proteome; Metal-binding; KW Methionine biosynthesis; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase; Zinc. FT CHAIN 1 323 Homocysteine S-methyltransferase 1. FT /FTId=PRO_0000114614. FT DOMAIN 3 317 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 235 235 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 302 302 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 303 303 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. SQ SEQUENCE 323 AA; 34927 MW; 1B1B8F19DA0B743D CRC64; MGVLEDLVAR AGGCAVIDGG FATQLEALGA DINDPLWSAA CLITRPHLVK EVHMQYLEAG ADVIISSSYQ ATIPGFIARG MSVAEAEDLL RTSVKLANEA RDEFWKSTLR KSKPIYNRAL VAASIGSYGA YLADGSEYSG SYGADITAEK LKDFHRRRLQ VLASAGPDLI AFEAIPNQME AQALVELLEE EKVQIPSWIC FSSVDGKNLC SGESFADCLK ILNASEKVAV VGVNCTPPQF IEGIICEFRK QTKKAIAVYP NSGEVWDGRA KRWLPVECLG HKSFDALAKR WQEAGASLIG GCCRTTPSTI RAVSKILKGR TGH // ID HMT2_ARATH Reviewed; 333 AA. AC Q9M1W4; Q9SDL6; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 29-APR-2015, entry version 82. DE RecName: Full=Homocysteine S-methyltransferase 2; DE EC=2.1.1.10; DE AltName: Full=S-methylmethionine:homocysteine methyltransferase 2; DE Short=AtHMT-2; DE Short=SMM:Hcy S-methyltransferase 2; GN Name=HMT-2; OrderedLocusNames=At3g63250; ORFNames=F16M2.100; 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 [GENOMIC DNA], ENZYME ACTIVITY, AND SUBUNIT. RX PubMed=10747987; DOI=10.1074/jbc.M001116200; RA Ranocha P., Bourgis F., Ziemak M.J., Rhodes D., Gage D.A., RA Hanson A.D.; RT "Characterization and functional expression of cDNAs encoding RT methionine-sensitive and -insensitive homocysteine S- RT methyltransferases from Arabidopsis."; RL J. Biol. Chem. 275:15962-15968(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=11130713; DOI=10.1038/35048706; RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., RA Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., RA Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., RA De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P., RA Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., RA Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., RA Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., RA Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., RA Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., RA Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., RA Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., RA Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., RA Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., RA Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., RA Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., RA Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., RA Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., RA Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., RA Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., RA Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., RA Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., RA Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis RT thaliana."; RL Nature 408:820-822(2000). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. RN [4] 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 [5] RP PROBABLE FUNCTION OF SMM CYCLE, BIOPHYSICOCHEMICAL PROPERTIES, AND RP TISSUE SPECIFICITY. RX PubMed=11309147; DOI=10.1046/j.1365-313x.2001.00988.x; RA Ranocha P., McNeil S.D., Ziemak M.J., Li C., Tarczynski M.C., RA Hanson A.D.; RT "The S-methylmethionine cycle in angiosperms: ubiquity, antiquity and RT activity."; RL Plant J. 25:575-584(2001). CC -!- FUNCTION: Catalyzes methyl transfer from S-methylmethionine (SMM) CC to adenosyl-L-homocysteine (AdoMet). SMM degradation (by HMT-1, CC HMT-2 and HMT-3) and biosynthesis (by MMT1) constitute the SMM CC cycle in plants, which is probably required to achieve short term CC control of AdoMet level. CC -!- CATALYTIC ACTIVITY: S-methyl-L-methionine + L-homocysteine = 2 L- CC methionine. {ECO:0000269|PubMed:10747987}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00333}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=50 uM for S-methylmethionine {ECO:0000269|PubMed:11309147}; CC KM=225 uM for (S,S)-AdoMet {ECO:0000269|PubMed:11309147}; CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10747987}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=1; CC Comment=A number of isoforms are produced. According to EST CC sequences.; CC Name=1; CC IsoId=Q9M1W4-1; Sequence=Displayed; CC -!- TISSUE SPECIFICITY: Expressed predominantly in roots. Expressed in CC rosette leaves, cauline leaves and developing seeds. CC {ECO:0000269|PubMed:11309147}. CC -!- MISCELLANEOUS: In contrast to HMT-1, it is not inhibited by CC methionine. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF219223; AAF23822.1; -; Genomic_DNA. DR EMBL; AL138648; CAB86426.1; -; Genomic_DNA. DR EMBL; CP002686; AEE80456.1; -; Genomic_DNA. DR EMBL; AF428402; AAL16170.1; -; mRNA. DR EMBL; BT010165; AAQ22634.1; -; mRNA. DR PIR; T48114; T48114. DR PIR; T51939; T51939. DR RefSeq; NP_191884.1; NM_116190.4. [Q9M1W4-1] DR UniGene; At.21554; -. DR ProteinModelPortal; Q9M1W4; -. DR SMR; Q9M1W4; 21-333. DR PaxDb; Q9M1W4; -. DR PRIDE; Q9M1W4; -. DR DNASU; 825500; -. DR EnsemblPlants; AT3G63250.1; AT3G63250.1; AT3G63250. [Q9M1W4-1] DR GeneID; 825500; -. DR KEGG; ath:AT3G63250; -. DR TAIR; AT3G63250; -. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR InParanoid; Q9M1W4; -. DR KO; K00547; -. DR OMA; SEWCKDG; -. DR PhylomeDB; Q9M1W4; -. DR BioCyc; ARA:AT3G63250-MONOMER; -. DR BioCyc; ARA:GQT-156-MONOMER; -. DR BRENDA; 2.1.1.10; 399. DR SABIO-RK; Q9M1W4; -. DR PRO; PR:Q9M1W4; -. DR Proteomes; UP000006548; Chromosome 3. DR ExpressionAtlas; Q9M1W4; baseline and differential. DR Genevestigator; Q9M1W4; -. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IDA:TAIR. DR GO; GO:0009086; P:methionine biosynthetic process; IDA:TAIR. DR GO; GO:0033528; P:S-methylmethionine cycle; IMP:TAIR. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 1: Evidence at protein level; KW Alternative splicing; Amino-acid biosynthesis; Complete proteome; KW Metal-binding; Methionine biosynthesis; Methyltransferase; KW Reference proteome; S-adenosyl-L-methionine; Transferase; Zinc. FT CHAIN 1 333 Homocysteine S-methyltransferase 2. FT /FTId=PRO_0000114612. FT DOMAIN 8 327 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 245 245 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 312 312 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 313 313 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT CONFLICT 103 103 T -> C (in Ref. 1; AAF23822). FT {ECO:0000305}. SQ SEQUENCE 333 AA; 36451 MW; CB44D8F3BAC15D85 CRC64; MTGNSFNSMK DFLKQTGGYA VIDGGLATEF ERHGADLNDP LWSAKCLVTS PHLIHTVHLD YLEAGADIIS SASYQATIQG FEAKGFSREE SESLLKKSVE IATEARNSYY DKCGTSSSMD DKILKKRPIL VAASVGSYGA YLADGSEYSG IYGDSITLEK LKDFHRRRLQ VLAESGADLI AFETIPNKIE AQAFADLLEE GDVKIPGWFS FNSKDGVNVV SGDSIKECIS IAENCEKVVA VGINCTPPRF IEGLVLEIEK VTSKPILVYP NSGESYDADR KEWVENTGVG DEDFVSYVEK WMDAGVSLLG GCCRTTPTTI RAIHKRLVNR RSL // ID HMT2_MAIZE Reviewed; 339 AA. AC Q9FUM9; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 01-APR-2015, entry version 60. DE RecName: Full=Homocysteine S-methyltransferase 2; DE EC=2.1.1.10; DE AltName: Full=S-methylmethionine:homocysteine methyltransferase 2; DE Short=SMM:Hcy S-methyltransferase 2; DE AltName: Full=ZmHMT-2; GN Name=HMT-2; 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 [MRNA]. RX PubMed=11309147; DOI=10.1046/j.1365-313x.2001.00988.x; RA Ranocha P., McNeil S.D., Ziemak M.J., Li C., Tarczynski M.C., RA Hanson A.D.; RT "The S-methylmethionine cycle in angiosperms: ubiquity, antiquity and RT activity."; RL Plant J. 25:575-584(2001). CC -!- FUNCTION: Catalyzes methyl transfer from S-methylmethionine (SMM) CC to adenosyl-L-homocysteine (AdoMet). SMM degradation (by HMT-1, CC HMT-2, HMT-3 and HMT-4) and biosynthesis (by MMT1) constitute the CC SMM cycle in plants, which is probably required to achieve short CC term control of AdoMet level (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: S-methyl-L-methionine + L-homocysteine = 2 L- CC methionine. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00333}; CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF297045; AAG22538.1; -; mRNA. DR RefSeq; NP_001105012.1; NM_001111542.1. DR UniGene; Zm.529; -. DR ProteinModelPortal; Q9FUM9; -. DR EnsemblPlants; GRMZM2G117240_T01; GRMZM2G117240_P01; GRMZM2G117240. DR GeneID; 541874; -. DR KEGG; zma:541874; -. DR Gramene; Q9FUM9; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; SSVEGFM; -. DR Proteomes; UP000007305; Chromosome 1. DR ExpressionAtlas; Q9FUM9; baseline and differential. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Amino-acid biosynthesis; Complete proteome; Metal-binding; KW Methionine biosynthesis; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase; Zinc. FT CHAIN 1 339 Homocysteine S-methyltransferase 2. FT /FTId=PRO_0000114615. FT DOMAIN 12 326 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 244 244 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 311 311 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 312 312 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. SQ SEQUENCE 339 AA; 36959 MW; 12B2144B5501F51D CRC64; MVVTAAGSAE EAVRRWVDAA GGRLVLDGGL ATELEANGAD LNDPLWSAKC LLSSPHLIRK VHMDYLEAGA NIIITASYQA TIQGFESKGF SKEQSENLLT KSVEIALEAR EMFLKEHLEK STPIQHPVLV AASLGSYGAY LADGSEYSGD YGEAGTKEFL KDFHRRRLQV LAEAGPDLIA FETIPNKLEA EAYVELLEEC NINIPAWFSF NSKDGVHIVS GDSLIECTTI ADKCAKVGAV GINCTPPRFI HGLILSIRKV TDKPILIYPN SGERYDGEKK EWVESTGVSD GDFVSYVNEW CKDGAVLIGG CCRTTPNTIR AIHRTLNKSP NKQQLPAVE // ID HMT3_ARATH Reviewed; 347 AA. AC Q8LAX0; Q9LUI7; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 2. DT 29-APR-2015, entry version 83. DE RecName: Full=Homocysteine S-methyltransferase 3; DE EC=2.1.1.10; DE AltName: Full=S-methylmethionine:homocysteine methyltransferase 3; DE Short=AtHMT-3; DE Short=SMM:Hcy S-methyltransferase 3; GN Name=HMT3; OrderedLocusNames=At3g22740; ORFNames=MWI23.11; 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 [MRNA], ENZYME ACTIVITY, PROBABLE FUNCTION OF SMM RP CYCLE, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY. RC STRAIN=cv. Columbia; TISSUE=Leaf; RX PubMed=11309147; DOI=10.1046/j.1365-313x.2001.00988.x; RA Ranocha P., McNeil S.D., Ziemak M.J., Li C., Tarczynski M.C., RA Hanson A.D.; RT "The S-methylmethionine cycle in angiosperms: ubiquity, antiquity and RT activity."; RL Plant J. 25:575-584(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=10819329; DOI=10.1093/dnares/7.2.131; RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC RT clones."; RL DNA Res. 7:131-135(2000). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX PubMed=11910074; DOI=10.1126/science.1071006; RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., RA Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., RA Shibata K., Shinagawa A., Shinozaki K.; RT "Functional annotation of a full-length Arabidopsis cDNA collection."; RL Science 296:141-145(2002). RN [5] 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., RA Feldmann K.A.; RT "Full-length cDNA from Arabidopsis thaliana."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes methyl transfer from S-methylmethionine (SMM) CC to adenosyl-L-homocysteine (AdoMet). SMM degradation (by HMT-1, CC HMT-2 and HMT-3) and biosynthesis (by MMT1) constitute the SMM CC cycle in plants, which is probably required to achieve short term CC control of AdoMet level. CC -!- CATALYTIC ACTIVITY: S-methyl-L-methionine + L-homocysteine = 2 L- CC methionine. {ECO:0000269|PubMed:11309147}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00333}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=335 uM for S-methylmethionine {ECO:0000269|PubMed:11309147}; CC KM=1760 uM for (S,S)-AdoMet {ECO:0000269|PubMed:11309147}; CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Expressed predominantly in rosette leaves. CC Expressed in roots, cauline leaves and developing seeds. CC {ECO:0000269|PubMed:11309147}. CC -!- MISCELLANEOUS: In contrast to HMT-1, it is not inhibited by CC methionine. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF297394; AAG10301.1; -; mRNA. DR EMBL; AB022223; BAB01249.1; -; Genomic_DNA. DR EMBL; CP002686; AEE76672.1; -; Genomic_DNA. DR EMBL; AK118021; BAC42654.1; -; mRNA. DR EMBL; BT005318; AAO63382.1; -; mRNA. DR EMBL; AY087554; AAM65096.1; -; mRNA. DR RefSeq; NP_566715.1; NM_113173.2. DR UniGene; At.6305; -. DR ProteinModelPortal; Q8LAX0; -. DR SMR; Q8LAX0; 6-344. DR STRING; 3702.AT3G22740.1-P; -. DR PaxDb; Q8LAX0; -. DR PRIDE; Q8LAX0; -. DR EnsemblPlants; AT3G22740.1; AT3G22740.1; AT3G22740. DR GeneID; 821845; -. DR KEGG; ath:AT3G22740; -. DR TAIR; AT3G22740; -. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR InParanoid; Q8LAX0; -. DR KO; K00547; -. DR OMA; YGRSVTK; -. DR PhylomeDB; Q8LAX0; -. DR BioCyc; ARA:AT3G22740-MONOMER; -. DR BRENDA; 2.1.1.10; 399. DR SABIO-RK; Q8LAX0; -. DR PRO; PR:Q8LAX0; -. DR Proteomes; UP000006548; Chromosome 3. DR Genevestigator; Q8LAX0; -. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IDA:TAIR. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IBA:GO_Central. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0033528; P:S-methylmethionine cycle; IBA:GO_Central. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 1: Evidence at protein level; KW Amino-acid biosynthesis; Complete proteome; Metal-binding; KW Methionine biosynthesis; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase; Zinc. FT CHAIN 1 347 Homocysteine S-methyltransferase 3. FT /FTId=PRO_0000114613. FT DOMAIN 12 333 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 251 251 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 318 318 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 319 319 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT CONFLICT 24 24 A -> E (in Ref. 6; AAM65096). FT {ECO:0000305}. FT CONFLICT 45 45 L -> I (in Ref. 6; AAM65096). FT {ECO:0000305}. FT CONFLICT 117 117 C -> W (in Ref. 6; AAM65096). FT {ECO:0000305}. SQ SEQUENCE 347 AA; 37882 MW; 45CDC34973F820CC CRC64; MGSFVKEETS SLMTDFLEKC GGYAVVDGGF ATELQRHGAD INDPLWSAKC LITSPHLVTK VHLDYLESGA NIIITASYQA TIQGFVAKGL SVGEAENLLR RSVEITYEAR EIFYNRCTKG SWDFAYAGKA SRRPILVAAS VGSYGAYLAD GSEYSGIYGD SVSKETLKDF HRRRVQILAK SGADLIAFET IPNKLEAEAY ADLLEEEDID IPAWFSFTSK DGVSVPRGDS VVECAKVADS CKNVVAIGIN CTAPRYIHAL IISLRQMTRK PIVVYPNSGE VYDGLNKKWI KSEGESEEDF VSYVSKWRDA GASLFGGCCR TTPNTIRAIA KVLSDEPSAA SKPKFGQ // ID HMT3_MAIZE Reviewed; 338 AA. AC Q9FUM8; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 04-MAR-2015, entry version 59. DE RecName: Full=Homocysteine S-methyltransferase 3; DE EC=2.1.1.10; DE AltName: Full=S-methylmethionine:homocysteine methyltransferase 3; DE Short=SMM:Hcy S-methyltransferase 3; DE AltName: Full=ZmHMT-3; GN Name=HMT-3; 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 [MRNA]. RX PubMed=11309147; DOI=10.1046/j.1365-313x.2001.00988.x; RA Ranocha P., McNeil S.D., Ziemak M.J., Li C., Tarczynski M.C., RA Hanson A.D.; RT "The S-methylmethionine cycle in angiosperms: ubiquity, antiquity and RT activity."; RL Plant J. 25:575-584(2001). CC -!- FUNCTION: Catalyzes methyl transfer from S-methylmethionine (SMM) CC to adenosyl-L-homocysteine (AdoMet). SMM degradation (by HMT-1, CC HMT-2, HMT-3 and HMT-4) and biosynthesis (by MMT1) constitute the CC SMM cycle in plants, which is probably required to achieve short CC term control of AdoMet level (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: S-methyl-L-methionine + L-homocysteine = 2 L- CC methionine. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00333}; CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF297046; AAG22539.1; -; mRNA. DR RefSeq; NP_001105013.1; NM_001111543.1. DR UniGene; Zm.530; -. DR ProteinModelPortal; Q9FUM8; -. DR EnsemblPlants; GRMZM2G152470_T01; GRMZM2G152470_P01; GRMZM2G152470. DR GeneID; 541875; -. DR KEGG; zma:541875; -. DR Gramene; Q9FUM8; -. DR KO; K00547; -. DR OMA; SEWCKDG; -. DR Proteomes; UP000007305; Chromosome 3. DR ExpressionAtlas; Q9FUM8; baseline. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Amino-acid biosynthesis; Complete proteome; Metal-binding; KW Methionine biosynthesis; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase; Zinc. FT CHAIN 1 338 Homocysteine S-methyltransferase 3. FT /FTId=PRO_0000114616. FT DOMAIN 12 326 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 244 244 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 311 311 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 312 312 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. SQ SEQUENCE 338 AA; 36757 MW; 9C787F9F10D794E2 CRC64; MVGTAEGGAE RAVRRWVDAA GGRLVLDGGL ATELEANGAD LNDPLWSAKC LLSSPHLIRK VHMDYLEAGA NIIITASYQA TIQGFESKGF SKEQSENLLT KSVQIALEAR EMFLKEHLEK STPIQHPILV AAALGSYGAY LADGSEYSGD YGEAGTKEFL KDFHRRRLQV LAEAGPDLIA FETIPNKLEA QAYVELLEEC NINIPSWLSF NSKDGVHVVS GDSLIECATI ADKCAKVGAV GINCTPPRFI HGLILSIRKV TDKPILIYPN SGERYDGEKK EWVESTGVSD GDFVSYVNEW CKDGAALIGG CCRTTPNTIR AIHRTLNQGC HKHQLPVA // ID HMT4_MAIZE Reviewed; 342 AA. AC Q9FUM7; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 04-FEB-2015, entry version 54. DE RecName: Full=Homocysteine S-methyltransferase 4; DE EC=2.1.1.10; DE AltName: Full=S-methylmethionine:homocysteine methyltransferase 4; DE Short=SMM:Hcy S-methyltransferase 4; DE AltName: Full=ZmHMT-4; GN Name=HMT-4; 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 [MRNA]. RX PubMed=11309147; DOI=10.1046/j.1365-313x.2001.00988.x; RA Ranocha P., McNeil S.D., Ziemak M.J., Li C., Tarczynski M.C., RA Hanson A.D.; RT "The S-methylmethionine cycle in angiosperms: ubiquity, antiquity and RT activity."; RL Plant J. 25:575-584(2001). CC -!- FUNCTION: Catalyzes methyl transfer from S-methylmethionine (SMM) CC to adenosyl-L-homocysteine (AdoMet). SMM degradation (by HMT-1, CC HMT-2, HMT-3 and HMT-4) and biosynthesis (by MMT1) constitute the CC SMM cycle in plants, which is probably required to achieve short CC term control of AdoMet level (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: S-methyl-L-methionine + L-homocysteine = 2 L- CC methionine. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00333}; CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF297047; AAG22540.1; -; mRNA. DR RefSeq; NP_001105014.1; NM_001111544.1. DR UniGene; Zm.2414; -. DR ProteinModelPortal; Q9FUM7; -. DR GeneID; 541876; -. DR KEGG; zma:541876; -. DR Gramene; Q9FUM7; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR Proteomes; UP000007305; Unplaced. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Amino-acid biosynthesis; Complete proteome; Metal-binding; KW Methionine biosynthesis; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase; Zinc. FT CHAIN 1 342 Homocysteine S-methyltransferase 4. FT /FTId=PRO_0000114617. FT DOMAIN 13 328 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 245 245 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 313 313 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 314 314 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. SQ SEQUENCE 342 AA; 36460 MW; 922EE23117D10FBB CRC64; MWFGGGPIDA AGALRGFVRE AGGCAVVDGG LGTELEAHGA DLHDALWSAK CLASAPHLIR KVHLDYLEAG ADVIISASYQ ATIEGFQSRG FSRDESEELL RRSVHVAQEA RRVFAAEGDR SSRRGRPPAL VAASVGSYGA YRADGSEYSG DYGKSMTKED LKNFHRRRLQ VLAGAGPDLI AFETIPNKLE AQVYAELLEE NGIRIPAWFS FTSKDGVNAA SGDPINECAA VADSCPRVDA VGVNCTAPRF IHGLILSIKK VTSKPIVVYP NSGETYVAET NEWVDSDGAT GTDDFVSRVG EWRRAGAALI GGCCRTSPAT VRAIARAVRE AEYDDIPAVA VL // ID I0AJS7_IGNAJ Unreviewed; 296 AA. AC I0AJS7; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Betaine-homocysteine S-methyltransferase {ECO:0000313|EMBL:AFH49234.1}; GN OrderedLocusNames=IALB_1526 {ECO:0000313|EMBL:AFH49234.1}; OS Ignavibacterium album (strain DSM 19864 / JCM 16511 / NBRC 101810 / OS Mat9-16). OC Bacteria; Ignavibacteriae; Ignavibacteria; Ignavibacteriales; OC Ignavibacteriaceae; Ignavibacterium. OX NCBI_TaxID=945713 {ECO:0000313|EMBL:AFH49234.1, ECO:0000313|Proteomes:UP000007394}; RN [1] {ECO:0000313|EMBL:AFH49234.1, ECO:0000313|Proteomes:UP000007394} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19864 / JCM 16511 / NBRC 101810 / Mat9-16 RC {ECO:0000313|Proteomes:UP000007394}; RX PubMed=22661972; DOI=10.3389/fmicb.2012.00185; RA Liu Z., Frigaard N.-U., Vogl K., Iino T., Ohkuma M., Overmann J., RA Bryant D.A.; RT "Complete genome of Ignavibacterium album, a metabolically versatile, RT flagellated, facultative anaerobe from the phylum Chlorobi."; RL Front. Microbiol. 3:185-185(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; CP003418; AFH49234.1; -; Genomic_DNA. DR RefSeq; WP_014560387.1; NC_017464.1. DR RefSeq; YP_005846502.1; NC_017464.1. DR EnsemblBacteria; AFH49234; AFH49234; IALB_1526. DR KEGG; ial:IALB_1526; -. DR KO; K00547; -. DR OMA; HISEGIN; -. DR BioCyc; IALB945713:GLEW-1550-MONOMER; -. DR Proteomes; UP000007394; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007394}; KW Methyltransferase {ECO:0000313|EMBL:AFH49234.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007394}; KW Transferase {ECO:0000313|EMBL:AFH49234.1}. SQ SEQUENCE 296 AA; 33357 MW; 6832B6C205FCF916 CRC64; MNLLSEFNIF SFSKKIKRPL VLDGAMGSFL EKMGLTETDN AWSAKANIKY PDKVLKIHRS YIEAGADVIT TNTFRTNPYS LGQVGIKNFE RYVKKAISLA FEAKENLPVL IAGSNAPAED CYQVQRTITK KQLELNHRCH IDSLIDNGCH FILNETQGHF DEIKIISKHC EKYEIPFVMS LYFDENLCLL SGEKVSDVIN FLNDTNVLSL GFNCISDKIL IKLINQISMP ANWGFYLNCF STSEKQSKVC SISVAEYLAI VQEVIHFNPS FIGACCGSNP EFIKAIKGFL DGRIKH // ID I0AKL8_IGNAJ Unreviewed; 297 AA. AC I0AKL8; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Methionine synthase I methyltransferase subunit {ECO:0000313|EMBL:AFH49525.1}; GN Name=metH {ECO:0000313|EMBL:AFH49525.1}; GN OrderedLocusNames=IALB_1818 {ECO:0000313|EMBL:AFH49525.1}; OS Ignavibacterium album (strain DSM 19864 / JCM 16511 / NBRC 101810 / OS Mat9-16). OC Bacteria; Ignavibacteriae; Ignavibacteria; Ignavibacteriales; OC Ignavibacteriaceae; Ignavibacterium. OX NCBI_TaxID=945713 {ECO:0000313|EMBL:AFH49525.1, ECO:0000313|Proteomes:UP000007394}; RN [1] {ECO:0000313|EMBL:AFH49525.1, ECO:0000313|Proteomes:UP000007394} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19864 / JCM 16511 / NBRC 101810 / Mat9-16 RC {ECO:0000313|Proteomes:UP000007394}; RX PubMed=22661972; DOI=10.3389/fmicb.2012.00185; RA Liu Z., Frigaard N.-U., Vogl K., Iino T., Ohkuma M., Overmann J., RA Bryant D.A.; RT "Complete genome of Ignavibacterium album, a metabolically versatile, RT flagellated, facultative anaerobe from the phylum Chlorobi."; RL Front. Microbiol. 3:185-185(2012). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003418; AFH49525.1; -; Genomic_DNA. DR RefSeq; WP_014560676.1; NC_017464.1. DR RefSeq; YP_005846793.1; NC_017464.1. DR EnsemblBacteria; AFH49525; AFH49525; IALB_1818. DR KEGG; ial:IALB_1818; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR BioCyc; IALB945713:GLEW-1848-MONOMER; -. DR Proteomes; UP000007394; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007394}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:AFH49525.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007394}; KW Transferase {ECO:0000313|EMBL:AFH49525.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 209 209 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 275 275 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 276 276 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 297 AA; 32349 MW; 4E8C5E4143AA4625 CRC64; MKKFFEQLDN KKILVSDGAW GTELFKLGLR SGECPELWNE TNREVILKIA KSYISAGSDI ISTNSFGGSS IKLSHYNLDN KTYELNKIAA EISREAAGDK LVMGSVGPTG KFLMTGDISS EELIESFTLQ TKALLDGGVD AILLETFYDI DEAECAIKAV KDFPDVPLIC SFTYDRNSSG EYRTMMGSTP KDVLQAMITL GVDVIGVNCG SGYNSMIDLV KELRGFSHNI PLLVQPNAGL PETIESNIVY SETSEAIINS VKSFLSIGIN IIGGCCGTTP EHIKIIRKTV DEFLSNV // ID I0API8_IGNAJ Unreviewed; 1397 AA. AC I0API8; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AFH50895.1}; GN Name=metH {ECO:0000313|EMBL:AFH50895.1}; GN OrderedLocusNames=IALB_3192 {ECO:0000313|EMBL:AFH50895.1}; OS Ignavibacterium album (strain DSM 19864 / JCM 16511 / NBRC 101810 / OS Mat9-16). OC Bacteria; Ignavibacteriae; Ignavibacteria; Ignavibacteriales; OC Ignavibacteriaceae; Ignavibacterium. OX NCBI_TaxID=945713 {ECO:0000313|EMBL:AFH50895.1, ECO:0000313|Proteomes:UP000007394}; RN [1] {ECO:0000313|EMBL:AFH50895.1, ECO:0000313|Proteomes:UP000007394} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19864 / JCM 16511 / NBRC 101810 / Mat9-16 RC {ECO:0000313|Proteomes:UP000007394}; RX PubMed=22661972; DOI=10.3389/fmicb.2012.00185; RA Liu Z., Frigaard N.-U., Vogl K., Iino T., Ohkuma M., Overmann J., RA Bryant D.A.; RT "Complete genome of Ignavibacterium album, a metabolically versatile, RT flagellated, facultative anaerobe from the phylum Chlorobi."; RL Front. Microbiol. 3:185-185(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; CP003418; AFH50895.1; -; Genomic_DNA. DR RefSeq; WP_014562029.1; NC_017464.1. DR RefSeq; YP_005848163.1; NC_017464.1. DR EnsemblBacteria; AFH50895; AFH50895; IALB_3192. DR KEGG; ial:IALB_3192; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; IALB945713:GLEW-3231-MONOMER; -. DR Proteomes; UP000007394; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR007569; DUF559. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF04480; DUF559; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF52980; SSF52980; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007394}; KW Methyltransferase {ECO:0000313|EMBL:AFH50895.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007394}; KW Transferase {ECO:0000313|EMBL:AFH50895.1}. SQ SEQUENCE 1397 AA; 156569 MW; 1A5666A01BB41DAB CRC64; MNTETFKKLL SERILLLDGA MGTMIQRHKL TEEQYRGERF KDHPYDLKGN NDILCLTQPE IIKSIHRAYF EAGADIVETN TFNGTPISQS DYHTQHLVYE INFEAARIAK EVADEFNRKN PYKPRFVAGA LGPTNKTLSI SPNVNDPGYR AVTFDEMVDA YYQQTKGLVD GGADILLIET IFDTLNAKAA IIAIQNYLEE KSIELPLMIS GTIVDMSGRT LSGQTVEAFY ISISHAKNLV SVGLNCALGA KQMRPFVEDL SNISDKFISV YPNAGLPNEM GGYDETPQSM ASVLEDFLAS GFVNIVGGCC GTTPDHIKAI AEIVRHHKPR IPKSQEPYLR LSGLEPVILR PDSNFMNIGE RTNVAGSKTF ARLIREEKYD EALSVARDQV EGGAQVLDVN MDEGMLDSEK AMTKFLNLLE AEPDIAKLPI MIDSSKWSVI EAGLKCLQGK GIVNSISLKE GEEVFKEHAN KILSYGAAVI VMAFDEKGQA DTFERKIEIC KRAYDILTKE VGFPPQDIIF DPNILAIATG MPEHNNYAVD YIEATRWIKQ NLPLAKVSGG VSNLSFSFRG NDVVREAMHS AFLYHAIKAG MDMGIVNAGQ LVVYEEIPKD LLELVEDVIL NRRPDATERL IEFAEKIKKQ DKVHIEEKKD EWRNLSVEER LKHALIKGIT DYIDEDIAEA LKKYSAPLEI IEGPLMAGMN VVGDLFGAGK MFLPQVVKSA RVMKKAVAIL EPFIAKPQIS SGNESLIPSP SQKEKGAKAS SSESDKFDWM TADPGVYGLL KEFVKQNRSN PTETEEKMWE LLRDRRLGNY KFRRQHIIGK YIADFVCLEQ KLVIEIDGLI HQLPDNKESD EIRTQWLNEI GFKVIRFTNE QVIKDTKNVL EEIIKNLKVP SLGGELGEAS NREVLIETKN EDLGGASVLL ATVKGDVHDI GKNIVGVVLG CNSYKVIDLG VMVHTEKIIQ TAIDQKVDLI GLSGLITPSL DEMVYVAKEM QRRGLKIPLL IGGATTSRVH TAVKIDPNYD GAVIHVLDAS RSVPVVSNLL NPDKIEREKF IKSVKEEYKK LREDYLKKKS DKQLIPLEKA RENKVKIDWS KSQIKKPNKL GVTALKNYSL SILKNYIDWT PFFQTWELKG KYPTIFEDDK IKSEAKKLFD DANKLLDKVV SENLLTANAV FGIFPANSVG DDIEVYSDES RKGVLTVLHT LRQQMQKTEG QPNIALADFI APKDSGLIDY IGAFAVTAGI GIERLIQEFE KNHDDYNSIM IKAIADRLAE AFAEHLHELV RKEYWGYAPE ENLTNEELIR ESYIGIRPAP GYPAQPDHTE KPIIFSLLKV EENSGIKLTE SMAMYPAASV SGLYFANPEA KYFQVGKIDK DQVLDYHRRK GMSVEEIERW LSPILNY // ID I0BIK7_9BACL Unreviewed; 1144 AA. AC I0BIK7; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AFH62204.1}; GN ORFNames=B2K_15990 {ECO:0000313|EMBL:AFH62204.1}; OS Paenibacillus mucilaginosus K02. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=997761 {ECO:0000313|EMBL:AFH62204.1, ECO:0000313|Proteomes:UP000007392}; RN [1] {ECO:0000313|EMBL:AFH62204.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=K02 {ECO:0000313|EMBL:AFH62204.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP003422; AFH62204.1; -; Genomic_DNA. DR RefSeq; WP_014370104.1; NC_017672.3. DR RefSeq; YP_006189969.1; NC_017672.3. DR EnsemblBacteria; AFH62204; AFH62204; B2K_15990. DR KEGG; pmw:B2K_15990; -. DR KO; K00548; -. DR BioCyc; PMUC997761:GLI6-3211-MONOMER; -. DR Proteomes; UP000007392; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007392}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AFH62204.1}; KW Transferase {ECO:0000313|EMBL:AFH62204.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 722 722 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1144 AA; 126198 MW; BAFF9B8A4E5C23E2 CRC64; MSKPSLQEQL KKKIMILDGA MGTMIQQENL TEADFGSEDL DGCNEILVVT RPDVIQKIHE AYFAAGADMV ETNTFGATSV VLAEYDLQDR ARELNLAAAK LAIEAANKYS TPEWPRYVIG AMGPTTKTLS VTGGVTFDEL VESYQEQAEA LIEAGVDALL LETSQDTLNV KAGSIGIRSA FDKLGVKLPL MISGTIEPMG TTLAGQNIES FYVSLEHLNP VSFGLNCATG PEFMRDHIRT LSEIAGTAVS CYPNAGLPDE NGKYHESPES LALKLAGFAE QGWLNIAGGC CGTTPDHIRA MAETLGKFEP RKQAGVHPPA ISGIETVYVE PDNRPIMVGE RTNISGSRKF KRLIKEGKFE EASEIARTQV KNGAHIIDIN LQDTDIDEAY AINEFLPQVV KKVKVPLMID STYDHIIELG LKYSQGKAIV NSINLEDGES KFEAIVPLLH KYGAAVVMIL IDERGQAVSR QAKMEVADRA YELLTKKYGM KPQDIIFDPN MFPVGSGDPQ YIGSAVETIE GIRMIKEKYP ETMTILGLSN ISFGLPDAGR EVLNSVYLYH CTKAGLDYAI VNTEKLERYA SIPEEERALA EELIFNTNDD TLAKFVAYFR VKKVEKKEKI SNLTLEERLA SYVVEGTKEG LIPDLEEALK KYAPLDIING PLMKGMEEVG RLFNNNELIV AEVLQSAEVM KASVAHLEQY MEKADSAVKG KIILATVKGD VHDIGKNLVE IILSNNGYKI VNLGIKVPPE QLIEAYRKEK PDAIGLSGLL VKSAQQMVVT AQDMKNAGID VPILVGGAAL TRKFTKTRIA PEYDGMVLYA KDAMDGLDIA NKLSDPEQRQ VLIRELRESM DSDVKEAGRK EESMPALTRV MTSTVDRTVP VQVPPDLKRR VLRDYPISHL VPYVNMQMLL GHHLGLKGKV ENLIAEKDPK ALQLKETVDG ILAEAQQAGI IKAQGMYRFF PAQSDGNDVL IYDPEDTGRV VQKFTFPRQE KEPYLCLADY LKPVSSGEMD YVGFLVVTAG HGVSELSAQW REKGDYLRSH ALQAAALELA EGFAERVHQM MRDQWGFPDP AEMTMAERFG AKYRGQRFSF GYPACPNLDD QQQLFALLHP EDIGVTLTEG SMMEPEASVS AIVFAHPQAR YFNA // ID I0BPN3_9BACL Unreviewed; 627 AA. AC I0BPN3; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 2. DT 01-APR-2015, entry version 21. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=B2K_27170 {ECO:0000313|EMBL:AFH64330.2}; OS Paenibacillus mucilaginosus K02. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=997761 {ECO:0000313|EMBL:AFH64330.2, ECO:0000313|Proteomes:UP000007392}; RN [1] {ECO:0000313|EMBL:AFH64330.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=K02 {ECO:0000313|EMBL:AFH64330.2}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; AFH64330.2; -; Genomic_DNA. DR RefSeq; WP_016362866.1; NC_017672.3. DR RefSeq; YP_006192095.2; NC_017672.3. DR EnsemblBacteria; AFH64330; AFH64330; B2K_27170. DR KEGG; pmw:B2K_27170; -. DR KO; K00547; -. DR BioCyc; PMUC997761:GLI6-5377-MONOMER; -. DR Proteomes; UP000007392; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007392}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:AFH64330.2}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:AFH64330.2}. SQ SEQUENCE 627 AA; 68004 MW; 598D37D3517DF3CB CRC64; MKPGLREALR SQVLVGDGAM GTYLYQMGFP IGISYEELNL LKPDVIMDVH RRYYEAGARL IETNTFSANR EKLSKFGLEG EVEAINRAGV ELARRAVGED AYVVGAVGSI RAGKRKNVRT NKVREDLREQ ISILCDTKVD GLLLESFLDL DEMLIALKEV RRISDLPVIC QFATEGAGVT QDGVPLKEAF AKLLEAGADV VGLNCRSGPN GLLRSLEGAA AAEADHPPYS VFPNAGLADY VDGRYSFPAT PQYFGETARR FADLGTRIIG GCCGTTPEHI AAVAGALAGY VPNPEAAKRA AAAPAAEVAE RAAAGAGAEV PTEPSIVDLV RQRHTVIVEL DPPKDLDIGK FMEGTEALKK AGVDALTMAD NSLAVTRMSN LALGSIVKER TGIRPLIHIA CRDRNLIGTQ SHMMGLHALG IDHVLAVTGD PARFGDLPGS SSVYDLTSFE IIRMIKQLNE GIAFSGKPLK KQANFVIGAA FNPNVKYLDK AVQRLERKVE AGADYIMTQP VYNAELIEQV YEATKHLSVP IFIGIMPLAS GNNAEYLHNE VPGIQLSDDV RKRMSGLRGE EGRAMGVQIG RELLDAAMRR FNGIYLMTPF LAYEMTVQLT EYVWEKAGRR HLSPLPK // ID I0DT80_PROSM Unreviewed; 1227 AA. AC I0DT80; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:AFH93548.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AFH93548.1}; GN Name=metH {ECO:0000313|EMBL:AFH93548.1}; GN OrderedLocusNames=S70_08425 {ECO:0000313|EMBL:AFH93548.1}; OS Providencia stuartii (strain MRSN 2154). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Providencia. OX NCBI_TaxID=1157951 {ECO:0000313|EMBL:AFH93548.1, ECO:0000313|Proteomes:UP000005012}; RN [1] {ECO:0000313|Proteomes:UP000005012} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MRSN 2154 {ECO:0000313|Proteomes:UP000005012}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP003488; AFH93548.1; -; Genomic_DNA. DR RefSeq; WP_014656935.1; NC_017731.1. DR RefSeq; YP_006216239.1; NC_017731.1. DR EnsemblBacteria; AFH93548; AFH93548; S70_08425. DR KEGG; psi:S70_08425; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; PSTU1157951:GLIN-1671-MONOMER; -. DR Proteomes; UP000005012; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000005012}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AFH93548.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005012}; KW Transferase {ECO:0000313|EMBL:AFH93548.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136564 MW; E05936D602C2A4AD CRC64; MVYKISMLEQ ELQKRILVLD GAMGTMIQRH KLTEEQFRGE RFADWPCDLK GNNDLLVLTQ PEIIRDIHDQ YFAAGADIVE TNTFNSTTIA MADYKMESLS AEINEAAARI ARECADEWTR KTPEQPRYVA GVLGPTNRTA SISPDVNDPA FRNINFDQLV EAYRESTRAL IKGGVDLIMI ETIFDTLNAK AAIFAVETEF EALGVTLPVM ISGTITDASG RTLSGQTTEA FYNSLRHARP LSFGLNCALG PNELRQYVSE LSRIAECYVS AHPNAGLPNA FGEYDLDAQN MAEQIREWAQ AGFLNIVGGC CGTTPLHIKK IVEAVKGIAP RALPKLPVEC RLSGLEPLNI GKDSLFVNVG ERTNVTGSAK FKRLIKEGNY QEALDIARQQ VENGAQIIDI NMDEGMLDSE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGESAFIEHA KLVRKYGAAV IVMAFDEVGQ ADTRERKIEI CRRAYHVLTD TVGFPPEDII FDPNIFAVAT GIEEHNNYAV DFIEVCQDIK QQLPHAMISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPK ELKDAVEDVI LNRREDSTER LLELAEKYRA SGSEEQQVQQ AEWRSWAVEK RLEYALVKGI TEFIIPDTEE ARQLAASPIE VIEGPLMNGM NVVGDLFGEG KMFLPQVVKS ARVMKQAVAY LEPYIQALKQ SGSSAGKILL ATVKGDVHDI GKNIVGVVLQ CNNYEIVDLG VMVPCETILK TAREQNVDVI GLSGLITPSL DEMVHVAKEM ERQGFTIPLM IGGATTSKAH TAVKIEPNYS HSVTYVQNAS RTVGVVSALL SATQKAEFVA RTRREYEIVR EQHGRKKPKT PPVSLEVARA NSVKIDWQNY QPPVPRFLGV KEVKASIETL RHYIDWTPFF MTWSLAGKYP RILEDEVVGE EARKLLKDAN NMLDQLAKDN ALTPRGIFGL FPANSVGDDI EIYRSSARDS ADVIALNLRQ QTEKKEFPNY CLSDFVAPKA SGKADYIGAF AVTGGLEEDA LADGYEQQHD DYNKIMLKAL ADRLAEAFAE YLHQQVRKEY WGYAPDEDLP NDELIREKYQ GIRPAPGYPA CPEHTEKAKI WQLLDVENQI GMQLTSSYAM WPGASVSGWY FSHPESKYFA VAQVQRDQVE DYAKRKGMSV SELERWLAPN LGYDPED // ID I0EZX6_9BACI Unreviewed; 315 AA. AC I0EZX6; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 01-APR-2015, entry version 16. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:AFI26782.1}; GN ORFNames=MY9_0242 {ECO:0000313|EMBL:AFI26782.1}; OS Bacillus sp. JS. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1127744 {ECO:0000313|EMBL:AFI26782.1, ECO:0000313|Proteomes:UP000005213}; RN [1] {ECO:0000313|EMBL:AFI26782.1, ECO:0000313|Proteomes:UP000005213} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JS {ECO:0000313|EMBL:AFI26782.1}; 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; AFI26782.1; -; Genomic_DNA. DR RefSeq; WP_014662626.1; NC_017743.1. DR RefSeq; YP_006230038.1; NC_017743.1. DR EnsemblBacteria; AFI26782; AFI26782; MY9_0242. DR KEGG; bjs:MY9_0242; -. DR KO; K00547; -. DR BioCyc; BSP1127744:GL8I-290-MONOMER; -. DR Proteomes; UP000005213; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005213}; KW Methyltransferase {ECO:0000313|EMBL:AFI26782.1}; KW Transferase {ECO:0000313|EMBL:AFI26782.1}. SQ SEQUENCE 315 AA; 34641 MW; 21F2C0F04439B596 CRC64; MNPIQHILDT FPLIVLDGAM ATELERKGCD LNDSLWSAKI LMEEPDLIKQ VHTDYFAAGA DCAITASYQS TFEGFAARGL SKAEARRLIE LSVSIAAEAR DEFWSFEENR LNRPKPIIAA SVGPYGAYLA DGSEYRGNYA ISEDELIEFH RPRMKALIEA GADVLACETI PCLTEAKAIV RLLKEFPETY AWISFSAKDG LHISDGTPAA DCAAWLDEHR QIAALGINCT PLQHISSLIE ELKKNTSKPI IVYPNSGEQY DPGTKTWNGA ACAESYGASA RIWHEKGAKL IGGCCRTKPE DIQEIAAWVR SLKTT // ID I0F2N2_9BACI Unreviewed; 612 AA. AC I0F2N2; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 01-APR-2015, entry version 23. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=MY9_1199 {ECO:0000313|EMBL:AFI27738.1}; OS Bacillus sp. JS. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1127744 {ECO:0000313|EMBL:AFI27738.1, ECO:0000313|Proteomes:UP000005213}; RN [1] {ECO:0000313|EMBL:AFI27738.1, ECO:0000313|Proteomes:UP000005213} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JS {ECO:0000313|EMBL:AFI27738.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; AFI27738.1; -; Genomic_DNA. DR RefSeq; WP_014663494.1; NC_017743.1. DR RefSeq; YP_006230994.1; NC_017743.1. DR EnsemblBacteria; AFI27738; AFI27738; MY9_1199. DR KEGG; bjs:MY9_1199; -. DR KO; K00547; -. DR BioCyc; BSP1127744:GL8I-1281-MONOMER; -. DR Proteomes; UP000005213; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005213}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 612 AA; 67933 MW; E0D5FA7A5AB5153C CRC64; MGLLEDLQRQ VLIGDGAMGT LLYSYGIDRC FEELNISKPE EIQRIHKAYV EAGANIIQTN TYGANYIKLS RHGLEDDIKK MNQEAVKIAR ASAGDAYVLG TMGGIRTFNK NAYSLDDIKR SFREQLYLLL HEEPDGLLLE TYYDLEEARE VLKIARKETD LPIMLNVSMH EQGVLQDGTP LSDALRSIAD LGADIVGINC RLGPYHMIEA LSEVPIFNDV FLSVYPNSSL PSLEEGRLVY ETDDTYFQNS ASEFRKQGAR IIGGCCGTTP NHIRAMAEAV SGLAPITEKE VKTRAKEFIS VQHERTEPGL NEIAAKKRSI IVELDPPKKL SFDKFLSAAA ELKEAGIDAL TLADNSLATP RISNVACGAL VKQQLDMRSL VHITCRDRNI IGLQSHLMGL DTLGLNDVLA ITGDPSKIGD FPGATSVYDL TSFDLIRLIK QFNEGLSLSG KPLGKKTNFS VAAAFNPNVR HLDKAVKRLE KKIDCGADYF VSQPVYSEQQ LVDIHNETKH LKTPIYIGIM PLTSSRNAEF IHNEIPGIKL SDTIREKMAH AGEDKEKQKA EGLAIARSLL DTACELFNGI YLITPFLRSD LTAELTSYIQ QKDEQRQNIF LH // ID I0FRW8_MACMU Unreviewed; 1264 AA. AC I0FRW8; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 01-APR-2015, entry version 18. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AFI37194.1}; GN Name=MTR {ECO:0000313|EMBL:AFI37194.1}; OS Macaca mulatta (Rhesus macaque). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9544 {ECO:0000313|EMBL:AFI37194.1}; RN [1] {ECO:0000313|EMBL:AFI37194.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Testis {ECO:0000313|EMBL:AFI37194.1}; RX PubMed=25319552; DOI=10.1186/1745-6150-9-20; RA Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X., RA Pandey S., Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P., RA Tharp G.K., Marcais G., Roberts M., Ferguson B., Fox H.S., RA Treangen T., Salzberg S.L., Yorke J.A., Norgren R.B.Jr.; RT "A new rhesus macaque assembly and annotation for next-generation RT sequencing analyses."; RL Biol. Direct 9:20-20(2014). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; JV047123; AFI37194.1; -; mRNA. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 2: Evidence at transcript level; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 259 259 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 784 784 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1264 AA; 140633 MW; 627DE62D20BB27CE CRC64; MSPALQDLSQ PGLKKTPRDE IDAILQKRIM VLDGGMGTMI QRQKLNEEHF RGQEFKDHAR PLKGNNDILS ITQPDVIYQI HKEYLLAGAD IIETNTFSST SIAQADYGLE HLAYRMNKCS AGVARKAAEE ITLQTGIKRF VAGALGPTNK TLSVSPSVER PDYRNIKFDE LVEAYQEQAK GLLDGGVDIL LIETIFDTAN AKAAVFALQN LFEEKYAPRP IFISGTIVDK SGRTLSGQTG EAFVISLSHA EPLCIGLNCA LGAAEMRPFI EMIGKCTTAY VLCYPNAGLP NTFGDYDETP STMAKHLKDF AMDGLVNIVG GCCGSTPDHI REIAEAVKNC KPRVPLATVF EGHMLLSGLE PFRIGQYTNF VNIGERCNVA GSRKFAKLIM AGNYEEALGV ARVQVEMGAQ VLDINMDDGM LDGPSAMTRF CNLIASEPDI AKVPLCIDSS NFAVIEAGLK CCQGKCIVNS ISLKEGEDDF LEKARKIKKF GAAMVVMAFD EEGQATETDT KIRVCTRAYH LLVKKLGFNP NDIIFDPNIL TIGTGMEEHN LYAINFIHAT KVIKETLPGA RISGGLSNLS FSFRGMEAIR EAMHGVFLYH AIKSGMDMGI VNAGNLPVYD DIHKELLQLC EDLIWNKDPE ATEKLLRYAQ TQGTGGKKVI QTDEWRNGPV EERLEYALVK GIEKHIIEDT EEARLNQERY PRPLNIIEGP LMNGMKIVGD LFGAGKMFLP QVIKSARVMK KAVGHLIPFM EKEREETRVL NGTTEEEDPY QGTIVLATVK GDVHDIGKNI VGVVLGCNNF RVIDLGVMTP CDKILKAALD HKADIIGLSG LITPSLDEMI FVAKEMERLA IKIPLLIGGA TTSRTHTAVK IAPRYSAPVI HVLDASKSVV VCSQLLDENL KDEYFEEIME EYEDIRQDHY ESLKERRYLP LSQARKSGFQ MDWLSEPHPV KPTFIGTQVF EDYDLQKLVD YIDWKPFFDV WQLRGKYPNR GFPKIFNDKT VGEEAKKVYD DAQNMLNTLI NQKKLQARGV VGFWPAQSIQ DDIHLYTESA VPQAAEPIAT FYGLRQQAEK DSASTEPYYC LSDFIAPLHS GIRDYLGLFA VACFGVEELS KAYEDDGDDY SSIMVKALGD RLAEAFAEEL HERVRRELWA YCGSEQLDVA DLRRLRYEGI RPAPGYPSQP DHTEKLTMWR LADIEQSTGI RLTESLAMAP ASAVSGLYFS NLKSKYFAVG KISRDQVEDY ALRKNMAVAE VEKWLGPILG YDTD // ID I0G0B1_9BRAD Unreviewed; 1285 AA. AC I0G0B1; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 01-APR-2015, entry version 22. DE SubName: Full=B12-dependent homocysteine-N5-methyltetrahydrofolate transmethylase {ECO:0000313|EMBL:BAL74198.1}; GN Name=metH {ECO:0000313|EMBL:BAL74198.1}; GN ORFNames=S23_09790 {ECO:0000313|EMBL:BAL74198.1}; OS Bradyrhizobium sp. S23321. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=335659 {ECO:0000313|EMBL:BAL74198.1, ECO:0000313|Proteomes:UP000007886}; RN [1] {ECO:0000313|EMBL:BAL74198.1, ECO:0000313|Proteomes:UP000007886} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S23321 {ECO:0000313|EMBL:BAL74198.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP012279; BAL74198.1; -; Genomic_DNA. DR RefSeq; WP_014439604.1; NC_017082.1. DR RefSeq; YP_005448310.1; NC_017082.1. DR EnsemblBacteria; BAL74198; BAL74198; S23_09790. DR KEGG; brs:S23_09790; -. DR KO; K00548; -. DR BioCyc; BSP335659:GL9K-979-MONOMER; -. DR Proteomes; UP000007886; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007886}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAL74198.1}; KW Transferase {ECO:0000313|EMBL:BAL74198.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 770 770 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1285 AA; 140327 MW; 82113ED05DA14D94 CRC64; MTVPISPKRT ALLNAARERI LVLDGAMGTM IQNLQFDEAA FRGERFKNFH RDLRGNNDLL ILTQPQAIED IHAAYLRAGA DIVATNTFST TSIAQADYDL TDIVYEMARE GARLAGNAAR RVEAEDSKPR FVAGAIGPTN RTASISPDVS NPGYRAVTFD DLRKSYGEQI NGMLDGGVDL LLVETIFDTL NAKAALYAIA EITEARGIDV PVMVSGTITD KSGRLLSGQM PEAFWHSVRH AKPITIGFNC ALGAEDLRAH IADIGRVADT LVCAYPNAGL PNEFGQYDET PEYMARLVGE FARDGLVNIV GGCCGTTPEH IAAIAAAVAP HKPRIVPEIE PRLRLSGLEP FVLTDAIPFV NVGERTNVTG SARFRKLITA GDYTAALQVA RDQVENGAQI IDVNMDEGLL DSEAAMVTFL NLVAAEPDIA RVPVMVDSSK FSVIEAGLKC VQGKPVVNSI SMKEGEEKFI HEANIARRHG AAVVVMAFDE AGQADTFARK TEICKRAYDI LVDRVGFPPE DIIFDPNIFA IATGIEEHNN YGVDFIEATR WIRQNLPGAH ISGGVSNLSF SFRGNEPVRE AMHSVFLYHA IKAGMDMGIV NAGQMIVYDD IDAELRQVCE DVVLNRDPGA SERLLALAEK FRGNKTQTKE ADLAWREWPV AKRLSHSLVH GITEFIEVDT EEARKESSRP LDVIEGPLMA GMNVVGDLFG DGKMFLPQVV KSARVMKQAV AWLMPFMEEE KARNLANGIG TEGSSSAGKI VLATVKGDVH DIGKNIVGIV LQCNNFEVID LGVMVPAAKI VETVKAEKAD IVGLSGLITP SLDEMAFFAS ELQREGLKLP LLIGGATTSR VHTAVKIDPN YRAGPVVHVN DASRAVGVAS SLLSPEKREA YAADVRAEYA KISDAHFRAQ ADKKRLKLDV ARANRVPVDF AAHKPVKPTF LGIRSFDDYD LAELVPYIDW TPFFQTWELA GRFPAILDDA KVGEVARSLY DDARKMLDLI VREKWFRARA TVGFWPANAQ GDDIVLYADE SRTKTIATLH TLRQQLEKRE GRFNAALSDF IAPAGTGIPD YVGGFVVTAG IGEDAVADRF KMANDDYSSI LCKALADRLA EAFAERMHAR VRREFWAYAP DEALSTDELI LEKYQGIRPA PGYPAQPDHT EKATLFELLD AENTAGVKLT ESFAMWPGSS VSGLYLANPE SYYFGVGKIE RDQVEDYAAR KGMTVTETER WLAPVLNYIP SREGADKAFT ATPANDETPK DLASHPPGCT CAVHLVWQKK RAGAG // ID I0GUT3_SELRL Unreviewed; 793 AA. AC I0GUT3; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Putative 5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|EMBL:BAL84520.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:BAL84520.1}; GN OrderedLocusNames=SELR_28120 {ECO:0000313|EMBL:BAL84520.1}; OS Selenomonas ruminantium subsp. lactilytica (strain NBRC 103574 / OS TAM6421). OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; OC Selenomonas. OX NCBI_TaxID=927704 {ECO:0000313|EMBL:BAL84520.1, ECO:0000313|Proteomes:UP000007887}; RN [1] {ECO:0000313|EMBL:BAL84520.1, ECO:0000313|Proteomes:UP000007887} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 103574 / TAM6421 {ECO:0000313|Proteomes:UP000007887}; 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; BAL84520.1; -; Genomic_DNA. DR RefSeq; WP_014425937.1; NC_017068.1. DR RefSeq; YP_005434543.1; NC_017068.1. DR EnsemblBacteria; BAL84520; BAL84520; SELR_28120. DR KEGG; sri:SELR_28120; -. DR KO; K00548; -. DR BioCyc; SRUM927704:GLJZ-2905-MONOMER; -. DR Proteomes; UP000007887; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007887}; KW Methyltransferase {ECO:0000313|EMBL:BAL84520.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007887}; KW Transferase {ECO:0000313|EMBL:BAL84520.1}. SQ SEQUENCE 793 AA; 83656 MW; 6DDC69A36EBAF82C CRC64; MSRIEIFDGA MGTMLQAGGL QPGACPELMN VENPEVVKNI HRAYIEAGAT IIETNTFGAS PLKLEHYGLT DRMAELNKAA VTIAKEAAQG RAKVAGSMGP TGRFIEPLGD LSFDDAYTNF FDQATALAEA GADFLIIETC IDLQEMRAAL LAAKAACDIP VICQLSYSED GRTVTGTDPQ SAAILLDAMG ADIIGVNCSL GPEELVPIVK TLAENCTCPI SVLPNAGMPY LKDGQTVFPM GPEDFGKWGV KLLEAGASYL GGCCGTTPEH IRELANAVKD LPLPERRLPA KRLWLTSRSK AVCIDRSLPT RLIGERINPT GRKKLAAEIK EGSLLGVKKE AVNQVKAGAH LLDVNMGVGG IDQAAAMKRA VTEISQLTDA PLSIDTSDAK ALEAGLKAYP GRALINSVSY EPERIAEFLP LAKKYGAAIL CLPITPDGVP KTAEERIAVM HKIIAAAKEQ GLDDGDFLLD ALVMTVSADK NACYEVLITL QMYRERFGYP TTMGLSNISF GLPNRPLINS TFFAMCLAAG LDAPIMNPYD EAMQRALMAS AALLGDDPNG LAYSKNEANL AVPKAAATAK VTELSPLEAI KQAVIDGEKD EIPSLVENAL KSGLEANTIT EQALTAAMTD IGVDFGAGRM FLPQVLLSAE TMRSAFNKLK ELTPANAAAP NQGTVVIATV KGDVHDLGKN ITGALLANSG FKLIDLGKDV DSTEIVKAAI ENNADIVGLC ALMTTTMVQI DKVIADLKEA GCDAKVMVGG AAVTQDYADS AGADAYAPDG VKAVELAKEL VKK // ID I0H1N3_ACTM4 Unreviewed; 1214 AA. AC I0H1N3; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 25. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine S-methyltransferase {ECO:0000313|EMBL:BAL86920.1}; GN OrderedLocusNames=AMIS_17000 {ECO:0000313|EMBL:BAL86920.1}; 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 {ECO:0000313|EMBL:BAL86920.1, ECO:0000313|Proteomes:UP000007882}; RN [1] {ECO:0000313|EMBL:BAL86920.1, ECO:0000313|Proteomes:UP000007882} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NCIMB 12654 / RC NBRC 102363 / 431 {ECO:0000313|Proteomes:UP000007882}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP012319; BAL86920.1; -; Genomic_DNA. DR RefSeq; WP_014441817.1; NC_017093.1. DR RefSeq; YP_005461436.1; NC_017093.1. DR EnsemblBacteria; BAL86920; BAL86920; AMIS_17000. DR KEGG; ams:AMIS_17000; -. DR KO; K00548; -. DR OMA; QPFFNAW; -. DR BioCyc; AMIS512565:GL7J-1738-MONOMER; -. DR Proteomes; UP000007882; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007882}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAL86920.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007882}; KW Transferase {ECO:0000313|EMBL:BAL86920.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 246 246 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 763 763 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1214 AA; 131610 MW; 0A62C80AFDD8D086 CRC64; MYPVTSTVTT LRELLAERIL VLDGAWGTML QGAKLTPADY RNELIPADHP KDVTGDPDLL ILTRPDVILD VHRQYLAAGA DITTTNTFTA TSIAQADYGL EHLVREMNVQ GARLARQAAD EATARDGKPR FVAGSVGPLN VTLSLSPKVD DPAYRAVTFD KVKATYAEQI AALAEGGVDL LLVETIFDTL NAKAAIAAAH EVAPELPLWI SVTIVDLSGR TLSGQTVEAF WRSIERAKPL VVGVNCSLGA TEMRPHVTDL ARLSDVYVAS HPNAGLPNAF GGYDETPAET SALVAGFASD GLVNIVGGCC GTTPAHIGAI ATAVAGMTPR VIDPPAPTTR FSGLEPFEIG PDTGFVMIGE RTNVTGSAKF RRLIEAGDHQ AAVDVALEQV RGGANLLDVN MDADLLDSEQ AMTTFLNLIA TEPEVARIPI MIDSSKWSVL EAGLKCVQGK GVVNSISLKE GVDQFLTQAR RIRDFGAGVV VMAFDEHGQA DTADRKVAIC ARAYDLLVED GFDPNDIIFD PNVLAVATGI AEHNGYAKAF IDALPRIKER CPGARTSGGI SNLSFAFRGN DVVREAMHSA FLFHAVKAGL DMGIVNAGQL AVYQDIPADL LELVEDVLFD RREDATDRLV TFASTVTGSG AKREVDLSWR EAPVGERLTH ALVHGIVDFI EEDTEEARQE LPRPLEVIEG PLMDGMKVVG DLFGSGRMFL PQVVKSARVM KRSVAYLEPF MEAEKEQARL EGRIDPGRGQ GKVVLATVKG DVHDIGKNIV GVVLGCNNYD VIDLGVMVPA AKILETAVAE NADVIGLSGL ITPSLDEMVA VGAEMQRRGM NLPLLIGGAT TSKQHTAVRI APAYEGSTIH VLDASRVVGV VSNLLDPARA KTLDEDNRIE QERLRVQHEQ RHSQPLLTLA AARANREVVD FSDLPTPAFT GVREVAPPIA ELRRMIDWQF LFLAWELKGK YPAILDQPVA RELFDDANTM LDQIIADGSF QARGRYGFWP AHADGDDIIL ENGYSFPMLR QQTEKPAGRA NRCLADYIAP AGAGSRDHLG GFAVAIHGAD ELARRYEAEH DDYRAIMVKA LADRLAEAFA EYLHLKARRE WFEPDADPKL EDLHAERFRG IRPALGYPAC PDHSEKKDLF KLLGTDAIGV NLTESYAMTP AAAVSGLIFA HPEARYFTVG RLAKDQIEDY ATRRDVPVAE VERWLRPNLA YNID // ID I0HKL6_RUBGI Unreviewed; 352 AA. AC I0HKL6; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:BAL93553.1}; GN OrderedLocusNames=RGE_02080 {ECO:0000313|EMBL:BAL93553.1}; OS Rubrivivax gelatinosus (strain NBRC 100245 / IL144). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Rubrivivax. OX NCBI_TaxID=983917 {ECO:0000313|EMBL:BAL93553.1, ECO:0000313|Proteomes:UP000007883}; RN [1] {ECO:0000313|Proteomes:UP000007883} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 100245 / IL144 {ECO:0000313|Proteomes:UP000007883}; 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 ----------------------------------------------------------------------- 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; BAL93553.1; -; Genomic_DNA. DR RefSeq; WP_014426445.1; NC_017075.1. DR RefSeq; YP_005435052.1; NC_017075.1. DR EnsemblBacteria; BAL93553; BAL93553; RGE_02080. DR KEGG; rge:RGE_02080; -. DR KO; K00548; -. DR BioCyc; RGEL983917:GLJR-209-MONOMER; -. DR Proteomes; UP000007883; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007883}; KW Methyltransferase {ECO:0000313|EMBL:BAL93553.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007883}; KW Transferase {ECO:0000313|EMBL:BAL93553.1}. SQ SEQUENCE 352 AA; 37972 MW; 729F61C55B7DAC99 CRC64; MNARTPAYTR GQALADLLPR RIVVIDGAMG TMIQRWKLGE ADFRNEALRE HPKDLKGDND LLSITRPDVI REIHAQYLAA GADIIETNTF GATTIAQEDY DLAHLAREMN LASARVAREA ADAAATPDKP RFVAGALGPT PRTASISPDV NDPGARNITF DQLREAYREQ AEALLDGGVD LFLVETIFDT LNAKAAIFAL DELMEERGER LPVIVSGTVT DASGRILSGQ TVGAFWHSVR HARPLAIGLN CALGAALMRP YIEELSRIAD DTYVSCYPNA GLPNPMSETG FDETPPVTGA LMADFAKAGF LNIVGGCCGT TPDHIAEIAR RVSAYRPRSR RDPLFTGLVA AA // ID I0HNA3_RUBGI Unreviewed; 310 AA. AC I0HNA3; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Homocysteine S-methyltransferase MmuM {ECO:0000313|EMBL:BAL94490.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:BAL94490.1}; GN Name=mmuM {ECO:0000313|EMBL:BAL94490.1}; GN OrderedLocusNames=RGE_11490 {ECO:0000313|EMBL:BAL94490.1}; OS Rubrivivax gelatinosus (strain NBRC 100245 / IL144). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Rubrivivax. OX NCBI_TaxID=983917 {ECO:0000313|EMBL:BAL94490.1, ECO:0000313|Proteomes:UP000007883}; RN [1] {ECO:0000313|Proteomes:UP000007883} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 100245 / IL144 {ECO:0000313|Proteomes:UP000007883}; 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 ----------------------------------------------------------------------- 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; BAL94490.1; -; Genomic_DNA. DR RefSeq; WP_014427361.1; NC_017075.1. DR RefSeq; YP_005435989.1; NC_017075.1. DR EnsemblBacteria; BAL94490; BAL94490; RGE_11490. DR KEGG; rge:RGE_11490; -. DR KO; K00547; -. DR BioCyc; RGEL983917:GLJR-1162-MONOMER; -. DR Proteomes; UP000007883; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007883}; KW Methyltransferase {ECO:0000313|EMBL:BAL94490.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007883}; KW Transferase {ECO:0000313|EMBL:BAL94490.1}. SQ SEQUENCE 310 AA; 33116 MW; 34D9F497F3EE6C2F CRC64; MIATTLAVQD ILVLDGALAT ELERRGADLK DPLWSAKLLI ERPELIREVH LDYFRAGADV ATTASYQATF EGFARRGFSH DEAGALMRRS VALAIEARDA FWAEPANRAG RRRPLVAASV GPYGAMLADG SEYRGYPGVT REQLAAFHRP RLQVLAAAGA DLLACETIPC LDEALAIASL LPGLQPALPA WISFSCRDGE HVSQGERFAD CAAALDGLPG VAAVGLNCTA PEHVPALVAA AQARTRLPIV VYPNSGEQWD AVAKCWHGER DAADFAAQAQ RWRRGGARLI GGCCRTGPDE IRALRAALLG // ID I0I428_CALAS Unreviewed; 305 AA. AC I0I428; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:BAM00016.1}; GN OrderedLocusNames=CLDAP_19760 {ECO:0000313|EMBL:BAM00016.1}; 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 {ECO:0000313|EMBL:BAM00016.1, ECO:0000313|Proteomes:UP000007880}; RN [1] {ECO:0000313|EMBL:BAM00016.1, ECO:0000313|Proteomes:UP000007880} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14535 / JCM 11387 / NBRC 104270 / STL-6-O1 RC {ECO:0000313|Proteomes:UP000007880}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; BAM00016.1; -; Genomic_DNA. DR RefSeq; WP_014433251.1; NC_017079.1. DR RefSeq; YP_005441913.1; NC_017079.1. DR EnsemblBacteria; BAM00016; BAM00016; CLDAP_19760. DR KEGG; cap:CLDAP_19760; -. DR KO; K00548; -. DR BioCyc; CAER926550:GLA5-2013-MONOMER; -. DR Proteomes; UP000007880; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007880}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000007880}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 192 192 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 258 258 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 259 259 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 305 AA; 32563 MW; 2B104ECC7B7B6E4F CRC64; MGTELFKRGL ISGGCPEEWN VSHPDRVQDV HRAYVEAGSD IILTNSFGGT RYRLKLHNLQ DRVVELNRAA AQNARAVADA AGRTVLVAGS MGPTGELLIP MGSMRYEECR DAFAEQARGL IEGGVDLLWI ETMSDLNEVK AAIEGARTVS PEIPICATMS YDTRGRTMMG VTGAQMAKEL AGLGLTAIGA NCGNNLIDTE AALAEMRAAA PEMILIAKAN AGMPRYEGDK LIYDGTPEVM AAYADRVRRN GVALIGGCCG SGPAHIRMMR QVLDGIIPVP EAPPPTPSAA ASEPTGRTRE RRVRK // ID I0I4A8_CALAS Unreviewed; 322 AA. AC I0I4A8; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:BAM00096.1}; GN Name=mmuM {ECO:0000313|EMBL:BAM00096.1}; GN OrderedLocusNames=CLDAP_20560 {ECO:0000313|EMBL:BAM00096.1}; 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 {ECO:0000313|EMBL:BAM00096.1, ECO:0000313|Proteomes:UP000007880}; RN [1] {ECO:0000313|EMBL:BAM00096.1, ECO:0000313|Proteomes:UP000007880} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14535 / JCM 11387 / NBRC 104270 / STL-6-O1 RC {ECO:0000313|Proteomes:UP000007880}; 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 ----------------------------------------------------------------------- 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; BAM00096.1; -; Genomic_DNA. DR RefSeq; WP_014433331.1; NC_017079.1. DR RefSeq; YP_005441993.1; NC_017079.1. DR EnsemblBacteria; BAM00096; BAM00096; CLDAP_20560. DR KEGG; cap:CLDAP_20560; -. DR KO; K00547; -. DR BioCyc; CAER926550:GLA5-2093-MONOMER; -. DR Proteomes; UP000007880; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007880}; KW Methyltransferase {ECO:0000313|EMBL:BAM00096.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007880}; KW Transferase {ECO:0000313|EMBL:BAM00096.1}. SQ SEQUENCE 322 AA; 35150 MW; D4C9B6977DBC1CCD CRC64; MFNPLTPFLE ANGVIIIDGA LATELERRGA DLSDALWSAR LLIDAPELIR SVHLDYLRAG ADVLITASYQ ASIEGFKRRG LNEAQVRNLF RLSVQLAAEA IEEYLAETQA GPARLPPLIA ASIGPYGAYL ADGSEYRGDY GLSVEALIAW HRPRVSALAE TEADLFACET IPCLAEAEAL IRLLEEYPDM PAWLSFSCRD GESLSSGEPF AEAVRLANRS EQIVAVGVNC TAPRFVESLL QIARPLTDKP LLCYPNSGEA WDAEARCWVE GTGVTDFAEP ARRWYAAGAR LIGGCCRTTP ADIAAMAQAL RREVEQRRHQ AL // ID I0I8I9_CALAS Unreviewed; 625 AA. AC I0I8I9; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 21. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=CLDAP_35370 {ECO:0000313|EMBL:BAM01577.1}; 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 {ECO:0000313|EMBL:BAM01577.1, ECO:0000313|Proteomes:UP000007880}; RN [1] {ECO:0000313|EMBL:BAM01577.1, ECO:0000313|Proteomes:UP000007880} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14535 / JCM 11387 / NBRC 104270 / STL-6-O1 RC {ECO:0000313|Proteomes:UP000007880}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; BAM01577.1; -; Genomic_DNA. DR RefSeq; WP_014434803.1; NC_017079.1. DR RefSeq; YP_005443474.1; NC_017079.1. DR EnsemblBacteria; BAM01577; BAM01577; CLDAP_35370. DR KEGG; cap:CLDAP_35370; -. DR KO; K00547; -. DR BioCyc; CAER926550:GLA5-3588-MONOMER; -. DR Proteomes; UP000007880; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007880}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000007880}. SQ SEQUENCE 625 AA; 68478 MW; 96CEECBF71FCDEC4 CRC64; MRDHPFLQRL AERPLLIDGA MGTMLYARGA SSEQCLEHLV VSKPAWVSEI HQAYANAGAD ILKTHTFGAN RIRLADYGLA ERVRDLNFRA VRLVRDVREV SGRAIFIAGD VGPLGKRLQP EGPLSATEAE EAFREQISVL WEAGADLLLF ETFIDLEELE LAVRTARKVC DLPIVASMTF AEDGLTLVGH TPEEAVRRLH AAGADVVGVN CSVGPAAMAQ TLEQMHAAAP DVRLIIMPNA GFPERVEGRF YYPASPEYFA RQTALFLTQG ARIVGGCCGT TPMHIRAMRA ALDEHLTVQV GIARPTLVVQ EEPPPAVKAD YGVTDEVEPT ELLRKLRAGK FVISVEVDPP RSFSAEKQIE GARHAMKMGA DAVNVADSPM ARVRMSALAL CVQIQQQVGI ETIVHFTTRD RSLMGLQADL IGARALGVRN ILALTGDPPT LGDNKQSTAV YDVDSIGLVR IISRFNEGVD VAGQDMGQKG GFTIAVACDP TRADLVQEVD RFHQKVIGGA HFTMTQPIFD PQLWLNFVRL YEERHGKFPV PVLIGVLPLQ GHKHATFLHN EVPGITLSEE ALERMRKAGP NGRQEGVKMA QELLLELKEL PYVQGVYLMP SFGRYETACQ VLEVL // ID I0IEC9_PHYMF Unreviewed; 640 AA. AC I0IEC9; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:BAM03617.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:BAM03617.1}; GN OrderedLocusNames=PSMK_14580 {ECO:0000313|EMBL:BAM03617.1}; OS Phycisphaera mikurensis (strain NBRC 102666 / KCTC 22515 / OS FYK2301M01). OC Bacteria; Planctomycetes; Phycisphaerae; Phycisphaerales; OC Phycisphaeraceae; Phycisphaera. OX NCBI_TaxID=1142394 {ECO:0000313|EMBL:BAM03617.1, ECO:0000313|Proteomes:UP000007881}; RN [1] {ECO:0000313|EMBL:BAM03617.1, ECO:0000313|Proteomes:UP000007881} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 102666 / KCTC 22515 / FYK2301M01 RC {ECO:0000313|Proteomes:UP000007881}; 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 ----------------------------------------------------------------------- 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; BAM03617.1; -; Genomic_DNA. DR RefSeq; WP_014436835.1; NC_017080.1. DR RefSeq; YP_005445514.1; NC_017080.1. DR EnsemblBacteria; BAM03617; BAM03617; PSMK_14580. DR KEGG; phm:PSMK_14580; -. DR KO; K00548; -. DR BioCyc; PMIK1142394:GLIF-1482-MONOMER; -. DR Proteomes; UP000007881; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007881}; KW Methyltransferase {ECO:0000313|EMBL:BAM03617.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007881}; KW Transferase {ECO:0000313|EMBL:BAM03617.1}. SQ SEQUENCE 640 AA; 69228 MW; 787A9A017EE4A40B CRC64; MSTFAQTALR RVLFLDGAMG TSIHNIDDLD LERDYLGREN CTEVLLLTRP EVIQGIHEDF LRAGSDAVET DSFNAQLHTM EDQDLVDRVH ELNVLAAQTA RLACDSFATP ERPRFVVGSM GPGTKLVTLG NIGYDEMRAS YAAQVRGLLD GGSDALLIET AQDILQVKCT LDAIFGVLDE RGLTPDVDGT GDVPVMVQVT IEQFGTTLIG TDIAGVVATL RNYPIFSLGM NCATGPAEMA EHLKHIARNW PGAISLLPNA GLPTLVEGRT IFPLQAEPFA EKMAEFVLTA GLNIVGGCCG TTPAHIAALV EKVGRDTPVT EVEVQPWQPA IASLMGAVEM RQDNSILNIG ERTNASGSRK FKRLLEEEDW DEIVSLARDM VREGSHVIDV NVDYAGRDNV RDMTTVVSKL VNQVNAPLML DSTQPATIEA GLKAAGGKCL INSANLEDGE EKFALMCRLA KKYNAGLVLG TIDEDPEEAM ARTRERKLEI ATRMHDLATR VHGLDEADLM FDPLVLPVST GMEQDRRSGL ETIEGTRLIS ERFPRCQITC GLSNISFGLK PAARQVLNSV FLAELIQAGM TSAILHVSKI LPESRIPREQ WDAAIRLLYD RRGAAAEAAV AETVAAGGGE AHVHGAACSH // ID I0IPX1_LEPFC Unreviewed; 828 AA. AC I0IPX1; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 01-APR-2015, entry version 19. DE SubName: Full=5-methyltetrahydrofolatehomocysteine methyltransferase {ECO:0000313|EMBL:BAM07320.1}; GN OrderedLocusNames=LFE_1639 {ECO:0000313|EMBL:BAM07320.1}; OS Leptospirillum ferrooxidans (strain C2-3). OC Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; Leptospirillum. OX NCBI_TaxID=1162668 {ECO:0000313|EMBL:BAM07320.1, ECO:0000313|Proteomes:UP000007382}; RN [1] {ECO:0000313|Proteomes:UP000007382} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C2-3 {ECO:0000313|Proteomes:UP000007382}; 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 ----------------------------------------------------------------------- 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; BAM07320.1; -; Genomic_DNA. DR RefSeq; WP_014449805.1; NC_017094.1. DR RefSeq; YP_005469450.1; NC_017094.1. DR EnsemblBacteria; BAM07320; BAM07320; LFE_1639. DR KEGG; lfc:LFE_1639; -. DR KO; K00548; -. DR BioCyc; LFER1162668:GLFM-1635-MONOMER; -. DR Proteomes; UP000007382; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007382}; KW Methyltransferase {ECO:0000313|EMBL:BAM07320.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007382}; KW Transferase {ECO:0000313|EMBL:BAM07320.1}. SQ SEQUENCE 828 AA; 88200 MW; BD06B6F37907BE0E CRC64; MKPLLERLKY EVLLLDGSMG ALLQSRGLPA GYAPDLWNIE KPQEIQAVHT EYVNAGSDII LTNTFGASRL RLSEYNAQDR IREINFQAVD LAQRASRGKA YVAGDIGPSG TTIAPFGDLP FDDAIAIFYE QAKLLLEAGA DLIAIETMFD IQEMRAALIG VREATNGRIP LMALMTFNMD GITDSGSDPE TAASVLEGFG VDIMGLNCSV GPEAMVPVVS RLGQTTDTFI AVEPNAGLPV HRNGETLYLT GAEEVAKFAP SFVEAGANII GGCCGTTPEY IRILAKTVKG ASPISRPTPS LLKISSRTSM TLIGDGVPFL IVGEKINPTG KKIFSEAIAN GQVDLIVAEA RKEAEAGAGA LDVNVGVPLV NEAEMMAKAI TAIQNVVSLP LVIDSSYASA LESGLKLYPG RALVNSVNAE DERLEEVLPL IRKYGAAVIA LVSGDNIPET AAERMKNAEK ILRRAEELGL KPRDLIFDTL ALTVSAVQEA AKQTLDTITL IKKELRLPTI LGLSNVSFGL PARKIVHNNF LSMAIGAGLD AAICDPYDQV LHQTIAASSL FARRDPDCRI YLNKAAAWTP AQGNHPASKE AAPKTTSEAI RQAILEGERD GIAALCQKGL DEGLSAFTIF LDIMTPAIRH LGDLFGQRVK FIPHLIAGAD AMKKGVEVLQ PHLEADGPVE PKGCVVFATV KGDIHDIGKN ICILMLRNFG FSVIDLGRNV PLDDILAAAE KHQAQIIALS ALMTTTMMQM KTAIETIREK NLPYKVMVGG AVVTPKFSTE IKADGYGKDV GDVVPLAEKL ISAFSGLDVP VASSGSGSDS EAIVGRKN // ID I0JIU0_HALH3 Unreviewed; 349 AA. AC I0JIU0; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CCG44058.1}; DE EC=2.1.1.5 {ECO:0000313|EMBL:CCG44058.1}; GN OrderedLocusNames=HBHAL_1691 {ECO:0000313|EMBL:CCG44058.1}; 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 {ECO:0000313|EMBL:CCG44058.1, ECO:0000313|Proteomes:UP000007397}; RN [1] {ECO:0000313|EMBL:CCG44058.1, ECO:0000313|Proteomes:UP000007397} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35676 / DSM 2266 / JCM 20832 / NBRC 102448/ NCIMB 2269 RC {ECO:0000313|Proteomes:UP000007397}; 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(2012). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; CCG44058.1; -; Genomic_DNA. DR RefSeq; WP_014641963.1; NC_017668.1. DR RefSeq; YP_006179335.1; NC_017668.1. DR EnsemblBacteria; CCG44058; CCG44058; HBHAL_1691. DR KEGG; hhd:HBHAL_1691; -. DR KO; K00544; -. DR BioCyc; HHAL866895:GLDT-724-MONOMER; -. DR Proteomes; UP000007397; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007397}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:CCG44058.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007397}; KW Transferase {ECO:0000313|EMBL:CCG44058.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 210 210 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 298 298 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 349 AA; 39259 MW; 75ED2391DF88BBAA CRC64; MKRSLEQRLQ DGPVICGEGY LFELERRGYL QAGSFVPEVA LDNPQALKQT YRDYMLAGSD VVLAFTYNGH REKMRIIGKE ELLEPLNRQA IRLAKEVAQE HPEEEALVAG NISNTNLFNP DDPEAVEKTR SMFAEMIGWC KEEGVDFVNG ETFYYYEEAL IALEEIQKQD LPAVITFGLM GENILRDGYE VEEACRLLKE KGALVVGMNC FRGPATMQPY VEKIRNTLDG YVGALPIPYR TTEEHPTFFN LPDGGCACTL PTETTFPTSL DPLYTNRYEL AEWAREAHSI GVNYLGLCCG ASPAMLREVA ETVGRTAVNS TYSPDMEKHF LFGKDDTLQD HITSYKTKA // ID I0JZN3_9BACT Unreviewed; 611 AA. AC I0JZN3; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN Name=metF {ECO:0000313|EMBL:CCG92702.1}; GN ORFNames=MFUM_730011 {ECO:0000313|EMBL:CCG92702.1}; OS Methylacidiphilum fumariolicum SolV. OC Bacteria; Verrucomicrobia; unclassified Verrucomicrobia; OC Methylacidiphilales; Methylacidiphilaceae; Methylacidiphilum. OX NCBI_TaxID=1156937 {ECO:0000313|EMBL:CCG92702.1}; RN [1] {ECO:0000313|EMBL:CCG92702.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SolV {ECO:0000313|EMBL:CCG92702.1}; 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] {ECO:0000313|EMBL:CCG92702.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SolV {ECO:0000313|EMBL:CCG92702.1}; RA Op den Camp H.; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCG92702.1}. 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; CAHT01000081; CCG92702.1; -; Genomic_DNA. DR RefSeq; WP_009060720.1; NZ_CAHT01000081.1. DR EnsemblBacteria; CCG92702; CCG92702; MFUM_730011. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862, KW ECO:0000313|EMBL:CCG92702.1}. SQ SEQUENCE 611 AA; 66855 MW; BA0FFBD253845392 CRC64; MATLIDRLNE SLLIGDGALG TYLYSLGIPR GYCIEELSLS HPDLLEKVHR DYIDAGAKII RTNTAESNAY HLSFFKLEKK LKEIVSRSVQ LAKKALGSRE GWIAGTVGPI WTKPTESPID MATRQSLYEE LIASLIEEGV DLLFFETFTE LPELLLVLDI ARKKGAEKLF AFIASFEEGK LSSGETLGEA FSKLRLAGAT LVGINGACGV QASIHLLEEI ELKAGDFLGA YPNAGKPEFY DGTFTYSASP SYFGENVARF AEEGVCLLGG DYGTEPAHIA AMAQRAATIK PLKEKPPKRR PRYLVSEQEV LPQIEPSLLD LLALKPVFMV EYDSPKTLAI GKFLEGVKAI EKAGADAITL ADNSLAILRI SNFAAAIHVR RVSKMIPILH VACRDRNLLG LQSELMGLGT LGFRHILALT GDPAKSGDHP GATSVYDLNS VGLIRLLASL NRGFNAAGKD LKGKTDFIIG CAFNPNTTQF EAQVKKLEAK LAAGAQFVMT QPVFDIQLIK KTYNYLKPLG IPVFIGLMPL LNYRNAEFLH NEVPGISIPE AVREKLKALD GEKATELGVG FAQLLGEEIL SLFKCVYLIT PFLRYDISVR LLELLYSRKK S // ID I0KGX9_9BACT Unreviewed; 1259 AA. AC I0KGX9; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 29-APR-2015, entry version 24. DE SubName: Full=Drat genome {ECO:0000313|EMBL:CCH03382.1}; GN ORFNames=FAES_5383 {ECO:0000313|EMBL:CCH03382.1}; OS Fibrella aestuarina BUZ 2. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae; OC Fibrella. OX NCBI_TaxID=1166018 {ECO:0000313|EMBL:CCH03382.1, ECO:0000313|Proteomes:UP000011058}; RN [1] {ECO:0000313|EMBL:CCH03382.1, ECO:0000313|Proteomes:UP000011058} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BUZ 2 {ECO:0000313|EMBL:CCH03382.1}; RX PubMed=22689241; DOI=10.1128/JB.00550-12; RA Filippini M., Qi W., Blom J., Goesmann A., Smits T.H., Bagheri H.C.; RT "Genome Sequence of Fibrella aestuarina BUZ 2T, a Filamentous Marine RT Bacterium."; RL J. Bacteriol. 194:3555-3555(2012). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; HE796683; CCH03382.1; -; Genomic_DNA. DR RefSeq; WP_015334479.1; NC_020054.1. DR RefSeq; YP_007323975.1; NC_020054.1. DR EnsemblBacteria; CCH03382; CCH03382; FAES_5383. DR KEGG; fae:FAES_5383; -. DR KO; K00548; -. DR BioCyc; FAES1166018-WGS:GSNK-5444-MONOMER; -. DR Proteomes; UP000011058; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 2. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 2. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000011058}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000011058}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 755 755 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1259 AA; 139711 MW; DCFDC10A6FCDB2F2 CRC64; MQQLTDLLQQ RILILDGAMG TMIQRYNLSE DDYRGDRFRD FPHDVKGNND LLSLTRPDII AEIHRQYFEA GSDIVETNTF SGTSIAMADY HMEELVYELN YESARIARAI ADEFTQADPT KPRFVAGAMG PTNRTASLSP DVNNPGYRAV TFDELVDAYY EQVRGLVDGG SDILLVETIF DTLNAKAALF AIDRYFADQG KPSLPIMVSG TITDASGRTL SGQTTEAFLY SVSHLPLLSV GLNCALGAEL LRPYVQTLAN ESPFYTSAYP NAGLPNEMGE YDQSPDEMAA QIESFAKDGF VNIVGGCCGS TPDHIRAIAG AMAKYQPRPK PTPEPYQKLS GLEPLKITEQ TNFVNVGERT NVTGSKAFAR LIKAGDYEAA LAVARQQVEN GAQVIDVNMD EGMLDSAEVM TTYLNLIAAE PDIARVPVMI DSSKWEVIEA GLKCVQGKAI VNSISLKEGE QAFIERAQLV KRYGAAVVVM AFDEDGQADS YERRIQICER AYRILVDQVK FAPQDIIFDP NILTVATGID EHNNYAVDFI NATRWIKENL PLAKVSGGVS NISFSFRGND PVREAMHSAF LYHAIRAGMD MGIVNAGQLA IYDDIPKELL ERVEDVLLNR RDDATERLVT FADTVKAKGK EVVVDEAWRS NTVAERLKYA LIKGITDFID EDVEEARLQA ERPLHVIEGP LMDGMNVVGD LFGEGKMFLP QVVKSARVMK KAVAHLTPYI EAEKQVGDAA GAGKILLATV KGDVHDIGKN IVGVVLGCNN YEIIDLGVMV PTQKILDAAR EHNVDIIGLS GLITPSLDEM VGVAKEMERQ GFTIPLLIGG ATTSRIHTAV KIDPHYSGPV IHVLDASRSV PVAGRLVSDE RTTRDQIFNE IKAEYAKLRD EHARRQKEKN LLTIEQARRN RVSIDWASFT ATKPTYLGNR YFDDYPLDEI ARYIDWTPFF QTWQLHGKYP AIFEDATVGG EARKLYDDAN ALLQQIIRDK SLTAKAVVGF YPANATDDDV LIHDFEEITR EVPCERHGSH RHVEYKISQA AASQAAVTPA GELVYDTKTV VHFLRQQNQK AAGLPNLCLA DFVAPLESGR EDYIGAFAVT AGIGIEVLLE QFEREHDDYN SIMVKALADR LAEAFAELMH ERTRKEFWPY ATNEQLTNDE LIREKYQGIR PAPGYPACPD HTEKATLFDL LDAGRADIVL TESFAMYPAS SVSGFYFSHP ESKYFAVGKL NKDQVIDYAH RKDMTLDEAE RWLSPVLAY // ID I0KQE3_STEMA Unreviewed; 363 AA. AC I0KQE3; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=MetH2 protein {ECO:0000313|EMBL:CCH13283.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CCH13283.1}; GN Name=metH2 {ECO:0000313|EMBL:CCH13283.1}; GN ORFNames=SMD_2753 {ECO:0000313|EMBL:CCH13283.1}; OS Stenotrophomonas maltophilia D457. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Stenotrophomonas; OC Stenotrophomonas maltophilia group. OX NCBI_TaxID=1163399 {ECO:0000313|EMBL:CCH13283.1, ECO:0000313|Proteomes:UP000007390}; RN [1] {ECO:0000313|EMBL:CCH13283.1, ECO:0000313|Proteomes:UP000007390} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=D457 {ECO:0000313|EMBL:CCH13283.1}; 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). CC ----------------------------------------------------------------------- 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; CCH13283.1; -; Genomic_DNA. DR RefSeq; WP_014647681.1; NC_017671.1. DR RefSeq; YP_006185454.1; NC_017671.1. DR EnsemblBacteria; CCH13283; CCH13283; SMD_2753. DR KEGG; smz:SMD_2753; -. DR KO; K00548; -. DR BioCyc; SMAL1163399:GLKX-2753-MONOMER; -. DR Proteomes; UP000007390; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007390}; KW Methyltransferase {ECO:0000313|EMBL:CCH13283.1}; KW Transferase {ECO:0000313|EMBL:CCH13283.1}. SQ SEQUENCE 363 AA; 38426 MW; 68ACC93BC572ADA4 CRC64; MPALPWLHPD RANALLDALR ERILIIDGAM GTMIQRHGLQ EDDYRGERFA GGYDHAHGPG CDHGTPEGHD LKGNNDLLLL TRPQVIADIH TAYLDAGADL VETNTFNATS VSQADYHLEH LVYELNKAGA AVARACCDAV AAATPGKPRF VIGVIGPTSR TASISPDVND PGFRNTSFDE LRDTYREAIE GLIDGGADTL MVETIFDTLN AKAALYALEE AFDARGARLP VMISGTITDA SGRTLSGQTA EAFHASLAHA RPLSIGLNCA LGAEAMRPHV ETLSQVADCY VSAHPNAGLP NAFGEYDETP EEMATTLRGF AEDGLLNLVG GCCGSTPDHI RAIARAVAGL PPRALPGVQE QAA // ID I0L3N4_9ACTO Unreviewed; 1171 AA. AC I0L3N4; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:CCH18431.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CCH18431.1}; GN Name=metH {ECO:0000313|EMBL:CCH18431.1}; GN ORFNames=MILUP08_43341 {ECO:0000313|EMBL:CCH18431.1}; OS Micromonospora lupini str. Lupac 08. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micromonosporineae; Micromonosporaceae; Micromonospora. OX NCBI_TaxID=1150864 {ECO:0000313|EMBL:CCH18431.1}; RN [1] {ECO:0000313|EMBL:CCH18431.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Lupac 08 {ECO:0000313|EMBL:CCH18431.1}; 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] {ECO:0000313|EMBL:CCH18431.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Lupac 08 {ECO:0000313|EMBL:CCH18431.1}; RA Trujillo M.; RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:CCH18431.1}. 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; CAIE01000026; CCH18431.1; -; Genomic_DNA. DR RefSeq; WP_007459803.1; NZ_HF570108.1. DR EnsemblBacteria; CCH18431; CCH18431; MILUP08_43341. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CCH18431.1}; KW Transferase {ECO:0000313|EMBL:CCH18431.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 223 223 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 734 734 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1171 AA; 127504 MW; 9CEE68CAE77A7584 CRC64; MRTSLLDVLA DRILIADGAM GTMLQAADLT LDDFDGLEGC NEILNVTRPD VVRGVHDAYL AAGADCVETN TFGANLANLA EYDIPQRIRE LSEAGARIAR EAADAASTPQ RPRFVLGSIG PGTKLPTLGH APYATLRDAY QENAAGLIVG GADALIIETC QDLLQVKAAV VGSKRAMAEL GRSVPIICHV AVETTGTMLV GSEIGAALAA IEPLGVDLIG LNCSTGPAEM SEHLRYLSQH SRIPLSVMPN AGLPVLTADG AYFPLTPVEL AEALERFITE YGVGLVGGCC GTTPEHIRVL SERLHGLTAP AREPRHEAGV SSVYHPVPFA QDASVLMVGE RTNANGSKAF REAMLAGDFR ACVEIARSQA RDGSHLLDLC VDYVGRDGTQ DMRELAGRFA TASTLPIMLD STEPNVVEAG LEMLGGRCVV NSVNFEDGDG PDSRYARVMP VVREHGASVV ALLIDEEGQA RTQEWKVRVA ARLIDDLTGR WGMDRADILI DALTFPIATG QEETRRDGLE TIEAIREISR RYPGVNFTLG ISNISFGLNP AARQVLNSVF LHECVQAGLT SAIVHASKIL PMSKIPDEQR EVALDLVYDR RREGYDPVQR FLELFEGVDV TSARATRAQE LAALPLDERL KRRIVDGERN GLEADLDEAM AGGRSPLSII NDILLDGMKV VGELFGSGQM QLPFVLQSAE VMKTAVAYLE PHMETTEDGG KGRIVLATVR GDVHDIGKNL VDIILSNNGY EVVNIGIKQP ISAILDAAEQ HRADAIGMSG LLVKSTVIMK ENLAEMATRG VAERWPVLLG GAALTRAYVE DDLRSMFPGQ VHYARDAFEG LSLMDKVMTA KRGGAPVIDP EREAALATRR ARRERQRSVV TESLPELHDS SVRSDVATDV AVPTPPFFGT RVVKGVPMAD YAALLDERAT FRGQWGLNGA RGGNGPSYDE LVETEGRPRL RYWLDRLIAD QVLEAAVVYG YFPAYSEGND LVVLDENGHA ERARFSFPRQ RQERRLCLAD FFKPKGDQLD VVALQLVTVG QPVSEYAAKL FARNEYRDYL EVHGLSVQLT EALAEYWHRR IRAELTLPDG RPLGHDDPTD LAGILRNDYR GCRYAFGYPA CPDLEDRAKI VELLGSERIG VELSEEFQLM PEQATDAIVV HHPEASYFNA K // ID I0PWE8_MYCAB Unreviewed; 1255 AA. AC I0PWE8; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EIC70968.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EIC70968.1}; GN Name=metH {ECO:0000313|EMBL:EIC70968.1}; GN ORFNames=S7W_02310 {ECO:0000313|EMBL:EIC70968.1}; OS Mycobacterium abscessus M94. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium abscessus. OX NCBI_TaxID=1158135 {ECO:0000313|EMBL:EIC70968.1, ECO:0000313|Proteomes:UP000005345}; RN [1] {ECO:0000313|EMBL:EIC70968.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M94 {ECO:0000313|EMBL:EIC70968.1}; RA Ngeow Y.F., Choo S.W., Wong Y.L.; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EIC70968.1}. 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; AJGG01000003; EIC70968.1; -; Genomic_DNA. DR RefSeq; WP_005086549.1; NZ_AJGG01000003.1. DR EnsemblBacteria; EIC70968; EIC70968; S7W_02310. DR Proteomes; UP000005345; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000005345}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EIC70968.1}; KW Transferase {ECO:0000313|EMBL:EIC70968.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 255 255 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 318 318 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 319 319 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 781 781 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1255 AA; 137426 MW; 87F22DEFC9BD2E67 CRC64; MHVTNLQPNV RPDCTEALTA ALEQRILVID GAMGTAIQRD RPDEAGYRGE RFADWPSDLV GNNDLLTLTQ PHIIEGIHRE YLEAGADILE TNTFNANAVS LSDYGMEELS YELNYAGAAL ARVAADEYST PAKPRYVAGA LGPTTRTASI SPDVNDPGAR NVSYDQLVAA YLEAANGLVD GGADIILVET IFDSLNAKAA VFAIETLFEQ RGRRWPIIIS GTITDASGRT LSGQVTEAFW NAIRHARPIA VGLNCALGAP EMRPYIAEMS RIADTFVSCY PNAGLPNAFG EYDESPEHQA GYLAEFAEAG LVNLVGGCCG TAPAHIAEIA KVVEGVKPRD VPSIDVATRL SGLEPLNITD DSLFVNIGER TNITGSARFR NLIKAEDYDT ALSVALQQVE VGAQVIDINM DEGMIDGVAA MDRFTKLIAA EPDISRVPVM IDSSKWEVIE AGLKNVQGKP IVNSISMKEG EEKFIREARL CRKYGAAVVV MAFDEKGQAD NLERRKEICG RAYRILTEEV GFPAEDIIFD PNCFALATGI EEHATYGIDF IEACAWIKEN LPGVHISGGI SNVSFSFRGN NPVREAIHAV FLFHAIKAGL DMGIVNAGAL VPYDSIDSEL RDRIEDVVLN RRADAAERLL EIAERFNSTE NSGGGDDRAA QEWRSLPVRE RITHALVKGI DAHVDDDTEE LRAEIAAAGG RPIEVIEGPL MDGMNVVGDL FGSGKMFLPQ VVKSARVMKK AVAYLLPFIE AEKEDNGTAG DSKSKDTNGT IVMATVKGDV HDIGKNIVGV VLQCNNFEVI DLGVMVPAQK ILDAAKEHDA DIIGLSGLIT PSLDEMANFA VEMEREGLEI PLLIGGATTS RAHTAVKISP RRKGPVVWVK DASRSVPVAA ALLDDKQRPG LLEATEKDYA SLRERHAQKN ERPTLTLEKA RANRTPVEWD GYTPPVPAQG LGVREFLDYD LAEVREYIDW QPFFNAWEMK GRFPDILNNP ATGEAARKLY DDAQQMLDTL IKEKWLTANG VIGFFPANAV GPGFEDIEVY TDDTRTEVLT TLHNLRQQGE HRDGIPNRSL GDYIAPKETG LRDYIGAFAV TAGLGSQDKI MEFKADLDDY SAILLESIAD RLAEAFAERM HQRVRTEFWG FQPDEQLDNE ALIGEKYRGI RPAPGYPACP EHTEKVTLFD LLDVTKRTGI ELTESMAMWP GAAVSGWYFA HPQSQYFVVG RLAQDQVADY AKRKGWTLQE AERWLGPNLG YNPED // ID I0Q004_9BACE Unreviewed; 308 AA. AC I0Q004; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EIC73057.1}; GN ORFNames=BSIG_5926 {ECO:0000313|EMBL:EIC73057.1}; OS Bacteroides sp. 1_1_6. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=469586 {ECO:0000313|EMBL:EIC73057.1}; RN [1] {ECO:0000313|EMBL:EIC73057.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_1_6 {ECO:0000313|EMBL:EIC73057.1}; 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. {ECO:0000313|EMBL:EIC73057.1}. 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; ACIC02000021; EIC73057.1; -; Genomic_DNA. DR RefSeq; WP_008764881.1; NZ_JH636030.1. DR ProteinModelPortal; I0Q004; -. DR EnsemblBacteria; EIC73057; EIC73057; BSIG_5926. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 308 AA; 34416 MW; DC48647CE245C009 CRC64; MNFKDCIDSY PFILMEGALG ERLKREFDLD ISGTVAMADL VYQQKGRLAL ETLWNEYIDI AYRYQLPFLA TTPTRRANKE RIYMAGYNES IIADNVDFLR SIKEAANVDM YIGGLMGCKG DAYTGEEALN LEEAIDFHSW QAGLFKSAKV DFLYAGIMPV LTEAIGMAVA MSDTDIPYII SFTIQRDGKL IDGHTIDDAI HCIDNHVSNK PVCYMTNCVH PDIVYEALSH KFNQTQTVKS RFWGIQANTS QLSYKELDGA NHLHTSSAAD LSEAILKLKS DCHLKIFGGC CGTDSSHMEK IAKISEVT // ID I0QHP8_STRSL Unreviewed; 322 AA. AC I0QHP8; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 01-OCT-2014, entry version 10. DE SubName: Full=Homocysteine S-methyltransferase (S-methylmethionine) {ECO:0000313|EMBL:EIC80808.1}; GN ORFNames=PS4_41838 {ECO:0000313|EMBL:EIC80808.1}; OS Streptococcus salivarius PS4. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1157946 {ECO:0000313|EMBL:EIC80808.1}; RN [1] {ECO:0000313|EMBL:EIC80808.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PS4 {ECO:0000313|EMBL:EIC80808.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIC80808.1}. 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; AJFW01000046; EIC80808.1; -; Genomic_DNA. DR EnsemblBacteria; EIC80808; EIC80808; PS4_41838. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EIC80808.1}; KW Transferase {ECO:0000313|EMBL:EIC80808.1}. SQ SEQUENCE 322 AA; 35579 MW; 15D463F312748C69 CRC64; MVRRSFMAIF KDYLENKSPL ILHGALGTEM EALGYDISGK LWSAKYLLEK PEVIQEIHET YVAAGADLIT TSSYQATLPG LMESGLTERE AEQIIALTVQ LAKAARDKVW VTLDETEKAK RPYPLISGDV GPYAAYLANG SEYSGDYGQI TVETLKDFHR PRIQILLDQG VDLLALETIP NHLEAQALIE LLAEEFPDVE AYISFTIQVP DAISDGTSLS DIAKLVSQSS QILAVGINCS SPILYEQALP VLKKAGKALI TYPNSGEVYD GDSQTWKPKD KDALTLLEHS KDWHAHFGVQ ILGGCCRTRP NDIKALYQEF RT // ID I0QNC7_9ENTR Unreviewed; 1227 AA. AC I0QNC7; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 01-APR-2015, entry version 18. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EIC82800.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EIC82800.1}; GN Name=metH {ECO:0000313|EMBL:EIC82800.1}; GN ORFNames=SPM24T3_19902 {ECO:0000313|EMBL:EIC82800.1}; OS Serratia sp. M24T3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Serratia. OX NCBI_TaxID=932213 {ECO:0000313|EMBL:EIC82800.1}; RN [1] {ECO:0000313|EMBL:EIC82800.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M24T3 {ECO:0000313|EMBL:EIC82800.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EIC82800.1}. 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; AJHJ01000035; EIC82800.1; -; Genomic_DNA. DR RefSeq; WP_009638583.1; NZ_AJHJ01000035.1. DR EnsemblBacteria; EIC82800; EIC82800; SPM24T3_19902. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EIC82800.1}; KW Transferase {ECO:0000313|EMBL:EIC82800.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136636 MW; C115751737B8BCD5 CRC64; MTNRVNALHE QLAKRILVLD GGMGTMIQSY RLEEEDYRGT RFADWESDLK GNNDLLVLTK PEVITAIHYG YLEAGADILE TNTFNATPIA MADYHMESLS AEINYEAARL ARICADEWTA RTPDKPRYVA GVLGPTNRTA SISPDVNDPS FRNVSFDQLV EAYRESTRAL IEGGVDLIMV ETIFDTLNAK AATFAVETVF EEMGVLLPVM ISGTITDASG RTLSGQTTEA FYNSLRHVKP LTFGLNCALG PDELRQYVAE LSRISECYVT AHPNAGLPNA FGEYDLEAKE MAEHIGEWAR SGFLNIVGGC CGTTPAHIAA MVKVLEGVPP RQLPKIPVAC RLAGLEPLTI DAQTLFVNVG ERTNVTGSAR FKKLIKEEKY LEALAVARQQ VESGAQIIDI NMDEGMLDAE AAMVKFLHLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGEEAFLKYA RKVRRYGAAM VVMAFDEVGQ ADTRARKIEI CRRAYKLLTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAV DFIEACADIK AELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYHAIRN GMDMGIVNAG QLAIYDDLST ELRDAVEDVI LNRREDGTER LLDLAEKYRG SKDDGEANKQ QAEWRGWEVK KRLEYSLVKG ITEFIELDTE EARQLAARPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLQPYIEASK EKGKTNGKIL LATVKGDVHD IGKNIVGVVL QCNNYEIIDL GVMVPTDKIL KTAIEENVDI IGLSGLITPS LDEMVNVAKE MQRRGFTIPL LIGGATTSKA HTAVKIEQNY KGSTTYVQNA SRSVGVVSAL LSDEQRDAFI EKTRKEYDTV RIQHGRKKPR TPPVSLEKAR ANASQLDWES YTPPVARHLG IHQVEASIET LRRYIDWTPF FMTWSLAGKY PRILEDEVVG EEAKRLFQDA NDLLDKLSRD KSLNPRGVFG LFPANRVDDD IEIYRDESRE EMLVVSHHLR QQTEKTDFAN YCLADFVAPK SSGKADYMGA FAVTGGLEED ALAEAYDKKH DDYNKIMIKA LSDRLAEGFA EYLHEQVRKL HWGFAADENL SNEELIRENY QGIRPAPGYP ACPEHTEKGQ IWKLLDVETH TGMQLTESFA MWPGAAVSGW YFSHPESKYF AVAQIQRDQV EDYAARKGMP ITEVERWLAP NLGYDAD // ID I0QQ79_9ENTR Unreviewed; 302 AA. AC I0QQ79; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EIC83452.1}; GN ORFNames=SPM24T3_16980 {ECO:0000313|EMBL:EIC83452.1}; OS Serratia sp. M24T3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Serratia. OX NCBI_TaxID=932213 {ECO:0000313|EMBL:EIC83452.1}; RN [1] {ECO:0000313|EMBL:EIC83452.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M24T3 {ECO:0000313|EMBL:EIC83452.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIC83452.1}. 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; AJHJ01000024; EIC83452.1; -; Genomic_DNA. DR RefSeq; WP_009638006.1; NZ_AJHJ01000024.1. DR EnsemblBacteria; EIC83452; EIC83452; SPM24T3_16980. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EIC83452.1}; KW Transferase {ECO:0000313|EMBL:EIC83452.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 207 207 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 302 AA; 32142 MW; 671AE3CC7F85B3C2 CRC64; MSKNIVILDG GMGRELARMG APFRQPEWSA LALMEAPRFV RQAHDAFISA GSQVITTNSY AVVPFHVGDE VFAERGAELI ALSGKLAREA ADAAIVPVKV GGSLPPVLGS YRPDLFEPLK AKALLEVLVA GLTDYVDFWL AETQSSIAEV ELVREVVGED ARPLWLSFTL QDTLNPQGQA LLRSGESVAD AVKAALRLSA KAVLFNCSRP EVMASAVTEA HTTAQQQDSD LDIGVYANAF EPSDNKRGAN EGLSEMRKDT DPQGYLGFAE EWVAAGATMV GGCCGIGPEH IAALTQALAS RD // ID I0R0Q6_9MICO Unreviewed; 355 AA. AC I0R0Q6; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EIC91442.1}; GN ORFNames=IMCC13023_09950 {ECO:0000313|EMBL:EIC91442.1}; OS Candidatus Aquiluna sp. IMCC13023. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Microbacteriaceae; Candidatus Aquiluna. OX NCBI_TaxID=1081644 {ECO:0000313|EMBL:EIC91442.1}; RN [1] {ECO:0000313|EMBL:EIC91442.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=IMCC13023 {ECO:0000313|EMBL:EIC91442.1}; RA Kang I., Yang S.-J., Lee K., Cho J.-C.; RT "Genome Sequence of Candidatus Aquiluna sp. strain IMCC13023."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIC91442.1}. 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; AJKR01000003; EIC91442.1; -; Genomic_DNA. DR RefSeq; WP_007541938.1; NZ_AJKR01000003.1. DR EnsemblBacteria; EIC91442; EIC91442; IMCC13023_09950. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EIC91442.1}; KW Transferase {ECO:0000313|EMBL:EIC91442.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 215 215 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 355 AA; 39011 MW; BFAA83761C8A948A CRC64; MNELTFSERL LEPEPIILSG GYLFEAERRG YLTAGEFVPL VALEHPEVLK QITTDFLRAG SDIALAFTYN GHREKLKLLG QEHLLEPLNR AAMSIAREAA SEQRAAQSRD IYVAGNISNS NIFDPADESS KSAVRQMYRE MIKWAKEEGA DLIVGETMYY FEEAKIALEE IQLAGLPSII NVAIFANGVL RDGVSAQDAC RQLAEAGADV VGTNCFHGPQ TIRPIVEAIV EATKGHNVCA MPATYRTTTK HPTLFNLPDP LNTAALRNER TFPDALEAQN SNRYETAEFG KFALGLGVKV IGLCCGASVI HHRELAEGLG RRTYLSKYSP DMSRHFLFGD EDVIPASSTQ FGSQA // ID I0RBE7_9FIRM Unreviewed; 590 AA. AC I0RBE7; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 16. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=HMPREF9970_0698 {ECO:0000313|EMBL:EIC97005.1}; OS Lachnoanaerobaculum saburreum F0468. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Lachnoanaerobaculum. OX NCBI_TaxID=1095750 {ECO:0000313|EMBL:EIC97005.1}; RN [1] {ECO:0000313|EMBL:EIC97005.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0468 {ECO:0000313|EMBL:EIC97005.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIC97005.1}. 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; AJGH01000012; EIC97005.1; -; Genomic_DNA. DR RefSeq; WP_008752938.1; NZ_AJGH01000012.1. DR EnsemblBacteria; EIC97005; EIC97005; HMPREF9970_0698. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EIC97005.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EIC97005.1}. SQ SEQUENCE 590 AA; 65707 MW; 75ED2FFF6A9AB73A CRC64; MENIRDYLKN NILLFDGAMG TYYDELTDDG IGCELANIKN PELIKGIHNE YIEAGAKAIL TNTFAVGIDV FNGDRKLQKE VIVAGIDIAN NAAKDRAYVF ADIGPIHMSR NELVFEEYKV LIDIFLEKGI KNFLFETQSN TSGMVLSAGY IKKKCSDAFI AASFAVMPDG YSSEGYQYKA LFAEVTDSGL FDAVGLNCVS GANHMAKLLR GVDTKGLYLF AKPNAGYPVV RDDRVYYSSL ANYFANQIED ILDMGVNIVG GCCGTTPKHI ELLKKSMSGK LIKPRRAIKS EKNTTQNIRL NRFKNKLESG QKAIAVELDS PIDTNVNKFI ENAKKLKLAG ADIVTIADNP IARARMDSCL LACKVRNELD FDVLPHMTCR DRNVNASRGL LLGANAMGVD NVLVITGDPI PNAQRDEIRS VFEFNSVKFA NFIKSLNEEV FESPMNICAA LNVNSRNFSA ELKKAKRKQE NGVEVLFTQP VLTKRAVENL KTARENLDIK IMGGIIPIVS ERNARYMQSE VNGIYITDDI VEKYIGKERE EAEEIALSMS KEIANEIYDL VDGYYLITVL NRVSLMERLI KTVKEVCEKR // ID I0RBF3_9FIRM Unreviewed; 788 AA. AC I0RBF3; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 12. DE SubName: Full=Homocysteine S-methyltransferase / pterin-binding enzyme / B12 binding domain / B12 binding domain multi-domain protein {ECO:0000313|EMBL:EIC97011.1}; GN ORFNames=HMPREF9970_0697 {ECO:0000313|EMBL:EIC97011.1}; OS Lachnoanaerobaculum saburreum F0468. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Lachnoanaerobaculum. OX NCBI_TaxID=1095750 {ECO:0000313|EMBL:EIC97011.1}; RN [1] {ECO:0000313|EMBL:EIC97011.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0468 {ECO:0000313|EMBL:EIC97011.1}; 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. {ECO:0000313|EMBL:EIC97011.1}. 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; AJGH01000012; EIC97011.1; -; Genomic_DNA. DR RefSeq; WP_008752944.1; NZ_AJGH01000012.1. DR EnsemblBacteria; EIC97011; EIC97011; HMPREF9970_0697. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EIC97011.1}; KW Transferase {ECO:0000313|EMBL:EIC97011.1}. SQ SEQUENCE 788 AA; 86083 MW; E2053AD3466B5E1D CRC64; MHNLLILDGA MGTMLQAAGM KAGEHPEVFG FDNPEIVKNI HLKYIESGSN VIYTNTFGAN AHKLEGCKID VDTAVKTAIK SAKEAIDESK RDVKVALDIG PIGELLEPLG VLRFEDAYEI YKEMVVAGEK YGADIIIFET FTDLYDVRAG VLAAKENTNL PVWVTMTYET TGRTFTGTKI ESMAVTLEGL GVDAIGFNCS LGPKEILPLA KKLKEWTNLP IIIKPNAGLP NPSTGEYDLH AADFAKLMAD YKSIGISYAG GCCGTSPEFI SELKKEFENR KFSEIKSTKA KTGICSANEM VELNGVRVVG ERLNPTGKKR FQEALLNHEM EYICKVAIEE EESGADILDI NVGVPGGDEV ALMIEAVKAV QSVVNIPLQI DSSNPEAIEA GLRVYNGRAI VNSVNAEDER LDLILPIVKK YGAAVIGLAL NENGIPTTAQ ERFDNAKHIL DKALEYGLKK EDVIIDCLTL TVSAQQDQAK ETLEAVRMVT KDLGLHTTLG VSNISFGLPA RSHITENFLI QAMYAGLDLP IVNPNIEGIM DAIYSFKVLS GEDKDSAKYI DRFAAVKTET KVTEVLNTGE VTKELVEDAI LKGLKEETYN NAKKLLETKG ELEIINEYLI PALDTVGDLY ERQVIFLPQL INAANAASSA FELIKERIAN KGEQNVSKGK IVVCTVKGDI HDIGKNIVKV ILENYGYRMI DLGRDVDIQR VVDTVIREDV KLVGLSALMT TTLPAMKKTI EEIRKVSKDC KVWVGGAVLT KEYADEMGAD FYAPDARSSV DIAKTVLG // ID I0RQY2_MYCXE Unreviewed; 297 AA. AC I0RQY2; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 11. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:EID13535.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EID13535.1}; GN Name=mmuM {ECO:0000313|EMBL:EID13535.1}; GN ORFNames=MXEN_10996 {ECO:0000313|EMBL:EID13535.1}; OS Mycobacterium xenopi RIVM700367. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=1150591 {ECO:0000313|EMBL:EID13535.1}; RN [1] {ECO:0000313|EMBL:EID13535.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=RIVM700367 {ECO:0000313|EMBL:EID13535.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EID13535.1}. 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; AJFI01000060; EID13535.1; -; Genomic_DNA. DR RefSeq; WP_003921034.1; NZ_AJFI01000060.1. DR EnsemblBacteria; EID13535; EID13535; MXEN_10996. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EID13535.1}; KW Transferase {ECO:0000313|EMBL:EID13535.1}. SQ SEQUENCE 297 AA; 31407 MW; EC8700C6C61E0B35 CRC64; MGFAVADDTV LIGDGGLATE LEARGHDLSD PLWSARLLID APEEITAVHA AYFRAGAMIA TTASYQASFD GFAARGIGRD DTVRLLRRSV ELAAIARDRV GANCRWVAAS VGPYGAALAD GSEYRGRYGL SVAALEAWHR PRLEVLAEAG ADVLALETVP DIDEAEALVN VVRRLAVPAW LSYTIDGTRT RAEQPLAEAF AVAAEVPEIV AVGVNCCAPD DVLHAVAAAR QTGKPVIVYP NSGERWDSAR RAWVGQSRFS PELAPKWVSA GARIVGGCCR VHPADIAAVA RAVAQAR // ID I0RSW1_MYCPH Unreviewed; 1253 AA. AC I0RSW1; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EID14214.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EID14214.1}; GN Name=metH {ECO:0000313|EMBL:EID14214.1}; GN ORFNames=MPHLEI_11619 {ECO:0000313|EMBL:EID14214.1}; OS Mycobacterium phlei RIVM601174. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=1150599 {ECO:0000313|EMBL:EID14214.1}; RN [1] {ECO:0000313|EMBL:EID14214.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=RIVM601174 {ECO:0000313|EMBL:EID14214.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EID14214.1}. 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; AJFJ01000053; EID14214.1; -; Genomic_DNA. DR RefSeq; WP_003888209.1; NZ_AJFJ01000053.1. DR EnsemblBacteria; EID14214; EID14214; MPHLEI_11619. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EID14214.1}; KW Transferase {ECO:0000313|EMBL:EID14214.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 262 262 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 325 325 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 326 326 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 782 782 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1253 AA; 138071 MW; 6EFD277ED78DF8D1 CRC64; MNAVQSTTVT SEFTPNIRPD STEELTAELR QRIMVIDGAM GTAIQRDRPD EAGYRGERFK DWPSDVVGNN DLLTLTQPQI IEGIHREYLE AGADIIETNT FNANAVSLSD YGMEELAYEL NYAGAALARK AADEFSTPER PRYVAGALGP TTRTASISPD VNDPGARNVT YDQLVDAYLT AARGLVDGGA DILIVETIFD TLNAKAAIFA IETLFEERGR RWPVIISGTI TDASGRTLSG QTTEAFWNSV RHARPLAVGL NCALGAPEMR PYIAEMARIA DTFVSCYPNA GLPNAFGEYD ESPTRQASYV EEFAEAGFVN LVGGCCGTTP AHIAEIAKVV EGKTPRKVPE VPVATRLAGL EPLNIDEDSL FVNIGERTNI TGSARFRNLI KAEDYDTALS VALQQVENGA QVIDINMDEG MIDGVAAMDR FTRLIASEPD ISRIPVMIDS SKWEVIETGL KNVQGKPIVN SISLKEGEEK FIREARLCRK YGAAVVVMAF DEEGQADNLE RRKQICGRAY RILTEEVGFP AEDIIFDPNC FALATGIEEH ASYGIDFIEA CRWIKANLPG VHISGGISNV SFSFRGNNPV REAIHAVFLY HAIEAGLDMG IVNAGALVPY DSIDPELRER IEDVVLNRRE DAAERLLEIA ERYRQSGQGA ESTDPAAAEW RSMPVRERIT HALVKGIDAH VDEDTEELRA EIAAAGGRPI EVIEGPLMDG MNVVGDLFGS GKMFLPQVVK SARVMKKAVA YLLPFIEAEK KPGDAERSNG TIIMATVKGD VHDIGKNIVG VVLQCNNYTV IDLGVMVPAQ KILDAAKEHN ADIIGLSGLI TPSLDEMANF AVEMEREGLD IPLLIGGATT SRAHTAVKIA PRRSGPVIWV KDASRSVPVA AALLDDRQRP KLLEETEKDY ASLRERHAQK NERPMVPLEK ARANRTPIDW SDYTPPVPAQ GLGVKEFHDY DLAELREYID WQPFFNAWEM KGRFPDILNN PASGEAARKL YEDAQEMLDT LIKEKWLTAN GVIGFFPANA VGDDIEVYTD ESRTEVRTVL HNLRQQGEHR DGIPNRSLGD FVAPKETGLA DYIGAFAVTA GLGSVEKIKE FKAANDDYSA ILLESLADRL AEAFAERMHQ RVRTEFWGYQ PDEQLDNEAL IAEKYRGIRP APGYPACPEH TEKVTLFELL DVTTRTGIEL TESMAMWPGA AVSGWYFSHP QSQYFVVGRL AQDQVADYAR RKGWTLREAE RWLAPNLGYN PED // ID I0S1Y1_MYCXE Unreviewed; 1192 AA. AC I0S1Y1; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase metH {ECO:0000313|EMBL:EID17384.1}; GN ORFNames=MXEN_01507 {ECO:0000313|EMBL:EID17384.1}; OS Mycobacterium xenopi RIVM700367. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=1150591 {ECO:0000313|EMBL:EID17384.1}; RN [1] {ECO:0000313|EMBL:EID17384.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=RIVM700367 {ECO:0000313|EMBL:EID17384.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EID17384.1}. 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; AJFI01000016; EID17384.1; -; Genomic_DNA. DR RefSeq; WP_003918997.1; NZ_AJFI01000016.1. DR EnsemblBacteria; EID17384; EID17384; MXEN_01507. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EID17384.1}; KW Transferase {ECO:0000313|EMBL:EID17384.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 231 231 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 297 297 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 298 298 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 742 742 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1192 AA; 130206 MW; 970DEDCBBF13FC56 CRC64; MTLVNDHAYD TDLLDALAER VMVGDGAMGT QLQAAELTLD DFRGLEGCNE ILNQTRPDVI ERIHRAYFEA GADAVETNTF GCNLSNLGDY DIADQIRELA HNGTAIARRV ADELATPDRK RYVLGSMGPG TKLPTLGHTE YALIRDAYTE AALGMLDGGA DAILVETCQD LLQLKAAVLG SRRAMAQSGR YIPVFTHVTV ETTGTMLLGS EIGAALTAVE PLGVDMIGLN CATGPAEMSE HLRHLSRHAR IPVSVMPNAG LPVLGPNGAE YPLQPDELAE ALAGFIAEFG LSLVGGCCGT TPEHIRRVAE AVRTVTPGER HITYEPSVSS LYTAVPFKQE ASVLVIGERT NANGSKAFRE AMIAEDYQKC LDIAKEQTRD GAHLLDLCVD YVGRDGVADM TALASRLATA STLPIMLDST ETAVLRAGLE HLGGRCAINS VNYEDGDGPE SRFAKTMELV AEHGAAVVAL TIDEEGQART ADKKVAIAER LIDDITRNWG VDESSILIDC LTFTIATGQE ESRRDGIETI EAIRELKKRH PNVQTTLGLS NISFGLNPAA RQVLNSVFLH ECQEAGLDSA IVHASKILPI NRIAEDQRTV ALDLIYDRRR EGYDPLQELM GLFEGVSSAS SKESRAAELA RLPVLERLAQ RIVDGERNGL EADLDEAMTL KPPLEIINDN LLAGMKTVGE LFGSGQMQLP FVLQSAEVMK AAVAYLEPHM EKSENDSGKG RIVLATVKGD VHDIGKNLVD IILSNNGYEV VNLGIKQPIA NILEVAEDKS ADVVGMSGLL VKSTVVMKEN LQEMNTRGVA GKFPVLLGGA ALTRSYVEND LAEVYEGEVH YARDAFEGLK LMDNIMSAKR GEAPDTASPE AIAAREKEAE RKARHERSKR IAAQRKATEE PIVIPERSDV AADVEVPAPP FWGSRVVKGL AVADYSALLD ERALFLGQWG LRGARGGKGP SYEELVETEG RPRLRYWLDR LSTDGILAHA AVVYGYFPAV SERDDVIVLA EPTVDAPERF RFTFPRQQRG RFLCISDFVR SRALAAERGQ VDVLPFQLVT MGDPIAEFAN QLFASNSYRD YLEVHGIGVQ LTEALAEYWH RRIREELRFA GDRAMAAEDP ETKEDYFKLG YRGARFSFGY GACPDLEDRV KTMALLQPER IGVTLSEEMQ LHPEQSTDAF ILHHPEAKYF NV // ID I0TF63_9BACT Unreviewed; 914 AA. AC I0TF63; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 01-APR-2015, entry version 16. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EID34266.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EID34266.1}; GN Name=metH {ECO:0000313|EMBL:EID34266.1}; GN ORFNames=HMPREF9969_1283 {ECO:0000313|EMBL:EID34266.1}; OS Prevotella sp. oral taxon 306 str. F0472. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=1095752 {ECO:0000313|EMBL:EID34266.1}; RN [1] {ECO:0000313|EMBL:EID34266.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F0472 {ECO:0000313|EMBL:EID34266.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EID34266.1}. 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; AJIN01000011; EID34266.1; -; Genomic_DNA. DR EnsemblBacteria; EID34266; EID34266; HMPREF9969_1283. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EID34266.1}; KW Transferase {ECO:0000313|EMBL:EID34266.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 240 240 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 757 757 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 914 AA; 101331 MW; 199E74F7F3B23B4C CRC64; MTIRDSIKER ILILDGAMGT MIQGYKLTEM DFRGNLELLQ MLNYQGNNDM LNLTRPDIIE DIHRRYLKAG ADIISTNTFS AQRISQADYH MEDFSYDIAL LGAKLARKCA DEYSTTNKPR FVAGSIGPTN KTCSMSPDVS DPAKRDLTYD TLFHAYSEQV EAMIKGGIDA ILIETIFDTL NAKVAIDASL SEMRKMGIDL PIMLSVTITD LSGRTLSGQT LEAFLASISS YPIFSVGLNC SFGAEQMRPY IKELASKAPY YISIYPNAGL PNSMGEYDET AEVMVPQIQT YVDEGLVNII GGCCGTTDEF IAGYTKIVKD QLPHVPTPVS KEMILSGLEQ FRLTPEITFV NVGERCNVAG SRKFLRLIKE HNYEEALTIA RKQVDDGALV LDINMDDGLL EAKDEMVHFV NMISSEPEIA RVPLMIDSSD WDVVVAALKC VQGKSIVNSI SLKEGEETFI RHAKDVLRYG AAVVVMCFDE EGQATSFERR IEIASRAYKI LTEQVGIQAK DIIFDPNILA ICTGMKEHNN YAVEFIRATE WIKKNLPGAH ISGGVSNLSF SFRGNNYIRE AMHAVFLYHA IQVGMDFGIV NPATKITYAD IPQDELKIIE DVVLDREEGA DEKLIELANR ILAQKDILKQ NGKESNQQEE WRNSSLEDRL VYALRKGISN YLNDDIHEAL EKYPNAVSII EGPLMRGMNE VGDLFGAGKM FLPQVVKTAR TMKDAVAILQ PYIEKEKVGG KATAGKVLLA TVKGDVHDIG KNIVGVVMAC NNYEVIDMGV MVPADKIIKK AKEECVDLIG LSGLITPSLH EMVNDVIAFK EAGLHIPVMV GGATTSKLHV ALKIAPLYDA PVVWVKDASV NPSIAASLLN EAERPAFCEE LNKSYEELRA NYKEQQQKIL SLEKARENKL NLFD // ID I0V360_9PSEU Unreviewed; 330 AA. AC I0V360; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 12. DE SubName: Full=Homocysteine/selenocysteine methylase (S-methylmethionine-dependent) {ECO:0000313|EMBL:EID54563.1}; GN ORFNames=SacxiDRAFT_2334 {ECO:0000313|EMBL:EID54563.1}; OS Saccharomonospora xinjiangensis XJ-54. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Pseudonocardineae; Pseudonocardiaceae; Saccharomonospora. OX NCBI_TaxID=882086 {ECO:0000313|EMBL:EID54563.1}; RN [1] {ECO:0000313|EMBL:EID54563.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=XJ-54 {ECO:0000313|EMBL:EID54563.1}; 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 ----------------------------------------------------------------------- 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; EID54563.1; -; Genomic_DNA. DR RefSeq; WP_006238710.1; NZ_JH636049.1. DR EnsemblBacteria; EID54563; EID54563; SacxiDRAFT_2334. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EID54563.1}; KW Transferase {ECO:0000313|EMBL:EID54563.1}. SQ SEQUENCE 330 AA; 34543 MW; B1BCFD4C1A9665C4 CRC64; MKCRHPCRKC GHPCRKCGHG GLGSLTAPLI TVGFVELAGL FDGNAVVSDG GLATELETRH DLGDALWSAR LLLDAPEEIV AAHRAFFDAG AVIATTASYQ ASYSGFAARG IDRKAATALL HRSVELARQA RDEVAGDGVR RWVAASVGPY GAALADGSEY RGDYGLSVTA LRDWHLPRIE ALVEAEPDLL AVETVPDVVE AEALVAALGG ADVPAWLTYN VEGDRTRAGQ PLTEAFAVAA EAPEVVAVGV NCCAPDDVAG ALACARQVTD KPLVAYPNSG EGWDHDLRSW TGPATFSPEH LREWIAEGAQ VVGGCCRVGP ADIAALTRAL // ID I0V6F1_9PSEU Unreviewed; 1182 AA. AC I0V6F1; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EID55704.1}; GN ORFNames=SacxiDRAFT_3505 {ECO:0000313|EMBL:EID55704.1}; OS Saccharomonospora xinjiangensis XJ-54. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Pseudonocardineae; Pseudonocardiaceae; Saccharomonospora. OX NCBI_TaxID=882086 {ECO:0000313|EMBL:EID55704.1}; RN [1] {ECO:0000313|EMBL:EID55704.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=XJ-54 {ECO:0000313|EMBL:EID55704.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; JH636049; EID55704.1; -; Genomic_DNA. DR RefSeq; WP_006239886.1; NZ_JH636049.1. DR EnsemblBacteria; EID55704; EID55704; SacxiDRAFT_3505. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EID55704.1}; KW Transferase {ECO:0000313|EMBL:EID55704.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 223 223 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 733 733 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1182 AA; 130015 MW; C1D9506A93CAAC02 CRC64; MDSRFLAELD RRVLVADGGM GTALQEFDLT LDDFAQLEGC NEILNDTRPD VVSAVYRSFL EAGSDAIETN TFGTNYGNFG EYGILDRIRE LAEKGTTLAR RCADEYSTRD KPRFVLGSMG PGTKLPTLGH APYSVLRDAY VENALGMLDG GVDAVLVETS QDLLQTKAAV VGAKRAMAVA GRRVPIIAQV TVEQTGTMLV GSEIGAALTA LEPLGIDLIG MNCATGPAEM SEHLRVLSDH ARVPLSVMPN AGLPELGPNG AVYPLSPDEL AEALATFVRD FGARLVGGCC GTTPEHLRAV VDAVSALPPR QRTPRHLPSM SSVYQSVPFE QDASILNVGE RTNANGSKKF REAMLDERYD DCVEIAKAQT REGAHVLDLC VDYVGRDGTR DMAELASRLA TASTLPIMVD STEPDVVRTG LEHLGGRCAI NSVNYEDGTG QESRYQRVME LAVEHGAAVV VTCIDEEGQA RTADWKVRIA ERAIEDLTTN WGLDISSIII DCLVFPITTG QEEVRKDAAE TIEAIRTLKT RHPDVLTTLG LSNVSFGLNP AARQVLNSVF LHECREAGLD SAILNSSKIL PMNKIDDEAR QVALDLVYDR RRDGYDPLQR LMGLFEGKTA SSTRESRAEE LAKLPLFERL EKRIVEGEVN GLEADLDAAM RQKKPIDIIN ENLLAGMKVV GDLFGSGQMQ LPFVLQSAEV MKTAVAYLEP HMEKTDSGGK GKLLLATVKG DVHDIGKNLV DIIVSNNGYD VVNIGIKQPI NAILEAAEEH RVDAIGMSGL LVKSTVIMKD NLQEMNARGV ARRYPVLLGG AALTRTYVEN DLDDVYEGEV RYAKDAFEGL KLMDRVMAVK RGEVGEEDEA ERAKRAERKA RRERSLRIAE KRKAEQGPEP DLYDTTRSDV DPDVAVPTPP FWGAKVVKGI AVADYLSLLD ERATFFGQWG LRGARDGEGP SYEELVESEG RPRLRAWIDE LSTQGVLAHA ALVYGYFPCY SDGNDLVVLE KDEPDALERL RFTFPRQRRD RRLCLADFFR SREKAEQTGQ VDVLPVQLVT MGQPIADHAN ELFASNAYRD YLEIHGLGVQ LTEALAEYWH RRIRQELRFA SGAPVAAEDP DDLREFFRLG YRGARFSFGY GACPDLEDRA KIVELLGAER IGVTLSEEFQ LHPEQSTDAI VAHHPEAKYF NT // ID I0VXY4_ECOLX Unreviewed; 795 AA. AC I0VXY4; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 04-FEB-2015, entry version 16. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EID69000.1}; GN ORFNames=ECW26_05720 {ECO:0000313|EMBL:EID69000.1}; OS Escherichia coli W26. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1090926 {ECO:0000313|EMBL:EID69000.1}; RN [1] {ECO:0000313|EMBL:EID69000.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=W26 {ECO:0000313|EMBL:EID69000.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EID69000.1}. 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; AGIA01000012; EID69000.1; -; Genomic_DNA. DR EnsemblBacteria; EID69000; EID69000; ECW26_05720. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 795 AA; 87524 MW; BA1BB24BEFE7F05D CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKISLAWCC NVTTTKLSIS ALWCLRKKFS VPLKK // ID I0WKI1_9FLAO Unreviewed; 338 AA. AC I0WKI1; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EID76897.1}; GN ORFNames=W5A_02700 {ECO:0000313|EMBL:EID76897.1}; OS Imtechella halotolerans K1. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Imtechella. OX NCBI_TaxID=946077 {ECO:0000313|EMBL:EID76897.1}; RN [1] {ECO:0000313|EMBL:EID76897.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=K1 {ECO:0000313|EMBL:EID76897.1}; 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. {ECO:0000313|EMBL:EID76897.1}. 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; AJJU01000002; EID76897.1; -; Genomic_DNA. DR RefSeq; WP_008237141.1; NZ_AJJU01000002.1. DR EnsemblBacteria; EID76897; EID76897; W5A_02700. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EID76897.1}; KW Transferase {ECO:0000313|EMBL:EID76897.1}. SQ SEQUENCE 338 AA; 37325 MW; FC8662029924203C CRC64; MSIETRTTGK ITINKLLQER ILVLDGAMGT MLQRYKFTEE DFRGERFKDF PHPLKGNNDL LSLTQPQAIG DIHRKYLEAG ADIVETNTFS STTIGMADYH MESLVYELNF ESARIAREIA DEFTASNPDK PRFVAGSIGP TNRTASMSPD VNDPGFRAVT FEDLRVAYRQ QVEALLDGGA DILLVETVFD TLNAKAAIYA IEEVKEERGI EVPIMVSGTI TDASGRTLSG QTVEAFLISI SHIPLLSIGF NCALGANMLK PYLKRLANDT QFYVSAHPNA GLPNAFGEYD ETPEEMSAQI KEYLDENMIN IIGGCCGTNP DHIRLIAELA ATYTPRKL // ID I0WMS8_9NOCA Unreviewed; 1189 AA. AC I0WMS8; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 20. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EID77694.1}; GN ORFNames=W59_22133 {ECO:0000313|EMBL:EID77694.1}; OS Rhodococcus imtechensis RKJ300 = JCM 13270. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Nocardiaceae; Rhodococcus. OX NCBI_TaxID=1165867 {ECO:0000313|EMBL:EID77694.1}; RN [1] {ECO:0000313|EMBL:EID77694.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=RKJ300 {ECO:0000313|EMBL:EID77694.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EID77694.1}. 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; AJJH01000125; EID77694.1; -; Genomic_DNA. DR RefSeq; WP_007299047.1; NZ_AJJH01000125.1. DR EnsemblBacteria; EID77694; EID77694; W59_22133. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 229 229 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 296 296 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 739 739 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1189 AA; 129659 MW; 6124D869A7121736 CRC64; MSAPFHSALL DALNQRVVIG DGAMGTMLQA ADLTLDDFLG LEGCNEILND TRPDVLKDIH RAYFEAGADA VETNTFGCNL PNLADYDISD RIRELAEKGT RLARDVADEM GPGRDGIGRF VLGSMGPGTK LPTLGHAPFA VLRDAYAEAA MGMIDGGADA ILVETCQDLL QVKAAILGSQ RAMETLGSRL PIITHVTVET TGTMLLGSEI GAALTALEPL GIDMIGLNCA TGPAEMSEHL RHLSKYSSLP VSVMPNAGLP QLGPNGAEYP LTAEELAEAL SGFVTEFGLG LVGGCCGTTP EHIRQVAEAV RLVEKAERNP VHESGTSSLY TAVPFQQDAS ILMIGERTNT NGSKAFREAM IAEDYQKCLD IAKDQTRDGA HMLDLNVDYV GRDGAVDMAA LASRFATSST LPIMLDSTEP AVLQAGLEHL GGRCAVNSVN YEDGDGPDSR FQKIMRLVTE HGAAVVALTI DEEGQARTAE HKVRIAERLL EDLTVNWGLD ESDIIIDALT FPISTGQEEV RRDGIETIEA IRELKKRHPR VHFTLGVSNI SFGLNPAARQ VLNSVFLHEC TEAGLDTAIV HASKILPMAR IPDEQRETAL DLVYDRRREG YDPLQKLMEL FEGVSAASAR ESRAQELAAL PLFERLERRI VDGERNGLDD DLTAAMEEKP PLAIINETLL SGMKTVGELF GSGQMQLPFV LQSAEVMKAA VAYLEPHMEA TDEDGKGRIV IATVKGDVHD IGKNLVDIIL SNNGYDVVNL GIKQPIATIL DAAIEQKADV IGMSGLLVKS TVVMKDNLQE LNAKGVAEKF PVLLGGAALT RSYVENDLAE VYEGDVSYAR DAFEGLHRMD EIMAVKRGGG PDPDSPEAIA AREKAAERKA RHERSKRIAE KRKAAETPIE VPERSDVATD IVVPTPPFWG NRIVKGVSLS DYSGLLDERA LFLGQWGLRG QRSGDGPTYE ELVETEGRPR LRYWLDRLST EGILAHAAVV YGYFPAVSEG DDVVVLTDPT PDAEERFRFT FPRQHRDRFL CVADFVRSRT EAKETGQVDV FPMQLVTMGQ PIADFANELF AANAYRDYLE VHGIGVQLTE SLAEYWHQRV REELVLPGGH NVAEQDPSEV SGFFDLAYRG ARYSFGYGAC PNLEDRAKMV ALLEPERIGV KLSEELQLHP EQSTDAFVLH HPEAKYFNV // ID I0X8T3_9SPIO Unreviewed; 840 AA. AC I0X8T3; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 01-APR-2015, entry version 14. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EID85049.1}; GN ORFNames=MSI_14350 {ECO:0000313|EMBL:EID85049.1}; OS Treponema sp. JC4. OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema. OX NCBI_TaxID=1124982 {ECO:0000313|EMBL:EID85049.1}; RN [1] {ECO:0000313|EMBL:EID85049.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=JC4 {ECO:0000313|EMBL:EID85049.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EID85049.1}. 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; AJGU01000013; EID85049.1; -; Genomic_DNA. DR RefSeq; WP_009105237.1; NZ_AJGU01000013.1. DR EnsemblBacteria; EID85049; EID85049; MSI_14350. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EID85049.1}; KW Transferase {ECO:0000313|EMBL:EID85049.1}. SQ SEQUENCE 840 AA; 89413 MW; A6F2303EEB63842C CRC64; MAKAVLAKDI FKKAYSDFVF IDGGCGSILQ AQGLQPGELP ETWNILHPEI IQKMHRDYLL AGANILTSNT FGANINKFQP GDIKFSLDAV IGAAIKNARQ AIADVESDPA TPEIVRNQPH FVALDIGPLG KLLKPLGDLD FEDAVKIFSY TVKIGAKHGA DLVLIETMND LHEAKAALLA AKENCELPVL ITTAYDESEK LLTGADPMTV VATMEGLGAD AVGVNCSLGP DQMFGIVEQL ARYASVPVVV SPNAGLPRSE GGKTVYDVAP ADFAASMEKI ADLGATMLGG CCGTTPAHIK AMSDAVRTHK AHEVTPKNDT IITSYTHSVI FDKKPVLIGE RINPTGKKKF KEALRNRDMD YILGEALTQK EKKADVLDVN VGLPEIDEPQ MMIDVVKELQ AVIDLPLQID TTNPVAMEKA LRIYNGKPMI NSVNGKEEIM KEIFPLAKKY GGLIVALTID ESGIPETAQG RVEIARKIYA RAAEYGIKPK DIIIDPLAMS ISSDPQSAIT TLDALRLIKE QLNGKTSLGV SNISFGLPQR DFVNASFFTM AMHNGLNAGI MNPGSLEMMK AYYTYCALLA VDQNCANYID FATNLPATVA APVAAAGSAG GSAPAAAGSG AVSAAAVSAG GSANTSELIE AIKRGLKDRA AALTGEYLKS KDALQIIDGE LIPALDIVGK GFEKKTVFLP QLLMAAEAAS AAFGVIKQTL AAAGGDQQKK GKIVLATVKG DIHDIGKNIV KVLLENYAYD VIDLGKDVDP QLIVETVQRE NIRLVGLSAL MTTTVPAMEE TIKLLREAGS PAKVVVGGAV MTQNYADMIG ADKYCHDAME TVRYAEEIFA // ID I0XQ28_9LEPT Unreviewed; 1245 AA. AC I0XQ28; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EIE00986.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EIE00986.1}; GN Name=metH {ECO:0000313|EMBL:EIE00986.1}; GN ORFNames=LEP1GSC185_3695 {ECO:0000313|EMBL:EIE00986.1}; OS Leptospira licerasiae serovar Varillal str. VAR 010. OC Bacteria; Spirochaetes; Spirochaetales; Leptospiraceae; Leptospira. OX NCBI_TaxID=1049972 {ECO:0000313|EMBL:EIE00986.1, ECO:0000313|Proteomes:UP000004889}; RN [1] {ECO:0000313|EMBL:EIE00986.1, ECO:0000313|Proteomes:UP000004889} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VAR 010 {ECO:0000313|EMBL:EIE00986.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EIE00986.1}. 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; AHOO02000009; EIE00986.1; -; Genomic_DNA. DR RefSeq; WP_008596744.1; NZ_AHOO02000009.1. DR EnsemblBacteria; EIE00986; EIE00986; LEP1GSC185_3695. DR Proteomes; UP000004889; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000004889}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EIE00986.1}; KW Transferase {ECO:0000313|EMBL:EIE00986.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 255 255 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 318 318 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 319 319 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 767 767 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1245 AA; 138782 MW; 276EE16E0033BC54 CRC64; MKHKFPTYTN PKAQELLKLL EERILVLDGA MGTMIQRYGL GEEDFRDERL KDHPSALKGN NDLLVITKPE VIEEIHYKFL EAGANILETN TFSSNRISQA DYNAEAYVDE LNRKAVKVAR AAMEKFSKTH PDQPLFLAGS IGPTTRTASL SPDVNNPAFR AVTFDELVET FYEQVRALVE EGVDILLSET NIDTLNLKAI IVAIENVFKD LNVRIPVSLS VTITDASGRT LSGQTIEAFY NSIYHANPLS VGINCALGAG EMRPYIEELS RISGCYISCY PNAGLPNAFG GYDQTPEEFG SFLDDFSNQG WLNIAGGCCG TTPAHIKEGA KAVQGKKPRV IPEIEGKTRL SGLEPLNIDE ATGFVLIGER TNVTGSPKFK KLILEGNFEE AVSVALQQVE AGANIIDINF DEALLDGEAS MREFLNLIAV EPDIAKVPFM VDSSKWSVLE TGLKCIQGKP IVNSISLKEG EEKFLQQAKT IKMYGASVIV MAFDEQGQAA TKDDKVRICK RAYDLLVEKA NFSPFDIIFD PNILTVGTGI EEHNNYAVDF IEAIKEIKAV CPGAKISGGL SNISFSFRGN NPVREAMHSA FLFHAIKAGM DMAIVNAGML AVYEEIPKDL LERVEDVLLN RRSDATERLI EFAESFKSGE KAEKKEEAWR EGTVEQRLEY SLVKGIVEYI DQDTEEARLK YDQPLQVIEG PLMDGMRVVG DLFGSGKMFL PQVVKSARVM KKSVAYLLPF MEEENRKQAQ ISKKQKFLIA TVKGDVHDIG KNIVAVVLAC NNYEVIDLGV MVPCEKILEE ARKENVDIIG LSGLITPSLD EMVHVASEMK RTGFDIPLLI GGATTSSAHT SVKISEKYDQ PVVHVLDASR VVNVVGKLLN PSLKPDYIKQ IKEEQKIQRE IYFNTRSDRK LVSIEDAREN RYVTDWNVSK VTKPNFVGVR VFDNEISLEE LVPFIDWSPF FQAWELKGRY PSILESETYG KQAKELFKDA QKLLEDIVSN KRYTTRGVIG VFPANSVGDD IEVYEDETRT KIKTVFHTLR QQISKEEKDE PNYCLADYIA PKESGIADYI GGFAVTAGHG VEAFASIFDS RLDDYNSIMA KALGDRFAEA FAEYMHLKIR KEIWGYAADE NLSTEELIRE RYQGIRPAAG YPASPDHTEK RTLFDLLEVE KNTGITLTEH FAMMPASSVS GLYFAHPAAK YFAVAKINKD QIQDYANRKG MTVSDVEKWL SPNLAYDPQE AVSRV // ID I0YMA9_9CHLO Unreviewed; 296 AA. AC I0YMA9; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 01-OCT-2014, entry version 12. DE SubName: Full=Homocysteine S-methyltransferase AtHMT-1 {ECO:0000313|EMBL:EIE19528.1}; GN ORFNames=COCSUDRAFT_38052 {ECO:0000313|EMBL:EIE19528.1}; OS Coccomyxa subellipsoidea C-169. OC Eukaryota; Viridiplantae; Chlorophyta; Trebouxiophyceae; OC Coccomyxaceae; Coccomyxa. OX NCBI_TaxID=574566 {ECO:0000313|EMBL:EIE19528.1}; RN [1] {ECO:0000313|EMBL:EIE19528.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C-169 {ECO:0000313|EMBL:EIE19528.1}; 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. {ECO:0000313|EMBL:EIE19528.1}. 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; AGSI01000018; EIE19528.1; -; Genomic_DNA. DR RefSeq; XP_005644072.1; XM_005644015.1. DR GeneID; 17037500; -. DR KEGG; csl:COCSUDRAFT_38052; -. DR KO; K00547; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EIE19528.1}; KW Transferase {ECO:0000313|EMBL:EIE19528.1}. SQ SEQUENCE 296 AA; 31904 MW; E3330833233A6F5C CRC64; MTTAVTQDRL WSARMLAEDP AAVTQVHAAF YEAGADVATT ASYQASFKGF EQAGFGRADA EELLRKSVQL ADNARRLFWS EGSELHGWRA KRLRPLVAFS AGPYGAALAD GSEYDGSYAE RVSEEQLMDF HRQRLQAIVG APGVDLIAFE TVPCLKELRA ISRLLCTEQL GIPAWISCSA RSGTAICHGE DLLEECLPVM CEPASVVAVG VNCLPPQLVD PLIKQGLPTK LLLAYPNSGE EWDAAARDWK GSSGLEVQNF GCSARQWADS GASIIGGCCR TTPEHIRSVA ECLADP // ID I1AVG6_9RHOB Unreviewed; 1254 AA. AC I1AVG6; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 01-APR-2015, entry version 18. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EIE50487.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EIE50487.1}; GN Name=metH {ECO:0000313|EMBL:EIE50487.1}; GN ORFNames=C357_13977 {ECO:0000313|EMBL:EIE50487.1}; OS Citreicella sp. 357. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Citreicella. OX NCBI_TaxID=766499 {ECO:0000313|EMBL:EIE50487.1}; RN [1] {ECO:0000313|EMBL:EIE50487.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=357 {ECO:0000313|EMBL:EIE50487.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EIE50487.1}. 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; AJKJ01000110; EIE50487.1; -; Genomic_DNA. DR RefSeq; WP_009505272.1; NZ_AJKJ01000110.1. DR EnsemblBacteria; EIE50487; EIE50487; C357_13977. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EIE50487.1}; KW Transferase {ECO:0000313|EMBL:EIE50487.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 261 261 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 325 325 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 780 780 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1254 AA; 135940 MW; E9794D93BA36D432 CRC64; MTRTAPVRSS VFDQLEKAAS DRILILDGAM GTQIQQLGLA EGDFQGCGGG ACSCHLPHAS DKPQQGNNDI LNLTAPDKVE EIHYLYAMAG ADIVETNTFS STTIAQADYD MQGAVHDLNV AGARIARKAM DRAEATDGRA RFVAGALGPT NRTASISPDV NNPGYRAVSF DDLRAAYAEQ LHGLIEGGID IVLIETIFDT LNAKAAIFAC EEVFEQTGTR LPVMISGTIT DLSGRTLSGQ TPTAFWHSVR HAQPWTIGLN CALGADAMRP HLAEISGVAD TLTCAYPNAG LPNEMGEYDQ TPEEMADLIA GFAREGLLNV VGGCCGSTYD HIAAVAKAVE GHAPRAIPAH KPLMGLSGLE PFTLTSDIPF VNVGERTNVT GSARFRKLVT NADYAAALDV ARDQVENGAQ IIDINMDEGL IDSKQAMVEF LNLIAAEPDI ARVPIMIDSS KWEIIEAGLK CVQGKSVVNS ISMKEGEEAF LHQATLCRRY GAAVIVMAFD EKGQADTEDR KVEICTRAYK LLTEQVGFPP EDIIFDPNVF AVATGIEEHD NYGVDFIEAT RRITTDCPHV HISGGVSNLS FSFRGNEPVR EAMHAVFLYH AIQNGMDMGI VNAGQLAVYD QIDADLREAC EDVVLNRTPA SGTPTENLLD IAERYRGKDG AKGREKDLSW RELPVEKRME HALVNGITEY IDADTEEARL QADRPLHVIE GPLMAGMNVV GDLFGAGKMF LPQVVKSARV MKQAVALLLP YMEEEKRLNG GSGRESAGKV LMATVKGDVH DIGKNIVGVV LACNNYEIID LGVMVPAEKI LATARAEGVD VIGLSGLITP SLDEMVHVAS EMERTGFDIP LLIGGATTSR VHTAVKIHPR YGKGQAVYVT DASRAVGVVS SLLSPTQKPG YVANIRGEYA DVAQKHARAE LAKKRISVEQ ARDNALKLDF DNHAPAPSFL GNKTLADWDL AELADYIDWT PFFQTWELKG IYPKILNDEK QGEAARALFA DAQAMLNQII AEKWFTPRAV VGFWPANATG DDIAVFTDET RSMPLATLHT LRQQTAKRDG RPNVALSDFV APIGKPDYVG GFVVTAGAEE ETIAKRFEAE NDDYAAIMVK ALADRFAEAL AERMHEKVRR ELWGYAPDES LSPADLIAEK YDGIRPAPGY PAQPDHTEKR TLFDLLGATE ATGVELTESF AMWPGSSVSG LYIGHPDSYY FGVARVERDQ VEDYAARKGM SLTDAERWLA PILNYVPTKA VAAE // ID I1CCM8_RHIO9 Unreviewed; 1222 AA. AC I1CCM8; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 01-APR-2015, entry version 22. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EIE86208.1}; GN ORFNames=RO3G_10919 {ECO:0000313|EMBL:EIE86208.1}; 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 {ECO:0000313|EMBL:EIE86208.1, ECO:0000313|Proteomes:UP000009138}; RN [1] {ECO:0000313|EMBL:EIE86208.1, ECO:0000313|Proteomes:UP000009138} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880 RC {ECO:0000313|Proteomes:UP000009138}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CH476739; EIE86208.1; -; Genomic_DNA. DR InParanoid; I1CCM8; -. DR OrthoDB; EOG7XH70V; -. DR Proteomes; UP000009138; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000009138}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000009138}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 231 231 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 747 747 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1222 AA; 135835 MW; 5E0D67AFB65A2E8F CRC64; MFLDGAMGTM VQRLKLEESD FRGQEFLDWP TDLRGNNDLL TLTKPDAIYH IHRQYLEAGA DMIETNTFSS TSIAQLDYSL EKYAYRLNKE GAALAKKACE DVTKETGIRR FVCGAIGPTN RTCSISPSVE NPAYRNVTFD ELVTAYSEQV RGLLDGGSDI LLVETIFDTL NAKAAIFAID LVFEEDNRPK VPIFISGTIV DQSGRTLSGQ TGEAFVTSLN HARPVAFGLN CALGAEQMKP FVQNISRFTD AHIICYPNAG LPNAMGEYDE SPEAMAKNVE PFAKEGLVTI VGGCCGTTPD HIKAVAEVCR QYSPRRKPAS KQDVMLLSGL EVLRVNETTG FVNVGERCNV AGSRKFCRHI LKNEYEEALA IARAQVESGA QVVDVNFDEG LLDGKAAMTK FLNMLASDPD CARVPLMVDS SNFAVIEAGL RCAQGKCIVN SISLKEGEEE FIKKAKIIKR FGAAVVVMAF DEVGQAAEAD RKVEICTRSY RILVDKVGFN PYDIIFDPNI LTIATGMEEH NNYAVEFIQA CETIKKTLPG AKVSGGVSNL SFAFRGMDKV REAMHSVFLY YTVKVGMDMG IVNAGFLTVY DDIPKDLLQL CEDAVWNRDP DVTEKLLEYA KAHSKDAKKD EDQEEWRTWA VTERITHALV KGIMKFIVED TEEARSDKEK YPRALNVIEG PLMTGMNVVG DLFGKVHVMI ISVMKKAVAH LVEYIKLEKE ADMALSGETE IKGNGTIVMA TVKGDVHDIG KNICGVVLGC NNYRVIDLGV MVPCDKIIKT AIEEKADVIG LSGLITPSLE EMVIVAKECE KAGIKIPILI GGATTSKMHT AVKIAPQYSC PAIYVLDASR SVPVVASLLD DNLKEEFAED IRDEYEEMRE EYYEGLEERH LLSIENAREK KLKINWALSP PPNKPTFLGT KVYNNYPLEK LVDHIDWNPF FQVFQLRGRY PNRGFPKIFD DEHVGPEAKR LYDDAQEMLK TIVDKKLLTA RGIVGFYPAH AAGDDILIYK DEDREEVSAV FYGLRQQAEK EVDEPYYCLS DFVAPKETGI PDYLGMFAVS TGFGCDELVE QYEKDGDDYN SIMAKALADR LAEAFAELLH EEVRKVEWGY ASEEHLSSSE LFSVRYQGIR PAPGYPSQPD HTEKKTMWDL GQIAEKTGIT LTESLAMDPP ASVSGLIFGH EQSKYFAVGK IEKDQIEDYA ERKKMDVPTV EKWLGTILAY DA // ID I1CMM3_RHIO9 Unreviewed; 291 AA. AC I1CMM3; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 07-JAN-2015, entry version 14. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EIE89703.1}; GN ORFNames=RO3G_14414 {ECO:0000313|EMBL:EIE89703.1}; 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 {ECO:0000313|EMBL:EIE89703.1, ECO:0000313|Proteomes:UP000009138}; RN [1] {ECO:0000313|EMBL:EIE89703.1, ECO:0000313|Proteomes:UP000009138} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880 RC {ECO:0000313|Proteomes:UP000009138}; 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; CH476745; EIE89703.1; -; Genomic_DNA. DR InParanoid; I1CMM3; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000009138; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009138}; KW Reference proteome {ECO:0000313|Proteomes:UP000009138}. SQ SEQUENCE 291 AA; 32415 MW; 187E48F84680F7DE CRC64; MSFQYPIVLD GGFATELEKQ FKKDLSGANV ATTCSYQASI EGFLQAGYTR EHGVELMNKS ISLACEARDE FRKEHPEDKE ERLVALSIGC YGAILANGSE YTGDYGNITI DRLVQFHKDR LEIFLGNKGV DFVLFETIPS VLEAEAIVKI MKEMNDLPPV GVAFQCRSDH QIADGTDLLY VLSLFDKLDC VFAVGVNCTK PQHIERLVSR IVEVNKEKED KKALLLYPDG GEVWDAVARS WDSSCKLAKD KFGFLLSKCV QDYDSRVLVG GCCGTGPDHI KSLKSYLSRK Q // ID I1D4R3_9PSEU Unreviewed; 1182 AA. AC I1D4R3; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EIE99937.1}; GN ORFNames=SacglDRAFT_03071 {ECO:0000313|EMBL:EIE99937.1}; OS Saccharomonospora glauca K62. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Pseudonocardineae; Pseudonocardiaceae; Saccharomonospora. OX NCBI_TaxID=928724 {ECO:0000313|EMBL:EIE99937.1, ECO:0000313|Proteomes:UP000005087}; RN [1] {ECO:0000313|EMBL:EIE99937.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=K62 {ECO:0000313|EMBL:EIE99937.1}; 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] {ECO:0000313|EMBL:EIE99937.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=K62 {ECO:0000313|EMBL:EIE99937.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CM001484; EIE99937.1; -; Genomic_DNA. DR RefSeq; WP_005465636.1; NZ_CM001484.1. DR EnsemblBacteria; EIE99937; EIE99937; SacglDRAFT_03071. DR Proteomes; UP000005087; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000005087}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EIE99937.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005087}; KW Transferase {ECO:0000313|EMBL:EIE99937.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 223 223 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 733 733 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1182 AA; 130193 MW; 3FCE8BE7ACB1F284 CRC64; MDSRFLAELG QRILVADGGM GTALQGFDLS LDDFAQLEGC NEILNDTRPD VVSAVHRSFL EVGCDAIETN TFGTNYGNFG EYGILDRIRE LAEKGTVLAR RCADEYSTPE RPRFVLGSMG PGTKLPTLGH APYAVLRDAY VENALGMLDG GVDAVLVETS QDLLQTKAAV VGAKRAMERA GRRVPIIAQV TVEQTGTMLV GSEIGAALTA LEPLGIDMIG MNCATGPTEM SEHLRVLSEH ARVPISVMPN AGLPELGPDG AVYPLRPDEL AEALATFVTD FGARLVGGCC GTTPEHLRAV VEAVSSLPGK ERRPRHQPSL SSVYQPVPFE QDASILNVGE RTNANGSKKF REAMLDERYD DCVEIAKAQT REGAHVLDLC VDYVGRDGTR DMAELASRLA TASTLPIMVD STEPEVVRTG LEHLGGRCAI NSVNYEDGTG PGSRYQRIME LAVEHGAAVV VTCIDEEGQA RTADWKLRVA ERAIEDLTTN WGLAKSSIII DCLVFPITTG QEEVRRDALE TIEAIRELKK RHPDVLTTLG LSNVSFGLNP AARQVLNSVF LHECRQAGLD SAILNSSKIL PMNKIDDEAR QVALDLVYDR RRDGYDPLQR LMELFEGKTA SSARASRAEE LAKLPLFERL EKRIVEGEVN GLEADLDAAM REKSPIDIIN ENLLAGMKVV GDLFGSGQMQ LPFVLASAEV MKTAVAYLEP HMEKTDAGGK GKLLLATVKG DVHDIGKNLV DIIVSNNGYD VVNIGIKQPI NAILEAAEKH RVDVIGMSGL LVKSTVVMKE NLQEMNSRGV AKKYPVLLGG AALTRTYVEN DLDEIYEGDV RYAKDAFEGL KLMDRVMAIK RGETPEEDEA ERAKKAERKA RRERSLRIAE KRRAEQGPEA DPNDTTRSDV DPDVPVPTPP FWGSKIVKGI AVADYLALLD ERATFLGQWG LRGARKGEGP SYEELVETEG RPRLRAWIDE LSTRGVLAHA AVVYGYFPCY SEGNDLVVVE KDEPDALERL RFRFPRQRRD RRLCLADFFR PREKVESTGQ VDVLPLQLVT MGQPIADYAN ELFARNSYRD YLEVHGLGVQ LTEALAEYWH RRIRQELRFP SGTPVAAEDP EDVQQFFKLG YRGARFSLGY GACPNLEDRT KIMELLDAER IGVTLSEEFQ LHPEQATDAI VAHHPEAKYF NT // ID I1D7P9_9PSEU Unreviewed; 294 AA. AC I1D7P9; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 15. DE SubName: Full=Homocysteine/selenocysteine methylase (S-methylmethionine-dependent) {ECO:0000313|EMBL:EIF00974.1}; GN ORFNames=SacglDRAFT_04142 {ECO:0000313|EMBL:EIF00974.1}; OS Saccharomonospora glauca K62. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Pseudonocardineae; Pseudonocardiaceae; Saccharomonospora. OX NCBI_TaxID=928724 {ECO:0000313|EMBL:EIF00974.1, ECO:0000313|Proteomes:UP000005087}; RN [1] {ECO:0000313|EMBL:EIF00974.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=K62 {ECO:0000313|EMBL:EIF00974.1}; 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] {ECO:0000313|EMBL:EIF00974.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=K62 {ECO:0000313|EMBL:EIF00974.1}; 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 ----------------------------------------------------------------------- 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; EIF00974.1; -; Genomic_DNA. DR RefSeq; WP_005466832.1; NZ_CM001484.1. DR EnsemblBacteria; EIF00974; EIF00974; SacglDRAFT_04142. DR Proteomes; UP000005087; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005087}; KW Methyltransferase {ECO:0000313|EMBL:EIF00974.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005087}; KW Transferase {ECO:0000313|EMBL:EIF00974.1}. SQ SEQUENCE 294 AA; 30925 MW; 946239051A2A8A72 CRC64; MELFDGGPVV SDGGLATELE ARGHDLSDAL WSARLLLDAP DEIVAAHRAF YEAGAVVATT ASYQASFPGF AERGLDRAET TRLLHRSVAL ARRAGEEFSG DGRRRFVAAS VGPYGAALAD GSEYRGDYGL TVAQLRDWHL PRLEALAEAE PDLLAVETVP DVVEAEALVG ALAGLGVPAW LTYTVEGDRT RAGQPLAEAL AVAAEAPDVV AVGVNCCAPT DVADAIACAR AVTDKPVVVY PNSGEKWDAR RRAWTGPSRY SSELARQWVA AGARVIGGCC RVSPADIAEV ARVL // ID I1DFG8_9VIBR Unreviewed; 289 AA. AC I1DFG8; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EIF03693.1}; GN ORFNames=VT1337_11982 {ECO:0000313|EMBL:EIF03693.1}; OS Vibrio tubiashii NCIMB 1337 = ATCC 19106. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=866909 {ECO:0000313|EMBL:EIF03693.1, ECO:0000313|Proteomes:UP000004438}; RN [1] {ECO:0000313|EMBL:EIF03693.1, ECO:0000313|Proteomes:UP000004438} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCIMB 1337 {ECO:0000313|EMBL:EIF03693.1}; 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). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIF03693.1}. 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; AHHF01000060; EIF03693.1; -; Genomic_DNA. DR EnsemblBacteria; EIF03693; EIF03693; VT1337_11982. DR Proteomes; UP000004438; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000004438}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EIF03693.1}; KW Transferase {ECO:0000313|EMBL:EIF03693.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 194 194 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 269 269 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 270 270 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 289 AA; 31328 MW; E428827F5C50200B CRC64; MGRELKRMGA PFSQPLWSAQ ALIESPQYVE LAHTSFIDAG AQIITTNSYA CVPFHLGQER FNAEGANLAA KAAKIARLSA DKASHAVQVA GALPPAFGSY RPDLFRPAEA KQIFNLLYQA QDKYVDIWLA ETISSLEELN AIISVLSQTD KASYYAFTLA DTTSEPAQLR SGQSAREATT RVCEAGGDGV FFNCSVPEVM ANAVTEAKQV LDELGCSIEI GVYANNFTPI GNEHEANDTI QAMRDLTPQD YLEYSKAWFE SGATIIGGCC GIGPEHIKTL SEWQSTLKS // ID I1DGU5_9VIBR Unreviewed; 1225 AA. AC I1DGU5; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EIF04170.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EIF04170.1}; GN Name=metH {ECO:0000313|EMBL:EIF04170.1}; GN ORFNames=VT1337_09962 {ECO:0000313|EMBL:EIF04170.1}; OS Vibrio tubiashii NCIMB 1337 = ATCC 19106. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=866909 {ECO:0000313|EMBL:EIF04170.1, ECO:0000313|Proteomes:UP000004438}; RN [1] {ECO:0000313|EMBL:EIF04170.1, ECO:0000313|Proteomes:UP000004438} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCIMB 1337 {ECO:0000313|EMBL:EIF04170.1}; 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). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EIF04170.1}. 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; AHHF01000056; EIF04170.1; -; Genomic_DNA. DR RefSeq; WP_004748610.1; NZ_AHHF01000056.1. DR EnsemblBacteria; EIF04170; EIF04170; VT1337_09962. DR GeneID; 23443393; -. DR Proteomes; UP000004438; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000004438}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EIF04170.1}; KW Transferase {ECO:0000313|EMBL:EIF04170.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1225 AA; 136131 MW; 0172E17D7480B181 CRC64; MGSNVRQQIE AQLKQRILLI DGGMGTMIQD YKLEEQDYRG ERFADWHCDL KGNNDLLVLS QPQLIKDIHS AYLEAGADIL ETNTFNATTI AMADYEMESL SEEINFAAAK LAREAADEWT AKTPEKPRYV AGVLGPTNRT CSISPDVNDP GYRNVSFDEL VEAYSESTRA LIKGGSDLIL IETIFDTLNA KACAFAVDTV FEELGSKLPV MISGTITDAS GRTLSGQTTE AFYNSLRHVN PISFGLNCAL GPDELRPYVE ELSRISETFV STHPNAGLPN AFGEYDLSPE DMAVHVKEWA ESGFLNLIGG CCGTTPEHIR QMAIAVEGVK PRALPELITA CRLSGLEPLT IEKETLFVNV GERTNVTGSA RFKRLIKEEL YDEALEVARQ QVENGAQIID INMDEGMLDA EACMVRFLNL CASEPEISKV PIMVDSSKWE VIEAGLKCIQ GKGIVNSISL KEGKEKFVEQ AKLIRRYGAA VIVMAFDEVG QAETRERKLE ICTNAYNILV DEIGFPPEDI IFDPNIFAVA TGIEEHNNYA VDFIEAVADI KRDLPYAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK NGMDMGIVNA GQLEIYDNVP DKLREAVEDV VLNRRDDGTE RLLDIAAEYA GKGVGKEEDA SALEWRTWSV EKRLEHALVK GITEFIVEDT EEARVNASKP LEVIEGPLMD GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AHLEPYINAS KQAGSSNGKI LLATVKGDVH DIGKNIVGVV LQCNNYEIID LGVMVPCEQI LKVAKEENVD IIGLSGLITP SLDEMVHVAK EMERLDFDLP LLIGGATTSK AHTAVKIEQN YKHPVVYVNN ASRAVGVCTS LLSDELRPAF VEKLDADYVR VRDQHNRKKP RTKPVILEQA RANKVAIDWE CYTPPEPAKP GVHVFDDFDV ATLRNYIDWT PFFMTWSLVG KYPAILDHEE VGEEAKRLFK DANDLLDRVE NEGLLKARGM CALFPAASVG DDIEVYTDES RTEVAKVLYN LRQQTEKPKG FNYCLSDYIA PKESGKKDWI GAFAVTGGIG ERELADQYKA AGDDYNAIMI QAVADRLAEA FAEYLHEQVR KEIWGYSADE NLSNDELIRE KYQGIRPAPG YPACPEHTEK GSLWELLKVE ETIDMSLTTS YAMWPGASVS GWYFSHPDSR YFAIAQIQQD QAQSYADRKG WDMLEAEKWL GPNLN // ID I1DZI8_9GAMM Unreviewed; 354 AA. AC I1DZI8; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:GAB59466.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:GAB59466.1}; GN Name=mmuM {ECO:0000313|EMBL:GAB59466.1}; GN ORFNames=RNAN_2472 {ECO:0000313|EMBL:GAB59466.1}; OS Rheinheimera nanhaiensis E407-8. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Rheinheimera. OX NCBI_TaxID=562729 {ECO:0000313|EMBL:GAB59466.1}; RN [1] {ECO:0000313|EMBL:GAB59466.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=E407-8 {ECO:0000313|EMBL:GAB59466.1}; 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] {ECO:0000313|EMBL:GAB59466.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=E407-8 {ECO:0000313|EMBL:GAB59466.1}; 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. {ECO:0000313|EMBL:GAB59466.1}. 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; BAFK01000013; GAB59466.1; -; Genomic_DNA. DR RefSeq; WP_008222082.1; NZ_BAFK01000013.1. DR EnsemblBacteria; GAB59466; GAB59466; RNAN_2472. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:GAB59466.1}; KW Transferase {ECO:0000313|EMBL:GAB59466.1}. SQ SEQUENCE 354 AA; 38493 MW; 37B30865D1E181F4 CRC64; MTARLTPDHF RKLLSERIFI LDGAMGTMIQ QHRLEEADYR GSEFANWPCD VKGNNDLLVL TQPDLIADIH RQYLLAGADI VETNSFNATT IAMADYQMEG LSARINREAA ALARKVCDEV TKLEPHKPRF VAGVLGPTNR TASISPDVND PGFRNVSFDE LVAAYTESTR ALIDGGADII MLETIFDTLN AKAAAFAVLQ VFDEVGFKLP VMISGTITDA SGRTLSGQTT EAFYHSLAHV EPVCFGLNCA LGPDLLRPYV ETLSGVSEAY VSVHPNAGLP NEFGEYDLGA TEMASEISDW ARQGFLNIVG GCCGTTPEHI KAIFDAVKDA PPRQPKAPSH SFHLAGLEAF SLEW // ID I1E8Q0_AMPQE Unreviewed; 189 AA. AC I1E8Q0; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:PAC:15699891}; GN Name=LOC100638323 {ECO:0000313|EnsemblMetazoa:PAC:15699891}; OS Amphimedon queenslandica (Sponge). OC Eukaryota; Metazoa; Porifera; Demospongiae; Haplosclerida; Niphatidae; OC Amphimedon. OX NCBI_TaxID=400682 {ECO:0000313|EnsemblMetazoa:PAC:15699891, ECO:0000313|Proteomes:UP000007879}; RN [1] {ECO:0000313|EnsemblMetazoa:PAC:15699891} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lucas S., Shapiro H., Lindquist E., Tice H., Dalin E., RA Glavina del Rio T., Bruce D., Barry K., Pitluck S., Srivastava M., RA Simakov O., Chapman J., Mitros T., Hellsten U., Putnam N.H., Fahey B., RA Gauthier M., Larroux C. Richards G.S., Stanke M., Adamska M., RA Darling A., Dacre M., Degnan S.M., Zhai Y., Adamski M., Calcino A., RA Cummins S.F., Goodstein D.M., Harris C., Shu S., Woodcroft B., RA Leys S.P., Manning G., Degnan B.M., Rokhsar D.S.; RT "The genome of the haplosclerid demosponge Amphimedon queenslandica RT and the evolution of animal complexity."; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblMetazoa:PAC:15699891} RP IDENTIFICATION. RG EnsemblMetazoa; 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 EnsemblMetazoa; PAC:15699891; PAC:15699891; Aqu1.201363. DR InParanoid; I1E8Q0; -. DR OMA; VAGEICQ; -. DR Proteomes; UP000007879; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007879}; KW Reference proteome {ECO:0000313|Proteomes:UP000007879}. SQ SEQUENCE 189 AA; 21482 MW; 9DCB52A876C43649 CRC64; MAYTRLFNNS LAGFLKASRS FTKSAGSTSL LTSRSYSLNK SRGLQERLNA GESILCAEGY LLALSRRGYI THGVWVPEFI LEDPAVLKSV HYEMAHAGSD VMEAFQYYTH REKMREIGRE DDLEKINRIA LKIAREVAEE KCLLFAGGIS NTNIYVKGET EERVRAMFEE QVRWSKEEGV DYMIGETFS // ID I1E9E1_AMPQE Unreviewed; 239 AA. AC I1E9E1; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 16. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:PAC:15700148}; DE Flags: Fragment; GN Name=LOC100633661 {ECO:0000313|EnsemblMetazoa:PAC:15700148}; OS Amphimedon queenslandica (Sponge). OC Eukaryota; Metazoa; Porifera; Demospongiae; Haplosclerida; Niphatidae; OC Amphimedon. OX NCBI_TaxID=400682 {ECO:0000313|EnsemblMetazoa:PAC:15700148, ECO:0000313|Proteomes:UP000007879}; RN [1] {ECO:0000313|EnsemblMetazoa:PAC:15700148} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lucas S., Shapiro H., Lindquist E., Tice H., Dalin E., RA Glavina del Rio T., Bruce D., Barry K., Pitluck S., Srivastava M., RA Simakov O., Chapman J., Mitros T., Hellsten U., Putnam N.H., Fahey B., RA Gauthier M., Larroux C. Richards G.S., Stanke M., Adamska M., RA Darling A., Dacre M., Degnan S.M., Zhai Y., Adamski M., Calcino A., RA Cummins S.F., Goodstein D.M., Harris C., Shu S., Woodcroft B., RA Leys S.P., Manning G., Degnan B.M., Rokhsar D.S.; RT "The genome of the haplosclerid demosponge Amphimedon queenslandica RT and the evolution of animal complexity."; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblMetazoa:PAC:15700148} RP IDENTIFICATION. RG EnsemblMetazoa; 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 EnsemblMetazoa; PAC:15700148; PAC:15700148; Aqu1.201620. DR InParanoid; I1E9E1; -. DR OMA; VERPEYP; -. DR Proteomes; UP000007879; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007879}; KW Reference proteome {ECO:0000313|Proteomes:UP000007879}. FT NON_TER 1 1 {ECO:0000313|EnsemblMetazoa:PAC: FT 15700148}. SQ SEQUENCE 239 AA; 26124 MW; E0BC5165FD7B2D8E CRC64; EEFKDHPKPL RGDNDLLCLT QPDIIYNIHK QYFEAGADFS ETNTFNGTSI SQSDYGLEHL VYRINKSAAE IARRAATDVS KATGLPKYVV GALGPTNRTL SVSPSVERPD FRNITFDELV DSYSEQAQGL LDGGVDVLMV ETIFDTANSK AALYAIETLF ESKYKPIPVF VSGTIVDKSG RTLSGQTSEA FLFSVTHSKP LCIGLNCALG ATEMRPFIQT VSRSTEAFVL CYPNAGMLS // ID I1EGB6_AMPQE Unreviewed; 462 AA. AC I1EGB6; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:PAC:15702648}; GN Name=LOC100639967 {ECO:0000313|EnsemblMetazoa:PAC:15702648}; OS Amphimedon queenslandica (Sponge). OC Eukaryota; Metazoa; Porifera; Demospongiae; Haplosclerida; Niphatidae; OC Amphimedon. OX NCBI_TaxID=400682 {ECO:0000313|EnsemblMetazoa:PAC:15702648, ECO:0000313|Proteomes:UP000007879}; RN [1] {ECO:0000313|EnsemblMetazoa:PAC:15702648} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lucas S., Shapiro H., Lindquist E., Tice H., Dalin E., RA Glavina del Rio T., Bruce D., Barry K., Pitluck S., Srivastava M., RA Simakov O., Chapman J., Mitros T., Hellsten U., Putnam N.H., Fahey B., RA Gauthier M., Larroux C. Richards G.S., Stanke M., Adamska M., RA Darling A., Dacre M., Degnan S.M., Zhai Y., Adamski M., Calcino A., RA Cummins S.F., Goodstein D.M., Harris C., Shu S., Woodcroft B., RA Leys S.P., Manning G., Degnan B.M., Rokhsar D.S.; RT "The genome of the haplosclerid demosponge Amphimedon queenslandica RT and the evolution of animal complexity."; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblMetazoa:PAC:15702648} RP IDENTIFICATION. RG EnsemblMetazoa; 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 EnsemblMetazoa; PAC:15702648; PAC:15702648; Aqu1.204120. DR InParanoid; I1EGB6; -. DR OMA; TVICADG; -. DR Proteomes; UP000007879; Unassembled WGS sequence. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007879}; KW Reference proteome {ECO:0000313|Proteomes:UP000007879}. SQ SEQUENCE 462 AA; 51237 MW; 82346F129E31B979 CRC64; MTLELVNDIV QVCPPEKIGA LPIAYRTTPK EPGFMDLTDS ICPANNPVYP RGMEPFCVSP AEIESFTKSC TSLGMKYLGI CCGNSGELTR TMAETMGRRP PASRSTRKDL NINWSMASRR LLKSRGLQER LNAGESILCA EGYLLALSRR GYITHGVWVP EFILEDPAIL KSVHYEMAHA GSDVIEAFQY NTHREKMKQI GREDDIEKIN RTALKIAREV AEEKNLLFAG GISNTNQYVK GETEEKVRAM FEEQVRWSKE EGVDYMIGET FSFLGEAQIA LEVIQSFDLP AVVTLTVYTA RGEDGVVRTR DGVPIGEACK DLIDRGVTIT GVNCTRGPEM TLELVNDIVQ VCPPEKIGAL PIAYRTTPKE PSFMDLTDSI CPANNPVYPR GMEPFCISPV EIESFTKSCT SLGMKYLGIC CGNSGELTRT MAETMGRKPP ASRYLDHTQF GFLMKLKMSG EL // ID I1EIY2_AMPQE Unreviewed; 128 AA. AC I1EIY2; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 12. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:PAC:15703582}; OS Amphimedon queenslandica (Sponge). OC Eukaryota; Metazoa; Porifera; Demospongiae; Haplosclerida; Niphatidae; OC Amphimedon. OX NCBI_TaxID=400682 {ECO:0000313|EnsemblMetazoa:PAC:15703582, ECO:0000313|Proteomes:UP000007879}; RN [1] {ECO:0000313|EnsemblMetazoa:PAC:15703582} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lucas S., Shapiro H., Lindquist E., Tice H., Dalin E., RA Glavina del Rio T., Bruce D., Barry K., Pitluck S., Srivastava M., RA Simakov O., Chapman J., Mitros T., Hellsten U., Putnam N.H., Fahey B., RA Gauthier M., Larroux C. Richards G.S., Stanke M., Adamska M., RA Darling A., Dacre M., Degnan S.M., Zhai Y., Adamski M., Calcino A., RA Cummins S.F., Goodstein D.M., Harris C., Shu S., Woodcroft B., RA Leys S.P., Manning G., Degnan B.M., Rokhsar D.S.; RT "The genome of the haplosclerid demosponge Amphimedon queenslandica RT and the evolution of animal complexity."; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblMetazoa:PAC:15703582} RP IDENTIFICATION. RG EnsemblMetazoa; 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 EnsemblMetazoa; PAC:15703582; PAC:15703582; Aqu1.205054. DR Proteomes; UP000007879; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007879}; KW Reference proteome {ECO:0000313|Proteomes:UP000007879}. SQ SEQUENCE 128 AA; 13934 MW; 646445AB161C3E58 CRC64; MHDKVWCATA TETSPEILAD VHEDYIRAGA QVIITNTFST NRNMLDPAGL GDRFESLNRS AVEIARLARK RAGAEEEVVV AGSMSHQVPM QKGTAQRDAE QVPDPKIAAG RFREMAETLA EAGVDLLL // ID I1F6L6_AMPQE Unreviewed; 355 AA. AC I1F6L6; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 18. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:PAC:15711711}; DE Flags: Fragment; GN Name=LOC100640174 {ECO:0000313|EnsemblMetazoa:PAC:15711711}; OS Amphimedon queenslandica (Sponge). OC Eukaryota; Metazoa; Porifera; Demospongiae; Haplosclerida; Niphatidae; OC Amphimedon. OX NCBI_TaxID=400682 {ECO:0000313|EnsemblMetazoa:PAC:15711711, ECO:0000313|Proteomes:UP000007879}; RN [1] {ECO:0000313|EnsemblMetazoa:PAC:15711711} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lucas S., Shapiro H., Lindquist E., Tice H., Dalin E., RA Glavina del Rio T., Bruce D., Barry K., Pitluck S., Srivastava M., RA Simakov O., Chapman J., Mitros T., Hellsten U., Putnam N.H., Fahey B., RA Gauthier M., Larroux C. Richards G.S., Stanke M., Adamska M., RA Darling A., Dacre M., Degnan S.M., Zhai Y., Adamski M., Calcino A., RA Cummins S.F., Goodstein D.M., Harris C., Shu S., Woodcroft B., RA Leys S.P., Manning G., Degnan B.M., Rokhsar D.S.; RT "The genome of the haplosclerid demosponge Amphimedon queenslandica RT and the evolution of animal complexity."; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblMetazoa:PAC:15711711} RP IDENTIFICATION. RG EnsemblMetazoa; RL Submitted (APR-2012) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EnsemblMetazoa; PAC:15711711; PAC:15711711; Aqu1.213183. DR InParanoid; I1F6L6; -. DR OMA; REECITI; -. DR Proteomes; UP000007879; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007879}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000007879}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT NON_TER 1 1 {ECO:0000313|EnsemblMetazoa:PAC: FT 15711711}. SQ SEQUENCE 355 AA; 39330 MW; 64BC7A94D0A17C02 CRC64; AGSTSLLTSR SYSLNKSRGL QERLNAGESI LCAEGYLLAL SRRGYITHGV WVPEFILDDP AVLKSVHYEM AHAGSDVMEA FQYYTHREKM REIGREDDLE KINRIALKIA REVAEEKSLL FAGGISNTNI YVKGETEERV RAMFEEQVRW SKEEGVDYMI GETFSFLGEA QIALEVIQSF DLPAVITLTV YTTRGEDGVV RTRDGVPIGE ACKDLIDRGV TITGVNCTRG PEMTLELVND IVQVCPPEKI GALPIAYRTT SKEPGFMDLT DSICPANNPV YPRGMEPFCV SPAEIESFTK SCTSLGMKYL GICCGNSGEL TRTMAETMGR RPPASRYLDD TQFGLLNKLK MSGQL // ID I1F6L7_AMPQE Unreviewed; 347 AA. AC I1F6L7; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:PAC:15711712}; GN Name=LOC100640299 {ECO:0000313|EnsemblMetazoa:PAC:15711712}; OS Amphimedon queenslandica (Sponge). OC Eukaryota; Metazoa; Porifera; Demospongiae; Haplosclerida; Niphatidae; OC Amphimedon. OX NCBI_TaxID=400682 {ECO:0000313|EnsemblMetazoa:PAC:15711712, ECO:0000313|Proteomes:UP000007879}; RN [1] {ECO:0000313|EnsemblMetazoa:PAC:15711712} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lucas S., Shapiro H., Lindquist E., Tice H., Dalin E., RA Glavina del Rio T., Bruce D., Barry K., Pitluck S., Srivastava M., RA Simakov O., Chapman J., Mitros T., Hellsten U., Putnam N.H., Fahey B., RA Gauthier M., Larroux C. Richards G.S., Stanke M., Adamska M., RA Darling A., Dacre M., Degnan S.M., Zhai Y., Adamski M., Calcino A., RA Cummins S.F., Goodstein D.M., Harris C., Shu S., Woodcroft B., RA Leys S.P., Manning G., Degnan B.M., Rokhsar D.S.; RT "The genome of the haplosclerid demosponge Amphimedon queenslandica RT and the evolution of animal complexity."; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblMetazoa:PAC:15711712} RP IDENTIFICATION. RG EnsemblMetazoa; RL Submitted (APR-2012) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; 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_003389502.1; XM_003389454.1. DR EnsemblMetazoa; PAC:15711712; PAC:15711712; Aqu1.213184. DR GeneID; 100640299; -. DR KEGG; aqu:100640299; -. DR InParanoid; I1F6L7; -. DR KO; K00544; -. DR OMA; NICNTNC; -. DR Proteomes; UP000007879; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007879}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000007879}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 219 219 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 347 AA; 38491 MW; 23540D37FA8A3881 CRC64; MASRRLLKSR GLQERLNAGE SILCAEGYLL ALSRRGYITH GVWVPEFILE DPAVLKSVHY EMAHAGSDVI EAFQYNTHRE KMKQIGREDD IEKINRTALK IAHEVAEEKN LLFAGGISNT NQYVKGETEE KVRAMFEEQV RWSKEEGVDY MIGETFSFLG EAQIALEVIQ SFDLPAVVTL TVHGAKGEDG VVRTRDGVPI GEACKDLIDR GVTITGVNCT RGPEMTLELV NNIVQVCPPE KIGALPIAYR TTPKEPSFMD LTDSICPANN PVYPRGMEPF CVSPVEIESF TKSCTSLGMK YLGICCGNSG ELTRTMAETM GRKPPASRYL DHTQFGFLMK LKMSGEL // ID I1FAB7_AMPQE Unreviewed; 1208 AA. AC I1FAB7; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 22. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:PAC:15713023}; GN Name=LOC100642068 {ECO:0000313|EnsemblMetazoa:PAC:15713023}; OS Amphimedon queenslandica (Sponge). OC Eukaryota; Metazoa; Porifera; Demospongiae; Haplosclerida; Niphatidae; OC Amphimedon. OX NCBI_TaxID=400682 {ECO:0000313|EnsemblMetazoa:PAC:15713023, ECO:0000313|Proteomes:UP000007879}; RN [1] {ECO:0000313|EnsemblMetazoa:PAC:15713023} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lucas S., Shapiro H., Lindquist E., Tice H., Dalin E., RA Glavina del Rio T., Bruce D., Barry K., Pitluck S., Srivastava M., RA Simakov O., Chapman J., Mitros T., Hellsten U., Putnam N.H., Fahey B., RA Gauthier M., Larroux C. Richards G.S., Stanke M., Adamska M., RA Darling A., Dacre M., Degnan S.M., Zhai Y., Adamski M., Calcino A., RA Cummins S.F., Goodstein D.M., Harris C., Shu S., Woodcroft B., RA Leys S.P., Manning G., Degnan B.M., Rokhsar D.S.; RT "The genome of the haplosclerid demosponge Amphimedon queenslandica RT and the evolution of animal complexity."; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblMetazoa:PAC:15713023} RP IDENTIFICATION. RG EnsemblMetazoa; RL Submitted (APR-2012) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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 EnsemblMetazoa; PAC:15713023; PAC:15713023; Aqu1.214495. DR InParanoid; I1FAB7; -. DR OMA; MEENADI; -. DR Proteomes; UP000007879; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 2. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007879}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007879}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 262 262 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 325 325 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 326 326 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 803 803 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1208 AA; 133368 MW; E05DE75760740C22 CRC64; MPTEVPLHFR PTYPKITPGL GETLANEMRK RIMVLDGAMG TMIQGHNLTE EQFRGEEFKD HPKPLRGDND LLCLTQPDII YNIHKQYFEA GADFSETNTF NGTSISQSDY GLEHLVYRIN KSAAEIARRA AADVSKATGL PKYVVGALGP TNRTLSVSPS VERPDFRNIT FDELVDSYSE QAQGLLDGGV DVLMVETIFD TANSKAALYA IETLFESKYK PIPVFVSGTI VDKSGRTLSG QTSEAFLFSV THSKPLCIGL NCALGATEMR PFIQTVSRST EAFVLCYPNA GLPNALGGYD ETPEVMASHL KSFAVDGLVN IVGGCCGTTP LFIKAIAEAV KGLKPREPPT NLYHDALILS GLEGVKINST TNFVNIGERC NVAGSRRFAR LIIAGKFEEA LAVAKQQVEM GAQVLDLNMD EGMLDGVKAM ARFCNYISTE PDIAKLPLCI DSSNFSVVLA GLKCSQGKCI VNSISLKEGE EDFIEKAKII KKFGGAAVVM AFDEVGQATT TENKVSICTR SYNILVDVVG FNPNDIIFDP NILTIATGME EHNNYGISFI EATRLIKVRG GARRLMTIII QTLPGARISG GLSNLSFSFR GKEVIREAMH SVFLYHAIQA GMDMGIVNAG NLPLYDDIKK DLLNLCEDLL WNRDPNTTEK LLEYAQSLGE GAKKQVATDE WRNTTVEERL EYSLVKGIDK FVVSDTEEAR SNFDKYPRPL HIIEGPLMSG MSIVGDLFGS GKMFLPQVIK SARVMKKAVG YLIPFMEEEK EKAAKEEGTV ISEDENDRFS GTVVIATVKG DVHDIGKNIV GVVLGCNNFR VIDLGVMTPC EKIIETARKN KADIIGLSGL ITPSLDEMIY VAKEMEREGL KIPLLIGGAT TTKTHTAVKI APCYSQPTIH VVDASKSVVV VSTLLDATAK DDFTDDISEE YTDIREDHYD SIKDKQYVSI AKARSEALAL NVNSYKPVKP RQLGITVFQD YDLNRLVSYI DWKPFFDVWQ LKGKYPNRGY PKIFNDKDVG AEAKRTFDDA QVLLNRIIKE KLLIARGVVG IFKAVRDGDD IKILSEENTT IATLYGLRQQ VEKASMSTTG PYMCLSDFIY DSSGPTDYIG MFAVSTGFGC KELCDKYKEQ FDDYNVIMLE AVADRLAEAF AEELHERVRR EVWGYADTED LDASDLHKIR YQVEDYAKRK GMTLSEAEKW LGSSLGYV // ID I1FAC0_AMPQE Unreviewed; 992 AA. AC I1FAC0; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:PAC:15713026}; OS Amphimedon queenslandica (Sponge). OC Eukaryota; Metazoa; Porifera; Demospongiae; Haplosclerida; Niphatidae; OC Amphimedon. OX NCBI_TaxID=400682 {ECO:0000313|EnsemblMetazoa:PAC:15713026, ECO:0000313|Proteomes:UP000007879}; RN [1] {ECO:0000313|EnsemblMetazoa:PAC:15713026} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lucas S., Shapiro H., Lindquist E., Tice H., Dalin E., RA Glavina del Rio T., Bruce D., Barry K., Pitluck S., Srivastava M., RA Simakov O., Chapman J., Mitros T., Hellsten U., Putnam N.H., Fahey B., RA Gauthier M., Larroux C. Richards G.S., Stanke M., Adamska M., RA Darling A., Dacre M., Degnan S.M., Zhai Y., Adamski M., Calcino A., RA Cummins S.F., Goodstein D.M., Harris C., Shu S., Woodcroft B., RA Leys S.P., Manning G., Degnan B.M., Rokhsar D.S.; RT "The genome of the haplosclerid demosponge Amphimedon queenslandica RT and the evolution of animal complexity."; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblMetazoa:PAC:15713026} RP IDENTIFICATION. RG EnsemblMetazoa; RL Submitted (APR-2012) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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 EnsemblMetazoa; PAC:15713026; PAC:15713026; Aqu1.214498. DR InParanoid; I1FAC0; -. DR OMA; QPFFNAW; -. DR Proteomes; UP000007879; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007879}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007879}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 254 254 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 318 318 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 782 782 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 992 AA; 108738 MW; 94BCBFB00452E582 CRC64; MPTEVPLHFR PTYPKITPGL GETLANEMCK RIMVLDGAMG TMIQGHNLTE EQFRGEEFKD HPKPLRGDND LLCLTQPDII YNIHKQYFEA GADFSETNTF NGTSISQSDY GLEHLVYCIN KSAAEIARQA AADVSKATGL PKYVVGALGP TNRTLSVSPS VERPDFRNIT FDELVDSYSE QAQGLLDGGV DVLMVETIFD TANSKAALYA VETLFESKYK PIPVFVSSSV AVVSGTIVDK SGRTLSGQTI GLNCALGATE MRPFIQTVSR STEAFVLCYP NAGLPNALGG YDETPEVMAS HLKSFAVDGL VNIVGGCCGT TPLFIKAIAE AVKGLKPREP PTNLYHDALI LSGLEGVKIN STTNFVNIGE RCNVAGSRRF ARLIIAGKFE EALAVAKQQV EMGAQVLDLN MDEGMLDGVK AMARFCNYIS TEPDIAKLPL CIDSSNFSVV LAGLKCSQGK CIVNSISLKE GEEDFIEKAK IIKKFGGAAV VMAFDEVGQA TTTENKVSIC TRSYNILVDV VGFNPNDIIF DPNILTIATG MEEHNNYGIS FIEATRLIKQ TLPGARISGG LSNLSFSFRG KEVIREAMHS VFLYHAIQAG MDMGIVNAGN LPLYDDIKKD LLNLCEDLLW NRDPNTTEKL LEYAQSLGEG AKKQVATDEW RNATVEERLE YSLVKGIDKF VVSDTEEARS NFDKYPRPLH IIEGPLMSGM SIVGDLFGSG KMFLPQVIKS ARVMKKAVGY LIPFMEEEKE KAAKEEGTVI SEDENDRFSG TVVIATVKGD VHDIGKNIVG VVLGCNNFRV IDLGVMTPCE KIIETARKNK ADIIGLSGLI TPSLDEMIYV AKEMEREGLK IPLLIGGATT TKTHTAVKIA PCYSQPTIHV VALNVNCYKP VKPRQLGITV FQDYDLNRLV SYIDWKPFFD VWQLKGKYPN RGYPKIFNDK DVLKLSVYTF DDAQVLLNCI IKEKLLIARG VVGIFKAVRD GDDIKILSEE NT // ID I1GI92_AMPQE Unreviewed; 240 AA. AC I1GI92; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:PAC:15728137}; GN Name=LOC100638667 {ECO:0000313|EnsemblMetazoa:PAC:15728137}; OS Amphimedon queenslandica (Sponge). OC Eukaryota; Metazoa; Porifera; Demospongiae; Haplosclerida; Niphatidae; OC Amphimedon. OX NCBI_TaxID=400682 {ECO:0000313|EnsemblMetazoa:PAC:15728137, ECO:0000313|Proteomes:UP000007879}; RN [1] {ECO:0000313|EnsemblMetazoa:PAC:15728137} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lucas S., Shapiro H., Lindquist E., Tice H., Dalin E., RA Glavina del Rio T., Bruce D., Barry K., Pitluck S., Srivastava M., RA Simakov O., Chapman J., Mitros T., Hellsten U., Putnam N.H., Fahey B., RA Gauthier M., Larroux C. Richards G.S., Stanke M., Adamska M., RA Darling A., Dacre M., Degnan S.M., Zhai Y., Adamski M., Calcino A., RA Cummins S.F., Goodstein D.M., Harris C., Shu S., Woodcroft B., RA Leys S.P., Manning G., Degnan B.M., Rokhsar D.S.; RT "The genome of the haplosclerid demosponge Amphimedon queenslandica RT and the evolution of animal complexity."; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblMetazoa:PAC:15728137} RP IDENTIFICATION. RG EnsemblMetazoa; 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 EnsemblMetazoa; PAC:15728137; PAC:15728137; Aqu1.229609. DR InParanoid; I1GI92; -. DR OMA; QCKDENT; -. DR Proteomes; UP000007879; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007879}; KW Reference proteome {ECO:0000313|Proteomes:UP000007879}. SQ SEQUENCE 240 AA; 26705 MW; FC592268F1411DA8 CRC64; MEDRLYILDG GLATEIERRG VSLLNDPLWS ARILHTQPEL ILNVHKSFLQ NGADIITTAS YQASIDGYYQ HLGLSSENAL KLIANSVYLA QEARDWFSQQ PEHKDRAQPL IAGSVGPYGA CLCDGSEYTG AYLNHTSLEV IKDWHKPRIR QLLESGVDLL ALETIPSIIE AKILLEILAD YPQAKAWISF TCKDEGHTCY GEVFSDVVKA MCSYKQLVAV GINCSPPQYI GVDYLFCCSM // ID I1H7Z4_BRADI Unreviewed; 334 AA. AC I1H7Z4; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:BRADI1G69627.1}; GN Name=BRADI1G69627 {ECO:0000313|EnsemblPlants:BRADI1G69627.1}; 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 {ECO:0000313|EnsemblPlants:BRADI1G69627.1, ECO:0000313|Proteomes:UP000008810}; RN [1] {ECO:0000313|EnsemblPlants:BRADI1G69627.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:BRADI1G69627.1}; 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] {ECO:0000313|EnsemblPlants:BRADI1G69627.1} RP IDENTIFICATION. RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:BRADI1G69627.1}; 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_010228957.1; XM_010230655.1. DR EnsemblPlants; BRADI1G69627.1; BRADI1G69627.1; BRADI1G69627. DR GeneID; 100841399; -. DR KEGG; bdi:100841399; -. DR InParanoid; I1H7Z4; -. DR KO; K00547; -. DR OMA; AINDPLW; -. DR Proteomes; UP000008810; Chromosome 1. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008810}; KW Reference proteome {ECO:0000313|Proteomes:UP000008810}. SQ SEQUENCE 334 AA; 36216 MW; 6F536C50C6574179 CRC64; MAGVVEELVK KAGGCAVIDG GFATQLEALG ADINDSLWSA ACLITKPHLI KEVHMQYLEA GADVIISSSY QATIPGFLAR GLRQEEAEGL LRTSVHLALE ARDEFWKSTL TKPKPIYNRA LVAASIGSYG AFLADGSEYS GSYGDNIMAE KLKDFHRRRL QVLASAGPDL IAFEAIPNKM EAQALVELLE EEDIQVPSWI CFSSVDGKHL CSGESFGDCL QILNASEKVA IVGVNCTPPQ FIEGIIREFK KQTGKAIAVY PNSGEVWDGR AKRWLPAECF GRKSFDVMAR RWQEAGASLI GGCCRTTPST IRAVSKALKG RDRALISLES SESV // ID I1HS50_BRADI Unreviewed; 359 AA. AC I1HS50; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 04-FEB-2015, entry version 15. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:BRADI2G51410.1}; GN Name=BRADI2G51410 {ECO:0000313|EnsemblPlants:BRADI2G51410.1}; 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 {ECO:0000313|EnsemblPlants:BRADI2G51410.1, ECO:0000313|Proteomes:UP000008810}; RN [1] {ECO:0000313|EnsemblPlants:BRADI2G51410.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:BRADI2G51410.1}; 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] {ECO:0000313|EnsemblPlants:BRADI2G51410.1} RP IDENTIFICATION. RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:BRADI2G51410.1}; 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_003567164.1; XM_003567116.2. DR EnsemblPlants; BRADI2G51410.1; BRADI2G51410.1; BRADI2G51410. DR GeneID; 100838685; -. DR KEGG; bdi:100838685; -. DR InParanoid; I1HS50; -. DR KO; K00547; -. DR OMA; YGRSVTK; -. DR Proteomes; UP000008810; Chromosome 2. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008810}; KW Reference proteome {ECO:0000313|Proteomes:UP000008810}. SQ SEQUENCE 359 AA; 38121 MW; D7CEF4EB44902463 CRC64; MGRGDGYDDA AGALRGLVRE AGECLVLDGA LGTELEAHGA DLQDELWSAS CLVSAPHIIR KVHLDYLEAG ANIITTASYQ ATLQGFQSRG LSSEQSETLL RRSVEIAQEA RAIFVEGRSK GPYAGRENDG SRERRPVLVA ASVGSYGAYL ADGSEYTGDY GRSVTKEALK NFHRRRLQVL ADAGPDLIAF ETIPNKLEAQ AYSELLEEND IRIPAWFSFT SKDGANAASG DPITECAAVA DSCRRVASVG INCTAPGLIH GLILSIRKVT SKAIVVYPNS GETYVAETKE WVDSAGASGT TDFASCVGKW REAGASVVGG CCRTSPATVG AIARALREAD AADVFYRPKP CSLVFSQKS // ID I1IGN2_BRADI Unreviewed; 340 AA. AC I1IGN2; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 04-FEB-2015, entry version 15. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:BRADI4G02350.1}; GN Name=BRADI4G02350 {ECO:0000313|EnsemblPlants:BRADI4G02350.1}; 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 {ECO:0000313|EnsemblPlants:BRADI4G02350.1, ECO:0000313|Proteomes:UP000008810}; RN [1] {ECO:0000313|EnsemblPlants:BRADI4G02350.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:BRADI4G02350.1}; 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] {ECO:0000313|EnsemblPlants:BRADI4G02350.1} RP IDENTIFICATION. RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:BRADI4G02350.1}; 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_003577787.1; XM_003577739.2. DR EnsemblPlants; BRADI4G02350.1; BRADI4G02350.1; BRADI4G02350. DR GeneID; 100836808; -. DR KEGG; bdi:100836808; -. DR InParanoid; I1IGN2; -. DR KO; K00547; -. DR OMA; SEWCKDG; -. DR Proteomes; UP000008810; Chromosome 4. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008810}; KW Reference proteome {ECO:0000313|Proteomes:UP000008810}. SQ SEQUENCE 340 AA; 36509 MW; 6CB0A19CE777FEA0 CRC64; MVVKSGGGGV GEEGAACAAV RRWLEAGGGR LVLDGGLATE LEAHGADLND PLWSAKCILA SPHLIRKVHL DYIEAGANII ITASYQATIQ GFESKGFSKQ QGEDLLTKSV KVAQEAREMF LKEHPDQSTP MQHPILVAAS IGSYGAYLAD GSEYSGDYGE AGTLEFLKDF HRRRLQVLAE AGPDLIAFET IPNKLEAQAY VELLDECNIS IPSWFSFNSK DGVNVVSGDS LIECATIANA CAKVGAVGIN CTPPRFIHGL ILSIRKVTDK PILIYPNSGE RYDAEKKEWV ESTGVCDGDF VSYVSEWCKD GAALIGGCCR TTPNTIRAIN RSLNQCLPAP // ID I1IGN3_BRADI Unreviewed; 339 AA. AC I1IGN3; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 07-JAN-2015, entry version 11. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:BRADI4G02350.2}; GN Name=BRADI4G02350 {ECO:0000313|EnsemblPlants:BRADI4G02350.2}; 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 {ECO:0000313|EnsemblPlants:BRADI4G02350.2, ECO:0000313|Proteomes:UP000008810}; RN [1] {ECO:0000313|EnsemblPlants:BRADI4G02350.2} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:BRADI4G02350.2}; 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] {ECO:0000313|EnsemblPlants:BRADI4G02350.2} RP IDENTIFICATION. RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:BRADI4G02350.2}; 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 EnsemblPlants; BRADI4G02350.2; BRADI4G02350.2; BRADI4G02350. DR Proteomes; UP000008810; Chromosome 4. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008810}; KW Reference proteome {ECO:0000313|Proteomes:UP000008810}. SQ SEQUENCE 339 AA; 36410 MW; 7676651942966178 CRC64; MVVKSGGGGV GEEGAACAAV RRWLEAGGGR LVLDGGLATE LEAHGADLND PLWSAKCILA SPHLIRKVHL DYIEAGANII ITASYQATIQ GFESKGFSKQ QGEDLLTKSV KVAQEAREMF LKEHPDQSTP MQHPILVAAS IGSYGAYLAD GSEYSGDYGE AGTLEFLKDF HRRRLQVLAE AGPDLIAFET IPNKLEAQAY VELLDECNIS IPSWFSFNSK DGVNVVSGDS LIECATIANA CAKVGAVGIN CTPPRFIHGL ILSIRKVTDK PILIYPNSGE RYDAEKKEWE STGVCDGDFV SYVSEWCKDG AALIGGCCRT TPNTIRAINR SLNQCLPAP // ID I1KWU9_SOYBN Unreviewed; 323 AA. AC I1KWU9; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:GLYMA08G30150.1}; 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 {ECO:0000313|EnsemblPlants:GLYMA08G30150.1, ECO:0000313|Proteomes:UP000008827}; RN [1] {ECO:0000313|EnsemblPlants:GLYMA08G30150.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:GLYMA08G30150.1}; 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] {ECO:0000313|EnsemblPlants:GLYMA08G30150.1} RP IDENTIFICATION. RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:GLYMA08G30150.1}; RG EnsemblPlants; RL Submitted (MAY-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 RefSeq; XP_003531927.1; XM_003531879.2. DR EnsemblPlants; GLYMA08G30150.1; GLYMA08G30150.1; GLYMA08G30150. DR GeneID; 100812265; -. DR KEGG; gmx:100812265; -. DR InParanoid; I1KWU9; -. DR KO; K00547; -. DR OMA; AINDPLW; -. DR Proteomes; UP000008827; Chromosome 8. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008827}; KW Reference proteome {ECO:0000313|Proteomes:UP000008827}. SQ SEQUENCE 323 AA; 35484 MW; 140633EE71C0D461 CRC64; MKRQMLHDLI ENAGGCAVTD GGFATQLEKH GASINDPLWS AIYLIKDPHL IKQVHLEYLE AGADILVTSS YQATLPGFSS KGLSIEEGES LLEKSVKLAV EARDGFWNSA IINPGNKYRR ALVAASIGSY GSYLADGSEY SGCYGPDVNL KKLKDFHRRR LQVLVEAGPD LLAFETIPNK LEAQACVELL EEESVKIPSW ICFTTVDGEN APSGESFKDC LEALNKSNKV DAVGINCAPP HLMENLICKF KQLTKKAIIV YPNSGEVWDG KAKKWLPSKC FHDDEFGFNA TRWRDLGAKI IGGCCRTTPS TIQIISNALR EKS // ID I1KWV0_SOYBN Unreviewed; 278 AA. AC I1KWV0; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 01-APR-2015, entry version 13. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:GLYMA08G30150.2}; 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 {ECO:0000313|EnsemblPlants:GLYMA08G30150.2, ECO:0000313|Proteomes:UP000008827}; RN [1] {ECO:0000313|EnsemblPlants:GLYMA08G30150.2} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:GLYMA08G30150.2}; 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] {ECO:0000313|EnsemblPlants:GLYMA08G30150.2} RP IDENTIFICATION. RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:GLYMA08G30150.2}; RG EnsemblPlants; RL Submitted (MAY-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 EnsemblPlants; GLYMA08G30150.2; GLYMA08G30150.2; GLYMA08G30150. DR Proteomes; UP000008827; Chromosome 8. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008827}; KW Reference proteome {ECO:0000313|Proteomes:UP000008827}. SQ SEQUENCE 278 AA; 30663 MW; 3909E10DA45876F5 CRC64; MRFFPSNQVH LEYLEAGADI LVTSSYQATL PGFSSKGLSI EEGESLLEKS VKLAVEARDG FWNSAIINPG NKYRRALVAA SIGSYGSYLA DGSEYSGCYG PDVNLKKLKD FHRRRLQVLV EAGPDLLAFE TIPNKLEAQA CVELLEEESV KIPSWICFTT VDGENAPSGE SFKDCLEALN KSNKVDAVGI NCAPPHLMEN LICKFKQLTK KAIIVYPNSG EVWDGKAKKW LPSKCFHDDE FGFNATRWRD LGAKIIGGCC RTTPSTIQII SNALREKS // ID I1N9J8_SOYBN Unreviewed; 333 AA. AC I1N9J8; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 01-APR-2015, entry version 17. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:GLYMA19G34120.1}; 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 {ECO:0000313|EnsemblPlants:GLYMA19G34120.1, ECO:0000313|Proteomes:UP000008827}; RN [1] {ECO:0000313|EnsemblPlants:GLYMA19G34120.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:GLYMA19G34120.1}; 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] {ECO:0000313|EnsemblPlants:GLYMA19G34120.1} RP IDENTIFICATION. RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:GLYMA19G34120.1}; RG EnsemblPlants; RL Submitted (MAY-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 RefSeq; XP_003554264.1; XM_003554216.2. DR EnsemblPlants; GLYMA19G34120.1; GLYMA19G34120.1; GLYMA19G34120. DR GeneID; 100790567; -. DR KEGG; gmx:100790567; -. DR InParanoid; I1N9J8; -. DR KO; K00547; -. DR OMA; SSVEGFM; -. DR Proteomes; UP000008827; Chromosome 19. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008827}; KW Reference proteome {ECO:0000313|Proteomes:UP000008827}. SQ SEQUENCE 333 AA; 36376 MW; F862AF058A935C27 CRC64; MSSLITDLLR QTGGTAVIDG GLATELERHG ADLNDPLWSA KCLFSFPHLI RQVHLDYLEN GADIIITASY QATIQGFKAK GYSDEESEAL LRSSVEIARE AREVYYKNCA GCRSGDGDDD GRILKQRPIL VAASVGSYGA YLADGSEYSG DYGDAITVET LKDFHRRRVQ ILADSGADLL AFETVPNKLE AEAYAQLLEE EDIKIPAWFS FNSKDGVNVV SGDSLMECGS IAESCNKVVA VGINCTPPRF IHGLIVLLKK VTTKPIVIYP NSGETYDADL KEWVQNTGVT DEDFISYVNK WCELGASLVG GCCRTTPDTI RKIYRTLSSS QSI // ID I1NGH7_SOYBN Unreviewed; 342 AA. AC I1NGH7; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 01-APR-2015, entry version 16. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:GLYMA20G28720.1}; 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 {ECO:0000313|EnsemblPlants:GLYMA20G28720.1, ECO:0000313|Proteomes:UP000008827}; RN [1] {ECO:0000313|EnsemblPlants:GLYMA20G28720.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:GLYMA20G28720.1}; 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] {ECO:0000313|EnsemblPlants:GLYMA20G28720.1} RP IDENTIFICATION. RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:GLYMA20G28720.1}; RG EnsemblPlants; RL Submitted (MAY-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 EnsemblPlants; GLYMA20G28720.1; GLYMA20G28720.1; GLYMA20G28720. DR InParanoid; I1NGH7; -. DR OMA; SYIGKWR; -. DR Proteomes; UP000008827; Chromosome 20. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008827}; KW Reference proteome {ECO:0000313|Proteomes:UP000008827}. SQ SEQUENCE 342 AA; 37684 MW; 7C7A784243C3EFF2 CRC64; MGLEGKETPS FMRDFLDKCG GCAVIDGGFA TELERHGADL NDELWSAKCL ISSPHLVRRV HLDYLDAGAN IILTASYQAT IQGFEAKGFS REEGETMLRR SVEIAREARE IYYDRCTKDS SDFMRDERYR KRPILIAASV GSYGAYLADG SEYVGDYGDA VTVQTLKDFH RERVKILVEA GADLIAFETI PNKLEAQAYA ELLEEEGIET PAWFSFSCKD ESNVVSGDSI FECASIADSC RQVVAVGVNC TAPRFIHGLI SFIKKQATSK PVLVYPNSGE TYIAESNQWV KSSGAAEHDF VSYIGKWRDA GASLFGGCCR TTPNTIRGIA EATYGKLKDK CI // ID I1NGH8_SOYBN Unreviewed; 245 AA. AC I1NGH8; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 01-APR-2015, entry version 13. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:GLYMA20G28720.2}; 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 {ECO:0000313|EnsemblPlants:GLYMA20G28720.2, ECO:0000313|Proteomes:UP000008827}; RN [1] {ECO:0000313|EnsemblPlants:GLYMA20G28720.2} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:GLYMA20G28720.2}; 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] {ECO:0000313|EnsemblPlants:GLYMA20G28720.2} RP IDENTIFICATION. RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:GLYMA20G28720.2}; RG EnsemblPlants; RL Submitted (MAY-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 EnsemblPlants; GLYMA20G28720.2; GLYMA20G28720.2; GLYMA20G28720. DR Proteomes; UP000008827; Chromosome 20. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008827}; KW Reference proteome {ECO:0000313|Proteomes:UP000008827}. SQ SEQUENCE 245 AA; 27095 MW; 127EE08EB8FA9B21 CRC64; MLRRSVEIAR EAREIYYDRC TKDSSDFMRD ERYRKRPILI AASVGSYGAY LADGSEYVGD YGDAVTVQTL KDFHRERVKI LVEAGADLIA FETIPNKLEA QAYAELLEEE GIETPAWFSF SCKDESNVVS GDSIFECASI ADSCRQVVAV GVNCTAPRFI HGLISFIKKA TSKPVLVYPN SGETYIAESN QWVKSSGAAE HDFVSYIGKW RDAGASLFGG CCRTTPNTIR GIAEATYGKL KDKCI // ID I1NGH9_SOYBN Unreviewed; 341 AA. AC I1NGH9; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 01-APR-2015, entry version 14. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:GLYMA20G28720.3}; 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 {ECO:0000313|EnsemblPlants:GLYMA20G28720.3, ECO:0000313|Proteomes:UP000008827}; RN [1] {ECO:0000313|EnsemblPlants:GLYMA20G28720.3} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:GLYMA20G28720.3}; 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] {ECO:0000313|EnsemblPlants:GLYMA20G28720.3} RP IDENTIFICATION. RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:GLYMA20G28720.3}; RG EnsemblPlants; RL Submitted (MAY-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 EnsemblPlants; GLYMA20G28720.3; GLYMA20G28720.3; GLYMA20G28720. DR Proteomes; UP000008827; Chromosome 20. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008827}; KW Reference proteome {ECO:0000313|Proteomes:UP000008827}. SQ SEQUENCE 341 AA; 37556 MW; A4B3426997B0B4F6 CRC64; MGLEGKETPS FMRDFLDKCG GCAVIDGGFA TELERHGADL NDELWSAKCL ISSPHLVRRV HLDYLDAGAN IILTASYQAT IQGFEAKGFS REEGETMLRR SVEIAREARE IYYDRCTKDS SDFMRDERYR KRPILIAASV GSYGAYLADG SEYVGDYGDA VTVQTLKDFH RERVKILVEA GADLIAFETI PNKLEAQAYA ELLEEEGIET PAWFSFSCKD ESNVVSGDSI FECASIADSC RQVVAVGVNC TAPRFIHGLI SFIKKATSKP VLVYPNSGET YIAESNQWVK SSGAAEHDFV SYIGKWRDAG ASLFGGCCRT TPNTIRGIAE ATYGKLKDKC I // ID I1NGI0_SOYBN Unreviewed; 340 AA. AC I1NGI0; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 01-APR-2015, entry version 13. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:GLYMA20G28720.4}; 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 {ECO:0000313|EnsemblPlants:GLYMA20G28720.4, ECO:0000313|Proteomes:UP000008827}; RN [1] {ECO:0000313|EnsemblPlants:GLYMA20G28720.4} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:GLYMA20G28720.4}; 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] {ECO:0000313|EnsemblPlants:GLYMA20G28720.4} RP IDENTIFICATION. RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:GLYMA20G28720.4}; RG EnsemblPlants; RL Submitted (MAY-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 EnsemblPlants; GLYMA20G28720.4; GLYMA20G28720.4; GLYMA20G28720. DR Proteomes; UP000008827; Chromosome 20. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008827}; KW Reference proteome {ECO:0000313|Proteomes:UP000008827}. SQ SEQUENCE 340 AA; 37457 MW; 5125A5E3F6633A7D CRC64; MGLEGKETPS FMRDFLDKCG GCAVIDGGFA TELERHGADL NDELWSAKCL ISSPHLVRRV HLDYLDAGAN IILTASYQAT IQGFEAKGFS REEGETMLRR SVEIAREARE IYYDRCTKDS SDFMRDERYR KRPILIAASV GSYGAYLADG SEYVGDYGDA VTVQTLKDFH RERVKILVEA GADLIAFETI PNKLEAQAYA ELLEEEGIET PAWFSFSCKD ESNVVSGDSI FECASIADSC RQVVAVGVNC TAPRFIHGLI SFIKKATSKP VLVYPNSGET YIAESNQWKS SGAAEHDFVS YIGKWRDAGA SLFGGCCRTT PNTIRGIAEA TYGKLKDKCI // ID I1NGI2_SOYBN Unreviewed; 280 AA. AC I1NGI2; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 01-APR-2015, entry version 13. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:GLYMA20G28720.6}; 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 {ECO:0000313|EnsemblPlants:GLYMA20G28720.6, ECO:0000313|Proteomes:UP000008827}; RN [1] {ECO:0000313|EnsemblPlants:GLYMA20G28720.6} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:GLYMA20G28720.6}; 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] {ECO:0000313|EnsemblPlants:GLYMA20G28720.6} RP IDENTIFICATION. RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:GLYMA20G28720.6}; RG EnsemblPlants; RL Submitted (MAY-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 EnsemblPlants; GLYMA20G28720.6; GLYMA20G28720.6; GLYMA20G28720. DR Proteomes; UP000008827; Chromosome 20. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008827}; KW Reference proteome {ECO:0000313|Proteomes:UP000008827}. SQ SEQUENCE 280 AA; 31109 MW; 3F7D9AC95A9E2B1D CRC64; MGLEGKETPS FMRDFLDKCG GCAVIDGGFA TELERHGADL NDELWSAKCL ISSPHLVRRV HLDYLDAGAN IILTASYQAT IQGFEAKGFS REEGETMLRR SVEIAREARE IYYDRCTKDS SDFMRDERYR KRPILIAASV GSYGAYLADG SEYVGDYGDA VTVQTLKDFH RERVKILVEA GADLIAFETI PNKLEAQAYA ELLEEEGIET PAWFSFSCKD ESNVVSGDSI FECASIADSC RQVVAVGVNC TAPRFIHGLI SFIKKVQLSN NTLLYTIKMC // ID I1P901_ORYGL Unreviewed; 329 AA. AC I1P901; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 14. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:ORGLA03G0084700.1}; 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 {ECO:0000313|EnsemblPlants:ORGLA03G0084700.1, ECO:0000313|Proteomes:UP000007306}; RN [1] {ECO:0000313|EnsemblPlants:ORGLA03G0084700.1} 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] {ECO:0000313|EnsemblPlants:ORGLA03G0084700.1} 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; ORGLA03G0084700.1; ORGLA03G0084700.1; ORGLA03G0084700. DR OMA; AINDPLW; -. DR Proteomes; UP000007306; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007306}; KW Reference proteome {ECO:0000313|Proteomes:UP000007306}. SQ SEQUENCE 329 AA; 35820 MW; 7B0F3E0728C1F7A8 CRC64; MAVAVEEIVR RAGGCAVIDG GFATQLEALG ADINDPLWSA ACLITKPHLI KEVHMQYLEA GADVIISSSY QATIPGFLAR GMLLEEAEGL LRRSIELALE ARDEFWKSTL RKSKPVYNHA LVAASIGSYG AYLADGSEYS GSYGEDISAE KLKDFHRRRL QVLASAGPDL IAFEAIPNKM EAQALVELLE EENIQVPSWI CFSSVDGKNL CSGESFAECL QFLNASDKVT IVGVNCTPPQ FIEGIIRELK KQTKKAIAVY PNSGEIWDGR EKRWLPAQCF GHKSFDALAK RWQEAGASLV GGCCRTTPST IRAVSKVLKG KTAYSATQI // ID I1QE71_ORYGL Unreviewed; 330 AA. AC I1QE71; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 11. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:ORGLA07G0241300.1}; 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 {ECO:0000313|EnsemblPlants:ORGLA07G0241300.1, ECO:0000313|Proteomes:UP000007306}; RN [1] {ECO:0000313|EnsemblPlants:ORGLA07G0241300.1} 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] {ECO:0000313|EnsemblPlants:ORGLA07G0241300.1} 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; ORGLA01G0266300.1; ORGLA01G0266300.1; ORGLA01G0266300. DR EnsemblPlants; ORGLA07G0241300.1; ORGLA07G0241300.1; ORGLA07G0241300. DR EnsemblPlants; ORGLA09G0168400.1; ORGLA09G0168400.1; ORGLA09G0168400. DR OMA; SYIGKWR; -. DR Proteomes; UP000007306; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 2. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007306}; KW Reference proteome {ECO:0000313|Proteomes:UP000007306}. SQ SEQUENCE 330 AA; 34739 MW; 91DFC43CA6077F2D CRC64; MGRGGDVDGA AGALRRFVRE AGGCAVVDGG LATELEAHGA DLHDELWSAS CLVSAPHLIR KVHLDYLDTG ANIITSASYQ ATIQGFQARG LSRERSEALL RRSVHIAQEA RAIFAEGWSK GPYANHRSSP RRPVLVAASI GSYGAYLADG SEYTGDYGIS VTKETLKSFH RRRLQVLADA GPDLIAFETI PNKLEAQAAA SGDPITECAA VADACARVGA VGVNCTAPRL VHGLILSIRK VTSKPVVVYP NSGETYVAEN KEWVESEGGA SETDFVSCVG KWRQAGAALV GGCCRTSPAT VRAISWALRE SDDAVGGDGD RDDFPAVAVL // ID I1QUL9_ORYGL Unreviewed; 335 AA. AC I1QUL9; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 13. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:ORGLA10G0090200.1}; 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 {ECO:0000313|EnsemblPlants:ORGLA10G0090200.1, ECO:0000313|Proteomes:UP000007306}; RN [1] {ECO:0000313|EnsemblPlants:ORGLA10G0090200.1} 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] {ECO:0000313|EnsemblPlants:ORGLA10G0090200.1} 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; ORGLA10G0090200.1; ORGLA10G0090200.1; ORGLA10G0090200. DR OMA; QCKDENT; -. DR Proteomes; UP000007306; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007306}; KW Reference proteome {ECO:0000313|Proteomes:UP000007306}. SQ SEQUENCE 335 AA; 36527 MW; 067B5612E99A4D75 CRC64; MSQQGEYHAD MMAEFLRGSG GAAVIDGGLA TELEANGADL KDALWSARCL FTCPDLIRKV HLDYLEAGAS VLITGSYQAT IQGFLSKGFS QEESESFLRR SVELACEARA IYLEKCSNGS DEAKDVTKYR KRPILIAASV GSYGAYLADG SEYSGDYGNE GTLEFLKNFH LRRLQVLAEA GPDVIVFETI PNKIETQAYV ELLEECKLRI PAWFGFTSKD GVNVVSGDSL IECASIADSC KEVAAVGINC TPPRFIHELV LSIRKVTSKP ILIYPNSGES YDPIRKEWVE CSGISNEDFV SYVKKWHEAG ASLIGGCCRT SPDTIRGISK ALRGV // ID I1R7Q3_ORYGL Unreviewed; 75 AA. AC I1R7Q3; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 11. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:ORGLA12G0155900.1}; 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 {ECO:0000313|EnsemblPlants:ORGLA12G0155900.1, ECO:0000313|Proteomes:UP000007306}; RN [1] {ECO:0000313|EnsemblPlants:ORGLA12G0155900.1} 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] {ECO:0000313|EnsemblPlants:ORGLA12G0155900.1} 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; ORGLA12G0155900.1; ORGLA12G0155900.1; ORGLA12G0155900. DR OMA; CILHTAT; -. DR Proteomes; UP000007306; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007306}; KW Reference proteome {ECO:0000313|Proteomes:UP000007306}. SQ SEQUENCE 75 AA; 7646 MW; A8800BA6DC30C578 CRC64; MVGKSGGGGG AAEEDGAAAV RRWVEAGGGR LVMDGGLATE LEANGADLND PLWSAKCLLS SSHLIRKSIR PKKPT // ID I1R7Q4_ORYGL Unreviewed; 153 AA. AC I1R7Q4; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAY-2015, entry version 12. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:ORGLA12G0156000.1}; DE Flags: Fragment; 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 {ECO:0000313|EnsemblPlants:ORGLA12G0156000.1, ECO:0000313|Proteomes:UP000007306}; RN [1] {ECO:0000313|EnsemblPlants:ORGLA12G0156000.1} 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] {ECO:0000313|EnsemblPlants:ORGLA12G0156000.1} 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; ORGLA12G0156000.1; ORGLA12G0156000.1; ORGLA12G0156000. DR OMA; ARLIGCC; -. DR Proteomes; UP000007306; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007306}; KW Reference proteome {ECO:0000313|Proteomes:UP000007306}. FT NON_TER 1 1 {ECO:0000313|EnsemblPlants: FT ORGLA12G0156000.1}. SQ SEQUENCE 153 AA; 16653 MW; FC800D4FE712187E CRC64; NKLEAQAYVE LLDECNISIP AWFSFNSKDG VHIVSGDSLI ECATIANGCS KVGAVGINCT PPRFIHGLIL SIRKVTDKPI LIYPNSGERY DAEKKEWVES TGVSDGDFVS YVNEWCKDGA VLIGGCCRTT PNTIKAISRS LNQRHSSLHL PVA // ID I1RXY7_GIBZE Unreviewed; 341 AA. AC I1RXY7; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 29-APR-2015, entry version 18. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ESU15755.1}; GN ORFNames=FGSG_09214 {ECO:0000313|EMBL:ESU15755.1}; 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 {ECO:0000313|EMBL:ESU15755.1}; RN [1] {ECO:0000313|EMBL:ESU15755.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PH-1 {ECO:0000313|EMBL:ESU15755.1}; 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS231668; ESU15755.1; -; Genomic_DNA. DR KEGG; fgr:FG09214.1; -. DR InParanoid; I1RXY7; -. DR KO; K00547; -. DR OrthoDB; EOG79SF86; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 341 AA; 37475 MW; 5895B951287A0B5E CRC64; MPSKILILDG GLGTSLESKY SVTFSRSTPL WSSHLLVADQ PTLQSCQSDF GAVPVDVLLT ATYQVSLHGF ADTRTEEFPN GISRENVPRF LDDSVSIAER AVGDKGCVAL SIGPYGACMI PGQEYSGKYD DKHDSLQDLE SWHRERLGVF SEVNDIQKRL GYVALETIPR LDEIIAMRKA LAATPALSKL PYWTALLSPE KDLRLPDGNS IEAAVEAMLD PEVSANIPWG IGINCTKVDK LDSLLQIFES TVSNMVEKGK IAEWPALVLY PDGTNGEVYN TTTQKWEMPD GAENQRRTSW EGQLEDVVKA TEGRGKWPAI LVGGCCRAGS EDIKKLRDRL V // ID METH_BOVIN Reviewed; 1265 AA. AC Q4JIJ3; DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 02-AUG-2005, sequence version 1. DT 07-JAN-2015, entry version 73. DE RecName: Full=Methionine synthase; DE EC=2.1.1.13; DE AltName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase; DE AltName: Full=Vitamin-B12 dependent methionine synthase; DE Short=MS; GN Name=MTR; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RA Palin M.-F., Beaudry D., Charest R., Girard C.; RT "Interactions of folic acid-vitamin B12-methionine: effects on liver RT metabolism and production of dairy cows."; RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the transfer of a methyl group from methyl- CC cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and CC methionine. Subsequently, remethylates the cofactor using CC methyltetrahydrofolate (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + L-homocysteine = CC tetrahydrofolate + L-methionine. CC -!- COFACTOR: CC Name=methyl(III)cobalamin; Xref=ChEBI:CHEBI:28115; CC Evidence={ECO:0000250}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (MetH route): step CC 1/1. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- DOMAIN: Modular enzyme with four functionally distinct domains. CC The isolated Hcy-binding domain catalyzes methyl transfer from CC free methylcobalamin to homocysteine. The Hcy-binding domain in CC association with the pterin-binding domain catalyzes the CC methylation of cob(I)alamin by methyltetrahydrofolate and the CC methylation of homocysteine. The B12-binding domain binds the CC cofactor. The AdoMet activation domain binds S-adenosyl-L- CC methionine. Under aerobic conditions cob(I)alamin can be converted CC to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L- CC methionine and flavodoxin regenerates methylcobalamin (By CC similarity). {ECO:0000250}. CC -!- MISCELLANEOUS: L-homocysteine is bound via the zinc atom. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine CC synthase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 AdoMet activation domain. CC {ECO:0000255|PROSITE-ProRule:PRU00346}. CC -!- SIMILARITY: Contains 1 B12-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00666}. CC -!- SIMILARITY: Contains 1 B12-binding N-terminal domain. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC -!- SIMILARITY: Contains 1 pterin-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00334}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DQ084519; AAY86762.1; -; mRNA. DR RefSeq; NP_001025469.1; NM_001030298.1. DR UniGene; Bt.47673; -. DR ProteinModelPortal; Q4JIJ3; -. DR SMR; Q4JIJ3; 664-920, 926-1264. DR STRING; 9913.ENSBTAP00000016262; -. DR PRIDE; Q4JIJ3; -. DR GeneID; 280869; -. DR KEGG; bta:280869; -. DR CTD; 4548; -. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR HOVERGEN; HBG006347; -. DR InParanoid; Q4JIJ3; -. DR KO; K00548; -. DR UniPathway; UPA00051; UER00081. DR NextBio; 20805009; -. DR Proteomes; UP000009136; Unplaced. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 2: Evidence at transcript level; KW Amino-acid biosynthesis; Cobalamin; Cobalt; Complete proteome; KW Cytoplasm; Metal-binding; Methionine biosynthesis; Methyltransferase; KW Reference proteome; Repeat; S-adenosyl-L-methionine; Transferase; KW Zinc. FT CHAIN 1 1265 Methionine synthase. FT /FTId=PRO_0000251734. FT DOMAIN 19 338 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT DOMAIN 371 632 Pterin-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00334}. FT DOMAIN 662 759 B12-binding N-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00666}. FT DOMAIN 772 907 B12-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00666}. FT DOMAIN 923 1265 AdoMet activation. {ECO:0000255|PROSITE- FT ProRule:PRU00346}. FT REGION 860 861 Cobalamin-binding. {ECO:0000250}. FT REGION 1227 1228 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT METAL 260 260 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 323 323 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 324 324 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 785 785 Cobalt (cobalamin axial ligand). FT {ECO:0000250}. FT BINDING 830 830 Cobalamin. {ECO:0000250}. FT BINDING 974 974 S-adenosyl-L-methionine. {ECO:0000250}. FT BINDING 1172 1172 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000250}. FT BINDING 1176 1176 Cobalamin; via carbonyl oxygen. FT {ECO:0000250}. SQ SEQUENCE 1265 AA; 140478 MW; 7E1E03AB95134529 CRC64; MAPTLQDLTP SAGMKKTLQD EIEAILQERI MVLDGGMGTM IQRHKLSEED FRGQEFKDHA RPLKGNNDIL SITQPNVIYQ IHKEYLLAGA DIIETNTFSS TSIAQADYGL EHLAYRMNMC SAGVARKAAE DISLQTGIKR YVAGALGPTN KTLSVSPSVE RPDYRNITFD ELVEAYKEQA KGLLDGGVDI LLIETIFDTA NAKAALFAVQ KLFEEEYVPR PVFISGTIVD KSGRTLSGQT GEAFVISVSH ADPLCIGLNC ALGAAEMRPF IETIGKCTTA YVLCYPNAGL PNTFGDYDET PHVMAMHLKD FAVDGLVNIV GGCCGTTPDH IREIAEAVKN CKPRVPPATV FEGHMLLSGL EPFRIGPYTN FVNIGERCNV AGSRRFAKLI MAGNYEEALS VAKMQVEMGA QVLDINMDDG MLDGPSAMTR FCNFIASEPD IAKVPLCIDS SNFAVIEAGL KCCQGKCIVN SISLKEGEDD FLEKARKIKK FGAAVVVMAF DEEGQATETD PKIRVCTRAY HLLLKKLGFN PNDIIFDPNI LTIGTGMEEH NLYAVNFINA TKVIKETLPG AKVSGGLSNL SFSFRGMEAI REAMHGVFLY HAIKFGMDMG IVNAGSLPVY DDIHKELLQL CEDLIWNRDP EATEKLLHYA QTQGKGGKKV IQTDEWRNGP LEERLEYALV KGIEKYIIED TEEARLNQEK YPRPLNIIEG PLMNGMKIVG DLFGAGKMFL PQVIKSARVM KKAVGHLIPF MEKEREETKV LTGKIEDEDP YQGTIVLATV KGDVHDIGKN IVGVVLGCNN FRVIDLGVMT PCDKILKAAL DHKADIIGLS GLITPSLDEM IFVAKEMERL AIKIPLLIGG ATTSRTHTAV KIAPRYSAPV IHVLDASKSV VVCSQLLDEN LKDEYFEEIL EEYEDIRQDH YESLKERRYL TLRQARENGF HIDWLSEPPP VKPTFLGTRV FEDYDLQKLV DYIDWKPFFD VWQLRGKYPN RGFPKIFDDK TVGEEAKKVY DDAQNMLQAL ISQKKLQARG VVGFWPAQSI QDDIHLYAEG AVPQASEPIA TFYGLRQQAE KDSASSDPYL CLSDFIAPLH SGIPDYLGLF AVACFGVEEL SKAYEEECDD YSSIMVKALG DRLAEAFAEE LHERARRELW GYCSGEQLAV ADLRRLRYEG IRPAPGYPSQ PDHTEKLTVW RLADVEQRTG IRLTESLAMA PASAVSGLYF SNLKSKYFAV GKISKDQIED YASRKNMSVA EVEKWLGPIL GYDTD // ID METH_CAEBR Reviewed; 1273 AA. AC A8XY95; DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot. DT 16-DEC-2008, sequence version 2. DT 07-JAN-2015, entry version 52. DE RecName: Full=Probable methionine synthase; DE EC=2.1.1.13; DE AltName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase; DE AltName: Full=Vitamin-B12 dependent methionine synthase; DE Short=MS; GN Name=metr-1; ORFNames=CBG20636; OS Caenorhabditis briggsae. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6238; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AF16; RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045; RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N., RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., RA D'Eustachio P., Fitch D.H.A., Fulton L.A., Fulton R.E., RA Griffiths-Jones S., Harris T.W., Hillier L.W., Kamath R., RA Kuwabara P.E., Mardis E.R., Marra M.A., Miner T.L., Minx P., RA Mullikin J.C., Plumb R.W., Rogers J., Schein J.E., Sohrmann M., RA Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K., Durbin R.M., RA Waterston R.H.; RT "The genome sequence of Caenorhabditis briggsae: a platform for RT comparative genomics."; RL PLoS Biol. 1:166-192(2003). CC -!- FUNCTION: Catalyzes the transfer of a methyl group from methyl- CC cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and CC methionine. Subsequently, remethylates the cofactor using CC methyltetrahydrofolate (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + L-homocysteine = CC tetrahydrofolate + L-methionine. CC -!- COFACTOR: CC Name=methyl(III)cobalamin; Xref=ChEBI:CHEBI:28115; CC Evidence={ECO:0000250}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (MetH route): step CC 1/1. CC -!- DOMAIN: Modular enzyme with four functionally distinct domains. CC The isolated Hcy-binding domain catalyzes methyl transfer from CC free methylcobalamin to homocysteine. The Hcy-binding domain in CC association with the pterin-binding domain catalyzes the CC methylation of cob(I)alamin by methyltetrahydrofolate and the CC methylation of homocysteine. The B12-binding domain binds the CC cofactor. The AdoMet activation domain binds S-adenosyl-L- CC methionine. Under aerobic conditions cob(I)alamin can be converted CC to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L- CC methionine and flavodoxin regenerates methylcobalamin (By CC similarity). {ECO:0000250}. CC -!- MISCELLANEOUS: L-homocysteine is bound via the zinc atom. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine CC synthase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 AdoMet activation domain. CC {ECO:0000255|PROSITE-ProRule:PRU00346}. CC -!- SIMILARITY: Contains 1 B12-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00666}. CC -!- SIMILARITY: Contains 1 B12-binding N-terminal domain. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC -!- SIMILARITY: Contains 1 pterin-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00334}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE600991; CAP37612.2; -; Genomic_DNA. DR STRING; 6238.CBG20636; -. DR EnsemblMetazoa; CBG20636; CBG20636; CBG20636. DR WormBase; CBG20636; CBP26766; WBGene00039583; Cbr-metr-1. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR InParanoid; A8XY95; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG7TF786; -. DR UniPathway; UPA00051; UER00081. DR Proteomes; UP000008549; Chromosome II. DR Proteomes; UP000008549; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Cobalamin; Cobalt; Complete proteome; KW Metal-binding; Methionine biosynthesis; Methyltransferase; KW Reference proteome; Repeat; S-adenosyl-L-methionine; Transferase; KW Zinc. FT CHAIN 1 1273 Probable methionine synthase. FT /FTId=PRO_0000412913. FT DOMAIN 7 327 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT DOMAIN 360 621 Pterin-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00334}. FT DOMAIN 652 749 B12-binding N-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00666}. FT DOMAIN 762 897 B12-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00666}. FT DOMAIN 927 1273 AdoMet activation. {ECO:0000255|PROSITE- FT ProRule:PRU00346}. FT REGION 850 851 Cobalamin-binding. {ECO:0000250}. FT REGION 1225 1226 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT METAL 249 249 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 312 312 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 313 313 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 775 775 Cobalt (cobalamin axial ligand). FT {ECO:0000250}. FT BINDING 820 820 Cobalamin. {ECO:0000250}. FT BINDING 977 977 S-adenosyl-L-methionine. {ECO:0000250}. FT BINDING 1171 1171 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000250}. FT BINDING 1175 1175 Cobalamin; via carbonyl oxygen. FT {ECO:0000250}. SQ SEQUENCE 1273 AA; 141762 MW; 7178233645CE06AE CRC64; MTRSSLFKEL ADIAKERIMI IDGAMGTMIQ REYMEEHDFR GEILKDHDKP LKGNNDLLSI TRPDIIYKIH KLYLEAGADF IETNTFSGTT IAQADYHCEH LVHEINYQSA LVARRACDDV GAATGIRRYV CGAIGPTNRT LSISPSVEKP DFRNVTFQEL VKAYGDQARS LIQGGVDVLL VETVFDSANA KAALFAIRTL FEDEGVPEIP VFLSGTIVDM SGRTLSGQTG EAFLVSTKQG KPIAVGLNCA LGAKDMRQFV QNMSLWSDTL ILCYPNAGLP NALGGYDETP EEMAEVLREF AQDGLVNIIG GCCGTTPDHI NAMYKAVQGI SPRVPPADPH AGKMLLSGLE PSIVGPETNF VNIGERCNVA GSRRFCNLIK NENYDTAIDV ARVQVDSGAQ ILDVNMDDGL LDGPYAMSKF LRLISSEPDV AKIPVCIDSS DFDVIIAGLE STQGKCVVNS ISLKEGEEKF KERARIVKRY GAAVVVMAFD EEGQAAETER KFEICERSYR ILTEEVGFNP NDIIFDANIL TIATGMDEHA NYGMYFIEAT RMIRENLPGA HVSGGVSNIS FSFRGMEAIR EAMHSVFLFY AIKAGMDMGI VNAGALPVYE DIDKPLLQLL EDLLFNRDPE ATEKLLVAAQ EMKKDGKKAD TKTDEWRNTS VEERLKFALV KGIDQFVVAD TEEARQNTEK YPRPLNVIER PLMDGMAVVG ELFGAGKMFL PQVIKSARVM KKAVAHLLPF MDAERQANIE KMGLDEDESP YQGTVVIATV KGDVHDIGKN IVAVVLGCNN FKVVDLGVMT PCENIIKAAI EEKADFIGLS GLITPSLDEM VHVAKEMNRV GLKIPLLIGG ATTSKTHTAV KIAPRYPHPV VHCLDASKSV VVCSSLSDMT VRDAFLQDLN EDYEDVRTKM CLVSYLNHFF ITEHYESLKD RRFVALGKTR EKKFNIDWNK FSPVKPSFIG RREFQNFDFK ELIPYIDWKP FFDVWQLRGK YPNRSYPKIF DDADVGGEAK RVFDDAQTWL KKLIDEKVLT ANAVVSFLPA ASEGDDIHVY DPETGNKLDT FYGLRQQSGR EHDQSHFCLS DFIRPLKIGV PDDYLGLFAC TAGLGAEEYC KVLEENHDDY ASIMVKALAD RLAEAYAEYL HKEVRVNLWG YSTNEQLTET DLLSIKYEGI RPACGYPSQP DHTEKRTLWK LLEAEKNGIV LTEHLAMLPA ASVSGLYFAN PQSQYFAVGK IDEDQVAFIY VRSKNVTDYA ARKNVPKEEV ERWLSPIIGY ELD // ID METH_CAEEL Reviewed; 1249 AA. AC Q09582; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAY-2015, entry version 125. DE RecName: Full=Probable methionine synthase; DE EC=2.1.1.13; DE AltName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase; DE AltName: Full=Vitamin-B12 dependent methionine synthase; DE Short=MS; GN Name=metr-1; ORFNames=R03D7.1; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for RT investigating biology."; RL Science 282:2012-2018(1998). CC -!- FUNCTION: Catalyzes the transfer of a methyl group from methyl- CC cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and CC methionine. Subsequently, remethylates the cofactor using CC methyltetrahydrofolate (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + L-homocysteine = CC tetrahydrofolate + L-methionine. CC -!- COFACTOR: CC Name=methyl(III)cobalamin; Xref=ChEBI:CHEBI:28115; CC Evidence={ECO:0000250}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (MetH route): step CC 1/1. CC -!- DOMAIN: Modular enzyme with four functionally distinct domains. CC The isolated Hcy-binding domain catalyzes methyl transfer from CC free methylcobalamin to homocysteine. The Hcy-binding domain in CC association with the pterin-binding domain catalyzes the CC methylation of cob(I)alamin by methyltetrahydrofolate and the CC methylation of homocysteine. The B12-binding domain binds the CC cofactor. The AdoMet activation domain binds S-adenosyl-L- CC methionine. Under aerobic conditions cob(I)alamin can be converted CC to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L- CC methionine and flavodoxin regenerates methylcobalamin (By CC similarity). {ECO:0000250}. CC -!- MISCELLANEOUS: L-homocysteine is bound via the zinc atom. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine CC synthase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 AdoMet activation domain. CC {ECO:0000255|PROSITE-ProRule:PRU00346}. CC -!- SIMILARITY: Contains 1 B12-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00666}. CC -!- SIMILARITY: Contains 1 B12-binding N-terminal domain. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC -!- SIMILARITY: Contains 1 pterin-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00334}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z46828; CAA86855.1; -; Genomic_DNA. DR PIR; T23868; T23868. DR RefSeq; NP_496353.1; NM_063952.4. DR UniGene; Cel.16853; -. DR ProteinModelPortal; Q09582; -. DR SMR; Q09582; 5-640. DR BioGrid; 39991; 1. DR DIP; DIP-26122N; -. DR IntAct; Q09582; 1. DR MINT; MINT-1116270; -. DR STRING; 6239.R03D7.1; -. DR PaxDb; Q09582; -. DR PRIDE; Q09582; -. DR EnsemblMetazoa; R03D7.1; R03D7.1; WBGene00010988. DR GeneID; 174681; -. DR KEGG; cel:CELE_R03D7.1; -. DR UCSC; R03D7.1; c. elegans. DR CTD; 174681; -. DR WormBase; R03D7.1; CE01609; WBGene00010988; metr-1. DR eggNOG; COG1410; -. DR GeneTree; ENSGT00420000029824; -. DR HOGENOM; HOG000251409; -. DR InParanoid; Q09582; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG7TF786; -. DR PhylomeDB; Q09582; -. DR Reactome; REACT_274901; Methylation. DR Reactome; REACT_320610; Sulfur amino acid metabolism. DR Reactome; REACT_347550; Cobalamin (Cbl, vitamin B12) transport and metabolism. DR UniPathway; UPA00051; UER00081. DR NextBio; 885042; -. DR PRO; PR:Q09582; -. DR Proteomes; UP000001940; Chromosome II. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IBA:GO_Central. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Cobalamin; Cobalt; Complete proteome; KW Metal-binding; Methionine biosynthesis; Methyltransferase; KW Reference proteome; Repeat; S-adenosyl-L-methionine; Transferase; KW Zinc. FT CHAIN 1 1249 Probable methionine synthase. FT /FTId=PRO_0000204531. FT DOMAIN 1 327 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT DOMAIN 360 621 Pterin-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00334}. FT DOMAIN 652 749 B12-binding N-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00666}. FT DOMAIN 762 897 B12-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00666}. FT DOMAIN 913 1249 AdoMet activation. {ECO:0000255|PROSITE- FT ProRule:PRU00346}. FT REGION 850 851 Cobalamin-binding. {ECO:0000250}. FT REGION 1211 1212 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT METAL 249 249 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 312 312 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 313 313 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 775 775 Cobalt (cobalamin axial ligand). FT {ECO:0000250}. FT BINDING 820 820 Cobalamin. {ECO:0000250}. FT BINDING 963 963 S-adenosyl-L-methionine. {ECO:0000250}. FT BINDING 1157 1157 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000250}. FT BINDING 1161 1161 Cobalamin; via carbonyl oxygen. FT {ECO:0000250}. SQ SEQUENCE 1249 AA; 138899 MW; 4D16028AD02CD550 CRC64; MTRSSLFEEL AEIAKERIMI IDGAMGTMIQ REYMEEEDFR GEILKDHDKP LKGNNDLLSI TRPDIIYKIH KLYLEAGADF VETNTFSGTT IAQADYRCEH LVHEINYQSA LVARRACDDV GAATGRRRYV CGAIGPTNRT LSISPSVEKP DFRNVTFQEL VKAYGDQARS LIQGGVDVLL VETVFDSANA KAALFAIRTL FEDEGVPEMP VFLSGTIVDM SGRTLSGQTG EAFLVSTKQG KPMAVGLNCA LGAKDMRQFV DNMSKWSDSF IICYPNAGLP NALGGYDETP EEMADVLREF ARDGLVNIIG GCCGTTPDHI NAMYKAVQGI TPRVPPQDPH AGKMLLSGLE PSIVGPETNF VNIGERCNVA GSRRFCNLIK NENYDTAIDV ARVQVDSGAQ ILDVNMDDGL LDGPYAMSKF LRLISSEPDV AKIPVCIDSS DFDVIIAGLE STQGKCVVNS ISLKEGEEKF KERARIIKRY GAAVVVMAFD EQGQAAETDP KFEICERSYR ILTEEVGFNP NDIIFDANIL TIATGMEEHS NYGMYFIEAA RMIRENLPGA HVSGGVSNIS FSFRGMEAIR EAMHSVFLFY AIKAGMDMGI VNAGALPVYE DIDKPLLQLL EDLLFNRDPE ATEKLLVAAQ EMKKDGKKAD TKTDEWRSLT VEERLKFALV KGVDQFVVAD TEEARQNTAK YPRPLNVIER PLMDGMAVVG ELFGAGKMFL PQVIKSARVM KKAVAHLLPF MEIERQANIE TMGLAEDESP YQGTVVIATV KGDVHDIGKN IVSVVLGCNN FKVVDLGVMT PCENIIKAAI EEKADFIGLS GLITPSLDEM VYVAKEMNRV GLNIPLLIGG ATTSKTHTAV KISPRYPHPV VHCLDASKSV VVCSSLSDMS VRDAFLQDLN EDYEDVRQEH YASLKDRRFT DLNKTREKKF KIDWDKFTAV KPSFVGRREY QNFDLNELIP YIDWKPFFDV WQLRGKYPNR SYPKIFDDAD VGAEAKKVFD DAQTWLKKLI DEKILVANAV VSFLPAASEG DDMHVYDPET GNKLDTFYGL RQQSGREHDQ PHFCLSDFIK PLKNGVPDDY LGLFACTAGL GAEEYCKTLE KNHDDYASIM VKALADRLAE AYAEYLHKEV RTTLWGYSTN EDLTESDLLS IKYQGIRPAC GYPSQPDHTE KRTLWKLLEA EKNGIGLTEH LAMLPAASVS GLYFANPQSE YFAVGKIDQD QVIDYAARKN VPKEEVERWL SPILGYDTD // ID METH_DICDI Reviewed; 1260 AA. AC Q54P92; DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 24-MAY-2005, sequence version 1. DT 27-MAY-2015, entry version 69. DE RecName: Full=Methionine synthase; DE EC=2.1.1.13; DE AltName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase; DE AltName: Full=Vitamin-B12 dependent methionine synthase; DE Short=MS; GN Name=mtr; ORFNames=DDB_G0284699; OS Dictyostelium discoideum (Slime mold). OC Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; Dictyostelium. OX NCBI_TaxID=44689; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AX4; RX PubMed=15875012; DOI=10.1038/nature03481; RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., RA Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., RA Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., RA Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., RA Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., RA Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., RA Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., RA Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., RA Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., RA Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., RA Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., RA Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., RA Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., RA Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., RA Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., RA Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., RA Kuspa A.; RT "The genome of the social amoeba Dictyostelium discoideum."; RL Nature 435:43-57(2005). CC -!- FUNCTION: Catalyzes the transfer of a methyl group from methyl- CC cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and CC methionine. Subsequently, remethylates the cofactor using CC methyltetrahydrofolate (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + L-homocysteine = CC tetrahydrofolate + L-methionine. CC -!- COFACTOR: CC Name=methyl(III)cobalamin; Xref=ChEBI:CHEBI:28115; CC Evidence={ECO:0000250}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (MetH route): step CC 1/1. CC -!- DOMAIN: Modular enzyme with four functionally distinct domains. CC The isolated Hcy-binding domain catalyzes methyl transfer from CC free methylcobalamin to homocysteine. The Hcy-binding domain in CC association with the pterin-binding domain catalyzes the CC methylation of cob(I)alamin by methyltetrahydrofolate and the CC methylation of homocysteine. The B12-binding domain binds the CC cofactor. The AdoMet activation domain binds S-adenosyl-L- CC methionine. Under aerobic conditions cob(I)alamin can be converted CC to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L- CC methionine and flavodoxin regenerates methylcobalamin (By CC similarity). {ECO:0000250}. CC -!- MISCELLANEOUS: L-homocysteine is bound via the zinc atom. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine CC synthase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 AdoMet activation domain. CC {ECO:0000255|PROSITE-ProRule:PRU00346}. CC -!- SIMILARITY: Contains 1 B12-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00666}. CC -!- SIMILARITY: Contains 1 B12-binding N-terminal domain. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC -!- SIMILARITY: Contains 1 pterin-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00334}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAFI02000070; EAL65119.1; -; Genomic_DNA. DR RefSeq; XP_638483.1; XM_633391.1. DR ProteinModelPortal; Q54P92; -. DR SMR; Q54P92; 657-913, 919-1254. DR STRING; 44689.DDB_0230138; -. DR PRIDE; Q54P92; -. DR EnsemblProtists; DDB0230138; DDB0230138; DDB_G0284699. DR GeneID; 8624734; -. DR KEGG; ddi:DDB_G0284699; -. DR dictyBase; DDB_G0284699; mtr. DR eggNOG; COG1410; -. DR InParanoid; Q54P92; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR PhylomeDB; Q54P92; -. DR Reactome; REACT_312990; Sulfur amino acid metabolism. DR Reactome; REACT_324921; Methylation. DR Reactome; REACT_348495; Cobalamin (Cbl, vitamin B12) transport and metabolism. DR UniPathway; UPA00051; UER00081. DR PRO; PR:Q54P92; -. DR Proteomes; UP000002195; Chromosome 4. DR Proteomes; UP000002195; Unassembled WGS sequence. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; ISS:UniProtKB. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; ISS:UniProtKB. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Cobalamin; Cobalt; Complete proteome; KW Metal-binding; Methionine biosynthesis; Methyltransferase; KW Reference proteome; Repeat; S-adenosyl-L-methionine; Transferase; KW Zinc. FT CHAIN 1 1260 Methionine synthase. FT /FTId=PRO_0000327799. FT DOMAIN 13 333 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT DOMAIN 364 625 Pterin-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00334}. FT DOMAIN 655 749 B12-binding N-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00666}. FT DOMAIN 766 883 B12-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00666}. FT DOMAIN 916 1256 AdoMet activation. {ECO:0000255|PROSITE- FT ProRule:PRU00346}. FT REGION 853 854 Cobalamin-binding. {ECO:0000250}. FT REGION 1218 1219 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT METAL 255 255 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 318 318 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 319 319 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 778 778 Cobalt (cobalamin axial ligand). FT {ECO:0000250}. FT BINDING 823 823 Cobalamin. {ECO:0000250}. FT BINDING 966 966 S-adenosyl-L-methionine. {ECO:0000250}. FT BINDING 1163 1163 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000250}. FT BINDING 1167 1167 Cobalamin; via carbonyl oxygen. FT {ECO:0000250}. SQ SEQUENCE 1260 AA; 140122 MW; 095402C1F5889CF0 CRC64; MINSNDKNES DTFGIIRKIL SERIMVLDGA MGTEIQKFKL KDNDYRGEEF KDFPHELGGN NDLLSLTQPH IIREIHCKYL EAGADFIETN TFNGNIFSQA DYKMEHLVKR INIESARLAK SACEEYTKKD PSRPRFVCGA VGPTNKTASI SPSVERPEAR NVLFDELVSG YLEQVEALVE GGIDVILVET VFDSLNCKAA LFAIEEFFKT YSPRLPVFVS GTIVDKSGRT LSGQTGEAFY TSVASANLMV FGLNCALGAQ EMRPFLQNIS KCSECYVSCY PNAGLPNTFG GYDETPEMMA EQIKEFAESG LLNIVGGCCG TSPDHIRAFC NAIEGIAPRA IPTLVPNTTL SGLEPLVFTK ELNFVNVGER CNVSGSRRFA NLIKANKYEE ALSVARQQVE AGAQIIDINM DEGMIDAVAA IQKFLFFIGS EPEISKVPIM LDSSNFDVVE AGLKCVQGKC IVNSISLKVG EELFIKQAKI VKQYGASVVV MAFDENGQAT SKEEKVRICY RSYKILTEQV GFYPQDIIFD PNILTIATGL EEHNNYGVEF IEATREIKAL MPLTRVSGGV SNLSFSFRGN EPLREAMHSA FLYYAIAAGM DMGIVNAGAL PIYDDIPKDL LKLVEDAILN RTNDATEKLL EYAQANNKSE KANVEVEEWR NKPVSERIAH ALVKGITTYI IEDTEEARNT LPSSLSVIEG PLMGGMNVVG DLFGAGKMFL PQVIKSARVM KKAVAHLIPF MEEEKRLKRL EKGNDEAAED EPDNAGVVVL ATVKGDVHDI GKNIVGVVLG CNNYKVIDIG VMTPCEKIVE AIIANKADVV GLSGLITPSL DEMIYVASEL ERLKFKIPLM IGGATTSQIH TAVKISPHYS QPTVHVLDAS RSVTVVQSLL DPNNKEVFAE DVSQQYAELR EKHYASLKDR KYTSLEKARQ HCVKVNWKTI QPVKPTFLGT QVFKEYSLEK LVTKIDWNPF FVTWQLRGKY PNRGYPRIFN DETVGAEAKK LFDDAQTMLK EIVDKKLLNA RGVIGFYPAN SIDEDIIIYD HNDDETRSKP IATLFGLRQQ NEKETDEPYI AIGDYIAPVS SGVKDYIGLF AVSSGFGLED MVEKYKKEND DYSSIMAKAL ADRLAEALAE AVHEDVRREH WAYEKDQALS NEDLFKIKYK GIRPAPGYPA QPDHTEMKTI WSLMNVNENT SIELTDHMAM LPGAAVCGVY FSHEHAKYFS VGKITKEQIE SYASRKQITK EEAERWLSSI LSYDRLPLVK // ID METH_ECOLI Reviewed; 1227 AA. AC P13009; Q2M6T5; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 5. DT 27-MAY-2015, entry version 161. DE RecName: Full=Methionine synthase; DE EC=2.1.1.13; DE AltName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase; DE AltName: Full=Methionine synthase, vitamin-B12-dependent; DE Short=MS; GN Name=metH; OrderedLocusNames=b4019, JW3979; 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=2185137; DOI=10.1016/0378-1119(90)90490-I; RA Old I.G., Margarita D., Glass R.E., Saint-Girons I.; RT "Nucleotide sequence of the metH gene of Escherichia coli K-12 and RT comparison with that of Salmonella typhimurium LT2."; RL Gene 87:15-21(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. RC STRAIN=K12; RX PubMed=2668277; RA Banerjee R.V., Johnston N.L., Sobeski J.K., Datta P., Matthews R.G.; RT "Cloning and sequence analysis of the Escherichia coli metH gene RT encoding cobalamin-dependent methionine synthase and isolation of a RT tryptic fragment containing the cobalamin-binding domain."; RL J. Biol. Chem. 264:13888-13895(1989). RN [3] RP SEQUENCE REVISION. RX PubMed=8369296; DOI=10.1021/bi00087a004; RA Drummond J.T., Loo R.R., Matthews R.G.; RT "Electrospray mass spectrometric analysis of the domains of a large RT enzyme: observation of the occupied cobalamin-binding domain and RT redefinition of the carboxyl terminus of methionine synthase."; RL Biochemistry 32:9282-9289(1993). RN [4] 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 [5] 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 [6] 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 [7] RP PROTEIN SEQUENCE OF 2-7, CHARACTERIZATION, DOMAIN, AND MUTAGENESIS OF RP CYS-310 AND CYS-311. RC STRAIN=K12; RX PubMed=9201956; DOI=10.1021/bi9705164; RA Goulding C.W., Postigo D., Matthews R.G.; RT "Cobalamin-dependent methionine synthase is a modular protein with RT distinct regions for binding homocysteine, methyltetrahydrofolate, RT cobalamin, and adenosylmethionine."; RL Biochemistry 36:8082-8091(1997). RN [8] RP CRYSTALLIZATION. RX PubMed=1593636; DOI=10.1016/0022-2836(92)90940-L; RA Luschinsky C.L., Drummond J.T., Matthews R.G., Ludwig M.L.; RT "Crystallization and preliminary X-ray diffraction studies of the RT cobalamin-binding domain of methionine synthase from Escherichia RT coli."; RL J. Mol. Biol. 225:557-560(1992). RN [9] RP CHARACTERIZATION, AND MUTAGENESIS OF ASP-757; HIS-759 AND SER-810. RC STRAIN=K12; RX PubMed=8652590; DOI=10.1021/bi952389m; RA Jarrett J.T., Amaratunga M., Drennan C.L., Scholten J.D., Sands R.H., RA Ludwig M.L., Matthews R.G.; RT "Mutations in the B12-binding region of methionine synthase: how the RT protein controls methylcobalamin reactivity."; RL Biochemistry 35:2464-2475(1996). RN [10] RP ZINC BINDING SITES. RC STRAIN=K12; RX PubMed=9398304; DOI=10.1021/bi971988l; RA Goulding C.W., Matthews R.G.; RT "Cobalamin-dependent methionine synthase from Escherichia coli: RT involvement of zinc in homocysteine activation."; RL Biochemistry 36:15749-15757(1997). RN [11] RP IDENTIFICATION BY 2D-GEL. RX PubMed=9298644; DOI=10.1002/elps.1150180805; RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., RA Neidhardt F.C.; RT "Escherichia coli proteome analysis using the gene-protein database."; RL Electrophoresis 18:1243-1251(1997). RN [12] RP ZINC BINDING SITES, AND ROLE OF ZINC IN SUBSTRATE BINDING. RC STRAIN=K12; RX PubMed=11170420; DOI=10.1021/bi001711c; RA Peariso K., Zhou Z.S., Smith A.E., Matthews R.G., Penner-Hahn J.E.; RT "Characterization of the zinc sites in cobalamin-independent and RT cobalamin-dependent methionine synthase using zinc and selenium X-ray RT absorption spectroscopy."; RL Biochemistry 40:987-993(2001). RN [13] RP REVIEW. RX PubMed=11513576; DOI=10.1021/ar0000051; RA Matthews R.G.; RT "Cobalamin-dependent methyltransferases."; RL Acc. Chem. Res. 34:681-689(2001). RN [14] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 651-896 IN COMPLEX WITH RP COBALAMIN. RX PubMed=7992050; DOI=10.1126/science.7992050; RA Drennan C.L., Huang S., Drummond J.T., Matthews R.G., Ludwig M.L.; RT "How a protein binds B12: a 3.0 A X-ray structure of B12-binding RT domains of methionine synthase."; RL Science 266:1669-1674(1994). RN [15] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 897-1227 IN COMPLEX WITH RP S-ADENOSYL-L-METHIONINE. RC STRAIN=K12; RX PubMed=8939751; DOI=10.1016/S0969-2126(96)00135-9; RA Dixon M.M., Huang S., Matthews R.G., Ludwig M.L.; RT "The structure of the C-terminal domain of methionine synthase: RT presenting S-adenosylmethionine for reductive methylation of B12."; RL Structure 4:1263-1275(1996). RN [16] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 651-1227 OF WILD-TYPE AND RP MUTANT GLY-759 IN COMPLEX WITH COBALAMIN. RC STRAIN=K12; RX PubMed=11731805; DOI=10.1038/nsb738; RA Bandarian V., Pattridge K.A., Lennon B.W., Huddler D.P., RA Matthews R.G., Ludwig M.L.; RT "Domain alternation switches B(12)-dependent methionine synthase to RT the activation conformation."; RL Nat. Struct. Biol. 9:53-56(2002). CC -!- FUNCTION: Catalyzes the transfer of a methyl group from methyl- CC cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and CC methionine. Subsequently, remethylates the cofactor using CC methyltetrahydrofolate. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + L-homocysteine = CC tetrahydrofolate + L-methionine. CC -!- COFACTOR: CC Name=methyl(III)cobalamin; Xref=ChEBI:CHEBI:28115; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 1 zinc ion per subunit.; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (MetH route): step CC 1/1. CC -!- DOMAIN: Modular enzyme with four functionally distinct domains. CC The isolated Hcy-binding domain catalyzes methyl transfer from CC free methylcobalamin to homocysteine. The Hcy-binding domain in CC association with the pterin-binding domain catalyzes the CC methylation of cob(I)alamin by methyltetrahydrofolate and the CC methylation of homocysteine. The B12-binding domain binds the CC cofactor. The AdoMet activation domain binds S-adenosyl-L- CC methionine. Under aerobic conditions cob(I)alamin can be converted CC to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L- CC methionine and flavodoxin regenerates methylcobalamin. CC {ECO:0000269|PubMed:9201956}. CC -!- MISCELLANEOUS: L-homocysteine is bound via the zinc atom. CC -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine CC synthase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 AdoMet activation domain. CC {ECO:0000255|PROSITE-ProRule:PRU00346}. CC -!- SIMILARITY: Contains 1 B12-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00666}. CC -!- SIMILARITY: Contains 1 B12-binding N-terminal domain. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC -!- SIMILARITY: Contains 1 pterin-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00334}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X16584; CAA34601.1; -; Genomic_DNA. DR EMBL; J04975; AAA02995.1; -; Unassigned_DNA. DR EMBL; U00006; AAC43113.1; -; Genomic_DNA. DR EMBL; U00096; AAC76989.1; -; Genomic_DNA. DR EMBL; AP009048; BAE78021.1; -; Genomic_DNA. DR PIR; B65209; XYECMH. DR RefSeq; NP_418443.1; NC_000913.3. DR PDB; 1BMT; X-ray; 3.00 A; A/B=651-896. DR PDB; 1K7Y; X-ray; 3.00 A; A=651-1227. DR PDB; 1K98; X-ray; 3.75 A; A=651-1227. DR PDB; 1MSK; X-ray; 1.80 A; A=897-1227. DR PDB; 3BUL; X-ray; 2.30 A; A=649-1227. DR PDB; 3IV9; X-ray; 3.25 A; A=649-1227. DR PDB; 3IVA; X-ray; 2.70 A; A=649-1227. DR PDBsum; 1BMT; -. DR PDBsum; 1K7Y; -. DR PDBsum; 1K98; -. DR PDBsum; 1MSK; -. DR PDBsum; 3BUL; -. DR PDBsum; 3IV9; -. DR PDBsum; 3IVA; -. DR ProteinModelPortal; P13009; -. DR SMR; P13009; 6-639, 651-1227. DR IntAct; P13009; 13. DR STRING; 511145.b4019; -. DR SWISS-2DPAGE; P13009; -. DR PaxDb; P13009; -. DR PRIDE; P13009; -. DR EnsemblBacteria; AAC76989; AAC76989; b4019. DR EnsemblBacteria; BAE78021; BAE78021; BAE78021. DR GeneID; 948522; -. DR KEGG; ecj:Y75_p3906; -. DR KEGG; eco:b4019; -. DR PATRIC; 32123567; VBIEscCol129921_4132. DR EchoBASE; EB0582; -. DR EcoGene; EG10587; metH. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR InParanoid; P13009; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR PhylomeDB; P13009; -. DR BioCyc; EcoCyc:HOMOCYSMETB12-MONOMER; -. DR BioCyc; ECOL316407:JW3979-MONOMER; -. DR BioCyc; MetaCyc:HOMOCYSMETB12-MONOMER; -. DR BioCyc; RETL1328306-WGS:GSTH-2949-MONOMER; -. DR BRENDA; 2.1.1.13; 2026. DR UniPathway; UPA00051; UER00081. DR EvolutionaryTrace; P13009; -. DR PRO; PR:P13009; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR Genevestigator; P13009; -. DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0031419; F:cobalamin binding; IDA:BHF-UCL. DR GO; GO:0008705; F:methionine synthase activity; IDA:BHF-UCL. DR GO; GO:0008276; F:protein methyltransferase activity; IDA:BHF-UCL. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IDA:EcoCyc. DR GO; GO:0008270; F:zinc ion binding; IMP:EcoCyc. DR GO; GO:0050667; P:homocysteine metabolic process; IDA:BHF-UCL. DR GO; GO:0009086; P:methionine biosynthetic process; IDA:BHF-UCL. DR GO; GO:0006479; P:protein methylation; IDA:GOC. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IDA:BHF-UCL. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Cobalamin; Cobalt; KW Complete proteome; Direct protein sequencing; Metal-binding; KW Methionine biosynthesis; Methyltransferase; Reference proteome; KW Repeat; S-adenosyl-L-methionine; Transferase; Zinc. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:9201956}. FT CHAIN 2 1227 Methionine synthase. FT /FTId=PRO_0000204532. FT DOMAIN 2 325 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT DOMAIN 356 617 Pterin-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00334}. FT DOMAIN 650 744 B12-binding N-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00666}. FT DOMAIN 746 881 B12-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00666}. FT DOMAIN 897 1227 AdoMet activation. {ECO:0000255|PROSITE- FT ProRule:PRU00346}. FT REGION 834 835 Cobalamin-binding. FT REGION 1189 1190 S-adenosyl-L-methionine binding. FT METAL 247 247 Zinc. FT METAL 310 310 Zinc. FT METAL 311 311 Zinc. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000269|PubMed:7992050}. FT BINDING 804 804 Cobalamin. {ECO:0000269|PubMed:11731805, FT ECO:0000269|PubMed:7992050}. FT BINDING 946 946 S-adenosyl-L-methionine. FT {ECO:0000269|PubMed:8939751}. FT BINDING 1134 1134 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000269|PubMed:8939751}. FT BINDING 1138 1138 Cobalamin; via carbonyl oxygen. FT {ECO:0000269|PubMed:11731805, FT ECO:0000269|PubMed:7992050}. FT MUTAGEN 310 310 C->A,S: Loss of zinc binding. Loss of FT catalytic activity. FT {ECO:0000269|PubMed:9201956}. FT MUTAGEN 311 311 C->A,S: Loss of zinc binding. Loss of FT catalytic activity. FT {ECO:0000269|PubMed:9201956}. FT MUTAGEN 757 757 D->E: Decreases activity by about 70%. FT {ECO:0000269|PubMed:8652590}. FT MUTAGEN 757 757 D->N: Decreases activity by about 45%. FT {ECO:0000269|PubMed:8652590}. FT MUTAGEN 759 759 H->G: Loss of catalytic activity. FT {ECO:0000269|PubMed:8652590}. FT MUTAGEN 810 810 S->A: Decreases activity by about 40%. FT {ECO:0000269|PubMed:8652590}. FT CONFLICT 113 113 A -> R (in Ref. 1 and 2). {ECO:0000305}. FT CONFLICT 641 641 S -> T (in Ref. 1 and 2). {ECO:0000305}. FT CONFLICT 1079 1080 QH -> HD (in Ref. 1; CAA34601). FT {ECO:0000305}. FT CONFLICT 1195 1227 IQRDQVEDYARRKGMSVTEVERWLAPNLGYDAD -> TSAR FT SG (in Ref. 1; CAA34601). {ECO:0000305}. FT HELIX 653 656 {ECO:0000244|PDB:3BUL}. FT HELIX 659 669 {ECO:0000244|PDB:3BUL}. FT HELIX 675 685 {ECO:0000244|PDB:3BUL}. FT STRAND 686 688 {ECO:0000244|PDB:3BUL}. FT HELIX 691 694 {ECO:0000244|PDB:3BUL}. FT HELIX 696 710 {ECO:0000244|PDB:3BUL}. FT HELIX 715 737 {ECO:0000244|PDB:3BUL}. FT STRAND 738 741 {ECO:0000244|PDB:1K7Y}. FT STRAND 748 754 {ECO:0000244|PDB:3BUL}. FT HELIX 761 771 {ECO:0000244|PDB:3BUL}. FT TURN 772 774 {ECO:0000244|PDB:3BUL}. FT STRAND 776 779 {ECO:0000244|PDB:3BUL}. FT STRAND 782 784 {ECO:0000244|PDB:3BUL}. FT HELIX 786 796 {ECO:0000244|PDB:3BUL}. FT STRAND 799 804 {ECO:0000244|PDB:3BUL}. FT HELIX 809 823 {ECO:0000244|PDB:3BUL}. FT STRAND 830 834 {ECO:0000244|PDB:3BUL}. FT STRAND 835 837 {ECO:0000244|PDB:3IV9}. FT HELIX 839 845 {ECO:0000244|PDB:3BUL}. FT HELIX 847 849 {ECO:0000244|PDB:3BUL}. FT STRAND 854 856 {ECO:0000244|PDB:3BUL}. FT HELIX 860 870 {ECO:0000244|PDB:3BUL}. FT TURN 873 875 {ECO:0000244|PDB:3BUL}. FT HELIX 876 893 {ECO:0000244|PDB:3BUL}. FT HELIX 906 911 {ECO:0000244|PDB:1MSK}. FT HELIX 918 920 {ECO:0000244|PDB:3BUL}. FT STRAND 930 935 {ECO:0000244|PDB:1MSK}. FT HELIX 938 941 {ECO:0000244|PDB:1MSK}. FT HELIX 942 944 {ECO:0000244|PDB:1MSK}. FT HELIX 948 953 {ECO:0000244|PDB:1MSK}. FT HELIX 962 965 {ECO:0000244|PDB:1MSK}. FT TURN 967 969 {ECO:0000244|PDB:1MSK}. FT HELIX 970 990 {ECO:0000244|PDB:1MSK}. FT STRAND 996 1007 {ECO:0000244|PDB:1MSK}. FT STRAND 1010 1016 {ECO:0000244|PDB:1MSK}. FT STRAND 1022 1027 {ECO:0000244|PDB:1MSK}. FT STRAND 1036 1038 {ECO:0000244|PDB:1MSK}. FT HELIX 1043 1046 {ECO:0000244|PDB:1MSK}. FT HELIX 1050 1052 {ECO:0000244|PDB:1MSK}. FT STRAND 1057 1065 {ECO:0000244|PDB:1MSK}. FT HELIX 1069 1078 {ECO:0000244|PDB:1MSK}. FT HELIX 1082 1109 {ECO:0000244|PDB:1MSK}. FT HELIX 1122 1126 {ECO:0000244|PDB:1MSK}. FT STRAND 1130 1133 {ECO:0000244|PDB:1K7Y}. FT HELIX 1145 1147 {ECO:0000244|PDB:1MSK}. FT HELIX 1148 1154 {ECO:0000244|PDB:1MSK}. FT HELIX 1157 1161 {ECO:0000244|PDB:1MSK}. FT STRAND 1167 1169 {ECO:0000244|PDB:3IV9}. FT STRAND 1171 1182 {ECO:0000244|PDB:1MSK}. FT HELIX 1197 1207 {ECO:0000244|PDB:1MSK}. FT HELIX 1211 1218 {ECO:0000244|PDB:1MSK}. FT HELIX 1219 1221 {ECO:0000244|PDB:1MSK}. FT STRAND 1222 1224 {ECO:0000244|PDB:1MSK}. SQ SEQUENCE 1227 AA; 135997 MW; 91F0CAA1E9127D9A CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAD // ID METH_HUMAN Reviewed; 1265 AA. AC Q99707; A1L4N8; A9Z1W4; B7ZLW7; B9EGF7; Q99713; Q99723; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 2. DT 27-MAY-2015, entry version 158. DE RecName: Full=Methionine synthase; DE EC=2.1.1.13; DE AltName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase; DE AltName: Full=Vitamin-B12 dependent methionine synthase; DE Short=MS; GN Name=MTR; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS HMAG ILE-881 DEL RP AND ASP-920. RC TISSUE=Fibroblast; RX PubMed=8968737; DOI=10.1093/hmg/5.12.1867; RA Leclerc D., Campeau E., Goyette P., Adjalla C.E., Christensen B., RA Ross M., Eydoux P., Rosenblatt D.S., Rozen R., Gravel R.A.; RT "Human methionine synthase: cDNA cloning and identification of RT mutations in patients of the cblG complementation group of RT folate/cobalamin disorders."; RL Hum. Mol. Genet. 5:1867-1874(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Liver; RX PubMed=8968735; DOI=10.1093/hmg/5.12.1851; RA Li Y.N., Gulati S., Baker P.J., Brody L.C., Banerjee R., Kruger W.D.; RT "Cloning, mapping and RNA analysis of the human methionine synthase RT gene."; RL Hum. Mol. Genet. 5:1851-1858(1996). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS TYR-255 AND RP GLY-919. RC TISSUE=Fetal liver; RX PubMed=9013615; DOI=10.1074/jbc.272.6.3444; RA Chen L.H., Liu M.-L., Hwang H.-Y., Chen L.-S., Korenberg J., Shane B.; RT "Human methionine synthase. cDNA cloning, gene localization, and RT expression."; RL J. Biol. Chem. 272:3628-3634(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT RP GLY-919. RC TISSUE=Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [8] RP VARIANTS HMAG ILE-881 DEL AND LEU-1173, AND VARIANT LYS-61. RX PubMed=8968736; DOI=10.1093/hmg/5.12.1859; RA Gulati S., Baker P.J., Li Y.N., Fowler B., Kruger W.D., Brody L.C., RA Banerjee R.; RT "Defects in human methionine synthase in cblG patients."; RL Hum. Mol. Genet. 5:1859-1865(1996). RN [9] RP ASSOCIATION OF VARIANT GLY-919 WITH SUSCEPTIBILITY TO FS-NTD. RX PubMed=12375236; DOI=10.1086/344209; RA Doolin M.-T., Barbaux S., McDonnell M., Hoess K., Whitehead A.S., RA Mitchell L.E.; RT "Maternal genetic effects, exerted by genes involved in homocysteine RT remethylation, influence the risk of spina bifida."; RL Am. J. Hum. Genet. 71:1222-1226(2002). RN [10] RP NO ASSOCIATION OF VARIANT GLY-919 WITH SUSCEPTIBILITY TO FS-NTD. RX PubMed=15979034; DOI=10.1016/j.ymgme.2005.02.003; RA O'Leary V.B., Mills J.L., Pangilinan F., Kirke P.N., Cox C., RA Conley M., Weiler A., Peng K., Shane B., Scott J.M., RA Parle-McDermott A., Molloy A.M., Brody L.C.; RT "Analysis of methionine synthase reductase polymorphisms for neural RT tube defects risk association."; RL Mol. Genet. Metab. 85:220-227(2005). CC -!- FUNCTION: Catalyzes the transfer of a methyl group from methyl- CC cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and CC methionine. Subsequently, remethylates the cofactor using CC methyltetrahydrofolate (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + L-homocysteine = CC tetrahydrofolate + L-methionine. CC -!- COFACTOR: CC Name=methyl(III)cobalamin; Xref=ChEBI:CHEBI:28115; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (MetH route): step CC 1/1. CC -!- INTERACTION: CC Q9Y4U1:MMACHC; NbExp=3; IntAct=EBI-1045782, EBI-9775184; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q99707-1; Sequence=Displayed; CC Name=2; CC IsoId=Q99707-2; Sequence=VSP_057283; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at the highest CC levels in pancreas, heart, brain, skeletal muscle and placenta. CC Expressed at lower levels in lung, liver and kidney. CC -!- DOMAIN: Modular enzyme with four functionally distinct domains. CC The isolated Hcy-binding domain catalyzes methyl transfer from CC free methylcobalamin to homocysteine. The Hcy-binding domain in CC association with the pterin-binding domain catalyzes the CC methylation of cob(I)alamin by methyltetrahydrofolate and the CC methylation of homocysteine. The B12-binding domain binds the CC cofactor. The AdoMet activation domain binds S-adenosyl-L- CC methionine. Under aerobic conditions cob(I)alamin can be converted CC to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L- CC methionine and flavodoxin regenerates methylcobalamin (By CC similarity). {ECO:0000250}. CC -!- DISEASE: Homocystinuria-megaloblastic anemia, cblG complementation CC type (HMAG) [MIM:250940]: An autosomal recessive inborn error of CC metabolism resulting from defects in the cobalamin-dependent CC pathway that converts homocysteine to methionine. It causes CC delayed psychomotor development, megaloblastic anemia, CC homocystinuria, and hypomethioninemia. CC {ECO:0000269|PubMed:8968736, ECO:0000269|PubMed:8968737}. Note=The CC disease is caused by mutations affecting the gene represented in CC this entry. CC -!- DISEASE: Folate-sensitive neural tube defects (FS-NTD) CC [MIM:601634]: The most common NTDs are open spina bifida CC (myelomeningocele) and anencephaly. {ECO:0000269|PubMed:12375236}. CC Note=Disease susceptibility is associated with variations CC affecting the gene represented in this entry. CC -!- MISCELLANEOUS: L-homocysteine is bound via the zinc atom. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine CC synthase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 AdoMet activation domain. CC {ECO:0000255|PROSITE-ProRule:PRU00346}. CC -!- SIMILARITY: Contains 1 B12-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00666}. CC -!- SIMILARITY: Contains 1 B12-binding N-terminal domain. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC -!- SIMILARITY: Contains 1 pterin-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00334}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=5-methyltetrahydrofolate- CC homocysteine methyltransferase entry; CC URL="http://en.wikipedia.org/wiki/5-Methyltetrahydrofolate-homocysteine_methyltransferase"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U71285; AAC51188.1; -; mRNA. DR EMBL; U75743; AAB58906.1; -; mRNA. DR EMBL; U73338; AAB39704.1; -; mRNA. DR EMBL; AL359185; CAH73198.1; -; Genomic_DNA. DR EMBL; AL359259; CAH73198.1; JOINED; Genomic_DNA. DR EMBL; AL359259; CAH70983.1; -; Genomic_DNA. DR EMBL; AL359185; CAH70983.1; JOINED; Genomic_DNA. DR EMBL; CH471098; EAW70066.1; -; Genomic_DNA. DR EMBL; BC130616; AAI30617.1; -; mRNA. DR EMBL; BC136440; AAI36441.1; -; mRNA. DR EMBL; BC144095; AAI44096.1; -; mRNA. DR CCDS; CCDS1614.1; -. [Q99707-1] DR CCDS; CCDS73054.1; -. [Q99707-2] DR RefSeq; NP_000245.2; NM_000254.2. [Q99707-1] DR RefSeq; NP_001278868.1; NM_001291939.1. [Q99707-2] DR RefSeq; NP_001278869.1; NM_001291940.1. DR UniGene; Hs.498187; -. DR PDB; 2O2K; X-ray; 1.60 A; A/B=925-1265. DR PDB; 4CCZ; X-ray; 2.70 A; A=16-657. DR PDBsum; 2O2K; -. DR PDBsum; 4CCZ; -. DR ProteinModelPortal; Q99707; -. DR SMR; Q99707; 17-651, 926-1264. DR BioGrid; 110642; 20. DR DIP; DIP-40306N; -. DR IntAct; Q99707; 3. DR STRING; 9606.ENSP00000355536; -. DR BindingDB; Q99707; -. DR ChEMBL; CHEMBL2150844; -. DR DrugBank; DB00115; Cyanocobalamin. DR DrugBank; DB00200; Hydroxocobalamin. DR DrugBank; DB00134; L-Methionine. DR DrugBank; DB00116; Tetrahydrofolic acid. DR PhosphoSite; Q99707; -. DR BioMuta; MTR; -. DR DMDM; 2842762; -. DR MaxQB; Q99707; -. DR PaxDb; Q99707; -. DR PRIDE; Q99707; -. DR Ensembl; ENST00000366577; ENSP00000355536; ENSG00000116984. [Q99707-1] DR Ensembl; ENST00000535889; ENSP00000441845; ENSG00000116984. [Q99707-2] DR GeneID; 4548; -. DR KEGG; hsa:4548; -. DR UCSC; uc001hyi.4; human. [Q99707-1] DR UCSC; uc010pxx.2; human. DR CTD; 4548; -. DR GeneCards; GC01P236958; -. DR GeneReviews; MTR; -. DR HGNC; HGNC:7468; MTR. DR HPA; HPA044474; -. DR MIM; 156570; gene. DR MIM; 250940; phenotype. DR MIM; 601634; phenotype. DR MIM; 603174; phenotype. DR neXtProt; NX_Q99707; -. DR Orphanet; 2170; Methylcobalamin deficiency type cblG. DR PharmGKB; PA31272; -. DR eggNOG; COG1410; -. DR GeneTree; ENSGT00420000029824; -. DR HOGENOM; HOG000251409; -. DR HOVERGEN; HBG006347; -. DR InParanoid; Q99707; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG7TF786; -. DR PhylomeDB; Q99707; -. DR TreeFam; TF312829; -. DR BioCyc; MetaCyc:HS04076-MONOMER; -. DR Reactome; REACT_115639; Sulfur amino acid metabolism. DR Reactome; REACT_163862; Cobalamin (Cbl, vitamin B12) transport and metabolism. DR Reactome; REACT_169149; Defective MTR causes methylmalonic aciduria and homocystinuria type cblG. DR Reactome; REACT_169439; Defective MTRR causes methylmalonic aciduria and homocystinuria type cblE. DR Reactome; REACT_6946; Methylation. DR UniPathway; UPA00051; UER00081. DR ChiTaRS; MTR; human. DR EvolutionaryTrace; Q99707; -. DR GeneWiki; Methionine_synthase; -. DR GenomeRNAi; 4548; -. DR NextBio; 17533; -. DR PRO; PR:Q99707; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; Q99707; -. DR CleanEx; HS_MTR; -. DR ExpressionAtlas; Q99707; baseline and differential. DR Genevestigator; Q99707; -. DR GO; GO:0005737; C:cytoplasm; IDA:HPA. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IDA:CACAO. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome. DR GO; GO:0009235; P:cobalamin metabolic process; IMP:BHF-UCL. DR GO; GO:0009086; P:methionine biosynthetic process; IMP:BHF-UCL. DR GO; GO:0032259; P:methylation; TAS:Reactome. DR GO; GO:0007399; P:nervous system development; TAS:ProtInc. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR GO; GO:0000096; P:sulfur amino acid metabolic process; TAS:Reactome. DR GO; GO:0006766; P:vitamin metabolic process; TAS:Reactome. DR GO; GO:0006767; P:water-soluble vitamin metabolic process; TAS:Reactome. DR GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Amino-acid biosynthesis; KW Cobalamin; Cobalt; Complete proteome; Cytoplasm; Disease mutation; KW Metal-binding; Methionine biosynthesis; Methyltransferase; KW Polymorphism; Reference proteome; Repeat; S-adenosyl-L-methionine; KW Transferase; Zinc. FT CHAIN 1 1265 Methionine synthase. FT /FTId=PRO_0000204530. FT DOMAIN 19 338 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT DOMAIN 371 632 Pterin-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00334}. FT DOMAIN 662 759 B12-binding N-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00666}. FT DOMAIN 772 907 B12-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00666}. FT DOMAIN 923 1265 AdoMet activation. {ECO:0000255|PROSITE- FT ProRule:PRU00346}. FT REGION 860 861 Cobalamin-binding. {ECO:0000250}. FT REGION 1227 1228 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT METAL 260 260 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 323 323 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 324 324 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 785 785 Cobalt (cobalamin axial ligand). FT {ECO:0000250}. FT BINDING 830 830 Cobalamin. {ECO:0000250}. FT BINDING 974 974 S-adenosyl-L-methionine. {ECO:0000250}. FT BINDING 1172 1172 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000250}. FT BINDING 1176 1176 Cobalamin; via carbonyl oxygen. FT {ECO:0000250}. FT VAR_SEQ 682 732 Missing (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_057283. FT VARIANT 52 52 R -> Q (in dbSNP:rs12749581). FT /FTId=VAR_050033. FT VARIANT 61 61 R -> K. {ECO:0000269|PubMed:8968736}. FT /FTId=VAR_004326. FT VARIANT 255 255 C -> Y. {ECO:0000269|PubMed:9013615}. FT /FTId=VAR_004327. FT VARIANT 314 314 D -> N (in dbSNP:rs2229274). FT /FTId=VAR_061338. FT VARIANT 881 881 Missing (in HMAG). FT {ECO:0000269|PubMed:8968736, FT ECO:0000269|PubMed:8968737}. FT /FTId=VAR_004328. FT VARIANT 919 919 D -> G (may be associated with FT susceptibility to FS-NTD; FT dbSNP:rs1805087). FT {ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:9013615}. FT /FTId=VAR_004329. FT VARIANT 920 920 H -> D (in HMAG; dbSNP:rs28933097). FT {ECO:0000269|PubMed:8968737}. FT /FTId=VAR_004330. FT VARIANT 1173 1173 P -> L (in HMAG). FT {ECO:0000269|PubMed:8968736}. FT /FTId=VAR_004331. FT HELIX 18 28 {ECO:0000244|PDB:4CCZ}. FT HELIX 37 44 {ECO:0000244|PDB:4CCZ}. FT HELIX 49 51 {ECO:0000244|PDB:4CCZ}. FT HELIX 67 69 {ECO:0000244|PDB:4CCZ}. FT HELIX 70 73 {ECO:0000244|PDB:4CCZ}. FT HELIX 75 87 {ECO:0000244|PDB:4CCZ}. FT STRAND 92 94 {ECO:0000244|PDB:4CCZ}. FT HELIX 102 105 {ECO:0000244|PDB:4CCZ}. FT HELIX 106 108 {ECO:0000244|PDB:4CCZ}. FT HELIX 111 113 {ECO:0000244|PDB:4CCZ}. FT HELIX 114 136 {ECO:0000244|PDB:4CCZ}. FT STRAND 141 146 {ECO:0000244|PDB:4CCZ}. FT STRAND 153 155 {ECO:0000244|PDB:4CCZ}. FT STRAND 159 161 {ECO:0000244|PDB:4CCZ}. FT HELIX 169 185 {ECO:0000244|PDB:4CCZ}. FT STRAND 189 198 {ECO:0000244|PDB:4CCZ}. FT HELIX 199 213 {ECO:0000244|PDB:4CCZ}. FT TURN 214 216 {ECO:0000244|PDB:4CCZ}. FT STRAND 222 226 {ECO:0000244|PDB:4CCZ}. FT HELIX 241 248 {ECO:0000244|PDB:4CCZ}. FT HELIX 249 251 {ECO:0000244|PDB:4CCZ}. FT STRAND 254 263 {ECO:0000244|PDB:4CCZ}. FT TURN 264 267 {ECO:0000244|PDB:4CCZ}. FT HELIX 268 275 {ECO:0000244|PDB:4CCZ}. FT STRAND 279 287 {ECO:0000244|PDB:4CCZ}. FT STRAND 318 320 {ECO:0000244|PDB:4CCZ}. FT HELIX 328 338 {ECO:0000244|PDB:4CCZ}. FT TURN 348 353 {ECO:0000244|PDB:4CCZ}. FT STRAND 355 365 {ECO:0000244|PDB:4CCZ}. FT STRAND 372 375 {ECO:0000244|PDB:4CCZ}. FT TURN 380 382 {ECO:0000244|PDB:4CCZ}. FT HELIX 384 391 {ECO:0000244|PDB:4CCZ}. FT HELIX 395 407 {ECO:0000244|PDB:4CCZ}. FT STRAND 411 416 {ECO:0000244|PDB:4CCZ}. FT HELIX 424 437 {ECO:0000244|PDB:4CCZ}. FT HELIX 439 442 {ECO:0000244|PDB:4CCZ}. FT STRAND 446 449 {ECO:0000244|PDB:4CCZ}. FT HELIX 453 462 {ECO:0000244|PDB:4CCZ}. FT STRAND 468 472 {ECO:0000244|PDB:4CCZ}. FT HELIX 478 491 {ECO:0000244|PDB:4CCZ}. FT STRAND 494 501 {ECO:0000244|PDB:4CCZ}. FT HELIX 509 527 {ECO:0000244|PDB:4CCZ}. FT HELIX 531 533 {ECO:0000244|PDB:4CCZ}. FT STRAND 534 537 {ECO:0000244|PDB:4CCZ}. FT HELIX 548 552 {ECO:0000244|PDB:4CCZ}. FT HELIX 553 567 {ECO:0000244|PDB:4CCZ}. FT HELIX 577 584 {ECO:0000244|PDB:4CCZ}. FT HELIX 588 605 {ECO:0000244|PDB:4CCZ}. FT STRAND 609 612 {ECO:0000244|PDB:4CCZ}. FT HELIX 620 622 {ECO:0000244|PDB:4CCZ}. FT HELIX 625 635 {ECO:0000244|PDB:4CCZ}. FT HELIX 642 648 {ECO:0000244|PDB:4CCZ}. FT HELIX 932 937 {ECO:0000244|PDB:2O2K}. FT HELIX 944 946 {ECO:0000244|PDB:2O2K}. FT STRAND 956 962 {ECO:0000244|PDB:2O2K}. FT HELIX 966 970 {ECO:0000244|PDB:2O2K}. FT HELIX 976 987 {ECO:0000244|PDB:2O2K}. FT HELIX 995 998 {ECO:0000244|PDB:2O2K}. FT HELIX 1005 1022 {ECO:0000244|PDB:2O2K}. FT STRAND 1026 1040 {ECO:0000244|PDB:2O2K}. FT STRAND 1043 1046 {ECO:0000244|PDB:2O2K}. FT HELIX 1053 1055 {ECO:0000244|PDB:2O2K}. FT STRAND 1059 1063 {ECO:0000244|PDB:2O2K}. FT HELIX 1082 1085 {ECO:0000244|PDB:2O2K}. FT HELIX 1089 1091 {ECO:0000244|PDB:2O2K}. FT STRAND 1095 1106 {ECO:0000244|PDB:2O2K}. FT HELIX 1107 1116 {ECO:0000244|PDB:2O2K}. FT HELIX 1120 1147 {ECO:0000244|PDB:2O2K}. FT TURN 1152 1155 {ECO:0000244|PDB:2O2K}. FT HELIX 1160 1164 {ECO:0000244|PDB:2O2K}. FT STRAND 1168 1171 {ECO:0000244|PDB:2O2K}. FT HELIX 1185 1192 {ECO:0000244|PDB:2O2K}. FT HELIX 1195 1199 {ECO:0000244|PDB:2O2K}. FT STRAND 1209 1220 {ECO:0000244|PDB:2O2K}. FT HELIX 1235 1245 {ECO:0000244|PDB:2O2K}. FT HELIX 1249 1255 {ECO:0000244|PDB:2O2K}. FT HELIX 1257 1259 {ECO:0000244|PDB:2O2K}. SQ SEQUENCE 1265 AA; 140527 MW; B04C26BCBE9A57C2 CRC64; MSPALQDLSQ PEGLKKTLRD EINAILQKRI MVLDGGMGTM IQREKLNEEH FRGQEFKDHA RPLKGNNDIL SITQPDVIYQ IHKEYLLAGA DIIETNTFSS TSIAQADYGL EHLAYRMNMC SAGVARKAAE EVTLQTGIKR FVAGALGPTN KTLSVSPSVE RPDYRNITFD ELVEAYQEQA KGLLDGGVDI LLIETIFDTA NAKAALFALQ NLFEEKYAPR PIFISGTIVD KSGRTLSGQT GEGFVISVSH GEPLCIGLNC ALGAAEMRPF IEIIGKCTTA YVLCYPNAGL PNTFGDYDET PSMMAKHLKD FAMDGLVNIV GGCCGSTPDH IREIAEAVKN CKPRVPPATA FEGHMLLSGL EPFRIGPYTN FVNIGERCNV AGSRKFAKLI MAGNYEEALC VAKVQVEMGA QVLDVNMDDG MLDGPSAMTR FCNLIASEPD IAKVPLCIDS SNFAVIEAGL KCCQGKCIVN SISLKEGEDD FLEKARKIKK YGAAMVVMAF DEEGQATETD TKIRVCTRAY HLLVKKLGFN PNDIIFDPNI LTIGTGMEEH NLYAINFIHA TKVIKETLPG ARISGGLSNL SFSFRGMEAI REAMHGVFLY HAIKSGMDMG IVNAGNLPVY DDIHKELLQL CEDLIWNKDP EATEKLLRYA QTQGTGGKKV IQTDEWRNGP VEERLEYALV KGIEKHIIED TEEARLNQKK YPRPLNIIEG PLMNGMKIVG DLFGAGKMFL PQVIKSARVM KKAVGHLIPF MEKEREETRV LNGTVEEEDP YQGTIVLATV KGDVHDIGKN IVGVVLGCNN FRVIDLGVMT PCDKILKAAL DHKADIIGLS GLITPSLDEM IFVAKEMERL AIRIPLLIGG ATTSKTHTAV KIAPRYSAPV IHVLDASKSV VVCSQLLDEN LKDEYFEEIM EEYEDIRQDH YESLKERRYL PLSQARKSGF QMDWLSEPHP VKPTFIGTQV FEDYDLQKLV DYIDWKPFFD VWQLRGKYPN RGFPKIFNDK TVGGEARKVY DDAHNMLNTL ISQKKLRARG VVGFWPAQSI QDDIHLYAEA AVPQAAEPIA TFYGLRQQAE KDSASTEPYY CLSDFIAPLH SGIRDYLGLF AVACFGVEEL SKAYEDDGDD YSSIMVKALG DRLAEAFAEE LHERVRRELW AYCGSEQLDV ADLRRLRYKG IRPAPGYPSQ PDHTEKLTMW RLADIEQSTG IRLTESLAMA PASAVSGLYF SNLKSKYFAV GKISKDQVED YALRKNISVA EVEKWLGPIL GYDTD // ID METH_MOUSE Reviewed; 1253 AA. AC A6H5Y3; Q3UQP2; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 24-JUL-2007, sequence version 1. DT 27-MAY-2015, entry version 80. DE RecName: Full=Methionine synthase; DE EC=2.1.1.13; DE AltName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase; DE AltName: Full=Vitamin-B12 dependent methionine synthase; DE Short=MS; GN Name=Mtr; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-738. RC STRAIN=C57BL/6J; TISSUE=Heart; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). CC -!- FUNCTION: Catalyzes the transfer of a methyl group from methyl- CC cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and CC methionine. Subsequently, remethylates the cofactor using CC methyltetrahydrofolate (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + L-homocysteine = CC tetrahydrofolate + L-methionine. CC -!- COFACTOR: CC Name=methyl(III)cobalamin; Xref=ChEBI:CHEBI:28115; CC Evidence={ECO:0000250}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (MetH route): step CC 1/1. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- DOMAIN: Modular enzyme with four functionally distinct domains. CC The isolated Hcy-binding domain catalyzes methyl transfer from CC free methylcobalamin to homocysteine. The Hcy-binding domain in CC association with the pterin-binding domain catalyzes the CC methylation of cob(I)alamin by methyltetrahydrofolate and the CC methylation of homocysteine. The B12-binding domain binds the CC cofactor. The AdoMet activation domain binds S-adenosyl-L- CC methionine. Under aerobic conditions cob(I)alamin can be converted CC to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L- CC methionine and flavodoxin regenerates methylcobalamin (By CC similarity). {ECO:0000250}. CC -!- MISCELLANEOUS: L-homocysteine is bound via the zinc atom. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine CC synthase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 AdoMet activation domain. CC {ECO:0000255|PROSITE-ProRule:PRU00346}. CC -!- SIMILARITY: Contains 1 B12-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00666}. CC -!- SIMILARITY: Contains 1 B12-binding N-terminal domain. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC -!- SIMILARITY: Contains 1 pterin-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00334}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC145683; AAI45684.1; -; mRNA. DR EMBL; BC145685; AAI45686.1; -; mRNA. DR EMBL; AK142258; BAE24997.1; -; mRNA. DR CCDS; CCDS36591.1; -. DR RefSeq; NP_001074597.1; NM_001081128.3. DR UniGene; Mm.40335; -. DR ProteinModelPortal; A6H5Y3; -. DR SMR; A6H5Y3; 4-639, 914-1252. DR ChEMBL; CHEMBL3188; -. DR PhosphoSite; A6H5Y3; -. DR MaxQB; A6H5Y3; -. DR PaxDb; A6H5Y3; -. DR PRIDE; A6H5Y3; -. DR Ensembl; ENSMUST00000099856; ENSMUSP00000097442; ENSMUSG00000021311. DR GeneID; 238505; -. DR KEGG; mmu:238505; -. DR UCSC; uc007plh.2; mouse. DR CTD; 4548; -. DR MGI; MGI:894292; Mtr. DR eggNOG; COG1410; -. DR GeneTree; ENSGT00420000029824; -. DR HOGENOM; HOG000251409; -. DR HOVERGEN; HBG006347; -. DR InParanoid; A6H5Y3; -. DR KO; K00548; -. DR OMA; QPFFNAW; -. DR OrthoDB; EOG7TF786; -. DR PhylomeDB; A6H5Y3; -. DR TreeFam; TF312829; -. DR Reactome; REACT_277860; Sulfur amino acid metabolism. DR Reactome; REACT_283123; Methylation. DR Reactome; REACT_294704; Cobalamin (Cbl, vitamin B12) transport and metabolism. DR UniPathway; UPA00051; UER00081. DR NextBio; 383806; -. DR PRO; PR:A6H5Y3; -. DR Proteomes; UP000000589; Chromosome 13. DR Bgee; A6H5Y3; -. DR Genevestigator; A6H5Y3; -. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IMP:MGI. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009235; P:cobalamin metabolic process; ISO:MGI. DR GO; GO:0009086; P:methionine biosynthetic process; IMP:MGI. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 2: Evidence at transcript level; KW Amino-acid biosynthesis; Cobalamin; Cobalt; Complete proteome; KW Cytoplasm; Metal-binding; Methionine biosynthesis; Methyltransferase; KW Reference proteome; Repeat; S-adenosyl-L-methionine; Transferase; KW Zinc. FT CHAIN 1 1253 Methionine synthase. FT /FTId=PRO_0000312901. FT DOMAIN 6 326 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT DOMAIN 359 620 Pterin-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00334}. FT DOMAIN 650 747 B12-binding N-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00666}. FT DOMAIN 760 895 B12-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00666}. FT DOMAIN 911 1253 AdoMet activation. {ECO:0000255|PROSITE- FT ProRule:PRU00346}. FT REGION 848 849 Cobalamin-binding. {ECO:0000250}. FT REGION 1215 1216 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT METAL 248 248 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 311 311 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 312 312 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 773 773 Cobalt (cobalamin axial ligand). FT {ECO:0000250}. FT BINDING 818 818 Cobalamin. {ECO:0000250}. FT BINDING 962 962 S-adenosyl-L-methionine. {ECO:0000250}. FT BINDING 1160 1160 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000250}. FT BINDING 1164 1164 Cobalamin; via carbonyl oxygen. FT {ECO:0000250}. FT CONFLICT 343 343 M -> L (in Ref. 2; BAE24997). FT {ECO:0000305}. SQ SEQUENCE 1253 AA; 139069 MW; 5507CAD9F9522537 CRC64; MKKTLQDEIE AILRKRIMVL DGGMGTMIQR YKLSEEHFQG QEFKDHSRPL KGNNDILSIT QPDIIYQIHK EYLLAGADII ETNTFSSTSI AQADYGLEHL AYRMNKCSAD VARKAAEEIT LQTGVKRFVA GALGPTNKTL SVSPSVERPD YRNITFDELV DAYQEQAKGL LDGRVDILLI ETIFDTANAK AALFAIQNLF EENYAPPRPI FISGTIVDKS GRTLSGQTGE AFVTSVSHSD PLCIGLNCSL GAAEMRPFIE TIGKCTTAYV LCYPNAGLPN TFGDYDETPS TMATHLKDFA VDGLVNIVGG CCGSTPDHIR EIAEAVKKCK PRVPPASVFE GHMLLSGLEP FRIGPYTNFV NIGERCNVAG SRKFAKLIMA GNYEEALSIA KAQVEMGAQV LDINMDDGML DGPSAMTRFC NSIASEPDIA KVPLCIDSSN FAVIEAGLKC CQGKCIVNSI SLKEGEGDFL EKARKIKKFG AAVVVMAFDE EGQATETDVK VNVCTRAYHL LVDKVGFNPN DIIFDPNILT IGTGMEEHNL YAINFIHATR VIKETLPGVR ISGGLSNLSF SFRGMEAIRE AMHGVFLYHA IKFGMDMGIV NAGNLPVYDA IHKDLLQLCE DLIWNKDSEA TEKLLRYAQT HGTGGKKVIQ TDEWRNGSIE ERLEYALVKG IEKHIVEDTE EARLNGEKYP RPLNIIEGPL MNGMKVVGDL FGAGKMFLPQ VIKSARVMKK AVGHLIPFME KEREEARLIN GSVEEEDPYQ GTIVLATVKG DVHDIGKNIV GVVLACNNFR VIDLGVMTPC DKILQAALDH KADIIGLSGL ITPSLDEMIF VAKEMERLAI KIPLLIGGAT TSRTHTAVKI APRYSAPVIH VLDASKSVVV CSQLLDENLR DDYFEEILEE YEDIRQDHYE SLKERKYVPL SQARKHGFHI DWLSEPHPVK PTFIGTQVFE DYNLQKLVDY IDWKPFFDVW QLRGKYPNRG FPKIFNDKAV GEEARKVYND AQNMLNILIS QKKLQARGVV GFWPAQSVQD DIHLYAEGVV PQAAEPIATF YGLRQQAEKD SSSTDPYHCL SDFIAPLHSG VCDYLGLFAV ACFGVEELSK TYEDDGDDYS SIMVKALGDR LAEAFAEELH ERVRRELWAY SRSEQLGVPD LRRLRYEGIR PAPGYPSQPD HTEKLTMWRL ASIEQATGIR LTESLAMAPA SAVSGLYFSN VKAKYFAVGK ISKDQTEDYA LRKNMPVAEV EKWLGPILGY DTD // ID METH_MYCLE Reviewed; 1206 AA. AC Q49775; Q9CC37; Q9S378; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 27-APR-2001, sequence version 3. DT 27-MAY-2015, entry version 114. DE RecName: Full=Methionine synthase; DE EC=2.1.1.13; DE AltName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase; DE AltName: Full=Methionine synthase, vitamin-B12 dependent; DE Short=MS; GN Name=metH; OrderedLocusNames=ML1307; GN ORFNames=B2126_C1_157, MLCB2533.04; OS Mycobacterium leprae (strain TN). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=272631; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Smith D.R., Robison K.; RL Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases. RN [2] 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: Catalyzes the transfer of a methyl group from methyl- CC cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and CC methionine. Subsequently, remethylates the cofactor using CC methyltetrahydrofolate (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + L-homocysteine = CC tetrahydrofolate + L-methionine. CC -!- COFACTOR: CC Name=methyl(III)cobalamin; Xref=ChEBI:CHEBI:28115; CC Evidence={ECO:0000250}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (MetH route): step CC 1/1. CC -!- DOMAIN: Modular enzyme with four functionally distinct domains. CC The isolated Hcy-binding domain catalyzes methyl transfer from CC free methylcobalamin to homocysteine. The Hcy-binding domain in CC association with the pterin-binding domain catalyzes the CC methylation of cob(I)alamin by methyltetrahydrofolate and the CC methylation of homocysteine. The B12-binding domain binds the CC cofactor. The AdoMet activation domain binds S-adenosyl-L- CC methionine. Under aerobic conditions cob(I)alamin can be converted CC to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L- CC methionine and flavodoxin regenerates methylcobalamin (By CC similarity). {ECO:0000250}. CC -!- MISCELLANEOUS: L-homocysteine is bound via the zinc atom. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine CC synthase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 AdoMet activation domain. CC {ECO:0000255|PROSITE-ProRule:PRU00346}. CC -!- SIMILARITY: Contains 1 B12-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00666}. CC -!- SIMILARITY: Contains 1 B12-binding N-terminal domain. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC -!- SIMILARITY: Contains 1 pterin-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00334}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA17182.1; Type=Frameshift; Positions=873; Evidence={ECO:0000305}; CC Sequence=CAA22918.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00017; AAA17182.1; ALT_FRAME; Genomic_DNA. DR EMBL; AL035310; CAA22918.1; ALT_INIT; Genomic_DNA. DR EMBL; AL583921; CAC31688.1; -; Genomic_DNA. DR PIR; E87072; E87072. DR PIR; S72842; S72842. DR RefSeq; NP_301940.1; NC_002677.1. DR RefSeq; WP_010908261.1; NC_002677.1. DR ProteinModelPortal; Q49775; -. DR STRING; 272631.ML1307; -. DR EnsemblBacteria; CAC31688; CAC31688; CAC31688. DR GeneID; 910429; -. DR KEGG; mle:ML1307; -. DR PATRIC; 18054948; VBIMycLep78757_2411. DR Leproma; ML1307; -. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR UniPathway; UPA00051; UER00081. DR Proteomes; UP000000806; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Cobalamin; Cobalt; Complete proteome; KW Metal-binding; Methionine biosynthesis; Methyltransferase; KW Reference proteome; Repeat; S-adenosyl-L-methionine; Transferase; KW Zinc. FT CHAIN 1 1206 Methionine synthase. FT /FTId=PRO_0000204533. FT DOMAIN 1 314 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT DOMAIN 350 609 Pterin-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00334}. FT DOMAIN 642 735 B12-binding N-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00666}. FT DOMAIN 740 877 B12-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00666}. FT DOMAIN 907 1206 AdoMet activation. {ECO:0000255|PROSITE- FT ProRule:PRU00346}. FT REGION 830 831 Cobalamin-binding. {ECO:0000250}. FT REGION 1203 1204 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT METAL 233 233 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 299 299 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 300 300 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 753 753 Cobalt (cobalamin axial ligand). FT {ECO:0000250}. FT BINDING 798 798 Cobalamin. {ECO:0000250}. FT BINDING 954 954 S-adenosyl-L-methionine. {ECO:0000250}. FT BINDING 1149 1149 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000250}. FT BINDING 1153 1153 Cobalamin; via carbonyl oxygen. FT {ECO:0000250}. SQ SEQUENCE 1206 AA; 132392 MW; 7786CE5307D7CA86 CRC64; MRVTAANQHQ YDTDLLETLA QRVMVGDGAM GTQLQDAELT LDDFRGLEGC NEILNETRPD VLETIHRRYF EAGADLVETN TFGCNLSNLG DYDIADKIRD LSQRGTVIAR RVADELTTPD HKRYVLGSMG PGTKLPTLGH TEYRVVRDAY TESALGMLDG GADAVLVETC QDLLQLKAAV LGSRRAMTQA GRHIPVFVHV TVETTGTMLL GSEIGAALAA VEPLGVDMIG LNCATGPAEM SEHLRHLSKH ARIPVSVMPN AGLPVLGAKG AEYPLQPDEL AEALAGFIAE FGLSLVGGCC GTTPDHIREV AAAVARCNDG TVPRGERHVT YEPSVSSLYT AIPFAQKPSV LMIGERTNAN GSKVFREAMI AEDYQKCLDI AKDQTRGGAH LLDLCVDYVG RNGVADMKAL AGRLATVSTL PIMLDSTEIP VLQAGLEHLG GRCVINSVNY EDGDGPESRF VKTMELVAEH GAAVVALTID EQGQARTVEK KVEVAERLIN DITSNWGVDK SAILIDCLTF TIATGQEESR KDGIETIDAI RELKKRHPAV QTTLGLSNIS FGLNPSARQV LNSVFLHECQ EAGLDSAIVH ASKILPINRI PEEQRQAALD LVYDRRREGY DPLQKLMWLF KGVSSPSSKE TREAELAKLP LFDRLAQRIV DGERNGLDVD LDEAMTQKPP LAIINENLLD GMKTVGELFG SGQMQLPFVL QSAEVMKAAV AYLEPHMEKS DCDFGKGLAK GRIVLATVKG DVHDIGKNLV DIILSNNGYE VVNLGIKQPI TNILEVAEDK SADVVGMSGL LVKSTVIMKE NLEEMNTRGV AEKFPVLLGG AALTRSYVEN DLAEVYEGEV HYARDAFEGL KLMDTIMSAK RGEALAPGSP ESLAAEADRN KETERKARHE RSKRIAVQRK AAEEPVEVPE RSDVPSDVEV PAPPFWGSRI IKGLAVADYT GFLDERALFL GQWGLRGVRG GAGPSYEDLV QTEGRPRLRY WLDRLSTYGV LAYAAVVYGY FPAVSEDNDI VVLAEPRPDA EQRYRFTFPR QQRGRFLCIA DFIRSRDLAT ERSEVDVLPF QLVTMGQPIA DFVGELFVSN SYRDYLEVHG IGVQLTEALA EYWHRRIREE LKFSGNRTMS ADDPEAVEDY FKLGYRGARF AFGYGACPDL EDRIKMMELL QPERIGVTIS EELQLHPEQS TDAFVLHHPA AKYFNV // ID METH_MYCTU Reviewed; 1192 AA. AC O33259; L0T8Q3; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 27-MAY-2015, entry version 120. DE RecName: Full=Methionine synthase; DE EC=2.1.1.13; DE AltName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase; DE AltName: Full=Methionine synthase, vitamin-B12 dependent; DE Short=MS; GN Name=metH; OrderedLocusNames=Rv2124c; ORFNames=MTCY261.20c; 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 IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS]. RX PubMed=19099550; DOI=10.1186/1752-0509-2-109; RA Raman K., Yeturu K., Chandra N.; RT "targetTB: a target identification pipeline for Mycobacterium RT tuberculosis through an interactome, reactome and genome-scale RT structural analysis."; RL BMC Syst. Biol. 2:109-109(2008). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=ATCC 25618 / H37Rv; RX PubMed=21969609; DOI=10.1074/mcp.M111.011627; RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., RA Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H., RA Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., RA Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S., RA Dash D., Pandey A.; RT "Proteogenomic analysis of Mycobacterium tuberculosis by high RT resolution mass spectrometry."; RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011). CC -!- FUNCTION: Catalyzes the transfer of a methyl group from methyl- CC cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and CC methionine. Subsequently, remethylates the cofactor using CC methyltetrahydrofolate (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + L-homocysteine = CC tetrahydrofolate + L-methionine. CC -!- COFACTOR: CC Name=methyl(III)cobalamin; Xref=ChEBI:CHEBI:28115; CC Evidence={ECO:0000250}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (MetH route): step CC 1/1. CC -!- DOMAIN: Modular enzyme with four functionally distinct domains. CC The isolated Hcy-binding domain catalyzes methyl transfer from CC free methylcobalamin to homocysteine. The Hcy-binding domain in CC association with the pterin-binding domain catalyzes the CC methylation of cob(I)alamin by methyltetrahydrofolate and the CC methylation of homocysteine. The B12-binding domain binds the CC cofactor. The AdoMet activation domain binds S-adenosyl-L- CC methionine. Under aerobic conditions cob(I)alamin can be converted CC to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L- CC methionine and flavodoxin regenerates methylcobalamin (By CC similarity). {ECO:0000250}. CC -!- MISCELLANEOUS: L-homocysteine is bound via the zinc atom. CC {ECO:0000250}. CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target. CC -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine CC synthase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 AdoMet activation domain. CC {ECO:0000255|PROSITE-ProRule:PRU00346}. CC -!- SIMILARITY: Contains 1 B12-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00666}. CC -!- SIMILARITY: Contains 1 B12-binding N-terminal domain. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC -!- SIMILARITY: Contains 1 pterin-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00334}. CC ----------------------------------------------------------------------- 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; CCP44899.1; -; Genomic_DNA. DR PIR; G70513; G70513. DR RefSeq; NP_216640.1; NC_000962.3. DR RefSeq; WP_003900472.1; NZ_KK339370.1. DR RefSeq; YP_006515540.1; NC_018143.2. DR ProteinModelPortal; O33259; -. DR SMR; O33259; 16-621, 637-1192. DR STRING; 83332.Rv2124c; -. DR PRIDE; O33259; -. DR EnsemblBacteria; CCP44899; CCP44899; Rv2124c. DR GeneID; 888711; -. DR KEGG; mtu:Rv2124c; -. DR KEGG; mtv:RVBD_2124c; -. DR PATRIC; 18153284; VBIMycTub87468_2371. DR TubercuList; Rv2124c; -. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR InParanoid; O33259; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR PhylomeDB; O33259; -. DR BioCyc; MTBRV:RV2124C-MONOMER; -. DR UniPathway; UPA00051; UER00081. DR Proteomes; UP000001584; Chromosome. DR GO; GO:0005618; C:cell wall; IDA:MTBBASE. DR GO; GO:0005829; C:cytosol; IDA:MTBBASE. DR GO; GO:0005886; C:plasma membrane; IDA:MTBBASE. DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 1: Evidence at protein level; KW Amino-acid biosynthesis; Cobalamin; Cobalt; Complete proteome; KW Metal-binding; Methionine biosynthesis; Methyltransferase; KW Reference proteome; Repeat; S-adenosyl-L-methionine; Transferase; KW Zinc. FT CHAIN 1 1192 Methionine synthase. FT /FTId=PRO_0000204534. FT DOMAIN 1 312 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT DOMAIN 343 601 Pterin-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00334}. FT DOMAIN 635 728 B12-binding N-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00666}. FT DOMAIN 729 866 B12-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00666}. FT DOMAIN 893 1192 AdoMet activation. {ECO:0000255|PROSITE- FT ProRule:PRU00346}. FT REGION 819 820 Cobalamin-binding. {ECO:0000250}. FT REGION 1189 1190 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT METAL 231 231 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 297 297 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 298 298 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 742 742 Cobalt (cobalamin axial ligand). FT {ECO:0000250}. FT BINDING 787 787 Cobalamin. {ECO:0000250}. FT BINDING 940 940 S-adenosyl-L-methionine. {ECO:0000250}. FT BINDING 1135 1135 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000250}. FT BINDING 1139 1139 Cobalamin; via carbonyl oxygen. FT {ECO:0000250}. SQ SEQUENCE 1192 AA; 130323 MW; 820450DCE77BE15B CRC64; MTAADKHLYD TDLLDVLSQR VMVGDGAMGT QLQAADLTLD DFRGLEGCNE ILNETRPDVL ETIHRNYFEA GADAVETNTF GCNLSNLGDY DIADRIRDLS QKGTAIARRV ADELGSPDRK RYVLGSMGPG TKLPTLGHTE YAVIRDAYTE AALGMLDGGA DAILVETCQD LLQLKAAVLG SRRAMTRAGR HIPVFAHVTV ETTGTMLLGS EIGAALTAVE PLGVDMIGLN CATGPAEMSE HLRHLSRHAR IPVSVMPNAG LPVLGAKGAE YPLLPDELAE ALAGFIAEFG LSLVGGCCGT TPAHIREVAA AVANIKRPER QVSYEPSVSS LYTAIPFAQD ASVLVIGERT NANGSKGFRE AMIAEDYQKC LDIAKDQTRD GAHLLDLCVD YVGRDGVADM KALASRLATS STLPIMLDST ETAVLQAGLE HLGGRCAINS VNYEDGDGPE SRFAKTMALV AEHGAAVVAL TIDEEGQART AQKKVEIAER LINDITGNWG VDESSILIDT LTFTIATGQE ESRRDGIETI EAIRELKKRH PDVQTTLGLS NISFGLNPAA RQVLNSVFLH ECQEAGLDSA IVHASKILPM NRIPEEQRNV ALDLVYDRRR EDYDPLQELM RLFEGVSAAS SKEDRLAELA GLPLFERLAQ RIVDGERNGL DADLDEAMTQ KPPLQIINEH LLAGMKTVGE LFGSGQMQLP FVLQSAEVMK AAVAYLEPHM ERSDDDSGKG RIVLATVKGD VHDIGKNLVD IILSNNGYEV VNIGIKQPIA TILEVAEDKS ADVVGMSGLL VKSTVVMKEN LEEMNTRGVA EKFPVLLGGA ALTRSYVEND LAEIYQGEVH YARDAFEGLK LMDTIMSAKR GEAPDENSPE AIKAREKEAE RKARHQRSKR IAAQRKAAEE PVEVPERSDV AADIEVPAPP FWGSRIVKGL AVADYTGLLD ERALFLGQWG LRGQRGGEGP SYEDLVETEG RPRLRYWLDR LSTDGILAHA AVVYGYFPAV SEGNDIVVLT EPKPDAPVRY RFHFPRQQRG RFLCIADFIR SRELAAERGE VDVLPFQLVT MGQPIADFAN ELFASNAYRD YLEVHGIGVQ LTEALAEYWH RRIREELKFS GDRAMAAEDP EAKEDYFKLG YRGARFAFGY GACPDLEDRA KMMALLEPER IGVTLSEELQ LHPEQSTDAF VLHHPEAKYF NV // ID METH_PSEAE Reviewed; 1234 AA. AC Q9I2Q2; DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAY-2015, entry version 92. DE RecName: Full=Methionine synthase; DE EC=2.1.1.13; DE AltName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase; DE AltName: Full=Methionine synthase, vitamin-B12 dependent; DE Short=MS; GN Name=metH; OrderedLocusNames=PA1843; 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: Catalyzes the transfer of a methyl group from methyl- CC cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and CC methionine. Subsequently, remethylates the cofactor using CC methyltetrahydrofolate (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + L-homocysteine = CC tetrahydrofolate + L-methionine. CC -!- COFACTOR: CC Name=methyl(III)cobalamin; Xref=ChEBI:CHEBI:28115; CC Evidence={ECO:0000250}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (MetH route): step CC 1/1. CC -!- DOMAIN: Modular enzyme with four functionally distinct domains. CC The isolated Hcy-binding domain catalyzes methyl transfer from CC free methylcobalamin to homocysteine. The Hcy-binding domain in CC association with the pterin-binding domain catalyzes the CC methylation of cob(I)alamin by methyltetrahydrofolate and the CC methylation of homocysteine. The B12-binding domain binds the CC cofactor. The AdoMet activation domain binds S-adenosyl-L- CC methionine. Under aerobic conditions cob(I)alamin can be converted CC to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L- CC methionine and flavodoxin regenerates methylcobalamin (By CC similarity). {ECO:0000250}. CC -!- MISCELLANEOUS: L-homocysteine is bound via the zinc atom. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine CC synthase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 AdoMet activation domain. CC {ECO:0000255|PROSITE-ProRule:PRU00346}. CC -!- SIMILARITY: Contains 1 B12-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00666}. CC -!- SIMILARITY: Contains 1 B12-binding N-terminal domain. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC -!- SIMILARITY: Contains 1 pterin-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00334}. CC ----------------------------------------------------------------------- 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; AAG05232.1; -; Genomic_DNA. DR PIR; E83415; E83415. DR RefSeq; NP_250534.1; NC_002516.2. DR RefSeq; WP_003113602.1; NC_002516.2. DR ProteinModelPortal; Q9I2Q2; -. DR SMR; Q9I2Q2; 19-646, 658-1233. DR STRING; 208964.PA1843; -. DR EnsemblBacteria; AAG05232; AAG05232; PA1843. DR GeneID; 880631; -. DR KEGG; pae:PA1843; -. DR PATRIC; 19838071; VBIPseAer58763_1916. DR PseudoCAP; PA1843; -. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR InParanoid; Q9I2Q2; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR PhylomeDB; Q9I2Q2; -. DR UniPathway; UPA00051; UER00081. DR Proteomes; UP000002438; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Cobalamin; Cobalt; Complete proteome; KW Metal-binding; Methionine biosynthesis; Methyltransferase; KW Reference proteome; Repeat; S-adenosyl-L-methionine; Transferase; KW Zinc. FT CHAIN 1 1234 Methionine synthase. FT /FTId=PRO_0000287780. FT DOMAIN 12 332 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT DOMAIN 363 624 Pterin-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00334}. FT DOMAIN 655 749 B12-binding N-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00666}. FT DOMAIN 752 888 B12-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00666}. FT DOMAIN 904 1234 AdoMet activation. {ECO:0000255|PROSITE- FT ProRule:PRU00346}. FT REGION 840 841 Cobalamin-binding. {ECO:0000250}. FT REGION 1197 1198 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT METAL 254 254 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 317 317 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 318 318 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 765 765 Cobalt (cobalamin axial ligand). FT {ECO:0000250}. FT BINDING 810 810 Cobalamin. {ECO:0000250}. FT BINDING 954 954 S-adenosyl-L-methionine. {ECO:0000250}. FT BINDING 1142 1142 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000250}. FT BINDING 1146 1146 Cobalamin; via carbonyl oxygen. FT {ECO:0000250}. SQ SEQUENCE 1234 AA; 135063 MW; 9877F8AC8BEF44ED CRC64; MSSPLTDRSA RLQALQHALR ERILILDGGM GTMIQSYKLE EADYRGERFA DWPSDVKGNN DLLLLSRPDV IQAIEKAYLD AGADILETNT FNATQVSQAD YGMQSLAYEL NVEGARLARQ VADAKTAETP DKPRFVAGVL GPTSRTCSIS PDVNNPGYRN VTFDELVENY VEATRGLIEG GADLILIETI FDTLNAKAAI FAVQGVFEEL GVELPIMISG TITDASGRTL SGQTTEAFWN SVRHARPISV GLNCALGAKE LRPYIEELST KADTHVSAHP NAGLPNAFGE YDESPAEMAV VVEEFAAAGF LNIVGGCCGT TPAHIEAIAK AVAKYPPRAI PEIPRACRLS GLEPFTIDRS SLFVNVGERT NITGSAKFAR LIREENYAEA LEVAQQQVEA GAQVIDINMD EGMLDSKAAM VTFLNLIASE PDISRVPIMI DSSKWEVIEA GLKCIQGKGI VNSISMKEGV EAFKHHARLC KRYGAAVVVM AFDEDGQADT QARKEEICKR SYDILVDEVG FPPEDIIFDA NIFAIATGIE EHNNYAVDFI NACAYIRDNL PYALSSGGVS NVSFSFRGNN PVREAIHSVF LYYAIRNGLT MGIVNAGQLE IYDEIPKALR DRVEDVVLNR TPEATEALLA IADDYKGGGA VKEAEDEEWR SYSVEKRLEH ALVKGITTWI VEDTEECRQQ CARPIEVIEG PLMSGMNVVG DLFGAGKMFL PQVVKSARVM KQAVAHLIPF IEAEKGDKPE AKGKILMATV KGDVHDIGKN IVGVVLGCNG YDVVDLGVMV PAEKILQTAI AEKCDIIGLS GLITPSLDEM VHVAKEMQRQ NFQLPLMIGG ATTSKAHTAV KIDPQYSNDA VVYVTDASRA VGVATSLLSK ELKADYVART RADYAVVRER TANRSARTER LSYEQAIANK PAFDWAGYQA PTPSFTGVRV LDEIDLAVLA EYIDWTPFFI SWDLAGKYPR ILTDEVVGEA ATSLFNDAQA MLKKLIDEKL IKARAVFGFW PANQVEHDDL EVYGADGETL ATLHHLRQQT IKPDGKPNLS LADFVAPKES GVRDYIGGFI TTAGIGAEEV AKAYEAKGDD YNSIMVKALA DRLAEACAEW LHERVRKEYW GYARDEHLDN EALIKEQYVG IRPAPGYPAC PDHTEKGTLF ELLDPQGLSG VSLTEHYAMF PAAAVSGWYF AHPQAQYFAV GKIDKDQVER YSQRKGQEAS VSERWLAPNL GYDD // ID METH_PSEPU Reviewed; 607 AA. AC O33465; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 01-APR-2015, entry version 66. DE RecName: Full=Methionine synthase; DE EC=2.1.1.13; DE AltName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase; DE AltName: Full=Methionine synthase, vitamin-B12 dependent; DE Short=MS; DE Flags: Fragment; GN Name=metH; OS Pseudomonas putida (Arthrobacter siderocapsulatus). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=303; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=P8; RX PubMed=9361416; RA Holtwick R., Meinhardt F., Keweloh H.; RT "Cis-trans isomerization of unsaturated fatty acids: cloning and RT sequencing of the cti gene from Pseudomonas putida P8."; RL Appl. Environ. Microbiol. 63:4292-4297(1997). CC -!- FUNCTION: Catalyzes the transfer of a methyl group from methyl- CC cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and CC methionine. Subsequently, remethylates the cofactor using CC methyltetrahydrofolate (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + L-homocysteine = CC tetrahydrofolate + L-methionine. CC -!- COFACTOR: CC Name=methyl(III)cobalamin; Xref=ChEBI:CHEBI:28115; CC Evidence={ECO:0000250}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000305}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (MetH route): step CC 1/1. CC -!- DOMAIN: Modular enzyme with four functionally distinct domains. CC The isolated Hcy-binding domain catalyzes methyl transfer from CC free methylcobalamin to homocysteine. The Hcy-binding domain in CC association with the pterin-binding domain catalyzes the CC methylation of cob(I)alamin by methyltetrahydrofolate and the CC methylation of homocysteine. The B12-binding domain binds the CC cofactor. The AdoMet activation domain binds S-adenosyl-L- CC methionine. Under aerobic conditions cob(I)alamin can be converted CC to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L- CC methionine and flavodoxin regenerates methylcobalamin (By CC similarity). {ECO:0000250}. CC -!- MISCELLANEOUS: L-homocysteine is bound via the zinc atom. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine CC synthase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC -!- SIMILARITY: Contains 1 pterin-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00334}. CC -!- CAUTION: Ser-314 is present instead of the conserved Cys which is CC expected to be a zinc-binding residue. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ000978; CAA04437.1; -; Genomic_DNA. DR ProteinModelPortal; O33465; -. DR UniPathway; UPA00051; UER00081. DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Cobalamin; Cobalt; Metal-binding; KW Methionine biosynthesis; Methyltransferase; S-adenosyl-L-methionine; KW Transferase; Zinc. FT CHAIN 1 >607 Methionine synthase. FT /FTId=PRO_0000204535. FT DOMAIN 8 328 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT DOMAIN 359 >607 Pterin-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00334}. FT METAL 250 250 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 313 313 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT NON_TER 607 607 SQ SEQUENCE 607 AA; 65840 MW; BB7743CC28A922B3 CRC64; MSDRSARLQA LQNALKERIL ILDGGMGTMI QSYRLEEHDY RGTRFADWPS DVKGNNDLLL LSRPDVIAAI EKAYLDAGAD ILETNTFNAT QISQADYGME SLVYELNVEG ARIARQVADA KTLETPDKPR FVAGVLGPTS RTCSISPDVN DPGYRNVTFD ELVENYIEAT RGLIEGGADL ILIETIFDTL NAKAAIFAVQ QVFEEDAVEL PIMISGTITD ASGRTLSGQT TEAFWNSVRH AKPISVGLNC ALGAKDLRPY LEELSTKADT HVSAHPNAGL PNAFGEYDET PAEMAAVVEE FAASGFLNII GGCSGTTPGH IQAIAEAVAK YKPREIPEIA KACRLSGLEP FTIDGQSLFV NVGERTNITG SAKFARLIRE ENYTEALEVA LQQVEAGAQV IDINMDEGML DSQAAMVRFL NMIAGEPDIS RVPIMIDSSK GEVIEAGLKC IQGKGIVNSI SMKEGVEQFK HHARLCKRYG AAVVVMAFDE VGQADTAARK KEICKRSYDI LVNEVGFPPE DIIFDPNIFA VATGIEEHNN YAVDFIEACA YIRDHLPHAL TSGGVSNVSF SFRGNNPVRE AIHSVFLFHA ISNGLTMGIV NAGLLEI // ID METH_RAT Reviewed; 1253 AA. AC Q9Z2Q4; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 04-FEB-2015, entry version 101. DE RecName: Full=Methionine synthase; DE EC=2.1.1.13; DE AltName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase; DE AltName: Full=Vitamin-B12 dependent methionine synthase; DE Short=MS; GN Name=Mtr; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Wistar; TISSUE=Liver; RX PubMed=9972236; DOI=10.1271/bbb.62.2155; RA Yamada K., Tobimatsu T., Toraya T.; RT "Cloning, sequencing, and heterologous expression of rat methionine RT synthase cDNA."; RL Biosci. Biotechnol. Biochem. 62:2155-2160(1998). CC -!- FUNCTION: Catalyzes the transfer of a methyl group from methyl- CC cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and CC methionine. Subsequently, remethylates the cofactor using CC methyltetrahydrofolate (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + L-homocysteine = CC tetrahydrofolate + L-methionine. CC -!- COFACTOR: CC Name=methyl(III)cobalamin; Xref=ChEBI:CHEBI:28115; CC Evidence={ECO:0000250}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (MetH route): step CC 1/1. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- DOMAIN: Modular enzyme with four functionally distinct domains. CC The isolated Hcy-binding domain catalyzes methyl transfer from CC free methylcobalamin to homocysteine. The Hcy-binding domain in CC association with the pterin-binding domain catalyzes the CC methylation of cob(I)alamin by methyltetrahydrofolate and the CC methylation of homocysteine. The B12-binding domain binds the CC cofactor. The AdoMet activation domain binds S-adenosyl-L- CC methionine. Under aerobic conditions cob(I)alamin can be converted CC to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L- CC methionine and flavodoxin regenerates methylcobalamin (By CC similarity). {ECO:0000250}. CC -!- MISCELLANEOUS: L-homocysteine is bound via the zinc atom. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine CC synthase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 AdoMet activation domain. CC {ECO:0000255|PROSITE-ProRule:PRU00346}. CC -!- SIMILARITY: Contains 1 B12-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00666}. CC -!- SIMILARITY: Contains 1 B12-binding N-terminal domain. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC -!- SIMILARITY: Contains 1 pterin-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00334}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF034214; AAD05384.1; -; mRNA. DR PIR; T42376; T42376. DR RefSeq; NP_110491.1; NM_030864.1. DR UniGene; Rn.205061; -. DR ProteinModelPortal; Q9Z2Q4; -. DR SMR; Q9Z2Q4; 652-908, 914-1252. DR BioGrid; 249519; 1. DR IntAct; Q9Z2Q4; 1. DR STRING; 10116.ENSRNOP00000023973; -. DR PhosphoSite; Q9Z2Q4; -. DR PaxDb; Q9Z2Q4; -. DR PRIDE; Q9Z2Q4; -. DR GeneID; 81522; -. DR KEGG; rno:81522; -. DR UCSC; RGD:621283; rat. DR CTD; 4548; -. DR RGD; 621283; Mtr. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR HOVERGEN; HBG006347; -. DR InParanoid; Q9Z2Q4; -. DR KO; K00548; -. DR PhylomeDB; Q9Z2Q4; -. DR UniPathway; UPA00051; UER00081. DR NextBio; 615041; -. DR PRO; PR:Q9Z2Q4; -. DR Proteomes; UP000002494; Unplaced. DR Genevestigator; Q9Z2Q4; -. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0016597; F:amino acid binding; IDA:RGD. DR GO; GO:0031419; F:cobalamin binding; TAS:RGD. DR GO; GO:0005542; F:folic acid binding; IDA:RGD. DR GO; GO:0008705; F:methionine synthase activity; IDA:RGD. DR GO; GO:0008168; F:methyltransferase activity; IDA:RGD. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0061431; P:cellular response to methionine; IEP:RGD. DR GO; GO:0050667; P:homocysteine metabolic process; IDA:RGD. DR GO; GO:0009086; P:methionine biosynthetic process; IDA:RGD. DR GO; GO:0006555; P:methionine metabolic process; IMP:RGD. DR GO; GO:0006479; P:protein methylation; IDA:RGD. DR GO; GO:0046653; P:tetrahydrofolate metabolic process; IDA:RGD. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 2: Evidence at transcript level; KW Amino-acid biosynthesis; Cobalamin; Cobalt; Complete proteome; KW Cytoplasm; Metal-binding; Methionine biosynthesis; Methyltransferase; KW Reference proteome; Repeat; S-adenosyl-L-methionine; Transferase; KW Zinc. FT CHAIN 1 1253 Methionine synthase. FT /FTId=PRO_0000312902. FT DOMAIN 6 326 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT DOMAIN 359 620 Pterin-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00334}. FT DOMAIN 650 747 B12-binding N-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00666}. FT DOMAIN 760 895 B12-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00666}. FT DOMAIN 911 1253 AdoMet activation. {ECO:0000255|PROSITE- FT ProRule:PRU00346}. FT REGION 848 849 Cobalamin-binding. {ECO:0000250}. FT REGION 1215 1216 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT METAL 248 248 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 311 311 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 312 312 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 773 773 Cobalt (cobalamin axial ligand). FT {ECO:0000250}. FT BINDING 818 818 Cobalamin. {ECO:0000250}. FT BINDING 962 962 S-adenosyl-L-methionine. {ECO:0000250}. FT BINDING 1160 1160 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000250}. FT BINDING 1164 1164 Cobalamin; via carbonyl oxygen. FT {ECO:0000250}. SQ SEQUENCE 1253 AA; 139164 MW; 96BD40B796EBD75B CRC64; MKKTLQDEIE AILRKRIMVL DGGMGTMIQR YKLSEENFQG QEFKDHSRPL KGNNDILSIT QPDVIYQIHK EYLLAGADII ETNTFSSTSI AQADYGLEHL AYRMNKCSAD VARKAAEEIT LQTGVKRFVA GSLGPTNKTL SVSPSVERPD YRNITFDELV EAYQEQAKGL LDGGVDILLI ETIFDTANAK AALFALQKLF EENYASPRPI FISGTIVDKS GRTLSGQTGE AFVTSVSHSD PLCIGLNCAL GAAEMRPFIE TIGKCTTAYV LCYPNAGLPN TFGDYDETPA MMAMHLKDFA VDGLVNVVGG CCGSTPDHIR EIAEAVKNCK PRVPPDSVFE GHMLLSGLEP FRIGPYTNFV NIGERCNVAG SKKFAKLIMA GNYEEALSVA KVQVEMGAQV LDINMDDGML DGPSAMTKFC NFIASEPDIA KVPLCIDSSN FAVIEAGLKC CQGKCIVNSI SLKEGEEDFL EKARKIKKFG AAVVVMAFDE EGQATETDVK VSVCTRAYHL LVEKVGFNPN DIIFDPNILT IGTGMEEHNL YAINFIHATR VIKETLPGVR ISGGLSNLSF AFRGMDAIRE AMHGVFLYHA IKFGMDMGIV NAGSLPVYDD IHKDLLQLCE DLIWNRDAEA TEKLLRYAQT HGKGGKKVIQ TDEWRNGSIE ERLEYALVKG IEKHIVEDTE EARLNREKYP RPLNIIEGPL MNGMKVVGDL FGAGKMFLPQ VIKSARVMKK AVGHLIPFME KEREEARVLN GSVEEEDPYQ GTIVLATVKG DVHDIGKNIV GVVLGCNNFR VIDLGVMTPC DKILQAALDH KADIIGLSGL ITPSLDEMIF VAKEMERLAI KIPLLIGGAT TSRTHTAVKI APRYSAPVIH VLDASKSVVV CSQLLDENLK DDYFEEILEE YEDIRQDHYE SLKERKYLPL SQARKHSFHI DWLSEPHPVK PTFIGTQVFE DYNLQKLVDY IDWKPFFDVW QLRGKYPNRG FPKIFNDKAV GEEARKVYED AQNMLSILIS RKKLRARGVV GFWPAQSVQD DIHLYAEGAV PQAAEPIATF YGLRQQAEKD SSSTDPYHCL SDFVAPLHSG VRDYLGLFAV ACFGVEELSK AYEDDGDDYS SIMVKALGDR LAEAFAEELH ERVRRELWAY CGSEQLGVTD LRKLRYEGIR PAPGYPSQPD HTEKLTMWRL ANIEQATGIR LTESLAMAPA SAVSGLYFSN VKSKYFAVGK ISKDQIEDYA LRKNMSVAEV EKWLGPILGY DTD // ID METH_SALTY Reviewed; 1227 AA. AC P37586; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAY-2015, entry version 119. DE RecName: Full=Methionine synthase; DE EC=2.1.1.13; DE AltName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase; DE AltName: Full=Methionine synthase, vitamin-B12 dependent; DE Short=MS; GN Name=metH; OrderedLocusNames=STM4188; 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). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-371. RC STRAIN=LT2; RX PubMed=3072256; DOI=10.1016/0378-1119(88)90325-3; RA Urbanowski M.L., Stauffer G.V.; RT "The control region of the metH gene of Salmonella typhimurium LT2: an RT atypical met promoter."; RL Gene 73:193-200(1988). CC -!- FUNCTION: Catalyzes the transfer of a methyl group from methyl- CC cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and CC methionine. Subsequently, remethylates the cofactor using CC methyltetrahydrofolate (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + L-homocysteine = CC tetrahydrofolate + L-methionine. CC -!- COFACTOR: CC Name=methyl(III)cobalamin; Xref=ChEBI:CHEBI:28115; CC Evidence={ECO:0000250}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (MetH route): step CC 1/1. CC -!- DOMAIN: Modular enzyme with four functionally distinct domains. CC The isolated Hcy-binding domain catalyzes methyl transfer from CC free methylcobalamin to homocysteine. The Hcy-binding domain in CC association with the pterin-binding domain catalyzes the CC methylation of cob(I)alamin by methyltetrahydrofolate and the CC methylation of homocysteine. The B12-binding domain binds the CC cofactor. The AdoMet activation domain binds S-adenosyl-L- CC methionine. Under aerobic conditions cob(I)alamin can be converted CC to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L- CC methionine and flavodoxin regenerates methylcobalamin (By CC similarity). {ECO:0000250}. CC -!- MISCELLANEOUS: L-homocysteine is bound via the zinc atom. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine CC synthase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 AdoMet activation domain. CC {ECO:0000255|PROSITE-ProRule:PRU00346}. CC -!- SIMILARITY: Contains 1 B12-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00666}. CC -!- SIMILARITY: Contains 1 B12-binding N-terminal domain. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC -!- SIMILARITY: Contains 1 pterin-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00334}. CC -!- SEQUENCE CAUTION: CC Sequence=AAL23012.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE006468; AAL23012.1; ALT_INIT; Genomic_DNA. DR RefSeq; NP_463053.2; NC_003197.1. DR RefSeq; WP_000095958.1; NC_003197.1. DR ProteinModelPortal; P37586; -. DR SMR; P37586; 651-1227. DR STRING; 99287.STM4188.S; -. DR PaxDb; P37586; -. DR PRIDE; P37586; -. DR EnsemblBacteria; AAL23012; AAL23012; STM4188. DR GeneID; 1255714; -. DR KEGG; stm:STM4188.S; -. DR PATRIC; 32387269; VBISalEnt20916_4402. DR eggNOG; COG1410; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR PhylomeDB; P37586; -. DR BioCyc; SENT99287:GCTI-4218-MONOMER; -. DR UniPathway; UPA00051; UER00081. DR Proteomes; UP000001014; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Cobalamin; Cobalt; Complete proteome; KW Metal-binding; Methionine biosynthesis; Methyltransferase; KW Reference proteome; Repeat; S-adenosyl-L-methionine; Transferase; KW Zinc. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 1227 Methionine synthase. FT /FTId=PRO_0000204536. FT DOMAIN 2 325 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT DOMAIN 356 617 Pterin-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00334}. FT DOMAIN 650 744 B12-binding N-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00666}. FT DOMAIN 746 881 B12-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00666}. FT DOMAIN 897 1227 AdoMet activation. {ECO:0000255|PROSITE- FT ProRule:PRU00346}. FT REGION 834 835 Cobalamin-binding. {ECO:0000250}. FT REGION 1189 1190 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT METAL 247 247 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 310 310 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 311 311 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000250}. FT BINDING 804 804 Cobalamin. {ECO:0000250}. FT BINDING 946 946 S-adenosyl-L-methionine. {ECO:0000250}. FT BINDING 1134 1134 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000250}. FT BINDING 1138 1138 Cobalamin; via carbonyl oxygen. FT {ECO:0000250}. FT CONFLICT 115 115 A -> R (in Ref. 2). {ECO:0000305}. SQ SEQUENCE 1227 AA; 136004 MW; 11C8E21745FF5354 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLHEEDFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYRMESLS AEINYAAAKL ARACADEWTA RTPEKPRFVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKEEF EALGVDLPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPEHIAA MSRAVAGLLP RQLPDIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VESGAQIIDI NMDEGMLDAE AAMVRFLSLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVEAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLDLAEKYRG SKTDEAANAQ QAEWRSWDVK KRLEYSLVKG ITEFIEQDTE EARQQAARPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EKGSSNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAREVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHARKKPR TPPVTLEAAR DNDLAFDWER YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KLLNPRGVVG LFPANRVGDD IEIYRDETRT HVLTVSHHLR QQTEKVGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA IADRLAEAFA EYLHERVRKV YWGYAPNESL SNDELIRENY QGIRPAPGYP ACPEHTEKGT IWQLLDVEKH TGMKLTESFA MWPGASVSGW YFSHPESKYF AVAQIQRDQV TDYAFRKGMS VEDVERWLAP NLGYDAD // ID METH_SYNY3 Reviewed; 1195 AA. AC Q55786; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAY-2015, entry version 113. DE RecName: Full=Methionine synthase; DE EC=2.1.1.13; DE AltName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase; DE AltName: Full=Methionine synthase, vitamin-B12 dependent; DE Short=MS; GN Name=metH; OrderedLocusNames=slr0212; 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=ATCC 27184 / PCC 6803 / N-1; RX PubMed=8590279; DOI=10.1093/dnares/2.4.153; RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., RA Sugiura M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb RT region from map positions 64% to 92% of the genome."; RL DNA Res. 2:153-166(1995). RN [2] 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: Catalyzes the transfer of a methyl group from methyl- CC cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and CC methionine. Subsequently, remethylates the cofactor using CC methyltetrahydrofolate (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + L-homocysteine = CC tetrahydrofolate + L-methionine. CC -!- COFACTOR: CC Name=methyl(III)cobalamin; Xref=ChEBI:CHEBI:28115; CC Evidence={ECO:0000250}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (MetH route): step CC 1/1. CC -!- DOMAIN: Modular enzyme with four functionally distinct domains. CC The isolated Hcy-binding domain catalyzes methyl transfer from CC free methylcobalamin to homocysteine. The Hcy-binding domain in CC association with the pterin-binding domain catalyzes the CC methylation of cob(I)alamin by methyltetrahydrofolate and the CC methylation of homocysteine. The B12-binding domain binds the CC cofactor. The AdoMet activation domain binds S-adenosyl-L- CC methionine. Under aerobic conditions cob(I)alamin can be converted CC to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L- CC methionine and flavodoxin regenerates methylcobalamin (By CC similarity). {ECO:0000250}. CC -!- MISCELLANEOUS: L-homocysteine is bound via the zinc atom. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine CC synthase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 AdoMet activation domain. CC {ECO:0000255|PROSITE-ProRule:PRU00346}. CC -!- SIMILARITY: Contains 1 B12-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00666}. CC -!- SIMILARITY: Contains 1 B12-binding N-terminal domain. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC -!- SIMILARITY: Contains 1 pterin-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00334}. CC ----------------------------------------------------------------------- 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; BAA10438.1; -; Genomic_DNA. DR PIR; S76592; S76592. DR RefSeq; YP_005652428.1; NC_017277.1. DR RefSeq; YP_007452244.1; NC_020286.1. DR ProteinModelPortal; Q55786; -. DR STRING; 1148.slr0212; -. DR PaxDb; Q55786; -. DR EnsemblBacteria; BAA10438; BAA10438; BAA10438. DR KEGG; syn:slr0212; -. DR PATRIC; 23842418; VBISynSp132158_2749. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR InParanoid; Q55786; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR PhylomeDB; Q55786; -. DR UniPathway; UPA00051; UER00081. DR Proteomes; UP000001425; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Cobalamin; Cobalt; Complete proteome; KW Metal-binding; Methionine biosynthesis; Methyltransferase; KW Reference proteome; Repeat; S-adenosyl-L-methionine; Transferase; KW Zinc. FT CHAIN 1 1195 Methionine synthase. FT /FTId=PRO_0000204537. FT DOMAIN 1 309 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT DOMAIN 340 599 Pterin-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00334}. FT DOMAIN 629 722 B12-binding N-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00666}. FT DOMAIN 724 859 B12-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00666}. FT DOMAIN 896 1195 AdoMet activation. {ECO:0000255|PROSITE- FT ProRule:PRU00346}. FT REGION 812 813 Cobalamin-binding. {ECO:0000250}. FT REGION 1192 1193 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT METAL 228 228 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 294 294 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 295 295 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 737 737 Cobalt (cobalamin axial ligand). FT {ECO:0000250}. FT BINDING 782 782 Cobalamin. {ECO:0000250}. FT BINDING 945 945 S-adenosyl-L-methionine. {ECO:0000250}. FT BINDING 1138 1138 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000250}. FT BINDING 1142 1142 Cobalamin; via carbonyl oxygen. FT {ECO:0000250}. SQ SEQUENCE 1195 AA; 132540 MW; 1D9635B1B1DDB583 CRC64; MKSAFLDRIH SPDRPVLVFD GAMGTNLQVQ NLTAADFGGA EYEGCNEYLV HTKPEAVATV HRAFYEAGAD VVETDTFGGT PLVLAEYDLA DQSYYLNKAA AELAKAVAAE FSTPEKPRFV AGSMGPGTKL PTLGHVDYDS LKDAYVVQVR GLYDGGVDLL LVETCQDVLQ IKAALNAIEQ VFAEKGDRLP LMVSVTMETM GTMLVGTEMA AALAILEPYP IDILGLNCAT GPDLMKEHVK YLSEHSPFVV SCIPNAGLPE NVGGQAFYRL TPMELQMSLM HFIEDLGVQV IGGCCGTRPD HIKALADIAK DLQPKQRQPH YEPSAASIYS TQTYAQENSF LIIGERLNAS GSKKCRDLLN AEDWDSLVSL AKSQVKEGAQ ILDVNVDYVG RDGVRDMKEL ASRLVNNVTL PLMLDSTEWQ KMEAGLKVAG GKCILNSTNY EDGEERFYKV LEIAKEYGAG IVIGTIDEDG MGRTADKKFE IAKRAYEAAI AFGIPATEIF FDPLALPIST GIEEDRENGK ATVDAIRRIR QELPDCHILL GVSNVSFGLN PAARQVLNSI FLHECMQVGM DAAIVSANKI LPLAKIDPEQ QQVCLDLIYD RREFEGERCT YDPLTKLTTL FEGKTTKRDK SGDANLPVEE RLKRHIIDGE RLGLEEALNE ALKLYAPLDI INIYLLDGMK VVGELFGSGQ MQLPFVLQSA QTMKAAVAFL EPHMDKDDSA DNAKGTFLIA TVKGDVHDIG KNLVDIILSN NGYRVVNLGI KQPVENIIEA YKKHRPDCIA MSGLLVKSTA FMKENLEVFN QEGITVPVIL GGAALTPKFV HQDCQNTYKG QVIYGKDAFA DLHFMDKLMP AKNSHNWDDF QGFLGEYATE NGHNVTTDDG AKTNFGIEEE KLIDASEQSR EPEVIDTVRS EAVDPDLERP VPPFWGTKIL QSSDISLDEV FPLLDLQALF VGQWQFRKPR EQSREEYEQF LAEKVHPILA EWKGKVMAEN LLHPTVVYGY FPCQSQGNTL LIYDPELVSQ NNGQIPPDAT AIAKFEFPRQ KSGRRLCIAD FFASKESGIT DVFPLQAVTV GEIATEYARK LFAGDNYTDY LYFHGMAVQM AEALAEWTHQ RIRQELGFGH LDPDNIRDLL QQRYQGSRYS FGYPACPNMQ DQYTQLELLQ TERIGLYMDE SEQVYPEQST TAIISYHPAA KYFSA // ID METH_VIBCH Reviewed; 1226 AA. AC Q9KUW9; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAY-2015, entry version 91. DE RecName: Full=Methionine synthase; DE EC=2.1.1.13; DE AltName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase; DE AltName: Full=Methionine synthase, vitamin-B12 dependent; DE Short=MS; GN Name=metH; OrderedLocusNames=VC_0390; 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 -!- FUNCTION: Catalyzes the transfer of a methyl group from methyl- CC cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and CC methionine. Subsequently, remethylates the cofactor using CC methyltetrahydrofolate (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + L-homocysteine = CC tetrahydrofolate + L-methionine. CC -!- COFACTOR: CC Name=methyl(III)cobalamin; Xref=ChEBI:CHEBI:28115; CC Evidence={ECO:0000250}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (MetH route): step CC 1/1. CC -!- DOMAIN: Modular enzyme with four functionally distinct domains. CC The isolated Hcy-binding domain catalyzes methyl transfer from CC free methylcobalamin to homocysteine. The Hcy-binding domain in CC association with the pterin-binding domain catalyzes the CC methylation of cob(I)alamin by methyltetrahydrofolate and the CC methylation of homocysteine. The B12-binding domain binds the CC cofactor. The AdoMet activation domain binds S-adenosyl-L- CC methionine. Under aerobic conditions cob(I)alamin can be converted CC to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L- CC methionine and flavodoxin regenerates methylcobalamin (By CC similarity). {ECO:0000250}. CC -!- MISCELLANEOUS: L-homocysteine is bound via the zinc atom. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine CC synthase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 AdoMet activation domain. CC {ECO:0000255|PROSITE-ProRule:PRU00346}. CC -!- SIMILARITY: Contains 1 B12-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00666}. CC -!- SIMILARITY: Contains 1 B12-binding N-terminal domain. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC -!- SIMILARITY: Contains 1 pterin-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00334}. CC ----------------------------------------------------------------------- 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; AAF93563.1; -; Genomic_DNA. DR PIR; E82328; E82328. DR RefSeq; NP_230044.1; NC_002505.1. DR RefSeq; WP_000514261.1; NC_002505.1. DR ProteinModelPortal; Q9KUW9; -. DR SMR; Q9KUW9; 654-1224. DR STRING; 243277.VC0390; -. DR PRIDE; Q9KUW9; -. DR DNASU; 2614987; -. DR EnsemblBacteria; AAF93563; AAF93563; VC_0390. DR GeneID; 2614987; -. DR KEGG; vch:VC0390; -. DR PATRIC; 20079861; VBIVibCho83274_0365. DR eggNOG; COG1410; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; VCHO:VC0390-MONOMER; -. DR UniPathway; UPA00051; UER00081. DR Proteomes; UP000000584; Chromosome 1. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; ISS:TIGR. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; ISS:TIGR. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Cobalamin; Cobalt; Complete proteome; KW Metal-binding; Methionine biosynthesis; Methyltransferase; KW Reference proteome; Repeat; S-adenosyl-L-methionine; Transferase; KW Zinc. FT CHAIN 1 1226 Methionine synthase. FT /FTId=PRO_0000204538. FT DOMAIN 6 326 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT DOMAIN 357 618 Pterin-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00334}. FT DOMAIN 651 745 B12-binding N-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00666}. FT DOMAIN 747 882 B12-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00666}. FT DOMAIN 898 1226 AdoMet activation. {ECO:0000255|PROSITE- FT ProRule:PRU00346}. FT REGION 835 836 Cobalamin-binding. {ECO:0000250}. FT REGION 1191 1192 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT METAL 248 248 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 311 311 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 312 312 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000250}. FT BINDING 805 805 Cobalamin. {ECO:0000250}. FT BINDING 948 948 S-adenosyl-L-methionine. {ECO:0000250}. FT BINDING 1136 1136 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000250}. FT BINDING 1140 1140 Cobalamin; via carbonyl oxygen. FT {ECO:0000250}. SQ SEQUENCE 1226 AA; 135793 MW; 5CF4AB07A738D74F CRC64; MGKEVRQQLE QQLKQRILLI DGGMGTMIQS YKLQEEDYRG ARFVDWHCDL KGNNDLLVLT QPQIIKEIHS AYLEAGADIL ETNTFNSTTI AMADYDMQSL SAEINFAAAK LAREVADEWT AKDPSRPRYV AGVLGPTNRT CSISPDVNDP GFRNVTFDGL VEAYSESTRA LIKGGSDLIL IETIFDTLNA KACAFAVDSV FEELGISLPV MISGTITDAS GRTLSGQTTE AFYNALRHVR PISFGLNCAL GPDELRQYVE ELSRISECYV SAHPNAGLPN AFGEYDLSAE EMAEHIAEWA QAGFLNLVGG CCGTTPEHIA AIAKAVEGVK PRALPDLKVE CRLSGLEPLN IGPETLFVNV GERTNVTGSA RFKRLIKEEQ YDEALDVARE QVENGAQIID INMDEGMLDA EACMVRFLNL CASEPEISKV PVMVDSSKWE VIEAGLKCIQ GKGIVNSISL KEGKEKFIAQ AKLVRRYGAA VIVMAFDEVG QADTRERKLE ICRRAYHILV DEVGFPPEDI IFDPNIFAVA TGIDEHNNYA LDFINAVADI KRELPHAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK HGMDMGIVNA GQLEIYDNVP LKLREAVEDV ILNRRSDGTE RLLEIAEAYR ENSVGKEEDA SALEWRAWPV AKRLEHALVK GITEFIVQDT EEARQQASKP LEVIEGPLMD GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AYLEPFINAQ KSGSTSNGKI LLATVKGDVH DIGKNIVGVV LQCNNFEIID LGVMVPCEQI LKVAREQNVD IIGLSGLITP SLDEMVHVAK EMERQGFELP LLIGGATTSK AHTAVKIEQN YHAPVVYVNN ASRAVGVCTS LLSDEQRPGF IERLDLDYER TRDQHARKTP KSRPVTLEQA RANKAALDWA NYTPPAPAKP GVHVFENIAL ATLRPYIDWT PFFMTWSLMG KYPAILEHEE VGEEAKRLFH DANALLDKVE REGLLKASGM CALFPAASVG DDIEVYSDES RTQVAHVLYN LRQQTEKPKG ANYCLSDYVA PKESGKRDWI GAFAVTGGIG ERALADAYKA QGDDYNAIMI QAVADRLAEA FAEYLHEKVR KEIWGYASDE NLSNDDLIRE RYQGIRPAPG YPACPEHTEK ATLWQMLNVE ETIGMSLTTS YAMWPGASVS GWYFSHPDSR YFAVAQIQPD QLHSYAERKG WRLEEAEKWL APNLDA // ID METH_VIBF1 Reviewed; 1226 AA. AC Q5E814; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 27-MAY-2015, entry version 77. DE RecName: Full=Methionine synthase; DE EC=2.1.1.13; DE AltName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase; DE AltName: Full=Methionine synthase, vitamin-B12 dependent; DE Short=MS; GN Name=metH; OrderedLocusNames=VF_0337; 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: Catalyzes the transfer of a methyl group from methyl- CC cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and CC methionine. Subsequently, remethylates the cofactor using CC methyltetrahydrofolate (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + L-homocysteine = CC tetrahydrofolate + L-methionine. CC -!- COFACTOR: CC Name=methyl(III)cobalamin; Xref=ChEBI:CHEBI:28115; CC Evidence={ECO:0000250}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (MetH route): step CC 1/1. CC -!- DOMAIN: Modular enzyme with four functionally distinct domains. CC The isolated Hcy-binding domain catalyzes methyl transfer from CC free methylcobalamin to homocysteine. The Hcy-binding domain in CC association with the pterin-binding domain catalyzes the CC methylation of cob(I)alamin by methyltetrahydrofolate and the CC methylation of homocysteine. The B12-binding domain binds the CC cofactor. The AdoMet activation domain binds S-adenosyl-L- CC methionine. Under aerobic conditions cob(I)alamin can be converted CC to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L- CC methionine and flavodoxin regenerates methylcobalamin (By CC similarity). {ECO:0000250}. CC -!- MISCELLANEOUS: L-homocysteine is bound via the zinc atom. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine CC synthase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 AdoMet activation domain. CC {ECO:0000255|PROSITE-ProRule:PRU00346}. CC -!- SIMILARITY: Contains 1 B12-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00666}. CC -!- SIMILARITY: Contains 1 B12-binding N-terminal domain. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC -!- SIMILARITY: Contains 1 pterin-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00334}. CC ----------------------------------------------------------------------- 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; AAW84832.1; -; Genomic_DNA. DR RefSeq; WP_011261140.1; NC_006840.2. DR RefSeq; YP_203720.1; NC_006840.2. DR ProteinModelPortal; Q5E814; -. DR SMR; Q5E814; 655-1225. DR STRING; 312309.VF_0337; -. DR EnsemblBacteria; AAW84832; AAW84832; VF_0337. DR GeneID; 3277291; -. DR KEGG; vfi:VF_0337; -. DR PATRIC; 20111162; VBIVibFis127983_0328. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; AFIS312309:GIWP-343-MONOMER; -. DR UniPathway; UPA00051; UER00081. DR Proteomes; UP000000537; Chromosome I. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Cobalamin; Cobalt; Complete proteome; KW Metal-binding; Methionine biosynthesis; Methyltransferase; KW Reference proteome; Repeat; S-adenosyl-L-methionine; Transferase; KW Zinc. FT CHAIN 1 1226 Methionine synthase. FT /FTId=PRO_0000204539. FT DOMAIN 7 327 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT DOMAIN 358 619 Pterin-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00334}. FT DOMAIN 652 746 B12-binding N-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00666}. FT DOMAIN 748 883 B12-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00666}. FT DOMAIN 899 1226 AdoMet activation. {ECO:0000255|PROSITE- FT ProRule:PRU00346}. FT REGION 836 837 Cobalamin-binding. {ECO:0000250}. FT REGION 1192 1193 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT METAL 249 249 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 312 312 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 313 313 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000250}. FT BINDING 806 806 Cobalamin. {ECO:0000250}. FT BINDING 949 949 S-adenosyl-L-methionine. {ECO:0000250}. FT BINDING 1137 1137 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000250}. FT BINDING 1141 1141 Cobalamin; via carbonyl oxygen. FT {ECO:0000250}. SQ SEQUENCE 1226 AA; 136369 MW; A1464CA5E141F3BD CRC64; MAGSNIKVQI EKQLSERILL IDGGMGTMIQ GYKFEEEDYR GERFNKWHCD LKGNNDLLVL SQPQIIRDIH EAYLEAGADI LETNTFNATT IAMADYDMES LSEEINFEAA KLAREVADKW TEKTPNKPRY VAGVLGPTNR TCSISPDVND PGFRNVSFDE LVEAYSESTR ALIRGGSDLI LIETIFDTLN AKACSFAVES VFEELDITLP VMISGTITDA SGRTLSGQTT EAFYNALRHV KPISFGLNCA LGPDELREYV SDLSRISECY VSAHPNAGLP NAFGEYDLSP EDMAEHVAEW ASSGFLNLIG GCCGTTPEHI RQMALVVEGV KPRQLPELPV ACRLSGLEPL TIEKDSLFIN VGERTNVTGS ARFKRLIKEE LYDEALSVAQ EQVENGAQII DINMDEGMLD AEACMVRFLN LCASEPEISK VPVMVDSSKW EVIEAGLKCI QGKGIVNSIS LKEGKEKFVH QAKLIRRYGA AVIVMAFDEV GQADTRERKI EICTNAYNIL VDEVGFPPED IIFDPNIFAV ATGIDEHNNY AVDFIEAVGD IKRTLPHAMI SGGVSNVSFS FRGNNYVREA IHAVFLYHCF KNGMDMGIVN AGQLEIYDNV PEDLREAVED VVLNRRDDST ERLLDIATEY LERAVGKVED KSALEWRDWP VEKRLEHSLV KGITEFIVED TEEARINAEK PIEVIEGPLM DGMNVVGDLF GEGKMFLPQV VKSARVMKQA VAHLEPFINA SKEVGATNGK ILLATVKGDV HDIGKNIVGV VLQCNNYEII DLGVMVSCET ILKVAKEENV DIIGLSGLIT PSLDEMVHVA KEMERQGFDL PLLIGGATTS KAHTAVKIEQ NYSQPVVYVN NASRAVGVCT SLLSDELKPS FVEKLDIDYE RVREQHSRKQ PRTKPVTLEV ARANKVAIDW ASYTPPVPLK PGVHIFDNFD VSTLRNYIDW TPFFMTWSLV GKYPKILDHE EVGEEAKRLF KDANDLLDRV EKEGLLKARG MCALFPASSV GDDIEVYTDE SRTKVAKVLH NLRQQTEKPK GFNYCLSDYI APKESGKNDW IGGFAVTGGI GERELADEYK ANGDDYNAIM IQAVADRLAE AFAEYLHEKV RKEIWGYSPN ETLSNDDLIR EKYQGIRPAP GYPACPEHTE KGALWELMNV EESIGMSLTS SYAMWPGASV SGMYFSHPDS RYFAIAQIQQ DQAESYADRK GWNMLEAEKW LGPNLN // ID METH_ALIFS Reviewed; 1226 AA. AC Q9AJQ8; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 26-NOV-2014, entry version 68. DE RecName: Full=Methionine synthase; DE EC=2.1.1.13; DE AltName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase; DE AltName: Full=Methionine synthase, vitamin-B12 dependent; DE Short=MS; GN Name=metH; OS Aliivibrio fischeri (Vibrio fischeri). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Aliivibrio. OX NCBI_TaxID=668; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 7744 / DSM 507 / NCIMB 1281 / 398; RX PubMed=11250084; DOI=10.1016/S0378-1119(01)00339-0; RA Kasai S., Yamazaki T.; RT "Identification of the cobalamin-dependent methionine synthase gene, RT metH, in Vibrio fischeri ATCC 7744 by sequencing using genomic DNA as RT a template."; RL Gene 264:281-288(2001). CC -!- FUNCTION: Catalyzes the transfer of a methyl group from methyl- CC cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and CC methionine. Subsequently, remethylates the cofactor using CC methyltetrahydrofolate (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + L-homocysteine = CC tetrahydrofolate + L-methionine. CC -!- COFACTOR: CC Name=methyl(III)cobalamin; Xref=ChEBI:CHEBI:28115; CC Evidence={ECO:0000250}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (MetH route): step CC 1/1. CC -!- DOMAIN: Modular enzyme with four functionally distinct domains. CC The isolated Hcy-binding domain catalyzes methyl transfer from CC free methylcobalamin to homocysteine. The Hcy-binding domain in CC association with the pterin-binding domain catalyzes the CC methylation of cob(I)alamin by methyltetrahydrofolate and the CC methylation of homocysteine. The B12-binding domain binds the CC cofactor. The AdoMet activation domain binds S-adenosyl-L- CC methionine. Under aerobic conditions cob(I)alamin can be converted CC to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L- CC methionine and flavodoxin regenerates methylcobalamin (By CC similarity). {ECO:0000250}. CC -!- MISCELLANEOUS: L-homocysteine is bound via the zinc atom. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine CC synthase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 AdoMet activation domain. CC {ECO:0000255|PROSITE-ProRule:PRU00346}. CC -!- SIMILARITY: Contains 1 B12-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00666}. CC -!- SIMILARITY: Contains 1 B12-binding N-terminal domain. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC -!- SIMILARITY: Contains 1 pterin-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00334}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB039955; BAB39355.1; -; Genomic_DNA. DR ProteinModelPortal; Q9AJQ8; -. DR SMR; Q9AJQ8; 655-1225. DR PRIDE; Q9AJQ8; -. DR UniPathway; UPA00051; UER00081. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Cobalamin; Cobalt; Metal-binding; KW Methionine biosynthesis; Methyltransferase; Repeat; KW S-adenosyl-L-methionine; Transferase; Zinc. FT CHAIN 1 1226 Methionine synthase. FT /FTId=PRO_0000204540. FT DOMAIN 7 327 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT DOMAIN 358 619 Pterin-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00334}. FT DOMAIN 652 746 B12-binding N-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00666}. FT DOMAIN 748 883 B12-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00666}. FT DOMAIN 899 1226 AdoMet activation. {ECO:0000255|PROSITE- FT ProRule:PRU00346}. FT REGION 836 837 Cobalamin-binding. {ECO:0000250}. FT REGION 1192 1193 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT METAL 249 249 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 312 312 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 313 313 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000250}. FT BINDING 806 806 Cobalamin. {ECO:0000250}. FT BINDING 949 949 S-adenosyl-L-methionine. {ECO:0000250}. FT BINDING 1137 1137 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000250}. FT BINDING 1141 1141 Cobalamin; via carbonyl oxygen. FT {ECO:0000250}. SQ SEQUENCE 1226 AA; 136266 MW; AF210E43E119E50C CRC64; MAGSNIKVQI EKQLSERILL IDGGMGTMIQ GYKFEEKDYR GGRFNQWHCD LKGNNDLLVL SQPQIIRDIH EAYLEAGADI LETNTFNATT IAMADYDMES LSEEINFEAA KLAREVADKW TEKTPNKPRY VAGVLGPTNR TCSISPDVND PGFRNVSFDE LVEAYSESTR ALIRGGSDLI LIETIFDTLN AKACSFAVES VFEELGITLP VMISGTITDA SGRTLSGQTT EAFYNALRHV KPISFGLNCA LGPDELREYV SELSRISECY VSAHPNAGLP NAFGEYDLSP EDMAEHVAEW ASSGFLNLIG GCCGTTPEHI RQMALVVEGV KPRQLPELPV ACRLSGLEPL TIEKDSLFIN VGERTNVTGS ARFKRLIKEE LYDEALSVAQ EQVENGAQII DINMDEGMLD AEACMVRFLN LCASEPEISK VPVMVDSSKW EVIEAGLKCI QGKGIVNSIS LKEGKEKFVH QAKLIRRYGA AVIVMAFDEV GQADTRERKI EICTNAYNIL VDEVGFPPED IIFDPNIFAV ATGIDEHNNY AVDFIEAVGD IKRTLPHAMI SGGVSNVSFS FRGNNYVREA IHAVFLYHCF KNGMDMGIVN AGQLEIYDNV PEDLREAVED VVLNRRDDST ERLLDIATEY LERAVGKVED KSALEWRDWP VEKRLEHSLV KGITEFIVED TEEARINAER PIEVIEGPLM DGMNVVGDLF GEGKMFLPQV VKSARVMKQA VAHLEPFINA SKEVGATNGK ILLATVKGDV HDIGKNIVGV VLQCNNYEII DLGVMVSCET ILKVAKEENV DIIGLSGLIT PSLDEMVHVA KEMERQGFDL PLLIGGATTS KAHTAVKIEQ NYSQPVVYVN NASRAVGVCT SLLSNELKPS FVEKLDIDYE RVREQHSRKQ PRTKPVTLEV ARANKVAIDW ASYTPPVPLK PGVHIFDNFD VSTLRNYIDW TPFFMTWSLV GKYPKILEHE EVGEEAKRLF KDANDLLDRV EKEGLLKARG MCALFPASSV GDDIEVYTDE SRTTVAKVLH NLRQQTEKPK GFNYCLSDYI APKESGKNDW IGGFAVTGGI GERELADEYK ANGDDYNAIM IQAVADRLAE AFAEYLHEKV RKEIWGYSPN ETLSNDDLIR EKYQGIRPAP GYPACPEHTE KGALWELMNV EESIGMSLTS SYAMWPGASV SGMYFSHPDS RYFAIAQIQQ DQAESYADRK GWNMLEAEKW LGPNLN // ID METH_VIBPA Reviewed; 1226 AA. AC Q87L95; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAY-2015, entry version 82. DE RecName: Full=Methionine synthase; DE EC=2.1.1.13; DE AltName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase; DE AltName: Full=Methionine synthase, vitamin-B12 dependent; DE Short=MS; GN Name=metH; OrderedLocusNames=VP2717; 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: Catalyzes the transfer of a methyl group from methyl- CC cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and CC methionine. Subsequently, remethylates the cofactor using CC methyltetrahydrofolate (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + L-homocysteine = CC tetrahydrofolate + L-methionine. CC -!- COFACTOR: CC Name=methyl(III)cobalamin; Xref=ChEBI:CHEBI:28115; CC Evidence={ECO:0000250}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (MetH route): step CC 1/1. CC -!- DOMAIN: Modular enzyme with four functionally distinct domains. CC The isolated Hcy-binding domain catalyzes methyl transfer from CC free methylcobalamin to homocysteine. The Hcy-binding domain in CC association with the pterin-binding domain catalyzes the CC methylation of cob(I)alamin by methyltetrahydrofolate and the CC methylation of homocysteine. The B12-binding domain binds the CC cofactor. The AdoMet activation domain binds S-adenosyl-L- CC methionine. Under aerobic conditions cob(I)alamin can be converted CC to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L- CC methionine and flavodoxin regenerates methylcobalamin (By CC similarity). {ECO:0000250}. CC -!- MISCELLANEOUS: L-homocysteine is bound via the zinc atom. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine CC synthase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 AdoMet activation domain. CC {ECO:0000255|PROSITE-ProRule:PRU00346}. CC -!- SIMILARITY: Contains 1 B12-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00666}. CC -!- SIMILARITY: Contains 1 B12-binding N-terminal domain. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC -!- SIMILARITY: Contains 1 pterin-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00334}. CC ----------------------------------------------------------------------- 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; BAC60980.1; -; Genomic_DNA. DR RefSeq; NP_799096.1; NC_004603.1. DR RefSeq; WP_005453805.1; NC_004603.1. DR ProteinModelPortal; Q87L95; -. DR SMR; Q87L95; 654-1224. DR STRING; 223926.VP2717; -. DR PRIDE; Q87L95; -. DR EnsemblBacteria; BAC60980; BAC60980; BAC60980. DR GeneID; 1190262; -. DR KEGG; vpa:VP2717; -. DR PATRIC; 20143630; VBIVibPar50997_2612. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; VPAR223926:GHK4-2806-MONOMER; -. DR UniPathway; UPA00051; UER00081. DR Proteomes; UP000002493; Chromosome 1. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Cobalamin; Cobalt; Complete proteome; KW Metal-binding; Methionine biosynthesis; Methyltransferase; KW Reference proteome; Repeat; S-adenosyl-L-methionine; Transferase; KW Zinc. FT CHAIN 1 1226 Methionine synthase. FT /FTId=PRO_0000204541. FT DOMAIN 6 326 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT DOMAIN 357 618 Pterin-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00334}. FT DOMAIN 651 745 B12-binding N-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00666}. FT DOMAIN 747 882 B12-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00666}. FT DOMAIN 898 1226 AdoMet activation. {ECO:0000255|PROSITE- FT ProRule:PRU00346}. FT REGION 835 836 Cobalamin-binding. {ECO:0000250}. FT REGION 1191 1192 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT METAL 248 248 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 311 311 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 312 312 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000250}. FT BINDING 805 805 Cobalamin. {ECO:0000250}. FT BINDING 948 948 S-adenosyl-L-methionine. {ECO:0000250}. FT BINDING 1136 1136 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000250}. FT BINDING 1140 1140 Cobalamin; via carbonyl oxygen. FT {ECO:0000250}. SQ SEQUENCE 1226 AA; 136218 MW; 2F7A3269FB7C20A9 CRC64; MGSKVRQQIE AQLKQRILLI DGGMGTMIQG YKLEEQDYRG ERFANWHCDL KGNNDLLVLS QPQLIKEIHS AYLEAGADIL ETNTFNATTI AMADYEMESL SEEINFAAAK LAREVADEWT AKTPDKPRYV AGVLGPTNRT CSISPDVNDP GYRNVSFDEL VEAYSESTRA LIRGGADLIL IETIFDTLNA KACAFAVDSV FEELGVALPV MISGTITDAS GRTLSGQTTE AFYNSLRHVR PLSFGLNCAL GPDELRPYVE ELSRISESFV SAHPNAGLPN AFGEYDLSPE DMAEHVKEWA SSGFLNLIGG CCGTTPEHIR QMAQAVEGVT PRALPDLPVA CRLSGLEPLT IEKETLFINV GERTNVTGSA RFKRLIKEEQ YDEALEVARQ QVENGAQIID INMDEGMLDA QACMVRFLNL CASEPEISKV PIMVDSSKWE VIEAGLKCIQ GKGIVNSISL KEGKEKFVEQ AKLIRRYGAA VIVMAFDEVG QAETRTRKLE ICTNAYRILV DEVGFPPEDI IFDPNIFAVA TGIDEHNNYA VDFIEAVADI KRDLPHAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK NGMDMGIVNA GQLEIYDNVP EKLREAVEDV VLNRRDDATE RLLDIAAEYA DKGVGKEEDA SALEWRTWPV AKRLEHALVK GITEFIVADT EEARVNAVKP LEVIEGPLMD GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AHLEPFINAE KQSGSSNGKI LLATVKGDVH DIGKNIVGVV LQCNNYEIID LGVMVPCEKI LKVAIEENVD IIGLSGLITP SLDEMVHVAK EMERLNFDLP LLIGGATTSK AHTAVKIEQN YKNPVVYVNN ASRAVGVCSS LLSDERRPAF IEKLDADYER VRDQHNRKKP RTKPVTLEQA RANKVAIDWD AYTPPVPAKP GLHIFDDFDV ATLRKYIDWT PFFMTWSLVG KYPTIFKHEE VGEEAQRLFH DANELLDRVE REGLLKARGI CGLFPAASVG DDIEVYTDES RTEVAKVLRN LRQQTEKPKG FNYCLSDYIA PKESGKQDWV GAFAVTGGIG ERELADEYKA QGDDYNAIMI QAVADRLAEA FAEYLHERVR KEIWGYAADE NLSNDELIRE KYQGIRPAPG YPACPEHTEK GPLWELLNVE ENIGMSLTTS YAMYPGASVS GWYFSHPDSR YFAIAQIQDD QLESYADRKG WDRIEAEKWL GPNING // ID METH_VIBVU Reviewed; 1226 AA. AC Q8DCJ7; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAY-2015, entry version 90. DE RecName: Full=Methionine synthase; DE EC=2.1.1.13; DE AltName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase; DE AltName: Full=Methionine synthase, vitamin-B12 dependent; DE Short=MS; GN Name=metH; OrderedLocusNames=VV1_1423; 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 -!- FUNCTION: Catalyzes the transfer of a methyl group from methyl- CC cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and CC methionine. Subsequently, remethylates the cofactor using CC methyltetrahydrofolate (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + L-homocysteine = CC tetrahydrofolate + L-methionine. CC -!- COFACTOR: CC Name=methyl(III)cobalamin; Xref=ChEBI:CHEBI:28115; CC Evidence={ECO:0000250}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (MetH route): step CC 1/1. CC -!- DOMAIN: Modular enzyme with four functionally distinct domains. CC The isolated Hcy-binding domain catalyzes methyl transfer from CC free methylcobalamin to homocysteine. The Hcy-binding domain in CC association with the pterin-binding domain catalyzes the CC methylation of cob(I)alamin by methyltetrahydrofolate and the CC methylation of homocysteine. The B12-binding domain binds the CC cofactor. The AdoMet activation domain binds S-adenosyl-L- CC methionine. Under aerobic conditions cob(I)alamin can be converted CC to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L- CC methionine and flavodoxin regenerates methylcobalamin (By CC similarity). {ECO:0000250}. CC -!- MISCELLANEOUS: L-homocysteine is bound via the zinc atom. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine CC synthase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 AdoMet activation domain. CC {ECO:0000255|PROSITE-ProRule:PRU00346}. CC -!- SIMILARITY: Contains 1 B12-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00666}. CC -!- SIMILARITY: Contains 1 B12-binding N-terminal domain. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC -!- SIMILARITY: Contains 1 pterin-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00334}. CC ----------------------------------------------------------------------- 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; AAO09863.1; -; Genomic_DNA. DR RefSeq; NP_760336.1; NC_004459.3. DR RefSeq; WP_011079382.1; NC_004459.3. DR ProteinModelPortal; Q8DCJ7; -. DR SMR; Q8DCJ7; 654-1224. DR STRING; 216895.VV1_1423; -. DR PRIDE; Q8DCJ7; -. DR EnsemblBacteria; AAO09863; AAO09863; VV1_1423. DR KEGG; vvu:VV1_1423; -. DR PATRIC; 20159626; VBIVibVul94426_1325. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; VVUL216895:GIYM-1264-MONOMER; -. DR UniPathway; UPA00051; UER00081. DR Proteomes; UP000002275; Chromosome 1. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Cobalamin; Cobalt; Complete proteome; KW Metal-binding; Methionine biosynthesis; Methyltransferase; Repeat; KW S-adenosyl-L-methionine; Transferase; Zinc. FT CHAIN 1 1226 Methionine synthase. FT /FTId=PRO_0000204542. FT DOMAIN 6 326 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT DOMAIN 357 618 Pterin-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00334}. FT DOMAIN 651 745 B12-binding N-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00666}. FT DOMAIN 747 882 B12-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00666}. FT DOMAIN 898 1226 AdoMet activation. {ECO:0000255|PROSITE- FT ProRule:PRU00346}. FT REGION 835 836 Cobalamin-binding. {ECO:0000250}. FT REGION 1191 1192 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT METAL 248 248 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 311 311 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 312 312 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000250}. FT BINDING 805 805 Cobalamin. {ECO:0000250}. FT BINDING 948 948 S-adenosyl-L-methionine. {ECO:0000250}. FT BINDING 1136 1136 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000250}. FT BINDING 1140 1140 Cobalamin; via carbonyl oxygen. FT {ECO:0000250}. SQ SEQUENCE 1226 AA; 136241 MW; 51E8263EBD605A19 CRC64; MGSQIRAQIE AQLKQRILLI DGGMGTMIQG YKLQEQDYRG ERFADWHSDL KGNNDLLVLT QPQLIKEIHH AYLEAGADIL ETNTFNATTI AMADYDMESL SEEINFAAAR LAREAADEWT AQNPAKPRYV AGVLGPTNRT CSISPDVNDP GYRNVSFDEL VEAYSESTRA LIRGGSDLIL IETIFDTLNA KACAFAVDSV FEELGFALPV MISGTITDAS GRTLSGQTTE AFYNSLRHVR PISFGLNCAL GPDELRPYVE ELSRISETFV STHPNAGLPN AFGEYDLSPE EMAEHVKEWA QSGFLNLIGG CCGTTPEHIR HMAMAVEGVS PRVLPEIPVA CRLSGLEPLT IAKDTLFVNV GERTNVTGSA RFKRLIKEEL YDEALDVARE QVENGAQIID INMDEGMLDA EACMVRFLNL CASEPEISKV PIMVDSSKWE VIEAGLKCIQ GKGIVNSISL KEGKEKFVEQ AKLIRRYGAA VIVMAFDEVG QADTRERKLE ICTKAYRILV DEVGFPPEDV IFDPNIFAVA TGIDEHNNYA VDFIEAVADI KRDLPHAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK NGMDMGIVNA GQLEIYDNVP EKLREAVEDV VLNRRDDATE RLLEIAEEYR ENAVGKQEDA SALEWRTWSV EKRLEHALVK GITEFIVEDT EEARLNASKP LEVIEGPLMD GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AHLEPFINAS KQAGSSNGKI LLATVKGDVH DIGKNIVGVV LQCNNYEIID LGVMVPCEQI LKVAKEQQVD IIGLSGLITP SLDEMVHVAK EMERLGFDLP LLIGGATTSK AHTAVKIEQN YSHPVVYVNN ASRAVGVCTS LLSDELRPAF VERLQADYEL VRDQHNRKKP RTKPVTLEAA RANKVAIDWQ SYTPPAPSQP GVHVFDDFDV ATLRQYIDWT PFFLTWSLVG KYPTIFEHEE VGEEAKRLFG DANEWLDRIE QEGLLKARGM CGLFPAASVG DDIEVYTDES RTHVAKVLHN LRQQTEKPKG ANYCLSDYVA PKESGKKDWI GAFAVTGGVN ERELADQFKA QGDDYNAIMI QAVADRLAEA FAEYLHERVR KEIWGYAADE NLSNEELIRE KYQGIRPAPG YPACPEHTEK GPLWELLNVE ETIGMSLTSS YAMWPGASVS GWYFSHPDSR YFAIAQIQQD QVESYAERKG WDLLEAEKWL GPNING // ID METH_VIBVY Reviewed; 1226 AA. AC Q7MHB1; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 1. DT 27-MAY-2015, entry version 86. DE RecName: Full=Methionine synthase; DE EC=2.1.1.13; DE AltName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase; DE AltName: Full=Methionine synthase, vitamin-B12 dependent; DE Short=MS; GN Name=metH; OrderedLocusNames=VV2960; 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 -!- FUNCTION: Catalyzes the transfer of a methyl group from methyl- CC cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and CC methionine. Subsequently, remethylates the cofactor using CC methyltetrahydrofolate (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + L-homocysteine = CC tetrahydrofolate + L-methionine. CC -!- COFACTOR: CC Name=methyl(III)cobalamin; Xref=ChEBI:CHEBI:28115; CC Evidence={ECO:0000250}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (MetH route): step CC 1/1. CC -!- DOMAIN: Modular enzyme with four functionally distinct domains. CC The isolated Hcy-binding domain catalyzes methyl transfer from CC free methylcobalamin to homocysteine. The Hcy-binding domain in CC association with the pterin-binding domain catalyzes the CC methylation of cob(I)alamin by methyltetrahydrofolate and the CC methylation of homocysteine. The B12-binding domain binds the CC cofactor. The AdoMet activation domain binds S-adenosyl-L- CC methionine. Under aerobic conditions cob(I)alamin can be converted CC to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L- CC methionine and flavodoxin regenerates methylcobalamin (By CC similarity). {ECO:0000250}. CC -!- MISCELLANEOUS: L-homocysteine is bound via the zinc atom. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine CC synthase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 AdoMet activation domain. CC {ECO:0000255|PROSITE-ProRule:PRU00346}. CC -!- SIMILARITY: Contains 1 B12-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00666}. CC -!- SIMILARITY: Contains 1 B12-binding N-terminal domain. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC -!- SIMILARITY: Contains 1 pterin-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00334}. CC ----------------------------------------------------------------------- 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; BAC95724.1; -; Genomic_DNA. DR RefSeq; NP_935753.1; NC_005139.1. DR RefSeq; WP_011151258.1; NC_005139.1. DR ProteinModelPortal; Q7MHB1; -. DR SMR; Q7MHB1; 654-1224. DR STRING; 196600.VV2960; -. DR PRIDE; Q7MHB1; -. DR EnsemblBacteria; BAC95724; BAC95724; BAC95724. DR GeneID; 2625802; -. DR KEGG; vvy:VV2960; -. DR PATRIC; 20172780; VBIVibVul40472_2940. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; VVUL196600:GJ9W-3052-MONOMER; -. DR UniPathway; UPA00051; UER00081. DR Proteomes; UP000002675; Chromosome I. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Cobalamin; Cobalt; Complete proteome; KW Metal-binding; Methionine biosynthesis; Methyltransferase; Repeat; KW S-adenosyl-L-methionine; Transferase; Zinc. FT CHAIN 1 1226 Methionine synthase. FT /FTId=PRO_0000204543. FT DOMAIN 6 326 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT DOMAIN 357 618 Pterin-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00334}. FT DOMAIN 651 745 B12-binding N-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00666}. FT DOMAIN 747 882 B12-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00666}. FT DOMAIN 898 1226 AdoMet activation. {ECO:0000255|PROSITE- FT ProRule:PRU00346}. FT REGION 835 836 Cobalamin-binding. {ECO:0000250}. FT REGION 1191 1192 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT METAL 248 248 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 311 311 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 312 312 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000250}. FT BINDING 805 805 Cobalamin. {ECO:0000250}. FT BINDING 948 948 S-adenosyl-L-methionine. {ECO:0000250}. FT BINDING 1136 1136 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000250}. FT BINDING 1140 1140 Cobalamin; via carbonyl oxygen. FT {ECO:0000250}. SQ SEQUENCE 1226 AA; 136333 MW; 299B647CC6D24028 CRC64; MGSNIRAQIE AQLKQRILLI DGGMGTMIQG YKLQEQDYRG ERFADWHSDL KGNNDLLVLT QPQLIKEIHH AYLEAGADIL ETNTFNATTI AMADYDMESL SEEINFAAAK LAREAADEWT AKNPAKPRYV AGVLGPTNRT CSISPDVNDP GYRNVSFDEL VEAYSESTRA LIRGGSDLIL IETIFDTLNA KACAFAVESV FEELGFALPV MISGTITDAS GRTLSGQTTE AFYNSLRHVR PISFGLNCAL GPDELRPYVE ELSRISETFV STHPNAGLPN AFGEYDLSPE EMAEHVKEWA QSGFLNLIGG CCGTTPEHIR HMAMAVEGES PRVLPEIPVA CRLSGLEPLT IAKDTLFVNV GERTNVTGSA RFKRLIKEEL YDEALDVARE QVENGAQIID INMDEGMLDA EACMVRFLNL CASEPEISKV PIMVDSSKWE VIEAGLKCIQ GKGIVNSISL KEGKEKFVEQ AKLIRRYGAA VIVMAFDEVG QADTRERKLE ICTKAYRILV DEVGFPPEDV IFDPNIFAVA TGIDEHNNYA VDFIEAVADI KRDLPHAMIS GGVSNVSFSF RGNNYVREAI HAVFLYHCFK NGMDMGIVNA GQLEIYDNVP EKLREAVEDV VLNRRDDATE RLLEIAEEYR ENAVGKQEDA SALEWRTWSV EKRLEHALVK GITEFIVEDT EEARLNASKP LEVIEGPLMD GMNVVGDLFG EGKMFLPQVV KSARVMKQAV AHLEPFINAS KQVGSSNGKI LLATVKGDVH DIGKNIVGVV LQCNNYEIID LGVMVPCEQI LKVAKEQQVD IIGLSGLITP SLDEMVHVAK EMERLGFDLP LLIGGATTSK AHTAVKIEQN YSHPVVYVNN ASRAVGVCTS LLSDELRPAF VERLQADYEL VRDQHNRKKP RTKPVTLEAA RANKVAIDWQ SYTPPAPSQP GVHVFDDFDV ATLRQYIDWT PFFLTWSLVG KYPTIFEHEE VGEEAKRLFE DANEWLDRIE QEGLLKARGM CGLFPAASVG DDIEVYTDES RTQVAKVLHN LRQQTEKPKG ANYCLSDYVA PKESGKKDWI GAFAVTGGVN ERELADQFKA QGDDYNAIMI QAVADRLAEA FAEYLHERVR KEIWGYAADE NLSNEELIRE KYQGIRPAPG YPACPEHTEK GPLWELLNVE ETIGMSLTSS YAMWPGASVS GWYFSHPDSR YFAIAQIQQD QVESYAKRKG WDLLEAEKWL GPNING // ID MHT1_YEAST Reviewed; 324 AA. AC Q12525; D6VXU7; DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 29-APR-2015, entry version 97. DE RecName: Full=Homocysteine S-methyltransferase 1; DE EC=2.1.1.10; DE AltName: Full=S-methylmethionine:homocysteine methyltransferase 1; DE Short=SMM:Hcy S-methyltransferase 1; GN Name=MHT1; OrderedLocusNames=YLL062C; ORFNames=L0552; 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=ATCC 204511 / S288c / AB972; RA Wedler H., Wambutt R.; RT "Sequence of a 37 kb DNA fragment from chromosome XII of Saccharomyces RT cerevisiae including the subtelomeric region of the left arm."; RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169871; RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., RA Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., RA Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., RA Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., RA Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., RA Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., RA Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., RA Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., RA Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., RA Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., RA Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., RA Hani J., Hoheisel J.D.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."; RL Nature 387:87-90(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). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., RA Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., RA Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., RA Kolodner R.D., LaBaer J.; RT "Approaching a complete repository of sequence-verified protein- RT encoding clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [5] RP FUNCTION. RX PubMed=11013242; DOI=10.1074/jbc.M005967200; RA Thomas D., Becker A., Surdin-Kerjan Y.; RT "Reverse methionine biosynthesis from S-adenosylmethionine in RT eukaryotic cells."; RL J. Biol. Chem. 275:40718-40724(2000). RN [6] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [7] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). CC -!- FUNCTION: Homocysteine S-methyltransferase involved in the CC conversion of S-adenosylmethionine (AdoMet) to methionine to CC control the methionine/AdoMet ratio. Also converts S- CC methylmethionine (SMM) to methionine. CC {ECO:0000269|PubMed:11013242}. CC -!- CATALYTIC ACTIVITY: S-methyl-L-methionine + L-homocysteine = 2 L- CC methionine. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00333}; CC -!- INTERACTION: CC Q12043:TGL5; NbExp=1; IntAct=EBI-37133, EBI-34845; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. CC -!- MISCELLANEOUS: Present with 606 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z47973; CAA87995.1; -; Genomic_DNA. DR EMBL; Z73167; CAA97515.1; -; Genomic_DNA. DR EMBL; AY558194; AAS56520.1; -; Genomic_DNA. DR EMBL; BK006945; DAA09263.1; -; Genomic_DNA. DR PIR; S50958; S50958. DR RefSeq; NP_013038.1; NM_001181882.1. DR ProteinModelPortal; Q12525; -. DR SMR; Q12525; 3-313. DR BioGrid; 31254; 12. DR DIP; DIP-1934N; -. DR IntAct; Q12525; 3. DR MINT; MINT-397842; -. DR STRING; 4932.YLL062C; -. DR MaxQB; Q12525; -. DR PaxDb; Q12525; -. DR EnsemblFungi; YLL062C; YLL062C; YLL062C. DR GeneID; 850664; -. DR KEGG; sce:YLL062C; -. DR CYGD; YLL062c; -. DR EuPathDB; FungiDB:YLL062C; -. DR SGD; S000003985; MHT1. DR eggNOG; COG2040; -. DR GeneTree; ENSGT00510000049619; -. DR HOGENOM; HOG000066018; -. DR InParanoid; Q12525; -. DR KO; K00547; -. DR OMA; SEWCKDG; -. DR OrthoDB; EOG7X9GHR; -. DR BioCyc; YEAST:YLL062C-MONOMER; -. DR NextBio; 966638; -. DR PRO; PR:Q12525; -. DR Proteomes; UP000002311; Chromosome XII. DR Genevestigator; Q12525; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IDA:SGD. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0000096; P:sulfur amino acid metabolic process; IMP:SGD. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 1: Evidence at protein level; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; Metal-binding; KW Methionine biosynthesis; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase; Zinc. FT CHAIN 1 324 Homocysteine S-methyltransferase 1. FT /FTId=PRO_0000114618. FT DOMAIN 6 320 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 238 238 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 305 305 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 306 306 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. SQ SEQUENCE 324 AA; 36715 MW; A77194694B6E5C14 CRC64; MKRIPIKELI VEHPGKVLIL DGGQGTELEN RGININSPVW SAAPFTSESF WEPSSQERKV VEEMYRDFMI AGANILMTIT YQANFQSISE NTSIKTLAAY KRFLDKIVSF TREFIGEERY LIGSIGPWAA HVSCEYTGDY GPHPENIDYY GFFKPQLENF NQNRDIDLIG FETIPNFHEL KAILSWDEDI ISKPFYIGLS VDDNSLLRDG TTLEEISVHI KGLGNKINKN LLLMGVNCVS FNQSALILKM LHEHLPGMPL LVYPNSGEIY NPKEKTWHRP TNKLDDWETT VKKFVDNGAR IIGGCCRTSP KDIAEIASAV DKYS // ID MMUM_ECOLI Reviewed; 310 AA. AC Q47690; P77226; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 27-MAY-2015, entry version 104. DE RecName: Full=Homocysteine S-methyltransferase; DE EC=2.1.1.10; DE AltName: Full=S-methylmethionine:homocysteine methyltransferase; GN Name=mmuM; Synonyms=yagD; OrderedLocusNames=b0261, JW0253; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.; RT "Systematic sequencing of the Escherichia coli genome: analysis of the RT 4.0 - 6.0 min (189,987 - 281,416bp) region."; RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.; RT "Sequence of minutes 4-25 of Escherichia coli."; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. 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], AND SEQUENCE REVISION RP TO 123; 130; 142 AND 159. 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. RX PubMed=9882684; RA Thanbichler M., Neuhierl B., Boeck A.; RT "S-methylmethionine metabolism in Escherichia coli."; RL J. Bacteriol. 181:662-665(1999). RN [6] RP SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT. RC STRAIN=K12 / JM109 / ATCC 53323; RX PubMed=10026151; DOI=10.1074/jbc.274.9.5407; RA Neuhierl B., Thanbichler M., Lottspeich F., Boeck A.; RT "A family of S-methylmethionine-dependent thiol/selenol RT methyltransferases. Role in selenium tolerance and evolutionary RT relation."; RL J. Biol. Chem. 274:5407-5414(1999). CC -!- FUNCTION: Catalyzes methyl transfer from S-methylmethionine or S- CC adenosylmethionine (less efficient) to homocysteine, CC selenohomocysteine and less efficiently selenocysteine. CC {ECO:0000269|PubMed:9882684}. CC -!- CATALYTIC ACTIVITY: S-methyl-L-methionine + L-homocysteine = 2 L- CC methionine. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00333}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.045 mM for L-homocysteine {ECO:0000269|PubMed:10026151}; CC KM=0.59 mM for L-selenocysteine {ECO:0000269|PubMed:10026151}; CC KM=0.043 mM for DL-selenohomocysteine CC {ECO:0000269|PubMed:10026151}; CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10026151}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U70214; AAB08682.1; -; Genomic_DNA. DR EMBL; U00096; AAC73364.1; -; Genomic_DNA. DR EMBL; AP009048; BAA77929.2; -; Genomic_DNA. DR PIR; E64751; E64751. DR RefSeq; NP_414795.1; NC_000913.3. DR RefSeq; YP_001816637.1; NC_010558.1. DR ProteinModelPortal; Q47690; -. DR SMR; Q47690; 11-307. DR IntAct; Q47690; 5. DR STRING; 511145.b0261; -. DR EnsemblBacteria; AAC73364; AAC73364; b0261. DR EnsemblBacteria; BAA77929; BAA77929; BAA77929. DR GeneID; 6275998; -. DR GeneID; 946143; -. DR KEGG; ecj:Y75_p0252; -. DR KEGG; eco:b0261; -. DR KEGG; pg:6275998; -. DR PATRIC; 32115641; VBIEscCol129921_0264. DR EcoGene; EG13343; mmuM. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR InParanoid; Q47690; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR PhylomeDB; Q47690; -. DR BioCyc; EcoCyc:MMUM-MONOMER; -. DR BioCyc; ECOL316407:JW0253-MONOMER; -. DR BioCyc; MetaCyc:MMUM-MONOMER; -. DR BRENDA; 2.1.1.10; 2026. DR BRENDA; 2.1.1.280; 2026. DR PRO; PR:Q47690; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR Genevestigator; Q47690; -. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IDA:EcoCyc. DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0033528; P:S-methylmethionine cycle; IBA:GO_Central. DR GO; GO:0033477; P:S-methylmethionine metabolic process; IMP:EcoCyc. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 1: Evidence at protein level; KW Amino-acid biosynthesis; Complete proteome; Metal-binding; KW Methionine biosynthesis; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase; Zinc. FT CHAIN 1 310 Homocysteine S-methyltransferase. FT /FTId=PRO_0000114610. FT DOMAIN 1 310 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 229 229 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 295 295 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 296 296 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. SQ SEQUENCE 310 AA; 33423 MW; 8381CFF475E5FB7A CRC64; MSQNNPLRAL LDKQDILLLD GAMATELEAR GCNLADSLWS AKVLVENPEL IREVHLDYYR AGAQCAITAS YQATPAGFAA RGLDEAQSKA LIGKSVELAR KAREAYLAEN PQAGTLLVAG SVGPYGAYLA DGSEYRGDYH CSVEAFQAFH RPRVEALLDA GADLLACETL PNFSEIEALA ELLTAYPRAR AWFSFTLRDS EHLSDGTPLR DVVALLAGYP QVVALGINCI ALENTTAALQ HLHGLTVLPL VVYPNSGEHY DAVSKTWHHH GEHCAQLADY LPQWQAAGAR LIGGCCRTTP ADIAALKARS // ID O53185_MYCTU Unreviewed; 302 AA. AC O53185; I6XED1; L0T9V7; DT 01-JUN-1998, integrated into UniProtKB/TrEMBL. DT 01-JUN-1998, sequence version 1. DT 27-MAY-2015, entry version 87. DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:AIR15225.1}; DE SubName: Full=MmuM protein {ECO:0000313|EMBL:CCP45251.1}; GN Name=mmuM {ECO:0000313|EMBL:CCP45251.1}; GN OrderedLocusNames=Rv2458 {ECO:0000313|EMBL:CCP45251.1}; GN ORFNames=LH57_13435 {ECO:0000313|EMBL:AIR15225.1}; OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=83332 {ECO:0000313|EMBL:CCP45251.1, ECO:0000313|Proteomes:UP000031768}; RN [1] {ECO:0000313|EMBL:CCP45251.1, ECO:0000313|Proteomes:UP000001584} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25618 / H37Rv {ECO:0000313|Proteomes:UP000001584}, and RC H37Rv {ECO:0000313|EMBL:CCP45251.1}; 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] {ECO:0000313|EMBL:CCP45251.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=H37Rv {ECO:0000313|EMBL:CCP45251.1}; RX PubMed=12368430; RA Camus J.C., Pryor M.J., Medigue C., Cole S.T.; RT "Re-annotation of the genome sequence of Mycobacterium tuberculosis RT H37Rv."; RL Microbiology 148:2967-2973(2002). RN [3] {ECO:0000213|PubMed:21969609} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21969609; DOI=10.1074/mcp.M111.011445; RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., RA Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H., RA Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., RA Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S., RA Dash D., Pandey A.; RT "Proteogenomic analysis of Mycobacterium tuberculosis by high RT resolution mass spectrometry."; RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011). RN [4] {ECO:0000313|EMBL:CCP45251.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=H37Rv {ECO:0000313|EMBL:CCP45251.1}; RX PubMed=20980199; DOI=10.1016/j.tube.2010.09.008; RA Lew J.M., Kapopoulou A., Jones L.M., Cole S.T.; RT "TubercuList--10 years after."; RL Tuberculosis 91:1-7(2011). RN [5] {ECO:0000313|EMBL:CCP45251.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=H37Rv {ECO:0000313|EMBL:CCP45251.1}; RA Lew J.M.; RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000313|EMBL:AIR15225.1, ECO:0000313|Proteomes:UP000031768} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27294 / TMC 102 / H37Rv RC {ECO:0000313|Proteomes:UP000031768}, and RC H37Rv {ECO:0000313|EMBL:AIR15225.1}; RA Hazbon M.H., Riojas M.A., Damon A.M., Alalade R.O., Cantwell B.J., RA Monaco A., King S., Sohrabi A.; RT "Phylogenetic analysis of Mycobacterial species using whole genome RT sequences."; RL Submitted (SEP-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; CP009480; AIR15225.1; -; Genomic_DNA. DR EMBL; AL123456; CCP45251.1; -; Genomic_DNA. DR RefSeq; NP_216974.1; NC_000962.3. DR RefSeq; WP_003911868.1; NZ_KK339370.1. DR RefSeq; YP_006515895.1; NC_018143.2. DR ProteinModelPortal; O53185; -. DR SMR; O53185; 2-300. DR STRING; 83332.Rv2458; -. DR EnsemblBacteria; AFN50424; AFN50424; RVBD_2458. DR EnsemblBacteria; CCP45251; CCP45251; Rv2458. DR EnsemblBacteria; KBJ30785; KBJ30785; P425_02558. DR GeneID; 885871; -. DR KEGG; mtu:Rv2458; -. DR KEGG; mtv:RVBD_2458; -. DR PATRIC; 18154065; VBIMycTub87468_2756. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; YGRSVTK; -. DR OrthoDB; EOG6C019S; -. DR PhylomeDB; O53185; -. DR BioCyc; MTBRV:RV2458-MONOMER; -. DR Proteomes; UP000001584; Chromosome. DR Proteomes; UP000031768; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000001584}; KW Methyltransferase {ECO:0000313|EMBL:AIR15225.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001584}; KW Transferase {ECO:0000313|EMBL:AIR15225.1}. SQ SEQUENCE 302 AA; 31593 MW; 721C9D2DDF7F29CC CRC64; MELVSDSVLI SDGGLATELE ARGHDLSDPL WSARLLVDAP HAITAVHTAY FRAGAQIATT ASYQASFEGF AARGIGHDDA TVLLRRSVEL AQAARDEVGV GGLSVAASVG PYGAALADGS EYRGYYGLSV AALMKWHLPR LEVLVDAGAD MLALETIPDI DEAEALVNLV RRLATPAWLS YTINGTRTRA GQPLTDAFAV AAGVPEIVAV GVNCCAPDDV LPAIAFAVAH TGKPVIVYPN SGEGWDGRRR AWVGPRRFSG SSGQLAREWV AAGARIVGGC CRVRPIDIAE IGRALTTAPP RG // ID P74718_SYNY3 Unreviewed; 351 AA. AC P74718; DT 01-FEB-1997, integrated into UniProtKB/TrEMBL. DT 01-FEB-1997, sequence version 1. DT 27-MAY-2015, entry version 78. DE SubName: Full=Slr1189 protein {ECO:0000313|EMBL:BAA18837.1}; GN OrderedLocusNames=slr1189 {ECO:0000313|EMBL:BAA18837.1}; OS Synechocystis sp. (strain PCC 6803 / Kazusa). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechocystis. OX NCBI_TaxID=1111708 {ECO:0000313|Proteomes:UP000001425}; RN [1] {ECO:0000313|EMBL:BAA18837.1, ECO:0000313|Proteomes:UP000001425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 6803 / Kazusa {ECO:0000313|Proteomes:UP000001425}; 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 ----------------------------------------------------------------------- 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; BAA18837.1; -; Genomic_DNA. DR PIR; S76925; S76925. DR RefSeq; YP_005653084.1; NC_017277.1. DR RefSeq; YP_007452900.1; NC_020286.1. DR ProteinModelPortal; P74718; -. DR IntAct; P74718; 1. DR STRING; 1148.slr1189; -. DR PaxDb; P74718; -. DR EnsemblBacteria; BAA18837; BAA18837; BAA18837. DR KEGG; syn:slr1189; -. DR PATRIC; 23843906; VBISynSp132158_3483. DR eggNOG; COG2040; -. DR HOGENOM; HOG000179103; -. DR InParanoid; P74718; -. DR OMA; CCGTDHR; -. DR PhylomeDB; P74718; -. DR Proteomes; UP000001425; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001425}; KW Reference proteome {ECO:0000313|Proteomes:UP000001425}. SQ SEQUENCE 351 AA; 38413 MW; 9076B6A3FA02F613 CRC64; MGGTTGGGSN PCGHESSTLS PSPFLVKTII ANDKLAVKMT NLPHQCEQIF LLDGGLETEM IFNRGFDLPA FAAHTLLSDP LGREALKNYF HGFLDLAKEK QFGFLIDAPT WRAQPFFAEE LGVSLEEIRQ ANFRAVEFAR ALKQAYVNEI QPLLINGLIG PCGDAYGGEH FSNAEAAQVY HRQQISWLAE AGVDLLGAFT LTSVNEAIGI VRASQEFSLP VSISFTVETD GRLPTGTALS EAIAIVDEAT NQGAAYFMVN CAHPDHFRAV IREEAWLSRL GGFRCNPSRR SHAQLDQANF LDIGNPVELA HSYWTLKQKV PSANVFGACC GSDLRHIREI AKVFDEKISK I // ID Q01QP4_SOLUE Unreviewed; 622 AA. AC Q01QP4; DT 14-NOV-2006, integrated into UniProtKB/TrEMBL. DT 14-NOV-2006, sequence version 1. DT 27-MAY-2015, entry version 54. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=Acid_7115 {ECO:0000313|EMBL:ABJ88026.1}; OS Solibacter usitatus (strain Ellin6076). OC Bacteria; Acidobacteria; Solibacteres; Solibacterales; OC Solibacteraceae; Candidatus Solibacter. OX NCBI_TaxID=234267 {ECO:0000313|EMBL:ABJ88026.1, ECO:0000313|Proteomes:UP000000671}; RN [1] {ECO:0000313|Proteomes:UP000000671} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ellin6076 {ECO:0000313|Proteomes:UP000000671}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ABJ88026.1; -; Genomic_DNA. DR RefSeq; WP_011688745.1; NC_008536.1. DR RefSeq; YP_828311.1; NC_008536.1. DR ProteinModelPortal; Q01QP4; -. DR STRING; 234267.Acid_7115; -. DR EnsemblBacteria; ABJ88026; ABJ88026; Acid_7115. DR KEGG; sus:Acid_7115; -. DR PATRIC; 32016946; VBICanSol30224_7422. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; SUSI234267:GHSK-7166-MONOMER; -. DR Proteomes; UP000000671; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000671}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ABJ88026.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000000671}; KW Transferase {ECO:0000313|EMBL:ABJ88026.1}. SQ SEQUENCE 622 AA; 67727 MW; D660B6FFD527D64E CRC64; MNTTTSSRAQ EFRDQLARRV IVADGAMGTM LYSRGVFINR CFDELNLSAA DMVRQIHQEY VKAGAEILET NTFGATRQRL GAFGFAEKLQ AINHAGVRLA REAANGSAYV AGAVGPLNVR IEPLGPTSFA EARAAFREQI DALLEAGVDL LIFETFGNLD ELREAVYAGY DASRGEVPMI AQVTIDDFGH LPGGTDTETF TREMNNWPVD VIGLNCSVGP KATLETVERM MEFATKPLSA MPNAGLPMRV EGRNIYLCSP EYMSQYARRL LWAGVKVIGG CCGTTPDHIK LIRSETRSLQ PLQKQLAVTV EEPKVKAQAL QPVPVAEKSQ VGAKLAAGKF VTFVEILPPR GVDATREIAG AKLCAEHGID AINVPDGPRA SARMSAQVTC QLIQAQAGIE AVNHFCCRDR NILGIQSELL GTHGAGVRNL ICITGDPPRM GAYPDATAVF DVDAIGLVNI VRNLNHGLDI GGNPMGSQTA LLIGVGANPG ALNMDEEIRR FEWKVEAGAE YVVTQPVFDL DLLEAFLKRI EHVKIPVLCG IWPLTSYRNA EFMVNELRVP VPEMFMERMR RVDNAEKARE EGVAIAREMV ARVSKMVQGA QLSAPFGRYQ MAIDVADAIE SR // ID Q01YW7_SOLUE Unreviewed; 1185 AA. AC Q01YW7; DT 14-NOV-2006, integrated into UniProtKB/TrEMBL. DT 14-NOV-2006, sequence version 1. DT 27-MAY-2015, entry version 65. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABJ85148.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABJ85148.1}; GN OrderedLocusNames=Acid_4184 {ECO:0000313|EMBL:ABJ85148.1}; OS Solibacter usitatus (strain Ellin6076). OC Bacteria; Acidobacteria; Solibacteres; Solibacterales; OC Solibacteraceae; Candidatus Solibacter. OX NCBI_TaxID=234267 {ECO:0000313|EMBL:ABJ85148.1, ECO:0000313|Proteomes:UP000000671}; RN [1] {ECO:0000313|Proteomes:UP000000671} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ellin6076 {ECO:0000313|Proteomes:UP000000671}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000473; ABJ85148.1; -; Genomic_DNA. DR RefSeq; WP_011685902.1; NC_008536.1. DR RefSeq; YP_825433.1; NC_008536.1. DR ProteinModelPortal; Q01YW7; -. DR STRING; 234267.Acid_4184; -. DR EnsemblBacteria; ABJ85148; ABJ85148; Acid_4184. DR KEGG; sus:Acid_4184; -. DR PATRIC; 32010822; VBICanSol30224_4376. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SUSI234267:GHSK-4220-MONOMER; -. DR Proteomes; UP000000671; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000671}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABJ85148.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000671}; KW Transferase {ECO:0000313|EMBL:ABJ85148.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 231 231 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1185 AA; 130138 MW; B6AF9D50E31030A7 CRC64; MTNFLERQKA LNDSLEQRVL VLDGAMGTMI HQAPLSIETD YLGRENCPEI LNVTRPDVIQ DIHRQYLEAG ADIIETNTFG GTRIALADNK LEERAYELNF AAAKLAREVA DQFSTAAKPR FVAGSIGPTN KDLNITGSTT FPEIKAAYYE QAKGLVEGGA DYLLIETCFD TGSLKAGLVA VEQLGRELAI QIPVVASVTI ERTGTMLGGQ QIDALYASIG NHELLGVGMN CATGPDLMTD HIRTLNEMSA HRISCYPNAG LPNAEGKFGE TPDSLAAQLE KFANQGWLNF VGGCCGTTPA HIQAIAQMIQ GKRPRATPAS KHRAYYSGID LVEAEDSNRP LLVGERTNVI GSRLFKNLIA DEKWEEATDI ARRQVRNGAH VIDVCLQSTD REELEDIRPF YEKLIRKIKA PIMIDTTDPK AVELALTYCQ GKSIINSVNL EDGEEKFERL CPIAKLYGAA LVVGSIDEDK LQAQAFTRER KVAVAERSYR LLTEKYGIPG EDIIIDPLVF PCATGDVNYI GGAVETIEGI RLVKQALPYA KTVLGISNIS FGLPAAAREV VNSVFLYYCT KAGLDLAIVN AEKLERFASI PEEERRLAEH LLFNTPPAGA EDESLRTAAE DWRAQSPEQK AAINQFHIAA IAEHFRKAGA RVKKAAADMP LDQRLANYII EGTKDGLIAD LDRKRAEGAT PLEIINGPLM AGMSEVGRLF NNNELIVAEV LQSAEAMKAA VNHLEQFMEK ADTAARGKVL LATVKGDVHD IGKNLVEIIL ANNGYEVINL GIKVPPDVLI QAFREHMPDA IGLSGLLVKS TQQMVITATD LKAAGIDVPL LVGGAALSEK FTRTKIGPAY SEAVCYAKDA MTGLSLMNRL MDPAEREALI ATSTTLEAPA AVEAPAEPLG PLSTRRSRKV RTELPVPPAP YLERKVRDVP NLADVWSYIN PFMIYGRHLG YKGNFEKALA EHEEKALELF HNVEELKHEA AQFMHVKAVW QFFEAERDGN AIHLFAPGGA SPIHTFRFGR QRREDGLCLS DYILDSPDGK RDHLALFVTT AGAGIRERSE QWKKAGEFFK AHAIQALAIE TAEATAEWLH RRIREDWGFP DPPTTTMHDR FTSKYHGKRY SFGYPACPNL DDQQGVWKLI NPDDIGVKLT EGMMMEPEAS VSAIVFHHPD CAYFTADEGE SEATA // ID Q024B4_SOLUE Unreviewed; 304 AA. AC Q024B4; DT 14-NOV-2006, integrated into UniProtKB/TrEMBL. DT 14-NOV-2006, sequence version 1. DT 27-MAY-2015, entry version 43. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABJ83662.1}; GN OrderedLocusNames=Acid_2673 {ECO:0000313|EMBL:ABJ83662.1}; OS Solibacter usitatus (strain Ellin6076). OC Bacteria; Acidobacteria; Solibacteres; Solibacterales; OC Solibacteraceae; Candidatus Solibacter. OX NCBI_TaxID=234267 {ECO:0000313|EMBL:ABJ83662.1, ECO:0000313|Proteomes:UP000000671}; RN [1] {ECO:0000313|Proteomes:UP000000671} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ellin6076 {ECO:0000313|Proteomes:UP000000671}; 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; CP000473; ABJ83662.1; -; Genomic_DNA. DR RefSeq; WP_011684428.1; NC_008536.1. DR RefSeq; YP_823947.1; NC_008536.1. DR ProteinModelPortal; Q024B4; -. DR STRING; 234267.Acid_2673; -. DR EnsemblBacteria; ABJ83662; ABJ83662; Acid_2673. DR KEGG; sus:Acid_2673; -. DR PATRIC; 32007648; VBICanSol30224_2798. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265278; -. DR KO; K00548; -. DR OMA; GTNLFAM; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SUSI234267:GHSK-2699-MONOMER; -. DR Proteomes; UP000000671; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000671}; KW Methyltransferase {ECO:0000313|EMBL:ABJ83662.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000671}; KW Transferase {ECO:0000313|EMBL:ABJ83662.1}. SQ SEQUENCE 304 AA; 32584 MW; E6D8A4CE8F07C34F CRC64; MNEPLQDVIR RRPLLGDGAM GTQLMFAGLE QGNCGELWNL THPERVLGIQ RRYAEAGSDC ILTNTFGGSR IMLNRHGSSG KVVEINRAAV EIAREAFGGR AGYVIGDIGP FGGLMQPYGD FTEEDVRSAF GEQAGALVDA GADAIIIETQ TSLEELQLGI EAAREAGAPC VIGSMAYDVT LDGSTFRTMM GVDPERAAGF MQEHDADIVA LNCGTGMDMA RAREAVLRYR KATDLPVMVQ PNAGVPKLIS MKVVYDETPE QMASGVAPLL CAGANIIGAC CGSTPEHIRA FRAEMDKFYE NQTL // ID Q04NN4_LEPBJ Unreviewed; 1247 AA. AC Q04NN4; DT 14-NOV-2006, integrated into UniProtKB/TrEMBL. DT 14-NOV-2006, sequence version 1. DT 27-MAY-2015, entry version 67. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABJ77486.1}; GN Name=metH {ECO:0000313|EMBL:ABJ77486.1}; GN OrderedLocusNames=LBJ_4091 {ECO:0000313|EMBL:ABJ77486.1}; OS Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197). OC Bacteria; Spirochaetes; Spirochaetales; Leptospiraceae; Leptospira. OX NCBI_TaxID=355277 {ECO:0000313|EMBL:ABJ77486.1, ECO:0000313|Proteomes:UP000000656}; RN [1] {ECO:0000313|EMBL:ABJ77486.1, ECO:0000313|Proteomes:UP000000656} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JB197 {ECO:0000313|EMBL:ABJ77486.1, RC ECO:0000313|Proteomes:UP000000656}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000351; ABJ77486.1; -; Genomic_DNA. DR RefSeq; WP_011672173.1; NC_008511.1. DR RefSeq; YP_802244.1; NC_008511.1. DR ProteinModelPortal; Q04NN4; -. DR SMR; Q04NN4; 660-901. DR STRING; 355277.LBJ_4091; -. DR EnsemblBacteria; ABJ77486; ABJ77486; LBJ_4091. DR KEGG; lbj:LBJ_4091; -. DR PATRIC; 22362605; VBILepBor13265_3985. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; LBOR355277:GHYM-3072-MONOMER; -. DR Proteomes; UP000000656; Chromosome 2. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000656}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 255 255 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 318 318 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 319 319 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 769 769 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1247 AA; 138802 MW; 5F206928BF0FF253 CRC64; MTYKVQNYTN RSSQELLGLL EKQILVIDGA MGTMIQRFLL TEDDFRGEVL KNHPHPLKGN NELLCLTRPD VIEAIHIKFL EAGANILETN TFSSNQVSQG DYKTEFLVAD LNKAAVQCAR NAIEKFKRTN RHHPCFLAGA IGPTTRTATL SPDVNNPAFR AVTFEDLVAT FYEQARALVE AGVDLLLPET NIDTLNLKAA IFAIEQVFED LQVRIPVCLS VTITDASGRT LSGQTVEAFY NSIAHCKPLS VGINCALGAD EMRPYIEELA RISSCYISCY PNAGLPNAFG GYDQTPEEFG AYIQEFASSG WLNITGGCCG TTPEHIAAAT KAVQGKKPRI LPQIEEITRL SGLEPLNVTS DKGFLLVGER TNVTGSPKFK KLIIEGNFEE AVSVALQQVE AGANIIDINF DEALLDGEAS MRHFLNLIAG EPDIAKVPFM IDSSKWSVLE EGLKCIQGKP IVNSISLKEG EEKFLEHARK IQRYGASAIV MAFDERGQAA TKDEKVRICK RAYDLLVTKA NFSPTDIIFD PNILTVATGI EEHNNYAVDF IEAVREIKKF CPGAKVSGGL SNVSFSFRGN NPVREAMHSV FLYHAIQAGL DMAIVNAGML AVYEEISKDL LEYVEDVILN RRPDATERLV EFAESIKSSG DKSEKKGEAW REGTTVEERL SYALVKGIVE YIDQDTEEAR LKYGRPLTVI EGPLMDGMKI VGELFGAGKM FLPQVVKSAR VMKKSVAYLL PFMEEEKNQS EDVAARPKFL IATVKGDVHD IGKNIVGVVL ACNNYEVIDL GVMVPSDKIL EEARKHNVNI IGLSGLITPS LDEMVHVASE MKRTGFEIPL LIGGATTSSA HTAVKIAPVY DPPVVHVVDA SRVVNVVNQL LHPDLNEGYA QKIKEDQKTA RENYFNTRAE RKLISLEQAR ENREEIDWTA ATIDKPSFTG IRIFDEEISL ETLIPFIDWT PFFTAWELKG RYPAILESET TGKQARELFA DAQKLMKTIV DGKLFKTKGV IGIFPANSVG DDIEIYENEN RSKLLTVFHT LRQQIQKEDS SEPNYCLADY IAPKNSGRID YIGGFAVTAG HGVEEFAKDF ENHQDDYNSI MAKALGDRFA EAFAEYMHYK VRKEYWGYDK DENLSPEDLI REKYRGIRPA AGYPASPDHT EKRILFDLLQ VEKNTGITLT EHFAMWPASS VSGLYFAHPK SKYFAVAKIN RDQIEEYAKR KVMSVEEVER WLAPNLAYDP LAVSVVR // ID Q05SW6_9SYNE Unreviewed; 1202 AA. AC Q05SW6; DT 14-NOV-2006, integrated into UniProtKB/TrEMBL. DT 14-NOV-2006, sequence version 1. DT 27-MAY-2015, entry version 53. DE SubName: Full=Putative methionine synthase {ECO:0000313|EMBL:EAU73837.1}; GN ORFNames=RS9916_30049 {ECO:0000313|EMBL:EAU73837.1}; OS Synechococcus sp. RS9916. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechococcus. OX NCBI_TaxID=221359 {ECO:0000313|EMBL:EAU73837.1}; RN [1] {ECO:0000313|EMBL:EAU73837.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=RS9916 {ECO:0000313|EMBL:EAU73837.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EAU73837.1}. 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; AAUA01000002; EAU73837.1; -; Genomic_DNA. DR RefSeq; WP_007097944.1; NZ_DS022299.1. DR ProteinModelPortal; Q05SW6; -. DR EnsemblBacteria; EAU73837; EAU73837; RS9916_30049. DR PATRIC; 29884052; VBISynSp14719_0848. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 236 236 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 302 302 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1202 AA; 131225 MW; B13DAA4016F1A36D CRC64; MQAGTIAQTT SRFLDRLHSP ERPVLVFDGA TGTSLQQLNL TAADFGGEEL EGCNENLVVT RPDAVQSVHR LFLDAGCDVI ETDTFGAASV VLAEYGLEDQ AFELNRRAAE LAREVADEYS TDAKPRFVAG SMGPTTKLPT LGHIDFDTLK QAYCEQAEGL LVGGVDLFII ETCQDVLQIK AALQGVMDAF EKRGERRPLM VSVTMETTGT MLVGSDIAAV VAILEPFPID ILGLNCATGP EQMKEHIRYL SECSPFVVSC IPNAGLPENV GGVAHYRLQP LELKMQLMHF VEDLGVQVIG GCCGTTPAHI KALAELSEEL TPAVRPTRLQ HHERPVLKYE PSASSIYGAT SYHQDNSFLI IGERLNASGS KKVRELLNEE DWDGLVAVAR GQVKENAHVL DVNVDYVGRD GESDMRELVS RVVTNINLPL MLDSTEWQKM EAGLKVAGGK CILNSTNFED GDERFFKVLE LAKRYGAGVV VGTIDEDGMA RTAEKKVAIA KRAYRAAVEY GIPAREIFYD PLALPISTGI EEDRRNGLET IEAIRQIRED LPGVHVVLGV SNVSFGLSPA ARITLNSVFL HDCCEAGMDA AIVSPAKILP LIKISEEHQT VCRDLINDNR RFDGDVCVYD PLTELTSLFE GVSAKDARAS GPSLSDLPVE ERLKQHIIDG ERIGLEDALA LGLESYKPLE IVNTFLLDGM KVVGELFGSG QMQLPFVLQS AETMKAAVAY LEPYMEKSDG ERSAKAKFLI ATVKGDVHDI GKNLVDIILT NNGYEVINLG IKQDVGAIIE AQLKHQADCI AMSGLLVKST AFMKDNLQAF NEAGITVPVV LGGAALTPRF VNKDCSEVYN GKVIYGRDAF TDLRFMDAYV NANAENSWDD QQGFLNGTPE GLTLGGDTEA DSDANPETSS MSSDAPVQAA APVTTERSEA VPAEAPITAP FLGSCLLDSS QIPLEEVIAY LDRQALFAGQ WQMRKSKEQS REAYEQELAD KAEPVLQAWL TRIRNEGLLQ PAVAYGYFPC GRRDNSVEVF EPTGDGRLGR FTLPRQRGGN RYCIADFFND VVDDGPSDVL PMQAVTMGEV ASQFSQSLFA ADAYSDYLYF HGLAVQMAEA LAEWTHARIR RECGFSDPDG MPLRDVLAQR YQGSRYSFGY PACPNVGDSR DQLIWLGADR IGLTMDESEQ LHPEQSTTAL VALHSKARYF SA // ID Q067A1_9SYNE Unreviewed; 1208 AA. AC Q067A1; DT 14-NOV-2006, integrated into UniProtKB/TrEMBL. DT 14-NOV-2006, sequence version 1. DT 01-APR-2015, entry version 47. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EAU71726.1}; GN ORFNames=BL107_13000 {ECO:0000313|EMBL:EAU71726.1}; OS Synechococcus sp. BL107. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechococcus. OX NCBI_TaxID=313625 {ECO:0000313|EMBL:EAU71726.1}; RN [1] {ECO:0000313|EMBL:EAU71726.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BL107 {ECO:0000313|EMBL:EAU71726.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EAU71726.1}. 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; AATZ01000001; EAU71726.1; -; Genomic_DNA. DR RefSeq; WP_009789775.1; NZ_DS022298.1. DR ProteinModelPortal; Q067A1; -. DR EnsemblBacteria; EAU71726; EAU71726; BL107_13000. DR PATRIC; 29869182; VBISynSp76518_1668. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EAU71726.1}; KW Transferase {ECO:0000313|EMBL:EAU71726.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 238 238 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 763 763 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1208 AA; 131993 MW; 663345C7F8BAA960 CRC64; MVVTQAKAPV TASRFLDYIH GPTRPVLVFD GATGTSLQDQ GLTADDFGGP DLEGCNENLV ITRPDAVQAV HRQFLDVGCD VIETDTFGAA SIVLAEYGLE DQAFELNRRA AQLARDVADE YSTPEKPRFV AGSMGPTTKL PTLGHIDFDT MRDGFREQAE GLIAGNVDLI IVETCQDVLQ IKAALQGIEA AFESCGERRP LMVSVTMETT GTMLVGSDIA AVVAILEPFP IDILGLNCAT GPEQMKEHIR YLSENSPFIV SCIPNAGLPE NVGGVAHYRL TPTELKMQMM HFVEDLGVQV VGGCCGTTPA HIGALVELAL ELKPAERLSR SKDQKENVRP SFDYEPSAAS IYGVTPYHQD NSFLIIGERL NASGSRKVRE LLAEEDWDGL VGVARGQVKE NAHVLDVNVD YVGRDGEKDM NNLVSRLVTN VNLPLMLDST EWQKMEAGLK VAGGKCILNS TNYEDGDERF FKVLELARRY GAGVVVGTID EDGMARTADK KFAIAQRAYR DALEFGIPAR EIFYDPLALP ISTGIEEDRL NAKATVDSIR MIREGLPGVH VVLGVSNVSF GLSPAARINL NSVFLHDCCE AGMDAAIVSP AKILPLVKIS EEHQQVCRDL INDNRRFENN ICVYDPLTEL TKLFEGVSAK EARASGPSLS DLPIEKRLKQ HIIDGERIGL EPALDQAMND YAPLHIINTF LLDGMKVVGE LFGSGQMQLP FVLQSAETMK SAVAHLEPYM ETIEGESTSK GKFLIATVKG DVHDIGKNLV DIILTNNGYE VVNLGIKQSC DAIVDAQKEH QADCLAMSGL LVKSTAFMKD NLSAFNDAGI DVPVILGGAA LTPRFVQKDC RDVYNGKVIY GRDAFADLRF MDALMDAKKN ANWNNLTGFL ADAPEGVGLD EVVSNESDQA SAQAEVSEPA QPQNQEPVTT ERSSAVPPEP IPAAPFLGSA VLTEADLDLQ EVFTYLDRNA LFAGQWQFRK TKDQSRDDYE AMLAEKAEPV LKHWIERCLN ESLLAPGAVY GYFPVGRDGN ALRVFSSDQS TELGRFDLPR QRSGNRYCIA DFFSDISADG APTDVLPMQA VTMGEKASIV AQELFKGDQY SDYLYFHGLA VQMAEALAEW VHARIRQELG FADPLGMPLR DVLAQRYRGS RYSFGYPACP NVADSRQQLL WLDADRIGLT MDASDQLSPE QSTTALVALH SKARYFSA // ID Q07K32_RHOP5 Unreviewed; 1293 AA. AC Q07K32; DT 31-OCT-2006, integrated into UniProtKB/TrEMBL. DT 31-OCT-2006, sequence version 1. DT 01-APR-2015, entry version 61. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABJ07702.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABJ07702.1}; GN OrderedLocusNames=RPE_3773 {ECO:0000313|EMBL:ABJ07702.1}; OS Rhodopseudomonas palustris (strain BisA53). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Rhodopseudomonas. OX NCBI_TaxID=316055 {ECO:0000313|EMBL:ABJ07702.1, ECO:0000313|Proteomes:UP000000654}; RN [1] {ECO:0000313|EMBL:ABJ07702.1, ECO:0000313|Proteomes:UP000000654} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BisA53 {ECO:0000313|EMBL:ABJ07702.1, RC ECO:0000313|Proteomes:UP000000654}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000463; ABJ07702.1; -; Genomic_DNA. DR RefSeq; WP_011665168.1; NC_008435.1. DR RefSeq; YP_782682.1; NC_008435.1. DR ProteinModelPortal; Q07K32; -. DR SMR; Q07K32; 655-908. DR STRING; 316055.RPE_3773; -. DR EnsemblBacteria; ABJ07702; ABJ07702; RPE_3773. DR KEGG; rpe:RPE_3773; -. DR PATRIC; 23262170; VBIRhoPal93214_3816. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; RPAL316055:GHR9-3812-MONOMER; -. DR Proteomes; UP000000654; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000654}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABJ07702.1}; KW Transferase {ECO:0000313|EMBL:ABJ07702.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 770 770 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1293 AA; 140429 MW; 6305E1A0E26744D2 CRC64; MTVSVSAKRT ALLATARERI LVLDGAMGTM IQRLNFDEAA FRGARYHNFH RDLRGNNDLL ILTQPQAIED IHAQYLRAGA DIVATNTFSS TSIAQADYDM SELAYEMSRD GAKLARNAAA TVEAEDGRPR FVAGAIGPTN RTASISPDVS NPGYRAVTFD DLRIAYSEQI NGLLDGGADL LLVETIFDTL NAKAALYAIA EITEARGIDV PVMISGTITD KSGRLLSGQM PEAFWNSVRH ARPITIGFNC ALGAEDMRAH VADLSRIADT LICAYPNAGL PNEFGQYDES PAHMARIVGE FARDGLVNIV GGCCGTTPDH IAAIAQAVAP HKPRAVPTIE PRLRLSGLEP FELTKDIPFV NVGERTNVTG SARFRKLITE GDYNAALQVA RDQVENGAQI IDVNMDEGLL DSEAAMVTFL NLVAAEPDIA KVPVMVDSSK FNVIEAGLKC LQGKPVVNSI SMKEGEAKFI HEARIAQRHG AAVVVMAFDE QGQADTFARK TEICQRAYRI LVDRLNFPPE DIIFDPNIFA IATGLEEHNN YGVDFIEATR WIRQNLPHAH ISGGVSNLSF SFRGNEPVRE AMHSVFLYHA IKAGMDMGIV NAGQMIVYDD IDPELRQVCE DVILNRDPGA SERLLQLADK YRGQGKQQKE ADLSWREWPV EKRLSHALVH GITEYIEADT EAARLTVARP LHVIEGPLMA GMNVVGDLFG DGKMFLPQVV KSARVMKQAV AYLMPFMEEE KARNLAAGIE GDGRKNAGKI VIATVKGDVH DIGKNIVTIV LQCNNFEVID LGVMVPAATI IEAAKREGAD IIGLSGLITP SLDEMSFLAS EMQRNGLTAP LLIGGATTSR VHTAVKIDPN YPNGSVVHVH DASRAVGVAS SLLSAEKSEA YMAELRADYQ KVAAAHARAQ ADKKRQKLAD ARANAVKIDW AATRPAKPSF LGVKTFSDYS LKELADYIDW TPFFQAWELA GRFPAILDDV VVGEAARALY ADARAMLERI VAENWFTARA AIGFWPANAV GDDIIVYADD SREASITALH TLRQQLEKRE GRANAALSDF VAPRGTADYI GAFVVTAGIG EDVIADKFKN ANDDYSSIMC KALADRLAEA FAERMHQRVR TEFWGTAPDE KLTPDELIAE KYHGIRPAPG YPAQPDHTEK ATLFALLDAE VNAGVTLTES FAMWPGASVS GLYFGHPESY YFGVGKIERD QVQDYAARKG WSVAEAERWL APVLNYVPAR GGPTSEPMPP LAPANDVEDA ASRSAFATEL AGHPAGCGCA VHLRLRGKAV GAK // ID Q086U0_SHEFN Unreviewed; 1238 AA. AC Q086U0; DT 31-OCT-2006, integrated into UniProtKB/TrEMBL. DT 31-OCT-2006, sequence version 1. DT 29-APR-2015, entry version 66. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABI70725.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABI70725.1}; GN OrderedLocusNames=Sfri_0872 {ECO:0000313|EMBL:ABI70725.1}; OS Shewanella frigidimarina (strain NCIMB 400). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=318167 {ECO:0000313|EMBL:ABI70725.1, ECO:0000313|Proteomes:UP000000684}; RN [1] {ECO:0000313|EMBL:ABI70725.1, ECO:0000313|Proteomes:UP000000684} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCIMB 400 {ECO:0000313|EMBL:ABI70725.1, RC ECO:0000313|Proteomes:UP000000684}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000447; ABI70725.1; -; Genomic_DNA. DR RefSeq; WP_011636346.1; NC_008345.1. DR RefSeq; YP_749563.1; NC_008345.1. DR ProteinModelPortal; Q086U0; -. DR SMR; Q086U0; 663-900. DR STRING; 318167.Sfri_0872; -. DR EnsemblBacteria; ABI70725; ABI70725; Sfri_0872. DR KEGG; sfr:Sfri_0872; -. DR PATRIC; 23495589; VBISheFri14343_0903. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SFRI318167:GIXS-912-MONOMER; -. DR Proteomes; UP000000684; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000684}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABI70725.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000684}; KW Transferase {ECO:0000313|EMBL:ABI70725.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 252 252 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 315 315 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 316 316 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 768 768 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1238 AA; 137044 MW; 7159644905D6A584 CRC64; MAKSTSYSQT LKQLNALLAQ RIVILDGAMG TMIQDYKLEE EDYRGERFKD WHCDVKGNND LLVLSQPQII KDIHTQYLLN GADIIETNTF NATTIAMADY DMQSLAAEIN LAGARVARQA ADEVAAQTGS PRYVAGVLGP TNRTCSISPD VNDPGFRNVS FDQLVEAYVE STSALIEGGA DIIMVETIFD TLNAKAALFA IEKVFDQLGD RLPVMISGTI TDASGRTLTG QTTEAFYNSL RHIKPLSIGL NCALGPKELR PYVEELSRIA ECYVSAHPNA GLPNEFGGYD ETPEEMAEVI NQWAQEGMLN IVGGCCGSTP AHINAIREAV LRHEPRQIPD LPVACRLSGL EPLTIDKNSL FVNVGERANV TGSAKFLRLI KEEKFEEALD VVREQVENGA QIIDVNMDEG MLDGVASMAK FLNLIASEPD ISRVPIMIDS SKWEVIEAGL KCVQGKSIVN SISMKEGEAK FIEQATLVKR YGAAAIVMAF DEDGQADTRE RKTQICTRAY RILVDVVGFP PEDIIFDPNI FAIATGIDEH DNYAVDFIES IKDIKATLPH AMISGGVSNV SFSFRGNNPV REAIHAVFLY HAIQAGMDMG IVNAGQLAIY DDIDPELKKR VENVVQNLPC PVADSSNTEQ LLDIAESFRG DGSQVAKKED LAWRSWPVSK RLSHALVKGI TEFIDEDTEA ARLEAVRPLD VIEGSLMDGM NVVGDLFGAG KMFLPQVVKS ARVMKKAVAY LNPYIELEKV AGQSNGRILM VTVKGDVHDI GKNIVGVVLA CNGYEVVDLG VMVSVDKILD AVKEHNIDII GMSGLITPSL DEMVHNVKTF HREGLTIPAI IGGATCSKIH TAVKIAPHYP HGAIYIADAS RAVPMVSKLI NNATRQATID EAYAEYNMMR EKRLSQTKRK TIVSIEAARE NRCKHDWDSY TPFTPNVLGR QVFEDYPLED LVERIDWTPF FRSWELHGHY PEILKDKVVG EEAVKLFADG QAMLKQIIAE KWLTAKAVIG LFPANTVNHD DIELYTDESR TTLEMTTHHL RMQLERVGND NFCLSDFVAP KDSGVADYMG GFAVTTGHGI DEHVARFEAN HDDYNAIMLK CLADRLAEAF AERMHERVRK EFWGYAADEV LDNEALIRER YKGIRPAPGY PACPDHTEKG LLWDLLKPDE TIDLNITESF AMYPTAAVSG WYFAHPKSRY FGVTNIGKDQ VEDYAQRKGM TLAEAEKWLS PILDYDPE // ID Q08RV5_STIAD Unreviewed; 1170 AA. AC Q08RV5; DT 31-OCT-2006, integrated into UniProtKB/TrEMBL. DT 31-OCT-2006, sequence version 1. DT 01-APR-2015, entry version 60. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EAU63221.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EAU63221.1}; DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ADO70586.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ADO70586.1}; GN Name=metH {ECO:0000313|EMBL:EAU63221.1}; GN OrderedLocusNames=STAUR_2788 {ECO:0000313|EMBL:ADO70586.1}; GN ORFNames=STIAU_4100 {ECO:0000313|EMBL:EAU63221.1}; OS Stigmatella aurantiaca (strain DW4/3-1). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Cystobacteraceae; Stigmatella. OX NCBI_TaxID=378806 {ECO:0000313|EMBL:EAU63221.1, ECO:0000313|Proteomes:UP000001351}; RN [1] {ECO:0000313|EMBL:EAU63221.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:EAU63221.1}; RA Nierman W.C.; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000001351} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DW4/3-1 {ECO:0000313|Proteomes:UP000001351}; RA Huntley S., Hamann N., Wegener-Feldbruegge S., Treuner-Lange A., RA Kube M., Reinhardt R., Klages S., Mueller R., Ronning C.M., RA Nierman W.C., Sogaard-Andersen L.; RT "Evolution of fruiting body formation in Myxococcales: a comparative RT genomic analysis."; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:ADO70586.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:ADO70586.1}; RX PubMed=21037205; DOI=10.1093/molbev/msq292; RA Huntley S., Hamann N., Wegener-Feldbrugge S., Treuner-Lange A., RA Kube M., Reinhardt R., Klages S., Muller R., Ronning C.M., RA Nierman W.C., Sogaard-Andersen L.; RT "Comparative genomic analysis of fruiting body formation in RT Myxococcales."; RL Mol. Biol. Evol. 28:1083-1097(2011). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP002271; ADO70586.1; -; Genomic_DNA. DR EMBL; AAMD01000176; EAU63221.1; -; Genomic_DNA. DR RefSeq; WP_002618034.1; NZ_AAMD01000176.1. DR RefSeq; YP_003952413.1; NC_014623.1. DR ProteinModelPortal; Q08RV5; -. DR EnsemblBacteria; ADO70586; ADO70586; STAUR_2788. DR EnsemblBacteria; EAU63221; EAU63221; STIAU_4100. DR KEGG; sur:STAUR_2788; -. DR PATRIC; 38561689; VBIStiAur43712_6829. DR KO; K00548; -. DR BioCyc; SAUR378806:GCZI-2788-MONOMER; -. DR Proteomes; UP000001351; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001351}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EAU63221.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001351}; KW Transferase {ECO:0000313|EMBL:EAU63221.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 738 738 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1170 AA; 127904 MW; 888C1643D8C3765C CRC64; MSHLPAPLPP PPGENGRRIE ALRAAMRERV LVLDGAMGTL IQAQNLKMAD FGGSEYEGCN EHLVLTRPDV IQGIHAEYFA AGADVTETDS FGGTPLVLAE FGLEHKALEI NIQASRLARQ AAADAEAKDG RMRWVAGSIG PTTKAISVTG GITFDELVNQ FAAQTEGLAI GGSDYLLVET CQDTRNVKAA LLGIERAFRK LGYALPVAVS GTIEPMGTML AGQSVESLAA SLEHVELLYL GLNCATGPEF MTDHLRSLSG MSPFAVSCVP NAGLPDENGN YLESPEMLAR SLRRFCEHGW LNVVGGCCGT RPSHIRAIAE AVKGLRPRSA TVRPRSTLSG VDFLEVTDEL RPIIVGERTN VIGSKKFKEL IIAEQYEDAS EVARAQVKRG AQVIDICLAN PDRDELEDMN RFLDVVVKKV RVPLMIDSTD EKVIERALTY CQGKAIINSV NLEDGEERFE KVVPLARQYG AALVVGCIDE VGMAVTRQRK LEVAQRSVEL LTGKYGMKAE DLYFDPLVFP CASGDAQYTG SAVETIEGVR LIKQRFPQCK TVLGISNVSF GLPTAGREVL NSVFLYHCVQ AGLDMALVNS EKLERYPSLP QEERTLAEDL LYNRGADPVT PFAAHFRERK PQKAATSSLP LEERLQRYII EGSRDGLFAD LDLAMEKYGP LEIINGPLMK GMDEVGRLFG ANELIVAEVL QSAESMKAAV GHLEPRMSQT QTATRGKIVL ATVKGDVHDI GKNLVEIILA NNGFQVVNLG IKVPPEQLVQ AVREHRPDML GLSGLLVKSA HQMVATAEDL KRAGVEVPIL VGGAALSRNF VDKNIAPAYS GTVAYAQDAM SGLDLAKQIV DPEGHDKLRQ ELADRRAKLA QEVKDRPKAS APVVPATRSK SVRVLETVPA VPDYERHVLT NTPLDHIWKF INPVMLYGRH LGLRTSSRVL GTPAEAELSK TEEGRKALAL KEAVEELKTF LRGGVMHARA VFQFFKAGSD GNRVLLFDGL TGEQKAAFDF PRQEKEDGLC LADYVLPLEG GKPRDNLGMF VTTAGGGIRE ISEEFKARGE FLKMHAVQAL ALETAEGYAE LLHTQLRSMW GFPDRPEMTM LERFRAEYEG KRYSFGYPAC PRLEDQALLF AALRPEEIGV QLTDGFMMEP EASVSAVVFH HPQAHYFSVT // ID Q0A6R3_ALKEH Unreviewed; 1245 AA. AC Q0A6R3; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 27-MAY-2015, entry version 67. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABI57474.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABI57474.1}; GN OrderedLocusNames=Mlg_2132 {ECO:0000313|EMBL:ABI57474.1}; OS Alkalilimnicola ehrlichii (strain ATCC BAA-1101 / DSM 17681 / MLHE-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Alkalilimnicola. OX NCBI_TaxID=187272 {ECO:0000313|EMBL:ABI57474.1, ECO:0000313|Proteomes:UP000001962}; RN [1] {ECO:0000313|Proteomes:UP000001962} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1101 / DSM 17681 / MLHE-1 RC {ECO:0000313|Proteomes:UP000001962}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000453; ABI57474.1; -; Genomic_DNA. DR RefSeq; WP_011629868.1; NC_008340.1. DR RefSeq; YP_742964.1; NC_008340.1. DR ProteinModelPortal; Q0A6R3; -. DR SMR; Q0A6R3; 667-1244. DR STRING; 187272.Mlg_2132; -. DR PRIDE; Q0A6R3; -. DR EnsemblBacteria; ABI57474; ABI57474; Mlg_2132. DR KEGG; aeh:Mlg_2132; -. DR PATRIC; 20863519; VBIAlkEhr114327_2128. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; AEHR187272:GHAX-2179-MONOMER; -. DR Proteomes; UP000001962; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001962}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABI57474.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001962}; KW Transferase {ECO:0000313|EMBL:ABI57474.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 261 261 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 325 325 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 774 774 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1245 AA; 138782 MW; 00AE452B4F33E5D2 CRC64; MRFPCISRRR SHQTMTDCRK TLEDALARRI LILDSGMGTM IQNRKLEEAD FRGERFADHP CDLKGNNDLL VLTRPEVIRE IHAENLAVGA DIVETNTFSS TTIAQADYRM EHLAYEMNVA AARLAREACD AAERENPDHP RYVAGALGPT NRTASISPDV NNPGYRNITF DQLRAAYLEA ARGLVEGGAD LLLIETIFDT LNAKAAIYAL EELFEEIGRR LPVMISGTIT DASGRTLSGQ TTEAFWNSVR HANPFTVGLN CALGADQMRP FVKEISRVAD TYVTIYPNAG LPNEFGEYDQ TPEEMAAIVR EFAESGFVNV VGGCCGTTPE HIAALREAVA DCVPRPIPER ERAMRLSGLE PFNVGKDSLF VNVGERTNVT GSARFRRLIK EEDYDTALEV AREQVENGAQ IIDINMDEGM LDARACMVDF LNLIAAEPDI ARVPVMIDAS KWEVLEAGLQ CLQGKAVVNS ISLKEGEAPF LEQAEKLKRY GAAVVVMAFD EDGQADTYAR RIEICERAYR LLVDRAGFPP EDIIFDPNVF PVATGIPEHD NYGIDFIEAT RWIKANLPYA KVSGGLSNLS FSFRGNNAVR EAMHSAFLYH AIKAGLDMAI VNAGQIEVYD DIPKDLLERV EDVILNRRED ATERLLAFAE SVKDQGGAKK KEADLAWREL PVNKRLEHAL VKGIVDYIDD DVEEARQAHD RPIEVIEGPL MDGMNVVGDL FGEGKMFLPQ VVKSARVMKK AVAYLLPYIE AEKAEGDDKP AAHILMATVK GDVHDIGKNI VGVVLQCNNF KVTDIGVMQP AEAILETAEK EKVDIIGLSG LITPSLEEMA NVAKEMQRRG LTQPLLIGGA TTSRVHTAVK IAPQYDQEVI YVKDASRAVG VASNLMSETR REAYVAGLRE EYERVRRQHA NRQKKQKWVK IETARANRTP IDWDAFEPAF PNAPGVHVLD DYPLAELVDY IDWTPFFKSW ELAGSYPKIL DDEVVGEQAR TLFHDAKAML AQIIEERWLT ARAVFGLFPA NGVGDDTELY ADEDRAQVLL TLHHLRQQTE KPEGRPHQSL ADFIAPKETG KPDHIGAFAV TTGIGIDEHI ARFEADHDDY HAILLKALAD RLAEAFAERL HERVRKEFWG YAPDEQLDNR GLIKEHYQGI RPAAGYPACP DHTEKDLIWA LLDVDQRIGL TLTESKAMVP TAAVSGLYFA HPKSRYFGIG KIYQDQVEDY ARRKGMSRRA MERWLAPNLG YEPED // ID Q0AIP5_NITEC Unreviewed; 1237 AA. AC Q0AIP5; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 27-MAY-2015, entry version 70. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABI58776.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABI58776.1}; GN OrderedLocusNames=Neut_0500 {ECO:0000313|EMBL:ABI58776.1}; OS Nitrosomonas eutropha (strain C91). OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Nitrosomonadaceae; Nitrosomonas. OX NCBI_TaxID=335283 {ECO:0000313|EMBL:ABI58776.1, ECO:0000313|Proteomes:UP000001966}; RN [1] {ECO:0000313|EMBL:ABI58776.1, ECO:0000313|Proteomes:UP000001966} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C91 {ECO:0000313|EMBL:ABI58776.1, RC ECO:0000313|Proteomes:UP000001966}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000450; ABI58776.1; -; Genomic_DNA. DR RefSeq; WP_011633618.1; NC_008344.1. DR RefSeq; YP_746741.1; NC_008344.1. DR ProteinModelPortal; Q0AIP5; -. DR SMR; Q0AIP5; 649-902. DR STRING; 335283.Neut_0500; -. DR EnsemblBacteria; ABI58776; ABI58776; Neut_0500. DR KEGG; net:Neut_0500; -. DR PATRIC; 22718015; VBINitEut7577_0681. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; NEUT335283:GHT6-512-MONOMER; -. DR Proteomes; UP000001966; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001966}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABI58776.1}; KW Transferase {ECO:0000313|EMBL:ABI58776.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 249 249 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 315 315 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 767 767 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1237 AA; 136817 MW; 71D4F5E011978691 CRC64; MTMSDRADLL KQLLAERILI LDGAMGTMIQ SYKLSESDYR GERFADFPHD LKGNNDLLCL TKPEVIRAIH RAYLEAGSDI IETNTFNSNA PSMADYHMQD LVYELNVAGA RLACEEARAM EAKQPDKPRF VAGVIGPTTK TASLSPDVND PGFRAITFDD LVESYTESVS GLVDGGADIL LVETIFDTLN AKAALFAIEQ YFETHELRLP VMISVTITDA SGRNLSGQTP EAFWNSVRHA RPLSVGINCA LGAELMRPYV QELSNVSEVC TSAHPNAGLP NPLAETGYDE TPEYTARLIK DFAQSGFVNI VGGCCGTTPE HIAAIVEAVQ DIPPRKLPDL PKKLRLSGLE PLSIDESSLF VNVGERTNVT GSKAFARLVL SGNYAEGLVI ARNQVESGAQ IIDINMDEGM LDSQKAMVTF LNLVASEPDI SRLPIMVDSS RWSVIEAGLK CIQGKAIINS ISLKEGEEEF LLHAKLARRY GAAVIVMAFD ESGQADTLQR KVDICTRSYH TLIERADFPP EDIIFDPNIF AIATGIEEHS NYAVDFIEAT RLIRQTLPYA KISGGVSNVS FSFRGNEPIR EAIHTAFLYH AVKAGMTMGI VNAGQLGVYS DIPPDLLERV EDVLLNRRPD ATERLVEFAE NFKGQKKEQA EDLAWRDEPV RQRLIHALVR GINTYIVEDT ELIRQEIDSQ GGKPIEVIEG PLMDGMNVVG DLFGAGKMFL PQVVKSARVM KQAVAYLLPY IEAEKKISGD NKPKGKLVIA TVKGDVHDIG KNIVSVVLQC NNFEVVNLGV MIPSAQILET ARRENADMIG VSGLITPSLE EMAHVAREME REQFTIPLLI GGATTSRVHT AVKIAPHYSG VTIWVPDASR AVGVCSNLMS QDMRDGYIQQ VKAEQEKNRE QHKNKKGPSK LLTFEEARAN AFKTDWNRYT PPAPSFLGLR TLNNYPLETL VPYIDWTPFF QAWELHGRYP AILQDKVVGE AASNLFHDAQ VMLRKIIEQK WLAANAVIGL FPANTVNGDD IEIYADRSRS KVIMTWHSLR QQTTKPSGHP NLALADFIAP RETGINDTIG LFAVSSGFGI DERVRAFEAE NDDYSAIILK ALADRLAEAF AEHMHARVRR EFWGYMKDES LNNEQLIDEQ YLGIRPAPGY PACPDHTEKG PLFAVLEAEK RSGIIVTESF AMVPTAAVSG FYISHPESKY FAVGKIGKDQ VEDYARRKGW ALEKAERWLA PALAYER // ID Q0ALW4_MARMM Unreviewed; 352 AA. AC Q0ALW4; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 27-MAY-2015, entry version 55. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABI66729.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABI66729.1}; GN OrderedLocusNames=Mmar10_2437 {ECO:0000313|EMBL:ABI66729.1}; OS Maricaulis maris (strain MCS10). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Hyphomonadaceae; Maricaulis. OX NCBI_TaxID=394221 {ECO:0000313|EMBL:ABI66729.1, ECO:0000313|Proteomes:UP000001964}; RN [1] {ECO:0000313|EMBL:ABI66729.1, ECO:0000313|Proteomes:UP000001964} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MCS10 {ECO:0000313|EMBL:ABI66729.1, RC ECO:0000313|Proteomes:UP000001964}; 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; ABI66729.1; -; Genomic_DNA. DR RefSeq; WP_011644374.1; NC_008347.1. DR RefSeq; YP_757667.1; NC_008347.1. DR ProteinModelPortal; Q0ALW4; -. DR STRING; 394221.Mmar10_2437; -. DR EnsemblBacteria; ABI66729; ABI66729; Mmar10_2437. DR KEGG; mmr:Mmar10_2437; -. DR PATRIC; 22453064; VBIMarMar77530_2500. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; MMAR394221:GHNB-2488-MONOMER; -. DR Proteomes; UP000001964; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001964}; KW Methyltransferase {ECO:0000313|EMBL:ABI66729.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001964}; KW Transferase {ECO:0000313|EMBL:ABI66729.1}. SQ SEQUENCE 352 AA; 37491 MW; 00A11C28D3A30CA0 CRC64; MTRAARIAAL DAKARTEILI LDGAMGTQIQ DLKLDESGYR GARFAGWHVP VQGNNDILNL SAPEAVKAIH QAYFDAGADI VETNTFSATT IAQADYDMQA VAGDIAREGA RLAREAADEV AARTGTVRGV AGAIGPTNKT LSISPQVNDP GHRDVDFETV RQAYFEQAGA MAPFIDFFLI ETIFDTLNAK AAIKALLDLR AETGEEIPII ISGTITDRSG RTLSGQTASA FWSSVRHARP WAIGLNCALG ADEMRPYVSE LARIADTRII AYPNAGLPND MGEYDETPDQ TARHLGEWAS SGLVNILGGC CGTTPDHIRA IAAAAKPAAP RQPVPSRKAM MLSGLEPFEL AS // ID Q0AX05_SYNWW Unreviewed; 839 AA. AC Q0AX05; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 27-MAY-2015, entry version 65. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABI68749.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABI68749.1}; GN OrderedLocusNames=Swol_1442 {ECO:0000313|EMBL:ABI68749.1}; OS Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Syntrophomonadaceae; OC Syntrophomonas. OX NCBI_TaxID=335541 {ECO:0000313|EMBL:ABI68749.1, ECO:0000313|Proteomes:UP000001968}; RN [1] {ECO:0000313|Proteomes:UP000001968} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2245B / Goettingen {ECO:0000313|Proteomes:UP000001968}; 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 ----------------------------------------------------------------------- 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; ABI68749.1; -; Genomic_DNA. DR RefSeq; WP_011640848.1; NC_008346.1. DR RefSeq; YP_754120.1; NC_008346.1. DR ProteinModelPortal; Q0AX05; -. DR STRING; 335541.Swol_1442; -. DR EnsemblBacteria; ABI68749; ABI68749; Swol_1442. DR KEGG; swo:Swol_1442; -. DR PATRIC; 23857787; VBISynWol51738_1544. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SWOL335541:GHL1-1484-MONOMER; -. DR Proteomes; UP000001968; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001968}; KW Methyltransferase {ECO:0000313|EMBL:ABI68749.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001968}; KW Transferase {ECO:0000313|EMBL:ABI68749.1}. SQ SEQUENCE 839 AA; 91206 MW; 41C244A5BB80C8E1 CRC64; MSPNLYTLLQ SRILILDGAM GTMLQERGMV PGECPELFGV NNPLILEDIH YQYMEAGADI IQSNTFGGNR FKLAEYGLQD RVAEINAEAI RIARAGARGK ALVAASIGPS GKLLQPFGNA DFAELYAAFT EQMLSCEKAG ADLISIETMT DIGEMRAALI AACSNTRLPV IAHMTFEPGG RTLMGTDPLT ALIIMEALQP LAIGANCSGG ARELLPIIEE MGRYSSVFLS VEPNAGLPQL LGERTVFPDR PEEMAEYALK LRDVGANIIG GCCGTTPEHI KAIASTLRGL SPRKRTPRRI RALASRSQAV VLGEGKPLTF IGERINPTAR KKLAQDIKEG RMQMVVDEAR KQVEAGAAIL DVNMGVPGID EAMAMREAVV AVQAAVDVPL ALDSTSAQAI EEGLQSFVGR PLINSTTGED KQLEIILPLA KKYGAAVLGL CLDQNGIPER AEDRVEIARK IFEQAREYGL REEDIYIDCL VKTASAEQSQ VFETLKALRM VKEEMALGTV LGVSNVSHGL PARELLNSTY LAMAWAAGLD LPIMNPFESR MMDANRAAAV LLNRDLNSLE FIEKYKDYKA DKAQDSARIV RPNYCICQQC NIPELLENSE KIPLGVGNKA EEKNMKNPLS TLEIISQAVL QGDKGLLLEQ VQKALDQEKI APMEIVNKAL IPGIERAGEL YDQKKYFLPQ LMLAAESMKD AFTLVKTRLS GEAEEHKGLI VLATVEGDIH DIGKNIVAIL LENYGFKVLD MGKDVKAEVI LDVAEKEKAD IIGLSALMTT TMPRMQEVIQ GVKARGMPCK IMVGGAVLNQ EYADHIGADA YSEDARQAVL MAQRLLGGR // ID Q0B7N8_BURCM Unreviewed; 309 AA. AC Q0B7N8; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 27-MAY-2015, entry version 46. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABI89835.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ABI89835.1}; DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:AJY25809.1}; GN OrderedLocusNames=Bamb_4282 {ECO:0000313|EMBL:ABI89835.1}; GN ORFNames=CH72_4316 {ECO:0000313|EMBL:AJY25809.1}; 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 {ECO:0000313|EMBL:ABI89835.1, ECO:0000313|Proteomes:UP000032631}; 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. RN [2] {ECO:0000313|EMBL:ABI89835.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AMMD {ECO:0000313|EMBL:ABI89835.1}; 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., 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. RN [3] {ECO:0000313|EMBL:AJY25809.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AMMD {ECO:0000313|EMBL:AJY25809.1}; RA Davenport K.W., Gleasner C.D., Chain P.S., Chertkov O., Kunde Y., RA Daligault H.E., McMurry K., Erkkila T., Gu W., Johnson S.L., Lo C.-C., RA Munk C.A., Scholz M.B., Teshima H., Xu Y.; RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; ABI89835.1; -; Genomic_DNA. DR EMBL; CP009799; AJY25809.1; -; Genomic_DNA. DR RefSeq; WP_011659268.1; NC_008391.1. DR RefSeq; YP_776169.1; NC_008391.1. DR ProteinModelPortal; Q0B7N8; -. DR STRING; 339670.Bamb_4282; -. DR EnsemblBacteria; ABI89835; ABI89835; Bamb_4282. DR KEGG; bam:Bamb_4282; -. DR PATRIC; 19024457; VBIBurAmb61564_4485. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; DVITANS; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; BAMB339670:GH48-4353-MONOMER; -. DR Proteomes; UP000000662; Chromosome 2. DR Proteomes; UP000032631; Chromosome 2. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000032631}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ABI89835.1}; KW Transferase {ECO:0000313|EMBL:ABI89835.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 206 206 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 282 282 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 309 AA; 32416 MW; 9812DC2D3590ACF3 CRC64; MHDITVLDGG MGRELARIGA PFRQPEWSAL ALMEAPHYVG LAHDAFVAAG ADVITANSYA VVPFHIGEER FRRDGVALAS LAGQLARQAA DRAGRPVRVA GSLPPTGGSY RPDLFDAARA DAILATLVDG LDSYVDLWLA ETQSLTDEIG AVRRALGDNP KPLWVSFTLR DDVEPGATPV LRSGQPLNEA IDAAVSAGAT ALLFNCSQPE SMGAAIEMVQ RTLAQMGTPL AVGAYANAFP PQRADARANE ELHGLRGDID PPGYARWAEQ WLALGAQIVG GCCGIGPGHI AALRDAVDAR GALHPGFGE // ID Q0BBF2_BURCM Unreviewed; 355 AA. AC Q0BBF2; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 27-MAY-2015, entry version 57. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:AJY22518.1}; DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABI88521.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABI88521.1}; GN OrderedLocusNames=Bamb_2965 {ECO:0000313|EMBL:ABI88521.1}; GN ORFNames=CH72_1821 {ECO:0000313|EMBL:AJY22518.1}; 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 {ECO:0000313|EMBL:ABI88521.1, ECO:0000313|Proteomes:UP000032631}; 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. RN [2] {ECO:0000313|EMBL:ABI88521.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AMMD {ECO:0000313|EMBL:ABI88521.1}; 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., 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 (JAN-2009) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:AJY22518.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AMMD {ECO:0000313|EMBL:AJY22518.1}; RA Davenport K.W., Gleasner C.D., Chain P.S., Chertkov O., Kunde Y., RA Daligault H.E., McMurry K., Erkkila T., Gu W., Johnson S.L., Lo C.-C., RA Munk C.A., Scholz M.B., Teshima H., Xu Y.; RL Submitted (NOV-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; CP000440; ABI88521.1; -; Genomic_DNA. DR EMBL; CP009798; AJY22518.1; -; Genomic_DNA. DR RefSeq; WP_011658053.1; NC_008390.1. DR RefSeq; YP_774855.1; NC_008390.1. DR STRING; 339670.Bamb_2965; -. DR EnsemblBacteria; ABI88521; ABI88521; Bamb_2965. DR KEGG; bam:Bamb_2965; -. DR PATRIC; 19021688; VBIBurAmb61564_3105. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; BAMB339670:GH48-3034-MONOMER; -. DR Proteomes; UP000000662; Chromosome 1. DR Proteomes; UP000032631; Chromosome 1. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000032631}; KW Methyltransferase {ECO:0000313|EMBL:ABI88521.1}; KW Transferase {ECO:0000313|EMBL:ABI88521.1}. SQ SEQUENCE 355 AA; 38349 MW; C05437486F4D0A7A CRC64; MSATPLAASV PLDARYTRGA ELPALLKSRI LILDGAMGTM IQRYKLDEAA YRGERFKDFP RDIKGNNELL SLTQPQIIRE IHDQYFAAGA DIVETNTFGA TTVAQADYGM EDLVVEMNVE SARLARESAV RYATPDKPRF VAGAIGPTPK TASISPDVND PGARNVTFDE LRSAYYQQAK ALLDGGVDLF LVETIFDTLN AKAALFALDE LFEDTGERLP IMISGTVTDA SGRILSGQTV EAFWNSLRHA KPLTFGLNCA LGAALMRPYI AELAKLCDTY VSCYPNAGLP NPMSDTGFDE TPDVTSGLLK EFAQAGLVNL AGGCCGTTPE HIAEIAKALA DVKPRRWPSH YSDAA // ID Q0BQM8_GRABC Unreviewed; 313 AA. AC Q0BQM8; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 27-MAY-2015, entry version 49. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABI62874.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ABI62874.1}; GN OrderedLocusNames=GbCGDNIH1_1976 {ECO:0000313|EMBL:ABI62874.1}; OS Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Granulibacter. OX NCBI_TaxID=391165 {ECO:0000313|EMBL:ABI62874.1, ECO:0000313|Proteomes:UP000001963}; RN [1] {ECO:0000313|EMBL:ABI62874.1, ECO:0000313|Proteomes:UP000001963} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1260 / CGDNIH1 {ECO:0000313|Proteomes:UP000001963}; 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; ABI62874.1; -; Genomic_DNA. DR RefSeq; WP_011632676.1; NC_008343.1. DR RefSeq; YP_745797.1; NC_008343.1. DR ProteinModelPortal; Q0BQM8; -. DR STRING; 391165.GbCGDNIH1_1976; -. DR EnsemblBacteria; ABI62874; ABI62874; GbCGDNIH1_1976. DR KEGG; gbe:GbCGDNIH1_1976; -. DR PATRIC; 22080203; VBIGraBet83793_2051. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; GBET391165:GHON-2025-MONOMER; -. DR Proteomes; UP000001963; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001963}; KW Methyltransferase {ECO:0000313|EMBL:ABI62874.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001963}; KW Transferase {ECO:0000313|EMBL:ABI62874.1}. SQ SEQUENCE 313 AA; 33827 MW; 7DC55474CD690D20 CRC64; MMALISSLFR QARPLLLDGA LATELERAGY HLDDPLWSGR LLLDNPAAIA AVHRAYLEAG ADCIETASYQ LSLPGLQRRG LSRGRAMSVL ADAARLACSV RDDVWAGLPA AQRRNRIRPL VAGSLGPYGA CQADGSEYTG RYALSRSQYL AFHAPRMRAL AAGGADLIAC ETVPHLDEAL AFADLLQALS VPGWVSFSVR DAAHIADGTP LRLCVQAMAS CPFVAAIGIN CTDPVLVPAL IRCLRRGGLP VIVYPNAGEP FDLVTRCWGH RRSDDWAEQA RSWLRLGARI VGGCCRTRPD DIRALRRLIH AQA // ID Q0BVV3_GRABC Unreviewed; 1163 AA. AC Q0BVV3; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 27-MAY-2015, entry version 71. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:ABI61049.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABI61049.1}; GN OrderedLocusNames=GbCGDNIH1_0151 {ECO:0000313|EMBL:ABI61049.1}; OS Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Granulibacter. OX NCBI_TaxID=391165 {ECO:0000313|EMBL:ABI61049.1, ECO:0000313|Proteomes:UP000001963}; RN [1] {ECO:0000313|EMBL:ABI61049.1, ECO:0000313|Proteomes:UP000001963} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1260 / CGDNIH1 {ECO:0000313|Proteomes:UP000001963}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000394; ABI61049.1; -; Genomic_DNA. DR RefSeq; WP_011630859.1; NC_008343.1. DR RefSeq; YP_743972.1; NC_008343.1. DR ProteinModelPortal; Q0BVV3; -. DR STRING; 391165.GbCGDNIH1_0151; -. DR EnsemblBacteria; ABI61049; ABI61049; GbCGDNIH1_0151. DR KEGG; gbe:GbCGDNIH1_0151; -. DR PATRIC; 22076317; VBIGraBet83793_0159. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; GBET391165:GHON-153-MONOMER; -. DR Proteomes; UP000001963; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001963}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABI61049.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001963}; KW Transferase {ECO:0000313|EMBL:ABI61049.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 224 224 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 734 734 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1163 AA; 128681 MW; ABFD065CD47E3614 CRC64; MSRPHLLDAL RDQVLLCDGG MGSRVQALDL DVERDYLGKE NCTEILNLSR PDLVREIHRG YYEAGADMVE TNSFGGSPVT LGEFELGDRA REINRIAAEL AREAADSFSD GRHRYVVGSI GPGTKLPSLG NIDYDPLEAG LAEQCRGLID GGVDAFLIET CQDTLQIKAA VNGAKKARAE MGVDTPIFVQ VTVETTGTLL VGPDIAAAAT VIHAMDVPLI GLNCATGPQE MAEHVKWLAA NWTGLISMQP NAGLPELVDG QTHYPLSPEE MASWVERYIS EDGVNLIGGC CGTNVPHIRA LDAMLRRRAG ARLRPEPIKR NSIWVPSVAS LYGQTSLRQE NSYFSIGERC NANGSKKWRE AQEQHDWDTC ISMGREQVGE GSNALDICTA FVGRNEGLEM NEVIRRFTSS VNAPLVIDST ETPVIEAALK LHGGKPIINS INFEDGEHAA EERMILARKF GAAVIALTID EEGMAKTPER KLAIAERLVR FACEKHGLPQ SDLLIDPLTF TIATGNEDDR KLGEWTLEGI RMIREKFPEI QIILGLSNIS FGLNPAARAV LNSVFLDHAV RAGMTGAIVH VSKIRPLHQI PAEEAKVMED LIFDRRTEDY DPLQRLLEMF ADRKAADAVK KTRAATVEGR LKDRIVDGDR KGLTDELDEA LKTHAPLDII NTILLDGMKV VGELFGAGKM QLPFVLQSAE TMKAAVAYLE PMMERVEGQQ KGTIVLATVK GDVHDIGKNL VDIILTNNGY RVVNLGIKVP LADMVAAVKE HRAHAIGMSG LLVKSTVIMR ENLEEMSRQG VDVPVLLGGA ALTRNYVEDD CVAAYASGRV AYARDAFDGL HLMDKVTGNA FDDYLSAIQQ KRKGKSRNQS RTLGKADARA FQPVDINATR ARRHRLTNNV PAIEPPFWGA RVVEATPKAI IPFLNERSLY QFQWGFRKQG RSLDDFLGWA KQELRPVMKR MLALCEEQDI LKPQAAYGYW KAAGQGNELI LFEQDGSTEL CRFSLPRQPK EDGECIADFF RDVDDAERDV IGLQVVTVGQ KASDMARIWF EEDRYQDYLY LHGLSVEMAE AMAEYVHKRI RAECGFAAED ERDMEKMLAQ GYRGSRYSFG YPACPKLEDQ EPILKLLQAE RIGVDLSDEY QLHPEQSTSA LVVLNPHAKY FSV // ID Q0C0E4_HYPNA Unreviewed; 352 AA. AC Q0C0E4; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 27-MAY-2015, entry version 59. DE SubName: Full=Putative metionine synthase, homocysteine S-methyltransferase subunit {ECO:0000313|EMBL:ABI75899.1}; GN OrderedLocusNames=HNE_2102 {ECO:0000313|EMBL:ABI75899.1}; OS Hyphomonas neptunium (strain ATCC 15444). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Hyphomonadaceae; Hyphomonas. OX NCBI_TaxID=228405 {ECO:0000313|EMBL:ABI75899.1, ECO:0000313|Proteomes:UP000001959}; RN [1] {ECO:0000313|EMBL:ABI75899.1, ECO:0000313|Proteomes:UP000001959} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15444 {ECO:0000313|EMBL:ABI75899.1, RC ECO:0000313|Proteomes:UP000001959}; 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; ABI75899.1; -; Genomic_DNA. DR RefSeq; WP_011647098.1; NC_008358.1. DR RefSeq; YP_760799.1; NC_008358.1. DR ProteinModelPortal; Q0C0E4; -. DR STRING; 228405.HNE_2102; -. DR EnsemblBacteria; ABI75899; ABI75899; HNE_2102. DR KEGG; hne:HNE_2102; -. DR PATRIC; 32217047; VBIHypNep17450_2107. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; HNEP228405:GI69-2103-MONOMER; -. DR Proteomes; UP000001959; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; ISM:JCVI. DR GO; GO:0009086; P:methionine biosynthetic process; ISA:JCVI. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001959}; KW Methyltransferase {ECO:0000313|EMBL:ABI75899.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001959}; KW Transferase {ECO:0000313|EMBL:ABI75899.1}. SQ SEQUENCE 352 AA; 38101 MW; 499A53CA71AC7FC4 CRC64; MNSQDRFKAL EALANQRILV LDGAMGTQIQ NYKLTEEDFQ GNRFGDWEIP LKGNNDLLNL TRPDVIGEIH RKYIDAGADF VETNTFSATT IAMADYKMEA LAAEIAREGA RIARDVADKA EAELGRPVGV MGAIGPTNKT LSLSPNVNDP GYRDVTFDQV REAYFEQAEA MAPFIDVFLI ETVFDTLNAK AAIKALIDLR EQKGIDLPII ISGTITDASG RTLSGQTAEA FWNSVRHARP WAIGLNCALG ADLMRQHVAS ISRVADTRVI AYPNAGLPNA FGEYDETPDQ TAAHLKEWAN SGLVNVLGGC CGTSPGHIAA IAQAIRSAPP RKLPEVSRAM RLSGLEPFTV AS // ID Q0CYN5_ASPTN Unreviewed; 345 AA. AC Q0CYN5; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 27-MAY-2015, entry version 38. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EAU37956.1}; GN ORFNames=ATEG_01199 {ECO:0000313|EMBL:EAU37956.1}; OS Aspergillus terreus (strain NIH 2624 / FGSC A1156). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus. OX NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU37956.1, ECO:0000313|Proteomes:UP000007963}; RN [1] {ECO:0000313|Proteomes:UP000007963} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963}; 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; CH476595; EAU37956.1; -; Genomic_DNA. DR RefSeq; XP_001208564.1; XM_001208564.1. DR ProteinModelPortal; Q0CYN5; -. DR STRING; 33178.CADATEAP00000979; -. DR EnsemblFungi; CADATEAT00000979; CADATEAP00000979; CADATEAG00000979. DR GeneID; 4316223; -. DR EuPathDB; FungiDB:ATEG_01199; -. DR HOGENOM; HOG000265278; -. DR OMA; NCTKIYK; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000007963; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007963}; KW Reference proteome {ECO:0000313|Proteomes:UP000007963}. SQ SEQUENCE 345 AA; 37395 MW; F2D23F539064224C CRC64; MATIQILDGG LGTSLQDQYG VEFSSTTTPL WSSHLLVSDP GTLQSCQHDF GVAGVDVLLT ATYQVSIEGF ARTKTADFPN GIPKTAIAPY LQTAVTVAEQ AKARDSAKIA LSLGPYGACM IPGQEYSGEY DAEHDSEEAL FRWHLERLRL FQDAEGDLIS RVQYVAFETL PRLDEVRAVR RAIRAAGIAV PFWVSCVFPR EDDLLPDGSS IEQVVDAALA PMSDGGVPWG IGANCTKIHK LPGLVGKLGE YVAKRVASGQ ISTVPSLVLY PDGTNGEVYN TTTQQWEKPD GQESAGRDTR SWETQLAQVV KDARETGPFS SFLVGGCCKA SHHDIKKLRQ QFATE // ID Q0F311_9PROT Unreviewed; 1223 AA. AC Q0F311; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 27-MAY-2015, entry version 49. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EAU56130.1}; GN ORFNames=SPV1_04898 {ECO:0000313|EMBL:EAU56130.1}; OS Mariprofundus ferrooxydans PV-1. OC Bacteria; Proteobacteria; Zetaproteobacteria; Mariprofundales; OC Mariprofundaceae; Mariprofundus. OX NCBI_TaxID=314345 {ECO:0000313|EMBL:EAU56130.1}; RN [1] {ECO:0000313|EMBL:EAU56130.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PV-1 {ECO:0000313|EMBL:EAU56130.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EAU56130.1}. 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; AATS01000001; EAU56130.1; -; Genomic_DNA. DR RefSeq; WP_009851274.1; NZ_DS022295.1. DR ProteinModelPortal; Q0F311; -. DR SMR; Q0F311; 652-892. DR EnsemblBacteria; EAU56130; EAU56130; SPV1_04898. DR PATRIC; 28827475; VBIMarFer59489_2218. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EAU56130.1}; KW Transferase {ECO:0000313|EMBL:EAU56130.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1223 AA; 134658 MW; DF646DD07F4044CB CRC64; MTQTDILKQQ LDRRILILDG AMGTMIQRHQ LEEADYRGER FADWASELKG NNDLLNLTQP DIIQGIHQAY LDAGADILET NTFNSNTPSM ADYHMEELVY ELNVAGAALA RKAADAYATA DKPRFVAGVL GPTSRTCSIS PDVNDPGFRN VHFDELVTTY KDATRGLIDG GADIILIETV FDTLNAKAAV FAVQSYFEES GVELPIMISG TITDASGRTL SGQTATAFYN SLAHAKPISI GLNCALGAGE LRQYIEELSG TVACRINAHP NAGLPNAFGG YDETAEDMAA QIREWAESGF LNIIGGCCGT GPAHIRAMAE AVEGIAPRPL PVRGETLPVQ CRLSGLEPLH IDESSLFVNV GERANVTGSA VFKRLIMAGD YNTALNICRE QVENGAQIID INMDEAMLDG EKAMVTFLNL IASEPDISRV PIMLDSSKWS IIEAGLKCIQ GKGVVNSISL KEGEEAFIHH ARLLRRYGAA AVVMAFDEAG QADTFARKTE ICARSYKILT EVCDFPPEDI IFDPNIFAIA TGIEEHNNYA VDFIEATGWI KQHLPYAMVS GGVSNVSFSF RGNNPVREAI HSVFLYHAIK QGMDMGIVNA GQLAVYDDLS EELRERVEDV VLNRREDSTE RLLDIAEKYR GDGIEVKKAD DEWRKLPVAE RLAHALVKGI DTFVDEDTEE ARLAFATPIE VIEGPLMDGM NVVGDLFGDG KMFLPQVVKS ARVMKKAVAW LMPYIEAGKA VGSNSSNGKV LMATVKGDVH DIGKNIVGVV LQCNNFEVID LGVMVPAKTI LDEAVKHDVD IIGLSGLITP SLDEMVHIAK EMTRLGLTIP IMIGGATTSK AHAAVKIEPE YAHPLVWVKD ASRAVGVAQN LISALNRDSF VAGIRKEYKE VRERYLGRQQ QTDWLSLEAA RANSTGLASE TLAAAPAEPG IRVLQDIPLA EIREFIDWTP FFSAWELNGA YPRILNDPHK GKEAQKLFDD AQQRLDTIIN ENWFSARAVF GLFPARATDD DSVIVWKDEA HNDELARFHF VRQQLDKKDS RANLCLADFI SREQHDHLGG FAVGIFGAEE RAKAFEAEND DYNAIMIKVL ADRLAEALAE MLHADVRKRY WGYAADEKLS MDEMIGEKYQ GIRPAAGYPA CPEHSEKETL WKLLDVENNI GMQLTESFAM LPTAAVSGLY FANPEARYFT VGKINRDQVR DYARRKGWSI EKAERWLAPN LGY // ID Q0FED8_9RHOB Unreviewed; 289 AA. AC Q0FED8; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 27-MAY-2015, entry version 24. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EAU52206.1}; GN ORFNames=OM2255_08631 {ECO:0000313|EMBL:EAU52206.1}; OS Rhodobacterales bacterium HTCC2255. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales. OX NCBI_TaxID=367336 {ECO:0000313|EMBL:EAU52206.1}; RN [1] {ECO:0000313|EMBL:EAU52206.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2255 {ECO:0000313|EMBL:EAU52206.1}; 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. {ECO:0000313|EMBL:EAU52206.1}. 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; AATR01000002; EAU52206.1; -; Genomic_DNA. DR RefSeq; WP_008035283.1; NZ_DS022282.1. DR ProteinModelPortal; Q0FED8; -. DR EnsemblBacteria; EAU52206; EAU52206; OM2255_08631. DR PATRIC; 28470587; VBIRhoBac69559_1418. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EAU52206.1}; KW Transferase {ECO:0000313|EMBL:EAU52206.1}. SQ SEQUENCE 289 AA; 30831 MW; 23716F272B860D05 CRC64; MTITFLDGGM GQELVARAGK ATSLWSVQAL LDNPEMVTAV HNEYFMVGAD VATTNTYSIL PDRLEKHGLA DQLEKLQNLA CQLATEARDL NGKGIVAGSL GPQGFSYQPE LSPPADMAAE IYSQICKIQA NHVDVFIAET MSSVDQAKGA LMGASGFNKP IWLALSVDDR DGTKLRSGED LKDILPLLNE YKPAAVMINC SAPEAVSIAL PLLSEANIPT GGYANGFVEI AKNFNKIGAT VDLLKARTDL NPEAYANIAD DWIKSGATFI GGCCEVGPAH IAELKRRFG // ID Q0FGF8_9RHOB Unreviewed; 335 AA. AC Q0FGF8; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 27-MAY-2015, entry version 30. DE SubName: Full=Methionine synthase I {ECO:0000313|EMBL:EAU52681.1}; GN ORFNames=OM2255_04115 {ECO:0000313|EMBL:EAU52681.1}; OS Rhodobacterales bacterium HTCC2255. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales. OX NCBI_TaxID=367336 {ECO:0000313|EMBL:EAU52681.1}; RN [1] {ECO:0000313|EMBL:EAU52681.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2255 {ECO:0000313|EMBL:EAU52681.1}; 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. {ECO:0000313|EMBL:EAU52681.1}. 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; AATR01000001; EAU52681.1; -; Genomic_DNA. DR RefSeq; WP_008033798.1; NZ_DS022282.1. DR ProteinModelPortal; Q0FGF8; -. DR EnsemblBacteria; EAU52681; EAU52681; OM2255_04115. DR PATRIC; 28468744; VBIRhoBac69559_0518. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 335 AA; 35586 MW; 42250C1ED9A13CBB CRC64; MSDIIDEIIA KKGFLLADGA TGTNLFNLGL EAGDPPEFWN VDEPDKIRSL YQGSVDSGCD LFLTNSFGGN ASRLKLHNSE DRAYELSLAA SKLGREVADK SGREILVAGS IGPTGDIMGD AGWLSHNEAV QMFQVTAQGL MDGGADLIWV ETISSPEEFI AASEAIENIN APWVGTMSFD TAGRTMMGVT SHDMSNLVKK MKYAPIGFGA NCGVGASDLL RTVLGLNENA DRPIIAKGNA GIPKYVDGHI HYDGTPEVMA EYAVLARACG ATIIGGCCGT MPAHLKAMRR ALDNYEVRDV PSLSEISKAL GPFSSETDGT GDGPKPARVR RGQRR // ID Q0FP39_PELBH Unreviewed; 1256 AA. AC Q0FP39; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 27-MAY-2015, entry version 49. DE SubName: Full=Dihydropteroate synthase, DHPS:Homocysteine S-methyltransferase:Cobalamin-dependent methionine {ECO:0000313|EMBL:EAU46020.1}; GN ORFNames=R2601_27141 {ECO:0000313|EMBL:EAU46020.1}; OS Pelagibaca bermudensis (strain JCM 13377 / KCTC 12554 / HTCC2601). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Pelagibaca. OX NCBI_TaxID=314265 {ECO:0000313|EMBL:EAU46020.1}; RN [1] {ECO:0000313|EMBL:EAU46020.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2601 {ECO:0000313|EMBL:EAU46020.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EAU46020.1}. 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; AATQ01000019; EAU46020.1; -; Genomic_DNA. DR RefSeq; WP_007801287.1; NZ_DS022276.1. DR ProteinModelPortal; Q0FP39; -. DR SMR; Q0FP39; 671-1246. DR EnsemblBacteria; EAU46020; EAU46020; R2601_27141. DR PATRIC; 28150047; VBIRosSp73948_3841. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EAU46020.1}; KW Transferase {ECO:0000313|EMBL:EAU46020.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 261 261 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 325 325 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 781 781 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1256 AA; 137108 MW; 53C184087A417501 CRC64; MSSTAPTRSP VFDRLHAAAR ERILILDGAM GTQIQQLGLS EGDFQGCGGG ACSCHLPHDS DKPQQGNNDL LNLTKPEAIE EIHYLYAMAG ADIAETNTFS STTIAQADYA MEGAVYDLNF QGARLARRAM DRAEAEDGRP RFVAGALGPT NRTASISPDV NNPGYRAVTF DQLRIAYADQ ARALIDGGAD LLLIETIFDT LNAKAAIFAC EEVFAERGER LPVMISGTIT DLSGRTLSGQ TPTAFWHSVR HAEPFTIGLN CALGAEAMRP HLAEISGVAD TLICAYPNAG LPNEMGEYDE TPEQMAAQIA GFAKEGLLNV VGGCCGSTYE HIRAIAKAVE GFAPREIPQP KPLMRLSGLE PFMLTEDIPF VNVGERTNVT GSAKFRKLIT NADYATALDV ARDQVENGAQ IIDVNMDEGL IDSQQAMVEF LNLIAAEPDI ARVPIMIDSS KWEIIEAGLK CVQGKPVVNS ISMKEGEEAF LEQATLCRRY GAAVIVMAFD ETGQADTEDR KVEICTRAYK LLTEKVGFPP EDIIFDPNVF AVATGIEEHD NYGVDFIEAT RRITTDCPHV HISGGVSNLS FSFRGNEPVR EAMHAVFLYH AIQNGMDMGI VNAGQLAVYD QIDADLREAC EDVVLNRTPA NGGTATENML DIAERYRGQG GAKGREKDMS WRELPVEKRL EHALVNGITE FIEGDTEEAR QAAERPLHVI EGPLMAGMNV VGDLFGAGKM FLPQVVKSAR VMKQAVAVLL PYMEEEKRLG GGTEREAAGK VLMATVKGDV HDIGKNIVGV VLACNNYEII DLGVMVPAER ILATAKEQNV DVIGLSGLIT PSLDEMVHVA SEMEREGFDI PLLIGGATTS RVHTAVKIHP RYGKGQAVYV TDASRAVSVV SSLLSATQKP DYVANIQTEY ADVADKHARA ELAKKRISVE QARDNALKLD FGNHAPAPSF LGSKVVEDWD LAELARYIDW TPFFQTWEMK GVYPKILDDE KQGEAARALF ADAQAMLEKI IAEKWFHPRA VVGFWPANAV GDDIRLFKDA DRVEELATFY TLRQQTAKRG DRPNVALSDF VAPEGRPDHV GGFVVTAGIE EERIAKAFEA EHDDYSSIMV KALADRFAEA MAERLHERVR KEFWGYAPDE AFDNVELISE KYAGIRPAPG YPAQPDHTEK TTLFELLDAT NATGVELTES YAMWPGSSVS GLYIAHPESY YFGVAKVERD QVQDYAARKG MAVEEVERWL APILNYIPGA GAVAAE // ID Q0FQ02_PELBH Unreviewed; 337 AA. AC Q0FQ02; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 27-MAY-2015, entry version 31. DE SubName: Full=Methionine synthase I {ECO:0000313|EMBL:EAU46252.1}; GN ORFNames=R2601_25181 {ECO:0000313|EMBL:EAU46252.1}; OS Pelagibaca bermudensis (strain JCM 13377 / KCTC 12554 / HTCC2601). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Pelagibaca. OX NCBI_TaxID=314265 {ECO:0000313|EMBL:EAU46252.1}; RN [1] {ECO:0000313|EMBL:EAU46252.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2601 {ECO:0000313|EMBL:EAU46252.1}; 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. {ECO:0000313|EMBL:EAU46252.1}. 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; AATQ01000016; EAU46252.1; -; Genomic_DNA. DR RefSeq; WP_007800568.1; NZ_DS022276.1. DR ProteinModelPortal; Q0FQ02; -. DR EnsemblBacteria; EAU46252; EAU46252; R2601_25181. DR PATRIC; 28149241; VBIRosSp73948_3445. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 337 AA; 35508 MW; 7FA4D9DCC346DC0A CRC64; MTDALTELLS TRDWLMADGA TGTNLFNMGL ASGDAPEFWN IDHPERIRTL YRNAVEAGSD IFLTNSFGAN ASRLKLHDAA SRAFELSRLA AALGRDVADA AGRKVVVAGS VGPTGEIMGT VGTLSHETAV EMFEETAAGL KEGGADVLWV ETISAPEEFA AAAEAFANVG MPWCGTMSFD TAGRTMMGVT SDDFVRQVDA LPNPPLAFGA NCGVGASDLM RTVLGFAATG TERPIIAKGN AGIPRYEDGH IHYNGTPELM AEYAVLARNA GARIIGGCCG TMPEHLRAMR EALETRPTGP RPTLEQIAAA LGGFSSDSDG TGDTPAPKRE RRGRRRS // ID Q0G2R1_9RHIZ Unreviewed; 299 AA. AC Q0G2R1; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 27-MAY-2015, entry version 19. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EAU42120.1}; GN ORFNames=FP2506_16844 {ECO:0000313|EMBL:EAU42120.1}; OS Fulvimarina pelagi HTCC2506. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Aurantimonadaceae; Fulvimarina. OX NCBI_TaxID=314231 {ECO:0000313|EMBL:EAU42120.1}; RN [1] {ECO:0000313|EMBL:EAU42120.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2506 {ECO:0000313|EMBL:EAU42120.1}; 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. {ECO:0000313|EMBL:EAU42120.1}. 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; AATP01000002; EAU42120.1; -; Genomic_DNA. DR RefSeq; WP_007068488.1; NZ_DS022272.1. DR EnsemblBacteria; EAU42120; EAU42120; FP2506_16844. DR PATRIC; 27667291; VBIFulPel16688_1199. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EAU42120.1}; KW Transferase {ECO:0000313|EMBL:EAU42120.1}. SQ SEQUENCE 299 AA; 32614 MW; 36746C567C5DFAE9 CRC64; METYLIFHEG FELPLFASYP LLGTAEGRKR LRTYYRRHMI IAADCGMGFV LESPTWRASR RWGEQLGHDA VELRRFNLDA IALLSDLRAE APQGKPCIVS GNIGPRGDGY RPDETLTAEE AEAYHAEQIG WFAETDADIV SAFTITTVAE AVGIIRAAKK KSLRTVVSFT VETDGRLPDG TPLGEAIKRT DAETDGAAEY LMINCAHPDH FRHAVAAGAK WLERIGGIRA NASRLSHAEL DAAEELDDGN PAELAGAYDE LLDMLPNLRV LGGCCGTDHR HVAAIASACR HHNPQGVPV // ID Q0G312_9RHIZ Unreviewed; 1265 AA. AC Q0G312; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 27-MAY-2015, entry version 52. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EAU42019.1}; GN ORFNames=FP2506_16339 {ECO:0000313|EMBL:EAU42019.1}; OS Fulvimarina pelagi HTCC2506. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Aurantimonadaceae; Fulvimarina. OX NCBI_TaxID=314231 {ECO:0000313|EMBL:EAU42019.1}; RN [1] {ECO:0000313|EMBL:EAU42019.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2506 {ECO:0000313|EMBL:EAU42019.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EAU42019.1}. 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; AATP01000002; EAU42019.1; -; Genomic_DNA. DR RefSeq; WP_007068392.1; NZ_DS022272.1. DR ProteinModelPortal; Q0G312; -. DR SMR; Q0G312; 673-917. DR EnsemblBacteria; EAU42019; EAU42019; FP2506_16339. DR PATRIC; 27667089; VBIFulPel16688_1104. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 263 263 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 326 326 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 327 327 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 779 779 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1265 AA; 140050 MW; 512222C60189AB31 CRC64; MSDTTDQLFG PMTEGRNPAE TLEALTQAVS ERILVLDGAM GTEIQLLGLG EEDFRGHRFG NCECHLQGNN DLLNLTQPKQ IEDIHYNYAM AGADILETNT FSSTSIAQAD YTMEDQVYEL NRDGARLARR ACLRAEDTDG RRRFVAGALG PTNRTASISP DVNNPGYRAT SFDELRQAYG EQLRGLMDGG IDLVLIETIF DTLNAKAAIF ACEEIFAEKG VTLPIMISGT ITDLSGRTLS GQTPTGFWHS VRHAKPFTIG LNCALGAEAM KDHLAEISSV ADTFVCAYPN AGLPNEFGEY DQSPEAMGAE VEKFAKDGLV NIVGGCCGST PDHIAAVAKA VSKHSPRKVP EKEPQMRLSG LEPFTLTKDI PFVNVGERTN VTGSARFRKL IKENDYPTAL EVARQQVENG AQVIDVNMDE GLLDSEQAMV DYLNLIASEP DIARVPVMID SSKFEVIEAG LKCVQGKGIV NSISMKEGEE SFKKQARLVR EYGAAVVVMA FDETGQADTK DRKVEICERA YRILTEEVGF PPEDIIFDPN IFAVATGIEE HANYGVDFIE AAREIRKKMP LVHISGGVSN LSFSFRGNDA VREAMHAVFL YHAIKAGMDM GIVNAGQLIV YDAIDEELRE ACEDVILNRA PKNGEDATEN LLELAERYKD KGGSKGKEKD LSWREKPVNE RLSHSLVNGI TDFIEEDTEE ARQNAERPLH VIEGPLMDGM NIVGDLFGDG KMFLPQVVKS ARVMKQAVAY LNPYMEAEKS DDDEAKGKIL MATVKGDVHD IGKNIVGVVL ACNNYEVIDL GVMVPAAKIL EEAKKNKVDI IGLSGLITPS LDEMVNVAAE MEKQDFQVPL LIGGATTSRV HTAVKIHPAY TKGQAIHVND ASRAVGVVSS LLSKETRASA IQKVRDQYAE VAEKHERSER DKKRLTLADA RANAVKIDWS AYAPKQPSFT GIRVFEEWDL EDLAKTFDWT PFFQSWELKG RYPAILDDEK QGETARSLFS DAQEMLKKII DEKWFTPKAV IGFWPANAVG DDIKLFRDDS RKDELQTFFT LRQQLTRRGE RPNIALSDFV APKDSGVKDY VGGFCVTAGL EEAEISKRFE NQNDDYNSIL VKALADRFAE AFAERMHERV RKEFWGYEPD EDLSNEDLIA EKYAGIRPAP GYPAQPDHTE KETLFELLDA KEKIGVQLTE NFAMWPSSSV SGLYIGHPES HYFGVAKIEQ DQVADYAERK GMAVEEIERW LGPVLNYTPK PTVGDEVQIT QEAAE // ID Q0GC24_MEDSA Unreviewed; 295 AA. AC Q0GC24; DT 03-OCT-2006, integrated into UniProtKB/TrEMBL. DT 03-OCT-2006, sequence version 1. DT 29-OCT-2014, entry version 20. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABI34093.1}; DE Flags: Fragment; OS Medicago sativa (Alfalfa). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; OC Trifolieae; Medicago. OX NCBI_TaxID=3879 {ECO:0000313|EMBL:ABI34093.1}; RN [1] {ECO:0000313|EMBL:ABI34093.1} RP NUCLEOTIDE SEQUENCE. RA Barrow M.J., Singh J., Bagga S., Sengupta-Gopalan C.; RT "Isolation of Genes in the Medicago sativa (Alfalfa) Methonine RT Metabolic Pathway."; 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; DQ873667; ABI34093.1; -; mRNA. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Methyltransferase {ECO:0000313|EMBL:ABI34093.1}; KW Transferase {ECO:0000313|EMBL:ABI34093.1}. FT NON_TER 1 1 {ECO:0000313|EMBL:ABI34093.1}. FT NON_TER 295 295 {ECO:0000313|EMBL:ABI34093.1}. SQ SEQUENCE 295 AA; 32628 MW; 233513B4E54530DB CRC64; LNKCGGYGII DGGFATELER HGVDLNDPLW SAKCLFTSPH LVRRVHLDYL DSGANIILTS SYQATIQGFE AKGFSKEEGQ ALLRRRVELA REARDIYYDR CTKDSFDFIR DERYRSRPIL IAASVGSYGA YLADGSEYTG DYGDAVTVQT LKDFHRERVK ILVDAGADLI AFETIPNKLD AQAYAELLEE EGIEIPAWFS FSCKDENKVA SGDSILECAS IADSCPQVVA VGVNCTAPRF IHGLISSIKK ATSKPILVYP NSGETYNADN NTWVKSSGEA EEDFVPYIGK WRYAG // ID Q0GU39_PARLI Unreviewed; 381 AA. AC Q0GU39; DT 03-OCT-2006, integrated into UniProtKB/TrEMBL. DT 03-OCT-2006, sequence version 1. DT 04-MAR-2015, entry version 29. DE SubName: Full=Betaine homocysteine methyltransferase {ECO:0000313|EMBL:ABF82445.1}; DE Flags: Fragment; GN Name=BHMT {ECO:0000313|EMBL:ABF82445.1}; OS Paracentrotus lividus (Common sea urchin). OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; OC Echinoidea; Euechinoidea; Echinacea; Echinoida; Echinidae; OC Paracentrotus. OX NCBI_TaxID=7656 {ECO:0000313|EMBL:ABF82445.1}; RN [1] {ECO:0000313|EMBL:ABF82445.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=17038519; DOI=10.1242/dev.02603; RA Rottinger E., Croce J., Lhomond G., Besnardeau L., Gache C., RA Lepage T.; RT "Nemo-like kinase (NLK) acts downstream of Notch/Delta signalling to RT downregulate TCF during mesoderm induction in the sea urchin embryo."; RL Development 133:4341-4353(2006). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DQ531773; ABF82445.1; -; mRNA. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ABF82445.1}; KW Transferase {ECO:0000313|EMBL:ABF82445.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT NON_TER 381 381 {ECO:0000313|EMBL:ABF82445.1}. SQ SEQUENCE 381 AA; 42193 MW; 6321B1B4732C94B7 CRC64; MSDAKKPKTD KKGFLERLDA DEIVVGDGGY VFALEKRGYV KAGPWTPEAT VEHPEAVRQL SKEFLRAGAD VIQAFTFYAS DDKLENRANK SLEKHTGALI NQRACDIASE VADIGNGNGP GLFAGGVCQT PGYLSGGTKE SVQAIFRKQV DVFVKNKVDF LLAEYFEHVE EAEWAVEELK KTGIPVACSL CIGPEGDMHG VSAGDCAVRM AKAGADVVGM NCHFDPWISL KTVALMKEGL EKAGIKRHLM IQPLGFSTPD CGKQGFIDLP EFPFGLEPRI VTRWECHRYA REAYDMGIRY IGGCCGFEPY HIRAVCEELN KERGFYPEGT EKHAPWGDGL RQHTKPWVRA RARRDYWENL KPASGRPDCP SMSKPDAWGE T // ID Q0HRT7_SHESR Unreviewed; 1244 AA. AC Q0HRT7; DT 03-OCT-2006, integrated into UniProtKB/TrEMBL. DT 03-OCT-2006, sequence version 1. DT 01-APR-2015, entry version 67. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABI44168.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABI44168.1}; GN OrderedLocusNames=Shewmr7_3184 {ECO:0000313|EMBL:ABI44168.1}; OS Shewanella sp. (strain MR-7). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=60481 {ECO:0000313|EMBL:ABI44168.1, ECO:0000313|Proteomes:UP000001960}; RN [1] {ECO:0000313|Proteomes:UP000001960} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MR-7 {ECO:0000313|Proteomes:UP000001960}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000444; ABI44168.1; -; Genomic_DNA. DR RefSeq; WP_011627067.1; NC_008322.1. DR RefSeq; YP_739225.1; NC_008322.1. DR STRING; 60481.Shewmr7_3184; -. DR EnsemblBacteria; ABI44168; ABI44168; Shewmr7_3184. DR KEGG; shm:Shewmr7_3184; -. DR PATRIC; 23591587; VBISheSp85603_3282. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SSP60481:GHW6-3310-MONOMER; -. DR Proteomes; UP000001960; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001960}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABI44168.1}; KW Transferase {ECO:0000313|EMBL:ABI44168.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 258 258 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 774 774 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1244 AA; 138040 MW; 13272BA93F38538A CRC64; MAISLHRASQ TLADIRNQLS KRILILDGAM GTMIQGYKLE EADYRGERFK DWHTDVKGNN DLLVLTQPHI IKQIHTDYLL AGADIIETNT FNATTIAMAD YDMQSLSAEI NREGARLARE ACDEIEKATG KPRYVAGVLG PTNRTCSISP DVNDPGYRNI HFDELVTAYC ESTRALIEGG ADIIMVETIF DTLNAKAALF AIETVFDELF GANSPARLPV MISGTITDAS GRTLTGQTTE AFYNSLRHIK PLSIGLNCAL GPKELRPYVE ELSRIAECYV SAHPNAGLPN EFGGYDETPE DMASVIQEWA SEGMLNIIGG CCGSTPEHIK VIREAVEPFA PRVLPEIPVA CRLSGLEPLT IDAQTLFVNV GERTNVTGSA KFLKLIKEGK FEQALDVARE QVESGAQIID INMDEGMLDG VEVMHKFLNL IASEPDISRV PIMIDSSKWE VIEAGLKCIQ GKGIVNSISL KEGEEKFIEQ ATLVKRYGAA AIIMAFDEQG QADTKARKVE ICTRAYRVLV DKVGFPPEDI IFDPNIFAIA TGIDEHDNYA VDFIEAIKEI KATLPHAMIS GGVSNVSFSF RGNNPVREAI HAVFLYHAIK VGMDMGIVNA GQLAIYDDID PELKDKVENV VLNLPCPVEG SNNTEQLLEI AEKFRGDGSS AAKKEDLEWR SWPVNQRLAH ALVKGITEFI DEDTEAARQL ASRPLDVIEG PLMDGMNIVG DLFGSGKMFL PQVVKSARVM KKAVAYLNPF IEQEKVEGQS NGRILMVTVK GDVHDIGKNI VGVVLACNGF EVFDLGVMVS VERILEAVKE HNIDIIGMSG LITPSLDEMV HNVKTFHREG LTIPAIIGGA TCSKIHTAVK IAPHYPHGAI YIADASRAVP MVSKLVSNET RQATIDETYA EYEEMRVKRL SQTKRKEIVS LEAARENRCQ HDWANYTPFK PNVLGRQVFE DYPLTDLVDR IDWTPFFRAW ELHGHYPEIL TDKVVGVEAQ KLFADGQAML KKIIDEKWLT AKGVIGLFPA NTVGFDDIEL YTDETRTEVE MTTHHLRMQL ERVGNDNFCL ADFVAPKDSG VADYMGGFAV TAGHGIDEHI ARFEANHDDY NAIMLKCLAD RLAEAFAERM HERVRKEFWG YAADEQLDNE ALIREKYKGI RPAPGYPACP DHTEKGLLWE LLKPNETIDL NITESYAMFP TAAVSGWYFA HPKSRYFGVT NIGRDQVEDY AKRKGMTVAE TEKWLAPVLD YDPE // ID Q0IAG2_SYNS3 Unreviewed; 1206 AA. AC Q0IAG2; DT 03-OCT-2006, integrated into UniProtKB/TrEMBL. DT 03-OCT-2006, sequence version 1. DT 27-MAY-2015, entry version 70. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABI47814.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABI47814.1}; GN Name=metH {ECO:0000313|EMBL:ABI47814.1}; GN OrderedLocusNames=sync_1353 {ECO:0000313|EMBL:ABI47814.1}; OS Synechococcus sp. (strain CC9311). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechococcus. OX NCBI_TaxID=64471 {ECO:0000313|EMBL:ABI47814.1, ECO:0000313|Proteomes:UP000001961}; RN [1] {ECO:0000313|EMBL:ABI47814.1, ECO:0000313|Proteomes:UP000001961} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CC9311 {ECO:0000313|EMBL:ABI47814.1, RC ECO:0000313|Proteomes:UP000001961}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000435; ABI47814.1; -; Genomic_DNA. DR RefSeq; WP_011619278.1; NC_008319.1. DR RefSeq; YP_730560.1; NC_008319.1. DR ProteinModelPortal; Q0IAG2; -. DR STRING; 64471.sync_1353; -. DR EnsemblBacteria; ABI47814; ABI47814; sync_1353. DR KEGG; syg:sync_1353; -. DR PATRIC; 23793714; VBISynSp88089_1415. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SSP64471:GIVP-1353-MONOMER; -. DR Proteomes; UP000001961; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001961}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABI47814.1}; KW Transferase {ECO:0000313|EMBL:ABI47814.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 238 238 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1206 AA; 132227 MW; 0EEE61501D66CEB8 CRC64; MQAVTETPTL VASRFLKRLH DPSRPVLVFD GATGTSLQQM DLSAEDFGGE ALEGCNENLV VTRPDAVQSV HRQFLDAGCD VIETDTFGAA SVVLAEYGLE SKTFELNKRA AELAKEVAME YSTDEKPRFV AGSMGPTTKL PTLGHISFDL LRDSYQEQAE GLIAGDVDLL IIETCQDVLQ IKAALQGIEQ AFETSGERRP LMVSVTMETT GTMLVGSDIA AVVAILEPFP IDVLGLNCAT GPEQMKEHMR YLTENAPFVV SCIPNAGLPE NVGGVAHYRL TPLELKMQLM HFVEDLGVQV IGGCCGTTPA HIAALSEISS ELSAAPRKVR SHHHERKALS YEAAASSIYG ATPYLQDNSF LIIGERLNAS GSKKVRELLN KEDWDGLVAV ARGQVKENAH ILDVNVDYVG RDGERDMQEL VNRVVTNVNL PLMLDSTEWQ KMEAGLKVAG GKCILNSTNY EDGDERFFKV LEISKRYGAG VVIGTIDEDG MARTADQKVA IAKRAYRDAV EFGIPAREIF YDALALPIST GIEEDRRNGA ETIEAIRRIR EDLPQVHIVL GVSNVSFGLS PAARITLNSV FLHDCCEAGM DAAIISPAKI LPLIKISEEH QKVCRDLIND RRGFEGDVCT YDPLTELTTL FEGVSAKAAR ESGPSLSDLP VEERLKQHII DGERIGLEDA LKEGLSSYPP LEIVNTFLLD GMKVVGELFG SGQMQLPFVL QSAETMKSAV AFLEPFMEKE EGERSAKAKF LIATVKGDVH DIGKNLVDII LTNNGYEVIN LGIKQDVNAI IAAQEEHQAD CIAMSGLLVK STAFMKDNLK AFNEAGINVP VVLGGAALTP RFVNKDCSDV YDGKVIYGRD AFTDLRFMDA LVAAKSKDRW DDRSGFLDGT PEGLSIGGDA DHSDSANAST QSSSQQVETP DLKLPVTYHR SDAVPEEKAV ITPFLGASVL QGEDQIPLDE VIAFLDRQAL FAGQWQMRKA KNQSREEYEQ DLSDKAEPIL QKWLARAKED QLLQPAVAYG YFPSGRDGNS VVVFNPEGGA ELGRFDVPRQ RSGNRYCIAD FFLDLNEGEP CDVLPMQAVT MGAEASRFSE ELFRNDAYSD YLFFHGLAVQ MAEALAEWTH ARIRRECGFS DPDGMPLRDI LAQRYRGSRY SFGYPACPNV ADSRQQLEWL QADRIGLTMD ESDQLHPEQS TTALVALHST ARYFSA // ID Q0KFB9_CUPNH Unreviewed; 319 AA. AC Q0KFB9; DT 03-OCT-2006, integrated into UniProtKB/TrEMBL. DT 03-OCT-2006, sequence version 1. DT 27-MAY-2015, entry version 58. DE SubName: Full=BhmT protein {ECO:0000313|EMBL:CAJ91302.1}; DE EC=2.1.1.5 {ECO:0000313|EMBL:CAJ91302.1}; GN Name=bhmT {ECO:0000313|EMBL:CAJ91302.1}; GN OrderedLocusNames=H16_A0150 {ECO:0000313|EMBL:CAJ91302.1}; 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 {ECO:0000313|EMBL:CAJ91302.1, ECO:0000313|Proteomes:UP000008210}; RN [1] {ECO:0000313|EMBL:CAJ91302.1, ECO:0000313|Proteomes:UP000008210} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17699 / H16 / DSM 428 / Stanier 337 RC {ECO:0000313|Proteomes:UP000008210}; 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., Potter 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; CAJ91302.1; -; Genomic_DNA. DR RefSeq; WP_011614374.1; NC_008313.1. DR RefSeq; YP_724670.1; NC_008313.1. DR STRING; 381666.H16_A0150; -. DR EnsemblBacteria; CAJ91302; CAJ91302; H16_A0150. DR KEGG; reh:H16_A0150; -. DR PATRIC; 35229661; VBIRalEut6770_0502. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; CNEC381666:GJUJ-150-MONOMER; -. DR Proteomes; UP000008210; Chromosome 1. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008210}; KW Methyltransferase {ECO:0000313|EMBL:CAJ91302.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008210}; KW Transferase {ECO:0000313|EMBL:CAJ91302.1}. SQ SEQUENCE 319 AA; 34446 MW; A07C4570C3B4346E CRC64; MGTMIQRYKL TEADYRGARF AEHKVDVKGN NELLLLTRPQ VISEIHEQYL AAGADLIETN TFGATGVAQE DYKMADLAYE MNVEAARLAR AACDKYSTPE KPRFVAGAFG PTPKTASISP DVNDPGARNV TFEELRDSYY EQGKGLLEGG ADVFLVETIF DTLNAKAALF AIDQLFEDTG ERLPVMISGT VTDASGRILS GQTVEAFWNS LRHARPITFG LNCALGATLM RPYIAELAKI CDAAVSCYPN AGLPNPMSDT GFDETPEVTS SLVEEFAASG LVNLVGGCCG TTPEHIAAIA QRVANKTPRT WPGQYRDAA // ID Q0RU92_FRAAA Unreviewed; 1200 AA. AC Q0RU92; DT 05-SEP-2006, integrated into UniProtKB/TrEMBL. DT 05-SEP-2006, sequence version 1. DT 27-MAY-2015, entry version 70. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CAJ58851.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAJ58851.1}; GN Name=metH {ECO:0000313|EMBL:CAJ58851.1}; GN OrderedLocusNames=FRAAL0172 {ECO:0000313|EMBL:CAJ58851.1}; OS Frankia alni (strain ACN14a). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Frankineae; Frankiaceae; Frankia. OX NCBI_TaxID=326424 {ECO:0000313|EMBL:CAJ58851.1, ECO:0000313|Proteomes:UP000000657}; RN [1] {ECO:0000313|EMBL:CAJ58851.1, ECO:0000313|Proteomes:UP000000657} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ACN14a {ECO:0000313|Proteomes:UP000000657}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CT573213; CAJ58851.1; -; Genomic_DNA. DR RefSeq; WP_011601433.1; NC_008278.1. DR RefSeq; YP_710464.1; NC_008278.1. DR ProteinModelPortal; Q0RU92; -. DR SMR; Q0RU92; 626-879. DR STRING; 326424.FRAAL0172; -. DR KEGG; fal:FRAAL0172; -. DR PATRIC; 21910345; VBIFraAln347_0145. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; QPFFNAW; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; FALN326424:GJ82-167-MONOMER; -. DR Proteomes; UP000000657; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000657}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAJ58851.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000657}; KW Transferase {ECO:0000313|EMBL:CAJ58851.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 744 744 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1200 AA; 129112 MW; 0D2F5C7ADAEB84B7 CRC64; MVVLDGAWGT MLQNAGLTPA DYQLDSLRDH PKDVTGDPDL LNLTRPDIIL DVHRQYLAAG ADITTTNTFT ATSIGQADYG LESLVREMNL RGAQLARQAA DEAGGRFVAG SIGPLNVTLS LSPRVEDPAY RAVTFDQVRA AYAEQIQALA DGGVDLLLIE TIFDTLNAKA AIAAAREVAP QLPLWISVTI VDLSGRTLSG QTVEAFWDSI AHANPLVVGV NCSLGAEEMR PHVEALARIA GTYTACHPNA GLPNAFGGYD QTPEEAGRLI GEFAAAGMVN IVGGCCGTTP AHIARIAAAV DGTAPRQVPT PTPRTRFSGL EPFEIGEDTG FVMIGERTNV TGSARFRRLV EADDYQAAVD VALEQVRGGA NLLDVNMDAD LLDSEQAMTT FLNLLATEPE AARLPIMIDS SRWSVLEAGL RCVQGKGVVN SISLKEGEEV FLDHARRIRD FGAGVVVMAF DEQGQADTTE RKVAICGRAY DLLTGKLGFP ATDIIFDPNV LAVATGIPEH NGYAKAFIDA LPLIKQRCPG VRISGGISNL SFSFRGNDVV REAMHSAFLL HAVRAGLDMG IVNAGQLAVY ADIPAELLEL VEDVLFDRRE DATDRLVAFA ETVSGKGTQR VVDLSWREAP VAARLSHALV HGIVDFIEAD TEEARAAAAR PLDVIEGPLM DGMKIVGDLF GSGKMFLPQV VKSARVMKRS VAYLEPFMEA EKAQAALDDS AAGRPAARRG NGKVVLATVK GDVHDIGKNI VGVVLGCNNY EVIDLGVMVP AKVILDTAVA EGADAVGLSG LITPSLDEMV AVGAEMQRRG LRLPLLIGGA TTSRQHTAVR IAPVYEATTV HVLDASRVVG VVSDLLDAER AEQLDVRNRA EQARLREQHE NRRAQPLLGL EQARANREQV SFDELPVPAF TGRRIVTPDL TALREMIDWQ FFFLAWELKG KFPAILDEPV ARELFDEANV LLDQIIKDGS LQAKGVYGFW PAFADGDDLV IEAGEVAGAR DGVLRLPMLR QQTTKPTGRP NRSLADYVAP AGDHLGGFAV AVHGADTLAA EFEARQDDYR SIMVKALADR LAEAFAEYIH LAARREWFEP DAEPSLADLH AERFRGIRPA LGYPASPDHS EKQALFDLLD AGQAGLGLTE SFAMTPASAV SGIIFAHPES KYFTVGRIGR DQVEDYARRR GLGVGDVERW LRPNLAYDPA // ID Q0SIE4_RHOJR Unreviewed; 1189 AA. AC Q0SIE4; DT 05-SEP-2006, integrated into UniProtKB/TrEMBL. DT 05-SEP-2006, sequence version 1. DT 27-MAY-2015, entry version 73. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABG92692.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABG92692.1}; GN Name=metH {ECO:0000313|EMBL:ABG92692.1}; GN OrderedLocusNames=RHA1_ro00859 {ECO:0000313|EMBL:ABG92692.1}; OS Rhodococcus jostii (strain RHA1). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Nocardiaceae; Rhodococcus. OX NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG92692.1, ECO:0000313|Proteomes:UP000008710}; RN [1] {ECO:0000313|Proteomes:UP000008710} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000431; ABG92692.1; -; Genomic_DNA. DR RefSeq; WP_011594083.1; NC_008268.1. DR RefSeq; YP_700850.1; NC_008268.1. DR ProteinModelPortal; Q0SIE4; -. DR STRING; 101510.RHA1_ro00859; -. DR PRIDE; Q0SIE4; -. DR EnsemblBacteria; ABG92692; ABG92692; RHA1_ro00859. DR GeneID; 4218285; -. DR KEGG; rha:RHA1_ro00859; -. DR PATRIC; 23200505; VBIRhoJos26306_0878. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; RJOS101510:GJJ1-858-MONOMER; -. DR Proteomes; UP000008710; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008710}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABG92692.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008710}; KW Transferase {ECO:0000313|EMBL:ABG92692.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 229 229 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 296 296 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 739 739 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1189 AA; 129649 MW; 76E65ADA9D6E5860 CRC64; MSAPFHSALL DALNQRVVIG DGAMGTMLQA ADLTLDDFLG LEGCNEILND TRPDVLKDIH RAYFEAGADA VETNTFGCNL PNLADYDISD RIRELAEKGT RLARDVADEM GPGRDGMGRF VLGSMGPGTK LPTLGHAPFA ILRDAYAEAA MGMIDGGADA ILVETCQDLL QVKAAILGSQ RAMETLGSRL PIITHVTVET TGTMLLGSEI GAALTALEPL GIDMIGLNCA TGPAEMSEHL RHLSKYSSLP VSVMPNAGLP QLGPNGAEYP LTAEELAEAL SGFVTEFGLG LVGGCCGTTP EHIRQVAEAV RLVEKAERNP VHESGTSSLY TAVPFQQDAS ILMIGERTNT NGSKAFREAM IAEDYQKCLD IAKDQTRDGA HMLDLNVDYV GRDGAVDMAA LASRFATSST LPIMLDSTEP AVLQAGLEHL GGRCAVNSVN YEDGDGPDSR FQKIMRLVTE HGAAVVALTI DEEGQARTAE HKVRIAERLL DDITANWGLD ESDIIIDALT FPISTGQEEV RRDGIETIEA IRELKKRHPR VHFTLGVSNI SFGLNPAARQ VLNSVFLHEC TEAGLDTAIV HASKILPMAR IPDEQRETAL DLVYDRRREG YDPLQKLMEL FEGVSAASAR ESRAQELAAL PLFERLERRI VDGERNGLDD DLTAAMEEKP PLAIINETLL SGMKTVGELF GSGQMQLPFV LQSAEVMKAA VAYLEPHMEA TDEDGKGRIV IATVKGDVHD IGKNLVDIIL SNNGYDVVNL GIKQPIATIL DAAIEQKADV IGMSGLLVKS TVVMKDNLQE LNAKGVAEKF PVLLGGAALT RSYVENDLAE VYEGDVSYAR DAFEGLHRMD EIMAVKRGGG PDPDSPEAIA AREKAAERKA RHERSKRIAE KRKAAETPIE VPERSDVATD IVVPTPPFWG NRIVKGVSLS DYSGLLDERA LFLGQWGLRG QRSGDGPTYE ELVETEGRPR LRYWLDRLST EGILAHAAVV YGYFPAVSEG DDVVVLTDPT PDAEERFRFT FPRQHRDRFL CVADFVRSRT EAKETGQVDV FPMQLVTMGQ PIADFANELF AANAYRDYLE VHGIGVQLTE SLAEYWHQRV REELVLPGGH NVAEQDPSEV SGFFDLAYRG ARYSFGYGAC PNLEDRAKMV ALLEPERIGV KLSEELQLHP EQSTDAFVLH HPEAKYFNV // ID Q0ST32_CLOPS Unreviewed; 279 AA. AC Q0ST32; DT 05-SEP-2006, integrated into UniProtKB/TrEMBL. DT 05-SEP-2006, sequence version 1. DT 27-MAY-2015, entry version 53. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:ABG86486.1}; GN OrderedLocusNames=CPR_1406 {ECO:0000313|EMBL:ABG86486.1}; OS Clostridium perfringens (strain SM101 / Type A). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=289380 {ECO:0000313|EMBL:ABG86486.1, ECO:0000313|Proteomes:UP000001824}; RN [1] {ECO:0000313|EMBL:ABG86486.1, ECO:0000313|Proteomes:UP000001824} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM101 / Type A {ECO:0000313|Proteomes:UP000001824}; 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 ----------------------------------------------------------------------- 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; ABG86486.1; -; Genomic_DNA. DR RefSeq; WP_011592371.1; NC_008262.1. DR RefSeq; YP_698725.1; NC_008262.1. DR ProteinModelPortal; Q0ST32; -. DR STRING; 289380.CPR_1406; -. DR EnsemblBacteria; ABG86486; ABG86486; CPR_1406. DR KEGG; cpr:CPR_1406; -. DR PATRIC; 19491103; VBICloPer122123_1381. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265278; -. DR KO; K00548; -. DR OMA; GTNLFAM; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CPER289380:GI76-1419-MONOMER; -. DR Proteomes; UP000001824; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001824}; KW Methyltransferase {ECO:0000313|EMBL:ABG86486.1}; KW Transferase {ECO:0000313|EMBL:ABG86486.1}. SQ SEQUENCE 279 AA; 31024 MW; 54C957CFBC226F1C CRC64; MKNLDLKNGV IIADGAMGTR IMELGVNLKE TPSELLNIKK PELIEKIHRE YIESGANLIL SNTFMCNIIN AKRNNYNLEE VIEGGISSAK KACGDHGLVA LDIGPLSYYI EENDSSFKEI VYENTERIIN ASKDKFDLVI FETLGSLKEG EFAVKKAKTL TDKKVICSFT LAYKKDIPNF IKNMVSTLEP LGVDALGINC TGYEEILMAL DILKENTNLP IMIKANLGIP KKVGEEFIYD KTLEEFKNLS KRALEKGVNI IGGCCGTTPE YIRTICNLK // ID Q0SXY9_SHIF8 Unreviewed; 1227 AA. AC Q0SXY9; DT 05-SEP-2006, integrated into UniProtKB/TrEMBL. DT 05-SEP-2006, sequence version 1. DT 27-MAY-2015, entry version 71. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:ABF06076.1}; GN Name=metH {ECO:0000313|EMBL:ABF06076.1}; GN OrderedLocusNames=SFV_4090 {ECO:0000313|EMBL:ABF06076.1}; OS Shigella flexneri serotype 5b (strain 8401). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=373384 {ECO:0000313|EMBL:ABF06076.1, ECO:0000313|Proteomes:UP000000659}; RN [1] {ECO:0000313|EMBL:ABF06076.1, ECO:0000313|Proteomes:UP000000659} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=8401 {ECO:0000313|EMBL:ABF06076.1, RC ECO:0000313|Proteomes:UP000000659}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000266; ABF06076.1; -; Genomic_DNA. DR RefSeq; WP_000096020.1; NC_008258.1. DR RefSeq; YP_691381.1; NC_008258.1. DR ProteinModelPortal; Q0SXY9; -. DR SMR; Q0SXY9; 651-1227. DR STRING; 373384.SFV_4090; -. DR EnsemblBacteria; ABF06076; ABF06076; SFV_4090. DR KEGG; sfv:SFV_4090; -. DR PATRIC; 18732433; VBIShiFle33408_4642. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SFLE373384:GHZM-4086-MONOMER; -. DR Proteomes; UP000000659; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000659}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135895 MW; 2E28CD6AD800CAC5 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLA AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGIITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKADDTANAQ QAEWRSWDVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RIAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFAIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTCKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID Q0TXM4_PHANO Unreviewed; 319 AA. AC Q0TXM4; DT 05-SEP-2006, integrated into UniProtKB/TrEMBL. DT 05-SEP-2006, sequence version 1. DT 27-MAY-2015, entry version 51. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EAT76875.1}; GN ORFNames=SNOG_15780 {ECO:0000313|EMBL:EAT76875.1}; 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 {ECO:0000313|Proteomes:UP000001055}; RN [1] {ECO:0000313|Proteomes:UP000001055} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173 RC {ECO:0000313|Proteomes:UP000001055}; RX PubMed=18024570; DOI=10.1105/tpc.107.052829; RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., RA Spatafora J.W., Crous P.W., Kodira C., Birren B.W., Galagan J.E., RA Torriani S.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; CH445364; EAT76875.1; -; Genomic_DNA. DR RefSeq; XP_001805918.1; XM_001805866.1. DR ProteinModelPortal; Q0TXM4; -. DR EnsemblFungi; SNOT_15780; SNOT_15780; SNOG_15780. DR GeneID; 5982848; -. DR KEGG; pno:SNOG_15780; -. DR InParanoid; Q0TXM4; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000001055; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001055}; KW Reference proteome {ECO:0000313|Proteomes:UP000001055}. SQ SEQUENCE 319 AA; 34590 MW; 465BA7426D86D88C CRC64; MRPNKISTHL NSSPDIPLLI DGALATYLEH LGADISGSLW SASILLSRPD LIKKTHLDYY RAGANIAITA SYQASIPGLV KHLGLGENEA KDVVKKSVQL AIEARDEYVQ SKLEESCERS VDAASLREDL FVAGSVGPYG AYLSDGSEYR GDYDVAHEAM KDFHRGRVQA LVDAGVDVLA CETIPSRRET EALLDLLQSE FRDAEAWFTF TLRDAEHIAD GTSLVDIAAL FETAEQVVGL GFNCVPDDLA LAALKNLKPL VKRGTMVVYP NSGEQWNAKA REWEGSRTEG EGLASKTVEW ERAGAGLIGG CCRTTPGGY // ID Q0VPX6_ALCBS Unreviewed; 1233 AA. AC Q0VPX6; DT 03-OCT-2006, integrated into UniProtKB/TrEMBL. DT 03-OCT-2006, sequence version 1. DT 27-MAY-2015, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CAL16772.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAL16772.1}; GN OrderedLocusNames=ABO_1324 {ECO:0000313|EMBL:CAL16772.1}; OS Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 OS / SK2). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Alcanivoracaceae; Alcanivorax. OX NCBI_TaxID=393595 {ECO:0000313|EMBL:CAL16772.1, ECO:0000313|Proteomes:UP000008871}; RN [1] {ECO:0000313|EMBL:CAL16772.1, ECO:0000313|Proteomes:UP000008871} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2 RC {ECO:0000313|Proteomes:UP000008871}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AM286690; CAL16772.1; -; Genomic_DNA. DR RefSeq; WP_011588606.1; NC_008260.1. DR RefSeq; YP_693044.1; NC_008260.1. DR ProteinModelPortal; Q0VPX6; -. DR SMR; Q0VPX6; 652-1229. DR STRING; 393595.ABO_1324; -. DR EnsemblBacteria; CAL16772; CAL16772; ABO_1324. DR KEGG; abo:ABO_1324; -. DR PATRIC; 20840413; VBIAlcBor124741_1389. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; ABOR393595:GHRI-1359-MONOMER; -. DR Proteomes; UP000008871; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008871}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAL16772.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008871}; KW Transferase {ECO:0000313|EMBL:CAL16772.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 246 246 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1233 AA; 137311 MW; 9AF6F009734202C8 CRC64; MSQNSRAQLT AQLKERILIL DGGMGTMIQR CKFTEEEFRG ARFADWPSDL KGNNDLLSMT QPERIKALHK GYLDAGADII ETNSFNSTSI AMADYDMQDL AREINVASAR VAREAADEAS TPDKPRYVAG VLGPTNRTAS ISPDVNDPGY RNTHFDALVE AYLEALDGLV EGGIDMVLIE TIFDTLNAKA AVFAVDQYCY ENNLDLPVMV SGTITDASGR TLTGQTTEAF YNSLRHARPI SFGLNCALGP MELRPYIEEL SRICETYVSA HPNAGLPNEM GEYDLDPATM AKEVRAWAEK GFLNIIGGCC GTTPEHIDAM AKAVEGLAPR PLPEIEVACR LSGLEPCTIA KDSLFVNVGE RTNVTGSKRF LRLIKEEDYD AALDVARDQV ENGAQIIDIN MDEGMLESAE CMVKFLNLVA SEPEISKVPI MIDSSKWEVI EAGLKCIQGK GVVNSISMKE GEAAFLHQAR LLRRYGAAVI VMAFDEEGQA DTRERKVEIC TRAYKLLTEE VNFPAEDIIF DPNIFAIATG IEEHNNYAVD FIEAVADIKR TLPHAMISGG VSNVSFSFRG NDTVREAIHA VFLYYAIKNG MDMGIVNPTM LAIYADIPEE LRNAVEDVVL NRNEDATEVL LDLAEKYRGS GAEKVKKEDL AWREWEVEKR LEHALVKGVA DYVEEDTELA RQNATRPLHV IEGPLMDGMN VVGDLFGEGK MFLPQVVKSA RVMKKAVAYL LPFMEKEKEE MGTQDEANGK ILMATVKGDV HDIGKNIVGV VLQCNGYDVV DMGVMVPCEK ILETAKEEKV DIIGLSGLIT PSLEEMVHVA SEMQRLGMDL PLMIGGATTS RIHTAVKIDP AYDQAVVHVA DASRAVGVAS KLLSKTAKPE YVAEIKETYE TLRVRRQQQQ VDRSLISIDQ AREHRFQPDW SDYTPHEPKV KGLKVLDDYP LEDLVQRIDW TPFFRAWELA GKFPRILEDE VVGVEATKLY RDAREMLDKI VEEKWLTARG VIGFWPANSK MDDIELYRNP GDSEAFMTLH HLRQQLDRSK NNKPDYCLSD FIAPKETGLT DWLGGFAVTA GIGIDEHVAR FEADHDDYSA IMLKALADRL AEAFAERLHE KVRKDYWGYA SDEALSNQDM ISEKYQGIRP APGYPACPDH TEKALLWELL DPETHAGMTL TESYAMLPTA AVSGWYFSHP EAKYFGTGKL AKDQMDDYAA RKGMSRKEIE RMVPHLLGYM DEN // ID Q0WTD0_ARATH Unreviewed; 333 AA. AC Q0WTD0; DT 05-SEP-2006, integrated into UniProtKB/TrEMBL. DT 05-SEP-2006, sequence version 1. DT 07-JAN-2015, entry version 54. DE SubName: Full=Homocysteine S-methyltransferase AtHMT-2 {ECO:0000313|EMBL:BAE99618.1}; GN OrderedLocusNames=At3g63250 {ECO:0000313|EMBL:BAE99618.1, GN ECO:0000313|TAIR:AT3G63250}; 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 {ECO:0000313|EMBL:BAE99618.1}; RN [1] {ECO:0000313|EMBL:BAE99618.1} 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK227627; BAE99618.1; -; mRNA. DR RefSeq; NP_191884.1; NM_116190.4. DR UniGene; At.21554; -. DR ProteinModelPortal; Q0WTD0; -. DR SMR; Q0WTD0; 21-333. DR PRIDE; Q0WTD0; -. DR DNASU; 825500; -. DR GeneID; 825500; -. DR KEGG; ath:AT3G63250; -. DR TAIR; AT3G63250; -. DR KO; K00547; -. DR OMA; SEWCKDG; -. DR PhylomeDB; Q0WTD0; -. DR ExpressionAtlas; Q0WTD0; baseline and differential. DR Genevestigator; Q0WTD0; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Methyltransferase {ECO:0000313|EMBL:BAE99618.1}; KW Transferase {ECO:0000313|EMBL:BAE99618.1}. SQ SEQUENCE 333 AA; 36451 MW; CB44D8F3BAC15D85 CRC64; MTGNSFNSMK DFLKQTGGYA VIDGGLATEF ERHGADLNDP LWSAKCLVTS PHLIHTVHLD YLEAGADIIS SASYQATIQG FEAKGFSREE SESLLKKSVE IATEARNSYY DKCGTSSSMD DKILKKRPIL VAASVGSYGA YLADGSEYSG IYGDSITLEK LKDFHRRRLQ VLAESGADLI AFETIPNKIE AQAFADLLEE GDVKIPGWFS FNSKDGVNVV SGDSIKECIS IAENCEKVVA VGINCTPPRF IEGLVLEIEK VTSKPILVYP NSGESYDADR KEWVENTGVG DEDFVSYVEK WMDAGVSLLG GCCRTTPTTI RAIHKRLVNR RSL // ID Q0YUB4_9CHLB Unreviewed; 1228 AA. AC Q0YUB4; DT 05-SEP-2006, integrated into UniProtKB/TrEMBL. DT 05-SEP-2006, sequence version 1. DT 27-MAY-2015, entry version 50. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EAT60112.1}; GN ORFNames=CferDRAFT_2119 {ECO:0000313|EMBL:EAT60112.1}; OS Chlorobium ferrooxidans DSM 13031. OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Chlorobium. OX NCBI_TaxID=377431 {ECO:0000313|EMBL:EAT60112.1}; RN [1] {ECO:0000313|EMBL:EAT60112.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 13031 {ECO:0000313|EMBL:EAT60112.1}; 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] {ECO:0000313|EMBL:EAT60112.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 13031 {ECO:0000313|EMBL:EAT60112.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EAT60112.1}. 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; AASE01000001; EAT60112.1; -; Genomic_DNA. DR RefSeq; WP_006365388.1; NZ_AASE01000001.1. DR ProteinModelPortal; Q0YUB4; -. DR SMR; Q0YUB4; 648-894. DR EnsemblBacteria; EAT60112; EAT60112; CferDRAFT_2119. DR PATRIC; 27056138; VBIChlFer75923_0290. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EAT60112.1}; KW Transferase {ECO:0000313|EMBL:EAT60112.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1228 AA; 134909 MW; 368EBCDEAEF08B78 CRC64; MKETLFTLLE KRILVLDGAM GTMIQRHKLQ EEDYRGSRFA THSHPLMGNN DILVLTRPDI IYALHCDFLE AGSDIIETNT FNANPISQSD YSAEHLVREL NVEAAKLARK AADEYTARTP DKPRFVAGSI GPTNKTLSMS PDVNNPGYRA VSFEEVVDNY TLQLEGLMEV GVDMLLVETV FDTLNCKAAL FSIEEFFNRT GVRIPVMVSG TVVDASGRTL SGQTTEAFWI SIAHMPDLLS IGLNCALGSK QMRPFIESIS GIAESLVSVY PNAGLPNEFG EYDDSPEYMA AQIADFATSG FVNIVGGCCG TTPQHIKAIA EAVKGLTPRQ RPVKKHELQL SGLEPLFVNS TTGFINVGER TNVTGSKKFA RLIKEGNYDE ALSIARQQVE SGAQVIDVNV DEGMLESEKV MKEFLNLIAS EPEISRVPVM IDSSKWSVIE NGLQCVQGKS IVNSISLKEG EELFKERARK VLQYGAATVV MAFDEKGQAD SLERRKEICK RAYDILVNEV GFPPEDIIFD PNVLTVATGI EEHNNYAVDF IESVRWIKEN LPFAKVSGGI SNVSFSFRGN EPVREAMHAA FLYHAIKAGL NMGIVNAGQL AIYEDIEPEL LLRVEDVLLN RREDATERLV SFAETIQGGG EKIEAKAAEW RNAPVEERLR HALIKGIVEF IEEDTEEARQ LYPSPLQVIE GPLMNGMNAI GDLFAEGKMF LPQVVKSARV MKRSVACLIP YIEEEKAKNK DTRAAAKILL ATVKGDVHDI GKNIVAVVLA CNNYEVVDIG VMMPCEKILE AVEREKADLL GLSGLITPSL DEMVHVAREM ERLGMKIPLL IGGATTSRMH TAVKIAPVYS GAVVQVLDAS RSVPVVNSLL NPALSPDYIA KLKEEQAGLR ESHASRSSAK SYIPLSAARS NTPSLKWDSA SVYKPLKPGI TLLEDVTVEA LRPYIDWTPF FMAWELHGRY PQILGDAKYG VEATKLFNDA ETLLDRIAGE QMLGLKGVAG IFPANSTGDD IAVYSDESRT TTLATLHTLR QQEKKAGGEP NLALADFVAP VNSGVKDYIG GFAVTAGLGI EKALKQFSLE QDDYHKIMTQ ALADRLAEAF AEMLHEKVRR ELWGYAPDEA FKPEELSGEK YQGIRPAPGY PACPDHTEKA ELFTLLNAEV STGITLTETF AMNPAASVSG LYFAHPAAKY FMLGKIGRDQ VEDYAGRKGM SIGEAEKWLA PVLDYERD // ID Q10PU4_ORYSJ Unreviewed; 282 AA. AC Q10PU4; DT 22-AUG-2006, integrated into UniProtKB/TrEMBL. DT 22-AUG-2006, sequence version 1. DT 27-MAY-2015, entry version 66. DE SubName: Full=Homocysteine S-methyltransferase 1, putative, expressed {ECO:0000313|EMBL:ABF94696.1}; DE SubName: Full=Os03g0221200 protein {ECO:0000313|EMBL:BAF11325.1}; DE SubName: Full=cDNA clone:J013128N24, full insert sequence {ECO:0000313|EMBL:BAG90705.1}; GN Name=Os03g0221200 {ECO:0000313|EMBL:BAF11325.1}; GN OrderedLocusNames=LOC_Os03g12110 {ECO:0000313|EMBL:ABF94696.1}; 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 {ECO:0000313|EMBL:ABF94696.1, ECO:0000313|Proteomes:UP000000763}; RN [1] {ECO:0000313|EMBL:BAG90705.1} 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] {ECO:0000313|EMBL:ABF94696.1, ECO:0000313|Proteomes:UP000000763} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000000763}; RX PubMed=16109971; DOI=10.1101/gr.3869505; RG The rice chromosome 3 sequencing consortium; RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., RA Haas B., Wortman J., Pertea M., Jones K.M., Kim M., Overton L., RA Tsitrin T., Fadrosh D., Bera J., Weaver B., Jin S., Johri S., RA Reardon M., Webb K., Hill J., Moffat K., Tallon L., Van Aken S., RA Lewis M., Utterback T., Feldblyum T., Zismann V., Iobst S., Hsiao J., RA de Vazeille A.R., Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., RA Rambo T., Currie J., Collura K., Kernodle-Thompson S., Wei F., RA Kudrna K., Ammiraju J.S.S., Luo M., Goicoechea J.L., Wing R.A., RA Henry D., Oates R., Palmer M., Pries G., Saski C., Simmons J., RA Soderlund C., Nelson W., de la Bastide M., Spiegel L., Nascimento L., RA Huang E., Preston R., Zutavern T., Palmer L., O'Shaughnessy A., RA Dike S., McCombie W.R., Minx P., Cordum H., Wilson R., Jin W., RA Lee H.R., Jiang J., Jackson S.; RT "Sequence, annotation, and analysis of synteny between rice chromosome RT 3 and diverged grass species."; RL Genome Res. 15:1284-1291(2005). RN [3] {ECO:0000313|EMBL:BAF11325.1} RP NUCLEOTIDE SEQUENCE. RG International Rice Genome Sequencing Project; RA Matsumoto T., Wu J., Kanamori H., Katayose Y., Fujisawa M., Namiki N., RA Mizuno H., Yamamoto K., Antonio B.A., Baba T., Sakata K., Nagamura Y., RA Aoki H., Arikawa K., Arita K., Bito T., Chiden Y., Fujitsuka N., RA Fukunaka R., Hamada M., Harada C., Hayashi A., Hijishita S., Honda M., RA Hosokawa S., Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., RA Ito K., Ito S., Ito T., Ito Y., Ito Y., Iwabuchi A., Kamiya K., RA Karasawa W., Kurita K., Katagiri S., Kikuta A., Kobayashi H., RA Kobayashi N., Machita K., Maehara T., Masukawa M., Mizubayashi T., RA Mukai Y., Nagasaki H., Nagata Y., Naito S., Nakashima M., Nakama Y., RA Nakamichi Y., Nakamura M., Meguro A., Negishi M., Ohta I., Ohta T., RA Okamoto M., Ono N., Saji S., Sakaguchi M., Sakai K., Shibata M., RA Shimokawa T., Song J., Takazaki Y., Terasawa K., Tsugane M., Tsuji K., RA Ueda S., Waki K., Yamagata H., Yamamoto M., Yamamoto S., Yamane H., RA Yoshiki S., Yoshihara R., Yukawa K., Zhong H., Yano M., Yuan Q., RA Ouyang S., Liu J., Jones K.M., Gansberger K., Moffat K., Hill J., RA Bera J., Fadrosh D., Jin S., Johri S., Kim M., Overton L., Reardon M., RA Tsitrin T., Vuong H., Weaver B., Ciecko A., Tallon L., Jackson J., RA Pai G., Aken S.V., Utterback T., Reidmuller S., Feldblyum T., RA Hsiao J., Zismann V., Iobst S., de Vazeille A.R., Buell C.R., Ying K., RA Li Y., Lu T., Huang Y., Zhao Q., Feng Q., Zhang L., Zhu J., Weng Q., RA Mu J., Lu Y., Fan D., Liu Y., Guan J., Zhang Y., Yu S., Liu X., RA Zhang Y., Hong G., Han B., Choisne N., Demange N., Orjeda G., RA Samain S., Cattolico L., Pelletier E., Couloux A., Segurens B., RA Wincker P., D'Hont A., Scarpelli C., Weissenbach J., Salanoubat M., RA Quetier F., Yu Y., Kim H.R., Rambo T., Currie J., Collura K., Luo M., RA Yang T., Ammiraju J.S.S., Engler F., Soderlund C., Wing R.A., RA Palmer L.E., de la Bastide M., Spiegel L., Nascimento L., Zutavern T., RA O'Shaughnessy A., Dike S., Dedhia N., Preston R., Balija V., RA McCombie W.R., Chow T., Chen H., Chung M., Chen C., Shaw J., Wu H., RA Hsiao K., Chao Y., Chu M., Cheng C., Hour A., Lee P., Lin S., Lin Y., RA Liou J., Liu S., Hsing Y., Raghuvanshi S., Mohanty A., Bharti A.K., RA Gaur A., Gupta V., Kumar D., Ravi V., Vij S., Kapur A., Khurana P., RA Khurana P., Khurana J.P., Tyagi A.K., Gaikwad K., Singh A., Dalal V., RA Srivastava S., Dixit A., Pal A.K., Ghazi I.A., Yadav M., Pandit A., RA Bhargava A., Sureshbabu K., Batra K., Sharma T.R., Mohapatra T., RA Singh N.K., Messing J., Nelson A.B., Fuks G., Kavchok S., Keizer G., RA Linton E., Llaca V., Song R., Tanyolac B., Young S., Ho-Il K., RA Hahn J.H., Sangsakoo G., Vanavichit A., de Mattos Luiz.A.T., RA Zimmer P.D., Malone G., Dellagostin O., de Oliveira A.C., Bevan M., RA Bancroft I., Minx P., Cordum H., Wilson R., Cheng Z., Jin W., RA Jiang J., Leong S.A., Iwama H., Gojobori T., Itoh T., Niimura Y., RA Fujii Y., Habara T., Sakai H., Sato Y., Wilson G., Kumar K., RA McCouch S., Juretic N., Hoen D., Wright S., Bruskiewich R., Bureau T., RA Miyao A., Hirochika H., Nishikawa T., Kadowaki K., Sugiura M., RA Burr B., Sasaki T.; RT "The map-based sequence of the rice genome."; RL Nature 436:793-800(2005). RN [4] {ECO:0000313|Proteomes:UP000000763} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000000763}; 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 [5] {ECO:0000313|EMBL:BAF11325.1} RP NUCLEOTIDE SEQUENCE. RG IRGSP(International Rice Genome Sequencing Project); RT "Oryza sativa nipponbare(GA3) genomic DNA, chromosome 3."; RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000313|EMBL:BAF11325.1} RP NUCLEOTIDE SEQUENCE. RG The Rice Annotation Project (RAP); RT "The Second Rice Annotation Project Meeting (RAP2)."; RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000313|EMBL:BAF11325.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=16381971; DOI=10.1093/nar/gkj094; RA Ohyanagi H., Tanaka T., Sakai H., Shigemoto Y., Yamaguchi K., RA Habara T., Fujii Y., Antonio B.A., Nagamura Y., Imanishi T., Ikeo K., RA Itoh T., Gojobori T., Sasaki T.; RT "The Rice Annotation Project Database (RAP-DB): hub for Oryza sativa RT ssp. japonica genome information."; RL Nucleic Acids Res. 34:D741-D744(2006). RN [8] {ECO:0000313|EMBL:ABF94696.1} RP NUCLEOTIDE SEQUENCE. RA Buell R., Wing R.A., McCombie W.A., Ouyang S.; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. RN [9] {ECO:0000313|EMBL:BAF11325.1} RP NUCLEOTIDE SEQUENCE. RG The Rice Annotation Project (RAP); RA Itoh T., Tanaka T., Barrero R.A., Yamasaki C., Fujii Y., Hilton P.B., RA Antonio B.A., Aono H., Apweiler R., Bruskiewich R., Bureau T., RA Burr F., Costa de Oliveira A., Fuks G., Habara T., Haberer G., Han B., RA Harada E., Hiraki A.T., Hirochika H., Hoen D., Hokari H., Hosokawa S., RA Hsing Y., Ikawa H., Ikeo K., Imanishi T., Ito Y., Jaiswal P., RA Kanno M., Kawahara Y., Kawamura T., Kawashima H., Khurana J.P., RA Kikuchi S., Komatsu S., Koyanagi K.O., Kubooka H., Lieberherr D., RA Lin Y.C., Lonsdale D., Matsumoto T., Matsuya A., McCombie W.R., RA Messing J., Miyao A., Mulder N., Nagamura Y., Nam J., Namiki N., RA Numa H., Nurimoto S., O'donovan C., Ohyanagi H., Okido T., Oota S., RA Osato N., Palmer L.E., Quetier F., Raghuvanshi S., Saichi N., RA Sakai H., Sakai Y., Sakata K., Sakurai T., Sato F., Sato Y., RA Schoof H., Seki M., Shibata M., Shimizu Y., Shinozaki K., Shinso Y., RA Singh N.K., Smith-White B., Takeda J., Tanino M., Tatusova T., RA Thongjuea S., Todokoro F., Tsugane M., Tyagi A.K., Vanavichit A., RA Wang A., Wing R.A., Yamaguchi K., Yamamoto M., Yamamoto N., Yu Y., RA Zhang H., Zhao Q., Higo K., Burr B., Gojobori T., Sasaki T.; RT "Curated Genome Annotation of Oryza sativa ssp. japonica and RT Comparative Genome Analysis with Arabidopsis thaliana."; RL Genome Res. 17:175-183(2007). RN [10] {ECO:0000313|EMBL:BAF11325.1} RP NUCLEOTIDE SEQUENCE. RG The Rice Annotation Project (RAP); RA Tanaka T., Antonio B.A., Kikuchi S., Matsumoto T., Nagamura Y., RA Numa H., Sakai H., Wu J., Itoh T., Sasaki T., Aono R., Fujii Y., RA Habara T., Harada E., Kanno M., Kawahara Y., Kawashima H., Kubooka H., RA Matsuya A., Nakaoka H., Saichi N., Sanbonmatsu R., Sato Y., Shinso Y., RA Suzuki M., Takeda J., Tanino M., Todokoro F., Yamaguchi K., RA Yamamoto N., Yamasaki C., Imanishi T., Okido T., Tada M., Ikeo K., RA Tateno Y., Gojobori T., Lin Y.C., Wei F.J., Hsing Y.I., Zhao Q., RA Han B., Kramer M.R., McCombie R.W., Lonsdale D., O'Donovan C.C., RA Whitfield E.J., Apweiler R., Koyanagi K.O., Khurana J.P., RA Raghuvanshi S., Singh N.K., Tyagi A.K., Haberer G., Fujisawa M., RA Hosokawa S., Ito Y., Ikawa H., Shibata M., Yamamoto M., RA Bruskiewich R.M., Hoen D.R., Bureau TE., Namiki N., Ohyanagi H., RA Sakai Y., Nobushima S., Sakata K., Barrero R.A., Sato Y., Souvorov A., RA Smith-White B., Tatusova T., An S., An G., OOta S., Fuks G., RA Messing J., Christie K.R., Lieberherr D., Kim H., Zuccolo A., RA Wing R.A., Nobuta K., Green P.J., Lu C., Meyers BC., Chaparro C., RA Piegu B., Panaud O., Echeverria M.; RT "The Rice Annotation Project Database (RAP-DB): 2008 update."; RL Nucleic Acids Res. 36:D1028-D1033(2008). RN [11] {ECO:0000313|Proteomes:UP000000763} RP GENOME REANNOTATION. RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000000763}; 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). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DP000009; ABF94696.1; -; Genomic_DNA. DR EMBL; AP008209; BAF11325.1; -; Genomic_DNA. DR EMBL; AK068002; BAG90705.1; -; mRNA. DR RefSeq; NP_001049411.1; NM_001055946.1. DR UniGene; Os.37866; -. DR EnsemblPlants; OS03T0221200-01; OS03T0221200-01; OS03G0221200. DR GeneID; 4332095; -. DR KEGG; osa:4332095; -. DR Gramene; Q10PU4; -. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR Proteomes; UP000000763; Chromosome 3. DR ExpressionAtlas; Q10PU4; baseline. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Complete proteome {ECO:0000313|Proteomes:UP000000763}; KW Methyltransferase {ECO:0000313|EMBL:ABF94696.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000763}; KW Transferase {ECO:0000313|EMBL:ABF94696.1}. SQ SEQUENCE 282 AA; 30870 MW; 0ABDCB66ECEF35FF CRC64; MAVAVEEIVR RAGGCAVIDG GFATQLEALG ADINDPLWSA ACLITKPHLI KEVHMQYLEA GADVIISSSY QATIPGFLAR GMLLEEAEGL LRRSIELALE ARDEFWKSTL RKSKPVYNRA LVAASIGSYG AYLADGSEYS GSYGEDITAE KLKDFHRRRL QVLASAGPDL IAFEAIPNKM EAQALVELLE EENIQVPSWI CFSSVDGKNL CSGESFAECL QFLNASDKVT IVGVNCTPPQ FIEGIIRELK KQTKKAIAVY PNSGEIWDGR AKRWLVSTTC YT // ID Q111X5_TRIEI Unreviewed; 1224 AA. AC Q111X5; DT 22-AUG-2006, integrated into UniProtKB/TrEMBL. DT 22-AUG-2006, sequence version 1. DT 27-MAY-2015, entry version 73. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABG51699.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABG51699.1}; GN OrderedLocusNames=Tery_2492 {ECO:0000313|EMBL:ABG51699.1}; OS Trichodesmium erythraeum (strain IMS101). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Trichodesmium. OX NCBI_TaxID=203124 {ECO:0000313|EMBL:ABG51699.1, ECO:0000313|Proteomes:UP000008878}; RN [1] {ECO:0000313|EMBL:ABG51699.1, ECO:0000313|Proteomes:UP000008878} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IMS101 {ECO:0000313|EMBL:ABG51699.1, RC ECO:0000313|Proteomes:UP000008878}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000393; ABG51699.1; -; Genomic_DNA. DR RefSeq; WP_011612063.1; NC_008312.1. DR RefSeq; YP_722172.1; NC_008312.1. DR ProteinModelPortal; Q111X5; -. DR STRING; 203124.Tery_2492; -. DR EnsemblBacteria; ABG51699; ABG51699; Tery_2492. DR KEGG; ter:Tery_2492; -. DR PATRIC; 23989443; VBITriEry99848_3149. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; TWTFPRQ; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; TERY203124:GJDR-2516-MONOMER; -. DR Proteomes; UP000008878; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008878}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABG51699.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008878}; KW Transferase {ECO:0000313|EMBL:ABG51699.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 238 238 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 764 764 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1224 AA; 135276 MW; A10471E9F534363C CRC64; MLSVEIPKPQ LKTSFLQRLQ SPDRPVLIFD GAMGTNIQSQ NLTAEDFGGA EYEGCNEYLV VTKPEAVAKV HRDFLAAGAD VVETDSFGSS PLVLAEYNLA DRAYELSRKA AELARSCADE FTSPEKPRFV AGSIGPGTKL PTLGHITYDE LKASFMVQAE GLYDGGADLF IVETCQDVLQ IKAALSAFEA VFAKKGSRLP LMVSVTMEIQ GTMLVGTDIS GVLAILEPFP IDILGLNCAT GPNLMTSHIK YLSENSPFPI SCIPNAGLPE NIGGQAHYKM TPLEFKTSMS EFIGQYGVQI VGGCCGTRPA HIQALADAVE ETPLKERSVR KNAVGKVRTP LSYTPAAASI YSAQTYEQDN SFLIVGERLN ASGSKKVRKL LNEDDWDGLL AIAKSQVKEG AHMLDVNVDY VGRDGERDMR ELVSRLVTNT TLPLMLDSTE WTKMEAGLKV AGGKCLLNST NYEDGEERFF KVLELAKEYG AGVVIGCIDE EGMARTAKKK FEIAQRAYKD ALKFGIPPHE IFYDTLALPI STGIEEDREN AKATIESIRL IRENLPGVHF MLGVSNISFG LSPATRITLN SIFLNEAMKA GMDGAIVSAA KILPLSKIDE EHQQICCDLI YDNRKFEGDI CTYDPLTKLT EIFAGVSAKD ARSGPSLADL PIDQRLKQHI IDGERIGLED ALKVALDAGH KALEIINTFL LDGMKVVGEL FGSGQMQLPF VLQSAETMKS AVAFLEPYME KIEGEDEDRG KGKFLIATVK GDVHDIGKNL VDIILTNNGY KVINLGIKQA IEAIVEAYEQ HKPDCIAMSG LLVKSTAFMK ENLAAFNAKG ITVPVILGGA ALTPKFVYGD CQDTYQGQVI YGKDAFADLT FMDRLMPAKD KDCWVDTEGF TGEFAQFNQR GRKAIKDLER ELNGDGEKSD GEVNGNGKKP NKPTVIDTKR STDVAIDIER PAPPFWGTKI LQSGDLKLEE LFWYMDLQAL FAGQWQFRKP KGQPREEYDW FLASKVYPIL EEWKQKVRTE QWLEPTLVYG YFPCAAIGNS VHVYDPSVIE QGLTPTTATP FVTWTFPRQK SMRRLCIADF IRPLEHDQFD VLPMQAVTMG EIATQKAQEL YQGNEYTNYL YFHGMAVQLA EALAEWSHAR IRRELGYGDL EPDNIRDILA QRYQGSRYSF GYPACPVVID QVPQLQLLGA DRIGVSIDES EQLYPEQTTT AFVIYHPVAR YFSA // ID Q116Y2_TRIEI Unreviewed; 1197 AA. AC Q116Y2; DT 22-AUG-2006, integrated into UniProtKB/TrEMBL. DT 22-AUG-2006, sequence version 1. DT 27-MAY-2015, entry version 74. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABG50442.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABG50442.1}; GN OrderedLocusNames=Tery_1073 {ECO:0000313|EMBL:ABG50442.1}; OS Trichodesmium erythraeum (strain IMS101). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Trichodesmium. OX NCBI_TaxID=203124 {ECO:0000313|EMBL:ABG50442.1, ECO:0000313|Proteomes:UP000008878}; RN [1] {ECO:0000313|EMBL:ABG50442.1, ECO:0000313|Proteomes:UP000008878} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IMS101 {ECO:0000313|EMBL:ABG50442.1, RC ECO:0000313|Proteomes:UP000008878}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000393; ABG50442.1; -; Genomic_DNA. DR RefSeq; WP_011610828.1; NC_008312.1. DR RefSeq; YP_720915.1; NC_008312.1. DR ProteinModelPortal; Q116Y2; -. DR STRING; 203124.Tery_1073; -. DR PRIDE; Q116Y2; -. DR EnsemblBacteria; ABG50442; ABG50442; Tery_1073. DR KEGG; ter:Tery_1073; -. DR PATRIC; 23985788; VBITriEry99848_1333. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; ILESWIT; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; TERY203124:GJDR-1080-MONOMER; -. DR Proteomes; UP000008878; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008878}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABG50442.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008878}; KW Transferase {ECO:0000313|EMBL:ABG50442.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 229 229 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 296 296 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 738 738 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1197 AA; 132867 MW; 4E3FFC03F6C8EC46 CRC64; MMNSQFLNRL HSPERPVIVF DGAMGTSLQV QNLTAEDFGG KEYEGCNEYL VHTKPDAVAK VHRDFLAAGA DVIETDTFGG TKIVLAEYDL ADQAYYLNKT AAELAKSAAA EYSTPEKPRF VAGSIGPGTK LPTLGHIDFA TLKDSFTEQA EGLFDGGVDL FLVETCQDVL QIKAALNGIE EIFAKKGDRR PIMVSVTMES FGTMLVGSEI NAALTILEPY SIDILGLNCA TGPDLMKEHI RYLSENSPFI VSCIPNAGLP ENIGGQAHYK LTPVELKMAL MHFVEDLGVQ VIGGCCGTRP DHIKALAEIT ETLKPKERKP NYIPAAASIY SSETYEQDNS FLIVGERLNA SGSKKCRTLL NDEDWDGLVA LAKSQVKEGA QILDVNVDYV GRDGVRDMHE LASRLVTNVN LPLMLDSTEW EKMEAGLKVA GGKCLLNSTN YEDGEPRFYQ VLELAKKYGA GVVVGTIDED GMARTADKKF EIAKRAYDAA IEYGIPAREL FFDTLALPIS TGIEEDRENG KATIEAIKRI REELPGCHIM LGVSNVSFGL NPAARQVLNS VFLHESMAVG LDGAIVSANK ILPLAKIEPK HQDICRKLIY DQRQFEGDIC VYDPLTELTK MFEGKTTKKD RSATENLPIE ERLKQHIIDG ERIGLEDALR KALETYPPLD IINVFLLNGM KVVGELFGSG QMQLPFVLQS AQTMKAAVAY LQPYMEKEES GDNSKGTFLI ATVKGDVHDI GKNLVDIILS NNGYRVINLG IKQPVDNIIT AYREHNVDCI AMSGLLVKST AFMKDNLETF NQEGITVPVI LGGAALTPKF VHEDCQNTYK GKVVYGKDAF SDLNFMDKLM PAKAEKQWDD IQGFLNELAE ENGNGNGNGN GNGNGNGNGN GKVATSVKSE DQEESQTAAP VDTRRSDDVP VDIERPTPPF WGTKLLQPED MPFEELFWYL DLQALIAGQW QFRKPKDQSR EEYDEFLAEK VYPILETWKS RVITEKLLHP QAIYGYFPCQ AEGNTLLIYD SEEMSQTGKA TKVVNSFEFP RQKSGRRLCI TDFFAPKESG VIDVFPMHAV TVGEIATEFA QKLFADNQYT DYLYFHGMAV QTAEAMAEWL HARIRRELGF GSKDADNIKD ILRQRYQGSR YSFGYPACPN MQDQFKQLDL LETKRIDMYM DESEQLYPEQ STTAIVTYHS AAKYFSA // ID Q11KQ1_CHESB Unreviewed; 312 AA. AC Q11KQ1; DT 22-AUG-2006, integrated into UniProtKB/TrEMBL. DT 22-AUG-2006, sequence version 1. DT 27-MAY-2015, entry version 51. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABG62024.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ABG62024.1}; GN OrderedLocusNames=Meso_0624 {ECO:0000313|EMBL:ABG62024.1}; OS Chelativorans sp. (strain BNC1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Chelativorans. OX NCBI_TaxID=266779 {ECO:0000313|EMBL:ABG62024.1, ECO:0000313|Proteomes:UP000001820}; RN [1] {ECO:0000313|EMBL:ABG62024.1, ECO:0000313|Proteomes:UP000001820} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BNC1 {ECO:0000313|EMBL:ABG62024.1, RC ECO:0000313|Proteomes:UP000001820}; 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; ABG62024.1; -; Genomic_DNA. DR RefSeq; WP_011579967.1; NC_008254.1. DR RefSeq; YP_673189.1; NC_008254.1. DR ProteinModelPortal; Q11KQ1; -. DR STRING; 266779.Meso_0624; -. DR EnsemblBacteria; ABG62024; ABG62024; Meso_0624. DR KEGG; mes:Meso_0624; -. DR PATRIC; 21341146; VBICheSp72577_1218. DR eggNOG; COG2040; -. DR HOGENOM; HOG000179103; -. DR OMA; CCGTDHR; -. DR OrthoDB; EOG6R5C46; -. DR BioCyc; CSP266779:GI09-631-MONOMER; -. DR Proteomes; UP000001820; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001820}; KW Methyltransferase {ECO:0000313|EMBL:ABG62024.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001820}; KW Transferase {ECO:0000313|EMBL:ABG62024.1}. SQ SEQUENCE 312 AA; 34374 MW; DD85AA656B6383BE CRC64; MTDHRDRLPQ LSGSFLTDGG IETTLIFHKG LDLPHFASYA LLDDRAGRDA LKSYYRDYLR IAEERGVGFI LESPTWRCSR DWGAKLGHDT QRIETFNREA IKLMEELRRE ARTGAPIVIS GNIGPRGDGY APEAQLSPDE AEEYHIHQIR TFADTAADMV AAVTITHTGE AIGIARAARS AGIPVAISFT TETDGRLPSG ETLGEAIEKV DDATDATPAY YMVNCAHPDH FANALDEGEW RARILGVRAN ASRKSHAELD NSDVLDPGDP VELAQDYMRL RRKLPNLSVF GGCCGTDHRH IEQICITCLE AA // ID Q11LJ3_CHESB Unreviewed; 1264 AA. AC Q11LJ3; DT 22-AUG-2006, integrated into UniProtKB/TrEMBL. DT 22-AUG-2006, sequence version 1. DT 01-APR-2015, entry version 72. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABG61732.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABG61732.1}; GN OrderedLocusNames=Meso_0328 {ECO:0000313|EMBL:ABG61732.1}; OS Chelativorans sp. (strain BNC1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Chelativorans. OX NCBI_TaxID=266779 {ECO:0000313|EMBL:ABG61732.1, ECO:0000313|Proteomes:UP000001820}; RN [1] {ECO:0000313|EMBL:ABG61732.1, ECO:0000313|Proteomes:UP000001820} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BNC1 {ECO:0000313|EMBL:ABG61732.1, RC ECO:0000313|Proteomes:UP000001820}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000390; ABG61732.1; -; Genomic_DNA. DR RefSeq; WP_011579675.1; NC_008254.1. DR RefSeq; YP_672897.1; NC_008254.1. DR ProteinModelPortal; Q11LJ3; -. DR SMR; Q11LJ3; 676-1256. DR STRING; 266779.Meso_0328; -. DR EnsemblBacteria; ABG61732; ABG61732; Meso_0328. DR KEGG; mes:Meso_0328; -. DR PATRIC; 21340522; VBICheSp72577_0908. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CSP266779:GI09-333-MONOMER; -. DR Proteomes; UP000001820; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001820}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABG61732.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001820}; KW Transferase {ECO:0000313|EMBL:ABG61732.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 266 266 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 329 329 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 330 330 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 786 786 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1264 AA; 138787 MW; 5A72A8D0ABCB3C5F CRC64; MSQTNTPLAE LFGDIAAKPD GSEISAALKA AARERILVLD GAMGTQIQGL GFDESHFRGD RFGGCACHQQ GNNDLLILTQ PKAIEEIHYQ YAIAGADIIE TNTFSSTRIA QADYGMEEMV YELNRDGARL ARRAVKRAEQ EDGKRRFVAG ALGPTNRTAS ISPDVNNPGY RAITFDDLRI ANGEQIRGLI DGGVDIILIE TIFDTLNAKA AVFAAEEVFI EKGVRLPVMI SGTITDLSGR TLSGQTPTAF WHSVRHANPF TIGLNCALGA AAMRPHLAEL SSAADTFTCA YPNAGLPNEF GQYDESPEAM AAQIEEFARE GLVNIVGGCC GSTPEHIRAI AEAAAKHKPR ELPKPPRLMR LSGLEPFTLS KDIPFVNIGE RTNVTGSARF RKLITAGDFA AALDVARDQV ANGAQVIDVN MDEGLIDSKK AMVEYLNLIA AEPDIARVPV MIDSSKWEVI EAGLKCVQGK PIVNSISMKE GEEAFLHQAR LCRAYGAAVV VMAFDETGQA DTKARKVEIC TRAYKILTEK VGFPPEDIIF DPNIFAVATG IEEHDNYGVD FIEAAREITK TLPHVHVSGG VSNLSFSFRG NEPVREAMHA VFLYHAIHAG MDMGIVNAGQ LAVYDTIDPE LREACEDVVL NRKPEAGGTA TERLLELAER YKGTGGKEAK ERDLAWREWP VEKRLEHALV NGITEFIEED TEEARQKAER PLHVIEGPLM AGMNVVGDLF GAGKMFLPQV VKSARVMKQA VAVLLPYMEA EKLANGGGGR ESAGKILMAT VKGDVHDIGK NIVGVVLACN NYEIIDLGVM VPATKILQTA RDEKVDIIGL SGLITPSLDE MVHVASEMER EGFDIPLLIG GATTSRVHTA VKIHPRYSQG QAIYVTDASR AVGTVSNLLS PETKAEYVET LRAEYKKVAE AHARSEAEKQ RLPLAKARQN AYRIDWSNYQ PPKPTFLGTK VFETWDLAEL SRYIDWTPFF QTWELKGRYP KILEDEKQGA AARQLFDDAQ EMLKKIIDEK WFAPRAAIGF WPANSVGDDI RLYTDESRNE ELATLFTLRQ QLTKRDGKAN LALADFIAPE GIGKPDYLGG FVVTAGIEEV AIAERFERAN DDYSSILVKA LADRFAEAFA ERMHERVRKE FWGYASDEAF TPEELIGEPY KGIRPAPGYP AQPDHTEKTT LFALLDAEKN TGVTLTESYA MWPGSSVSGL YLAHPESYYF GVAKVERDQV EDYARRKGME TAEVERWLGP VLNYTAAPFA EAAE // ID Q11V62_CYTH3 Unreviewed; 338 AA. AC Q11V62; DT 22-AUG-2006, integrated into UniProtKB/TrEMBL. DT 22-AUG-2006, sequence version 1. DT 27-MAY-2015, entry version 55. DE SubName: Full=Methionine synthase I, homocysteine S-methyltransferase {ECO:0000313|EMBL:ABG58704.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABG58704.1}; GN Name=metH {ECO:0000313|EMBL:ABG58704.1}; GN OrderedLocusNames=CHU_1433 {ECO:0000313|EMBL:ABG58704.1}; OS Cytophaga hutchinsonii (strain ATCC 33406 / NCIMB 9469). OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae; OC Cytophaga. OX NCBI_TaxID=269798 {ECO:0000313|EMBL:ABG58704.1, ECO:0000313|Proteomes:UP000001822}; RN [1] {ECO:0000313|EMBL:ABG58704.1, ECO:0000313|Proteomes:UP000001822} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33406 / NCIMB 9469 {ECO:0000313|Proteomes:UP000001822}; 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; ABG58704.1; -; Genomic_DNA. DR RefSeq; WP_011584819.1; NC_008255.1. DR RefSeq; YP_678044.1; NC_008255.1. DR STRING; 269798.CHU_1433; -. DR EnsemblBacteria; ABG58704; ABG58704; CHU_1433. DR KEGG; chu:CHU_1433; -. DR PATRIC; 21593703; VBICytHut34013_1425. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; CHUT269798:GJ83-1430-MONOMER; -. DR Proteomes; UP000001822; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001822}; KW Methyltransferase {ECO:0000313|EMBL:ABG58704.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001822}; KW Transferase {ECO:0000313|EMBL:ABG58704.1}. SQ SEQUENCE 338 AA; 36850 MW; EA73CB724B093E6E CRC64; MTKADIRGEL AKRILILDGA MGTMIQRYTL EEEDFRNDKL KNHDHPLKGN NDLLSFTRPD VIKAIHTEYL AAGADIIETN TFSGTTIAQA DYRLEHMVYD INYYGAKIAR EAVDEFMKKN PSSPQRYVAG AIGPTNRTAS ISPDVNDPGY RAVTFDELAK AYKDQAIALL EGGADLLLIE TIFDTLNSKA AIYAIMELFE ETGNEVPVMV SATITDASGR TLSGQTTEAF LISVSHGPLL SVGLNCALGA KELRPYLQVL AKEAPFFVSA YPNAGLPNEF GQYDETPAQM AEQITVFLEE GLVNILGGCC GSTPDHIRAM AEVAAKFAPR KLDETVEA // ID Q12H55_POLSJ Unreviewed; 348 AA. AC Q12H55; DT 22-AUG-2006, integrated into UniProtKB/TrEMBL. DT 22-AUG-2006, sequence version 1. DT 27-MAY-2015, entry version 56. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABE42137.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABE42137.1}; GN OrderedLocusNames=Bpro_0172 {ECO:0000313|EMBL:ABE42137.1}; OS Polaromonas sp. (strain JS666 / ATCC BAA-500). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Polaromonas. OX NCBI_TaxID=296591 {ECO:0000313|EMBL:ABE42137.1, ECO:0000313|Proteomes:UP000001983}; RN [1] {ECO:0000313|EMBL:ABE42137.1, ECO:0000313|Proteomes:UP000001983} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JS666 / ATCC BAA-500 {ECO:0000313|Proteomes:UP000001983}; 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 ----------------------------------------------------------------------- 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; ABE42137.1; -; Genomic_DNA. DR RefSeq; WP_011481147.1; NC_007948.1. DR RefSeq; YP_547035.1; NC_007948.1. DR ProteinModelPortal; Q12H55; -. DR STRING; 296591.Bpro_0172; -. DR EnsemblBacteria; ABE42137; ABE42137; Bpro_0172. DR KEGG; pol:Bpro_0172; -. DR PATRIC; 22953380; VBIPolSp102244_0179. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; PSP296591:GHI4-893-MONOMER; -. DR Proteomes; UP000001983; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001983}; KW Methyltransferase {ECO:0000313|EMBL:ABE42137.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001983}; KW Transferase {ECO:0000313|EMBL:ABE42137.1}. SQ SEQUENCE 348 AA; 37863 MW; A5D5F43F3A3A347D CRC64; MKPLNYTRGQ QLPAILEQRI AILDGAMGTM IQRFKLNEAQ YRGERFKDFH KDVKGNNELL SLTRPDVIRD IHEGYLAAGA DMIETNTFGA TTVAQADYDM ADLAVEMNYE SARIARAACD KFSTPDKPRF VVGALGPTPK TASISPDVND PGARNTSFEE LRKAYYEQTE ALVKGGSDVL LVETIFDTLN AKAALFAIDE YFDNSGECLP LIISGTVTDA SGRILSGQTV TAFWHSVRHA RPLAIGLNCA LGATLMRPYI QELARVAGDT FISCYPNAGL PNPMSDTGFD ETPDVTSRLL REFADEGLVN IVGGCCGTTP EHIQAIAHAV APLPSRAVAS RFFYREAA // ID Q12Q73_SHEDO Unreviewed; 1241 AA. AC Q12Q73; DT 22-AUG-2006, integrated into UniProtKB/TrEMBL. DT 22-AUG-2006, sequence version 1. DT 27-MAY-2015, entry version 70. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABE54403.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABE54403.1}; GN OrderedLocusNames=Sden_1115 {ECO:0000313|EMBL:ABE54403.1}; OS Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=318161 {ECO:0000313|EMBL:ABE54403.1, ECO:0000313|Proteomes:UP000001982}; RN [1] {ECO:0000313|EMBL:ABE54403.1, ECO:0000313|Proteomes:UP000001982} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OS217 / ATCC BAA-1090 / DSM 15013 RC {ECO:0000313|Proteomes:UP000001982}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000302; ABE54403.1; -; Genomic_DNA. DR RefSeq; WP_011495565.1; NC_007954.1. DR RefSeq; YP_562126.1; NC_007954.1. DR ProteinModelPortal; Q12Q73; -. DR SMR; Q12Q73; 660-899. DR STRING; 318161.Sden_1115; -. DR EnsemblBacteria; ABE54403; ABE54403; Sden_1115. DR KEGG; sdn:Sden_1115; -. DR PATRIC; 23487974; VBISheDen79529_1185. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SDEN318161:GHKQ-1150-MONOMER; -. DR Proteomes; UP000001982; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001982}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABE54403.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001982}; KW Transferase {ECO:0000313|EMBL:ABE54403.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 251 251 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 315 315 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 767 767 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1241 AA; 137033 MW; D165A78C497968D8 CRC64; MATAAHSTTL VQLTELLAQR IVMLDGAMGT MIQDYKLEEA DYRGQRFKDW HCDVKGNNDL LVLSQPQIIK QIHLDYLLAG SDIIETNTFN ATTIAMADYD MQALAAEINQ VGARLAREAA DEISTQTGIR RYVAGVLGPT NRTCSISPDV NDPSFRNVSF DQLVKAYLES SLALIQGGAD IIMVETIFDT LNAKAALFAI EKAFDVLGER LPVMVSGTIT DASGRTLTGQ TTEAFYNSLR HIKPISIGLN CALGPKELRP YVEELARISE TYISVHPNAG LPNEFGGYDE TPAEMAEILA QWAEEGLVNI VGGCCGSTPA HIRAIAEAVD KFDARALPDI AIACRLSGLE PLTIDSNSLF VNVGERANVT GSAKFLRLIK EEKFEEALDV VREQVENGAQ IIDVNMDEGM LDGVAAMSQF LNLIASEPDI SRVPIMIDSS KWEVIEAGLK CVQGKAIVNS ISMKEGEAAF IKQATLVKRY GAAAIVMAFD EDGQADTRKR KTEICTRAYR LLVDVVGFPP EDIIFDPNIF AIATGIDEHD NYAVDFIESI KDIKANLPHA MISGGVSNVS FSFRGNNPVR EAIHAVFLYH AIQAGMDMGI VNAGQLAIYD DIDPELKLRV ENVVRNLPCP VADSSNTEQL LEIAEQFRGD GSQEVKKEDS AWRSLPVAER LSYALVKGIT EFIDEDTEAA RLESVRPLDV IEGPLMNGMN VVGDLFGSGK MFLPQVVKSA RVMKKAVAYL NPYIELEKVE GQSNGKILMV TVKGDVHDIG KNIVGVVLAC NGYEVIDLGV MVSIEKIIEV ARAEKVDIIG MSGLITPSLD EMVHNVKTLI REGLSLPVII GGATCSKIHT AVKIAPHYPP GAIYIADASR AVPMVAKLIG NQTRQDTIDA TYVEYQEMRE KRLSQTKRKT ITSLAKAREN RCQHDWQDYT PVKPKILGRQ VFEDYPLSDL VERIDWTPFF RSWELHGRYP EILNDKIVGV EAQKLFEDGK AMLEQIISEK WLTAKAVIGL FPANTVNFDD IELYACDGTD EDRSQPIMTT HHLRMQLERV GNDNFCLADF VAPKDSGVAD YMGGFAVTAG HGIDEHVARF EANHDDYSAI MLKCLADRLA EAFAERMHER VRKEFWGYAA DETLDNEALI REKYKGIRPA PGYPACPDHT EKGLLWELLK PDETIGLNIT ESYAMFPTAA VSGWYFAHPK SRYFGVTNIG RDQVEDYAAR KGMSVTETER WLAPVLDYDP E // ID Q133H5_RHOPS Unreviewed; 1293 AA. AC Q133H5; DT 31-OCT-2006, integrated into UniProtKB/TrEMBL. DT 31-OCT-2006, sequence version 1. DT 27-MAY-2015, entry version 64. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABE40764.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABE40764.1}; GN OrderedLocusNames=RPD_3541 {ECO:0000313|EMBL:ABE40764.1}; OS Rhodopseudomonas palustris (strain BisB5). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Rhodopseudomonas. OX NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE40764.1, ECO:0000313|Proteomes:UP000001818}; RN [1] {ECO:0000313|EMBL:ABE40764.1, ECO:0000313|Proteomes:UP000001818} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BisB5 {ECO:0000313|EMBL:ABE40764.1, RC ECO:0000313|Proteomes:UP000001818}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000283; ABE40764.1; -; Genomic_DNA. DR RefSeq; WP_011503930.1; NC_007958.1. DR RefSeq; YP_570665.1; NC_007958.1. DR ProteinModelPortal; Q133H5; -. DR SMR; Q133H5; 655-908. DR STRING; 316057.RPD_3541; -. DR EnsemblBacteria; ABE40764; ABE40764; RPD_3541. DR KEGG; rpd:RPD_3541; -. DR PATRIC; 23282223; VBIRhoPal120395_3667. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; RPAL316057:GHDC-3601-MONOMER; -. DR Proteomes; UP000001818; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001818}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABE40764.1}; KW Transferase {ECO:0000313|EMBL:ABE40764.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 770 770 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1293 AA; 140053 MW; 0831D3D1FF0EA71B CRC64; MTKPISPKRT ELLALAAERI LVLDGAMGTM IQQLQFDEAA FRGDRYKDFH RDLRGNNDLL ILTQPQAIED IHAAYLRAGA DIVATNTFSS TSIAQADYDL SEIAYEMSFE GARLARNAAA TVAAEDGKPR FVAGAIGPTN RTASISPDVS NPGYRAVTFD DLRIAYGEQI NGLLDGGADL LLLETIFDTL NAKAALYAIA EITEARGIDV PVMISGTITD KSGRLLSGQM PEAFWNSVRH ARPITIGFNC ALGAEDMRAH VADLSRVADA LVCAYPNAGL PNEFGQYDET PAQMARIVGE FARDGLVNIV GGCCGTTPDH IAAIAQAVAP HKPRVVPEIA PRLRLSGLEP FELTPDIPFV NVGERTNVTG SAKFRKLITA GDYAAALQVA RDQVENGAQI IDVNMDEGLL DSEAAMVTFL NLVAAEPDIA KVPVMVDSSK FAVIEAGLKC LQGKPVVNSI SLKEGEEKFL HEANIARRHG AAVVVMAFDE KGQADTYARK TEICKRAYDI LVDQIGFPPE DIIFDPNIFA IATGLEEHNN YGVDFIEATR WIRKNLPHAH VSGGVSNLSF SFRGNEPVRE AMHSVFLYHA IKAGMDMGIV NAGQMIVYDD IDAELRQVCE DVILNRDPGA SERLLALAEK YRGQGKAAKE QDLAWRGWPV EQRLSHALVH GITEYIETDT EEARAKAERP LHVIEGPLMA GMNVVGDLFG DGKMFLPQVV KSARVMKQAV AYLMPFMEAE KAAQLAAGTH TGERATAGKI VLATVKGDVH DIGKNIVGIV LQCNNFEVID LGVMVPAAKI IETAKAEGAD IIGLSGLITP SLDEMSFLAA EMQRNGLDMP LLIGGATTSR VHTAVKIDPS YPAGSVVHVN DASRAVGVAS SLLSRERGPA YAAEIRADYA KITAAHLRAQ ADKKRVALKD ARANATKIDW SAAKPVKPSF LGVRSFTNYP LAELVDTIDW TPFFQSWELA GRFPAILDDK VVGEAARSLY ADARKMLERI VAGNWFTAKA AIGFWPANAV GDDIILYADD KRDSSIGALH TLRQQLVKRE GRANAALSDF IAPRGVPDYI GAFVVTAGIG EDVIADKFKA DNDDYSSIMV KALADRLAEA FAERMHARVR REFWGYAPDE TLSVEELILE KYQGIRPAPG YPAQPDHTEK ATLFRLLDAE VNAGVTLTES YAMWPGSSVS GLYFSHPESA YFGVGKIERD QVEDYARRKG WSTAEAERWL APVLNYIPEP QPAGAAQEAM PPLAPSGELL PAANDADTEL PSHPPGCNCA VHLAWRKQKV AAK // ID Q146H9_BURXL Unreviewed; 359 AA. AC Q146H9; DT 22-AUG-2006, integrated into UniProtKB/TrEMBL. DT 22-AUG-2006, sequence version 1. DT 27-MAY-2015, entry version 50. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABE28760.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABE28760.1}; GN ORFNames=Bxe_A4240 {ECO:0000313|EMBL:ABE28760.1}; OS Burkholderia xenovorans (strain LB400). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE28760.1, ECO:0000313|Proteomes:UP000001817}; RN [1] {ECO:0000313|EMBL:ABE28760.1, ECO:0000313|Proteomes:UP000001817} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LB400 {ECO:0000313|EMBL:ABE28760.1, RC ECO:0000313|Proteomes:UP000001817}; RX PubMed=17030797; DOI=10.1073/pnas.0606924103; RA Chain P.S.G., 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 ----------------------------------------------------------------------- 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; ABE28760.1; -; Genomic_DNA. DR RefSeq; WP_011486602.1; NC_007951.1. DR RefSeq; YP_556812.1; NC_007951.1. DR STRING; 266265.Bxe_A4240; -. DR EnsemblBacteria; ABE28760; ABE28760; Bxe_A4240. DR GeneID; 4004026; -. DR KEGG; bxe:Bxe_A4240; -. DR PATRIC; 19325785; VBIBurXen52548_0234. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; BXEN266265:GJII-227-MONOMER; -. DR Proteomes; UP000001817; Chromosome 1. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001817}; KW Methyltransferase {ECO:0000313|EMBL:ABE28760.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001817}; KW Transferase {ECO:0000313|EMBL:ABE28760.1}. SQ SEQUENCE 359 AA; 38582 MW; DACCDEECAEA4410C CRC64; MNQPAQTATP VRPDAAYTRG AALPALLKSR ILILDGAMGT MIQRYKLDEA RYRGERFKDY GRDIKGNNEL LSITQPQIIS EIHEQYLAAG ADIVETNTFG ATTVAQADYG MEALAVEMNL ESAKLARAAC DKYSTPDKPR FVAGAIGPTP KTASISPDVN DPGARNVTFD ELRAAYYEQA RALLDGGVDL FLVETIFDTL NAKAALFALD ELFEDTGERL PIMISGTVTD ASGRILSGQT VEAFWNSLRH AKPLTFGLNC ALGAALMRPY IAELAKLCDT YVSCYPNAGL PNPMSDTGFD ELPADTSGLL KEFAQAGLVN IAGGCCGTTP EHIAAIAQAL AGVKPRVWAN YRETDTETV // ID Q15S12_PSEA6 Unreviewed; 304 AA. AC Q15S12; DT 25-JUL-2006, integrated into UniProtKB/TrEMBL. DT 25-JUL-2006, sequence version 1. DT 27-MAY-2015, entry version 51. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABG41326.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ABG41326.1}; GN OrderedLocusNames=Patl_2815 {ECO:0000313|EMBL:ABG41326.1}; OS Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=342610 {ECO:0000313|EMBL:ABG41326.1, ECO:0000313|Proteomes:UP000001981}; RN [1] {ECO:0000313|EMBL:ABG41326.1, ECO:0000313|Proteomes:UP000001981} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T6c / ATCC BAA-1087 {ECO:0000313|Proteomes:UP000001981}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; ABG41326.1; -; Genomic_DNA. DR RefSeq; WP_011575584.1; NC_008228.1. DR RefSeq; YP_662380.1; NC_008228.1. DR EnsemblBacteria; ABG41326; ABG41326; Patl_2815. DR KEGG; pat:Patl_2815; -. DR PATRIC; 23050858; VBIPseAtl25434_3001. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; PYVDVWL; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; PATL342610:GHGT-2867-MONOMER; -. DR Proteomes; UP000001981; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001981}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ABG41326.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001981}; KW Transferase {ECO:0000313|EMBL:ABG41326.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 212 212 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 304 AA; 33106 MW; BC5918454A980C4F CRC64; MSASTSASKS TITILDGGMG QELLRRSSRD VTPMWSADIM LNEPELVRDL HREFINSGAR VITLNTYTAT PQRLKRENQF EQFVHLHDAA MRAAQEAIAL TQRDDVMIAG SLPPLVASYH PEVSLSFEDS LVSYRQLVAL QSLGSDIFIC ETMSSICEAQ AACTAAKESG KPVWVAFTVS DTEPDQLRSG ELLKDALDAL KALSPDAIML NCSLPEAISA CWSLMQQSNA KIGAYANGFV SIDALYPGDT VEELEMRKDM SPEQYAAHAM HWVQNGASII GGCCEIGPDH IKALHSKLQS EGLI // ID Q161X1_ROSDO Unreviewed; 305 AA. AC Q161X1; DT 25-JUL-2006, integrated into UniProtKB/TrEMBL. DT 25-JUL-2006, sequence version 1. DT 27-MAY-2015, entry version 50. DE SubName: Full=Homocysteine S-methyltransferase, putative {ECO:0000313|EMBL:ABG33222.1}; GN OrderedLocusNames=RD1_3753 {ECO:0000313|EMBL:ABG33222.1}; 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 {ECO:0000313|EMBL:ABG33222.1, ECO:0000313|Proteomes:UP000007029}; RN [1] {ECO:0000313|EMBL:ABG33222.1, ECO:0000313|Proteomes:UP000007029} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33942 / OCh 114 {ECO:0000313|Proteomes:UP000007029}; 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; ABG33222.1; -; Genomic_DNA. DR RefSeq; WP_011569833.1; NC_008209.1. DR RefSeq; YP_683908.1; NC_008209.1. DR STRING; 375451.RD1_3753; -. DR EnsemblBacteria; ABG33222; ABG33222; RD1_3753. DR KEGG; rde:RD1_3753; -. DR PATRIC; 23365451; VBIRosDen86677_3591. DR eggNOG; COG2040; -. DR HOGENOM; HOG000179103; -. DR KO; K00547; -. DR OMA; CCGTDHR; -. DR OrthoDB; EOG6R5C46; -. DR BioCyc; RDEN375451:GJIZ-3538-MONOMER; -. DR Proteomes; UP000007029; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007029}; KW Methyltransferase {ECO:0000313|EMBL:ABG33222.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007029}; KW Transferase {ECO:0000313|EMBL:ABG33222.1}. SQ SEQUENCE 305 AA; 33165 MW; 64DE18435AA2C2B3 CRC64; MTMARQLPHE SEKKFLVYAG TGTDLIFTHG VELPGFASFP LLEQPRTRAI LASQMQSLVD LAKEMDVGCI LDAPTWMANA DRAAPLGYDA GRLVEVNKDA VSLMEEVRRT ANRDDVLVSA CIGPRHDPYA GIPPVSVEDA RHYHKAQMQS LHDTSVDLVT AYTFNRPSEA AGCILAAQDA KLPIIMSLVV ETDGCLADGS RLVEVIDQID EATNSAALFF MVNCAHPTHF SEALDNHPRL RGIVANASSC SHAELDEAEN LDAGDPGQLG RQMAEILRRN PSIQVLGGCC GTDMRHLRSM VREMA // ID Q162F9_ROSDO Unreviewed; 347 AA. AC Q162F9; DT 25-JUL-2006, integrated into UniProtKB/TrEMBL. DT 25-JUL-2006, sequence version 1. DT 27-MAY-2015, entry version 59. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABG33134.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABG33134.1}; GN Name=metH {ECO:0000313|EMBL:ABG33134.1}; GN OrderedLocusNames=RD1_3660 {ECO:0000313|EMBL:ABG33134.1}; 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 {ECO:0000313|EMBL:ABG33134.1, ECO:0000313|Proteomes:UP000007029}; RN [1] {ECO:0000313|EMBL:ABG33134.1, ECO:0000313|Proteomes:UP000007029} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33942 / OCh 114 {ECO:0000313|Proteomes:UP000007029}; 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; ABG33134.1; -; Genomic_DNA. DR RefSeq; WP_011569747.1; NC_008209.1. DR RefSeq; YP_683820.1; NC_008209.1. DR ProteinModelPortal; Q162F9; -. DR STRING; 375451.RD1_3660; -. DR EnsemblBacteria; ABG33134; ABG33134; RD1_3660. DR KEGG; rde:RD1_3660; -. DR PATRIC; 23365273; VBIRosDen86677_3502. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; RDEN375451:GJIZ-3450-MONOMER; -. DR Proteomes; UP000007029; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007029}; KW Methyltransferase {ECO:0000313|EMBL:ABG33134.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007029}; KW Transferase {ECO:0000313|EMBL:ABG33134.1}. SQ SEQUENCE 347 AA; 36450 MW; EE3817604FFEC618 CRC64; MSLHDHHCVN ALSATARERI LIMDGAMGTM IQGLGLGEDD YTGHGTGMPC AHATDLPQKG NNDLLSLTQP QAIEQIHYDF AIAGADIVET NTFSSTAIAQ ADYGLEAAVH DLNVEAARVA RRALDRATAL DGKPRYVAGA VGPTNRTASL SPDVSNPGYR AVTFDDLRLA YRDQIRALIM GGADLILIET IFDTLNAKAA IFAAIEAFQA QGIRLPIMIS GTITDASGRT LSGQTPTAFW HSVAHARPFS VGLNCALGAG AMRPHMAELA GVVDTLTCAY PNAGLPNAFG QYDEGPEETA AQLAGFAQEG LLNVVGGCCG TTPEHIRAIA EAVAPFAPRQ LEKEQAA // ID Q167J7_ROSDO Unreviewed; 340 AA. AC Q167J7; DT 25-JUL-2006, integrated into UniProtKB/TrEMBL. DT 25-JUL-2006, sequence version 1. DT 27-MAY-2015, entry version 54. DE SubName: Full=Homocysteine S-methyltransferase, putative {ECO:0000313|EMBL:ABG31846.1}; GN OrderedLocusNames=RD1_2260 {ECO:0000313|EMBL:ABG31846.1}; 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 {ECO:0000313|EMBL:ABG31846.1, ECO:0000313|Proteomes:UP000007029}; RN [1] {ECO:0000313|EMBL:ABG31846.1, ECO:0000313|Proteomes:UP000007029} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33942 / OCh 114 {ECO:0000313|Proteomes:UP000007029}; 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; ABG31846.1; -; Genomic_DNA. DR RefSeq; WP_011568463.1; NC_008209.1. DR RefSeq; YP_682532.1; NC_008209.1. DR ProteinModelPortal; Q167J7; -. DR STRING; 375451.RD1_2260; -. DR EnsemblBacteria; ABG31846; ABG31846; RD1_2260. DR KEGG; rde:RD1_2260; -. DR PATRIC; 23362559; VBIRosDen86677_2162. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265278; -. DR KO; K00548; -. DR OMA; GTNLFAM; -. DR OrthoDB; EOG693GKH; -. DR BioCyc; RDEN375451:GJIZ-2136-MONOMER; -. DR Proteomes; UP000007029; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007029}; KW Methyltransferase {ECO:0000313|EMBL:ABG31846.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007029}; KW Transferase {ECO:0000313|EMBL:ABG31846.1}. SQ SEQUENCE 340 AA; 35841 MW; 711D2C1EA911BE4B CRC64; MPNPFSDLLE TRGVLLADGA TGTNLFNMGL MSGDAPELWN TQEPQKIKAL YKGAVDAGSD LFLTNSFGAN AARLKLHSAE KRVHELSRVA AEIGREVADT AGRAVIVAGS VGPTGEIMEP VGTLSHALAV EMFHETADGL KAGGADIGWL ETISAPEEYR AAAEGFALAG LDWCGTMSFD TAGRTMMGLT SADMVKMVDD LGDLAPLAFG ANCGTGASDL LRTILGFAAQ GAERPIIAKG NAGIPKYVDG HIHYDGTPEL MADYAVMARA SGARIIGGCC GTMPEHLRHM REALDTRRMD HPPALEEIVD RLGAFSSVAD GTDKENTPAR RATRRSRRAG // ID Q16E35_ROSDO Unreviewed; 296 AA. AC Q16E35; DT 25-JUL-2006, integrated into UniProtKB/TrEMBL. DT 25-JUL-2006, sequence version 1. DT 27-MAY-2015, entry version 54. DE SubName: Full=Homocysteine S-methyltransferase, putative {ECO:0000313|EMBL:ABG29758.1}; GN OrderedLocusNames=RD1_0018 {ECO:0000313|EMBL:ABG29758.1}; 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 {ECO:0000313|EMBL:ABG29758.1, ECO:0000313|Proteomes:UP000007029}; RN [1] {ECO:0000313|EMBL:ABG29758.1, ECO:0000313|Proteomes:UP000007029} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33942 / OCh 114 {ECO:0000313|Proteomes:UP000007029}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; ABG29758.1; -; Genomic_DNA. DR RefSeq; WP_011566380.1; NC_008209.1. DR RefSeq; YP_680444.1; NC_008209.1. DR ProteinModelPortal; Q16E35; -. DR STRING; 375451.RD1_0018; -. DR EnsemblBacteria; ABG29758; ABG29758; RD1_0018. DR KEGG; rde:RD1_0018; -. DR PATRIC; 23358223; VBIRosDen86677_0017. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; PYVDVWL; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; RDEN375451:GJIZ-16-MONOMER; -. DR Proteomes; UP000007029; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007029}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ABG29758.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007029}; KW Transferase {ECO:0000313|EMBL:ABG29758.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 200 200 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 273 273 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 274 274 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 296 AA; 31222 MW; 4D98F33167A48C25 CRC64; MTQITLLDGG MGQELVHRAG DKPTPLWSAQ VMVDHPGLVE AVHADYFAAG ATVATTNSYA IHHDRLEGTG MEDAFEDLYQ RALSEASAAR ATHGSGRIAG ALGPLVASYR PDLHPSREVA VPLFVEAAAL LAPECDLLIL ETVASVAHAR DALEGARSTN LPVWLSLTVS DSDGMQLRSG EPLEDALEVA ANADAVLVNC SAPEAVTKAM PILAQSGKPF GGYANGFVQI SEDFLKEKPT VDTLETRRDM GPRAYAGYVM EWVSAGATIV GGCCEVGPKH IAELKKRLLA AGHTLV // ID Q17C46_AEDAE Unreviewed; 315 AA. AC Q17C46; DT 25-JUL-2006, integrated into UniProtKB/TrEMBL. DT 25-JUL-2006, sequence version 1. DT 27-MAY-2015, entry version 52. DE SubName: Full=AAEL004728-PA {ECO:0000313|EMBL:EAT43856.1}; GN ORFNames=AAEL004728 {ECO:0000313|EMBL:EAT43856.1}; OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; OC Culicidae; Culicinae; Aedini; Aedes; Stegomyia. OX NCBI_TaxID=7159 {ECO:0000313|EMBL:EAT43856.1, ECO:0000313|Proteomes:UP000008820}; RN [1] {ECO:0000313|EMBL:EAT43856.1, ECO:0000313|Proteomes:UP000008820} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LVPib12 {ECO:0000313|Proteomes:UP000008820}; RX PubMed=17510324; DOI=10.1126/science.1138878; RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J., RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., RA Lobo N.F., Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., RA Sinkins S.P., Hogenkamp D.G., Amedeo P., Arensburger P., RA Atkinson P.W., Bidwell S.L., Biedler J., Birney E., Bruggner R.V., RA Costas J., Coy M.R., Crabtree J., Crawford M., DeBruyn B., RA DeCaprio D., Eiglmeier K., Eisenstadt E., El-Dorry H., Gelbart W.M., RA Gomes S.L., Hammond M., Hannick L.I., Hogan J.R., Holmes M.H., RA Jaffe D., Johnston S.J., Kennedy R.C., Koo H., Kravitz S., RA Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S., Lovin D.D., RA Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P., Mori A., RA Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J., RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W., RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O., RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., RA White O.R., Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., RA Raikhel A.S., Soares M.B., Knudson D.L., Lee N.H., Galagan J., RA Salzberg S.L., Paulsen I.T., Dimopoulos G., Collins F.H., Bruce B., RA Fraser-Liggett C.M., Severson D.W.; RT "Genome sequence of Aedes aegypti, a major arbovirus vector."; RL Science 316:1718-1723(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; CH477313; EAT43856.1; -; Genomic_DNA. DR RefSeq; XP_001649650.1; XM_001649600.1. DR UniGene; Aae.15093; -. DR ProteinModelPortal; Q17C46; -. DR STRING; 7159.AAEL004728-PA; -. DR EnsemblMetazoa; AAEL004728-RA; AAEL004728-PA; AAEL004728. DR GeneID; 5565322; -. DR KEGG; aag:AaeL_AAEL004728; -. DR VectorBase; AAEL004728; Aedes aegypti. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR InParanoid; Q17C46; -. DR KO; K00547; -. DR OMA; QCKDENT; -. DR OrthoDB; EOG7GQXW0; -. DR PhylomeDB; Q17C46; -. DR Proteomes; UP000008820; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008820}; KW Reference proteome {ECO:0000313|Proteomes:UP000008820}. SQ SEQUENCE 315 AA; 35324 MW; 32A16AEAE55BE8AE CRC64; MDRVTVLDGG FATQLSVHVG KHIDGDPLWS ARFNATNPNA VFKTHLDFLE AGAECIMTNT YQASIEGYME YLDLSETGSL QLIKATVKLA QMARTKYMAD NEVRRVPLVV ASVGPYGAHL HDGSEYTGEY ADYVTVDTIQ KWHRARIDAC LEAGVDVLGI ETIPCKMEAE AMLDMMTEDY PHVRFWISFQ CKDNAHIAHG ENFADTVSNL WNKAKLFGNE NLVAIGVNCV HPQFVTPLFR AVNEKRPTKE RIPLIVYPNS GEVYSVETGW QGKEDCVPLE HYVPQWVELG ARYIGGCCRT YARDIERIKL AVNSL // ID Q181J6_PEPD6 Unreviewed; 793 AA. AC Q181J6; DT 25-JUL-2006, integrated into UniProtKB/TrEMBL. DT 25-JUL-2006, sequence version 1. DT 27-MAY-2015, entry version 66. DE SubName: Full=Peptoclostridium difficile 630, complete genome {ECO:0000313|EMBL:AJP13378.1}; DE SubName: Full=Putative homocysteine S-methyltransferase {ECO:0000313|EMBL:CAJ70503.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAJ70503.1}; GN OrderedLocusNames=CD630_35960 {ECO:0000313|EMBL:CAJ70503.1}; GN ORFNames=CDIF630_03918 {ECO:0000313|EMBL:AJP13378.1}; OS Peptoclostridium difficile (strain 630) (Clostridium difficile). OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Peptoclostridium. OX NCBI_TaxID=272563 {ECO:0000313|EMBL:CAJ70503.1, ECO:0000313|Proteomes:UP000032222}; RN [1] {ECO:0000313|EMBL:CAJ70503.1, ECO:0000313|Proteomes:UP000001978} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=630 {ECO:0000313|EMBL:CAJ70503.1, RC ECO:0000313|Proteomes:UP000001978}; 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). RN [2] {ECO:0000313|EMBL:CAJ70503.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=630 {ECO:0000313|EMBL:CAJ70503.1}; RX PubMed=21349987; DOI=10.1099/jmm.0.030452-0; RA Monot M., Boursaux-Eude C., Thibonnier M., Vallenet D., Moszer I., RA Medigue C., Martin-Verstraete I., Dupuy B.; RT "Reannotation of the genome sequence of Clostridium difficile strain RT 630."; RL J. Med. Microbiol. 60:1193-1199(2011). RN [3] {ECO:0000313|EMBL:CAJ70503.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=630 {ECO:0000313|EMBL:CAJ70503.1}; RX PubMed=24568651; DOI=10.1186/1471-2164-15-160; RA Pettit L.J., Browne H.P., Yu L., Smits W.K., Fagan R.P., Barquist L., RA Martin M.J., Goulding D., Duncan S.H., Flint H.J., Dougan G., RA Choudhary J.S., Lawley T.D.; RT "Functional genomics reveals that Clostridium difficile Spo0A RT coordinates sporulation, virulence and metabolism."; RL BMC Genomics 15:160-160(2014). RN [4] {ECO:0000313|EMBL:AJP13378.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=630 {ECO:0000313|EMBL:AJP13378.1}; RA Riedel T., Bunk B., Sproer C.; RT "Genome resequencing of the virulent and multidrug-resistant reference RT strain Clostridium difficile 630."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP010905; AJP13378.1; -; Genomic_DNA. DR EMBL; AM180355; CAJ70503.1; -; Genomic_DNA. DR RefSeq; WP_009903830.1; NC_009089.1. DR RefSeq; YP_001090120.1; NC_009089.1. DR ProteinModelPortal; Q181J6; -. DR STRING; 272563.CD3596; -. DR EnsemblBacteria; CAJ70503; CAJ70503; CD630_35960. DR GeneID; 4915367; -. DR KEGG; cdf:CD630_35960; -. DR PATRIC; 19445781; VBICloDif38397_3768. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CDIF272563:GJFE-3862-MONOMER; -. DR Proteomes; UP000001978; Chromosome. DR Proteomes; UP000032222; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001978}; KW Methyltransferase {ECO:0000313|EMBL:CAJ70503.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001978}; KW Transferase {ECO:0000313|EMBL:CAJ70503.1}. SQ SEQUENCE 793 AA; 86627 MW; 2F43288B231216AC CRC64; MEIRQYLKNN ILIFDGAMGT MLQQKGLKLG ENPEVFGLQN PDKLIEIHTA YLEAGSNVIL TNTFGCNELK LDSKYTVEEV IDNAVLVARK AIENVDNTKP RYVALDIGPI GEMLEPMGTL SFDKAYEIFK RQVLQGVKSG VDVIVIETMM DLYEAKVAVL AAKENSDLPI FCTMTFDEGG RSFTGCMPEC MVATIEGLGV DAIGVNCSLG PKQLLPIVEK IASRATVPVM VQANAGLPNI VDGEAIYDVD AKEFFEGVKK FVEVGATIIG GCCGTNPSFI KEISENINSV TKGCIEKIDK CVVCSPSKFV EVQSPTVVGE RLNPTGRKSL QEALKNENVD YAINLGLEQV NAGAQILGVN VGLPEIDEKK LMPKLIREIQ AVVDTPLQVD SSNVEALEQG LRYYNGRTIV NSVNGKEESL ESILPIVKKY GSCVVGLTLD EKGIPKKAEE RFEIAKRIVN RAVSYGIKPK DIFIDCLSLT VSAQQEEAIE TIKAITMVKT LGVKTILGVS NISFGLPNRK ALNASFLTLA LGAGLDLAII NPNEYSMMEA INSFKILNNT DKGCINYINQ YSNINNSKKS DSSTKIDKDL PLDILVERGL KDEAKNVTLN LLKEKDENYI LDEILIPALD KVGKRYDSGD IFLPQLIQSA ETVKVSLNTI KETLLSKSSN NVSKGKIIVA TVKGDIHDIG KNIVKIMLEN YGYEVIDLGK DVPIEEVVEV AKKRNIKLVG LSALMTTTVQ SMKDTIQALR DNEINAKVFV GGAVLTEEYA EEMGADYYSK DAKSAVEIAK LNF // ID Q1AXR8_RUBXD Unreviewed; 611 AA. AC Q1AXR8; DT 11-JUL-2006, integrated into UniProtKB/TrEMBL. DT 11-JUL-2006, sequence version 1. DT 27-MAY-2015, entry version 70. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=Rxyl_0843 {ECO:0000313|EMBL:ABG03810.1}; OS Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129). OC Bacteria; Actinobacteria; Rubrobacteridae; Rubrobacterales; OC Rubrobacterineae; Rubrobacteraceae; Rubrobacter. OX NCBI_TaxID=266117 {ECO:0000313|EMBL:ABG03810.1, ECO:0000313|Proteomes:UP000006637}; RN [1] {ECO:0000313|EMBL:ABG03810.1, ECO:0000313|Proteomes:UP000006637} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 9941 / NBRC 16129 {ECO:0000313|Proteomes:UP000006637}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {ECO:0000256|RuleBase:RU004255}. CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ABG03810.1; -; Genomic_DNA. DR RefSeq; WP_011563828.1; NC_008148.1. DR RefSeq; YP_643622.1; NC_008148.1. DR ProteinModelPortal; Q1AXR8; -. DR STRING; 266117.Rxyl_0843; -. DR EnsemblBacteria; ABG03810; ABG03810; Rxyl_0843. DR KEGG; rxy:Rxyl_0843; -. DR PATRIC; 23368498; VBIRubXyl52678_0862. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; RXYL266117:GH8O-851-MONOMER; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000006637; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004255}; KW Complete proteome {ECO:0000313|Proteomes:UP000006637}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ABG03810.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000006637}; KW Transferase {ECO:0000313|EMBL:ABG03810.1}. SQ SEQUENCE 611 AA; 65223 MW; 87E1F93815109F6B CRC64; MGTSFRDLLD GRVLVGDGAM GTLLADRGVG YGHPYARANL THPELVERLH GEYVRAGARA IETNTFSANR IKLAGHRLEE RVREINEAGA RLARRAAAEA AERVLVLGAI GPLGRPLAPV GRVPREEARA LFREQAEALL EGGSDALLLE TFTDLEELRL AWEAVRDLGA PVLAYKTFVE DGETLAEGLP ERAAREISGW GVELVGSNCT VGPQRMLGIV EQMSAAAGPV AAFPNPGLPQ LVEGTVRYSH DVEHFARYGL RLAEAGARFV GGCCGTTPEH IRALSEALRE FRPRRVTVAL RGAAGPRKEG AREGGAGPRS RLAGKLHGGG FAVAVEVDLP RGNDLSGVVE AARRLKERGA DAIDISDGAR ARLRMHPVAA ARIVQERAGI EAVAHMSCRD RNILGLQADL LAAAALGVRN ILAVTGDPAQ IGDYPEATGV FDTDAVGLVH ILSRMNRGED LAGNAIGRPP GFLIGAAFNP TAEDLDAEVE RLRRKLEAGA HAFWTQPVFE LPALERALER LEGTGARLLL GLMPLRSARQ AEFLHHEVPG VKIPAEVRRK LAELSPQDAP RYGVEVAGNL LARARPLVSG AYIMPPASAP ELAAEVMEAL R // ID Q1CZ82_MYXXD Unreviewed; 326 AA. AC Q1CZ82; DT 11-JUL-2006, integrated into UniProtKB/TrEMBL. DT 11-JUL-2006, sequence version 1. DT 27-MAY-2015, entry version 48. DE SubName: Full=Homocysteine S-methyltransferase domain protein {ECO:0000313|EMBL:ABF87652.1}; GN OrderedLocusNames=MXAN_6160 {ECO:0000313|EMBL:ABF87652.1}; OS Myxococcus xanthus (strain DK 1622). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Myxococcaceae; Myxococcus. OX NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF87652.1, ECO:0000313|Proteomes:UP000002402}; RN [1] {ECO:0000313|EMBL:ABF87652.1, ECO:0000313|Proteomes:UP000002402} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DK 1622 {ECO:0000313|EMBL:ABF87652.1, RC ECO:0000313|Proteomes:UP000002402}; 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 ----------------------------------------------------------------------- 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; ABF87652.1; -; Genomic_DNA. DR RefSeq; WP_011556104.1; NC_008095.1. DR RefSeq; YP_634291.1; NC_008095.1. DR ProteinModelPortal; Q1CZ82; -. DR STRING; 246197.MXAN_6160; -. DR EnsemblBacteria; ABF87652; ABF87652; MXAN_6160. DR KEGG; mxa:MXAN_6160; -. DR PATRIC; 22654837; VBIMyxXan43560_6063. DR eggNOG; COG2040; -. DR HOGENOM; HOG000179103; -. DR KO; K00547; -. DR OMA; CGLMSCR; -. DR OrthoDB; EOG6R5C46; -. DR BioCyc; MXAN246197:GIWU-6114-MONOMER; -. DR Proteomes; UP000002402; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002402}; KW Methyltransferase {ECO:0000313|EMBL:ABF87652.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002402}; KW Transferase {ECO:0000313|EMBL:ABF87652.1}. SQ SEQUENCE 326 AA; 34484 MW; 05ADF8703441DB38 CRC64; MGGLANHAAF LHALHNAPRM LTEGSVVERL RRHPAGLLDP HVANASLLLE PEGREALAAI YRDYRDIGLR HGLPTLLLTP TWRANAERLA RAGLAGRDVF TEAVRLLAGL RDELGERETR VFVGGLVGCR GDAYQPAEAL PRREAAAFHA PHVEALSRAG VDFLVAQALP ALSEAEGLAL AMARTGAPFL LSFVLRPTGT LLDGTPLAEA VARIDALPDA RPTAYMVNCV HPSVFREGLS HQLAASPSLG ARVVGLQANT SRLSPEELDG RAELDCAPPD AFAREMARVH AELGTRVLGG CCGTDERHIA ALAGILTEGT PGALPP // ID Q1DAW7_MYXXD Unreviewed; 1152 AA. AC Q1DAW7; DT 11-JUL-2006, integrated into UniProtKB/TrEMBL. DT 11-JUL-2006, sequence version 1. DT 27-MAY-2015, entry version 75. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:ABF89590.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABF89590.1}; GN Name=metH {ECO:0000313|EMBL:ABF89590.1}; GN OrderedLocusNames=MXAN_1971 {ECO:0000313|EMBL:ABF89590.1}; OS Myxococcus xanthus (strain DK 1622). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Myxococcaceae; Myxococcus. OX NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF89590.1, ECO:0000313|Proteomes:UP000002402}; RN [1] {ECO:0000313|EMBL:ABF89590.1, ECO:0000313|Proteomes:UP000002402} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DK 1622 {ECO:0000313|EMBL:ABF89590.1, RC ECO:0000313|Proteomes:UP000002402}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000113; ABF89590.1; -; Genomic_DNA. DR RefSeq; WP_011552061.1; NC_008095.1. DR RefSeq; YP_630206.1; NC_008095.1. DR ProteinModelPortal; Q1DAW7; -. DR STRING; 246197.MXAN_1971; -. DR EnsemblBacteria; ABF89590; ABF89590; MXAN_1971. DR KEGG; mxa:MXAN_1971; -. DR PATRIC; 22646493; VBIMyxXan43560_1939. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; MXAN246197:GIWU-1950-MONOMER; -. DR Proteomes; UP000002402; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002402}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABF89590.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002402}; KW Transferase {ECO:0000313|EMBL:ABF89590.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 226 226 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 720 720 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1152 AA; 125216 MW; 4D55FE7CAF29AC50 CRC64; MEALRAAMRE RVLVLDGAMG TLLQNEDLKA ADFGGPEYEG CNEHLVLTRP ELVESIHARY FAAGADVTET DSFGGTPLVL AEFGLGHKAL EINEVSARLA RNAAAAAEAK DGRMRWVAGS IGPTTKAISV TGGVTFEELV DNFAVQAEGL ALGGSDYLLI ETAQDTRNVK AALLGAERAF QKLGYALPVA VSGTIEPMGT MLAGQSVESL AASLEHTDLL YLGLNCATGP DFMTDHLRSL ASMSAFPVAC VPNAGLPDEN GNYLETPEML ARSVRRFCEQ GWLNVVGGCC GTHAGHIETM AKAVQGLKPR AGSPRPRASL SGVDYLEVTD EQRPLIVGER TNVIGSKKFK ELIVAGQFDD ASEIARAQVK RGAQVIDICL ANPDRDELED MRNFLEAVIK KVRVPLMIDS TDERVIEMAL TYSQGKAIIN SVNLEDGEER FEKVVPLARR FGAALVVGCI DEVGMAVTRQ RKLEVAERSY ELLTKKYGMK PEDLYFDPLV FPCATGDAQY IGSGVETIEG VRLIKQRFPR SKTVLGISNV SFGLPAAGRE VLNSVFLYHN VQAGLDMALV NSEKLERYPS LPEEERKLSE DLLYNRGADP VTPFAAAFRE RKAARVQVST LPLEERLQRY IIEGTRDGLT ADLEAAMQKY TPLEIINGPL MKGMDEVGRL FGANELIVAE VLQSAESMKA AVSFLEPHMS KAQAAMRGKV VLATVKGDVH DIGKNLVEII LANNGFHIVN LGIKVPPEQL VLAVREHQPD ILGLSGLLVK SAHQMVATAE DLKRAGVDVP ILVGGAALSR NFVDRNIAPA YGAGTVAYAQ DAMNGLELAK QIVDPSSHEK LRGELAVRRE KLAREVKERP PPAALVTRGR SAEVKVLDAV PTAPDWERHV LTNTPLDHIW KFINPVMLYG RHLGLRSSAR VLGTPAEAEL AKTEEGRKAL ALKEAVEELK GFLRGGLMQA RAVFQFYKAG SDGNRVVLFD GASGKEAASF DFPRQDREGG LCLADYLRPL EGGAPTDNVA MFVVTAGSGI RELSEELKAK GEFLKMHAVQ ALALETAEGY AELLHTQLRS MWGTPDRQDM TMLERFRAEY VGKRYSFGYP ACPRLEDQSK LFAALRPEDI GVQLTDGSMM EPEASVSAIV FHHPQASYFS VT // ID Q1GBT8_LACDA Unreviewed; 310 AA. AC Q1GBT8; DT 27-JUN-2006, integrated into UniProtKB/TrEMBL. DT 27-JUN-2006, sequence version 1. DT 27-MAY-2015, entry version 51. DE SubName: Full=Lactobacillus delbrueckii subsp. bulgaricus ATCC 11842 complete genome {ECO:0000313|EMBL:CAI97150.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:CAI97150.1}; GN OrderedLocusNames=Ldb0311 {ECO:0000313|EMBL:CAI97150.1}; OS Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM OS 20081 / JCM 1002 / NBRC 13953 / NCIMB 11778). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=390333 {ECO:0000313|EMBL:CAI97150.1, ECO:0000313|Proteomes:UP000001259}; RN [1] {ECO:0000313|EMBL:CAI97150.1, ECO:0000313|Proteomes:UP000001259} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 11842 / DSM 20081 / JCM 1002 / NBRC 13953 / NCIMB 11778 RC {ECO:0000313|Proteomes:UP000001259}; RX PubMed=16754859; DOI=10.1073/pnas.0603024103; RA van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., RA Nicolas P., Robert C., Oztas S., Mangenot S., Couloux A., Loux V., RA Dervyn R., Bossy R., Bolotin A., Batto J.M., Walunas T., Gibrat J.-F., RA Bessieres P., Weissenbach J., Ehrlich S.D., Maguin E.; RT "The complete genome sequence of Lactobacillus bulgaricus reveals RT extensive and ongoing reductive evolution."; RL Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(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; CR954253; CAI97150.1; -; Genomic_DNA. DR RefSeq; WP_011543603.1; NC_008054.1. DR RefSeq; YP_618452.1; NC_008054.1. DR ProteinModelPortal; Q1GBT8; -. DR STRING; 390333.Ldb0311; -. DR EnsemblBacteria; CAI97150; CAI97150; Ldb0311. DR GeneID; 4083248; -. DR KEGG; ldb:Ldb0311; -. DR PATRIC; 22216244; VBILacDel123523_0278. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; YGRSVTK; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; LDEL390333:GIXG-307-MONOMER; -. DR Proteomes; UP000001259; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001259}; KW Methyltransferase {ECO:0000313|EMBL:CAI97150.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001259}; KW Transferase {ECO:0000313|EMBL:CAI97150.1}. SQ SEQUENCE 310 AA; 33255 MW; EDF514E2C87ABD2F CRC64; MADLPTLLAQ GPVTLDGSMS TPLEAWGEDT NSDLWTAKAL ADNPDLVYRV HQEYFKAGAR VTITDSYQAS LPAFMKHGLS EDAARALIRE SAAVAIKARD DFEKETGIHN FVAGSVGPYG AYLADGSEYR GDYALSHEEY VDFHAPRIEE LVAGGVDCLA VETQPKLSEV RAILDYLKAK YPDLPVYVSF SLKDPATISE GLPLTEAVEE VSAYAQVFAA GANCFKLAWT VDVVKNLRAS KLPIVVYPNS GAEYDPSVKK WVYPPEAADF GQAGAAWLAA GAKLVGGCCT TMPEDIAGLA AAVKKVYTAF // ID Q1GGL5_RUEST Unreviewed; 340 AA. AC Q1GGL5; DT 27-JUN-2006, integrated into UniProtKB/TrEMBL. DT 27-JUN-2006, sequence version 1. DT 27-MAY-2015, entry version 54. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABF64201.1}; GN OrderedLocusNames=TM1040_1468 {ECO:0000313|EMBL:ABF64201.1}; OS Ruegeria sp. (strain TM1040) (Silicibacter sp.). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Ruegeria. OX NCBI_TaxID=292414 {ECO:0000313|EMBL:ABF64201.1, ECO:0000313|Proteomes:UP000000636}; RN [1] {ECO:0000313|Proteomes:UP000000636} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TM1040 {ECO:0000313|Proteomes:UP000000636}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; ABF64201.1; -; Genomic_DNA. DR RefSeq; WP_011538803.1; NC_008044.1. DR RefSeq; YP_613463.1; NC_008044.1. DR ProteinModelPortal; Q1GGL5; -. DR STRING; 292414.TM1040_1468; -. DR EnsemblBacteria; ABF64201; ABF64201; TM1040_1468. DR KEGG; sit:TM1040_1468; -. DR PATRIC; 23387102; VBIRueSp69653_2369. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265278; -. DR KO; K00548; -. DR OMA; GTNLFAM; -. DR OrthoDB; EOG693GKH; -. DR BioCyc; RSP292414:GHCT-1494-MONOMER; -. DR Proteomes; UP000000636; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000636}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ABF64201.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000636}; KW Transferase {ECO:0000313|EMBL:ABF64201.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 212 212 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 278 278 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 279 279 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 340 AA; 36223 MW; 4416C5444D4D03BE CRC64; MSNSFQELLD SRDVLLADGA TGTNLFNMGL QSGDAPELWN TDAPDKIKAL YQGSVDAGSD LFLTNSFGGT AARLKLHDAQ GRVRELNRIA AELGREVADK AERKIAVAGS VGPTGEIMQP VGELSHALAV EMFHEQADAL KEGGVDVLWL ETISAPEEFA AAAEAFKLVD MPWCGTMSFD TAGRTMMGVT SADLAKLVEE FDTPPLAFGA NCGTGASDIL RTVLGFAAQG TERPIISKGN AGIPKYVDGH IHYDGTPDLM GEYAVLARDS GAKIIGGCCG TMPDHLRKMR EALDSRPRGE RPTLEHIVEL LGPFSSANDG TEEGSDASAE RRGRRGRRRS // ID Q1GL82_RUEST Unreviewed; 349 AA. AC Q1GL82; DT 27-JUN-2006, integrated into UniProtKB/TrEMBL. DT 27-JUN-2006, sequence version 1. DT 27-MAY-2015, entry version 61. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABF62584.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABF62584.1}; GN OrderedLocusNames=TM1040_3617 {ECO:0000313|EMBL:ABF62584.1}; OS Ruegeria sp. (strain TM1040) (Silicibacter sp.). OG Plasmid megaplasmid TM1040 {ECO:0000313|Proteomes:UP000000636}. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Ruegeria. OX NCBI_TaxID=292414 {ECO:0000313|EMBL:ABF62584.1, ECO:0000313|Proteomes:UP000000636}; RN [1] {ECO:0000313|Proteomes:UP000000636} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TM1040 {ECO:0000313|Proteomes:UP000000636}; 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 ----------------------------------------------------------------------- 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; ABF62584.1; -; Genomic_DNA. DR RefSeq; WP_011537223.1; NC_008043.1. DR RefSeq; YP_611846.1; NC_008043.1. DR ProteinModelPortal; Q1GL82; -. DR STRING; 292414.TM1040_3617; -. DR EnsemblBacteria; ABF62584; ABF62584; TM1040_3617. DR KEGG; sit:TM1040_3617; -. DR PATRIC; 23383718; VBIRueSp69653_0704. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; RSP292414:GHCT-3688-MONOMER; -. DR Proteomes; UP000000636; Plasmid megaplasmid TM1040. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000636}; KW Methyltransferase {ECO:0000313|EMBL:ABF62584.1}; KW Plasmid {ECO:0000313|EMBL:ABF62584.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000636}; KW Transferase {ECO:0000313|EMBL:ABF62584.1}. SQ SEQUENCE 349 AA; 37403 MW; 1B6EB28EC70B5FC6 CRC64; MQNFNLPKSK AFEALSKTAQ ERILILDGAM GTQIQKLGLD EEAFRGHGGH SCAFHSNHPQ QGNNDLLILT QPEAVEQIHY DFAMAGADIV ETNTFSSTTI AQADYALEDA VHDLNAEGAR VARRAMDRAT AEDGKQRWVA GAVGPTNRTA SISPDVNDPG YRAVTFDDLR VAYGQQIRGL IAGGADLILI ETIFDTLNAK AAVFACFEAF AEHGERLPIM ISGTITDASG RTLSGQTPTA FWHSVRHARP FTVGLNCALG ADAMRPHLTE LAGVADTLVC AYPNAGLPNA FGQYDEEPED TAAKVEIFAK EGLVNVVGGC CGTTPEHIRA IAEQVAPYAP RRIREAANV // ID Q1GX60_SPHAL Unreviewed; 355 AA. AC Q1GX60; DT 27-JUN-2006, integrated into UniProtKB/TrEMBL. DT 27-JUN-2006, sequence version 1. DT 27-MAY-2015, entry version 58. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABF51762.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABF51762.1}; GN OrderedLocusNames=Sala_0036 {ECO:0000313|EMBL:ABF51762.1}; OS Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256) OS (Sphingomonas alaskensis). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingopyxis. OX NCBI_TaxID=317655 {ECO:0000313|EMBL:ABF51762.1, ECO:0000313|Proteomes:UP000006578}; RN [1] {ECO:0000313|EMBL:ABF51762.1, ECO:0000313|Proteomes:UP000006578} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13593 / LMG 18877 / RB2256 RC {ECO:0000313|Proteomes:UP000006578}; 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. RN [2] {ECO:0000313|EMBL:ABF51762.1, ECO:0000313|Proteomes:UP000006578} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RB2256 {ECO:0000313|EMBL:ABF51762.1}; 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 ----------------------------------------------------------------------- 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; ABF51762.1; -; Genomic_DNA. DR RefSeq; WP_011540377.1; NC_008048.1. DR RefSeq; YP_615095.1; NC_008048.1. DR ProteinModelPortal; Q1GX60; -. DR STRING; 317655.Sala_0036; -. DR EnsemblBacteria; ABF51762; ABF51762; Sala_0036. DR KEGG; sal:Sala_0036; -. DR PATRIC; 23689227; VBISphAla23391_0064. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; SALA317655:GHHY-36-MONOMER; -. DR Proteomes; UP000006578; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006578}; KW Methyltransferase {ECO:0000313|EMBL:ABF51762.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006578}; KW Transferase {ECO:0000313|EMBL:ABF51762.1}. SQ SEQUENCE 355 AA; 37948 MW; 8A43383FF084C3A9 CRC64; MTSSLASSAR DALKEAAKQR ILIKDGPFGT AFQHRNAYVG VDGAEHGLSI DPRGNGDYLN LARPDIVADI MRDYLVAGAD IIATNTFSAN RISQADYGAE HLVAGINLAS ARLARREADA MQQKDGRRRF VAGAVGPTNK TLSLSPDVNN PGFREIDFDE LKDVYLEQVV ALAEGGADFI LIETIFDTLN AKAGIAATLE AEAALGRELP LMISMTLTDL SGRNLSGHTV EAFWYAVRHA KPMTIGLNCS FGAAQLRPHV KVLSDIADAL VMVYPNAGLP NELGEYDELP ETTAELVREW AEHGQVNILG GCCGSTPDHI AAMAKAVEGL APRQVPEVPV RTRLAGLEPF TMAAA // ID Q1GYB3_METFK Unreviewed; 1262 AA. AC Q1GYB3; DT 27-JUN-2006, integrated into UniProtKB/TrEMBL. DT 27-JUN-2006, sequence version 1. DT 27-MAY-2015, entry version 69. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABE50774.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABE50774.1}; GN OrderedLocusNames=Mfla_2509 {ECO:0000313|EMBL:ABE50774.1}; OS Methylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875). OC Bacteria; Proteobacteria; Betaproteobacteria; Methylophilales; OC Methylophilaceae; Methylobacillus. OX NCBI_TaxID=265072 {ECO:0000313|EMBL:ABE50774.1, ECO:0000313|Proteomes:UP000002440}; RN [1] {ECO:0000313|EMBL:ABE50774.1, ECO:0000313|Proteomes:UP000002440} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KT / ATCC 51484 / DSM 6875 {ECO:0000313|Proteomes:UP000002440}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000284; ABE50774.1; -; Genomic_DNA. DR RefSeq; WP_011480727.1; NC_007947.1. DR ProteinModelPortal; Q1GYB3; -. DR SMR; Q1GYB3; 676-928. DR STRING; 265072.Mfla_2509; -. DR EnsemblBacteria; ABE50774; ABE50774; Mfla_2509. DR KEGG; mfa:Mfla_2509; -. DR PATRIC; 32270843; VBIMetFla97085_2630. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; MFLA265072:GHWJ-2568-MONOMER; -. DR Proteomes; UP000002440; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002440}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABE50774.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002440}; KW Transferase {ECO:0000313|EMBL:ABE50774.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 260 260 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 325 325 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 326 326 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 788 788 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1262 AA; 139433 MW; E6F8ABD16E3F51D7 CRC64; MKHYEMSPTE VLLREILSKR IMILDGAMGT MIQQYKLTEE DYRGGPQGRF ADFAAPEGER ELFVKGNNEL LTFTQPQIIQ EIHEQYLAAG ADIIETNTFG ATSVAQEDYF MAHLAYEMNV EAARLARAAC DKFSTSDKPR FVAGALGPTP KTASISPDVN DPAARNITFD QLVAAYHEQA RGLVDGGADI LMVETVFDTL NCKAALFAID QYFEETGKRL PIMISGTVTD ASGRILSGQT VPAFWYSIRH ARPLTIGLNC ALGAALMRPY AEELSRIADT FVCIYPNAGL PNPMSDTGFD EKPEDTSALL REFAESGFVN IAGGCCGTTP SHIAAIAEAV RDIPPRRIPQ IPVATRLAGL EPFTIDEDSL FVNVGERTNV TGSKAFARMI LNEQYEEALA VARQQVENGA QVIDINMDEG MLDAVRAMTH FLNLVASEPD IARVPIMIDS SKWAVIEAGL KCVQGKCIVN SISMKEGEAE FLRQAALCRR YGAAVIVMAF DETGQADTFE RKIEICKRAY DLLVEKLNFP PEDIIFDPNI FAVATGIEEH NNYAVDFINA TRWIKENLPH ARISGGVSNV SFSFRGNEAA REAIHTVFLY HAIKAGMTMG IVNAGMIGVY DDLDPELRER VEDVVLNRRE DATERMIEFA ATLAAGGKKQ EATLDWRGTP ENPVPVEKRL EYAMVHGITE FIVQDTEEAR QKVMSEGGRP IHVIEGPLMD GMNVVGDLFG QGKMFLPQVV KSARVMKQAV AHLIPFIEEE KRAEEARTGI VAKPKGKMVI ATVKGDVHDI GKNIVSVVLQ CNNFEVVNMG VMVPCAEILA QAKATGADII GLSGLITPSL EEMAYVAREM QRDPYFHGIK MPLLIGGATT SRAHTAVKIA PHYDGPVIYV PDASRSVSVM QSLLTPEQRD NYIAEVQQDY ERVRTQHANK KGIPLLTLAE ARANKAKLDF TGRFAPVKPK FIGRRVFKNI DLATIAQYID WGPFFQTWDL AGSYPAILQD DVVGAAASKL FAEGQAMLKK IIEGRWLTAS GVVALLPANS VNDDDIEIYT DDTRSQVAFT YYGMRQQTQK PIVKGEQRPN QCLADFIAPK ESGIADYIGM FAVTGGLGIE KYEQRFEAAH DDYSSIMLKS LADRLAEAFA EYMHERVRKD LWGYAPDEAL SKEALIKEQY RGIRPAPGYP ACPDHTVKPD MFNLMKCEEV GIRLTDSFAM MPGAAVSGFY FAHPEARYFS VDKIGEDQLL DMAKRRGLPR EYLERWLAPN LS // ID Q1HL00_CAMSI Unreviewed; 351 AA. AC Q1HL00; DT 13-JUN-2006, integrated into UniProtKB/TrEMBL. DT 13-JUN-2006, sequence version 1. DT 01-APR-2015, entry version 19. DE SubName: Full=Selenocysteine methyltransferase {ECO:0000313|EMBL:ABF47292.1}; OS Camellia sinensis (Tea). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; asterids; Ericales; Theaceae; Camellia. OX NCBI_TaxID=4442 {ECO:0000313|EMBL:ABF47292.1}; RN [1] {ECO:0000313|EMBL:ABF47292.1} RP NUCLEOTIDE SEQUENCE. RA Zhu L., Jiang C.-J., Deng W.-W., Gao X., Wang R.-J., Wan X.-C.; RT "Cloning and expression of selenocysteine methyltransferase cDNA from RT Camellia sinensis."; RL Acta Physiol. Plant. 30:167-174(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; DQ480337; ABF47292.1; -; mRNA. DR BRENDA; 2.1.1.280; 1084. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Methyltransferase {ECO:0000313|EMBL:ABF47292.1}; KW Transferase {ECO:0000313|EMBL:ABF47292.1}. SQ SEQUENCE 351 AA; 38146 MW; 9722B1E1317B9E9F CRC64; MGLSVAETSS SSSSSSPMMI PDLLRQSGSV AIIDGGLATE LERHGADLND PLWSAKCLLT SPHLIRRVHL DYLEAGADII ITASYQATIQ GFEAKGFSQE ESEAMLKRCV EIAREARDIY YENCRELSND SADDGRVLKH RSILVAASVG SYGAYLADGS EYSGDYGNAM DLEFLKDFHR RRVQILADAG ADLIAFETVP NKLEAQAYAR LLEEEDIKIP AWFSFNSKDG VHVVSGDSLL ECAAIAEACK KVVAVGINCT PPRFIHDLIL TVKKGTTKPI LIYPNSGESY DADKKEWVQN TGVSDDDFVS CVNTWCDVGA SLVGGCCRTT PNTIRAIYKT LSNRSAAPSL K // ID Q1I895_PSEE4 Unreviewed; 1235 AA. AC Q1I895; DT 13-JUN-2006, integrated into UniProtKB/TrEMBL. DT 13-JUN-2006, sequence version 1. DT 27-MAY-2015, entry version 70. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CAK16133.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAK16133.1}; GN Name=metH {ECO:0000313|EMBL:CAK16133.1}; GN OrderedLocusNames=PSEEN3382 {ECO:0000313|EMBL:CAK16133.1}; OS Pseudomonas entomophila (strain L48). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=384676 {ECO:0000313|EMBL:CAK16133.1, ECO:0000313|Proteomes:UP000000658}; RN [1] {ECO:0000313|EMBL:CAK16133.1, ECO:0000313|Proteomes:UP000000658} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=L48 {ECO:0000313|EMBL:CAK16133.1, RC ECO:0000313|Proteomes:UP000000658}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CT573326; CAK16133.1; -; Genomic_DNA. DR RefSeq; WP_011534520.1; NC_008027.1. DR RefSeq; YP_608924.1; NC_008027.1. DR STRING; 384676.PSEEN3382; -. DR EnsemblBacteria; CAK16133; CAK16133; PSEEN3382. DR KEGG; pen:PSEEN3382; -. DR PATRIC; 19864874; VBIPseEnt83862_3261. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PENT384676:GJB8-3206-MONOMER; -. DR Proteomes; UP000000658; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000658}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAK16133.1}; KW Transferase {ECO:0000313|EMBL:CAK16133.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1235 AA; 135312 MW; E6FA7ADE773E45A5 CRC64; MSDRSARLQA LQKALKERIL ILDGGMGTMI QSYRLEEHDY RGTRFADWPS DVKGNNDLLL LTRPDVIAAI EKAYLDAGAD ILETNTFNAT QISQADYGME ALVYELNVEG ARVARQVADA KTLETPDKPR FVAGVLGPTS RTCSISPDVN DPGYRNVTFD ELVTNYIEAT RGLIEGGADL LLIETIFDTL NAKAAIFAVQ QVFEEDNVEL PIMISGTITD ASGRTLSGQT TEAFWNSVRH AKPISIGLNC ALGAKDLRPY LEELAGKADT FVSAHPNAGL PNAFGEYDET PAEMAAVVEE FAASGFLNII GGCCGTTPPH IQAIAEAVAK HKPRAIPDIP KACRLSGLEP FTIDRQSLFV NVGERTNITG SAKFARLIRE ENYTEALEVA LQQVEAGAQV IDINMDEGML DSQAAMVRFL NLIAGEPDIS RVPIMIDSSK WEVIEAGLKC IQGKGIVNSI SMKEGVEQFK HHARLCKRYG AAVVVMAFDE VGQADTAARK KEICQRSYDI LVNEVGFPPE DIIFDPNIFA VATGIEEHNN YAVDFIEACA YIRDHLPYAL SSGGVSNVSF SFRGNNPVRE AIHSVFLYHA IQNGLTMGIV NAGQLEIYDE IPAALREKVE DVVLNRTPHG TDALLAIADD YKGGGATKEV ENEEWRSLPV AKRLEHALVK GITAHIVEDT EECRQQSARP IEVIEGPLMS GMNVVGDLFG AGKMFLPQVV KSARVMKQAV AHLIPFIEEE KGDKPEAKGK ILMATVKGDV HDIGKNIVGV VLGCNGYDIV DMGVMVPAEK ILQTAREQKC DIIGLSGLIT PSLDEMVHVA REMQRQDFHL PLMIGGATTS KAHTAVKIEP KYSNDAVVYV TDASRAVGVA TQLLSKELKA GFVAKTREEY VEVRERTANR SARTERLSYD QAIAAKPQYD WAGYQAAVPS FTGVKVLENI DLRTLAEYID WTPFFISWDL AGKFPRILTD EVVGEAATAL YKDAREMLDK LIDEKLISAR AVFGFWPANQ VEHDDIEVYG DNGDTLATLH HLRQQTIKPD GKPNWSLADF VAPKDSGVTD YVGGFITTAG IGAEEVAKAY QDKGDDYSSI MVKALADRLA EACAEWLHEQ VRKEHWGYAK DEHLDNEALI KEQYSGIRPA PGYPACPDHT EKETLFRLLD GTAIGETGPS GVFLTEHFAM FPAAAVSGWY FAHPQAQYFA VGKVDKDQVE RYSARKGQDV SVSERWLAPN LGYEG // ID Q1IL23_KORVE Unreviewed; 617 AA. AC Q1IL23; DT 13-JUN-2006, integrated into UniProtKB/TrEMBL. DT 13-JUN-2006, sequence version 1. DT 27-MAY-2015, entry version 63. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=Acid345_3426 {ECO:0000313|EMBL:ABF42427.1}; OS Koribacter versatilis (strain Ellin345). OC Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae; OC Candidatus Koribacter. OX NCBI_TaxID=204669 {ECO:0000313|EMBL:ABF42427.1, ECO:0000313|Proteomes:UP000002432}; RN [1] {ECO:0000313|EMBL:ABF42427.1, ECO:0000313|Proteomes:UP000002432} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ellin345 {ECO:0000313|EMBL:ABF42427.1, RC ECO:0000313|Proteomes:UP000002432}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ABF42427.1; -; Genomic_DNA. DR RefSeq; WP_011524226.1; NC_008009.1. DR RefSeq; YP_592501.1; NC_008009.1. DR ProteinModelPortal; Q1IL23; -. DR STRING; 204669.Acid345_3426; -. DR EnsemblBacteria; ABF42427; ABF42427; Acid345_3426. DR KEGG; aba:Acid345_3426; -. DR PATRIC; 31984042; VBICanKor57425_3652. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; KVER204669:GHL8-3453-MONOMER; -. DR Proteomes; UP000002432; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002432}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ABF42427.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000002432}; KW Transferase {ECO:0000313|EMBL:ABF42427.1}. SQ SEQUENCE 617 AA; 66068 MW; E7A30721DDCB6D3C CRC64; MGKSFLERLG DGPILCDGAM GTLLYSKGIF INRCYDELNL SQPELIGGIH ADYVANGAEI LETNTFGANS FRLARHGCQE KLADINRAGV ELVRKAIKNN QVYAAGAVGP LGIRIEPLGK TSRDEARDAF RDQIRVLVDS GVDLLILETF GYLGELHQAI LAARDVDPKI PVVAQVTIDE DGNCLDGSSP EHYGARLTEW GADVIGCNCS VGPVAMLDAL ERLRAATPKP LSAQPNAGIP RSVEGRNIYL CSPEYMASYA RKFVGVGVTL VGGCCGTTPD HIRSMKSALR VGEARTTSFK VKTEVEEHAV EPTPLGQRSR VGARIASGEF LTLVEIVPPK GVNAEKEVEG ARYLMSVGVD AINIPDSPRA SARMSNQALC LLTQQQVGIE TVLHYTCRDR NVLGIQSDLL GASAIGIRNL ICITGDPPKM GNYPDATAVF DVDAIGLVNI VSNLNRGLDI GGNTIGTATQ FTIAVGANPG AANLDEEIRR FEYKVEAGAE YAVTQPVFDL ALLEEFLKRI EHCRVPVVAG IWPLSSARNA EFMRDELNIS IPDAIYNRMA RTTNADAARA EGVAVAREML QAVRPMVQGT QLSAPFGRYS AAADVLEVLG SSDSACA // ID Q1IQK2_KORVE Unreviewed; 407 AA. AC Q1IQK2; DT 13-JUN-2006, integrated into UniProtKB/TrEMBL. DT 13-JUN-2006, sequence version 1. DT 27-MAY-2015, entry version 53. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABF40848.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABF40848.1}; GN OrderedLocusNames=Acid345_1847 {ECO:0000313|EMBL:ABF40848.1}; OS Koribacter versatilis (strain Ellin345). OC Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae; OC Candidatus Koribacter. OX NCBI_TaxID=204669 {ECO:0000313|EMBL:ABF40848.1, ECO:0000313|Proteomes:UP000002432}; RN [1] {ECO:0000313|EMBL:ABF40848.1, ECO:0000313|Proteomes:UP000002432} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ellin345 {ECO:0000313|EMBL:ABF40848.1, RC ECO:0000313|Proteomes:UP000002432}; 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; ABF40848.1; -; Genomic_DNA. DR RefSeq; WP_011522650.1; NC_008009.1. DR RefSeq; YP_590922.1; NC_008009.1. DR ProteinModelPortal; Q1IQK2; -. DR STRING; 204669.Acid345_1847; -. DR EnsemblBacteria; ABF40848; ABF40848; Acid345_1847. DR KEGG; aba:Acid345_1847; -. DR PATRIC; 31980640; VBICanKor57425_1964. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; KVER204669:GHL8-1860-MONOMER; -. DR Proteomes; UP000002432; Chromosome. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002432}; KW Methyltransferase {ECO:0000313|EMBL:ABF40848.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002432}; KW Transferase {ECO:0000313|EMBL:ABF40848.1}. SQ SEQUENCE 407 AA; 44353 MW; DDD07A02A0816E21 CRC64; MWKSGCSMQR VSFAWHAHPP DTAHRYNSKR LTAASNKQMK RPDQHPIERI LEDRIAIIDG AMGTTIRTYG MAEADIRGER FKDSSKGLLN NGDLFSLTQP QMIGDIHRRF LEAGADIIET NTFGATSIVQ SEFFVDDPRE HGGRKDADFY QKIIDDQFLG DLAWEINETS AQQCREWADR VANATSRPRF VAGALGPLTV SLSNSPDADD PGFRVVTFDQ VKIAYIQQVR ALIAGGVDFL LVETIFDSLN AKAALVAIRE VFDQDGKNIP VMISAAVGRG GETMISGQTV EAFWNAVSHV KPLSVGLNCS LGPDLMYPFL EDLSAKADVA ISCYPNAGLP NPLAATGFDF GPPDMARYLR EFAEAGLINI AGGCCGNTPE HIAAIAKALE GLPPRKIQPV GETQLAR // ID Q1IYQ2_DEIGD Unreviewed; 1226 AA. AC Q1IYQ2; DT 13-JUN-2006, integrated into UniProtKB/TrEMBL. DT 13-JUN-2006, sequence version 1. DT 27-MAY-2015, entry version 71. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:ABF45632.1}; GN OrderedLocusNames=Dgeo_1336 {ECO:0000313|EMBL:ABF45632.1}; OS Deinococcus geothermalis (strain DSM 11300). OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; OC Deinococcaceae; Deinococcus. OX NCBI_TaxID=319795 {ECO:0000313|EMBL:ABF45632.1, ECO:0000313|Proteomes:UP000002431}; RN [1] {ECO:0000313|Proteomes:UP000002431} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11300 {ECO:0000313|Proteomes:UP000002431}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000359; ABF45632.1; -; Genomic_DNA. DR RefSeq; WP_011530469.1; NC_008025.1. DR RefSeq; YP_604801.1; NC_008025.1. DR ProteinModelPortal; Q1IYQ2; -. DR SMR; Q1IYQ2; 645-887. DR STRING; 319795.Dgeo_1336; -. DR EnsemblBacteria; ABF45632; ABF45632; Dgeo_1336. DR KEGG; dge:Dgeo_1336; -. DR PATRIC; 21624573; VBIDeiGeo41128_1922. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; DGEO319795:GHMU-1359-MONOMER; -. DR Proteomes; UP000002431; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002431}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABF45632.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002431}; KW Transferase {ECO:0000313|EMBL:ABF45632.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 753 753 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1226 AA; 133304 MW; 803E068A769BB554 CRC64; MADTRDIRAH ARERILVLDG AWGTMLQRAG LTEADFRWPG ADPLRMYRGN FDLLQLTRPD VIQGVHRAYF EAGADIASTN TFNSTAISQA DYGTEHLVRA MNEAGARLAR EVADEFEARD GRPRWVAGSV GPTNRTATLS PDVERPDFRN VTFDDLVAAY LEQLEGLIAG GADLILIETV FDTLNAKAAL FACEEAFART GKRLPIMLSG TITDASGRTL SGQTPEAFVI STEHADLFSV GLNCALGADL LRPHLRAIAA NTAALVSVHP NAGLPNAFGE YDETPEHTAA VLRSFAEEGL VNIVGGCCGT TPDHIRAIAA AVADLPPRTA PRLPPYLRLS GLEALTISPE TNFVNVGERT NVTGSPKFAK AILAGDYDAG LKIARQQVQN GAQLVDVNFD EGMLDGEAAM VKFLNLLAGE PDISRVPLML DSSRWEILEA GLKRVQGKCV VNSISLKDGE AKFLERGRLL RRYGAAAVVM AFDEQGQADT LERRIEICSR AYRLLTEQAA FPPQDIIFDP NVLTVATGIE EHDRYALDFI EATRWIKANL PGALVSGGIS NVSFSFRGNN HVREAMHAVF LYHAIRAGLD MGIVNAGMLA VYEDIEPELR EAVEDVILAR RPDATERLIQ LAESYKDVKR EAGAQSAWRE LPVAERLKHA LVSGITDYVV EDAEEAYQLL GSPLAVIEGP LMDGMNVVGD LFGAGKMFLP QVVKSARVMK RAVAHLTPYL EAQKQEGGGK GKVLLATVKG DVHDIGKNIV GVVLACNGYQ VTDLGVMVPA EKILDTAQEL GADVIGLSGL ITPSLDEMVN VAREMTRRGL QTPLLIGGAT TSRAHTAVKI DPAYTGTVVH VLDASRAVGV VGDLLSQPDA VRARIREEYA ALRERHGERQ VRLIPLEQAR ARAPRLSPAL PPAPRERGRQ VIEQPLAELL DYIDWTPFFI AWEMKGIYPG ILTDPLRGAE ARRLFDDAQA LLQRIVKEGL LTARGVIGLW PARRVGDDIL VEADNPTRLH TLRQQRDQST PNTALADFVA LRGDHIGAFA VAIHGAEELA RSFEAQHDDY SAILVKSVAD RLAEAFAEKL HRDVRVRYWG YAPDEALGNH DLIKERYQGI RPAPGYPAQP DHTEKRTLFD LLQAEEVGLS LTESGAMTPA AAVSGLYFAH PEAHYFAVGR IGRDQVEDYA ARKGWTLAEA ERWLGPILAY DPTPPDFPPP SAAPLSPVPS VAGGRP // ID Q1JWJ4_DESAC Unreviewed; 803 AA. AC Q1JWJ4; DT 13-JUN-2006, integrated into UniProtKB/TrEMBL. DT 13-JUN-2006, sequence version 1. DT 27-MAY-2015, entry version 48. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EAT14574.1}; GN ORFNames=Dace_0403 {ECO:0000313|EMBL:EAT14574.1}; OS Desulfuromonas acetoxidans DSM 684. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Desulfuromonadaceae; Desulfuromonas. OX NCBI_TaxID=281689 {ECO:0000313|EMBL:EAT14574.1}; RN [1] {ECO:0000313|EMBL:EAT14574.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 684 {ECO:0000313|EMBL:EAT14574.1}; 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] {ECO:0000313|EMBL:EAT14574.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 684 {ECO:0000313|EMBL:EAT14574.1}; 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 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. {ECO:0000313|EMBL:EAT14574.1}. 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; AAEW02000021; EAT14574.1; -; Genomic_DNA. DR RefSeq; WP_006002422.1; NZ_AAEW02000021.1. DR ProteinModelPortal; Q1JWJ4; -. DR EnsemblBacteria; EAT14574; EAT14574; Dace_0403. DR PATRIC; 26635669; VBIDesAce8486_3097. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EAT14574.1}; KW Transferase {ECO:0000313|EMBL:EAT14574.1}. SQ SEQUENCE 803 AA; 85061 MW; 15330102D2C3C804 CRC64; MNRFLEAIQQ RVLILDGAMG TMLQARGLAA GGCPELMNLE KPEVVEGVHR DYAQAGAQII VTNTFGGTRS KLEHYGLEDK VYEINVQAAR LARAALADPA NDFVAGSIGP TGRFVEPVGD ATFDEMVEIY AEQVKALVAG GVDLLTCETF LDIRELKAAV MACREYADVP VMAMMTFDDG GRTVLGTPPA AAAVMLEGLG VDVVGTNCGL GIDGMYELLG QMRDVCSCPL IAQANAGLPI LKDGETIFPA TPVEMTSHHD QLIALGVRVL GGCCGTTPEH IRVMRQAMDE RGQQWTAPAR RGVLSSRTQV VAVGPEQPCA IIGERINPTG KKGYSAELRE GKTAYIRREA QQQTGAGATL LDVNCGAPGA DEPLALERAV HAITGVVGTP LVLDSSDPIA LERGLKAADG KVLINSVNGE EKSLATVLPL AKKYGAAIIG LTLDGQGIPQ TAEGRVEIAE RIIERAQAVG IQRCDIVIDC LALTVSAEQG QAIETLKAIR TLTQDHGMAT VLGVSNISFG LPRRPLMSST FFAMALQAGL SAAIINPKDQ AMMDAFRSAM VLLGKDLRAE RYIDAYAEVQ ETAPAVAAVA GAEPSIRERL AQAIIDGDQD GVVALVELAL KDGLDVLQIS NEGLLAGLEE VGRRFGANRI FLPQVLLSAE TMKTAFARLR QEMKGEQVAS LGKIMMATVE GDIHDIGKNI VCTLLENHGY EVIDLGKNVS AAHIVEQAQA AHVDAVGLSA LMTTTLQQMQ ITIDALKEAG VKVFTMVGGA VVTQDYADEI GADLYAEDAL EAVAKIKQML HNA // ID Q1K3H4_DESAC Unreviewed; 614 AA. AC Q1K3H4; DT 13-JUN-2006, integrated into UniProtKB/TrEMBL. DT 13-JUN-2006, sequence version 1. DT 27-MAY-2015, entry version 54. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=Dace_2866 {ECO:0000313|EMBL:EAT17000.1}; OS Desulfuromonas acetoxidans DSM 684. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Desulfuromonadaceae; Desulfuromonas. OX NCBI_TaxID=281689 {ECO:0000313|EMBL:EAT17000.1}; RN [1] {ECO:0000313|EMBL:EAT17000.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 684 {ECO:0000313|EMBL:EAT17000.1}; 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] {ECO:0000313|EMBL:EAT17000.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 684 {ECO:0000313|EMBL:EAT17000.1}; 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 Desulfuromonas RT acetoxidans DSM 684."; RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {ECO:0000256|RuleBase:RU004255}. CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAT17000.1}. 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; AAEW02000002; EAT17000.1; -; Genomic_DNA. DR RefSeq; WP_005997875.1; NZ_AAEW02000002.1. DR ProteinModelPortal; Q1K3H4; -. DR EnsemblBacteria; EAT17000; EAT17000; Dace_2866. DR PATRIC; 26630215; VBIDesAce8486_0386. DR UniPathway; UPA00193; -. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004255}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EAT17000.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EAT17000.1}. SQ SEQUENCE 614 AA; 64745 MW; A6FF653ACD84D250 CRC64; MSTPPFMQRI QETVLIGDGA MGTQLYSRGV PADSCFERLN LTRPELVTSV HEAYVKAGAQ LLETNTFTAN GVRLGGVGLD GQVRQINEAG ARLARKAIGS GRECFVAGSV GPLGSRDSEE THSVDDQKSL FREQMTGLVN GGVDLLLLET FASLAELQLA ASVAVEFGLP VIAQMAFFAE GRTREGLDGG QFVAALKSDV DVVGANCGVG PHEMLQLVRQ MVAATSGPVS AFANSGFPQY VNGRHVYLAT PDYFAARGLE MVEAGAGLVG GCCGTTPEHI AALTAQIQGV KPSRVAVPHP VERRKPVAVE VGESRQTTVS PLLDPARKTV PITVELDPPR GLDCSLTIER AKLLAQNGVD AINLAENPLA RIRMGNLALA AKIQDATGIP VIAHVTCRDR NLIGLHSDLM GAHLLGLRHI LAVTGDPVSV GETSGATSVF DLNSVGLLDL LSHLNQGRNM LGADLGEGTG FCLGAAFNPN VTHLQGQVNK LKKKLAAGAQ FFQTQPVYSS TVFQDMVQAL QDVSAPVFLG LLPLVSERNA EFLHNEVPGI TLPDEVRKRM RGTVGDSGVV AGMGIASELV RSCAPQADGY YIMPPFGKVD LALQLIEIIK ATSA // ID Q1KMD2_SPAAU Unreviewed; 401 AA. AC Q1KMD2; DT 30-MAY-2006, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 2. DT 04-MAR-2015, entry version 34. DE SubName: Full=Betaine homocysteine methyltransferase {ECO:0000313|EMBL:ABF06673.2}; GN Name=BHMT {ECO:0000313|EMBL:ABF06673.2}; OS Sparus aurata (Gilthead sea bream). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Spariformes; Sparidae; Sparus. OX NCBI_TaxID=8175 {ECO:0000313|EMBL:ABF06673.2}; RN [1] {ECO:0000313|EMBL:ABF06673.2} RP NUCLEOTIDE SEQUENCE. RA Laize V., Parameswaran V., Tiago D.M., Coelho N.C., Pombinho A.R., RA Cancela M.L.; RT "Cloning of betaine homocysteine methyltransferase cDNA from gilthead RT seabream Sparus aurata."; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DQ470488; ABF06673.2; -; mRNA. DR HOVERGEN; HBG080367; -. DR UniPathway; UPA00051; UER00083. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000313|EMBL:ABF06673.2}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000313|EMBL:ABF06673.2}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 210 210 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 292 292 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 401 AA; 44290 MW; FB13E57816313040 CRC64; MAPVKKGILE RLNAGEVVIG DGGFVFALEK RGYVKAGPWT PEATVTHPEA VRQLHREFLR AGANVMQTFT FYASDDKLEN RGQSLKYTGA QINEAACDLA KEVASEGDAL VAGGVCQTPS YLSCKSETEV KAIFKKQMEV FIKKNVDFLI AEYFEHVEEA EWAVQVLKTG GKPVAASMCI GPEGDMHGVS PAECAVRLVK AGAQIIGVNC HFDPMTCVQA VKMMKAGVEK AGLKAHYMVQ PLAYHTPDCN CQGFIDLPEF PFALEPRILT RWDMHKYARE AYKVGIRFIG GCCGFEPYHI RAVAEELAPE RGIMPPGSEK HGMWGSALEM HTKPWVRARS RREYWENVMP ASGRPKCPSL STPECWGVTK GHADLLQHKE ATSTQEMKHV LEMQKKAKSS A // ID Q1LSA3_RALME Unreviewed; 355 AA. AC Q1LSA3; DT 30-MAY-2006, integrated into UniProtKB/TrEMBL. DT 30-MAY-2006, sequence version 1. DT 27-MAY-2015, entry version 62. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABF06973.1}; DE EC=2.1.1.5 {ECO:0000313|EMBL:ABF06973.1}; GN Name=bhmT {ECO:0000313|EMBL:ABF06973.1}; GN OrderedLocusNames=Rmet_0087 {ECO:0000313|EMBL:ABF06973.1}; OS Ralstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Cupriavidus. OX NCBI_TaxID=266264 {ECO:0000313|EMBL:ABF06973.1, ECO:0000313|Proteomes:UP000002429}; RN [1] {ECO:0000313|EMBL:ABF06973.1, ECO:0000313|Proteomes:UP000002429} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CH34 / ATCC 43123 / DSM 2839 RC {ECO:0000313|Proteomes:UP000002429}; 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; ABF06973.1; -; Genomic_DNA. DR RefSeq; WP_011515008.1; NC_007973.1. DR RefSeq; YP_582242.1; NC_007973.1. DR ProteinModelPortal; Q1LSA3; -. DR STRING; 266264.Rmet_0087; -. DR EnsemblBacteria; ABF06973; ABF06973; Rmet_0087. DR KEGG; rme:Rmet_0087; -. DR PATRIC; 20284690; VBIRalMet4734_0462. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; CMET266264:GJ5G-89-MONOMER; -. DR Proteomes; UP000002429; Chromosome. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002429}; KW Methyltransferase {ECO:0000313|EMBL:ABF06973.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002429}; KW Transferase {ECO:0000313|EMBL:ABF06973.1}. SQ SEQUENCE 355 AA; 38356 MW; B7846CADDC2924ED CRC64; MSAAQSQPRP YTRAASLPKL LRDRILILDG AMGTMIQRYK LTEADYRGTR FADHRIDVKG NNELLLLTRP QVITEIHEQY LAAGADLIET NTFGATRVAQ EDYKMADLAY EMNVEAARLA RAACDKYSTP DKPRFVAGAF GPTPKTASIS PDVNDPGARN VTFEELRDSY YEQGKALLEG GADVFLVETI FDTLNAKAAL FAIDQLFEDT GERVPVMISG TVTDASGRIL SGQTVEAFWN SLRHAKPVTF GLNCALGATL MRPYIAELAK VCDAAVSCYP NAGLPNPMSD TGFDETPEVT SALVEEFAAS GLVNLVGGCC GTTPDHIAAI AKSVANKTPR TWPGQYREDT AQSAA // ID Q1M793_RHIL3 Unreviewed; 302 AA. AC Q1M793; DT 30-MAY-2006, integrated into UniProtKB/TrEMBL. DT 30-MAY-2006, sequence version 1. DT 27-MAY-2015, entry version 48. DE SubName: Full=Putative methyltransferase {ECO:0000313|EMBL:CAK10639.1}; GN OrderedLocusNames=pRL100413 {ECO:0000313|EMBL:CAK10639.1}; OS Rhizobium leguminosarum bv. viciae (strain 3841). OG Plasmid pRL10 {ECO:0000313|EMBL:CAK10639.1, OG ECO:0000313|Proteomes:UP000006575}. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=216596 {ECO:0000313|EMBL:CAK10639.1, ECO:0000313|Proteomes:UP000006575}; RN [1] {ECO:0000313|EMBL:CAK10639.1, ECO:0000313|Proteomes:UP000006575} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3841 {ECO:0000313|EMBL:CAK10639.1}; RX PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34; RA Young J.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 A., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM236084; CAK10639.1; -; Genomic_DNA. DR RefSeq; WP_011654437.1; NC_008381.1. DR RefSeq; YP_770689.1; NC_008381.1. DR ProteinModelPortal; Q1M793; -. DR STRING; 216596.pRL100413; -. DR EnsemblBacteria; CAK10639; CAK10639; pRL100413. DR KEGG; rle:pRL100413; -. DR PATRIC; 23147220; VBIRhiLeg32091_6508. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; DVITANS; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; RLEG216596:GKE5-6671-MONOMER; -. DR Proteomes; UP000006575; Plasmid pRL10. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006575}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:CAK10639.1}; KW Plasmid {ECO:0000313|EMBL:CAK10639.1}; KW Transferase {ECO:0000313|EMBL:CAK10639.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 209 209 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 302 AA; 32715 MW; 977B700B925E7B8A CRC64; MSTMRILDGG MSRELLRLGA ELKQPEWSAL ALINAPDIVR RVHQEFIAAG SEVITTNSYA LVPFHIGEDR FQKEGAALIR LAGRLAREAA DSVTDRKVLV AGSLPPIFGS YEPQNFQPSR VQDYLEVLVE NLSPFVDIWL GETLSLIAEA EAVRKAVATS GKPFWISFTL ADDEAAIRGG EPKLRSEERV EEAASWAVSS GADALLFNCS KPEVMQAAVE TAARVFRKMD AHIEIGVYAN AFQGEQGEAA ANEGLHETRA DLNDDAYSRY ACSWAEAGAT IIGGCCGIGA AHIHRLKKTL LG // ID Q1MDX8_RHIL3 Unreviewed; 1236 AA. AC Q1MDX8; DT 30-MAY-2006, integrated into UniProtKB/TrEMBL. DT 30-MAY-2006, sequence version 1. DT 27-MAY-2015, entry version 70. DE SubName: Full=Putative methionine synthase {ECO:0000313|EMBL:CAK08849.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAK08849.1}; GN Name=metH {ECO:0000313|EMBL:CAK08849.1}; GN OrderedLocusNames=RL3362 {ECO:0000313|EMBL:CAK08849.1}; OS Rhizobium leguminosarum bv. viciae (strain 3841). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=216596 {ECO:0000313|EMBL:CAK08849.1, ECO:0000313|Proteomes:UP000006575}; RN [1] {ECO:0000313|EMBL:CAK08849.1, ECO:0000313|Proteomes:UP000006575} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3841 {ECO:0000313|EMBL:CAK08849.1, RC ECO:0000313|Proteomes:UP000006575}; RX PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34; RA Young J.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 A., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AM236080; CAK08849.1; -; Genomic_DNA. DR RefSeq; WP_011652850.1; NC_008380.1. DR RefSeq; YP_768941.1; NC_008380.1. DR ProteinModelPortal; Q1MDX8; -. DR SMR; Q1MDX8; 645-1223. DR STRING; 216596.RL3362; -. DR EnsemblBacteria; CAK08849; CAK08849; RL3362. DR KEGG; rle:RL3362; -. DR PATRIC; 23143445; VBIRhiLeg32091_4643. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; RLEG216596:GKE5-3413-MONOMER; -. DR Proteomes; UP000006575; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006575}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAK08849.1}; KW Transferase {ECO:0000313|EMBL:CAK08849.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 239 239 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 302 302 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 755 755 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1236 AA; 136643 MW; 112A9AB070840928 CRC64; MRQAASERIL VLDGAMGTQI QGLGYDEDQF RGTRFIGCAC HQKGNNDLLI LTQPDAIEEI HYRYAKAGAD ILETNTFSST RIAQADYEME GAVYDLNKEG AEIVRRAAQR AEREDGRRRF VAGAIGPTNR TASISPDVNN PGFRAVTFDD LRTAYGEQID GLIDGGADII LIETIFDTLN AKAAIFACEE RFEAKGVRLP VMISGTITDL SGRTLSGQTP SAFWNSVRHA NPFTIGLNCA LGANAMRPHL QELSGVADTF ICAYPNAGLP NEFGQYDETP ELMAAQIDGF AREGLVNIVG GCCGSTPEHI KAIAETVAKY KPRPIPEHRP FMSLSGLEPF ELTKDIPFVN VGERTNVTGS ARFRKLITNA DFTAALDVAR DQVENGAQVI DINMDEGLID SEKAMVEFLN LIAAEPDIAR VPVMIDSSKF SIIESGLKRV QGKPIVNSIS LKEGEENFLA QARLLHNYGA AVVVMAFDET GQADSYERKV EICTRAYKLL TEKIGYPPED IIFDPNIFAV ATGIEEHNNY GVDFIEATRT IRERMPLVHI SGGVSNLSFS FRGNEPVREA MHAVFLYHAI QAGMDMGIVN AGQLAVYDNI DPELREACED VVLNRRPDGT ERLLEVAEKF RGGAAREGRV QDLSWREWSV EKRLEHALVN GITEYIEADT EEARLQAVRP LHVIEGPLMA GMNVVGDLFG SGKMFLPQVV KSARVMKQAV AVLLPYMEEE KRLNGGDERR SAGKILMATV KGDVHDIGKN IVGVVLACNN YEIVDLGVMV PATKILETAI AEKVDVIGLS GLITPSLDEM VHVAAEMERQ GFEIPLLIGG ATTSRVHTAV KIHPGYNKGQ TIYVTDASRA VGVVSALLSP ETRHSYVDDI RAEYAKVAAA HARSEAEKVR LPLPRARENA HKVDWSAYRP VKPQFFGTRV FEDYDLAELA KYVDWTPFFQ TWELRGRYPA ILEDEKQGEA ARALWADAQA MLKKIIDEKW FRPRAVIGFW PAGAVGDDIR LFTDESRKHE LETFYTLRQQ LSKRDGRPNV ALSDFVAPVS SGVEDYVGGF VVTAGIEEIA IAERFERAND DYSSILVKAL ADRFAEAFAE RMHEQVRREY WGYAKDETLS KEDLITEAYA GIRPAPGYPA QPDHTEKATL FKLLDAEKAA GVKLTESYAM WPGSSVSGLY IGHPDSYYFG VAKVERDQVE DYAKRKGMGI TEVERWLGPV LNYVPRKAET EIEDAA // ID Q1MJK6_RHIL3 Unreviewed; 315 AA. AC Q1MJK6; DT 30-MAY-2006, integrated into UniProtKB/TrEMBL. DT 30-MAY-2006, sequence version 1. DT 29-APR-2015, entry version 44. DE SubName: Full=Putative homocysteine S-methyltransferase {ECO:0000313|EMBL:CAK06854.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:CAK06854.1}; GN OrderedLocusNames=RL1357 {ECO:0000313|EMBL:CAK06854.1}; OS Rhizobium leguminosarum bv. viciae (strain 3841). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=216596 {ECO:0000313|EMBL:CAK06854.1, ECO:0000313|Proteomes:UP000006575}; RN [1] {ECO:0000313|EMBL:CAK06854.1, ECO:0000313|Proteomes:UP000006575} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3841 {ECO:0000313|EMBL:CAK06854.1, RC ECO:0000313|Proteomes:UP000006575}; RX PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34; RA Young J.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 A., 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; CAK06854.1; -; Genomic_DNA. DR RefSeq; WP_011651068.1; NC_008380.1. DR RefSeq; YP_766963.1; NC_008380.1. DR STRING; 216596.RL1357; -. DR EnsemblBacteria; CAK06854; CAK06854; RL1357. DR KEGG; rle:RL1357; -. DR PATRIC; 23139205; VBIRhiLeg32091_2545. DR eggNOG; COG2040; -. DR HOGENOM; HOG000179103; -. DR KO; K00547; -. DR OMA; CCGTDHR; -. DR OrthoDB; EOG6R5C46; -. DR BioCyc; RLEG216596:GKE5-1389-MONOMER; -. DR Proteomes; UP000006575; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006575}; KW Methyltransferase {ECO:0000313|EMBL:CAK06854.1}; KW Transferase {ECO:0000313|EMBL:CAK06854.1}. SQ SEQUENCE 315 AA; 34210 MW; B61BE030D300FAE1 CRC64; MAKYRNGLPQ LTGGTFITDG GMETTMIFQE GIELPHFAAF ILLASEDGRQ RMRNYYRRYL DVARRHGTGF VLDTATWRAN PEWGQKLGYT SEALKAVNEE AVDLLIGLRS AYERPEQPIV ISGAIGPRGD GYKAGVMDAT EAEDYHAFQI AAFAGTEADM VSAFTLTNID EAIGVARAAQ ALGMPSAISF TLETDGRLVT GRSLQEAIET TDAMTGGAPA YYMINCAHPT HFETALDHGS AWVKRISGIR ANASTMSHEQ LDNSETLDAG DPEDLGRRYR KLIDRMPAVR VLGGCCGTDH RHVAAICEAC LPQAA // ID Q1N6S0_9GAMM Unreviewed; 346 AA. AC Q1N6S0; DT 30-MAY-2006, integrated into UniProtKB/TrEMBL. DT 30-MAY-2006, sequence version 1. DT 27-MAY-2015, entry version 33. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EAT13522.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EAT13522.1}; GN Name=metH {ECO:0000313|EMBL:EAT13522.1}; GN ORFNames=RED65_09029 {ECO:0000313|EMBL:EAT13522.1}; OS Bermanella marisrubri. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Bermanella. OX NCBI_TaxID=207949 {ECO:0000313|EMBL:EAT13522.1}; RN [1] {ECO:0000313|EMBL:EAT13522.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=RED65 {ECO:0000313|EMBL:EAT13522.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAT13522.1}. 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; AAQH01000001; EAT13522.1; -; Genomic_DNA. DR RefSeq; WP_007016943.1; NZ_CH724113.1. DR ProteinModelPortal; Q1N6S0; -. DR EnsemblBacteria; EAT13522; EAT13522; RED65_09029. DR PATRIC; 27181658; VBIBerMar44794_0069. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EAT13522.1}; KW Transferase {ECO:0000313|EMBL:EAT13522.1}. SQ SEQUENCE 346 AA; 38087 MW; 453874406A0E14E5 CRC64; MTQSKYEQLY KTLRERIMVL DGAMGTSIQQ YDLDEDDFRK GHFDDHPSPL KGNNDLLSIT RPDIIEEIHD SFFEIGADFA CTNAFSGTTI AQADYNLEHA VYQINYEAAQ CARRSADKWT AKTPEQPRYV VGCLGPTNRT ASISPDVNDP GMRLVTFDDL VKAYKDAAEA LVDGGIDIIM VETVFDTLNA KAAVFACLEM KRERNIEMPV MVSGTITDAS GRTLSGQTAE AFWVSLMHGN LFSIGLNCAL GADDMLPHIK LLDKNATCMI SAHPNAGLPN EFGEYDQTAE QMAEQVRPFL SEGHVNIIGG CCGTTPAHIA ALKKLADEYK PRPFTEAFEQ KLQGGK // ID Q1N8M3_SPHSS Unreviewed; 348 AA. AC Q1N8M3; DT 30-MAY-2006, integrated into UniProtKB/TrEMBL. DT 30-MAY-2006, sequence version 1. DT 27-MAY-2015, entry version 32. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EAT07412.1}; GN ORFNames=SKA58_14192 {ECO:0000313|EMBL:EAT07412.1}; OS Sphingomonas sp. (strain SKA58). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingomonas. OX NCBI_TaxID=314266 {ECO:0000313|EMBL:EAT07412.1}; RN [1] {ECO:0000313|EMBL:EAT07412.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SKA58 {ECO:0000313|EMBL:EAT07412.1}; 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. {ECO:0000313|EMBL:EAT07412.1}. 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; AAQG01000021; EAT07412.1; -; Genomic_DNA. DR RefSeq; WP_009822588.1; NZ_CH959307.1. DR ProteinModelPortal; Q1N8M3; -. DR EnsemblBacteria; EAT07412; EAT07412; SKA58_14192. DR PATRIC; 29449695; VBISphSp87348_2601. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EAT07412.1}; KW Transferase {ECO:0000313|EMBL:EAT07412.1}. SQ SEQUENCE 348 AA; 37423 MW; AB0C6E1C230C7CE8 CRC64; MTAEQKFRQL AAEKILIFDG GYGTSIQKHG LAEADYRGEL DLAKDQKGNN DLLCLTRPDI VEGIHTAYLD AGADMVETNT FSSTKIAMAD YGCEHLVWDI NLAAARLARS ACEKASAKDG KPRFVCGSIG PTNKTLSISP DVNDPAYREV DYDTLKADYR EQCDALIAGG VDFLLVETCF DTLNAKAAGM AAREAEAAAG RSVPLMLSFT ITDMSGRNLS GHTINAFWYS LRHLKPLTIG VNCAFGADLL RPYLSELSKN ADTLILAYPN AGLPNELGQY DELPETTAKL IRDWVDEGLV NMVGGCCGTT PAHIGAVAKA LAGHKPRMVP DLPVVTRLAG LEPMHIAA // ID Q1NKM5_9DELT Unreviewed; 704 AA. AC Q1NKM5; DT 30-MAY-2006, integrated into UniProtKB/TrEMBL. DT 30-MAY-2006, sequence version 1. DT 27-MAY-2015, entry version 56. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=MldDRAFT_3065 {ECO:0000313|EMBL:EAT02251.1}; OS delta proteobacterium MLMS-1. OC Bacteria; Proteobacteria; Deltaproteobacteria. OX NCBI_TaxID=262489 {ECO:0000313|EMBL:EAT02251.1}; RN [1] {ECO:0000313|EMBL:EAT02251.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MLMS-1 {ECO:0000313|EMBL:EAT02251.1}; 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] {ECO:0000313|EMBL:EAT02251.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MLMS-1 {ECO:0000313|EMBL:EAT02251.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {ECO:0000256|RuleBase:RU004255}. CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAT02251.1}. 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; AAQF01000267; EAT02251.1; -; Genomic_DNA. DR RefSeq; WP_007294817.1; NZ_AAQF01000267.1. DR ProteinModelPortal; Q1NKM5; -. DR EnsemblBacteria; EAT02251; EAT02251; MldDRAFT_3065. DR PATRIC; 38448357; VBIDelPro91573_4506. DR UniPathway; UPA00193; -. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004255}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EAT02251.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EAT02251.1}. SQ SEQUENCE 704 AA; 76785 MW; 9C86661E0DE5CE79 CRC64; MFSFDYDYDN DNDKEENGNK SFARAAPQRL CCGAERFCSR QMVSGCFTTR GWLLPPPGNR ARVPRHQHDN RDRQPMKPDF LEYLQEKVIL GDGAIGTYLY SKGVELGKDT DRLNLSDPDL IYSLHEEYIR AGSQLIETNT FGANRLKLLA NGLENQAREI NLAGAGIAKR AAGEDIYVAG SVGPTGVEFP LEAGEIEPAE VAAAYEEQIS ALLEAEVDLL ILETFTHLDE LLIALETARR LAPQHPIVAQ MAYPAQGRTA RGDHALTCGT AAIAAGASLV GANCGRGVNS MLTAIEALSP LRDQVPLSAF PNAGFPEIVG HRMIYPAQPE YMARVVGEMI KLGARLVGGC CGTSPTHIQE FRKQLKIAKR PVAHARAASM EAQASDQPQT ANKVGSLLRE LQPDRMPILV ELDPPTHLDM GGVLEGAKAL AAGGTDAISL GESPLAVLRT ENLALAHRIQ QEAGIKTIIH LTCRDRNALG LQSHIMGAHL LGIDSILAVT GDPATSSDQP GVSGVFDVRS FGLVRMIDRF NQGFNMAGKN IKEKTDFSLG VAFSYRPSNP QVQIKRLERK AALGARYVMT QPFFAADEVE AMMEKTSHLD LLIFPGIFPL ISARNADFLH NEVPGISIPA TLRQKLHQYE QVEDQRRVAM DFTRELVEKI SSFSDGLYLI SPLNKWEVAN DLVTMVRQAG WQGSGRVARF AGKE // ID Q1NSQ8_9DELT Unreviewed; 704 AA. AC Q1NSQ8; DT 30-MAY-2006, integrated into UniProtKB/TrEMBL. DT 30-MAY-2006, sequence version 1. DT 27-MAY-2015, entry version 56. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=MldDRAFT_4660 {ECO:0000313|EMBL:EAT04747.1}; OS delta proteobacterium MLMS-1. OC Bacteria; Proteobacteria; Deltaproteobacteria. OX NCBI_TaxID=262489 {ECO:0000313|EMBL:EAT04747.1}; RN [1] {ECO:0000313|EMBL:EAT04747.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MLMS-1 {ECO:0000313|EMBL:EAT04747.1}; 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] {ECO:0000313|EMBL:EAT04747.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MLMS-1 {ECO:0000313|EMBL:EAT04747.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Note=FAD.; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {ECO:0000256|RuleBase:RU004255}. CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAT04747.1}. 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; AAQF01000053; EAT04747.1; -; Genomic_DNA. DR RefSeq; WP_007292668.1; NZ_AAQF01000053.1. DR ProteinModelPortal; Q1NSQ8; -. DR EnsemblBacteria; EAT04747; EAT04747; MldDRAFT_4660. DR PATRIC; 38443039; VBIDelPro91573_2004. DR UniPathway; UPA00193; -. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004255}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EAT04747.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:EAT04747.1}. SQ SEQUENCE 704 AA; 76799 MW; 244E828CB4CE5998 CRC64; MFSFDYDYDN DNDKEENGNK SFARAAPQRL CCGAERFCSR QMVSGCFTTR GWLLPPPGNR ARVPRHQHDN RDRQPMKPDF LEYLQEKVIL GDGAIGTYLY SKGIELGKDT DRLNLSDPDL IYSLHEEYIR AGSQLIETNT FGANRLKLLA NGLENQAREI NLAGAGIAKR AAGEDIYVAG SVGPTGVEFP LEAGEIEPAE VAAAYEEQIS ALLEAEVDLL ILETFTHLDE LLIALETARR LAPQHPIVAQ MAYPAQGRTA RGDHALTCGT AAIAAGASLV GANCGRGVNS MLTAIEALSP LRDQVPLSAF PNAGFPEIVG HRMIYPAQPE YMARVVGEMI KLGARLVGGC CGTSPTHIQE FRKQLKIAKR PVAHARAASM EAQASDQPQT ANKVGSLLRE LQPDRMPILV ELDPPTHLDM GGVLEGAKAL AAGGTDAISL GESPLAVLRT ENLALAHRIQ QEAGIKTIIH LTCRDRNALG LQSHIMGAHL LGIDSILAVT GDPATSSDQP GVSGVFDVRS FGLVRMIDRF NQGFNMAGKN IKEKTDFSLG VAFSYRPSNP QVQIKRLERK AALGARYVMT QPFFAADEVE AMMEKTSHLD LLIFPGIFPL ISARNADFLH NEVPGISIPA TLRQKLHQYE QVEDQRRVAM DFTRELVEKI SSFSDGLYLI SPLNKWEVAN DLVTMVRQAG WQGSGRVARF AGKE // ID Q1QDM1_PSYCK Unreviewed; 1271 AA. AC Q1QDM1; DT 16-MAY-2006, integrated into UniProtKB/TrEMBL. DT 16-MAY-2006, sequence version 1. DT 01-APR-2015, entry version 70. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABE74232.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABE74232.1}; GN OrderedLocusNames=Pcryo_0449 {ECO:0000313|EMBL:ABE74232.1}; OS Psychrobacter cryohalolentis (strain K5). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Psychrobacter. OX NCBI_TaxID=335284 {ECO:0000313|EMBL:ABE74232.1, ECO:0000313|Proteomes:UP000002425}; RN [1] {ECO:0000313|Proteomes:UP000002425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K5 {ECO:0000313|Proteomes:UP000002425}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000323; ABE74232.1; -; Genomic_DNA. DR RefSeq; WP_011512817.1; NC_007969.1. DR RefSeq; YP_579716.1; NC_007969.1. DR ProteinModelPortal; Q1QDM1; -. DR SMR; Q1QDM1; 699-937. DR STRING; 335284.Pcryo_0449; -. DR EnsemblBacteria; ABE74232; ABE74232; Pcryo_0449. DR KEGG; pcr:Pcryo_0449; -. DR PATRIC; 23060347; VBIPsyCry128170_0513. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PCRY335284:GHE9-464-MONOMER; -. DR Proteomes; UP000002425; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002425}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABE74232.1}; KW Transferase {ECO:0000313|EMBL:ABE74232.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 352 352 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 353 353 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 804 804 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1271 AA; 140424 MW; EE8166DD37442584 CRC64; MIPTARSQTN TSLTNLTDAS NPNANPNDFI LTPPAVFPYK DQQLTARARI TEQMAARILM LDGAMGTHIQ NYKLEEADYR GERFADIKQD VRGNNDLLVL TQPHMIKEIH LAHLESGADI IETNSFNGTR LSMADYDMQY LVPELNKTAA KIAREAADEY TAKNPEKPRF VAGVIGPTSR TCSLSPDVND PAFRNITFDE LVLNYREATL ALMEGGVDII LIETIFDTLN AKAAIFAVTG VFDDIGFELP IMISGTITDA SGRTLSGQTA EAFYNSIRHA KPLSVGFNCA LGADALRPHI QTLSNIANTY VSAHPNAGLP NEFGEYDETA DETAALLEGF AKAGILNIVG GCCGTTPEHI RQIANMVAKY PPRIIPEIPP ACRLSGLEPF TINKDSLFVN VGERTNVTGS KKFLRLIKTE AYLEALDVAR DQVEGGAQIV DINMDEGMLD SKQAMIHFVN LVSGEPDISR VPLMIDSSKW DIIEEGLKRT QGKCVVNSIS LKEGHAEFVE RAKLCMRYGA AIIVMAFDED GQADTFERKT QICKRSYDVL VDEVGFPSED IIFDPNIFAV ATGITEHNNY GADFINATKW ITENLPNAMV SGGVSNVSFS FRGNPIREAI NSVFLYHAIQ NGLTMGIVNP AMLELYDDIP VEARDAIEDV MLNRNQGETG QDATERLMTI AENYQDGGKK KDSTVDMTWR EGTVEERIAH ALVKGITTFI EADTKEAWEK YPRPLEVIEG PLMDGMNIVG DLFGAGKMFL PQVVKSARVM KQSVAWLNPY IEAEKVEGEK KGKILMATVK GDVHDIGKNI VGVVLGCNGY DIVDLGVMVP CEKILDTAIA EKVDIIGLSG LITPSLDEMV YVAKQMQERG MTLPLMIGGA TTSKAHTAVK VEPQYQNNGV IYVADASRSV GVVTKLLSKE HCQGLIDETR EEYIKVRERL AKRQPKAAKV TYAESVKIGF QYDWETYVPP VPNKLGQVIF DNYPIANLLP YIDWTPFFIS WGLAGKYPKI LQDDVVGEAA RDLFDNANEL MQKMIDEKLI VAKGVFKLMP ARRTGADTVT VYDKAPIEGG IAEYQFEHLR QQSDKASGKP NFSLADFISP SDTHTDYLGG FTVSIVGTEA LAEKYKAAGD DYNAIMVQAL SDRLAEAFAE HLHELIRKEY WGYQPTESLT NEDMIKEKYV GIRPAPGYPA CPEHTEKGKL FEWLGTVEAI GTTLTESYAM WPASSVSGFY YSHPDSEYFN VGKISRDQLE SYAERKGWDI KTAEKWLNPN L // ID Q1QR88_NITHX Unreviewed; 1261 AA. AC Q1QR88; DT 16-MAY-2006, integrated into UniProtKB/TrEMBL. DT 16-MAY-2006, sequence version 1. DT 29-APR-2015, entry version 68. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABE61259.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABE61259.1}; GN OrderedLocusNames=Nham_0363 {ECO:0000313|EMBL:ABE61259.1}; OS Nitrobacter hamburgensis (strain X14 / DSM 10229). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Nitrobacter. OX NCBI_TaxID=323097 {ECO:0000313|EMBL:ABE61259.1, ECO:0000313|Proteomes:UP000001953}; RN [1] {ECO:0000313|EMBL:ABE61259.1, ECO:0000313|Proteomes:UP000001953} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=X14 / DSM 10229 {ECO:0000313|Proteomes:UP000001953}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000319; ABE61259.1; -; Genomic_DNA. DR RefSeq; WP_011508963.1; NC_007964.1. DR RefSeq; YP_575719.1; NC_007964.1. DR ProteinModelPortal; Q1QR88; -. DR SMR; Q1QR88; 629-1212. DR STRING; 323097.Nham_0363; -. DR EnsemblBacteria; ABE61259; ABE61259; Nham_0363. DR KEGG; nha:Nham_0363; -. DR PATRIC; 22688105; VBINitHam61822_1090. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; NHAM323097:GHP7-369-MONOMER; -. DR Proteomes; UP000001953; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001953}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABE61259.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001953}; KW Transferase {ECO:0000313|EMBL:ABE61259.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 224 224 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 287 287 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 744 744 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1261 AA; 137475 MW; 596FBEF93ED78A50 CRC64; MGTMIQALQF DEAAFRGERF KDFHRDVRGN NDLLILTQPK AIEDIHAQYL RAGADLVAAN TFSSTSIAQA DYEMSDLAYE LNREGAKLAR AAAMRVSAED GKPRFVVGAI GPTNRTASIS PDVANPGYRA VTFDDLRKAY GEQINGLLDG GADLLLVETI FDTLNAKAAL YAIAEIGEAR GIDVPVMISG TITDKSGRLL SGQLPEAFWN SIRHAKPITV GFNCALGAED MRAHIADIGR VADTLVCAYP NAGLPNEFGQ YDESPDYMAR LVGEFAASGL VNIVGGCCGT TPDHIAAIAA AVAPHTPRVI PAIEPRLRLS GLEPFTLTSD IPFVNVGERT NVTGSARFRK LIKADDYAAA LQVARDQVEN GAQIIDVNMD EGLLDSEAAI VTFLNLVASE PDIARVPIMV DSSKFSVIEA GLKCIQGKPV VNSISMKEGE EKFIREATIA RRHGAAVVVM AFDEVGQADT FARKTEICKR AYDILVNRLD FPPEDIIFDP NIFAIATGLE EHNNYGVDFI EATGWIRQNL PHAHISGGVS NLSFSFRGNE PVREAMHSVF LYHAIKAGMD MGIVNAGQMI IYDDIDPELR QTCEDVILNR DAGASERLLQ LAEKFRGAGK EAKEKDLSWR EWPVEKRLAH ALVNGITEYI EEDTEAVRLT VERPLNVIEG PLMAGMNVVG DLFGDGKMFL PQVVKSARVM KQAVAYLMPF MEEEKARNQA AGVASESSNS AGKIVLATVK GDVHDIGKNI VSIVLQCNNY EVIDLGVMVP AAKIIETAKA EKADIVGLSG LITPSLDEMG HFAAELERQG LDLPLLIGGA TTSRVHTAVK IDPNYRNGPV VHVNDASRAV GVVASLMSPE RREAYAAGVR AEYAKISAAH FRAQQDKKRL PLAAARANAV PIDWSTYRPV KPTFLGTKAF ADYPLEELVE VIDWTPFFQV WELSGRYPAI LDDKVVGETA RALYDDARKM LDRIVKEKWF KASGVIGLWP ANRIGDDIAV YSDETRTTQI ATYHTLRQQL EKREGRHNAA LADFIAPQET GIADYIGGFA VTAGIGEDEI AVRFKNANDD YSSILVKALA DRLAEAFAER MHQRVRKEFW GYARDEALTN DQLIKEDYVG IRPAPGYPAQ PDHTEKATLF RLLDATCSTG VELTESFAMW PGSSVSGLYY SHPESQYFGV GKIERDQVED YAARKGMEVA EIERWLASIL NYIPGQSGKA AATPVPAPTP ANDASADVAN HPPGCQCAVH LQLRKTKARA G // ID Q1QWB7_CHRSD Unreviewed; 1245 AA. AC Q1QWB7; DT 16-MAY-2006, integrated into UniProtKB/TrEMBL. DT 16-MAY-2006, sequence version 1. DT 27-MAY-2015, entry version 75. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABE59241.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABE59241.1}; DE Flags: Precursor; GN OrderedLocusNames=Csal_1889 {ECO:0000313|EMBL:ABE59241.1}; OS Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB OS 13768). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Chromohalobacter. OX NCBI_TaxID=290398 {ECO:0000313|EMBL:ABE59241.1, ECO:0000313|Proteomes:UP000000239}; RN [1] {ECO:0000313|Proteomes:UP000000239} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 3043 / ATCC BAA-138 / NCIMB 13768 RC {ECO:0000313|Proteomes:UP000000239}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000285; ABE59241.1; -; Genomic_DNA. DR RefSeq; WP_011507187.1; NC_007963.1. DR RefSeq; YP_573940.1; NC_007963.1. DR ProteinModelPortal; Q1QWB7; -. DR SMR; Q1QWB7; 661-1245. DR STRING; 290398.Csal_1889; -. DR EnsemblBacteria; ABE59241; ABE59241; Csal_1889. DR KEGG; csa:Csal_1889; -. DR PATRIC; 21447590; VBIChrSal113723_1901. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR Proteomes; UP000000239; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000239}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABE59241.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000239}; KW Signal {ECO:0000313|EMBL:ABE59241.1}; KW Transferase {ECO:0000313|EMBL:ABE59241.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT SIGNAL 1 20 Potential. {ECO:0000313|EMBL:ABE59241.1}. FT CHAIN 21 1245 Potential. {ECO:0000313|EMBL:ABE59241.1}. FT /FTId=PRO_5000112812. FT METAL 256 256 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 319 319 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 320 320 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 768 768 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1245 AA; 137319 MW; 2A3C11E98E66CE9E CRC64; MPAAIASSLP LAASFASLQE QLSRRIMILD GGMGTMLQGY ELDEGDFRGQ RFADWPSELK GNNDLLVLTR PDVVRDIHRA YLEAGADIVE TNTFNSTQLS QSDYGMQSLV PELNREAARL AKDVCDAVAR ETGVPRYVAG VLGPTSRTAS LSPDVNDPAK RNVTFDQLCD NYYQAAEALL EGGADLIMIE TIFDTLNAKA AIYALEMLFE ARGERLPVMI SGTITDASGR TLSGQTTEAF WNSIRHAQPL SVGLNCALGA AELRPYLEEL SHKADTYVSA HPNAGLPNEF GEYDQTAEEM ATIVREFAES GLVNIIGGCC GTAPEHIAAI RDAVGELPPR QVVERPKACR LAGLEPFNIE ADSLFVNVGE RTNVTGSARF KRLIKEEDYT TALEVALEQV ENGAQVIDIN MDEGMLESQD AMVRFLNLIA SEPDISRVPV MIDSSKWEII EAGLKCVQGK AVVNSISLKE GEDAFRQQAT ACRRYGAAIV VMAFDEEGQA DTFQRKTEIC ERAYRLLVDD IGFPAEDIIF DPNIFAIATG IEEHNNYAVD FIEASKWIRE HLPHAMLSGG VSNVSFSFRG NNAVREAIHS VFLYHAIKAG LTMGIVNAGQ LAVYDDLPEE LREAVEDVVL NRRDDGTERL LDIADKYKGD GSGGEKKEDL EWRSWEVEKR IEHALIKGIT AYIEEDTEQA RQRAARPIEV IEGPLMDGMN VVGDLFGAGK MFLPQVVKSA RVMKQAVAYL IPYIEAEKSE GTQAKGKIVM ATVKGDVHDI GKNIVGVVLQ CNNYEVIDLG VMVPAEKIFA AAREHNADII GLSGLITPSL DEMVHVAKEM QRQGFTLPLL IGGATTSKAH TAVKIAPQYD QPVIYVSDAS RAVGVASRLL SPSLKPGYVA EISDEYDKVR ERNAKRRPKA ADLSYAEARK RRPALDWADY TPPTPTFSGL KVFDDYPLEE LVERIDWTPF FMSWQLSGKY PRILEDDVVG EAARSLFADA QTMLRKLIDE RHITARGVIG MWPANSVDDD TLEVYADTSR RTVIERLHHI RQQTTKNRDG VCQSLADFIA PRRLDNGEPS DQVDWIGGFA VTTGHGADAL AAQYEAAGDD YNAIMVKALA DRLAEAFAER MHERVRKEFW AYVPDETLDN DALIAEQYQG IRPAPGYPAC PDHTEKATLF RLLDATAKTG IELTDSYAMW PSAAVSGWYF SHPRSKYFST GKIGRDQVES LAARKGMSLA ELERWLSPVL SYDPE // ID Q1R1H9_CHRSD Unreviewed; 349 AA. AC Q1R1H9; DT 16-MAY-2006, integrated into UniProtKB/TrEMBL. DT 16-MAY-2006, sequence version 1. DT 27-MAY-2015, entry version 54. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABE57429.1}; GN OrderedLocusNames=Csal_0065 {ECO:0000313|EMBL:ABE57429.1}; OS Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB OS 13768). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Chromohalobacter. OX NCBI_TaxID=290398 {ECO:0000313|EMBL:ABE57429.1, ECO:0000313|Proteomes:UP000000239}; RN [1] {ECO:0000313|Proteomes:UP000000239} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 3043 / ATCC BAA-138 / NCIMB 13768 RC {ECO:0000313|Proteomes:UP000000239}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; ABE57429.1; -; Genomic_DNA. DR RefSeq; WP_011505375.1; NC_007963.1. DR RefSeq; YP_572128.1; NC_007963.1. DR ProteinModelPortal; Q1R1H9; -. DR STRING; 290398.Csal_0065; -. DR EnsemblBacteria; ABE57429; ABE57429; Csal_0065. DR KEGG; csa:Csal_0065; -. DR PATRIC; 21443818; VBIChrSal113723_0068. DR eggNOG; COG0646; -. DR HOGENOM; HOG000231636; -. DR KO; K00544; -. DR OMA; KAHYMSQ; -. DR OrthoDB; EOG6NSGDJ; -. DR Proteomes; UP000000239; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000239}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ABE57429.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000239}; KW Transferase {ECO:0000313|EMBL:ABE57429.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 209 209 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 298 298 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 349 AA; 38304 MW; 3EDEF1B213FB2B5A CRC64; MTQDLITQRL DQGPLICAEG FLFELERRGY LSAGEFVPEV ALLRPDALEA LHRDFQHAGS DVVQAFTYNG HREKMRVIGK EELLEPLNRA ALKIARKVAD EKPGNLMAGN ISNSNVWDPE DPAAQQSVRA MFDEMVQWAV EEGADFIIAE TFYYAGEAEA ALAAIKAQGL PAVVTLAPMA ENRMVDGLGI VETCVALEQQ GASVVGLNCF RGPDTMRPWI QQIRDAVTCH VAALPVTYRT TEQEPTFFNL SDNQGCSCPA PHGRAFPTAL DPLFCNRYEL GAFARDVHAL GVNYLGVCCG ASPMHVREVA MAVGREPEAA QFAERMENHF MYGSHERLPE HIAALGEKA // ID Q1R3S9_ECOUT Unreviewed; 1227 AA. AC Q1R3S9; DT 16-MAY-2006, integrated into UniProtKB/TrEMBL. DT 16-MAY-2006, sequence version 1. DT 27-MAY-2015, entry version 73. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:ABE09985.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABE09985.1}; GN Name=metH {ECO:0000313|EMBL:ABE09985.1}; GN OrderedLocusNames=UTI89_C4577 {ECO:0000313|EMBL:ABE09985.1}; OS Escherichia coli (strain UTI89 / UPEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=364106 {ECO:0000313|EMBL:ABE09985.1, ECO:0000313|Proteomes:UP000001952}; RN [1] {ECO:0000313|EMBL:ABE09985.1, ECO:0000313|Proteomes:UP000001952} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UTI89 / UPEC {ECO:0000313|Proteomes:UP000001952}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000243; ABE09985.1; -; Genomic_DNA. DR RefSeq; WP_000096034.1; NC_007946.1. DR RefSeq; YP_543516.1; NC_007946.1. DR ProteinModelPortal; Q1R3S9; -. DR SMR; Q1R3S9; 651-1227. DR STRING; 364106.UTI89_C4577; -. DR EnsemblBacteria; ABE09985; ABE09985; UTI89_C4577. DR KEGG; eci:UTI89_C4577; -. DR PATRIC; 18458562; VBIEscCol42261_4458. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; ECOL364106:GHPQ-4531-MONOMER; -. DR Proteomes; UP000001952; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001952}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABE09985.1}; KW Transferase {ECO:0000313|EMBL:ABE09985.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136147 MW; 7D6CFC46002A84C0 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPAEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPT ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANTQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KMLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAE // ID Q1UZR2_PELUQ Unreviewed; 353 AA. AC Q1UZR2; DT 16-MAY-2006, integrated into UniProtKB/TrEMBL. DT 16-MAY-2006, sequence version 1. DT 27-MAY-2015, entry version 34. DE SubName: Full=Betaine-homocysteine methyltransferase {ECO:0000313|EMBL:EAS84129.1}; GN ORFNames=PU1002_00365 {ECO:0000313|EMBL:EAS84129.1}; OS Candidatus Pelagibacter ubique HTCC1002. OC Bacteria; Proteobacteria; Alphaproteobacteria; SAR11 cluster; OC Candidatus Pelagibacter. OX NCBI_TaxID=314261 {ECO:0000313|EMBL:EAS84129.1, ECO:0000313|Proteomes:UP000005306}; RN [1] {ECO:0000313|EMBL:EAS84129.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC1002 {ECO:0000313|EMBL:EAS84129.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAS84129.1}. 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; AAPV01000002; EAS84129.1; -; Genomic_DNA. DR RefSeq; WP_006996716.1; NZ_CH724130.1. DR ProteinModelPortal; Q1UZR2; -. DR EnsemblBacteria; EAS84129; EAS84129; PU1002_00365. DR PATRIC; 30359712; VBICanPel113578_0067. DR Proteomes; UP000005306; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005306}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EAS84129.1}; KW Transferase {ECO:0000313|EMBL:EAS84129.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 213 213 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 302 302 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 353 AA; 39732 MW; 3D8B5BD3FABF9A8C CRC64; MSTNKLKERL DKGPVICAEG FLFEIERRGY MSSGEFVPMV SLDHPEVLEN LHREFQHAGS DVVEAFTYNG HREKMRVIGK EELLEPLNRS ALKIAKKVAL DTPKGSKPNL MAGNISNSNI WKHNDPQSQK EVEGMFTEMI GWAVEEGADM LIGETFYYAE EAFKALEIMK KTGLPTVLTI SPMGENKMRD GKSVVDTCKE LEQLGADVVG LNCFRGPATM FPFLKEIRKA VKCHVGALPI PYRTSEDYPT FFNLPDRSNC QCPSPHGRTF PTALDPHFCN RYEIGKFAKD AYELGINYLG VCCGANPMLI REVAESIGLT VPASKYRENM ENHFMYGKNK RIPKHMTEYG DKA // ID Q1V2F2_PELUQ Unreviewed; 302 AA. AC Q1V2F2; DT 16-MAY-2006, integrated into UniProtKB/TrEMBL. DT 16-MAY-2006, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EAS84576.1}; GN ORFNames=PU1002_02626 {ECO:0000313|EMBL:EAS84576.1}; OS Candidatus Pelagibacter ubique HTCC1002. OC Bacteria; Proteobacteria; Alphaproteobacteria; SAR11 cluster; OC Candidatus Pelagibacter. OX NCBI_TaxID=314261 {ECO:0000313|EMBL:EAS84576.1, ECO:0000313|Proteomes:UP000005306}; RN [1] {ECO:0000313|EMBL:EAS84576.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC1002 {ECO:0000313|EMBL:EAS84576.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAS84576.1}. 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; AAPV01000001; EAS84576.1; -; Genomic_DNA. DR RefSeq; WP_006997163.1; NZ_CH724130.1. DR ProteinModelPortal; Q1V2F2; -. DR EnsemblBacteria; EAS84576; EAS84576; PU1002_02626. DR PATRIC; 30360636; VBICanPel113578_0513. DR Proteomes; UP000005306; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005306}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EAS84576.1}; KW Transferase {ECO:0000313|EMBL:EAS84576.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 287 287 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 302 AA; 34177 MW; 5AC573E2E3C95EDA CRC64; MDINFFKTTR ILDGGMGQEL LARGMKPNGT LWSANAVLKE EYHQLLLDTH LDFIKAGAEV IVTATFTTRR IRLRDNKIED KFEYLNKKAG EIAQKAKEQH PNVLIAGGLP PQYLTYEEDT RPDDEIKQNF YDQAKLLDPY IDFFYLDVLS SVKEFKLAIE AIEEFNKPYL IGAHISEGIN LPSGEKISDI INNINHNNLL GLILSCVSPE NFYENLEEVK NLGVPFGFKL NAFVTTNPKD GYTNSYNVSK TGNPNEFLGQ RKDLTPELMA NFVKKFKNAG ATILGGCCET RPSHIKEMLQ FK // ID Q1WRK4_LACS1 Unreviewed; 307 AA. AC Q1WRK4; DT 02-MAY-2006, integrated into UniProtKB/TrEMBL. DT 02-MAY-2006, sequence version 1. DT 27-MAY-2015, entry version 52. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABE00494.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ABE00494.1}; GN OrderedLocusNames=LSL_1692 {ECO:0000313|EMBL:ABE00494.1}; OS Lactobacillus salivarius (strain UCC118). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=362948 {ECO:0000313|EMBL:ABE00494.1, ECO:0000313|Proteomes:UP000006559}; RN [1] {ECO:0000313|EMBL:ABE00494.1, ECO:0000313|Proteomes:UP000006559} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UCC118 {ECO:0000313|EMBL:ABE00494.1, RC ECO:0000313|Proteomes:UP000006559}; RX PubMed=16617113; DOI=10.1073/pnas.0511060103; RA Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P., RA Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C., RA Collins J.K., Higgins D., Shanahan F., Fitzgerald G.F., RA van Sinderen D., O'Toole P.W.; RT "Multireplicon genome architecture of Lactobacillus salivarius."; RL Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(2006). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000233; ABE00494.1; -; Genomic_DNA. DR RefSeq; WP_011476521.1; NC_007929.1. DR RefSeq; YP_536577.1; NC_007929.1. DR ProteinModelPortal; Q1WRK4; -. DR STRING; 362948.LSL_1692; -. DR EnsemblBacteria; ABE00494; ABE00494; LSL_1692. DR GeneID; 3977129; -. DR KEGG; lsl:LSL_1692; -. DR PATRIC; 22280365; VBILacSal43464_1787. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; LSAL362948:GJDJ-1799-MONOMER; -. DR Proteomes; UP000006559; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006559}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ABE00494.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006559}; KW Transferase {ECO:0000313|EMBL:ABE00494.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 223 223 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 307 AA; 34610 MW; D29E19EB3C22A314 CRC64; MDFTEFLTNH TVVLDGAMST PLERLGADTN NDLWTAKALI DNEELVYEIH KMYFEAGADL IITDTYQANV QAFEKVGYSE KEARNLIKKA VKIAQKARDD YENRTGKHNY IAGTIGPYGA YLANGSEYRG DYELSVEEYQ QFHLPRIEEL VNAEVDILAI ETQPKLDEVL AILELLKKKY PQQKVYVSYT LSDDDTISDG TPLPRAIHAL EDYSQVIAVG INCVKLELVE PALKNMKEIT DKHLIVYPNS SAVYDPKSKT WSQPKTSATF EELIPNWYEA GARIIGGCCT TGPKEIKAVA DFIKRNR // ID Q1YJL8_MOBAS Unreviewed; 1265 AA. AC Q1YJL8; DT 02-MAY-2006, integrated into UniProtKB/TrEMBL. DT 02-MAY-2006, sequence version 1. DT 27-MAY-2015, entry version 52. DE SubName: Full=Methionine synthase, 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EAS50855.1}; GN ORFNames=SI859A1_00981 {ECO:0000313|EMBL:EAS50855.1}; OS Manganese-oxidizing bacterium (strain SI85-9A1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Aurantimonadaceae; Aurantimonas. OX NCBI_TaxID=287752 {ECO:0000313|EMBL:EAS50855.1}; RN [1] {ECO:0000313|EMBL:EAS50855.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SI85-9A1 {ECO:0000313|EMBL:EAS50855.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EAS50855.1}. 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; AAPJ01000002; EAS50855.1; -; Genomic_DNA. DR RefSeq; WP_009208844.1; NZ_CH672387.1. DR ProteinModelPortal; Q1YJL8; -. DR SMR; Q1YJL8; 673-1251. DR EnsemblBacteria; EAS50855; EAS50855; SI859A1_00981. DR PATRIC; 24559082; VBIAurMan112117_1711. DR BioCyc; AURANTIMONAS:SI859A1_00981-MONOMER; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EAS50855.1}; KW Transferase {ECO:0000313|EMBL:EAS50855.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 263 263 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 326 326 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 327 327 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 783 783 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1265 AA; 138832 MW; 1FC8B9B3C955EBA0 CRC64; MTETSDKLFG AMTEGRSPAE ASRALRKAVS ERILVLDGAM GTEIQLLGLG EDDFRGHRFG ACECHLQGNN DLLNLTQPQA IEDIHYAYAM AGADILETNT FSSTTIAQAD YQMEDQVYEL NRDGARLARR ACIRAEEKDG KRRFVAGALG PTNRTASISP DVNNPGYRAV TFDDLRIAYG EQLRGLIDGG SDLILIETIF DTLNAKAAIF ACEEIFAEKG VTLPIMISGT ITDLSGRTLS GQTPTAFWHS VRHGRPFTIG LNCALGAAAM RDHLAEISAA ADTFVCAYPN AGLPNEFGEY DQSPEQMAKE VEIFCEEGLV NVLGGCCGST PDHIKAVAET AARYKPRKVP TIAPLMRLSG LEPFTLTKEI PFVNVGERTN VTGSARFRKM IEANDLPAAL DVARSQVENG AQIIDVNMDE GLIDSKQMMI DYLNLIAAEP DIAKVPVMID SSKFEVIEAG LKCVQGKALV NSISMKEGED AFLKQARLVR SYGAAVVVMA FDEQGQADTL ERKVSICSRA YKLLTEEAGF APEDIVFDPN VFAIATGIEE HNGYGVAFIE ATRQIRQNLP GAHISGGVSN LSFSFRGNEA VREAMHAVFL YHAIQAGMDM GIVNAGQLAV YESIDPELRE ACEDVVLDRK RDDGVDPTER LLELAERWRS AGGKEAKAKD LTWREKSVQD RIAHALVNGI TEYIVEDTEE ARLEADRPLH VIEGPLMDGM NIVGDLFGAG KMFLPQVVKS ARVMKQAVAH LLPYMEEEKR LNGTDERSNA GKVLMATVKG DVHDIGKNIV GVVLACNNYE VIDLGVMVPA AKILETARRE KVDVIGLSGL ITPSLDEMVH VAAEMEREGF DIPLLIGGAT TSKVHTAVKI DPGYNRGQTV YVTDASRAVG VVSHLLSEET RGSYIEGVKA DYQKVAEAHR KGERDKKRLP LAKARANAQV SDWAAYEPVK PAITGKQVFE DWDLEELSRY IDWTPFFQTW EMKGRYPGIL EDEKQGEAAR SLFNDAQAML KQIIAEKWFQ PRAVIGFWPA NSVGDDIRLF TGDDRKEELA TLYTLRQQLT KRGDRPNVAM ADFVAPLDSG KADYVGGFVV TAGIEEEAIA NRFAKANDDY SSIMVKALAD RFAEAFAERM HEKVRREFWG YAPDETFTPE DLISEDYAGI RPAPGYPAQP DHTEKTTLFE LLDAEATTGV KLTESFAMWP GSSVSGFYIG HPDSYYFGVA KIERDQVEDY AARKGMPVAE VERWLAPILN YIPTAAAEAP AQAAE // ID Q1YME9_MOBAS Unreviewed; 336 AA. AC Q1YME9; DT 02-MAY-2006, integrated into UniProtKB/TrEMBL. DT 02-MAY-2006, sequence version 1. DT 27-MAY-2015, entry version 32. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EAS51432.1}; GN ORFNames=SI859A1_02248 {ECO:0000313|EMBL:EAS51432.1}; OS Manganese-oxidizing bacterium (strain SI85-9A1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Aurantimonadaceae; Aurantimonas. OX NCBI_TaxID=287752 {ECO:0000313|EMBL:EAS51432.1}; RN [1] {ECO:0000313|EMBL:EAS51432.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SI85-9A1 {ECO:0000313|EMBL:EAS51432.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAS51432.1}. 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; AAPJ01000001; EAS51432.1; -; Genomic_DNA. DR RefSeq; WP_009210071.1; NZ_CH672387.1. DR ProteinModelPortal; Q1YME9; -. DR EnsemblBacteria; EAS51432; EAS51432; SI859A1_02248. DR PATRIC; 24561897; VBIAurMan112117_3091. DR BioCyc; AURANTIMONAS:SI859A1_02248-MONOMER; -. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EAS51432.1}; KW Transferase {ECO:0000313|EMBL:EAS51432.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 212 212 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 278 278 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 279 279 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 336 AA; 34891 MW; 67C4A873A46F568F CRC64; MPHSLTQLLD AKGVLLADGA TGTNLFEVGL EAGEAPEMWL ESHPDRITAL HQAFVDNGAD IILSCSFGAN RHRLKLHQAE GRTHALNRIA AELARAVADA AGRPVVVGGS VGPTGELLQP LGALSYAEAV EAFREQIAGL KDGGVDVVWI ETMSAGEEVR AAAEAALACD MPYVVTGSFD SAGRTMMGIH PCDFHKAVDG LSRRPVAVGA NCGVGASDML ATALELETGS PDSALVVKAN CGIPRFVDGG TVYSGTPDQM ADYARLAIDA GARIIGGCCG TSPQHLGAMR QAIDSHVRRQ RPSIAEIVEA VGPLVNKAAS AAGETAPRTG RRRSRD // ID Q1YT41_9GAMM Unreviewed; 1222 AA. AC Q1YT41; DT 02-MAY-2006, integrated into UniProtKB/TrEMBL. DT 02-MAY-2006, sequence version 1. DT 01-APR-2015, entry version 56. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EAS47646.1}; GN ORFNames=GB2207_02542 {ECO:0000313|EMBL:EAS47646.1}; OS gamma proteobacterium HTCC2207. OC Bacteria; Proteobacteria; Gammaproteobacteria; OMG group; SAR92 clade. OX NCBI_TaxID=314287 {ECO:0000313|EMBL:EAS47646.1}; RN [1] {ECO:0000313|EMBL:EAS47646.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2207 {ECO:0000313|EMBL:EAS47646.1}; 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 (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EAS47646.1}. 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; AAPI01000002; EAS47646.1; -; Genomic_DNA. DR RefSeq; WP_007232295.1; NZ_CH672397.1. DR ProteinModelPortal; Q1YT41; -. DR SMR; Q1YT41; 648-1220. DR PRIDE; Q1YT41; -. DR EnsemblBacteria; EAS47646; EAS47646; GB2207_02542. DR PATRIC; 25905673; VBIGamPro111486_1362. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 242 242 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 754 754 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1222 AA; 133971 MW; A86CCA3971058A93 CRC64; MTDKIRQAAE QRILILDGAM GTMIQRHTLE EEDFRGQRFA DWHTDLKGNN DLLSLTQPDI ICDIHRAYLD AGADIIETNT FNSTTISQAD YDMQAISREI NVVSAQLARK AADEFSTPEK PRFVAGILGP TSRTASLSPD VNDPGARNVT FDELVEAYIE STEALIEGGV DTIMVETIFD TLNAKAALFA VQVVFEKQGF ELPIMISGTI TDASGRTLSG QTPEAFWNSV RHSKPISVGL NCALGPKELR PHLLDISTVA DTLVSSHPNA GLPNEFGGYD LDADAMAETV AEFASAGLLN IVGGCCGTTP DHIRVIANAV ATIAPRVVPE IEPACRLSGL EPFTIKSDSL FVNVGERCNV TGSAVFKRLI LEENYDAALE VARQQVINGA QIIDINMDEG MLESLPAMVK FLNLIAGEPD ISRVPIMVDS SKWDVIEAGL KCIQGKSVVN SISLKEGEAE FIERAKLCKK HGAAIVVMAF DEDGQADNLE RRKQICQRSY DLLVNEIGFP AEDIIFDPNV FAVATGIEEH NRYGLDFIEA SGWIKQNLPH ALISGGISNV SFSFRGNNPV REAIHSVFLY HAIREGLTMG IVNAGQLAVY DDLPEELRQV VEDVVLFRNA EGTDALLAIA DKYRGDGSKQ ASVEDLSWRD ADVNRRLEHS LVKGITAYIT EDTEEARQQA DRPLHVIEGA LMDGMNIVGD LFGSGKMFLP QVVKSARVMK QAVAYLQPFI EDEKDATAST NGKILMATVK GDVHDIGKNI VGVVLQCNNY EVIDLGVMVS AEKILTTARE ENVDIIGLSG LITPSLDEMV TLGKEMQRQG FTVPLMIGGA TTSKAHTAVK IAPNYENNQA IYVSDASRAV GVASKLISKE HRDEFIADIR RDYDAVRLRT ANRTPRGTLY TYPDAIKQKP QINWRDYQPT LPATPGITVI DDYPLETLVP YIDWTPFFIT WDLIGKYPKI FQDEVVGDAA TTLFADAQAL LKDIIDNKRL TARAVFGLWE ANTVNHDDIE IYAEDGSTKA SLHHIRQQIQ KPGASEELCS LADFVAPKES GIKDHIGAFA VTTGIGADEL AAEYEAKHDD YNAIMVKALA DRLAEAFAEH LHECVRREHW GYAADESLDN EALIKEKYRG IRPAPGYPAC PDHTEKGTLF ELLDVENNIG LALTDSYAMT PAAAVSGWYF AHPDAKYFNT GKIAPDQVES LAQRKGMSLP DMARWLTPVL ID // ID Q1Z1U1_PHOPR Unreviewed; 1223 AA. AC Q1Z1U1; DT 02-MAY-2006, integrated into UniProtKB/TrEMBL. DT 02-MAY-2006, sequence version 1. DT 27-MAY-2015, entry version 56. DE SubName: Full=Putative cobalamin-dependent methionine synthase {ECO:0000313|EMBL:EAS42414.1}; GN ORFNames=P3TCK_23950 {ECO:0000313|EMBL:EAS42414.1}; OS Photobacterium profundum 3TCK. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Photobacterium. OX NCBI_TaxID=314280 {ECO:0000313|EMBL:EAS42414.1}; RN [1] {ECO:0000313|EMBL:EAS42414.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=3TCK {ECO:0000313|EMBL:EAS42414.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EAS42414.1}. 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; AAPH01000020; EAS42414.1; -; Genomic_DNA. DR RefSeq; WP_006232377.1; NZ_CH724136.1. DR ProteinModelPortal; Q1Z1U1; -. DR SMR; Q1Z1U1; 653-1223. DR EnsemblBacteria; EAS42414; EAS42414; P3TCK_23950. DR PATRIC; 30919761; VBIPhoPro77067_4326. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1223 AA; 135591 MW; FCD7EB5846FC0039 CRC64; MVVKSKEILQ KRLAENILII DGGMGTMIQG YKLDENDYRG ERFADWHSDL KGNNDLLVLT QPQLIKDIHS EYLEAGADIL ETNTFNATTI AMADYDMESL SAEINFEAAK LARQAADEWT LKTPSKPRFV AGVLGPTNRT CSISPDVNDP SFRNVTFDQL VEAYSESTRA LIAGGVDLIL VETIFDTLNA KACTFAVETV FDEDGVVLPI MISGTITDAS GRTLSGQTTE AFYNSLRHVK PISFGLNCAL GPDELRQYVD ELSRISESAV SAHPNAGLPN AFGEYDLSPE DMAEHIEEWA KSGFLNLVGG CCGTTPEHIR LMEQVTRNVK PRQLPDIPVA CRLSGLEPLT ISADTLFVNV GERTNVTGSA RFKRLIKDEL YDEALEVARQ QVEAGAQIID INMDEGMLDA EAAMVRFLNL CATEPEISKV PIMVDSSKWE VLEAGLKCVQ GKPIVNSISM KEGVDKFIAQ AKLIRRYGAA VIVMAFDEEG QADTRERKIE ICTNAYHILV DEVGFPPEDI IFDPNIFAVA TGIDEHNNYA VDFIEAVGDI KRTLPYAMVS GGVSNVSFSF RGNDPIREAI HAVFLYYCFK NGMDMGIVNA GQLAIYDDLT DELRNAVEDV VLNRRDDSTE RLLDIADKYR GSGKVEEDRT LQEWRGWPVE KRLSHALVKG ITEFIVEDTE EARTNASKPL EVIEGPLMAG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA HLEPYINAEK QAGYTNGKIL LATVKGDVHD IGKNIVGVVL QCNNYEIIDL GVMVSCDQIL KVAKEENVDI IGLSGLITPS LDEMVHVAKE MERQGFELPL LIGGATTSKA HTAVKIEENY HAPVVYVSNA SRAVGVCSAL LSDELRPAFI ERLDKEYITV REQHARKKPR TAPVTLEQAR ENKVAIDWDS YIPPVPAKSG IHVFTDFPIS KIRKYIDWTP FFMTWSLSGK YPTILRHEVV GEEAQRLFDD ANVLLDEIER TGMIKANGVC GLFPANNIGD DIEVYTDETR SEVMTVLCGL RQQTKKPKGP NYCLSDYIAP KESNKADWIG AFAVTGGIGE YDIAEQFKAK GDDYNAIMIQ AIADRLAEAF AECMHETVRK EIWGYAPEES LANEDLIREK YQGIRPAPGY PACPEHTEKG TIWSLLDAEA NTGMVLTESY AMWPGAAVSG WYFSHPESRY FAVAQIQEDQ RDSYADRKGW DLIEAEKWLG PNL // ID Q1Z9M7_PHOPR Unreviewed; 295 AA. AC Q1Z9M7; DT 02-MAY-2006, integrated into UniProtKB/TrEMBL. DT 02-MAY-2006, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:EAS45815.1}; GN ORFNames=P3TCK_05541 {ECO:0000313|EMBL:EAS45815.1}; OS Photobacterium profundum 3TCK. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Photobacterium. OX NCBI_TaxID=314280 {ECO:0000313|EMBL:EAS45815.1}; RN [1] {ECO:0000313|EMBL:EAS45815.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=3TCK {ECO:0000313|EMBL:EAS45815.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAS45815.1}. 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; AAPH01000001; EAS45815.1; -; Genomic_DNA. DR RefSeq; WP_006229121.1; NZ_CH724134.1. DR ProteinModelPortal; Q1Z9M7; -. DR EnsemblBacteria; EAS45815; EAS45815; P3TCK_05541. DR PATRIC; 30913289; VBIPhoPro77067_1291. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:EAS45815.1}; KW Transferase {ECO:0000313|EMBL:EAS45815.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 203 203 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 278 278 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 279 279 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 295 AA; 32586 MW; B795002FE1C75F5E CRC64; MKRLTILDGG MGRELQDIGA PFSQPLWSAQ ALIESPEYVR KAHQNFIDAG SEIIIVNSYA CVPFHLGEER YKTDGAKLAR QAAIIAESVA LNNNSVRVAG AIPPPFGSYR PDLFYADEAK KIITTLIKAQ EPHVDLWIAE TISSLQELEV IHSVLKNSTK DSYYSFSLND SGRNEAKLRS GQPVKMATAI VCLAGAKGIF FNCSVPEVME QAIKDAKEVI EQYGTDVEIG VYANNFMPIK TDHEANDTLQ SMRKLSPEDY LVYAKRWYEL GASTIGGCCG ISPSHIKALA EWKKH // ID Q1ZNV8_PHOAS Unreviewed; 1222 AA. AC Q1ZNV8; DT 02-MAY-2006, integrated into UniProtKB/TrEMBL. DT 02-MAY-2006, sequence version 1. DT 27-MAY-2015, entry version 52. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:EAS63621.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EAS63621.1}; GN Name=metH {ECO:0000313|EMBL:EAS63621.1}; GN ORFNames=VAS14_19426 {ECO:0000313|EMBL:EAS63621.1}; 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 {ECO:0000313|EMBL:EAS63621.1}; RN [1] {ECO:0000313|EMBL:EAS63621.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=S14 {ECO:0000313|EMBL:EAS63621.1}; RA Caviccholi R., Kjelleberg S., McDougald D., Egan S., Saunders N., RA Thomas T., 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. RN [2] {ECO:0000313|EMBL:EAS63621.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S14 {ECO:0000313|EMBL:EAS63621.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EAS63621.1}. 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; AAOJ01000005; EAS63621.1; -; Genomic_DNA. DR RefSeq; WP_005371021.1; NZ_CH902602.1. DR ProteinModelPortal; Q1ZNV8; -. DR SMR; Q1ZNV8; 651-1222. DR EnsemblBacteria; EAS63621; EAS63621; VAS14_19426. DR PATRIC; 31351763; VBIPhoAng36222_3511. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EAS63621.1}; KW Transferase {ECO:0000313|EMBL:EAS63621.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1222 AA; 135463 MW; 71B526447C971FC7 CRC64; MLNSKELLHK RLEEQILIID GGMGTMIQGY KLEEDDYRGQ RFADWHSDLK GNNDLLVLTQ PQLIKDIHLA YLEAGADILE TNTFNATTIA MADYDMESLS AEINYEAARL ARLAADEWTA KTPEKPRFVA GVLGPTNRTC SISPDVNDPG YRNVTFDELV EAYSESTHAL IRGGADIILL ETIFDTLNAK ACAFAVSGVF EELGFELPVM ISGTITDASG RTLSGQTTEA FYNSLRHVKP ISFGLNCALG PDELRQYVEE LSRISECAVS AHPNAGLPNA FGEYDLEAEE MAEHIHEWAQ SGFLNMVGGC CGTTPEHIRQ MYEATKNIKP RQLPDIPIAC RLSGLEPLTI DAETLFINVG ERTNVTGSAR FKRLIKEELY DEALEVARQQ VEAGAQIIDI NMDEGMLDAK AAMIRFLNLC ATEPEISKVP IMVDSSKWEV LEAGLKCVQG KPVVNSISLK EGKENFITQA KLLRRYGAAI IVMAFDEVGQ ADTRERKIEI CTNAYRLLVD EVGFPPEDII FDPNIFAVAT GIEEHNNYAV DFIEAVGDIK RTLPYAMVSG GVSNVSFSFR GNNAVREAIH AVFLYYCFKN GMDMGIVNAG QLAIYDDLPG ELRDAVEDVV LNRRDDSTER LLDIAAKYRD SGNAEEDRSA AEWRGWPVEK RLEHALVKGI TEFIVEDTEE SRQKASKPLE VIEGPLMAGM NVVGDLFGEG KMFLPQVVKS ARVMKQAVAY LEPYIDAEKK AGQTNGKILL ATVKGDVHDI GKNIVGVVLQ CNNYEIIDLG VMVSCDKILK VAKEENVDII GLSGLITPSL DEMVHVAKEM ERQGFDIPLL IGGATTSKAH TAVKIEQNYN QPVVYVSNAS RAVGVCSALL SDEQKPAFVE RLSQEYDVVR EQHARKKPRT APISLEEARA NAVDIDWQNY TPPVPKKAGV HTFTDFPVAE IRKYIDWTPF FMTWSLSGKY PTILRHEVVG EEATKLFNDA NKILDEIEKT GMIKANGVCG LFPANNVGDD IEVYTDDSRT VVLKVLHGLR QQTQKPKGPN YCLSDYIAPK ESGKADWIGA FAVTGGIGEY DIAEQFKAKG DDYNAIMVQA VADRLAEAFA ECMHEMVRKD IWGYAADENL NNDDLIREKY QGIRPAPGYA ACPEHTEKGA IWQLLDAEKN TGMVLTESYA MWPGAAVSGW YFSHPDSRYF AVAQIQKDQL ESYADRKGWD LIEAEKWLGP NL // ID Q1ZUZ2_PHOAS Unreviewed; 244 AA. AC Q1ZUZ2; DT 02-MAY-2006, integrated into UniProtKB/TrEMBL. DT 02-MAY-2006, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EAS66268.1}; GN ORFNames=VAS14_13164 {ECO:0000313|EMBL:EAS66268.1}; 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 {ECO:0000313|EMBL:EAS66268.1}; RN [1] {ECO:0000313|EMBL:EAS66268.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=S14 {ECO:0000313|EMBL:EAS66268.1}; RA Caviccholi R., Kjelleberg S., McDougald D., Egan S., Saunders N., RA Thomas T., 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. RN [2] {ECO:0000313|EMBL:EAS66268.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S14 {ECO:0000313|EMBL:EAS66268.1}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAS66268.1}. 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; AAOJ01000001; EAS66268.1; -; Genomic_DNA. DR RefSeq; WP_005365680.1; NZ_CH902599.1. DR EnsemblBacteria; EAS66268; EAS66268; VAS14_13164. DR PATRIC; 31346460; VBIPhoAng36222_0933. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EAS66268.1}; KW Transferase {ECO:0000313|EMBL:EAS66268.1}. SQ SEQUENCE 244 AA; 26941 MW; 1FCFCFF09B58298D CRC64; MVNLTILDGG MGRELKRIGA PFSQPLWSAQ ALIESPQHVT QAHQGFIDAG AQIITVNSYA CVPFHLGEEL YAEQGRELAE KAAKIARDVV TASQKQVLVA GAIPPIFGSY RPDLFEEMSA YDITESLFEA QQPHVDIWLA ETVASLGELR VITKVLSKTD TPVYISFTLE DEIGEVSRLR SGELVTDAVE ALLDTKATGI FFNCSIPEVI EQAIEDVNQV LERTGKTLRE DVNYWCLREQ LCAN // ID Q20HV9_RHIRD Unreviewed; 316 AA. AC Q20HV9; DT 18-APR-2006, integrated into UniProtKB/TrEMBL. DT 18-APR-2006, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=Msh {ECO:0000313|EMBL:ABB59520.1}; OS Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium OS radiobacter). OG Plasmid Ti {ECO:0000313|EMBL:ABB59520.1}. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium; OC Agrobacterium tumefaciens complex. OX NCBI_TaxID=358 {ECO:0000313|EMBL:ABB59520.1}; RN [1] {ECO:0000313|EMBL:ABB59520.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=K588 {ECO:0000313|EMBL:ABB59520.1}; RC PLASMID=Ti {ECO:0000313|EMBL:ABB59520.1}; RX PubMed=16547030; DOI=10.1128/JB.188.7.2435-2445.2006; RA Wang C., Zhang H.B., Chen G., Chen L., Zhang L.H.; RT "Dual control of quorum sensing by two TraM-type antiactivators in RT Agrobacterium tumefaciens octopine strain A6."; RL J. Bacteriol. 188:2435-2445(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; DQ195264; ABB59520.1; -; Genomic_DNA. DR RefSeq; WP_032491619.1; NG_036172.1. DR RefSeq; YP_009080385.1; NG_036172.1. DR ProteinModelPortal; Q20HV9; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Plasmid {ECO:0000313|EMBL:ABB59520.1}. SQ SEQUENCE 316 AA; 33696 MW; DEF6A5B3240BCF0A CRC64; MSSKVTILDG GMGRELLRNG APFRQPEWSA LSLIEAPEFV KMAHDAFVAA GAEVITTNSY ALVPFHIGDQ ALPHMGLLSP IYPAARSCRR AEGTTVCTGC RLSAPRLRLL PARFVRCRQG ACHSRYPRQS PKLLTSISGS PRPRAPSRRS KQIRNDIGLR LRGPAVGFLY ARRTTKSVAD VICLVSVPTL VSGEAVAQRR SQSSAACAGA LLFNCSQAEI MEAGVKSANQ ALKADNLDIP IGVYANAFVP KPETEESLAA NDGLSGLRDD LNPSGYLQFA QRWVSAGATI IGGCCGIGPE HIAELKDTFD PQPAAA // ID Q210B6_RHOPB Unreviewed; 1286 AA. AC Q210B6; DT 18-APR-2006, integrated into UniProtKB/TrEMBL. DT 18-APR-2006, sequence version 1. DT 27-MAY-2015, entry version 70. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABD89270.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABD89270.1}; GN OrderedLocusNames=RPC_3735 {ECO:0000313|EMBL:ABD89270.1}; OS Rhodopseudomonas palustris (strain BisB18). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Rhodopseudomonas. OX NCBI_TaxID=316056 {ECO:0000313|EMBL:ABD89270.1, ECO:0000313|Proteomes:UP000001948}; RN [1] {ECO:0000313|EMBL:ABD89270.1, ECO:0000313|Proteomes:UP000001948} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BisB18 {ECO:0000313|EMBL:ABD89270.1, RC ECO:0000313|Proteomes:UP000001948}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000301; ABD89270.1; -; Genomic_DNA. DR RefSeq; WP_011474152.1; NC_007925.1. DR RefSeq; YP_533589.1; NC_007925.1. DR ProteinModelPortal; Q210B6; -. DR SMR; Q210B6; 655-908. DR STRING; 316056.RPC_3735; -. DR EnsemblBacteria; ABD89270; ABD89270; RPC_3735. DR KEGG; rpc:RPC_3735; -. DR PATRIC; 23272292; VBIRhoPal29154_3824. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; RPAL316056:GH3E-3787-MONOMER; -. DR Proteomes; UP000001948; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001948}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABD89270.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001948}; KW Transferase {ECO:0000313|EMBL:ABD89270.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 770 770 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1286 AA; 139541 MW; BD74B841BAE3B568 CRC64; MTTPISAKRT ALLALARERI LVLDGAMGTM IQQLQFDEAA FRGARYHNFH RDLRGNNDLL ILTQPQAIEN IHAQYLRAGA DIVATNTFSS TSIAQADYDL SDIAYEMSRE GARLARNAAT LVEAEDGKPR FVAGSIGPTN RTASISPDVG NPGYRAVTFD DLRLAYAEQI NGLLDGGADL LLVETIFDTL NAKAALYAIA EIAEARGIDV PVMISGTITD KSGRLLSGQM PEAFWNSVRH AGPITIGFNC ALGAEDMRGH IADIGRVADT LICAYPNAGL PNEFGQYDET PEYMARLVGE FARDGLVNIV GGCCGTTPDH IAAIAQAVAP YKPRIVPTIE PRLRLSGLEP FELTADIPFV NVGERTNVTG SAKFRKLITA GDYDAALQVA RDQVENGAQI IDVNMDEGLL DSEAAMVTFL NLVAAEPDIA RVPVMVDSSK FAVIEAGLKC LQGKPVVNSI SMKEGEAKFI HEAQIARRHG AAVVVMAFDE QGQADTYARK TAICKRAYDI LVGQLNFPPE DIIFDPNVFA IATGLEEHNN YGVDFIEATR WIRQNLPHAH ISGGVSNLSF SFRGNEPVRE AMHSVFLYHA IKAGMDMGIV NAGQMIVYDD IDPELRQVCE DVILNRDPGA SERLLQLAEK YRGKEKQTKE QDLAWRDWPV EKRLSHALVH GITEYIEADT EAARLTVARP LHVIEGPLMA GMNVVGDLFG DGKMFLPQVV KSARVMKQAV AYLMPFMEKE KADNLAAGIA GDGRKNAGKI VIATVKGDVH DIGKNIVAIV LQCNNFEVID LGVMVPAAKI IEAAKREGAD IIGLSGLITP SLDEMSFLAS EMQRNGLTIP LLIGGATTSR VHTAVKIDAN YPDGAVVHVH DASRAVGVAS SLLAPDRRDA YAAEIRAEYQ KISAAHARAQ ADKKRLKLSD ARGNAVKLDW TKAKPAKPSF LGVKSFSNYP LAELVDYIDW TPFFQAWELA GRYPAILDDA VVGDAARALY ADARAMLQRI VAENWFTAKA AIGFWPANAV GDDIIVYADD TRQSSITTLH TLRQQLEKRE GRFNAALADF VAPTASGVAD YIGAFVVTAG IGEDVIADKF KTANDDYSSI LCKALADRLA EAFAERMHQR VRAELWGTSP DEALTPNDLI AEKYRGIRPA PGYPAQPDHT EKATLFALLD AEVNAGVTLT ESFAMWPGSS VSGLYFGHPE SFYFGVGKIE RDQVQDYAVR KGWSVAEAER WLAPVLNYIP ERAATPPLAP SQAPEVATDV ADVASHPLGC GCAFHLRYRD KAARAS // ID Q21J59_SACD2 Unreviewed; 1233 AA. AC Q21J59; DT 18-APR-2006, integrated into UniProtKB/TrEMBL. DT 18-APR-2006, sequence version 1. DT 27-MAY-2015, entry version 73. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABD81270.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABD81270.1}; GN OrderedLocusNames=Sde_2010 {ECO:0000313|EMBL:ABD81270.1}; OS Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Saccharophagus. OX NCBI_TaxID=203122 {ECO:0000313|EMBL:ABD81270.1, ECO:0000313|Proteomes:UP000001947}; RN [1] {ECO:0000313|EMBL:ABD81270.1, ECO:0000313|Proteomes:UP000001947} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2-40 / ATCC 43961 / DSM 17024 RC {ECO:0000313|Proteomes:UP000001947}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000282; ABD81270.1; -; Genomic_DNA. DR RefSeq; WP_011468488.1; NC_007912.1. DR RefSeq; YP_527482.1; NC_007912.1. DR ProteinModelPortal; Q21J59; -. DR SMR; Q21J59; 657-896. DR STRING; 203122.Sde_2010; -. DR EnsemblBacteria; ABD81270; ABD81270; Sde_2010. DR KEGG; sde:Sde_2010; -. DR PATRIC; 23402986; VBISacDeg56404_2168. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SDEG203122:GI2M-2045-MONOMER; -. DR Proteomes; UP000001947; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001947}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABD81270.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001947}; KW Transferase {ECO:0000313|EMBL:ABD81270.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 251 251 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 315 315 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 763 763 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1233 AA; 135700 MW; 118EC981C0E8AEEC CRC64; MNPQLKQRID SLYAALEERI LILDGAMGTM IQSYKLQEAD YRGERFANHH QDLGGNNDLL ALTQPVILRD IHRAYLDAGA DILETNTFNS TQISQADYDT QEIAYELNKE SAAIARAVAD EVTLETPNKP RFVAGVLGPT SRTCSISPDV NDPGARNVTY DELVTNYKEA TLGLIEGGAD IILIETIFDT LNAKAAVFAV KTVFEDIGYE LPIMISGTIT DASGRTLSGQ TTEAFYNSLA HAKPLSIGLN CALGAAELEP YVRELSRVSN CYVSAHPNAG LPNEFGEYDQ SAKEMADVVE KFAVKNYVNI IGGCCGTTPQ HIKAIAETVS KYPARKIPDI EPQCRLAGLE PFNISKDSLF VNVGERCNIT GSARFKRLIL EGDYTTAIEV ALQQVTDGAQ IIDINMDEGM LDAEAAMIKF LNLLAGEPDI ARVPIMVDSS KWDVIVAGLK CIQGKPIVNS ISLKEGEAEF IERARLCKLY GAAVIVMAFD EDGQADTAQR KIEICERSYK VLTEQAGFPP EDIIFDPNIF AVATGIEEHN NYAVDFIEAT RWIRQNLPYA GVSGGVSNVS FSFRGNDPVR EAIHSVFLYY AIQAGMNMGI VNAGQLAIYD DLPKELKDCV EDVILNKNDN GTEALLEIAE QYRGDGKAQA SKEDLAWREL PVEKRLEHSL VKGISAYIEA DTEEARQNAS KPIDVIEGPL MAGMNVVGDL FGSGKMFLPQ VVKSARVMKQ SVAYLQPFIE AEKTEGARSN GKILMATVKG DVHDIGKNIV GVVLQCNNFD VVDLGVMVPC EKIIDTAIAE NCDMIGLSGL ITPSLDEMVN VAREMQSRQV NLPLLIGGAT TSKAHTAVKI DPQFSLNQAV YVADASRAVG VASKLLSLDQ RGPFIASIKE EYEAVRERRA NRTSNKQLAT YADAVNKKLQ LDWNKFTPAV PAFTGTKVFE NYPLEKLVEY IDWTPFFISW DLVGKYPKIF KDEVIGEAAT QLFKDAQEIL KKLIDEKLIQ ASATIGFWRA NTIGDDDINV MDDNGKTLAE LHHIRQQQIK NGADDVLMSL ADFVAPQDTG LNDYIGGFVV TAGHGVDELA KEYEAKGDDY NAIMVKALAD RLAEAFAEHL HQRVRKEFWG YDQDENLANE DLIREKYQGI RPAPGYPACP DHTEKRALFD LLDAEATTGV QLTEHYAMYP TAAVSGWYFA HPKAKYFNTG KIAKDQVESL ASRKGLSTAE MEKWLQSVLD YDI // ID Q221U1_RHOFT Unreviewed; 348 AA. AC Q221U1; DT 18-APR-2006, integrated into UniProtKB/TrEMBL. DT 18-APR-2006, sequence version 1. DT 27-MAY-2015, entry version 59. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABD68212.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABD68212.1}; GN OrderedLocusNames=Rfer_0460 {ECO:0000313|EMBL:ABD68212.1}; OS Rhodoferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118) OS (Albidiferax ferrireducens). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Rhodoferax. OX NCBI_TaxID=338969 {ECO:0000313|EMBL:ABD68212.1, ECO:0000313|Proteomes:UP000008332}; RN [1] {ECO:0000313|Proteomes:UP000008332} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-621 / DSM 15236 / T118 RC {ECO:0000313|Proteomes:UP000008332}; 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; ABD68212.1; -; Genomic_DNA. DR RefSeq; WP_011462785.1; NC_007908.1. DR RefSeq; YP_521743.1; NC_007908.1. DR ProteinModelPortal; Q221U1; -. DR STRING; 338969.Rfer_0460; -. DR EnsemblBacteria; ABD68212; ABD68212; Rfer_0460. DR KEGG; rfr:Rfer_0460; -. DR PATRIC; 23233409; VBIRhoFer131161_0730. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; AFER338969:GHU9-462-MONOMER; -. DR Proteomes; UP000008332; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008332}; KW Methyltransferase {ECO:0000313|EMBL:ABD68212.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008332}; KW Transferase {ECO:0000313|EMBL:ABD68212.1}. SQ SEQUENCE 348 AA; 37561 MW; 36F321EAEB9CDA70 CRC64; MKALHYTRGQ KLPEILQHRI MVLDGAMGTM IQRFKLGEAQ YRGERFKDFH KDVKGNNELL SLTRPDVITD IHERYLAAGA DMIETNTFGA TRVAQADYDM ADLAFEMNLA SAKLARAACD KFSTPDKPRF VLGALGPTPK TASISPDVND PGARNVTFEQ LRAAYYEQVE ALVQGGADAL LVETIFDTLN AKAALFAIDE FFEASGQQLP IIISGTVTDA SGRILSGQTV TAFWHSVRHA QPLAVGLNCA LGAALMRPYI QELAKAAPDT FISCYPNAGL PNPMSDTGFD ETPADTSRLI GEFAAEGLVN IVGGCCGTTP EHIGAIHDKV APLAGRVLQR NVFYPEAA // ID Q22HI1_TETTS Unreviewed; 302 AA. AC Q22HI1; DT 18-APR-2006, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 2. DT 07-JAN-2015, entry version 47. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EAR84720.2}; GN ORFNames=TTHERM_00637220 {ECO:0000313|EMBL:EAR84720.2}; OS Tetrahymena thermophila (strain SB210). OC Eukaryota; Alveolata; Ciliophora; Intramacronucleata; OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae; OC Tetrahymena. OX NCBI_TaxID=312017 {ECO:0000313|EMBL:EAR84720.2, ECO:0000313|Proteomes:UP000009168}; RN [1] {ECO:0000313|Proteomes:UP000009168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SB210 {ECO:0000313|Proteomes:UP000009168}; RX PubMed=16933976; DOI=10.1371/journal.pbio.0040286; RA Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R., RA Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L., RA Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M., RA Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., RA Sun L., Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., RA Wang Y., Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., RA Weinberg Z., Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., RA Gorovsky M.A., Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., RA Stover N.A., Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., RA Barbeau R.A., Hamilton E.P., Orias E.; RT "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, RT a model eukaryote."; RL PLoS Biol. 4:1620-1642(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; GG662588; EAR84720.2; -; Genomic_DNA. DR STRING; 5911.XP_001032383; -. DR EnsemblProtists; EAR84720; EAR84720; TTHERM_00637220. DR Proteomes; UP000009168; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009168}; KW Methyltransferase {ECO:0000313|EMBL:EAR84720.2}; KW Reference proteome {ECO:0000313|Proteomes:UP000009168}; KW Transferase {ECO:0000313|EMBL:EAR84720.2}. SQ SEQUENCE 302 AA; 35433 MW; 969D27B7915186BA CRC64; MKNQHKIKIL DGAVGSLLQQ KYPEFYEQRT WMNRILKEKP EKLYDLHLEY CKQGADIITS FTFKTNPIAC QSLEESKKLV QIAVKECQKL KEIYKDIQIF GSNSPAEDCY QKERTLTKDE LIYNHKNHIQ FLYDCQVDCI FNETMSQLDE LIIVCQICQD MNIPYIISIY FDNNLKILSG ESVDDCVDTL LNKYKFKPIC LSFNCVQKKD LLNLFLQSKK IFQQKSSKNI NSENIKYGFY INCGGEDYTC NDFNYQIQPE ELPIFYQQLI DLDIIEKQDI LFLGSCCMST PGHTLQLSKF FK // ID Q24NX1_DESHY Unreviewed; 291 AA. AC Q24NX1; DT 18-APR-2006, integrated into UniProtKB/TrEMBL. DT 18-APR-2006, sequence version 1. DT 27-MAY-2015, entry version 55. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:BAE86271.1}; GN OrderedLocusNames=DSY4482 {ECO:0000313|EMBL:BAE86271.1}; OS Desulfitobacterium hafniense (strain Y51). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfitobacterium. OX NCBI_TaxID=138119 {ECO:0000313|Proteomes:UP000001946}; RN [1] {ECO:0000313|EMBL:BAE86271.1, ECO:0000313|Proteomes:UP000001946} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Y51 {ECO:0000313|Proteomes:UP000001946}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; BAE86271.1; -; Genomic_DNA. DR RefSeq; WP_011461860.1; NC_007907.1. DR RefSeq; YP_520715.1; NC_007907.1. DR ProteinModelPortal; Q24NX1; -. DR STRING; 138119.DSY4482; -. DR EnsemblBacteria; BAE86271; BAE86271; DSY4482. DR KEGG; dsy:DSY4482; -. DR PATRIC; 21678142; VBIDesHaf65307_5000. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265278; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; DHAF138119:GHT5-4556-MONOMER; -. DR Proteomes; UP000001946; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001946}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000001946}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 206 206 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 271 271 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 272 272 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 291 AA; 31428 MW; 1A81643D3AF3A0CA CRC64; MPGGFYMILD KDSYVIFDGA MGTMLQKYDL APGQPPEVLN ITRPEVIEEV HRKYIKAGSN IITTNTFGAI ETKLNGTGYS VEEVVQSAIA IARRAAGKNL VALDVGPTGE LIEPLGDLSF EEVYDLYACQ IKAAALTGNV DLVLIETFFD LTEAHAAIRA AKDHSSLPVI CTFTFQQKGR TLMGKDIKTV VASLEEYGVD AVGVNCSLGP GEMLSIVETM VSSTQLPILV QPNAGLPKLI GDRTVYDVEP EEFARYIQVM ANLGVKWFGG CCGTTPEFIS AIKESLGLKH N // ID Q28L24_JANSC Unreviewed; 316 AA. AC Q28L24; DT 04-APR-2006, integrated into UniProtKB/TrEMBL. DT 04-APR-2006, sequence version 1. DT 27-MAY-2015, entry version 52. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABD56588.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ABD56588.1}; GN OrderedLocusNames=Jann_3671 {ECO:0000313|EMBL:ABD56588.1}; OS Jannaschia sp. (strain CCS1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Jannaschia. OX NCBI_TaxID=290400 {ECO:0000313|EMBL:ABD56588.1, ECO:0000313|Proteomes:UP000008326}; RN [1] {ECO:0000313|Proteomes:UP000008326} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCS1 {ECO:0000313|Proteomes:UP000008326}; 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; ABD56588.1; -; Genomic_DNA. DR RefSeq; WP_011456788.1; NC_007802.1. DR RefSeq; YP_511613.1; NC_007802.1. DR ProteinModelPortal; Q28L24; -. DR STRING; 290400.Jann_3671; -. DR DNASU; 3936150; -. DR EnsemblBacteria; ABD56588; ABD56588; Jann_3671. DR KEGG; jan:Jann_3671; -. DR PATRIC; 22151252; VBIJanSp43325_3870. DR eggNOG; COG2040; -. DR HOGENOM; HOG000179103; -. DR KO; K00547; -. DR OMA; CCGTDHR; -. DR OrthoDB; EOG6R5C46; -. DR BioCyc; JSP290400:GI1R-3714-MONOMER; -. DR Proteomes; UP000008326; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008326}; KW Methyltransferase {ECO:0000313|EMBL:ABD56588.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008326}; KW Transferase {ECO:0000313|EMBL:ABD56588.1}. SQ SEQUENCE 316 AA; 33934 MW; 509C7C30F38CA5FC CRC64; MTRFRSTLPQ VNGTTLLTDS GLETTLIFHD GLDLPCFAAY PLMETAEGRA VLRDYFQRHL AIASERSAGF LLESPTWRAS RDWGAQLGHG PDDLARLNND AIAMLVDLRD DATGVGPIVI SGNIGPRGDG YVADAAMTAD EAEDYHAEQI GWFAQSEVDL ATAVTLSTVA EGVGVIRAAH RVDLPVVVSF TTETDGRLPD GTPLGRAIEQ TDALTDGAAA YFMVNCAHPD HFRPVLDTGT AWLNRIGGVR ANASRMSHAE LDEAETLDAG DPAELGRDYR DLRQILPNLT VIGGCCGTDH RHIEAMADRC LGHNAA // ID Q28P98_JANSC Unreviewed; 340 AA. AC Q28P98; DT 04-APR-2006, integrated into UniProtKB/TrEMBL. DT 04-APR-2006, sequence version 1. DT 27-MAY-2015, entry version 55. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABD55464.1}; GN OrderedLocusNames=Jann_2547 {ECO:0000313|EMBL:ABD55464.1}; OS Jannaschia sp. (strain CCS1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Jannaschia. OX NCBI_TaxID=290400 {ECO:0000313|EMBL:ABD55464.1, ECO:0000313|Proteomes:UP000008326}; RN [1] {ECO:0000313|Proteomes:UP000008326} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCS1 {ECO:0000313|Proteomes:UP000008326}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; ABD55464.1; -; Genomic_DNA. DR RefSeq; WP_011455668.1; NC_007802.1. DR RefSeq; YP_510489.1; NC_007802.1. DR ProteinModelPortal; Q28P98; -. DR STRING; 290400.Jann_2547; -. DR EnsemblBacteria; ABD55464; ABD55464; Jann_2547. DR KEGG; jan:Jann_2547; -. DR PATRIC; 22148898; VBIJanSp43325_2706. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265278; -. DR KO; K00548; -. DR OMA; DHAPLAY; -. DR OrthoDB; EOG693GKH; -. DR BioCyc; JSP290400:GI1R-2574-MONOMER; -. DR Proteomes; UP000008326; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008326}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ABD55464.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008326}; KW Transferase {ECO:0000313|EMBL:ABD55464.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 212 212 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 278 278 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 279 279 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 340 AA; 35720 MW; 46E612B3CB5A45A0 CRC64; MTNALSRMLS TRDWLLADGA TGTTLFNMGL QSGDAPELWN VDHPDRITQL YKGAVDAGSD LFLTNSFGGT AARLKLHDAQ TRVFELNKAA AEIGREVADS AGHDVIVAGS VGPTGEIMVP MGALTHALAV EMFHEQAEGL KAGGADVLWA ETISAPDEYK AASEAAKLAE MPWCGTMSFD TAGRTMMGLT SAAMSSMVEK LDHAPLAYGA NCGVGASDLL RTILGFRASG SERPVIAKGN AGIPKYVDGH IHYDGTPELM ARYAVLARDC GATIIGGCCG TTPEHLEKMR AALETVPRGN APSLEQIAKE LGGFSSGVDG TEEGGGGPTR ERRGRRRVRN // ID Q28RZ7_JANSC Unreviewed; 297 AA. AC Q28RZ7; DT 04-APR-2006, integrated into UniProtKB/TrEMBL. DT 04-APR-2006, sequence version 1. DT 27-MAY-2015, entry version 51. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABD54515.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ABD54515.1}; GN OrderedLocusNames=Jann_1598 {ECO:0000313|EMBL:ABD54515.1}; OS Jannaschia sp. (strain CCS1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Jannaschia. OX NCBI_TaxID=290400 {ECO:0000313|EMBL:ABD54515.1, ECO:0000313|Proteomes:UP000008326}; RN [1] {ECO:0000313|Proteomes:UP000008326} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCS1 {ECO:0000313|Proteomes:UP000008326}; 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; ABD54515.1; -; Genomic_DNA. DR RefSeq; WP_011454720.1; NC_007802.1. DR RefSeq; YP_509540.1; NC_007802.1. DR ProteinModelPortal; Q28RZ7; -. DR STRING; 290400.Jann_1598; -. DR EnsemblBacteria; ABD54515; ABD54515; Jann_1598. DR KEGG; jan:Jann_1598; -. DR PATRIC; 22146904; VBIJanSp43325_1722. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; QPEVMAA; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; JSP290400:GI1R-1610-MONOMER; -. DR Proteomes; UP000008326; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008326}; KW Methyltransferase {ECO:0000313|EMBL:ABD54515.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008326}; KW Transferase {ECO:0000313|EMBL:ABD54515.1}. SQ SEQUENCE 297 AA; 30857 MW; A899B0E122E21167 CRC64; MTEITILDGG MGQELVSRSD VPPTPLWSTD VMRAKPHLVG EVHRDFFNAG AQIATANTYA IHRDRLVRAD AEAEFASLHK TALDQARQAR DAHGSGLVAG AIGPLGASYR PDLTPQHSAA VALYAEIATL HAPLVDLLIC ETITSLAQAE AVLDACLGHG VPVWLAFSVD DRDGTRLRSG EGLGDVIAMA GEAAALLANC SVPEVMPAAL DILGRAGTPF GAYANGFTEI SAGFLDDAPT VDALTSRTDM GPEAYADHVM GWIDQGATIV GGCCEVGPAH IAEITRRVTA LGGKGPS // ID Q28UF5_JANSC Unreviewed; 311 AA. AC Q28UF5; DT 04-APR-2006, integrated into UniProtKB/TrEMBL. DT 04-APR-2006, sequence version 1. DT 27-MAY-2015, entry version 47. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABD53657.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ABD53657.1}; GN OrderedLocusNames=Jann_0740 {ECO:0000313|EMBL:ABD53657.1}; OS Jannaschia sp. (strain CCS1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Jannaschia. OX NCBI_TaxID=290400 {ECO:0000313|EMBL:ABD53657.1, ECO:0000313|Proteomes:UP000008326}; RN [1] {ECO:0000313|Proteomes:UP000008326} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCS1 {ECO:0000313|Proteomes:UP000008326}; 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; ABD53657.1; -; Genomic_DNA. DR RefSeq; WP_011453865.1; NC_007802.1. DR RefSeq; YP_508682.1; NC_007802.1. DR ProteinModelPortal; Q28UF5; -. DR STRING; 290400.Jann_0740; -. DR EnsemblBacteria; ABD53657; ABD53657; Jann_0740. DR KEGG; jan:Jann_0740; -. DR PATRIC; 22145118; VBIJanSp43325_0832. DR eggNOG; COG2040; -. DR HOGENOM; HOG000179103; -. DR OrthoDB; EOG6R5C46; -. DR BioCyc; JSP290400:GI1R-747-MONOMER; -. DR Proteomes; UP000008326; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008326}; KW Methyltransferase {ECO:0000313|EMBL:ABD53657.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008326}; KW Transferase {ECO:0000313|EMBL:ABD53657.1}. SQ SEQUENCE 311 AA; 33380 MW; A53730890F4ABED1 CRC64; MTREQPGDFA PTPDLFAAYL GMETDLIFTH GMDLPGFASF PMVETQEGRD LLQSYYINMI QLGRRSGLGV ILESATWVAN RDRSAPLGYG PDQLAEINRA AVAEMVKAKM ATAEVPIRLS LNLGPRADAD APSEQMSAAE AEAYHTEQIA AVAKSGIDMV SGYTLTYTAE AVGVARAAKA QGVPAVIAFK VELDGRLPTG MTLEDAIAEV DAQTEAYPDY HMINCAHPDH FSATLDGGPW MDRIGGIVAN ASRCSHEQLD NATELDGGNP EELGHVLADL RRRFPRIRVL GGCCGTNMRH MEAIAQAASA Q // ID Q29LT6_DROPS Unreviewed; 331 AA. AC Q29LT6; DT 04-APR-2006, integrated into UniProtKB/TrEMBL. DT 04-APR-2006, sequence version 1. DT 27-MAY-2015, entry version 47. DE SubName: Full=GA10443 {ECO:0000313|EMBL:EAL33959.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EAL33959.1}; GN Name=Dpse\GA10443 {ECO:0000313|EMBL:EAL33959.1}; GN ORFNames=Dpse_GA10443 {ECO:0000313|EMBL:EAL33959.1}, GN GA10443 {ECO:0000313|FlyBase:FBgn0070500}; OS Drosophila pseudoobscura pseudoobscura (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=46245 {ECO:0000313|EMBL:EAL33959.1, ECO:0000313|Proteomes:UP000001819}; RN [1] {ECO:0000313|EMBL:EAL33959.1, ECO:0000313|Proteomes:UP000001819} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MV2-25 / Tucson 14011-0121.94 RC {ECO:0000313|Proteomes:UP000001819}; RX PubMed=15632085; DOI=10.1101/gr.3059305; RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S., RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., RA Couronne O., Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., RA van Batenburg M.F., Howells S.L., Scherer S.E., Sodergren E., RA Matthews B.B., Crosby M.A., Schroeder A.J., Ortiz-Barrientos D., RA Rives C.M., Metzker M.L., Muzny D.M., Scott G., Steffen D., RA Wheeler D.A., Worley K.C., Havlak P., Durbin K.J., Egan A., Gill R., RA Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y., Waldron L., RA Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F., RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M., RA Weinstock G.M., Gibbs R.A.; RT "Comparative genome sequencing of Drosophila pseudoobscura: RT chromosomal, gene, and cis-element evolution."; RL Genome Res. 15:1-18(2005). RN [2] {ECO:0000313|EMBL:EAL33959.1, ECO:0000313|Proteomes:UP000001819} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MV2-25 {ECO:0000313|EMBL:EAL33959.1}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 genomes consortium; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(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; CH379060; EAL33959.1; -; Genomic_DNA. DR RefSeq; XP_001356893.1; XM_001356857.2. DR ProteinModelPortal; Q29LT6; -. DR STRING; 7237.FBpp0280757; -. DR EnsemblMetazoa; FBtr0282319; FBpp0280757; FBgn0070500. DR GeneID; 4817337; -. DR KEGG; dpo:Dpse_GA10443; -. DR FlyBase; FBgn0070500; Dpse\GA10443. DR InParanoid; Q29LT6; -. DR KO; K00547; -. DR OMA; GEAIRNW; -. DR OrthoDB; EOG7GQXW0; -. DR PhylomeDB; Q29LT6; -. DR Proteomes; UP000001819; Partially assembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001819}; KW Methyltransferase {ECO:0000313|EMBL:EAL33959.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001819}; KW Transferase {ECO:0000313|EMBL:EAL33959.1}. SQ SEQUENCE 331 AA; 36719 MW; 72BFDE1E984E8CA6 CRC64; MGLTRVLVKD GGFGTQMTVH VGNSVDGDPL WSARFNATNP AAIINTHLDF LQNGADIILT NTYQASVEGY MEYLELDEDQ SIELIRNTVR LAHIAKEKYL TECYQAQLAV PEGYPLIIAS IGPFGAHLHD GSEYTGSYAD YVPAKTITDW HRIRIEACLE AGVDALAIET IPCQMEAEAL VEMLCDDYPD VKFWVAFQCK DESTLAHGET FADAANAIWD MLAERNAQDK CLAVGVNCVH PKFVTSLFKS LNGDRSVEDQ IPLVVYPNSG EVYDVVKGWE GREHCVPLAN YVPEWSQLGA KIIGGCCRTY ARDIRHIGEA IRNWNKLKKV A // ID Q29LT7_DROPS Unreviewed; 349 AA. AC Q29LT7; DT 04-APR-2006, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 2. DT 07-JAN-2015, entry version 42. DE SubName: Full=GA10445 {ECO:0000313|EMBL:EAL33958.2}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EAL33958.2}; GN Name=Dpse\GA10445 {ECO:0000313|EMBL:EAL33958.2}; GN ORFNames=Dpse_GA10445 {ECO:0000313|EMBL:EAL33958.2}, GN GA10445 {ECO:0000313|FlyBase:FBgn0070502}; OS Drosophila pseudoobscura pseudoobscura (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=46245 {ECO:0000313|EMBL:EAL33958.2, ECO:0000313|Proteomes:UP000001819}; RN [1] {ECO:0000313|EMBL:EAL33958.2, ECO:0000313|Proteomes:UP000001819} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MV2-25 / Tucson 14011-0121.94 RC {ECO:0000313|Proteomes:UP000001819}; RX PubMed=15632085; DOI=10.1101/gr.3059305; RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S., RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., RA Couronne O., Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., RA van Batenburg M.F., Howells S.L., Scherer S.E., Sodergren E., RA Matthews B.B., Crosby M.A., Schroeder A.J., Ortiz-Barrientos D., RA Rives C.M., Metzker M.L., Muzny D.M., Scott G., Steffen D., RA Wheeler D.A., Worley K.C., Havlak P., Durbin K.J., Egan A., Gill R., RA Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y., Waldron L., RA Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F., RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M., RA Weinstock G.M., Gibbs R.A.; RT "Comparative genome sequencing of Drosophila pseudoobscura: RT chromosomal, gene, and cis-element evolution."; RL Genome Res. 15:1-18(2005). RN [2] {ECO:0000313|EMBL:EAL33958.2, ECO:0000313|Proteomes:UP000001819} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MV2-25 {ECO:0000313|EMBL:EAL33958.2}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 genomes consortium; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(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; CH379060; EAL33958.2; -; Genomic_DNA. DR RefSeq; XP_001356892.2; XM_001356856.2. DR STRING; 7237.FBpp0280756; -. DR EnsemblMetazoa; FBtr0282318; FBpp0280756; FBgn0070502. DR GeneID; 4816950; -. DR KEGG; dpo:Dpse_GA10445; -. DR FlyBase; FBgn0070502; Dpse\GA10445. DR InParanoid; Q29LT7; -. DR OMA; SSVEGFM; -. DR OrthoDB; EOG7GQXW0; -. DR Proteomes; UP000001819; Partially assembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001819}; KW Methyltransferase {ECO:0000313|EMBL:EAL33958.2}; KW Reference proteome {ECO:0000313|Proteomes:UP000001819}; KW Transferase {ECO:0000313|EMBL:EAL33958.2}. SQ SEQUENCE 349 AA; 38684 MW; C1E1804946433AFD CRC64; MYAFEEENEN QNRPEQPRVL VKCGGFSSQL AHNVDEKVDG DPLWGSRFDA TNPQAVIKTH LDFLRSGADI ILTNTYQSSV EGFMKYLALT REQSVALIEK SVHLTQQAKA QYLKEILQSG EIIKPFFPLI LASIGPYGAH LHDGSEYSGS YADKISKEKL QDWHRTRIET CLLAGVDGLA AETLPCQLEA LAITESILEN YTNVKFWVSF QCKDDTSLAD GESFAEAALA VWRMVQAYKA QTRLLGIGVN CVNPTFVTPL LRSLNAAAGL DRIPLVVYSN RGEIYDSVRG EWTGTGEDVA KFVPEWVRLG ARVVGGCCRV YPDDVLKIRK CVDSLNIGYS AESPQSHIV // ID Q2BAQ4_9BACI Unreviewed; 621 AA. AC Q2BAQ4; DT 04-APR-2006, integrated into UniProtKB/TrEMBL. DT 04-APR-2006, sequence version 1. DT 27-MAY-2015, entry version 42. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=B14911_27845 {ECO:0000313|EMBL:EAR66894.1}; OS Bacillus sp. NRRL B-14911. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=313627 {ECO:0000313|EMBL:EAR66894.1}; RN [1] {ECO:0000313|EMBL:EAR66894.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NRRL B-14911 {ECO:0000313|EMBL:EAR66894.1}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAR66894.1}. 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; AAOX01000006; EAR66894.1; -; Genomic_DNA. DR RefSeq; WP_009793772.1; NZ_CH672357.1. DR ProteinModelPortal; Q2BAQ4; -. DR EnsemblBacteria; EAR66894; EAR66894; B14911_27845. DR PATRIC; 36909353; VBIBacSp102338_1861. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:EAR66894.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862, KW ECO:0000313|EMBL:EAR66894.1}; KW Transferase {ECO:0000313|EMBL:EAR66894.1}. SQ SEQUENCE 621 AA; 68788 MW; 7BBB9F343301693C CRC64; MSLLDKMEKE IIIADGAMGT LLYSYGTDFC FEELNVSQPG HIQNIHQAYI DAGATLIQTN TYAANYLKLQ RYGLEDHVKE INSAAVTVAR KAAGNHAFVA GTIGGNRGIK PHSISIEEIK RSFREQLYCL LMEGVDAILL ETYYDLKELE TVLSIARKET ALPLIAQVSL QETGIMQDHT PISEALSRLD ALGADIVGLN CRLGPHHMLL TLEEVPLPQK AYLSAYPNAS LPAYTDGKFH YEGDAEYFRQ SAKAFRNQGV RLLGGCCGTT PAHIRAFSDE LKGSPPLEKK EVREPKAKIR IMPKEAQRDL PPLQDLVKKR QSVIVELDPP RKLETDKFFA GAKALQDAGI DAITLADNSL ASPRISNEAL GYLAKNRLGL RPLIHLTCRD RNIIGLQSHL MGLHTLGLHD ILAITGDPAR VGDFPGASSV YDMSSFELIQ MIKQLNEGRS ISGKDLGQKA AFSVAAAFNP NVRSLEKAVQ RLEKKAECGA DYFITQPVFS EEKLMEIYEA TKHMEQPIYI GLMPLTSSRN ADFLHNEVPG IKISDKIRER MNSLKDDPLQ SVREGISISK ELIDAAAELF NGIYLITPFM KYELTAELAA YARSEKLKTA RRSRNAKDFS I // ID Q2BAQ5_9BACI Unreviewed; 1149 AA. AC Q2BAQ5; DT 04-APR-2006, integrated into UniProtKB/TrEMBL. DT 04-APR-2006, sequence version 1. DT 27-MAY-2015, entry version 51. DE SubName: Full=5-methyltetrahydrofolate--homocysteine S-methyltransferase {ECO:0000313|EMBL:EAR66893.1}; GN ORFNames=B14911_27840 {ECO:0000313|EMBL:EAR66893.1}; OS Bacillus sp. NRRL B-14911. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=313627 {ECO:0000313|EMBL:EAR66893.1}; RN [1] {ECO:0000313|EMBL:EAR66893.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NRRL B-14911 {ECO:0000313|EMBL:EAR66893.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EAR66893.1}. 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; AAOX01000006; EAR66893.1; -; Genomic_DNA. DR RefSeq; WP_009793771.1; NZ_CH672357.1. DR ProteinModelPortal; Q2BAQ5; -. DR EnsemblBacteria; EAR66893; EAR66893; B14911_27840. DR PATRIC; 36909351; VBIBacSp102338_1860. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EAR66893.1}; KW Transferase {ECO:0000313|EMBL:EAR66893.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 724 724 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1149 AA; 126487 MW; 52794CF85EE0FBCF CRC64; MPKISLSERM NNKILIMDGA MGTMLQRADL SAEDFGGEQY DGCNEYLNLT APGVIKEIHL AYLKAGADII ETNTFGATSI VLDEYSLKEK AYEINRTASL IARKAADQIS TPSWPRFVAG SMGPTTKTLS VTGGTTFEEL SLSYEEQACG LIDGKADLLL LETSQDMLNV KAGYIGIQNA FKKTGITLPL IVSGTIEPMG TTLAGQPIEA FYISLEHMKP LAVGLNCATG PEFMQEHIRS LSSLADAAVS CYPNAGLPDE EGRYHETPES LAEKLAGFAS QGWLNIVGGC CGTTPEHIKA IADKMEHFAP RKISAASAHK VSGIEPLIYD DPTLRPIMVG ERTNVIGSRK FRRLIAEGKF EEASEVARAQ VKNGAHVIDI CLADPDRDEL EDMENFIKEV TKKVKAPIVI DSTDEKVIEK ALIYLQGKSV INSINLEDGE ERFEAIAPLI RLYGAAVVVG TIDEKGMGVS ADRKLEIASR SYTLLVEKYG IPPEDIIFDP LVFPVGTGDE QYIGSAEATV EGIRLIKERF PKTQTILGIS NVSFGLPPVG REILNSVFLY HCTQAGLDYA IVNTEKLERF ASIASEEIAL AEKLLFETTD ETLAQFTEFY RGKKKEEKSL LPDMSLAERL AYYIKEGTKE GLLEDLKAAL LEYSSPLEII NGPLMDGMKE VGRLFNDNQL IVAEVLQSAE VMKASVSYLE PFMEKGTSSG KGKIILATVK GDVHDIGKNL VDIILSNNGY EVIDLGIKVS PSELVEAVKK EKPNMVGLSG LLVKSAQQMV ITASDMKQAG IDIPILVGGA ALSRKFTDTK ISREYNGLVM YAKDAMNGLS IADQLRDEPE YNRLLAEQEA KRSLPLPSAL TERKTGALAA LKVRPSVRSD VPVFVPQDLE RHVLRSYTLG HIEPYINRQM LLGHHLGLKG NISRLIESGD EKALKLNDTV DSLIVQAKTE GWIIPSAVYQ FFPAQSDGNK VIIYDKDDHS RILEVFDFPR QQTEPFLCLA DYLKPAGGGE MDYVAFFSVT AGNAVRETAE ILKKEGRFLE NHALQALALE TAEGFAELVH RQIRDRWGFP DPVDFTMKER FSAKYQGQRF SFGYPACPEL EDQRKLFDLI KPEEIGIDLT EGFMMEPEAS VSAMVFAHPE ARYFNVLKN // ID Q2BMJ6_NEPCE Unreviewed; 1234 AA. AC Q2BMJ6; DT 04-APR-2006, integrated into UniProtKB/TrEMBL. DT 04-APR-2006, sequence version 1. DT 01-APR-2015, entry version 59. DE SubName: Full=Cobalamin-dependent methionine synthase {ECO:0000313|EMBL:EAR61801.1}; GN ORFNames=MED92_04362 {ECO:0000313|EMBL:EAR61801.1}; OS Neptuniibacter caesariensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Neptuniibacter. OX NCBI_TaxID=207954 {ECO:0000313|EMBL:EAR61801.1}; RN [1] {ECO:0000313|EMBL:EAR61801.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MED92 {ECO:0000313|EMBL:EAR61801.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EAR61801.1}. 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; AAOW01000006; EAR61801.1; -; Genomic_DNA. DR RefSeq; WP_007022887.1; NZ_CH724127.1. DR EnsemblBacteria; EAR61801; EAR61801; MED92_04362. DR PATRIC; 25475720; VBINepCae91145_3443. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 249 249 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1234 AA; 137321 MW; B4CCF824F0006248 CRC64; MTDKTLTDIL SESLKQRIMI LDGGMGTMIQ DYKLEEADYR GERFADWHIE VKGNNDLLVL TKPEIIKAIH KEYLEAGADI IETNTFNATQ IAMADYEMES LSREINVEAA RLAREACDEI TAQTPDRPRY VAGVLGPTNR TCSISPDVND PSFRNVSFND LVEAYTESID GLVEGGSDII LIETIFDTLN AKAAIYAVET YFDDNDIRLP VMISGTITDA SGRTLSGQTT EAFWNSVRHA KPISVGLNCA LGPKELRQYV EELSRISETF VSTHPNAGLP NAFGGYDETP EQMATEISEW AQSGFLNIIG GCCGTTPAHI KAMREAVENE APRALPQLPV ESRLSGLEPM NIGEDTLFVN VGERTNVTGS AMFKRLIKEQ DYETALDVAR QQVENGAQII DINMDEGMLD AHAAMVKFLN LIASEPDIAR VPIMIDSSKW DVIEAGLQCI QGKGIVNSIS LKEGEDNFIE QAKKLRRYGA AVVVMAFDET GQADTYERKI EICERSYRVL VDQVGYPPED IIFDPNIFAV ATGIEEHNNY AVDFIQATGW IKQNLPYAKV SGGVSNVSFS FRGNNPVREA IHCVFLYHAI KQGMDMGIVN AGQLAIYDDL PEELRLAVED VIQNSRDDAT ERLLDIAEKY RGDGSQEDDT KTQEWRSWDV NKRLEHALVK GITEFIEDDT EEARQNHERP LHVIEGPLMD GMSVVGDLFG AGKMFLPQVV KSARVMKKAV AYLMPFIEEE KDGTSQSNGK IVLATVKGDV HDIGKNIVGV VLQCNNYEII DLGVMVPAET ILRTAREENA DLIGLSGLIT PSLDEMVHMA KEMERQEFNI PLLIGGATTS KAHTAVKIDP AFNRDQVVHV TNASRAVNVA SSLLGGKKAD YVKEIQEEYQ AVRERHAARM NDKRRVTLDA ARENKFQIEW DEYTPPAPLQ PGIHVFDDIS LNDIQEYFDW TPFFHSWELA GRYPRILTDE VIGEEATKLF NDAQAMLKDL VDQKLLTAKA VVGIFPANTI GHDDIELYTD ENRSDVLMQL HHLRQQTEKV AGKANMCLAD FVAPKESGKQ DYLGAFAVTA GHGCDELVAK YEADHDDYNS IMVKALADRF AEALAEMMHD KVRKEIWGYG AAEQLSNDDL IAEKYKGIRP APGYPACPEH TEKGLLWELL DVEENTGMTL TDAYAMLPTA AVSGFYFSHP ESQYFGVAKI SEDQVESYAK RKGMEMKEAE RWLAPNLGYE PEEG // ID Q2C0E1_9GAMM Unreviewed; 1222 AA. AC Q2C0E1; DT 04-APR-2006, integrated into UniProtKB/TrEMBL. DT 04-APR-2006, sequence version 1. DT 01-APR-2015, entry version 55. DE SubName: Full=Putative cobalamin-dependent methionine synthase {ECO:0000313|EMBL:EAR54560.1}; GN ORFNames=SKA34_22879 {ECO:0000313|EMBL:EAR54560.1}; OS Photobacterium sp. SKA34. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Photobacterium. OX NCBI_TaxID=121723 {ECO:0000313|EMBL:EAR54560.1}; RN [1] {ECO:0000313|EMBL:EAR54560.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SKA34 {ECO:0000313|EMBL:EAR54560.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EAR54560.1}. 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; AAOU01000029; EAR54560.1; -; Genomic_DNA. DR RefSeq; WP_006647409.1; NZ_CH724145.1. DR EnsemblBacteria; EAR54560; EAR54560; SKA34_22879. DR PATRIC; 31361528; VBIPhoSp79054_3849. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1222 AA; 135515 MW; A4884EB402968C4F CRC64; MLNSKELLHK RLEEQILIID GGMGTMIQGY KLEEDDYRGQ RFADWHSDLK GNNDLLVLTQ PQLIKDIHLA YLEAGADILE TNTFNATTIA MADYDMESLS AEINYEAARL ARLAADEWTA QTPEKPRFVA GVLGPTNRTC SISPDVNDPG YRNVTFDELV EAYSESTHAL IKGGADIILL ETIFDTLNAK ACAFAVSGVF EELGFELPVM ISGTITDASG RTLSGQTTEA FYNSLRHVKP ISFGLNCALG PDELRQYVDE LSRISECAVS AHPNAGLPNA FGEYDLEAEE MAEHIREWAQ SGFLNMVGGC CGTTPEHIRH MYEATKNLKP RQLPDIPIAC RLSGLEPLTI DADSLFINVG ERTNVTGSAR FKRLIKEELY DEALEVARQQ VEAGAQIIDI NMDEGMLDAK AAMVRFLNLC ATEPEISKVP IMVDSSKWEV LEAGLKCVQG KPVVNSISMK EGKENFISQA KLLRRYGAAI IVMAFDEVGQ ADTRERKIEI CTNAYRVLVD EVGFPPEDII FDPNIFAVAT GIEEHNNYAV DFIEAVGDIK RTLPYAMVSG GVSNVSFSFR GNNAVREAIH AVFLYYCFKN GMDMGIVNAG QLAIYDDLPD ELRDAVEDVV LNRRDDSTER LLDIAAKYRD SGNVEEDRSA AEWRGWPVEK RLEHALVKGI TEFIVEDTEE SRQKASKPLE VIEGPLMAGM NVVGDLFGEG KMFLPQVVKS ARVMKQAVAY LEPYIDAEKQ AGQTNGKILL ATVKGDVHDI GKNIVGVVLQ CNNYEIIDLG VMVSCDKILK IAKEENVDII GLSGLITPSL DEMMHVAKEM ERQGFDLPLL IGGATTSKAH TAVKIEQNYN QPVVYVSNAS RAVGVCSALL SNEKKPAFVE RLSQEYDVVR EQHARKKPRT APITLEEARA NAVDIDWQSY TPPVPKKAGV HTFTDFPIAE IRKYIDWTPF FMTWSLSGKY PTILRHEVVG EEATKLFNDA NEILDEIEKT GMIKANGICG LFPANNVGDD IEVYTDDSRT DVLTVLHGLR QQTKKPKGPN YCLSDYIAPK ESGKADWIGA FAVTGGIGEY DIAEQFKAKG DDYNAIMVQA VADRLAEAFA ECMHEIVRKD IWGYAADENL NNDDLIREKY QGIRPAPGYA ACPEHTEKGA IWQLLDAEKN TGMVLTESYA MWPGAAVSGW YFSHPDSRYF AVAQIQQDQL ESYADRKGWD LIEAEKWLGP NL // ID Q2CDD1_OCEGH Unreviewed; 342 AA. AC Q2CDD1; DT 04-APR-2006, integrated into UniProtKB/TrEMBL. DT 04-APR-2006, sequence version 1. DT 27-MAY-2015, entry version 27. DE SubName: Full=Methionine synthase I {ECO:0000313|EMBL:EAR50659.1}; GN ORFNames=OG2516_06167 {ECO:0000313|EMBL:EAR50659.1}; OS Oceanicola granulosus (strain ATCC BAA-861 / DSM 15982 / KCTC 12143 / OS HTCC2516). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Oceanicola. OX NCBI_TaxID=314256 {ECO:0000313|EMBL:EAR50659.1}; RN [1] {ECO:0000313|EMBL:EAR50659.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HTCC2516 {ECO:0000313|EMBL:EAR50659.1}; 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. {ECO:0000313|EMBL:EAR50659.1}. 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; AAOT01000024; EAR50659.1; -; Genomic_DNA. DR RefSeq; WP_007254760.1; NZ_CH724107.1. DR EnsemblBacteria; EAR50659; EAR50659; OG2516_06167. DR PATRIC; 28499089; VBIOceGra115923_0693. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 342 AA; 35908 MW; B99D776C6A542FB4 CRC64; MTDALTRLLA DRDWILADGA TGTTLFNMGL QSGDSPEFWN VDHPERIKAL YSGAVEAGSD LFLTNSFGGN AARLKLHDGQ DRVGELNRRA AEIGREVADA AGRPVVVAGS VGPTGEIMAP MGVLTHELAV EMFHEQAEAL KAGGADVLWV ETISAAEEYK AAAEAFALAD MPWCGTMSFD TAGRTMMGFT AAQMVKMVSR LPNPPIAFGA NCGVGASDLL RTVLGFSAAG PENPIIAKGN AGIPRYVDGH IHYNGTPELM AEYALMARDS GATIIGGCCG TTPDHLRAMR AALETKPKGD APTLDTIVAT LGEFSSASDG SDGNSPAPAE RRGRRRARTS RD // ID Q2F5Q8_BOMMO Unreviewed; 325 AA. AC Q2F5Q8; DT 21-MAR-2006, integrated into UniProtKB/TrEMBL. DT 21-MAR-2006, sequence version 1. DT 27-MAY-2015, entry version 29. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABD36309.1}; OS Bombyx mori (Silk moth). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; OC Bombycoidea; Bombycidae; Bombycinae; Bombyx. OX NCBI_TaxID=7091 {ECO:0000313|EMBL:ABD36309.1}; RN [1] {ECO:0000313|EMBL:ABD36309.1} RP NUCLEOTIDE SEQUENCE. RA Niu B.L., Meng Z.Q., Weng H.B., Shen W.F., He L.H., Zheng K.F., RA Ye S.T., Lin T.B., Chen J.E.; RT "Blast silkworm EST database for functional genes."; RL Submitted (NOV-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; DQ311365; ABD36309.1; -; mRNA. DR RefSeq; NP_001040249.1; NM_001046784.1. DR UniGene; Bmo.5853; -. DR ProteinModelPortal; Q2F5Q8; -. DR GeneID; 692944; -. DR KEGG; bmor:692944; -. DR KO; K00547; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Methyltransferase {ECO:0000313|EMBL:ABD36309.1}; KW Transferase {ECO:0000313|EMBL:ABD36309.1}. SQ SEQUENCE 325 AA; 36239 MW; D110B470513C4F0A CRC64; MSNFEVSSKT VFVLDGGFST QLTCHAGHTA DGDPLGSARF LKTHPQDVIN THLDFLRAGS DIIETNTYQA SVDGLVKHLN LTVEESYELI KSAVEFARTA RDLYLQECQE SNLSGRKPLI AGSVGPYGAY LHDTSEYTGN YADNTTKETI KNWHRTRIQA LVEAGVDILA FETIPCQKEA EALVEILKEY PNMKAWLSFS CKNETSLAHG ENFQNVAKKC WKSNPDQLIA IGVNGCSPKI VTELFKDINN DQETSIQYIT YPNSGETYDH KLGWTESDKC ESLHNLVAEW LDLGVRYIGG CCRTNDVDIS RIRIETDLGL KKNSL // ID Q2G121_STAA8 Unreviewed; 613 AA. AC Q2G121; DT 21-MAR-2006, integrated into UniProtKB/TrEMBL. DT 21-MAR-2006, sequence version 1. DT 27-MAY-2015, entry version 65. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=SAOUHSC_00339 {ECO:0000313|EMBL:ABD29507.1}; OS Staphylococcus aureus (strain NCTC 8325). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=93061 {ECO:0000313|EMBL:ABD29507.1, ECO:0000313|Proteomes:UP000008816}; RN [1] {ECO:0000313|Proteomes:UP000008816} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC 8325 {ECO:0000313|Proteomes:UP000008816}; RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., RA Iandolo J.J.; RT "The Staphylococcus aureus NCTC 8325 genome."; RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.); RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, RL Washington D.C (2006). CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ABD29507.1; -; Genomic_DNA. DR RefSeq; WP_000077318.1; NC_007795.1. DR RefSeq; YP_498929.1; NC_007795.1. DR ProteinModelPortal; Q2G121; -. DR SMR; Q2G121; 8-292, 308-567. DR STRING; 93061.SAOUHSC_00339; -. DR EnsemblBacteria; ABD29507; ABD29507; SAOUHSC_00339. DR GeneID; 23196227; -. DR GeneID; 3921813; -. DR KEGG; sao:SAOUHSC_00339; -. DR PATRIC; 19578268; VBIStaAur99865_0310. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; SAUR93061:GIWJ-323-MONOMER; -. DR Proteomes; UP000008816; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008816}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000008816}. SQ SEQUENCE 613 AA; 68478 MW; AB027AAE53F5FD18 CRC64; MSQFLTQLKD NVLVADGAIG TILYSEGLDT CPEAYNLSHP DKVERIHRSY IEAGADVIQT NTYGANFEKL KRFGLEDKVK AIHQAAVRIA KKAANKDTYI LGTVGGFRGI KQEDISLQTI LYHTEIQIDT LIEEGVDALL FETYYDLEEL TNVISRTRKK YDIPIIAQLT ASNTNYLVNG QAINEGLKQL VQCGANIVGL NCHHGPHHMQ ESFTHIELPE HAFLSCYPNA SLLDIENSEF KYSDNAQYFG QVAQNLIREG VRLIGGCCGT TPEHIKFIKE SIQTLKPVND KKVIPIPTKA LFNPSQNKVR QSLTSKVQER PTVIIELDTP KHLDTDRFFE NIAKLDKANV DAVTLADNSL ATVRISNIAA ASLIKQYYNI EPLVHITCRD RNLIGLQSHL LGLSLIGVNE ILAITGDPSK VGHLPGATNV YDVNSKGLTE LALRFNQGIN TDGDALKKRT HFNIAGAFNP NVRKLYGAVK RLEKKIESGM SYFITQPVYS KEKIIEIYHA TKHLNKPFFI GIMPIASYKN ALFLHNEVPG IKMSDEILQQ FEAVKDDKAK TRELSLKLSK DLIDTVHEYF NGLYIITPFQ NVEDSLELAA YSKSITAHKE AIL // ID Q2G3D1_NOVAD Unreviewed; 358 AA. AC Q2G3D1; DT 21-MAR-2006, integrated into UniProtKB/TrEMBL. DT 21-MAR-2006, sequence version 1. DT 27-MAY-2015, entry version 61. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABD27642.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABD27642.1}; GN OrderedLocusNames=Saro_3207 {ECO:0000313|EMBL:ABD27642.1}; OS Novosphingobium aromaticivorans (strain DSM 12444 / F199). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Novosphingobium. OX NCBI_TaxID=279238 {ECO:0000313|EMBL:ABD27642.1, ECO:0000313|Proteomes:UP000009134}; RN [1] {ECO:0000313|Proteomes:UP000009134} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 12444 / F199 {ECO:0000313|Proteomes:UP000009134}; 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; ABD27642.1; -; Genomic_DNA. DR RefSeq; WP_011446844.1; NC_007794.1. DR RefSeq; YP_498476.1; NC_007794.1. DR ProteinModelPortal; Q2G3D1; -. DR STRING; 279238.Saro_3207; -. DR EnsemblBacteria; ABD27642; ABD27642; Saro_3207. DR KEGG; nar:Saro_3207; -. DR PATRIC; 22789274; VBINovAro50627_3289. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; NARO279238:GHBU-3279-MONOMER; -. DR Proteomes; UP000009134; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009134}; KW Methyltransferase {ECO:0000313|EMBL:ABD27642.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000009134}; KW Transferase {ECO:0000313|EMBL:ABD27642.1}. SQ SEQUENCE 358 AA; 38750 MW; EE1C807793A0CE17 CRC64; MTLIPSPLIP SGARTAFLEQ ASQRILITDG AFGTEIQNFK LSEEDYAGTL GLAKDQKGNN DILALTKPEV PESIHRAYFE AGADIAETNT FSANRISQAD YAAEHLVREI NVESARLARR VADEFTARDG KPRFVAGAIG PTNKTLSLSP DVNDPGFREI DWDHLVDVYA EQVHALVEGG ADFILIETVF DTLNAKAGVM SVRQVEKQLG REIPIMMSMT LTDLSGRNLS GHTVEAFWYA IRHARPLTVG LNCSFGATQL RPHVKALSEI ADTLIMVYPN AGLPNELGEY DEMPQTTAGL VKEWADHGQV NVLGGCCGST PAHIAAMAQA VKALPPRKMA VPETVTRLAG LEPFIMAA // ID Q2G5H0_NOVAD Unreviewed; 330 AA. AC Q2G5H0; DT 21-MAR-2006, integrated into UniProtKB/TrEMBL. DT 21-MAR-2006, sequence version 1. DT 27-MAY-2015, entry version 52. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABD26903.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ABD26903.1}; GN OrderedLocusNames=Saro_2467 {ECO:0000313|EMBL:ABD26903.1}; OS Novosphingobium aromaticivorans (strain DSM 12444 / F199). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Novosphingobium. OX NCBI_TaxID=279238 {ECO:0000313|EMBL:ABD26903.1, ECO:0000313|Proteomes:UP000009134}; RN [1] {ECO:0000313|Proteomes:UP000009134} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 12444 / F199 {ECO:0000313|Proteomes:UP000009134}; 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; ABD26903.1; -; Genomic_DNA. DR RefSeq; WP_011446109.1; NC_007794.1. DR RefSeq; YP_497737.1; NC_007794.1. DR ProteinModelPortal; Q2G5H0; -. DR STRING; 279238.Saro_2467; -. DR EnsemblBacteria; ABD26903; ABD26903; Saro_2467. DR KEGG; nar:Saro_2467; -. DR PATRIC; 22787682; VBINovAro50627_2522. DR eggNOG; COG2040; -. DR HOGENOM; HOG000179103; -. DR OMA; CCGTDHR; -. DR OrthoDB; EOG6R5C46; -. DR BioCyc; NARO279238:GHBU-2509-MONOMER; -. DR Proteomes; UP000009134; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009134}; KW Methyltransferase {ECO:0000313|EMBL:ABD26903.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000009134}; KW Transferase {ECO:0000313|EMBL:ABD26903.1}. SQ SEQUENCE 330 AA; 35473 MW; E46E5669CE8717A9 CRC64; MLGHGCASML NCRVNRDREG AMALAKLPQL ESVFLTDAGL ETDFIFNRGI DLPYFASITL LQSSDGKIAL EEYFRGFLEL ARRMRCGLIL ESATWRASPD WAEPLGLSQQ ELDTLNTSAI AILRDLRDEF GSTMPAVVIS GCLGPRGDGY DPGKIMSEEG AEAYHRHQAE VLASAGVDQL TAITMTNVPE AIGIAKAAKS LAVPVAISFT VETDGRLPTG DRLSDALRAV DQATASTPAY YMINCAHPSH FAAVLEDGAD WVNRIGGLRA NASRCSHAEV DAMSELDRGN PEELAALHSE LRLRFPHINV LGGCCGTDLD HITAIAEACL // ID Q2IIS1_ANADE Unreviewed; 287 AA. AC Q2IIS1; DT 07-MAR-2006, integrated into UniProtKB/TrEMBL. DT 07-MAR-2006, sequence version 1. DT 27-MAY-2015, entry version 51. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABC81551.1}; GN OrderedLocusNames=Adeh_1778 {ECO:0000313|EMBL:ABC81551.1}; OS Anaeromyxobacter dehalogenans (strain 2CP-C). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter. OX NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC81551.1, ECO:0000313|Proteomes:UP000001935}; RN [1] {ECO:0000313|Proteomes:UP000001935} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935}; 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 ----------------------------------------------------------------------- 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; ABC81551.1; -; Genomic_DNA. DR RefSeq; WP_011420834.1; NC_007760.1. DR RefSeq; YP_464988.1; NC_007760.1. DR ProteinModelPortal; Q2IIS1; -. DR STRING; 290397.Adeh_1778; -. DR EnsemblBacteria; ABC81551; ABC81551; Adeh_1778. DR KEGG; ade:Adeh_1778; -. DR PATRIC; 20919717; VBIAnaDeh31384_1840. DR eggNOG; NOG129730; -. DR HOGENOM; HOG000265278; -. DR OMA; VLTCTFN; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; ADEH290397:GI2Z-1803-MONOMER; -. DR Proteomes; UP000001935; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001935}; KW Methyltransferase {ECO:0000313|EMBL:ABC81551.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001935}; KW Transferase {ECO:0000313|EMBL:ABC81551.1}. SQ SEQUENCE 287 AA; 28094 MW; 3871B9A418BEC33A CRC64; MTRATPPVPF ERPTLLDGAM GTALLDAGLP AGALPEAWVL ERPEAIAAVH AAHAAAGAGV VLTCTFNAAG PRLDALVPAD RVGALCAAAV RLARRAAPRA RVAGDLGPTA LYGPGRPAPD AGAVRARYAR AAEALAAAGA DLLWVESQWD LAEARLALDA ARAAGLPVVV TFALGEEAGR LAAPDGTPAE ALLEAVAEAG AAAAGVNCVP AGAALAALAG WAARRLPAPF VAKPSPGLPG AVLGPDAFAE ALRPAVEAGL SVAGGCCGAG PAHLAALGRL LARPRAG // ID Q2IM33_ANADE Unreviewed; 1150 AA. AC Q2IM33; DT 07-MAR-2006, integrated into UniProtKB/TrEMBL. DT 07-MAR-2006, sequence version 1. DT 27-MAY-2015, entry version 76. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABC79862.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABC79862.1}; GN OrderedLocusNames=Adeh_0085 {ECO:0000313|EMBL:ABC79862.1}; OS Anaeromyxobacter dehalogenans (strain 2CP-C). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter. OX NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC79862.1, ECO:0000313|Proteomes:UP000001935}; RN [1] {ECO:0000313|Proteomes:UP000001935} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000251; ABC79862.1; -; Genomic_DNA. DR RefSeq; WP_011419145.1; NC_007760.1. DR RefSeq; YP_463299.1; NC_007760.1. DR ProteinModelPortal; Q2IM33; -. DR STRING; 290397.Adeh_0085; -. DR EnsemblBacteria; ABC79862; ABC79862; Adeh_0085. DR KEGG; ade:Adeh_0085; -. DR PATRIC; 20916175; VBIAnaDeh31384_0092. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; ADEH290397:GI2Z-87-MONOMER; -. DR Proteomes; UP000001935; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001935}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABC79862.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001935}; KW Transferase {ECO:0000313|EMBL:ABC79862.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 733 733 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1150 AA; 124694 MW; 12AFF759931FB023 CRC64; MTFREALERR PLVFDGAMGT QIQRHQLTAA EFGGKEGAND LLTLTRPDLI EEIHARYFAV GCDVVETNTF GSSRLKLDEY GLGHRTYEVN CRAAILARRA AERFSTPDHP RFVAGSIGPT GMLPSSSDPA LGNITSDALE RIFFEQAKGL VEGGVDALII ETQQDMLELR AAVLACDAVR REALRDVFVI AQPTLIDANG RMLLGTDVGS AVATLERLPV DAVGLNCSTG PDEMRASVKA LAERCSHWVS VLPNAGMPEN EDGRAVYKLS PDDLARALAG FVAEYGVDIV GGCCGTTPEH LRKVVEALRG LSAPRRRRPA PAAELSSAMK AVPLAMEPRP LVVGERLNSQ GSRKVKELLL ADDYAGLVQI ARGQVEAGAH VLDVCVALNE RDDEAAQMRT LAKLLAQSVD APLMIDSTEP DVIEGALKVY PGRCIVNSVN LEKSGERVRR VLPLVRRYGA AVVAMTIDEK GMAQTAERKA EVARRIVAVA KDHGIPPDSL VFDALTFTLA TGGEEYRRSA VETLEGIRRI KAENPGVLTT LGVSNVSFGL AKSAREVVNS VFLYHAVQAG LDLAIVNPKD ILPYPAIDAA ERALAEDLVF DRRPDALARL IAHFGAKGAP EKAAVDPLAG AAGKGAEERI HLQILHRRPE GIEALIDEAL TRRSAVDVLN QVLLPAMKDV GDRFGAGELI LPFVLQSAEV MKKAVAHLEQ FLEKKAGATK GNVVLATVYG DVHDIGKNLV KTILSNNGFT VHDLGKQVPV TTVLDKALQV NADAIGLSAL LVSTSKQMPF CVEELHRRNL SFPVIIGGAA INRRFGYRTH FAQDGTPYAG GVFYAKDAFE GLEVVEALVD PARREALKRE VLQKAVAEKE RPADKPMAPA PARRTGAVAP AARIPTPPFW GPRVVPSGSV ALADVWPHLD LAELFKLQWG VKAKGAEYER LVREEFGPKL EELKAEAQAQ GWLVPKVVYG YFPCHAEGND LVVLDPTHRK AEVARLALPR QPDDRNLCLA DYFREERGAD VCALQVVTVG DQATHLAEQA QERGDYTRAL FLHGLAVETA EALAEYWHRQ VRAELGLADG QGKRYSPGYP SWPELSDQRQ VWKLLDPVRT IGVSLTDACQ MVPEQSTSAI VLHHPDAIYF LVRGLERAAG // ID Q2IZ88_RHOP2 Unreviewed; 1304 AA. AC Q2IZ88; DT 07-MAR-2006, integrated into UniProtKB/TrEMBL. DT 07-MAR-2006, sequence version 1. DT 29-APR-2015, entry version 69. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABD06472.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABD06472.1}; GN OrderedLocusNames=RPB_1764 {ECO:0000313|EMBL:ABD06472.1}; OS Rhodopseudomonas palustris (strain HaA2). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Rhodopseudomonas. OX NCBI_TaxID=316058 {ECO:0000313|EMBL:ABD06472.1, ECO:0000313|Proteomes:UP000008809}; RN [1] {ECO:0000313|EMBL:ABD06472.1, ECO:0000313|Proteomes:UP000008809} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HaA2 {ECO:0000313|EMBL:ABD06472.1, RC ECO:0000313|Proteomes:UP000008809}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000250; ABD06472.1; -; Genomic_DNA. DR RefSeq; WP_011440660.1; NC_007778.1. DR RefSeq; YP_485383.1; NC_007778.1. DR STRING; 316058.RPB_1764; -. DR EnsemblBacteria; ABD06472; ABD06472; RPB_1764. DR KEGG; rpb:RPB_1764; -. DR PATRIC; 23298121; VBIRhoPal125544_1854. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; RPAL316058:GHF1-1784-MONOMER; -. DR Proteomes; UP000008809; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008809}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABD06472.1}; KW Transferase {ECO:0000313|EMBL:ABD06472.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 253 253 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 316 316 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 773 773 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1304 AA; 141400 MW; 1EBAEFE7FC6C1411 CRC64; MNSMTKPTSP KRTELLALTR ERILVLDGAM GTMIQALQFD EAAFRGERFK DFHRDLRGNN DLLILTQPQA IEDIHAQYLR AGADIVATNT FSSTSIAQAD YDLSEIAYEM SRDGARLARN AADTVQAEDG KPRFVAGAIG PTNRTASISP DVANPGYRAV TFDDLRIAYG EQINGLLDGG ADLLLVETIF DTLNAKAALY AIAEISEARG IDVPVMISGT ITDKSGRLLS GQLPEAFWNS VRHAKPITIG FNCALGAKDL RAHIADIGRV ADTLVCAYPN AGLPNEFGQY DESPDYMASL VGEFAEAGLV NIVGGCCGTT PAHIAAIAKA VAPHKPRVVP VIEPRLRLSG LEPFELTQAI PFVNVGERTN VTGSAKFRKL ITAGDYAAAL QVARDQVENG AQIIDVNMDE GLLDSEAAMV TFLNLVAAEP DIAKVPVMVD SSKFAVIEAG LKCVQGKPVV NSISLKEGED KFLHEARIAR RHGAAVVVMA FDEQGQADTY ARKTEICKRA YDILVERIGF PPEDIIFDPN IFAIATGLEE HNNYGVDFIE ATRWIRQNLP HAHISGGVSN LSFSFRGNEP VREAMHSVFL YHAIKAGMDM GIVNAGQMIV YDDIDPELRQ TCEDVILNRD PGASERLLAL AEKYRGQGKA VKEQDLAWRS WPVEQRLSHA LVHGITEYIE TDTEEARAKA ERPLHVIEGP LMAGMNVVGD LFGDGKMFLP QVVKSARVMK QAVAYLMPFM EAEKAAQLAA GTHTGERATA GKIVLATVKG DVHDIGKNIV GIVLQCNNFE VIDLGVMVPA AKIIETAIAE QADIIGLSGL ITPSLDEMSF LASEMQRNGL DMPLLIGGAT TSRVHTAVKI DPSYPAGSVV HVNDASRAVG VASSLLSRER GPAYAAEIRA DYARITAAHL RAQADKKRVA LKDARANATK IDWSAAKPVK PSFLGVRSFI NYPLAELAET IDWTPFFQSW ELAGRFPAIL DDKVVGEAAR SLYADARKML ERIVAENWFT AKAVIGFWPA NAVGDDIILY ADDDRDASIG ALHTLRQQLV KREGRANAAL SDFIAPRGVQ DYIGAFVVTA GIGEDVIADK FKADNDDYSS IMVKALADRL AEAFAERMHA RVRREFWGYA PDESLSVDEL ILEKYQGIRP APGYPAQPDH TEKATLFKLL EAEVNAGVTL TESYAMWPGS SVSGLYFSHP QSAYFGVGKI ERDQVEDYAL RKGWSVTEAE RWLAPVLNYI PEPQPAGARA QEPMPPLAPS GDLLPTEPPA DAAFTANDAA LAAHPAGCNC AVHLMWRKTA VGAK // ID Q2JGT6_FRASC Unreviewed; 1259 AA. AC Q2JGT6; DT 07-MAR-2006, integrated into UniProtKB/TrEMBL. DT 07-MAR-2006, sequence version 1. DT 27-MAY-2015, entry version 73. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABD09506.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABD09506.1}; GN OrderedLocusNames=Francci3_0112 {ECO:0000313|EMBL:ABD09506.1}; OS Frankia sp. (strain CcI3). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Frankineae; Frankiaceae; Frankia. OX NCBI_TaxID=106370 {ECO:0000313|EMBL:ABD09506.1, ECO:0000313|Proteomes:UP000001937}; RN [1] {ECO:0000313|EMBL:ABD09506.1, ECO:0000313|Proteomes:UP000001937} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CcI3 {ECO:0000313|EMBL:ABD09506.1, RC ECO:0000313|Proteomes:UP000001937}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000249; ABD09506.1; -; Genomic_DNA. DR RefSeq; WP_011434587.1; NC_007777.1. DR RefSeq; YP_479235.1; NC_007777.1. DR ProteinModelPortal; Q2JGT6; -. DR SMR; Q2JGT6; 672-923. DR STRING; 106370.Francci3_0112; -. DR EnsemblBacteria; ABD09506; ABD09506; Francci3_0112. DR KEGG; fra:Francci3_0112; -. DR PATRIC; 21922978; VBIFraSp10456_0125. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; QPFFNAW; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; FSP106370:GI1F-114-MONOMER; -. DR Proteomes; UP000001937; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001937}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABD09506.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001937}; KW Transferase {ECO:0000313|EMBL:ABD09506.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 268 268 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 331 331 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 332 332 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 788 788 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1259 AA; 135235 MW; 5B800256DE2F98D0 CRC64; MAGSRSVDEV AVHDGVVEAS TVGADAVEAG ERELRELLAQ RVVVLDGAWG TMLQNAGLTP ADYRTERFRD HPKDLAGDPD LLNLTRPDVI LDVHRQYLAA GADITTTNTF TATSIGQADY GLQSLVREMN LRGARLARQA ADEAARQTGG RRFVAGSIGP LNVTLSLSPR VEDPAYRAVT FDEVRAAYAE QIQALADGGV DLLLIETIFD TLNAKAAIAA AREVAPRLPL WISVTIVDLS GRTLSGQTVE AFWSSIAHAH PLVVGVNCSL GAEEMRPHVA ELARLAGTFT ACHPNAGLPN AFGGYDQTPD EAGQLIGEFA AAGLVNIVGG CCGTTPAHIA RIAAAVGGAP PRPVPTPPAR TRFSGLEPFE IGEDTGFVMI GERTNVTGSA RFRRLIEADD YQAAVDVALE QVRGGANLLD VNMDADLLDS ERAMTTFLNL LATEPEAARL PIMVDSSRWS VLEAGLRCVQ GKGVVNSISL KEGEEPFLEQ ARRIRDYGAG VVVMAFDERG QADTAERKVA ICARAYDLLT QRVGFPAEDI VFDPNVLAVA TGIAEHNGYA KAFLDALPLI KQHCPGARTS GGISNLSFSF RGNDIVREAM HSAFLFHAVR AGLDMGIVNA GQLAVYQDIP ADLLELVEDV LFDRRDDATD RLVAFAETVS GSGTKRTVDL SWREAPVEER LAHALVHGIV DFIESDTEEA RARAARPLDV IEGPLMDGMK IVGDLFGSGK MFLPQVVKSA RVMKRSVAYL EPFMEAEKQQ ALLAGTGTGR ANRGNGTVVL ATVKGDVHDI GKNIVGVVLG CNNYEVIDLG VMVPATVILD TAVAEGADAI GLSGLITPSL DEMVTVATEM QRRGLKLPLL IGGATTSRQH TAVRIAPAYD ATTVHVLDAS RVVGVVSDLL DADRAGELAV RNRAEQKLLR EQHENRQQRP LLPLAQARAN REQVTFDDLP VPAFTGVRVV TPDLGALRSM IDWQFFFLAW ELKGKFPAIL DQPVARELYD EANVLLDQII ADGSLQARGV YGFWPAVAED DDILIDQIDV GAVNSASSPG QGGTPGPGGT GRLRLPMLRQ QTAKPAGRPN RSLADYLAPA GDHIGGFAVA VHGADTLAAG FEARQDDYRA IMVKALADRL AEAFAEYVHL EARRAWFEPD AKPSLEDLHA ERFRGIRPAF GYPASPDHSE KQALFDLLDA GRVGMGLTES FAMTPAAAVS GLIFAHPSSR YFTVGRIGRD QVEDYAQRRG LKISDVERWL RPNLAYDPE // ID Q2JJL4_SYNJB Unreviewed; 1224 AA. AC Q2JJL4; DT 07-MAR-2006, integrated into UniProtKB/TrEMBL. DT 07-MAR-2006, sequence version 1. DT 27-MAY-2015, entry version 77. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABD03153.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABD03153.1}; GN Name=metH {ECO:0000313|EMBL:ABD03153.1}; GN OrderedLocusNames=CYB_2208 {ECO:0000313|EMBL:ABD03153.1}; 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 {ECO:0000313|EMBL:ABD03153.1, ECO:0000313|Proteomes:UP000001938}; RN [1] {ECO:0000313|EMBL:ABD03153.1, ECO:0000313|Proteomes:UP000001938} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JA-2-3B'a(2-13) {ECO:0000313|Proteomes:UP000001938}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000240; ABD03153.1; -; Genomic_DNA. DR RefSeq; WP_011433788.1; NC_007776.1. DR RefSeq; YP_478416.1; NC_007776.1. DR ProteinModelPortal; Q2JJL4; -. DR STRING; 321332.CYB_2208; -. DR EnsemblBacteria; ABD03153; ABD03153; CYB_2208. DR KEGG; cyb:CYB_2208; -. DR PATRIC; 23806770; VBISynSp29577_2217. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; ILESWIT; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SSP321332:GH1B-2208-MONOMER; -. DR Proteomes; UP000001938; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 2. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001938}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABD03153.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001938}; KW Transferase {ECO:0000313|EMBL:ABD03153.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 225 225 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 292 292 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 744 744 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1224 AA; 135280 MW; BF95D63BAFD2845B CRC64; MTHPFLQHLQ ERVIVFDGAM GSSLQAQNLT AADFGGPELE GCNEMLVLTK PEAVERVHRG FLEVGADVVE TNTFGATSIV LAEYGIPEKA YELNVAAARL AKRVAAEFAT PEKPRFVAGS IGPTTKLPTL GHISFDEMRA AYEEQVQGLV DGGADLLIIE TCQDILQTKA ALVAVQQEFA RRGIRLPVVV SLTFEVQGTM LVGTEIGAAL AILEPYPIDV LGLNCATGPD KMVEHIRYLS RHSPFPISCI PNAGLPENIG GKAHYKLTPE QLRFHLEHFV RDLGVAVVGG CCGTRPEHIA ALVEAVQGLR PKRRSIERIQ AAASIYTPQP YLQDNSFLII GERLNASGSK KMRELLNAED WDGLVALARE QVREGAHILD VNVDYVGRDG VRDMRELVSR LVTQIQIPLM LDSTDWQKME AGLKVAGGKC LLNSTNYEDG EERFLKVLEL AKTYGAGVVI GTIDEEGMAR TADKKFQIAE RAYRQAVEYG IPPYEIFFDP LALPISTGIE EDRANGAATL EAIRRIRQAF PETHILLGIS NISFGLSPAA RVVLNSVFLH ECREAGLDAA IVSAAKILPL NKIPAEQQQV CRDLIWDRRQ FNAVRVSGTE SSGICTYDPL ARLTELFAGV SGKELRSGGS FADLPLEERL RRHIIDGERI GLEETLAEAL QNYPPLEIIN TFLLDGMKEV GELFGAGKMQ LPFVLQSAET MKAAVKYLEP FMEKVGGEVC KGTLLIATVK GDVHDIGKNL VDIILTNNGY RVINLGIKQP VENIIEAYEK SKADCIAMSG LLVKSTAFMK ENLEVFNERG ITVPVILGGA ALTRRFVEED CRQTYKGQVI YGRDAFVDLH FMDRLMQAKA AGRWDDRLGF LDDLELGSPS ANGQKEASWV PEETDPSLPP AETTVGAAPA LTLSESQDTR RSEAVALETE RPIPPFWGSQ VLTSDQIPWP EVFFYIDKQA LVAGQWQIRK PRDQSAEEFA EFIATQVEPV IERWKERILA EDLLHPQIVY GYFPAQAEGN TLILFDPASF PELFSLEPGS TTYFQLPTVE RPQLSPGVRE LARFTFPRQK TGHRYCIADF FAARSTGLVD VFPMQAVTVG AEATAYAQRL FAEGQYTDYL YFHGLAVTLA EALAEWCHAR IRRELGFGHE DSPDIRKILH QGYRGSRYSF GYPACPNIAD QRVLLQVLQA ERIGLTMDES DQLDPEQSTT AIVAYHPAAR YFNT // ID Q2JS51_SYNJA Unreviewed; 1219 AA. AC Q2JS51; DT 07-MAR-2006, integrated into UniProtKB/TrEMBL. DT 07-MAR-2006, sequence version 1. DT 01-APR-2015, entry version 74. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABD00535.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABD00535.1}; GN Name=metH {ECO:0000313|EMBL:ABD00535.1}; GN OrderedLocusNames=CYA_2411 {ECO:0000313|EMBL:ABD00535.1}; OS Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium OS Yellowstone A-Prime). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechococcus. OX NCBI_TaxID=321327 {ECO:0000313|EMBL:ABD00535.1, ECO:0000313|Proteomes:UP000008818}; RN [1] {ECO:0000313|EMBL:ABD00535.1, ECO:0000313|Proteomes:UP000008818} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JA-3-3Ab {ECO:0000313|EMBL:ABD00535.1, RC ECO:0000313|Proteomes:UP000008818}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000239; ABD00535.1; -; Genomic_DNA. DR RefSeq; WP_011431208.1; NC_007775.1. DR RefSeq; YP_475798.1; NC_007775.1. DR ProteinModelPortal; Q2JS51; -. DR STRING; 321327.CYA_2411; -. DR EnsemblBacteria; ABD00535; ABD00535; CYA_2411. DR KEGG; cya:CYA_2411; -. DR PATRIC; 23813078; VBISynSp90045_2365. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SSP321327:GHFX-2403-MONOMER; -. DR Proteomes; UP000008818; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 2. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008818}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABD00535.1}; KW Transferase {ECO:0000313|EMBL:ABD00535.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 225 225 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 292 292 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 736 736 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1219 AA; 134855 MW; 99AF9301EBC72C42 CRC64; MTHPFLQHLQ ERVIVFDGAM GSSLQAQNLT AADFGGPELE GCNEILVLSK PEAVERVHRG FLEVGADVIE TDTFGATSIV LAEYGIAEKA YELNVAAARL AKRLAAEFST PEKPRFVAGS IGPTTKLPTL GHIGFDEMRA SYAEQVRGLI DGGVDLLIIE TCQDILQTKA ALVAVQQEFA RRGIRLPLVV SLTFEVQGTM LVGTEIGAAL AILEPYPIDV LGLNCATGPD KMAEHIRYLS RHSPFPISCI PNAGLPENIG GKAHYKLTPE QLRFHLEHFV RDLGVAVVGG CCGTRPGHIA ALVEAVRGLR PKRRSVERIQ AAASIYAPQP YLQENSFLII GERLNASGSK KMRELLNAED WDGLVALARE QVREGSHILD VNVDYVGRDG VRDMRELVSR LVTQIPIPLM LDSTDWQKME AGLKVAGGKC LLNSTNYEDG EERFFKVLEL AKTYGAGVVI GTIDEEGMAR TAEKKFQIAE RAYRQAVEYG IPPYEIFFDP LALPISTGIE EDRANGAATL EAIRRIRQAF PEAHILLGIS NISFGLSPAA RVVLNSVFLH ECRQAGLDAA IVSAAKILPL SKIPEEQQQV CRDLIWDRRQ FNAEGICTYD PLARLTELFA GVSGQELRAT GSLAKLPLEE RLRRHIIDGE RIGLEETLAE ALQKYPPLEI INTFLLDGMK EVGELFGAGK MQLPFVLQSA ETMKAAVKYL EPFMEKVGGE VCKGTFLIAT VKGDVHDIGK NLVDIILTNN GYKVINLGIK QPVENIIEAY EKYKPDCIAM SGLLVKSTAF MKENLEVFNE RGITVPVILG GAALTRRFVE EDCRQTYKGQ VIYGRDAFAD LHFMDRLMQA KAAGRWDDRL GFLDNFELGS RSDNRQRRAA AAVEERDPTL PAPEVTVGAA PAPAVSAGDG GADTRRSEAV TLDTERPIPP FWGSQVLEPD QIPWPEVFFY IDKQALVAGQ WQIRKPRDQS AEEFAQFLAT QVEPVIERWK ERIVTEDLLR PQVVYGYFPA QAEGNTVILF DPASFPELFA LEPGSTTYLQ LPTVDRPRLS PQVRELARFT FPRQKSGQRL CIADFFADRS TGLVDVFPMQ AVTVGPEATA YAQHLFAEGQ YTDYLYFHGL AVTLAEALAE WCHARIRREL GFGGEDSPDI RQILHQGYRG SRYSFGYPAC PNIADQRVLL ELLQTERIGL RMDESDQLDP EQSTTAIVAY HPAARYFNT // ID Q2K1K9_RHIEC Unreviewed; 302 AA. AC Q2K1K9; DT 07-MAR-2006, integrated into UniProtKB/TrEMBL. DT 07-MAR-2006, sequence version 1. DT 27-MAY-2015, entry version 51. DE SubName: Full=Probable homocysteine S-methyltransferase protein {ECO:0000313|EMBL:ABC93369.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ABC93369.1}; GN OrderedLocusNames=RHE_PC00163 {ECO:0000313|EMBL:ABC93369.1}; OS Rhizobium etli (strain CFN 42 / ATCC 51251). OG Plasmid p42c {ECO:0000313|EMBL:ABC93369.1, OG ECO:0000313|Proteomes:UP000001936}. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=347834 {ECO:0000313|EMBL:ABC93369.1, ECO:0000313|Proteomes:UP000001936}; RN [1] {ECO:0000313|EMBL:ABC93369.1, ECO:0000313|Proteomes:UP000001936} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CFN 42 / ATCC 51251 {ECO:0000313|Proteomes:UP000001936}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000136; ABC93369.1; -; Genomic_DNA. DR RefSeq; WP_011427789.1; NC_007764.1. DR RefSeq; YP_472096.1; NC_007764.1. DR ProteinModelPortal; Q2K1K9; -. DR STRING; 347834.RHE_PC00163; -. DR EnsemblBacteria; ABC93369; ABC93369; RHE_PC00163. DR KEGG; ret:RHE_PC00163; -. DR PATRIC; 23091081; VBIRhiEtl108884_5171. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; PYVDVWL; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; RETL347834:GJJ0-5746-MONOMER; -. DR Proteomes; UP000001936; Plasmid p42c. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001936}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ABC93369.1}; KW Plasmid {ECO:0000313|EMBL:ABC93369.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001936}; KW Transferase {ECO:0000313|EMBL:ABC93369.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 302 AA; 32360 MW; D009454E9A3A7AA7 CRC64; MSTTRILDGG MSRELLRLGA ELKQPEWSAL ALINSPDIVR EVHKEFIAAG SEIITTNSYA LVPFHIGEDR FRKEGAALIR LAGRLAREAA DSVTGRKVLV AGSLPPIFGS YEPQNFRPER VQDYLKVLVE NLAPFVDIWL GETLSLIAEG EAVREAVAAS GKPFWISFTL ADDKADIESG EPKLRSGESV EAAASWAASS GAEAFLFNCS KPEVMEAAVA TAAAVFRKMD AGIEIGVYAN AFEGEQGESA ANEGLHETRD DLNDDAYSRF ACSWAEAGAT IIGGCCGIGA AHIHRLGKTL RS // ID Q2K667_RHIEC Unreviewed; 1271 AA. AC Q2K667; DT 07-MAR-2006, integrated into UniProtKB/TrEMBL. DT 07-MAR-2006, sequence version 1. DT 27-MAY-2015, entry version 70. DE SubName: Full=5-methyltetrahydrofolate--homocysteine S-methyltransferase protein {ECO:0000313|EMBL:ABC91669.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABC91669.1}; GN Name=metH {ECO:0000313|EMBL:ABC91669.1}; GN OrderedLocusNames=RHE_CH02901 {ECO:0000313|EMBL:ABC91669.1}; OS Rhizobium etli (strain CFN 42 / ATCC 51251). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=347834 {ECO:0000313|EMBL:ABC91669.1, ECO:0000313|Proteomes:UP000001936}; RN [1] {ECO:0000313|EMBL:ABC91669.1, ECO:0000313|Proteomes:UP000001936} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CFN 42 / ATCC 51251 {ECO:0000313|Proteomes:UP000001936}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000133; ABC91669.1; -; Genomic_DNA. DR RefSeq; WP_011426145.1; NC_007761.1. DR RefSeq; YP_470396.1; NC_007761.1. DR ProteinModelPortal; Q2K667; -. DR SMR; Q2K667; 680-1258. DR STRING; 347834.RHE_CH02901; -. DR EnsemblBacteria; ABC91669; ABC91669; RHE_CH02901. DR KEGG; ret:RHE_CH02901; -. DR PATRIC; 23087423; VBIRhiEtl108884_3363. DR eggNOG; COG1410; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; RETL347834:GJJ0-2914-MONOMER; -. DR Proteomes; UP000001936; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001936}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABC91669.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001936}; KW Transferase {ECO:0000313|EMBL:ABC91669.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 274 274 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 337 337 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 338 338 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 790 790 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1271 AA; 140385 MW; DE8B9003952C2F0B CRC64; MIWTVWSYDV KEPPVFDNLF GPETGKRDGN EVFAALRKAA SERILVLDGA MGTQIQGLGY DEDQFRGTRF IGCACHQKGN NDLLILTQPD AIEEIHYRYA KAGADILETN TFSSTRIAQA DYQMEGAVYD LNKEGAEIVR RAALRAERED GRRRFVAGAI GPTNRTASIS PDVNNPGFRA VTFDDLRSAY GEQIDGLIDG GADIILIETI FDTLNAKAAI FACEERFEAK GVRLPVMISG TITDLSGRTL SGQTPSAFWN SVRHANPFTI GLNCALGANA MRPHLQELSG VADTFICAYP NAGLPNEFGQ YDETPELMAA QIDSFAREGL VNIVGGCCGS TPEHIRAIAE TVAKYKPRPI PEHRPFMSLS GLEPFELTKD IPFVNVGERT NVTGSAKFRK LITNADYTAA LDVARDQVEN GAQVIDINMD EGLIDSEKAM VEFLNLIAAE PDIARVPVMI DSSKFSIIES GLKRVQGKPI VNSISLKEGE ENFLAQARLL RNYGAAVVVM AFDETGQADN YDRKVEICTR AYKLLTEKIG FPPEDIIFDP NIFAVATGIE EHNNYGVDFI EAARTIRERM PLVHISGGVS NLSFSFRGNE PVREAMHAVF LYHAIQAGMD MGIVNAGQLA VYDNIDPELR EACEDVVLNR RADGTERLLE VAERFRGAGA KEGRVQDLSW REWSVEKRLE HALVNGITEY IEADTEEARR QAARPLHVIE GPLMAGMNVV GDLFGSGKMF LPQVVKSARV MKQAVAVLLP YMEEEKRLNG GDDRQSAGKI LMATVKGDVH DIGKNIVGVV LACNNYEIVD LGVMVPATKI LETAIAEKVD VIGLSGLITP SLDEMVHVAS EMERQGFEIP LLIGGATTSR VHTAVKIHPG YNKGQAVYVT DASRAVGVVS ALLSPETRQG YVDDIRAEYA KVAAAHARSE AEKVRLPLAR ARENAHKIDW SAYKPTKPEF FGTRVFEDYD LAELAKYIDW TPFFQTWELR GRFPAILEDE KQGEAARALW ADAQAMLKKI IDEKWFRPRA VIGFWPAGAV GDDIRLFTDE SRSQELATFY TLRQQLSKRD GRANVALSDF VAPVTSGVQD YVGGFVVTAG IEEIAIAERF ERSNDDYSSI LVKALADRFA EAFAERMHEQ VRREYWGYAS DEHLSNEDLI GEAYAGIRPA PGYPAQPDHT EKKTLFKLLD AEKAAGVKLT ESYAMWPGSS VSGLYIGHPD SYYFGVAKVE RDQVEDYAKR KGMDVSEVER WLGPVLNYVP RKADEEIDDA A // ID Q2KUI4_BORA1 Unreviewed; 1258 AA. AC Q2KUI4; DT 07-MAR-2006, integrated into UniProtKB/TrEMBL. DT 07-MAR-2006, sequence version 1. DT 01-APR-2015, entry version 69. DE SubName: Full=Methionine synthase (5-methyltetrahydrofolate--homocysteine methyltransferase) {ECO:0000313|EMBL:CAJ50676.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAJ50676.1}; DE Flags: Fragment; GN Name=metH {ECO:0000313|EMBL:CAJ50676.1}; GN OrderedLocusNames=BAV3066 {ECO:0000313|EMBL:CAJ50676.1}; OS Bordetella avium (strain 197N). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=360910 {ECO:0000313|EMBL:CAJ50676.1, ECO:0000313|Proteomes:UP000001977}; RN [1] {ECO:0000313|EMBL:CAJ50676.1, ECO:0000313|Proteomes:UP000001977} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=197N {ECO:0000313|EMBL:CAJ50676.1, RC ECO:0000313|Proteomes:UP000001977}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AM167904; CAJ50676.1; -; Genomic_DNA. DR RefSeq; WP_012418704.1; NC_010645.1. DR RefSeq; YP_787561.1; NC_010645.1. DR EnsemblBacteria; CAJ50676; CAJ50676; BAV3066. DR KEGG; bav:BAV3066; -. DR PATRIC; 21132445; VBIBorAvi43433_3101. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; QPFFNAW; -. DR BioCyc; BAVI360910:GCKI-3140-MONOMER; -. DR Proteomes; UP000001977; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001977}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAJ50676.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001977}; KW Transferase {ECO:0000313|EMBL:CAJ50676.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 256 256 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 789 789 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. FT NON_TER 1 1 {ECO:0000313|EMBL:CAJ50676.1}. SQ SEQUENCE 1258 AA; 139016 MW; 62288DC5FF5E6E34 CRC64; VSYPRMPYPL SAYTRGAEFV RLLAERILIL DGAMGTMIQR YKLSEADFRG ARFAEHHKDL KGDNELLSLV RPDVIAEIHR QYLEAGADVI ETNTFGATSI AQGDYDLPEL AYELNLASAR LAREACDAYS TPERPRFVAG ALGPQPKTAS ISPDVNDPGA RNVTFEALRA AYVEQLNGLL DGGIDIVLIE TIFDTLNAKA AIFAIEQVFE QRGVRLPVMI SGTVTDASGR ILSGQTVEAF WNSVRHARPV TIGLNCALGA ALMRPYVAEL SKICDTYVCV YPNAGLPNPM AETGFDETPA DTSALLEEFA ASGLVNMAGG CCGTTPDHIR AIADKIERLT PRQVPEVPVK TRLSGLEPLN IDEDTLFVNV GERTNVTGSK MFARLIREEQ YDEALAVARQ QVENGAQIID INMDEAMLDS VACMHRFLNL IASEPDIARV PIMIDSSKWE VIETGLKCVQ GKAVVNSISM KEGEAAFREH ARLCRRYGAA VVVMAFDELG QADTLERRKE ICARAYRILV DEEGFPPEDI IFDPNVFAVA TGIDEHNHYA VDFIEGVRWI RENLPHARMS GGISNVSFSF RGNEPMREAI HTVFLYYAIR EGLTMGIVNA GQLGVYADLD PVLRDLVEDV VLDRAEPLGK KAADDERTPT ERLVQFADTI RGSGAKKEED LLWRAKTVEE RLAHALVHGI TTFIVEDTEE VRQKIAERGG RPIEVIEGPL MDGMNVVGDL FGAGKMFLPQ VVKSARVMKQ AVAHLVPFIE EEKRQIAAAG GDVRAKGKIV IATVKGDVHD IGKNIVSVVL QCNNFEVVNM GVMVPCAQIL DKAKEENADI IGLSGLITPS LEEMAYVASE MQRDPYFRDR KTPLMIGGAT TSRVHTAVKI APNYEGPVIY VPDASRSVGV ATSLMSDQAQ AYLDELAQEY EDVRRRHANR KATPLMPLAE ARAARPQIDW AAYTPPRPKF IGRRTFKSYD LAEIARYIDW GPFFMTWSLF GPFPAILDDK VVGEQARKVY ADGQAMLKRI IEGRWLTANG VVGFYPANRI NDEDIEVYRD ETRREVLFTY RNLRQQGVKR EGVSNKCLAD YIAPKDSGKL DYIGLFAVTA GLGIEKKEAE FDAALDDYSS IMLKSLADRL AEAFAECLHA RVRRDLWGYA ADETLDNEAM IAEKYVGIRP APGYPACPEH VVKTDMFRVL EAEDIGMELT ESYAMFPASS VSGFYFSHPD SQYFNVGPIG EDQLADYAAR SGRSEDDLRR TLAPNLGG // ID Q2LQ11_SYNAS Unreviewed; 618 AA. AC Q2LQ11; DT 21-FEB-2006, integrated into UniProtKB/TrEMBL. DT 21-FEB-2006, sequence version 1. DT 27-MAY-2015, entry version 72. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=SYN_00176 {ECO:0000313|EMBL:ABC75944.1}; OS Syntrophus aciditrophicus (strain SB). OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales; OC Syntrophaceae; Syntrophus. OX NCBI_TaxID=56780 {ECO:0000313|EMBL:ABC75944.1, ECO:0000313|Proteomes:UP000001933}; RN [1] {ECO:0000313|Proteomes:UP000001933} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SB {ECO:0000313|Proteomes:UP000001933}; RA Gunsalus R., Rohlin L., Kim U., Krupp R., Bhattacharyya A., RA Campbell J., Mclerney 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {ECO:0000256|RuleBase:RU004255}. CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ABC75944.1; -; Genomic_DNA. DR RefSeq; WP_011415979.1; NC_007759.1. DR RefSeq; YP_460112.1; NC_007759.1. DR ProteinModelPortal; Q2LQ11; -. DR STRING; 56780.SYN_00176; -. DR EnsemblBacteria; ABC75944; ABC75944; SYN_00176. DR KEGG; sat:SYN_00176; -. DR PATRIC; 23860473; VBISynAci70500_0068. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; SACI56780:GHXT-65-MONOMER; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000001933; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004255}; KW Complete proteome {ECO:0000313|Proteomes:UP000001933}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000001933}. SQ SEQUENCE 618 AA; 66375 MW; 471E13C142D92A0D CRC64; MSALQNVLSR MTGTPLIFDG AMGTMIYEKG VFIQTCYDEL CLTEPGLILG IHEQYAQAGA QVLETNSFGA NRIKLRAYGL AEKVADINRA AARLARQAAG TTLYVAGSVG PCTQGGQVIT GRDMAEVEAA FREQMEALTE EGVDLLLLET FSDLKELQLA ARVARERGVP VLASFAVDDD GETAAGTPAE KMAAALEKDP HVDVIGLNCG TGPAGIYEAL LKVLPVAGKP VIVMPNAGMP REIGGRTLYL ANPEYFTEYA KKFIELGVRG IGGCCGVHPA HIATAARAVR GLSGVRKHVE VTTRQQAPAQ KPAIPTAAKS RLAAKICSGQ KVTSVEILPP RAGDFSNMLA KVRRCHEAGV DAINIPDGPR ASARVSPMIT ALVILREVGI EPVVHYCCRD RNLIGMQSDL LGGYAVGLVN YLIITGDPPK LGNCPEATGV FDVDSIGLTS VVHNLNSGWD IGGSPVDPPT GIFIGVGANP CAVDLEREID RYFQKIEAGA EFAITQPVFD EKALFRFLDR VEKHSKRVPV LAGVWPLLSY RNAEFMNNEV PGVMVPREIL ERMARCETRE ESQRTGIEIA RAICEKIHER VAGFQVCAPL NNVEIALSVL RKGEGREI // ID Q2LWJ5_SYNAS Unreviewed; 813 AA. AC Q2LWJ5; DT 21-FEB-2006, integrated into UniProtKB/TrEMBL. DT 21-FEB-2006, sequence version 1. DT 27-MAY-2015, entry version 71. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:ABC78456.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABC78456.1}; GN ORFNames=SYN_02703 {ECO:0000313|EMBL:ABC78456.1}; OS Syntrophus aciditrophicus (strain SB). OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales; OC Syntrophaceae; Syntrophus. OX NCBI_TaxID=56780 {ECO:0000313|EMBL:ABC78456.1, ECO:0000313|Proteomes:UP000001933}; RN [1] {ECO:0000313|Proteomes:UP000001933} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SB {ECO:0000313|Proteomes:UP000001933}; RA Gunsalus R., Rohlin L., Kim U., Krupp R., Bhattacharyya A., RA Campbell J., Mclerney 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 ----------------------------------------------------------------------- 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; ABC78456.1; -; Genomic_DNA. DR RefSeq; WP_011418475.1; NC_007759.1. DR RefSeq; YP_462624.1; NC_007759.1. DR ProteinModelPortal; Q2LWJ5; -. DR STRING; 56780.SYN_02703; -. DR EnsemblBacteria; ABC78456; ABC78456; SYN_02703. DR KEGG; sat:SYN_02703; -. DR PATRIC; 23866016; VBISynAci70500_2789. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SACI56780:GHXT-2627-MONOMER; -. DR Proteomes; UP000001933; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001933}; KW Methyltransferase {ECO:0000313|EMBL:ABC78456.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001933}; KW Transferase {ECO:0000313|EMBL:ABC78456.1}. SQ SEQUENCE 813 AA; 86984 MW; 796F653B55C2BF7D CRC64; MKSKETIRRL LKKKILVLDG ATGTELQKRG MPGGVCPELW CLEHPEIIKE IHRSYRQAGS DIVYTCTFGA NRYKLAQYGT REVREINRNL ARLARHAVGP KALVAGDIGP TGHFVEPFGD LPFEEAVSAF KEQIQGLLEG GVDLFVIETM MDIQEARAAL IAVKETCPAF TVVTLTYENG GRTLNGTDPA TALITLQSLG ADAVGCNCST GPEAMLAFIE AMKPHATVPL AAKPNAGLPR LEGEETFFDM DAETFASHGP AFAAAGVNLL GGCCGTTPDH IQALAGTLQN APPRPPVRAA LSAVSSARSY RLLTRNEPLV IVGERLNPTG KKALQQELLA GKMSLVRQMT REQEQQKADL LDVNVGVPGL DEVKTIREVI SLLATATELP LVIDSSKVET IETALRLYPG RALINSISGE KKKCERLLPL AARYGAMFIL LPLADGEVPE TADRRIAIVR EVYGKARRLG FTKEDIVVDG LVMTAATNAN APAETLKTIA WCTDRFQAKT ILGISNVSFG LPERKWLNAA FLAMAQLSGL TMAIANPSME ELMALKRAAD VLTARDAQAS AYIAHFAGTA EGKKPAGTSA MQPPAPAGPE EKVRAAVLEG NRDDIGDLVE GALSAGFEAR SIVDDLLIPA IVQVGELFDR KVYFLPQLIA SAETMKKALA ILEPRLKSGG IPEKARGTVV MATVQGDIHD IGKNIVVLML KNHGFRVLDL GKDVPVETIL ETIRTENPDV VGLSALMTTT MVSMKTTIEQ ARSADLTCPF LIGGAVVTRS YADSIGAAYA RDGVEAVRVV EQLIGSAGGE LSK // ID Q2N881_ERYLH Unreviewed; 348 AA. AC Q2N881; DT 07-FEB-2006, integrated into UniProtKB/TrEMBL. DT 07-FEB-2006, sequence version 1. DT 27-MAY-2015, entry version 59. DE SubName: Full=Methionine synthase I cobalamin-binding domain {ECO:0000313|EMBL:ABC64110.1}; GN OrderedLocusNames=ELI_10090 {ECO:0000313|EMBL:ABC64110.1}; OS Erythrobacter litoralis (strain HTCC2594). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Erythrobacteraceae; Erythrobacter. OX NCBI_TaxID=314225 {ECO:0000313|EMBL:ABC64110.1, ECO:0000313|Proteomes:UP000008808}; RN [1] {ECO:0000313|Proteomes:UP000008808} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HTCC2594 {ECO:0000313|Proteomes:UP000008808}; 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; ABC64110.1; -; Genomic_DNA. DR RefSeq; WP_011414937.1; NC_007722.1. DR RefSeq; YP_458907.1; NC_007722.1. DR STRING; 314225.ELI_10090; -. DR EnsemblBacteria; ABC64110; ABC64110; ELI_10090. DR KEGG; eli:ELI_10090; -. DR PATRIC; 21861173; VBIEryLit102657_2008. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; ELIT314225:GHLE-2053-MONOMER; -. DR Proteomes; UP000008808; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008808}; KW Reference proteome {ECO:0000313|Proteomes:UP000008808}. SQ SEQUENCE 348 AA; 37170 MW; C3E2CB2CC40B4E81 CRC64; MSALAKLREA AAANILIKDG PYGTEIQRAK LAAEDYAGDT GLVQDQKGNN DLVNLTQPQV IRTICDSYIA AGATVLATNT FNANRISQAD YGAEGLVHDI NASAARIIRE ACDDATAKDG IPRFVCGAMG PTNKTLSLSP DVEDPGFREV TFDEIVDVYR EQAAALLEGG AEFILIETVF DTLNCKAAIM AVKQLERERG EEIPLMISLT LTDLSGRNLS GHTVEAFWNT VRHAKPATIG LNCSFGAEQL RPHVQILSNI ADTLLMAYPN AGLPNDLGEY DEMPETTASL LKVWAENGRA NILGGCCGST PEHIAAIAQT VKGVEPRQVP DAVSEMRLAG LEPFSVAA // ID Q2QME6_ORYSJ Unreviewed; 342 AA. AC Q2QME6; DT 24-JAN-2006, integrated into UniProtKB/TrEMBL. DT 11-JUL-2006, sequence version 2. DT 01-APR-2015, entry version 74. DE SubName: Full=Homocysteine S-methyltransferase 3 {ECO:0000313|EMBL:AFI71275.1}; DE SubName: Full=Homocysteine S-methyltransferase 3, putative, expressed {ECO:0000313|EMBL:ABA99257.2}; DE SubName: Full=Os12g0607000 protein {ECO:0000313|EMBL:BAF30251.1}; GN OrderedLocusNames=LOC_Os12g41390 {ECO:0000313|EMBL:ABA99257.2}, GN Os12g0607000 {ECO:0000313|EMBL:BAF30251.1}; GN ORFNames=OsJ_36805 {ECO:0000313|EMBL:EAZ21157.1}; 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 {ECO:0000313|EMBL:ABA99257.2, ECO:0000313|Proteomes:UP000000763}; RN [1] {ECO:0000313|EMBL:ABA99257.2, ECO:0000313|Proteomes:UP000000763} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000000763}; 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] {ECO:0000313|Proteomes:UP000000763} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000000763}; 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] {ECO:0000313|EMBL:BAF30251.1} RP NUCLEOTIDE SEQUENCE. RG International Rice Genome Sequencing Project; RA Matsumoto T., Wu J., Kanamori H., Katayose Y., Fujisawa M., Namiki N., RA Mizuno H., Yamamoto K., Antonio B.A., Baba T., Sakata K., Nagamura Y., RA Aoki H., Arikawa K., Arita K., Bito T., Chiden Y., Fujitsuka N., RA Fukunaka R., Hamada M., Harada C., Hayashi A., Hijishita S., Honda M., RA Hosokawa S., Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., RA Ito K., Ito S., Ito T., Ito Y., Ito Y., Iwabuchi A., Kamiya K., RA Karasawa W., Kurita K., Katagiri S., Kikuta A., Kobayashi H., RA Kobayashi N., Machita K., Maehara T., Masukawa M., Mizubayashi T., RA Mukai Y., Nagasaki H., Nagata Y., Naito S., Nakashima M., Nakama Y., RA Nakamichi Y., Nakamura M., Meguro A., Negishi M., Ohta I., Ohta T., RA Okamoto M., Ono N., Saji S., Sakaguchi M., Sakai K., Shibata M., RA Shimokawa T., Song J., Takazaki Y., Terasawa K., Tsugane M., Tsuji K., RA Ueda S., Waki K., Yamagata H., Yamamoto M., Yamamoto S., Yamane H., RA Yoshiki S., Yoshihara R., Yukawa K., Zhong H., Yano M., Yuan Q., RA Ouyang S., Liu J., Jones K.M., Gansberger K., Moffat K., Hill J., RA Bera J., Fadrosh D., Jin S., Johri S., Kim M., Overton L., Reardon M., RA Tsitrin T., Vuong H., Weaver B., Ciecko A., Tallon L., Jackson J., RA Pai G., Aken S.V., Utterback T., Reidmuller S., Feldblyum T., RA Hsiao J., Zismann V., Iobst S., de Vazeille A.R., Buell C.R., Ying K., RA Li Y., Lu T., Huang Y., Zhao Q., Feng Q., Zhang L., Zhu J., Weng Q., RA Mu J., Lu Y., Fan D., Liu Y., Guan J., Zhang Y., Yu S., Liu X., RA Zhang Y., Hong G., Han B., Choisne N., Demange N., Orjeda G., RA Samain S., Cattolico L., Pelletier E., Couloux A., Segurens B., RA Wincker P., D'Hont A., Scarpelli C., Weissenbach J., Salanoubat M., RA Quetier F., Yu Y., Kim H.R., Rambo T., Currie J., Collura K., Luo M., RA Yang T., Ammiraju J.S.S., Engler F., Soderlund C., Wing R.A., RA Palmer L.E., de la Bastide M., Spiegel L., Nascimento L., Zutavern T., RA O'Shaughnessy A., Dike S., Dedhia N., Preston R., Balija V., RA McCombie W.R., Chow T., Chen H., Chung M., Chen C., Shaw J., Wu H., RA Hsiao K., Chao Y., Chu M., Cheng C., Hour A., Lee P., Lin S., Lin Y., RA Liou J., Liu S., Hsing Y., Raghuvanshi S., Mohanty A., Bharti A.K., RA Gaur A., Gupta V., Kumar D., Ravi V., Vij S., Kapur A., Khurana P., RA Khurana P., Khurana J.P., Tyagi A.K., Gaikwad K., Singh A., Dalal V., RA Srivastava S., Dixit A., Pal A.K., Ghazi I.A., Yadav M., Pandit A., RA Bhargava A., Sureshbabu K., Batra K., Sharma T.R., Mohapatra T., RA Singh N.K., Messing J., Nelson A.B., Fuks G., Kavchok S., Keizer G., RA Linton E., Llaca V., Song R., Tanyolac B., Young S., Ho-Il K., RA Hahn J.H., Sangsakoo G., Vanavichit A., de Mattos Luiz.A.T., RA Zimmer P.D., Malone G., Dellagostin O., de Oliveira A.C., Bevan M., RA Bancroft I., Minx P., Cordum H., Wilson R., Cheng Z., Jin W., RA Jiang J., Leong S.A., Iwama H., Gojobori T., Itoh T., Niimura Y., RA Fujii Y., Habara T., Sakai H., Sato Y., Wilson G., Kumar K., RA McCouch S., Juretic N., Hoen D., Wright S., Bruskiewich R., Bureau T., RA Miyao A., Hirochika H., Nishikawa T., Kadowaki K., Sugiura M., RA Burr B., Sasaki T.; RT "The map-based sequence of the rice genome."; RL Nature 436:793-800(2005). RN [4] {ECO:0000313|EMBL:EAZ21157.1, ECO:0000313|Proteomes:UP000000763} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000000763}; 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] {ECO:0000313|EMBL:BAF30251.1} RP NUCLEOTIDE SEQUENCE. RG IRGSP(International Rice Genome Sequencing Project); RT "Oryza sativa nipponbare(GA3) genomic DNA, chromosome 12."; RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000313|EMBL:BAF30251.1} RP NUCLEOTIDE SEQUENCE. RG The Rice Annotation Project (RAP); RT "The Second Rice Annotation Project Meeting (RAP2)."; RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000313|EMBL:ABA99257.2} 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 [8] {ECO:0000313|EMBL:BAF30251.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=16381971; DOI=10.1093/nar/gkj094; RA Ohyanagi H., Tanaka T., Sakai H., Shigemoto Y., Yamaguchi K., RA Habara T., Fujii Y., Antonio B.A., Nagamura Y., Imanishi T., Ikeo K., RA Itoh T., Gojobori T., Sasaki T.; RT "The Rice Annotation Project Database (RAP-DB): hub for Oryza sativa RT ssp. japonica genome information."; RL Nucleic Acids Res. 34:D741-D744(2006). RN [9] {ECO:0000313|EMBL:ABA99257.2} RP NUCLEOTIDE SEQUENCE. RA Buell R.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [10] {ECO:0000313|EMBL:EAZ21157.1} 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 [11] {ECO:0000313|EMBL:BAF30251.1} RP NUCLEOTIDE SEQUENCE. RG The Rice Annotation Project (RAP); RA Itoh T., Tanaka T., Barrero R.A., Yamasaki C., Fujii Y., Hilton P.B., RA Antonio B.A., Aono H., Apweiler R., Bruskiewich R., Bureau T., RA Burr F., Costa de Oliveira A., Fuks G., Habara T., Haberer G., Han B., RA Harada E., Hiraki A.T., Hirochika H., Hoen D., Hokari H., Hosokawa S., RA Hsing Y., Ikawa H., Ikeo K., Imanishi T., Ito Y., Jaiswal P., RA Kanno M., Kawahara Y., Kawamura T., Kawashima H., Khurana J.P., RA Kikuchi S., Komatsu S., Koyanagi K.O., Kubooka H., Lieberherr D., RA Lin Y.C., Lonsdale D., Matsumoto T., Matsuya A., McCombie W.R., RA Messing J., Miyao A., Mulder N., Nagamura Y., Nam J., Namiki N., RA Numa H., Nurimoto S., O'donovan C., Ohyanagi H., Okido T., Oota S., RA Osato N., Palmer L.E., Quetier F., Raghuvanshi S., Saichi N., RA Sakai H., Sakai Y., Sakata K., Sakurai T., Sato F., Sato Y., RA Schoof H., Seki M., Shibata M., Shimizu Y., Shinozaki K., Shinso Y., RA Singh N.K., Smith-White B., Takeda J., Tanino M., Tatusova T., RA Thongjuea S., Todokoro F., Tsugane M., Tyagi A.K., Vanavichit A., RA Wang A., Wing R.A., Yamaguchi K., Yamamoto M., Yamamoto N., Yu Y., RA Zhang H., Zhao Q., Higo K., Burr B., Gojobori T., Sasaki T.; RT "Curated Genome Annotation of Oryza sativa ssp. japonica and RT Comparative Genome Analysis with Arabidopsis thaliana."; RL Genome Res. 17:175-183(2007). RN [12] {ECO:0000313|Proteomes:UP000000763} RP GENOME REANNOTATION. RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000000763}; 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 [13] {ECO:0000313|EMBL:BAF30251.1} RP NUCLEOTIDE SEQUENCE. RG The Rice Annotation Project (RAP); RA Tanaka T., Antonio B.A., Kikuchi S., Matsumoto T., Nagamura Y., RA Numa H., Sakai H., Wu J., Itoh T., Sasaki T., Aono R., Fujii Y., RA Habara T., Harada E., Kanno M., Kawahara Y., Kawashima H., Kubooka H., RA Matsuya A., Nakaoka H., Saichi N., Sanbonmatsu R., Sato Y., Shinso Y., RA Suzuki M., Takeda J., Tanino M., Todokoro F., Yamaguchi K., RA Yamamoto N., Yamasaki C., Imanishi T., Okido T., Tada M., Ikeo K., RA Tateno Y., Gojobori T., Lin Y.C., Wei F.J., Hsing Y.I., Zhao Q., RA Han B., Kramer M.R., McCombie R.W., Lonsdale D., O'Donovan C.C., RA Whitfield E.J., Apweiler R., Koyanagi K.O., Khurana J.P., RA Raghuvanshi S., Singh N.K., Tyagi A.K., Haberer G., Fujisawa M., RA Hosokawa S., Ito Y., Ikawa H., Shibata M., Yamamoto M., RA Bruskiewich R.M., Hoen D.R., Bureau TE., Namiki N., Ohyanagi H., RA Sakai Y., Nobushima S., Sakata K., Barrero R.A., Sato Y., Souvorov A., RA Smith-White B., Tatusova T., An S., An G., OOta S., Fuks G., RA Messing J., Christie K.R., Lieberherr D., Kim H., Zuccolo A., RA Wing R.A., Nobuta K., Green P.J., Lu C., Meyers BC., Chaparro C., RA Piegu B., Panaud O., Echeverria M.; RT "The Rice Annotation Project Database (RAP-DB): 2008 update."; RL Nucleic Acids Res. 36:D1028-D1033(2008). RN [14] {ECO:0000313|EMBL:EAZ21157.1} 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. RN [15] {ECO:0000313|EMBL:AFI71275.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Immature seed {ECO:0000313|EMBL:AFI71275.1}; RA Yoon U.H.; RT "Structural and expression analysis of immature seed genes in Oryza RT sativa L."; 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; DP000011; ABA99257.2; -; Genomic_DNA. DR EMBL; JN944364; AFI71275.1; -; mRNA. DR EMBL; AP008218; BAF30251.1; -; Genomic_DNA. DR EMBL; CM000149; EAZ21157.1; -; Genomic_DNA. DR RefSeq; NP_001067232.1; NM_001073764.1. DR UniGene; Os.6156; -. DR PRIDE; Q2QME6; -. DR EnsemblPlants; OS12T0607000-02; OS12T0607000-02; OS12G0607000. DR GeneID; 4352747; -. DR KEGG; osa:4352747; -. DR Gramene; Q2QME6; -. DR eggNOG; COG2040; -. DR InParanoid; Q2QME6; -. DR KO; K00547; -. DR OMA; SEWCKDG; -. DR Proteomes; UP000000763; Chromosome 12. DR ExpressionAtlas; Q2QME6; baseline. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Complete proteome {ECO:0000313|Proteomes:UP000000763}; KW Methyltransferase {ECO:0000313|EMBL:ABA99257.2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000763}; KW Transferase {ECO:0000313|EMBL:ABA99257.2}. SQ SEQUENCE 342 AA; 36828 MW; DBDE28B9082746C5 CRC64; MVGKSGVAEE GGAAAAAAVR RWVEAGGGRL VMDGGLATEL EANGADLNDP LWSAKCLLSS PHLVRKVHLD YLEAGANIII TASYQATIQG FESKGFSKEQ SEDLLAKSVE IAREARDMFL KEHSDRPIQH PILVAASIGS YGAYLADGSE YSGDYGEAGT LEFLKDFHKR RLEVLAEAGP DLIAFETIPN KLEAQAYVEL LDECNISIPA WFSFNSKDGV HIVSGDSLIE CATIANGCSK VGAVGINCTP PRFIHGLILS IRKVTDKPIL IYPNSGERYD AEKKEWVEST GVSDGDFVSY VNEWCKDGAV LIGGCCRTTP NTIKAISRSL NQRHSSLHLP VA // ID Q2QME7_ORYSJ Unreviewed; 304 AA. AC Q2QME7; DT 24-JAN-2006, integrated into UniProtKB/TrEMBL. DT 24-JAN-2006, sequence version 1. DT 01-APR-2015, entry version 41. DE SubName: Full=Homocysteine S-methyltransferase 3, putative, expressed {ECO:0000313|EMBL:ABA99258.1}; DE SubName: Full=cDNA clone:J033125A08, full insert sequence {ECO:0000313|EMBL:BAG95998.1}; GN OrderedLocusNames=LOC_Os12g41390 {ECO:0000313|EMBL:ABA99258.1}; 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 {ECO:0000313|EMBL:ABA99258.1, ECO:0000313|Proteomes:UP000000763}; RN [1] {ECO:0000313|EMBL:BAG95998.1} 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] {ECO:0000313|EMBL:ABA99258.1, ECO:0000313|Proteomes:UP000000763} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000000763}; 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 [3] {ECO:0000313|EMBL:ABA99258.1} 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 [4] {ECO:0000313|EMBL:ABA99258.1} 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; ABA99258.1; -; Genomic_DNA. DR EMBL; AK103293; BAG95998.1; -; mRNA. DR Gramene; Q2QME7; -. DR HOGENOM; HOG000265278; -. DR ExpressionAtlas; Q2QME7; baseline. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Methyltransferase {ECO:0000313|EMBL:ABA99258.1}; KW Transferase {ECO:0000313|EMBL:ABA99258.1}. SQ SEQUENCE 304 AA; 32518 MW; AD8E9B77198FF76E CRC64; MVGKSGVAEE GGAAAAAAVR RWVEAGGGRL VMDGGLATEL EANGADLNDP LWSAKCLLSS PHLVRKVHLD YLEAGANIII TASYQATIQG FESKGFSKEQ SEDLLAKSVE IAREARDMFL KEHSDRPIQH PILVAASIGS YGAYLADGSE YSGDYGEAGT LEFLKDFHKR RLEVLAEAGP DLIAFETIPN KLEAQAYVEL LDECNISIPA WFSFNSKDGV HIVSGDSLIE CATIANGCSK VGAVGINCTP PRFIHGLILS IRKVCSCTCF SGSETCLSSV SYVLVKESCF LLVCACTNYI KHAD // ID Q2QME8_ORYSJ Unreviewed; 156 AA. AC Q2QME8; DT 24-JAN-2006, integrated into UniProtKB/TrEMBL. DT 11-JUL-2006, sequence version 2. DT 29-OCT-2014, entry version 35. DE SubName: Full=Homocysteine S-methyltransferase 3, putative, expressed {ECO:0000313|EMBL:ABA99259.2}; GN OrderedLocusNames=LOC_Os12g41390 {ECO:0000313|EMBL:ABA99259.2}; 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 {ECO:0000313|EMBL:ABA99259.2, ECO:0000313|Proteomes:UP000000763}; RN [1] {ECO:0000313|EMBL:ABA99259.2, ECO:0000313|Proteomes:UP000000763} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000000763}; 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). CC ----------------------------------------------------------------------- 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; ABA99259.2; -; Genomic_DNA. DR UniGene; Os.6156; -. DR STRING; 39947.LOC_Os12g41390.1; -. DR Gramene; Q2QME8; -. DR ExpressionAtlas; Q2QME8; baseline. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:ABA99259.2}; KW Transferase {ECO:0000313|EMBL:ABA99259.2}. SQ SEQUENCE 156 AA; 16639 MW; FAE9649A2B107F76 CRC64; MVGKSGVAEE GGAAAAAAVR RWVEAGGGRL VMDGGLATEL EANGADLNDP LWSAKCLLSS PHLVRKVHLD YLEAGANIII TASYQATIQG FESKGFSKEQ SEDLLAKSVE IAREARDMFL KEHSDRPIQH PILVAASIGS YGAYLADGSE YRYLTT // ID Q2RU64_RHORT Unreviewed; 1182 AA. AC Q2RU64; DT 24-JAN-2006, integrated into UniProtKB/TrEMBL. DT 24-JAN-2006, sequence version 1. DT 27-MAY-2015, entry version 77. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABC22331.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABC22331.1}; GN OrderedLocusNames=Rru_A1531 {ECO:0000313|EMBL:ABC22331.1}; OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG OS 4362 / NCIB 8255 / S1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Rhodospirillum. OX NCBI_TaxID=269796 {ECO:0000313|EMBL:ABC22331.1, ECO:0000313|Proteomes:UP000001929}; RN [1] {ECO:0000313|Proteomes:UP000001929} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1 RC {ECO:0000313|Proteomes:UP000001929}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000230; ABC22331.1; -; Genomic_DNA. DR RefSeq; WP_011389284.1; NC_007643.1. DR RefSeq; YP_426618.1; NC_007643.1. DR ProteinModelPortal; Q2RU64; -. DR STRING; 269796.Rru_A1531; -. DR EnsemblBacteria; ABC22331; ABC22331; Rru_A1531. DR GeneID; 3834946; -. DR KEGG; rru:Rru_A1531; -. DR PATRIC; 23326690; VBIRhoRub82919_1601. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; RRUB269796:GCN1-1554-MONOMER; -. DR Proteomes; UP000001929; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001929}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABC22331.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001929}; KW Transferase {ECO:0000313|EMBL:ABC22331.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 730 730 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1182 AA; 129333 MW; 355660926D8AD6AD CRC64; MSRFLDHLRN RVLLCDGGMG SLVQAMDLSV DGDFMGRENC TEVLNLSRPD VVRDIHTRYF AAGADCVETN TFGGSTLTLA EFDLADRTRE INRRAAEIAR EAAESFADGR DRFVLGSIGP GTKLPSLGHI DYDTLKDAIT VQCEGLIEGG ADAILVETCQ DPLQFKAAIN AAKAARLALG SDTAILLQVT VETTGTLLVG ADIAAAATVA HALGVDSLGL NCATGPQEMS EHVRWLKENW PGLISLQPNA GLPELLDGKT HYPLTPAELA DWHGRFIRED GVNLIGGCCG TTPDHIAAVN AMLETLGQGR RPAPVKRSVH WVPSVASLYG AVPMRQENAF LSIGERCNAN GSKKFRTFQD NEDWDAIVGM AREQVKEGSH TLDVCTAFVG RKEGADMTEV VSRLRGGVNA PLVIDSTETP VLTQALKLYG GKAIINSINF EDGEESAAQR LALAREFGAA VIALTIDEEG MAKDAEAKLR IAHRLYDFAV TQHGLPASDL MFDPLTFTIC TGNTDDRRLG LETLDAIRRI RTELPECQII LGLSNISFGL KPVARHVLNS VFLDKAVEAG MTGAIVHISK ILPLHKIPAD EVKAAEDLIF DRRAPGYDPL HAFIALFEDR SETKVAVKRA ETVEERLKQR IVDGDRLGLD ADLTEAMGKY PPLEIINSLL LDGMKVVGEL FGAGKMQLPF VLQSAETMKA AVAFLEPHME KIEGQEKGII VLATVKGDVH DIGKNLVDII LSNNGYKVIN IGIKQPIAAI LASARENRAD AIGMSGLLVK STVIMKDNLE EMAREGWNTP VLLGGAALTR AFVEEDCVSA YAGSGRVAYA RDAFDGLDLM AKVAEGRFDT HLSAVQQKRA GRPSRRPKAP PLWPANDPSS KIAPRTLDDQ DTAIHKISER PVDAEEILLR RAELARDHVV PTPPFWGAKV LESISLKSLV PYINEATLFQ FQWGFRKGGR TREEWKDWAA SEIRPIMFDM LKTCAQEEIL KPRAVYGFWK AASQGDAIVL FAEDGTTEVG RFDLPRQTIE GGICLADFVR DIDSGERDVI ALQAVTVGAR ASDVCRDWFA ANRYKDYLYL HGISVEVAEA MAEYVHKRIR AELGFAAEEA RDIERMIKQE YRGSRYSFGY PACPNLGDQR QLLDLLGAER IELDLSDEDE LVPEQSTSAL VLLHPQAKYF RI // ID Q2S678_SALRD Unreviewed; 320 AA. AC Q2S678; DT 24-JAN-2006, integrated into UniProtKB/TrEMBL. DT 24-JAN-2006, sequence version 1. DT 29-APR-2015, entry version 59. DE SubName: Full=Vitamin B12-dependent methionine synthase family protein {ECO:0000313|EMBL:ABC44869.1}; GN OrderedLocusNames=SRU_0150 {ECO:0000313|EMBL:ABC44869.1}; OS Salinibacter ruber (strain DSM 13855 / M31). OC Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis; OC Rhodothermaceae; Salinibacter. OX NCBI_TaxID=309807 {ECO:0000313|EMBL:ABC44869.1, ECO:0000313|Proteomes:UP000008674}; RN [1] {ECO:0000313|EMBL:ABC44869.1, ECO:0000313|Proteomes:UP000008674} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13855 / M31 {ECO:0000313|Proteomes:UP000008674}; 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; ABC44869.1; -; Genomic_DNA. DR RefSeq; WP_011402936.1; NC_007677.1. DR RefSeq; YP_444303.1; NC_007677.1. DR STRING; 309807.SRU_0150; -. DR EnsemblBacteria; ABC44869; ABC44869; SRU_0150. DR GeneID; 3850658; -. DR KEGG; sru:SRU_0150; -. DR PATRIC; 23422621; VBISalRub86502_0162. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; QPEVMAA; -. DR OrthoDB; EOG6Q5NS7; -. DR PhylomeDB; Q2S678; -. DR BioCyc; SRUB309807:GJJD-150-MONOMER; -. DR Proteomes; UP000008674; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008674}; KW Reference proteome {ECO:0000313|Proteomes:UP000008674}. SQ SEQUENCE 320 AA; 33749 MW; 21B815A61746E48F CRC64; MRDLSTRLSG GPVLLDGGLG QELIRRGMPS TEPSLWSANA LTEAPDLVQE VHEEYLRAGA DVITTNTYAT PPERLSEAGL DGRAEALNRE AGRLAERARA AVGRDALIAG SLPPIRGSYR PDLVGEAGEI EPQYREQAGY LAPHVDLFLC ETMSTPGEAR AAARGAASTG LPVLVSYTIA DPSSPEDAEP RLHNGESLEE AVEALSGLPV AGVLLNCSHP ESISAAVPVL RQLTDRAVGA YANAFTHIPD GFDERADALD SDARPDRRED LAPEAYGRHV EDWLSAGANI VGGCCEVGPG HIAHLRTTVD GAADARRAAE // ID Q2SJ31_HAHCH Unreviewed; 1235 AA. AC Q2SJ31; DT 24-JAN-2006, integrated into UniProtKB/TrEMBL. DT 24-JAN-2006, sequence version 1. DT 27-MAY-2015, entry version 74. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:ABC29343.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABC29343.1}; GN Name=metH {ECO:0000313|EMBL:ABC29343.1}; GN OrderedLocusNames=HCH_02542 {ECO:0000313|EMBL:ABC29343.1}; OS Hahella chejuensis (strain KCTC 2396). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Hahellaceae; Hahella. OX NCBI_TaxID=349521 {ECO:0000313|EMBL:ABC29343.1, ECO:0000313|Proteomes:UP000000238}; RN [1] {ECO:0000313|EMBL:ABC29343.1, ECO:0000313|Proteomes:UP000000238} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KCTC 2396 {ECO:0000313|EMBL:ABC29343.1, RC ECO:0000313|Proteomes:UP000000238}; 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., RA Hur C.-G., Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., RA Park H.-S., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000155; ABC29343.1; -; Genomic_DNA. DR RefSeq; WP_011396412.1; NC_007645.1. DR RefSeq; YP_433768.1; NC_007645.1. DR ProteinModelPortal; Q2SJ31; -. DR STRING; 349521.HCH_02542; -. DR EnsemblBacteria; ABC29343; ABC29343; HCH_02542. DR KEGG; hch:HCH_02542; -. DR PATRIC; 22085914; VBIHahChe29232_2335. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; QPFFNAW; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; HCHE349521:GHAL-2450-MONOMER; -. DR Proteomes; UP000000238; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000238}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABC29343.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000238}; KW Transferase {ECO:0000313|EMBL:ABC29343.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1235 AA; 137513 MW; 176D11A862628066 CRC64; MLTRIQRVEA LNDSLKKRIL ILDGAMGTMI QRYKLEEADY RGERFKDFHR DIKGNNDLLC LTQPHIIQAI HKAYLDAGAD IIETNSFNAT WVSQAEYGLE DIVYELNVAS AQVARAAADE KTAETPDIPR FVAGVLGPTS RTASISPDVN NPGYRNVDFQ TLVDNYYEAT KGLVDGGSDI ILIETIFDTL NAKACIYAVQ QYFDDHGVEL PIMISGTITD ASGRTLSGQT AEAFWNSVAH SRPISIGLNC ALGADALRPY VEELSNRATT YISAHPNAGL PNEFGEYDQT PEEMAAIVEG FAQDGFVNII GGCCGTTPDH IAAIKKAVEK HAPRAIPDIT PRLRLSGLEP FTLTDEIRFV NVGERTNVTG SRRFLRLIKE ECYEEALDVA RDQVENGAQV IDINMDEGML ESADAMKLFL NLIASEPDIS KVPIMVDSSK WEVIEAGLRC IQGKAVVNSI SLKEGEADFI AKAKSCMRYG AAVVVMAFDE AGQADTYERK TEICKRSYDI LVGLGYPPQD IIFDPNIFAI ATGIEEHNNY AVDFIQATRW IRQNLPYANV SGGVSNVSFS FRGNDTVREA IHSVFLFHAI NAGMNMGIVN PAQLVIYDEI PAELKELVED VVLNKHPDAT ERLLEAAERY RSTGEKKQEE SQEWRSWPVT KRLEHALVKG INAYITEDTE EARLAAARPI EVIEGPLMDG MNVVGDLFGS GKMFLPQVVK SARVMKQAVA HLIPYIEQEK DAKEKAKGRI LMATVKGDVH DIGKNIVGVV LQCNNYEVID LGVMVPCEKI LQVAKEENVD IIGLSGLITP SLDEMVHVAR EMQRLNFKIP LLIGGATTSK AHTAVKIEPE YKNDVTVYVT DASRSVSVAT RLMSDTQKAD YVQNIRTEYE DVRERRKNRE PSAKPIPLVA ARDNRFQGDW SDYTPPAPTF TGVKVFDDYP LQELVDYVDW TPFFISWDLA GKYPRILEDE KVGEAARQLF QDAQKMLSHI IDNNLLKARA VVGIWPSNRI SDEDTVLYTD ESKSAPLTTL SHLRQQTQRE QNRPNYSLAD FVAPVESGKD DYIGAFVVTA GIGAEELAKQ YESQHDDYSS IMVKALADRL AEAFAERMHE RVRKEFWGYA SSEQLDNEAL IKEKYAGIRP APGYPACPDH TEKAKLFSVL EAELHTGVKL TEHYAMYPAA SVSGWYFSHP EARYFAVGKI QRDQVEDYAA RKGMTLQEAE RWLSPNLGYD PSSAR // ID Q2T1N3_BURTA Unreviewed; 358 AA. AC Q2T1N3; DT 24-JAN-2006, integrated into UniProtKB/TrEMBL. DT 24-JAN-2006, sequence version 1. DT 27-MAY-2015, entry version 58. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:AIP26983.1}; DE SubName: Full=Homocysteine S-methyltransferase, putative {ECO:0000313|EMBL:ABC38013.1}; GN OrderedLocusNames=BTH_I0358 {ECO:0000313|EMBL:ABC38013.1}; GN ORFNames=DR63_2138 {ECO:0000313|EMBL:AIP26983.1}; 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 {ECO:0000313|EMBL:ABC38013.1, ECO:0000313|Proteomes:UP000001930}; RN [1] {ECO:0000313|EMBL:ABC38013.1, ECO:0000313|Proteomes:UP000001930} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=E264 {ECO:0000313|EMBL:ABC38013.1}, and RC E264 / ATCC 700388 / DSM 13276 / CIP 106301 RC {ECO:0000313|Proteomes:UP000001930}; 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). RN [2] {ECO:0000313|EMBL:ABC38013.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=E264; RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., RA Lathigra R., White O., Ketchum K.A., Palmer N., Dodson R., RA Hickey E.K., Gwinn M., Dougherty B., Fleischmann R.D., Richardson D., RA Peterson J., Kerlavage A.R., Quackenbush J., Salzberg S., Hanson M., RA van-Vugt R., Adams M.D., Gocayne J.D., Weidman J., Utterback T., RA Watthey L., McDonald L., Artiach P., Bowman C., Garland S., Fujii C., RA Cotton M.D., Horst K., Tomb J.-F., Roberts K., Hatch B., Smith H.O., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:AIP26983.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=E264 {ECO:0000313|EMBL:AIP26983.1}; RA Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O., Coyne S.R., RA Daligault H.E., Davenport K.W., Erkkila T., Frey K.G., Gibbons H.S., RA Gu W., Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C., RA Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N., RA Scholz M.B., Teshima H., Xu Y.; RL Submitted (JUN-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; CP000086; ABC38013.1; -; Genomic_DNA. DR EMBL; CP008785; AIP26983.1; -; Genomic_DNA. DR RefSeq; WP_009893253.1; NZ_CM000438.1. DR STRING; 271848.BTH_I0358; -. DR EnsemblBacteria; ABC38013; ABC38013; BTH_I0358. DR KEGG; bte:BTH_I0358; -. DR PATRIC; 19303414; VBIBurTha36512_3026. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; BTHA271848:GJMY-358-MONOMER; -. DR Proteomes; UP000001930; Chromosome I. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001930}; KW Methyltransferase {ECO:0000313|EMBL:ABC38013.1}; KW Transferase {ECO:0000313|EMBL:ABC38013.1}. SQ SEQUENCE 358 AA; 38406 MW; 6D0B002A87556326 CRC64; MSEPKPIAPS APSALAASYT RGAALPRLLQ QRILILDGAM GTMIQRYKLD EAAYRSERFK DFPRDVKGNN ELLSITQPQI IREIHDQYFA AGADIVETNT FGATAVAQAD YGMEDLAVEM NVASATLARE SAAKYATPDK PRFVAGAIGP TPKTASISPD VNDPGARNVT FDELRDAYYT QAKALLDGGV DLFLVETIFD TLNAKAALFA LDQLFEDTGE RLPIMISGTV TDASGRILSG QTVEAFWNSL RHARPLTFGL NCALGAALMR PYIAELAKLC DTYVSCYPNA GLPNPMSDTG FDETPDVTSG LLKEFAQAGL VNVAGGCCGT TPEHIAAIAK ALAEVKPRRW PSQYSEAA // ID Q2TXK9_ASPOR Unreviewed; 376 AA. AC Q2TXK9; DT 24-JAN-2006, integrated into UniProtKB/TrEMBL. DT 24-JAN-2006, sequence version 1. DT 07-JAN-2015, entry version 43. DE SubName: Full=Predicted protein {ECO:0000313|EMBL:BAE66014.1}; GN ORFNames=AO090010000103 {ECO:0000313|EMBL:BAE66014.1}; 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 {ECO:0000313|EMBL:BAE66014.1, ECO:0000313|Proteomes:UP000006564}; RN [1] {ECO:0000313|Proteomes:UP000006564} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 42149 / RIB 40 {ECO:0000313|Proteomes:UP000006564}; 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; AP007175; BAE66014.1; -; Genomic_DNA. DR RefSeq; XP_001827147.1; XM_001827095.2. DR ProteinModelPortal; Q2TXK9; -. DR STRING; 5062.CADAORAP00004142; -. DR EnsemblFungi; CADAORAT00004215; CADAORAP00004142; CADAORAG00004215. DR GeneID; 5999281; -. DR KEGG; aor:AOR_1_176024; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000006564; Chromosome 8. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 2. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006564}; KW Reference proteome {ECO:0000313|Proteomes:UP000006564}. SQ SEQUENCE 376 AA; 41665 MW; 9F27EBB967B87FC8 CRC64; MTTRQLPILL LDGGLGTTLG DPPHNITFTA ETPLWSAHLL ISSPSTLEEV HKAFATVGAD IILTATYQTS FEGFTLTDPR YTADDAAHFM RSAIPLARRA GSSSGRTVKV ALSLGPYGAT MSPVGAEYTG LYPEEMNSEA KLREWHARRL CVFVDETGSW DNFEYIAFET VRRADEVKAI RGAMSDVLAD MYQGQGPDSE KNQLAMGKKP WWICGVFPDE EVDEEDVRAW VRAAVGTQEG ETGVYLPRPW GIGVNCTRIG NVGRIVSIMQ DELRNLEDLR TKGYVDEWNS VTGKPWLVLY PDGTNGEKYD PVTKTWVATE TGKETRPWHE IYWDVVQGLP EGAWEGIVMG GCCRAGPEQI ATLRRRIDER SNAQGV // ID Q2WA92_MAGSA Unreviewed; 1172 AA. AC Q2WA92; DT 10-JAN-2006, integrated into UniProtKB/TrEMBL. DT 10-JAN-2006, sequence version 1. DT 27-MAY-2015, entry version 78. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:BAE49233.1}; GN OrderedLocusNames=amb0429 {ECO:0000313|EMBL:BAE49233.1}; OS Magnetospirillum magneticum (strain AMB-1 / ATCC 700264). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Magnetospirillum. OX NCBI_TaxID=342108 {ECO:0000313|Proteomes:UP000007058}; RN [1] {ECO:0000313|EMBL:BAE49233.1, ECO:0000313|Proteomes:UP000007058} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AMB-1 / ATCC 700264 {ECO:0000313|Proteomes:UP000007058}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP007255; BAE49233.1; -; Genomic_DNA. DR RefSeq; WP_011382873.1; NC_007626.1. DR RefSeq; YP_419792.1; NC_007626.1. DR ProteinModelPortal; Q2WA92; -. DR STRING; 342108.amb0429; -. DR EnsemblBacteria; BAE49233; BAE49233; amb0429. DR KEGG; mag:amb0429; -. DR PATRIC; 22435148; VBIMagMag129836_0442. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; MMAG342108:GJNU-433-MONOMER; -. DR Proteomes; UP000007058; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007058}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAE49233.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007058}; KW Transferase {ECO:0000313|EMBL:BAE49233.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 238 238 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 743 743 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1172 AA; 127578 MW; B37B9397CE800B37 CRC64; MPGSSLGMTA SKERPMTNIL DHLSRHVLLC DGGTGALVQA MNLSVEKDFQ GLENCTEILV KSRPDVIRGI HARYFEAGAD MVEADTFGAS PITLAEFGIA ERAHELNQAA IELAWEAAEQ FKGDGRTRFV LGAIGPGTKL PSLGHIGYDE LEAAYVIQAA GQIAGGVSAF LVETCQDPLQ IKAAVNGCKI ANAAAGTDVP VFVQVTVETT GTLLVGADIA AAATVVQSLG VPLMGLNCAA GPQEMGEHFK WLIDNWTGFV SIQPNAGLPE LVDGQTRYPL LPAELAVWHE RFVSAGANLL GGCCGTTPPH ISATNEMLKR IGNGYRPNPV KRSVHWVPSV ASLYTQVPLR QENAFLSIGE RCNANGSKKF RDLQDAEDWD GITAIAREQV KEGSHTLDVC TAFVGRNEVA DMTEVVSRLR GAVTTPLVID STELPVLEAG LKLYGGKAIL NSINFENGEK DAADRLVLAR KFGAAVVALT IDEDGMAKDA AAKLRIAKRL YDFAVTKHGL PASDLLFDPL TFTICTGNED DRKLAVETLD AIEMITREMP ECGIVLGLSN VSFGLKPAAR QVLNSVFIDH AIKRGMTGAI VHVSKIVPLH TLPEEEVKAA EDLIYDRDPQ ALSRYIALFG DRKAAEIKKE RPAKAEDRLK QRIIDGDRTG LEDDLAQVME EGWKPLDIIN TLLLDGMKVV GELFGSGKMQ LPFVLQSAET MKASVAFLEP HMEKADGQQK ATMVLATVKG DVHDIGKNLV DIILTNNGYK VINIGIKQPV AEIIKAAKEH KADAVGMSGL LVKSTVIMRE NLEEMTNAGL DVPVLLGGAA LTRKYVEEDC SKAYGSGRVA YARDAFDGLD LMAKVADGSF DAHVAAKAAS PHRPGSPSRT LGEAAQPATR PVDWDEINLR RAELHKDVPA PVPPFWGARV IESAPLQNLI PFLNETMLYQ FHWGYRKQGK SIEEFKAWAH KEIRPVAMDM LKRCAKEEIL RPQAVYGYWK AASDNDSVVL FAEDGTTEVA RFPFPRQAKD GGLCIADFFR PVSDPVRDVI GLQVVTMGKR ATEVAQDWFK ADKYQDYLYL HGLSVEMAEA MAEYVHKRIR SELGFAAEDA ADMDRLLKQN YRGSRFSFGY PACPRIEDQT QLLSLLGAER IGVTLSEEFQ LEPEQSTSAI VTVHPQAKYF SV // ID Q2XP48_ECOLX Unreviewed; 1227 AA. AC Q2XP48; DT 20-DEC-2005, integrated into UniProtKB/TrEMBL. DT 20-DEC-2005, sequence version 1. DT 27-MAY-2015, entry version 63. DE SubName: Full=B12-dependent methionine synthase {ECO:0000313|EMBL:CDP72974.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CDP72974.1}; DE SubName: Full=Cobalamin-dependent homocysteine transmethylase {ECO:0000313|EMBL:ABB79784.1}; GN Name=metH {ECO:0000313|EMBL:ABB79784.1}; GN ORFNames=PGD_03191 {ECO:0000313|EMBL:CDP72974.1}; OS Escherichia coli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562 {ECO:0000313|EMBL:ABB79784.1}; RN [1] {ECO:0000313|EMBL:ABB79784.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=B834 {ECO:0000313|EMBL:ABB79784.1}; RA Frederick R.O., Riters M.A., Dillon N., Kunert J., Phillips G.N. Jr, RA Markley J.L., Fox B.G.; RT "Genomic DNA sequence analysis of the Escherichia coli methionine RT auxotroph B834."; RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CDP72974.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=D6-117_07.11 {ECO:0000313|EMBL:CDP72974.1}; RA Kempf F., Loux V., Germon P.; RT "Genome sequence of four bovine mastitis-causing Escherichia coli RT strains."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:CDU40165.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=D6-117_07.11 {ECO:0000313|EMBL:CDU40165.1}; RA Kempf F., Loux V., Germon P.; RT "Genome sequence of four bovine mastitis-causing Escherichia coli RT strains."; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; DQ272318; ABB79784.1; -; Genomic_DNA. DR EMBL; CCCP010000029; CDP72974.1; -; Genomic_DNA. DR EMBL; HG976958; CDU40165.1; -; Genomic_DNA. DR RefSeq; WP_000095995.1; NZ_JSRJ01000127.1. DR ProteinModelPortal; Q2XP48; -. DR SMR; Q2XP48; 651-1227. DR EnsemblBacteria; CDU40165; CDU40165; PGD_03191. DR EnsemblBacteria; EYB43778; EYB43778; BU69_16385. DR EnsemblBacteria; KEP12507; KEP12507; EH62_22960. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABB79784.1}; KW Transferase {ECO:0000313|EMBL:ABB79784.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135983 MW; 7250C9EE48BA453B CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LSFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VTEVERWLAP NLGYDAD // ID Q2YD17_NITMU Unreviewed; 1267 AA. AC Q2YD17; DT 20-DEC-2005, integrated into UniProtKB/TrEMBL. DT 20-DEC-2005, sequence version 1. DT 27-MAY-2015, entry version 73. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABB73354.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABB73354.1}; GN OrderedLocusNames=Nmul_A0045 {ECO:0000313|EMBL:ABB73354.1}; OS Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849). OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Nitrosomonadaceae; Nitrosospira. OX NCBI_TaxID=323848 {ECO:0000313|EMBL:ABB73354.1, ECO:0000313|Proteomes:UP000002718}; RN [1] {ECO:0000313|Proteomes:UP000002718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25196 / NCIMB 11849 {ECO:0000313|Proteomes:UP000002718}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000103; ABB73354.1; -; Genomic_DNA. DR RefSeq; WP_011379409.1; NC_007614.1. DR RefSeq; YP_410746.1; NC_007614.1. DR STRING; 323848.Nmul_A0045; -. DR EnsemblBacteria; ABB73354; ABB73354; Nmul_A0045. DR KEGG; nmu:Nmul_A0045; -. DR PATRIC; 22722922; VBINitMul110821_0050. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; NMUL323848:GKEC-46-MONOMER; -. DR Proteomes; UP000002718; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002718}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABB73354.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002718}; KW Transferase {ECO:0000313|EMBL:ABB73354.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 273 273 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 338 338 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 339 339 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 797 797 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1267 AA; 138929 MW; D798A8CE449F81F9 CRC64; MSLPEGMVEK GMIESRLHPN FGIAMNEHPR IKLLEDLLAR RILLLDGAMG TMIQSHKLGE KDYRGERFAD FPHDLRGNND LLTLTQPQVI RSIHEAYLEA GADIVETNTF NSTAASMGDY HMQDLVYELN FAGARLAKEA AQAMEAKTPE KPRFVAGVLG PTTKTASISP DVNDPGFRGI TFDQLVEDYS ESIRGLLDGG ADILLVETIF DTLNAKAALF AIDRYFETHQ VRVPIMISAT ITDASGRTLS GQTPEAFWNS VSHARPLSVG LNCALGAELM RPYVEELSRV AGVYVSAHPN AGLPNPLAET GYDESPEYTA GLIKGYAQAG FVNIVGGCCG TTPAHIKAIA DAVGSIPPRV VPDVPKKLRL SGLEPLNIGD DSLFVNVGER TNVTGSKAFA RLILGNNYAE ALSVGRSQVE NGAQIIDINM DEAMLDSQKA MVTFLNLVAA EPDISRVPIM IDSSKWSVIE AGLKCVQGKP IINSISLKEG EAEFIEHAKL ARRYGAAVIV MAFDETGQAD TLARKVEICA RCYRILVDQV GFPPEDIIFD PNIFAIATGI EEHNNYGVDF IEATRAIKEK LPYAKVSGGV SNVSFSFRGN EPVREAIHTA FLYHAVRAGM TMGIVNAGQL GVYSDIPKDL LERVEDVLLN RPVPGDGETT ATERLVEFAE SFKGQSKEST EDLAWRNGSL QERLTHALVK GITTYIVEDT EAARQEIAAQ GGRPIQVIEG PLMNGMNVVG DLFGSGKMFL PQVVKSARVM KQAVAHLLPF IEAEKKLSGD SKPKGKIVIA TVKGDVHDIG KNIVTVVLQC NNYEVVNMGV MVPSAQILET ARRENADMIG LSGLITPSLE EMAHVAKEME REGFTIPLLI GGATTSRVHT AVKVAPKYSG VTVWVPDASR AVGVCSNLLS EDLRADYIQQ IQTEYERVRA QHKNKKGPAP MLSIADARKN AFKTDWETYS PPSPGFTGLR SLRNYPLEKL VPFIDWTPFF QAWELSGRFP AILEDEVVGE AASNLYRDAQ VMLKKIVEQK WLTANAVFGL FPANTVNSDD IEIYTDKARE RVAMTFHNLR QQTMKPDGKP NLCLADFIAP RESGITDTIG AFAVTAGMGI EAKLKVFEEA HDDYSAIILK ALADRLAEAF AEHMHWRIRR EFWGFVKDEN LSNEQLVAEE YQGIRPAPGY PACPDHTEKG PLFEMLKAPE NAGIIVTESF AMVPTAAVSG FYFSHPEARY FAVGKIGKDQ VEDYARRKGW TMEETETWLA PVLAYER // ID Q2YP51_BRUA2 Unreviewed; 1261 AA. AC Q2YP51; DT 07-FEB-2006, integrated into UniProtKB/TrEMBL. DT 07-FEB-2006, sequence version 1. DT 27-MAY-2015, entry version 69. DE SubName: Full=Brucella melitensis biovar Abortus 2308 chromosome I, complete sequence, strain 2308 {ECO:0000313|EMBL:CAJ10144.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAJ10144.1}; GN OrderedLocusNames=BAB1_0188 {ECO:0000313|EMBL:CAJ10144.1}; OS Brucella abortus (strain 2308). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=359391 {ECO:0000313|EMBL:CAJ10144.1, ECO:0000313|Proteomes:UP000002719}; RN [1] {ECO:0000313|EMBL:CAJ10144.1, ECO:0000313|Proteomes:UP000002719} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2308 {ECO:0000313|EMBL:CAJ10144.1, RC ECO:0000313|Proteomes:UP000002719}; 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., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S., 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; CAJ10144.1; -; Genomic_DNA. DR RefSeq; WP_002965438.1; NZ_KN046823.1. DR RefSeq; YP_413676.1; NC_007618.1. DR ProteinModelPortal; Q2YP51; -. DR SMR; Q2YP51; 673-921. DR STRING; 359391.BAB1_0188; -. DR EnsemblBacteria; CAJ10144; CAJ10144; BAB1_0188. DR EnsemblBacteria; KFJ50984; KFJ50984; DK47_2962. DR GeneID; 3786978; -. DR KEGG; bmf:BAB1_0188; -. DR PATRIC; 17843216; VBIBruMel86222_0199. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; BABO359391:GKDV-190-MONOMER; -. DR BioCyc; BMEL359391:GJOQ-190-MONOMER; -. DR PRO; PR:Q2YP51; -. DR Proteomes; UP000002719; Chromosome I. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002719}; KW Methyltransferase {ECO:0000313|EMBL:CAJ10144.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002719}; KW Transferase {ECO:0000313|EMBL:CAJ10144.1}. SQ SEQUENCE 1261 AA; 138652 MW; B65506A5F8F0B796 CRC64; MASSLDDLFG ATAAKPDGSE VLAALTQAAR ERILILDGAM GTQIQGLGFH EEHFRGDRFA TCDCQLQGNN DLLTLTQPKA IEEIHYAYAM AGADILETNT FSSTSIAQAD YGMEAMVYDL NRDGARLARR AALRAEQKDG RRRFVAGALG PTNRTASLSP DVNNPGFRAV TFDDLRIAYS EQIRGLIDGG SDIILIETIF DTLNAKAAVF ATEEVFAEKG VRLPVMISGT ITDLSGRTLS GQTPTAFWYS LRHARPFTIG LNCALGANAM RAHLDELSGI ADTFICAYPN AGLPNEFGQY DETPEAMAAQ IEGFARDGLV NVVGGCCGST PDHIRAIAQA VAKYEPRKPA KVPPLMRLSG LEPFTLTKDI PFVNIGERTN VTGSARFRKL VKAGDFAAAL DVARDQVANG AQIIDINMDE GLIDSEKAMV EFLNLIAAEP DIARVPIMLD SSKWEVIEAG LKCVQGKAVV NSISLKEGEE AFLHHARLVR AYGAAVVIMA FDETGQADTQ ARKIEICTRA YKILTEQVGF PPEDIIFDPN IFAVATGIEE HNNYGVDFIE ATREIVRTLP HVHISGGVSN LSFSFRGNEP VREAMHAVFL YHAIQAGMDM GIVNAGQLAV YDTIDAELRE ACEDVVLNRP TKTGESATER LLEIAERFRD SGSREARTQD LSWREWPVEK RLEHALVNGI TEYIEADTEE ARLAAERPLH VIEGPLMAGM NVVGDLFGSG KMFLPQVVKS ARVMKQAVAV LLPFMEEEKR LNGGEGRQSA GKVLMATVKG DVHDIGKNIV GVVLACNNYE IIDLGVMVPS QKILQVARDE KVDIIGLSGL ITPSLDEMAH VAAEMEREGF DIPLLIGGAT TSRVHTAVKI HSRYERGQAV YVVDASRAVG VVSNLLSPEG KQAYIDGLRN EYAKVAAAHA RNEAEKQRLP IARARANPHQ LDWENYEPVK PAFTGTKVFE TYDLAEIARY IDWTPFFQTW ELRGRYPAIL EDEKQGEAAR QLWADAQAML RKIIDEKWFT PRAVVGFWPA NAVGDDIRLF TDESRKEELA TLFTLRQQLT KRDGRPNVAM ADFVAPVESG KQDYVGGFVV TAGIGEIAIA ERFERANDDY SAILVKALAD RFAEAFAELM HERVRKEFWA YAPDEAFTPE ELISEPYKGI RPAPGYPAQP DHTEKTTLFR LLDATANTGV ELTESYAMWP GSSVSGLYIG HPESYYFGVA KVERDQVEDY ARRKDMDVEA VERWLTPILN YVPGASKDEA A // ID Q30NX6_SULDN Unreviewed; 1163 AA. AC Q30NX6; DT 06-DEC-2005, integrated into UniProtKB/TrEMBL. DT 06-DEC-2005, sequence version 1. DT 27-MAY-2015, entry version 77. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABB45305.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABB45305.1}; GN OrderedLocusNames=Suden_2031 {ECO:0000313|EMBL:ABB45305.1}; 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 {ECO:0000313|EMBL:ABB45305.1, ECO:0000313|Proteomes:UP000002714}; RN [1] {ECO:0000313|EMBL:ABB45305.1, ECO:0000313|Proteomes:UP000002714} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33889 / DSM 1251 {ECO:0000313|Proteomes:UP000002714}; RX PubMed=18065616; DOI=10.1128/AEM.01844-07; RA Sievert S.M., Scott K.M., Klotz M.G., Chain P.S.G., Hauser L.J., RA Hemp J., Huegler M., Land M., Lapidus A., Larimer F.W., Lucas S., RA Malfatti S.A., Meyer F., Paulsen I.T., Ren Q., Simon J., Bailey K., RA Diaz E., Fitzpatrick K.A., Glover B., Gwatney N., Korajkic A., RA Long A., Mobberley J.M., Pantry S.N., Pazder G., Peterson S., RA Quintanilla J.D., Sprinkle R., Stephens J., Thomas P., Vaughn R., RA Weber M.J., Wooten L.L.; RT "Genome of the epsilonproteobacterial chemolithoautotroph Sulfurimonas RT denitrificans."; RL Appl. Environ. Microbiol. 74:1145-1156(2008). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000153; ABB45305.1; -; Genomic_DNA. DR RefSeq; WP_011373645.1; NC_007575.1. DR RefSeq; YP_394540.1; NC_007575.1. DR ProteinModelPortal; Q30NX6; -. DR STRING; 326298.Suden_2031; -. DR EnsemblBacteria; ABB45305; ABB45305; Suden_2031. DR KEGG; tdn:Suden_2031; -. DR PATRIC; 23772760; VBISulDen68967_2109. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SDEN326298:GH9P-2086-MONOMER; -. DR Proteomes; UP000002714; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002714}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABB45305.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002714}; KW Transferase {ECO:0000313|EMBL:ABB45305.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 732 732 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1163 AA; 129473 MW; 6620809DFC2FAB13 CRC64; MTTKEYILKT IKNRPLIIDG AMGTQLQQRD DKISKEAWEG NEGCNELLNV TAPEILSEIF HAYLTSGADF VTTNTFGSFS WVLDEYQIGH RAYELTYAGA KLAKDECKKF STPTHPRFCL GSIGPGTKLP SLGHITYDEM YKGYTEFCLA LIDGGVDVFL LETAQDPLQI KAALHACNEA SKQRGVEIPI MVSVTIELSG TMLIGTDAQT IATILEPFDI LSLGFNCGTG PEQVLKHVKT LSEIWHKPIS VHANAGLPQN RGGYTYYPMG PDEFAAKQQS FLEFDGVSFL GGCCGTTPQH IRALVNLVSD IAPKAPSGKH ENSLASLFST VPLMQESSAL LIGERSNATG SKAFRELLLA EDYEGTLSVA QQQVRAGAHV LDVSVGFAGR DETKDMNRVM SLYAQKIALP LMPDSTQTAA LEEALKLIGA KPIINSVNLE DGIEKFDAVC SLAKKFGAAL VCLTIDEIGM AKSVERKLEV AERIYDLAVN KHGIRAENLV FDLLTFTLGS GDEEYLDAGI NTIEAIRELR RRHPEVGATL GLSNISFGLD KDARPYLNSM FLHHCNEAGL TSVIINVAHI IPINKISKED QEICDNLIFN RKPNAAALFE FIDHFSTKEA VDNNAVDEAY LAMSDEEKIA KLLMDGDKDR MIPLVEEARH KVAPEKIVNE ILIDAMKVVG ELFGSGQMQL PFVLQSAETM KKTVDYLNPY LPKIDKSVDT TLALGTVKGD VHDVGKNLVD IILSNNGFKV KNLGIKVDIG EFIQSIKESN ATALGMSGLL VKSTQVMKEN LETLQKEGIK IPVLLGGAAL TRSFIDDFCR PLYDGPIFYC KDAFDGVTAM SRIEAGNFDT NLHPKDSQEK IVKIKEEVII PPFSELKMPS RDVTVPTPPF WGRRELKLTP QQIEMAFDWI NHKLLFKSRW GYSSKGLSEE AYEKQLNDIV WPAYEKLKKR FIEEKLFEPT IIYGYWPCRS DDDSLLIFDE SRGYNSQEEI NREDLDKVRN QAIEKFTFPR QSRQPHRALS DFFHSDRDDV VAFTCVSAGS KLSDVERGIY DRGEYTEYYQ FHGLGVELAE ALAEIVHKQI RLDLNISDGE GSKLSDVQMN RYQGSRYSFG YAACPDLELN RPLFNLLKPE EFGIELSETF QIHPEQSTSA LVVYHPNATY YNV // ID Q30ZI4_DESAG Unreviewed; 810 AA. AC Q30ZI4; DT 06-DEC-2005, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 2. DT 27-MAY-2015, entry version 71. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:ABB38912.2}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABB38912.2}; GN OrderedLocusNames=Dde_2115 {ECO:0000313|EMBL:ABB38912.2}; OS Desulfovibrio alaskensis (strain G20) (Desulfovibrio desulfuricans OS (strain G20)). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=207559 {ECO:0000313|EMBL:ABB38912.2, ECO:0000313|Proteomes:UP000002710}; RN [1] {ECO:0000313|EMBL:ABB38912.2, ECO:0000313|Proteomes:UP000002710} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G20 {ECO:0000313|EMBL:ABB38912.2, RC ECO:0000313|Proteomes:UP000002710}; 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 ----------------------------------------------------------------------- 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; ABB38912.2; -; Genomic_DNA. DR RefSeq; WP_011368015.1; NC_007519.1. DR RefSeq; YP_388607.2; NC_007519.1. DR STRING; 207559.Dde_2115; -. DR EnsemblBacteria; ABB38912; ABB38912; Dde_2115. DR KEGG; dde:Dde_2115; -. DR PATRIC; 21743163; VBIDesDes50040_2092. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR BioCyc; DALA207559:GH1L-1891-MONOMER; -. DR Proteomes; UP000002710; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002710}; KW Methyltransferase {ECO:0000313|EMBL:ABB38912.2}; KW Reference proteome {ECO:0000313|Proteomes:UP000002710}; KW Transferase {ECO:0000313|EMBL:ABB38912.2}. SQ SEQUENCE 810 AA; 85853 MW; 98A8FB7E14EE1E96 CRC64; MPDFRRALSD DTLLFFDGAM GTMLQGRGLP AGMSPEVFCL SNPAVLQGVH LDYARAGADV LTTNTFGGTR LKLPEGMNVV EFNREMARAA KAAAGQAGRT VFVAGSVGPT GHFVKPLGDL EFSELVDIFR EQIRGLVQGG IDLVLAETHF DLAEVRAVVL AARAECNLPV GVSMTFEDGV SLTGTRPEVF VHTMQNMGVD LIATNCSAGP EQMAGVVAGL TAAGDIPVLV MPNAGLPELE NGNTVFRLGP EEFAAQTADF VRAGVRCLGG CCGTTPDHIA ALAREARSKP RPAVEKRRRS GIVLTTRAAC LRIGHDQPCR IIGERINPTG KKELTAQLQA GDFTLAMQFA QQQIDAGAPL LDVNVGAPMV DEKVLLPQLI SDLAAAHGVP LSIDSSDMDA VEASLAVYAG SPLVNSISGE PGRMERLGPL CRDYGAPFVL LPLKGRKLPV TAAERISIID ELLLQADDLG IPRRLVMVDV LALAVSSKAE AARHCFDTIR YCNEELGLPT TIGLSNISFG LPARELLNAT FLAMAVGAGL TSCIAHPGNV RLREALAAAE VLMARDSNAE RFIAGYSGWT SGGGSGGIIA GGGEEKKRPV SLEEAVIRGE RDIILELVED ELARGAQPYA LVNERLIPAI TEVGDKYERK EYYLPQLLRS AETMQKAFGR LKPLLEEASG GETKPVIIMA TVEGDIHDIG KNIVCLMLGN HGFDVVDLGK DVKAVDIVDA AVEHNAKLIG LSALMTTTMV RMEDTIQLLR ERGLSIPVFV GGAVVTPAFA EAIGAAGYSR DAVEAVRIAR GLVEAPARVQ // ID Q31AW2_PROM9 Unreviewed; 1188 AA. AC Q31AW2; DT 06-DEC-2005, integrated into UniProtKB/TrEMBL. DT 06-DEC-2005, sequence version 1. DT 27-MAY-2015, entry version 74. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABB49983.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABB49983.1}; GN OrderedLocusNames=PMT9312_0923 {ECO:0000313|EMBL:ABB49983.1}; OS Prochlorococcus marinus (strain MIT 9312). OC Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae; OC Prochlorococcus. OX NCBI_TaxID=74546 {ECO:0000313|EMBL:ABB49983.1, ECO:0000313|Proteomes:UP000002715}; RN [1] {ECO:0000313|Proteomes:UP000002715} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MIT 9312 {ECO:0000313|Proteomes:UP000002715}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000111; ABB49983.1; -; Genomic_DNA. DR RefSeq; WP_011376477.1; NC_007577.1. DR RefSeq; YP_397419.1; NC_007577.1. DR ProteinModelPortal; Q31AW2; -. DR STRING; 74546.PMT9312_0923; -. DR EnsemblBacteria; ABB49983; ABB49983; PMT9312_0923. DR KEGG; pmi:PMT9312_0923; -. DR PATRIC; 23005606; VBIProMar70153_0980. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PMAR74546:GHRG-945-MONOMER; -. DR Proteomes; UP000002715; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002715}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABB49983.1}; KW Transferase {ECO:0000313|EMBL:ABB49983.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 746 746 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1188 AA; 132402 MW; 404E7CB39FB2791F CRC64; MESFRTYLNR DEKPLIIFDG GTGTSFQNLN LTADDFGGKE LEGCNENLVL SSPEVVENVH NSFLEAGCHV IETNTFGASS IVLDEYDIAD KAYEINKNAA FIAKKAADKY SSVDKPRFVA GSIGPTTKLP TLGHIDFDEL KQSYKEQIYG LIDGGVDLLL IETCQDVLQI KSALLASKEI LESKNIDIPL MVSITMETTG TMLVGSDIAS ALTILEPFNI DILGLNCATG PEQMKEHIKY LSENSPFAIS CIPNAGLPEN IGGVAHYRLK PIELKMQLMN FIYDFNVQLI GGCCGTTPEH TKYLSSIIDE IIDNERTNNN GKKNSSGFIP SASSIYNSVP YKQDNSILIV GERLNASGSK KVRELLNNDD WDGLVAIAKQ QQKENAHVLD VNVDYVGRDG VKDMKEITSR LVTNINLPLM IDSTDADKME SGLKSAGGKC IINSTNYEDG NERFDQVLNL ALGYGSGLVV GTIDEDGMAR NSEKKYKIVK RAINRTRECG LSDYELFFDP LALPISTGIE EDRLNAKETI SAILKIRENF PDIHIILGIS NISFGLSPLS RINLNSIFLD ECIKAGLDSA IIAPNKILPL SKITEETKKL CLDLIYDKRE FEDDICIYDP LVELTKAFQD LSIQDFKKAS SDNKNQTLEE SLKNHIIDGE KIGLEDQLNK ALKKYKPLEI INTFLLDGMK VVGDLFGSGQ MQLPFVLQSA ETMKFAVSIL EPYMETVDEK ISNGKLLIAT VKGDVHDIGK NLVDIILTNN GYDVINLGIK QDVSAIIDAQ KKHNADCIAM SGLLVKSTAF MKDNLEAFNN ENISVPVILG GAALTPKFVN EDCSKIYKGK ILYGKDAFTD LKFMNEYMDN KKKGNWSNTE GFINNEGINI NLASSKSNSQ AVKQSISIQT ETSKLNLKEN FIRSKFINEE DPIQAPFLGT KVLNDVDIDL NKLIFYLDTK ALFSGQWQIK KGKNQSVDEY NNYLDSYAKP LLNKWLEIII EKKLISPKAV YGYFRCGRKD NSIFLFDEKS LNKISQFNFP RQKSGNNLCI ADFYCDLKND KPIDIFPMQA VTMGDIASEY SQKLFKEDKY SDYLLFHGLT VQLAEALAEY VHALIRIECG FRSEEPDKNR EILAQKYRGA RYSFGYPACP KVSDSNIQLS LLDAKRINLT MDESEQLHPE QSTTAIISLH SKAKYFSA // ID Q31JA5_THICR Unreviewed; 1239 AA. AC Q31JA5; DT 06-DEC-2005, integrated into UniProtKB/TrEMBL. DT 06-DEC-2005, sequence version 1. DT 27-MAY-2015, entry version 75. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABB40768.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABB40768.1}; GN OrderedLocusNames=Tcr_0172 {ECO:0000313|EMBL:ABB40768.1}; OS Thiomicrospira crunogena (strain XCL-2). OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Piscirickettsiaceae; Thiomicrospira. OX NCBI_TaxID=317025 {ECO:0000313|EMBL:ABB40768.1, ECO:0000313|Proteomes:UP000002713}; RN [1] {ECO:0000313|Proteomes:UP000002713} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=XCL-2 {ECO:0000313|Proteomes:UP000002713}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000109; ABB40768.1; -; Genomic_DNA. DR RefSeq; WP_011369594.1; NC_007520.2. DR ProteinModelPortal; Q31JA5; -. DR SMR; Q31JA5; 658-1235. DR STRING; 317025.Tcr_0172; -. DR EnsemblBacteria; ABB40768; ABB40768; Tcr_0172. DR KEGG; tcx:Tcr_0172; -. DR PATRIC; 23972214; VBIThiCru83387_0179. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; TCRU317025:GHE8-172-MONOMER; -. DR Proteomes; UP000002713; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002713}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABB40768.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002713}; KW Transferase {ECO:0000313|EMBL:ABB40768.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 252 252 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 315 315 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 316 316 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 763 763 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1239 AA; 137261 MW; 4603492F58C8A1B9 CRC64; MSEFENRPTR IAQLRSLLNQ RIVVLDGAMG TMVQDLALSE EDFRGDRFTD YHMDIKGNND ILVMTQPAMI RDIHLAFLRQ GADIIETNSF NATTIAQADY DMQDTVTELN IAAATVAREA CQIAEKEDGK PRFVAGVLGP TNRTASISPD VNDPGKRNTH FDELVTAYKQ ATHALLKGGA DVILIETIFD TLNAKAAIFA VKDVEEEIGY EVPIMLSGTI TDASGRTLSG QTTEAFYNAV AHAQPLSIGL NCALGPEELR QYVEELSRVC ETYVSVHPNA GLPNEFGEYD ETPEQMAHEI AIWAEKGWLN IIGGCCGTTP DHVEAMANAA LAHPARTLPE IAPACRLSGL EPLNIDDNSL FVNIGERNNV TGSAKFKRLI IEENYNEAID IAVKQVEDGA QIIDVNMDEG MLDAKACMVK FLNLLASEPE ASRVPIMIDS SKWEVIEAGL KCIQGKGVVN SISLKEGEDA FIQQARLVKK YGAAAIVMAF DEDGQADTLE RKIEICERSY NVLTQKVGFL PQDIIFDPNI FAVATGIEEH NNYGLDFINA VTWIKQNLPY AKISGGVSNV SFSFRGNNPV REAIHSVFLY YAIKEGMDMG IVNAGQMAIY DDLPEKLRVA VEDVILNKDP EAGERLLEVA EEYRGDGQAT SKVTDTAWRE TTVEKRLEHS LVKGITDYIE ADTEEAYQKL GAPINVIEGP LMDGMNVVGD LFGSGKMFLP QVVKSARVMK RAVAYLDPYL EAEKSEGQVQ GKIVMATVKG DVHDIGKNIV GVVLQCNNFE VIDLGVMVPA EKILDTAIEQ NANVIGLSGL ITPSLEEMVN VAKLMKERGM NLPLLIGGAT TSKAHTAVKI EPQYDHPVVY VKDASRAVGV AQSLISNDLK ETFAAKIKAE YEQVREERKA RAKQVKRIPI KQARLNPALD DQAWENYTPV KPSFLGTKVL ESFPLEKLLE RFDWSPFFQS WELHGLYPRI LDDKVVGDEA RKVFADAQAL LKTIIDQKWL TAKAVYGFYP ANRVGDDIEV YTDESRTEVL HTFHHLRQQA EKKRGGANNC LSDFIAPKES GVADYIGFFA VTAGIGIEEH IARFEKEHDD YHSIMLKALA DRFAEAFAET LHEIVRKEDW GYAPNEQLEN EDIIRERYQG IRPAPGYPAC PDHTEKGILW DLIKPDEKIG LEITESFAMT PTAAVSGTYF AHPKSRYFGV GSIGRDQVED YAIRKGWSIE ETEKWLAPNL GYDPEDFAN // ID Q31NG7_SYNE7 Unreviewed; 1190 AA. AC Q31NG7; DT 06-DEC-2005, integrated into UniProtKB/TrEMBL. DT 06-DEC-2005, sequence version 1. DT 27-MAY-2015, entry version 71. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABB57402.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABB57402.1}; GN OrderedLocusNames=Synpcc7942_1372 {ECO:0000313|EMBL:ABB57402.1}; OS Synechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechococcus. OX NCBI_TaxID=1140 {ECO:0000313|EMBL:ABB57402.1, ECO:0000313|Proteomes:UP000002717}; RN [1] {ECO:0000313|Proteomes:UP000002717} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7942 {ECO:0000313|Proteomes:UP000002717}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000100; ABB57402.1; -; Genomic_DNA. DR RefSeq; WP_011378007.1; NC_007604.1. DR RefSeq; YP_400389.1; NC_007604.1. DR ProteinModelPortal; Q31NG7; -. DR STRING; 1140.Synpcc7942_1372; -. DR EnsemblBacteria; ABB57402; ABB57402; Synpcc7942_1372. DR KEGG; syf:Synpcc7942_1372; -. DR PATRIC; 23788083; VBISynElo51371_1569. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SYNEL:SYNPCC7942_1372-MONOMER; -. DR Proteomes; UP000002717; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002717}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABB57402.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002717}; KW Transferase {ECO:0000313|EMBL:ABB57402.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 228 228 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 752 752 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1190 AA; 131519 MW; D78644DDEB460A89 CRC64; MQSLFLDRLH SPERPVLVFD GGMGTTLQFQ NLTAEDFGGP ETEGCNEWLI RTKPEAIATV HRQFLEAGAD VIETDTFGAT SIVLAEYGLE DHAYALNVEA AKLAKAIAAE FSTPEKPRFV AGSMGPTTKL PTLGHIGYDE MKASFAEQAR GLWEGGVDLF IVETCQDVLQ IKAALNGIAE IFSEKGDRRP LMVSVTMETT GTMLVGSDVA AMLAILEPYP IDILGLNCAT GPDRMVEHIK YLSEHSPFVI SCIPNAGIPE NVGGHAHYRL TPMELRMALH RFVEDLGVQV IGGCCGTKPE HIAQLAEVAT QLQAKDRPVR RDRDHQQRQP FNYVPSAASI YGTTPYIQDN SFLIIGERLN ASGSKKVREL LNEEDWDGLV AIARSQVKEG AHVLDVNVDY VGRDGERDMG ELVSRLVTNV NLPLMLDSTE WQKMEAGLKK AGGKCILNST NYEDGDERFF KVLELAKQYG AGIVVGTIDE EGMARTAEKK FAIAQRAYRD ALEFGIPAHE IFYDPLALPI STGIEEDRGN GRETIESIRL IRENLPGVHI LLGVSNISFG LNPAARIVLN SVFLHDACEA GMDGAIVSAA KILPLSKIDE KPLQVCRDLI GDRRRFENGI CVYDPLTELT TLFEGVSAKE ARASGPSLAD LPLEERLKQH IIDGERIGLD QALATALEQY PPLEIINTFL LDGMKVVGDL FGSGQMQLPF VLQSAETMKS AVAYLEPFMD KEETNDSGKG TFLIATVKGD VHDIGKNLVD IILTNNGYKV VNIGIKQPVE NIIQAYRDCN ADCIAMSGLL VKSTAFMKEN LATFNEEGIS VPVILGGAAL TPKFVYEDCQ QTYKGQVIYG KDAFADLHFM DQLMAAKSKD QWDDQLGFLD EQGQPLQVAA IASEAAEPTE SRESVAEVVI DLERSEAVAV DIDRPTPPFW GSKILGPDEI PFAEVFSYLD RQALFVGQWQ FRKPKEQSRE EYDAFIAEKV EPILQQWTTR ILAEDLLEPQ VVYGYFPCVA VGNSLQLFDP NDRDRPTARF DFPRQRSLRR LCIADFFAPE ELGIQDVFPM QAVTVGHKAT EFAAQLFAGD QYSDYLYFHG LAVQLAEALA EWTHARIRRE LGYGSLEPES LRDILAQRYQ GSRYSFGYPA CPNVADSRIQ LELLEADRIG MSMDESEQLY PEQSTTAIVA YHPAAKYFSA // ID Q31TY4_SHIBS Unreviewed; 1227 AA. AC Q31TY4; DT 06-DEC-2005, integrated into UniProtKB/TrEMBL. DT 06-DEC-2005, sequence version 1. DT 27-MAY-2015, entry version 73. DE SubName: Full=B12-dependent homocysteine-N5-methyltetrahydrofolate transmethylase {ECO:0000313|EMBL:ABB68474.1}; GN Name=metH {ECO:0000313|EMBL:ABB68474.1}; GN OrderedLocusNames=SBO_4040 {ECO:0000313|EMBL:ABB68474.1}; OS Shigella boydii serotype 4 (strain Sb227). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=300268 {ECO:0000313|EMBL:ABB68474.1, ECO:0000313|Proteomes:UP000007067}; RN [1] {ECO:0000313|EMBL:ABB68474.1, ECO:0000313|Proteomes:UP000007067} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sb227 {ECO:0000313|EMBL:ABB68474.1, RC ECO:0000313|Proteomes:UP000007067}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000036; ABB68474.1; -; Genomic_DNA. DR RefSeq; WP_000096023.1; NC_007613.1. DR RefSeq; YP_410302.1; NC_007613.1. DR ProteinModelPortal; Q31TY4; -. DR SMR; Q31TY4; 651-1227. DR STRING; 300268.SBO_4040; -. DR EnsemblBacteria; ABB68474; ABB68474; SBO_4040. DR KEGG; sbo:SBO_4040; -. DR PATRIC; 18687954; VBIShiBoy33460_4825. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SBOY300268:GJFL-4037-MONOMER; -. DR Proteomes; UP000007067; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007067}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABB68474.1}; KW Transferase {ECO:0000313|EMBL:ABB68474.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135972 MW; 43E6D61164877125 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYCESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEAQDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTDNAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNCIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID Q328N9_SHIDS Unreviewed; 1232 AA. AC Q328N9; DT 06-DEC-2005, integrated into UniProtKB/TrEMBL. DT 06-DEC-2005, sequence version 1. DT 27-MAY-2015, entry version 74. DE SubName: Full=B12-dependent homocysteine-N5-methyltetrahydrofolate transmethylase {ECO:0000313|EMBL:ABB64216.1}; GN Name=metH {ECO:0000313|EMBL:ABB64216.1}; GN OrderedLocusNames=SDY_4322 {ECO:0000313|EMBL:ABB64216.1}; OS Shigella dysenteriae serotype 1 (strain Sd197). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=300267 {ECO:0000313|EMBL:ABB64216.1, ECO:0000313|Proteomes:UP000002716}; RN [1] {ECO:0000313|EMBL:ABB64216.1, ECO:0000313|Proteomes:UP000002716} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sd197 {ECO:0000313|EMBL:ABB64216.1, RC ECO:0000313|Proteomes:UP000002716}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000034; ABB64216.1; -; Genomic_DNA. DR RefSeq; WP_000095944.1; NC_007606.1. DR RefSeq; YP_405707.1; NC_007606.1. DR ProteinModelPortal; Q328N9; -. DR SMR; Q328N9; 651-1224. DR STRING; 300267.SDY_4322; -. DR EnsemblBacteria; ABB64216; ABB64216; SDY_4322. DR GeneID; 3796495; -. DR KEGG; sdy:SDY_4322; -. DR PATRIC; 18699504; VBIShiDys99784_5101. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SDYS300267:GJEW-4318-MONOMER; -. DR Proteomes; UP000002716; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002716}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABB64216.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002716}; KW Transferase {ECO:0000313|EMBL:ABB64216.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1232 AA; 136502 MW; 956C0DFD196C270E CRC64; MSSKVEQLRA QLNEHILVLD SGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVNTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSQIAECYVT AHPNAGLPNA FGEYALDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRAWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVVVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPSASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYGDAANL LI // ID Q39CG3_BURL3 Unreviewed; 372 AA. AC Q39CG3; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 27-MAY-2015, entry version 58. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABB09853.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABB09853.1}; GN OrderedLocusNames=Bcep18194_A6259 {ECO:0000313|EMBL:ABB09853.1}; OS Burkholderia lata (strain ATCC 17760 / LMG 22485 / NCIMB 9086 / R18194 OS / 383). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=482957 {ECO:0000313|EMBL:ABB09853.1, ECO:0000313|Proteomes:UP000002705}; RN [1] {ECO:0000313|Proteomes:UP000002705} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17760 / LMG 22485 / NCIMB 9086 / R18194 / 383 RC {ECO:0000313|Proteomes:UP000002705}; 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 ----------------------------------------------------------------------- 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; ABB09853.1; -; Genomic_DNA. DR RefSeq; WP_011353359.1; NC_007510.1. DR RefSeq; YP_370497.1; NC_007510.1. DR STRING; 269483.Bcep18194_A6259; -. DR EnsemblBacteria; ABB09853; ABB09853; Bcep18194_A6259. DR KEGG; bur:Bcep18194_A6259; -. DR PATRIC; 19290064; VBIBurSp120713_4406. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; BSP269483:GHLS-3148-MONOMER; -. DR Proteomes; UP000002705; Chromosome 1. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002705}; KW Methyltransferase {ECO:0000313|EMBL:ABB09853.1}; KW Transferase {ECO:0000313|EMBL:ABB09853.1}. SQ SEQUENCE 372 AA; 40176 MW; 065ED8336CF3CA5E CRC64; MRTGYNDGFP VFAGLSPMSA TPLAASVPLD APYTRGAALP ALLKSRILIL DGAMGTMIQR YKLDEAAYRG ERFKDFPRDI KGNNELLSIT QPQIIREIHD QYFAAGADIV ETNTFGATTV AQSDYEMEDL VVEMNIESAK LAREAAEKYA TPEKPRFVAG AIGPTPKTAS ISPDVNDPGA RNVTFDELRA SYYQQAKALL DGGVDLFLVE TIFDTLNAKA ALFALDELFE DTGERLPIMI SGTVTDASGR ILSGQTVEAF WNSLRHAKPL TFGLNCALGA ALMRPYIAEL AKLCDTYVSC YPNAGLPNPM AETGFDETPD VTSGLLKEFA QAGLVNLAGG CCGTTPEHIA EIAKALADVK PRRWPNQYSD NA // ID Q39Y82_GEOMG Unreviewed; 804 AA. AC Q39Y82; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 29-APR-2015, entry version 72. DE SubName: Full=5-methyltetrahydrofolate--homocysteine S-methyltransferase, cobalamin-dependent {ECO:0000313|EMBL:ABB30792.1}; GN Name=metH {ECO:0000313|EMBL:ABB30792.1}; GN OrderedLocusNames=Gmet_0549 {ECO:0000313|EMBL:ABB30792.1}; OS Geobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=269799 {ECO:0000313|EMBL:ABB30792.1, ECO:0000313|Proteomes:UP000007073}; RN [1] {ECO:0000313|EMBL:ABB30792.1, ECO:0000313|Proteomes:UP000007073} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GS-15 / ATCC 53774 / DSM 7210 RC {ECO:0000313|Proteomes:UP000007073}; 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; ABB30792.1; -; Genomic_DNA. DR RefSeq; WP_004512245.1; NC_007517.1. DR RefSeq; YP_006719512.1; NC_007517.1. DR ProteinModelPortal; Q39Y82; -. DR STRING; 269799.Gmet_0549; -. DR EnsemblBacteria; ABB30792; ABB30792; Gmet_0549. DR KEGG; gme:Gmet_0549; -. DR PATRIC; 22000246; VBIGeoMet55070_0570. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; GMET269799:GHNY-551-MONOMER; -. DR Proteomes; UP000007073; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007073}; KW Methyltransferase {ECO:0000313|EMBL:ABB30792.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007073}; KW Transferase {ECO:0000313|EMBL:ABB30792.1}. SQ SEQUENCE 804 AA; 84747 MW; 0FFB9C4722C2A2B6 CRC64; MKTPFLQAIK ERVLVLDGAM GTMLQERGLR PGQSPEELNL TMPDVVAGVH REYLEAGADI IVTNTFGGTR PKLEHYGLEE KVREINARAV EIAREVCGDR AYVAASMGPT GLFVEPVGEA TFDAMAAFFR EQAAALIEAG ADLITLETFL DIKEIRAAVI AIREVSPTIP VIAQLTFDNE GRTVLGTPPE AAAVTLAAAG ADIVGSNCGL GPDGICAVLG AMRGVTRLPL ISQANAGLPK LVDGKTVFPG TPDDMTAFHD RMLGLNVRVI GGCCGTTPTH IRAIKEALAG RDQSWRDCGP PAGVTFLASR TSVVALGGGL PAAIIGERIN PTGKKAFAQE LREGKITTIR REAMEQTAAG AHLLDVNVGT PGIDEPAAME RAVFCVTGSV AVPLVLDSSD PAALERGLKA ADGKVLVNSV NGETKSIERV LPLVKKYGAA VIGLALDETG IPETAEGRLA VAERIVAAAE GRGISRNDVV IDCLTLTVSA EQKRAMETLR AVRLVKEIIG CPTVLGVSNI SFGLPRRPLI SSAFFAMALA AGLDAAIVNP KEEEMMAAWR SAMVLLNRDP SAAAYIAAYA GTAAAAPEPA ASGEALDIRE RLKRAVITGD RENIVALVEE ALGQGLEPLQ VSNEGLLPGL EEVGRRFEKN LVFLPQVMQS ADTMQAAFGR LREVMKGSPA ASRGKILMAT VEGDIHDIGK NIVCTLLENH GFEVIDLGKN VPADRIVGKA RELGVDAVGL SALMTTTMTE MENVIARLKE AGIRTFTMVG GAVVTQEYAD EIGADLYARD AMEAVARIKA LLEK // ID Q39YC7_GEOMG Unreviewed; 605 AA. AC Q39YC7; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 27-MAY-2015, entry version 72. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN Name=metF-2 {ECO:0000313|EMBL:ABB30747.1}; GN OrderedLocusNames=Gmet_0504 {ECO:0000313|EMBL:ABB30747.1}; OS Geobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=269799 {ECO:0000313|EMBL:ABB30747.1, ECO:0000313|Proteomes:UP000007073}; RN [1] {ECO:0000313|EMBL:ABB30747.1, ECO:0000313|Proteomes:UP000007073} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GS-15 / ATCC 53774 / DSM 7210 RC {ECO:0000313|Proteomes:UP000007073}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {ECO:0000256|RuleBase:RU004255}. CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ABB30747.1; -; Genomic_DNA. DR RefSeq; WP_004512200.1; NC_007517.1. DR RefSeq; YP_006719467.1; NC_007517.1. DR ProteinModelPortal; Q39YC7; -. DR STRING; 269799.Gmet_0504; -. DR EnsemblBacteria; ABB30747; ABB30747; Gmet_0504. DR KEGG; gme:Gmet_0504; -. DR PATRIC; 22000154; VBIGeoMet55070_0524. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; GMET269799:GHNY-506-MONOMER; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000007073; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004255}; KW Complete proteome {ECO:0000313|Proteomes:UP000007073}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ABB30747.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000007073}; KW Transferase {ECO:0000313|EMBL:ABB30747.1}. SQ SEQUENCE 605 AA; 64560 MW; C1135904DFF984D3 CRC64; MNFLERLNSE VLVGDGAIGT MLYAKGVSLD ANVEHLNLVR PELVLELHRE YLGAGAKVIE TNTFGANWTK LSAIGLDKRE REIILRGARL AREAAEGTDA FVAGSMGPLA RVKGDERELS PAETTEIFRR QALALAEGGV DLLILETFTD LAQILCALSA ARETGLPVVA NMAFLENGRL AGGADVERAA RELTAAGASV VGANCGAGPL EVLGTIRRMA GATALPIAAY PNSGFPEYVN GRHVYRTTPD YFAERAAEMV AAGAALVGGC CGTTPEHILR LAERLAGLRP AVRNVAVPAV SVEERRGEST EAEGFLARWG EEPVVTVELD PPKGFDCGKV IEGSRVLKGA GADAINIAEN PLARIRMGNI ALGHLIQQEV GIEVIVHVTC RDRNLLGLQS DLMGASLLGI RSILAVTGDP ARIGEQAGAS SVYDLNSFTL IKLLADLNAG VNALGNPLGR GAGFAIGCVF NPNSQRMEVQ AERLAKKVAN GARFVQTQPL YDLARLDEML ERTSPLGIPV LPGILPLVSE RNCEFLHNEV PGIVIPEDIR ARMRGKEKDE GVREGLAIAR EFIDAVRGRV GGFYLMPPFG RYEIAVELVR HIKGK // ID Q3A0Z9_PELCD Unreviewed; 801 AA. AC Q3A0Z9; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 27-MAY-2015, entry version 68. DE SubName: Full=5-methyltetrahydrofolate--homocysteine S-methyltransferase, cobalamin-dependent {ECO:0000313|EMBL:ABA89958.1}; GN Name=metH {ECO:0000313|EMBL:ABA89958.1}; GN OrderedLocusNames=Pcar_2722 {ECO:0000313|EMBL:ABA89958.1}; OS Pelobacter carbinolicus (strain DSM 2380 / Gra Bd 1). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Pelobacteraceae; Pelobacter. OX NCBI_TaxID=338963 {ECO:0000313|EMBL:ABA89958.1, ECO:0000313|Proteomes:UP000002534}; RN [1] {ECO:0000313|Proteomes:UP000002534} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2380 / Gra Bd 1 {ECO:0000313|Proteomes:UP000002534}; 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; ABA89958.1; -; Genomic_DNA. DR RefSeq; WP_011342501.1; NC_007498.2. DR RefSeq; YP_006718499.1; NC_007498.2. DR ProteinModelPortal; Q3A0Z9; -. DR STRING; 338963.Pcar_2722; -. DR EnsemblBacteria; ABA89958; ABA89958; Pcar_2722. DR KEGG; pca:Pcar_2722; -. DR PATRIC; 22891830; VBIPelCar86875_2953. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PCAR338963:GKDU-2987-MONOMER; -. DR Proteomes; UP000002534; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002534}; KW Methyltransferase {ECO:0000313|EMBL:ABA89958.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002534}; KW Transferase {ECO:0000313|EMBL:ABA89958.1}. SQ SEQUENCE 801 AA; 84574 MW; EADDCC67804C506A CRC64; MADFIAAIKQ RVLVLDGAMG TMLQERGLKA GGCPEEMNLT APDVVEAVHR EYADAGADII VTNSFGGSRP KLAHYGLEDK VHEINARAVV LARNAAGPDR FVAASIGPTG RFLRPVGDAD FDDMVEVFGE QVRAFAEAGA DLITMETFLD IAELRAAVIA CRRYSDLPIM ALMTFENEGR SVLGTSPEAA AVTLEALGVT VIGTNCGLGV EGIYEMLARM RSVCSTPLIA QPNAGLPQLI DGQTVFNATP QDMVVYHQQL LDIGVRVIGG CCGTTPAHIR AMREALQGTE QDWTPPARRC LLSSRTGVVE IGGPAACAII GERINPTGRK AYAQELREAK TAYIRREAQA QVAAGAHLLD VNCGAPGVDE PAALERAVLA VEGVAQVPLV LDSSDPAALE RALKVADGKV LINSVSGEEK SLKGILPLAK KYGAAVIALA LDGSGIPETA EERLAVARRI RDAALEAGLA PEDIVVDCLT LTVSAEQKRA METIRTLRLV RDELGLPTAL GVSNISFGLP CRPVLSSVFF AMALDAGLSA AIINPRDERM MDAYLAAMVL LGKDVRAESY IAAYADVSAA PAAAAPQDAP TGIRDRLAAA VIEGDKDGVV ALVEQALTEG LDTATISNEG LLPGLEEVGR RFGENRVFLP QVMQSAETMQ TAFGRLKQEM QGASVASLGR ILMATVEGDI HDIGKNIVCT LLENHGFEVI DLGKNVSADR IVEQAVELKV DAVGLSALMT TTIEQMRVTV DRLRAAGVKV FTMVGGAVVT QEYADEIGAD MYAADALEAV AKAKKLLAAE H // ID Q3A7Z3_PELCD Unreviewed; 609 AA. AC Q3A7Z3; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 27-MAY-2015, entry version 70. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN Name=metF-2 {ECO:0000313|EMBL:ABA87499.1}; GN OrderedLocusNames=Pcar_0238 {ECO:0000313|EMBL:ABA87499.1}; OS Pelobacter carbinolicus (strain DSM 2380 / Gra Bd 1). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Pelobacteraceae; Pelobacter. OX NCBI_TaxID=338963 {ECO:0000313|EMBL:ABA87499.1, ECO:0000313|Proteomes:UP000002534}; RN [1] {ECO:0000313|Proteomes:UP000002534} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2380 / Gra Bd 1 {ECO:0000313|Proteomes:UP000002534}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {ECO:0000256|RuleBase:RU004255}. CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; ABA87499.1; -; Genomic_DNA. DR RefSeq; WP_011339904.1; NC_007498.2. DR RefSeq; YP_006715897.1; NC_007498.2. DR ProteinModelPortal; Q3A7Z3; -. DR STRING; 338963.Pcar_0238; -. DR EnsemblBacteria; ABA87499; ABA87499; Pcar_0238. DR KEGG; pca:Pcar_0238; -. DR PATRIC; 22886358; VBIPelCar86875_0260. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; PCAR338963:GKDU-264-MONOMER; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000002534; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004255}; KW Complete proteome {ECO:0000313|Proteomes:UP000002534}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:ABA87499.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000002534}; KW Transferase {ECO:0000313|EMBL:ABA87499.1}. SQ SEQUENCE 609 AA; 64494 MW; E88EC279AF921CCF CRC64; MKRAEKSLME RLEQGVIVGD GAMGTLLYHR GVPLSTCFEL LNLQHPETVR QIHRDYLAAG AQLLETNTFA ANRLRLAAIG QEDQVRSINS LGAQLARQAA GSEALVAGAI GPLGRTPGET ADLAGDERRE LFREQMEGLA EGGADLLLLE TFASLEELEL AVTVASRIGL PIVAQMAFFE GGRTREGVTA DEAARRLVAA GASLVGANCG SGPRDVLAVL RTMAAETDCP LSGFANSGFP EYVDGRYIYL ATPEYFAARG REMVEAGARL IGGCCGTTPE HIRALAAAVA DLKPAARCVV PALPKAATVA TEPGPEHRGF LSAWGKRPII TVELDPPRGL DCDKILAGAR RLADAGADAI SLAENPLARI RMGNIALAKQ IQDQIGIETI IHVTGRDRNL IGLHSEMMGA HLLGLRNVLA VTGDPVAVGG EAGASNVFDL NSIGVLQLLS ALNNGHTLVG GELGEATRFQ AGAAFNPNVS DMSGQLRRLK KKVAAGARFV QTQPIYSVDV LDAMLACLAD IRIPILVGIL PLVSERNAEF LHNEVPGILL PETVRARMRG TRGEEGKRQG LAIARELIEA GRGRVDGFYL MPPFGKVDIA VALIEVIRG // ID Q3AJX3_SYNSC Unreviewed; 1208 AA. AC Q3AJX3; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 27-MAY-2015, entry version 77. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:ABB35109.1}; GN OrderedLocusNames=Syncc9605_1355 {ECO:0000313|EMBL:ABB35109.1}; OS Synechococcus sp. (strain CC9605). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechococcus. OX NCBI_TaxID=110662 {ECO:0000313|EMBL:ABB35109.1, ECO:0000313|Proteomes:UP000002711}; RN [1] {ECO:0000313|EMBL:ABB35109.1, ECO:0000313|Proteomes:UP000002711} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CC9605 {ECO:0000313|EMBL:ABB35109.1, RC ECO:0000313|Proteomes:UP000002711}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000110; ABB35109.1; -; Genomic_DNA. DR RefSeq; WP_011364327.1; NC_007516.1. DR RefSeq; YP_381664.1; NC_007516.1. DR ProteinModelPortal; Q3AJX3; -. DR STRING; 110662.Syncc9605_1355; -. DR EnsemblBacteria; ABB35109; ABB35109; Syncc9605_1355. DR KEGG; syd:Syncc9605_1355; -. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SSP110662:GJ7R-1394-MONOMER; -. DR Proteomes; UP000002711; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002711}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABB35109.1}; KW Transferase {ECO:0000313|EMBL:ABB35109.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 238 238 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 764 764 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1208 AA; 132181 MW; 414C4A78FA61DAAD CRC64; MVVTQADRQV TTSAFLDHLH GPQRPVLVFD GATGTSLQGL GLTAEDFGGP DLEGCNENLA VTKPDAVKAV HRQFLEVGCD VIETDTFGAA SIVLAEYGLE DKAFELNKRA AELAREMADE FSTPEKPRFV AGSMGPTTKL PTLGHIDFDT MRDSFREQAE GLIAGNVDLF IVETCQDVLQ IKAALQGIEE AFAATGERRA LMVSVTMETT GTMLVGTDIA AVVSILEPFP IDILGLNCAT GPEQMKEHIR YLSEHSPFTV SCIPNAGLPE NIGGVAHYRL TPVELKMQLM HFVEDLGVQV IGGCCGTTPA HIGSLAELAQ ELKPAERPSR WDRASAKDVR PSPNYEPAAS SIYGVTPYHQ DNSFLIIGER LNASGSRKVR ELLAEEDWDG LVSVARGQVK ENAHVLDVNV DYVGRDGERD MHELVSRLVT NVNLPLMLDS TEWQKMEAGL KVAGGKCILN STNYEDGDER FFKVLELARR YGAAVVVGTI DEDGMARTAE KKFAIAQRAY RDALEFGIPA HEIFYDPLAL PISTGIEEDR LNGRATVDAI RMIRENLPGV HVVLGVSNVS FGLSPAARIT LNSVFLHDCC EAGMDSAIVS PAKILPLIKI SDDHQKVCRD LINDNRRFED GICVYDPLTE LTKLFEGVST KEARASGPSL ADLPIEERLK QHIIDGERIG LEPSLDEALQ TYPPLQIINT FLLDGMKVVG ELFGSGQMQL PFVLQSAETM KSAVAHLEPH MEKSEGESTS KGKFLIATVK GDVHDIGKNL VDIILTNNGY EVINLGIKQS CEAIIEAQRE HQADCIAMSG LLVKSTAFMK DNLQAFNDAG IDVPVILGGA ALTPRFVQKD CREVYDGKVI YGRDAFADLR FMDALMDAKR SENWTNTKGF LADAPQGVGL DEESTTSEKA EETSISATDA PAADLPPVSS DRSDAVPAEA APLAPFLGSS VITEADIDIA EVFHYLDRNA LFAGQWMLRK TKEQSRDDYE AMLAEKADPV LKEWMKRCMD ESLLTPRAVY GYFPVGRDGN SLRVFDADGT RELGRFELPR QRSGNRFCIA DFFNDLDAEG GPTDVLPIQA VTMGQKASVV AQELFKGDRY SDYLYFHGLA VQMAEAMAEW VHARIRSELG FADPDGMALR DVLAQRYRGS RYSFGYPACP NVADSRQQLD WLGAERIGLS MDASDQLEPE QSTTALVALH SQARYFSA // ID Q3APY1_CHLCH Unreviewed; 1224 AA. AC Q3APY1; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 27-MAY-2015, entry version 74. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABB28944.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABB28944.1}; GN OrderedLocusNames=Cag_1692 {ECO:0000313|EMBL:ABB28944.1}; OS Chlorobium chlorochromatii (strain CaD3). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Chlorobium. OX NCBI_TaxID=340177 {ECO:0000313|EMBL:ABB28944.1, ECO:0000313|Proteomes:UP000002708}; RN [1] {ECO:0000313|EMBL:ABB28944.1, ECO:0000313|Proteomes:UP000002708} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CaD3 {ECO:0000313|EMBL:ABB28944.1, RC ECO:0000313|Proteomes:UP000002708}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000108; ABB28944.1; -; Genomic_DNA. DR RefSeq; WP_011362706.1; NC_007514.1. DR RefSeq; YP_379987.1; NC_007514.1. DR ProteinModelPortal; Q3APY1; -. DR SMR; Q3APY1; 629-875. DR STRING; 340177.Cag_1692; -. DR EnsemblBacteria; ABB28944; ABB28944; Cag_1692. DR KEGG; cch:Cag_1692; -. DR PATRIC; 21371127; VBIChlChl46571_1758. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; QPFFNAW; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CCHL340177:GHBW-1708-MONOMER; -. DR Proteomes; UP000002708; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002708}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABB28944.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002708}; KW Transferase {ECO:0000313|EMBL:ABB28944.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 226 226 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 739 739 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1224 AA; 133932 MW; 0019842EED9D4B2F CRC64; MGTMIQRHKL KEEDYRGSRF ADHSHPLLGN NDMLVLTQPD IIYTLHCAFL EAGSDIIETN SFNANPISQA DYSAVELVHE LNVEACRLAR RAADEFSAKT PNKPRFVAGS IGPTNKTLSL SPDVNRPGYR AVTFREVVDN YLVQLEGLRE GGVDLLLVET VFDTLNCKAA LFAISEIFER TGWRVPVMVS GTVVDASGRT LSGQTTEAFW SSVCHLPELL SIGLNCALGS KQMRPFIEAM ANVAESYVSV YPNAGLPNEF GQYDDSPEYM ATQIADFATS GFVNIVGGCC GTTPDHIKAI AEAVQTISPR KRPTKKHELL LSGLEPLVVN HTTGFINIGE RTNVTGSKKF ARLIKEGNYD EALSIARQQV ENGAQVIDVN VDEGMLDSEK VMKEFLNLIA SEPEISRVPI MIDSSKWSVI ESGLQCVQGK GIVNSISLKE GDELFRERAR KILRYGAATV VMAFDEQGQA DNLQRRIEIC QRAYNILVNE VGFPPEDIIF DPNVLTVATG IEEHNNYAVD FIESVRWIKE NLPHAKVSGG ISNVSFSFRG NEPVREAMHA AFLYHAIRAG LDMGIVNAGQ LAIYEDIEPE LLVRVEDVLL NRRADATERL VSFAETIATG GEKVEAKAAE WRNLPVAERL RHALIKGIVE HIEEDTEEAR QLYPSPLQVI EGPLMDGMNA IGDLFAVGKM FLPQVVKSAR VMKRSVAHLI PFIEAEKAKN KDTSAQAKVL LATVKGDVHD IGKNIVAVVL ACNNYEVIDI GVMMPCEKIL EAVEREKADL LGLSGLITPS LDEMVHVAAE MERRGMKIPL LIGGATTSRM HTAVKIAPVY SGAVVQVLDA SRSVPVVNSL LNPALSPKYI ADLKNEQAGL RESHAAAQAA RNYVSLADAR NNAAKVEPVA VQPKKVGLTL FEDVAVAELR AYIDWTPLFM TWELHGRYPQ ILSDAKYGSE AQKLLNDANA LLDRIELEKL LGVKGVVGIF PANSTGDDIA IYTDESRTKV LTTLHTLRQQ QEKANGEANV ALADFIASAD SGVADYLGAF AVTTGLGIAK TLERFVAEHD DYHRILMQTV ADRLAEAFAE MLHECVRREV WGYEEVCSKT SSCCACHAES ATTSQANHLE ELLAGNYQGI RPAPGYPACP DHSEKAEIFT LLNAEVNTGI TLTENFAMNP AASVSGLYLA HPEARYFMLG KIGKDQVEDY AQRKGINVAE AEKLLATSLN YQAG // ID Q3AXU0_SYNS9 Unreviewed; 1208 AA. AC Q3AXU0; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 01-APR-2015, entry version 73. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABB26087.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABB26087.1}; GN OrderedLocusNames=Syncc9902_1123 {ECO:0000313|EMBL:ABB26087.1}; OS Synechococcus sp. (strain CC9902). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechococcus. OX NCBI_TaxID=316279 {ECO:0000313|EMBL:ABB26087.1, ECO:0000313|Proteomes:UP000002712}; RN [1] {ECO:0000313|Proteomes:UP000002712} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CC9902 {ECO:0000313|Proteomes:UP000002712}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000097; ABB26087.1; -; Genomic_DNA. DR RefSeq; WP_011359917.1; NC_007513.1. DR RefSeq; YP_377131.1; NC_007513.1. DR ProteinModelPortal; Q3AXU0; -. DR STRING; 316279.Syncc9902_1123; -. DR EnsemblBacteria; ABB26087; ABB26087; Syncc9902_1123. DR KEGG; sye:Syncc9902_1123; -. DR PATRIC; 23799567; VBISynSp76179_1245. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SSP316279:GJCI-1134-MONOMER; -. DR Proteomes; UP000002712; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002712}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABB26087.1}; KW Transferase {ECO:0000313|EMBL:ABB26087.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 238 238 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 763 763 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1208 AA; 132008 MW; 79DF25F8F8263BDA CRC64; MVVTQAKAPV TASRFLDYIH GPTRPVLVFD GATGTSLQDQ GLTAEDFGGL DLEGCNENLV ITRPDAVQAV HRQFLDVGCD VIETDTFGAA SIVLAEYGLE DQAFELNRRA AQLARDVADE YSTPEKPRFV AGSMGPTTKL PTLGHIEFDT MRDGFREQAE GLIAGNVDLI IVETCQDVLQ IKAALQGIEA AFESCGERRP LMVSVTMETT GTMLVGSDIA AVVAILEPFP IDILGLNCAT GPEQMKEHIR YLSENSPFIV SCIPNAGLPE NVGGVAHYRL TPTELKMQMM HFVEDLGVQV IGGCCGTTPA HIGSLVELAL ELKPAERLSR SKDQKDDVRP SFDYEPSAAS IYGVTPYHQD NSFLIIGERL NASGSRKVRE LLAEEDWDGL VGVARGQVKE NAHVLDVNVD YVGRDGEKDM NNLVSRLVTN VNLPLMLDST EWQKMEAGLK VAGGKCILNS TNYEDGNERF FKVLELARRY GAGVVVGTID EDGMARTAEK KFAIAQRAYR DALEFGIPAR EIFYDPLALP ISTGIEEDRL NAKATVDSIR MIREGLPGVH VVLGVSNVSF GLSPAARINL NSVFLHDCCE AGMDAAIVSP AKILPLVKIS DEHQQVCRDL INDNRRFEDK ICVYDPLTEL TKLFEGVSAK EARASGPSLS DLPIEKRLKQ HIIDGERIGL EPALDQAMND YAPLHIINTF LLDGMKVVGE LFGSGQMQLP FVLQSAETMK SAVAHLEPHM ETLEGESTSK GKFLIATVKG DVHDIGKNLV DIILTNNGYE VVNLGIKQSC DAIVDAQKEH QADCLAMSGL LVKSTAFMKD NLSAFNEAGI DVPVILGGAA LTPRFVQKDC RDVYNGKVIY GRDAFADLRF MDALMDAKKK DNWSNLSGFL ADAPEGVGLD EATPNDSDQA SAPAEASEPE QPQSQQPVST ERSSAVPPEP IPVAPFLGSA VLTEADLDLQ EVFTYLDRNA LFAGQWQFRK TKDQSRDDYD AMLAEKAEPV LQLWIDRCLN ESLLAPGAVY GYFPVGRDGN ALRVFSADKT TELGRFDLPR QRSGNRYCIA DFFSDVSADG APTDVLPMQA VTMGEKASIV AQELFKGDQY SDYLYFHGLA VQMAEALAEW VHARIRQELG FADPTGMPLR DVLAQRYRGS RYSFGYPACP NVADSRQQLL WLDADRICLT MDASDQLSPE QSTTALIALH SKARYFSA // ID Q3B628_PELLD Unreviewed; 1225 AA. AC Q3B628; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 27-MAY-2015, entry version 72. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABB23203.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABB23203.1}; GN OrderedLocusNames=Plut_0315 {ECO:0000313|EMBL:ABB23203.1}; 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 {ECO:0000313|EMBL:ABB23203.1, ECO:0000313|Proteomes:UP000002709}; RN [1] {ECO:0000313|Proteomes:UP000002709} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 273 {ECO:0000313|Proteomes:UP000002709}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000096; ABB23203.1; -; Genomic_DNA. DR RefSeq; WP_011357078.1; NC_007512.1. DR RefSeq; YP_374246.1; NC_007512.1. DR ProteinModelPortal; Q3B628; -. DR SMR; Q3B628; 648-894. DR STRING; 319225.Plut_0315; -. DR EnsemblBacteria; ABB23203; ABB23203; Plut_0315. DR KEGG; plt:Plut_0315; -. DR PATRIC; 21378077; VBIChlLut1287_0326. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PLUT319225:GHDM-325-MONOMER; -. DR Proteomes; UP000002709; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002709}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABB23203.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002709}; KW Transferase {ECO:0000313|EMBL:ABB23203.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1225 AA; 134348 MW; 7D7099C666F640F2 CRC64; MKATLRELLR ERILVLDGAM GTMIQRHKLT ENDYRGERFK SHTHPLLGNN DILVLTRPDI IYQIHCDFLE AGSDIIETNT FNANPISQGD YGTEDLIKEL NLEASRLARK AADSYTAKDP AKPRFVAGSI GPTNKTLSLS PDVNNPGYRA VSFRDVVDNY LLQLEGLMEG GVDVLLVETV FDTLNCKAAL FAIEEFFTRT NKRVPVMVSG TVVDQSGRTL SGQTTEAFWI SIAHMPDLLS VGLNCALGSK QMRPFIEAIS TVAESFVSVY PNAGLPNEFG EYDDSPEYMA DQIAGFAESG FVNIVGGCCG TTPGHIKAIA DAVVALQPRK RPTASHELQL SGLEPLRVNS TTGFINVGER TNVTGSKKFA RLIREGNYDE ALSIARQQVE SGAQVIDVNV DEGMLDSEKV MQEFLNLIAS EPEIAKVPVM IDSSKWSVIE KGLQCVQGKS IVNSISLKEG EEPFRQRAAK ILEYGAATVV MAFDEAGQAD SLERRKEICG RAYRILTEEV GFPPEDIIFD PNVLTVATGI EEHDTYALDF IESVRWIKES LPHAKVSGGI SNVSFSFRGN EPVREAMHAA FLYHAIQAGL DMGIVNAGQL AIYEDIDPEL LVRVEDVLLN RRSDATERLV SFAETIRDGG EKTEAKAAEW RSLPVVERLR HALIKGIVEY IDEDTEEARK LYPSPLQVIE GPLMDGMNAI GDLFAEGKMF LPQVVKSARV MKRSVAWLIP FIEEEKARNK DTKAAAKILL ATVKGDVHDI GKNIVSVVLS CNNYEVIDIG VMMPCEKILE AAVREKADII GLSGLITPSL DEMVHVAKEM ERLGMKIPLI LGGATTSKIH TAVKIAPVYS GPVVQVLDAS RSVPVAGSLL NPQLKEGYVA KLKDEQEAMR LGHAERSAAK RFVSVEEARR NRLRPDWNAT LPPLPKKPGT TVLDNVTAGA LRPYIDWTPF FQTWELHGRY PEILSDPKVG AEATKLLGDA NAMLDLIEKE KLLGIRGVAG LFPAASAGDD IEVYTDETHT AVLATIHTLR QQQEKPAGEP NLALADFLAP KESGLKDHIG GFAVTTGLGI KPILERYRGM HDDYSAILLQ ALADRLAEAF AEMLHEKVRR ELWGYAPAEI LGSEALIGED YQGIRPAPGY PACPDHTEKA GLFTLLNAEA NTGITLTETY AMDPAASVSG FYFANPEARY FVLGKVQKDQ VEDYAGRKGF SLQDAEKWLA PNLSY // ID Q3BV79_XANC5 Unreviewed; 376 AA. AC Q3BV79; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 27-MAY-2015, entry version 62. DE SubName: Full=Meth protein {ECO:0000313|EMBL:CAJ23256.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAJ23256.1}; GN Name=meth {ECO:0000313|EMBL:CAJ23256.1}; GN OrderedLocusNames=XCV1603 {ECO:0000313|EMBL:CAJ23256.1}; OS Xanthomonas campestris pv. vesicatoria (strain 85-10). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=316273 {ECO:0000313|Proteomes:UP000007069}; RN [1] {ECO:0000313|EMBL:CAJ23256.1, ECO:0000313|Proteomes:UP000007069} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=85-10 {ECO:0000313|EMBL:CAJ23256.1, RC ECO:0000313|Proteomes:UP000007069}; 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 Schneicker 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 ----------------------------------------------------------------------- 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; CAJ23256.1; -; Genomic_DNA. DR RefSeq; WP_011346986.1; NC_007508.1. DR RefSeq; YP_363334.1; NC_007508.1. DR ProteinModelPortal; Q3BV79; -. DR STRING; 316273.XCV1603; -. DR EnsemblBacteria; CAJ23256; CAJ23256; XCV1603. DR KEGG; xcv:XCV1603; -. DR PATRIC; 24092706; VBIXanCam71633_1847. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; XCAM316273:GJF8-1645-MONOMER; -. DR Proteomes; UP000007069; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007069}; KW Methyltransferase {ECO:0000313|EMBL:CAJ23256.1}; KW Transferase {ECO:0000313|EMBL:CAJ23256.1}. SQ SEQUENCE 376 AA; 40089 MW; B603EB22346CD418 CRC64; MTPAALHSPV AHALPWLRPE RAAKLTAALA ERILIIDGAM GTMIQRHDLQ EPDYRGTRFA EGYDSAHVHG PGCDHAHVPQ GHDLKGNNDL LLLTRPQIIA GIHRAYLDAG ADLLETNTFN ATSVSQADYH LEHLVYELNK AGAQVARACC DEVEALTPHK PRFVIGVLGP TSRTASISPD VNDPGYRNTS FDALRETYRE AIEGLIDGGA DTLMVETIFD TLNAKAALYA IEEVFEARGG RLPVMVSGTI TDASGRTLSG QTAEAFYASV AHGRPLSIGL NCALGAKDLR PHVETLAQIA DAYVSAHPNA GLPNAFGEYD ETPEEMASTL REFAQAGLLN LVGGCCGTSP DHIRAIAEAV ADLPPRQLPG AQELAA // ID Q3BVN3_XANC5 Unreviewed; 321 AA. AC Q3BVN3; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 27-MAY-2015, entry version 54. DE SubName: Full=MmuM protein {ECO:0000313|EMBL:CAJ23080.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:CAJ23080.1}; GN Name=mmuM {ECO:0000313|EMBL:CAJ23080.1}; GN OrderedLocusNames=XCV1449 {ECO:0000313|EMBL:CAJ23080.1}; OS Xanthomonas campestris pv. vesicatoria (strain 85-10). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=316273 {ECO:0000313|Proteomes:UP000007069}; RN [1] {ECO:0000313|EMBL:CAJ23080.1, ECO:0000313|Proteomes:UP000007069} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=85-10 {ECO:0000313|EMBL:CAJ23080.1, RC ECO:0000313|Proteomes:UP000007069}; 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 Schneicker 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 ----------------------------------------------------------------------- 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; CAJ23080.1; -; Genomic_DNA. DR RefSeq; WP_011346877.1; NC_007508.1. DR RefSeq; YP_363180.1; NC_007508.1. DR ProteinModelPortal; Q3BVN3; -. DR STRING; 316273.XCV1449; -. DR EnsemblBacteria; CAJ23080; CAJ23080; XCV1449. DR KEGG; xcv:XCV1449; -. DR PATRIC; 24092374; VBIXanCam71633_1682. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; XCAM316273:GJF8-1489-MONOMER; -. DR Proteomes; UP000007069; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007069}; KW Methyltransferase {ECO:0000313|EMBL:CAJ23080.1}; KW Transferase {ECO:0000313|EMBL:CAJ23080.1}. SQ SEQUENCE 321 AA; 34140 MW; 884869FD3DFCB865 CRC64; MTILPRQPRA NAPFSQALQH DGYVVLDGAL ATELEQRGCD LNDALWSARV LMEQPELIYQ VHRDYFAAGA QCAITASYQA TPLGFAARGL DAAQAQALIA RSVALAAQAR ADHLTLHPYA APLWVAGSVG PYGAYLADGS EYRGDYVLPI EQLMDFHRPR IAALAEAGVD LLACETLPSA SEIVALRQLL QHEFPQLHAW FSFTLRDAAH LSDGTPLAQV VPALDACAQV IAVGINCIAL DQARAALHSL AALTALPLVV YPNSGEHYDA SDKRWHAGHG AALTLADQHA HWLAAGARLI GGCCRTAPRD IAALAAARAL G // ID Q3EQ84_BACTI Unreviewed; 1133 AA. AC Q3EQ84; DT 08-NOV-2005, integrated into UniProtKB/TrEMBL. DT 08-NOV-2005, sequence version 1. DT 27-MAY-2015, entry version 58. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EAO53469.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EAO53469.1}; GN ORFNames=RBTH_04246 {ECO:0000313|EMBL:EAO53469.1}; OS Bacillus thuringiensis serovar israelensis ATCC 35646. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=339854 {ECO:0000313|EMBL:EAO53469.1}; RN [1] {ECO:0000313|EMBL:EAO53469.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35646 {ECO:0000313|EMBL:EAO53469.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EAO53469.1}. 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; AAJM01000253; EAO53469.1; -; Genomic_DNA. DR RefSeq; WP_003260169.1; NZ_AAJM01000253.1. DR EnsemblBacteria; EAO53469; EAO53469; RBTH_04246. DR PATRIC; 38352335; VBIBacThu7829_4352. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EAO53469.1}; KW Transferase {ECO:0000313|EMBL:EAO53469.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 223 223 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 287 287 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 719 719 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1133 AA; 126012 MW; F568D4E98D8640FD CRC64; MMKCIEEKLQ NSILILDGAM GTMIQQEDLT AEDFGGEEYE GCNEYLVETR PDVILKIHKA YIEAGADIIE TNTFGATNIV LSDYELSHLD EELNEKAALL AKQAVKESGK EVYVAGAMGP TTKAISVTGG VTFEELIEAY TRQARGLLKG EVDVLLVETS QDMRNVKAAY IGIQAAFEEM KKTVPIMISG TIEPMGTTLA GQTIEAFYLS VEHMKPLSVG LNCATGPEFM RDHIRSLSDL SECYISCYPN AGLPDEDGHY HESPSSLAEK VKRFAEEGWV NIIGGCCGTT PEHIKAMKSA LASLKPRDHH EREGHGISGL EALQYDESMR PLFVGERTNV IGSLKFKRLV AEGKFEEAAE VARAQVKKNA HIIDICMADP DRDEIEDMEK FLTEVTKVLK VPIMIDSTDE NVMARALTYI QGKAVINSIN LEDGEERFEK VTPLLRKYGA AIVVGTIDED GMAVSAERKL EIAKRSYELL TTKYGIRPSD IIFDALVFPV GTGDEEYIGS AAATIEGIRL IKEALPECLT ILGVSNISFG LPPAGREVLN SVFLYHATKA GLDYAIVNTE KLERYASIPE EEKHLADALL FETTKETLEE FTNFYRVAKK KDVVVQETLT LNERLANYIV EGTKXGLHED LSLALEEGRK PLDIINGPLM TGMDEVGRLF NNNELIVAEV LQSAESMKAA VSYLEPYMES SDSAKKGKVL LATVKGDVHD IGKNLVEIIL ANNGYEIINL GINVRSDRIV QEVQEKNPDI IGLSGLLVKS AQQMVTTAED LKAANIDVPI VVGGAALTRK FTDNRISPSY KGLVCYASDA MTGLDIINKL QKEEEREKMK QDKKERHLHI VKKEEKKVEI PAVIEPLPKA EVIVPDSTKR IVLRDIPALH LAPFLNRQML LGHHLGLKGN VKKLLKEGDK RAHELNDLID ELLQEGQSWL KPKAVYQFFP AQSDGQNIVI YDPEDHTRVI ERFTFPRQGK APYRTLGDYL RPIGDEMDYV AFLSVTVGEG VRDIAEEWKA KGDYLRSHAI QSLALELAEG LAEKTHMLIR DRWGIPDSPE LTMEERFRTK YRGIRVSFGY PACPELADQE KLFRLIHPEE IGISLTEGFM MEPEASVTAM VFSHPEARYF SVL // ID Q3EVV9_BACTI Unreviewed; 325 AA. AC Q3EVV9; DT 08-NOV-2005, integrated into UniProtKB/TrEMBL. DT 08-NOV-2005, sequence version 1. DT 27-MAY-2015, entry version 21. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EAO55439.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EAO55439.1}; GN ORFNames=RBTH_01738 {ECO:0000313|EMBL:EAO55439.1}; OS Bacillus thuringiensis serovar israelensis ATCC 35646. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=339854 {ECO:0000313|EMBL:EAO55439.1}; RN [1] {ECO:0000313|EMBL:EAO55439.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35646 {ECO:0000313|EMBL:EAO55439.1}; 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. {ECO:0000313|EMBL:EAO55439.1}. 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; AAJM01000071; EAO55439.1; -; Genomic_DNA. DR RefSeq; WP_000066234.1; NZ_AAJM01000071.1. DR EnsemblBacteria; EAO55439; EAO55439; RBTH_01738. DR PATRIC; 38347805; VBIBacThu7829_2200. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EAO55439.1}; KW Transferase {ECO:0000313|EMBL:EAO55439.1}. SQ SEQUENCE 325 AA; 36369 MW; 607DB5A4FEB1C9FD CRC64; MSNKINPIDD ILSQQSIMLL DGALATELEA HGCNLDDPLW SARVLLENPE LIYQVHSDYF RAGADCAITA SYQATISGFS TRGIQEQEAL ELIKKTVLLA RRARDDFWKE NTQTNRPKPL VVASVGPYGA YLADGSEYVG NYGVTDKTLA DFHRSRMSAL IEAGADLLAF ETIPSLQEAR VLDTLLREFP ETYAWLSFSL KNEKEISEGM KLVECARVFE KSEQIVAIGI NCAPVTVVTG AIQELRANTK KPIIVYPNSG ETYNPETKTW HGHEQCNALN IQSEEWYQAG ARLIGGCCRT TPYHIEEISN KWRSSEFFYS NEAKQ // ID Q3IHM9_PSEHT Unreviewed; 359 AA. AC Q3IHM9; DT 08-NOV-2005, integrated into UniProtKB/TrEMBL. DT 08-NOV-2005, sequence version 1. DT 27-MAY-2015, entry version 62. DE SubName: Full=Pseudoalteromonas haloplanktis str. TAC125 chromosome I, complete sequence {ECO:0000313|EMBL:CAI87279.1}; GN OrderedLocusNames=PSHAa2223 {ECO:0000313|EMBL:CAI87279.1}; OS Pseudoalteromonas haloplanktis (strain TAC 125). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI87279.1, ECO:0000313|Proteomes:UP000006843}; RN [1] {ECO:0000313|EMBL:CAI87279.1, ECO:0000313|Proteomes:UP000006843} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843}; RX PubMed=16169927; DOI=10.1101/gr.4126905; RA Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P., RA Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G., RA Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z., RA Sekowska A., Tutino M.L., Vallenet D., von Heijne G., 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; CAI87279.1; -; Genomic_DNA. DR RefSeq; WP_011328880.1; NC_007481.1. DR RefSeq; YP_340721.1; NC_007481.1. DR ProteinModelPortal; Q3IHM9; -. DR STRING; 326442.PSHAa2223; -. DR EnsemblBacteria; CAI87279; CAI87279; PSHAa2223. DR GeneID; 3708060; -. DR KEGG; pha:PSHAa2223; -. DR PATRIC; 32298041; VBIPseHal105694_2144. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; PHAL326442:GJIU-2280-MONOMER; -. DR Proteomes; UP000006843; Chromosome I. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006843}; KW Reference proteome {ECO:0000313|Proteomes:UP000006843}. SQ SEQUENCE 359 AA; 39400 MW; ADCB6720E7E6D588 CRC64; MPNNPLNNDQ NKHDELSAAL KERILILDGA MGTMIQAHQL EEQDYRGERF KDWHVLIRGN NDLLSLTQPK IITDIHRSFL AAGADIIETN TFNSTTISME DYDMANLSRE INLESAKLAR LLCDEFSAKT PEKPRYVAGV LGPTSKTCSL SPDVNDPGYR NVTFDRLVTA YVESTLALME GGADIILIET IFDTLNAKAA SFAVEEAFEQ AGRTLPVMIS GTITDASGRT LSGQTTEAFY NSIRHIKPLS IGLNCALGPD LLRQYVQELS RVCETFTSVH PNAGLPNEFG GYDLEAKEMA TEIIDWGKSG FINIVGGCCG TTPAHIRAFA KGLEGVKPRQ LPEIEVRMRL SGLEACNLN // ID Q3IWY3_RHOS4 Unreviewed; 359 AA. AC Q3IWY3; DT 08-NOV-2005, integrated into UniProtKB/TrEMBL. DT 08-NOV-2005, sequence version 1. DT 27-MAY-2015, entry version 55. DE SubName: Full=Rhodobacter sphaeroides 2.4.1 chromosome 2, complete sequence {ECO:0000313|EMBL:ABA80951.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABA80951.1}; GN ORFNames=RSP_3347 {ECO:0000313|EMBL:ABA80951.1}; 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 {ECO:0000313|EMBL:ABA80951.1, ECO:0000313|Proteomes:UP000002703}; RN [1] {ECO:0000313|Proteomes:UP000002703} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158 RC {ECO:0000313|Proteomes:UP000002703}; 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; ABA80951.1; -; Genomic_DNA. DR RefSeq; WP_011339230.1; NC_007494.2. DR RefSeq; YP_354852.1; NC_007494.2. DR STRING; 272943.RSP_3347; -. DR EnsemblBacteria; ABA80951; ABA80951; RSP_3347. DR GeneID; 3722048; -. DR KEGG; rsp:RSP_3347; -. DR PATRIC; 23156873; VBIRhoSph57909_3782. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR PhylomeDB; Q3IWY3; -. DR BioCyc; RSPH272943:GJAS-3475-MONOMER; -. DR Proteomes; UP000002703; Chromosome 2. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002703}; KW Methyltransferase {ECO:0000313|EMBL:ABA80951.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002703}; KW Transferase {ECO:0000313|EMBL:ABA80951.1}. SQ SEQUENCE 359 AA; 38210 MW; 0457DCE4ACD058FF CRC64; MKPFPLWSPL LLLIRPDSML TFSLPPSRAV PALEALVRQR ILILDGAMGT QIQALGLSEE DYAGCGCRHH AERPQKGNND LLILTQPQAI EEIHFRYAMA GADIVETNTF SATTIAQADY GMESAVEDLN REGARIVRRA LDRATALDGR PRFVAGAVGP TNRTASISPD VNDPGYRAVS FDDLRMAYGT QVRALIAGGA DLILIETIFD TLNAKAAIFA CFEAFAEAGR RLPLMISGTI TDASGRTLSG QTPTAFWHSV RHARPFTVGL NCALGAAAMR PHLAELAGVA DAAICAYPNA GLPNAFGQYD EGPDETAAQV ARFAREGLVN VVGGCCGTTP DHVRAIACAV ADLPPRTLV // ID Q3J4K6_RHOS4 Unreviewed; 335 AA. AC Q3J4K6; DT 08-NOV-2005, integrated into UniProtKB/TrEMBL. DT 08-NOV-2005, sequence version 1. DT 27-MAY-2015, entry version 55. DE SubName: Full=Rhodobacter sphaeroides 2.4.1 chromosome 1, complete sequence {ECO:0000313|EMBL:ABA78278.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABA78278.1}; GN ORFNames=RSP_2124 {ECO:0000313|EMBL:ABA78278.1}; 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 {ECO:0000313|EMBL:ABA78278.1, ECO:0000313|Proteomes:UP000002703}; RN [1] {ECO:0000313|Proteomes:UP000002703} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158 RC {ECO:0000313|Proteomes:UP000002703}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; ABA78278.1; -; Genomic_DNA. DR RefSeq; WP_011337253.1; NZ_AKVW01000001.1. DR RefSeq; YP_352179.1; NC_007493.2. DR ProteinModelPortal; Q3J4K6; -. DR STRING; 272943.RSP_2124; -. DR EnsemblBacteria; ABA78278; ABA78278; RSP_2124. DR GeneID; 3719594; -. DR KEGG; rsp:RSP_2124; -. DR PATRIC; 23151246; VBIRhoSph57909_1018. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265278; -. DR KO; K00548; -. DR OMA; GTNLFAM; -. DR OrthoDB; EOG693GKH; -. DR PhylomeDB; Q3J4K6; -. DR BioCyc; RSPH272943:GJAS-731-MONOMER; -. DR Proteomes; UP000002703; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002703}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ABA78278.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002703}; KW Transferase {ECO:0000313|EMBL:ABA78278.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 212 212 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 278 278 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 279 279 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 335 AA; 35341 MW; 251001B86A6FA50E CRC64; MTDALSRLLR TRDWLMADGA TGTNLFNMGL SSGEPPELWT VDRPDNIRSL YRAAVEAGSD IFLTNSFGGN AARLKLHEAQ GRVGELNRIA AELGREVADA AGRPVVVAGS MGPTGEIFEP MGTLTHRMAV EIFHEQAEAL KAGGADVLWV ETISAAEEFK AAAEAARLAG MPWCGTMSFD TAGRTMMGIT AAALVDLVTK LPNPPLAFGA NCGVGASDLL RTVLGFAAQG IEVPIIAKGN AGIPKYHDGH IHYDGTPELM AEYAVLARDA GARIIGGCCG TMPEHLKAMR AALEGRPRGP RPSLETISET LGGFSSASDG SDDAGPTRER RRRRS // ID Q3JBT9_NITOC Unreviewed; 1232 AA. AC Q3JBT9; DT 08-NOV-2005, integrated into UniProtKB/TrEMBL. DT 08-NOV-2005, sequence version 1. DT 01-APR-2015, entry version 68. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABA57707.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABA57707.1}; GN OrderedLocusNames=Noc_1206 {ECO:0000313|EMBL:ABA57707.1}; OS Nitrosococcus oceani (strain ATCC 19707 / NCIMB 11848). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Nitrosococcus. OX NCBI_TaxID=323261 {ECO:0000313|EMBL:ABA57707.1, ECO:0000313|Proteomes:UP000006838}; RN [1] {ECO:0000313|Proteomes:UP000006838} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19707 / NCIMB 11848 {ECO:0000313|Proteomes:UP000006838}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000127; ABA57707.1; -; Genomic_DNA. DR RefSeq; WP_002809905.1; NC_007484.1. DR RefSeq; YP_343237.1; NC_007484.1. DR ProteinModelPortal; Q3JBT9; -. DR SMR; Q3JBT9; 657-1231. DR STRING; 323261.Noc_1206; -. DR EnsemblBacteria; ABA57707; ABA57707; Noc_1206. DR KEGG; noc:Noc_1206; -. DR PATRIC; 22706398; VBINitOce57959_1428. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; QPFFNAW; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; NOCE323261:GCI3-1226-MONOMER; -. DR Proteomes; UP000006838; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006838}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABA57707.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006838}; KW Transferase {ECO:0000313|EMBL:ABA57707.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 762 762 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1232 AA; 137308 MW; 0429AB7238BAF615 CRC64; MSVKSPRITA LKEQLIKRIL ILDGALGTMI QSYGLTEAEF RGDRFADWSC DLKGNNDLLA LTQPQILREI HGNYLAAGAD IIETNTFNAT RIAMADYRME ELAVEINQTA AQLAREMADD MTAKTPDRPR FVAGVLGPTN RTASISPDVN DPGFRNTSFD ELVAAYTESI RGLIQGGTDI LLVETIFDTL NAKAAVYAIE QYFEDHQIRF PVMISGTITD ASGRTLSGQT TEAFWNSLRH AEPLAFGLNC ALGPKQLRQY VEELAGLADT HVAAHPNAGL PNEFGGYDET PEEMAQEIGE WAQAGFLNIV GGCCGTTPEH IRAIREAVEK HPPRKIPQRP VACRLSGLEP SNIDADSLFV NVGERTNITG SAKFRRLIKE EDYETALEVA RQQVESGAQI IDINMDEGLL DSQKAMVRFL NLIAVEPDIS RVPVMIDSSK WEIIEAGLKC IQGKGIVNSI SLKEGEEPFL QQAKQVRRYG AAAVIMAFDE QGQAETTERK VGICARAYQL LTEKIGFPAE DIIFDPNIFA VATGIEEHNN YGVTYIEAAR EIKRTLPPAL VSGGVSNVSF SFRGNEKVRE AIHAVFLYHA IQAGMDMGIV NAGQLAVYDE IDQDLRERVE DVILNRHPEA TERLLEIAEK YRGAGGEAAE RKEDLAWREL PVNERLAHAL VKGIIDFVEA DTEEARLAAK RPLDVIEGPL MDGMNVVGDL FGSGKMFLPQ VVKSARVMKK AVAYLLPFME NEKESYKSHG KVVLATVKGD VHDIGKNIVA VVLQCNSFEV IDLGVMVPAE KILQTAKEES CDFVGLSGLI TPSLDEMVHV AKEMERQNFD LPLLIGGATT SKMHTAVRIE PQYSQPVVYV PDASRVVGVA QRLLNPSLKA EYAAEITEEY GQMRRRRTEQ QTERSHTPLP QARANKLKTD WTAYVPPRPT FLGLKSFADY PLEELTARID WTPFFHAWEL AGKYPRILKD EVVGEEARKL LKDAQALLKQ VLEEKWLEAR AVIGFFPANT VNEDDIELYT DESRQEVLTT LHHIRQQMVR RSGQPNYCLA DYVAPKETGV ADYIGAFAVT AGLGIDERLE EFARQYDDYN SILLKAIADR LAEAFAECMH ERVRKEFWHY APDEALTNEE LISENYRGVR PAPGYPACPD HTEKATLWQL IEPDKNAGII LTESYAMVPT AAVSGWYFPH PESRYFGTGK IQKDQVKDYA RRKGISVEQV ERWLRSILGY EI // ID Q3JWP4_BURP1 Unreviewed; 359 AA. AC Q3JWP4; DT 08-NOV-2005, integrated into UniProtKB/TrEMBL. DT 08-NOV-2005, sequence version 1. DT 27-MAY-2015, entry version 56. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:ABA50821.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABA50821.1}; GN OrderedLocusNames=BURPS1710b_0595 {ECO:0000313|EMBL:ABA50821.1}; OS Burkholderia pseudomallei (strain 1710b). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=320372 {ECO:0000313|EMBL:ABA50821.1, ECO:0000313|Proteomes:UP000002700}; RN [1] {ECO:0000313|EMBL:ABA50821.1, ECO:0000313|Proteomes:UP000002700} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1710b {ECO:0000313|EMBL:ABA50821.1, RC ECO:0000313|Proteomes:UP000002700}; 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; ABA50821.1; -; Genomic_DNA. DR RefSeq; WP_004204527.1; NC_007434.1. DR RefSeq; YP_332009.1; NC_007434.1. DR ProteinModelPortal; Q3JWP4; -. DR STRING; 320372.BURPS1710b_0595; -. DR EnsemblBacteria; ABA50821; ABA50821; BURPS1710b_0595. DR KEGG; bpm:BURPS1710b_0595; -. DR PATRIC; 19233438; VBIBurPse115837_0610. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; BPSE320372:GBYB-595-MONOMER; -. DR Proteomes; UP000002700; Chromosome I. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002700}; KW Methyltransferase {ECO:0000313|EMBL:ABA50821.1}; KW Transferase {ECO:0000313|EMBL:ABA50821.1}. SQ SEQUENCE 359 AA; 38459 MW; 1013B7D60E53B797 CRC64; MSEPTPIAPF ASSAAPAAPY TRGAALPQLL RQRILILDGA MGTMIQRYKL DEAAYRGERF KDFPRDVKGN NELLSITQPR IIREIHDQYF AAGADIVETN TFGATAVAQA DYGMEALVVE MNVASAALAR ESAAKYATPE KPRFVAGAIG PTPKTASISP DVNDPGARNV TFDELRDAYY QQAKALLDGG VDLFLVETIF DTLNAKAALF ALDQLFDDTG ERLPIMISGT VTDASGRILS GQTVEAFWNS LRHAKPLTFG LNCALGAALM RPYIAELAKL CDTYVSCYPN AGLPNPMSDT GFDETPDVTS GLLKEFAQAG LVNLAGGCCG TTPEHIAAIA KALAEVKPRR WPSQYSEAA // ID Q3KBK9_PSEPF Unreviewed; 1236 AA. AC Q3KBK9; DT 08-NOV-2005, integrated into UniProtKB/TrEMBL. DT 08-NOV-2005, sequence version 1. DT 27-MAY-2015, entry version 81. DE SubName: Full=5-Methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:ABA74845.1}; GN OrderedLocusNames=Pfl01_3107 {ECO:0000313|EMBL:ABA74845.1}; OS Pseudomonas fluorescens (strain Pf0-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA74845.1, ECO:0000313|Proteomes:UP000002704}; RN [1] {ECO:0000313|EMBL:ABA74845.1, ECO:0000313|Proteomes:UP000002704} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA74845.1, RC ECO:0000313|Proteomes:UP000002704}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000094; ABA74845.1; -; Genomic_DNA. DR RefSeq; WP_011334495.1; NC_007492.2. DR RefSeq; YP_348836.1; NC_007492.2. DR ProteinModelPortal; Q3KBK9; -. DR STRING; 205922.Pfl01_3107; -. DR EnsemblBacteria; ABA74845; ABA74845; Pfl01_3107. DR KEGG; pfo:Pfl01_3107; -. DR PATRIC; 19888359; VBIPseFlu44242_3129. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PFLU205922:GJBD-3155-MONOMER; -. DR Proteomes; UP000002704; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002704}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABA74845.1}; KW Transferase {ECO:0000313|EMBL:ABA74845.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1236 AA; 135775 MW; 9177ABAF4ACDDDF9 CRC64; MSDRSVRLQA LKQALKERIL ILDGGMGTMI QSYKLEEQDY RGKRFADWPS DVKGNNDLLV LTRPDVIGGI EKAYLDAGAD ILETNTFNAT QISMADYGME ELVYELNVEG ARLARKVADA KTLETPDKPR FVAGVLGPTS RTCSLSPDVN NPGYRNVTFD ELVENYTEAT KGLIEGGADL ILIETIFDTL NAKAAIFAVQ GVFEELGFEL PIMISGTITD ASGRTLSGQT TEAFWNSVAH AKPISVGLNC ALGARELRPY LEELSDKAST HVSAHPNAGL PNEFGEYDEL PVDTAKVIEE FAQSGFLNIV GGCCGTTPGH IEAIAKAVAG YAPRQIPDIP KACRLSGLEP FTIDRSSLFV NVGERTNITG SAKFARLIRE DNYTEALEVA LQQVEAGAQV IDINMDEGML DSKKAMVTFL NLIAGEPDIS RVPIMIDSSK WDVIEAGLKC IQGKGIVNSI SMKEGVEQFI HHAKLCKRYG AAVVVMAFDE AGQADTEARK KEICKRSYDI LVNEVGFPPE DIIFDPNIFA VATGIEEHNN YAVDFINACA YIRDELPYAL SSGGVSNVSF SFRGNNPVRE AIHSVFLLYA IRAGLTMGIV NAGQLEIYDQ IPQELRDAVE DVILNRTPEG TDALLAIADK YKGDGSVKEA ETEEWRGWDV NKRLEHALVK GITTHIVEDT EESRQSFARP IEVIEGPLMS GMNIVGDLFG AGKMFLPQVV KSARVMKQAV AHLIPFIELE KGDKPEAKGK ILMATVKGDV HDIGKNIVGV VLGCNGYDIV DLGVMVPAEK ILQVAKEQKC DIIGLSGLIT PSLDEMVHVA REMQRQDFHL PLMIGGATTS KAHTAVKIEP KYSNDAVVYV TDASRAVGVA TQLLSKELKA GFVQKTREEY IDVRERTANR SARTERLSYA AAIAKKPQFD WATYTPVKPT FTGTRVLDNI DLNVLAEYID WTPFFISWDL AGKFPRILED EVVGEAATAL YKDAREMLTK LIDEKLISAR AVFGFWPANQ VHDDDIELYG DDGKPMARLH HLRQQIIKTD GKPNFSLADF VAPKDSEVTD YVGGFITTAG IGAEEVAKAY QDAGDDYNSI MVKALADRLA EACAEWLHQQ VRKEHWGYAK DEALDNEALI KEQYSGIRPA PGYPACPDHT EKATLFALLD PEAQEMRAGR SGVFLTEHYA MFPAAAVSGW YFAHPQAQYF AVGKVDKDQV QSYTSRKGQE LSLTERWLAP NLGYDN // ID Q3KCI5_PSEPF Unreviewed; 308 AA. AC Q3KCI5; DT 08-NOV-2005, integrated into UniProtKB/TrEMBL. DT 08-NOV-2005, sequence version 1. DT 27-MAY-2015, entry version 65. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:ABA74520.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:ABA74520.1}; GN Name=mmuM {ECO:0000313|EMBL:ABA74520.1}; GN OrderedLocusNames=Pfl01_2779 {ECO:0000313|EMBL:ABA74520.1}; OS Pseudomonas fluorescens (strain Pf0-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA74520.1, ECO:0000313|Proteomes:UP000002704}; RN [1] {ECO:0000313|EMBL:ABA74520.1, ECO:0000313|Proteomes:UP000002704} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA74520.1, RC ECO:0000313|Proteomes:UP000002704}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; ABA74520.1; -; Genomic_DNA. DR RefSeq; WP_011334192.1; NC_007492.2. DR RefSeq; YP_348510.1; NC_007492.2. DR ProteinModelPortal; Q3KCI5; -. DR STRING; 205922.Pfl01_2779; -. DR EnsemblBacteria; ABA74520; ABA74520; Pfl01_2779. DR KEGG; pfo:Pfl01_2779; -. DR PATRIC; 19887719; VBIPseFlu44242_2812. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; QPEVMAA; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; PFLU205922:GJBD-2825-MONOMER; -. DR Proteomes; UP000002704; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002704}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:ABA74520.1}; KW Transferase {ECO:0000313|EMBL:ABA74520.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 206 206 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 282 282 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 308 AA; 33087 MW; 434795578981974E CRC64; MTRANVRVLD GGMGRELKRI GAPFRQPEWS ALALIEAPEY VLQAHQAFVT AGARIITTNS YAVVPFHIGD ERFAEQGRAL AERAGRLARQ AAGESTDPVT VAGSLPPALG SYRPDLFDHQ GSVAIHRELI AGLQAHVDVW LAETHSSIAE VRAVVEALGT DPAPLWVSFT LLDEEGREPR LRSNEAVADA VRVAAELGAK AVLFNCSQPE VMAAALIEAR AVIENLDHPV ELGVYANAFP PVSAKAEANS DLLEIRRDLG PESYLDWSKS WVAAGASIVG GCCGIGPEHI AQLHLHLHYQ KGEEAAHE // ID Q3M8M4_ANAVT Unreviewed; 1178 AA. AC Q3M8M4; DT 25-OCT-2005, integrated into UniProtKB/TrEMBL. DT 25-OCT-2005, sequence version 1. DT 27-MAY-2015, entry version 78. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABA22662.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABA22662.1}; GN OrderedLocusNames=Ava_3052 {ECO:0000313|EMBL:ABA22662.1}; OS Anabaena variabilis (strain ATCC 29413 / PCC 7937). OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena. OX NCBI_TaxID=240292 {ECO:0000313|EMBL:ABA22662.1, ECO:0000313|Proteomes:UP000002533}; RN [1] {ECO:0000313|Proteomes:UP000002533} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29413 / PCC 7937 {ECO:0000313|Proteomes:UP000002533}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000117; ABA22662.1; -; Genomic_DNA. DR RefSeq; WP_011319793.1; NC_007413.1. DR RefSeq; YP_323557.1; NC_007413.1. DR ProteinModelPortal; Q3M8M4; -. DR STRING; 240292.Ava_3052; -. DR EnsemblBacteria; ABA22662; ABA22662; Ava_3052. DR KEGG; ava:Ava_3052; -. DR PATRIC; 35427075; VBIAnaVar43351_4079. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; ILESWIT; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; AVAR240292:GCY3-3089-MONOMER; -. DR Proteomes; UP000002533; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002533}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABA22662.1}; KW Transferase {ECO:0000313|EMBL:ABA22662.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 228 228 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 737 737 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1178 AA; 130838 MW; D5C01DABA088286B CRC64; MTHPFLKRLH SPEFPVIVFD GAMGTNLQTQ NLTAEDFGGV QYEGCNEYLV HTKPEAVAKV HRDFLAVGAD VIETDTFGAT SIVLAEYDLA DQTYYLNKKA AELAKSVAAE FSTPDKPRFV AGSIGPTTKL PTLGHIDFDT LKTAFAEQAE ALLDGGVDLL LVETCQDVLQ IKAALNGIEE VFAKRGERIP LMVSVTMESM GTMLVGSEIN AVLTILEPFP IDILGLNCAT GPDLMKPHIK YLAEHSPFVV SCIPNAGLPE NVGGQAHYRL TPMELRMALM HFVEDLGVQV IGGCCGTRPE HIQQLAEIAK DLKPKVRQPS LEPAAASIYS TQTYEQDNSF LIVGERLNAS GSKKCRDLLN AEDWDGLVSM ARSQVKEGAH ILDVNVDYVG RDGVRDMHEL VSRIVNNVTL PLMLDSTEWE KMEAGLKVAG GKCLLNSTNY EDGEPRFLKV LELAKKYGAG VVIGTIDEEG MARTAEKKFQ IAQRAYRQAV EYGIPPTEIF FDTLALPIST GIEEDRENGK ATIESISRIR QQLPGCHVIL GVSNISFGLS PASRMVLNSV FLHEATAAGM DAAIVSASKI LPLSKIEDRH QEVCRQLIYD QRQFDGDVCI YDPLTELTKL FEGVTTKRNK GVDESLPIEE RLKRHIIDGE RIGLEAQLTK ALEQYPPLEI INTFLLDGMK VVGELFGSGQ MQLPFVLQSA ETMKAAVAYL EPFMEKSESG NNAKGKVIIA TVKGDVHDIG KNLVDIILSN NGYKVINLGI KQPVENIIEA YNQHKADCIA MSGLLVKSTA FMKENLEVFN EKGINVPVIL GGAALTPKFV HKDCQNTYKG KVIYGKDAFS DLHFMDKLMP AKATGKWDNF LGFLDEVETE ETEPTNSQSP VPNSQSPVPS PQSPVPVDTR RSEAVAVDIP RPTPPFWGTQ LLQPSDISLE EIFWHMDLQA LVAGQWQFRK PKEQSKEEYQ AFLNEQVYPI LETWKQRIIA ENLLHPQVIY GYFPCQSEGN TLYVYDSNSP NAKEITQFEF PRQKSSRRLC IADFFAPKDS GIIDVFPMQA VTVGDIATEF AQKLFANNQY TDYLYFHGLA VQVAEALAEW THARIRRELG FGAEEPDNIR DILAQRYQGS RYSFGYPACP NIQDQFKQLD LLETSRINLY MDESEQLYPE QSTTAIITYH PVAKYFTA // ID Q3SM63_THIDA Unreviewed; 1237 AA. AC Q3SM63; DT 11-OCT-2005, integrated into UniProtKB/TrEMBL. DT 11-OCT-2005, sequence version 1. DT 27-MAY-2015, entry version 74. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AAZ96187.1}; GN OrderedLocusNames=Tbd_0234 {ECO:0000313|EMBL:AAZ96187.1}; OS Thiobacillus denitrificans (strain ATCC 25259). OC Bacteria; Proteobacteria; Betaproteobacteria; Hydrogenophilales; OC Hydrogenophilaceae; Thiobacillus. OX NCBI_TaxID=292415 {ECO:0000313|EMBL:AAZ96187.1, ECO:0000313|Proteomes:UP000008291}; RN [1] {ECO:0000313|EMBL:AAZ96187.1, ECO:0000313|Proteomes:UP000008291} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25259 {ECO:0000313|EMBL:AAZ96187.1, RC ECO:0000313|Proteomes:UP000008291}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000116; AAZ96187.1; -; Genomic_DNA. DR RefSeq; WP_011310747.1; NC_007404.1. DR RefSeq; YP_313992.1; NC_007404.1. DR ProteinModelPortal; Q3SM63; -. DR SMR; Q3SM63; 660-1237. DR STRING; 292415.Tbd_0234; -. DR EnsemblBacteria; AAZ96187; AAZ96187; Tbd_0234. DR KEGG; tbd:Tbd_0234; -. DR PATRIC; 23966609; VBIThiDen82923_0236. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; TDEN292415:GHWG-237-MONOMER; -. DR Proteomes; UP000008291; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008291}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AAZ96187.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008291}; KW Transferase {ECO:0000313|EMBL:AAZ96187.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 256 256 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 319 319 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 320 320 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 767 767 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1237 AA; 135003 MW; B5794032D47AD422 CRC64; MRDCPASLTT MSRTDLLHSL LAQRILVLDG AMGTMIQSYK LGEADYRGER FADFAHDLKG NNDLLCLTQP AIIKEIHAKY LAAGADILET NSFNATAISM ADYRMEHLVP ELNFAAAKLA REAADEATAQ NPAKPRFVAG VLGPTSRTAT ISPDVNDPGF RNVTFDQLRE AYLEAIDGLV KGGADILMVE TIFDTLNAKA ALFAIEEYFE INNMRLPVMI SGTITDASGR TLSGQTGEAF WNSVRHARPL SIGLNCALGP DLLRQYVEEL SNKAEVFISA HPNAGLPNAF GEYDMDGAEM AKHIGEWARA GLLNIVGGCC GTSPSHIAAI AKAVEGVAPR VPPVLEPAMR LSGLEPFNVG KDSLFVNVGE RTNVTGSKAF ARMILEGRYD DALSVARQQV ENGAQVIDIN MDEGMLDAEA AMVRFLHLIA SEPDIARVPI MIDSSKWNVI EAGLKCIQGK GIVNSISMKE GEAEFIERAK LCLRYGAAVI VMAFDETGQA DTYARKTEIC TRAYKLLTET VGFPAEDIIF DPNIFAVATG IEEHANYAVD FIEATRWIRQ NLPYAHVSGG VSNVSFSFRG NDAVREAIHT AFLYHAIQAG MDMGIVNAGQ LGVYENLDPE LKERVEDVLL NRRADATERL VAFAEGVKGG AKEKVEDLAW RSLPVNERLT HALVQGITQY IVEDTEAARL EAERPLHVIE GPLMAGMNVV GDLFGAGKMF LPQVVKSARV MKQAVAHLIP YIEADKRAGD SQSAGKIVMA TVKGDVHDIG KNIVGVVLGC NGYEIVDLGV MVPAQKILDA AREHKADIIG LSGLITPSLE EMAHVAKEMQ RQGFTIPLLI GGATTSLAHT AVKIEPNYEH PVVYVKDASR AVGVCTQLLS GELRDAFAAE VRADYAQTRA RHLKHKSDTA RLTLADARAN KFGIDWASYT PPVPNQPGVH VLKAYDLAKL VETIDWTPFF ASWELHGKYP KILDDEVVGA EATKLFSDAQ AMLNRMVAEN WVEARAVFGL FPANAVDDDI EVYADESRSQ ALTTWHNLRQ QAKKPEGRAN LCLADFVAPK ASGLKDYLGA FVVTAGIGED ERAKAFEAAH DDYSAILFKS LCDRLAEAFA EHLHLRVRRE FWGYAADEAL PNDDLIAEKY RGIRPAPGYP ACPEHSEKAA LFGLLDATNA IGVELTENFA MWPGAAVSGF YLSHPDSQYF AVAKIERDQV EDYARRKGWD VKTAERWLGP NLGYQPE // ID Q3SVZ1_NITWN Unreviewed; 1290 AA. AC Q3SVZ1; DT 11-OCT-2005, integrated into UniProtKB/TrEMBL. DT 11-OCT-2005, sequence version 1. DT 27-MAY-2015, entry version 73. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABA03550.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:ABA03550.1}; GN OrderedLocusNames=Nwi_0283 {ECO:0000313|EMBL:ABA03550.1}; OS Nitrobacter winogradskyi (strain Nb-255 / ATCC 25391). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Nitrobacter. OX NCBI_TaxID=323098 {ECO:0000313|EMBL:ABA03550.1, ECO:0000313|Proteomes:UP000002531}; RN [1] {ECO:0000313|EMBL:ABA03550.1, ECO:0000313|Proteomes:UP000002531} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nb-255 / ATCC 25391 {ECO:0000313|Proteomes:UP000002531}; RX PubMed=16517654; DOI=10.1128/AEM.72.3.2050-2063.2006; RA Starkenburg S.R., Chain P.S.G., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000115; ABA03550.1; -; Genomic_DNA. DR RefSeq; WP_011313616.1; NC_007406.1. DR RefSeq; YP_316902.1; NC_007406.1. DR ProteinModelPortal; Q3SVZ1; -. DR SMR; Q3SVZ1; 658-1241. DR STRING; 323098.Nwi_0283; -. DR EnsemblBacteria; ABA03550; ABA03550; Nwi_0283. DR KEGG; nwi:Nwi_0283; -. DR PATRIC; 22696922; VBINitWin102302_0311. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; QPFFNAW; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; NWIN323098:GJEG-289-MONOMER; -. DR Proteomes; UP000002531; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002531}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:ABA03550.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002531}; KW Transferase {ECO:0000313|EMBL:ABA03550.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 253 253 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 316 316 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 773 773 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1290 AA; 140731 MW; E37A08A59E688DAE CRC64; MTRVTKSSNT IADKFRALAR ERILVLDGAM GTMIQNRGFD EAAFRGERFK NFHRDVRGNN DLLILTQPQA IEDIHAQYLR AGADLVATNT FSSTSIAQAD YDMSDLVYEL NREGAKLARS AAEKVSAEDG KPRFVVGAIG PTNRTASISP DVANPGYRAV TFDDLRKSYG EQINGLLDGG ADLLLVETIF DTLNAKAALY AIAEIGEQRG IDIPVMVSGT ITDKSGRLLS GQLPEAFWHS VRHAGPITIG FNCALGAEDL RAHVAEIGRV ADTLVCAYPN AGLPNEFGEY DESPDYMARL IGEFAQAGLV NVVGGCCGTT PDHIAAIAAA VAPHKPRVVP VIEPRLRLSG LEPFSLTSDI PFVNVGERTN VTGSAKFRNL IKAGDYAAAL DVARNQVENG AQIIDVNMDE GLLDSEAAMV TFLNLIAAEP DIARVPVMVD SSKFSVIEAG LKCLQGKPVV NSISLKEGEE KFLHEARIAR RHGAAVVVMA FDEQGQADTC QRKMEICKRA YDILVEQVGF PPEDIIFDPN IFAIATGLEE HNNYGVDFIE ATRWIRQNLP HAHISGGVSN LSFSFRGNEP VREAMHSVFL YHAIKAGMDL GIVNAGQMVI YDDIDPELRQ VCEDVVLNRD PDAGERLLNL AEKFRGQGKQ AKEADLSWRE WPVEKRLSHA LVNGITEYIE QDTEEARKSA DRPLSVIEGP LMAGMNVVGD LFGDGKMFLP QVVKSARVMK HAVAYLMPFM EEEKARNQAA GIEGAGSTSA GKILLATVKG DVHDIGKNIV GIVLQCNNYE VIDLGVMVPA AKIIETAKAE KADIVGLSGL ITPSLDEMGY FAAELERQGL NLPLLIGGAT TSRVHTAVKI DPNYRNGPVI HVNDASRAVG VVASLMSPER REAYAAGVRA EYAKISAAHF RAQQDKKRLP LAAARANAVP IDWSSYRPVK PTFLGTKAFA DYPLEELVEV IDWTPFFQVW ELAGRFPAIL DDKVVGETAR ALYDDARKML DRIVKEKWFT ASSVIGFWPA NRIGDDIAVY SDESRTTQIA TYHTLRQQLE KREGRHNAAL ADFIAPKETG IADYIGGFAV TAGLGEDEIA ARFKNANDDY SSILVKALAD RLAEAFAERM HQRVRTEFWG YAPDEALTND QLIREEYVGI RPAPGYPAQP DHTEKATLFR LLDATRATGV ELTESFAMWP GSSVSGLYYS HPESQYFGVG KIERDQVEDY AARKGMEVAE IERWLASILN YIPGQDASGK PATTPVPAPA NDASADVANH PPGCQCAVHL RLRKTTARAG // ID Q3UEP0_MOUSE Unreviewed; 212 AA. AC Q3UEP0; DT 11-OCT-2005, integrated into UniProtKB/TrEMBL. DT 11-OCT-2005, sequence version 1. DT 29-APR-2015, entry version 63. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:BAE28871.1}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|EMBL:BAE28871.1}; RN [1] {ECO:0000313|EMBL:BAE28871.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE28871.1}; RC TISSUE=Liver {ECO:0000313|EMBL:BAE28871.1}; RX PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9; RA Carninci P., Hayashizaki Y.; RT "High-efficiency full-length cDNA cloning."; RL Methods Enzymol. 303:19-44(1999). RN [2] {ECO:0000313|EMBL:BAE28871.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE28871.1}; RC TISSUE=Liver {ECO:0000313|EMBL:BAE28871.1}; RX PubMed=11042159; DOI=10.1101/gr.145100; RA Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M., RA Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.; RT "Normalization and subtraction of cap-trapper-selected cDNAs to RT prepare full-length cDNA libraries for rapid discovery of new genes."; RL Genome Res. 10:1617-1630(2000). RN [3] {ECO:0000313|EMBL:BAE28871.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE28871.1}; RC TISSUE=Liver {ECO:0000313|EMBL:BAE28871.1}; RX PubMed=11076861; DOI=10.1101/gr.152600; RA Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P., RA Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., RA Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., RA Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., RA Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., RA Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., RA Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.; RT "RIKEN integrated sequence analysis (RISA) system--384-format RT sequencing pipeline with 384 multicapillary sequencer."; RL Genome Res. 10:1757-1771(2000). RN [4] {ECO:0000313|EMBL:BAE28871.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE28871.1}; RC TISSUE=Liver {ECO:0000313|EMBL:BAE28871.1}; RG The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium; RT "Functional annotation of a full-length mouse cDNA collection."; RL Nature 409:685-690(2001). RN [5] {ECO:0000313|EMBL:BAE28871.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE28871.1}; RC TISSUE=Liver {ECO:0000313|EMBL:BAE28871.1}; RG The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team; RT "Analysis of the mouse transcriptome based on functional annotation of RT 60,770 full-length cDNAs."; RL Nature 420:563-573(2002). RN [6] {ECO:0000313|EMBL:BAE28871.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE28871.1}; RC TISSUE=Liver {ECO:0000313|EMBL:BAE28871.1}; RA Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K., RA Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S., RA Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N., RA Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D., RA Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A., RA Muramatsu M., Hayashizaki Y.; RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000313|EMBL:BAE28871.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE28871.1}; RC TISSUE=Liver {ECO:0000313|EMBL:BAE28871.1}; RG The FANTOM Consortium; RG Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group); RT "The Transcriptional Landscape of the Mammalian Genome."; RL Science 309:1559-1563(2005). RN [8] {ECO:0000313|EMBL:BAE28871.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE28871.1}; RC TISSUE=Liver {ECO:0000313|EMBL:BAE28871.1}; RX PubMed=16141073; DOI=10.1126/science.1112009; RG RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium; RT "Antisense Transcription in the Mammalian Transcriptome."; RL Science 309:1564-1566(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; AK149431; BAE28871.1; -; mRNA. DR UniGene; Mm.329582; -. DR UniGene; Mm.423099; -. DR ProteinModelPortal; Q3UEP0; -. DR SMR; Q3UEP0; 10-159. DR STRING; 10090.ENSMUSP00000096912; -. DR PRIDE; Q3UEP0; -. DR UCSC; uc007rlj.1; mouse. DR Genevestigator; Q3UEP0; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; SQ SEQUENCE 212 AA; 23730 MW; 5327C99822ECD764 CRC64; MAPVAGKKAK KGILERLNAG EVVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAVRQLH REFLRAGSNV MQTFTFYASE DKLENRGNYV AEKISGQKVN EAACDIARQV ADEGDALVAG GVSQTPSYLS CKSEVEVKKI FRQQLEVFMK KNVDFLIAEV SKGNPFRKKE TFLTLRRPEQ DAVQTSTRSD NIYLTFQIFF HLRPLQPLTQ FT // ID Q3YUX1_SHISS Unreviewed; 1227 AA. AC Q3YUX1; DT 27-SEP-2005, integrated into UniProtKB/TrEMBL. DT 27-SEP-2005, sequence version 1. DT 01-APR-2015, entry version 81. DE SubName: Full=B12-dependent homocysteine-N5-methyltetrahydrofolate transmethylase, repressor of metE and metF {ECO:0000313|EMBL:AAZ90691.1}; GN Name=metH {ECO:0000313|EMBL:AAZ90691.1}; GN OrderedLocusNames=SSON_4190 {ECO:0000313|EMBL:AAZ90691.1}; OS Shigella sonnei (strain Ss046). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=300269 {ECO:0000313|EMBL:AAZ90691.1, ECO:0000313|Proteomes:UP000002529}; RN [1] {ECO:0000313|EMBL:AAZ90691.1, ECO:0000313|Proteomes:UP000002529} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ss046 {ECO:0000313|EMBL:AAZ90691.1, RC ECO:0000313|Proteomes:UP000002529}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000038; AAZ90691.1; -; Genomic_DNA. DR RefSeq; WP_000096019.1; NC_007384.1. DR RefSeq; YP_312926.1; NC_007384.1. DR ProteinModelPortal; Q3YUX1; -. DR SMR; Q3YUX1; 651-1227. DR STRING; 300269.SSON_4190; -. DR EnsemblBacteria; AAZ90691; AAZ90691; SSON_4190. DR KEGG; ssn:SSON_4190; -. DR PATRIC; 18743393; VBIShiSon107113_4959. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SSON300269:GJJF-4185-MONOMER; -. DR Proteomes; UP000002529; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002529}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AAZ90691.1}; KW Transferase {ECO:0000313|EMBL:AAZ90691.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136056 MW; 2186C495FEDC616D CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV VAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF ETLGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNEPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID Q3ZKK0_SHIBL Unreviewed; 1227 AA. AC Q3ZKK0; DT 27-SEP-2005, integrated into UniProtKB/TrEMBL. DT 27-SEP-2005, sequence version 1. DT 29-APR-2015, entry version 62. DE SubName: Full=B12-dependent homocysteine-N5-methyltetrahydrofolate transmethylase {ECO:0000313|EMBL:AAW65980.1}; GN Name=metH {ECO:0000313|EMBL:AAW65980.1}; GN ORFNames=EbMetH01 {ECO:0000313|EMBL:AAW65980.1}; OS Shimwellia blattae (Escherichia blattae). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shimwellia. OX NCBI_TaxID=563 {ECO:0000313|EMBL:AAW65980.1}; RN [1] {ECO:0000313|EMBL:AAW65980.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 4481 {ECO:0000313|EMBL:AAW65980.1}; RX PubMed=16088217; DOI=10.1159/000085788; RA Andres S., Wiezer A., Bendfeldt H., Waschkowitz T., Toeche-Mittler C., RA Daniel R.; RT "Insights into the genome of the enteric bacterium Escherichia RT blattae: cobalamin (B12) biosynthesis, B12-dependent reactions, and RT inactivation of the gene region encoding B12-dependent glycerol RT dehydratase by a new mu-like prophage."; RL J. Mol. Microbiol. Biotechnol. 8:150-168(2004). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AY739651; AAW65980.1; -; Genomic_DNA. DR RefSeq; YP_006321253.1; NC_017910.1. DR ProteinModelPortal; Q3ZKK0; -. DR SMR; Q3ZKK0; 652-1227. DR KEGG; ebt:EBL_c36910; -. DR KO; K00548; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AAW65980.1}; KW Transferase {ECO:0000313|EMBL:AAW65980.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135985 MW; BFD9265AC6928E74 CRC64; MSNKTEKLHQ QLAQRILVLD GGMGTMIQGY RLDERAFRGE RFADWPCDLK GNNDLLVLTQ PEIITAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINYAAARL ARECADAWSA REPEKPRYVA GVLGPTNRTA SISPDVNDPA YRNITFDQLV AAYRESTRAL VEGGVDLILI ETVFDTLNAK AAIFAVETEF EALGQSLPVM ISGTITDASG RTLSGQTTEA FYNSLRHAGA LSFGLNCALG PDELRQYVAE MSRIAECYVS AHPNAGLPNA FGEYDLDADT MAAQVKEWAE SGFLNIVGGC CGTTPAHIAA MSRAVAGVAP RKRPVLPVAC RLSGLEPLNI GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVEAFTEHA KRVRRYGAAM VVMAFDEQGQ ADTRERKREI CTRAYNILTR EVGFPPEDII FDPNIFAVAT GIEEHNNYAV DFIGACEDIK RDLPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPG ELRDAVEDVI LNRRDDGTER LLALAEKYRG SKTDEAANTQ LAEWRNWEVK KRLEYSLVKG ITEFIEQDTE EARQQADRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EKGQSNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIIDL GVMVPAEKIL KTAREENADL IGLSGLITPS LDEMVHVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVSSL LSATQRDDFI ARTRKEYETV RTQHGRKKPR TPPVTLQAAR ENDFAFDWES YTPPVAHRLG VQEVTASIET LRNYIDWTPF FMTWTLAGKY PRILEDEVVG EEAQRLFADA NAMLDMLSET KALNPRGVVG LFPANRVGDD VEIYQDETRT RVLAVGHHLR QQTEKVGYAN YCLADFVAPR HTRKADYIGA FAVTGGLEED ALADAYEARH DDYNKIMVKS VADRLAEAFA EYLHERVRKV YWGYAPTENL SNEALIRENY QGIRPAPGYP ACPEHTEKET IWKLLDVEAR IGMKLTESCA MWPGASVSGW YFSHPESKYF AVAQIQRDQV EDYARRKGMS LAEAERWLAP NLGYDAD // ID Q44371_RHIRD Unreviewed; 315 AA. AC Q44371; DT 01-NOV-1996, integrated into UniProtKB/TrEMBL. DT 01-NOV-1996, sequence version 1. DT 01-APR-2015, entry version 52. DE SubName: Full=Msh {ECO:0000313|EMBL:AAC44507.1}; GN Name=msh {ECO:0000313|EMBL:AAC44507.1}; OS Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium OS radiobacter). OG Plasmid Ti {ECO:0000313|EMBL:AAC44507.1}. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium; OC Agrobacterium tumefaciens complex. OX NCBI_TaxID=358 {ECO:0000313|EMBL:AAC44507.1}; RN [1] {ECO:0000313|EMBL:AAC44507.1} RP NUCLEOTIDE SEQUENCE. RC PLASMID=Ti {ECO:0000313|EMBL:AAC44507.1}; RX PubMed=8809772; DOI=10.1111/j.1365-2958.1996.tb02640.x; RA Fuqua C., Winans S.C.; RT "Localization of OccR-activated and TraR-activated promoters that RT express two ABC-type permeases and the traR gene of Ti plasmid RT pTiR10."; RL Mol. Microbiol. 20:1199-1210(1996). RN [2] {ECO:0000313|EMBL:AAC44507.1} RP NUCLEOTIDE SEQUENCE. RC PLASMID=Ti {ECO:0000313|EMBL:AAC44507.1}; RA Winans S.C., Zhu J., Oger P.M., Schrammeijer B., Hooykaas P.J., RA Farrand S.K.; RT "Octopine-type Ti plasmid sequence."; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF242881; AAC44507.1; -; Genomic_DNA. DR PIR; S77571; S77571. DR RefSeq; NP_059707.1; NC_002377.1. DR RefSeq; WP_010892395.1; NC_002377.1. DR ProteinModelPortal; Q44371; -. DR GeneID; 1224226; -. DR KEGG; pg:1224226; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Plasmid {ECO:0000313|EMBL:AAC44507.1}. SQ SEQUENCE 315 AA; 33782 MW; 7E2E08F98DE9C8FF CRC64; MSSKVTILDG GMGRELLRNG APFRQPEWSA LSLIEAPEFV KMAHDAFVAA GAEVITTNSY ALVPFHIGDQ ALPHMGLLSP IYPRARSCRR AEGTTVCTGC RLSAPRLRLL PARFVRCRQG ACHSRYPRQS PKLLTSISGS PRPRAPSRRS KQIRNDIGLR LRGPAVGFLY ARRTTKSVAD VICLVSVPTL VSGEAVAQRR SQSSAACAGA LLFNCSQAEI MEAGVKSANQ ALKADNLDIP IGLRQRLVPK PETEESLAAN DGLSGLRDDL NPSGYLQFAQ RWVSAGATII GGCCGIGPEH IAELKDTFDP QPAAA // ID Q46L03_PROMT Unreviewed; 1182 AA. AC Q46L03; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 27-MAY-2015, entry version 77. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:AAZ57825.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AAZ57825.1}; GN OrderedLocusNames=PMN2A_0333 {ECO:0000313|EMBL:AAZ57825.1}; OS Prochlorococcus marinus (strain NATL2A). OC Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae; OC Prochlorococcus. OX NCBI_TaxID=59920 {ECO:0000313|EMBL:AAZ57825.1, ECO:0000313|Proteomes:UP000002535}; RN [1] {ECO:0000313|EMBL:AAZ57825.1, ECO:0000313|Proteomes:UP000002535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NATL2A {ECO:0000313|EMBL:AAZ57825.1, RC ECO:0000313|Proteomes:UP000002535}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000095; AAZ57825.1; -; Genomic_DNA. DR RefSeq; WP_011293867.1; NC_007335.2. DR RefSeq; YP_291528.1; NC_007335.2. DR ProteinModelPortal; Q46L03; -. DR STRING; 59920.PMN2A_0333; -. DR EnsemblBacteria; AAZ57825; AAZ57825; PMN2A_0333. DR KEGG; pmn:PMN2A_0333; -. DR PATRIC; 23024053; VBIProMar14922_0966. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR PhylomeDB; Q46L03; -. DR BioCyc; PMAR59920:GI1O-983-MONOMER; -. DR Proteomes; UP000002535; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002535}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AAZ57825.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002535}; KW Transferase {ECO:0000313|EMBL:AAZ57825.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 226 226 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 292 292 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 744 744 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1182 AA; 131348 MW; 165B5E978D47E939 CRC64; MTHFLDYLNS EKRPIIVFDG ATGTSLQDQQ LTADDYGGAS LEGCNENLVL TSVSSVEKVH QSFLEAGCDV IETNTFGATS IVLDEYGIGN KAYEINFKAA QIARSIANKY QTAEKPRFVA GSIGPTTKLP TLGHISFDEL KKSYLEQAKA LIEGGIDLFL IETCQDVLQI KAALQSVNEA IGDGIKIPVM VSVTMETTGQ MLIGSDISSI TTILEPFNID ILGLNCATGP EEMKDHIKYL SEHSPFHISC IPNAGLPENV GGKAHYRLTP MELKFQLSHF INDLGVQLIG GCCGTRPEHI KQLSDLSLEL LSSDRRLINL SKERSIIPAA SSIYESIPYE QDNSFLIVGE RLNASGSKKV RELLNIEDWD GLVGIAKSQL KENAHVLDVN VDFVGRNGIE DMSNLVKRLV NNINLPLMLD STDYEKMESG LKHAGGKCIL NSTNYEDGQD RFHKVIDLAK EHGSAVVIGT IDEDGMARSA EKKAEIATRA FKDATNSGLK PYEIFYDPLA LPISTGLEED RKNGFETIKA IKLIKDRHPQ VHLILGISNV SFGLSSSARV VLNSIFLNEA IKAGLDSAIV SPSKILPLNK ISEEEIKICL DLIYDKRIID NSVCTYDPLT TLTSYFDDSK KLLNNSSIDE DINLPIEDKL KNHIIDGEKT NLHSNLDLAL NKYKPLVIIN EYLLDGMKVV GELFGSGQMQ LPFVLQSAET MKYAVSYLED FMDKSEVNQS KGKFIIATVK GDVHDIGKNL VDIILSNNGY DVINLGIKQD VNAIINAQKE HHADCIAMSG LLVKSTAFMK DNLKALNEED IDVPIILGGA ALTPKFVNQD CASVYKGKVI YGRDAFTDLK FMDAYMKAKL ANNWNNKTGF SEGAPEGITI GTYKSSNSDP KVIKESLEVK KVNDNSRSKD ISSVKSIKPP FLGPKVLLEK DIDLSNVYKF LDRNALFAGQ WQMKRSKDMS ASDYKEFLKK KAEPKLDYWM NKIINDNLIS PSLVYGYFPC GREGNYLNVY DTDHKSLLGK FLLPRQRSGK RYCIADFYND LVDNHPSDYL PMQAVTMGEK ASDYSHKLFS KDSYSDYLFF HGLTVQLAEA LAEYIHSIIR IECGFKYEEP DNIKDILDVK YRGCRYSFGY PACPEVSDSR KQLDWLDADK INISMDESEQ LHPEQSTTAI VALHPVAKYF GI // ID Q477D3_CUPPJ Unreviewed; 351 AA. AC Q477D3; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 27-MAY-2015, entry version 57. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:AAZ59500.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AAZ59500.1}; GN OrderedLocusNames=Reut_A0118 {ECO:0000313|EMBL:AAZ59500.1}; 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 {ECO:0000313|EMBL:AAZ59500.1, ECO:0000313|Proteomes:UP000002697}; RN [1] {ECO:0000313|Proteomes:UP000002697} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JMP134 / LMG 1197 {ECO:0000313|Proteomes:UP000002697}; 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; AAZ59500.1; -; Genomic_DNA. DR RefSeq; WP_011296308.1; NC_007347.1. DR RefSeq; YP_294344.1; NC_007347.1. DR STRING; 264198.Reut_A0118; -. DR EnsemblBacteria; AAZ59500; AAZ59500; Reut_A0118. DR KEGG; reu:Reut_A0118; -. DR PATRIC; 20225667; VBIRalEut24049_0712. DR eggNOG; COG0646; -. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; CPIN264198:GIW3-118-MONOMER; -. DR Proteomes; UP000002697; Chromosome 1. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002697}; KW Methyltransferase {ECO:0000313|EMBL:AAZ59500.1}; KW Transferase {ECO:0000313|EMBL:AAZ59500.1}. SQ SEQUENCE 351 AA; 38186 MW; 85ED00E1F45A7F1E CRC64; MSAPEQPSVR PYTRAANLPR LLRERILILD GAMGTMIQRY KLTEADYRGE RFAEHKVDVK GNNELLLLTR PQVISEIHEQ YLAAGADIIE TNTFGATSVA QEDYKMAELA YEMNVEAAKL ARAACDKYST PDKPRFVAGA FGPTPKTASI SPDVNDPGAR NITFEELRES YYEQGKGLLD GGADVFLVET IFDTLNAKAC LFAIDQLFED TGERLPVMIS GTVTDASGRI LSGQTVEAFW NSLRHVKPVT FGLNCALGAT LMRPYIAELA KVCDVAISCY PNAGLPNPMS ETGFDETPEV TSSLVDEFAA SGLVNLVGGC CGTTPEHIAA IAERMAKRNP RTWPGQYSEA A // ID Q47K26_DECAR Unreviewed; 1220 AA. AC Q47K26; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 27-MAY-2015, entry version 70. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:AAZ44805.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AAZ44805.1}; GN OrderedLocusNames=Daro_0046 {ECO:0000313|EMBL:AAZ44805.1}; OS Dechloromonas aromatica (strain RCB). OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Rhodocyclaceae; Dechloromonas. OX NCBI_TaxID=159087 {ECO:0000313|EMBL:AAZ44805.1, ECO:0000313|Proteomes:UP000000550}; RN [1] {ECO:0000313|Proteomes:UP000000550} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RCB {ECO:0000313|Proteomes:UP000000550}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000089; AAZ44805.1; -; Genomic_DNA. DR RefSeq; WP_011285815.1; NC_007298.1. DR RefSeq; YP_283275.1; NC_007298.1. DR ProteinModelPortal; Q47K26; -. DR SMR; Q47K26; 652-898. DR STRING; 159087.Daro_0046; -. DR EnsemblBacteria; AAZ44805; AAZ44805; Daro_0046. DR KEGG; dar:Daro_0046; -. DR PATRIC; 21598660; VBIDecAro89105_0046. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; DARO159087:GI5B-46-MONOMER; -. DR Proteomes; UP000000550; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000550}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AAZ44805.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000550}; KW Transferase {ECO:0000313|EMBL:AAZ44805.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 763 763 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1220 AA; 133227 MW; E641F2FB435C7DD5 CRC64; MQPNRTAELS SLLQQRLLVL DGAMGTMIQR HGLQEADYRG ERFKDHPHDL KGNNDLLVLT RPDIIGGIHR EYLEAGADIL ETCTFNSTAV SQADYNLSEL VYELNFEGAK LARQLCDEFT AANPAKPRFV AGVLGPTSRT ASISPDVNDP GYRNVTFDEL VANYVEAITG LVEGGADILL VETVFDTLNA KAALFAIEKF FDIAQRRWPV MISGTITDAS GRTLSGQTAE AFWNSLRHVQ PVSFGLNCAL GAKELRQYVE ELSRVCDCYV SAHPNAGLPN AFGGYDETAD MLADEIESWA KAGIVNIVGG CCGTSPEHIA AIAQRVATVS PRQRPAIEPA LRLSGLEAFN VTPGSLYVNV GERTNVTGSK AFARMILEGR FDDALAVARQ QVENGAQIID INMDEAMLDS LAAMDKFLKL IASEPDISRV PIMIDSSKWE VIEAGLKCIQ GKGIVNSISM KEGEAKFIEQ AKLARRYGAA VIVMAFDEKG QADTFARKTE ISKRAYDLLL SIGFPAEDII FDPNIFAIAT GIPEHDNYAV DFIESVRWIK QNLPHAHISG GVSNVSFSFR GNDPVREAIH TVFLYHAIKN GMTMGIVNAG MLGIYDDLEP ELRQKVEDVV LNRNPNAGEA LVDFAQTVKE GKAKDTGPDL SWREQSVEKR LEHALIKGIT DFVVADTEEV RAQLEAEGKP PLAVIEGPLM AGMNHVGDLF GAGKMFLPQV VKSARVMKQA VAHLLPYIEA EKTRTGLGSK GKILMATVKG DVHDIGKNIV GVVLGCNGYD VIDLGVMVSC DNILKAALEH RVDIIGLSGL ITPSLEEMAH VASEMQRQGM KQPLLIGGAT TSRAHTAIKI APNTEGAVVY VPDASRAVGV ATKLLSTEQR DGYMAEIVAE YEAVRAEHSG RKGATMVTLA EARANRFTWN EPFTPAKPKQ LGLQTLNPSL SDLALLIDWT PFFQSWDLAG RYPAILDNET VGETARQLFT DAKEMLGKII SENWLSARAV FGLYPAKAEN EDIIIYSDES RTTELTRWVG LRQQHKQPKG RFNMALADFI GENDYVGAFA VTAGHRIEER VAAFEAAHDD YSAIMLKSLA DRLAEAAAEW LHLQVRTQYW GYAHDETFTN AELIAEQYKG IRPAPGYPAC PDHTAKRELF ALLDAPANAG MQLTESCAMT PAAAVSGFYI AHPAAAYFAI PKIGRDQLED WAARKGMSLK DAEYWLAPLL // ID Q47NW1_THEFY Unreviewed; 1158 AA. AC Q47NW1; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 27-MAY-2015, entry version 84. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:AAZ55858.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AAZ55858.1}; GN OrderedLocusNames=Tfu_1825 {ECO:0000313|EMBL:AAZ55858.1}; OS Thermobifida fusca (strain YX). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptosporangineae; Nocardiopsaceae; Thermobifida. OX NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ55858.1, ECO:0000313|Proteomes:UP000000434}; RN [1] {ECO:0000313|Proteomes:UP000000434} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YX {ECO:0000313|Proteomes:UP000000434}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000088; AAZ55858.1; -; Genomic_DNA. DR RefSeq; WP_011292249.1; NC_007333.1. DR RefSeq; YP_289881.1; NC_007333.1. DR ProteinModelPortal; Q47NW1; -. DR STRING; 269800.Tfu_1825; -. DR EnsemblBacteria; AAZ55858; AAZ55858; Tfu_1825. DR KEGG; tfu:Tfu_1825; -. DR PATRIC; 23904258; VBITheFus33945_1963. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; TFUS269800:GI42-1829-MONOMER; -. DR Proteomes; UP000000434; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000434}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AAZ55858.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000434}; KW Transferase {ECO:0000313|EMBL:AAZ55858.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 225 225 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 292 292 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 736 736 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1158 AA; 127293 MW; DC80819272C5A000 CRC64; MSARLSFREV LGSRVLVADG AMGTMLQTYD LSMDDFEGHE GCNEVLNITR PDVVREIHEA YLQAGVDCVE TNTFGANFGN LGEYGIAERT YELAEAGARL AREAADAYTT ADHVRYVLGS VGPGTKLPTL GHAPYAVLRD HYEQCARGLI DGGVDAIVIE TCQDLLQAKA AIVGARRARK AAGTDTPIIV QVTIETTGTM LVGSEIGAAL TSLEPLGVDM IGLNCATGPA EMSEHLRYLS HHSRIPLSCM PNAGLPELGA DGAVYPLQPH ELTEAHDTFI REFGLALVGG CCGTTPEHLA QVVERVQGRG VPDRKPHVEP AAASIYQSVP FRQDTSYLAI GERTNANGSK AFREAMLAER YDDCVEIARQ QIRDGAHMLD LCVDYVGRDG VRDMRELASR LATASTLPLV LDSTEVAVLE AGLEMLGGRA VLNSVNYEDG DGPDSRFAKV AALAVEHGAA LMALTIDEQG QARTAERKVE VAERLIRQLT TEYGIRKHDI IVDCLTFTIA TGQEESRRDA LETIEAIREL KRRHPDVQTT LGVSNVSFGL NPAARIVLNS VFLHECVQAG LDSAIVHASK ILPINRIPEE QRQVALDMIY DRRTDDYDPL QRFLQLFEGV DAQAMRASRE EELAALPLWE RLERRIVDGE AAGMEADLDE ALTQRSALDI INTTLLAGMK TVGDLFGSGQ MQLPFVLKSA EVMKAAVAYL EPHMEKVDGD LGKGRIVLAT VKGDVHDIGK NLVDIILSNN GYEVINLGIK QPISAILEAA ERHRADVIGM SGLLVKSTVV MRENLEEMNA RGVADRYPVL LGGAALTRSY VEQDLAEIFK GEVRYARDAF EGLKLMDAIM AVKRGVKGAK LPPLRTRRVK RGAQLTVTEP EKMPTRSDVA TDNPVPTPPF WGDRICKGIP LADYAAFLDE RATFMGQWGL RGSRGDGPTY EELVETEGRP RLRMWLDRIQ TEGWLEPAVV YGYYRCYSEG NDLVVLGEDE NELTRFTFPR QRRDRHLCLA DFFRPKESGE LDTVAFQVVT VGSTISKATA ELFEKNAYRD YLELHGLSVQ LTEALAEYWH TRVRAELGFA GEDPDPADLD AYFKLGYRGA RFSLGYGACP NLEDRAKIVA LLRPERVGVT LSEEFQLVPE QSTDAIVVHH PEAKYFNV // ID Q487C0_COLP3 Unreviewed; 1230 AA. AC Q487C0; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 27-MAY-2015, entry version 69. DE SubName: Full=5-methyltetrahydrofolate--homocysteine S-methyltransferase {ECO:0000313|EMBL:AAZ28519.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AAZ28519.1}; GN Name=metH {ECO:0000313|EMBL:AAZ28519.1}; GN OrderedLocusNames=CPS_1101 {ECO:0000313|EMBL:AAZ28519.1}; OS Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio OS psychroerythus). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Colwelliaceae; Colwellia. OX NCBI_TaxID=167879 {ECO:0000313|EMBL:AAZ28519.1, ECO:0000313|Proteomes:UP000000547}; RN [1] {ECO:0000313|EMBL:AAZ28519.1, ECO:0000313|Proteomes:UP000000547} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=34H / ATCC BAA-681 {ECO:0000313|Proteomes:UP000000547}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000083; AAZ28519.1; -; Genomic_DNA. DR RefSeq; WP_011041939.1; NC_003910.7. DR RefSeq; YP_267845.1; NC_003910.7. DR ProteinModelPortal; Q487C0; -. DR SMR; Q487C0; 655-1230. DR STRING; 167879.CPS_1101; -. DR EnsemblBacteria; AAZ28519; AAZ28519; CPS_1101. DR KEGG; cps:CPS_1101; -. DR PATRIC; 21465469; VBIColPsy94388_0987. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; QPFFNAW; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CPSY167879:GI48-1101-MONOMER; -. DR Proteomes; UP000000547; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000547}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AAZ28519.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000547}; KW Transferase {ECO:0000313|EMBL:AAZ28519.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 249 249 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1230 AA; 136451 MW; B4B7A00B058A0444 CRC64; MKKSSSFALF EQQLAKNILI LDGAMGTMIQ AYKFEEQDFR AERFADWHTD VKGNNDMLVL TQPEIIKAIH LEYLEAGADI LETNTFNATT IAMADYDMQE YSAEINRVAA QIAREAADEY TKKNPDRPRF VAGVLGPTNR TCSISPDVND PAYRNVTFDE LKDAYIESTL ALIEGGSDII LIETIFDTLN AKAAVFAVET VFDQLGERLP VMISGTITDA SGRTLSGQTT EAFYNSLRHA KPVSFGLNCA LGPVELRQYV AELSRICDTA VSAHPNAGLP NAFGEYDFTV EDMNTHVEEW ASSGFLNIIG GCCGTTPEHI RGMADSVAKI KPRKVEKREI ACRLSGLEAL TINKDSLFVN VGERTNVTGS AMFKRLIVEE DYDKAISVAL QQVENGAQII DINMDEGMLD SKTAMVRFLN LIAGEPDIAK VPIMIDSSKW DIIEAGLKCI QGKGIVNSIS LKEGEENFRH QAELLRRYGA AVIVMAFDEE GQADTRKRKY EICHRAYHML VDEIGYPPED IIFDPNIFAV ATGIEEHNNY AVDFIEAVDD IKKNLPYAMI SGGVSNVSFS FRGNNPVREA IHAVFLYYAI KNGMDMGIVN AGQLAIYSDL PANLKQAVED VIQNKDDGAT ERLLDIAQEF HGKAGGQASK TDLTWRELPI NARLSHALVK GINEFIIEDT EEARLASEKP LDVIEGPLMD GMNTVGDLFG AGEMFLPQVV KSARVMKQAV AYLNPYIEEG KTEISTNGKV LLATVKGDVH DIGKNIVGVV LQCNNYEIID LGVMVSCDDI LRVAKEENVD IIGLSGLITP SLDEMVYVAK EMKRTGLKLP LLIGGATTSK AHTAVKIEPQ YDEPVVYVSN ASRAVSVVSN LLSSEHKAKF FASTQEEYER VRVRHYKKGP RSSLISLEAA RANATKINFE DYTPKKPNKL GVTVLDNIDL NEVRKYIDWT PFFMTWQMSG KYPLILKHEV IGVEATSLFN DANAMLDDVI NNKKICARAV FGLFPANSNQ DDIQLYTDES RSDKLMRLHQ LRQQSKKPAG QFNRCLADYI APEDSGIEDY VGAFAVSAGF GVEDLVKVFD ADHDAYNSIL LKAVADRLAE ASAEYLHEKV RKEYWGFAPD EDLNNDALIR ESYQGIRPAP GYPACPEHTE KGLLWELLNV KENIDMDLTS SYAMWPGAAV SGWYFSHPES KYFAVAKLAK DQVLDYAVRK GFTLEQAERW LSANLDYEPE // ID Q48IG8_PSE14 Unreviewed; 1239 AA. AC Q48IG8; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 27-MAY-2015, entry version 75. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AAZ35701.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AAZ35701.1}; GN Name=metH {ECO:0000313|EMBL:AAZ35701.1}; GN OrderedLocusNames=PSPPH_2620 {ECO:0000313|EMBL:AAZ35701.1}; OS Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6) OS (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=264730 {ECO:0000313|EMBL:AAZ35701.1, ECO:0000313|Proteomes:UP000000551}; RN [1] {ECO:0000313|EMBL:AAZ35701.1, ECO:0000313|Proteomes:UP000000551} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1448A / Race 6 {ECO:0000313|Proteomes:UP000000551}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000058; AAZ35701.1; -; Genomic_DNA. DR RefSeq; WP_011168681.1; NC_005773.3. DR RefSeq; YP_274813.1; NC_005773.3. DR ProteinModelPortal; Q48IG8; -. DR STRING; 264730.PSPPH_2620; -. DR EnsemblBacteria; AAZ35701; AAZ35701; PSPPH_2620. DR KEGG; psp:PSPPH_2620; -. DR PATRIC; 19974541; VBIPseSyr78478_2753. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PSAV264730:GKDE-2623-MONOMER; -. DR Proteomes; UP000000551; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000551}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AAZ35701.1}; KW Transferase {ECO:0000313|EMBL:AAZ35701.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1239 AA; 136060 MW; 4B62A8C9E1A09559 CRC64; MSDRSARHQA FLTALKQRIL ILDGGMGTMI QSYRLEEQDY RGKRFADWPS DVKGNNDLLI LTRPDVIGAI EKAYLDAGAD ILETNTFNAT QVSQADYGME SIVYELNVEG ARLARKVADA KTLETPDKPR FVAGVLGPTS RTCSLSPDVN NPGYRNVTFD ELVENYSEAT KGLIEGGADL ILIETIFDTL NAKAAIFAVQ GVFEEVGFEL PIMISGTITD ASGRTLSGQT TEAFWNSISH AKPISVGLNC ALGASELRPY LQELANKANT HVSAHPNAGL PNAFGEYDEL PSQTAKIIEE FAQSGFLNIV GGCCGTTPAH IKAIAEAVSG YAPRKIPDIP KACRLSGLEP FTIDRQSLFV NVGERTNITG SARFARLIRE DNYTEALEVA LQQVEAGAQV IDINMDEGML DSKKAMVTFL NLIAGEPDIY RVPIMIDSSK WEVIEAGLKC IQGKGIVNSI SMKEGVEQFI HHARLCKRYG AAVVVMAFDE QGQADTEARK KEICKRSYDI LVNEVGFPPE DIIFDPNIFA IATGIEEHNN YAVDFINACA YIRDELPYAL TSGGVSNVSF SFRGNNPVRE AIHSVFLLHA IRNGLSMGIV NAGQLEIYDQ IPAELRDCVE DVVLNRNAEG TDALLAIADK FKGDGSVKEA ETEEWRSWPV NQRLEHALVK GITIHIVQDT EESRLAFTRP IEVIEGPLMA GMNVVGDLFG AGKMFLPQVV KSARVMKQAV AHLIPFIELE KGDKPEAKGK ILMATVKGDV HDIGKNIVGV VLGCNGYDIV DLGVMVPAEK ILQVARDEKC DIIGLSGLIT PSLDEMVHVA REMQRQDFHL PLMIGGATTS KAHTAVKIEP KYSNDAVIYV TDASRAVGVA TQLLSKELKP AFIEKTRLEY VEVRERTSAR SARTERLSYG AAVAKKPQFD WENYTPAQPT FTGTRVLQDI DLNVLAEYID WTPFFISWDL AGKYPRILTD EVVGEAATAL YADATQMLRK LIDEKLISAR AVFGFWPANQ VNDDDLEVYG DDGKPQAKLH HLRQQTIKPD GKPNFSLADF VAPKDSGLTD YIGGFITTAG IGAEEVAKAY QDKGDDYNSI MVKALADRLA EACAEWLHQQ VRKEYWGYAK DEALDNEALI KEQYMGIRPA PGYPACPDHT EKGTLFALLD PLPEGTPEHT PGKSGVFLTE HYAMFPAAAV SGWYFAHPQA QYFAVGKVDK DQVESYTARK GQDLSVTERW LAPNLGYDE // ID Q48MS7_PSE14 Unreviewed; 298 AA. AC Q48MS7; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 27-MAY-2015, entry version 52. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:AAZ33299.1}; GN OrderedLocusNames=PSPPH_1024 {ECO:0000313|EMBL:AAZ33299.1}; OS Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6) OS (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=264730 {ECO:0000313|EMBL:AAZ33299.1, ECO:0000313|Proteomes:UP000000551}; RN [1] {ECO:0000313|EMBL:AAZ33299.1, ECO:0000313|Proteomes:UP000000551} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1448A / Race 6 {ECO:0000313|Proteomes:UP000000551}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; AAZ33299.1; -; Genomic_DNA. DR RefSeq; WP_011167860.1; NC_005773.3. DR RefSeq; YP_273295.1; NC_005773.3. DR ProteinModelPortal; Q48MS7; -. DR STRING; 264730.PSPPH_1024; -. DR EnsemblBacteria; AAZ33299; AAZ33299; PSPPH_1024. DR KEGG; psp:PSPPH_1024; -. DR PATRIC; 19971142; VBIPseSyr78478_1077. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; PYVDVWL; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; PSAV264730:GKDE-1026-MONOMER; -. DR Proteomes; UP000000551; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; ISM:JCVI. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0008152; P:metabolic process; ISM:JCVI. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000551}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:AAZ33299.1}; KW Transferase {ECO:0000313|EMBL:AAZ33299.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 207 207 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 298 AA; 31475 MW; B2F5A017C74A0EB5 CRC64; MTQGTTVILD GGMGRELQRR GAPFRQPEWS ALALSEAPEA VSAVHAAYIE SGAQVITSNS YAVVPFHIGE ERFAHEGQAL AALAGQLARE SADASGGRAQ VAGSIPPLFG SYRPDLYKPE LAADVLRPLV AGLSPYVDLW LAETQSCILE AQTIRAGLPN DGKPFWLSFT LQDEDTDEVP RLRSGEPVAD AAKAAAGMGV ATLLFNCSQP EVIGGAIDAA REVFKALNVD IAIGAYANAF PPQPKDAKAN DGLDELREDL DPQGYQQWAA DWVTRGATHI GGCCGIGPEH IAVLSKSL // ID Q49UL1_STAS1 Unreviewed; 613 AA. AC Q49UL1; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 27-MAY-2015, entry version 70. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=SSP2415 {ECO:0000313|EMBL:BAE19560.1}; OS Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / OS DSM 20229). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=342451 {ECO:0000313|EMBL:BAE19560.1, ECO:0000313|Proteomes:UP000006371}; RN [1] {ECO:0000313|EMBL:BAE19560.1, ECO:0000313|Proteomes:UP000006371} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15305 / DSM 20229 {ECO:0000313|Proteomes:UP000006371}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; BAE19560.1; -; Genomic_DNA. DR RefSeq; WP_011304003.1; NC_007350.1. DR RefSeq; YP_302505.1; NC_007350.1. DR ProteinModelPortal; Q49UL1; -. DR STRING; 342451.SSP2415; -. DR EnsemblBacteria; BAE19560; BAE19560; SSP2415. DR GeneID; 23779109; -. DR KEGG; ssp:SSP2415; -. DR PATRIC; 19626433; VBIStaSap90642_2400. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; SSAP342451:GKFA-2499-MONOMER; -. DR Proteomes; UP000006371; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006371}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:BAE19560.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000006371}; KW Transferase {ECO:0000313|EMBL:BAE19560.1}. SQ SEQUENCE 613 AA; 68062 MW; D31629EC1C5B5C00 CRC64; MSQLLDKLKH NILVADGAIG TILYSEGLDT CPEAYNITHP DKVARIHRSY IDAGADIIQT NTYGANFEKL KPFGLEHKVK DIHYAAVEIA KQAANDDTFI LGTVGGFRGI KQEDLELSSI QYHTEIQIET LIDAGVDGIL FETYYDLEEL TTIIKATKRK YDIPIIAQIT ALNTNYLRNG TEINTALQQV VKSGADIVGL NCHHGPHHMQ QSFSHIELPD GAYLSCYPNA SLLDIENSQF KYSDNAAYFG KVAEQLINEG VRLIGGCCGT TPEHIQYIKS SVSDLKPVNQ KNVIPIAKYT GHSEKPTQKQ NLTSKVKHRP TIIVELDTPK HLDTDLFFRN IKKLDDAKID AVTLADNSLA TVRISNVAAA SIIKQQYDIE PLVHITCRDR NLIGLQSHLL GLSLLGINEI LTITGDPSKI GHLPGATNVY DVNSKGLTEI ALRFNQGINT DGDALKTQTN FNIAGAFDPN VRKLDGAVRR LEKKLESGTH YFITQPVYSK EKIKEVYEAT KHLDVPLFIG IMPVTSYNNA LFLHNEVPGI KLSEDILEQF EAVKDDKAKT KSLSIELSKA LIDTVHEYFN GLYLITPFQK VDYTLELANY SKSITSTKQE AIL // ID Q49V93_STAS1 Unreviewed; 301 AA. AC Q49V93; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 27-MAY-2015, entry version 53. DE SubName: Full=Putative homocysteine S-methyltransferase {ECO:0000313|EMBL:BAE19317.1}; GN OrderedLocusNames=SSP2172 {ECO:0000313|EMBL:BAE19317.1}; OS Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / OS DSM 20229). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=342451 {ECO:0000313|EMBL:BAE19317.1, ECO:0000313|Proteomes:UP000006371}; RN [1] {ECO:0000313|EMBL:BAE19317.1, ECO:0000313|Proteomes:UP000006371} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15305 / DSM 20229 {ECO:0000313|Proteomes:UP000006371}; 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; AP008934; BAE19317.1; -; Genomic_DNA. DR RefSeq; WP_011303804.1; NC_007350.1. DR RefSeq; YP_302262.1; NC_007350.1. DR ProteinModelPortal; Q49V93; -. DR STRING; 342451.SSP2172; -. DR EnsemblBacteria; BAE19317; BAE19317; SSP2172. DR GeneID; 23779303; -. DR KEGG; ssp:SSP2172; -. DR PATRIC; 19625921; VBIStaSap90642_2163. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; SSAP342451:GKFA-2236-MONOMER; -. DR Proteomes; UP000006371; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006371}; KW Methyltransferase {ECO:0000313|EMBL:BAE19317.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006371}; KW Transferase {ECO:0000313|EMBL:BAE19317.1}. SQ SEQUENCE 301 AA; 33212 MW; 77FF6CF5B990B1F6 CRC64; MRLLEKLKAQ SPLVLDGGLA TTLEQAGCSL KTSLWSSEVL KNNPTQIKQA HQAFTDVGAD ILLTSTYQAS YQTFSDIGMK ATEIDQLYNT AVNQIMEATT DTQVIVGSLG PYGAYLSDGS EYTGAYDLSK EDYFQFHKTR IEALVKRGIN DFVFETVPNF EEIKAIVEYI VPHYTNQTFW LSVTVNEDGD LSDDTEFEKL CAYIKQYAER IPVFGINCSS VAGINKAISK GLKNVPQTIA LYPNGGAQYN AVEKEWESVG NQGLIVEQIP GWLDQGVKII GGCCQTTPEN IKSIKEAIET Q // ID Q4C4U7_CROWT Unreviewed; 1224 AA. AC Q4C4U7; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 27-MAY-2015, entry version 57. DE SubName: Full=Dihydropteroate synthase, DHPS:Homocysteine S-methyltransferase:Cobalamin-dependent methionine synthase, B12-binding:Vitamin B12 dependent methionine synthase, activation region:Coenzyme B12-binding {ECO:0000313|EMBL:EAM51152.1}; GN ORFNames=CwatDRAFT_4245 {ECO:0000313|EMBL:EAM51152.1}; OS Crocosphaera watsonii WH 8501. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Crocosphaera. OX NCBI_TaxID=165597 {ECO:0000313|EMBL:EAM51152.1}; RN [1] {ECO:0000313|EMBL:EAM51152.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=WH 8501 {ECO:0000313|EMBL:EAM51152.1}; RG DOE Joint Genome Institute; RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EAM51152.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=WH 8501 {ECO:0000313|EMBL:EAM51152.1}; 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] {ECO:0000313|EMBL:EAM51152.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=WH 8501 {ECO:0000313|EMBL:EAM51152.1}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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. {ECO:0000313|EMBL:EAM51152.1}. 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; AADV02000007; EAM51152.1; -; Genomic_DNA. DR RefSeq; WP_007305156.1; NZ_AADV02000007.1. DR ProteinModelPortal; Q4C4U7; -. DR EnsemblBacteria; EAM51152; EAM51152; CwatDRAFT_4245. DR PATRIC; 27701167; VBICroWat128338_2651. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EAM51152.1}; KW Transferase {ECO:0000313|EMBL:EAM51152.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 238 238 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 764 764 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1224 AA; 135602 MW; 339977BC279C1B73 CRC64; MLSIENPKPQ LKTSFLERLQ SPERPVIIFD GAMGTNIQSQ NLTAEDFGGP EYEGCNEYLV ITKPEAVARV HRNFLKAGAD VVETDSFGSS PLVLAEYDLA DRAYELSRKS AELARRCADE FTTPEKPRFV AGSIGPGTKL PTLGHITYDE LRSSFMVQAE GLFDGGADLF IVETCQDVLQ IKAALSAFEA VFAKKGSRLP LMVSVTMEIQ GTMLVGTDIS GVLAILEPFP IDILGLNCAT GPNLMTSHIQ YLSENSPFPI SCIPNAGLPE NVGGQAVYKM TPEEYTTAMT GFIAEHGVQI VGGCCGTRPA HIKALAEAVE HTQIKERSVR KNAVGELREP ISYTPAAASI YSAQTYEQDN SFLIVGERLN ASGSKKVRTL LNEDDWDGLL AIAKSQVKEG AHMLDVNVDY VGRDGERDMR ELVSRLVTNT TLPLMLDSTE WTKMEAGLKV AGGKCLLNST NYEDGEERFF KVLELAKEYG AGVVIGCIDE EGMARTAQKK FEIAKRAYED ALKFGIPPHE IFYDTLALPI STGIEEDREN AKATIESIKM IREHLPGVHF MLGVSNISFG LSPATRITLN SVFLNEAMKA GMDGSIVSAA KILPLSKIEE EHQQVCRDLI YDNRQFEGDI CTYDPLTKLT EIFAGVSAKD ARSGPSLADL PIDQRLKQHI IDGERIGLDD ALKIGLDAGY KALDIVNTFL LDGMKVVGEL FGSGQMQLPF VLQSAETMKS AVAFLEPYME KIEGEDEDRG KGKFLIATVK GDVHDIGKNL VDIILTNNGY KVVNLGIKQA IEAIVEAYEQ HQPDCIAMSG LLVKSTAFMK DNLSAFNAKG ITVPVILGGA ALTPKFVYGD CQETYNGQVI YGKDAFADLT FMDRLMPAKE QESWVDTEGF TGEFAQFNQK GRKAIEDSER EANGDASKSD GEVNGNGKKS DEPIVIDTKR SEDVAIDIER PTPPFWGTKI LQSGDLDLEE LFWYMDLQAL FAGQWQFRKP KGQSREEYDW FLASKVNPIL EEWKEKIRTE RWLEPTLVYG YFPCAAIDNS VHVYEPSVIE QGLTPKTATP FVTWTFPRQK SGRRLCISDF ILPLEYNEFD VFPMQAVTMG EISTEKAQEL YKDNKYTDYL YFHGMAVQLA EGLAEWSHAR IRRELGYGDL EPDNIRDILA QRYQGSRYSF GYPACPTVMD QVPQLQLLGC DRIGLSIDES EQLYPEQSTT AFVSYHPVAR YFSA // ID Q4CP82_TRYCC Unreviewed; 410 AA. AC Q4CP82; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 07-JAN-2015, entry version 36. DE SubName: Full=Homocysteine S-methyltransferase, putative {ECO:0000313|EMBL:EAN82085.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EAN82085.1}; GN ORFNames=Tc00.1047053508993.20 {ECO:0000313|EMBL:EAN82085.1}; OS Trypanosoma cruzi (strain CL Brener). OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Trypanosoma; OC Schizotrypanum. OX NCBI_TaxID=353153 {ECO:0000313|Proteomes:UP000002296}; RN [1] {ECO:0000313|EMBL:EAN82085.1, ECO:0000313|Proteomes:UP000002296} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CL Brener {ECO:0000313|EMBL:EAN82085.1, RC ECO:0000313|Proteomes:UP000002296}; RX PubMed=16020725; DOI=10.1126/science.1112631; RA El-Sayed N.M., Myler P.J., Bartholomeu D.C., Nilsson D., Aggarwal G., RA Tran A.N., Ghedin E., Worthey E.A., Delcher A.L., Blandin G., RA Westenberger S.J., Caler E., Cerqueira G.C., Branche C., Haas B., RA Anupama A., Arner E., Aslund L., Attipoe P., Bontempi E., Bringaud F., RA Burton P., Cadag E., Campbell D.A., Carrington M., Crabtree J., RA Darban H., da Silveira J.F., de Jong P., Edwards K., Englund P.T., RA Fazelina G., Feldblyum T., Ferella M., Frasch A.C., Gull K., Horn D., RA Hou L., Huang Y., Kindlund E., Klingbeil M., Kluge S., Koo H., RA Lacerda D., Levin M.J., Lorenzi H., Louie T., Machado C.R., RA McCulloch R., McKenna A., Mizuno Y., Mottram J.C., Nelson S., RA Ochaya S., Osoegawa K., Pai G., Parsons M., Pentony M., Pettersson U., RA Pop M., Ramirez J.L., Rinta J., Robertson L., Salzberg S.L., RA Sanchez D.O., Seyler A., Sharma R., Shetty J., Simpson A.J., Sisk E., RA Tammi M.T., Tarleton R., Teixeira S., Van Aken S., Vogt C., Ward P.N., RA Wickstead B., Wortman J., White O., Fraser C.M., Stuart K.D., RA Andersson B.; RT "The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas RT disease."; RL Science 309:409-415(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. {ECO:0000313|EMBL:EAN82085.1}. 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; AAHK01002702; EAN82085.1; -; Genomic_DNA. DR RefSeq; XP_803936.1; XM_798843.1. DR ProteinModelPortal; Q4CP82; -. DR GeneID; 3533238; -. DR KEGG; tcr:508993.20; -. DR KO; K00547; -. DR Proteomes; UP000002296; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002296}; KW Methyltransferase {ECO:0000313|EMBL:EAN82085.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002296}; KW Transferase {ECO:0000313|EMBL:EAN82085.1}. SQ SEQUENCE 410 AA; 45165 MW; 716BCB83DF1B02AF CRC64; MSTRRVNGVL IKDGAMGTLL ESWDVDYAKA GSMWSSSVLL SEMDLVKRAH RAYIDAGCDV LLTCTYQMHE EGCAASKVTM CELVDRAVQA ARHTMPKQKQ KGLTEESTAK ERRTGGIDVF RYALSSIKDN GQERVVLLAG SLGPYGSFLP GGQEYLGEYS IHEAVINSFH ARRLEAFLCN VGEKHAFKVD FFLLETFPRL DEALGILSFV NQHEILRTAP FCFSFIAAPV KNPLPENADD DALDNWWNAA ASSIRLPDGN TFEGALSELR GNCGTALVGM GCNCSGPLEV SLVATALLHK KRQGTEGPLV LLLYPNSGEK FTDGQWKKPP QQIQTSAAKK LSMRDLKRIL ARGGGNLITF MKFLLQLLQQ RPEATDWLFE IIVCGACCRS TPEDIAALNQ LAREEPYLHA // ID Q4DI99_TRYCC Unreviewed; 410 AA. AC Q4DI99; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 07-JAN-2015, entry version 35. DE SubName: Full=Homocysteine S-methyltransferase, putative {ECO:0000313|EMBL:EAN92259.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EAN92259.1}; GN ORFNames=Tc00.1047053506479.120 {ECO:0000313|EMBL:EAN92259.1}; OS Trypanosoma cruzi (strain CL Brener). OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Trypanosoma; OC Schizotrypanum. OX NCBI_TaxID=353153 {ECO:0000313|Proteomes:UP000002296}; RN [1] {ECO:0000313|EMBL:EAN92259.1, ECO:0000313|Proteomes:UP000002296} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CL Brener {ECO:0000313|EMBL:EAN92259.1, RC ECO:0000313|Proteomes:UP000002296}; RX PubMed=16020725; DOI=10.1126/science.1112631; RA El-Sayed N.M., Myler P.J., Bartholomeu D.C., Nilsson D., Aggarwal G., RA Tran A.N., Ghedin E., Worthey E.A., Delcher A.L., Blandin G., RA Westenberger S.J., Caler E., Cerqueira G.C., Branche C., Haas B., RA Anupama A., Arner E., Aslund L., Attipoe P., Bontempi E., Bringaud F., RA Burton P., Cadag E., Campbell D.A., Carrington M., Crabtree J., RA Darban H., da Silveira J.F., de Jong P., Edwards K., Englund P.T., RA Fazelina G., Feldblyum T., Ferella M., Frasch A.C., Gull K., Horn D., RA Hou L., Huang Y., Kindlund E., Klingbeil M., Kluge S., Koo H., RA Lacerda D., Levin M.J., Lorenzi H., Louie T., Machado C.R., RA McCulloch R., McKenna A., Mizuno Y., Mottram J.C., Nelson S., RA Ochaya S., Osoegawa K., Pai G., Parsons M., Pentony M., Pettersson U., RA Pop M., Ramirez J.L., Rinta J., Robertson L., Salzberg S.L., RA Sanchez D.O., Seyler A., Sharma R., Shetty J., Simpson A.J., Sisk E., RA Tammi M.T., Tarleton R., Teixeira S., Van Aken S., Vogt C., Ward P.N., RA Wickstead B., Wortman J., White O., Fraser C.M., Stuart K.D., RA Andersson B.; RT "The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas RT disease."; RL Science 309:409-415(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. {ECO:0000313|EMBL:EAN92259.1}. 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; AAHK01000449; EAN92259.1; -; Genomic_DNA. DR RefSeq; XP_814110.1; XM_809017.1. DR ProteinModelPortal; Q4DI99; -. DR GeneID; 3545600; -. DR KEGG; tcr:506479.120; -. DR KO; K00547; -. DR Proteomes; UP000002296; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002296}; KW Methyltransferase {ECO:0000313|EMBL:EAN92259.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002296}; KW Transferase {ECO:0000313|EMBL:EAN92259.1}. SQ SEQUENCE 410 AA; 45207 MW; FA781F3DCB84FFCF CRC64; MSTRQFTGVL IKDGAMGTLL ESWDVDYAKA GSMWSSSVLL SEMDLVKRAH RAYIDAGCDV LLTCTYQMHE EGCAASKVTM CELVDRAVQA ARHTMPQRKQ KGLTEESTAK ERRTGGIDVF RYALSSIKDN GQERVVLLAG SLGPYGSSLP GGQEYLGEYS IHEAVINAFH ARRLEAFLCN VGEKHAFKVD FLLLETFPRL DEALGILSFV NQHEILRTAP FCFSFIAVPV KNPLPENADD DALDNWWNAA ASSIRLPDGN TFEGALSELR GNCGTALVGM GCNCSGPLEV SLVATALLHK KRQDTEGPLV LLLYPNSGEK FTDGQWKKPL QQIQTSAAER LSMRDLKRIL ARGGGNLITF MKFLLQLLQQ RPEATDWLFE IIVCGACCRS TPEDIAALNQ VAREEPYLHA // ID Q4FLG1_PELUB Unreviewed; 353 AA. AC Q4FLG1; DT 30-AUG-2005, integrated into UniProtKB/TrEMBL. DT 30-AUG-2005, sequence version 1. DT 01-APR-2015, entry version 58. DE SubName: Full=Betaine-homocysteine methyltransferase {ECO:0000313|EMBL:AAZ21977.1}; DE EC=2.1.1.5 {ECO:0000313|EMBL:AAZ21977.1}; GN Name=bhmT {ECO:0000313|EMBL:AAZ21977.1}; GN OrderedLocusNames=SAR11_1173 {ECO:0000313|EMBL:AAZ21977.1}; OS Pelagibacter ubique (strain HTCC1062). OC Bacteria; Proteobacteria; Alphaproteobacteria; SAR11 cluster; OC Candidatus Pelagibacter. OX NCBI_TaxID=335992 {ECO:0000313|EMBL:AAZ21977.1, ECO:0000313|Proteomes:UP000002528}; RN [1] {ECO:0000313|EMBL:AAZ21977.1, ECO:0000313|Proteomes:UP000002528} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HTCC1062 {ECO:0000313|EMBL:AAZ21977.1, RC ECO:0000313|Proteomes:UP000002528}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; AAZ21977.1; -; Genomic_DNA. DR RefSeq; WP_011282189.1; NC_007205.1. DR RefSeq; YP_266581.1; NC_007205.1. DR ProteinModelPortal; Q4FLG1; -. DR STRING; 335992.SAR11_1173; -. DR EnsemblBacteria; AAZ21977; AAZ21977; SAR11_1173. DR KEGG; pub:SAR11_1173; -. DR PATRIC; 31991845; VBICanPel5618_1163. DR HOGENOM; HOG000231636; -. DR KO; K00544; -. DR OMA; KAHYMSQ; -. DR OrthoDB; EOG6NSGDJ; -. DR BioCyc; CPEL335992:GH3Z-1186-MONOMER; -. DR Proteomes; UP000002528; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002528}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:AAZ21977.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002528}; KW Transferase {ECO:0000313|EMBL:AAZ21977.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 213 213 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 302 302 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 353 AA; 39617 MW; 2051F0D3EFAB8B89 CRC64; MSTNKLKERL DKGPVICAEG FLFEIERRGY MSSGEFVPMV SLDHPEVLEN LHREFQHAGS DVVEAFTYNG HREKMRVIGK EELLEPLNRS ALKIAKKVAL DTPKGSKPNL MAGNISNSNI WKHNDPQSQK EVEGMFTEMI GWAVEEGADM LIGETFYYAE EAFKALEIMK KTGLPTVLTI SPMGENKMRD GKSVVDTCKE LEQLGADVVG LNCFRGPATM FPFLKEIRKA VKCHVGALPI PYRTSEDYPT FFNLPDRSNC ACPSPHGRTF PTALDPHFCN RYEIGKFAKD AYALGINYLG VCCGANPMLI REVAESIGLT VPASKYRENM ENHFMYGKNK RIPKHMTEYG DKA // ID Q4FMM0_PELUB Unreviewed; 302 AA. AC Q4FMM0; DT 30-AUG-2005, integrated into UniProtKB/TrEMBL. DT 30-AUG-2005, sequence version 1. DT 27-MAY-2015, entry version 51. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AAZ21569.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:AAZ21569.1}; GN Name=mmuM {ECO:0000313|EMBL:AAZ21569.1}; GN OrderedLocusNames=SAR11_0750 {ECO:0000313|EMBL:AAZ21569.1}; OS Pelagibacter ubique (strain HTCC1062). OC Bacteria; Proteobacteria; Alphaproteobacteria; SAR11 cluster; OC Candidatus Pelagibacter. OX NCBI_TaxID=335992 {ECO:0000313|EMBL:AAZ21569.1, ECO:0000313|Proteomes:UP000002528}; RN [1] {ECO:0000313|EMBL:AAZ21569.1, ECO:0000313|Proteomes:UP000002528} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HTCC1062 {ECO:0000313|EMBL:AAZ21569.1, RC ECO:0000313|Proteomes:UP000002528}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; AAZ21569.1; -; Genomic_DNA. DR RefSeq; WP_011281915.1; NC_007205.1. DR RefSeq; YP_266172.1; NC_007205.1. DR ProteinModelPortal; Q4FMM0; -. DR STRING; 335992.SAR11_0750; -. DR EnsemblBacteria; AAZ21569; AAZ21569; SAR11_0750. DR KEGG; pub:SAR11_0750; -. DR PATRIC; 31990983; VBICanPel5618_0748. DR KO; K00547; -. DR OMA; HISEGIN; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; CPEL335992:GH3Z-761-MONOMER; -. DR Proteomes; UP000002528; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002528}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:AAZ21569.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002528}; KW Transferase {ECO:0000313|EMBL:AAZ21569.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 287 287 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 302 AA; 34177 MW; 31AE1E43138C4A8B CRC64; MDINFFKTTR ILDGGMGQEL LARGMKPNGT LWSANAVLKE EYHQLLLDTH LDFIKAGAEV IVTATFTTRR IRLRDNKIED KFEYLNKKAG EIAQKAKEQH PNVLIAGGLP PQYLTYEEDT RPDDEIKQNF YDQAKLLDPY IDFFYLDVLS SVKEFKLAIE AIEEFNKPYL IGAHISEGIN LPSGEKISDI INNIKHNNLL GLILSCVSPE NFYENLEEVK NLGVPFGFKL NAFVTTNPKD GYTNSYNVSK TGNPNEFLGQ RKDLTPELMA NFVKKFKNAG ATILGGCCET RPSHIKEMVQ FK // ID Q4FUN8_PSYA2 Unreviewed; 1271 AA. AC Q4FUN8; DT 30-AUG-2005, integrated into UniProtKB/TrEMBL. DT 30-AUG-2005, sequence version 1. DT 27-MAY-2015, entry version 72. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:AAZ18270.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AAZ18270.1}; GN Name=metH {ECO:0000313|EMBL:AAZ18270.1}; GN OrderedLocusNames=Psyc_0403 {ECO:0000313|EMBL:AAZ18270.1}; OS Psychrobacter arcticus (strain DSM 17307 / 273-4). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Psychrobacter. OX NCBI_TaxID=259536 {ECO:0000313|EMBL:AAZ18270.1, ECO:0000313|Proteomes:UP000000546}; RN [1] {ECO:0000313|EMBL:AAZ18270.1, ECO:0000313|Proteomes:UP000000546} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17307 / 273-4 {ECO:0000313|Proteomes:UP000000546}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000082; AAZ18270.1; -; Genomic_DNA. DR RefSeq; WP_011279708.1; NC_007204.1. DR RefSeq; YP_263704.1; NC_007204.1. DR ProteinModelPortal; Q4FUN8; -. DR SMR; Q4FUN8; 699-937. DR STRING; 259536.Psyc_0403; -. DR EnsemblBacteria; AAZ18270; AAZ18270; Psyc_0403. DR KEGG; par:Psyc_0403; -. DR PATRIC; 23055131; VBIPsyArc98534_0498. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PARC259536:GI3A-418-MONOMER; -. DR Proteomes; UP000000546; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000546}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AAZ18270.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000546}; KW Transferase {ECO:0000313|EMBL:AAZ18270.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 352 352 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 353 353 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 804 804 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1271 AA; 140363 MW; E6556AA171BF8145 CRC64; MTPTARSQTD ISPTKIIDDS NPNANPNDFI LTPPTVFPYK DQQLTARTRI TEQMAARILM LDGAMGTHIQ NYKLEEADYR GERFANISQD VRGNNDLLVL TQPHMIKEIH LAHLESGADI IETNSFNGTR LSMADYDMQY LVPELNKTAA KIAREAADEY TAKNPDKPRF VAGVIGPTSR TCSLSPDVND PAFRNITFDE LVLNYREATL ALMEGGVDII LIETIFDTLN AKAAIFAVTG VFDDIGFELP IMISGTITDA SGRTLSGQTA EAFYNSIRHA KPLSVGFNCA LGADALRPHI QTLSNIANTY VSAHPNAGLP NEFGEYDETA DETAALLEGF AKAGILNIVG GCCGTTPEHI RQIANMVAKY PPRVIPEIAP ACRLSGLEPF TINSDSLFVN VGERTNVTGS KKFLRLIKTE AYTEALDVAR DQVEGGAQIV DINMDEGMLD SKQAMIHFVN LVSGEPDISR VPLMLDSSKW DIIEEGLKRT QGKCIVNSIS LKEGHAEFVE RAKLCMRYGA AIIVMAFDED GQADTFERKT QICKRSYDVL VDEVGFPSED IIFDPNIFAV ATGITEHNNY GADFINATKW ITDNLPNAMV SGGVSNVSFS FRGNPIREAI NSVFLYHAIQ NGLTMGIVNP AMLELYDDIP KEARDAIEDV MLNRNQGETG QDATERLMTI AENYQDGGKK KESTVDMTWR EGTVEERIAH ALVKGITTFI EADTKEAWEK YPRPLEVIEG PLMDGMNIVG DLFGAGKMFL PQVVKSARVM KQSVAWLNPY IEAEKVEGEK KGKILMATVK GDVHDIGKNI VGVVLGCNGY DIVDLGVMVP CEKILDTAIA EEVDIIGLSG LITPSLDEMV YVAKQMQERG MTLPLMIGGA TTSKAHTAVK IEPQYQNDAV IYVSDASRSV GVVTKLLSKE HRQGLIDETR EEYIKVRERL AKRQPKAAKI SYAESIEIGF QYDWDNYVPP TPNKLGQVIF DDYPITNLLP YIDWTPFFIS WGLAGKYPKI LQDDVVGEAA RDLFGNAEDM LQKMIDEKLI VAKGVFKLMP ACRTGADTVT VYDKAPTEGG TAEYQFEHLR QQSDKASGKP NFSLADFISP SDMHTDYLGG FTVSIVGTEA LAEKYKAAGD DYNAIMVQAL SDRLAEAFAE HLHELIRKEY WGYQPTESLT NEDMIKEKYV GIRPAPGYPA CPEHTEKGKL FEWLGTGDAI GTILTESYAM WPASSVSGFY YSHPDSVYFN VGKISTDQLE SYAERKGWDM KTAEKWLNPN L // ID Q4GZ92_TRYB2 Unreviewed; 433 AA. AC Q4GZ92; DT 30-AUG-2005, integrated into UniProtKB/TrEMBL. DT 30-AUG-2005, sequence version 1. DT 29-APR-2015, entry version 42. DE SubName: Full=Trypanosoma brucei brucei strain 927/4 GUTat10.1 chromosome 1, complete sequence {ECO:0000313|EMBL:CAJ16076.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:CAJ16076.1}; GN ORFNames=TB927.1.1270 {ECO:0000313|EMBL:CAJ16076.1}; OS Trypanosoma brucei brucei (strain 927/4 GUTat10.1). OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Trypanosoma. OX NCBI_TaxID=185431 {ECO:0000313|EMBL:CAJ16076.1, ECO:0000313|Proteomes:UP000008524}; RN [1] {ECO:0000313|EMBL:CAJ16076.1, ECO:0000313|Proteomes:UP000008524} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=927/4 GUTat10.1 {ECO:0000313|EMBL:CAJ16076.1, RC ECO:0000313|Proteomes:UP000008524}; RX PubMed=12907729; DOI=10.1093/nar/gkg674; RA Hall N., Berriman M., Lennard N.J., Harris B.R., Hertz-Fowler C., RA Bart-Delabesse E.N., Gerrare C.S., Atkin R.J., Barron A.J., Bowman S., RA Bray-Allen S.P., Bringaud F., Clark L.N., Corton C.H., Cronin A., RA Davies R., Doggett J., Fraser A., Gruter E., Hall S., Harper A.D., RA Kay M.P., Leech V., Mayes R., Price C., Quail M.A., Rabbinowitch E., RA Reitter C., Rutherford K., Sasse J., Sharp S., Shownkeen R., RA Macleod A., Taylor S., Tweedie A., Turner C.M.R., Tait A., Gull K., RA Barrell B., Melville S.E.; RT "The DNA sequence of chromosome I of an African trypanosome: gene RT content, chromosome organisation, recombination and polymorphism."; RL Nucleic Acids Res. 31:4864-4873(2003). RN [2] {ECO:0000313|Proteomes:UP000008524} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=927/4 GUTat10.1 {ECO:0000313|Proteomes:UP000008524}; RX PubMed=16020726; DOI=10.1126/science.1112642; RA Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H., RA Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B., RA Bohme U., Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L., RA Wickstead B., Alsmark U.C.M., Arrowsmith C., Atkin R.J., Barron A.J., RA Bringaud F., Brooks K., Carrington M., Cherevach I., RA Chillingworth T.J., Churcher C., Clark L.N., Corton C.H., Cronin A., RA Davies R.M., Doggett J., Djikeng A., Feldblyum T., Field M.C., RA Fraser A., Goodhead I., Hance Z., Harper D., Harris B.R., Hauser H., RA Hostetler J., Ivens A., Jagels K., Johnson D., Johnson J., Jones K., RA Kerhornou A.X., Koo H., Larke N., Landfear S., Larkin C., Leech V., RA Line A., Lord A., Macleod A., Mooney P.J., Moule S., Martin D.M., RA Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G., RA Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E., RA Rajandream M.A., Reitter C., Salzberg S.L., Sanders M., Schobel S., RA Sharp S., Simmonds M., Simpson A.J., Tallon L., Turner C.M., Tait A., RA Tivey A.R., Van Aken S., Walker D., Wanless D., Wang S., White B., RA White O., Whitehead S., Woodward J., Wortman J., Adams M.D., RA Embley T.M., Gull K., Ullu E., Barry J.D., Fairlamb A.H., RA Opperdoes F., Barrell B.G., Donelson J.E., Hall N., Fraser C.M., RA Melville S.E., El-Sayed N.M.A.; RT "The genome of the African trypanosome Trypanosoma brucei."; RL Science 309:416-422(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; AL929603; CAJ16076.1; -; Genomic_DNA. DR RefSeq; XP_001218829.1; XM_001218828.1. DR ProteinModelPortal; Q4GZ92; -. DR STRING; 5691.Tb927.1.1270; -. DR GeneID; 4357202; -. DR KEGG; tbr:Tb927.1.1270; -. DR eggNOG; COG2040; -. DR InParanoid; Q4GZ92; -. DR KO; K00547; -. DR Proteomes; UP000008524; Chromosome 1. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; ISA:GeneDB. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008524}; KW Methyltransferase {ECO:0000313|EMBL:CAJ16076.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008524}; KW Transferase {ECO:0000313|EMBL:CAJ16076.1}. SQ SEQUENCE 433 AA; 48278 MW; A9E70A1898319CF1 CRC64; MKDISCPTGE TGSIFEKSKK FQHFFTMDGA VGTLVERCGL DPSKMGSMWS TSALITDEEI VRYVHKSYLD VGADVILTNT YQMHAAGCAQ AGVTMNEVVN TAVRVLCDGI TPERAAATKE AKVWAQHVMN NKRSEFVNVF APLFYGPRDD ASKCPVLVGG SLGSYGASLG NAQEYRGEYE VNEDIIRDYY VGRFMAFVNH VDEKEAHLKV DFIMIETIPL LNEAIEIFTW LKYQKEDETL RSAPVCLSFI SCLREPRPDV TVDDATLNEW WLAAESNIRL IDGNTFEKAF NSLMELQLPQ LVGFGTNCCS PLEASVVASA FLKKKKHKVT DPSLALFLYS NSGENFKEGE WHWGGQLPRG SHSPTSSPKE TLPFTTLQRL MLCCEADVRT AAFFAYQLLL QRPEADDWLF DIIICGGCCR STPEDIAMIR SLV // ID Q4K3H3_PSEF5 Unreviewed; 299 AA. AC Q4K3H3; DT 02-AUG-2005, integrated into UniProtKB/TrEMBL. DT 02-AUG-2005, sequence version 1. DT 27-MAY-2015, entry version 49. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:AAY95340.1}; GN OrderedLocusNames=PFL_6152 {ECO:0000313|EMBL:AAY95340.1}; OS Pseudomonas fluorescens (strain Pf-5 / ATCC BAA-477). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=220664 {ECO:0000313|EMBL:AAY95340.1, ECO:0000313|Proteomes:UP000008540}; RN [1] {ECO:0000313|EMBL:AAY95340.1, ECO:0000313|Proteomes:UP000008540} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pf-5 / ATCC BAA-477 {ECO:0000313|Proteomes:UP000008540}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; AAY95340.1; -; Genomic_DNA. DR RefSeq; WP_011064317.1; NC_004129.6. DR RefSeq; YP_263210.1; NC_004129.6. DR ProteinModelPortal; Q4K3H3; -. DR STRING; 220664.PFL_6152; -. DR EnsemblBacteria; AAY95340; AAY95340; PFL_6152. DR GeneID; 3480522; -. DR KEGG; pfl:PFL_6152; -. DR PATRIC; 19881841; VBIPseFlu72549_6281. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; PYVDVWL; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; PFLU220664:GIX8-6195-MONOMER; -. DR Proteomes; UP000008540; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008540}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:AAY95340.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008540}; KW Transferase {ECO:0000313|EMBL:AAY95340.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 207 207 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 299 AA; 31736 MW; 6FFE183E93D4BD59 CRC64; MGAGSTVILD GGMGRELQRR GAPFRQPEWS ALALSEDPRA VEAVHAAYID SGADVITSNS YAVVPFHIGE ERFAAEGQAL AALAGELARR AVEASGKPVR VAGSLPPLFG SYRPDLFDAA RVEEILSPLV KGLAPHVDLW LAETQSSIVE ARAIHAGLPK DGKPFWLSFT LKDEEVDEVP RLRSGETVAE AAAVAAQLGV QTLLFNCSQP EVIGAAVDAA RETFERLGVQ IHIGVYANAF PPQPEDATAN DGLCPLREDL DPPGYLQWVA DWHQRGASHV GGCCGIGPEH IAVLAQKLG // ID Q4KAG9_PSEF5 Unreviewed; 1236 AA. AC Q4KAG9; DT 02-AUG-2005, integrated into UniProtKB/TrEMBL. DT 02-AUG-2005, sequence version 1. DT 27-MAY-2015, entry version 72. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AAY92928.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AAY92928.1}; GN Name=metH {ECO:0000313|EMBL:AAY92928.1}; GN OrderedLocusNames=PFL_3662 {ECO:0000313|EMBL:AAY92928.1}; OS Pseudomonas fluorescens (strain Pf-5 / ATCC BAA-477). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=220664 {ECO:0000313|EMBL:AAY92928.1, ECO:0000313|Proteomes:UP000008540}; RN [1] {ECO:0000313|EMBL:AAY92928.1, ECO:0000313|Proteomes:UP000008540} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pf-5 / ATCC BAA-477 {ECO:0000313|Proteomes:UP000008540}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000076; AAY92928.1; -; Genomic_DNA. DR RefSeq; WP_011061938.1; NC_004129.6. DR RefSeq; YP_260764.1; NC_004129.6. DR ProteinModelPortal; Q4KAG9; -. DR STRING; 220664.PFL_3662; -. DR EnsemblBacteria; AAY92928; AAY92928; PFL_3662. DR GeneID; 3475578; -. DR KEGG; pfl:PFL_3662; -. DR PATRIC; 19876697; VBIPseFlu72549_3750. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PFLU220664:GIX8-3677-MONOMER; -. DR Proteomes; UP000008540; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; ISM:JCVI. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; ISM:JCVI. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008540}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AAY92928.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008540}; KW Transferase {ECO:0000313|EMBL:AAY92928.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1236 AA; 135692 MW; 0D2C6F209B548282 CRC64; MSDRSARLHA LQQALKERIL ILDGGMGTMI QSYKLEEHDY RGKRFADWPS DVKGNNDLLV LTRPDVIGAI EKAYLDAGAD ILETNTFNAT QVSQADYGME ELVYELNVEG ARLARKVADA KTLETPDKPR FVAGVLGPTS RTCSLSPDVN NPGYRNVTFD ELVENYTEAT KGLIEGGADL ILIETIFDTL NAKAAIFAVQ GVFEELGFEL PIMISGTITD ASGRTLSGQT TEAFWNSVAH AKPISVGLNC ALGASELRPY LEELSNKAST HVSAHPNAGL PNEFGEYDEL PEQTAKVIEE FAQSGFLNIV GGCCGTTPGH IGAIAKAVAG YAPRQIPDIP KACRLSGLEP FTIDRNSLFV NVGERTNITG SAKFARLIRE DNYTEALEVA LQQVEAGAQV IDINMDEGML DSKKAMVTFL NLIAGEPDIS RVPIMIDSSK WEVIEAGLKC IQGKGIVNSI SMKEGVEQFI HHARLCKRYG AAVVVMAFDE VGQADTEARK KEICKRSYDI LVNEVGFPPE DIIFDPNIFA VATGIEEHNN YAVDFINACA YIRDELPYAL SSGGVSNVSF SFRGNNPVRE AIHSVFLLYA IRNGLTMGIV NAGQLEIYDQ IPQQLRDAVE DVVLNRTPNG TDALLAIADQ FKGDGSVKEA ETEEWRGWEV NKRLEHALVK GITTHIVEDT EESRQSFSRP IEVIEGPLMS GMNVVGDLFG AGKMFLPQVV KSARVMKQAV AHLIPFIELE KGDKPEAKGK ILMATVKGDV HDIGKNIVGV VLGCNGYDIV DLGVMVPAEK ILQVAKEQKC DIIGLSGLIT PSLDEMVHVA REMQRQDFHL PLMIGGATTS KAHTAVKIEP KYSNDAVVYV TDASRAVGVA TQLLSKELKA GFVQKTREEY VEVRERTANR SARTERLSYP AAIAKKPQFD WSSYQPVKPT FTGARVLDNI DLKVLAEYID WTPFFISWDL AGKFPRILED EVVGEAATAL YKDAREMLDK LINEKLISAR AVFGFWPANQ VQDDDLEVYG DDGRPLARLH HLRQQIIKTD GKPNFSLADF VAPKDSGVTD YVGGFITTAG IGAEEVAKAY QDAGDDYNSI MVKALADRLA EACAEWLHQQ VRKEYWGYAK DEQLDNEALI KEQYSGIRPA PGYPACPDHT EKSTLFALLD PEASEGRAGR SGVFLTEHFA MFPAAAVSGW YFAHPQAQYF AVGKVDQDQV QSYTERKGQD LAVSERWLAP NLGYDN // ID Q4L331_STAHJ Unreviewed; 612 AA. AC Q4L331; DT 02-AUG-2005, integrated into UniProtKB/TrEMBL. DT 02-AUG-2005, sequence version 1. DT 27-MAY-2015, entry version 78. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=SH2637 {ECO:0000313|EMBL:BAE05946.1}; OS Staphylococcus haemolyticus (strain JCSC1435). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=279808 {ECO:0000313|EMBL:BAE05946.1, ECO:0000313|Proteomes:UP000000543}; RN [1] {ECO:0000313|EMBL:BAE05946.1, ECO:0000313|Proteomes:UP000000543} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCSC1435 {ECO:0000313|EMBL:BAE05946.1, RC ECO:0000313|Proteomes:UP000000543}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; BAE05946.1; -; Genomic_DNA. DR RefSeq; WP_011276876.1; NC_007168.1. DR RefSeq; YP_254552.1; NC_007168.1. DR ProteinModelPortal; Q4L331; -. DR STRING; 279808.SH2637; -. DR EnsemblBacteria; BAE05946; BAE05946; SH2637. DR KEGG; sha:SH2637; -. DR PATRIC; 19621367; VBIStaHae67511_2586. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; SHAE279808:GJX7-2712-MONOMER; -. DR Proteomes; UP000000543; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000543}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 612 AA; 67988 MW; 435CE376598E6A96 CRC64; MSRLLNQLQN NVLVADGAMG TILYSEGLDT CPEAYNLTHP EKVESIHRSY IEAGADIIQT NTYGANFEKL RRFGLEHKVK DIHKAAVAIA KRAARPDTFI LGTVGGFRSL QQEELPLSTI QYHAENQIDT LVEEGVDGLL FETYYDLEEL TNIVTTTRRK YDIPIIAQLT ASNTNYLVDG TEINKALQQL VACGANVVGL NCHHGPHHMQ RSFSHIELPE TAYLSCYPNA SLLDIENSEF KYSDNAQYFG DVAQELINEG VRLIGGCCGT TPQHIAYIKS SVKDLKPVKN KNVIPINRQT NRAVTHTYKH NLTTKVKNGP TVIVELDTPK HLDTDLFFEN IGKLDEANID AVTLADNSLA TVRVSNIAAA SIIRQRYNIE PLVHITCRDR NLIGLQSHLL GLSLIGVNEI LAITGDPSKV GHLPGATNVY DVNSKGLTEL ALRFNQGINT DGDALKKHTN FNIAGAFDPN VRKLDGAVKR LEKKVAAGMN YFITQPVYSK EKIKEVYEAT KHLNVPLFIG IMPIASYNNA LFLHNEVPGI KMSEDVLSQF KAVKDDKEKT KALSLRLSKE LIDTVHEYFN GLYIITPFQR IDYSLELAAY SKAITQNKEA IS // ID Q4MNT8_BACCE Unreviewed; 1132 AA. AC Q4MNT8; DT 02-AUG-2005, integrated into UniProtKB/TrEMBL. DT 02-AUG-2005, sequence version 1. DT 27-MAY-2015, entry version 62. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AJI03206.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AJI03206.1}; GN Name=metH {ECO:0000313|EMBL:AJI03206.1}; GN ORFNames=AQ16_3772 {ECO:0000313|EMBL:AJI03206.1}; OS Bacillus cereus G9241. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=269801 {ECO:0000313|EMBL:AJI03206.1, ECO:0000313|Proteomes:UP000031837}; RN [1] {ECO:0000313|EMBL:AJI03206.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=G9241 {ECO:0000313|EMBL:AJI03206.1}; RA Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O., Coyne S.R., RA Daligault H.E., Davenport K.W., Erkkila T., Frey K.G., Gibbons H.S., RA Gu W., Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C., RA Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N., RA Scholz M.B., Teshima H., Xu Y.; RL Submitted (OCT-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; CP009590; AJI03206.1; -; Genomic_DNA. DR RefSeq; WP_002194518.1; NZ_AAEK01000021.1. DR ProteinModelPortal; Q4MNT8; -. DR EnsemblBacteria; EAL13835; EAL13835; BCE_G9241_4286. DR Proteomes; UP000031837; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000031837}; KW Methyltransferase {ECO:0000313|EMBL:AJI03206.1}; KW Transferase {ECO:0000313|EMBL:AJI03206.1}. SQ SEQUENCE 1132 AA; 125920 MW; 0CFA4A921F5489D2 CRC64; MKCIEEKLRN NILLLDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYELSYLDE ELNEKAARLA KQAVEESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGE VDVLLVETSQ DMRNVKAAYI GIQAAFDELN KIVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWVN IIGGCCGTTP EHIKAMKSAL ASLKPREQQE RAGHGVSGLE ALQYDDSMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMENF LAEVTKVLKV PIMIDSTDEN VMERALTYIQ GKAVINSINL EDGEERFIKV TPLLQKYGAA IVVGTIDEDG MAVSAERKLE IAKRSYELLT TKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KETLPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPEE EKRLADALLF ETTQETLEEF TNFYRAAKKK DVVIQETLTL DERLANYIVE GTKQGLQEDL SIALTEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILA NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAADIDIPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV TKEEKKVEIP AVIEPLPKSE VMVPDSTKRI VLRDIPALHL APFLNRQMLL GHHLGLKGSV KKLLREGDKR AHELNDLIDE LLQEGQSWLK PKAVYQFFPA QSDGQNIVIY DPQDHTRVIE RFTFPRQGKA PYRTLGDYLR PIGDEMDYVA FLSVTVGEGV RDIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID Q4MNT9_BACCE Unreviewed; 610 AA. AC Q4MNT9; DT 02-AUG-2005, integrated into UniProtKB/TrEMBL. DT 02-AUG-2005, sequence version 1. DT 27-MAY-2015, entry version 51. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:AJI06492.1}; GN ORFNames=AQ16_3771 {ECO:0000313|EMBL:AJI06492.1}; OS Bacillus cereus G9241. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=269801 {ECO:0000313|EMBL:AJI06492.1, ECO:0000313|Proteomes:UP000031837}; RN [1] {ECO:0000313|EMBL:AJI06492.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=G9241 {ECO:0000313|EMBL:AJI06492.1}; RA Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O., Coyne S.R., RA Daligault H.E., Davenport K.W., Erkkila T., Frey K.G., Gibbons H.S., RA Gu W., Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C., RA Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N., RA Scholz M.B., Teshima H., Xu Y.; RL Submitted (OCT-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; CP009590; AJI06492.1; -; Genomic_DNA. DR RefSeq; WP_000770330.1; NZ_AAEK01000021.1. DR ProteinModelPortal; Q4MNT9; -. DR EnsemblBacteria; EAL13836; EAL13836; BCE_G9241_4287. DR Proteomes; UP000031837; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000031837}; KW Methyltransferase {ECO:0000313|EMBL:AJI06492.1}; KW Transferase {ECO:0000313|EMBL:AJI06492.1}. SQ SEQUENCE 610 AA; 67210 MW; 2A5E2353CD2C989C CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNISDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTE INRAAVKLAK ASVTDRNAIL GTIGGMKHIG AVTTTDMERE FMLLEQASAL LEEQVDGLLL ETFYDEFELL HAVQVLRKET NIPIVAQLAL HEAGTTQNGN DVNEILKQLL DYGANVVGLN CQLGPLHMTE AFKMISIPKN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPKFIEQGI RLLGGCCGTT PEHIESMKRA TLNVTPVIEK DTIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRISNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIA LIEEVYEATK HLEQPIFIGI MPLISKRNAD FLHFEVPGIT LPEAVRERMD GHETKEAAIE EGIRISQELI DAAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID Q4Q0C9_LEIMA Unreviewed; 339 AA. AC Q4Q0C9; DT 19-JUL-2005, integrated into UniProtKB/TrEMBL. DT 19-JUL-2005, sequence version 1. DT 27-MAY-2015, entry version 55. DE SubName: Full=Complete genome, chromosome 36 {ECO:0000313|EMBL:CAJ09606.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:CAJ09606.1}; GN ORFNames=LMJF_36_6310 {ECO:0000313|EMBL:CAJ09606.1}; OS Leishmania major. OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; OC Leishmaniinae; Leishmania. OX NCBI_TaxID=5664 {ECO:0000313|Proteomes:UP000000542}; RN [1] {ECO:0000313|EMBL:CAJ09606.1, ECO:0000313|Proteomes:UP000000542} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542}; RX PubMed=16020728; DOI=10.1126/science.1112680; RA Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G., RA Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A., RA Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M., RA Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., RA Cadag E., Ciarloni L., Clayton C., Coulson R.M., Cronin A., Cruz A.K., RA Davies R.M., De Gaudenzi J., Dobson D.E., Duesterhoeft A., RA Fazelina G., Fosker N., Frasch A.C., Fraser A., Fuchs M., Gabel C., RA Goble A., Goffeau A., Harris D., Hertz-Fowler C., Hilbert H., Horn D., RA Huang Y., Klages S., Knights A., Kube M., Larke N., Litvin L., RA Lord A., Louie T., Marra M., Masuy D., Matthews K., Michaeli S., RA Mottram J.C., Muller-Auer S., Munden H., Nelson S., Norbertczak H., RA Oliver K., O'neil S., Pentony M., Pohl T.M., Price C., Purnelle B., RA Quail M.A., Rabbinowitsch E., Reinhardt R., Rieger M., Rinta J., RA Robben J., Robertson L., Ruiz J.C., Rutter S., Saunders D., RA Schafer M., Schein J., Schwartz D.C., Seeger K., Seyler A., Sharp S., RA Shin H., Sivam D., Squares R., Squares S., Tosato V., Vogt C., RA Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J., Zhou S., RA Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D., Barrell B., RA Myler P.J.; RT "The genome of the kinetoplastid parasite, Leishmania major."; RL Science 309:436-442(2005). RN [2] {ECO:0000313|EMBL:CAJ09606.1, ECO:0000313|Proteomes:UP000000542} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Friedlin {ECO:0000313|EMBL:CAJ09606.1}; RX PubMed=22038252; DOI=10.1101/gr.122945.111; RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A., RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D., RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F., RA Hertz-Fowler C., Mottram J.C.; RT "Chromosome and gene copy number variation allow major structural RT change between species and strains of Leishmania."; RL Genome Res. 21:2129-2142(2011). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR796432; CAJ09606.1; -; Genomic_DNA. DR RefSeq; XP_001687219.1; XM_001687167.1. DR ProteinModelPortal; Q4Q0C9; -. DR EnsemblProtists; LmjF.36.6310:mRNA; LmjF.36.6310:pep; LmjF.36.6310. DR GeneID; 5655936; -. DR KEGG; lma:LMJF_36_6310; -. DR HOGENOM; HOG000265278; -. DR InParanoid; Q4Q0C9; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR Proteomes; UP000000542; Chromosome 36. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000542}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:CAJ09606.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000542}; KW Transferase {ECO:0000313|EMBL:CAJ09606.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 318 318 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 339 AA; 36559 MW; E12EDD6A60C062B5 CRC64; MKNHYFSCCG LPAKWKVGDM EAYLADPNYV VMLDGGLATE LETRGCDLRD PLWSGKVLLE SPQQLQNVAL AYLRAGARCI ITASYQITPQ SLMEHRRLTE DAAVAAIEES VRIAQSARER HLREKPQAAP IFVAGSVGPY GAYLADGSEY RGDYVRSAEE FKEFHRLRIA ALLRAGADVL AIETQPSAAE VRAIVALLQE EHPNCRAWVS FTTSRISPVE AISDGTKWAD IISFLEKAPQ IVAVGVNCIP MAEASAVLAH LHTLTTMPLV VYTNSGESYD AVTRTWHPIS MSDGTTLSLG ALAREWASHG ARLVGGCCRT GPSDIAGAAA ALGSADFVV // ID Q4QIT5_LEIMA Unreviewed; 1252 AA. AC Q4QIT5; DT 19-JUL-2005, integrated into UniProtKB/TrEMBL. DT 19-JUL-2005, sequence version 1. DT 29-APR-2015, entry version 69. DE SubName: Full=Complete genome, chromosome 7 {ECO:0000313|EMBL:CAJ06968.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAJ06968.1}; GN ORFNames=LMJF_07_0090 {ECO:0000313|EMBL:CAJ06968.1}; OS Leishmania major. OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; OC Leishmaniinae; Leishmania. OX NCBI_TaxID=5664 {ECO:0000313|Proteomes:UP000000542}; RN [1] {ECO:0000313|EMBL:CAJ06968.1, ECO:0000313|Proteomes:UP000000542} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542}; RX PubMed=16020728; DOI=10.1126/science.1112680; RA Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G., RA Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A., RA Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M., RA Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., RA Cadag E., Ciarloni L., Clayton C., Coulson R.M., Cronin A., Cruz A.K., RA Davies R.M., De Gaudenzi J., Dobson D.E., Duesterhoeft A., RA Fazelina G., Fosker N., Frasch A.C., Fraser A., Fuchs M., Gabel C., RA Goble A., Goffeau A., Harris D., Hertz-Fowler C., Hilbert H., Horn D., RA Huang Y., Klages S., Knights A., Kube M., Larke N., Litvin L., RA Lord A., Louie T., Marra M., Masuy D., Matthews K., Michaeli S., RA Mottram J.C., Muller-Auer S., Munden H., Nelson S., Norbertczak H., RA Oliver K., O'neil S., Pentony M., Pohl T.M., Price C., Purnelle B., RA Quail M.A., Rabbinowitsch E., Reinhardt R., Rieger M., Rinta J., RA Robben J., Robertson L., Ruiz J.C., Rutter S., Saunders D., RA Schafer M., Schein J., Schwartz D.C., Seeger K., Seyler A., Sharp S., RA Shin H., Sivam D., Squares R., Squares S., Tosato V., Vogt C., RA Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J., Zhou S., RA Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D., Barrell B., RA Myler P.J.; RT "The genome of the kinetoplastid parasite, Leishmania major."; RL Science 309:436-442(2005). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Friedlin; RA Peacock C.S, Murphy L., Ivens A.C, Berriman M., Blackwell J., RA Smith D., Collins M., Fosker N., Harris D., Oliver K., O'Neil S., RA Saunders D., Seeger K., Warren T., Rajandream M., and Barrell B.G.; RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:CAJ06968.1, ECO:0000313|Proteomes:UP000000542} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Friedlin {ECO:0000313|EMBL:CAJ06968.1}; RX PubMed=22038252; DOI=10.1101/gr.122945.111; RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A., RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D., RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F., RA Hertz-Fowler C., Mottram J.C.; RT "Chromosome and gene copy number variation allow major structural RT change between species and strains of Leishmania."; RL Genome Res. 21:2129-2142(2011). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; FR796403; CAJ06968.1; -; Genomic_DNA. DR RefSeq; XP_001680913.1; XM_001680861.1. DR ProteinModelPortal; Q4QIT5; -. DR SMR; Q4QIT5; 664-915. DR EnsemblProtists; LmjF.07.0090:mRNA; LmjF.07.0090:pep; LmjF.07.0090. DR GeneID; 5649165; -. DR KEGG; lma:LMJF_07_0090; -. DR HOGENOM; HOG000251409; -. DR InParanoid; Q4QIT5; -. DR KO; K00548; -. DR OMA; QPFFNAW; -. DR Proteomes; UP000000542; Chromosome 7. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000542}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAJ06968.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000542}; KW Transferase {ECO:0000313|EMBL:CAJ06968.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 254 254 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 318 318 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 782 782 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1252 AA; 138590 MW; 17B2A4A62D40CB8E CRC64; MSAMRGERSP VFEELEELFQ KRILVLDGGM GTMLQRYKLE ETDFRGEEFK NATKDLKGNN DLLCLTQPAK VRDVHYKYAI AGADVVETNT FNSQAVSQSD YETQHLVRRI NLAAAKICRD AAEQASRETG RRIFVAGVLG PLNRTASISP SVERPDYRNI TYDEIVAAYT EQATALLDGG VDVLLIETIF DSLNAKAALF AVNTLFEDKG YTRLPIMVSG TITDLSGRTL SGQTVDAFYS SMRHGNIISI GLNCALGCRE MRPYVERLAE ISEGYVTCHP NAGLPNAMGE YDELPEDMAR DIRDFAANGW VNLVGGCCGT TPDHIRAIAT AVKGIPPRPR GHSSETMVIS GLEALHFTHH IGFCNIGERC NISGSLKFKR LVKEGKWEEC LAVARQQVEE GAMVLDVNMD DGLIDGVTAM TRFLNMIASD PEVARVPVMI DSSKFHVIEA GLKCTQGTPI VNSISLKVGE EEFLRQARLI RRYGAAVVVM AFDENGQAAD DANKTRICKR AYDMLVADGF PPENIVFDPN VLTICTGMEE HNNYAIDFMN AATWIKANLP RAKVSGGISN LSFSFRGFEA IRMAMHSAFL KKMIADGSLD MAIVNAGALP VYTDIEPDLL QLVEDAIYNR TPHSSERILE YAERLKAEKA SGGGAEEAKV SKVDEWRNAS VEERLSHALI KGIVEFIEDD VEEARTCGKY ERPLHIIEGP LMGGMGKVGE LFGSGKMFLP QVIKSARVMK KAVAVLVPYM EAEKAALMAD TNGASTSRAK RVLMATVKGD VHDIGKNIVG VVLGCNSYEV LDLGVMVSCE KILAAAREHD VDVIGLSGLI TPSLDEMVHV AKEMKRMGFN IPLMVGGATT SKQHTAVKIQ PHYNKTVHVL DASKAVVTVS NMLGSSEEEF WEEVHETYQE IAEDYLANLK DRVYKPLAFC RENALKIDFV EHPPAPRPRK LGTITISDYS VEMIATRIDW NPFFSVWQVR GTYPNRGFPK LFNCPTVGAE AKRLFDDAQE MLKDIIATRS FRAKAVVTLM PVNSVGDDIE VYKDDTRNEK IATFFGLRQQ SEKERGEPYL CISDFIAPKG VAPDYLGSLV VGIFGADKMS EQYEKDNDSY RSIMIKALAD RFAEAFTEEV HRIIRTDLWG YAEKETAKTA DLIQMQYQGI RPAPGYPSQP DHTEMDTMWR IGEVEERTGV KLSESYAMIP AASVSALVFA HAQSKYFAVG KIQKDQVKDY AERKGWNLDR AESQLSSSLA YN // ID Q4RB63_TETNG Unreviewed; 119 AA. AC Q4RB63; DT 19-JUL-2005, integrated into UniProtKB/TrEMBL. DT 19-JUL-2005, sequence version 1. DT 29-OCT-2014, entry version 36. DE SubName: Full=Chromosome undetermined SCAF22184, whole genome shotgun sequence {ECO:0000313|EMBL:CAG14370.1}; DE Flags: Fragment; GN ORFNames=GSTENG00036228001 {ECO:0000313|EMBL:CAG14370.1}; OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon OS nigroviridis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; OC Tetraodon. OX NCBI_TaxID=99883; RN [1] {ECO:0000313|EMBL:CAG14370.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15496914; DOI=10.1038/nature03025; RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N., RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., RA Nicaud S., Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., RA Dasilva C., Salanoubat M., Levy M., Boudet N., Castellano S., RA Anthouard V., Jubin C., Castelli V., Katinka M., Vacherie B., RA Biemont C., Skalli Z., Cattolico L., Poulain J., De Berardinis V., RA Cruaud C., Duprat S., Brottier P., Coutanceau J.-P., Gouzy J., RA Parra G., Lardier G., Chapple C., McKernan K.J., McEwan P., Bosak S., RA Kellis M., Volff J.-N., Guigo R., Zody M.C., Mesirov J., RA Lindblad-Toh K., Birren B., Nusbaum C., Kahn D., Robinson-Rechavi M., RA Laudet V., Schachter V., Quetier F., Saurin W., Scarpelli C., RA Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.; RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals RT the early vertebrate proto-karyotype."; RL Nature 431:946-957(2004). RN [2] {ECO:0000313|EMBL:CAG14370.1} RP NUCLEOTIDE SEQUENCE. RG Genoscope; RG Whitehead Institute Centre for Genome Research; RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAAE01022184; CAG14370.1; -; Genomic_DNA. DR STRING; 99883.ENSTNIP00000022668; -. DR eggNOG; NOG325165; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. PE 4: Predicted; FT NON_TER 1 1 {ECO:0000313|EMBL:CAG14370.1}. SQ SEQUENCE 119 AA; 12983 MW; 89E033E22BDCECE8 CRC64; GAQINEAACD LAREVANEGN ALVAGGVSQT PAYLSCKSEE EVKAIFKKQL DVFVKKDVDF LIAEYFEHVE EAEWAVHVLK TAGKPVAATL GGSERSQPRG MWRQACQSWS SDCGHQLPF // ID Q4RPR6_TETNG Unreviewed; 484 AA. AC Q4RPR6; DT 19-JUL-2005, integrated into UniProtKB/TrEMBL. DT 19-JUL-2005, sequence version 1. DT 29-OCT-2014, entry version 36. DE SubName: Full=Chromosome 12 SCAF15007, whole genome shotgun sequence {ECO:0000313|EMBL:CAG09616.1}; DE Flags: Fragment; GN ORFNames=GSTENG00030962001 {ECO:0000313|EMBL:CAG09616.1}; OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon OS nigroviridis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; OC Tetraodon. OX NCBI_TaxID=99883; RN [1] {ECO:0000313|EMBL:CAG09616.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15496914; DOI=10.1038/nature03025; RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N., RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., RA Nicaud S., Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., RA Dasilva C., Salanoubat M., Levy M., Boudet N., Castellano S., RA Anthouard V., Jubin C., Castelli V., Katinka M., Vacherie B., RA Biemont C., Skalli Z., Cattolico L., Poulain J., De Berardinis V., RA Cruaud C., Duprat S., Brottier P., Coutanceau J.-P., Gouzy J., RA Parra G., Lardier G., Chapple C., McKernan K.J., McEwan P., Bosak S., RA Kellis M., Volff J.-N., Guigo R., Zody M.C., Mesirov J., RA Lindblad-Toh K., Birren B., Nusbaum C., Kahn D., Robinson-Rechavi M., RA Laudet V., Schachter V., Quetier F., Saurin W., Scarpelli C., RA Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.; RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals RT the early vertebrate proto-karyotype."; RL Nature 431:946-957(2004). RN [2] {ECO:0000313|EMBL:CAG09616.1} RP NUCLEOTIDE SEQUENCE. RG Genoscope; RG Whitehead Institute Centre for Genome Research; RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAAE01015007; CAG09616.1; -; Genomic_DNA. DR ProteinModelPortal; Q4RPR6; -. DR STRING; 99883.ENSTNIP00000019814; -. DR eggNOG; COG0646; -. DR HOVERGEN; HBG080367; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; FT NON_TER 484 484 {ECO:0000313|EMBL:CAG09616.1}. SQ SEQUENCE 484 AA; 52897 MW; ED2026203A35E719 CRC64; MHVGVIGGAS VPGAFPPGNP GPKQVVQKMK SLFPPARTSS FVSSSVAGQH TAAVAQAPPP PRGDLKSAKH LSNVASASQS LSSRESTQLQ EYGTGKRRER LNAGEIVIGD GGFVFALEKR GYVKAGPWTP EATKEHPEAV RQLHREFLRA GANVMQTFTF YASDDKLENR GNKVTYTGVQ INEAACDLAR EVANEGDALV AGGVCQTPSY LSCKSEKEVK DIFKRQLDVF VKKNVDFLIA EYFEHVEEAV WAVEVLKTTG KPVAASLCIG PKGDMHGVSP GECAVRLVKA GAQIVGVNCH FDPMTCVETV KLMKEGVEKA GLKAHYMVQP LAFHTPDCNC QGFIDLPEFP FGLEPRILTR WDMHKYAREA YNAGIRFIGG CCGFEPYHIR ALAEELAPER GFLPVGSDKH GNWGAGLEMH TKPWVRARAR RDYWEALKPA SGRPLCPSLS TPDCWGVTKG DTELMQQKEA TSKEQLKQLF DRSK // ID Q4S116_TETNG Unreviewed; 372 AA. AC Q4S116; DT 19-JUL-2005, integrated into UniProtKB/TrEMBL. DT 19-JUL-2005, sequence version 1. DT 27-MAY-2015, entry version 41. DE SubName: Full=Chromosome 1 SCAF14770, whole genome shotgun sequence {ECO:0000313|EMBL:CAG05666.1}; GN ORFNames=GSTENG00025770001 {ECO:0000313|EMBL:CAG05666.1}; OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon OS nigroviridis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; OC Tetraodon. OX NCBI_TaxID=99883; RN [1] {ECO:0000313|EMBL:CAG05666.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15496914; DOI=10.1038/nature03025; RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N., RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., RA Nicaud S., Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., RA Dasilva C., Salanoubat M., Levy M., Boudet N., Castellano S., RA Anthouard V., Jubin C., Castelli V., Katinka M., Vacherie B., RA Biemont C., Skalli Z., Cattolico L., Poulain J., De Berardinis V., RA Cruaud C., Duprat S., Brottier P., Coutanceau J.-P., Gouzy J., RA Parra G., Lardier G., Chapple C., McKernan K.J., McEwan P., Bosak S., RA Kellis M., Volff J.-N., Guigo R., Zody M.C., Mesirov J., RA Lindblad-Toh K., Birren B., Nusbaum C., Kahn D., Robinson-Rechavi M., RA Laudet V., Schachter V., Quetier F., Saurin W., Scarpelli C., RA Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.; RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals RT the early vertebrate proto-karyotype."; RL Nature 431:946-957(2004). RN [2] {ECO:0000313|EMBL:CAG05666.1} RP NUCLEOTIDE SEQUENCE. RG Genoscope; RG Whitehead Institute Centre for Genome Research; RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAAE01014770; CAG05666.1; -; Genomic_DNA. DR ProteinModelPortal; Q4S116; -. DR HOGENOM; HOG000039956; -. DR HOVERGEN; HBG062720; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 372 AA; 40039 MW; BE02EA970BF24E81 CRC64; MESSPRLNRY LCDDGPFILD GGLATDLEAQ GVHLQGDPLW SARLLYTNPQ AIRDAHCRFL LSGADVISTA TYQASVEGFM DHLNVSSEGA KELIMSGVQL AKEAVESFVP GTNPNTTVQS GEGKVNSEGS EGLAGQCSSG RRCPLVAGSL GPYGAFLHNG SEYTGDYAEK MSVQELKAWH RPQVECLAAA EADVLAFETI PSIKEAEALV ELLKEFPNTK AWLSLSCKDV KRLSDGSLFR DAVQIANRSE QLIAVGVNCC PPELVEPLLD SARTLLSPEI SWVVYPNSGE SWDPEQGWCT SEAALPALLE MSGTWVKQGA ALIGGCCRIS PAHVAKLRRH LKGSRGSPTS EPRPKCKPSL HTGRKRDHAL VV // ID Q4SVW5_TETNG Unreviewed; 375 AA. AC Q4SVW5; DT 19-JUL-2005, integrated into UniProtKB/TrEMBL. DT 19-JUL-2005, sequence version 1. DT 27-MAY-2015, entry version 47. DE SubName: Full=Chromosome undetermined SCAF13712, whole genome shotgun sequence {ECO:0000313|EMBL:CAF95217.1}; DE Flags: Fragment; GN ORFNames=GSTENG00011776001 {ECO:0000313|EMBL:CAF95217.1}; OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon OS nigroviridis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; OC Tetraodon. OX NCBI_TaxID=99883; RN [1] {ECO:0000313|EMBL:CAF95217.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15496914; DOI=10.1038/nature03025; RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N., RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., RA Nicaud S., Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., RA Dasilva C., Salanoubat M., Levy M., Boudet N., Castellano S., RA Anthouard V., Jubin C., Castelli V., Katinka M., Vacherie B., RA Biemont C., Skalli Z., Cattolico L., Poulain J., De Berardinis V., RA Cruaud C., Duprat S., Brottier P., Coutanceau J.-P., Gouzy J., RA Parra G., Lardier G., Chapple C., McKernan K.J., McEwan P., Bosak S., RA Kellis M., Volff J.-N., Guigo R., Zody M.C., Mesirov J., RA Lindblad-Toh K., Birren B., Nusbaum C., Kahn D., Robinson-Rechavi M., RA Laudet V., Schachter V., Quetier F., Saurin W., Scarpelli C., RA Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.; RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals RT the early vertebrate proto-karyotype."; RL Nature 431:946-957(2004). RN [2] {ECO:0000313|EMBL:CAF95217.1} RP NUCLEOTIDE SEQUENCE. RG Genoscope; RG Whitehead Institute Centre for Genome Research; RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAAE01013712; CAF95217.1; -; Genomic_DNA. DR STRING; 99883.ENSTNIP00000008411; -. DR eggNOG; COG1410; -. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; FT NON_TER 1 1 {ECO:0000313|EMBL:CAF95217.1}. FT NON_TER 375 375 {ECO:0000313|EMBL:CAF95217.1}. SQ SEQUENCE 375 AA; 40896 MW; BA8B55F259091008 CRC64; LEPELRGILE RRIMILDGGM GTMIQQHKLE ECNFRGDEFK DHPQPLMGNN DLLSLTCPDI VYKIHKDYLL AGADIIETNT FSGTSVAQAD YGLEHMAYRL NKASAELARK AADDVTSSTG VKRYVAGALG PTNKTLSVSP SVEKPHFRNI TFDALVEAYT EQVKGLLDGG VDILLVETIF DTANAKAALF AIDLLFEKSY SRKPIFISGT VVDRSGRTLS GQTVEAFVVS VSHAKPLCIG LNCALGATEM RPFIEAIGKC TTAFVICYPN AGNPHLFKNV LCCLCQFSVD GLVNIVGGCC GTTPEHIRAL CEAVKMCQPR VAPAEMYKDY MMLSGLEPFK VGPYTNFVNI GERCNVAGSR KFAKLITSGL YEVRL // ID Q4V7P6_XENLA Unreviewed; 116 AA. AC Q4V7P6; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 27-MAY-2015, entry version 36. DE SubName: Full=MGC115492 protein {ECO:0000313|EMBL:AAH97785.1}; GN Name=MGC115492 {ECO:0000313|EMBL:AAH97785.1}; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; OC Xenopus. OX NCBI_TaxID=8355 {ECO:0000313|EMBL:AAH97785.1}; RN [1] {ECO:0000313|EMBL:AAH97785.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Egg {ECO:0000313|EMBL:AAH97785.1}; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (JUN-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; BC097785; AAH97785.1; -; mRNA. DR RefSeq; NP_001089521.1; NM_001096052.1. DR UniGene; Xl.52588; -. DR ProteinModelPortal; Q4V7P6; -. DR GeneID; 734575; -. DR Xenbase; XB-GENE-5936157; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; SQ SEQUENCE 116 AA; 12290 MW; A64A23834B21F4AA CRC64; MAEAVKILSG GLSTELENAG FLLQGDPLWS ARLLQTNPQA IKNVHTSFLK SGAEVLSTAT YQASVKGFQE HLGLSIDEAE ELFHVGVRLA KEAAAEVKGI KGLAQVADAV LGLCWD // ID Q4WE23_ASPFU Unreviewed; 343 AA. AC Q4WE23; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 29-APR-2015, entry version 49. DE SubName: Full=Homocysteine S-methyltransferase, putative {ECO:0000313|EMBL:EAL86154.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:EAL86154.1}; GN ORFNames=AFUA_5G01500 {ECO:0000313|EMBL:EAL86154.1}; 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 {ECO:0000313|EMBL:EAL86154.1, ECO:0000313|Proteomes:UP000002530}; RN [1] {ECO:0000313|EMBL:EAL86154.1, ECO:0000313|Proteomes:UP000002530} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100 RC {ECO:0000313|Proteomes:UP000002530}; 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., RA Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., RA Farman M., Fedorova N., Fedorova N., 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., RA Haas H., Harris D., Horiuchi H., Huang J., Humphray S., Jimenez J., RA Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., RA Kulkarni R., Kumagai T., Lafon A., Latge J.P., Li W., Lord A., Lu C., RA Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., RA Mouyna I., Mulligan S., Murphy L., 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., Yu J.H., Fraser C., Galagan J.E., Asai K., RA Machida M., Hall N., Barrell B., 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. {ECO:0000313|EMBL:EAL86154.1}. 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; AAHF01000011; EAL86154.1; -; Genomic_DNA. DR RefSeq; XP_748192.1; XM_743099.1. DR STRING; 5085.CADAFUAP00002592; -. DR EnsemblFungi; CADAFUAT00002592; CADAFUAP00002592; CADAFUAG00002592. DR GeneID; 3505414; -. DR KEGG; afm:AFUA_5G01500; -. DR EuPathDB; FungiDB:Afu5g01500; -. DR HOGENOM; HOG000265278; -. DR InParanoid; Q4WE23; -. DR KO; K00547; -. DR OMA; YGRSVTK; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000002530; Chromosome 5. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002530}; KW Methyltransferase {ECO:0000313|EMBL:EAL86154.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002530}; KW Transferase {ECO:0000313|EMBL:EAL86154.1}. SQ SEQUENCE 343 AA; 37173 MW; E34626535B723647 CRC64; MTSIQILDGG LGTSLQDQHG VTFDSSTPLW SSHLLVSDPT TLLACQRNFI TAGCDVLLTA TYQVSIEGFA RTKTPEFPDG IPRPAIGKYL RTALAVAEQA RVSPSAAKIA LSLGPYGACM IPGQEYSGKY DAEHDSEETL FQWHLERLRL FLEADEKLAE RVQYVAFETL PRLDEIRAVR RAIRTAGLNV PFWVACVFPG EEATLPDGSS IGQIVQAALA EMDGAAVPWG VGINCTKIHK LDGLVREFGE EVASAVGQGQ VGAVPSLVLY PDGTNGEVYN TTTQTWEKQE GYTSDARGPW EVQLAQIVTN ARATGPFTSF LVGGCCKASH RDIRKLAEQL KNE // ID Q4WFR2_ASPFU Unreviewed; 313 AA. AC Q4WFR2; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 29-APR-2015, entry version 48. DE SubName: Full=Homocysteine S-methyltransferase, putative {ECO:0000313|EMBL:EAL86415.1}; DE EC=2.1.1.- {ECO:0000313|EMBL:EAL86415.1}; GN ORFNames=AFUA_3G01320 {ECO:0000313|EMBL:EAL86415.1}; 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 {ECO:0000313|EMBL:EAL86415.1, ECO:0000313|Proteomes:UP000002530}; RN [1] {ECO:0000313|EMBL:EAL86415.1, ECO:0000313|Proteomes:UP000002530} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100 RC {ECO:0000313|Proteomes:UP000002530}; 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., RA Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., RA Farman M., Fedorova N., Fedorova N., 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., RA Haas H., Harris D., Horiuchi H., Huang J., Humphray S., Jimenez J., RA Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., RA Kulkarni R., Kumagai T., Lafon A., Latge J.P., Li W., Lord A., Lu C., RA Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., RA Mouyna I., Mulligan S., Murphy L., 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., Yu J.H., Fraser C., Galagan J.E., Asai K., RA Machida M., Hall N., Barrell B., 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. {ECO:0000313|EMBL:EAL86415.1}. 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; AAHF01000010; EAL86415.1; -; Genomic_DNA. DR RefSeq; XP_748453.1; XM_743360.1. DR STRING; 5085.CADAFUAP00000116; -. DR EnsemblFungi; CADAFUAT00000116; CADAFUAP00000116; CADAFUAG00000116. DR GeneID; 3506126; -. DR KEGG; afm:AFUA_3G01320; -. DR EuPathDB; FungiDB:Afu3g01320; -. DR HOGENOM; HOG000179103; -. DR InParanoid; Q4WFR2; -. DR OMA; CCGTDHR; -. DR OrthoDB; EOG7XH70V; -. DR Proteomes; UP000002530; Chromosome 3. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002530}; KW Methyltransferase {ECO:0000313|EMBL:EAL86415.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002530}; KW Transferase {ECO:0000313|EMBL:EAL86415.1}. SQ SEQUENCE 313 AA; 33680 MW; 0421F3EE3ECE8B66 CRC64; MALPQLLSPK PFLTECGMET SLVYKDKVHL PCFSSLPLVD SDSSRKLISH YYDSYISIAA ANGTGIVLDT RTWRGATPWA QPMGLSADKL LELNRAAVRL AKEARNRAVG GENNIPVVIS GTMGPLRDAY VDTSELITLE DAREGYREQV EVLADAGVDM LAIMTVTNLN EAIAVVELAK EVRLPVVVSF SIESDGRLLG GRSLGSAIRT VDEKTGGSVV YYGVNCAHPV RISAALRDVP EDVRGRIGLI KGNASLKSHD ELDNSETLDR GDISVFTDGF EGVLPLVPNV KVIGGCCGTD EEHLEAVAKR CIK // ID Q4Y025_PLACH Unreviewed; 504 AA. AC Q4Y025; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 27-MAY-2015, entry version 36. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:CAH77485.1}; GN ORFNames=PC000275.02.0 {ECO:0000313|EMBL:CAH77485.1}; OS Plasmodium chabaudi. OC Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia). OX NCBI_TaxID=5825 {ECO:0000313|Proteomes:UP000002509}; RN [1] {ECO:0000313|EMBL:CAH77485.1, ECO:0000313|Proteomes:UP000002509} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AS {ECO:0000313|Proteomes:UP000002509}; RX PubMed=15637271; DOI=10.1126/science.1103717; RA Hall N., Karras M., Raine J.D., Carlton J.M., Kooij T.W.A., RA Berriman M., Florens L., Janssen C.S., Pain A., Christophides G.K., RA James K., Rutherford K., Harris B., Harris D., Churcher C.M., RA Quail M.A., Ormond D., Doggett J., Trueman H.E., Mendoza J., RA Bidwell S.L., Rajandream M.A., Carucci D.J., Yates J.R. III, RA Kafatos F.C., Janse C.J., Barrell B.G., Turner C.M.R., Waters A.P., RA Sinden R.S.; RT "A comprehensive survey of the Plasmodium life cycle by genomic, RT transcriptomic, and proteomic analyses."; RL Science 307:82-86(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; CAAJ01002002; CAH77485.1; -; Genomic_DNA. DR RefSeq; XP_745704.1; XM_740611.1. DR ProteinModelPortal; Q4Y025; -. DR GeneID; 3498828; -. DR KEGG; pcb:PC000275.02.0; -. DR EuPathDB; PlasmoDB:PCHAS_145060; -. DR HOGENOM; HOG000283439; -. DR InParanoid; Q4Y025; -. DR Proteomes; UP000002509; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 4. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 2. DR SUPFAM; SSF82282; SSF82282; 4. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002509}; KW Reference proteome {ECO:0000313|Proteomes:UP000002509}. SQ SEQUENCE 504 AA; 59436 MW; A4012A0F90BCF2FE CRC64; MNKRLYTLDG GKISEFERLG LSHFDFLSCK YNEEEKAKGI ENLKNIHLSY LLSGSNIITT NTYQVNLHFK RNNISIENGK EIIDTYIDIA YESCEKYKQI KKRNTCLYSD LETYKSPYDY VNHFQNVRQN LNVSHANDKI NVQEYFNYVD LQNDILGKKI KMKKSSENFI AFSNGSYNSS FRNFTEYSGV FQKGGISQGV KKKKNETSTL QNRLGKQFDI KLNLTQFKKT FKEVRSPIEM VPKCKKVYEK CETNEDNNFR CDFFPTQKLF NYGIEYYIDV TDEEILANCK FKLESFCRNK NKLNFFSLLT CTNIREVFTF YNTIKYYATN FNNNVIINFF CNHPKNIGCS NYSFFDIVSL LLYLDSYNKY IYAIGLNCVN INYVYNLFLP FKKYTSKYNN INIELYKSEN QQINPFIKNV LNDIKKNRYI YDVNFFCSPN KTLDKVSFDN NTVDFQTHSK NKKMHVYNHI EKWIDVGING FGGCCYYTPY DISLINYGLS KIVT // ID Q4YHP2_PLABA Unreviewed; 466 AA. AC Q4YHP2; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 27-MAY-2015, entry version 35. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:CAI02474.1}; DE Flags: Fragment; GN ORFNames=PB300776.00.0 {ECO:0000313|EMBL:CAI02474.1}; OS Plasmodium berghei (strain Anka). OC Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia). OX NCBI_TaxID=5823 {ECO:0000313|Proteomes:UP000007720}; RN [1] {ECO:0000313|EMBL:CAI02474.1, ECO:0000313|Proteomes:UP000007720} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ANKA {ECO:0000313|Proteomes:UP000007720}; RX PubMed=15637271; DOI=10.1126/science.1103717; RA Hall N., Karras M., Raine J.D., Carlton J.M., Kooij T.W.A., RA Berriman M., Florens L., Janssen C.S., Pain A., Christophides G.K., RA James K., Rutherford K., Harris B., Harris D., Churcher C.M., RA Quail M.A., Ormond D., Doggett J., Trueman H.E., Mendoza J., RA Bidwell S.L., Rajandream M.A., Carucci D.J., Yates J.R. III, RA Kafatos F.C., Janse C.J., Barrell B.G., Turner C.M.R., Waters A.P., RA Sinden R.S.; RT "A comprehensive survey of the Plasmodium life cycle by genomic, RT transcriptomic, and proteomic analyses."; RL Science 307:82-86(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; CAAI01005004; CAI02474.1; -; Genomic_DNA. DR RefSeq; XP_674427.1; XM_669335.1. DR GeneID; 3422870; -. DR KEGG; pbe:PB300776.00.0; -. DR EuPathDB; PlasmoDB:PBANKA_144830; -. DR HOGENOM; HOG000283439; -. DR InParanoid; Q4YHP2; -. DR Proteomes; UP000007720; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 4. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 4. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007720}; KW Reference proteome {ECO:0000313|Proteomes:UP000007720}. FT NON_TER 466 466 {ECO:0000313|EMBL:CAI02474.1}. SQ SEQUENCE 466 AA; 55385 MW; 197D1DFDAB792046 CRC64; MSKRLYILDG GKISEFERLG LPHFDFLSCK YNDEDKKKAM KSLENIHLSY LLSGSNIITT NTYQVNLHSL EKNNISIEKG EEIINTYIDI AYESCEKYKQ IKKRNICLYS DLETYKSPYE YVENFQNIRQ NLNVCNSNDK INAHEYFNYL DLQNDIFGNK IKMTKSSENF IAFSNGSYNS SFRNFTEYSG VFQKGNISRD VEKKENENMG FVQNKKQKNK IKKLYNNRLG KEFDIKLNLI HLKKTFKEVR SSIEMVPKCK KLYEKCETNK IENNDFKYDF FPTQKLFNYG IEYYIDVTDE EILANCKFKL EAFCRNKNKL NFFSLLTCTN IREVFTFYNT IKYYATSFNN NIIINFFCNN PKNIGCNYSF FDIVSLLLYL DSYNKYIYAI GLNCVNINYV YNLFLPFKKY TSTYNNINIE LYKSENHQIN SFIKNILNEI KKNRYIYDVN FFCSPNKTLE KVSFDN // ID Q4Z7S0_PLABA Unreviewed; 105 AA. AC Q4Z7S0; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 27-MAY-2015, entry version 34. DE SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:CAH93576.1}; DE Flags: Fragment; GN ORFNames=PB000029.00.0 {ECO:0000313|EMBL:CAH93576.1}; OS Plasmodium berghei (strain Anka). OC Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia). OX NCBI_TaxID=5823 {ECO:0000313|Proteomes:UP000007720}; RN [1] {ECO:0000313|EMBL:CAH93576.1, ECO:0000313|Proteomes:UP000007720} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ANKA {ECO:0000313|Proteomes:UP000007720}; RX PubMed=15637271; DOI=10.1126/science.1103717; RA Hall N., Karras M., Raine J.D., Carlton J.M., Kooij T.W.A., RA Berriman M., Florens L., Janssen C.S., Pain A., Christophides G.K., RA James K., Rutherford K., Harris B., Harris D., Churcher C.M., RA Quail M.A., Ormond D., Doggett J., Trueman H.E., Mendoza J., RA Bidwell S.L., Rajandream M.A., Carucci D.J., Yates J.R. III, RA Kafatos F.C., Janse C.J., Barrell B.G., Turner C.M.R., Waters A.P., RA Sinden R.S.; RT "A comprehensive survey of the Plasmodium life cycle by genomic, RT transcriptomic, and proteomic analyses."; RL Science 307:82-86(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; CAAI01000027; CAH93576.1; -; Genomic_DNA. DR RefSeq; XP_677093.1; XM_672001.1. DR GeneID; 3425617; -. DR KEGG; pbe:PB000029.00.0; -. DR EuPathDB; PlasmoDB:PBANKA_144830; -. DR Proteomes; UP000007720; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007720}; KW Reference proteome {ECO:0000313|Proteomes:UP000007720}. FT NON_TER 105 105 {ECO:0000313|EMBL:CAH93576.1}. SQ SEQUENCE 105 AA; 12268 MW; 63742D6C8EAB392F CRC64; MSKRLYILDG GKISEFERLG LPHFDFLSCK YNDEDKKKAM KSLENIHLSY LLSGSNIITT NTYQVNLHSL EKNNISIEKG EEIINTYIDI AYESCEKYKQ IKKRN // ID Q4ZTL9_PSEU2 Unreviewed; 1239 AA. AC Q4ZTL9; DT 07-JUN-2005, integrated into UniProtKB/TrEMBL. DT 07-JUN-2005, sequence version 1. DT 27-MAY-2015, entry version 73. DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:AAY37503.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AAY37503.1}; GN OrderedLocusNames=Psyr_2464 {ECO:0000313|EMBL:AAY37503.1}; OS Pseudomonas syringae pv. syringae (strain B728a). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae. OX NCBI_TaxID=205918 {ECO:0000313|EMBL:AAY37503.1, ECO:0000313|Proteomes:UP000000426}; RN [1] {ECO:0000313|EMBL:AAY37503.1, ECO:0000313|Proteomes:UP000000426} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B728a {ECO:0000313|EMBL:AAY37503.1, RC ECO:0000313|Proteomes:UP000000426}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000075; AAY37503.1; -; Genomic_DNA. DR RefSeq; WP_011267702.1; NC_007005.1. DR RefSeq; YP_235541.1; NC_007005.1. DR ProteinModelPortal; Q4ZTL9; -. DR SMR; Q4ZTL9; 654-1238. DR STRING; 205918.Psyr_2464; -. DR EnsemblBacteria; AAY37503; AAY37503; Psyr_2464. DR GeneID; 3367981; -. DR KEGG; psb:Psyr_2464; -. DR PATRIC; 19985512; VBIPseSyr42314_2522. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PSYR205918:GJ94-2506-MONOMER; -. DR Proteomes; UP000000426; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000426}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AAY37503.1}; KW Transferase {ECO:0000313|EMBL:AAY37503.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1239 AA; 135974 MW; 92F056EF0469AC80 CRC64; MSDRSARHQA FLTALKQRIL ILDGGMGTMI QSYRLEEQDY RGKRFADWPS DVKGNNDLLI LTRPDVIGAI EKAYLDAGAD ILETNTFNAT QVSQADYGME SIVYELNVEG ARLARKVADA KTLETPDRPR FVAGVLGPTS RTCSLSPDVN NPGYRNVTFD ELVENYTEAT KGLIEGGADL ILIETIFDTL NAKAAIFAVQ GVFEEVGFEL PIMISGTITD ASGRTLSGQT TEAFWNSISH AKPISVGLNC ALGASELRPY LQELANKANT HVSAHPNAGL PNAFGEYDEL PSQTAKIIEE FAQSGFLNIV GGCCGTTPAH IKAIAEAVSG YAPREIPDIP KACRLSGLEP FTIDRQSLFV NVGERTNITG SARFARLIRE DNYTEALEVA LQQVEAGAQV IDINMDEGML DSKKAMVTFL NLIAGEPDIS RVPIMIDSSK WEVIEAGLKC IQGKGIVNSI SMKEGVEQFI HHARLCKRYG AAVVVMAFDE QGQADTEARK KEICKRSYDI LVDEVGFPPE DIIFDPNIFA IATGIEEHNN YAVDFINACA YIRDELPYAL TSGGVSNVSF SFRGNNPVRE AIHSVFLLHA IRNGLSMGIV NAGQLEIYDQ IPAELRDCVE DVVLNRNPEG TDALLAIADK FKGDGSVKEA ETEEWRSWPV NQRLEHALVK GITTHIVQDT EESRVGFARP IEVIEGPLMA GMNVVGDLFG AGKMFLPQVV KSARVMKQAV AHLIPFIELE KGDKPEAKGK ILMATVKGDV HDIGKNIVGV VLGCNGYDIV DLGVMVPAEK ILQVARDEKC DIIGLSGLIT PSLDEMVHVA REMQRQDFHL PLMIGGATTS KAHTAVKIEP KYSNDAVIYV TDASRAVGVA TQLLSKELKP AFIEKTRLEY VEVRERTSAR SARTERLSYG AAVAKKPQFD WENYTPAQPT FTGTRVLQDI DLNVLAEYID WTPFFISWDL AGKYPRILTD EVVGEAATAL YADATQMLRK LIDEKLISAR AVFGFWPANQ VNDDDLEVYD DDGKPLAKLH HLRQQTIKPD GKPNFSLADF VAPKDSGLTD YIGGFITTAG IGAEEVAKAY QDKGDDYNSI MVKALADRLA EACAEWLHQQ VRKEYWGYAQ DEALDNEALI KEQYMGIRPA PGYPACPDHT EKGTLFALLD PLPEGSAEHT AGKSGVFLTE HYAMFPAAAV SGWYFAHPQA QYFAVGKIDK DQVESYTARK GQDLSVTERW LAPNLGYDE // ID Q4ZXU1_PSEU2 Unreviewed; 310 AA. AC Q4ZXU1; DT 07-JUN-2005, integrated into UniProtKB/TrEMBL. DT 07-JUN-2005, sequence version 1. DT 27-MAY-2015, entry version 54. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AAY36031.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:AAY36031.1}; GN OrderedLocusNames=Psyr_0975 {ECO:0000313|EMBL:AAY36031.1}; OS Pseudomonas syringae pv. syringae (strain B728a). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae. OX NCBI_TaxID=205918 {ECO:0000313|EMBL:AAY36031.1, ECO:0000313|Proteomes:UP000000426}; RN [1] {ECO:0000313|EMBL:AAY36031.1, ECO:0000313|Proteomes:UP000000426} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B728a {ECO:0000313|EMBL:AAY36031.1, RC ECO:0000313|Proteomes:UP000000426}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; AAY36031.1; -; Genomic_DNA. DR RefSeq; WP_011266750.1; NC_007005.1. DR RefSeq; YP_234069.1; NC_007005.1. DR ProteinModelPortal; Q4ZXU1; -. DR STRING; 205918.Psyr_0975; -. DR EnsemblBacteria; AAY36031; AAY36031; Psyr_0975. DR GeneID; 3366469; -. DR KEGG; psb:Psyr_0975; -. DR PATRIC; 19982431; VBIPseSyr42314_1004. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; PYVDVWL; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; PSYR205918:GJ94-994-MONOMER; -. DR Proteomes; UP000000426; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000426}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:AAY36031.1}; KW Transferase {ECO:0000313|EMBL:AAY36031.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 219 219 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 296 296 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 310 AA; 33079 MW; 80A71E9C87EFB9FE CRC64; MSFFHIHISR SHMTQGTTVI LDGGMGRELQ RRGAPFRQPE WSALALSEAP EAVSAVHAAY IESGAQVITS NSYAVVPFHI GEERFAREGQ ALAALAGQLA RESADASGGR ARVAGSIPPL FGSYRPDLYK PEQATDVLKP LVAGLSPYVD LWLAETQSCI LEAQTIRAGL PNDGKPFWLS FTLQDEDTDE VPRLRSGEPV ADAARAAAAM GVATLLFNCS QPEVIGGAID AAREVFTSLN VDIAIGAYAN AFPPQPKDAT ANDGLDELRE DLDPQGYQQW AADWVKRGAT HIGGCCGIGP EHIAVLSRSL // ID Q57FI9_BRUAB Unreviewed; 1261 AA. AC Q57FI9; DT 10-MAY-2005, integrated into UniProtKB/TrEMBL. DT 10-MAY-2005, sequence version 1. DT 27-MAY-2015, entry version 73. DE SubName: Full=MetH, 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AAX73595.1}; GN Name=metH {ECO:0000313|EMBL:AAX73595.1}; GN OrderedLocusNames=BruAb1_0184 {ECO:0000313|EMBL:AAX73595.1}; OS Brucella abortus biovar 1 (strain 9-941). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=262698 {ECO:0000313|EMBL:AAX73595.1, ECO:0000313|Proteomes:UP000000540}; RN [1] {ECO:0000313|EMBL:AAX73595.1, ECO:0000313|Proteomes:UP000000540} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=9-941 {ECO:0000313|EMBL:AAX73595.1, RC ECO:0000313|Proteomes:UP000000540}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AE017223; AAX73595.1; -; Genomic_DNA. DR RefSeq; WP_002965438.1; NC_006932.1. DR RefSeq; YP_220956.1; NC_006932.1. DR ProteinModelPortal; Q57FI9; -. DR SMR; Q57FI9; 673-921. DR STRING; 262698.BruAb1_0184; -. DR EnsemblBacteria; AAX73595; AAX73595; BruAb1_0184. DR GeneID; 3786978; -. DR KEGG; bmb:BruAb1_0184; -. DR PATRIC; 17821920; VBIBruAbo15061_0203. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; BABO262698:GJC2-186-MONOMER; -. DR PRO; PR:Q57FI9; -. DR Proteomes; UP000000540; Chromosome I. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000540}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AAX73595.1}; KW Transferase {ECO:0000313|EMBL:AAX73595.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 263 263 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 326 326 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 327 327 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 783 783 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1261 AA; 138652 MW; B65506A5F8F0B796 CRC64; MASSLDDLFG ATAAKPDGSE VLAALTQAAR ERILILDGAM GTQIQGLGFH EEHFRGDRFA TCDCQLQGNN DLLTLTQPKA IEEIHYAYAM AGADILETNT FSSTSIAQAD YGMEAMVYDL NRDGARLARR AALRAEQKDG RRRFVAGALG PTNRTASLSP DVNNPGFRAV TFDDLRIAYS EQIRGLIDGG SDIILIETIF DTLNAKAAVF ATEEVFAEKG VRLPVMISGT ITDLSGRTLS GQTPTAFWYS LRHARPFTIG LNCALGANAM RAHLDELSGI ADTFICAYPN AGLPNEFGQY DETPEAMAAQ IEGFARDGLV NVVGGCCGST PDHIRAIAQA VAKYEPRKPA KVPPLMRLSG LEPFTLTKDI PFVNIGERTN VTGSARFRKL VKAGDFAAAL DVARDQVANG AQIIDINMDE GLIDSEKAMV EFLNLIAAEP DIARVPIMLD SSKWEVIEAG LKCVQGKAVV NSISLKEGEE AFLHHARLVR AYGAAVVIMA FDETGQADTQ ARKIEICTRA YKILTEQVGF PPEDIIFDPN IFAVATGIEE HNNYGVDFIE ATREIVRTLP HVHISGGVSN LSFSFRGNEP VREAMHAVFL YHAIQAGMDM GIVNAGQLAV YDTIDAELRE ACEDVVLNRP TKTGESATER LLEIAERFRD SGSREARTQD LSWREWPVEK RLEHALVNGI TEYIEADTEE ARLAAERPLH VIEGPLMAGM NVVGDLFGSG KMFLPQVVKS ARVMKQAVAV LLPFMEEEKR LNGGEGRQSA GKVLMATVKG DVHDIGKNIV GVVLACNNYE IIDLGVMVPS QKILQVARDE KVDIIGLSGL ITPSLDEMAH VAAEMEREGF DIPLLIGGAT TSRVHTAVKI HSRYERGQAV YVVDASRAVG VVSNLLSPEG KQAYIDGLRN EYAKVAAAHA RNEAEKQRLP IARARANPHQ LDWENYEPVK PAFTGTKVFE TYDLAEIARY IDWTPFFQTW ELRGRYPAIL EDEKQGEAAR QLWADAQAML RKIIDEKWFT PRAVVGFWPA NAVGDDIRLF TDESRKEELA TLFTLRQQLT KRDGRPNVAM ADFVAPVESG KQDYVGGFVV TAGIGEIAIA ERFERANDDY SAILVKALAD RFAEAFAELM HERVRKEFWA YAPDEAFTPE ELISEPYKGI RPAPGYPAQP DHTEKTTLFR LLDATANTGV ELTESYAMWP GSSVSGLYIG HPESYYFGVA KVERDQVEDY ARRKDMDVEA VERWLTPILN YVPGASKDEA A // ID Q57H39_SALCH Unreviewed; 1256 AA. AC Q57H39; DT 10-MAY-2005, integrated into UniProtKB/TrEMBL. DT 10-MAY-2005, sequence version 1. DT 01-APR-2015, entry version 77. DE SubName: Full=B12-dependent homocysteine-N5-methyltetrahydrofolate transmethylase, repressor of metE and metF {ECO:0000313|EMBL:AAX67973.1}; GN Name=metH {ECO:0000313|EMBL:AAX67973.1}; GN OrderedLocusNames=SCH_4067 {ECO:0000313|EMBL:AAX67973.1}; OS Salmonella choleraesuis (strain SC-B67). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=321314 {ECO:0000313|EMBL:AAX67973.1, ECO:0000313|Proteomes:UP000000538}; RN [1] {ECO:0000313|EMBL:AAX67973.1, ECO:0000313|Proteomes:UP000000538} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SC-B67 {ECO:0000313|EMBL:AAX67973.1, RC ECO:0000313|Proteomes:UP000000538}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AE017220; AAX67973.1; -; Genomic_DNA. DR RefSeq; YP_219054.2; NC_006905.1. DR ProteinModelPortal; Q57H39; -. DR SMR; Q57H39; 680-1256. DR STRING; 321314.SC4067; -. DR EnsemblBacteria; AAX67973; AAX67973; SCH_4067. DR PATRIC; 32329537; VBISalEnt136302_4682. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SENT321314:GJCS-4260-MONOMER; -. DR Proteomes; UP000000538; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000538}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AAX67973.1}; KW Transferase {ECO:0000313|EMBL:AAX67973.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 276 276 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 339 339 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 340 340 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 788 788 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1256 AA; 139099 MW; 8326E52F3468C874 CRC64; MSHVARCSLF RQHALCQYGS LRGALSGASV SSKVEQLRAQ LNERILVLDG GMGTMIQSYR LHEEDFRGER FADWPCDLKG NNDLLVLSKP EVIAAIHNAY FEAGADIIET NTFNSTTIAM ADYRMESLSA EINYAAAKLA RACADEWTVR TPNKPRYVAG VLGPTNRTAS ISPDVNDPAF RNITFDQLVA AYRESTKALV EGGADLILIE TVFDTLNAKA AVFAVKEEFE ALGVDLPIMI SGTITDASGR TLSGQTTEAF YNSLRHAEAL TFGLNCALGP DELRQYVQEL SRIAECYVTA HPNAGLPNAF GEYDLDADTM AKQIREWAEA GFLNIVGGCC GTTPEHIAAM SRAVAGLPPR QLPDIPVACR LSGLEPLNIG DDSLFVNVGE RTNVTGSAKF KRLIKEEKYS EALDVARQQV EGGAQIIDIN MDEGMLDAEA AMVRFLSLIA GEPDIARVPI MIDSSKWEVI EKGLKCIQGK GIVNSISMKE GVEAFIHHAK LLRRYGAAVV VMAFDEQGQA DTRERKIEIC RRAYKILTEE VGFPPEDIIF DPNIFAVATG IEEHNNYAQD FIGACEDIKR ELPHALISGG VSNVSFSFRG NDPVREAIHA VFLYYAIRNG MDMGIVNAGQ LAIYDDLPAE LRDAVEDVIL NRRDDGTERL LELAEKYRGS KTDEAANAQQ AEWRSWDVKK RLEYSLVKGI TEFIEQDTEE ARQQAARPIE VIEGPLMDGM NVVGDLFGEG KVFLPQVVKS ARVMKQAVAY LEPFIEASKE KGSSNGKMVI ATVKGDVHDI GKNIVGVVLQ CNNYEIVDLG VMVPAEKILR TAREVNADLI GLSGLITPSL DEMVNVAKEM ERQGFTIPVL IGGATTSKAH TAVKIEQNYS GPTVYVQNAS RTVGVVAALL SDTQRDDFVA RTRKEYETVR IQHARKKPRT PPVTLEAARD NDLAFDWERY TPPVAHRLGV QEVEASIETL RNYIDWTPFF MTWSLAGKYP RILEDEVVGI EAQRLFKDAN DMLDKLSAEK LLNPRGVVGL FPANRIGDDI EIYRDETRTH VLTVSHHLRQ QTEKVGFANY CLADFVAPKL SGKADYIGAF AVTGGLEEDA LADAFEAQHD DYNKIMVKAI ADRLAEAFAE YLHERVRKVY WGYAPNESLS NDELIRENYQ GIRPAPGYPA CPEHTEKGTI WQLLDVEKHT GMKLTESFAM WPGASVSGWY FSHPESKYFA VAQIQRDQVT DYAFRKGMSV EDVERWLAPN LGYDAD // ID Q59QD2_CANAL Unreviewed; 311 AA. AC Q59QD2; DT 26-APR-2005, integrated into UniProtKB/TrEMBL. DT 26-APR-2005, sequence version 1. DT 01-APR-2015, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EAK92666.1}; GN Name=SAM4 {ECO:0000313|CGD:CAL0004923, ECO:0000313|EMBL:EAK92666.1}; GN ORFNames=CaO19.386 {ECO:0000313|EMBL:EAK92666.1}, GN CaO19.8016 {ECO:0000313|EMBL:EAK92695.1}; OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Debaryomycetaceae; OC Candida/Lodderomyces clade; Candida. OX NCBI_TaxID=237561 {ECO:0000313|EMBL:EAK92666.1, ECO:0000313|Proteomes:UP000000559}; RN [1] {ECO:0000313|EMBL:EAK92666.1, ECO:0000313|Proteomes:UP000000559} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SC5314 {ECO:0000313|EMBL:EAK92666.1}, and RC SC5314 / ATCC MYA-2876 {ECO:0000313|Proteomes:UP000000559}; 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAK92666.1}. 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; AACQ01000177; EAK92666.1; -; Genomic_DNA. DR EMBL; AACQ01000176; EAK92695.1; -; Genomic_DNA. DR RefSeq; XP_711874.1; XM_706781.1. DR RefSeq; XP_711903.1; XM_706810.1. DR STRING; 5476.CAL0004923; -. DR GeneID; 3646467; -. DR GeneID; 3646506; -. DR KEGG; cal:CaO19.386; -. DR KEGG; cal:CaO19.8016; -. DR CGD; CAL0004923; SAM4. DR eggNOG; COG2040; -. DR InParanoid; Q59QD2; -. DR KO; K00547; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000000559; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000559}; KW Reference proteome {ECO:0000313|Proteomes:UP000000559}. SQ SEQUENCE 311 AA; 34383 MW; C3F71818C942B179 CRC64; MGRVQDILDK RKLVIDGALG TELERLLPTT STYLPSGSPL WSGQVLIKNP ELVEQVHLDY INVGADMIIT STYQTSYASL HKYIGYDMDQ AIALWNSALN VAKNAVKKSG RDDVIIAGSI GPYATLLANG SEYNGDYQGV TDEELIEYHT PLFEFYENSD VDIICIETIP SFQELKVIIG LAKKYTSKEF FISINPQTGS ALSDGTSLIE VAQLFAEIND PRFVAVGINC TSYENVDQIS TYLTDFPLFI YPNLGFVYDT TVHKFVSKVL QESTWSKSVA KWLAFPNVKA IGGCCSTTPA EIKQVAQLIN Q // ID Q5B7V2_EMENI Unreviewed; 355 AA. AC Q5B7V2; C8VHP4; DT 26-APR-2005, integrated into UniProtKB/TrEMBL. DT 26-APR-2005, sequence version 1. DT 27-MAY-2015, entry version 58. DE SubName: Full=TPA: Aspergillus nidulans FGSC A4 chromosome VI {ECO:0000313|EMBL:CBF82826.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EAA63346.1}; GN ORFNames=AN3378.2 {ECO:0000313|EMBL:EAA63346.1}, GN ANIA_03378 {ECO:0000313|EMBL:CBF82826.1}; 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 {ECO:0000313|EMBL:EAA63346.1, ECO:0000313|Proteomes:UP000000560}; RN [1] {ECO:0000313|EMBL:EAA63346.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FGSC A4; RA Birren B., Nusbaum C., Abebe A., Abouelleil A., Adekoya E., RA Ait-zahra M., Allen N., Allen T., An P., Anderson M., Anderson S., RA Arachchi H., Armbruster J., Bachantsang P., Baldwin J., Barry A., RA Bayul T., Blitshsteyn B., Bloom T., Blye J., Boguslavskiy L., RA Borowsky M., Boukhgalter B., Brunache A., Butler J., Calixte N., RA Calvo S., Camarata J., Campo K., Chang J., Cheshatsang Y., Citroen M., RA Collymore A., Considine T., Cook A., Cooke P., Corum B., Cuomo C., RA David R., Dawoe T., Degray S., Dodge S., Dooley K., Dorje P., RA Dorjee K., Dorris L., Duffey N., Dupes A., Elkins T., Engels R., RA Erickson J., Farina A., Faro S., Ferreira P., Fischer H., RA Fitzgerald M., Foley K., Gage D., Galagan J., Gearin G., Gnerre S., RA Gnirke A., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., RA Hagopian D., Hagos B., Hall J., Hatcher B., Heller A., Higgins H., RA Honan T., Horn A., Houde N., Hughes L., Hulme W., Husby E., Iliev I., RA Jaffe D., Jones C., Kamal M., Kamat A., Kamvysselis M., Karlsson E., RA Kells C., Kieu A., Kisner P., Kodira C., Kulbokas E., Labutti K., RA Lama D., Landers T., Leger J., Levine S., Lewis D., Lewis T., RA Lindblad-toh K., Liu X., Lokyitsang T., Lokyitsang Y., Lucien O., RA Lui A., Ma L.J., Mabbitt R., Macdonald J., Maclean C., Major J., RA Manning J., Marabella R., Maru K., Matthews C., Mauceli E., RA Mccarthy M., Mcdonough S., Mcghee T., Meldrim J., Meneus L., RA Mesirov J., Mihalev A., Mihova T., Mikkelsen T., Mlenga V., Moru K., RA Mozes J., Mulrain L., Munson G., Naylor J., Newes C., Nguyen C., RA Nguyen N., Nguyen T., Nicol R., Nielsen C., Nizzari M., Norbu C., RA Norbu N., O'donnell P., Okoawo O., O'leary S., Omotosho B., RA O'neill K., Osman S., Parker S., Perrin D., Phunkhang P., Piqani B., RA Purcell S., Rachupka T., Ramasamy U., Rameau R., Ray V., Raymond C., RA Retta R., Richardson S., Rise C., Rodriguez J., Rogers J., Rogov P., RA Rutman M., Schupbach R., Seaman C., Settipalli S., Sharpe T., RA Sheridan J., Sherpa N., Shi J., Smirnov S., Smith C., Sougnez C., RA Spencer B., Stalker J., Stange-thomann N., Stavropoulos S., RA Stetson K., Stone C., Stone S., Stubbs M., Talamas J., Tchuinga P., RA Tenzing P., Tesfaye S., Theodore J., Thoulutsang Y., Topham K., RA Towey S., Tsamla T., Tsomo N., Vallee D., Vassiliev H., RA Venkataraman V., Vinson J., Vo A., Wade C., Wang S., Wangchuk T., RA Wangdi T., Whittaker C., Wilkinson J., Wu Y., Wyman D., Yadav S., RA Yang S., Yang X., Yeager S., Yee E., Young G., Zainoun J., Zembeck L., RA Zimmer A., Zody M., Lander E.; RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EAA63346.1, ECO:0000313|Proteomes:UP000000560} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FGSC A4 {ECO:0000313|EMBL:EAA63346.1}, and RC FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139 RC {ECO:0000313|Proteomes:UP000000560}; 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., Basturkmen M., Spevak C.C., Clutterbuck J., RA Kapitonov V., Jurka J., Scazzocchio C., Farman M., 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., Hynes M., Paoletti M., Fischer R., Miller B., Dyer P., RA 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 [3] {ECO:0000313|Proteomes:UP000000560} RP GENOME REANNOTATION. RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139 RC {ECO:0000313|Proteomes:UP000000560}; 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). RN [4] {ECO:0000313|EMBL:CBF82826.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FGSC A4 {ECO:0000313|EMBL:CBF82826.1}; RA Russo Wortman J., Mabey Gilsenan J., Joardar V., Deegan J., RA Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., RA Coutinho P., von Dohren H., Doonan J., Driessen A.J.M., Durek P., RA Espeso E., Fekete E., Flipphi M., Garcia Estrada C., Geysens S., RA Goldman G., de Groot P.W.J., Hansen K., Harris S.D., Heinekamp T., RA Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., RA Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., RA Keller N., Kelly D.E., Kiel J.A.K.W., Kim J-M., van der Klei I.J., RA Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., RA MacCabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., RA Paszewski A., Paulsen I., Pilsyk S., Posci I., Punt P.J., Ram A.F.J., RA Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., RA Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., RA vanKuyk P.A., Visser H., van der Vondervoot P.J.I., de Vries R.P., RA Walton J., Xiang X., Xiong Y., Ping Zeng A., Brandt B.W., RA Cornell M.J., van den Hondel C.A.M.J.J., Visser J., Oliver S.G., RA Turner G.; RT "The 2008 update of the Aspergillus nidulans genome annotation: A RT community effort."; RL Fungal Genet. Biol. 46:S2-S13(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; BN001306; CBF82826.1; -; Genomic_DNA. DR EMBL; AACD01000055; EAA63346.1; -; Genomic_DNA. DR RefSeq; XP_660982.1; XM_655890.1. DR ProteinModelPortal; Q5B7V2; -. DR STRING; 162425.CADANIAP00009662; -. DR EnsemblFungi; CADANIAT00009662; CADANIAP00009662; CADANIAG00009662. DR GeneID; 2874359; -. DR KEGG; ani:AN3378.2; -. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; YGRSVTK; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000000560; Chromosome VI. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000560}; KW Reference proteome {ECO:0000313|Proteomes:UP000000560}. SQ SEQUENCE 355 AA; 39334 MW; E05C265214647977 CRC64; MKILLLDGGL GTTLESYPFN ITFTSETPLW SSHLLISSPS TLQSAHRAFY DAGADILLTA TYQSSIEGFA RTDASHTIND AGDYMRSAIP LVRGAIPSSA RQRPQQCRVA LSLGPYGATM SPVAAEYTGA YPPEMDGEDA LRQWHAGRLN VFVDDRESWD QVDFVAFETL IRADEVCAVR GAMKDVCVGP EIHRRRKPWW ICGVFPAEEV DRTQVRQWVD AAVGQRPGLP RPWGIGLNCT RIENVAKIVA IMRDELHCLL SRGKEDGFVD EWDAASGKPW LVLYPDGTKG EKYDPVTKTW VARETVVRCP WDESLWDVVQ GQSEGDWEGI IVGGCCRAGP ADIAALRRRI DSSLH // ID Q5FKC1_LACAC Unreviewed; 310 AA. AC Q5FKC1; DT 01-MAR-2005, integrated into UniProtKB/TrEMBL. DT 01-MAR-2005, sequence version 1. DT 27-MAY-2015, entry version 54. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AAV42853.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:AAV42853.1}; GN OrderedLocusNames=LBA1003 {ECO:0000313|EMBL:AAV42853.1}; OS Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=272621 {ECO:0000313|Proteomes:UP000006381}; RN [1] {ECO:0000313|EMBL:AAV42853.1, ECO:0000313|Proteomes:UP000006381} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700396 / NCK56 / N2 / NCFM RC {ECO:0000313|Proteomes:UP000006381}; RX PubMed=15671160; DOI=10.1073/pnas.0409188102; RA Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., RA Buck B.L., McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., RA Lick S., Hamrick A., Cano R., Klaenhammer T.R.; RT "Complete genome sequence of the probiotic lactic acid bacterium RT Lactobacillus acidophilus NCFM."; RL Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000033; AAV42853.1; -; Genomic_DNA. DR RefSeq; WP_003547183.1; NC_006814.3. DR RefSeq; YP_193884.1; NC_006814.3. DR ProteinModelPortal; Q5FKC1; -. DR STRING; 272621.LBA1003; -. DR EnsemblBacteria; AAV42853; AAV42853; LBA1003. DR GeneID; 3252151; -. DR KEGG; lac:LBA1003; -. DR PATRIC; 22197078; VBILacAci7974_0953. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; SSVEGFM; -. DR OrthoDB; EOG6C019S; -. DR Proteomes; UP000006381; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006381}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:AAV42853.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006381}; KW Transferase {ECO:0000313|EMBL:AAV42853.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 223 223 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 288 288 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 310 AA; 35223 MW; 1EF0839B02A96E20 CRC64; MNLVNQARNF GLILDGAMST ALEKQGVNTN NDLWTAVALE NDLDKVYKVH MNYFKSGAQM TITNTYQANV QAFKKHGYSD EHTKKLITDA VQIAKKARDD YQTQTGKHNW VAASVGPYGA YLSDGDEFRG DYSLTPKEYL AFHLPRLKIL LENKPDCLAI ETQPKLDEVI AILDWLKEYA NQIPVYVTFT LHDTTKISDG TPLKKVMQKL NEYEQVFAVG ANCFKPFLAT TAIDRMRMFT QKTIIVYPNL GGVYDEFERN WIPFNADLDF TKLSKEWYKH GAHIIGGCCS TGTKQIQQIA TFFQTIRSTN // ID Q5FP86_GLUOX Unreviewed; 1168 AA. AC Q5FP86; DT 01-MAR-2005, integrated into UniProtKB/TrEMBL. DT 01-MAR-2005, sequence version 1. DT 27-MAY-2015, entry version 76. DE SubName: Full=5-Methyltetrahydrofolate-S-homocysteine methyltransferase {ECO:0000313|EMBL:AAW61810.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AAW61810.1}; GN OrderedLocusNames=GOX2074 {ECO:0000313|EMBL:AAW61810.1}; OS Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Gluconobacter. OX NCBI_TaxID=290633 {ECO:0000313|EMBL:AAW61810.1, ECO:0000313|Proteomes:UP000006375}; RN [1] {ECO:0000313|EMBL:AAW61810.1, ECO:0000313|Proteomes:UP000006375} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=621H {ECO:0000313|EMBL:AAW61810.1, RC ECO:0000313|Proteomes:UP000006375}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000009; AAW61810.1; -; Genomic_DNA. DR RefSeq; WP_011253587.1; NC_006677.1. DR RefSeq; YP_192466.1; NC_006677.1. DR ProteinModelPortal; Q5FP86; -. DR STRING; 290633.GOX2074; -. DR EnsemblBacteria; AAW61810; AAW61810; GOX2074. DR KEGG; gox:GOX2074; -. DR PATRIC; 32612084; VBIGluOxy81109_2378. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; GOXY290633:GHB3-2072-MONOMER; -. DR Proteomes; UP000006375; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006375}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AAW61810.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006375}; KW Transferase {ECO:0000313|EMBL:AAW61810.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 225 225 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 292 292 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 735 735 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1168 AA; 128966 MW; 3FD3C836897D01B1 CRC64; MSSRPHLLDA LADQVLLCDG GMGSRVQMLD LEVERDYWGQ ENCTEILNLS RPELVREIHR GYFEAGADMV ETNTFGGSIV TLAEFGLQDR TREINRTAAT LAREAAETFA DGRHRYVMGS IGPGTKLPTL GNIAYDDLEA GLVEQCRGLI DGGVDGFLIE TCQDTLQIKA AVNAAKIARI ELGSDAPIFV QVTVETTGTL LVGPDIAAAA TTVQALDVPS LGLNCATGPQ EMGEHVRWLS ENWPGLISMQ PNAGLPELVD GKTVYPLSPE EMAVWMERFV KEDGLNLIGG CCGTSTPHIQ ALDGMLRRLG GTKLRPAPVK RSTIWMPSVS SLYTQTPLRQ ENSYFSIGER CNANGSKKWR ELQEANDWDG CVAIGREQAA EGSNALDICT AFVGRDEVRE MNEVVTRFTS SVNAPLVIDS TETPVIEAAL KLHGGKPIIN SINFEDGEQQ AHDRMKLARK FGAAMIALTI DEVGMAKEPQ DKLRIAERLV DFACNQYGLP QSDLMIDPLT FTIATGVEDD RKLGQWTLEG IKLIRDKFPD IQIILGLSNI SFGLNPAARA VLNSVFLDHA VKAGMTGAIV HVSKIRPLHL IAPEEVKVAE DLIFDRRTED YDPLQKLLEL FAGRKAADAV KKRRAETPAE RLKDRIVDGD RKGIEQDLED AMAEMPPLDI INNVLLDGMK VVGELFGSGK MQLPFVLQSA ETMKTAVAWL EPHMERVEGQ HRGTMVLATV KGDVHDIGKN LVDIILTNNG YQVINLGIKV PLADMIAAVK EHKADALGMS GLLVKSTVIM RENLEEMHRQ GFDVPVILGG AALTRNYVEE ECARSYGAGE PGRVAYARDA FDGLGLMDKI ANKELDSYLG AIQTRRASQA SRKTARAPEI AETRGFGVVD REAAKARRER ISGSEPVITP PFWGGRVLEA TPNAVLPFLN ERSLYQFQWG FRKQGRSLDE FMEYAKTELR PVLKRMLALS AEQDIIRPQA IYGYWKAAGD GNDLVLFEED GKTEAARFTM PRQPKDDGEC IADFVRDISD DTRDVVGLQV VTVGQKASDL ARVWFEENRY QDYLYLHGLS VEMAEAMAEY THKRIRAELG FAGEDDRDME KLLSQSYRGS RYSFGYPACP RLEDQEPILK MLDAERIGVS LSDGYQLHPE QSTSALVMLN PRAKYFTV // ID Q5H143_XANOR Unreviewed; 379 AA. AC Q5H143; DT 01-MAR-2005, integrated into UniProtKB/TrEMBL. DT 01-MAR-2005, sequence version 1. DT 27-MAY-2015, entry version 61. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyl transferase {ECO:0000313|EMBL:AAW75328.1}; GN Name=metH {ECO:0000313|EMBL:AAW75328.1}; GN OrderedLocusNames=XOO2074 {ECO:0000313|EMBL:AAW75328.1}; OS Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=291331 {ECO:0000313|EMBL:AAW75328.1, ECO:0000313|Proteomes:UP000006735}; RN [1] {ECO:0000313|EMBL:AAW75328.1, ECO:0000313|Proteomes:UP000006735} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KACC10331 / KXO85 {ECO:0000313|Proteomes:UP000006735}; 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 ----------------------------------------------------------------------- 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; AAW75328.1; -; Genomic_DNA. DR RefSeq; WP_011258785.1; NC_006834.1. DR RefSeq; YP_200713.1; NC_006834.1. DR ProteinModelPortal; Q5H143; -. DR STRING; 291331.XOO2074; -. DR EnsemblBacteria; AAW75328; AAW75328; XOO2074. DR GeneID; 3262102; -. DR KEGG; xoo:XOO2074; -. DR PATRIC; 24103303; VBIXanOry111333_2288. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; XORY291331:GJBV-1929-MONOMER; -. DR Proteomes; UP000006735; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006735}; KW Reference proteome {ECO:0000313|Proteomes:UP000006735}; KW Transferase {ECO:0000313|EMBL:AAW75328.1}. SQ SEQUENCE 379 AA; 40658 MW; 9E1121C000FE040C CRC64; MTHARIPNSE SPIPFALPWL HPERAAKLTA ALAERILIID GAMGTMIQRH DLQEPDYRGT RFADGYDSAH VHGRGCDHAH APESHDLKGN NDLLLLSRPE IIAGIHRAYL DAGADLLETN TFNATSVSQA DYHLEHLVYE LNKAGAQVAR ACCDAVEALT PHKPRFVIGV LGPTSRTASI SPDVNDPGYR NTSFDALRET YREAIKGLID GGADTLMVET IFDTLNAKAA LYAIEEVFEA RGGRLPVMIS GTITDASGRT LSGQTAEAFY ASVAHGRPLS VGLNCALGAK DLRPHVETLS QIADAYVSAH PNAGLPNAFG EYDETPEEMA ETLREFAESG LLNLVGGCCG TSPDHIRAIA EAVADLPPRQ RPGVQELAA // ID Q5H1I7_XANOR Unreviewed; 352 AA. AC Q5H1I7; DT 01-MAR-2005, integrated into UniProtKB/TrEMBL. DT 01-MAR-2005, sequence version 1. DT 07-JAN-2015, entry version 48. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AAW75184.1}; GN Name=mmuM {ECO:0000313|EMBL:AAW75184.1}; GN OrderedLocusNames=XOO1930 {ECO:0000313|EMBL:AAW75184.1}; OS Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=291331 {ECO:0000313|EMBL:AAW75184.1, ECO:0000313|Proteomes:UP000006735}; RN [1] {ECO:0000313|EMBL:AAW75184.1, ECO:0000313|Proteomes:UP000006735} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KACC10331 / KXO85 {ECO:0000313|Proteomes:UP000006735}; 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 ----------------------------------------------------------------------- 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; AAW75184.1; -; Genomic_DNA. DR ProteinModelPortal; Q5H1I7; -. DR STRING; 291331.XOO1930; -. DR EnsemblBacteria; AAW75184; AAW75184; XOO1930. DR PATRIC; 24103008; VBIXanOry111333_2140. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; XORY291331:GJBV-1806-MONOMER; -. DR Proteomes; UP000006735; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006735}; KW Methyltransferase {ECO:0000313|EMBL:AAW75184.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006735}; KW Transferase {ECO:0000313|EMBL:AAW75184.1}. SQ SEQUENCE 352 AA; 37673 MW; 5CB26C7A476B544B CRC64; MVRRSVRCAV LRRLRTYPTA CGPETARMTI AFRQPRADAP FSQLLQHDGC VLLDGALATE LEHRGCDLND ALWSARVLIE QPELIYQVHR DYFAAGAQCA ITASYQATPL GFAARGLDVA QSQALIARSV ELAVQARADH LHAQPQAAPL WVAGSVGPYG AYLADGSEYR GDYVLPIAQL MDFHRPRIAA LADAGVDVLA CETLPSASEI VALRQLLQSE FPQLHAWFSF TLRDAAHLSD GTPLAQVVPA LDACTQVIAV GINCIALDQV TAALHSLSAL TALPLVVYPN SGEHYDASDK RWHAGHASAL TLADQHAHWL AAGARLIGGC CRTTPRDIAA LAAARLADSP GL // ID Q5HS04_STAEQ Unreviewed; 612 AA. AC Q5HS04; DT 15-FEB-2005, integrated into UniProtKB/TrEMBL. DT 15-FEB-2005, sequence version 1. DT 27-MAY-2015, entry version 71. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=SERP0035 {ECO:0000313|EMBL:AAW53411.1}; OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=176279 {ECO:0000313|EMBL:AAW53411.1, ECO:0000313|Proteomes:UP000000531}; RN [1] {ECO:0000313|EMBL:AAW53411.1, ECO:0000313|Proteomes:UP000000531} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35984 / RP62A {ECO:0000313|Proteomes:UP000000531}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; AAW53411.1; -; Genomic_DNA. DR RefSeq; WP_002437221.1; NC_002976.3. DR RefSeq; YP_187635.1; NC_002976.3. DR ProteinModelPortal; Q5HS04; -. DR STRING; 176279.SERP0035; -. DR PRIDE; Q5HS04; -. DR EnsemblBacteria; AAW53411; AAW53411; SERP0035. DR KEGG; ser:SERP0035; -. DR PATRIC; 19610935; VBIStaEpi130894_0034. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; SEPI176279:GJJB-35-MONOMER; -. DR Proteomes; UP000000531; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000531}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:AAW53411.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000000531}; KW Transferase {ECO:0000313|EMBL:AAW53411.1}. SQ SEQUENCE 612 AA; 67910 MW; AC846E33CB8F05F9 CRC64; MSHLLNQLKS NVLVADGAIG TIFYSEGLDT CPESYNLTHP DKVERIHRSY IEAGADVIQT NTYGANFEKL KSFGLEHKVK EIHQAAVQIA KHAANEDTII LGTVGGFRGV RQEDISLSTI QYHTELQIDT LIDEGVDALL FETYYDLDEL TRIVTATRQK YDIPIIAQLT ASNTNYLVDG TEINAALKYV VECGANVVGL NCHHGPHHMQ RSFSHIELPK HAYLSCYPNA SLLDIENSEF KYSDNAQYFG DIAQELINEG VRLIGGCCGT TPEHIRYIKS AVKHLKPVKD KKVIPINKAS SQKQTRVLKQ NLTSKVKNGP TVIVELDTPK HLDTDTFFDN VGKLDEAGID AVTLADNSLA TVRVSNIAAA SLIKQRYDIE PLVHVTCRDR NLIGLQSHLL GLSLIGVNEI LAITGDPSKV GHLPGATNVY DVNSKGLTEL ALRFNKGINT DGDALKKHTN FNIAGAFDPN VRKLDGAIKR LEKKVASGMS YFITQPVYSK EKIIQVYEET KHLNTPFFIG IMPIASYNNA LFLHNEVPGI KMSDDVLNQF KAVKDDKEKT KELSLRLSKE LIDTVHEYFN GLYIITPFQK VDYSLELAAY SKSITANKEA IL // ID Q5KA93_CRYNJ Unreviewed; 381 AA. AC Q5KA93; Q55L90; DT 15-FEB-2005, integrated into UniProtKB/TrEMBL. DT 15-FEB-2005, sequence version 1. DT 29-APR-2015, entry version 65. DE SubName: Full=Homocysteine S-methyltransferase, putative {ECO:0000313|EMBL:AAW46026.1}; GN OrderedLocusNames=CNJ02520 {ECO:0000313|EMBL:AAW46026.1}; 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 {ECO:0000313|EMBL:AAW46026.1, ECO:0000313|Proteomes:UP000002149}; RN [1] {ECO:0000313|EMBL:AAW46026.1, ECO:0000313|Proteomes:UP000002149} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JEC21 / ATCC MYA-565 {ECO:0000313|Proteomes:UP000002149}; 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., Koo H.L., Krzywinski M.I., RA Kwon-Chung J.K., 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; AE017350; AAW46026.1; -; Genomic_DNA. DR RefSeq; XP_567543.1; XM_567543.1. DR ProteinModelPortal; Q5KA93; -. DR STRING; 214684.CNJ02520; -. DR EnsemblFungi; AAW46026; AAW46026; CNJ02520. DR GeneID; 3254105; -. DR KEGG; cne:CNJ02520; -. DR EuPathDB; FungiDB:CNJ02520; -. DR InParanoid; Q5KA93; -. DR KO; K00547; -. DR OMA; EVEWIAF; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000002149; Chromosome 10. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 2. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002149}; KW Methyltransferase {ECO:0000313|EMBL:AAW46026.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002149}; KW Transferase {ECO:0000313|EMBL:AAW46026.1}. SQ SEQUENCE 381 AA; 41541 MW; F0AF5A63A64E5BA3 CRC64; MSSNILVLDG GMGTTLESLG VDISSPLWGS EALRTNPDVI RKVHEGYVQG GADLVETATY QLTPQNLCDH LHCPREEAEC ILCSGVKLVA SCIASCSSRN EEHNTKSKGG NKSKVVLSFG PYGSTLQPGQ EYGGIYPPPF GPSTSTNAFP PDSNDEEEAA IQALAYHHLD KLEAISHDGA AWREVEWIAF ETIPVLHEVR GIRRAMAILR GKLSALYADG DNIDLWWEKK FWITSPFPMG QHPQLLPDGS HASIPQVIHS LFSGPDPIPN GIGINCTNPS YLHFLSSSFT SHLPFEFFGK VEMVIYPDGG QMYDTTTRAW VVAPQSPENA EKWAEVVGDV AKGVRGAERE GKGVWKGVVV GGCCKSSFDE IRALRRFVDS Q // ID Q5L228_GEOKA Unreviewed; 615 AA. AC Q5L228; DT 01-FEB-2005, integrated into UniProtKB/TrEMBL. DT 01-FEB-2005, sequence version 1. DT 01-APR-2015, entry version 69. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=GK0717 {ECO:0000313|EMBL:BAD75002.1}; OS Geobacillus kaustophilus (strain HTA426). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=235909 {ECO:0000313|EMBL:BAD75002.1, ECO:0000313|Proteomes:UP000001172}; RN [1] {ECO:0000313|EMBL:BAD75002.1, ECO:0000313|Proteomes:UP000001172} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HTA426 {ECO:0000313|EMBL:BAD75002.1, RC ECO:0000313|Proteomes:UP000001172}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; BAD75002.1; -; Genomic_DNA. DR RefSeq; WP_011230220.1; NC_006510.1. DR RefSeq; YP_146570.1; NC_006510.1. DR ProteinModelPortal; Q5L228; -. DR STRING; 235909.GK0717; -. DR EnsemblBacteria; BAD75002; BAD75002; GK0717. DR GeneID; 3184095; -. DR KEGG; gka:GK0717; -. DR PATRIC; 21962651; VBIGeoKau81518_0797. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; GKAU235909:GJO7-791-MONOMER; -. DR Proteomes; UP000001172; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001172}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000001172}. SQ SEQUENCE 615 AA; 67414 MW; 5B5474A5AB574FAB CRC64; MGLLDELKER ILIADGAMGT LLYSHGIDRC FEELNLSNPD EIVHIHEAYI AAGADVIQTN TYGANYVKLA RYGLEDEVPA INRAAVRLAR QAANGRAYVL GTIGGLRTLN KSVVTLEEVK RTFREQLFVL LAEGVDGVLL ETYYDLEELE TVLAIARKET DLPIIAHVSL HEVGVLQDGT PLADALARLE ALGADVVGLN CRLGPYHMLR SLEEVPLPKQ AFLSAYPNAS LPDYRDGRLV YETNAEYFEE TAKAFRDQGV RLIGGCCGTT PKHIEAMAKA LADRTPVTEK TVKRRTASVS VQADRPAPTP LPELARTRRS VIVELDPPKK LGIDKFLAGA KALHDAGIDA LTLADNSLAT PRISNAAVAT IIKEQLGIRP LVHITCRDRN LIGLQSHLMG LHTLGITDVL AITGDPSKIG DFPGATSVYD LSSFDLIRLI RQFNEGLSYS GKPLGQKTNF SIGAAFNPNV RHLDKAVERM EKKIQCGAHY FLTQPIYSEE KIVEVHEATK HLDTPIYIGI MPLVSARNAD FLHHEVPGIT LSDEIRARMA ACGNDPVQAA KEGIAIAKSL IDAAFDLFNG IYLITPFLRY DMTVELVRYI HEKEAAAKER KVVHG // ID Q5L229_GEOKA Unreviewed; 1136 AA. AC Q5L229; DT 01-FEB-2005, integrated into UniProtKB/TrEMBL. DT 01-FEB-2005, sequence version 1. DT 27-MAY-2015, entry version 76. DE SubName: Full=5-methyltetrahydrofolate--homocysteine S-methyltransferase {ECO:0000313|EMBL:BAD75001.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:BAD75001.1}; GN OrderedLocusNames=GK0716 {ECO:0000313|EMBL:BAD75001.1}; OS Geobacillus kaustophilus (strain HTA426). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=235909 {ECO:0000313|EMBL:BAD75001.1, ECO:0000313|Proteomes:UP000001172}; RN [1] {ECO:0000313|EMBL:BAD75001.1, ECO:0000313|Proteomes:UP000001172} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HTA426 {ECO:0000313|EMBL:BAD75001.1, RC ECO:0000313|Proteomes:UP000001172}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; BA000043; BAD75001.1; -; Genomic_DNA. DR RefSeq; WP_011230219.1; NC_006510.1. DR RefSeq; YP_146569.1; NC_006510.1. DR ProteinModelPortal; Q5L229; -. DR STRING; 235909.GK0716; -. DR EnsemblBacteria; BAD75001; BAD75001; GK0716. DR GeneID; 3185537; -. DR KEGG; gka:GK0716; -. DR PATRIC; 21962649; VBIGeoKau81518_0796. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; QPFFNAW; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; GKAU235909:GJO7-790-MONOMER; -. DR Proteomes; UP000001172; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001172}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAD75001.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001172}; KW Transferase {ECO:0000313|EMBL:BAD75001.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 724 724 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1136 AA; 125590 MW; 2C2076605280B55F CRC64; MANVTLEQQL QRKILVIDGA MGTMIQSANL SAADFGGEAY EGCNEYLTLT APHVIRRIHE AYLEAGADII ETNTFGATRI VLDEYGLGHL ALELNIEAAK LAKQTAESFS TPDWPRFVAG SMGPTTKTLS VTGGATFEEL VAAYEEQARG LLLGGVDLLL LETCQDTLNV KAGFLGISKA FEAVGRRVPL MISGTIEPMG TTLAGQAIDA FFISVRHMKP IAVGLNCATG PEFMTDHLRT LASLADTAVS CYPNAGLPDE EGHYHETPNM LAEKIRRFAE KGWINIVGGC CGTTPDHIRA IAEAVRDLPP RAIPSSFDVH AVSGIEALIY DETMRPLFVG ERTNVIGSRK FKRLIAEGKY EEAAEIARAQ VKNGAHVIDI CLADPDRDEL HDMEQFVREV VKKVKVPLVI DSTDERVIER ALTYSQGKAI INSINLEDGE ERFAKVVPLL HQYGAAVVVG TIDEQGMAVT AERKLEIALR SYDLLVNRYG VPERDIIFDP LVFPVGTGDE QYIGAAKETI EGIRLIKERL PHCLTMLGIS NVSFGLPPAG REVLNSVFLY HCTQAGLDYA IVNTEKLERF ASIPEEEVRM AEALLFDTND ETLNAFIEFY RSKITAAKPA QTNLSLEERL ARYVIEGSKD GLIPDLEKAL ETYSDPLSII NGPLMAGMDE VGRLFNNNQL IVAEVLQSAE VMKAAVAFLE PYMEKKEGST KGKVILATVK GDVHDIGKNL VDIILSNNGY EVIDLGIKVA PQQLIEAVRE HQPDIIGLSG LLVKSAQQMV VTAQDLRQAG ISTPILVGGA ALTRKFTENK IAPEYDGVVL YAKDAMDGLA LANQIQQGEI DYKKKETAES EPTRQTMVVT AVKSNVSTDV PVYIPADLER HVLRNVPLDH ILPYVNWQMV LGHHLGLKGK VKRLLEEKDE KALALKAVID ELVHEAKERR WIQPAGVYRF FPAQSDGNRV YIYDPTDGKT VLEMFDFPRQ PRAPYLCLAD YLKSKESGEM DYVGLFAVTA GHGVRELAQR WKEEGEFLKS HAIQALALEI AEGFAERVHQ IMRDRWGFPD DPDFTMEERF AAKYQGQRYS FGYPACPNLE DQEKLFRLLH PEDIGIRLTD GYMMEPEASV SAIVFAHPEA RYFNVL // ID Q5LA29_BACFN Unreviewed; 318 AA. AC Q5LA29; DT 21-JUN-2005, integrated into UniProtKB/TrEMBL. DT 21-JUN-2005, sequence version 1. DT 27-MAY-2015, entry version 52. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CAH09045.1}; GN ORFNames=BF9343_3264 {ECO:0000313|EMBL:CAH09045.1}; OS Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / JCM 11019 / NCTC OS 9343). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=272559 {ECO:0000313|EMBL:CAH09045.1, ECO:0000313|Proteomes:UP000006731}; RN [1] {ECO:0000313|EMBL:CAH09045.1, ECO:0000313|Proteomes:UP000006731} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25285 / DSM 2151 / JCM 11019 / NCTC 9343 RC {ECO:0000313|Proteomes:UP000006731}; 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; CAH09045.1; -; Genomic_DNA. DR RefSeq; WP_010993382.1; NC_003228.3. DR RefSeq; YP_212962.1; NC_003228.3. DR ProteinModelPortal; Q5LA29; -. DR STRING; 272559.BF3353; -. DR EnsemblBacteria; CAH09045; CAH09045; BF9343_3264. DR KEGG; bfs:BF9343_3264; -. DR PATRIC; 21043406; VBIBacFra29119_3415. DR eggNOG; COG2040; -. DR HOGENOM; HOG000279054; -. DR OMA; CCGTDHR; -. DR OrthoDB; EOG6R5C46; -. DR BioCyc; BFRA272559:GKF0-3313-MONOMER; -. DR Proteomes; UP000006731; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006731}; KW Reference proteome {ECO:0000313|Proteomes:UP000006731}. SQ SEQUENCE 318 AA; 35982 MW; B0FC7C68102A6799 CRC64; MEQLSFIESF RTSPFILTEG AIVERLRHEF HISPDKHIAH AALIYDDSHR EILASIYRQY LQIATEFRLP LMLMTPTRRA NIEQIAASDY RHKNVLADTM AFLSHFRDEA STPVYIGGLA GCRGNAYDGR YYLSVEEAME FHFPTVRTLA QSGADYLFAG IMPQLTEAIG MANAMAATGL PYIISFMVCR DGRLIDGTFI HDAINAIEKE TSTRPLCYMA NCVHPDVLHQ ALLHPRNDTP LVRQRFQGIQ ANAANLSPEE LDGCDHLISS SPEELADRLM TLLWDFPLKI CGGCCGTNQQ HMHRFAEMLA YRRDNKAW // ID Q5LAY8_BACFN Unreviewed; 916 AA. AC Q5LAY8; DT 21-JUN-2005, integrated into UniProtKB/TrEMBL. DT 21-JUN-2005, sequence version 1. DT 27-MAY-2015, entry version 75. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:CAH08734.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAH08734.1}; GN Name=metH {ECO:0000313|EMBL:CAH08734.1}; GN ORFNames=BF9343_2953 {ECO:0000313|EMBL:CAH08734.1}; OS Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / JCM 11019 / NCTC OS 9343). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=272559 {ECO:0000313|EMBL:CAH08734.1, ECO:0000313|Proteomes:UP000006731}; RN [1] {ECO:0000313|EMBL:CAH08734.1, ECO:0000313|Proteomes:UP000006731} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25285 / DSM 2151 / JCM 11019 / NCTC 9343 RC {ECO:0000313|Proteomes:UP000006731}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CR626927; CAH08734.1; -; Genomic_DNA. DR RefSeq; WP_010993239.1; NC_003228.3. DR RefSeq; YP_212653.1; NC_003228.3. DR ProteinModelPortal; Q5LAY8; -. DR SMR; Q5LAY8; 652-896. DR STRING; 272559.BF3039; -. DR DNASU; 3289244; -. DR EnsemblBacteria; CAH08734; CAH08734; BF9343_2953. DR KEGG; bfs:BF9343_2953; -. DR PATRIC; 21042698; VBIBacFra29119_3069. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; BFRA272559:GKF0-2995-MONOMER; -. DR Proteomes; UP000006731; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006731}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAH08734.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006731}; KW Transferase {ECO:0000313|EMBL:CAH08734.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 916 AA; 100293 MW; 2A4F401F3D578B68 CRC64; MKKTIQQLVL ERILILDGAM GTMIQQYNLR EEDFRNERFA HIPGQLKGNN DLLCLTRPDV IRDIHRKYLE AGADIIETNT FSSTTISMAD YHVQEYVREM NQAAVKLARE VADEYTALNP DKPRFVAGSV GPTNKTCSMS PDVNNPAYRA VTYDEMADAY QQQMEAMLES GVDALLIETI FDTLNAKAAI LAAERAMKAT GVKVPVMLSV TVSDTGGRTL SGQTLEAFLA SVQHADIFSV GLNCSFGARQ LKPFLEQLAA RAPYYISAYP NAGLPNSLGK YDQTPADMAH EVKEYVHEGL INIIGGCCGT TDAYIAEYPA LIAGAKPHIP VCKPDCMWLS GLELLEVKPE INFVNVGERC NVAGSRKFLR LINEKKYDEA LSIARKQVED GALIIDVNMD DGLLDAKEEM TTFLNLVASE PEIARVPVMI DSSKWEVIEA GLKCLQGKSI VNSISLKEGE EKFLEHARTV RQYGAAVVVM AFDEKGQADT ATRKIEVCER AYHLLVDKIG FNPHDIIFDP NVLAVATGIE EHNNYAVDFI EATAWIKKNL PGAHISGGVS NLSFSFRGNN YIREAMHAVF LYHAIQKGMD MGIVNPGTSV LYTDIPADVL ERIEDVVLNR RSDAAERLIE LADRLKEASA GNTSAGQPVK HDAWRDGTVE ERLQYALVKG IGDFLEEDLA EALPKYDKAV DVIEGPLMNG MNHVGELFGA GKMFLPQVVK TARTMKKAVA ILQPIIESEK VEGTASAGKV LLATVKGDVH DIGKNIVSVV MACNGYDIID LGVMVPAESI VQKAIEEKVD MIGLSGLITP SLEEMVHVAM ELEKAGLDIP LLIGGATTSK LHTALKIAPV YHAPVVHLKD ASQNAGVAAR LMSPKSKEEL AKELSGEYEA LRDKSGMMKR ETVSLKEAQE NRLKLF // ID Q5LN14_RUEPO Unreviewed; 298 AA. AC Q5LN14; DT 01-FEB-2005, integrated into UniProtKB/TrEMBL. DT 01-FEB-2005, sequence version 1. DT 27-MAY-2015, entry version 56. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:AAV96625.1}; GN OrderedLocusNames=SPO3398 {ECO:0000313|EMBL:AAV96625.1}; 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 {ECO:0000313|EMBL:AAV96625.1, ECO:0000313|Proteomes:UP000001023}; RN [1] {ECO:0000313|EMBL:AAV96625.1, ECO:0000313|Proteomes:UP000001023} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3 RC {ECO:0000313|Proteomes:UP000001023}; 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; AAV96625.1; -; Genomic_DNA. DR RefSeq; WP_011049081.1; NC_003911.12. DR RefSeq; YP_168594.1; NC_003911.12. DR ProteinModelPortal; Q5LN14; -. DR STRING; 246200.SPO3398; -. DR EnsemblBacteria; AAV96625; AAV96625; SPO3398. DR KEGG; sil:SPO3398; -. DR PATRIC; 23380251; VBIRuePom114501_3462. DR HOGENOM; HOG000265278; -. DR OMA; PYVDVWL; -. DR OrthoDB; EOG6Q5NS7; -. DR Proteomes; UP000001023; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001023}; KW Methyltransferase {ECO:0000313|EMBL:AAV96625.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001023}; KW Transferase {ECO:0000313|EMBL:AAV96625.1}. SQ SEQUENCE 298 AA; 31484 MW; 56F5AFB5BBB567C8 CRC64; MTDITLLDGS IGQELVKRAG KRPTPLWSTS VMLEAPYHVG AVHRDYFDAG ATIATTNTYA VLRDRLEPAG IGDRFEALID TALDQAESAR AAHGSGRIAG ALGPLGASYR PDICPPPEEA EALYADSVRA MNDRVDLFLI ETAASVAQAE GALRGASLGT KPVWLSVTVM DDDGSRLRSG EGVGELAAIV KQYQPQAVLV NCSRPEAVAA ALDIIAGFGL PFGAYANGFT RITEAFLESR PTVEALTARV DLTPEAYADF ALGWVDQSAT IVGGCCEVGP DHIAHLARRL RAAGHRIV // ID Q5LS84_RUEPO Unreviewed; 339 AA. AC Q5LS84; DT 01-FEB-2005, integrated into UniProtKB/TrEMBL. DT 01-FEB-2005, sequence version 1. DT 27-MAY-2015, entry version 58. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:AAV95163.1}; GN OrderedLocusNames=SPO1884 {ECO:0000313|EMBL:AAV95163.1}; 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 {ECO:0000313|EMBL:AAV95163.1, ECO:0000313|Proteomes:UP000001023}; RN [1] {ECO:0000313|EMBL:AAV95163.1, ECO:0000313|Proteomes:UP000001023} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3 RC {ECO:0000313|Proteomes:UP000001023}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; AAV95163.1; -; Genomic_DNA. DR RefSeq; WP_011047617.1; NC_003911.12. DR RefSeq; YP_167121.1; NC_003911.12. DR ProteinModelPortal; Q5LS84; -. DR STRING; 246200.SPO1884; -. DR EnsemblBacteria; AAV95163; AAV95163; SPO1884. DR KEGG; sil:SPO1884; -. DR PATRIC; 23377101; VBIRuePom114501_1912. DR HOGENOM; HOG000265278; -. DR KO; K00548; -. DR OMA; GTNLFAM; -. DR OrthoDB; EOG693GKH; -. DR Proteomes; UP000001023; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001023}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:AAV95163.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001023}; KW Transferase {ECO:0000313|EMBL:AAV95163.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 212 212 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 278 278 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 279 279 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 339 AA; 35518 MW; 7C99C4D189440DCF CRC64; MTNVFAEMLA SHDVLLADGA TGTNLFAMGL QSGDAPELWN TDEPDKIRAL YQGSVQAGSD LFLTNTFGGT AARLKLHEAQ GRVRELNRVG AELGREVADR AGRKVIVAGS VGPTGEIMEP VGSLSHAAAV EMFHEQAEGL KEGGVDVLWL ETISAPEEFR AAAEAFALAG MPWCGTMSFD TAGRTMMGVT SADMAQLVET LPNPPLAFGA NCGTGASDIL RTVLGFVAQG TERAIISKGN AGIPKYVDGH IHYDGTPELM GVYATMARDA GAKIIGGCCG TMPAHLTAMR AALDSTPRGE RPTLEEIVDK IGPFTSASDG TGDDAGPERR ARGGRRRRA // ID Q5M5A7_STRT2 Unreviewed; 322 AA. AC Q5M5A7; DT 01-FEB-2005, integrated into UniProtKB/TrEMBL. DT 01-FEB-2005, sequence version 1. DT 29-APR-2015, entry version 52. DE SubName: Full=Homocysteine S-methyltransferase (S-methylmethionine) {ECO:0000313|EMBL:AAV60290.1}; GN Name=mmuM {ECO:0000313|EMBL:AAV60290.1}; GN OrderedLocusNames=stu0584 {ECO:0000313|EMBL:AAV60290.1}; OS Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=264199 {ECO:0000313|EMBL:AAV60290.1, ECO:0000313|Proteomes:UP000001170}; RN [1] {ECO:0000313|EMBL:AAV60290.1, ECO:0000313|Proteomes:UP000001170} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-250 / LMG 18311 {ECO:0000313|Proteomes:UP000001170}; RX PubMed=15543133; DOI=10.1038/nbt1034; RA Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D., RA Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., RA Fonstein M., Overbeek R., Kyprides N., Purnelle B., Prozzi D., RA Ngui K., Masuy D., Hancy F., Burteau S., Boutry M., Delcour J., RA Goffeau A., Hols P.; RT "Complete sequence and comparative genome analysis of the dairy RT bacterium Streptococcus thermophilus."; RL Nat. Biotechnol. 22:1554-1558(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; CP000023; AAV60290.1; -; Genomic_DNA. DR RefSeq; WP_011225673.1; NC_006448.1. DR RefSeq; YP_139105.1; NC_006448.1. DR ProteinModelPortal; Q5M5A7; -. DR STRING; 264199.stu0584; -. DR EnsemblBacteria; AAV60290; AAV60290; stu0584. DR KEGG; stl:stu0584; -. DR PATRIC; 19802762; VBIStrThe97850_0591. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; STHE264199:GI6K-626-MONOMER; -. DR Proteomes; UP000001170; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001170}; KW Methyltransferase {ECO:0000313|EMBL:AAV60290.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001170}; KW Transferase {ECO:0000313|EMBL:AAV60290.1}. SQ SEQUENCE 322 AA; 35528 MW; EE34A76D5C62A947 CRC64; MVRRSFMATF KDYLENNSPL ILHGALGTEM EALGYDISGK LWSAKYLLEK SEVIQELHET YVAAGADLIT TSSYQATLPG LVEAGLTEKA AEQIIALTVR LAKAARDKVW GALDETEKAK RPYPLISGDV GPYAAYLANG SEYSGDYGQI TIKELKDFHR PRIQILLDQG VDLLALETIP NRLETQALIE LLAEEFPEAE AYMSFTVQIP DAISDGTSLA EMAKLVSQSN QILAVGINCS SPLLYNQALA FLKNAGKALI TYPNSGEVYD GDSQTWKPKD KDALTLVEHS KYWHAHFGVK ILGGCCRTRP NDIKALYQEF RT // ID Q5NLP0_ZYMMO Unreviewed; 351 AA. AC Q5NLP0; DT 01-FEB-2005, integrated into UniProtKB/TrEMBL. DT 01-FEB-2005, sequence version 1. DT 27-MAY-2015, entry version 58. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AAV90370.1}; GN OrderedLocusNames=ZMO1746 {ECO:0000313|EMBL:AAV90370.1}; OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Zymomonas. OX NCBI_TaxID=264203 {ECO:0000313|EMBL:AAV90370.1, ECO:0000313|Proteomes:UP000001173}; RN [1] {ECO:0000313|EMBL:AAV90370.1, ECO:0000313|Proteomes:UP000001173} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 31821 / ZM4 / CP4 {ECO:0000313|Proteomes:UP000001173}; 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., RA Lee J.-S., Jin S.-J., Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., RA Kang H.L., Lee S.Y., 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; AAV90370.1; -; Genomic_DNA. DR RefSeq; WP_011241487.1; NC_006526.2. DR RefSeq; YP_163481.1; NC_006526.2. DR ProteinModelPortal; Q5NLP0; -. DR STRING; 264203.ZMO1746; -. DR EnsemblBacteria; AAV90370; AAV90370; ZMO1746. DR KEGG; zmo:ZMO1746; -. DR PATRIC; 32568758; VBIZymMob102260_1654. DR HOGENOM; HOG000265279; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR Proteomes; UP000001173; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001173}; KW Methyltransferase {ECO:0000313|EMBL:AAV90370.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001173}; KW Transferase {ECO:0000313|EMBL:AAV90370.1}. SQ SEQUENCE 351 AA; 38204 MW; 0A6A0CBADDCF0ED5 CRC64; MKKSIAAERL REEASKRILL TDGAFGTMIQ RYNLDEAAYR GKYELGHDQK GNNDLLVLTR PDVIDAITRA YLDAGSDMVS TNSFNANKIS QSDYNAESLV TDMNRQAAAI ARKAADEYQA KDGRPRFVAG AVGPTNKTLS LSPDVNDPGY RAIDFDHLKE VYAHQVSGLI EGGADFILIE TIFDTLNAKA GIMAVLEESQ RLQREIPMMI SMTITDMSGR NLSGHSIEAF WYAVRHAKPL TIGLNCSFGA DKLRSHVKTL SALADTLLMA YPNAGLPNDL GQYDEMPETT GHFIEEWAQS GMVNIVGGCC GSTPEHIAAM AKAVKGYPPR KSAKMAPAMR LAGLDPMIVP A // ID Q5P448_AROAE Unreviewed; 1254 AA. AC Q5P448; DT 04-JAN-2005, integrated into UniProtKB/TrEMBL. DT 04-JAN-2005, sequence version 1. DT 27-MAY-2015, entry version 82. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CAI07915.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAI07915.1}; GN Name=metH {ECO:0000313|EMBL:CAI07915.1}; GN ORFNames=ebA3184 {ECO:0000313|EMBL:CAI07915.1}; OS Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)). OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Rhodocyclaceae; Aromatoleum. OX NCBI_TaxID=76114 {ECO:0000313|EMBL:CAI07915.1, ECO:0000313|Proteomes:UP000006552}; RN [1] {ECO:0000313|EMBL:CAI07915.1, ECO:0000313|Proteomes:UP000006552} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EbN1 {ECO:0000313|EMBL:CAI07915.1, RC ECO:0000313|Proteomes:UP000006552}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CR555306; CAI07915.1; -; Genomic_DNA. DR RefSeq; WP_011237629.1; NC_006513.1. DR RefSeq; YP_158816.1; NC_006513.1. DR ProteinModelPortal; Q5P448; -. DR SMR; Q5P448; 654-905. DR STRING; 76114.ebA3184; -. DR EnsemblBacteria; CAI07915; CAI07915; ebA3184. DR KEGG; eba:ebA3184; -. DR PATRIC; 20969691; VBIAroAro98752_1796. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; AARO76114:GJTA-1819-MONOMER; -. DR Proteomes; UP000006552; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006552}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAI07915.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006552}; KW Transferase {ECO:0000313|EMBL:CAI07915.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 765 765 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1254 AA; 135181 MW; 2ED7707F8E0E1B6E CRC64; MQADRTEELR TLLAQRILIL DGAMGTMIQQ HKLGEPDYRG ERFRDHPKDL KGNNDLLVLT RPDVVAGIHR AYLDAGADII ETNTFNGTRV SQAEYGLADC AYEINVAGSR LVRELCDEYT AKNPDKPRFC AGVLGPTSRT LSISPDVNDP GFRNVTFDAL VDDYFDSARG LLEGGADLLL IETIFDTLNA KAAVFAVEKL FAELGRRVPV MISGTITDAS GRTLSGQTAE AFWNSLAHAQ PISFGLNCAL GAKELRQYVE ELSTVCDTHV SAHPNAGLPN PLSPTGYDET PEALATAIRE WAEAGLVNIV GGCCGTTPEH IAAIAQVVAN LAPRQGPDIE KKLRLSGLEP FNVGADSLFV NVGERTNVTG SKAFARMILE GRFDDALAVA RQQVENGAQV IDINMDEAML DSQAAMERFC KLIASEPDIS RVPIMLDSSK WSVIEAGLKC IQGKGVVNSI SMKEGEAEFL RQARLCRQYG AAVIVMAFDE KGQADTYERK TGICTRAYEL LTGMGFPPED IIFDPNIFAI ATGIEEHDNY AVDFINAVAW IKANLPFAKT SGGVSNVSFS FRGNDAVREA IHTVFLFHAI RAGLSMGIVN AGQLGVYDDL DPVLRDKVED VVLNRKPGAG EALVELAQSV KEGRAKNAGP DLSWRALSVE ERLSHALVKG ITDFVVADTE EVRAKLEAAG KPPLSVIEGP LMAGMNVVGD LFGAGKMFLP QVVKSARVMK QAVAHLIPYI EAEKLRTGAT SKGRIVVATV KGDVHDIGKN IVGVVLGCNG YEVIDLGVMV PAEKILNAAR EHGAQAVGVS GLITPSLEEM GHVAAEMQRQ GFADGKPMPL LIGGATTSRA HTAIKIAPHY TGPVVYVPDA SRAVGVVTAL LSEGGADEFK AQVVADYDKI RAQHANKKGV QLVSLEAARA NAFRTDWAPV APVAGEEIGE NGGRTAAAAK GYVPPKPTVF GVHAVDVPLA SLVDYIDWGP FFQTWDLSGS FPKILDDEIV GEAARNVFAD GRAMLEDIVA ESWLRARAVF GLFPANSDGD DIAFYGDETR SAALMVWHGL RQQHERPADK PHYCLADFVA PKDSGVADYA GAFAVTAGLG IEQKLAEFHE AHDDYRAIML KSLADRLAEA CAEWLHERVR KEHWGFAADE ALGGEALIRE QYRGIRPAPG YPACPDHTAK RGLFELLDVP RNTGMTLTES CAMSPAASVS GFYFSHPQAR YFAISKIGRD QLEDWAERTG MAVDEAARWL APLL // ID Q5PNQ2_DANRE Unreviewed; 140 AA. AC Q5PNQ2; DT 04-JAN-2005, integrated into UniProtKB/TrEMBL. DT 04-JAN-2005, sequence version 1. DT 01-APR-2015, entry version 44. DE SubName: Full=Novel protein containing a homocysteine S-methyltransferase domain {ECO:0000313|EMBL:CAI21299.1}; DE Flags: Fragment; GN ORFNames=DKEY-98P3.5-002 {ECO:0000313|EMBL:CAI21299.1}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|EMBL:CAI21299.1}; RN [1] {ECO:0000313|EMBL:CAI21299.1} RP NUCLEOTIDE SEQUENCE. RA Donaldson S.; RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX537106; CAI21299.1; -; Genomic_DNA. DR ProteinModelPortal; Q5PNQ2; -. DR PRIDE; Q5PNQ2; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:CAI21299.1}; KW Transferase {ECO:0000313|EMBL:CAI21299.1}. FT NON_TER 1 1 {ECO:0000313|EMBL:CAI21299.1}. SQ SEQUENCE 140 AA; 15563 MW; 9877DB482EE0D222 CRC64; EGFVKYLGVQ PEEAQHMMMS AVQLAKETVS EFISQSPMSD RREPLVAGSV GPYGSFLHDG SEYTGAYEDK MTVEELKDWH RPQIQCLVKA GADLVAMETI PGLKEAEALV KVLKEFPETK AWLSFSCKVT HINAYALPQL // ID Q5PNQ3_DANRE Unreviewed; 318 AA. AC Q5PNQ3; DT 04-JAN-2005, integrated into UniProtKB/TrEMBL. DT 04-JAN-2005, sequence version 1. DT 27-MAY-2015, entry version 45. DE SubName: Full=Novel protein containing a homocysteine S-methyltransferase domain {ECO:0000313|EMBL:CAI21298.1}; DE Flags: Fragment; GN ORFNames=DKEY-98P3.5-001 {ECO:0000313|EMBL:CAI21298.1}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|EMBL:CAI21298.1}; RN [1] {ECO:0000313|EMBL:CAI21298.1} RP NUCLEOTIDE SEQUENCE. RA Donaldson S.; RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX537106; CAI21298.1; -; Genomic_DNA. DR ProteinModelPortal; Q5PNQ3; -. DR STRING; 7955.ENSDARP00000043495; -. DR HOGENOM; HOG000265278; -. DR HOVERGEN; HBG062720; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:CAI21298.1}; KW Transferase {ECO:0000313|EMBL:CAI21298.1}. FT NON_TER 1 1 {ECO:0000313|EMBL:CAI21298.1}. SQ SEQUENCE 318 AA; 35004 MW; DE71F6107D4D79D2 CRC64; PLISAAEMDS SPFILDGGLA TELEASGFQL QGDPLWSARV LHTDPQAIKD VHYRYLQSGS DVITTATYQA SIEGFVKYLG VQPEEAQHMM MSAVQLAKET VSEFISQSPM SDRREPLVAG SVGPYGSFLH DGSEYTGAYE DKMTVEELKD WHRPQIQCLV KAGADLVAME TIPGLKEAEA LVKVLKEFPE TKAWLSFSSI NLFQDNNSIS SGRRFSEAVE MACRSTQLVA VGVNCCPALL VKPLLESAKS HKRADLSWVV YPNSGEGWDV TTGWKTEMRT SFANLSLEWK AQGALWIGGC CRVRPADITE LKQLHVQP // ID Q5SKM5_THET8 Unreviewed; 1185 AA. AC Q5SKM5; DT 21-DEC-2004, integrated into UniProtKB/TrEMBL. DT 21-DEC-2004, sequence version 1. DT 27-MAY-2015, entry version 81. DE SubName: Full=5-methyltetrahydrofolate homocysteine S-methyltransferase {ECO:0000313|EMBL:BAD70441.1}; GN OrderedLocusNames=TTHA0618 {ECO:0000313|EMBL:BAD70441.1}; OS Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579). OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; OC Thermus. OX NCBI_TaxID=300852 {ECO:0000313|EMBL:BAD70441.1, ECO:0000313|Proteomes:UP000000532}; RN [1] {ECO:0000313|EMBL:BAD70441.1, ECO:0000313|Proteomes:UP000000532} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HB8 / ATCC 27634 / DSM 579 {ECO:0000313|Proteomes:UP000000532}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP008226; BAD70441.1; -; Genomic_DNA. DR RefSeq; WP_011228073.1; NC_006461.1. DR RefSeq; YP_143884.1; NC_006461.1. DR ProteinModelPortal; Q5SKM5; -. DR STRING; 300852.TTHA0618; -. DR PRIDE; Q5SKM5; -. DR EnsemblBacteria; BAD70441; BAD70441; BAD70441. DR GeneID; 3168986; -. DR KEGG; ttj:TTHA0618; -. DR PATRIC; 23956215; VBITheThe93045_0616. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR PhylomeDB; Q5SKM5; -. DR BioCyc; TTHE300852:GH8R-645-MONOMER; -. DR Proteomes; UP000000532; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000532}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAD70441.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000532}; KW Transferase {ECO:0000313|EMBL:BAD70441.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 256 256 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1185 AA; 130932 MW; 8429F34743D04D8F CRC64; MVEVHACSPG CRHHLGGAGW GDAPLVRLGY NKEARAKKFP YLKALLERPL VFDGAMGTEL QKRDLTPEDY GGEAYFGCPE VLNRTRPEVV REIHLAYLEA GAEVIETNTF GALRHVLAEY GLEEAAEELA FLGARIAREA ADPHGAFVAG ALGPGTKLVS LGQISWDALY RAYKEAARGL LKGGVDLILL ETAQDILQVR CAVLAVREAM AEVGREVPLQ VQVTFEATGT MLVGTDEQAA LAALESLPVD VVGMNCATGP DLMDSKVRYF AEHSTRFVSC LPNAGLPRNE GGRVVYDLTP EELAKWHLKF VAEYGVNAVG GCCGTGPEHI RKVAEAVKGL APKPRPESFP PQVASLYQAV SLKQEASLFL VGERLNATGS KRFREMLFAR DLEGILALAR EQVEEGAHAL DLSVAWTGRD ELEDLRWLLP HLATALTVPV MVDSTSPEAM ELALKYLPGR VLLNSANLED GLERFDRVAS LAKAHGAALV VLAIDEKGMA KTREEKVRVA LRMYERLTEH HGLRPEDLLF DLLTFPITQG DEESRPLAKE TLLAMEELRE RLPGVGFVLG VSNVSFGLKP RARRVLNSVF LDEARKRGLT AAIVDAGKIL PISQIPEEAY ALALDLIYDR RKEGFDPLLA FMAYFEAHKE DPGKREDAFL ALPLLERLKR RVVEGRKQGL EADLEEALKA GHKPLDLING PLLAGMKEVG DLFGAGKMQL PFVLQAAEVM KRAVAYLEPH MEKKGEGKGT LVLATVKGDV HDIGKNLVDI ILSNNGYRVV NLGIKVPIEE ILKAVEAHKP HAVGMSGLLV KSTLVMKENL EYMRDRGYTL PVILGGAALT RSYVEELRAI YPNVYYAEDA FEGLRLMEEL TGHAPPELTR KAPARPKREA PKVAPRARPV GEAPAVPRPP FFGVRVEEGL DLATIAHYVN KLALYRGQWG YSRKGLSREA WQALVEREAE PVFQRLLKEA MAEGWLEPKV LYGFFPVARE GEELLVFSPE TGEVLERFRF PRQKGGGLSL VDYFRPRFAA PLGDEADWMP KEAFRAGARD VLGVQLVTMG EAPSRKAQAL FASGAYQDYL FVHGFSVEMT EALAEYWHKR MRQMWGIAHQ DATEIQKLFQ QGYQGARYSF GYPACPDLAD QAKLDRLMGF HRVGVRLTEN FQLEPEHATS ALVVHHPEAR YFSVD // ID Q5TTR9_ANOGA Unreviewed; 1123 AA. AC Q5TTR9; DT 07-DEC-2004, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 4. DT 07-JAN-2015, entry version 66. DE SubName: Full=AGAP002469-PA {ECO:0000313|EMBL:EAL40920.4}; GN ORFNames=AgaP_AGAP002469 {ECO:0000313|EMBL:EAL40920.4}; OS Anopheles gambiae (African malaria mosquito). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; OC Culicidae; Anophelinae; Anopheles. OX NCBI_TaxID=7165 {ECO:0000313|Proteomes:UP000007062}; RN [1] {ECO:0000313|EMBL:EAL40920.4, ECO:0000313|Proteomes:UP000007062} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PEST {ECO:0000313|EMBL:EAL40920.4, RC ECO:0000313|Proteomes:UP000007062}; RX PubMed=12364791; DOI=10.1126/science.1076181; RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R., RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M., Wides R., RA Salzberg S.L., Loftus B., Yandell M., Majoros W.H., Rusch D.B., RA Lai Z., Kraft C.L., Abril J.F., Anthouard V., Arensburger P., RA Atkinson P.W., Baden H., de Berardinis V., Baldwin D., Benes V., RA Biedler J., Blass C., Bolanos R., Boscus D., Barnstead M., Cai S., RA Center A., Chaturverdi K., Christophides G.K., Chrystal M.A., RA Clamp M., Cravchik A., Curwen V., Dana A., Delcher A., Dew I., RA Evans C.A., Flanigan M., Grundschober-Freimoser A., Friedli L., Gu Z., RA Guan P., Guigo R., Hillenmeyer M.E., Hladun S.L., Hogan J.R., RA Hong Y.S., Hoover J., Jaillon O., Ke Z., Kodira C., Kokoza E., RA Koutsos A., Letunic I., Levitsky A., Liang Y., Lin J.J., Lobo N.F., RA Lopez J.R., Malek J.A., McIntosh T.C., Meister S., Miller J., RA Mobarry C., Mongin E., Murphy S.D., O'Brochta D.A., Pfannkoch C., RA Qi R., Regier M.A., Remington K., Shao H., Sharakhova M.V., RA Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J., Thomasova D., RA Ton L.Q., Topalis P., Tu Z., Unger M.F., Walenz B., Wang A., Wang J., RA Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M., Yao A., RA Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I., RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., RA Mural R.J., Myers E.W., Adams M.D., Smith H.O., Broder S., RA Gardner M.J., Fraser C.M., Birney E., Bork P., Brey P.T., Venter J.C., RA Weissenbach J., Kafatos F.C., Collins F.H., Hoffman S.L.; RT "The genome sequence of the malaria mosquito Anopheles gambiae."; RL Science 298:129-149(2002). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAL40920.4}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAAB01008859; EAL40920.4; -; Genomic_DNA. DR RefSeq; XP_563710.4; XM_563710.4. DR ProteinModelPortal; Q5TTR9; -. DR STRING; 7165.AGAP002469-PA; -. DR EnsemblMetazoa; AGAP002469-RA; AGAP002469-PA; AGAP002469. DR GeneID; 3290624; -. DR KEGG; aga:AgaP_AGAP002469; -. DR VectorBase; AGAP002469; Anopheles gambiae. DR eggNOG; COG0515; -. DR InParanoid; Q5TTR9; -. DR KO; K08853; -. DR OrthoDB; EOG7PP566; -. DR PhylomeDB; Q5TTR9; -. DR Proteomes; UP000007062; Chromosome 2R. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007062}; KW Reference proteome {ECO:0000313|Proteomes:UP000007062}. SQ SEQUENCE 1123 AA; 120007 MW; D3CC001D8D4882AF CRC64; MKKFISKFET KNEPCSAGGS SSRETNSFVG KTFKLSKENV VTVEEVLAEG GFAVVFLVKG AKGERYALKR LYVNNEYDLG VCNREIKIAS NLSGHKNIIG YIDHSINAKG NGVHEILLLM PYCKTNLLTQ MNARLGTGFT EPEVLQIFCD VAEAVARLHQ CQTPIIHRDL KVENVLQNDL GHYVLCDFGS ATARILNPTS HGRTTVEEEI QRYTTLSYRA PEMIDLFNGQ DITVKADIWA LGCLLYKVCF FTLPFGESTL AIQSGQFSIP DGSKYSRGVH QLIRYMLEPD ADRRPNIYQV CEVAFGIAGR ANPVRNLTKC SVPPLDTLPV PPFESETKRL PTASGGPAGG QHGGSTPKPA KPSAGQLPLE GGTSVAPRQR PKASQVATPG QMGVSSFSLG LPPNPSPKNI ISSPTPGMAP VAGTIGTTAP TDAPEAFVAK FAANFPPASN SSSVPTVAAA SAGSIDPTAP TVAGKDGTAV TALPAQPVAV AALFQTTYPD PFREAELAPI PSGGEMPTAS APNSSSSSLS MVHSPSHAGT QQQHPGPSSA AAQTPTLGGS NSSSSSGVHG AGVGILAPPK PSGHRRNVSD TSAFNKAFAT ETSQFLAPFD QSTNNYQPSS SVSPSVGQTA ASVGASMASG SNSSLHKQQQ QHASSLASSS NPQLFQQQRS TSSAGGSANW NPFGDPTPFS QMTEDHIFGE EFDKIREQGS QGSLKTPPEV PRHSSLPLIQ TAASAAGNMA ALSTVQQAAP FSPENIPDTL GDDEDDPFSS APFSLPVRTD KSKSFKLASR KVIVIDGGFS TQLTEHVGAK LDKDPLWTSR FNATNPAAVL ETHLDYLKAG ADCILTNTYQ ASIEGYMDFL DLNEDESLKL IRASVELARR ARTRYLAEKL ENKSHKIPWV VGSIGPYGAH LHDGSEYTGA YAEHVPANRL QKWHRPRINA IVEAGVDALA IETIPCRMEA EALLDLLSAD HPTVRFWISF QCRDGASLAH GENFAETVLG LWNRARQLAN PNLLAIGVNC VNPQHVLPLL RSVHELLQQR AAGTPPESER IPLIVYPNSG EHWDAAASCW RGAENLTPLE TYLPQWVEMG VKFVGGCCRT NARDIKRIKK AVIGLYGSRS NEN // ID Q5UEY6_9PROT Unreviewed; 309 AA. AC Q5UEY6; DT 07-DEC-2004, integrated into UniProtKB/TrEMBL. DT 07-DEC-2004, sequence version 1. DT 27-MAY-2015, entry version 23. DE SubName: Full=Putative homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:AAV31636.1}; GN ORFNames=Red2C11_51 {ECO:0000313|EMBL:AAV31636.1}; OS uncultured alpha proteobacterium EBAC2C11. OC Bacteria; Proteobacteria; Alphaproteobacteria; SAR116 cluster; OC environmental samples. OX NCBI_TaxID=295349 {ECO:0000313|EMBL:AAV31636.1}; RN [1] {ECO:0000313|EMBL:AAV31636.1} RP NUCLEOTIDE SEQUENCE. RA Sabehi G., Beja O.; RT "SAR116."; RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY744399; AAV31636.1; -; Genomic_DNA. DR ProteinModelPortal; Q5UEY6; -. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:AAV31636.1}; KW Transferase {ECO:0000313|EMBL:AAV31636.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 217 217 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 292 292 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 309 AA; 33708 MW; E13332415250C6DA CRC64; MTYFYAELIK KREQLLPIIL DSGVSTELER RGAKMRNGQW SGCVAIDDYE KLVETHIAYI EAGADIITVN SYASSRLMLG PAGLGDEVER INRLNISAAI EAREKTGANV SVAGSISHAL PFTDGVEGAK QQPDISPEEL SNCYGEMISI FENKGVDLIL LEMMSIPARM APLFNCANKS SLPIWCGLSA KRETPLAALT SWHDTSVSFE DIVIQACQYD FDAIGIMHTS VDAIEAALVV IKNHFSGMLM AYPDSGYFVA PNWQFEDIIE PHALVEYAKG WQKSGCSIFG GCCGLGPEHT TALTELKSV // ID Q5UF27_9PROT Unreviewed; 339 AA. AC Q5UF27; DT 07-DEC-2004, integrated into UniProtKB/TrEMBL. DT 07-DEC-2004, sequence version 1. DT 01-OCT-2014, entry version 34. DE SubName: Full=Predicted methionine synthase I {ECO:0000313|EMBL:AAV31660.1}; GN ORFNames=Red2C11_10 {ECO:0000313|EMBL:AAV31660.1}; OS uncultured alpha proteobacterium EBAC2C11. OC Bacteria; Proteobacteria; Alphaproteobacteria; SAR116 cluster; OC environmental samples. OX NCBI_TaxID=295349 {ECO:0000313|EMBL:AAV31660.1}; RN [1] {ECO:0000313|EMBL:AAV31660.1} RP NUCLEOTIDE SEQUENCE. RA Sabehi G., Beja O.; RT "SAR116."; RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY744399; AAV31660.1; -; Genomic_DNA. DR ProteinModelPortal; Q5UF27; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 339 AA; 35589 MW; 646BFF9728B13901 CRC64; MHNPLSNLIN AKGWCVADGA TGTNLFNRGL ETGYPPELWS VERPDDVLWL HNGFLQAGSD LILTNSFGGT GFRLKLHNAQ DRTQALNIAA AKLARKAVDT HFGATGKKAV VAGSIGPTGE LFEPLGSLTH SSAIAGFSEQ ADALAEGGVD VLWIETMSCN EEVAAAIEAA KATGLPICAT MTFDTASRSM MGVMPADFAE FVRGLGVDFV GANCGIGPAE LLHSVRGILA ASGSLPVVAK GNCGIPAYVD GAIHYHGTPE LMAEYALFAR DAGAKIIGGC CGTSPAHVEA MVAALDKTPL RDFDEVAMVA ALGEAWANVN IEHSGEDDRR KRRSRRRQT // ID Q5WGV1_BACSK Unreviewed; 1148 AA. AC Q5WGV1; DT 23-NOV-2004, integrated into UniProtKB/TrEMBL. DT 23-NOV-2004, sequence version 1. DT 27-MAY-2015, entry version 76. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:BAD64404.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:BAD64404.1}; GN OrderedLocusNames=ABC1869 {ECO:0000313|EMBL:BAD64404.1}; OS Bacillus clausii (strain KSM-K16). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=66692 {ECO:0000313|EMBL:BAD64404.1, ECO:0000313|Proteomes:UP000001168}; RN [1] {ECO:0000313|Proteomes:UP000001168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSM-K16 {ECO:0000313|Proteomes:UP000001168}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP006627; BAD64404.1; -; Genomic_DNA. DR RefSeq; WP_011246712.1; NC_006582.1. DR RefSeq; YP_175365.1; NC_006582.1. DR ProteinModelPortal; Q5WGV1; -. DR STRING; 66692.ABC1869; -. DR EnsemblBacteria; BAD64404; BAD64404; ABC1869. DR KEGG; bcl:ABC1869; -. DR PATRIC; 18923256; VBIBacCla58185_1991. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; QPFFNAW; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; BCLA66692:GHMP-1937-MONOMER; -. DR Proteomes; UP000001168; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001168}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAD64404.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001168}; KW Transferase {ECO:0000313|EMBL:BAD64404.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 724 724 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1148 AA; 126487 MW; 5F169B03ACFEA9A6 CRC64; MTESLFEKQL KQSILVLDGA MGTMLQEANL TAADFGGEAY EGCNEYLNQT APHIVSDIYK KYLEAGADII STNTFGSTSI VLADYDLAHL AYDLSKEAAR LARIEADRAS KPEKPRFVAG AMGPTTKSLS VTGGTTFQEL IEAYEEQARA LIDGGCDVLL LETSQDMRNV KAAYLGISEA FRRTGRTLPL MVSGTIEPMG TTLAGQTVEA FYLSLEHMKP AVVGLNCATG PEFMRDHIRS LAELAETNVS CYPNAGLPDE DGVYHETPDS LVKKLEGFAA KGWLNVVGGC CGTTPAHIKK MVEVIKKYPP RKAKTRQTHA VSGIEPLLYD DSMRPLFVGE RTNVIGSRKF KRLIEEGEYE QASEIARAQV KRGAHVIDIC LADPDRNEQE DMAAFLNYVV NKVKVPLMID STDEAVIERA LTYSQGKAII NSINLEDGEE RFAAVLPLVK KYGAAIVVGT IDETGMAVTA ERKLAVAKRS YKLLTEKYNI PPHDIIFDPL VFPVGTGDEQ YIGSAAATVE GIALIKKELP QCLTILGVSN VSFGLPPVGR EVLNAVFLYH CTQAGLDYAI VNTEKLERYA SIPDEEKQLA DRLLFQTNDA HLAAFTDFYR GKKTEKKVEY ANMSLEERLS AYIVEGTKER LETDLAEALR LYDTPLAIIN GPLMAGMDEV GRLFNANELI VAEVLQSAEV MKAAVAYLEP HMEKSEQEQG KGKILLATVK GDVHDIGKNL VDIILSNNGF SIVNLGIKVT SNELLDAIKK EQPTAIGLSG LLVKSAQQMV LTAQDLRQQH VDIPILVGGA ALTKKFTDTR IAPEYEGLVV YAKDAMNGLE LANRLTTPEG RNELALELAT ARQQKAEFND QRKTKAPTLA KREKSDIAHH HAVFKPTDLD EHIIRDYKID HIYPYVNMQM LLGRHLGIQG KVSRLLAEKD QRTTSLKAQV DAFFQEAKTK KTLQANAIYR FYPANADGDE LVIFDPYDVG RELERFAFPR QTQAPFLCLA DYVRPVGEGV DYVGFLAVTA GAGVREAAEA AKAKGDYLYS HLIQAAALET AEGLAERVHE QMRDRWGFPD GADFTMNERF AAKYQGIRVS FGYPACPNLE DQAKLFQLLR PEKIGIELTD GYMMEPEASV TALVFSHPEA RYFNVGSL // ID Q5WGV2_BACSK Unreviewed; 621 AA. AC Q5WGV2; DT 23-NOV-2004, integrated into UniProtKB/TrEMBL. DT 23-NOV-2004, sequence version 1. DT 27-MAY-2015, entry version 69. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=ABC1868 {ECO:0000313|EMBL:BAD64403.1}; OS Bacillus clausii (strain KSM-K16). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=66692 {ECO:0000313|EMBL:BAD64403.1, ECO:0000313|Proteomes:UP000001168}; RN [1] {ECO:0000313|Proteomes:UP000001168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSM-K16 {ECO:0000313|Proteomes:UP000001168}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; BAD64403.1; -; Genomic_DNA. DR RefSeq; WP_011246711.1; NC_006582.1. DR RefSeq; YP_175364.1; NC_006582.1. DR ProteinModelPortal; Q5WGV2; -. DR STRING; 66692.ABC1868; -. DR EnsemblBacteria; BAD64403; BAD64403; ABC1868. DR KEGG; bcl:ABC1868; -. DR PATRIC; 18923254; VBIBacCla58185_1990. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00297; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; BCLA66692:GHMP-1936-MONOMER; -. DR Proteomes; UP000001168; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001168}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862, KW ECO:0000313|EMBL:BAD64403.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001168}. SQ SEQUENCE 621 AA; 67800 MW; 7B14A777A60E74EF CRC64; MELRDKLKTS LIVGDGAMGT LLYEQGFDLC YEELNLSQPD AVYHVHRSYI EAGAKLLQTN TYAANAVKLK KYGLNESVAD INSAAVGIAK KAIGNNEQLA LVGTIGGIRG FLHEDTENKV ITAALLEQIT ALLEAGVDGL LFETFYDFEE AKEAVALARR LTDKAIIMNV SMGDIGVLNG GIPLGEALEQ LHELGADVLG INCRMGPYHM LRSLEQLELS SAFPLACYPN ASLPGYRDGR FVYASNTDYF YEMTGAFIEQ GVHLIGGCCG TTPAHIAAIA KAVETNTPKT RSLIVRRPSQ LQEEGPGRGE RLNEPLDQLA RRKQTIIVEL DPPKKLMIAK FMEGAKALKE AGVDALTLAD NSLANPRVDN QTLAMLVREQ LGLRSLVHLT CRDRNLIGMQ SHLMGLHLAE LHDLLVITGD PSKIGDFPGA TSVYDVSSLK LLPLIKQMNE GISFSGNSLG SKATFSTAAA FNPHVKHLDK AVRRLEKKIE AGADYFLTQP IFDEQQFEQL YDATKHLPVP IFVGIMPLTS SRNAEFLHNE VPGMTLSDET RARMAACGND KEKAEQEGLQ IAMELADAAS AYFNGLYLVT PFLRYELTAA LATHCRAIAN PINHTMEGER I // ID Q5YUV1_NOCFA Unreviewed; 1198 AA. AC Q5YUV1; DT 23-NOV-2004, integrated into UniProtKB/TrEMBL. DT 23-NOV-2004, sequence version 1. DT 27-MAY-2015, entry version 85. DE SubName: Full=Putative 5-methyltetrahydrofolate:homocysteine S-methyltransferase {ECO:0000313|EMBL:BAD58040.1}; GN Name=metH {ECO:0000313|EMBL:BAD58040.1}; GN OrderedLocusNames=NFA_31930 {ECO:0000313|EMBL:BAD58040.1}; OS Nocardia farcinica (strain IFM 10152). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Nocardiaceae; Nocardia. OX NCBI_TaxID=247156 {ECO:0000313|EMBL:BAD58040.1, ECO:0000313|Proteomes:UP000006820}; RN [1] {ECO:0000313|EMBL:BAD58040.1, ECO:0000313|Proteomes:UP000006820} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IFM 10152 {ECO:0000313|EMBL:BAD58040.1, RC ECO:0000313|Proteomes:UP000006820}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP006618; BAD58040.1; -; Genomic_DNA. DR RefSeq; WP_011209725.1; NC_006361.1. DR RefSeq; YP_119404.1; NC_006361.1. DR ProteinModelPortal; Q5YUV1; -. DR STRING; 247156.nfa31930; -. DR EnsemblBacteria; BAD58040; BAD58040; NFA_31930. DR KEGG; nfa:nfa31930; -. DR PATRIC; 22736004; VBINocFar94200_3238. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; NFAR247156:GJ9T-3242-MONOMER; -. DR Proteomes; UP000006820; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006820}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAD58040.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006820}; KW Transferase {ECO:0000313|EMBL:BAD58040.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 233 233 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 749 749 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1198 AA; 130933 MW; 26D836941F9C3FD5 CRC64; MSVSKSAGFD TTLLDTLRRR VVIGDGAMGT MLQAVDLTLD DFRGLEGCNE ILNETRPDVL RAIHRAYFEA GADAVETNTF GCNLSNLGDY DIADRIRDLS ERGTRLAREV ADEMGPGPDG TPRYVLGSMG PGTKLPTLGH APYTALRDAY VESALGMLDG GADAILIETC QDLLQVKAAV TGSRRAMELA GRRIPIITHV TVETTGTMLV GSEIGAALTA LEPLGIDVIG LNCATGPDEM SEHLRHLSKH ATVPVSVMPN AGLPVLGPNG AEYPLTPEEL AVALRGFVSE FGLALVGGCC GTTPEHIRQV AEAVREVEAT LPPPEQRRSP EPEPAVSSMY TSVPFAQDAS VLMIGERTNA NGSKAFREAM LAEDWQKCLD IAKDQTRDGA HMLDLCVDYV GRDGTRDMTE LASRLATSST LPIMLDSTEP AVLQAGLEHL GGRCAVNSVN YEDGAGPQSR FQQIMRLVAE HGAAVVALTI DEEGQARTAE KKVEIAERLI ADITGNWGLD ESDIIIDTLT FTLGTGQEES RRDGLETIEA IRELKRRHPR VQTTLGLSNI SFGLNPAARQ VLNSVFMHEC VQAGLDSAIV HASKILPMSR IPEEQRTTAL DLIYDRRTPD YDPLQQLMAM FEGVSSSSSK ASRAEELAAL PLFERLERRI VDGEKAGMEA DLDEAMREVP PLRIINETLL SGMKTVGELF GSGQMQLPFV LQSAEVMKAA VAYLEPHMES TDDSGKGRIV LATVKGDVHD IGKNLVDIIL SNNGYEVVNL GIKQPITSIL DAAVDKKADV IGMSGLLVKS TVVMKENLEE LNSRGVADQF PVLLGGAALT RAYVENDLTD VYEGDVHYAR DAFEGLRLMD EIMARKRGEA PDPNSPEAVA EREKAAERKA RHERSKRIAE KRKAAETPVE VPARSDVAAD LPVPVPPFWG TRVVKGLAVH EYSGLLDERA LFLGQWGLRG QRGGDGPSYE ELVESEGRPR LRAWLDRLAT EGVLQHAAVV YGYFPAVSEG DDVIVLTEPE PDAPQRYRFT FPRQQRDRFL CIADFIRSRE LARETGQVDV LPFQLVTMGQ PIADFANELF AADNYRDYLE VHGIGVQLTE ALAEYWHRRI REELVLEGHA VAESDPEDVQ EYFKLGYRGA RYSFGYGACP DLEDRAKLVD LLEADRIGVV LSEELQLHPE QSTDAFVLLH PEAKYFNA // ID Q5ZBZ6_ORYSJ Unreviewed; 328 AA. AC Q5ZBZ6; DT 23-NOV-2004, integrated into UniProtKB/TrEMBL. DT 23-NOV-2004, sequence version 1. DT 01-APR-2015, entry version 74. DE SubName: Full=Os01g0772900 protein {ECO:0000313|EMBL:BAF06310.1}; DE SubName: Full=Putative homocysteine S-methyltransferase 4 {ECO:0000313|EMBL:BAD52936.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EAZ13705.1}; DE SubName: Full=cDNA clone:001-116-A06, full insert sequence {ECO:0000313|EMBL:BAG97045.1}; DE SubName: Full=cDNA clone:J033030E05, full insert sequence {ECO:0000313|EMBL:BAG93417.1}; GN Name=P0490D09.5 {ECO:0000313|EMBL:BAD52936.1}; GN Synonyms=P0695H10.27 {ECO:0000313|EMBL:BAD82075.1}; GN OrderedLocusNames=Os01g0772900 {ECO:0000313|EMBL:BAF06310.1}; GN ORFNames=OsJ_03627 {ECO:0000313|EMBL:EAZ13705.1}; 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 {ECO:0000313|Proteomes:UP000000763}; RN [1] {ECO:0000313|EMBL:BAD52936.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12447438; DOI=10.1038/nature01184; RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y., RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H., RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., RA Okamoto M., Ando T., Aoki H., Arita K., Hamada M., Harada C., RA Hijishita S., Honda M., Ichikawa Y., Idonuma A., Iijima M., Ikeda M., RA Ikeno M., Ito S., Ito T., Ito Y., Ito Y., Iwabuchi A., Kamiya K., RA Karasawa W., Katagiri S., Kikuta A., Kobayashi N., Kono I., RA Machita K., Maehara T., Mizuno H., Mizubayashi T., Mukai Y., RA Nagasaki H., Nakashima M., Nakama Y., Nakamichi Y., Nakamura M., RA Namiki N., Negishi M., Ohta I., Ono N., Saji S., Sakai K., Shibata M., RA Shimokawa T., Shomura A., Song J., Takazaki Y., Terasawa K., Tsuji K., RA Waki K., Yamagata H., Yamane H., Yoshiki S., Yoshihara R., Yukawa K., RA Zhong H., Iwama H., Endo T., Ito H., Hahn J.H., Kim H.-I., Eun M.-Y., RA Yano M., Jiang J., Gojobori T.; RT "The genome sequence and structure of rice chromosome 1."; RL Nature 420:312-316(2002). RN [2] {ECO:0000313|EMBL:BAG93417.1} 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 [3] {ECO:0000313|Proteomes:UP000000763} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000000763}; 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 [4] {ECO:0000313|EMBL:BAF06310.1} RP NUCLEOTIDE SEQUENCE. RG International Rice Genome Sequencing Project; RA Matsumoto T., Wu J., Kanamori H., Katayose Y., Fujisawa M., Namiki N., RA Mizuno H., Yamamoto K., Antonio B.A., Baba T., Sakata K., Nagamura Y., RA Aoki H., Arikawa K., Arita K., Bito T., Chiden Y., Fujitsuka N., RA Fukunaka R., Hamada M., Harada C., Hayashi A., Hijishita S., Honda M., RA Hosokawa S., Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., RA Ito K., Ito S., Ito T., Ito Y., Ito Y., Iwabuchi A., Kamiya K., RA Karasawa W., Kurita K., Katagiri S., Kikuta A., Kobayashi H., RA Kobayashi N., Machita K., Maehara T., Masukawa M., Mizubayashi T., RA Mukai Y., Nagasaki H., Nagata Y., Naito S., Nakashima M., Nakama Y., RA Nakamichi Y., Nakamura M., Meguro A., Negishi M., Ohta I., Ohta T., RA Okamoto M., Ono N., Saji S., Sakaguchi M., Sakai K., Shibata M., RA Shimokawa T., Song J., Takazaki Y., Terasawa K., Tsugane M., Tsuji K., RA Ueda S., Waki K., Yamagata H., Yamamoto M., Yamamoto S., Yamane H., RA Yoshiki S., Yoshihara R., Yukawa K., Zhong H., Yano M., Yuan Q., RA Ouyang S., Liu J., Jones K.M., Gansberger K., Moffat K., Hill J., RA Bera J., Fadrosh D., Jin S., Johri S., Kim M., Overton L., Reardon M., RA Tsitrin T., Vuong H., Weaver B., Ciecko A., Tallon L., Jackson J., RA Pai G., Aken S.V., Utterback T., Reidmuller S., Feldblyum T., RA Hsiao J., Zismann V., Iobst S., de Vazeille A.R., Buell C.R., Ying K., RA Li Y., Lu T., Huang Y., Zhao Q., Feng Q., Zhang L., Zhu J., Weng Q., RA Mu J., Lu Y., Fan D., Liu Y., Guan J., Zhang Y., Yu S., Liu X., RA Zhang Y., Hong G., Han B., Choisne N., Demange N., Orjeda G., RA Samain S., Cattolico L., Pelletier E., Couloux A., Segurens B., RA Wincker P., D'Hont A., Scarpelli C., Weissenbach J., Salanoubat M., RA Quetier F., Yu Y., Kim H.R., Rambo T., Currie J., Collura K., Luo M., RA Yang T., Ammiraju J.S.S., Engler F., Soderlund C., Wing R.A., RA Palmer L.E., de la Bastide M., Spiegel L., Nascimento L., Zutavern T., RA O'Shaughnessy A., Dike S., Dedhia N., Preston R., Balija V., RA McCombie W.R., Chow T., Chen H., Chung M., Chen C., Shaw J., Wu H., RA Hsiao K., Chao Y., Chu M., Cheng C., Hour A., Lee P., Lin S., Lin Y., RA Liou J., Liu S., Hsing Y., Raghuvanshi S., Mohanty A., Bharti A.K., RA Gaur A., Gupta V., Kumar D., Ravi V., Vij S., Kapur A., Khurana P., RA Khurana P., Khurana J.P., Tyagi A.K., Gaikwad K., Singh A., Dalal V., RA Srivastava S., Dixit A., Pal A.K., Ghazi I.A., Yadav M., Pandit A., RA Bhargava A., Sureshbabu K., Batra K., Sharma T.R., Mohapatra T., RA Singh N.K., Messing J., Nelson A.B., Fuks G., Kavchok S., Keizer G., RA Linton E., Llaca V., Song R., Tanyolac B., Young S., Ho-Il K., RA Hahn J.H., Sangsakoo G., Vanavichit A., de Mattos Luiz.A.T., RA Zimmer P.D., Malone G., Dellagostin O., de Oliveira A.C., Bevan M., RA Bancroft I., Minx P., Cordum H., Wilson R., Cheng Z., Jin W., RA Jiang J., Leong S.A., Iwama H., Gojobori T., Itoh T., Niimura Y., RA Fujii Y., Habara T., Sakai H., Sato Y., Wilson G., Kumar K., RA McCouch S., Juretic N., Hoen D., Wright S., Bruskiewich R., Bureau T., RA Miyao A., Hirochika H., Nishikawa T., Kadowaki K., Sugiura M., RA Burr B., Sasaki T.; RT "The map-based sequence of the rice genome."; RL Nature 436:793-800(2005). RN [5] {ECO:0000313|EMBL:EAZ13705.1, ECO:0000313|Proteomes:UP000000763} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000000763}; 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 [6] {ECO:0000313|EMBL:BAF06310.1} RP NUCLEOTIDE SEQUENCE. RG IRGSP(International Rice Genome Sequencing Project); RT "Oryza sativa nipponbare(GA3) genomic DNA, chromosome 1."; RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000313|EMBL:BAF06310.1} RP NUCLEOTIDE SEQUENCE. RG The Rice Annotation Project (RAP); RT "The Second Rice Annotation Project Meeting (RAP2)."; RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases. RN [8] {ECO:0000313|EMBL:BAF06310.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=16381971; DOI=10.1093/nar/gkj094; RA Ohyanagi H., Tanaka T., Sakai H., Shigemoto Y., Yamaguchi K., RA Habara T., Fujii Y., Antonio B.A., Nagamura Y., Imanishi T., Ikeo K., RA Itoh T., Gojobori T., Sasaki T.; RT "The Rice Annotation Project Database (RAP-DB): hub for Oryza sativa RT ssp. japonica genome information."; RL Nucleic Acids Res. 34:D741-D744(2006). RN [9] {ECO:0000313|EMBL:BAF06310.1} RP NUCLEOTIDE SEQUENCE. RG The Rice Annotation Project (RAP); RA Itoh T., Tanaka T., Barrero R.A., Yamasaki C., Fujii Y., Hilton P.B., RA Antonio B.A., Aono H., Apweiler R., Bruskiewich R., Bureau T., RA Burr F., Costa de Oliveira A., Fuks G., Habara T., Haberer G., Han B., RA Harada E., Hiraki A.T., Hirochika H., Hoen D., Hokari H., Hosokawa S., RA Hsing Y., Ikawa H., Ikeo K., Imanishi T., Ito Y., Jaiswal P., RA Kanno M., Kawahara Y., Kawamura T., Kawashima H., Khurana J.P., RA Kikuchi S., Komatsu S., Koyanagi K.O., Kubooka H., Lieberherr D., RA Lin Y.C., Lonsdale D., Matsumoto T., Matsuya A., McCombie W.R., RA Messing J., Miyao A., Mulder N., Nagamura Y., Nam J., Namiki N., RA Numa H., Nurimoto S., O'donovan C., Ohyanagi H., Okido T., Oota S., RA Osato N., Palmer L.E., Quetier F., Raghuvanshi S., Saichi N., RA Sakai H., Sakai Y., Sakata K., Sakurai T., Sato F., Sato Y., RA Schoof H., Seki M., Shibata M., Shimizu Y., Shinozaki K., Shinso Y., RA Singh N.K., Smith-White B., Takeda J., Tanino M., Tatusova T., RA Thongjuea S., Todokoro F., Tsugane M., Tyagi A.K., Vanavichit A., RA Wang A., Wing R.A., Yamaguchi K., Yamamoto M., Yamamoto N., Yu Y., RA Zhang H., Zhao Q., Higo K., Burr B., Gojobori T., Sasaki T.; RT "Curated Genome Annotation of Oryza sativa ssp. japonica and RT Comparative Genome Analysis with Arabidopsis thaliana."; RL Genome Res. 17:175-183(2007). RN [10] {ECO:0000313|EMBL:BAF06310.1} RP NUCLEOTIDE SEQUENCE. RG The Rice Annotation Project (RAP); RA Tanaka T., Antonio B.A., Kikuchi S., Matsumoto T., Nagamura Y., RA Numa H., Sakai H., Wu J., Itoh T., Sasaki T., Aono R., Fujii Y., RA Habara T., Harada E., Kanno M., Kawahara Y., Kawashima H., Kubooka H., RA Matsuya A., Nakaoka H., Saichi N., Sanbonmatsu R., Sato Y., Shinso Y., RA Suzuki M., Takeda J., Tanino M., Todokoro F., Yamaguchi K., RA Yamamoto N., Yamasaki C., Imanishi T., Okido T., Tada M., Ikeo K., RA Tateno Y., Gojobori T., Lin Y.C., Wei F.J., Hsing Y.I., Zhao Q., RA Han B., Kramer M.R., McCombie R.W., Lonsdale D., O'Donovan C.C., RA Whitfield E.J., Apweiler R., Koyanagi K.O., Khurana J.P., RA Raghuvanshi S., Singh N.K., Tyagi A.K., Haberer G., Fujisawa M., RA Hosokawa S., Ito Y., Ikawa H., Shibata M., Yamamoto M., RA Bruskiewich R.M., Hoen D.R., Bureau TE., Namiki N., Ohyanagi H., RA Sakai Y., Nobushima S., Sakata K., Barrero R.A., Sato Y., Souvorov A., RA Smith-White B., Tatusova T., An S., An G., OOta S., Fuks G., RA Messing J., Christie K.R., Lieberherr D., Kim H., Zuccolo A., RA Wing R.A., Nobuta K., Green P.J., Lu C., Meyers BC., Chaparro C., RA Piegu B., Panaud O., Echeverria M.; RT "The Rice Annotation Project Database (RAP-DB): 2008 update."; RL Nucleic Acids Res. 36:D1028-D1033(2008). RN [11] {ECO:0000313|Proteomes:UP000000763} RP GENOME REANNOTATION. RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000000763}; 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 [12] {ECO:0000313|EMBL:EAZ13705.1} 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 (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; AP003265; BAD52936.1; -; Genomic_DNA. DR EMBL; AP003295; BAD82075.1; -; Genomic_DNA. DR EMBL; AP008207; BAF06310.1; -; Genomic_DNA. DR EMBL; AK073362; BAG93417.1; -; mRNA. DR EMBL; AK104962; BAG97045.1; -; mRNA. DR EMBL; CM000138; EAZ13705.1; -; Genomic_DNA. DR RefSeq; NP_001044396.1; NM_001050931.1. DR UniGene; Os.32439; -. DR ProteinModelPortal; Q5ZBZ6; -. DR STRING; 39947.LOC_Os01g56610.1; -. DR EnsemblPlants; OS01T0772900-01; OS01T0772900-01; OS01G0772900. DR EnsemblPlants; OS01T0772900-02; OS01T0772900-02; OS01G0772900. DR GeneID; 4324713; -. DR KEGG; osa:4324713; -. DR Gramene; Q5ZBZ6; -. DR eggNOG; COG2040; -. DR InParanoid; Q5ZBZ6; -. DR KO; K00547; -. DR OMA; SYIGKWR; -. DR Proteomes; UP000000763; Chromosome 1. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 2. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Complete proteome {ECO:0000313|Proteomes:UP000000763}; KW Methyltransferase {ECO:0000313|EMBL:BAD52936.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000763}; KW Transferase {ECO:0000313|EMBL:BAD52936.1}. SQ SEQUENCE 328 AA; 34554 MW; 35E87556DA984EA1 CRC64; MGRGGDVDGA AGALRRFVRE AGGCAVVDGG LATELEAHGA DLHDELWSAS CLVSAPHLIR KVHLDYLDAG ANIITSASYQ ATIQGFQARG LSRERSEALL RRSVHIAQEA RAIFAEGWSK GPYANHRSSP RRPVLVAASI GSYGAYLADG SEYTGDYGIS VTKETLKSFH RRRLQVLADA GPDLIAFETI PNKLEAQASG DPITECAAVA DACARVGAVG VNCTAPRLVH GLILSIRKVT SKPVVVYPNS GETYVAETKE WVESEGGASE TDFVSCVGKW RQAGAALVGG CCRTSPATVR AISWALRESD DAVGGDGDRD DFPAVAVL // ID Q5ZIC7_CHICK Unreviewed; 1253 AA. AC Q5ZIC7; DT 23-NOV-2004, integrated into UniProtKB/TrEMBL. DT 23-NOV-2004, sequence version 1. DT 27-MAY-2015, entry version 75. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CAG32516.1}; GN ORFNames=RCJMB04_27p10 {ECO:0000313|EMBL:CAG32516.1}; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; OC Phasianidae; Phasianinae; Gallus. OX NCBI_TaxID=9031 {ECO:0000313|EMBL:CAG32516.1}; RN [1] {ECO:0000313|EMBL:CAG32516.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CB {ECO:0000313|EMBL:CAG32516.1}; RC TISSUE=Bursa {ECO:0000313|EMBL:CAG32516.1}; RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6; RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., RA Fiedler P., Kutter S., Blagodatski A., Kostovska D., Koter M., RA Plachy J., Carninci P., Hayashizaki Y., Buerstedde J.M.; RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene RT function analysis."; RL Genome Biol. 6:R6.1-R6.9(2005). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AJ720857; CAG32516.1; -; mRNA. DR RefSeq; NP_001026275.1; NM_001031104.1. DR UniGene; Gga.21288; -. DR ProteinModelPortal; Q5ZIC7; -. DR SMR; Q5ZIC7; 661-917, 923-1252. DR STRING; 9031.ENSGALP00000017592; -. DR PaxDb; Q5ZIC7; -. DR GeneID; 422069; -. DR CTD; 4548; -. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR HOVERGEN; HBG006347; -. DR PhylomeDB; Q5ZIC7; -. DR NextBio; 20824755; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 2: Evidence at transcript level; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 258 258 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 782 782 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1253 AA; 139431 MW; 31AFDFE803E15BC9 CRC64; MARVGADPPA DTQESVEDEI ESVLRERIMI LDGGMGTMIQ QHALSEEDFR GHEFKDHSKP LKGNNDLLSI TQPDIICDIH KEYLLAGADI IETNTFSSTR VAQADYGLEH LAYRLNRISA EVARKAADDV TAQTGIKRYV AGSMGPTNRT LSVSPSVERP DYRNITFDEL VEAYTEQAKG LLDGGVDVML VETIFDTANA KAALFALHKL FEEEYAPRPI FVSGTIVDKS GRTLSGQTGE AFVISVSHSK PLCIGLNCAL GAVEMRPFIE TIGKCTTAYV ICYPNAGLPN TFGGYDETPE VTAKHIKNFA LDGLVNIVGG CCGTTPAHIR KIAEAVKLCK PRVPPPLCQG YMLLSGLEPF RIGPYTNFVN IGERCNVAGS RKFAKLIMAG NYEEALTVAK SQVEMGAQIL DINMDDGMLD GPSAMTRFCN LISSEPDIAK VPLCIDSSNF SVIEAGLKCC QGKCIVNSIS LKEGEEDFLE KARKIKLYGA AVVVMAFDEV GQATETETKI AVCSRAYHLL VEKVHFNPND IIFDPNILTI GTGMEEHNLY AINFINATKT IKETLPGVRI SGGLSNLSFS FRGMDAIREA MHGVFLYHAI RYGMDMGIVN AGNLPVYDDI HKELLQLCEN LIWNKDPDAT EKLLRYAQNH AQGGKKVIQT DEWRNSSVEE RLEYALVKGI EKYVTADTEE ARLNQEKYPR PLNIIEGPLM NGMKIVGDLF GAGKMFLPQV IKSARVMKKA VGHLIPYMEK EREERRAKQG SSEEEDPYNG TIVLATVKGD VHDIGKNIVG VVLGCNNFRV IDLGVMTPCD KILRAAVENK ADIIGLSGLI TPSLDEMIFV AKEMERLAIK IPLLIGGATT SKTHTAVKIA PRYSAPVIHV LDASKSVVVC SQLLDESVKD DFFEEILEEY EEIRQEHYES LKERRYLSLQ QARRKGFHND WLSDHKPVKP KFIGTKVFED YDLKRLVEYI DWKPFFDVWQ LRGKYPNRGF PKVFNDKTVG EEAQKVYNDA QNLLKILINQ KKLQARGVQD DIYLYAVEEA VGSSEPIAKF CGLRQQAEKD SACTDPYYCL SDFIAPLDSG VCDYLGLFAV ACFGVDELCN ELRRQDDEYN IIMVKALGDR LAEAFAEELH ERVRREFWAY CSDEQLDLSE LRKIKYEGIR PAPGYPSQPD HTEKLTMWKL ANIEETTGIG LTESLAMTPA SAVSGLYFSS PKSKYFAVGK ICKDQVEDYA LRKKLSVAEV EKWLGPILGY DTE // ID Q608E7_METCA Unreviewed; 1237 AA. AC Q608E7; DT 23-NOV-2004, integrated into UniProtKB/TrEMBL. DT 23-NOV-2004, sequence version 1. DT 27-MAY-2015, entry version 77. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AAU92201.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AAU92201.1}; GN Name=metH {ECO:0000313|EMBL:AAU92201.1}; GN OrderedLocusNames=MCA1545 {ECO:0000313|EMBL:AAU92201.1}; OS Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath). OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales; OC Methylococcaceae; Methylococcus. OX NCBI_TaxID=243233 {ECO:0000313|EMBL:AAU92201.1, ECO:0000313|Proteomes:UP000006821}; RN [1] {ECO:0000313|EMBL:AAU92201.1, ECO:0000313|Proteomes:UP000006821} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33009 / NCIMB 11132 / Bath RC {ECO:0000313|Proteomes:UP000006821}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AE017282; AAU92201.1; -; Genomic_DNA. DR RefSeq; WP_010960817.1; NC_002977.6. DR RefSeq; YP_114000.1; NC_002977.6. DR ProteinModelPortal; Q608E7; -. DR SMR; Q608E7; 660-1237. DR STRING; 243233.MCA1545; -. DR EnsemblBacteria; AAU92201; AAU92201; MCA1545. DR KEGG; mca:MCA1545; -. DR PATRIC; 22606932; VBIMetCap22254_1578. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR Proteomes; UP000006821; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000006821}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AAU92201.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006821}; KW Transferase {ECO:0000313|EMBL:AAU92201.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 253 253 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 316 316 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 317 317 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 767 767 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1237 AA; 136702 MW; D93C49E8FD1D16A0 CRC64; MNLPVTAMER SSLLKRLLKE RILFLDGAMG TMIQRYKLAE ADYRGQRFAD WPRDLKGNND LLSLTRPDVI EAIHWAYLEA GADIVETNSF NATRISMADY GMEPLVYEIN VASARLARQV ADRMSRQTPD RPRFVAGVLG PTSRTASISP SVNDPGFRNI GFDELVASYD EAVRGLVDGG ADIILIETIF DTLNAKAAVF AVERFFEQEG YTLPVMISGT ITDASGRTLS GQTTEAFWNS LRHARPISIG LNCALGAKQL RQHVEELSRI ADTYVSAHPN AGLPNEFGEY DESPEAMARE IADWAEQGFL NIIGGCCGTT PAHIEAIHDA VQHFPPRRIP EIPPACRLAG LEPCNITAGS LFVNVGERTN VTGSAAFRRM IREAKYDEAL EVARQQVESG AQIIDVNMDE GMLDSRAAMV QFLNLIAAEP DIARVPVMID SSKWEILEAG LKCLQGKGIV NSISLKEGEA AFLHHARLVR RYGAAVIVMA FDEQGQADTR ERKVEICERA YRLLTEKAGF PAEDIIFDPN IFAVATGIEE HDRYGLDFIE AVAEIKSRLP HALVSGGVSN VSFSFRGNDA VREAIHAVFL YHAIRAGMDM GIVNAGQLAI YEEVPEELRD AVEDVILARR EDATERLLAI ADRYRGEEGA GSERKADMAW RSLPVDKRLE HALVKGIDEF IEVDTEEARR QFERPLHVIE GPLMAGMNVV GDLFGAGKMF LPQVVKSARV MKKAVAYLMP YMDAEKAGTE VGTNGKILMA TVKGDVHDIG KNIVGVVLQC NGFEVIDLGV MVPCDKILQT AREENVDIIG LSGLITPSLD EMVHVAREME RLGFEIPLMI GGATTSRAHT AVKIEPNYHG PTVYVTDASR SVGVAGSLLS ADLKDEFTAR LRKEYEEVRR HHAGRRIQGT LLSLQQARAR AFHTDWAHYV PPAPHLLGLE VFDAYPLEEI AGYIDWSPFF HTWELAGSYP RILDDEVVGE HARTLLQDAR AMLALLTEQR WLTARGVIGF FPANSEGDDV VLWTDESRTE RLAVLHHLRQ QQDKPGGQPA YCLADFVAPV GSGVADYLGG FAVTVGHGIE APLERFARVH DDYSGIMLKA LADRLAEAFA ERMHQRVRRE FWGYAPEESL DNEALIAEAY RGIRPAPGYP ACPDHTEKAT LFRLLDAEAN SGISLTESFA MYPASSVSGW YFSHASAKYF NVGKIGRDQV EDYARRKGMT VREVERWLAS SLGYDAD // ID Q634T1_BACCZ Unreviewed; 610 AA. AC Q634T1; DT 25-OCT-2004, integrated into UniProtKB/TrEMBL. DT 25-OCT-2004, sequence version 1. DT 27-MAY-2015, entry version 74. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN Name=metE {ECO:0000313|EMBL:AAU16261.1}; GN OrderedLocusNames=BCE33L4006 {ECO:0000313|EMBL:AAU16261.1}; OS Bacillus cereus (strain ZK / E33L). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=288681 {ECO:0000313|EMBL:AAU16261.1, ECO:0000313|Proteomes:UP000002612}; RN [1] {ECO:0000313|Proteomes:UP000002612} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ZK / E33L {ECO:0000313|Proteomes:UP000002612}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; AAU16261.1; -; Genomic_DNA. DR RefSeq; WP_000770331.1; NC_006274.1. DR RefSeq; YP_085586.1; NC_006274.1. DR ProteinModelPortal; Q634T1; -. DR STRING; 288681.BCZK4006; -. DR EnsemblBacteria; AAU16261; AAU16261; BCE33L4006. DR KEGG; bcz:BCZK4006; -. DR PATRIC; 18891808; VBIBacCer95304_4242. DR eggNOG; COG0685; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; BCER288681:GHG7-4067-MONOMER; -. DR Proteomes; UP000002612; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002612}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:AAU16261.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:AAU16261.1}. SQ SEQUENCE 610 AA; 67298 MW; 3F0A2353CD3128EB CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNISDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTE INRAAVKLAK ASVTDRNAIL GTIGGMKHIG AVTTTDMERE FMLLEQASAL LEEQVDGLLL ETFYDEFELL HAVQVLRKET NIPIVAQLAL HEAGTTQNGN DVNEILKQLL DYGANVVGLN CQLGPLHMTE AFKMISIPKN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPKFIEQGI RLLGGCCGTT PEHIESMKRA TLNVTPVIEK DTIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRISNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIA LIEEVYEATK HLEQPIFIGI MPLISKRNAD FLHFEVPGIT LPEAVRERMD GHETKEAAIE EGIRISQELI DETMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID Q634T2_BACCZ Unreviewed; 1133 AA. AC Q634T2; DT 25-OCT-2004, integrated into UniProtKB/TrEMBL. DT 25-OCT-2004, sequence version 1. DT 29-APR-2015, entry version 87. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AAU16263.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AAU16263.1}; GN Name=metH {ECO:0000313|EMBL:AAU16263.1}; GN OrderedLocusNames=BCE33L4005 {ECO:0000313|EMBL:AAU16263.1}; OS Bacillus cereus (strain ZK / E33L). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=288681 {ECO:0000313|EMBL:AAU16263.1, ECO:0000313|Proteomes:UP000002612}; RN [1] {ECO:0000313|Proteomes:UP000002612} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ZK / E33L {ECO:0000313|Proteomes:UP000002612}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CP000001; AAU16263.1; -; Genomic_DNA. DR RefSeq; WP_011198983.1; NC_006274.1. DR RefSeq; YP_085585.1; NC_006274.1. DR ProteinModelPortal; Q634T2; -. DR STRING; 288681.BCZK4005; -. DR EnsemblBacteria; AAU16263; AAU16263; BCE33L4005. DR KEGG; bcz:BCZK4005; -. DR PATRIC; 18891806; VBIBacCer95304_4241. DR eggNOG; COG1410; -. DR KO; K00548; -. DR OMA; QPFFNAW; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; BCER288681:GHG7-4066-MONOMER; -. DR Proteomes; UP000002612; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002612}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AAU16263.1}; KW Transferase {ECO:0000313|EMBL:AAU16263.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 223 223 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 287 287 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 719 719 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1133 AA; 126117 MW; 08F39817A83B7D51 CRC64; MMKCIEEKLQ NNILLLDGAM GTMIQQEDLT AEDFGGEEYE GCNEYLVETR PDVILKIHKA YIEAGADIIE TNTFGATNIV LSDYELSHLD EELNEKAARL AKQAVKESGK EVYVAGAMGP TTKAISVTGG VTFEELIEAY TRQARGLLKG EVDVLLVETS QDMRNVKAAY IGIQAAFDEL KKVVPIMISG TIEPMGTTLA GQTIEAFYLS VEHMKPLSVG LNCATGPEFM RDHIRSLSDL SECYISCYPN AGLPDEDGHY HESPSSLAEK VKRFAEEGWV NIIGGCCGTT PEHIKAMKEA LASLKPREHH EREGHGVSGL EALQYDDSMR PLFVGERTNV IGSRKFKRLV AEGKFEEAAE VARAQVKKNA HIIDICMADP DRDEIEDMEN FLAEVTKVLK VPIMIDSTDE HVMERALTYI QGKAVINSIN LEDGEERFIK VTPLLQKYGA AIVVGTIDED GMAVSAERKL EIAKRSYELL TTKYGIRPSD IIFDALVFPV GTGDEEYIGS AAATIEGIRL IKEALPECLT ILGVSNISFG LPPAGREVLN SVFLYHATKA GLDYAIVNTE KLERYASIPD EEKRLADALL FETTQETLEE FTNFYRVAKK KDVVVQETLT LDERLANYIV EGTKQGLHED LSLALTEGRK PLDIINGPLM TGMDEVGRLF NNNELIVAEV LQSAESMKAA VSYLEPHMES SDSAKKGKVL LATVKGDVHD IGKNLVEIIL ANNGYEIINL GINVRSDRIV QEVQEKKPDI IGLSGLLVKS AQQMVTTAED LKAADIDIPI VVGGAALTRK FTDNRISPSY KGLVCYASDA MTGLDIINKL QKEEEREKMK QDKKERHLHI VTKEEKKIEI PAVIEPLPKS EVMVPDSTKR IVLRDVPALH LAPFLNRQML LGHHLGLKGS VKKLLKEGDK RAHELNDLID ELLQEGQSWL KPKAVYQFFP AQSDGQNIVI YDPEDHTRVI ERFTFPRQGR APYRTLGDYL RPIGDEMDYV AFLSVTVGEG VRDIAEEWKA KGDYLRSHAI QSLALELAEG LAEKTHMLIR DRWGIPDSPE LTMEERFRTK YRGIRVSFGY PACPELADQE KLFRLIHPEE IGISLTEGFM MEPEASVTAM VFSHPEARYF SVL // ID Q63Y03_BURPS Unreviewed; 359 AA. AC Q63Y03; DT 25-OCT-2004, integrated into UniProtKB/TrEMBL. DT 25-OCT-2004, sequence version 1. DT 27-MAY-2015, entry version 59. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:CAH34374.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAH34374.1}; GN Name=metH2 {ECO:0000313|EMBL:CAH34374.1}; GN OrderedLocusNames=BPSL0386 {ECO:0000313|EMBL:CAH34374.1}; OS Burkholderia pseudomallei (strain K96243). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=272560 {ECO:0000313|EMBL:CAH34374.1, ECO:0000313|Proteomes:UP000000605}; RN [1] {ECO:0000313|EMBL:CAH34374.1, ECO:0000313|Proteomes:UP000000605} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K96243 {ECO:0000313|EMBL:CAH34374.1, RC ECO:0000313|Proteomes:UP000000605}; 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., 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., Crosset 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; CAH34374.1; -; Genomic_DNA. DR RefSeq; WP_004204527.1; NC_006350.1. DR RefSeq; YP_107012.1; NC_006350.1. DR ProteinModelPortal; Q63Y03; -. DR STRING; 272560.BPSL0386; -. DR EnsemblBacteria; CAH34374; CAH34374; BPSL0386. DR GeneID; 3093220; -. DR KEGG; bps:BPSL0386; -. DR PATRIC; 19260407; VBIBurPse99623_0435. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; BPSE272560:GJNI-393-MONOMER; -. DR Proteomes; UP000000605; Chromosome 1. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000605}; KW Methyltransferase {ECO:0000313|EMBL:CAH34374.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000605}; KW Transferase {ECO:0000313|EMBL:CAH34374.1}. SQ SEQUENCE 359 AA; 38459 MW; 1013B7D60E53B797 CRC64; MSEPTPIAPF ASSAAPAAPY TRGAALPQLL RQRILILDGA MGTMIQRYKL DEAAYRGERF KDFPRDVKGN NELLSITQPR IIREIHDQYF AAGADIVETN TFGATAVAQA DYGMEALVVE MNVASAALAR ESAAKYATPE KPRFVAGAIG PTPKTASISP DVNDPGARNV TFDELRDAYY QQAKALLDGG VDLFLVETIF DTLNAKAALF ALDQLFDDTG ERLPIMISGT VTDASGRILS GQTVEAFWNS LRHAKPLTFG LNCALGAALM RPYIAELAKL CDTYVSCYPN AGLPNPMSDT GFDETPDVTS GLLKEFAQAG LVNLAGGCCG TTPEHIAAIA KALAEVKPRR WPSQYSEAA // ID Q64QE1_BACFR Unreviewed; 318 AA. AC Q64QE1; DT 25-OCT-2004, integrated into UniProtKB/TrEMBL. DT 25-OCT-2004, sequence version 1. DT 27-MAY-2015, entry version 48. DE SubName: Full=Putative homocysteine S-methyltransferase {ECO:0000313|EMBL:BAD50290.1}; GN OrderedLocusNames=BF3547 {ECO:0000313|EMBL:BAD50290.1}; OS Bacteroides fragilis (strain YCH46). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=295405 {ECO:0000313|EMBL:BAD50290.1, ECO:0000313|Proteomes:UP000002197}; RN [1] {ECO:0000313|EMBL:BAD50290.1, ECO:0000313|Proteomes:UP000002197} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YCH46 {ECO:0000313|EMBL:BAD50290.1, RC ECO:0000313|Proteomes:UP000002197}; 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; BAD50290.1; -; Genomic_DNA. DR RefSeq; WP_005790322.1; NC_006347.1. DR RefSeq; YP_100824.1; NC_006347.1. DR ProteinModelPortal; Q64QE1; -. DR STRING; 295405.BF3547; -. DR EnsemblBacteria; BAD50290; BAD50290; BF3547. DR GeneID; 3084629; -. DR KEGG; bfr:BF3547; -. DR PATRIC; 21052654; VBIBacFra17906_3407. DR OMA; CCGTDHR; -. DR OrthoDB; EOG6R5C46; -. DR Proteomes; UP000002197; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002197}; KW Methyltransferase {ECO:0000313|EMBL:BAD50290.1}; KW Transferase {ECO:0000313|EMBL:BAD50290.1}. SQ SEQUENCE 318 AA; 36016 MW; 08196E3D987D0044 CRC64; MEQLSFIESF RTSPFILTEG AIVERLRHEF HISPDKHIAH AALIYDDSHR EILASIYRQY LQIATEFRLP LMLMTPTRRA NIEQIAASDY RHKNVLADTM AFLSRFRDEA STPVYIGGLA GCRGNAYDGR YYLSVEEAME FHFPTVRTLA QSGADYLFAG IMPQLTEAIG MANAMAATGL PYIISFMICR DGRLIDGTFI HDAIDAIEKE TSTRPLCYMA NCVHPDVLHQ ALLHPRNDTP LVRQRFQGIQ ANAANLSPEE LDGCDHLISS SPEELADRLM TLLWDFPLKI CGGCCGTNQQ HMHRFAEMLA YRRDNKAW // ID Q64RD7_BACFR Unreviewed; 916 AA. AC Q64RD7; DT 25-OCT-2004, integrated into UniProtKB/TrEMBL. DT 25-OCT-2004, sequence version 1. DT 29-APR-2015, entry version 73. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|EMBL:BAD49944.1}; GN OrderedLocusNames=BF3199 {ECO:0000313|EMBL:BAD49944.1}; OS Bacteroides fragilis (strain YCH46). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=295405 {ECO:0000313|EMBL:BAD49944.1, ECO:0000313|Proteomes:UP000002197}; RN [1] {ECO:0000313|EMBL:BAD49944.1, ECO:0000313|Proteomes:UP000002197} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YCH46 {ECO:0000313|EMBL:BAD49944.1, RC ECO:0000313|Proteomes:UP000002197}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AP006841; BAD49944.1; -; Genomic_DNA. DR RefSeq; WP_011203181.1; NC_006347.1. DR RefSeq; YP_100478.1; NC_006347.1. DR ProteinModelPortal; Q64RD7; -. DR SMR; Q64RD7; 652-896. DR STRING; 295405.BF3199; -. DR EnsemblBacteria; BAD49944; BAD49944; BF3199. DR GeneID; 3083101; -. DR KEGG; bfr:BF3199; -. DR PATRIC; 21051954; VBIBacFra17906_3066. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR Proteomes; UP000002197; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002197}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAD49944.1}; KW Transferase {ECO:0000313|EMBL:BAD49944.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 916 AA; 100337 MW; 24447389D3A61596 CRC64; MKKTIQQLVL ERILILDGAM GTMIQQYNLR EEDFRNERFA HIPGQLKGNN DLLCLTRPDV IRDIHRKYLE AGADIIETNT FSSTTISMAD YHVQEYVREM NQAAVKLARE VADEYTVLNP DKPRFVAGSV GPTNKTCSMS PDVNNPAYRA VTYDEMADAY QQQMEAMLES GVDALLIETI FDTLNAKAAI LAAERAMKAT GVKVPVMLSV TVSDTGGRTL SGQTLEAFLA SVQHADIFSV GLNCSFGARQ LKPFLEQLAA RAPYYISAYP NAGLPNSLGK YDQTPADMAH EVKEYVHEGL INIIGGCCGT TDAYIAEYPA LIAGAKPHIP VCKPDCMWLS GLELLEVKPE INFVNVGERC NVAGSRKFLR LINEKKYDEA LSIARKQVED GALIIDVNMD DGLLDAKEEM TTFLNLVASE PEIARVPVMI DSSKWEVIEA GLKCLQGKSI VNSISLKEGE EKFLEHARTV RQYGAAVVVM AFDEKGQADT ATRKIEVCER AYHLLVDKIG FNPHDIIFDP NVLAVATGIE EHNNYAVDFI EATAWIKKNL PGSHISGGVS NLSFSFRGNN YIREAMHAVF LYHAIQKGMD MGIVNPGTSV LYTDIPADVL ERIEDVVLNR RSDAAERLIE LADRLKEASA GNTSAGQPVK HDAWRDGTVE ERLQYALVKG IGDFLEEDLA EALPKYDKAV DVIEGPLMNG MNHVGELFGA GKMFLPQVVK TARTMKKAVA ILQPIIESEK VEGTASAGKV LLATVKGDVH DIGKNIVSVV MACNGYDIID LGVMVPAESI VQKAIEEKVD MIGLSGLITP SLEEMVHVAM ELEKAGLDIP LLIGGATTSK LHTALKIAPV YHAPVVHLKD ASQNAGVAAR LMSPKSKEEL AKELSGEYEA LRDKSGMMKR ETVSLKEAQE NRLKLF // ID Q65LG3_BACLD Unreviewed; 609 AA. AC Q65LG3; Q62WV4; DT 25-OCT-2004, integrated into UniProtKB/TrEMBL. DT 25-OCT-2004, sequence version 1. DT 27-MAY-2015, entry version 85. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AAU22754.1}; GN Name=yitJ {ECO:0000313|EMBL:AAU22754.1}; GN OrderedLocusNames=BL01307 {ECO:0000313|EMBL:AAU22754.1}; OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / NBRC OS 12200 / NCIMB 9375 / NRRL NRS-1264 / Gibson 46). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=279010 {ECO:0000313|EMBL:AAU22754.1, ECO:0000313|Proteomes:UP000000606}; RN [1] {ECO:0000313|EMBL:AAU22754.1, ECO:0000313|Proteomes:UP000000606} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / NBRC 12200 / NCIMB 9375 / NRRL RC NRS-1264 / Gibson 46 {ECO:0000313|Proteomes:UP000000606}; 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 ----------------------------------------------------------------------- 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; AAU22754.1; -; Genomic_DNA. DR RefSeq; WP_009328867.1; NC_006322.1. DR RefSeq; YP_006712574.1; NC_006322.1. DR RefSeq; YP_078392.1; NC_006270.3. DR ProteinModelPortal; Q65LG3; -. DR STRING; 279010.BL01307; -. DR EnsemblBacteria; AAU22754; AAU22754; BL01307. DR EnsemblBacteria; AAU40101; AAU40101; BLi01193. DR GeneID; 3030177; -. DR KEGG; bld:BLi01193; -. DR KEGG; bli:BL01307; -. DR PATRIC; 18947951; VBIBacLic203714_1180. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; BLIC279010:GJ2P-1184-MONOMER; -. DR Proteomes; UP000000606; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000606}; KW Methyltransferase {ECO:0000313|EMBL:AAU22754.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000606}; KW Transferase {ECO:0000313|EMBL:AAU22754.1}. SQ SEQUENCE 609 AA; 67588 MW; 34BFFE92FC99C151 CRC64; MGFLEDIKNK TLIADGAMGT LLYSYGIDRC FEELNISKPE EIRRVHEAYV QAGADIIQTN TYGANFIKLS RYGLEDETKQ INEKAVRLAR AAAGSAYVLG TLGGIRTFNK NSYSLEDIKR SFREQLYLLL NEQPDGLLLE TYYDLEEARE VLKIARKETE LPIILNVSMH EEGVLQDGTP LADGLKQLAS LGADVVGINC RLGPYHMIRA LEEVPLLEDA YLSVYPNSSL PSLVEGRLVY ETDDEYFRES AEEFRNQGAR IIGGCCGTTP NHIRAMAEAV KGLPPVTEKR VKIRKKAALA VQNERTEPAL DDLAKQKRSI IVELDPPKQL NFEKFLHAAE ELKSAGIDAL TLADNSLATP RISNVACGAL LKQRLDMRSL IHITCRDRNL IGLQSHLMGL DTLGLSDVLA ITGDPSKIGD FPGATSVYDL TSFDLISLIK QFNEGLSYSG KPLGKKTNFS VAAAFNPNVR HIDKAVKRLE KKIACGADYF ISQPVYSEEQ LIKIHKETRH LETPIYIGVM PLTSSRNAEF IHNEIPGIKL SDSIREKMAL AGNDKQKQAE EGLAIARSLL DAACDLFNGI YLITPFLRSD LTAELTAYIH QKEKEKTNV // ID Q65LG4_BACLD Unreviewed; 1138 AA. AC Q65LG4; Q62WV5; DT 25-OCT-2004, integrated into UniProtKB/TrEMBL. DT 25-OCT-2004, sequence version 1. DT 27-MAY-2015, entry version 92. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase MetH {ECO:0000313|EMBL:AAU22753.1}; GN Name=metH {ECO:0000313|EMBL:AAU22753.1}; GN OrderedLocusNames=BL01308 {ECO:0000313|EMBL:AAU22753.1}; OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / NBRC OS 12200 / NCIMB 9375 / NRRL NRS-1264 / Gibson 46). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=279010 {ECO:0000313|EMBL:AAU22753.1, ECO:0000313|Proteomes:UP000000606}; RN [1] {ECO:0000313|EMBL:AAU22753.1, ECO:0000313|Proteomes:UP000000606} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / NBRC 12200 / NCIMB 9375 / NRRL RC NRS-1264 / Gibson 46 {ECO:0000313|Proteomes:UP000000606}; 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 ----------------------------------------------------------------------- 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; AAU22753.1; -; Genomic_DNA. DR RefSeq; WP_011197752.1; NC_006322.1. DR RefSeq; YP_006712573.1; NC_006322.1. DR RefSeq; YP_078391.1; NC_006270.3. DR ProteinModelPortal; Q65LG4; -. DR STRING; 279010.BL01308; -. DR EnsemblBacteria; AAU22753; AAU22753; BL01308. DR EnsemblBacteria; AAU40100; AAU40100; BLi01192. DR GeneID; 3030176; -. DR KEGG; bld:BLi01192; -. DR KEGG; bli:BL01308; -. DR PATRIC; 18947949; VBIBacLic203714_1179. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; ILESWIT; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; BLIC279010:GJ2P-1183-MONOMER; -. DR Proteomes; UP000000606; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000606}; KW Methyltransferase {ECO:0000313|EMBL:AAU22753.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000606}; KW Transferase {ECO:0000313|EMBL:AAU22753.1}. SQ SEQUENCE 1138 AA; 125242 MW; 03B4648FB1D63B53 CRC64; MSNINDQLKK KILVLDGAMG TMIQDAGLSA ADFGGEAYEG CNEFLSITAP HVIQGIHEAY LEAKADIIET NTFGATRLVL DEYDLGHRAY EVNLASVKLA KAAAEKFSTP EWPRFVAGAM GPTTKTLSVT GGTTFDELID NYEEQARALI TGGADLLLLE TSQDMLNVKA GFIGIRQAFE KTGKTLPLMV SGTIEPMGTT LAGQDIESFY ISLEHMKPVS VGLNCATGPE FMTDHIRTLS SLARTAVSCY PNAGLPDEEG QYHESPQSLA KKIKAFAEEG WLNIVGGCCG TTPAHIEALA DEVALLPPRT VPSGAKPHTV SGIDGLIYEE TMRPLFVGER TNVIGSRKFK RLIAEHKFEE ASEIARAQVK NGAHVIDICL ADPDRDEAED MEGFLKKAMK KVKAPFVIDS TDKTVIEKAL KYSQGKAIIN SINLEDGEER FADILPLVKQ FGGALVVGTI DEEGMAVTAA KKLAVAVRSH QLLTEKYGIP ASDIIFDPLV FPVGTGDEQY IGSAKETIEG IRLIKEQLPE CLTILGVSNV SFGLPPVGRE ILNAVFLYHA TQAGLDYAIV NTEKLERFAS IPKEEVEMAE KLLFHTDDKT LASFTDFYRG KKKADKQPKT SLSLEERLAE YVIEGTKEGL IPDLEQALKK FATPLDVVNG PLMDGMAEVG RLFNNNELIV AEVLQSAEVM KAAVSFLEQY MEKKDDSGKG KIILATVKGD VHDIGKNLVD IILSNNGYKV VDLGIKVTPQ ELIEAIRKEN PDIIGLSGLL VKSAQQMVVT AKDLDKADIS IPIMVGGAAL SRKFTNMKIS PEYKGPVLYA KDAMDGLSLA NQLRTDPSQF LEKKEAAAPA AVAEKKQTKA VIEMLEKRAH VPKAPVFQPE DLKRHYLKNI DLSYIVPYVN EQMLLGHHLG LKGKVKKLLA EQHPKALELK ELIDELLRDG KEHGWFDPAV VYQFFPAYSD GDSLHILDPV NKDSILETFV FPRQEKLPYR CISDYVRPKG ELDYVSFFAV TAGRHVRAAA NRFKEEGDYL KSHAVQALAL ELAEGLAERT HQVIRDRWGF PDAPDFTMEQ RFQAKYQGQR YSFGYPACPN LEDQEKLFRL IQPEGIGVHL TDGFMMEPEA SVSAIVVSHP EARYFNVH // ID Q65NY8_BACLD Unreviewed; 315 AA. AC Q65NY8; Q62ZD5; DT 25-OCT-2004, integrated into UniProtKB/TrEMBL. DT 25-OCT-2004, sequence version 1. DT 27-MAY-2015, entry version 75. DE SubName: Full=Homocysteine S-methyltransferase YbgG {ECO:0000313|EMBL:AAU21873.1}; GN Name=ybgG {ECO:0000313|EMBL:AAU21873.1}; GN OrderedLocusNames=BL01781 {ECO:0000313|EMBL:AAU21873.1}; OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / NBRC OS 12200 / NCIMB 9375 / NRRL NRS-1264 / Gibson 46). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=279010 {ECO:0000313|EMBL:AAU21873.1, ECO:0000313|Proteomes:UP000000606}; RN [1] {ECO:0000313|EMBL:AAU21873.1, ECO:0000313|Proteomes:UP000000606} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / NBRC 12200 / NCIMB 9375 / NRRL RC NRS-1264 / Gibson 46 {ECO:0000313|Proteomes:UP000000606}; 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 ----------------------------------------------------------------------- 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; AAU21873.1; -; Genomic_DNA. DR RefSeq; WP_011197504.1; NC_006322.1. DR RefSeq; YP_006711701.1; NC_006322.1. DR RefSeq; YP_077511.1; NC_006270.3. DR ProteinModelPortal; Q65NY8; -. DR STRING; 279010.BL01781; -. DR EnsemblBacteria; AAU21873; AAU21873; BL01781. DR EnsemblBacteria; AAU39226; AAU39226; BLi00266. DR GeneID; 3027910; -. DR KEGG; bld:BLi00266; -. DR KEGG; bli:BL01781; -. DR PATRIC; 18946013; VBIBacLic203714_0245. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; BLIC279010:GJ2P-260-MONOMER; -. DR Proteomes; UP000000606; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000606}; KW Methyltransferase {ECO:0000313|EMBL:AAU21873.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000606}; KW Transferase {ECO:0000313|EMBL:AAU21873.1}. SQ SEQUENCE 315 AA; 34557 MW; 8B674FBE34E33CCA CRC64; MTNPIRTSLQ QFSVIILDGA MATELERYGC DLNDSLWSAK ILIENPELIK QVHLDYFRAG ADCAITASYQ STVEGFTKRG LSEQEALHLI RESVRLAAEA RDEFWAAPEN REGRPKPFVA ASVGPYGAFL ADGSEYQGNY GVTEDELADF HRRRMGALIE AGADILACET IPCLSEAKAI VHLLKEFPDT HAWISFSAKD GRHISDGTKA GECAKWLDQH DQVAAVGVNC TRLEHVSSLI GGIKKHTAKP IIVYPNSGEQ YDPETKTWHG AACKASFGES ARSWYNQGAQ LIGGCCRTTP EDIKAVAAWA RKLEV // ID Q65TU4_MANSM Unreviewed; 1227 AA. AC Q65TU4; DT 25-OCT-2004, integrated into UniProtKB/TrEMBL. DT 25-OCT-2004, sequence version 1. DT 01-APR-2015, entry version 81. DE SubName: Full=MetH protein {ECO:0000313|EMBL:AAU37616.1}; GN Name=metH {ECO:0000313|EMBL:AAU37616.1}; GN OrderedLocusNames=MS1009 {ECO:0000313|EMBL:AAU37616.1}; OS Mannheimia succiniciproducens (strain MBEL55E). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Basfia. OX NCBI_TaxID=221988 {ECO:0000313|EMBL:AAU37616.1, ECO:0000313|Proteomes:UP000000607}; RN [1] {ECO:0000313|EMBL:AAU37616.1, ECO:0000313|Proteomes:UP000000607} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MBEL55E {ECO:0000313|EMBL:AAU37616.1, RC ECO:0000313|Proteomes:UP000000607}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AE016827; AAU37616.1; -; Genomic_DNA. DR RefSeq; WP_011200186.1; NC_006300.1. DR RefSeq; YP_088201.1; NC_006300.1. DR ProteinModelPortal; Q65TU4; -. DR SMR; Q65TU4; 649-888. DR STRING; 221988.MS1009; -. DR EnsemblBacteria; AAU37616; AAU37616; MS1009. DR KEGG; msu:MS1009; -. DR PATRIC; 22445383; VBIManSuc86752_0923. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; QPFFNAW; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; BMAN221988:GHGM-1045-MONOMER; -. DR Proteomes; UP000000607; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000607}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000607}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 756 756 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135942 MW; 757BE5893ED044CC CRC64; MHNKIDILKA SLAQRILILD GAMGTMIQQY KLSEQQFRGE RFKQSSVDLR GNNDLLSLTQ PLLIQAIHEK YLQAGADIIE TNTFSSTSIA QADYDLQAIA YELNFAGAKL ARIAADKYSS ADKPRFVAGV LGPTNRTASI SPDVNDPGFR NITFMQLAEA YGEATRGLIA GGADIIMLET IFDTLNAKAA VFAIEQVFEE LGVRLPVMIS GTITDASGRT LSGQTTEAFY NSLRHAKPLS FGLNCALGPK ELRQYVEQLS KISECYVSAH PNAGLPNAFG GYDLGAEEMA AQLKEWAESG FLNIVGGCCG TTPEHIKAFA EAMQGVKPRP LPQIKTAMRL SGLEPLSIDD DSLFVNVGER NNVTGSAKFK RLIKEEKFGE AIEIAIDQVE NGAQVIDVNM DEALLDSQKC MTRFLNIMAT EPDAAKVPVM IDSSKWEVIE AGLQSIQGKG IVNSISLKEG EEKFIRQAKL IRRYGAAAVV MAFDEKGQAD TEARKVEICT RAYDILVNQA GFPPEDIIFD PNIFAIGTGI EEHNNYGVDF INATGRIKQT LPYAKVSGGV SNVSFSFRGN NPMREAIHAV FLYHAIKQGM DMGIVNAGQL AIYDDLDPEL REVVEDAVLN RRPDATDRLL EIAEKYRNQD STGEDNGVAE WRSWSVEERL KHALVKGITH FIIEDTEEAR QKFSLPLEVI EGPLMAGMDV VGDLFGDGKM FLPQVVKSAR VMKQSVAYLE PFINATKQKG SSNGKVVIAT VKGDVHDIGK NIVSVVLQCN NFEVIDLGVM VPADKIIETA IAEKADIIGL SGLITPSLDE MEYFLGEMNR LNLNIPVLIG GATTSKEHTA IKLYPKYKYE VIYTTNASRA VTVCAALMNP ESKAELWART RKEYEKIQQS FAERKPLRSS LSLEQARANG FNPFAGEWAN YQVPQPKQPG ISEFKDVPIA MLRKFIDWSP FFRVWGLMGG YPDAFDYPEG GEEARKVWHD AQIMLDEFEN NGKLTPSGVL GIFPAERAGD DIKIYQNSDR TLLAGVARHL RQQSERGKNS KIPYNLCLSD FIAEGSNGQQ DWLGMFAVCA GTQEHALVDS FKAKGDDYNA ILLQAVGDRL AEAMAEYLHF ELRTRLWGYS DETFDNQALI DEKYIGIRPA PGYPSCPEHT EKQLIWDLLE VEQRIGMKLT ESYAMWPAAS VCGWYFSHPA SSYFTLGRID EDQAADYAKR KGWDEREMRK WLGVSMK // ID Q65V50_MANSM Unreviewed; 298 AA. AC Q65V50; DT 25-OCT-2004, integrated into UniProtKB/TrEMBL. DT 25-OCT-2004, sequence version 1. DT 01-APR-2015, entry version 52. DE SubName: Full=MHT1 protein {ECO:0000313|EMBL:AAU37160.1}; GN Name=mHT1 {ECO:0000313|EMBL:AAU37160.1}; GN OrderedLocusNames=MS0553 {ECO:0000313|EMBL:AAU37160.1}; OS Mannheimia succiniciproducens (strain MBEL55E). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Basfia. OX NCBI_TaxID=221988 {ECO:0000313|EMBL:AAU37160.1, ECO:0000313|Proteomes:UP000000607}; RN [1] {ECO:0000313|EMBL:AAU37160.1, ECO:0000313|Proteomes:UP000000607} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MBEL55E {ECO:0000313|EMBL:AAU37160.1, RC ECO:0000313|Proteomes:UP000000607}; 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 ----------------------------------------------------------------------- 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; AAU37160.1; -; Genomic_DNA. DR RefSeq; WP_011199732.1; NC_006300.1. DR RefSeq; YP_087745.1; NC_006300.1. DR ProteinModelPortal; Q65V50; -. DR STRING; 221988.MS0553; -. DR EnsemblBacteria; AAU37160; AAU37160; MS0553. DR KEGG; msu:MS0553; -. DR PATRIC; 22444518; VBIManSuc86752_0507. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; DVITANS; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; BMAN221988:GHGM-575-MONOMER; -. DR Proteomes; UP000000607; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000607}; KW Reference proteome {ECO:0000313|Proteomes:UP000000607}. SQ SEQUENCE 298 AA; 32265 MW; 7E71C20D06470E67 CRC64; MPITILDGGM SRELMRRNAP FRQPEWSACA LYEEPSAVQA VHEDFIAHGA EVITTDSYAV VPFHIGEQRF HTDGKTLADL AGRLAKSAVK NSGVLTTKIA GSLPPMFGSY RADLIQPERF AEIAQPLIDG LSPYVDIWLC ETQSAIIEPV SIKALLPKDD RPFWVSFTLT DDELTCEPQL RSGETVKSAV EKMVDLGVDA ILFNCCQPEV IGEALAVTTA TLTALNATHI QTGAYANAFA PQPKDATAND GLDEVRKDLD PPAYLAWAKK WTAQGASIIG GCCGIGVEYI ETLAKNLK // ID Q664W6_YERPS Unreviewed; 1230 AA. AC Q664W6; DT 11-OCT-2004, integrated into UniProtKB/TrEMBL. DT 11-OCT-2004, sequence version 1. DT 29-APR-2015, entry version 79. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CAH22891.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAH22891.1}; GN Name=metH {ECO:0000313|EMBL:CAH22891.1}; GN OrderedLocusNames=YPTB3653 {ECO:0000313|EMBL:CAH22891.1}; OS Yersinia pseudotuberculosis serotype I (strain IP32953). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=273123 {ECO:0000313|EMBL:CAH22891.1, ECO:0000313|Proteomes:UP000001011}; RN [1] {ECO:0000313|EMBL:CAH22891.1, ECO:0000313|Proteomes:UP000001011} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IP32953 {ECO:0000313|Proteomes:UP000001011}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; BX936398; CAH22891.1; -; Genomic_DNA. DR RefSeq; WP_011193209.1; NC_006155.1. DR RefSeq; YP_072134.1; NC_006155.1. DR ProteinModelPortal; Q664W6; -. DR SMR; Q664W6; 654-1230. DR STRING; 273123.YPTB3653; -. DR EnsemblBacteria; CAH22891; CAH22891; YPTB3653. DR KEGG; yps:YPTB3653; -. DR PATRIC; 18646693; VBIYerPse22266_4386. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; YPSE273123:GI1M-3765-MONOMER; -. DR Proteomes; UP000001011; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001011}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAH22891.1}; KW Transferase {ECO:0000313|EMBL:CAH22891.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 251 251 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 315 315 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 762 762 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1230 AA; 136022 MW; 58D685B9AB3A452A CRC64; MDTVIDNKVK ELHQQLAQRI LVLDGGMGTM IQSYRLEEAD YRGARFADWA SDLKGNNDLL VLSKPEVITA IHNAYLEAGA DILETNTFNS TSIAMADYQM ASLSAEINYE AARLARICAD EWSARTPEKP RYVAGVLGPT NRTASISPKV NDPAFRNVSF DQLVEAYRES TRALIEGGVD LIMIETVFDT LNAKAATFAV ESEFEAMGVL LPVMISGTIT DASGRTLSGQ TTEAFYNSLR HVKPLSFGLN CALGPDELRQ YVAELSRISE YYVSAHPNAG LPNAFGEYDL EAKEMAEQIG EWARAGFLNI VGGCCGTTPR HIAAMVNAVA GVPPRPLPDI PVACRLAGLE PLTIDANTLF VNVGERTNVT GSARFKRLIK EEKYGEALDV ARQQVESGAQ IIDINMDEGM LDAEAAMVRF LNLIAGEPDI ARVPIMIDSS RWDVIEKGLK CIQGKGIVNS ISMKEGVDAF IHHAKLVRRY GAAMVVMAFD ETGQADTRAR KIEICRRAYK ILTETVGFPP EDIIFDPNIF AVATGIEEHN NYAVDFIEAC ADIKAELPHA LISGGVSNVS FSFRGNDPVR EAIHAVFLYY AIRNGMDMGI VNAGQLAIYD DLSDELRDAV EDVILNRRDD STERLLDLAE KYRDSKSGEV AIQQAEWRGW PVVKRLEYSL VKGITEFIEL DTEEARQQAD RPIEVIEGPL MSGMNVVGDL FGEGKMFLPQ VVKSARVMKQ AVAYLEPYIE ASKQKGTTAG KILLATVKGD VHDIGKNIVG VVLQCNNYEI IDLGVMVPTE KILRTAREEK VDIIGLSGLI TPSLDEMVNV AKEMERQGFT LPLLIGGATT SKAHTAVKIE QNYSGSTTYV SNASRSVGVV SALLSDTQRE AFVAKTRKEY ETVRIQHARK KPRTPPVSLQ AARNNPTVID WENYTPPVAH KLGVQVVEAS IETLRNYIDW TPFFMTWSLA GKYPRILEDE VVGEEAKRLL ADANALLDKL SAEDLLHPKG VVGLFPANSV GDDIEIYRDE RRDEVLAISY HLRQQTEKTD FPNYCLADYV APKSSGKADY FGAFAVTGGL EEDALADAYD AQHDDYNKIM IKALSDRLAE AFAEYLHERV RKVYWGFAPN ENLSNEELVR ENYQGIRPAP GYPACPEHTE KGQIWQLLDV ETHTGMKLTE SYAMWPGASV SGWYFSHPDS KYFAVAQIQR DQVEDYAARK GMPTAEVERW LAPNLGYDAD // ID Q67LG1_SYMTH Unreviewed; 859 AA. AC Q67LG1; DT 11-OCT-2004, integrated into UniProtKB/TrEMBL. DT 11-OCT-2004, sequence version 1. DT 27-MAY-2015, entry version 71. DE SubName: Full=5-methyltetrahydrofolate S-homocysteine methyltransferase {ECO:0000313|EMBL:BAD41485.1}; GN OrderedLocusNames=STH2500 {ECO:0000313|EMBL:BAD41485.1}; OS Symbiobacterium thermophilum (strain T / IAM 14863). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Symbiobacteriaceae; OC Symbiobacterium. OX NCBI_TaxID=292459 {ECO:0000313|Proteomes:UP000000417}; RN [1] {ECO:0000313|EMBL:BAD41485.1, ECO:0000313|Proteomes:UP000000417} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T / IAM 14863 {ECO:0000313|Proteomes:UP000000417}; 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 ----------------------------------------------------------------------- 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; BAD41485.1; -; Genomic_DNA. DR RefSeq; WP_011196623.1; NC_006177.1. DR RefSeq; YP_076329.1; NC_006177.1. DR ProteinModelPortal; Q67LG1; -. DR STRING; 292459.STH2500; -. DR EnsemblBacteria; BAD41485; BAD41485; STH2500. DR KEGG; sth:STH2500; -. DR PATRIC; 23783172; VBISymThe116959_2494. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; STHE292459:GJMM-2581-MONOMER; -. DR Proteomes; UP000000417; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000417}; KW Methyltransferase {ECO:0000313|EMBL:BAD41485.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000417}; KW Transferase {ECO:0000313|EMBL:BAD41485.1}. SQ SEQUENCE 859 AA; 90899 MW; 3BCEAA8485178FF0 CRC64; MKLEDMLGRE VLVFDGAMGT MLQAQGLAPG ACPDVWNLER PEDVIAVHRA YVEAGAQILE TNTFGSTPIR LGHYGLQDRC RDIVVAGVRC AREAAAGRAW VAGSMGPLGA LVEPLGELPF DEAYAQFAVQ ARAFAEAQPD FIIIETIADL NELRAAVLAC RDHAPGIRII AQITLDPSGR AFTGTDPETA ALVLQSLGAD VIGFNCSVGP DLLVEAVARM ARVARVPISV QPNAGLPLLQ PDGATRFPMG PEEFAAYGPK LVEAGAALVG GCCGTTPEHI RRLRAAVEGL KPPARPGPLA HTLGLASRTR SLFFVEQNLP VVIGERINPT GRKLLTRDIR EGAFQRVRAE AKQQVEAGAA VLDVNVGVPL IDEPAAMARA VRVIQDAVDV PLCLDSPDPA ALEAGLKACV GKPLLNSFSL EEGRAEAVLP LARRYGAAVL GLTIDEKGIP ASAEQRLAIA RRLVAAAEAH GIPRHDVVID PLALTAGAQQ AEAKETLKAI RWITDELGVL ASLGVSNISF GLPNRHFLNA VYLSMAVTEG LAMAIMNPLD ERMMDTVRAL RLFLNRDRNA AVYMQAVGPK RLVHTVEEAL KAAAKAGEIA PAAVTPSSGA ASGPAPAGGR DGAATPAEPA TPAPADLADE LGRRLHDAIL EGDREAIVPL VEQGLAEGRD PMDMLNRHLI PAIEEVGRLF GEGIYFLPQL MLSAQAMKKA FARLKPEIQK AKVGQTEIGT VVLATVQGDI HDIGKNIVAV LLENYGFRVV DLGRDVKNEV VLEEARKVGA DMVGLSALMT TTMPQMKRVI ELFAREGFDC PVIVGGAATT KAFAEQIGAR GHGRDAQEAV ALALEVLKER RAGRKGDAG // ID Q6AL45_DESPS Unreviewed; 316 AA. AC Q6AL45; DT 13-SEP-2004, integrated into UniProtKB/TrEMBL. DT 13-SEP-2004, sequence version 1. DT 27-MAY-2015, entry version 57. DE SubName: Full=Chromosome {ECO:0000313|EMBL:CAG36930.1}; GN OrderedLocusNames=DP2201 {ECO:0000313|EMBL:CAG36930.1}; OS Desulfotalea psychrophila (strain LSv54 / DSM 12343). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales; OC Desulfobulbaceae; Desulfotalea. OX NCBI_TaxID=177439 {ECO:0000313|EMBL:CAG36930.1, ECO:0000313|Proteomes:UP000000602}; RN [1] {ECO:0000313|Proteomes:UP000000602} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LSv54 / DSM 12343 {ECO:0000313|Proteomes:UP000000602}; 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., Glockner 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; CAG36930.1; -; Genomic_DNA. DR RefSeq; WP_011189442.1; NC_006138.1. DR RefSeq; YP_065937.1; NC_006138.1. DR ProteinModelPortal; Q6AL45; -. DR STRING; 177439.DP2201; -. DR EnsemblBacteria; CAG36930; CAG36930; DP2201. DR KEGG; dps:DP2201; -. DR PATRIC; 21714438; VBIDesPsy67261_2410. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; DPSY177439:GJW5-2267-MONOMER; -. DR Proteomes; UP000000602; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000602}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000602}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 218 218 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 316 AA; 34226 MW; A898C58322A3579E CRC64; MAFTDESLLI FDGACGTTLQ SMNIAPSAWG DLAGCNEFLN ISAPEYIIEL HKKFLEAGAM VVETNTFGAS SIVLTEYGLE NKVDEINREA VKNAKKAISQ LKDSSQPRYI AGSIGPTTKL PSLGHIETKV LAQSIREQVI SLLEAGVDAL IVETCQDLLQ LKTALISCFE ILDVAPKKLP VLASVTFEKQ GTMLLGTDIA AVCATLAPFP LFSLGLNCAT GPTDMVSQIQ YLSQTWDKRI SCIPNQGMPE LKDGKTHYPL SPEEYSQHML KFVAEYGVSI VGGCCGTGPE HIRQLATCLR GQKPQRQLQT NTESII // ID Q6BZK6_DEBHA Unreviewed; 351 AA. AC Q6BZK6; DT 16-AUG-2004, integrated into UniProtKB/TrEMBL. DT 16-AUG-2004, sequence version 1. DT 29-APR-2015, entry version 57. DE SubName: Full=Chromosome A complete sequence {ECO:0000313|EMBL:CAG84308.1}; GN OrderedLocusNames=DEHA2A00616g {ECO:0000313|EMBL:CAG84308.1}; 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 {ECO:0000313|EMBL:CAG84308.1, ECO:0000313|Proteomes:UP000000599}; RN [1] {ECO:0000313|EMBL:CAG84308.1, ECO:0000313|Proteomes:UP000000599} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968 RC {ECO:0000313|Proteomes:UP000000599}; 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 Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., RA Zeniou-Meyer M., Zivanovic I., 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; CR382133; CAG84308.1; -; Genomic_DNA. DR RefSeq; XP_456363.1; XM_456363.1. DR ProteinModelPortal; Q6BZK6; -. DR STRING; 4959.Q6BZK6; -. DR GeneID; 2899355; -. DR KEGG; dha:DEHA2A00616g; -. DR HOGENOM; HOG000265278; -. DR InParanoid; Q6BZK6; -. DR KO; K00547; -. DR OMA; WESAINI; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000000599; Chromosome A. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000599}; KW Reference proteome {ECO:0000313|Proteomes:UP000000599}. SQ SEQUENCE 351 AA; 39445 MW; C191E517B019968A CRC64; MINDINTLIN TKPLVIDGAL GTQLETKFSK LLQQDNINIQ THPLWSALVL LKNPELIQEV HYDYMCSGAN IITTSTYQAS KRGLLEYAPG IENDDEVNAV YDKAIELAVD ARSQYLENMG KGMNTLTNKE IFICGSIGPF GAYLANGAEY TGKYGSHITE PQELKKFHYD ITSQFISNPK CDIIGFETIP NYSEFQQIVH LMEELLQKTN KPFYISLNFK DPKTICDGTP ITQVVDYLNE RLSNNEKLRS AFIGLGCNCV PLEIATNILL NMSDLNNVHR FPLIAYPNAG LNYDLSKGEY SIKSSEKQVW EDSCREWLEK LNVRLVGACC GSGPDEILTI REVTDKFAGQ R // ID Q6C0D6_YARLI Unreviewed; 348 AA. AC Q6C0D6; DT 16-AUG-2004, integrated into UniProtKB/TrEMBL. DT 16-AUG-2004, sequence version 1. DT 29-APR-2015, entry version 59. DE SubName: Full=Chromosome F complete sequence {ECO:0000313|EMBL:CAG78687.1}; GN ORFNames=YALI0_F25641g {ECO:0000313|EMBL:CAG78687.1}; 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 {ECO:0000313|EMBL:CAG78687.1, ECO:0000313|Proteomes:UP000001300}; RN [1] {ECO:0000313|EMBL:CAG78687.1, ECO:0000313|Proteomes:UP000001300} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CLIB 122 / E 150 {ECO:0000313|Proteomes:UP000001300}; 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 Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., RA Zeniou-Meyer M., Zivanovic I., 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; CR382132; CAG78687.1; -; Genomic_DNA. DR RefSeq; XP_505876.1; XM_505876.1. DR ProteinModelPortal; Q6C0D6; -. DR STRING; 4952.Q6C0D6; -. DR EnsemblFungi; CAG78687; CAG78687; YALI0_F25641g. DR GeneID; 2907792; -. DR KEGG; yli:YALI0F25641g; -. DR HOGENOM; HOG000265278; -. DR InParanoid; Q6C0D6; -. DR KO; K00547; -. DR OMA; HIDYLAY; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000001300; Chromosome F. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001300}; KW Reference proteome {ECO:0000313|Proteomes:UP000001300}. SQ SEQUENCE 348 AA; 38050 MW; 4315ABC77EBB5CA5 CRC64; MLILDGGMGT ELENRGIDCS DPLWLTLWSA KFLLPINSDF LKCIESADPW TVDQLEKVNR ALDEHPEWLE SSQDNSNLLY RIHKDYVVAG ADIVTSASYQ ASLEGTIKAG AVQRWPEALW MLRKSEQLVR KAVTEAKVKR KVLLAASVGP FGAWLGGGQE YNGDYTGYTK DDIRRHHEFK IRAVLGGSPD MLLIETIPSI IEVEVLVDVL NTILPPSPIP VCLSLSVKSA DYDRVALADG SELSNIAELA ASCPSFTHLG VNCCAETVAK LSLDILQQHT SLQLIVYPNS GEVYDGATKT WSGNCDSSFL EAATLSDWQT SVSILGGCCR TGPPHIAFLR HKVDGFLS // ID Q6CSF1_KLULA Unreviewed; 331 AA. AC Q6CSF1; DT 16-AUG-2004, integrated into UniProtKB/TrEMBL. DT 16-AUG-2004, sequence version 1. DT 29-APR-2015, entry version 59. DE SubName: Full=Strain NRRL Y-1140 chromosome D complete sequence {ECO:0000313|EMBL:CAH00234.1}; GN ORFNames=KLLA0_D01551g {ECO:0000313|EMBL:CAH00234.1}; 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 {ECO:0000313|Proteomes:UP000000598}; RN [1] {ECO:0000313|EMBL:CAH00234.1, ECO:0000313|Proteomes:UP000000598} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / RC WM37 {ECO:0000313|Proteomes:UP000000598}; 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 Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., RA Zeniou-Meyer M., Zivanovic I., 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; CR382124; CAH00234.1; -; Genomic_DNA. DR RefSeq; XP_453138.1; XM_453138.1. DR ProteinModelPortal; Q6CSF1; -. DR STRING; 28985.Q6CSF1; -. DR GeneID; 2893019; -. DR KEGG; kla:KLLA0D01551g; -. DR HOGENOM; HOG000066018; -. DR InParanoid; Q6CSF1; -. DR KO; K00547; -. DR OMA; AINDPLW; -. DR OrthoDB; EOG7X9GHR; -. DR Proteomes; UP000000598; Chromosome D. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000598}; KW Reference proteome {ECO:0000313|Proteomes:UP000000598}. SQ SEQUENCE 331 AA; 37410 MW; 989B3020766F091B CRC64; MRVPIKKYFE ENPDVVLVMD GGQGTELENR GINVANPVWS TVPFINESFW SSDASKDRII VKQMFEDFIE AGADILMTIT YQTSFKSVSE NTPIRTLEEY NGLLDRIVSF SRSCIGEDRY LIGCIGAWGA HVCSEFTGDY GPHPDQIDYF EYFRPQLGNF VQSKDIDIIG FETIPNIHEL RAILSWDETV LSKPFYIGLS VHEYGVLRDG TSMQQIADLI SSLGDKLNSN LMFIGINCCA FNQSHMILES LHNSCPNMPL IVYPNSGEIY DTVKKIWLKN ENQLCTWDDV VKSYIENGAR IIGGCCRTTV DDIKEVRLAV NKYAKQTTSS L // ID Q6D014_PECAS Unreviewed; 1227 AA. AC Q6D014; DT 16-AUG-2004, integrated into UniProtKB/TrEMBL. DT 16-AUG-2004, sequence version 1. DT 29-APR-2015, entry version 78. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:CAG76884.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAG76884.1}; GN Name=metH {ECO:0000313|EMBL:CAG76884.1}; GN OrderedLocusNames=ECA3987 {ECO:0000313|EMBL:CAG76884.1}; 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 {ECO:0000313|EMBL:CAG76884.1, ECO:0000313|Proteomes:UP000007966}; RN [1] {ECO:0000313|Proteomes:UP000007966} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SCRI 1043 / ATCC BAA-672 {ECO:0000313|Proteomes:UP000007966}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; BX950851; CAG76884.1; -; Genomic_DNA. DR RefSeq; WP_011095481.1; NC_004547.2. DR RefSeq; YP_052074.1; NC_004547.2. DR ProteinModelPortal; Q6D014; -. DR SMR; Q6D014; 651-1227. DR STRING; 218491.ECA3987; -. DR EnsemblBacteria; CAG76884; CAG76884; ECA3987. DR GeneID; 2883939; -. DR KEGG; eca:ECA3987; -. DR PATRIC; 20483399; VBIPecAtr54885_4050. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PATR218491:GJNB-4065-MONOMER; -. DR Proteomes; UP000007966; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007966}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAG76884.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007966}; KW Transferase {ECO:0000313|EMBL:CAG76884.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 135467 MW; 31C931B3110B9C76 CRC64; MSNRVDELRR QLAQRIMVLD GGMGTMIQGY RLQEADYRGE RFADWPSDVK GNNDLLVLTR PQVISEIHNA YLEAGADILE TNTFNSTTIA MADYDMASLS AEINTVAAQL ARASADKWTA LTPDKPRYVA GVLGPTNRTA SISPDVNDPA FRNVSFDQLV EAYRESTRAL IAGGVDLIMI ETIFDTLNAK AASFAVESEF EALGIVLPVM ISGTITDASG RTLSGQTTEA FYNSLRHSRP LSFGLNCALG PDELRQYVAE LSRISECYVS AHPNAGLPNA FGEYDLDPAD MAKHIGEWAR SGFLNIVGGC CGSTPAHIAA MAKVVEGVPP RKLPEIPVAC RLSGLEPLTI DANTLFVNVG ERTNVTGSAR FKRLIKEEKY NEALDVARQQ VESGAQIIDI NMDEGMLDAE AAMTRFLNLI AGEPDIARVP IMIDSSKWDV VEKGLKCIQG KGIVNSISMK EGVEAFIHHA KLVRRYGAAV VVMAFDEVGQ ADTRARKIEI CRRAYRILTE EVGFPPEDII FDPNIFAVAT GIDEHNNYAV DFIEACADIK AQLPHAMISG GVSNVSFSFR GNDLVREAIH AVFLYYAIRN GMDMGIVNAS QLAIYDDLPA ELRDAVEDVI LNRRSDATER MLELAEKYRG SKTEDEGSKT QAEWRGWDVK KRLEYSLVKG ITEFIELDTE EARQQASRPI EVIEGPLMDG MNVVGDLFGA GKMFLPQVVK SARVMKQAVA YLEPYIDASK DKGSSAGKIL LATVKGDVHD IGKNIVGVVL QCNNYEIIDL GVMVPTDKIL KTAREEKVDI IGLSGLITPS LDEMVNVAKE MERQGFTLPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRSVGVVSAL LSSTQYGDFV ARTRKEYETV RIQHARKKPR TPPVTLEAAR ANASDLDWEN YTPPIAHRPG VQAVTANIET LRNYIDWTPF FMTWSLAGKY PRILEDDVVG EEAKRLFADA NAMLDDLSAR GALNPRGVVG LFPANRVGDD VVIYTDERRE TVLSVSHHLR QQTEKPDFPN YCLSDFVAPK SSGKPDYLGA FAVTGGLEED ALADLWEAQH DDYNKIMVKA ISDRLAEAFA EYLHERVRKV YWGYAPNENL SNELLIRENY QGVRPAPGYP ACPDHTEKVQ IWQLLDVEKH TGMKLTESYA MWPGASVSGW YFSHPDSKYF AVAQIQRDQV EDYAVRKGMN VGEVERWLAP NLGYDAD // ID Q6D3E7_PECAS Unreviewed; 311 AA. AC Q6D3E7; DT 16-AUG-2004, integrated into UniProtKB/TrEMBL. DT 16-AUG-2004, sequence version 1. DT 29-APR-2015, entry version 56. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:CAG75697.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:CAG75697.1}; GN Name=mmuM {ECO:0000313|EMBL:CAG75697.1}; GN OrderedLocusNames=ECA2797 {ECO:0000313|EMBL:CAG75697.1}; 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 {ECO:0000313|EMBL:CAG75697.1, ECO:0000313|Proteomes:UP000007966}; RN [1] {ECO:0000313|Proteomes:UP000007966} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SCRI 1043 / ATCC BAA-672 {ECO:0000313|Proteomes:UP000007966}; 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 ----------------------------------------------------------------------- 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; CAG75697.1; -; Genomic_DNA. DR RefSeq; WP_011094332.1; NC_004547.2. DR RefSeq; YP_050888.1; NC_004547.2. DR ProteinModelPortal; Q6D3E7; -. DR STRING; 218491.ECA2797; -. DR DNASU; 2882944; -. DR EnsemblBacteria; CAG75697; CAG75697; ECA2797. DR GeneID; 2882944; -. DR KEGG; eca:ECA2797; -. DR PATRIC; 20480905; VBIPecAtr54885_2835. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; PATR218491:GJNB-2841-MONOMER; -. DR Proteomes; UP000007966; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007966}; KW Methyltransferase {ECO:0000313|EMBL:CAG75697.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007966}; KW Transferase {ECO:0000313|EMBL:CAG75697.1}. SQ SEQUENCE 311 AA; 33515 MW; CCBF8A3512887C6D CRC64; MRKNRITEML ATASTIVLDG ALATELEARG CDLTDPLWSA KVLVENPALI YQVHFDYFKA GAQCAITASY QATPQGFEAR GYSEAESLAL IAKSVQLAAQ ARDDYRRDNT QAGTLLVAGS VGPYGAYLAD GSEYRGDYQL PQADMMAFHR PRIAALHEAG ADLLACETLP SFAEIEALIA LLAEFPQAQA WFSFTLRDSE HLSDGTPLRT VLERVNACSQ VVAVGLNCIA LEKVTPALMH LSSLTDLPLV VYPNSGEQYD AVTKTWSSAH DTACSLTAYL PEWQTAGARL IGGCCRTTPA DIAGIARCCQ Q // ID Q6FCC8_ACIAD Unreviewed; 292 AA. AC Q6FCC8; DT 19-JUL-2004, integrated into UniProtKB/TrEMBL. DT 19-JUL-2004, sequence version 1. DT 27-MAY-2015, entry version 60. DE SubName: Full=Acinetobacter sp. ADP1 complete genome {ECO:0000313|EMBL:CAG68283.1}; DE EC=2.1.1.- {ECO:0000313|EMBL:CAG68283.1}; GN OrderedLocusNames=ACIAD1418 {ECO:0000313|EMBL:CAG68283.1}; OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=62977 {ECO:0000313|EMBL:CAG68283.1, ECO:0000313|Proteomes:UP000000430}; RN [1] {ECO:0000313|EMBL:CAG68283.1, ECO:0000313|Proteomes:UP000000430} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33305 / BD413 / ADP1 {ECO:0000313|Proteomes:UP000000430}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; CAG68283.1; -; Genomic_DNA. DR RefSeq; WP_004925547.1; NC_005966.1. DR RefSeq; YP_046105.1; NC_005966.1. DR ProteinModelPortal; Q6FCC8; -. DR STRING; 62977.ACIAD1418; -. DR EnsemblBacteria; CAG68283; CAG68283; ACIAD1418. DR KEGG; aci:ACIAD1418; -. DR PATRIC; 20740650; VBIAciSp98416_1277. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; PYVDVWL; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; ASP62977:GJVV-1347-MONOMER; -. DR Proteomes; UP000000430; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000430}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:CAG68283.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000430}; KW Transferase {ECO:0000313|EMBL:CAG68283.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 202 202 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 275 275 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 276 276 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 292 AA; 32125 MW; B2C058B54618F7F3 CRC64; MKILDGGFGR ELARRGAPFR QPEWSALALT EAPEIVKEVH LDFIRAGAQV ITTNNYAVVP FHIGQERFDR EVTQLVKVAT SQARLAVQES GQPVQIAGCL PPLFGSYRAD LFDQSKAEAL AKPIIEALSP DVDFWLAETQ SCLAEVRTIH QLLPKDGREF WVSFTLQDEQ ALTEAKLRSG ENIQQAAQLV HELGANAILF NCCQPEVILQ AIEEIRSLLP SGVKIGAYAN AFPPQNSDAT ANDGLDEVRK DLDPDAYLTF AKQWQHAGAS MIGGCCGIGP EHIQKLSQFF QE // ID Q6FDC4_ACIAD Unreviewed; 1228 AA. AC Q6FDC4; DT 19-JUL-2004, integrated into UniProtKB/TrEMBL. DT 19-JUL-2004, sequence version 1. DT 27-MAY-2015, entry version 84. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CAG67934.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAG67934.1}; GN Name=metH {ECO:0000313|EMBL:CAG67934.1}; GN OrderedLocusNames=ACIAD1045 {ECO:0000313|EMBL:CAG67934.1}; OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=62977 {ECO:0000313|EMBL:CAG67934.1, ECO:0000313|Proteomes:UP000000430}; RN [1] {ECO:0000313|EMBL:CAG67934.1, ECO:0000313|Proteomes:UP000000430} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33305 / BD413 / ADP1 {ECO:0000313|Proteomes:UP000000430}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CR543861; CAG67934.1; -; Genomic_DNA. DR RefSeq; WP_004921699.1; NC_005966.1. DR RefSeq; YP_045756.1; NC_005966.1. DR ProteinModelPortal; Q6FDC4; -. DR SMR; Q6FDC4; 654-893. DR STRING; 62977.ACIAD1045; -. DR EnsemblBacteria; CAG67934; CAG67934; ACIAD1045. DR KEGG; aci:ACIAD1045; -. DR PATRIC; 20739944; VBIAciSp98416_0936. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; ASP62977:GJVV-986-MONOMER; -. DR Proteomes; UP000000430; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000430}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAG67934.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000430}; KW Transferase {ECO:0000313|EMBL:CAG67934.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1228 AA; 135835 MW; 912B8F414D909ADA CRC64; MSTLTTLKAL LAERILIIDG AMGTMIQRHK LEEDDYRGER FADWASDLKG NNDLLVLTQP QIIQGIHEAY LDAGADIIET NSFNGTRVSM SDYHMEDLVP EINREAARLA RAACDKYSTP DKPRFVAGVL GPTSRTCSIS PNVNDPAFRN ITFDELKENY IEATHALIEG GADILLIETV FDTLNCKAAI FAVKEVFKQL GHELPLMISG TITDASGRTL TGQTAEAFWN SVRHGDLLSI GFNCALGADA MRPHVKTISD VADTFVSAHP NAGLPNAFGE YDETPEQTAA FLKEFAMSGL INITGGCCGT TPDHIRAIYN AVKDIQPRQI PETKPACRLS GLEPFNIYDD SLFVNVGERT NVTGSKKFLR LIREEKFAEA LEVAQQQVEA GAQIIDINMD EGMLDSQNAM VHFLNLVASE PDISRVPIMI DSSKWEIIEA GLKCVQGKPV VNSISLKEGY DEFVEKARLC RQYGAAIIVM AFDETGQADT AARKREICKR SYDVLVNEVG FPAEDIIFDP NVFAVATGIE EHNNYGVDFI EATGWIKQNL PHAMISGGVS NVSFSFRGNE PVREAIHSVF LYHAIKQGMT MGIVNAGQMA IYDDIPKELK DAVEDVVLNQ NQGESGQNAT EKLLEVAEKF RGHSGAQREA ENLEWRNESV EKRLEYALVK GITTYIDEDT EEARLKAKRP LDVIEGALMD GMNVVGDLFG SGKMFLPQVV KSARVMKQAV AWLNPYIEAE KTGSQSKGKV LMATVKGDVH DIGKNIVGVV LGCNGYDIVD LGVMVPAEKI LQTAIDEKCD IIGLSGLITP SLDEMVFVAK EMQRKGFNIP LLIGGATTSK AHTAVKIDPQ YQNDAVIYVA DASRAVGVAT TLLSKEMRGN FIAEHRAEYA KIRERLANKQ PKAAKLSYQE AVKNGFNIDW NAYVPPKPNL LGEQVITNYP LEKLVPYFDW TPFFISWSLT GKFPKILTDE IVGEAATDLY NQAQAMLKDI IENKRFDARA VFALYPAKRT GDDTVSVYDM QGNITHTFEH LRQQSDKVTG KPNLSLADFI STSQEHTDYL GGFTVSIFGA EELANEYKAK GDDYSAILVQ SLGDRFAEAF AEHLHELIRK DYWGYQPDEA LDNEALIKEK YVGIRPAPGY PACPEHSEKA VLFDWLGSTD KIGTFLTSSF AMWPPSSVSG FYYSLPQSEY FNVGKISQDQ LEDYAKRKGW TMDEAKRWLA PNLDDSIS // ID Q6HDR1_BACHK Unreviewed; 610 AA. AC Q6HDR1; DT 19-JUL-2004, integrated into UniProtKB/TrEMBL. DT 19-JUL-2004, sequence version 1. DT 27-MAY-2015, entry version 71. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN Name=metE {ECO:0000313|EMBL:AAT60796.1}; GN OrderedLocusNames=BT9727_3996 {ECO:0000313|EMBL:AAT60796.1}; OS Bacillus thuringiensis subsp. konkukian (strain 97-27). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=281309 {ECO:0000313|EMBL:AAT60796.1, ECO:0000313|Proteomes:UP000001301}; RN [1] {ECO:0000313|Proteomes:UP000001301} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=97-27 {ECO:0000313|Proteomes:UP000001301}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; AAT60796.1; -; Genomic_DNA. DR RefSeq; WP_000770331.1; NC_005957.1. DR RefSeq; YP_038315.1; NC_005957.1. DR ProteinModelPortal; Q6HDR1; -. DR STRING; 281309.BT9727_3996; -. DR EnsemblBacteria; AAT60796; AAT60796; BT9727_3996. DR GeneID; 2856148; -. DR KEGG; btk:BT9727_3996; -. DR PATRIC; 18989070; VBIBacThu119411_4261. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; BTHU281309:GJID-4069-MONOMER; -. DR Proteomes; UP000001301; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001301}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:AAT60796.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:AAT60796.1}. SQ SEQUENCE 610 AA; 67298 MW; 3F0A2353CD3128EB CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNISDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTE INRAAVKLAK ASVTDRNAIL GTIGGMKHIG AVTTTDMERE FMLLEQASAL LEEQVDGLLL ETFYDEFELL HAVQVLRKET NIPIVAQLAL HEAGTTQNGN DVNEILKQLL DYGANVVGLN CQLGPLHMTE AFKMISIPKN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPKFIEQGI RLLGGCCGTT PEHIESMKRA TLNVTPVIEK DTIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRISNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIA LIEEVYEATK HLEQPIFIGI MPLISKRNAD FLHFEVPGIT LPEAVRERMD GHETKEAAIE EGIRISQELI DETMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID Q6HDR2_BACHK Unreviewed; 1133 AA. AC Q6HDR2; DT 19-JUL-2004, integrated into UniProtKB/TrEMBL. DT 19-JUL-2004, sequence version 1. DT 01-APR-2015, entry version 83. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AAT60795.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AAT60795.1}; GN Name=metH {ECO:0000313|EMBL:AAT60795.1}; GN OrderedLocusNames=BT9727_3995 {ECO:0000313|EMBL:AAT60795.1}; OS Bacillus thuringiensis subsp. konkukian (strain 97-27). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=281309 {ECO:0000313|EMBL:AAT60795.1, ECO:0000313|Proteomes:UP000001301}; RN [1] {ECO:0000313|Proteomes:UP000001301} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=97-27 {ECO:0000313|Proteomes:UP000001301}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AE017355; AAT60795.1; -; Genomic_DNA. DR RefSeq; WP_011181858.1; NC_005957.1. DR RefSeq; YP_038314.1; NC_005957.1. DR ProteinModelPortal; Q6HDR2; -. DR STRING; 281309.BT9727_3995; -. DR PRIDE; Q6HDR2; -. DR EnsemblBacteria; AAT60795; AAT60795; BT9727_3995. DR GeneID; 2854248; -. DR KEGG; btk:BT9727_3995; -. DR PATRIC; 18989068; VBIBacThu119411_4260. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; BTHU281309:GJID-4068-MONOMER; -. DR Proteomes; UP000001301; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001301}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AAT60795.1}; KW Transferase {ECO:0000313|EMBL:AAT60795.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 223 223 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 287 287 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 719 719 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1133 AA; 126013 MW; 3B9D959A85EBB820 CRC64; MMKCIEEKLK NNILLLDGAM GTMIQQEDLT AEDFGGEEYE GCNEYLVETR PDVILKIHKA YIEAGADIIE TNTFGATNIV LSDYELSHLD EELNEKAARL AKQAVKESGK EVYVAGAMGP TTKAISVTGG VTFEELIEAY TRQARGLLKG EVDVLLVETS QDMRNVKAAY IGIQAAFDEL KKIVPIMISG TIEPMGTTLA GQTIEAFYLS VEHMKPLSVG LNCATGPEFM RDHIRSLSDL SGGYISCYPN AGLPDEDGHY HESPSSLAEK VKRFAEEGWV NIIGGCCGTT PEHIKAMKEA LASLKPREHH EREGHGVSGL EALQYDDSMR PLFVGERTNV IGSRKFKRLV AEGKFEEAAE VARAQVKKNA HIIDICMADP DRDEIEDMEN FLAEVTKVLK VPIMIDSTDE HVMERALTYI QGKAVINSIN LEDGEERFIK VTPLLQKYGA AIVVGTIDED GMAVSAERKL EIAKRSYELL TTKYGIRPSD IIFDALVFPV GTGDEEYIGS AAATIEGIRL IKEALPECLT ILGVSNISFG LPPAGREVLN SVFLYHATKA GLDYAIVNTE KLERYASIPD EEKRLADALL FETTQETLEE FTNFYRVAKK KDVVVQETLT LDERLANYIV EGTKQGLHED LSLALTEGRK PLDIINGPLM TGMDEVGRLF NNNELIVAEV LQSAESMKAA VSYLEPHMES SDSAKKGKVL LATVKGDVHD IGKNLVEIIL ANNGYEIINL GINVRSDRIV QEVQEKKPDI IGLSGLLVKS AQQMVTTAED LKAADIDIPI VVGGAALTRK FTDNRISPSY KGLVCYASDA MTGLDIINKL QKEEEREKMK QDKKERHLHI VTKEEKKIEI PAVIEPLPKS EVMVPDSTKR IVLRDVPALH LAPFLNRQML LGHHLGLKGS VKKLLKEGDK RAHELNDLID ELLQEGQSWL KPKAVYQFFP AQSDGQNIVI YDPEDHTRVI ERFTFPRQGR APYRTLGDYL RPIGDEMDYV AFLSVTVGEG VRDIAEEWKA KGDYLRSHAI QSLALELAEG LAEKTHMLIR DRWGIPDSPE LTMEERFRTK YRGIRVSFGY PACPELADQE KLFRLIHPEE IGISLTEGFM MEPEASVTAM VFSHPEARYF SVL // ID Q6LM78_PHOPR Unreviewed; 1223 AA. AC Q6LM78; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 29-APR-2015, entry version 80. DE SubName: Full=METH protein {ECO:0000313|EMBL:CAG21599.1}; GN Name=METH {ECO:0000313|EMBL:CAG21599.1}; GN OrderedLocusNames=PBPRA3294 {ECO:0000313|EMBL:CAG21599.1}; OS Photobacterium profundum (Photobacterium sp. (strain SS9)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Photobacterium. OX NCBI_TaxID=74109 {ECO:0000313|EMBL:CAG21599.1, ECO:0000313|Proteomes:UP000000593}; RN [1] {ECO:0000313|Proteomes:UP000000593} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SS9 {ECO:0000313|Proteomes:UP000000593}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; CR378673; CAG21599.1; -; Genomic_DNA. DR RefSeq; YP_131401.1; NC_006370.1. DR ProteinModelPortal; Q6LM78; -. DR SMR; Q6LM78; 653-1223. DR STRING; 298386.PBPRA3294; -. DR EnsemblBacteria; CAG21599; CAG21599; PBPRA3294. DR KEGG; ppr:PBPRA3294; -. DR PATRIC; 22937649; VBIPhoPro109272_3440. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PPRO298386-WGS:GSSB-3287-MONOMER; -. DR Proteomes; UP000000593; Chromosome 1. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000593}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000593}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 248 248 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 312 312 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1223 AA; 135666 MW; BB11E5B6802B1BA4 CRC64; MVVKSKEILQ KRLAENILII DGGMGTMIQG YKLDENDYRG ERFADWHSDL KGNNDLLVLT QPQLIKDIHN EYLEAGADIL ETNTFNATTI AMADYDMESL SAEINFEAAK LARQAADEWT LKTPSKPRFV AGVLGPTNRT CSISPDVNDP SFRNVTFDQL VEAYSESTRA LIAGGVDLIL VETIFDTLNA KACTFAVETV FDEDGVVLPI MISGTITDAS GRTLSGQTTE AFYNSLRHVK PISFGLNCAL GPDELRQYVD ELSRISESAV SAHPNAGLPN AFGEYDLSPE DMAEHIEEWA KSGFLNLVGG CCGTTPEHIR LMEQVTRNVK PRQLPDIPIA CRLSGLEPLT ISADTLFVNV GERTNVTGSA RFKRLIKDEL YDEALEVARQ QVEAGAQIID INMDEGMLDA EAAMVRFLNL CATEPEISKV PIMVDSSKWE ILEAGLKCIQ GKPIVNSISM KEGVEKFIAQ AKLIRRYGAA VIVMAFDEEG QADTRERKIE ICTNAYHILV NEVGFPPEDI IFDPNIFAVA TGIEEHNNYA VDFIEAVGDI KRTLPYAMVS GGVSNVSFSF RGNDPIREAI HAVFLYYCFK NGMDMGIVNA GQLAIYDDLT DELRNAVEDV VLNRRDDSTE RLLDIAEKYR GSGKVEEDRT LQEWRGWPVE KRLSHALVKG ITEFIVEDTE EARTNASKPL EVIEGPLMAG MNIVGDLFSE GKMFLPQVVK SARVMKQAVA HLEPYINAEK QAGYTNGKIL LATVKGDVHD IGKNIVGVVL QCNNYEIIDL GVMVSCEKIL KVAKEKNVDI IGLSGLITPS LDEMVHVAKE MERQGFELPL LIGGATTSKA HTAVKIEENY HGPVVYVSNA SRAVGVCSAL LSDVLRPAFI ERLDKEYITV REQHARKKPR TPPVTLEQAR ENKVAIDWES YTPPAPVKPG IHVFTDFPIS KIRKYIDWTP FFMTWSLSGK YPTILRHEVV GEEAQRLFDD ANVLLDEIER TGMIKANGVC GLFPANNIGD DIEVYTDETR SEVMTVLCGL RQQTKKPKGP NYCLSDYIAP KESNKADWIG AFAVTGGIGE YDIAEQFKAK GDDYNAIMVQ AIADRLAEAF AECMHETVRK DIWGYAPEES LANEDLIREK YQGIRPAPGY PACPEHTEKG AIWTLLDAEA NTGMVLTESY AMWPGAAVSG WYFSHPESRY FAVAQIQTDQ RDSYADRKGW DLLDAEKWLG PNL // ID Q6N3J1_RHOPA Unreviewed; 1293 AA. AC Q6N3J1; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 29-APR-2015, entry version 77. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CAE29143.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAE29143.1}; GN Name=metH {ECO:0000313|EMBL:CAE29143.1}; GN OrderedLocusNames=RPA3702 {ECO:0000313|EMBL:CAE29143.1}; OS Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Rhodopseudomonas. OX NCBI_TaxID=258594 {ECO:0000313|EMBL:CAE29143.1, ECO:0000313|Proteomes:UP000001426}; RN [1] {ECO:0000313|EMBL:CAE29143.1, ECO:0000313|Proteomes:UP000001426} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-98 / CGA009 {ECO:0000313|Proteomes:UP000001426}; RX PubMed=14704707; DOI=10.1038/nbt923; RA Larimer F.W., Chain P., Hauser L., Lamerdin J., Malfatti S., Do L., RA Land M.L., Pelletier D.A., Beatty T.J., Lang A.S., Tabita F.R., RA Gibson J.L., Hanson T.E., Torres y Torres J., Peres C., Harrison F.H., RA 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; BX572604; CAE29143.1; -; Genomic_DNA. DR RefSeq; NP_949040.1; NC_005296.1. DR RefSeq; WP_011159241.1; NC_005296.1. DR ProteinModelPortal; Q6N3J1; -. DR SMR; Q6N3J1; 655-1238. DR STRING; 258594.RPA3702; -. DR EnsemblBacteria; CAE29143; CAE29143; RPA3702. DR KEGG; rpa:RPA3702; -. DR PATRIC; 23291945; VBIRhoPal84835_3888. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR PhylomeDB; Q6N3J1; -. DR Proteomes; UP000001426; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001426}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAE29143.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001426}; KW Transferase {ECO:0000313|EMBL:CAE29143.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 770 770 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1293 AA; 140067 MW; 61435B0EEE4D858A CRC64; MTKPISAKRT QLLALAAQRI LVLDGAMGTM IQQLQLDEAA FRGERFKDFH RDLRGNNDLL ILTQPQAIED IHAQYLRAGA DIVATNTFSS TSIAQADYEM SELAYEMSRD GARLARNAAA KVEAEDGKPR FVAGAIGPTN RTASISPDVA NPGYRAVTFD DLRIAYSEQI NGLLDGGADI LLLETIFDTL NAKAALYAIA EITEARGIDV PVMISGTITD KSGRLLSGQM PEAFWNSVRH ARPITIGFNC ALGAKDLRAH IADISRVADT LVCAYPNAGL PNEFGQYDES PEYMASLVGE FAEAGLVNIV GGCCGTTPAH IKAIAEAVAP HKPRVIPTID PRLRLSGLEP FELTKDIPFV NVGERTNVTG SAKFRKLITA GDYAAALQVA RDQVENGAQI IDVNMDEGLL DSEAAMITFL NLVAAEPDIA KVPVMVDSSK FNVIEAGLKC LQGKPVVNSI SLKEGEDKFL HEARIARRHG AAVVVMAFDE TGQADTYARK TEICARAYDI LVNRVGFPPE DIIFDPNIFA IATGLEEHNN YGVDFIEATR WIRQNLPHAH ISGGVSNLSF SFRGNEPVRE AMHSVFLYHA IKAGMDMGIV NAGQMIVYDD IDPELRQVCE DVILNRDPGA SERLLALADK YRGQGKQQKE QDLAWRSWPV EQRLSHALVH GITEFIELDT EEARAKAERP LHVIEGPLMA GMNVVGDLFG DGKMFLPQVV KSARVMKQAV AYLMPFMEEE KARNLAAGTD TGERATAGKI VLATVKGDVH DIGKNIVGIV LQCNNFEVID LGVMVPAAKI IETAKAENAD IVGLSGLITP SLDEMSFLAG ELQRSGFNIP LLIGGATTSR VHTAVKIDPA YPSGSVVHVN DASRAVGVAS SLLSKDRGAA YAAEVRADYA KISAAHHRAQ ADKKRLTLAA ARANATKIDW AATSPVKPSF IGTRSFSGYS LAELAEYIDW TPFFQAWELA GRFPAILDDS VVGEAARSLY ADARKMLDRI VTENWFTAKA TIGFWPANAD GDDILVYADE TRTTPIATLH TLRQQLDKRE GRANAALSDF IAPVASSVAD YIGGFVVTAG IGEDVIADKF KAERDDYSSI MVKALADRLA EAFAERMHAR VRREFWGYAA DENLSAEDLI LEKYQGIRPA PGYPAQPDHT EKATLFELLD AEASAGVTLT ESFAMWPGSS VSGLYFSHPQ SAYFGVGKIE RDQVEDYAAR KGWDVATAER WLAPVLNYIP SRSTGATDET GMPPLAPQAA APLSAEDAAL ASHPQGCTCA LHLAWRKQKV AAK // ID Q6NH83_CORDI Unreviewed; 1201 AA. AC Q6NH83; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 27-MAY-2015, entry version 87. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:CAE49788.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAE49788.1}; GN Name=metH {ECO:0000313|EMBL:CAE49788.1}; GN OrderedLocusNames=DIP1259 {ECO:0000313|EMBL:CAE49788.1}; OS Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype OS gravis). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=257309 {ECO:0000313|Proteomes:UP000002198}; RN [1] {ECO:0000313|EMBL:CAE49788.1, ECO:0000313|Proteomes:UP000002198} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis RC {ECO:0000313|Proteomes:UP000002198}; 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., Bentley S.D., Besra G.S., Churcher C., 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., Thomson N.R., Unwin L., Whitehead S., RA 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; BX248357; CAE49788.1; -; Genomic_DNA. DR RefSeq; NP_939614.1; NC_002935.2. DR RefSeq; WP_010934932.1; NC_002935.2. DR ProteinModelPortal; Q6NH83; -. DR STRING; 257309.DIP1259; -. DR EnsemblBacteria; CAE49788; CAE49788; DIP1259. DR KEGG; cdi:DIP1259; -. DR PATRIC; 21483714; VBICorDip47633_1241. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR Proteomes; UP000002198; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002198}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAE49788.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002198}; KW Transferase {ECO:0000313|EMBL:CAE49788.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 234 234 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 300 300 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 301 301 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 752 752 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1201 AA; 131500 MW; 538339355B6CADDF CRC64; MMNTATPQFK TAFLDAMKNR VLIGDGAMGT QLQGFDLDVD SDFLGLEGCN EILNHTRPDV VSAIHRAYFE AGADLVETNT FGCNLPNLAD YDIADRCKEL AFKGVKIARE VADELGPSAD GTPRFVLGSM GPGTKLPSLG HAPYEALKNH YTEASLGMIE GGADAILVET AQDLLQVKAA VHGCQTAFET SGIQLPIVCH VTVETTGTML LGSEIGAALT AIEPLNVDMI GLNCATGPDE MSEHLRYLSR NAHIPVSVMP NAGLPVLGKN GAEYPLTEQE LASALRGFVE EYGLSMVGGC CGTTPTHIRE VRKAVLGDSE HQPALQAERN PDVGDAVSSL YTSVNLTQDT GITMIGERTN ANGSKAFREA MLVGDLEKCV DIAKQQTRDG AHMLDLCVDY VGRDGTADMA QLASLLATSS TLPIMIDSTE PDVIQVGLEH LGGRCAVNSV NFEDGDGPDS RYQRIMRLVK RHGAAVVALT IDEEGQARTA EKKIEIAERL IADITSTWGL DESDIIVDTL TFPISTGQEE TRRDGIETIE AIRELKKRHP KIHTTLGLSN ISFGLNPAAR QVLNSVFLNE CIEAGLDSAI AHSSKIVPMN RIDEEQRRVA LDLVYDRRSE GYDPLQTFMR LFEGVSAASA SDARAEALAA MPLFKRIAQR IIDGEKAGFE DDLDAGMKEK EPLQIINEDL LEGMKTVGDL FGSGQMQLPF VLQSAETMKH AVAYLEQFIE ADEDAGDGNG TIVIATVKGD VHDIGKNLVD IILSNNGFNV VNIGIKQPIA NILEAAEKHK ADAIGMSGLL VKSTVIMKEN LQEMNQAQKS DYPVILGGAA LTRAYVEDDL TEVYEGNVHY AKDAFESLRL MQEFMAEARG ERLDPQSPEA LAAAKKKAER KARRERSKQI VAQRKAKEIP IEVPERSEVA ADVPIATPPF WGTRIVKGIN LSEYLPLLDE RALFVGRWGL KATRGGEGPS YEELVETEGR PRLRYWIDRL KAEKILDHAA VVYGYFPAVS EGDTVILLES PDPTSAEVAR FNFPRQQRGK FLCVADFIRS REHAIKTKTV DVFPLQLVTM GQPIADFANV LFADNNYRDY LEVHGIGVQL TEALAEYWHA RIRHELSLSD GSHAGDEDSA DLQEFFNLKY RGARYSFGYG SCPNLEDRET LVDLLDSRRI GVDISEEFQL HPEQSTDAFV LYHPEAKYFN V // ID Q6PBE1_XENTR Unreviewed; 307 AA. AC Q6PBE1; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 27-MAY-2015, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAH59753.1}; GN Name=MGC75760 {ECO:0000313|EMBL:AAH59753.1}; OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; OC Silurana. OX NCBI_TaxID=8364 {ECO:0000313|EMBL:AAH59753.1}; RN [1] {ECO:0000313|EMBL:AAH59753.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Embryo {ECO:0000313|EMBL:AAH59753.1}; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism. CC {ECO:0000256|PIRNR:PIRNR037505}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR037505, CC ECO:0000256|PIRSR:PIRSR037505-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (BhmT route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR037505}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR037505}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC059753; AAH59753.1; -; mRNA. DR RefSeq; NP_988891.1; NM_203560.1. DR UniGene; Str.3801; -. DR ProteinModelPortal; Q6PBE1; -. DR STRING; 8364.ENSXETP00000054282; -. DR GeneID; 394486; -. DR Xenbase; XB-GENE-5936142; -. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR HOVERGEN; HBG062720; -. DR UniPathway; UPA00051; UER00083. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037505, KW ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037505}; KW Transferase {ECO:0000256|PIRNR:PIRNR037505}; KW Zinc {ECO:0000256|PIRNR:PIRNR037505, ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 307 AA; 33335 MW; DD67544A388B72CE CRC64; MAETVKILSG GLSTELENSG FLLQGDPLWS ARLLQTNPQA IKNVHTSFLK SGAEVLSTAT YQASVKGFQE HLGLSIDEVA ELFHVGVRLA KEAAAEIKDN RNILIAGSIG PYGAFLSDGS EYTGNYLRNM SVEELKDWHR LQMQCLASAG IELFALETIP GQKEAEALLE LLREFPNTNA WLSYSCRDMS STSYGDAFEK AVGIAHKSKQ LVAVGMNCCP PTFVSSLLTS ANKNRGLDIG WIVYPNSGKI WDHNLGWQGG GTEKTLSEYA LEWVNLGAKW IGGCCTTTPS AIATLLQTLR PHAADLH // ID Q6R7M2_RHIFR Unreviewed; 1256 AA. AC Q6R7M2; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 01-APR-2015, entry version 58. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase 2 {ECO:0000313|EMBL:AAR99583.1}; GN Name=metH {ECO:0000313|EMBL:AAR99583.1}; OS Rhizobium fredii (Sinorhizobium fredii). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=380 {ECO:0000313|EMBL:AAR99583.1}; RN [1] {ECO:0000313|EMBL:AAR99583.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=RT19 {ECO:0000313|EMBL:AAR99583.1}; RX PubMed=15451112; DOI=10.1016/j.femsle.2004.08.029; RA Jiang J.Q., Wei W., Du B.H., Li X.H., Wang L., Yang S.S.; RT "Salt-tolerance genes involved in cation efflux and osmoregulation of RT Sinorhizobium fredii RT19 detected by isolation and characterization RT of Tn5 mutants."; RL FEMS Microbiol. Lett. 239:139-146(2004). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AY509252; AAR99583.1; -; Genomic_DNA. DR ProteinModelPortal; Q6R7M2; -. DR SMR; Q6R7M2; 668-916. DR PRIDE; Q6R7M2; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AAR99583.1}; KW Transferase {ECO:0000313|EMBL:AAR99583.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 262 262 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 325 325 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 326 326 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 778 778 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1256 AA; 137930 MW; 6BBD464C980A3B70 CRC64; MPAAAFLFGD VSPKPDGSEI FRVLRQATAG RILIMDGAMG TEIQQLGLAE DHFRGDRFGG CSCHQQGNND LLTLTQPKAI EDIHYRYAIA GADILETNTF SSTRIAQADY GMEDMVYELN RDGARLARRA AKRAEAEDGR RRFVAGALGP TNRTASISPD VNNPGYRAVT FDDLRLAYAE QVHGLIDGGA DIILIETVFD TLNAKAAIFA TQEIFAEKGV RLPIMISGTI TDLSGRTLSG QTSEAFWYSV RHAEPFTIGL NCALGANAMR AHIDELSSVA DTLICAYPNA GLPNEFGRYD ESPEAMAAQI EGFARDGLVN IVGGCCGSTP DHIRAIAEAV EKYPPREIPQ IERRMRLSGL EPFTFTDEIP FVNVGERTNV TGSAKFRKLI TAGDYAAALD VARDQVANGA QIIDVNMDEG LIDSKQVMVE FLNLVASEPD IARVPVMIDS SKWEVIEAGL QCVQGKALVN SISLKEGEEA FLDHARLVRA YGAAVVVMAF DEKGQADTKA RKVEICTRAY RLLTENVGFP PEDIIFDPNI FAVATGIEEH NNYGVDFIEA AHEIIASLPH VHVSGGVSNL SFSFRGNEPV REAMHAVFLY HAIQAGMDMG IVNAGQLAVY DAIDPDLREA CEDVVLNRRA DATERLLEVA KGYRGQGGAQ GREKDLAWRQ WSVEKRLEHA LVNGITEFIE ADTEEARRAA ERPLHVIEGP LMAGMNVVGD LFGAGKMFLP QVVKSARVMK QAVAVLLPYM EVEKAANGGD ARESAGKILM ATVKGDVHDI GKNIVGVVLA CNNYEIIDLG VMVPSARILE VAREQKVDAI GLSGLITPSL DEMVHVASEL EREGFDIPLL IGGATTSRVH TAVKINPRYT LGQTVYVTDA SRAVGVVSSL MSPEAREAYQ ETVRAEYLKV AEAHARNEAE KRRLPLSKAR ANAHRLDWDA YRPKTPSFLG TRVFESWDLA ELARYIDWTP FFQAWELKGV YPRILADEKQ GAAARQLFDD AQAMVAKIVA EKWFAPKAVV GFWPAGSIGD DIRLFTDENR RSELATLFTL RQQLAKRDGR PNVALSDFVA PAESGRGDYV GGFVVTAGIE EVALAERFER ANDDYSSIMV KALADRFAEA FAERMHEYVR KELWAYAPEE AFTPEELIAE PYRGIRPAPG YPAQPDHTEK ETLFRLLDAE AAIGVKLTES FAMWPGSSVS GLYIGHPDAY YFGVAKIERD QVEDYAQRKR MGVHEAERWL SPILNYVPMP ETQAAE // ID Q6TGQ4_CAVPO Unreviewed; 355 AA. AC Q6TGQ4; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 04-MAR-2015, entry version 44. DE SubName: Full=Betaine-homocysteine S-methyltransferase {ECO:0000313|EMBL:AAR08188.1}; DE Flags: Fragment; OS Cavia porcellus (Guinea pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; OC Hystricognathi; Caviidae; Cavia. OX NCBI_TaxID=10141 {ECO:0000313|EMBL:AAR08188.1}; RN [1] {ECO:0000313|EMBL:AAR08188.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=15331385; DOI=10.1152/ajpregu.00406.2004; RA Delgado-Reyes C.V., Garrow T.A.; RT "High sodium chloride intake decreases betaine-homocysteine S- RT methyltransferase expression in guinea pig liver and kidney."; RL Am. J. Physiol. Regul. Integr. Comp. Physiol. 288:R182-R187(2005). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY398694; AAR08188.1; -; mRNA. DR ProteinModelPortal; Q6TGQ4; -. DR STRING; 10141.ENSCPOP00000020430; -. DR eggNOG; COG0646; -. DR HOGENOM; HOG000231636; -. DR HOVERGEN; HBG080367; -. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:AAR08188.1}; KW Transferase {ECO:0000313|EMBL:AAR08188.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 182 182 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 264 264 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 265 265 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT NON_TER 1 1 {ECO:0000313|EMBL:AAR08188.1}. FT NON_TER 355 355 {ECO:0000313|EMBL:AAR08188.1}. SQ SEQUENCE 355 AA; 39118 MW; 397D0A11B369DD6B CRC64; RGYVKAGPWT PKAASEHPEA VRQLHGEFLR AGSNVMQTFT FYASEDKLEN RGNYVAEKIS GQKVNEAACD IARQVAEEGD ALVAGGVSQT PSYLSCKSES EVKKIFQQQL EVFMKKNVDF LIAEYFEHVE EAVWAVEALK ASGKPVAATM CIGPEGDLHG VSPGECAVRL VRAGASIVGV NCHFDPTTSL QTVKLMKQGL TAARLKAHLM CQPLAYHTPD CGKQGFIDLP EFPFGLEPRV ATRWDIQKYA REAYELGVRY IGGCCGFEPY HIRAIAEELA PERGFLPPAS EKHGGWGSGL DMHTKPWIRA RARKEYWQSL RIASGRPYNP ALSKPDAWGV TKGTTELMQQ KEATT // ID Q6W1U6_RHISN Unreviewed; 302 AA. AC Q6W1U6; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 27-MAY-2015, entry version 67. DE SubName: Full=Homocysteine S-methyltransferase (S-methylmethionine) {ECO:0000313|EMBL:AAQ87272.1}; DE EC=2.1.1.- {ECO:0000313|EMBL:AAQ87272.1}; DE SubName: Full=Predicted MHT1, Homocysteine/selenocysteine methylase {ECO:0000313|EMBL:ACP21810.1}; GN OrderedLocusNames=NGR_b03460 {ECO:0000313|EMBL:ACP21810.1}; GN ORFNames=RNGR00499 {ECO:0000313|EMBL:AAQ87272.1}; OS Rhizobium sp. (strain NGR234). OG Plasmid megaplasmid 2 {ECO:0000313|EMBL:AAQ87272.1}, OG Plasmid pNGR234b {ECO:0000313|EMBL:ACP21810.1}, and OG Plasmid sym pNGR234b {ECO:0000313|Proteomes:UP000001054}. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=394 {ECO:0000313|EMBL:AAQ87272.1, ECO:0000313|Proteomes:UP000001054}; RN [1] {ECO:0000313|EMBL:AAQ87272.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NGR234 {ECO:0000313|EMBL:AAQ87272.1}; RC PLASMID=megaplasmid 2 {ECO:0000313|EMBL:AAQ87272.1}; RA Broughton W.J., Perret X., Staehelin C., Schmitz R.A., Raasch C., RA Liesegang H., Gottschalk G., Streit W.R.; RT "Comparative DNA analysis of two large contigs of the Rhizobium sp. RT NGR234 megaplasmid 2."; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000001054} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NGR234 {ECO:0000313|Proteomes:UP000001054}; 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 [3] {ECO:0000313|EMBL:ACP21810.1, ECO:0000313|Proteomes:UP000001054} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NGR234 {ECO:0000313|EMBL:ACP21810.1, RC ECO:0000313|Proteomes:UP000001054}; RC PLASMID=pNGR234b {ECO:0000313|EMBL:ACP21810.1}; 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-Roeser 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; AY316747; AAQ87272.1; -; Genomic_DNA. DR EMBL; CP000874; ACP21810.1; -; Genomic_DNA. DR RefSeq; WP_012706409.1; NC_012586.1. DR RefSeq; YP_002822563.1; NC_012586.1. DR ProteinModelPortal; Q6W1U6; -. DR STRING; 394.NGR_b03460; -. DR EnsemblBacteria; ACP21810; ACP21810; NGR_b03460. DR GeneID; 7789882; -. DR KEGG; rhi:NGR_b03460; -. DR PATRIC; 32302314; VBIRhiSp122450_0792. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; PYVDVWL; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; SFRE394:GBYN-4042-MONOMER; -. DR Proteomes; UP000001054; Plasmid sym pNGR234b. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001054}; KW Methyltransferase {ECO:0000313|EMBL:AAQ87272.1}; KW Plasmid {ECO:0000313|EMBL:AAQ87272.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001054}; KW Transferase {ECO:0000313|EMBL:AAQ87272.1}. SQ SEQUENCE 302 AA; 32125 MW; 5EC207E3AAB086BC CRC64; MNQIRILDGG MSRELSRLGA ELRQPEWSAL ALMENPEIVG QVHREFIEAG ADVITTNSYA LVPFHIGEER FRSEGPSLTE LAGKLAREAA DGSADRKVLV AGSLPPIFGS YEPERFDPSR VQDYLKVLVE GLAPYVDVWL GETLSLIAEG DAVRAAVAAT GKPFWVSFTL ADDAEALASD MPKLRSGESV AAAADWAAGS GAEALLFNCS RPEVMAGAVA AAAATFRQRQ ANIGIGVYAN AFEAEETDGA ANETLHHTRA DLTADRYSRF ACDWVEAGAS IVGGCCGIGA RHIHNLAYSL KG // ID Q72BP9_DESVH Unreviewed; 804 AA. AC Q72BP9; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 27-MAY-2015, entry version 84. DE SubName: Full=Vitamin B12-dependent methionine synthase family protein {ECO:0000313|EMBL:AAS96063.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AAS96063.1}; GN OrderedLocusNames=DVU_1585 {ECO:0000313|EMBL:AAS96063.1}; OS Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB OS 8303). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=882 {ECO:0000313|EMBL:AAS96063.1, ECO:0000313|Proteomes:UP000002194}; RN [1] {ECO:0000313|EMBL:AAS96063.1, ECO:0000313|Proteomes:UP000002194} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hildenborough / ATCC 29579 / NCIMB 8303 RC {ECO:0000313|Proteomes:UP000002194}; 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 ----------------------------------------------------------------------- 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; AAS96063.1; -; Genomic_DNA. DR RefSeq; WP_010938876.1; NC_002937.3. DR RefSeq; YP_010804.1; NC_002937.3. DR ProteinModelPortal; Q72BP9; -. DR STRING; 882.DVU1585; -. DR EnsemblBacteria; AAS96063; AAS96063; DVU_1585. DR GeneID; 2796021; -. DR KEGG; dvu:DVU1585; -. DR PATRIC; 32062968; VBIDesVul119526_1461. DR eggNOG; COG1410; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR PhylomeDB; Q72BP9; -. DR BioCyc; DVUL882:GJIL-1621-MONOMER; -. DR Proteomes; UP000002194; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002194}; KW Methyltransferase {ECO:0000313|EMBL:AAS96063.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002194}; KW Transferase {ECO:0000313|EMBL:AAS96063.1}. SQ SEQUENCE 804 AA; 84255 MW; 878E61D320CEAAF1 CRC64; MPDFRQALRA GRRLLFDGGL GTMLQARGLP AGVSPEQFCL DRPDVLRGIH ADYVRAGADI LTTNTFGGSR FKLGDGFDVV DFNRRMAAIA REAADASGRQ AFVAGSIGPT GHFVKPLGEV EPAALVAAFR EQVRGLVAGG ADLLMIETQF DLAEARAAVV AARAECSLPI AVSMTFENGV SLTGSTPEVF VATMLNLGVD LLGTNCSAGP DQMHDVVASL LASASVPVLV EPNAGLPELI DGKTVFRLPP APFAEKTAAF AAMGARVLGG CCGTTPDHIA ALRQAVADIP ATLPVDSGVG IVLTTRSHLV RVGGDAPVRI IGERINPTGK KQLIAELQAG DFSLALRFSD EQVEAGAPIL DVNVGAPMVD EEVLLPDLVQ RLITRHGVPL SIDSSNAAAI ERALPYCPGS TLVNSISGEP GRMERLGPLC RDHGAPFILL PLKGRKLPVA ATERIAIIEE LLVQAEGLGI PRRLVMVDVL ALAVSSKAEA ARQCLETIRW CTANGFATTI GLSNISFGLP ARELLNGTFL AMAAGAGLSS CIAHPGNGRI RETVACADVL LARDANAERF IDAYAAWTPA TQGGPVASGP GLASQPPATT LEEAVVKGDR DGVTAIVESE LAAGADPFDL VQTKLIPAIN EVGVKYERRE YFLPQLIRSA ETMQTAFRRL QPLLEEMRGA EVRPVIIMAT VEGDIHDIGK NIVSLMLGNH GFEVVDLGKD VKAETIVDAA ETHGARIIGL SALMTTTMVR MEDTVKLVRA RGLDVKVIVG GAVVTKAFAD AIGADGYSAD AVEAVRLAKS LLAG // ID Q72L12_THET2 Unreviewed; 1184 AA. AC Q72L12; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 27-MAY-2015, entry version 84. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|EMBL:AAS80601.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AAS80601.1}; GN OrderedLocusNames=TT_C0253 {ECO:0000313|EMBL:AAS80601.1}; OS Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039). OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; OC Thermus. OX NCBI_TaxID=262724 {ECO:0000313|EMBL:AAS80601.1, ECO:0000313|Proteomes:UP000000592}; RN [1] {ECO:0000313|EMBL:AAS80601.1, ECO:0000313|Proteomes:UP000000592} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HB27 / ATCC BAA-163 / DSM 7039 RC {ECO:0000313|Proteomes:UP000000592}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AE017221; AAS80601.1; -; Genomic_DNA. DR RefSeq; WP_011172704.1; NC_005835.1. DR RefSeq; YP_004228.1; NC_005835.1. DR ProteinModelPortal; Q72L12; -. DR STRING; 262724.TTC0253; -. DR EnsemblBacteria; AAS80601; AAS80601; TT_C0253. DR KEGG; tth:TTC0253; -. DR PATRIC; 23950903; VBITheThe54392_0254. DR eggNOG; COG1410; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; TTHE262724:GCAT-259-MONOMER; -. DR Proteomes; UP000000592; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000592}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AAS80601.1}; KW Transferase {ECO:0000313|EMBL:AAS80601.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 255 255 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 760 760 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1184 AA; 130822 MW; 3034CB8BDBBD99BA CRC64; MEVHACSPGC RHHLGGAGWG DAPLVRLGYN KEARAKKFPY LKALLERPLV FDGAMGTELQ KRDLTPEDYG GEAYFGCPEV LNRTRPEVVR EIHLAYLEAG AEVIETNTFG ALRHVLAEYG LEEAAEELAF LGARIAREAA DPYGAFVAGA LGPGTKLVSL GQISWDALYR AYKEAARGLL KGGVDLILLE TAQDILQVRC AVLAVREAMA EVGREVPLQV QVTFEATGTM LVGTDEQAAL AALESLPVDV VGMNCATGPD LMDSKVRYFA EHSTRFVSCL PNAGLPRNEG GRVVYDLTPE ELAKWHLKFV AEYGVNAVGG CCGTGPEHIR KVAEAVKGLA PKPRPESFPP QVASLYQAVS LKQEASLFLV GERLNATGSK RFREMLFARD LEGILALARE QVEEGAHALD LSVAWTGRDE LEDLRWLLPH LATALTVPVM VDSTSPEAME LALKYLPGRV LLNSANLEDG LERFDRVASL AKAHGAALVV LAIDEKGMAK TREEKVRVAL RMYERLTEHH GLRPEDLLFD LLTFPITQGD EESRPLAKET LLAIEELRER LPGVGFVLGV SNVSFGLKPR ARRVLNSVFL DEARKRGLTA AIVDAGKILP ISQIPEEAYA LALDLIYDRR KEGFDPLLAF MAYFEAHKED PGKREDAFLA LPLLERLKRR VVEGRKQGLE ADLEEALKAG HKPLDLINGP LLAGMKEVGD LFGAGKMQLP FVLQAAEVMK RAVAYLEPHM EKKGEGKGTL VLATVKGDVH DIGKNLVDII LSNNGYRVVN LGIKVPIEEI LKAVEAHKPH AVGMSGLLVK STLVMKENLE YMRDRGYTLP VILGGAALTR SYVEELKAIY PNVYYAEDAF EGLRLMEELT GHAPPELTRK APARPKREAP KVAPRARPVG EAPAVPRPPF FGVRVEEGLD LATIAHYVNK LALYRGQWGY SRKGLSREAW QALVEREAEP VFQRLLKEAM AEGWLEPKVL YGFFPVAREG EELLVFSPET GEVLERFRFP RQRGGGLSLV DYFRPRFAAP LGDEADWMPK EAFRAGARDV LGVQLVTMGE APSRKAQALF ASGAYQDYLF VHGFSVEMTE ALAEYWHKRM RQMWGIAHKD ATEIQKLFQQ GYQGARYSFG YPACPDLADQ AKLDRLMGFH RVGVHLTENF QLEPEHATSA LVVHHPEARY FSVD // ID Q730T3_BACC1 Unreviewed; 610 AA. AC Q730T3; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 27-MAY-2015, entry version 76. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=BCE_4333 {ECO:0000313|EMBL:AAS43234.1}; OS Bacillus cereus (strain ATCC 10987 / NRS 248). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=222523 {ECO:0000313|EMBL:AAS43234.1, ECO:0000313|Proteomes:UP000002527}; RN [1] {ECO:0000313|EMBL:AAS43234.1, ECO:0000313|Proteomes:UP000002527} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10987 / NRS 248 {ECO:0000313|Proteomes:UP000002527}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; AAS43234.1; -; Genomic_DNA. DR RefSeq; NP_980626.1; NC_003909.8. DR RefSeq; WP_000770327.1; NC_003909.8. DR ProteinModelPortal; Q730T3; -. DR STRING; 222523.BCE_4333; -. DR EnsemblBacteria; AAS43234; AAS43234; BCE_4333. DR KEGG; bca:BCE_4333; -. DR PATRIC; 18857299; VBIBacCer118379_4148. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR KO; K00548; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR Proteomes; UP000002527; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome; FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:AAS43234.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Transferase {ECO:0000313|EMBL:AAS43234.1}. SQ SEQUENCE 610 AA; 67212 MW; 48A297C981AB67AB CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNISDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTE INRAAVKLAK ASVTDRNAIL GTIGGMKHIG AVTTTDMERE FMLLEQASAL LEEQVDGLLL ETFYDEFELL HAVQVLRKET NIPIVAQLAL HEAGTTQNGN DVNEILKQLL DYGANVVGLN CQLGPLHMTE AFKMISIPKN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPKFIEQGI RLLGGCCGTT PEHIESMKRA TLNVMPVIEK DTVQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRISNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSVL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIA LIEEVYEATK HLEQPIFIGI MPLISKRNAD FLHFEVPGIT LPEAVRERMD GHETKEAAIE EGIRISQELI DAAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID Q730T4_BACC1 Unreviewed; 1132 AA. AC Q730T4; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 27-MAY-2015, entry version 91. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AAS43233.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AAS43233.1}; GN Name=metH {ECO:0000313|EMBL:AAS43233.1}; GN OrderedLocusNames=BCE_4332 {ECO:0000313|EMBL:AAS43233.1}; OS Bacillus cereus (strain ATCC 10987 / NRS 248). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=222523 {ECO:0000313|EMBL:AAS43233.1, ECO:0000313|Proteomes:UP000002527}; RN [1] {ECO:0000313|EMBL:AAS43233.1, ECO:0000313|Proteomes:UP000002527} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10987 / NRS 248 {ECO:0000313|Proteomes:UP000002527}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AE017194; AAS43233.1; -; Genomic_DNA. DR RefSeq; NP_980625.1; NC_003909.8. DR RefSeq; WP_000649694.1; NC_003909.8. DR ProteinModelPortal; Q730T4; -. DR STRING; 222523.BCE_4332; -. DR EnsemblBacteria; AAS43233; AAS43233; BCE_4332. DR KEGG; bca:BCE_4332; -. DR PATRIC; 18857297; VBIBacCer118379_4147. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; ILESWIT; -. DR OrthoDB; EOG6091CH; -. DR Proteomes; UP000002527; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; Complete proteome; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AAS43233.1}; KW Transferase {ECO:0000313|EMBL:AAS43233.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 125868 MW; 9293C3AE71DF6156 CRC64; MKCIEEKLQN NILILDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYELSHLDE ELNEKAARLA KQAVEESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGE VDVLLVETSQ DMRNVKAAYI GIQAAFDELN TIVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWVN IIGGCCGTTP EHIKAMKSAL TSLKPREQQE RAGHGVSGLE ALQYDDSMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEI ARAQVKKNAH IIDICMADPD RDEIEDMENF LAEVTKVLKV PIMIDSTDEH VMERALTYIQ GKAVINSINL EDGEERFKKV TPLLRKYGAA IVVGTIDEDG MAVSAERKLE IAKRSYELLT TKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPDE EKRLADALLF ETTQETLEKF TNFYRVAKKK DVVVQETLTL DERLANYIVE GTKQGLHEDL SLALTEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILA NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAADIDIPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV TKEEKKVEIP AVIEPLPKAE VIVPDSTKRI VLRDVPVSHL APFLNRQMLL GHHLGLKGSV KKLLREGDKR AHELNDLIDE LLQEGQSWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRVIE RFTFPRQGKA PYRTLGDYLR PVGDEMDYVA FLSVTVGEGV RDIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID Q73XN0_MYCPA Unreviewed; 306 AA. AC Q73XN0; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 29-APR-2015, entry version 56. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAS04596.1}; GN OrderedLocusNames=MAP_2279 {ECO:0000313|EMBL:AAS04596.1}; 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 {ECO:0000313|EMBL:AAS04596.1, ECO:0000313|Proteomes:UP000000580}; RN [1] {ECO:0000313|EMBL:AAS04596.1, ECO:0000313|Proteomes:UP000000580} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-968 / K-10 {ECO:0000313|Proteomes:UP000000580}; 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 ----------------------------------------------------------------------- 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; AAS04596.1; -; Genomic_DNA. DR RefSeq; NP_961213.1; NC_002944.2. DR RefSeq; WP_010949546.1; NC_002944.2. DR ProteinModelPortal; Q73XN0; -. DR STRING; 262316.MAP2279; -. DR EnsemblBacteria; AAS04596; AAS04596; MAP_2279. DR KEGG; mpa:MAP2279; -. DR PATRIC; 17997202; VBIMycAvi108102_2425. DR KO; K00547; -. DR OMA; YGRSVTK; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; MAVI262316:GCQR-2305-MONOMER; -. DR Proteomes; UP000000580; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000580}; KW Reference proteome {ECO:0000313|Proteomes:UP000000580}. SQ SEQUENCE 306 AA; 31969 MW; EFABFD12DD79E7B0 CRC64; MGSARGFTWP SDPVLLDGGL ATELEARGHD LSDPLWSARL LADAPQEIVA VHAAYFRAGA MIATTASYQA SFEGFAARGI SRSDTAGLLR RSVELAKAAR DEAGVAGHVA ASVGPYGAAL ADGSEYRGRY GISVRQLEDW HRPRLEVLAG ADADVLAVET IPDVDEAEAL VNLVRSLGVP AWLSYTIDGA HTRAGQPLAD AFAVAAGVPE IVAVGVNCCA PDDVLPTIEI AAAIGKPVIV YPNSGEHWNA LRHNWTGPSR FSAPLAARWI SAGARIVGGC CQVRPTDIAA VRRACSDGEN SAKKSP // ID Q73YU6_MYCPA Unreviewed; 1262 AA. AC Q73YU6; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 27-MAY-2015, entry version 79. DE SubName: Full=MetH {ECO:0000313|EMBL:AAS04176.1}; GN Name=metH {ECO:0000313|EMBL:AAS04176.1}; GN OrderedLocusNames=MAP_1859c {ECO:0000313|EMBL:AAS04176.1}; 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 {ECO:0000313|EMBL:AAS04176.1, ECO:0000313|Proteomes:UP000000580}; RN [1] {ECO:0000313|EMBL:AAS04176.1, ECO:0000313|Proteomes:UP000000580} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-968 / K-10 {ECO:0000313|Proteomes:UP000000580}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AE016958; AAS04176.1; -; Genomic_DNA. DR RefSeq; NP_960793.1; NC_002944.2. DR RefSeq; WP_010949381.1; NC_002944.2. DR ProteinModelPortal; Q73YU6; -. DR SMR; Q73YU6; 671-1261. DR STRING; 262316.MAP1859c; -. DR EnsemblBacteria; AAS04176; AAS04176; MAP_1859c. DR GeneID; 2721534; -. DR KEGG; mpa:MAP1859c; -. DR PATRIC; 17996282; VBIMycAvi108102_1969. DR KO; K00548; -. DR OMA; QPFFNAW; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; MAVI262316:GCQR-1881-MONOMER; -. DR Proteomes; UP000000580; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000580}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000580}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 267 267 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 330 330 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 331 331 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 788 788 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1262 AA; 138473 MW; 4421F7F99F9CBCDF CRC64; MEGVHVTAPV TTPASDSFAP NIRPDCTDEL TAALRQRIMV IDGAMGTAIQ RDRPDEAGYR GERFKDWPSD LVGNNDLLNL TQPQIIEGIH REYLEAGADI LETNTFNANA ISLSDYGMEE LSYELNYAGA ALARKAADEF STPDKPRYVA GALGPTSRTA SISPDVNDPG ARNVTYDELV AAYLEAANGL VDGGVDLLIV ETIFDTLNAK AAVFALETLF EQRGRRWPVI ISGTITDASG RTLSGQVTEA FWNSIRHAKP IAVGLNCALG APEMRPYIAE VSRIADTFVS CYPNAGLPNA FGEYDESPER QASYIADFTE AGLVNLVGGC CGTAPPHIAE IAKVVEGKPP REVPQIPVAT RLSGLEPLNI TDDSLFVNIG ERTNITGSAR FRNLIKAEDY DTALSVALQQ VEVGAQVIDI NMDEGMIDGV AAMDRFTRLI AAEPDISRVP VMIDSSKWEV IEAGLKNVQG KPIVNSISLK EGEEKFVREA RLCRKYGAAV VVMAFDEQGQ ADNLERRKQI CARAYRVLTE EVGFPPEDII FDPNCFALAT GIEEHATYGI DFIEACAWIK ENLPGVHLSG GISNVSFSFR GNNPVREAIH SVFLFHAIKA GLDMGIVNAG ALVPYDSIDP ELRDRIEDVV LNRREDAAER LLEIAERFNK SADASEDSAA AEWRGLPVRE RITHALVKGI DAHVDEDTEE LRAEIAAAGG RPIEVIEGPL MDGMNVVGDL FGSGKMFLPQ VVKSARVMKK AVAYLLPFIE AEKEESGVSG SKDTNGTIVM ATVKGDVHDI GKNIVGVVLQ CNNFEVIDLG VMVPAQKILD AAKEHDADII GLSGLITPSL DEMSNFAAEM EREGLQIPLL IGGATTSRAH TAVKISPRRS GPVVWVKDAS RSVPVAAALL DDKQRPALLE ATEKDYASLR ERHAQKNERP MVTLEKARAN RTPIDWDGYT PPVPAIGAGI REFQDYDLAE LREYIDWQPF FNAWEMKGRF PDILNNPATG EAARKLYDDA QEMLDTLIEE KWLTPNAVIG FFPANAIGPG FEDIELYTDD TRTEVLTTLH NLRQQGEHRD GIPNRSLGDF IAPKETGHRD YIGAFAVTAG LGSQEKIAEF KAALDDYSAI LLESIADRLA EAFAERMHQR VRKEFWGYQP DEQLDNDALI DEKYRGIRPA PGYPACPEHT EKVTLWKLMD VKERTGIELT ESMAMWPGAA VSGWYFSHPQ SQYFVVGRLA QDQVADYAKR KGWTLAEAER WLAPNLGYNP ED // ID Q748M7_GEOSL Unreviewed; 605 AA. AC Q748M7; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 29-APR-2015, entry version 76. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN Name=metF-2 {ECO:0000313|EMBL:AAR36366.1}; GN OrderedLocusNames=GSU2974 {ECO:0000313|EMBL:AAR36366.1}; OS Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=243231 {ECO:0000313|EMBL:AAR36366.1, ECO:0000313|Proteomes:UP000000577}; RN [1] {ECO:0000313|EMBL:AAR36366.1, ECO:0000313|Proteomes:UP000000577} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51573 / DSM 12127 / PCA RC {ECO:0000313|Proteomes:UP000000577}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {ECO:0000256|RuleBase:RU004255}. CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; AAR36366.1; -; Genomic_DNA. DR RefSeq; NP_954016.1; NC_002939.5. DR RefSeq; WP_010943603.1; NC_002939.5. DR ProteinModelPortal; Q748M7; -. DR STRING; 243231.GSU2974; -. DR EnsemblBacteria; AAR36366; AAR36366; GSU2974. DR GeneID; 2687368; -. DR KEGG; gsu:GSU2974; -. DR PATRIC; 22028805; VBIGeoSul17553_3000. DR HOGENOM; HOG000028409; -. DR InParanoid; Q748M7; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; GSUL243231:GH27-3013-MONOMER; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000000577; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004255}; KW Complete proteome {ECO:0000313|Proteomes:UP000000577}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:AAR36366.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000000577}; KW Transferase {ECO:0000313|EMBL:AAR36366.1}. SQ SEQUENCE 605 AA; 65048 MW; 0EAB8C20B5B3FC02 CRC64; MTFLERLHDE VLIGDGAIGT MLYAKGVSLD ANVEHLNLVR PSLVLELHRE YLAAGARVIE TNTFGANWTR LAAIGLEKKE REINLRGAQL AREAAQGTDA FVAGSVGPLV RMKGDEQELS AQETVDIFRR QTHALAEGEV DLLILETFTD LAQMRHALTA ARETGLPVVA NMAFLENGRL AGGIEVERVA VELTAAGACV VGANCGAGPL EILGTIQRMG RVTDLPLAAY PNSGFPEYVN GRHVYRTTPD YFADRAVEMV GAGAALVGGC CGTTPEHVRC LAQRLAGLRP AARTVAVSAL PKDERRPESR EYAGFLARWG REPIVTVELD PPKGLDCAKI IEGSRALREA GADAINIAEN PLARIRMGNI ALGSLIQREA GIDVIVHVTC RDRNLLGLQS DLMGASLLGI RHVLAVTGDP ARIGEQAGAT SVYDLNSFGL IKLLADLNAG VNALGSPIGG GTGFVIGAAF NPNSARMEVQ VERLARKVAN GARFVQTQPL YDVARLEEMA ERTAHLGIPI LPGILPLVSE RNCEFLHNEV PGIVIPEEIR HRMRGKEKED GVREGLAIAR EFIDAVRDRV GGFYLIPPFG KYGIAVELTR YIKGT // ID Q748T0_GEOSL Unreviewed; 804 AA. AC Q748T0; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 27-MAY-2015, entry version 76. DE SubName: Full=5-methyltetrahydrofolate--homocysteine S-methyltransferase, cobalamin-dependent {ECO:0000313|EMBL:AAR36313.1}; GN Name=metH {ECO:0000313|EMBL:AAR36313.1}; GN OrderedLocusNames=GSU2921 {ECO:0000313|EMBL:AAR36313.1}; OS Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=243231 {ECO:0000313|EMBL:AAR36313.1, ECO:0000313|Proteomes:UP000000577}; RN [1] {ECO:0000313|EMBL:AAR36313.1, ECO:0000313|Proteomes:UP000000577} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51573 / DSM 12127 / PCA RC {ECO:0000313|Proteomes:UP000000577}; 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 ----------------------------------------------------------------------- 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; AAR36313.1; -; Genomic_DNA. DR RefSeq; NP_953963.1; NC_002939.5. DR RefSeq; WP_010943552.1; NC_002939.5. DR ProteinModelPortal; Q748T0; -. DR STRING; 243231.GSU2921; -. DR EnsemblBacteria; AAR36313; AAR36313; GSU2921. DR GeneID; 2688532; -. DR KEGG; gsu:GSU2921; -. DR PATRIC; 22028701; VBIGeoSul17553_2948. DR HOGENOM; HOG000251408; -. DR InParanoid; Q748T0; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; GSUL243231:GH27-2962-MONOMER; -. DR Proteomes; UP000000577; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000577}; KW Methyltransferase {ECO:0000313|EMBL:AAR36313.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000577}; KW Transferase {ECO:0000313|EMBL:AAR36313.1}. SQ SEQUENCE 804 AA; 84670 MW; C43223BB1D30FB97 CRC64; MKQPFLQAIA ERVLVLDGAM GTMLQERGLR PGQSPEELNL TLPEVVAGVH REYLDAGADI IVTNTFGGSR AKLEHYGLQD RVAEINARAV AIAREVCGDR AYVAASIGPT GQFVEPVGDV SFDEMAAIFR EQAQALINAG ADLITLETFL DIKEIRAAVI AIREISPETP VIAQLTFDNE GRTVLGTSPE AAAVTLEAAG ADIVGSNCGL GPDGICDVMA AMRRVTRLPL ISQANAGLPT LVDGATVFPG TPDDMTAFHD RLLDLNVRVI GGCCGTTPAH IRAIREALAL RDQSLRACGP AEGVTFLSSR TTVVAIGAGL PAAIIGERIN PTGKKGFAQE LQDGKVSYIR REALEQTARG AVLLDVNVGT PGIDEPAAME RAVVTVATAV GAPLVLDSSD PAALERGLKA ADGKVLLNSV NGEAKSMERV LPLARKYGAA VIGLALDETG IPETAEGRLA VAERIVKAAG KAGIRRPDVV IDCLTLTVSA EQKRAMETLR AVRLVKERLG CPTVLGVSNI SFGLPRRPLI SSAFFAMALA AGLDAAIVNP KEEEMMAAWH SSMVLLNRDP NAAAYIAAYA GVAPPAAEPA ATGELPDIRQ RLARAVITGD GEGIVSLVEE ALSHGLEPLQ VSNEGLLPGL EEVGRRFEKN QVFLPQVMQS AEAMQAAFAR LKQEMTGEAE SKGTILMATV EGDIHDIGKN IVCTLLENHG FRVIDLGKNV PADRIVAEAE RNGADAVGLS ALMTTTMTEM ENVLARLRAA GIRTFTMVGG AVVTQEYADR IGADLYARDA MDAVARIKAL LGVD // ID Q74DI9_GEOSL Unreviewed; 318 AA. AC Q74DI9; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 04-MAR-2015, entry version 55. DE SubName: Full=Homocysteine S-methyltransferase domain protein {ECO:0000313|EMBL:AAR34703.1}; GN OrderedLocusNames=GSU1327 {ECO:0000313|EMBL:AAR34703.1}; OS Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=243231 {ECO:0000313|EMBL:AAR34703.1, ECO:0000313|Proteomes:UP000000577}; RN [1] {ECO:0000313|EMBL:AAR34703.1, ECO:0000313|Proteomes:UP000000577} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51573 / DSM 12127 / PCA RC {ECO:0000313|Proteomes:UP000000577}; 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 ----------------------------------------------------------------------- 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; AAR34703.1; -; Genomic_DNA. DR RefSeq; NP_952380.1; NC_002939.5. DR RefSeq; WP_010941981.1; NC_002939.5. DR ProteinModelPortal; Q74DI9; -. DR STRING; 243231.GSU1327; -. DR EnsemblBacteria; AAR34703; AAR34703; GSU1327. DR GeneID; 2688050; -. DR KEGG; gsu:GSU1327; -. DR PATRIC; 22025429; VBIGeoSul17553_1324. DR HOGENOM; HOG000179103; -. DR InParanoid; Q74DI9; -. DR OMA; CGLMSCR; -. DR OrthoDB; EOG6R5C46; -. DR BioCyc; GSUL243231:GH27-1336-MONOMER; -. DR Proteomes; UP000000577; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000577}; KW Methyltransferase {ECO:0000313|EMBL:AAR34703.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000577}; KW Transferase {ECO:0000313|EMBL:AAR34703.1}. SQ SEQUENCE 318 AA; 33667 MW; 67885D916C1A8148 CRC64; MTDYVSFSAF LAESPVILGE GAVIERLRRA GVDLDPWLVN SALVYAPAGR AALATICREY LDIGARHDLP LLLSTPTWRA SRERIEAAGL AGSDVNGDNF RFLDELRRSY GAYGRKVLIC GLMSCRGDAY RPAEALSEDE AREFHSWQAD ALAAAGVDFL LAATLPALGE AVGLARAMAA TGMPHVVSFV VRPGGTLLDG TPLREAVAAL DAAVSPRPVA YLVNCTHASF FRSALLHEAN SSPLVRQRVV GLLANTAALS PEELDNAAEL VEESPGTFGR TVAALHRDLG MKVLGGCCGT DGRHIECLAA ELSGSPVR // ID Q753B4_ASHGO Unreviewed; 326 AA. AC Q753B4; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 2. DT 07-JAN-2015, entry version 69. DE SubName: Full=AFR410Wp {ECO:0000313|EMBL:AAS53781.2}; GN ORFNames=AGOS_AFR410W {ECO:0000313|EMBL:AAS53781.2}; 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 {ECO:0000313|EMBL:AAS53781.2, ECO:0000313|Proteomes:UP000000591}; RN [1] {ECO:0000313|EMBL:AAS53781.2, ECO:0000313|Proteomes:UP000000591} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056 RC {ECO:0000313|Proteomes:UP000000591}; 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., Pohlmann 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] {ECO:0000313|Proteomes:UP000000591} RP GENOME REANNOTATION. RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056 RC {ECO:0000313|Proteomes:UP000000591}; 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; AAS53781.2; -; Genomic_DNA. DR RefSeq; NP_985957.2; NM_211312.2. DR STRING; 33169.AGOS_AFR410W; -. DR EnsemblFungi; AAS53781; AAS53781; AGOS_AFR410W. DR GeneID; 4622230; -. DR KEGG; ago:AGOS_AFR410W; -. DR HOGENOM; HOG000066018; -. DR InParanoid; Q753B4; -. DR KO; K00547; -. DR OMA; YLNISEH; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000000591; Chromosome VI. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000591}; KW Reference proteome {ECO:0000313|Proteomes:UP000000591}. SQ SEQUENCE 326 AA; 36437 MW; 01DD1FDD688F060B CRC64; MAAKCAITEF LERNVLVMDG GMGVELERRG MDVKSPLWST APFLRGDRAA LDTIRGLYRE FRAAGSRGIS TLTYQASFHS MVKYSGSVSS RADYEKFLEQ VVDFTYRECV DPARDYIIGS VGPYAAFLCN GAEYTGDYGF ETINFFNYFE PQVSKFATDP RIDAIAFETV PNVVELMAML QPEFHALLKN KPFYISISAK DEHVLRDGTP LAVVGQLIRE RMDDLPPNLL CFGLNCVDLT RSAAMLAELN MQLQDCPIKF QAIYPNGTSV FDESLSAWRP SKDAESLTWA EAVKLYLNQD CRMIGGCCGT TPQDMRQIAE ALDVNM // ID Q75DZ8_ASHGO Unreviewed; 336 AA. AC Q75DZ8; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 01-APR-2015, entry version 71. DE SubName: Full=ABL125Wp {ECO:0000313|EMBL:AAS50646.1}; GN ORFNames=AGOS_ABL125W {ECO:0000313|EMBL:AAS50646.1}; 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 {ECO:0000313|EMBL:AAS50646.1, ECO:0000313|Proteomes:UP000000591}; RN [1] {ECO:0000313|EMBL:AAS50646.1, ECO:0000313|Proteomes:UP000000591} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056 RC {ECO:0000313|Proteomes:UP000000591}; 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., Pohlmann 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] {ECO:0000313|Proteomes:UP000000591} RP GENOME REANNOTATION. RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056 RC {ECO:0000313|Proteomes:UP000000591}; 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; AE016815; AAS50646.1; -; Genomic_DNA. DR RefSeq; NP_982822.1; NM_208175.1. DR ProteinModelPortal; Q75DZ8; -. DR STRING; 33169.AGOS_ABL125W; -. DR EnsemblFungi; AAS50646; AAS50646; AGOS_ABL125W. DR GeneID; 4618902; -. DR KEGG; ago:AGOS_ABL125W; -. DR HOGENOM; HOG000066018; -. DR InParanoid; Q75DZ8; -. DR KO; K00547; -. DR OMA; HIDYLAY; -. DR OrthoDB; EOG7X9GHR; -. DR Proteomes; UP000000591; Chromosome II. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000591}; KW Reference proteome {ECO:0000313|Proteomes:UP000000591}. SQ SEQUENCE 336 AA; 36166 MW; F9FE438EE86C664D CRC64; MPRIPIRQYL EEDPTRVLVM DGGQGTELEN RGIVVASPVW SAAPFLDAAA WQQPDSRERA IVASVLRDFV AAGAEVIMTI TYQASFTSVT TNTGITTLQD YNALLDRIVG FCRETVGDDK YLVGSIGAWG AHVCAEFTGD YGPRPDHIDY LAYFKPQLDN FNAQPALDLI GFETIPNAHE LRAILSWDES VIAKPFYVAL SVHDAGTLRD GTPMADVAAI VAAAAPLNPN FLGLGINCSS LSRTPAILAE LHALLPALPM TIYPNSGEIY DPVKKVWNAS PHVVDWGAVV ASYIRSGARI IGGCCRTIPN DIRQIADAVR THARASSTDV PGHASP // ID Q75FU6_LEPIC Unreviewed; 1247 AA. AC Q75FU6; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 27-MAY-2015, entry version 82. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AAS72114.1}; GN Name=metH {ECO:0000313|EMBL:AAS72114.1}; GN OrderedLocusNames=LIC_20085 {ECO:0000313|EMBL:AAS72114.1}; OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar OS copenhageni (strain Fiocruz L1-130). OC Bacteria; Spirochaetes; Spirochaetales; Leptospiraceae; Leptospira. OX NCBI_TaxID=267671 {ECO:0000313|EMBL:AAS72114.1, ECO:0000313|Proteomes:UP000007037}; RN [1] {ECO:0000313|EMBL:AAS72114.1, ECO:0000313|Proteomes:UP000007037} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Fiocruz L1-130 {ECO:0000313|EMBL:AAS72114.1, RC ECO:0000313|Proteomes:UP000007037}; RX PubMed=15028702; DOI=10.1128/JB.186.7.2164-2172.2004; RA Nascimento A.L.T.O., Ko A.I., Martins E.A.L., 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.M., Leite L.C.C., Carrer H., RA Coutinho L.L., Degrave W.M., Dellagostin O.A., El-Dorry H., RA Ferro E.S., Ferro M.I.T., Furlan L.R., Gamberini M., Giglioti E.A., RA Goes-Neto A., Goldman G.H., Goldman M.H.S., Harakava R., RA Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M., Kimura E.T., RA Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L., Nunes L.R., RA de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A., RA Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A., RA Camargo L.E.A., Kitajima J.P., Setubal J.C., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AE016824; AAS72114.1; -; Genomic_DNA. DR RefSeq; WP_000262613.1; NC_005824.1. DR RefSeq; YP_003477.1; NC_005824.1. DR ProteinModelPortal; Q75FU6; -. DR SMR; Q75FU6; 657-901. DR STRING; 267671.LIC20085; -. DR EnsemblBacteria; AAS72114; AAS72114; LIC_20085. DR KEGG; lic:LIC20085; -. DR PATRIC; 22380363; VBILepInt6257_4326. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; LINT267671:GHQI-3569-MONOMER; -. DR Proteomes; UP000007037; Chromosome II. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000007037}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 255 255 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 318 318 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 319 319 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 769 769 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1247 AA; 138768 MW; E55374595CEBC1B9 CRC64; MVYKVQNYTN PSSKELLSLL EKQILVIDGA MGTMIQRFSL QEEDFRGEIL KNHLHPLKGN NELLCLTRPD VIESIHLKFL EAGANIVETN TFSSNQISQG DYKTEFLVAD LNKAAVVCAR NAITKFQKTN PDHPCLIAGA IGPTTKTATL SPDVNNPAFR AVTFDDLVAT FYEQARALVE SGVDLLLPET NIDTLNLKAA IFAIEQVFED LQVRIPVCLS VTITDASGRT LSGQTVEAFY NSIAHCNPLS VGINCALGAD EMRPYIEELA RVSPCYISCY PNAGLPNAFG GYDQTPEEFG KYIQEFASSG WLNIAGGCCG TTPEHIEAAA KAVRGKKPRI LPKIEEVTRL SGLEPLNITP DKGFLLVGER TNVTGSPKFK KLIIEGNFEE AVSVALQQVE AGANIIDINF DEALLDGEAS MRHFLNLIAG EPDIAKVPFM IDSSKWSVLE EGLKCIQGKP ILNSISLKEG EDKFLEYAKK IQRYGASAIV MAFDEQGQAA TKEDKVRICK RAYDLLVTKA NFSPTDIIFD PNILTVATGI EEHNNYAVDF IEAVREIKKL CPGAKVSGGL SNVSFSFRGN NPVREAMHSV FLYYAIQAGM DMAIVNAGML AVYEEIPKDL LEYVEDVILN RRPDATERLV EFAESVKSTG DKTEKKEEAW REGTSVEERL SHALVKGIVE YIDQDTEEAR LKYGRPLTVI EGPLMDGMKI VGELFGAGKM FLPQVVKSAR VMKKSVAYLL PFMEEEKNQI ENSTARPKFL IATVKGDVHD IGKNIVGVVL ACNNYEVIDL GVMVPPDKIL EEAKKHNVSI IGLSGLITPS LDEMVHVASE MKRIGLEIPL LIGGATTSSA HTAVKIAPVY DHPVVHVVDA SRVVNVVNQL LHPDLHEAYS QKVKEDQKIA RENYFNTRAE RKLISLEQAR ENRDPIDWST TVIDKPSFIG IKVFDEEISL ETLVPFIDWT PFFTAWELKG RYPAILESET TGKQARELFA DAQKLMKTII TGKLFRTKGV IGIFPANSVR DDIFVYEDEN CSKLLTVFHT LRQQIQKQDE TEPNYCLADY VAPKESGRVD YIGGFAVTAG HGVEEFAKEF ENNQDDYNSI MAKALGDRFA EAFAEYMHYK VRKEYWGYDK NENLSPEDLI REKYRGIRPA AGYPASPDHT EKRALFDLLQ VEKNTGITLT EHFAMWPASS VSGLYFAHPK SKYFAVAKIN RDQVEDYAKR KEMSVEVVER WLAPNLSYDP LAVSAVR // ID Q7CLE0_YERPE Unreviewed; 1231 AA. AC Q7CLE0; Q74RF5; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 27-MAY-2015, entry version 82. DE SubName: Full=5-Methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:CAL22309.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAL22309.1}; DE SubName: Full=B12-dependent homocysteine-N5-methyltetrahydrofolate transmethylase, repressor of metE and metF {ECO:0000313|EMBL:AAM83616.1}; GN Name=metH {ECO:0000313|EMBL:AAM83616.1}; GN OrderedLocusNames=y0020 {ECO:0000313|EMBL:AAM83616.1}, GN YPO3722 {ECO:0000313|EMBL:CAL22309.1}; OS Yersinia pestis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=632 {ECO:0000313|Proteomes:UP000002490}; RN [1] {ECO:0000313|EMBL:CAL22309.1, ECO:0000313|Proteomes:UP000000815} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CO-92 / Biovar Orientalis {ECO:0000313|Proteomes:UP000000815}, RC and CO92 {ECO:0000313|EMBL:CAL22309.1}; 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] {ECO:0000313|EMBL:AAM83616.1, ECO:0000313|Proteomes:UP000002490} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KIM {ECO:0000313|EMBL:AAM83616.1}, and RC KIM10+ / Biovar Mediaevalis {ECO:0000313|Proteomes:UP000002490}; 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] {ECO:0000313|EMBL:CAL22309.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CO92 {ECO:0000313|EMBL:CAL22309.1}; RX PubMed=12834539; DOI=10.1186/1471-2180-3-13; RA Delihas N.; RT "Annotation and evolutionary relationships of a small regulatory RNA RT gene micF and its target ompF in Yersinia species."; RL BMC Microbiol. 3:13-13(2003). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AE009952; AAM83616.1; -; Genomic_DNA. DR EMBL; AL590842; CAL22309.1; -; Genomic_DNA. DR PIR; AB0453; AB0453. DR RefSeq; NP_667365.1; NC_004088.1. DR RefSeq; NP_994377.1; NC_005810.1. DR RefSeq; WP_002212080.1; NZ_KN150725.1. DR RefSeq; YP_002348603.1; NC_003143.1. DR ProteinModelPortal; Q7CLE0; -. DR SMR; Q7CLE0; 655-1231. DR STRING; 214092.YPO3722; -. DR DNASU; 1144967; -. DR EnsemblBacteria; AAM83616; AAM83616; y0020. DR EnsemblBacteria; AAS63254; AAS63254; YP_3084. DR EnsemblBacteria; KGA55508; KGA55508; DJ56_3493. DR GeneID; 1176541; -. DR KEGG; ype:YPO3722; -. DR KEGG; ypk:y0020; -. DR KEGG; ypm:YP_3084; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; YPES214092:GKDD-3678-MONOMER; -. DR Proteomes; UP000000815; Chromosome. DR Proteomes; UP000002490; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000815}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AAM83616.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000815}; KW Transferase {ECO:0000313|EMBL:AAM83616.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 252 252 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 315 315 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 316 316 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 763 763 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1231 AA; 136149 MW; ED23132892137500 CRC64; MVDTVIDNKV KELHQQLAQR ILVLDGGMGT MIQSYRLEEA DYRGARFADW ASDLKGNNDL LVLSKPEVIT AIHNAYLEAG ADILETNTFN STSIAMADYQ MASLSAEINY EAARLARICA DEWSARTPEK PRYVAGVLGP TNRTASISPK VNDPAFRNVS FDQLVEAYRE STRALIEGGV DLIMIETVFD TLNAKAATFA VESEFEVMGV LLPVMISGTI TDASGRTLSG QTTEAFYNSL RHVKPLSFGL NCALGPDELR QYVAELSRIS EYYVSAHPNA GLPNAFGEYD LEAKEMAEQI GEWARAGFLN IVGGCCGTTP RHIAAMVNAV AGVPPRPLPD IPVACRLAGL EPLTIDANTL FVNVGERTNV TGSARFKRLI KEEKYGEALD VARQQVESGA QIIDINMDEG MLDAEAAMVR FLNLIAGEPD IARVPIMIDS SRWDVIEKGL KCIQGKGIVN SISMKEGVDA FIHHAKLVRR YGAAMVVMAF DETGQADTRA RKIEICRRAY KILTETVGFP PEDIIFDPNI FAVATGIEEH NNYAVDFIEA CADIKAELPH ALISGGVSNV SFSFRGNDPV REAIHAVFLY YAIRNGMDMG IVNAGQLAIY DDLSDELRDA VEDVILNRRD DSTERLLDLA EKYRDSKSGE VAIQQAEWRG WPVVKRLEYS LVKGITEFIE LDTEEARQQA DRPIEVIEGP LMSGMNVVGD LFGEGKMFLP QVVKSARVMK QAVAYLEPYI EASKQKGTTA GKILLATVKG DVHDIGKNIV GVVLQCNNYE IIDLGVMVPT EKILRTAREE KVDIIGLSGL ITPSLDEMVN VAKEMERQGF TLPLLIGGAT TSKAHTAVKI EQNYSGSTTY VSNASRSVGV VSALLSDTQR EAFVAKTRKE YETVRIQHAR KKPRTPPVSL QAARNNPTVI DWENYTPPVA HKLGVQVVEA SIETLRNYID WTPFFMTWSL AGKYPRILED EVVGEEAKRL LADANALLDK LSAEDLLHPK GVVGLFPANS VGDDIEIYRD ERRDEVLAIS YHLRQQTEKT DFPNYCLADY VAPKSSGKAD YFGAFAVTGG LEEDALADAY DAQHDDYNKI MIKALSDRLA EAFAEYLHER VRKVYWGFAP NENLSNEELV RENYQGIRPA PGYPACPEHT EKGQIWQLLD VETHTGMKLT ESYAMWPGAS VSGWYFSHPD SKYFAVAQIQ RDQVEDYAAR KGMPTAEVER WLAPNLGYDA D // ID Q7CXR2_AGRT5 Unreviewed; 1257 AA. AC Q7CXR2; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 2. DT 27-MAY-2015, entry version 85. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AAK87902.2}; GN Name=metH {ECO:0000313|EMBL:AAK87902.2}; GN OrderedLocusNames=Atu2155 {ECO:0000313|EMBL:AAK87902.2}; 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 {ECO:0000313|EMBL:AAK87902.2, ECO:0000313|Proteomes:UP000000813}; RN [1] {ECO:0000313|EMBL:AAK87902.2, ECO:0000313|Proteomes:UP000000813} 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] {ECO:0000313|EMBL:AAK87902.2, ECO:0000313|Proteomes:UP000000813} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C58 / ATCC 33970 {ECO:0000313|Proteomes:UP000000813}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AE007869; AAK87902.2; -; Genomic_DNA. DR RefSeq; NP_355117.2; NC_003062.2. DR RefSeq; WP_010972100.1; NC_003062.2. DR ProteinModelPortal; Q7CXR2; -. DR SMR; Q7CXR2; 666-914, 918-1244. DR STRING; 176299.Atu2155; -. DR EnsemblBacteria; AAK87902; AAK87902; Atu2155. DR GeneID; 1139598; -. DR KEGG; atu:Atu2155; -. DR PATRIC; 20814089; VBIAgrTum91616_2165. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; AGRO:ATU2155-MONOMER; -. DR Proteomes; UP000000813; Chromosome circular. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000813}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000813}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 260 260 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 776 776 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1257 AA; 138706 MW; B583BED5BA8065E4 CRC64; MFDDLFGPEG AKRDGAEIFK ALRDAASERI LILDGAMGTQ IQGLGFDEDH FRGDRFIGCA CHQKGNNDLL ILTQPDAIEE IHYRYAMAGA DILETNTFSS TRIAQADYEM ENAVYDLNRE GAAIVRRAAQ RAEREDGRRR FVAGAIGPTN RTASISPDVN NPGYRAVSFD DLRIAYGEQI DGLIDGGADI ILIETIFDTL NAKAAIFACE ERFEAKGIRL PVMISGTITD LSGRTLSGQT PSAFWNSVRH ANPFTIGLNC ALGADAMRPH LQELSDVADT FVCAYPNAGL PNEFGQYDET PEMMARQVEG FVRDGLVNIV GGCCGSTPEH IRAIAEAVKD YKPREIPEHK PFMSLSGLEP FVLTKDIPFV NVGERTNVTG SARFRKLITA GDYTAALAVA RDQVENGAQI IDINMDEGLI DSEKAMVEFL NLIAAEPDIA RVPVMIDSSK FEIIEAGLKC VQGKSIVNSI SLKEGEEKFL QQARLVHNYG AAVVVMAFDE VGQADTYQRK VEICARAYKL LTEKAGLSPE DIIFDPNVFA VATGIEEHNN YGVDFIEATK TIRETMPLTH ISGGVSNLSF SFRGNEPVRE AMHAVFLYHA IQVGMDMGIV NAGQLAVYDN IDAELREACE DVVLNRRDDA TERLLEVAER FRGTGEKQAK VQDLSWREYP VEKRLEHALV NGITDYIEAD TEEARQQAAR PLHVIEGPLM AGMNVVGDLF GSGKMFLPQV VKSARVMKQA VAVLLPYMEE EKRLNGGSER SAAGKVLMAT VKGDVHDIGK NIVGVVLACN NYEIIDLGVM VPTTKILETA IAEKVDVIGL SGLITPSLDE MVHVAAEMER QGFDIPLLIG GATTSRVHTA VKIHPRYEQG QAIYVTDASR AVGVVSALLS EEQKPAYIDG IRAEYAKVAE AHARNEREKQ RLPLSRAREN AHKIDWSSYS VVKPQFFGTK VFETYDLEEL SRYIDWTPFF QTWELKGRFP AILEDEKQGE AARQLYADAQ AMLAKIIEEK WFRPRAVIGF WPANAVGDDI RLFTDEGRKE ELATFFTLRQ QLSKRDGRPN VALSDFVAPV DSGVADYVGG FVVTAGIEEV AIAERFERAN DDYSSILVKA LADRFAEAFA ERMHERVRKE FWGYAPDEAL AGDDLIGEAY AGIRPAPGYP AQPDHTEKKT LFALLDATNA AGVELTESYA MWPGSSVSGL YIGHPESYYF GVAKVERDQV LDYARRKDMP VTEVERWLGP VLNYVPTNGE EKIDSAA // ID Q7D740_MYCTO Unreviewed; 302 AA. AC Q7D740; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 27-MAY-2015, entry version 57. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AAK46833.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:AAK46833.1}; GN Name=mmuM {ECO:0000313|EMBL:AAK46833.1}; GN OrderedLocusNames=MT2533 {ECO:0000313|EMBL:AAK46833.1}; OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=83331 {ECO:0000313|EMBL:AAK46833.1, ECO:0000313|Proteomes:UP000001020}; RN [1] {ECO:0000313|EMBL:AAK46833.1, ECO:0000313|Proteomes:UP000001020} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CDC 1551 / Oshkosh {ECO:0000313|Proteomes:UP000001020}; 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 ----------------------------------------------------------------------- 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; AAK46833.1; -; Genomic_DNA. DR RefSeq; NP_337019.1; NC_002755.2. DR RefSeq; WP_003899329.1; NZ_KK341227.1. DR ProteinModelPortal; Q7D740; -. DR SMR; Q7D740; 2-300. DR STRING; 83331.MT2533; -. DR EnsemblBacteria; AAK46833; AAK46833; MT2533. DR EnsemblBacteria; KBN13694; KBN13694; V735_02542. DR KEGG; mtc:MT2533; -. DR PATRIC; 18127324; VBIMycTub22151_2770. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OrthoDB; EOG6C019S; -. DR Proteomes; UP000001020; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001020}; KW Methyltransferase {ECO:0000313|EMBL:AAK46833.1}; KW Transferase {ECO:0000313|EMBL:AAK46833.1}. SQ SEQUENCE 302 AA; 31532 MW; D819AB178F9A551D CRC64; MELVSDSVLI SDGGLATELE ARGHDLSDPL WSARLLVDAP HAITAVHTAY FRAGAQIATT ASYQASFEGF AARGIGHDDA TVLLRRSVEL AQAARDEVGV GGLSVAASVG PYGAALADGS EYRGCYGLSV AALMKWHLPR LEVLVDAGAD MLALKTIPDI DEAEALVNLV RRLATPAWLS YTINGTRTRA GQPLTDAFAV AAGVPEIVAV GVNCCAPDDV LPAIAFAVAH TGKPVIVYPN SGEGWDGRRR AWVGPRRFSG SSGQLAREWV AAGARIVGGC CRVRPIDIAE IGRALTTAPP RG // ID Q7M929_WOLSU Unreviewed; 1120 AA. AC Q7M929; DT 15-DEC-2003, integrated into UniProtKB/TrEMBL. DT 15-DEC-2003, sequence version 1. DT 29-APR-2015, entry version 81. DE SubName: Full=Wolinella succinogenes, complete genome; segment 4/7 {ECO:0000313|EMBL:CAE10314.1}; GN OrderedLocusNames=WS1234 {ECO:0000313|EMBL:CAE10314.1}; 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 {ECO:0000313|Proteomes:UP000000422}; RN [1] {ECO:0000313|EMBL:CAE10314.1, ECO:0000313|Proteomes:UP000000422} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29543 / DSM 1740 / LMG 7466 / NCTC 11488 / FDC 602W RC {ECO:0000313|Proteomes:UP000000422}; RX PubMed=14500908; DOI=10.1073/pnas.1932838100; RA Baar C., Eppinger M., Raddatz G., Simon JM., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; BX571660; CAE10314.1; -; Genomic_DNA. DR RefSeq; NP_907414.1; NC_005090.1. DR RefSeq; WP_011139101.1; NC_005090.1. DR ProteinModelPortal; Q7M929; -. DR STRING; 273121.WS1234; -. DR EnsemblBacteria; CAE10314; CAE10314; WS1234. DR KEGG; wsu:WS1234; -. DR PATRIC; 24039486; VBIWolSuc63014_1161. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR Proteomes; UP000000422; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000422}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000422}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 218 218 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 721 721 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1120 AA; 123940 MW; 0B9719DCA12B724F CRC64; MKMEQFFEIH RQRVMILDGA MGTEIQKFDL KEEDWEEKAG CSEILNVTRG DVILSIHRSY LEAGADILKS NTFGALPWVL EEYGIGGRAY EMAFAGAQIA KEACDSFAPS PRFVAGSLGP GTKLPSLGHI DYDTMFEGYK EAARGLKEGG ADLFLLETCQ DPLQIKAAVH ACKEVDSSMP IMVSATIETT GTMLIGTDIK TLAVILEPLE IFSLGINCGL GPDMAEKHLK ALAQYAPFPL SIHANAGLPQ NVGGCTFYPM EPKEFAEIEE EFLGIEGVAF LGGCCGTTPE HIRQLKERVG ISRPTPPAKR TPVALASLFE SVELKQSPAP LLIGERSNAT GSKAFRELLV AEDYEGALGV GLAQVKSGAH VLDVSVGFAG RDERRDMREV VSRYATNLPL PLMPDSTQSE VLEVALKCIG GRPIINSANL EDGIEKFDRV CALAKRFGAV LICLTIDEEG MAKTKERKVA CAKRMMERAV SVHGLRERDI IFDTLTFTIG SGDEEYFTAG IETLDAIQEL SQLYPEAGTT LGLSNISFGL SKEARIYLNS IFLYHAVQRG LTSAIVNVSH LLPYAKVSDE DRASCEALIF NQTQGAAPLY AFIDHFSDKK AELASDSTLE GMDTQEKIAH LLIQGDKEGM KALLPSAKEE IAAERIINEI LIEAMKVVGE RFGKGEMQLP FVLQSAEVMK MSVDYLNAYL PKTEKKNQTT MILGTVKGDV HDVGKNLVDI ILTNNGYKIV NIGIKADIEQ FIQAYHEHKA DAIGMSGLLV KSTLVMKENL EELARRGIHC PVILGGAALN RAFVDDYCRG IYPGIIFYCK DAFDGMAAME KIEKQDFSDL RLPSDKSVPE VEEQIAPSVE DSLPPVKITP PLFEQKIYKP PFWGRQVISD LDPETIFSII DRNLLYKHRW GYGKRGLKKE EYAKLCEELL HPTYERLKSQ ILDQGLFEPV VLYGYFELTR EGECLMAKNP KGGEVSFDFP RQKKGEFLSI PDFFPLQGGV LPLSLVSSGH RFSPFEQKLY ERGEYHEYFL IHALGAELAE ALADFVHQRV REELGIGERQ GCRYSFGYPA CPDLTQNQGI FTLLEPQEFH ITLSETFQMH PEQSTCAIIT PHPEASYFAI // ID Q7NND4_GLOVI Unreviewed; 1196 AA. AC Q7NND4; DT 15-DEC-2003, integrated into UniProtKB/TrEMBL. DT 15-DEC-2003, sequence version 1. DT 29-APR-2015, entry version 85. DE SubName: Full=5-methyltetrahydrofolate--homocysteine S-methyltransferase {ECO:0000313|EMBL:BAC88418.1}; GN Name=metH {ECO:0000313|EMBL:BAC88418.1}; GN OrderedLocusNames=gll0477 {ECO:0000313|EMBL:BAC88418.1}; OS Gloeobacter violaceus (strain PCC 7421). OC Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacter. OX NCBI_TaxID=251221 {ECO:0000313|EMBL:BAC88418.1, ECO:0000313|Proteomes:UP000000557}; RN [1] {ECO:0000313|EMBL:BAC88418.1, ECO:0000313|Proteomes:UP000000557} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7421 {ECO:0000313|EMBL:BAC88418.1, RC ECO:0000313|Proteomes:UP000000557}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; BA000045; BAC88418.1; -; Genomic_DNA. DR RefSeq; NP_923423.1; NC_005125.1. DR RefSeq; WP_011140480.1; NC_005125.1. DR ProteinModelPortal; Q7NND4; -. DR STRING; 251221.gvip051; -. DR EnsemblBacteria; BAC88418; BAC88418; BAC88418. DR GeneID; 2599678; -. DR KEGG; gvi:gvip051; -. DR PATRIC; 22040319; VBIGloVio86258_0485. DR InParanoid; Q7NND4; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR PhylomeDB; Q7NND4; -. DR BioCyc; GVIO251221:GH9A-480-MONOMER; -. DR Proteomes; UP000000557; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000557}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAC88418.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000557}; KW Transferase {ECO:0000313|EMBL:BAC88418.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 230 230 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 296 296 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 297 297 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 737 737 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1196 AA; 130890 MW; 243248F30FBC44D7 CRC64; MTHPFLELLR HKIVVFDGAM GTSIQKMGLG PEDFGGAHLE GCNEYLVFSK PEAIEQVHAS FLEAGADVIE TDTFGCSTIV LAEYGIEAMA YELSKVAAAL ARQVAARYST LDKPRFVAGS IGPGTKIATL GQTDYDALKE AYLDNVRGLI DGGADVLMIE TCQDLLQIKA VLAAAEIAFD ERGVRLPVIT SVTLERDDRN VADKMLVGSD IATVVSALQP YTIDVLGLNC ATGPDLMSEN IRYLSHNSPF YISVIPNAGL PENIGGHAHY HLTPGELVRY VRHYVDELGI NIVGGCCGTT PDHIRALATA VSGVKPRNRS VEVVPQVSSL YSAVPMHMDP APLLVGERLN SNGSKKFREL LLAEDWDGIA GMAREQEREG AHVLDVCVDY VGRDGVRDMG EVVSRLKTRS TLPLMIDSTE VPVIHTALKQ LGGRAIVNSI NLEDGEVRLQ KLLPLCREFG SAVVALTIDE GEGMARTAER KLEVARRIHD LTVHKYGMKS EDLIFDPLTF TLGSGDADSR RLGIETLEGI RLIKENLPGV RTILGLSNIS FGLNPGARQA LNSVYLYYAV QNGLDMAIVH ASKILPLNRI DAEERELHRK LIFDEHDNGD PLQNLLAFYA KQEGGGKARK TAVVDASAPI EERLRRRIID GNRVGLDKDL TEALRIYAPL DIINQHLLDG MRVVGELFGS GQMQLPFVLQ SAETMKAAVG YLEPFMEKSD HSAKGTVVIA TVKGDVHDIG KNLVDIILSN NGYRVVNLGI RQPVENIIAA FGEHQADCIA MSGLLVKSTA FMKENLEIFN ERGITAPVIL GGAALTRRFV ESDCQQVYRG KVIYGKDAFA DLHFLDALVE AKAKSAWKDG EGFVDGFAPV GEELKRLMAS SEGGAPPAPA SFRSSEALVQ PPEDGPIVRS RVAIGVPRPR PPFWGTRVLG GSDGPDLSEV FRYLDLNALF AGQWNYRKSP DQSRAEYEAK RDTEMGPVLE RLKCEVIDQQ LLHPQVAYGY FPCQAESNSL RIYSLESFER FQQSGDPADL LVCARLAFPR QKGQDHLCIA DYFADAASGQ IDALALQAVT VGHVASEHGQ KLFKADRYSE YLYYYGLSVQ TAEALADWTH ARIRRELGID GQDTAEMRRL VAGGYQGARF SYGYPACPNL EDQAILLDLV GARRIDLAMD ESHQLLPEQS TTAIVCHHPE ARYFAV // ID Q7P1L0_CHRVO Unreviewed; 1237 AA. AC Q7P1L0; DT 15-DEC-2003, integrated into UniProtKB/TrEMBL. DT 15-DEC-2003, sequence version 1. DT 27-MAY-2015, entry version 93. DE SubName: Full=Probable 5-methyltetrahydrofolate-homocysteine S-methyltransferase {ECO:0000313|EMBL:AAQ57882.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AAQ57882.1}; GN OrderedLocusNames=CV_0203 {ECO:0000313|EMBL:AAQ57882.1}; OS Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / OS NBRC 12614 / NCIMB 9131 / NCTC 9757). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Chromobacteriaceae; Chromobacterium. OX NCBI_TaxID=243365 {ECO:0000313|Proteomes:UP000001424}; RN [1] {ECO:0000313|Proteomes:UP000001424} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / RC NCTC 9757 {ECO:0000313|Proteomes:UP000001424}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AE016825; AAQ57882.1; -; Genomic_DNA. DR RefSeq; NP_899873.1; NC_005085.1. DR RefSeq; WP_011133758.1; NC_005085.1. DR ProteinModelPortal; Q7P1L0; -. DR SMR; Q7P1L0; 660-906. DR STRING; 243365.CV_0203; -. DR EnsemblBacteria; AAQ57882; AAQ57882; CV_0203. DR KEGG; cvi:CV_0203; -. DR PATRIC; 21435166; VBIChrVio67196_0194. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CVIO243365:GHUD-203-MONOMER; -. DR Proteomes; UP000001424; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001424}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AAQ57882.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001424}; KW Transferase {ECO:0000313|EMBL:AAQ57882.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 770 770 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1237 AA; 135808 MW; 975DDD11F127E277 CRC64; MTKPLPHSIY QHLSQRILIL DGGMGTMIQR HQLTEADYRG ARFADWRCDV KGNNDLLVLT RPDVIAGIHQ AYLDAGADIV ETNTFNATSI AMADYQMEEL VWEINREAAR LVKELCEAET VKNPAKPRYC AGVLGPTNRT CSISPDVNDP GYRNVSFDQL VASYTEAIDG LVAGGADLLL VETIFDTLNA KAAVFAIHKY FDERPAIARL PIMISGTITD QSGRTLTGQT TEAFYNSLSH ADAASFGLNC ALGPDLLRPY VEEMARVSST YVSVHANAGL PNAFGGYDLE PEKMGEYVRE WAESGLINIV GGCCGTTPEH IAAIARAVDG IAPRALPSIE AKCRLSGLEP FNIGDEDLFV NVGERTNVTG SRAFAKLILN GDYATALDVA RQQVENGAQV IDINMDEGML DAHAAMVRFL NLIASEPDIA RVPIMIDSSK WDVIEAGLKC IQGKGIVNSI SLKEGKEKFV EQARLIRRYG AAVIVMAFDE KGQADTYARK IEICDHSYRI LVDEVGFPPE DIIFDPNIFA VATGIDEHAR YGLDFIEATG WIKQHLPHAK ISGGVSNVSF SFRGNNKVRE AIHAVFLYHA IQRGMTMGIV NAGALEVYDE VDPELRARIE DVVLMRQPKD GGDATERLIE LAEKFKGEAA GEKKGEDLAW RSWPVEKRLE HALVKGITTF IVEDTEEVRL KSARPIHVIE GPLMDGMNVV GDLFGAGKMF LPQVVKSARV MKAAVAHLEP FIEEEKIRLG LADAPAKGVI IMATVKGDVH DIGKNIVGVV LRCNNYKVID LGVMVPCQTI LDAAREHKAD IIGLSGLITP SLEEMSHVAK EKQRQGFDIP LLIGGATTSK VHTAVKIAPH YQHPVVYVPD ASRAVGVCSN LLSDTLKDAF VAENLAEQQR AREGHANKAN RKVVSLEAAR ANKEKIDWAG YVPPKPAWLG VRRFEHYPLS EIAQYIDWTP FFQSWELAGR FPRILDDEIV GESARALYED AQVMLKRIVD ENWLTANAVI GLFPAASVDD DDIEIRRPDN GASLMTWVGL RQQLPKTDGK ANWALADYVA PKDSGVDDYI GAFAVTAGIG IEPHVKRFED ANDDYSAILL KALADRLAEA FAELMHARVR REFWGYAADE QIDNEGLIDE QYRGIRPAPG YPACPDHTVK TELFKLLDAP AIGMTLTEGY AMLPTAAVSG FYFSHPASRY FGVGKVEKDQ VSSYAQRRGV TLEQAERDLA PNLGYDA // ID Q7P7L1_FUSNV Unreviewed; 320 AA. AC Q7P7L1; DT 15-DEC-2003, integrated into UniProtKB/TrEMBL. DT 15-DEC-2003, sequence version 1. DT 27-MAY-2015, entry version 38. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:EAA24858.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EAA24858.1}; GN ORFNames=FNV1524 {ECO:0000313|EMBL:EAA24858.1}; OS Fusobacterium nucleatum subsp. vincentii ATCC 49256. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=209882 {ECO:0000313|EMBL:EAA24858.1}; RN [1] {ECO:0000313|EMBL:EAA24858.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 49256 {ECO:0000313|EMBL:EAA24858.1}; 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] {ECO:0000313|EMBL:EAA24858.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 49256 {ECO:0000313|EMBL:EAA24858.1}; 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. {ECO:0000313|EMBL:EAA24858.1}. 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; AABF01000013; EAA24858.1; -; Genomic_DNA. DR RefSeq; WP_005888585.1; NZ_AABF02000013.1. DR ProteinModelPortal; Q7P7L1; -. DR EnsemblBacteria; EAA24858; EAA24858; FNV1524. DR PATRIC; 30268824; VBIFusNuc72376_0463. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:EAA24858.1}; KW Transferase {ECO:0000313|EMBL:EAA24858.1}. SQ SEQUENCE 320 AA; 35413 MW; F354185CD4BEAEBA CRC64; MKKIMFEIEK ELKERILVLD GAMGTVLQKY ELPAEDFNGT KGCYEILNET RPDIIFEVHK KYIEAGADII ETNSFNCNAI SLKNYHLEDK VYDLAKKSAE IAKDAVRKSE KKVYVFGSVG PTNKGLSFPE KDVSCKRAVS FDEMKEVIKV QVAGLIDGGV DGILLETIFD GLTAKAALLA IEEVFAEKDT KLPISISATV NKQGKLLTGQ SIESLMVDLD RDSVISFGFN CSFGAKDLVP FVLKIKELTA KFISLHANAG LPNQNGEYEE TAQKMRDDLL PLIENQAINI LGGCCGTDYE HIKLIAELIK GQKPRVLLEK // ID Q7PNI0_ANOGA Unreviewed; 333 AA. AC Q7PNI0; DT 15-DEC-2003, integrated into UniProtKB/TrEMBL. DT 23-OCT-2007, sequence version 4. DT 07-JAN-2015, entry version 65. DE SubName: Full=AGAP008537-PA {ECO:0000313|EMBL:EAA12151.5}; DE Flags: Fragment; GN ORFNames=AgaP_AGAP008537 {ECO:0000313|EMBL:EAA12151.5}; OS Anopheles gambiae (African malaria mosquito). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; OC Culicidae; Anophelinae; Anopheles. OX NCBI_TaxID=7165 {ECO:0000313|Proteomes:UP000007062}; RN [1] {ECO:0000313|EMBL:EAA12151.5, ECO:0000313|Proteomes:UP000007062} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PEST {ECO:0000313|EMBL:EAA12151.5, RC ECO:0000313|Proteomes:UP000007062}; RX PubMed=12364791; DOI=10.1126/science.1076181; RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R., RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M., Wides R., RA Salzberg S.L., Loftus B., Yandell M., Majoros W.H., Rusch D.B., RA Lai Z., Kraft C.L., Abril J.F., Anthouard V., Arensburger P., RA Atkinson P.W., Baden H., de Berardinis V., Baldwin D., Benes V., RA Biedler J., Blass C., Bolanos R., Boscus D., Barnstead M., Cai S., RA Center A., Chaturverdi K., Christophides G.K., Chrystal M.A., RA Clamp M., Cravchik A., Curwen V., Dana A., Delcher A., Dew I., RA Evans C.A., Flanigan M., Grundschober-Freimoser A., Friedli L., Gu Z., RA Guan P., Guigo R., Hillenmeyer M.E., Hladun S.L., Hogan J.R., RA Hong Y.S., Hoover J., Jaillon O., Ke Z., Kodira C., Kokoza E., RA Koutsos A., Letunic I., Levitsky A., Liang Y., Lin J.J., Lobo N.F., RA Lopez J.R., Malek J.A., McIntosh T.C., Meister S., Miller J., RA Mobarry C., Mongin E., Murphy S.D., O'Brochta D.A., Pfannkoch C., RA Qi R., Regier M.A., Remington K., Shao H., Sharakhova M.V., RA Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J., Thomasova D., RA Ton L.Q., Topalis P., Tu Z., Unger M.F., Walenz B., Wang A., Wang J., RA Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M., Yao A., RA Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I., RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., RA Mural R.J., Myers E.W., Adams M.D., Smith H.O., Broder S., RA Gardner M.J., Fraser C.M., Birney E., Bork P., Brey P.T., Venter J.C., RA Weissenbach J., Kafatos F.C., Collins F.H., Hoffman S.L.; RT "The genome sequence of the malaria mosquito Anopheles gambiae."; RL Science 298:129-149(2002). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAA12151.5}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAAB01008964; EAA12151.5; -; Genomic_DNA. DR RefSeq; XP_316898.4; XM_316898.5. DR STRING; 7165.AGAP008537-PA; -. DR GeneID; 1277483; -. DR KEGG; aga:AgaP_AGAP008537; -. DR VectorBase; AGAP008537; Anopheles gambiae. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR InParanoid; Q7PNI0; -. DR KO; K00547; -. DR OMA; AINDPLW; -. DR OrthoDB; EOG7GQXW0; -. DR PhylomeDB; Q7PNI0; -. DR Proteomes; UP000007062; Chromosome 3R. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007062}; KW Reference proteome {ECO:0000313|Proteomes:UP000007062}. FT NON_TER 1 1 {ECO:0000313|EMBL:EAA12151.5}. SQ SEQUENCE 333 AA; 37043 MW; F555F5E5BECCAB37 CRC64; INNTPTTMTN VTVLDGGFAT QLSVHVGKSI DGDPLWSARF NATDPNAVFR THLDFLEAGA EAIMTNTYQA SIEGYVEHLH LTEDTSLNLI KSTVRVAQMA RNHFLAKGPT NEQRSVPLLV ASIGPYGAHL HDGSEYTGRY AADVCADTIQ KWHRPRIDAC LEAGVDVLGI ETIPCKMEAE ALLDMLCDEY PTVRFWISFQ CKDNQHLANG ELFADTVNSL WAKARSRRAK NLLALGVNCV HPQIVTPLFR SVNEKKLPAV RIPLIVYPNS GEVYTVEDGW QGREDCVPLE HYVPQWIDLG ARFIGGCCRT YARDIQRIKQ TVINHASNSN HCQ // ID Q7R6V6_PLAYO Unreviewed; 150 AA. AC Q7R6V6; DT 15-DEC-2003, integrated into UniProtKB/TrEMBL. DT 15-DEC-2003, sequence version 1. DT 27-MAY-2015, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EAA20376.1}; DE Flags: Fragment; GN ORFNames=PY07836 {ECO:0000313|EMBL:EAA20376.1}; OS Plasmodium yoelii yoelii. OC Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia). OX NCBI_TaxID=73239 {ECO:0000313|EMBL:EAA20376.1, ECO:0000313|Proteomes:UP000008553}; RN [1] {ECO:0000313|EMBL:EAA20376.1, ECO:0000313|Proteomes:UP000008553} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=17XNL {ECO:0000313|EMBL:EAA20376.1, RC ECO:0000313|Proteomes:UP000008553}; RX PubMed=12368865; DOI=10.1038/nature01099; RA Carlton J.M., Angiuoli S.V., Suh B.B., Kooij T.W., Pertea M., RA Silva J.C., Ermolaeva M.D., Allen J.E., Selengut J.D., Koo H.L., RA Peterson J.D., Pop M., Kosack D.S., Shumway M.F., Bidwell S.L., RA Shallom S.J., van Aken S.E., Riedmuller S.B., Feldblyum T.V., RA Cho J.K., Quackenbush J., Sedegah M., Shoaibi A., Cummings L.M., RA Florens L., Yates J.R., Raine J.D., Sinden R.E., Harris M.A., RA Cunningham D.A., Preiser P.R., Bergman L.W., Vaidya A.B., RA van Lin L.H., Janse C.J., Waters A.P., Smith H.O., White O.R., RA Salzberg S.L., Venter J.C., Fraser C.M., Hoffman S.L., Gardner M.J., RA Carucci D.J.; RT "Genome sequence and comparative analysis of the model rodent malaria RT parasite Plasmodium yoelii yoelii."; RL Nature 419:512-519(2002). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAA20376.1}. 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; AABL01002948; EAA20376.1; -; Genomic_DNA. DR RefSeq; XP_728811.1; XM_723718.1. DR GeneID; 3801355; -. DR KEGG; pyo:PY07836; -. DR EuPathDB; PlasmoDB:PY07836; -. DR eggNOG; NOG268857; -. DR Proteomes; UP000008553; Unassembled WGS sequence. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008553}; KW Reference proteome {ECO:0000313|Proteomes:UP000008553}. FT NON_TER 1 1 {ECO:0000313|EMBL:EAA20376.1}. SQ SEQUENCE 150 AA; 17614 MW; 2E5BC3DFC4713199 CRC64; SLLLYLDSYN KYIYAIGLNC VNINYAYNLF LPFKKYTSTY NNINVELYKS ENHQVNSFIK NILNDIKKNR YIYDVNFFCS PNKTLEKVSF SDNTVNFQTH SRNKQIHVYN NIEKWINVGI NGFGGCCYYT PYDISLINYK LSKMATSPVI // ID Q7SFT2_NEUCR Unreviewed; 361 AA. AC Q7SFT2; DT 15-DEC-2003, integrated into UniProtKB/TrEMBL. DT 15-DEC-2003, sequence version 1. DT 29-APR-2015, entry version 55. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:EAA35719.1}; GN ORFNames=NCU00799 {ECO:0000313|EMBL:EAA35719.1}; 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 {ECO:0000313|EMBL:EAA35719.1, ECO:0000313|Proteomes:UP000001805}; RN [1] {ECO:0000313|EMBL:EAA35719.1, ECO:0000313|Proteomes:UP000001805} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987 RC {ECO:0000313|Proteomes:UP000001805}; 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; CM002236; EAA35719.1; -; Genomic_DNA. DR RefSeq; XP_964955.1; XM_959862.2. DR ProteinModelPortal; Q7SFT2; -. DR STRING; 5141.NCU00799.1; -. DR EnsemblFungi; EFNCRT00000000907; EFNCRP00000000907; EFNCRG00000000906. DR GeneID; 3881104; -. DR KEGG; ncr:NCU00799; -. DR EuPathDB; FungiDB:NCU00799; -. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR InParanoid; Q7SFT2; -. DR KO; K00547; -. DR OrthoDB; EOG79SF86; -. DR Proteomes; UP000001805; Chromosome 1, Linkage Group I. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001805}; KW Methyltransferase {ECO:0000313|EMBL:EAA35719.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001805}; KW Transferase {ECO:0000313|EMBL:EAA35719.1}. SQ SEQUENCE 361 AA; 39727 MW; C40C243707FCA22E CRC64; MATPIPVQIL DGGMGTTLED MHDITFSFET PLWSSHLLVS GEEDKLSDCH EAFKQAGANI ISTATYQISI NGFAATKAPR SGTVDEEREG IEKEEIPRFL SRAVVLAANA AGTEGKVALS LGPYGATMIP STEYSGRYDP EHQHVQALGK WHKERLDLFK DVDPNQVNYI AFETVPRLDE IVAIRNLLSA DNIPTSLRGR PVWISSPYPN DDGKLPDGST VEEVVKAVLT HREGLETPWG IGINCTKVEK LDSLVKRYED AIQTCIKNGE QMAWPSLVLY PDGTKGEVYN TATKTWELSP GHKETEAPWE TVLASVVEAA RQRGNWKSIV VGGCCKASPE HIRRLRRTLQ DYGHMSTSPA A // ID Q7U6U8_SYNPX Unreviewed; 1209 AA. AC Q7U6U8; DT 01-OCT-2003, integrated into UniProtKB/TrEMBL. DT 01-OCT-2003, sequence version 1. DT 29-APR-2015, entry version 85. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CAE07753.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAE07753.1}; GN Name=metH {ECO:0000313|EMBL:CAE07753.1}; GN OrderedLocusNames=SYNW1238 {ECO:0000313|EMBL:CAE07753.1}; OS Synechococcus sp. (strain WH8102). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Synechococcus. OX NCBI_TaxID=84588 {ECO:0000313|EMBL:CAE07753.1, ECO:0000313|Proteomes:UP000001422}; RN [1] {ECO:0000313|EMBL:CAE07753.1, ECO:0000313|Proteomes:UP000001422} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WH8102 {ECO:0000313|EMBL:CAE07753.1, RC ECO:0000313|Proteomes:UP000001422}; RX PubMed=12917641; DOI=10.1038/nature01943; RA Palenik B., Brahamsha B., Larimer F., Land M., Hauser L., Chain P., RA Lamerdin J., Regala W., Allen E.A., McCarren J., Paulsen I., RA Dufresne A., Partensky F., Webb E., Waterbury J.; RT "The genome of a motile marine Synechococcus."; RL Nature 424:1037-1042(2003). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; BX569692; CAE07753.1; -; Genomic_DNA. DR RefSeq; NP_897331.1; NC_005070.1. DR RefSeq; WP_011128102.1; NC_005070.1. DR ProteinModelPortal; Q7U6U8; -. DR STRING; 84588.SYNW1238; -. DR EnsemblBacteria; CAE07753; CAE07753; SYNW1238. DR KEGG; syw:SYNW1238; -. DR PATRIC; 23833998; VBISynSp27240_1300. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR Proteomes; UP000001422; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001422}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAE07753.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001422}; KW Transferase {ECO:0000313|EMBL:CAE07753.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 238 238 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 764 764 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1209 AA; 132174 MW; 0B032E4870BA72D0 CRC64; MVVAQASRQL TNSRFLDHLN GPERPVLVFD GATGTSLQGL DLTAEDFGGP ELEGCNENLA VTKPEAVKAV HRQFLEVGCD VIETDTFGAA SIVLAEYGLE DKAFELNKRA AELAREMADE FSTPDKPRFV AGSMGPTTKL PTLGHIDFDT MRDSFREQAE GLIAGDVDLF IVETCQDVLQ IKAALQGIEE AFEASGERRA LMVSVTMETT GTMLVGTDIA AVVSILEPFP IDILGLNCAT GPEQMKEHIR YLSEHSPFTV SCIPNAGLPE NVGGVAHYRL TPVELKMQLM HFVEDLGVQV IGGCCGTTPS HIGSLAELAA ELKPALRSSR HDAASDANVR PALNYEPAAA SIYGVTPYQQ DNSFLIIGER LNASGSRKVR ELLAEEDWDG LVSVARGQVK ENAHVLDVNV DYVGRDGEQD MHQLVSRLVT NVNLPLMLDS TEWQKMEAGL KVAGGKCILN STNYEDGDER FFKVLELARR YGAGVVVGTI DEDGMARTAE KKFAIAQRAY RDALEFGIPA HEIFYDPLAL PISTGIEEDR LNGKATVDSI RMIRENLPGV HVVLGVSNVS FGLSPAARIT LNSVFLHDCC EAGMDAAIVS PAKILPLIKI TEEHQTVCRD LINDNRRFDD GICVYDPLTE LTKLFEGVSA KEARASGPSL ADLPIEERLK QHIIDGERIG LEPSLDEALQ AYPPLQIINT FLLDGMKVVG ELFGSGQMQL PFVLQSAETM KSAVAYLEPH METAEGESTS KGKFLIATVK GDVHDIGKNL VDIILTNNGY EVVNLGIKQS CEAIVEAQHE HQADCIAMSG LLVKSTAFMK DNLKAFNDAG IDVPVILGGA ALTPRFVQKD CREVYNGKVI YGRDAFADLR FMDALMDAKG NDNWNNLEGF ITDVPSGVGL DEETESSTVE RSTAEEKSQQ DAPSPQLPVT TVRSEAVPAE PTPTAPFLGS VVITEADVDI EEVFGFLDRN ALFAGQWQLR KVQQQSRDEY DAMLKEKAEP VLQQWVDRCL QESLLTPRAA YGYFPVGRDG NALRVFDASG ETELGRFDLP RQRSGNRYCI ADFFQDMTAD GRPGDVLPMQ AVTMGDKASE VAQELFKGDQ YSDYLYFHGL AVQMAEAMAE WVHARIRREL GFADPDGMPL RDVLAQRYRG SRYSFGYPAC PNVADSRQQL SWLGADRIGL SMDASDQLSP EQSTTALVAL HSKARYFSA // ID Q7UKY7_RHOBA Unreviewed; 1246 AA. AC Q7UKY7; DT 01-OCT-2003, integrated into UniProtKB/TrEMBL. DT 01-OCT-2003, sequence version 1. DT 27-MAY-2015, entry version 85. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CAD76493.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAD76493.1}; GN Name=metH {ECO:0000313|EMBL:CAD76493.1}; GN OrderedLocusNames=RB9857 {ECO:0000313|EMBL:CAD76493.1}; OS Rhodopirellula baltica (strain SH1). OC Bacteria; Planctomycetes; Planctomycetia; Planctomycetales; OC Planctomycetaceae; Rhodopirellula. OX NCBI_TaxID=243090 {ECO:0000313|EMBL:CAD76493.1, ECO:0000313|Proteomes:UP000001025}; RN [1] {ECO:0000313|EMBL:CAD76493.1, ECO:0000313|Proteomes:UP000001025} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SH1 {ECO:0000313|Proteomes:UP000001025}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; BX294150; CAD76493.1; -; Genomic_DNA. DR RefSeq; NP_869107.1; NC_005027.1. DR RefSeq; WP_011122502.1; NC_005027.1. DR ProteinModelPortal; Q7UKY7; -. DR SMR; Q7UKY7; 669-910. DR STRING; 243090.RB9857; -. DR EnsemblBacteria; CAD76493; CAD76493; RB9857. DR GeneID; 1791598; -. DR KEGG; rba:RB9857; -. DR PATRIC; 23250967; VBIRhoBal59814_4744. DR HOGENOM; HOG000251409; -. DR InParanoid; Q7UKY7; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR Proteomes; UP000001025; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001025}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAD76493.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001025}; KW Transferase {ECO:0000313|EMBL:CAD76493.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 263 263 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 326 326 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 327 327 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 779 779 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1246 AA; 139005 MW; CAF2825176B5109F CRC64; MIFIPSPAFG LSMLQATSTD QLLAELIRER ILMLDGAMGT MIQRLELDEA AVRSDRFADH HKDLKNFSDI LCLTHPEKIT EIHSKYYEAG SDIVETNSFG ASPIGMVEFD LPLELVNEIN VAAVACARKA ADQWTEKTPD KPRFVAGSIG PTTMQLAIST DVEDAAFRAT TFDKLADSYY AQVKSLCEAG VDILLPETAI DTLNLKSCLF AIQRYFDEGG RRVPVMVSGT FDKGGRTFVS GQSVEAFVTA LSHFPVLSVG MNCALGPDIM RPHVEEMSKA TGLPISCHPN AGLPNEMGAF DLDPKPMAEI VGEYADNGWI NILGGCCGTT PDHIRVMTER VQGCKPKQED KSGPVWTRLS GQLPMVMRPE IPFTMVGERT NVTGSRKFAR LIRNEEYDEA VEVAREQVEN GATIIDVNFD DALLDGVEAM TRFLRLIAGD SVVAAVPVMI DSSRWEVIEA GLQNVQGKAI VNSISLKDGE EEFLRRARLV RQYGAATVVM AFDEEGQAAD EDNKVRICKR AYDLLVNEVH FPPEDIIFDP NILTVATGME EHNNYAVDFV NAVERIKKEC PGAKTSGGVS NISFSFRGND PVREAIHSAF LYRAVKAGLD MGIVNAGQLE VYEEIPKDLL EHVEDVLWNR RDDATDRMLE FAETVKGSGK KKSGEDLTWR ENSIEERMKH ALIKGIDKYI VEDTEEARQH YDKCLHIIEG PLMAGMSVVG DLFGQGKMFL PQVVKSARVM KKAVAYLEPF MEQEKIESGT QDHKARGKFL IATVKGDVHD IGKNIVGVVL QCNNYEVIDL GVMVSSEKIL EEAVKQDADM IGLSGLITPS LDEMVHVARE MKRIGMKKPL LVGGATTSAK HTAVRIAPAY DGPVLHVLDA SRSVGVVEKL LSDESRDAFL EANVSEQEKL VSSFRERKQT LVSYEQALEK RFQTDWETVR IDQPEFIGTK VLEDFPLATL REYIDWSPYF MTWELKGKYP KIFQDETVGP IAKEVFEKAN KMLDRVIDEK LIRAKGVYGF WPAASDGDDI IVYTDESRTE ERTRFHCLRQ QWERRGQKDF RSLADYIAPV DSGRKDYLGG FAVTAGLGAE ELSMRFKKEL DDESSIIASA VADRCAEAFA EYLHQQVRQQ WQYGKEENLS NEDMIAEKYR GIRPAAGYPA CPDHTEKRTL FDLLEAEKNT GINLTESYAM SPGASVSGLY FSHPDAKYFT VDRMTKDQIE SYAARKGWPI SEVERWLSPN LAYDPS // ID Q7V1J3_PROMP Unreviewed; 1186 AA. AC Q7V1J3; DT 01-OCT-2003, integrated into UniProtKB/TrEMBL. DT 01-OCT-2003, sequence version 1. DT 27-MAY-2015, entry version 88. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CAE19336.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAE19336.1}; GN Name=metH {ECO:0000313|EMBL:CAE19336.1}; GN OrderedLocusNames=PMM0877 {ECO:0000313|EMBL:CAE19336.1}; OS Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / MED4). OC Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae; OC Prochlorococcus. OX NCBI_TaxID=59919 {ECO:0000313|EMBL:CAE19336.1, ECO:0000313|Proteomes:UP000001026}; RN [1] {ECO:0000313|EMBL:CAE19336.1, ECO:0000313|Proteomes:UP000001026} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCMP1986 / MED4 {ECO:0000313|Proteomes:UP000001026}; RX PubMed=12917642; DOI=10.1038/nature01947; RA Rocap G., Larimer F.W., Lamerdin J., Malfatti S., Chain P., RA Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., RA Johnson Z.I., Land M., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; BX548174; CAE19336.1; -; Genomic_DNA. DR RefSeq; NP_892995.1; NC_005072.1. DR RefSeq; WP_011132510.1; NC_005072.1. DR ProteinModelPortal; Q7V1J3; -. DR STRING; 59919.PMM0877; -. DR EnsemblBacteria; CAE19336; CAE19336; PMM0877. DR KEGG; pmm:PMM0877; -. DR PATRIC; 23032670; VBIProMar68066_1000. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PMAR59919:GJMQ-902-MONOMER; -. DR Proteomes; UP000001026; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001026}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAE19336.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001026}; KW Transferase {ECO:0000313|EMBL:CAE19336.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 745 745 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1186 AA; 132094 MW; 6828E7F77B40C4F3 CRC64; MVSFRNYLNR DDKPIIIFDG GTGTSFQNLN LSSHDFGGDD LEGCNENLVL SSPNTVEQVH NSFLEAGCHV IETNTFGASS IVLDEYSISN KAYEINKKAA QIAKKCANLF SSINTPRFVA GSIGPTTKLP TLGHISFDKL KDSYEEQING LIDGGIDLLL IETCQDVLQI KSALSASQEV IKNRNIELPI MISITMETTG TMLVGSDIAS ALTILEPYNI DILGLNCATG PVQMKEHIKY LAENSPFAIS CIPNAGLPEN IGGVAHYKLT PLELKMQLMN FIYDFNVQLI GGCCGTTPEH IKHLSSIIEE IVDKKINKRL PTVKTNFVPS AASIYNAVPY KQDNSILIVG ERLNASGSKK VRELLNEDDW DGLLSIAKQQ QKENAHILDV NVDYVGRDGV KDMKEITSRL VTNINLPLMI DSTEADKMES GLKTVGGKCI INSTNYEDGD DRFNQVLRLA LDYGAGIVIG TIDEDGMART SQKKYDIAKR ALIKTRSSGL ADYEIFFDPL ALPISTGIEE DRLNAKATIE AISKIRKSFP DIHIILGISN ISFGLSPLSR INLNSIFLDE CIKAGLDSAI IAPNKILPLS KISAETKKLC LDLIYDRRNF ENEICIYDPL VELTKAFQDI TISDFKKGST SNKNLTLEEK LKNHIVDGEK IGLEEQLNNA LKKYKPLEII NTYLLDGMKV VGELFGSGQM QLPFVLQSAE TMKFAVSVLE PHMETVDEKI SNGKLLIATV KGDVHDIGKN LVDIILSNNG FDVINLGIKQ DVSAIIDAQK KHKADCIAMS GLLVKSTAFM KDNLEAFNNA EINVPVILGG AALTPKFVNE DCSQIYKGKI LYGKDAFTDL QFMNDYMDSK KKGNWSNENG FTNTDDIQIK LASPRSSAKD KNLNKNFEKT KSIQLIENFN RSNFVEEEEP IKAPFLGTRV LQDIEIDFDK LIFYLDKKAL FSGQWQIKKN KGQSVEEYNN YLDSYANPLL EKWINIILDK GLISPKVVYG YFRCGRNDNS IYLFDNVSNK RISEFNFPRQ KSGNNLCIAD FYCDLKNNDP VDIFPMQAVT MGEIASEYSQ ELFKADKYSD YLIFHGLTVQ LAEALAEYVH SIVRIECGFK SYEPNNNRDI LAQKYRGARY SFGYPACPKV SDSNIQLSLL DTKRINLTMD ESEQLHPEQS TTAIISLHSK AKYFSA // ID Q7V7L3_PROMM Unreviewed; 1214 AA. AC Q7V7L3; DT 01-OCT-2003, integrated into UniProtKB/TrEMBL. DT 01-OCT-2003, sequence version 1. DT 29-APR-2015, entry version 86. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CAE20904.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAE20904.1}; GN Name=metH {ECO:0000313|EMBL:CAE20904.1}; GN OrderedLocusNames=PMT_0729 {ECO:0000313|EMBL:CAE20904.1}; OS Prochlorococcus marinus (strain MIT 9313). OC Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae; OC Prochlorococcus. OX NCBI_TaxID=74547 {ECO:0000313|EMBL:CAE20904.1, ECO:0000313|Proteomes:UP000001423}; RN [1] {ECO:0000313|EMBL:CAE20904.1, ECO:0000313|Proteomes:UP000001423} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MIT 9313 {ECO:0000313|Proteomes:UP000001423}; RX PubMed=12917642; DOI=10.1038/nature01947; RA Rocap G., Larimer F.W., Lamerdin J., Malfatti S., Chain P., RA Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., RA Johnson Z.I., Land M., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; BX548175; CAE20904.1; -; Genomic_DNA. DR RefSeq; NP_894561.1; NC_005071.1. DR RefSeq; WP_011130107.1; NC_005071.1. DR ProteinModelPortal; Q7V7L3; -. DR STRING; 74547.PMT0729; -. DR EnsemblBacteria; CAE20904; CAE20904; PMT_0729. DR KEGG; pmt:PMT0729; -. DR PATRIC; 23009437; VBIProMar135351_0873. DR eggNOG; COG1410; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR Proteomes; UP000001423; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001423}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAE20904.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001423}; KW Transferase {ECO:0000313|EMBL:CAE20904.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 242 242 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 766 766 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1214 AA; 134266 MW; 03E9D4E68D257350 CRC64; MRDRMTAGPL DITRPESAFL ARLHSSERPV LVFDGATGTS LQKQNLSADD FGGALLEGCN ENLVVTRPDA VKEVHRQFLE SGCDVIETNS FGAASIVLAE YGLEDQAFEL NRQAAQLAKS MAVQYSTKDQ PRFVAGSIGP TTKLPTLGHI AFDTMRDSFQ EQAEGLLAGD VDLFIVETCQ DVLQIKAALQ GIECAFLKAN ERRPIMVSVT METTGTMLLG SDIASVVTIL EPFPIDILGL NCATGPEQMK EHIRYLSEHS PFTISCIPNA GLPENIGGVA HYRLKPLELK MQLMHFVEDL GVQVIGGCCG TTPEHTSALA ELAKEMRAAQ RPCRQGENEQ QRQLFGYEPS AASIYGITPY HQDNSFLIIG ERLNASGSKK VRELLNSEDW DGLVGLARGQ LKENAHILDV NVDYVGRDGE KDMNQLVSRL VTNINLPLML DSTEWQKMEA GLKVAGGKCI LNSTNYEDGE ERFFKVLDLA KKYGAGLVIG TIDENGMART AMQKVAIAKR AYRDATEYGI PAHEIFYDPL ALPISTGIEE DRRNGLETIE AIRVIREELE AVHVVLGVSN VSFGLSPAAR ITLNSVFLHD CTDAGMDAAI VSPAKILPLN KVSDEQQKIC RDLINDHRRF ENEICTYDPL TELTSLFEGV SAKEARASGP SLADLPVEDR LKQHIIDGER IGLNEALDEG LESYKPLQLV NTFLLDGMKV VGELFGSGKM QLPFVLQSAQ TMKAAVAYLE PYMEKSAGDK SSKAKFLIAT VKGDVHDIGK NLVDIILTNN GYEVINLGIK QDSASIINAQ MTHQADCIAM SGLLVKSTAF MKSNLQEFND SGITVPVILG GAALTPRFVN HDCSEVYKGK LIYGKDAFTD LRFMDAYVKA LSNDRWDDCR GFLDGTPDGL TLGGQSTESD SPHSSNDEDP QEENQKNIQD INLAVNTNRS EKVSQEDAVT PPFLGSKHLK LDKIPLDEII QYLDRNALFS GQWQIRKRKD QSREQYDQYI NDEIEPILQH WLHRIRNESL LHPGVAYGYF PCGRRDNDLL VFNSEGQSLL GKFNLPRQKG GNRYCIADFY RDLEGGLPKD ILPMQAVTMG ENASIFAQKL FESDAYTDYL FFHGLAVQLA EALAEWTHSL IRCECGFKSD EPKTLQDVLA QRYRGSRFSF GYPACPNVGD SRQQLNWLKA DLIGLTMDPN DQLHPEQSTT ALVTLHSKAR YFSA // ID Q7VBY3_PROMA Unreviewed; 1182 AA. AC Q7VBY3; DT 01-OCT-2003, integrated into UniProtKB/TrEMBL. DT 01-OCT-2003, sequence version 1. DT 27-MAY-2015, entry version 87. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AAQ00004.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AAQ00004.1}; GN Name=metH {ECO:0000313|EMBL:AAQ00004.1}; GN OrderedLocusNames=Pro_0959 {ECO:0000313|EMBL:AAQ00004.1}; OS Prochlorococcus marinus (strain SARG / CCMP1375 / SS120). OC Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae; OC Prochlorococcus. OX NCBI_TaxID=167539 {ECO:0000313|EMBL:AAQ00004.1, ECO:0000313|Proteomes:UP000001420}; RN [1] {ECO:0000313|EMBL:AAQ00004.1, ECO:0000313|Proteomes:UP000001420} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SARG / CCMP1375 / SS120 {ECO:0000313|Proteomes:UP000001420}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AE017126; AAQ00004.1; -; Genomic_DNA. DR RefSeq; NP_875351.1; NC_005042.1. DR RefSeq; WP_011125111.1; NC_005042.1. DR ProteinModelPortal; Q7VBY3; -. DR STRING; 167539.Pro0959; -. DR EnsemblBacteria; AAQ00004; AAQ00004; Pro_0959. DR GeneID; 1462341; -. DR KEGG; pma:Pro_0959; -. DR PATRIC; 23028633; VBIProMar8617_1008. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PMAR167539:GJN2-985-MONOMER; -. DR Proteomes; UP000001420; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001420}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AAQ00004.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001420}; KW Transferase {ECO:0000313|EMBL:AAQ00004.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 742 742 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1182 AA; 131761 MW; 8DBEBCED2E7E560F CRC64; MIDFKSYINS SKSSVLVFDG AMGTSLQSLN LTADDFGGTL LEGCNENLVL TNPQAVRNVH RSYLEVGCDV IETNTFGATS IVLEEYNLQD KTYEINLEAA RLAKGIVKEF STDDKPRFVA GSVGPTTKLP TLGHISFDKL SSSYQEQIEA LIDGEVDLIL LETCQDVLQI KSALVGINNA FEIKDKYLPI MVSVTMETTG TMLLGTDISA VVNILAPFNI DILGLNCATG PHEMKRHIEY LSEYSPFLIS CIPNAGLPEN IGGKAHYRLT PIELKMQLSH FINDLGVKVI GGCCGTGPTH IEQLVKLSQE VIDTIEQKEF KKNTDYGVSS LYEMTSYNQD QSILIIGERL NASGSRKVRE LLNENNWDGL IAVAKDQLKE QAHVLDVNVD YVGRDGVEDM SKVVSQLVTN INLPLMLDST DYTKMESGLK NAGGKCILNS TNYEDGPERF YKVLDLCKKY GSAVVIGTID ENGMARTSDL KIKIAERSFN DATKYGIAEF DIFYDPLVLP ISTGLEEDRN NASETIKAIS ILRKRFPHVH ITLGISNVSF GLNPAARITL NSVFLEECIV AGLDSAIISP AKILPTQKIK PEHRKVCIDL IYDKRLYKDD ICIYDPLTEL TSLFSDVTSQ SLKQRTDELK SLPLEERLKK HIIDGEKNDL REHLLVALDD YKALDIINNF LLDGMKVVGE LFGSGKMQLP FVLQSAETMK YAVSVLEPYM ETNESVQSKG KFIIATVKGD VHDIGKNLVD IILTNNGYDV INLGIKQDIS EIINAQKKFQ ADCIAMSGLL VKSTAFMKDN LQELNNNLIS IPVILGGAAL TPKFVNQDCN NVYKGQVIYG KDAFTDLTFM DAYMKAKSNA KWDNYKGFLD HNPTGIQLFE KSNCSISEAA EKSSPTKTNS IKLSTSKSPV IKEEISISPP FIGSKIVHDD NINLDNLMFY LDKRALFAGQ WQFKKTKDQT KESYQEFIDT EATSILNHWI NRIKEDNLIS PAFVYGYFPC GSNGNNLEIF DFDGKKRIGC FTFPRQKANN KYCISDFYNP LKENSPVDYI PMQAVTMGNV SSEFAQVLFA EDRYSDYLYF HGLTVQLAEA LAEYSHANIR QECGFVINEP DNIRDILAQR YQGCRYSFGY PACPNVSDSK KQLDWLQASR IGISMDESDQ LIPEQSTTAI ISLHSQAKYF SA // ID Q7VTE8_BORPE Unreviewed; 1257 AA. AC Q7VTE8; DT 01-OCT-2003, integrated into UniProtKB/TrEMBL. DT 01-OCT-2003, sequence version 1. DT 27-MAY-2015, entry version 85. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:CAE43853.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAE43853.1}; GN Name=metH {ECO:0000313|EMBL:CAE43853.1}; GN OrderedLocusNames=BP3594 {ECO:0000313|EMBL:CAE43853.1}; OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=257313 {ECO:0000313|Proteomes:UP000002676}; RN [1] {ECO:0000313|Proteomes:UP000002676} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251 RC {ECO:0000313|Proteomes:UP000002676}; RX PubMed=12910271; DOI=10.1038/ng1227; RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N., RA Harris D.E., Holden M.T., Churcher C.M., Bentley S.D., Mungall K.L., RA Cerdeno-Tarraga A.M., Temple L., James K., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; BX640421; CAE43853.1; -; Genomic_DNA. DR RefSeq; NP_882106.1; NC_002929.2. DR RefSeq; WP_010931556.1; NC_002929.2. DR ProteinModelPortal; Q7VTE8; -. DR SMR; Q7VTE8; 673-928. DR STRING; 257313.BP3594; -. DR EnsemblBacteria; CAE43853; CAE43853; BP3594. DR GeneID; 2667253; -. DR KEGG; bpe:BP3594; -. DR PATRIC; 21160848; VBIBorPer7866_3889. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; BPER257313:BP3594-MONOMER; -. DR Proteomes; UP000002676; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002676}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAE43853.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002676}; KW Transferase {ECO:0000313|EMBL:CAE43853.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 256 256 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 789 789 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1257 AA; 138068 MW; 9D35AFABDEA26E7D CRC64; MPYPRIPFPL SAYTHGGEFV RQLDKRILIL DGAMGTMIQR YKLGEADFRG ERFAEHHKDL KGDNELLSLV RPDVIAEIHR QYLEAGADVI ETNTFGATSI AQGDYDLPEL AYEMNLESAR LARAACDAYS TPEHPRFVAG ALGPQPKTAS ISPDVNDPGA RNVTFDELRA AYVEQLNGLL DGGIDIVLIE TIFDTLNAKA AIFAVEEAFE ARGVRLPVMI SGTVTDASGR ILSGQTVEAF WNSVRHARPV TIGLNCALGA ALMRPYVAEL SKICDTYVCV YPNAGLPNPM AETGFDETPA DTSALLEEFA QAGLVNMAGG CCGTTPEHIR AIAGKVAALT PRAVPEVPVK TRLSGLEALN IDDETLFVNV GERTNVTGSK MFARLVREEK YDEALAVARQ QVENGAQIID VNMDEAMLDS VACMHRFLNL IASEPDIARV PVMIDSSKWE VIETGLKCVQ GKAVVNSISM KEGEEPFRHH ARLCRRYGAA MVVMAFDEQG QADSLERRKE ICGRAYRILV EEEGFPPEDI IFDPNVFAVA TGIDEHNHYA VDFIEGARWI RANLPHARIS GGISNVSFSF RGNEPMREAI HTVFLYYAIE AGLTMGIVNA GQLGVYADLA PHLRDLVEDV ILDRPEPVGR SDSADERSPT ERLVQFAETV KGSGAKKEED LTWRTGSVEQ RLAHALVHGI TTFIVEDTEE VRQQVAARGG RTIEVIEGPL MDGMNVVGDL FGAGKMFLPQ VVKSARVMKQ AVAHLIPFIE EEKRQIAAAG GDVRAKGKIV IATVKGDVHD IGKNIVSVVL QCNNFEVVNM GVMVPCAQIL QKAKDENADM IGLSGLITPS LEEMAYVASE MQRDPYFRER AMPLMIGGAT TSRVHTAVKI APNYDGPVIY VPDASRSVGV ATSLMSDQAP AYLAELAQEY EDVRRCHANR KAVPLVSLAE ARAARPQIDW SGYQPPRPKF LGRRAFKSYD LAEIARYIDW GPFFQTWSLF GPFPAILDDK VVGEQARKVY EEGQAMLKRI IDGRWLTASG VVGFYPANRV NDEDIEVYAD ETRSEMLFTY RNLRQQGVKR EGVSNKCLAD YIAPRDSGLL DYIGMFAVTA GLGIEKKEAE FQAALDDYSS IMLKSLADRL AEAFAECMHA RVRRDLWGYA ADEALSNDEL IAEKYSGIRP APGYPACPEH VVKTDLFRVL DAADVGMELT DSYAMFPASS VSGFYFSHPE SQYFNVGNIG ADQLADYVAR SGRAEEDVRR TLAPNLG // ID Q7W3P8_BORPA Unreviewed; 1257 AA. AC Q7W3P8; DT 01-OCT-2003, integrated into UniProtKB/TrEMBL. DT 01-OCT-2003, sequence version 1. DT 01-APR-2015, entry version 87. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:CAE39266.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAE39266.1}; GN Name=metH {ECO:0000313|EMBL:CAE39266.1}; GN OrderedLocusNames=BPP3983 {ECO:0000313|EMBL:CAE39266.1}; OS Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=257311 {ECO:0000313|Proteomes:UP000001421}; RN [1] {ECO:0000313|Proteomes:UP000001421} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=12822 / ATCC BAA-587 / NCTC 13253 RC {ECO:0000313|Proteomes:UP000001421}; RX PubMed=12910271; DOI=10.1038/ng1227; RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N., RA Harris D.E., Holden M.T., Churcher C.M., Bentley S.D., Mungall K.L., RA Cerdeno-Tarraga A.M., Temple L., James K., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; BX640435; CAE39266.1; -; Genomic_DNA. DR RefSeq; NP_886129.1; NC_002928.3. DR RefSeq; WP_010929331.1; NC_002928.3. DR ProteinModelPortal; Q7W3P8; -. DR SMR; Q7W3P8; 673-928. DR STRING; 257311.BPP3983; -. DR EnsemblBacteria; CAE39266; CAE39266; BPP3983. DR KEGG; bpa:BPP3983; -. DR PATRIC; 21152044; VBIBorPar43418_4180. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; BPAR257311:BPP3983-MONOMER; -. DR Proteomes; UP000001421; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001421}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAE39266.1}; KW Transferase {ECO:0000313|EMBL:CAE39266.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 256 256 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 789 789 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1257 AA; 138141 MW; 83115B1A2FEB9F1C CRC64; MPYPRIPFPL SAYTHGGEFV RQLDKRILIL DGAMGTMIQR YKLGEADFRG ERFAEHHKDL KGDNELLSLV RPDVISEIHR QYLEAGADVI ETNTFGATSI AQGDYDLPEL AYEMNLESAR LARAACDAYS TPEHPRFVAG ALGPQPKTAS ISPDVNDPGA RNVTFDELRA AYVEQLNGLL DGGIDIVLIE TIFDTLNAKA AIFAVEETFE ARGVRLPVMI SGTVTDASGR ILSGQTVEAF WNSVRHARPV TIGLNCALGA ALMRPYVAEL SKICDTYVCV YPNAGLPNPM AETGFDETPA DTSALLEEFA QAGLVNMAGG CCGTTPEHIR AIAGKVASLT PRAVPEVPVK TRLSGLEALN IDDETLFVNV GERTNVTGSK MFARLVREEK YDEALAVARQ QVENGAQIID VNMDEAMLDS VACMHRFLNL IASEPDIARV PVMIDSSKWE VIETGLKCVQ GKAVVNSISM KEGEEPFRHH ARLCRRYGAA MVVMAFDEQG QADSLERRKE ICGRAYRILV EEEGFPPEDI IFDPNVFAVA TGIDEHNHYA VDFIEGARWI RANLPHARIS GGISNVSFSF RGNEPMREAI HTVFLYYAIE AGLTMGIVNA GQLGVYADLA PHLRDLVEDV ILDRPEPVGR SDSADERSPT ERLVQFAETV KGSGAKKEED LTWRTGSVEQ RLAHALVHGI TTFIVEDTEE VRQQVAARGG RTIEVIEGPL MDGMNVVGDL FGAGKMFLPQ VVKSARVMKQ AVAHLIPFIE EEKRQIAAAG GDVRAKGKIV IATVKGDVHD IGKNIVSVVL QCNNFEVVNM GVMVPCAQIL QKAKDENADM IGLSGLITPS LEEMAYVASE MQRDPYFRER AMPLMIGGAT TSRVHTAVKI APNYDGSVIY VPDASRSVGV ATSLMSDQAP AYLAELAQEY EDVRRRHANR KAVPLVSLAE ARAARPQIDW SGYQPPRPKF LGRRAFKSYD LAEIARYIDW GPFFQTWSLF GPFPAILDDK VVGEQARKVY EEGQAMLKRI IDGRWLTASG VVGFYPANRV NDEDIEVYAD ETRSEVLFTY RNLRQQGVKR EGVSNKCLAD YIAPRDSGLL DYIGMFAVTA GLGIEKKEAE FQAALDDYSS IMLKSLADRL AEAFAECMHA RVRRDLWGYA ADEALSNDEL IAEKYSGIRP APGYPACPEH VVKTDLFRVL DAADVGMELT DSYAMFPASS VSGFYFSHPE SQYFNVGNIG ADQLADYVAR SGRAEEDVRR TLAPNLG // ID Q7X1M0_9BACT Unreviewed; 220 AA. AC Q7X1M0; DT 01-OCT-2003, integrated into UniProtKB/TrEMBL. DT 01-OCT-2003, sequence version 1. DT 29-OCT-2014, entry version 31. DE SubName: Full=Lfe114p1 {ECO:0000313|EMBL:AAO38280.1}; DE Flags: Fragment; OS Leptospirillum ferrooxidans. OC Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; Leptospirillum. OX NCBI_TaxID=180 {ECO:0000313|EMBL:AAO38280.1}; RN [1] {ECO:0000313|EMBL:AAO38280.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=12808145; DOI=10.1073/pnas.1230487100; RA Parro V., Moreno-Paz M.; RT "Gene function analysis in environmental isolates: the nif regulon of RT the strict iron oxidizing bacterium Leptospirillum ferrooxidans."; RL Proc. Natl. Acad. Sci. U.S.A. 100:7883-7888(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; AY204363; AAO38280.1; -; Genomic_DNA. DR ProteinModelPortal; Q7X1M0; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; FT NON_TER 220 220 {ECO:0000313|EMBL:AAO38280.1}. SQ SEQUENCE 220 AA; 23973 MW; 3BECA2997F0FAFAF CRC64; MKPLLERLKY EVLLLDGSMG ALLQSRGLPA GYAPDLWNIE KPQEIQAVHT EYVNAGSDII LTNTFGASRL RLSEYNSQDR IREINFHAVE LAQRAARGKA YVAGDIGPSG TTIAPFGDLP FDDAIAIFYE QAKLLLEAGA DLIAIETMFD IQEMRAALIG VREAVNGRIP VMALMTFNMD GITDSGSDPE TAASVLEGFS VGHHGTELLP LDRRPWVLSS // ID Q7XEH2_ORYSJ Unreviewed; 335 AA. AC Q7XEH2; DT 01-OCT-2003, integrated into UniProtKB/TrEMBL. DT 01-OCT-2003, sequence version 1. DT 01-APR-2015, entry version 82. DE SubName: Full=Homocysteine S-methyltransferase 2, putative, expressed {ECO:0000313|EMBL:AAP53817.1}; DE SubName: Full=Os10g0422200 protein {ECO:0000313|EMBL:BAF26542.1}; DE SubName: Full=cDNA clone:001-123-H11, full insert sequence {ECO:0000313|EMBL:BAG88938.1}; DE SubName: Full=cDNA clone:J033080I03, full insert sequence {ECO:0000313|EMBL:BAG95344.1}; DE SubName: Full=cDNA clone:J033138N02, full insert sequence {ECO:0000313|EMBL:BAG96239.1}; GN Name=Os10g0422200 {ECO:0000313|EMBL:BAF26542.1}; GN OrderedLocusNames=LOC_Os10g28630 {ECO:0000313|EMBL:AAP53817.1}; GN ORFNames=OsJ_31561 {ECO:0000313|EMBL:EAZ16115.1}; 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 {ECO:0000313|EMBL:AAP53817.1, ECO:0000313|Proteomes:UP000000763}; RN [1] {ECO:0000313|EMBL:AAP53817.1, ECO:0000313|Proteomes:UP000000763} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000000763}; RX PubMed=12791992; DOI=10.1126/science.1083523; RA Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., RA Thompson S., Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., RA Henry D., Oates R., Palmer M., Pries G., Gibson J., Anderson H., RA Paradkar M., Crane L., Dale J., Carver M.B., Wood T., Frisch D., RA Engler F., Soderlund C., Palmer L.E., Teytelman L., Nascimento L., RA De la Bastide M., Spiegel L., Ware D., O'Shaughnessy A., Dike S., RA Dedhia N., Preston R., Huang E., Ferraro K., Kuit K., Miller B., RA Zutavern T., Katzenberger F., Muller S., Balija V., Martienssen R.A., RA Stein L., Minx P., Johnson D., Cordum H., Mardis E., Cheng Z., RA Jiang J., Wilson R., McCombie W.R., Wing R.A., Yuan Q., Ouyang S., RA Liu J., Jones K.M., Gansberger K., Moffat K., Hill J., Tsitrin T., RA Overton L., Bera J., Kim M., Jin S., Tallon L., Ciecko A., Pai G., RA Van Aken S., Utterback T., Reidmuller S., Bormann J., Feldblyum T., RA Hsiao J., Zismann V., Blunt S., de Vazeille A.R., Shaffer T., Koo H., RA Suh B., Yang Q., Haas B., Peterson J., Pertea M., Volfovsky N., RA Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R., RA Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., RA Bowers J.E., Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.; RT "In-depth view of structure, activity, and evolution of rice RT chromosome 10."; RL Science 300:1566-1569(2003). RN [2] {ECO:0000313|EMBL:BAG88938.1} 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 [3] {ECO:0000313|EMBL:AAP53817.1} RP NUCLEOTIDE SEQUENCE. RA Buell C.R., Wing R.A., McCombie W.R., Messing J., Yuan Q., Ouyang S.; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:BAF26542.1} RP NUCLEOTIDE SEQUENCE. RG International Rice Genome Sequencing Project; RA Matsumoto T., Wu J., Kanamori H., Katayose Y., Fujisawa M., Namiki N., RA Mizuno H., Yamamoto K., Antonio B.A., Baba T., Sakata K., Nagamura Y., RA Aoki H., Arikawa K., Arita K., Bito T., Chiden Y., Fujitsuka N., RA Fukunaka R., Hamada M., Harada C., Hayashi A., Hijishita S., Honda M., RA Hosokawa S., Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., RA Ito K., Ito S., Ito T., Ito Y., Ito Y., Iwabuchi A., Kamiya K., RA Karasawa W., Kurita K., Katagiri S., Kikuta A., Kobayashi H., RA Kobayashi N., Machita K., Maehara T., Masukawa M., Mizubayashi T., RA Mukai Y., Nagasaki H., Nagata Y., Naito S., Nakashima M., Nakama Y., RA Nakamichi Y., Nakamura M., Meguro A., Negishi M., Ohta I., Ohta T., RA Okamoto M., Ono N., Saji S., Sakaguchi M., Sakai K., Shibata M., RA Shimokawa T., Song J., Takazaki Y., Terasawa K., Tsugane M., Tsuji K., RA Ueda S., Waki K., Yamagata H., Yamamoto M., Yamamoto S., Yamane H., RA Yoshiki S., Yoshihara R., Yukawa K., Zhong H., Yano M., Yuan Q., RA Ouyang S., Liu J., Jones K.M., Gansberger K., Moffat K., Hill J., RA Bera J., Fadrosh D., Jin S., Johri S., Kim M., Overton L., Reardon M., RA Tsitrin T., Vuong H., Weaver B., Ciecko A., Tallon L., Jackson J., RA Pai G., Aken S.V., Utterback T., Reidmuller S., Feldblyum T., RA Hsiao J., Zismann V., Iobst S., de Vazeille A.R., Buell C.R., Ying K., RA Li Y., Lu T., Huang Y., Zhao Q., Feng Q., Zhang L., Zhu J., Weng Q., RA Mu J., Lu Y., Fan D., Liu Y., Guan J., Zhang Y., Yu S., Liu X., RA Zhang Y., Hong G., Han B., Choisne N., Demange N., Orjeda G., RA Samain S., Cattolico L., Pelletier E., Couloux A., Segurens B., RA Wincker P., D'Hont A., Scarpelli C., Weissenbach J., Salanoubat M., RA Quetier F., Yu Y., Kim H.R., Rambo T., Currie J., Collura K., Luo M., RA Yang T., Ammiraju J.S.S., Engler F., Soderlund C., Wing R.A., RA Palmer L.E., de la Bastide M., Spiegel L., Nascimento L., Zutavern T., RA O'Shaughnessy A., Dike S., Dedhia N., Preston R., Balija V., RA McCombie W.R., Chow T., Chen H., Chung M., Chen C., Shaw J., Wu H., RA Hsiao K., Chao Y., Chu M., Cheng C., Hour A., Lee P., Lin S., Lin Y., RA Liou J., Liu S., Hsing Y., Raghuvanshi S., Mohanty A., Bharti A.K., RA Gaur A., Gupta V., Kumar D., Ravi V., Vij S., Kapur A., Khurana P., RA Khurana P., Khurana J.P., Tyagi A.K., Gaikwad K., Singh A., Dalal V., RA Srivastava S., Dixit A., Pal A.K., Ghazi I.A., Yadav M., Pandit A., RA Bhargava A., Sureshbabu K., Batra K., Sharma T.R., Mohapatra T., RA Singh N.K., Messing J., Nelson A.B., Fuks G., Kavchok S., Keizer G., RA Linton E., Llaca V., Song R., Tanyolac B., Young S., Ho-Il K., RA Hahn J.H., Sangsakoo G., Vanavichit A., de Mattos Luiz.A.T., RA Zimmer P.D., Malone G., Dellagostin O., de Oliveira A.C., Bevan M., RA Bancroft I., Minx P., Cordum H., Wilson R., Cheng Z., Jin W., RA Jiang J., Leong S.A., Iwama H., Gojobori T., Itoh T., Niimura Y., RA Fujii Y., Habara T., Sakai H., Sato Y., Wilson G., Kumar K., RA McCouch S., Juretic N., Hoen D., Wright S., Bruskiewich R., Bureau T., RA Miyao A., Hirochika H., Nishikawa T., Kadowaki K., Sugiura M., RA Burr B., Sasaki T.; RT "The map-based sequence of the rice genome."; RL Nature 436:793-800(2005). RN [5] {ECO:0000313|Proteomes:UP000000763} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000000763}; 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 [6] {ECO:0000313|EMBL:EAZ16115.1, ECO:0000313|Proteomes:UP000000763} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000000763}; 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 [7] {ECO:0000313|EMBL:BAF26542.1} RP NUCLEOTIDE SEQUENCE. RG IRGSP(International Rice Genome Sequencing Project); RT "Oryza sativa nipponbare(GA3) genomic DNA, chromosome 10."; RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases. RN [8] {ECO:0000313|EMBL:BAF26542.1} RP NUCLEOTIDE SEQUENCE. RG The Rice Annotation Project (RAP); RT "The Second Rice Annotation Project Meeting (RAP2)."; RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases. RN [9] {ECO:0000313|EMBL:BAF26542.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=16381971; DOI=10.1093/nar/gkj094; RA Ohyanagi H., Tanaka T., Sakai H., Shigemoto Y., Yamaguchi K., RA Habara T., Fujii Y., Antonio B.A., Nagamura Y., Imanishi T., Ikeo K., RA Itoh T., Gojobori T., Sasaki T.; RT "The Rice Annotation Project Database (RAP-DB): hub for Oryza sativa RT ssp. japonica genome information."; RL Nucleic Acids Res. 34:D741-D744(2006). RN [10] {ECO:0000313|EMBL:AAP53817.1} RP NUCLEOTIDE SEQUENCE. RA Buell R.; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. RN [11] {ECO:0000313|EMBL:EAZ16115.1} 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 [12] {ECO:0000313|EMBL:BAF26542.1} RP NUCLEOTIDE SEQUENCE. RG The Rice Annotation Project (RAP); RA Itoh T., Tanaka T., Barrero R.A., Yamasaki C., Fujii Y., Hilton P.B., RA Antonio B.A., Aono H., Apweiler R., Bruskiewich R., Bureau T., RA Burr F., Costa de Oliveira A., Fuks G., Habara T., Haberer G., Han B., RA Harada E., Hiraki A.T., Hirochika H., Hoen D., Hokari H., Hosokawa S., RA Hsing Y., Ikawa H., Ikeo K., Imanishi T., Ito Y., Jaiswal P., RA Kanno M., Kawahara Y., Kawamura T., Kawashima H., Khurana J.P., RA Kikuchi S., Komatsu S., Koyanagi K.O., Kubooka H., Lieberherr D., RA Lin Y.C., Lonsdale D., Matsumoto T., Matsuya A., McCombie W.R., RA Messing J., Miyao A., Mulder N., Nagamura Y., Nam J., Namiki N., RA Numa H., Nurimoto S., O'donovan C., Ohyanagi H., Okido T., Oota S., RA Osato N., Palmer L.E., Quetier F., Raghuvanshi S., Saichi N., RA Sakai H., Sakai Y., Sakata K., Sakurai T., Sato F., Sato Y., RA Schoof H., Seki M., Shibata M., Shimizu Y., Shinozaki K., Shinso Y., RA Singh N.K., Smith-White B., Takeda J., Tanino M., Tatusova T., RA Thongjuea S., Todokoro F., Tsugane M., Tyagi A.K., Vanavichit A., RA Wang A., Wing R.A., Yamaguchi K., Yamamoto M., Yamamoto N., Yu Y., RA Zhang H., Zhao Q., Higo K., Burr B., Gojobori T., Sasaki T.; RT "Curated Genome Annotation of Oryza sativa ssp. japonica and RT Comparative Genome Analysis with Arabidopsis thaliana."; RL Genome Res. 17:175-183(2007). RN [13] {ECO:0000313|EMBL:BAF26542.1} RP NUCLEOTIDE SEQUENCE. RG The Rice Annotation Project (RAP); RA Tanaka T., Antonio B.A., Kikuchi S., Matsumoto T., Nagamura Y., RA Numa H., Sakai H., Wu J., Itoh T., Sasaki T., Aono R., Fujii Y., RA Habara T., Harada E., Kanno M., Kawahara Y., Kawashima H., Kubooka H., RA Matsuya A., Nakaoka H., Saichi N., Sanbonmatsu R., Sato Y., Shinso Y., RA Suzuki M., Takeda J., Tanino M., Todokoro F., Yamaguchi K., RA Yamamoto N., Yamasaki C., Imanishi T., Okido T., Tada M., Ikeo K., RA Tateno Y., Gojobori T., Lin Y.C., Wei F.J., Hsing Y.I., Zhao Q., RA Han B., Kramer M.R., McCombie R.W., Lonsdale D., O'Donovan C.C., RA Whitfield E.J., Apweiler R., Koyanagi K.O., Khurana J.P., RA Raghuvanshi S., Singh N.K., Tyagi A.K., Haberer G., Fujisawa M., RA Hosokawa S., Ito Y., Ikawa H., Shibata M., Yamamoto M., RA Bruskiewich R.M., Hoen D.R., Bureau TE., Namiki N., Ohyanagi H., RA Sakai Y., Nobushima S., Sakata K., Barrero R.A., Sato Y., Souvorov A., RA Smith-White B., Tatusova T., An S., An G., OOta S., Fuks G., RA Messing J., Christie K.R., Lieberherr D., Kim H., Zuccolo A., RA Wing R.A., Nobuta K., Green P.J., Lu C., Meyers BC., Chaparro C., RA Piegu B., Panaud O., Echeverria M.; RT "The Rice Annotation Project Database (RAP-DB): 2008 update."; RL Nucleic Acids Res. 36:D1028-D1033(2008). RN [14] {ECO:0000313|Proteomes:UP000000763} RP GENOME REANNOTATION. RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000000763}; 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 [15] {ECO:0000313|EMBL:EAZ16115.1} 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; DP000086; AAP53817.1; -; Genomic_DNA. DR EMBL; AP008216; BAF26542.1; -; Genomic_DNA. DR EMBL; AK063962; BAG88938.1; -; mRNA. DR EMBL; AK102020; BAG95344.1; -; mRNA. DR EMBL; AK103743; BAG96239.1; -; mRNA. DR EMBL; CM000147; EAZ16115.1; -; Genomic_DNA. DR RefSeq; NP_001064628.1; NM_001071163.1. DR UniGene; Os.46891; -. DR ProteinModelPortal; Q7XEH2; -. DR EnsemblPlants; OS10T0422200-01; OS10T0422200-01; OS10G0422200. DR EnsemblPlants; OS10T0422200-02; OS10T0422200-02; OS10G0422200. DR GeneID; 4348656; -. DR KEGG; osa:4348656; -. DR Gramene; Q7XEH2; -. DR eggNOG; COG2040; -. DR InParanoid; Q7XEH2; -. DR KO; K00547; -. DR OMA; QCKDENT; -. DR Proteomes; UP000000763; Chromosome 10. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Complete proteome {ECO:0000313|Proteomes:UP000000763}; KW Methyltransferase {ECO:0000313|EMBL:AAP53817.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000763}; KW Transferase {ECO:0000313|EMBL:AAP53817.1}. SQ SEQUENCE 335 AA; 36508 MW; 067B43F2E99A4D75 CRC64; MSQQGEYHAD MMAEFLRGSG GAAVIDGGLA TELEANGADL KDALWSARCL FTCPDLIRKV HLDYLEAGAS VLITGSYQAT IQGFLSKGFS QEESESFLRR SVELACEARA IYLEKCSNGS DEAKDVTKYR KRPILIAASV GSYGAYLADG SEYSGDYGNE GTLEFLKNFH LRRLQVLAEA GPDVIVFETI PNKIETQAYV ELLEECKLRI PAWFGFTSKD GVNVVSGDSL IECASIADSC KEVAAVGINC TPPRFIHELV LSIRKVTSKP ILIYPNSGES YDPIRKEWVE CSGISNEDFV SYVKKWHEAG ASLIGGCCRT SPDTIRGISK ALHGV // ID Q818J9_BACCR Unreviewed; 610 AA. AC Q818J9; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 27-MAY-2015, entry version 81. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=BC_4251 {ECO:0000313|EMBL:AAP11166.1}; OS Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / OS NCIMB 9373 / NRRL B-3711). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=226900 {ECO:0000313|EMBL:AAP11166.1, ECO:0000313|Proteomes:UP000001417}; RN [1] {ECO:0000313|EMBL:AAP11166.1, ECO:0000313|Proteomes:UP000001417} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL RC B-3711 {ECO:0000313|Proteomes:UP000001417}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; AAP11166.1; -; Genomic_DNA. DR RefSeq; NP_833965.1; NC_004722.1. DR RefSeq; WP_000770352.1; NC_004722.1. DR ProteinModelPortal; Q818J9; -. DR STRING; 226900.BC4251; -. DR EnsemblBacteria; AAP11166; AAP11166; BC_4251. DR GeneID; 1206596; -. DR KEGG; bce:BC4251; -. DR PATRIC; 32604584; VBIBacCer54481_4395. DR eggNOG; COG0685; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; BCER226900:GJEU-4247-MONOMER; -. DR Proteomes; UP000001417; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001417}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:AAP11166.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000001417}; KW Transferase {ECO:0000313|EMBL:AAP11166.1}. SQ SEQUENCE 610 AA; 67207 MW; 6AAA70A0BB40008A CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNVSDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTE INRAAVKLAK ASVTDKNAIL GTIGGMKHIG AVTTTDMERE FMLLEQAGAL LEEQVDGLLL ETFYDEFELL HAVKVLRKQT NIPIVAQLAL HEAGTTQNGN DVNEILKQLI DYGANVVGLN CQLGPLHMTE AFKMISIPQN GYLSAYPNAG LPNYVDGRYV YEGSPAYFEA MTPRFIEQGI RLLGGCCGTT PEHIQSMKRA VANITPVIEK DTIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRVSNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIK LIEEVYEATK HLEQPIFIGI MPLVSKRNAD FLHFEVPGIT LPEEIRERMD GHETKEAAIE EGIRISQELV DAAMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID Q818K0_BACCR Unreviewed; 1133 AA. AC Q818K0; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 29-APR-2015, entry version 94. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AAP11165.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AAP11165.1}; GN OrderedLocusNames=BC_4250 {ECO:0000313|EMBL:AAP11165.1}; OS Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / OS NCIMB 9373 / NRRL B-3711). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=226900 {ECO:0000313|EMBL:AAP11165.1, ECO:0000313|Proteomes:UP000001417}; RN [1] {ECO:0000313|EMBL:AAP11165.1, ECO:0000313|Proteomes:UP000001417} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL RC B-3711 {ECO:0000313|Proteomes:UP000001417}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AE016877; AAP11165.1; -; Genomic_DNA. DR RefSeq; NP_833964.1; NC_004722.1. DR RefSeq; WP_011110380.1; NC_004722.1. DR ProteinModelPortal; Q818K0; -. DR STRING; 226900.BC4250; -. DR EnsemblBacteria; AAP11165; AAP11165; BC_4250. DR GeneID; 1206595; -. DR KEGG; bce:BC4250; -. DR PATRIC; 32604582; VBIBacCer54481_4394. DR eggNOG; COG1410; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; BCER226900:GJEU-4246-MONOMER; -. DR Proteomes; UP000001417; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001417}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AAP11165.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001417}; KW Transferase {ECO:0000313|EMBL:AAP11165.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 223 223 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 287 287 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 719 719 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1133 AA; 125963 MW; 10F28DF09227F283 CRC64; MMKCIEEKLK NSILILDGAM GTMIQQEDLT AEDFGGEEYE GCNEYLVETR PDVILKIHKA YIEAGADIIE TNTFGATNIV LSDYDLSHLD EELNEEAALL AKQAVKESGK EVYVAGAMGP TTKAISVTGG VTFEELIEAY TRQARGLLKG AVDVVLVETS QDMRNVKAAY IGIQAAFEEL KKTVPIMISG TIEPMGTTLA GQTIEAFYLS VEHMKPLSVG LNCATGPEFM RDHIRSLSDL SECYISCYPN AGLPDEDGHY HESPSSLAEK VKRFAEEGWV NIIGGCCGTT PEHIKAMKSA LASLRPRDHH EREGHGISGL EALQYDESMR PLFVGERTNV IGSRKFKRLV AEGKFEEAAE VARAQVKKNA HIIDICMADP DRDEIEDMEN FLAEVTKVLK VPIMIDSTDE NVMERALTYI QGKAVINSIN LEDGEERFKK VTPLLQKYGA AIVVGTIDED GMAVSAERKI EIAKRSYELL TKKYGIRPSD IIFDALVFPV GTGDEEYIGS AAATIEGIRL IKEALPECLT ILGVSNISFG LPPAGREVLN SVFLYHATKA GLDYAIVNTE KLERYASIPE EEKRLADALL FETTKETLEE FTNFYRVAKK KDVVVQETLT LDERLANYIV EGTKQGLHED LSLALEEGRK PLDIINGPLM TGMDEVGRLF NNNELIVAEV LQSAESMKAA VSYLEPHMES SDSAKKGKVL LATVKGDVHD IGKNLVEIIL ANNGYEIINL GINVRSDRIV QEVQEKKPDI IGLSGLLVKS AQQMVTTAED LKAANIDVPI VVGGAALTRK FTDNRISPSY KGLVCYASDA MTGLDIINKL QKEEEREKMK QDKKERHLHI VKKEEKKVEI PAVIEPLPKS EVMVPDSTKR IVLRDVPALH LAPFLNRQML LGHHLGLKGN VKKLLKEGDK RAHELNDLID ELLQEGQSWL KPKAVYQFFP AQSDGQNIVI YDPEDHTRVI ERFTFPRQGK APYRTLGDYL RPIGDEMDYV AFLSVTVGEG VRDIAEELKA KGDYLRSHAI QSLALELAEG LAEKTHMLIR DRWGIPDSPE LTMEERFRTK YRGIRVSFGY PACPELADQE KLFRLIHPEE IGISLTEGFM MEPEASVTAM VFSHPEARYF SVL // ID Q81LY0_BACAN Unreviewed; 610 AA. AC Q81LY0; E9R6D4; E9R6D5; Q6HTD2; Q6KMM4; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 27-MAY-2015, entry version 104. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=GBAA_4479 {ECO:0000313|EMBL:AAT33597.1}; GN ORFNames=BF27_3235 {ECO:0000313|EMBL:AJH85888.1}, GN TM00_21775 {ECO:0000313|EMBL:AJG30957.1}; OS Bacillus anthracis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=1392 {ECO:0000313|Proteomes:UP000031917}; RN [1] {ECO:0000313|EMBL:AAT33597.1, ECO:0000313|Proteomes:UP000000594} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ames Ancestor {ECO:0000313|EMBL:AAT33597.1}, and RC Ames ancestor {ECO:0000313|Proteomes:UP000000594}; 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 [2] {ECO:0000313|EMBL:AJH85888.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=2002013094 {ECO:0000313|EMBL:AJH85888.1}; RA Davenport K.W., Bishop-Lilly K.A., Broomall S.M., Chain P.S., RA Chertkov O., Coyne S.R., Daligault H.E., Erkkila T., Frey K.G., RA Gibbons H.S., Gu W., Jaissle J., Johnson S.L., Koroleva G.I., RA Ladner J.T., Lo C.-C., Minogue T.D., Munk C., Palacios G.F., RA Redden C.L., Rosenzweig C.N., Scholz M.B., Teshima H., Xu Y.; RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:AJG30957.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Pollino {ECO:0000313|EMBL:AJG30957.1}; RA Fasanella A., Braun P., Grass G., Hanczaruk M., Aceti A., RA Serrecchia L., Marino L., Georgi E., Antwerpen M.H.; RT "Genome sequence of Bacillus anthracis Pollino isolated from a bovine RT anthrax-burial site in Italy."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017334; AAT33597.1; -; Genomic_DNA. DR EMBL; CP010813; AJG30957.1; -; Genomic_DNA. DR EMBL; CP009902; AJH85888.1; -; Genomic_DNA. DR RefSeq; NP_846704.1; NC_003997.3. DR RefSeq; WP_000770331.1; NZ_KN050651.1. DR RefSeq; YP_021122.1; NC_007530.2. DR RefSeq; YP_030406.1; NC_005945.1. DR ProteinModelPortal; Q81LY0; -. DR STRING; 198094.BA_4479; -. DR DNASU; 1087947; -. DR EnsemblBacteria; AAP28190; AAP28190; BA_4479. DR EnsemblBacteria; AAT33597; AAT33597; GBAA_4479. DR EnsemblBacteria; AAT56457; AAT56457; BAS4157. DR EnsemblBacteria; AIF58428; AIF58428; HYU01_21850. DR EnsemblBacteria; AIK10481; AIK10481; DH23_4356. DR EnsemblBacteria; AIK32024; AIK32024; DJ48_5472. DR EnsemblBacteria; AIK53647; AIK53647; DJ45_1546. DR EnsemblBacteria; AIK56439; AIK56439; DJ44_2585. DR EnsemblBacteria; AIM08175; AIM08175; BACvac02_4602. DR EnsemblBacteria; AIM13652; AIM13652; BAHan_4708. DR EnsemblBacteria; AJA88466; AJA88466; RT54_21615. DR EnsemblBacteria; KFJ80862; KFJ80862; DJ42_2865. DR EnsemblBacteria; KFL67603; KFL67603; DJ49_642. DR EnsemblBacteria; KFL71344; KFL71344; DJ43_3599. DR EnsemblBacteria; KGZ42762; KGZ42762; NX97_25135. DR EnsemblBacteria; KGZ45203; KGZ45203; OY22_23350. DR EnsemblBacteria; KGZ49647; KGZ49647; OY21_10065. DR EnsemblBacteria; KGZ64044; KGZ64044; OY25_19205. DR EnsemblBacteria; KGZ69950; KGZ69950; OY24_07725. DR EnsemblBacteria; KGZ75326; KGZ75326; OY26_17660. DR EnsemblBacteria; KGZ77258; KGZ77258; OY27_22005. DR EnsemblBacteria; KGZ98796; KGZ98796; OY29_08080. DR EnsemblBacteria; KHA00619; KHA00619; OY30_05710. DR EnsemblBacteria; KHA02557; KHA02557; OY32_10920. DR EnsemblBacteria; KHA32348; KHA32348; OY37_03980. DR EnsemblBacteria; KHA35702; KHA35702; OY38_05600. DR EnsemblBacteria; KHA38388; KHA38388; OY40_25065. DR EnsemblBacteria; KHA39620; KHA39620; OY39_15340. DR EnsemblBacteria; KHG52650; KHG52650; OY31_07435. DR GeneID; 1087947; -. DR GeneID; 2851209; -. DR KEGG; ban:BA_4479; -. DR KEGG; bar:GBAA_4479; -. DR KEGG; bat:BAS4157; -. DR HOGENOM; HOG000028409; -. DR KO; K00548; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; BANT260799:GJAJ-4213-MONOMER; -. DR BioCyc; BANT261594:GJ7F-4355-MONOMER; -. DR Proteomes; UP000000594; Chromosome. DR Proteomes; UP000031917; Chromosome. DR Proteomes; UP000031920; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000594}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:AAT33597.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000000594}; KW Transferase {ECO:0000313|EMBL:AAT33597.1}. SQ SEQUENCE 610 AA; 67298 MW; 3F0A2353CD3128EB CRC64; MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNISDPD LIISIHKQYV AAGADVIQTN TYGANEAKLR MYGLENQVTE INRAAVKLAK ASVTDRNAIL GTIGGMKHIG AVTTTDMERE FMLLEQASAL LEEQVDGLLL ETFYDEFELL HAVQVLRKET NIPIVAQLAL HEAGTTQNGN DVNEILKQLL DYGANVVGLN CQLGPLHMTE AFKMISIPKN GYLSAYPNAG LPNYVEGRYV YEGSPAYFEA MTPKFIEQGI RLLGGCCGTT PEHIESMKRA TLNVTPVIEK DTIQRPKVVH THEKRSKAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA SPRISNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM ERKIDAGAEY FLTQPIYDIA LIEEVYEATK HLEQPIFIGI MPLISKRNAD FLHFEVPGIT LPEAVRERMD GHETKEAAIE EGIRISQELI DETMKYFNGI YLITPFLKYE ITEHLVKYVR EKQEVKEGIN // ID Q81LY1_BACAN Unreviewed; 1132 AA. AC Q81LY1; E9QT69; E9QT70; Q6HTD3; Q6KMM5; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 27-MAY-2015, entry version 110. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AAT33596.2}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AAT33596.2}; DE SubName: Full=Bacillus anthracis strain Pollino sequence {ECO:0000313|EMBL:AJG30956.1}; GN Name=metH {ECO:0000313|EMBL:AAT33596.2}; GN OrderedLocusNames=GBAA_4478 {ECO:0000313|EMBL:AAT33596.2}; GN ORFNames=TM00_21770 {ECO:0000313|EMBL:AJG30956.1}; OS Bacillus anthracis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=1392 {ECO:0000313|Proteomes:UP000000594, ECO:0000313|Proteomes:UP000031917}; RN [1] {ECO:0000313|EMBL:AAT33596.2, ECO:0000313|Proteomes:UP000000594} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ames Ancestor {ECO:0000313|EMBL:AAT33596.2}, and RC Ames ancestor {ECO:0000313|Proteomes:UP000000594}; 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 [2] {ECO:0000313|EMBL:AJG30956.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Pollino {ECO:0000313|EMBL:AJG30956.1}; RA Fasanella A., Braun P., Grass G., Hanczaruk M., Aceti A., RA Serrecchia L., Marino L., Georgi E., Antwerpen M.H.; RT "Genome sequence of Bacillus anthracis Pollino isolated from a bovine RT anthrax-burial site in Italy."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AE017334; AAT33596.2; -; Genomic_DNA. DR EMBL; CP010813; AJG30956.1; -; Genomic_DNA. DR RefSeq; NP_846703.1; NC_003997.3. DR RefSeq; WP_000271582.1; NZ_KN050651.1. DR RefSeq; YP_021121.2; NC_007530.2. DR RefSeq; YP_030405.1; NC_005945.1. DR ProteinModelPortal; Q81LY1; -. DR STRING; 198094.BA_4478; -. DR DNASU; 1087945; -. DR EnsemblBacteria; AAP28189; AAP28189; BA_4478. DR EnsemblBacteria; AAT33596; AAT33596; GBAA_4478. DR EnsemblBacteria; AAT56456; AAT56456; BAS4156. DR EnsemblBacteria; AIK10480; AIK10480; DH23_4355. DR EnsemblBacteria; AIK51073; AIK51073; DJ45_1547. DR EnsemblBacteria; AIK60179; AIK60179; DJ44_2584. DR EnsemblBacteria; AIM13651; AIM13651; BAHan_4707. DR EnsemblBacteria; AJA88465; AJA88465; RT54_21610. DR EnsemblBacteria; KFJ80726; KFJ80726; DJ42_2866. DR EnsemblBacteria; KFL64816; KFL64816; DJ49_643. DR EnsemblBacteria; KGZ42761; KGZ42761; NX97_25130. DR EnsemblBacteria; KGZ45202; KGZ45202; OY22_23345. DR EnsemblBacteria; KGZ49648; KGZ49648; OY21_10070. DR EnsemblBacteria; KGZ61574; KGZ61574; OY23_17015. DR EnsemblBacteria; KGZ64043; KGZ64043; OY25_19200. DR EnsemblBacteria; KGZ69951; KGZ69951; OY24_07730. DR EnsemblBacteria; KGZ77259; KGZ77259; OY27_22010. DR EnsemblBacteria; KGZ81220; KGZ81220; OY28_22155. DR EnsemblBacteria; KGZ98797; KGZ98797; OY29_08085. DR EnsemblBacteria; KHA00620; KHA00620; OY30_05715. DR EnsemblBacteria; KHA02558; KHA02558; OY32_10925. DR EnsemblBacteria; KHA12338; KHA12338; OY35_13825. DR EnsemblBacteria; KHA18849; KHA18849; OY34_03575. DR EnsemblBacteria; KHA20562; KHA20562; OY36_15225. DR EnsemblBacteria; KHA32347; KHA32347; OY37_03975. DR EnsemblBacteria; KHA35701; KHA35701; OY38_05595. DR EnsemblBacteria; KHA39619; KHA39619; OY39_15335. DR EnsemblBacteria; KHG46783; KHG46783; OY33_25770. DR EnsemblBacteria; KHG52651; KHG52651; OY31_07440. DR EnsemblBacteria; KHG58900; KHG58900; OY20_21600. DR GeneID; 1087945; -. DR GeneID; 2851208; -. DR KEGG; ban:BA_4478; -. DR KEGG; bar:GBAA_4478; -. DR KEGG; bat:BAS4156; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; ANTHRA:METH-MONOMER; -. DR BioCyc; BANT260799:GJAJ-4212-MONOMER; -. DR BioCyc; BANT261594:GJ7F-4354-MONOMER; -. DR Proteomes; UP000000594; Chromosome. DR Proteomes; UP000031917; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000594}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AAT33596.2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000594}; KW Transferase {ECO:0000313|EMBL:AAT33596.2}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 222 222 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 286 286 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 718 718 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1132 AA; 126009 MW; A6D276356717B3B6 CRC64; MYCIEEKLQN NILLLDGAMG TMIQQEDLTA EDFGGEEYEG CNEYLVETRP DVILKIHKAY IEAGADIIET NTFGATNIVL SDYELSHLDE ELNEKAARLA KQAVKESGKE VYVAGAMGPT TKAISVTGGV TFEELIEAYT RQARGLLKGE VDVLLVETSQ DMRNMKAAYI GIQAAFDELK KIVPIMISGT IEPMGTTLAG QTIEAFYLSV EHMKPLSVGL NCATGPEFMR DHIRSLSDLS ECYISCYPNA GLPDEDGHYH ESPSSLAEKV KRFAEEGWVN IIGGCCGTTP EHIKAMKEAL ASLKPREHHE REGHGVSGLE ALQYDDSMRP LFVGERTNVI GSRKFKRLVA EGKFEEAAEV ARAQVKKNAH IIDICMADPD RDEIEDMENF LAEVTKVLKV PIMIDSTDEH VMERALTYIQ GKAVINSINL EDGEERFIKV TPLLQKYGAA IVVGTIDEDG MAVSAERKLE IAKRSYELLT TKYGIRPSDI IFDALVFPVG TGDEEYIGSA AATIEGIRLI KEALPECLTI LGVSNISFGL PPAGREVLNS VFLYHATKAG LDYAIVNTEK LERYASIPDE EKRLADALLF ETTQETLEEF TNFYRVAKKK DVVVQETLTL DERLANYIVE GTKQGLHEDL SLALTEGRKP LDIINGPLMT GMDEVGRLFN NNELIVAEVL QSAESMKAAV SYLEPHMESS DSAKKGKVLL ATVKGDVHDI GKNLVEIILA NNGYEIINLG INVRSDRIVQ EVQEKKPDII GLSGLLVKSA QQMVTTAEDL KAADIDIPIV VGGAALTRKF TDNRISPSYK GLVCYASDAM TGLDIINKLQ KEEEREKMKQ DKKERHLHIV TKEEKKIEIP AVIEPLPKSE VMVPDSTKRI VLRDVPALHL APFLNRQMLL GHHLGLKGSV KKLLKEGDKR AHELNDLIDE LLQEGQSWLK PKAVYQFFPA QSDGQNIVIY DPEDHTRVIE RFTFPRQGRA PYRTLGDYLR PIGDEMDYVA FLSVTVGEGV RGIAEEWKAK GDYLRSHAIQ SLALELAEGL AEKTHMLIRD RWGIPDSPEL TMEERFRTKY RGIRVSFGYP ACPELADQEK LFRLIHPEEI GISLTEGFMM EPEASVTAMV FSHPEARYFS VL // ID Q820L0_NITEU Unreviewed; 1237 AA. AC Q820L0; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 27-MAY-2015, entry version 84. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CAD85534.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAD85534.1}; GN Name=metH {ECO:0000313|EMBL:CAD85534.1}; GN OrderedLocusNames=NE1623 {ECO:0000313|EMBL:CAD85534.1}; OS Nitrosomonas europaea (strain ATCC 19718 / NBRC 14298). OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Nitrosomonadaceae; Nitrosomonas. OX NCBI_TaxID=228410 {ECO:0000313|EMBL:CAD85534.1, ECO:0000313|Proteomes:UP000001416}; RN [1] {ECO:0000313|EMBL:CAD85534.1, ECO:0000313|Proteomes:UP000001416} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19718 / NBRC 14298 {ECO:0000313|Proteomes:UP000001416}; RX PubMed=12700255; DOI=10.1128/JB.185.9.2759-2773.2003; RA Chain P., Lamerdin J., Larimer F., Regala W., Land M., Hauser L., RA Hooper A., Klotz M., Norton J., Sayavedra-Soto L., Arciero D., RA Hommes N., Whittaker M., Arp D.; RT "Complete genome sequence of the ammonia-oxidizing bacterium and RT obligate chemolithoautotroph Nitrosomonas europaea."; RL J. Bacteriol. 185:2759-2773(2003). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AL954747; CAD85534.1; -; Genomic_DNA. DR RefSeq; NP_841658.1; NC_004757.1. DR RefSeq; WP_011112183.1; NC_004757.1. DR ProteinModelPortal; Q820L0; -. DR SMR; Q820L0; 655-902. DR STRING; 228410.NE1623; -. DR DNASU; 1082575; -. DR EnsemblBacteria; CAD85534; CAD85534; NE1623. DR KEGG; neu:NE1623; -. DR PATRIC; 22714446; VBINitEur56163_1815. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR PhylomeDB; Q820L0; -. DR BioCyc; NEUR228410:GJNO-1654-MONOMER; -. DR Proteomes; UP000001416; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001416}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAD85534.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001416}; KW Transferase {ECO:0000313|EMBL:CAD85534.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 249 249 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 315 315 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 767 767 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1237 AA; 137029 MW; 0AE9A99E2FF09DE7 CRC64; MTMHERADLL KRLLAERILM LDGAMGTMIQ SYKLTESDYR GERFADFPHD LKGNNDLLCL TRPEVIRSIH RAYLEAGSDI IETNTFNSNA PSMADYHMQD LVYELNVAGA RLACEEARAM ETQQPDRPRF VAGVIGPTTK TASLSPDVND PGFRAITFDD LVESYTESVR GLIDGGADIL LVETIFDTLN AKAALFAIDQ YFETHGLRLP VMISVTITDA SGRNLSGQTP EAFWNSVRHA RPLSVGINCA LGAELMRPYV EELSNVAEVF TSAHPNAGLP NPLAETGYDE TPEYTARLIK DFAQSGFVNI VGGCCGTTPK HIAAIAEAVR DIPPRPLPDI PKKLRLSGLE PLNIDEHSLF VNVGERTNVT GSKAFARLIL NGGYAEGLVI ARSQVENGAQ IIDINMDEAM LDSQKAMVTF LNLLAAEPDI SRLPIMLDSS KWSVIEAGLK CVQGKAVINS ISLKEGEAEF LHHARLARRY GAAVIVMAFD ETGQADTLQR KVEICTRCYH TLIEQADFPP EDIIFDPNIF AIATGIEEHS NYAVDFIEAT HVIRQTLPYA KVSGGVSNVS FSFRGNEPIR EAIHTAFLYH AVKAGMTMGI VNAGQLGVYS DIPPDLLEHV EDVLLNRRPD ATERLVEFAE HFKGQKKEQI EDLSWRDEPV RQRLIHALVR GISTYIVEDT ELVRQEIDSQ GGKPIEVIEG PLMDGMNVVG DLFGAGKMFL PQVVKSARVM KQAVAYLLPY IEAEKKISGD SKPKGKVVIA TVKGDVHDIG KNIVSVVLQC NNFEVINMGV MVPSAQILET ARREQVDMIG LSGLITPSLE EMAHVAREME REQFTVPLLI GGATTSRMHT AVKIAPHYGG VTVWVPDASR AVGVCSNLMS QDLRDDYVRQ VKAEQEKSRV QHRNKKGPSK LLTFEEARAN ALKTDWARYT PPAPDFLGLR TLNNYPLETL VPHIDWTPFF QAWELHGRYP AILQDELVGE AASNLFRDAQ NMLRKIVEQK WLTANAVIGL FPANTVNGDD IEIYADRSRS QVIMTWHTLR QQTAKPAGRP NLALADFIAP RETGLDDTIG LFAVSAGFGI DERIRAFEAA NDDYSAIILK ALADRLAEAF AEHMHARVRR EFWGYVKDES LDNEQLIDEQ YLGIRPAPGY PACPDHTEKG PLFALLEAEK RSGIVITESF AMVPTAAVSG FYLSYPESSY FAVGKIGKDQ VEDYARRKGW TLEEAERWLA PVLAYER // ID Q828K2_STRAW Unreviewed; 1190 AA. AC Q828K2; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 27-MAY-2015, entry version 94. DE SubName: Full=Putative 5-methyltetrahydrofolate:homocysteine S-methyltransferase {ECO:0000313|EMBL:BAC74378.1}; GN Name=metH {ECO:0000313|EMBL:BAC74378.1}; GN OrderedLocusNames=SAV_6667 {ECO:0000313|EMBL:BAC74378.1}; 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 {ECO:0000313|EMBL:BAC74378.1, ECO:0000313|Proteomes:UP000000428}; RN [1] {ECO:0000313|EMBL:BAC74378.1, ECO:0000313|Proteomes:UP000000428} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / RC MA-4680 {ECO:0000313|Proteomes:UP000000428}; 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] {ECO:0000313|EMBL:BAC74378.1, ECO:0000313|Proteomes:UP000000428} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; BA000030; BAC74378.1; -; Genomic_DNA. DR RefSeq; NP_827843.1; NC_003155.4. DR RefSeq; WP_010988067.1; NC_003155.4. DR ProteinModelPortal; Q828K2; -. DR STRING; 227882.SAV_6667; -. DR EnsemblBacteria; BAC74378; BAC74378; SAV_6667. DR KEGG; sma:SAV_6667; -. DR PATRIC; 23727440; VBIStrAve112782_7068. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SAVE227882:GJU1-6753-MONOMER; -. DR Proteomes; UP000000428; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000428}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAC74378.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000428}; KW Transferase {ECO:0000313|EMBL:BAC74378.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 258 258 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 324 324 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 325 325 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 768 768 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1190 AA; 129516 MW; EEF0C77BF44ADE89 CRC64; MGSAKPTAVA LQGASSMASL PNPSPSSASA ASRSRTDALR EALATRVVVA DGAMGTMLQA QDPTLEDFEN LEGCNEILNL TRPDIVRSVH EAYFAVGVDC VETNTFGANH SALAEYDIAD RVFELSEAGA RLAREVADEF GTGDGRQRWV LGSIGPGTKL PTLGHVGYGT LRDGFQANAE GLIAGGADAL IVETTQDLLQ TKTSVLGARR AMDATGVDLP LLVSMAFETT GTMLLGSEIG AALTALEPLG IDMIGLNCST GPAEMSEHLR YLTRHSRIPL LCMPNAGLPV LTKDGAHFPL GPEGLADAQE NFVRDYGLSL VGGCCGTTPE HLRQLVERVR GVEPTERRPQ PEPGAASLYQ TVPFRQDTAY MAIGERTNAN GSKKFREAML DARWDDCVEM ARDQIREGAH MLDLCVDYVG RDGVADMEEL AGRFATASTL PIVLDSTEVD VLRAGLEKLG GRAVINSVNY EDGDGPESRF AKVTRLAQEH GAALIALTID EEGQARTVET KVAIAERLIE DLTTNWGIHE SDILMDCLTF TICTGQEESR GDGIATIEAI RELKRRRPDV QTTLGLSNIS FGLNPAARIL LNSVFLDECV KAGLDSAIVH ASKILPIARF DEEQVTTALD LIYDRRSEGY DPLQKLMALF EGATTKSLKA GKAEELAALP LDERLKRRII DGEKNGLEAD LDAALQDRPA LDIVNETLLD GMKVVGELFG SGQMQLPFVL QSAEVMKTAV AHLEPHMEKS DAEGKGTIVL ATVRGDVHDI GKNLVDIILS NNGYNVVNLG IKQPVSAILD AAEEHRADVI GMSGLLVKST VIMKENLEEL NQRGLSADYP VILGGAALTR AYVEQDLHEI YQGEVRYARD AFEGLRLMDA LIGVKRGVPG AALPELKQRR VRAAAVEVEE RPEEGAVRSD VATDNPVPAP PFRGTRVIKG IQLKEYASWL DEGALFKGQW GLKQARTGDG PTYEELVESE GRPRLRGLLD KLQTENLLEA AVVYGYFPCV SKDDDLIILD EQGNERTRFT FPRQRRGRRL CLADFFRPEE SGERDVVGLQ VVTVGSRIGT ETAKLFEANS YRDYLELHGL SVQLAEALAE YWHARVRSEL GFAGEDPDRM EDMFALQYRG ARFSLGYGAC PNLEDRAKIA ALLEPERIGV HLSEEFQLHP EQSTDAIVIH HPEAKYFNAR // ID Q82LA0_STRAW Unreviewed; 313 AA. AC Q82LA0; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 01-APR-2015, entry version 63. DE SubName: Full=Putative homocysteine S-methyltransferase {ECO:0000313|EMBL:BAC69822.1}; GN Name=mmuM {ECO:0000313|EMBL:BAC69822.1}; GN OrderedLocusNames=SAV_2111 {ECO:0000313|EMBL:BAC69822.1}; 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 {ECO:0000313|EMBL:BAC69822.1, ECO:0000313|Proteomes:UP000000428}; RN [1] {ECO:0000313|EMBL:BAC69822.1, ECO:0000313|Proteomes:UP000000428} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / RC MA-4680 {ECO:0000313|Proteomes:UP000000428}; 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] {ECO:0000313|EMBL:BAC69822.1, ECO:0000313|Proteomes:UP000000428} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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 ----------------------------------------------------------------------- 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; BAC69822.1; -; Genomic_DNA. DR RefSeq; NP_823287.1; NC_003155.4. DR RefSeq; WP_010983551.1; NZ_BAVY01000019.1. DR ProteinModelPortal; Q82LA0; -. DR STRING; 227882.SAV_2111; -. DR EnsemblBacteria; BAC69822; BAC69822; SAV_2111. DR KEGG; sma:SAV_2111; -. DR PATRIC; 23717689; VBIStrAve112782_2262. DR HOGENOM; HOG000076048; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; SAVE227882:GJU1-2124-MONOMER; -. DR Proteomes; UP000000428; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000428}; KW Methyltransferase {ECO:0000313|EMBL:BAC69822.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000428}; KW Transferase {ECO:0000313|EMBL:BAC69822.1}. SQ SEQUENCE 313 AA; 32575 MW; FD3BAB933FA0E563 CRC64; MTRSTTLAEA LAAAPVVLDG GLSNQLESAG HDLSDELWSA RLLAERPEAI TEAHLAYFEA GADVAITSSY QATFEGFAKR GIPEERAAEL LGLSVGLARE AAVRARADGV TRPLWVAASV GPYGAMLADG SEYRGRYGLT VAELEAFHRP RLEVLAAAGP DVLALETVPD ADEAEALLRA VRGLGVPAWL SYSVSGDRTR AGQSLEEAFA PAAEADEVIA VGVNCCAPED VDGAVETAAR VTGKPVVVYP NSGETWDAGA RAWSGRSTFT AEQVTGWRRA GARLIGGCCR VGPAAITSIA GTLGEQGRAR PTE // ID Q83IR7_SHIFL Unreviewed; 1227 AA. AC Q83IR7; Q7UBA6; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 4. DT 27-MAY-2015, entry version 98. DE SubName: Full=B12-dependent methionine synthase,Methionine synthase,B12-dependent methionine synthase,Predicted cobalamin binding protein,methionine synthase,Homocysteine S-methyltransferase {ECO:0000313|EMBL:CDX09509.1}; GN Name=metH {ECO:0000313|EMBL:CDX09509.1}; GN ORFNames=NCTC1_04441 {ECO:0000313|EMBL:CDX09509.1}; OS Shigella flexneri. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=623 {ECO:0000313|EMBL:CDX09509.1}; RN [1] {ECO:0000313|EMBL:CDX09509.1} RP NUCLEOTIDE SEQUENCE. RA Aslett A.Martin., De Silva Nishadi; RL Submitted (JUL-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; LM651928; CDX09509.1; -; Genomic_DNA. DR RefSeq; NP_709803.2; NC_004337.2. DR RefSeq; WP_000096021.1; NZ_JMRK01000099.1. DR ProteinModelPortal; Q83IR7; -. DR SMR; Q83IR7; 651-1227. DR STRING; 198214.SF4085; -. DR EnsemblBacteria; AAN45510; AAN45510; SF4085. DR EnsemblBacteria; AAP18689; AAP18689; S3645. DR GeneID; 1025407; -. DR KEGG; sfl:SF4085; -. DR KEGG; sfx:S3645; -. DR PATRIC; 18709098; VBIShiFle31049_3987. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:CDX09509.1}; KW Transferase {ECO:0000313|EMBL:CDX09509.1}. SQ SEQUENCE 1227 AA; 135857 MW; DA24CC6AD801C059 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLA AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKADDTANAQ QAEWRSWDVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RIAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFAIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTCKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDHARRKGMS VSDVERWLAP NLGYDAD // ID Q83X55_STRRO Unreviewed; 1135 AA. AC Q83X55; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 01-APR-2015, entry version 74. DE SubName: Full=Probable 5-methyltetrahydrofolate-homocysteine S-methyltransferase {ECO:0000313|EMBL:BAC76507.1}; GN Name=lkmR {ECO:0000313|EMBL:BAC76507.1}; OS Streptomyces rochei (Streptomyces parvullus). OG Plasmid pSLA2-L {ECO:0000313|EMBL:BAC76507.1}. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1928 {ECO:0000313|EMBL:BAC76507.1}; RN [1] {ECO:0000313|EMBL:BAC76507.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=7434AN4 {ECO:0000313|EMBL:BAC76507.1}; RC PLASMID=pSLA2-L {ECO:0000313|EMBL:BAC76507.1}; RX PubMed=9836424; DOI=10.1271/bbb.62.1892; RA Kinashi H., Fujii S., Hatani A., Kurokawa T., Shinkawa H.; RT "Physical mapping of the linear plasmid pSLA2-L and localization of RT the eryAI and actI homologs."; RL Biosci. Biotechnol. Biochem. 62:1892-1897(1998). RN [2] {ECO:0000313|EMBL:BAC76507.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=7434AN4 {ECO:0000313|EMBL:BAC76507.1}; RC PLASMID=pSLA2-L {ECO:0000313|EMBL:BAC76507.1}; RX PubMed=10767533; DOI=10.1016/S0378-1119(00)00060-3; RA Suwa M., Sugino H., Sasaoka A., Mori E., Fujii S., Shinkawa H., RA Nimi O., Kinashi H.; RT "Identification of two polyketide synthase gene clusters on the linear RT plasmid pSLA2-L in Streptomyces rochei."; RL Gene 246:123-131(2000). RN [3] {ECO:0000313|EMBL:BAC76507.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=7434AN4 {ECO:0000313|EMBL:BAC76507.1}; RC PLASMID=pSLA2-L {ECO:0000313|EMBL:BAC76507.1}; RX PubMed=10954087; DOI=10.1007/PL00008689; RA Hiratsu K., Mochizuki S., Kinashi H.; RT "Cloning and analysis of the replication origin and the telomeres of RT the large linear plasmid pSLA2-L in Streptomyces rochei."; RL Mol. Gen. Genet. 263:1015-1021(2000). RN [4] {ECO:0000313|EMBL:BAC76507.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=7434AN4 {ECO:0000313|EMBL:BAC76507.1}; RC PLASMID=pSLA2-L {ECO:0000313|EMBL:BAC76507.1}; RX PubMed=12791134; DOI=10.1046/j.1365-2958.2003.03523.x; RA Mochizuki S., Hiratsu K., Suwa M., Ishii T., Sugino F., Yamada K., RA Kinashi H.; RT "The large linear plasmid pSLA2-L of Streptomyces rochei has an RT unusually condensed gene organization for secondary metabolism."; RL Mol. Microbiol. 48:1501-1510(2003). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AB088224; BAC76507.1; -; Genomic_DNA. DR RefSeq; NP_851471.1; NC_004808.2. DR RefSeq; WP_011113130.1; NC_004808.2. DR ProteinModelPortal; Q83X55; -. DR PRIDE; Q83X55; -. DR GeneID; 4267765; -. DR KEGG; pg:4267765; -. DR KO; K00548; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAC76507.1}; KW Plasmid {ECO:0000313|EMBL:BAC76507.1}; KW Transferase {ECO:0000313|EMBL:BAC76507.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 212 212 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 278 278 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 279 279 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 722 722 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1135 AA; 123067 MW; 03A2CB812A06EF44 CRC64; MVVADGAMGT MLQAQDPTLD DFQQLEGCNE ILNVTRPDIV RSVHEAYFAV GVDCVETNTF GANHAALGEY DISDRVHELS AAGARVAREV ADEFTARDGR ARWVLGSMGP GTKLPTLGHA PYRTLRDAYQ ANAEGLVEGG ADALLVETTQ DLLQTKAAVL GARRALAAAG ADLPVIVSVT VETTGTMLLG SEIGAALTAL EPLGIDMIGL NCATGPAEMS EHLRYLARNA RVPLSCMPNA GLPVLGKDGA HYPLSPGELA EAQGTFVREN GVSLVGGCCG TTPEHLRQVV ERVRGLAPSA RDPRPEAGAA SLYQSVPFRQ DTSYLAIGER TNANGSKKFR EAMLEARWDD CVEIAREQIR EGAHMLDLCV DYVGRDGVAD MAELAGRLAT ASTLPIVLDS TEVDVIEAGL ERLGGRAVIN SVNYEDGDGP ESRFARVTAL AREHGAALIA LTIDEEGQAR TAGHKVAIAE RLIADLTGNW GIRESDILID TLTFTICTGQ EESRGDGVAT IEAIRELKRR HPRVQTTLGL SNISFGLNPA ARILLNSVFL DECVKAGLDS AIVHASKILP IARFSEEEVQ TALDLIYDRR AEGYDPLQKL MQLFEGATAK SLKAGKAEEL AALPLEERLK RRIIDGERNG LEADLDTALR ERPALDIVNE TLLDGMKVVG ELFGSGQMQL PFVLQSAEVM KAAVAHLEPH MEKSDADGKG TIVLATVRGD VHDIGKNLVD IILSNNGYNV VNLGIKQPVS AILEAAEEHR ADVIGMSGLL VKSTVIMKEN LEELNQRDLA GTYPVILGGA ALTRAYVEQD LHEIYQGEVR YARDAFEGLR LMDALIGVKR GVPGAKLPEL KQRRVAARRA VPEEPAEAGR SDVATDNPVP APPFWGTRVV KGIQLREYAS WLDEGALFKG QWGLKGETIE GEGRPRLRMW LDRLLTGNLL EAAVVHGYFP CVSKDDDLIV LDEHGNERTR FTFPRQRRGR RLCLADFFRP QESGETDVVG FQVVTVGSRI GAETAKLFEA DAYRDYLELH GLSVQLAEAL AEYWHARVRG ELGIGGSDPA AMEGMFRTEY QGCRYSFGYP ACPDLEDRAK IAELLRPERI GVHLSEEFQL HPEQSTDALV VHHPEAGYFN AGGRA // ID Q881Z7_PSESM Unreviewed; 1239 AA. AC Q881Z7; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 27-MAY-2015, entry version 90. DE SubName: Full=MetH protein {ECO:0000313|EMBL:AAO56233.1}; GN Name=metH {ECO:0000313|EMBL:AAO56233.1}; GN OrderedLocusNames=PSPTO_2732 {ECO:0000313|EMBL:AAO56233.1}; OS Pseudomonas syringae pv. tomato (strain DC3000). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=223283 {ECO:0000313|EMBL:AAO56233.1, ECO:0000313|Proteomes:UP000002515}; RN [1] {ECO:0000313|EMBL:AAO56233.1, ECO:0000313|Proteomes:UP000002515} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DC3000 {ECO:0000313|EMBL:AAO56233.1, RC ECO:0000313|Proteomes:UP000002515}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AE016853; AAO56233.1; -; Genomic_DNA. DR RefSeq; NP_792538.1; NC_004578.1. DR RefSeq; WP_011104161.1; NC_004578.1. DR ProteinModelPortal; Q881Z7; -. DR SMR; Q881Z7; 654-894. DR STRING; 223283.PSPTO_2732; -. DR EnsemblBacteria; AAO56233; AAO56233; PSPTO_2732. DR GeneID; 1184386; -. DR KEGG; pst:PSPTO_2732; -. DR PATRIC; 19996808; VBIPseSyr93040_2788. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR PhylomeDB; Q881Z7; -. DR BioCyc; PSYR223283:GJIX-2779-MONOMER; -. DR Proteomes; UP000002515; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002515}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002515}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1239 AA; 136120 MW; 42E1E6A4519A3713 CRC64; MSDRSARHQA FITALKQRIL ILDGGMGTMI QSYRLEEEDY RGKRFADWPS DVKGNNDLLI LTRPDVIGAI EKAYLDAGAD ILETNTFNAT QVSQADYGME SIVYELNVEG ARLARKVADA KTLETPDKPR FVAGVLGPTS RTCSLSPDVN NPGYRNVTFD ELVENYTEAT KGLIEGGADL ILIETIFDTL NAKAAIFAVQ GVFEELGFEL PIMISGTITD ASGRTLSGQT TEAFWNSISH AKPVSVGLNC ALGASELRPY LQELANKANT HVSAHPNAGL PNAFGEYDEL PSQTAKIIEE FAQSGFLNIV GGCCGTTPEH IKAIAEAVSG YAPREIPDIP KACRLSGLEP FTIDRQSLFV NVGERTNITG SARFARLIRE DNYTEALEVA LQQVEAGAQV IDINMDEGML DSKKAMVTFL NLIAGEPDIS RVPIMIDSSK WEVIEAGLKC IQGKGIVNSI SMKEGVEQFI HHARLCKRYG AAVVVMAFDE QGQADTEARK KEICKRSYDI LVNEVGFPPE DIIFDPNIFA IATGIEEHNN YAVDFINACA YIRDELPHAL TSGGVSNVSF SFRGNNPVRE AIHSVFLLHA IRNGLSMGIV NAGQLEIYDQ IPAELRDCVE DVVLNRNPEG TEALLAIADK YKGDGSVKEA ETEEWRSWPV NQRLEHALVK GITTHIVQDT EESRLGFTRP IEVIEGPLMS GMNVVGDLFG AGKMFLPQVV KSARVMKQAV AHLIPFIELE KGDKPEAKGK ILMATVKGDV HDIGKNIVGV VLGCNGYDIV DLGVMVPAEK ILQVARDEKC DIIGLSGLIT PSLDEMVHVA REMQRQDFHL PLMIGGATTS KAHTAVKIEP KYSNDAVIYV TDASRAVGVA TQLLSKELKP AFIEKTRLEY VEVRERTSAR SARTERLSYG AAVAKKPKFD WESYTPAKPT FTGTRVLQDI DLNVLADYID WTPFFISWDL AGKYPRILTD EVVGEAATAL FEDAQQMLRK LIDEKLISAR AVFGFWPTNQ INDDDLEVYG EDGKPLAKLH HLRQQTIKPD GKPNFSLADF VAPKDSGLTD YIGGFITTAG IGAEEVAKAY QDNGDDYNSI MVKALADRLA EACAEWLHQQ VRKDYWGYAK DEALDNEALI KEQYMGIRPA PGYPACPDHT EKGTLFALLD PLPEGTPEHT PGKSGVFLTE HYAMFPAAAV SGWYFAHPQA QYFAVGKVDK DQVESYTARK GQDLSVTERW LAPNLGYDE // ID Q887Z5_PSESM Unreviewed; 298 AA. AC Q887Z5; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 27-MAY-2015, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAO54664.1}; GN OrderedLocusNames=PSPTO_1135 {ECO:0000313|EMBL:AAO54664.1}; OS Pseudomonas syringae pv. tomato (strain DC3000). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=223283 {ECO:0000313|EMBL:AAO54664.1, ECO:0000313|Proteomes:UP000002515}; RN [1] {ECO:0000313|EMBL:AAO54664.1, ECO:0000313|Proteomes:UP000002515} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DC3000 {ECO:0000313|EMBL:AAO54664.1, RC ECO:0000313|Proteomes:UP000002515}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; AAO54664.1; -; Genomic_DNA. DR RefSeq; NP_790969.1; NC_004578.1. DR RefSeq; WP_005768811.1; NC_004578.1. DR ProteinModelPortal; Q887Z5; -. DR STRING; 223283.PSPTO_1135; -. DR DNASU; 1182771; -. DR EnsemblBacteria; AAO54664; AAO54664; PSPTO_1135. DR GeneID; 1182771; -. DR KEGG; pst:PSPTO_1135; -. DR PATRIC; 19993491; VBIPseSyr93040_1147. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; PYVDVWL; -. DR OrthoDB; EOG6Q5NS7; -. DR PhylomeDB; Q887Z5; -. DR BioCyc; PSYR223283:GJIX-1159-MONOMER; -. DR Proteomes; UP000002515; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002515}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000002515}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 207 207 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 283 283 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 298 AA; 31533 MW; 05756320D2F4984D CRC64; MTQRSTVILD GGMGRELQRR GAPFRQPEWS ALALSEAPDA VSAVHAAYIE SGAQVITSNS YAVVPFHIGE ERFAREGQAL AALAGQLARG SADASGGRAL VAGSIPPLFG SYRPDLYQPE LAADVLKPLV AGLSPYVDLW LAETQSCILE AQTIRAGLPA DGKPFWLSFT LQDEDTDDVP RLRSGEPVAD AAKAAAEMGV ATLLFNCSQP EVIGAAIDAA REVFNALNVD IAIGAYANAF PPQPKDAKAN DGLDELREDL DPQGYQQWAA DWVKRGATHI GGCCGIGPEH IAVLSQKL // ID Q88J73_PSEPK Unreviewed; 307 AA. AC Q88J73; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 27-MAY-2015, entry version 67. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:AAN68384.1}; GN OrderedLocusNames=PP_2776 {ECO:0000313|EMBL:AAN68384.1}; OS Pseudomonas putida (strain KT2440). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=160488 {ECO:0000313|EMBL:AAN68384.1, ECO:0000313|Proteomes:UP000000556}; RN [1] {ECO:0000313|EMBL:AAN68384.1, ECO:0000313|Proteomes:UP000000556} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KT2440 {ECO:0000313|EMBL:AAN68384.1, RC ECO:0000313|Proteomes:UP000000556}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; AAN68384.1; -; Genomic_DNA. DR RefSeq; NP_744920.1; NC_002947.3. DR RefSeq; WP_010953687.1; NC_002947.3. DR ProteinModelPortal; Q88J73; -. DR STRING; 160488.PP_2776; -. DR DNASU; 1042315; -. DR EnsemblBacteria; AAN68384; AAN68384; PP_2776. DR GeneID; 1042315; -. DR KEGG; ppu:PP_2776; -. DR PATRIC; 19943994; VBIPsePut30601_2942. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; QPEVMAA; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; PPUT160488:GIXO-2852-MONOMER; -. DR Proteomes; UP000000556; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000556}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:AAN68384.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000556}; KW Transferase {ECO:0000313|EMBL:AAN68384.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 208 208 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 284 284 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 285 285 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 307 AA; 33152 MW; D259B96006A3B72E CRC64; MTRRAWTLLD GGMGRELKRI GAPFRQPEWS ALALFEAPEY VTQVHRAFIA AGARVITTNS YAVVPFHIGE ERFARSGRAL AELSGRLARG AADEAGASVQ VAGSLPPALG SYRPDLFDPA RSQAIHRELI CGLTPHVDFW LAETQSSLAE ARAVHAALDG DGKPLWLSFT LLDPDTEHAV PLLRSGESVQ QAVLLALELG ASALLFNCSQ PESMGAALRS ARQVLKQEAR ELALGVYANA FPPVREDAQA NDTLLDIRAD LGPEAYLQWA QQWVEEGADI VGGCCGIGPE HIARLDEHLQ ACKQGME // ID Q88KB5_PSEPK Unreviewed; 1235 AA. AC Q88KB5; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 01-APR-2015, entry version 83. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AAN67988.1}; GN Name=metH {ECO:0000313|EMBL:AAN67988.1}; GN OrderedLocusNames=PP_2375 {ECO:0000313|EMBL:AAN67988.1}; OS Pseudomonas putida (strain KT2440). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=160488 {ECO:0000313|EMBL:AAN67988.1, ECO:0000313|Proteomes:UP000000556}; RN [1] {ECO:0000313|EMBL:AAN67988.1, ECO:0000313|Proteomes:UP000000556} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KT2440 {ECO:0000313|EMBL:AAN67988.1, RC ECO:0000313|Proteomes:UP000000556}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AE015451; AAN67988.1; -; Genomic_DNA. DR RefSeq; NP_744524.1; NC_002947.3. DR RefSeq; WP_010953333.1; NC_002947.3. DR ProteinModelPortal; Q88KB5; -. DR SMR; Q88KB5; 654-1235. DR STRING; 160488.PP_2375; -. DR EnsemblBacteria; AAN67988; AAN67988; PP_2375. DR GeneID; 1045407; -. DR KEGG; ppu:PP_2375; -. DR PATRIC; 19943140; VBIPsePut30601_2516. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; PPUT160488:GIXO-2448-MONOMER; -. DR Proteomes; UP000000556; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000556}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AAN67988.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000556}; KW Transferase {ECO:0000313|EMBL:AAN67988.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 761 761 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1235 AA; 135409 MW; D0487FE99DDEE3E4 CRC64; MSDRSARLQA LQNALKERIL ILDGGMGTMI QSYRLEEHDY RGTRFADWPS DVKGNNDLLL LSRPDVIAAI EKAYLDAGAD ILETNTFNAT QISQADYGME SLVYELNVEG ARIARQVADA KTLETPDKPR FVAGVLGPTS RTCSISPDVN DPGFRNVTFD ELVENYIEAT RGLIEGGADL ILIETIFDTL NAKAAIFAVQ QVFEDDNVEL PIMISGTITD ASGRTLSGQT TEAFWNSVRH AKPISVGLNC ALGAKDLRPY LEELATKADT HVSAHPNAGL PNAFGEYDET PAEMAAVVEE FAASGFLNII GGCCGTTPGH IQAIAEAVAK YKPREIPEIA KACRLSGLEP FTIDRQSLFV NVGERTNITG SAKFARLIRE ENYTEALEVA LQQVEAGAQV IDINMDEGML DSQAAMVRFL NLIAGEPDIS RVPIMIDSSK WEVIEAGLKC IQGKGIVNSI SMKEGVEQFK HHARLCKRYG AAVVVMAFDE VGQADTAARK KEICQRSYDI LVNEVGFPPE DIIFDPNIFA VATGIEEHNN YAVDFIEACA YIRDHLPHAL SSGGVSNVSF SFRGNNPVRE AIHSVFLYHA IQNGLTMGIV NAGQLEIYDE IPAQLREKVE DVVLNRTPHG TDALLAIADD YKGGGATKEV ENEEWRSLPV EKRLEHALVK GITAFIVEDT EACRQQCARP IEVIEGPLMN GMNVVGDLFG AGKMFLPQVV KSARVMKQAV AHLIPFIEAE KGDKPEAKGK ILMATVKGDV HDIGKNIVGV VLGCNGYDIV DLGVMVPAEK ILQTAREQKC DIIGLSGLIT PSLDEMVHVA REMQRQGFEL PLMIGGATTS KAHTAVKIEP KYSNDAVIYV TDASRAVGVA TQLLSKELKP GFVEKTRLEY VDVRERTANR SARTERLSYA QAIAAKPQYD WAGYQPTAPS FTGVKVLEDI DLRTLAEYID WTPFFISWDL AGKFPRILTD EVVGEAATAL YKDAREMLDK LIDEKLISAR AVFGFWPANQ VDDDDIEVYG EDGQALATLH HLRQQTIKPD GKPNWSLADF VAPKDSGVTD YVGGFITTAG IGAEEVAKAY QDKGDDYSSI MVKALADRLA EACAEWLHEQ VRKEHWGYAR DEHLDNEALI KEQYSGIRPA PGYPACPDHT EKETLFRLLD GTAIGETGPS GVYLTEHFAM FPAAAVSGWY FAHPQAKYFA VGKVDKDQIE RYSARKGQDI SVSERWLAPN LGYDS // ID Q88Q40_PSEPK Unreviewed; 311 AA. AC Q88Q40; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 29-APR-2015, entry version 60. DE SubName: Full=Homocysteine S-methyltransferase family protein {ECO:0000313|EMBL:AAN66283.1}; GN OrderedLocusNames=PP_0658 {ECO:0000313|EMBL:AAN66283.1}; OS Pseudomonas putida (strain KT2440). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=160488 {ECO:0000313|EMBL:AAN66283.1, ECO:0000313|Proteomes:UP000000556}; RN [1] {ECO:0000313|EMBL:AAN66283.1, ECO:0000313|Proteomes:UP000000556} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KT2440 {ECO:0000313|EMBL:AAN66283.1, RC ECO:0000313|Proteomes:UP000000556}; 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 ----------------------------------------------------------------------- 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; AAN66283.1; -; Genomic_DNA. DR RefSeq; NP_742819.1; NC_002947.3. DR RefSeq; WP_010951916.1; NC_002947.3. DR ProteinModelPortal; Q88Q40; -. DR STRING; 160488.PP_0658; -. DR EnsemblBacteria; AAN66283; AAN66283; PP_0658. DR GeneID; 1044482; -. DR KEGG; ppu:PP_0658; -. DR PATRIC; 19939429; VBIPsePut30601_0704. DR eggNOG; COG2040; -. DR HOGENOM; HOG000265278; -. DR OMA; DVITANS; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; PPUT160488:GIXO-687-MONOMER; -. DR Proteomes; UP000000556; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000556}; KW Methyltransferase {ECO:0000313|EMBL:AAN66283.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000556}; KW Transferase {ECO:0000313|EMBL:AAN66283.1}. SQ SEQUENCE 311 AA; 33407 MW; 063F791A51EE3D19 CRC64; MNFTHKNLQR SYMAERTMVI LDGGMGRELQ RSGAPFRQPE WSALALSEAP EAVVGVHAAF IDAGAQVITS NSYAVVPFHI GEERFAAEGR QLAHIAGQLA RHAADSGAHP VRVAGSLPPL FGSYRPDLFQ PERVAEVLTP LLQGLAPHVD LWLAETQSSV AEVRAIHSHL PADGRPFWVS FTLQDEEVDE VPRLRSGEPV AEAIEAAVGL GVAAVLFNCS QPEVIGAAID VARSVIERHN AEIAIGAYAN AFPPQPKEAT ANDGLDELRE DLDPPGYLAW AKDWRARGAS MVGGCCGIGP EHIAELKRNL A // ID Q893L2_CLOTE Unreviewed; 791 AA. AC Q893L2; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 27-MAY-2015, entry version 85. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AAO36330.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AAO36330.1}; GN OrderedLocusNames=CTC_01806 {ECO:0000313|EMBL:AAO36330.1}; OS Clostridium tetani (strain Massachusetts / E88). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=212717 {ECO:0000313|EMBL:AAO36330.1, ECO:0000313|Proteomes:UP000001412}; RN [1] {ECO:0000313|EMBL:AAO36330.1, ECO:0000313|Proteomes:UP000001412} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Massachusetts / E88 {ECO:0000313|Proteomes:UP000001412}; 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; AAO36330.1; -; Genomic_DNA. DR RefSeq; NP_782393.1; NC_004557.1. DR RefSeq; WP_011099990.1; NC_004557.1. DR ProteinModelPortal; Q893L2; -. DR STRING; 212717.CTC01806; -. DR EnsemblBacteria; AAO36330; AAO36330; CTC_01806. DR KEGG; ctc:CTC01806; -. DR PATRIC; 19511655; VBICloTet101274_1875. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CTET212717:GJAM-1660-MONOMER; -. DR Proteomes; UP000001412; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001412}; KW Methyltransferase {ECO:0000313|EMBL:AAO36330.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001412}; KW Transferase {ECO:0000313|EMBL:AAO36330.1}. SQ SEQUENCE 791 AA; 87611 MW; 77E41F8ADB6018E1 CRC64; MELVKIKDIL GKEILIFDGA MGTMLQKYGL AVGEIPEILN IKEREKIIEI HKKYIEAGAN IITINTFGAN DKKLLNTGYS VEDIIEAAVE NAKIASKEKN IAIALDIGPI GELIEPMGTL SFEEAYNIFQ KQVLQGVKRG VDLILIETMS DLYETKAAIL AAKENSNLPI FCTMTFEEDG RTFTGCSIPS MVTVLQGLGV DALGVNCSLG PLELESIVKE MLKYSQIPVM VQPNAGLPKV IDGKTLYKIT PEEFLQAQKR MVDNGVAIVG GCCGTDNNFI KLIAKEFKGK KVINKKVEKN TMICTPSKAV IVDEIKIVGE RINPTGKKFL KESLKNKNMN YVLKEAINQV EEGADILDIN VGLPDIDEGK IMVKVIKEIQ SVLDIPLQID SNDPEVIEKA LRAYNGKAIV NSVNGEEENL NKILPIIKKY GASIIGLTFD EKGIPLRAEE RFHVAKKIVD KAMEYGIKRE DIIIDCLTLT TSAQQKEVLE TLKALTLVKK NLGVKTTLGV SNISFGLPNR ELLNRTFLNM ALFAGLDLPI INTKNREMVD TIKAFKVLSN IDIGGEKFIK EYGGVKKNKE KVDIVKDEEL KEIIIKGLRE RAVYATKELL KKKTEIQIVE EDLVPALDIV GDRYEKGEVF LPQLIQSAET VQKAFEILKE TLTLKDKKNI SKGKIVLATV KGDVHDIGKN IVKTLLENYG YTVIDLGKDV SKEKIAEEVK KNEVKLVGLS ALMTTTVKSM EETIEMLKNE GLDCKIMVGG AVLNEEYANM IKADYYAKDA KDAIKIARKV I // ID Q89UJ8_BRADU Unreviewed; 1285 AA. AC Q89UJ8; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 27-MAY-2015, entry version 88. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:BAC46683.1}; GN Name=metH {ECO:0000313|EMBL:BAC46683.1}; GN OrderedLocusNames=bll1418 {ECO:0000313|EMBL:BAC46683.1}; 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 {ECO:0000313|EMBL:BAC46683.1, ECO:0000313|Proteomes:UP000002526}; RN [1] {ECO:0000313|Proteomes:UP000002526} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110 RC {ECO:0000313|Proteomes:UP000002526}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; BA000040; BAC46683.1; -; Genomic_DNA. DR RefSeq; NP_768058.1; NC_004463.1. DR RefSeq; WP_011084235.1; NC_004463.1. DR ProteinModelPortal; Q89UJ8; -. DR STRING; 224911.bll1418; -. DR EnsemblBacteria; BAC46683; BAC46683; BAC46683. DR GeneID; 1055168; -. DR KEGG; bja:bll1418; -. DR PATRIC; 21186424; VBIBraJap65052_1474. DR HOGENOM; HOG000251409; -. DR InParanoid; Q89UJ8; -. DR KO; K00548; -. DR OrthoDB; EOG6091CH; -. DR PhylomeDB; Q89UJ8; -. DR BioCyc; BJAP224911:GJEJ-1436-MONOMER; -. DR Proteomes; UP000002526; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002526}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002526}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 314 314 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 770 770 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1285 AA; 139907 MW; 6BE7C3BBB98E71D5 CRC64; MTVPTSPKRT ALLNAAHERI LVLDGAMGTM IQNLQLDEAA FRGERFKNFH RDLRGNNDLL ILTQPQAIED IHAAYLRAGA DIVATNTFST TSIAQADYDL TDIVYEMARE GARLAGNAAR RVEAEDGKPR FVAGAIGPTN RTASISPDVS NPGYRAVTFD DLRKSYGEQI NGMLDGGVDL LLVETIFDTL NAKAALYAIA EITEARGIDV PVMVSGTITD KSGRLLSGQM PEAFWNSVRH AKPVTIGFNC ALGAEDLRAH IADIGRVADT LVCAYPNAGL PNEFGQYDET PEYMARLVGE FARDGLVNIV GGCCGTTPDH IAAIAAAVAP HKPRIVPEIE PRLRLSGLEP FILTDAIPFV NVGERTNVTG SARFRKLITA GDYTAALQVA RDQVENGAQI IDVNMDEGLL DSEAAMVTFL NLVAAEPDIA RVPVMVDSSK FSVIEAGLKC VQGKPVVNSI SMKEGEEKFI HEAKIARRHG AAVVVMAFDE VGQADTFARK TEICKRAYDI LVNRVGFPPE DIIFDPNIFA IATGIEEHNN YGVDFIEATR WIRQNLPGAH ISGGVSNLSF SFRGNEPVRE AMHSVFLYHA IKAGMDMGIV NAGQMIVYDD IDPELRQVCE DVILNRDPGA SERLLALAEK FRGNKTQTKE ADLAWREWPV AKRLSHSLVH GITEFIEVDT EEARKASSRP LDVIEGPLMA GMNVVGDLFG DGKMFLPQVV KSARVMKQAV AWLMPFMEEE KARNLANGIG TEGSSSAGKI VLATVKGDVH DIGKNIVGIV LQCNNFEVID LGVMVPAARI VETVKAEKAD IVGLSGLITP SLDEMAFFAG ELQREGLKLP LLIGGATTSR VHTAVKIDPS YRAGPVVHVN DASRAVGVAS ALLSPEKRVA YAAEVRAEYA KISDAHLRAQ ADKKRLKLAD ARKNRVPVDF AANKPVKPTF LGTKSFDAYD LAELVPYIDW TPFFQTWELA GRFPAILDDA KVGEVARSLY DDARKMLDLI VKEKWFRARA TVGFWPANAV GDDIALYADE SRTKQIATLH TLRQQLEKRE GRFNAALADF IAPVDTGVPD YVGGFVVTAG IGEDAVADRF KMANDDYSSI LCKALADRLA EAFAERMHAR VRREFWAYAP DEALSCDDLI LEKYQGIRPA PGYPAQPDHT EKATLFELLD AEATAGVKLT ESFAMWPGSS VSGLYFANPA SYYFGVGKIE RDQVEDYAAR KGMSITEAER WLAPVLNYIP AREGTDKAFA ATPANDETSK DLASHPPGCT CAVHLVWQKK RAGAG // ID Q8A7W5_BACTN Unreviewed; 308 AA. AC Q8A7W5; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 27-MAY-2015, entry version 65. DE SubName: Full=Putative homocysteine S-methyltransferase {ECO:0000313|EMBL:AAO76516.1}; GN OrderedLocusNames=BT_1409 {ECO:0000313|EMBL:AAO76516.1}; 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 {ECO:0000313|EMBL:AAO76516.1, ECO:0000313|Proteomes:UP000001414}; RN [1] {ECO:0000313|EMBL:AAO76516.1, ECO:0000313|Proteomes:UP000001414} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VPI-5482 {ECO:0000313|EMBL:AAO76516.1}; 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] {ECO:0000313|EMBL:AAO76516.1, ECO:0000313|Proteomes:UP000001414} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482 RC {ECO:0000313|Proteomes:UP000001414}; 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; AAO76516.1; -; Genomic_DNA. DR RefSeq; NP_810322.1; NC_004663.1. DR RefSeq; WP_008764881.1; NC_004663.1. DR ProteinModelPortal; Q8A7W5; -. DR STRING; 226186.BT_1409; -. DR EnsemblBacteria; AAO76516; AAO76516; BT_1409. DR GeneID; 1072922; -. DR KEGG; bth:BT_1409; -. DR PATRIC; 21057685; VBIBacThe70966_1442. DR InParanoid; Q8A7W5; -. DR OMA; CCGTDHR; -. DR OrthoDB; EOG6R5C46; -. DR BioCyc; BTHE226186:GJXV-1438-MONOMER; -. DR Proteomes; UP000001414; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001414}; KW Methyltransferase {ECO:0000313|EMBL:AAO76516.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001414}; KW Transferase {ECO:0000313|EMBL:AAO76516.1}. SQ SEQUENCE 308 AA; 34416 MW; DC48647CE245C009 CRC64; MNFKDCIDSY PFILMEGALG ERLKREFDLD ISGTVAMADL VYQQKGRLAL ETLWNEYIDI AYRYQLPFLA TTPTRRANKE RIYMAGYNES IIADNVDFLR SIKEAANVDM YIGGLMGCKG DAYTGEEALN LEEAIDFHSW QAGLFKSAKV DFLYAGIMPV LTEAIGMAVA MSDTDIPYII SFTIQRDGKL IDGHTIDDAI HCIDNHVSNK PVCYMTNCVH PDIVYEALSH KFNQTQTVKS RFWGIQANTS QLSYKELDGA NHLHTSSAAD LSEAILKLKS DCHLKIFGGC CGTDSSHMEK IAKISEVT // ID Q8ABD0_BACTN Unreviewed; 915 AA. AC Q8ABD0; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 27-MAY-2015, entry version 93. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|EMBL:AAO75287.1}; GN OrderedLocusNames=BT_0180 {ECO:0000313|EMBL:AAO75287.1}; 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 {ECO:0000313|EMBL:AAO75287.1, ECO:0000313|Proteomes:UP000001414}; RN [1] {ECO:0000313|EMBL:AAO75287.1, ECO:0000313|Proteomes:UP000001414} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VPI-5482 {ECO:0000313|EMBL:AAO75287.1}; 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] {ECO:0000313|EMBL:AAO75287.1, ECO:0000313|Proteomes:UP000001414} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482 RC {ECO:0000313|Proteomes:UP000001414}; 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). RN [3] {ECO:0000213|PDB:3K13} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 345-641. RA Cuff M.E., Li H., Cobb G., Joachimiak A.; RT "Structure of the pterin-binding domain MeTr of 5- RT methyltetrahydrofolate-homocysteine methyltransferase from Bacteroides RT thetaiotaomicron."; RL Submitted (SEP-2009) to the PDB data bank. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AE015928; AAO75287.1; -; Genomic_DNA. DR RefSeq; NP_809093.1; NC_004663.1. DR RefSeq; WP_011107153.1; NC_004663.1. DR PDB; 3K13; X-ray; 2.00 A; A/B/C=345-641. DR PDBsum; 3K13; -. DR ProteinModelPortal; Q8ABD0; -. DR SMR; Q8ABD0; 650-895. DR STRING; 226186.BT_0180; -. DR PRIDE; Q8ABD0; -. DR EnsemblBacteria; AAO75287; AAO75287; BT_0180. DR GeneID; 1075492; -. DR KEGG; bth:BT_0180; -. DR PATRIC; 21055099; VBIBacThe70966_0177. DR HOGENOM; HOG000251409; -. DR InParanoid; Q8ABD0; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; BTHE226186:GJXV-181-MONOMER; -. DR EvolutionaryTrace; Q8ABD0; -. DR Proteomes; UP000001414; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3K13}; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001414}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AAO75287.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001414}; KW Transferase {ECO:0000313|EMBL:AAO75287.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 915 AA; 99999 MW; F181B9B3EB7BF227 CRC64; MKKTISQIVS ERILILDGAM GTMIQQYNLK EEDFRGERFA HIPGQLKGNN DLLCLTRPDV IQDIHRKYLE AGADIIETNT FSSTTVSMAD YHVEEYVREI NLAATRLARE LADEYTAKSP DKPRFVAGSV GPTNKTCSMS PDVNNPAFRA LSYDELAASY QQQMEAMLEG GVDAILIETI FDTLNAKAAI FAAGQAMKVT GIEVPVMLSV TVSDIGGRTL SGQTLEAFLA SVQHANIFSV GLNCSFGARQ LKPFLEQLAS RAPYYISAYP NAGLPNSLGK YDQTPADMAH EVKEYIQEGL VNIIGGCCGT TDAYIAEYQT LIAGAKPHVP APKPDCMWLS GLELLEVKPE INFVNIGERC NVAGSRKFLR LVNEKKYDEA LSIARQQVED GALVIDVNMD DGLLDARTEM TTFLNLIMSE PEIARVPVMI DSSKWEVIEA GLKCLQGKSI VNSISLKEGE EVFLEHARII KQYGAATVVM AFDEKGQADT AARKIEVCER AYRLLVDKVG FNPHDIIFDP NVLAVATGIE EHNNYAVDFI EATGWIRKNL PGAHVSGGVS NLSFSFRGNN YIREAMHAVF LYHAIQQGMD MGIVNPGTSV LYSDIPADTL EKIEDVVLNR RPDAAERLIE LAEALKETMG GTSGQAAVKQ DAWREESVQE RLKYALMKGI GDYLEQDLAE ALPLYDKAVD VIEGPLMDGM NYVGELFGAG KMFLPQVVKT ARTMKKAVAI LQPIIESEKV EGSSSAGKVL LATVKGDVHD IGKNIVAVVM ACNGYDIVDL GVMVPAETIV QRAIEEKVDM IGLSGLITPS LEEMTHVAAE LEKAGLDIPL LIGGATTSKM HTALKIAPVY HAPVVHLKDA SQNASVASRL LNSQMKAELI NELDAEYQAL REKSGLLRRE TVSLEEAQKN KLNLF // ID Q8CJP1_STRCO Unreviewed; 304 AA. AC Q8CJP1; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 27-MAY-2015, entry version 60. DE SubName: Full=Putative transferase {ECO:0000313|EMBL:CAD55372.1}; GN OrderedLocusNames=SCO6137 {ECO:0000313|EMBL:CAD55372.1}; 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 {ECO:0000313|Proteomes:UP000001973}; RN [1] {ECO:0000313|EMBL:CAD55372.1, ECO:0000313|Proteomes:UP000001973} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-471 / A3(2) / M145 RC {ECO:0000313|Proteomes:UP000001973}; 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., Oliver K., O'Neil S., RA Rabbinowitsch E., Rajandream M.A., Rutherford K., Rutter S., RA Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., RA Warren T., Wietzorrek A., Woodward J., 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL939126; CAD55372.1; -; Genomic_DNA. DR PIR; T34650; T34650. DR PIR; T35920; T35920. DR RefSeq; NP_733689.1; NC_003888.3. DR RefSeq; WP_011030679.1; NC_003888.3. DR ProteinModelPortal; Q8CJP1; -. DR STRING; 100226.SCO6137; -. DR EnsemblBacteria; CAD55372; CAD55372; CAD55372. DR GeneID; 1101578; -. DR KEGG; sco:SCO6137; -. DR PATRIC; 23742188; VBIStrCoe124346_6241. DR HOGENOM; HOG000265278; -. DR InParanoid; Q8CJP1; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR PhylomeDB; Q8CJP1; -. DR Proteomes; UP000001973; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001973}; KW Reference proteome {ECO:0000313|Proteomes:UP000001973}; KW Transferase {ECO:0000313|EMBL:CAD55372.1}. SQ SEQUENCE 304 AA; 32305 MW; 73D5CED85FC4AFD4 CRC64; MTSDFADALA SGPLVLDGGL SNQLEAAGHD LGDALWSARL LAEDPEAITR AHLAYFEAGA EVAITSSYQA TFEGFARRGI GRERAAELLA LSVASAREAA RRARTARPER ALWVAASAGP YGAMLADGSE YRGRYGLGRG ALERFHRPRL EVLAAARPDV LALETVPDTD EAAALLRAVR GLDVPAWLSY TVAGDRTRAG QPLDEAFALA ADVDEVIAVG VNCCAPEDVS GAVETAARVT GKPVVAYPNS GETWDAKSRG WRGRSSYTAE RVRDWRERGA RLVGGCCRVG PETITSIARA LPRE // ID Q8DK43_THEEB Unreviewed; 1176 AA. AC Q8DK43; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 29-APR-2015, entry version 89. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:BAC08580.1}; GN Name=metH {ECO:0000313|EMBL:BAC08580.1}; OS Thermosynechococcus elongatus (strain BP-1). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Thermosynechococcus. OX NCBI_TaxID=197221 {ECO:0000313|EMBL:BAC08580.1, ECO:0000313|Proteomes:UP000000440}; RN [1] {ECO:0000313|EMBL:BAC08580.1, ECO:0000313|Proteomes:UP000000440} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BP-1 {ECO:0000313|EMBL:BAC08580.1, RC ECO:0000313|Proteomes:UP000000440}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; BA000039; BAC08580.1; -; Genomic_DNA. DR RefSeq; NP_681818.1; NC_004113.1. DR RefSeq; WP_011056870.1; NC_004113.1. DR ProteinModelPortal; Q8DK43; -. DR STRING; 197221.tll1027; -. DR EnsemblBacteria; BAC08580; BAC08580; BAC08580. DR GeneID; 1012376; -. DR KEGG; tel:tll1027; -. DR PATRIC; 23927356; VBITheElo119873_1078. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR Proteomes; UP000000440; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000440}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAC08580.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000440}; KW Transferase {ECO:0000313|EMBL:BAC08580.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 226 226 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 292 292 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 293 293 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 735 735 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1176 AA; 130222 MW; 845EB73E543149B4 CRC64; MSFLEYLHAE PRRVIVFDGA MGTNLQAQNL TAEDFGGKEY EGCNEYLVIS QPEPVAKVHR DFLAAGADVI ETNTFGSSSI VLSEYNLGDR AYEISKTAAE LAKSVAAEFS TPEKPRFVAG SMGPGTKLPT LGHIDYDTLY RAFREQAAGL FDGGVDLFII ETCQDVLQIK AALNGVMAVF QERGERRPLM VSVTMEQQGT MLVGSEIGAA LTILEPYPID ILGLNCATGP DLMTEHIRYL AQHSPFVISC IPNAGLPENI GGHAHYKLTP MELRLALTRF VEDFGVQVIG GCCGTRPDHI AALAEIAATL TPKARSPQRI PAAASIYSPQ PYDQENSFLI IGERLNASGS KKCRDLLNAE DWDGLVALAR AQVREGAHIL DVNVDYVGRD GVRDMRELVS RLVTNVTLPL MLDSTEWQKM EAGLKVAGGK CLLNSTNFED GEPRFYKVLE LAKTYGAGVV IGTIDEEGMA RTAEKKFAIA QRAYRAALDY GIPPWEIFFD PLALPISTGI EEDRGNGRET IEAIRRIRAE LPGCHILLGV SNISFGLNPA ARQVLNSMFL HEAIQAGMDA AIVSAAKILP LAKIEPEQQQ VCRDLIYDRR RFEGDVCVYD PLAELTRLFE GKSAKQNRSQ VENLPIEERL KRHIIDGDRL GLEDTLAQAL ETYAPLEIIN TFLLDGMKVV GELFASGQMQ LPFVLQSAET MKAAVAYLEP FMEKSATGDT AKGTVVIATV KGDVHDIGKN LVDIILTNNG YRVINLGIKQ PVENIIQAYE EHQADCIAMS GLLVKSTAFM KENLEVFNER GITVPVILGG AALTPKFVYE DCQSTYHGQV IYGKDAFADL HFMDRLMSAK AAGQWDDRQG FLDGTTISTP SPRAIALEPT AVPEPETPEV VDTRRSEAVA VDIPRPTPPF WGIRHLKPDQ IPLSEVFAYL DLQALIAGQW QFRKPKDQDR ATYDAFLAEK VYPILEAWKQ RILAENLLHP ELIYGYFPCQ SEGNTVYIYD PLGDKDAWVP ERAIAQFTFP RQKGGRRLCI ADFFAPVESG IIDVFPMQAV TVGEIATQVA QELFAANQYS DYLYFHGMAV QTAEALAEWC HARIRRELGC TPDPESIRDI LAQRYQGSRY SFGYPACPNM QDQYTQLRLL ESDRMGMYMD ESEQLYPEQS TTAIICYHPT AKYFSV // ID Q8DUH7_STRMU Unreviewed; 316 AA. AC Q8DUH7; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 27-MAY-2015, entry version 61. DE SubName: Full=Putative methyltransferase {ECO:0000313|EMBL:AAN58656.1}; GN OrderedLocusNames=SMU_952 {ECO:0000313|EMBL:AAN58656.1}; OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=210007 {ECO:0000313|EMBL:AAN58656.1, ECO:0000313|Proteomes:UP000002512}; RN [1] {ECO:0000313|EMBL:AAN58656.1, ECO:0000313|Proteomes:UP000002512} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700610 / UA159 {ECO:0000313|Proteomes:UP000002512}; RX PubMed=12397186; DOI=10.1073/pnas.172501299; RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., RA Carson M.B., Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., RA Qian Y., Li S., Zhu H., Najar F.Z., Lai H., White J., Roe B.A., RA Ferretti J.J.; RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental RT pathogen."; RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(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; AE014133; AAN58656.1; -; Genomic_DNA. DR RefSeq; NP_721350.1; NC_004350.2. DR RefSeq; WP_002262819.1; NC_004350.2. DR ProteinModelPortal; Q8DUH7; -. DR STRING; 210007.SMU.952; -. DR EnsemblBacteria; AAN58656; AAN58656; SMU_952. DR GeneID; 1028300; -. DR KEGG; smu:SMU_952; -. DR PATRIC; 19664033; VBIStrMut61772_0849. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR PhylomeDB; Q8DUH7; -. DR BioCyc; SMUT210007:GC7Z-906-MONOMER; -. DR Proteomes; UP000002512; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002512}; KW Methyltransferase {ECO:0000313|EMBL:AAN58656.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002512}; KW Transferase {ECO:0000313|EMBL:AAN58656.1}. SQ SEQUENCE 316 AA; 35083 MW; 4AC2627B582F4446 CRC64; MGRFKTLLNQ EDYLILHGAL GTELEFLGYD VSGKLWSAKY LLENPSIIQT IHETYLRSGS DIVTTSSYQA SYQGLCDYGL SQEEAEKMIA LTVSLAKNAR EKVWQELSEK EKQVRPYPLI SGDVGPYAAY LADGSEYTGN YGQLDKEVLK DFHRSRIKIL VDEGSDLLAL ETIPNFLEAQ ALVELLQEEF PSVEAYMSFT AQNGTTISDG TAIEEVAELI DKASQILALG INCSSPSVYS SLLKKIADIT DKPLVTYPNS GEVYDGQHQM WTQSADISHT LLENTKIWHT FGAKVVGGCC RTRPNDIESL SRGLRE // ID Q8DUN2_STRMU Unreviewed; 618 AA. AC Q8DUN2; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 27-MAY-2015, entry version 79. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=SMU_874 {ECO:0000313|EMBL:AAN58589.1}; OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=210007 {ECO:0000313|EMBL:AAN58589.1, ECO:0000313|Proteomes:UP000002512}; RN [1] {ECO:0000313|EMBL:AAN58589.1, ECO:0000313|Proteomes:UP000002512} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700610 / UA159 {ECO:0000313|Proteomes:UP000002512}; RX PubMed=12397186; DOI=10.1073/pnas.172501299; RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., RA Carson M.B., Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., RA Qian Y., Li S., Zhu H., Najar F.Z., Lai H., White J., Roe B.A., RA Ferretti J.J.; RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental RT pathogen."; RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002). CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE014133; AAN58589.1; -; Genomic_DNA. DR RefSeq; NP_721283.1; NC_004350.2. DR RefSeq; WP_002262022.1; NC_004350.2. DR ProteinModelPortal; Q8DUN2; -. DR STRING; 210007.SMU.874; -. DR EnsemblBacteria; AAN58589; AAN58589; SMU_874. DR GeneID; 1028241; -. DR KEGG; smu:SMU_874; -. DR PATRIC; 19663895; VBIStrMut61772_0780. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR PhylomeDB; Q8DUN2; -. DR BioCyc; SMUT210007:GC7Z-839-MONOMER; -. DR Proteomes; UP000002512; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002512}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000002512}. SQ SEQUENCE 618 AA; 68055 MW; CA1794AFFD66A86B CRC64; MSRLLDKLKT DILVADGAMG TLLYADGLES CHEYYNISHP ERILAIHQAY IAAGADIIQT NTYGAKRHRL KSFGHDKEVK AINQAAVHLA RQAAGDNTFV LGTIGASHGL KHCELSLEDI ISQTVEQARF LLETKQIDGL LLETYYDIEE LEAALKALRP LTDLPIITNV ALHEPGITEN GRPLVEAFSN LVMLGADIVG LNCHLGPYHM IQSFKQVPLF AQSYLSAYPN ASLLSFSSDD NETPYHFSQN ADYFEYCAKL FVEEGVRLIG GCCGTTPEHI KAIKRGIRGL KPIERKVTTP LISQEDLIYE VEKKESLVDK VKKGITIIAE IDPPKTLAVD KFVDGVKALD EKGIAAITLA DNSLARTRIC NLSMASMLKD EIATPFLLHL SCRDHNMIGL QSRLLGMDLL GFDHILAITG DPSKIGDFPG ATSVYDATSF KLLSLIKQLN QGHGYSGASL KKATHFTVAA AFNPNVKNLS RTGRLIEKKV AAGADYFITQ PVFSETVIQE LSEVTKPYEQ PFFVGIMPIT SYNNAVFLHN EVPGISLSES FLAKLEAVKD DKETCQKVAL AESKKLIDAI LAHFNGIYLI TPFLRYDLTV ELIDYIQVKT ATVAKKRT // ID Q8DX11_STRA5 Unreviewed; 614 AA. AC Q8DX11; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 27-MAY-2015, entry version 69. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=SAG2048 {ECO:0000313|EMBL:AAN00907.1}; OS Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=208435 {ECO:0000313|EMBL:AAN00907.1, ECO:0000313|Proteomes:UP000000821}; RN [1] {ECO:0000313|EMBL:AAN00907.1, ECO:0000313|Proteomes:UP000000821} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-611 / 2603 V/R {ECO:0000313|Proteomes:UP000000821}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; AAN00907.1; -; Genomic_DNA. DR RefSeq; NP_689034.1; NC_004116.1. DR RefSeq; WP_000032989.1; NC_004116.1. DR ProteinModelPortal; Q8DX11; -. DR STRING; 208435.SAG2048; -. DR EnsemblBacteria; AAN00907; AAN00907; SAG2048. DR GeneID; 1014859; -. DR KEGG; sag:SAG2048; -. DR PATRIC; 19630937; VBIStrAga72745_2051. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; SAGA208435:GHVY-2146-MONOMER; -. DR Proteomes; UP000000821; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000821}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Methyltransferase {ECO:0000313|EMBL:AAN00907.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000000821}; KW Transferase {ECO:0000313|EMBL:AAN00907.1}. SQ SEQUENCE 614 AA; 68034 MW; BAB409F963937584 CRC64; MSKFLEKLKT DILVADGAMG TLLYTYGLDT CHESYNVTHP EKVLAIHQAY IEAGADVIQT NTYGAQRHRL KNYGLEDQVV SINQAAVNIA HQATLGKETF ILGTVGGFRS QRQCDLTLDN IVEETLEQVE ALLATGQLDG LLFETYYDIE EITTVLKIVR EMTDLPIITN ISLHEAGVTS NGKPIVEALS QLVMLGADVI GLNCHLGPYH MIQSLKQVPL FAQSYLSVYP NASQLSLDGE NSQYQFSQNS EYFGKSAELL VAEGVRLIGG CCGTTPDHIR AVKRSIRGLK PIERKVVTPI IPVKDFVRRI RRTDTLVDKV KKEVTIIAEL DPPKHLDIVQ FQKAIRAIDQ KGIAAITLAD NSLSNTRICN LSIASLLKDE ISTPFLLHIA CRDHNLIGLQ SRLLGMELLG FNHILAITGD PTKLGDFPGA TSVYDVTSFK LLSLIKQLNQ GLSYSGASLR RPTDFTVAAA FNPNVKNLTR TVKLIEKKVA SGADYFMTQP IFDHSVLKEL ADLTKTVEQP FFIGIMPITS YNNAVFLHNE VPGIKLSESF LSALEKVKDD KEACLTLALN ESKSLIDEAL NYFNGIYLIT PFLRYDLTLE LIDYIQKKQV RKSS // ID Q8DZ17_STRA5 Unreviewed; 314 AA. AC Q8DZ17; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 27-MAY-2015, entry version 53. DE SubName: Full=Homocysteine S-methyltransferase MmuM, putative {ECO:0000313|EMBL:AAN00176.1}; GN OrderedLocusNames=SAG1305 {ECO:0000313|EMBL:AAN00176.1}; OS Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=208435 {ECO:0000313|EMBL:AAN00176.1, ECO:0000313|Proteomes:UP000000821}; RN [1] {ECO:0000313|EMBL:AAN00176.1, ECO:0000313|Proteomes:UP000000821} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-611 / 2603 V/R {ECO:0000313|Proteomes:UP000000821}; 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 ----------------------------------------------------------------------- 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; AAN00176.1; -; Genomic_DNA. DR RefSeq; NP_688303.1; NC_004116.1. DR RefSeq; WP_000532342.1; NC_004116.1. DR ProteinModelPortal; Q8DZ17; -. DR STRING; 208435.SAG1305; -. DR EnsemblBacteria; AAN00176; AAN00176; SAG1305. DR GeneID; 1014112; -. DR KEGG; sag:SAG1305; -. DR PATRIC; 19629453; VBIStrAga72745_1314. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; SAGA208435:GHVY-1399-MONOMER; -. DR Proteomes; UP000000821; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000821}; KW Methyltransferase {ECO:0000313|EMBL:AAN00176.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000821}; KW Transferase {ECO:0000313|EMBL:AAN00176.1}. SQ SEQUENCE 314 AA; 34096 MW; CF64421985B9B86B CRC64; MGRFKELLES KKTLILHGAL GTELESRGCD VSGKLWSAKY LIEDPAAIQT IHEDYIRAGA DIVTTSTYQA TLQGLAQVGV SESQTEDLIR LTVQLAKAAR EQVWKSLTKE EKSERIYPLI SGDVGPYAAF LADGSEYTGL YDIDKQGLKN FHRHRIELLL DEGVDILALE TIPNAQEAEA LIELLAEDFP QVEAYMSFTS QDGKTISDGS AVADLAKAID VSPQVVALGI NCSSPSLVAD FLQAIAEQTN KPLVTYPNSG EVYDGASQSW QSSPDHSHTL LENTSDWQKL GAQVVGGCCR TRPADIADLS AHLK // ID Q8E2W0_STRA3 Unreviewed; 614 AA. AC Q8E2W0; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 27-MAY-2015, entry version 75. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=gbs2004 {ECO:0000313|EMBL:CAD47663.1}; OS Streptococcus agalactiae serotype III (strain NEM316). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=211110 {ECO:0000313|EMBL:CAD47663.1, ECO:0000313|Proteomes:UP000000823}; RN [1] {ECO:0000313|EMBL:CAD47663.1, ECO:0000313|Proteomes:UP000000823} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NEM316 {ECO:0000313|EMBL:CAD47663.1, RC ECO:0000313|Proteomes:UP000000823}; RX PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x; RA Glaser P., Rusniok C., Chevalier F., Buchrieser C., Frangeul L., RA Zouine M., Couve E., Lalioui L., Msadek T., 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL766855; CAD47663.1; -; Genomic_DNA. DR RefSeq; NP_736437.1; NC_004368.1. DR RefSeq; WP_000032989.1; NC_004368.1. DR ProteinModelPortal; Q8E2W0; -. DR STRING; 211110.gbs2004; -. DR EnsemblBacteria; CAD47663; CAD47663; CAD47663. DR KEGG; san:gbs2004; -. DR PATRIC; 19639939; VBIStrAga3577_2054. DR GenoList; gbs2004; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR Proteomes; UP000000823; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000823}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 614 AA; 68034 MW; BAB409F963937584 CRC64; MSKFLEKLKT DILVADGAMG TLLYTYGLDT CHESYNVTHP EKVLAIHQAY IEAGADVIQT NTYGAQRHRL KNYGLEDQVV SINQAAVNIA HQATLGKETF ILGTVGGFRS QRQCDLTLDN IVEETLEQVE ALLATGQLDG LLFETYYDIE EITTVLKIVR EMTDLPIITN ISLHEAGVTS NGKPIVEALS QLVMLGADVI GLNCHLGPYH MIQSLKQVPL FAQSYLSVYP NASQLSLDGE NSQYQFSQNS EYFGKSAELL VAEGVRLIGG CCGTTPDHIR AVKRSIRGLK PIERKVVTPI IPVKDFVRRI RRTDTLVDKV KKEVTIIAEL DPPKHLDIVQ FQKAIRAIDQ KGIAAITLAD NSLSNTRICN LSIASLLKDE ISTPFLLHIA CRDHNLIGLQ SRLLGMELLG FNHILAITGD PTKLGDFPGA TSVYDVTSFK LLSLIKQLNQ GLSYSGASLR RPTDFTVAAA FNPNVKNLTR TVKLIEKKVA SGADYFMTQP IFDHSVLKEL ADLTKTVEQP FFIGIMPITS YNNAVFLHNE VPGIKLSESF LSALEKVKDD KEACLTLALN ESKSLIDEAL NYFNGIYLIT PFLRYDLTLE LIDYIQKKQV RKSS // ID Q8E4M4_STRA3 Unreviewed; 314 AA. AC Q8E4M4; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 27-MAY-2015, entry version 58. DE SubName: Full=Gbs1377 protein {ECO:0000313|EMBL:CAD47036.1}; GN OrderedLocusNames=gbs1377 {ECO:0000313|EMBL:CAD47036.1}; OS Streptococcus agalactiae serotype III (strain NEM316). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=211110 {ECO:0000313|EMBL:CAD47036.1, ECO:0000313|Proteomes:UP000000823}; RN [1] {ECO:0000313|EMBL:CAD47036.1, ECO:0000313|Proteomes:UP000000823} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NEM316 {ECO:0000313|EMBL:CAD47036.1, RC ECO:0000313|Proteomes:UP000000823}; RX PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x; RA Glaser P., Rusniok C., Chevalier F., Buchrieser C., Frangeul L., RA Zouine M., Couve E., Lalioui L., Msadek T., 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL766850; CAD47036.1; -; Genomic_DNA. DR RefSeq; NP_735814.1; NC_004368.1. DR RefSeq; WP_000532330.1; NC_004368.1. DR ProteinModelPortal; Q8E4M4; -. DR STRING; 211110.gbs1377; -. DR EnsemblBacteria; CAD47036; CAD47036; CAD47036. DR KEGG; san:gbs1377; -. DR PATRIC; 19638637; VBIStrAga3577_1407. DR GenoList; gbs1377; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR Proteomes; UP000000823; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000823}. SQ SEQUENCE 314 AA; 34232 MW; 21B6FAA96850EC06 CRC64; MGRFKELLES KKALILHGAL GTELESRGCD VSGKLWSDKY LIEDPAAIQT IHEDYIRAGA DIVTTSTYQA TLQGLAQVGV SESQAEDLIR LTVQLAKAVR EQVWKSLTKE EKSERIYPLI SGDVGPYAAF LADGSEYTGL YDIYKEGLKN FHRHRIELLL DEGVDLLALE TIPNAQEAEA LIELLVEDFP QVEAYMSFTS QDGKTISDGS AVAGLAKAID VSPQVVALGI NCSSPSLVAD FLQAIAEQTD KPLVTYPNSG EIYDGASQSW QSSRDHSHTL LENTSDWQKL GAQVVGGCCR TRPADIADLS EHLT // ID Q8EI23_SHEON Unreviewed; 1244 AA. AC Q8EI23; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 01-APR-2015, entry version 87. DE SubName: Full=B12-dependent 5-methyltetrahydrofolate--homocysteine methyltransferase MetH {ECO:0000313|EMBL:AAN54103.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AAN54103.1}; GN Name=metH {ECO:0000313|EMBL:AAN54103.1}; GN OrderedLocusNames=SO_1030 {ECO:0000313|EMBL:AAN54103.1}; OS Shewanella oneidensis (strain MR-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=211586 {ECO:0000313|EMBL:AAN54103.1, ECO:0000313|Proteomes:UP000008186}; RN [1] {ECO:0000313|EMBL:AAN54103.1, ECO:0000313|Proteomes:UP000008186} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MR-1 {ECO:0000313|EMBL:AAN54103.1, RC ECO:0000313|Proteomes:UP000008186}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AE014299; AAN54103.1; -; Genomic_DNA. DR RefSeq; NP_716658.1; NC_004347.2. DR RefSeq; WP_011071290.1; NC_004347.2. DR ProteinModelPortal; Q8EI23; -. DR SMR; Q8EI23; 668-1244. DR STRING; 211586.SO_1030; -. DR EnsemblBacteria; AAN54103; AAN54103; SO_1030. DR GeneID; 1168870; -. DR KEGG; son:SO_1030; -. DR PATRIC; 23521707; VBISheOne101494_0987. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR PhylomeDB; Q8EI23; -. DR Proteomes; UP000008186; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008186}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AAN54103.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008186}; KW Transferase {ECO:0000313|EMBL:AAN54103.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 258 258 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 774 774 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1244 AA; 137861 MW; AE500C3D017E4621 CRC64; MAISPNRASH TLADIRNQLS TRILILDGAM GTMIQGYKLE EADYRGERFK DWHTDVKGNN DLLVLTQPHI IKQIHTDYLL AGADIIETNT FNATTIAMAD YDMQSLSAEI NREGARLARE ACDAIEQATG KPRYVAGVLG PTNRTCSISP DVNDPGFRNI HFDELVTAYC ESTRALIEGG ADIIMVETIF DTLNAKAALF AIETVFDELF GANSPARLPV MISGTITDAS GRTLTGQTTE AFYNSLRHIK PLSIGLNCAL GPKELRPYVE ELSRIAECYV SAHPNAGLPN EFGGYDETPE DMAKVIQEWA REGMLNIIGG CCGSTPEHIK VIREAVEQFA PRVLPEIPVA CRLAGLEPLT IDAQTLFVNV GERTNVTGSA KFLKLIKEGK FEQALDVARE QVESGAQIID INMDEGMLDG VEIMHKFLNL IASEPDISRV PIMIDSSKWE VIEAGLKCIQ GKGIVNSISL KEGEEKFIEQ ATLVKRYGAA AIIMAFDEQG QADTKARKVE ICTRAYRVLV DKVGFPPEDI IFDPNIFAIA TGIDEHDNYA VDFIDAIKEI KATLPHAMIS GGVSNVSFSF RGNNPVREAI HAVFLYHAIK VGMDMGIVNA GQLAIFDDID PELKVRVENV VLNLPCPVEG SNNTEQLLEI AEKFRGDGSS SAKKEDLEWR SWPVNQRLAH ALVKGITEFI DEDTEAARQA ASRPLDVIEG PLMDGMNIVG DLFGSGKMFL PQVVKSARVM KKAVAYLNPF IEKEKVAGQS NGKILMVTVK SDVHDIGKNI VGVVLACNGF EVFDLGVMVS VERILEAVKE HNIDIIGMSG LITPSLDEMV HNVKTFHREG LTIPAIIGGA TCSKIHTAVK IAPHYPHGAI YIADASRAVP MVSKLVNNET RQATIDETYA EYDDMRTKRL SQAKRKEIVS LEAARENRCQ HDWANYSPFK PNVLGRQVFD DYPLTDLVDR IDWTPFFRAW ELHGHYPEIL SDKVVGVEAQ KLFSDGKAML KKIIEEKWLT AKGVIGLFPA NTVGFDDIEL YTDETRTEVE LTTHHLRMQL ERVGNDNFCL ADFVAPKDSG VADYMGGFAV TAGHGIDEHV ARFEANHDDY NAIMLKCLAD RLAEAFAERM HERVRKEFWG YAADEQLDNE ALIREKYKGI RPAPGYPACP DHTEKGLLWE LLKPNETIDL NITESYAMFP TAAVSGWYFA HPKSRYFGVS NIGRDQVEDY AKRKGMTVAE TEKWLAPVLD YDPE // ID Q8ESE8_OCEIH Unreviewed; 349 AA. AC Q8ESE8; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 27-MAY-2015, entry version 61. DE SubName: Full=Betaine-homocysteine methyltransferase {ECO:0000313|EMBL:BAC12647.1}; GN OrderedLocusNames=OB0691 {ECO:0000313|EMBL:BAC12647.1}; OS Oceanobacillus iheyensis (strain DSM 14371 / JCM 11309 / KCTC 3954 / OS HTE831). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; OC Oceanobacillus. OX NCBI_TaxID=221109 {ECO:0000313|EMBL:BAC12647.1, ECO:0000313|Proteomes:UP000000822}; RN [1] {ECO:0000313|EMBL:BAC12647.1, ECO:0000313|Proteomes:UP000000822} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14371 / JCM 11309 / KCTC 3954 / HTE831 RC {ECO:0000313|Proteomes:UP000000822}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; BAC12647.1; -; Genomic_DNA. DR RefSeq; NP_691612.1; NC_004193.1. DR RefSeq; WP_011065099.1; NC_004193.1. DR ProteinModelPortal; Q8ESE8; -. DR STRING; 221109.OB0691; -. DR EnsemblBacteria; BAC12647; BAC12647; BAC12647. DR KEGG; oih:OB0691; -. DR PATRIC; 22792341; VBIOceIhe82024_0706. DR HOGENOM; HOG000231636; -. DR OMA; KAHYMSQ; -. DR OrthoDB; EOG6NSGDJ; -. DR BioCyc; OIHE221109:GI2A-756-MONOMER; -. DR Proteomes; UP000000822; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000822}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:BAC12647.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000822}; KW Transferase {ECO:0000313|EMBL:BAC12647.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 210 210 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 298 298 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 299 299 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 349 AA; 39340 MW; FBF05831D7E201A4 CRC64; MKRSLQRRLQ EGTVIAGEGY LFELERRGYL QAGSFVPEVA LENPDALKQT YRDFMNAGSD VVLAFTYNAH REKMRIIGKE QLLEPLNRSA IRLAKEVAKE HPQEEALVAG NISNTNIFDP NDESSKHKVR EMFAEMAQWS KEEDVDFING ETFYYHEEAE IALEEILKKD LPAVITLGLM GENILRDCYT VEESCKILSE KGALVVGMNC FRGPDTMQPY IAKIRQHVDG YVGALPIPYR TSNEHPTFFN LPDGGCSCHL PTETTFPTAL DPLYHNRYEL AAWAKEAKEI GVNYIGLCCG ASPAMLRAVA ESVGKETVNS PYSPDMEKHF LFGKDKSLKE HNVGYRFKA // ID Q8EXU9_LEPIN Unreviewed; 1247 AA. AC Q8EXU9; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 27-MAY-2015, entry version 87. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AAN51667.1}; GN Name=metH {ECO:0000313|EMBL:AAN51667.1}; GN OrderedLocusNames=LB_108 {ECO:0000313|EMBL:AAN51667.1}; OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai OS (strain 56601). OC Bacteria; Spirochaetes; Spirochaetales; Leptospiraceae; Leptospira. OX NCBI_TaxID=189518 {ECO:0000313|EMBL:AAN51667.1, ECO:0000313|Proteomes:UP000001408}; RN [1] {ECO:0000313|EMBL:AAN51667.1, ECO:0000313|Proteomes:UP000001408} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=56601 {ECO:0000313|EMBL:AAN51667.1, RC ECO:0000313|Proteomes:UP000001408}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AE010301; AAN51667.1; -; Genomic_DNA. DR RefSeq; NP_714652.1; NC_004343.2. DR RefSeq; WP_000262613.1; NC_004343.2. DR ProteinModelPortal; Q8EXU9; -. DR SMR; Q8EXU9; 657-901. DR STRING; 189518.LB108; -. DR EnsemblBacteria; AAN51667; AAN51667; LB_108. DR GeneID; 1154034; -. DR KEGG; lil:LB_108; -. DR PATRIC; 22389771; VBILepInt91350_4435. DR HOGENOM; HOG000251409; -. DR InParanoid; Q8EXU9; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; LINT189518:GJBB-3544-MONOMER; -. DR Proteomes; UP000001408; Chromosome II. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001408}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001408}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 255 255 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 318 318 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 319 319 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 769 769 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1247 AA; 138768 MW; E55374595CEBC1B9 CRC64; MVYKVQNYTN PSSKELLSLL EKQILVIDGA MGTMIQRFSL QEEDFRGEIL KNHLHPLKGN NELLCLTRPD VIESIHLKFL EAGANIVETN TFSSNQISQG DYKTEFLVAD LNKAAVVCAR NAITKFQKTN PDHPCLIAGA IGPTTKTATL SPDVNNPAFR AVTFDDLVAT FYEQARALVE SGVDLLLPET NIDTLNLKAA IFAIEQVFED LQVRIPVCLS VTITDASGRT LSGQTVEAFY NSIAHCNPLS VGINCALGAD EMRPYIEELA RVSPCYISCY PNAGLPNAFG GYDQTPEEFG KYIQEFASSG WLNIAGGCCG TTPEHIEAAA KAVRGKKPRI LPKIEEVTRL SGLEPLNITP DKGFLLVGER TNVTGSPKFK KLIIEGNFEE AVSVALQQVE AGANIIDINF DEALLDGEAS MRHFLNLIAG EPDIAKVPFM IDSSKWSVLE EGLKCIQGKP ILNSISLKEG EDKFLEYAKK IQRYGASAIV MAFDEQGQAA TKEDKVRICK RAYDLLVTKA NFSPTDIIFD PNILTVATGI EEHNNYAVDF IEAVREIKKL CPGAKVSGGL SNVSFSFRGN NPVREAMHSV FLYYAIQAGM DMAIVNAGML AVYEEIPKDL LEYVEDVILN RRPDATERLV EFAESVKSTG DKTEKKEEAW REGTSVEERL SHALVKGIVE YIDQDTEEAR LKYGRPLTVI EGPLMDGMKI VGELFGAGKM FLPQVVKSAR VMKKSVAYLL PFMEEEKNQI ENSTARPKFL IATVKGDVHD IGKNIVGVVL ACNNYEVIDL GVMVPPDKIL EEAKKHNVSI IGLSGLITPS LDEMVHVASE MKRIGLEIPL LIGGATTSSA HTAVKIAPVY DHPVVHVVDA SRVVNVVNQL LHPDLHEAYS QKVKEDQKIA RENYFNTRAE RKLISLEQAR ENRDPIDWST TVIDKPSFIG IKVFDEEISL ETLVPFIDWT PFFTAWELKG RYPAILESET TGKQARELFA DAQKLMKTII TGKLFRTKGV IGIFPANSVR DDIFVYEDEN CSKLLTVFHT LRQQIQKQDE TEPNYCLADY VAPKESGRVD YIGGFAVTAG HGVEEFAKEF ENNQDDYNSI MAKALGDRFA EAFAEYMHYK VRKEYWGYDK NENLSPEDLI REKYRGIRPA AGYPASPDHT EKRALFDLLQ VEKNTGITLT EHFAMWPASS VSGLYFAHPK SKYFAVAKIN RDQVEDYAKR KEMSVEVVER WLAPNLSYDP LAVSAVR // ID Q8FTD2_COREF Unreviewed; 1213 AA. AC Q8FTD2; C8NNU6; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 29-APR-2015, entry version 95. DE SubName: Full=Putative 5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:BAC18447.1}; 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 {ECO:0000313|EMBL:BAC18447.1, ECO:0000313|Proteomes:UP000001409}; RN [1] {ECO:0000313|EMBL:BAC18447.1, ECO:0000313|Proteomes:UP000001409} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395 RC {ECO:0000313|Proteomes:UP000001409}; 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 ----------------------------------------------------------------------- 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; BAC18447.1; -; Genomic_DNA. DR RefSeq; NP_738247.1; NC_004369.1. DR RefSeq; WP_006767637.1; NZ_GG700683.1. DR ProteinModelPortal; Q8FTD2; -. DR STRING; 196164.CE1637; -. DR EnsemblBacteria; BAC18447; BAC18447; BAC18447. DR EnsemblBacteria; EEW49748; EEW49748; HMPREF0290_1671. DR KEGG; cef:CE1637; -. DR PATRIC; 21489415; VBICorEff9312_1630. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR Proteomes; UP000001409; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001409}; KW Methyltransferase {ECO:0000313|EMBL:BAC18447.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001409}; KW Transferase {ECO:0000313|EMBL:BAC18447.1}. SQ SEQUENCE 1213 AA; 132785 MW; 6284480AED4EF3D8 CRC64; MSDTATSSAF LDALRSHVLI GDGAMGTQLQ AFDLDVEDDF LGLEGCNEIL NHTRPDVLRQ IHRAYFEAGA DLVETNTFGC NLPNLADYDI ADRCRELAYK GTAVAREVAD EMGPGRNGMR RFVVGSLGPG TKLPSLGHAP YGDLRGHYKE AALGIIEGGG DAFLIETAQD LLQVKAAVHG VQDAMTELGV TLPIICHVTV ETTGTMLMGS EIGAALTALE PLGIDMIGLN CATGPAEMSE HLRYLSKHAS IPVSVMPNAG LPVLGKNGAE YPLTAEELAE ALRGFVTDYG LSMVGGCCGT TPEHIRAVRD AVVGVPEGET SALESVPVGP VERAEREIEV EDAVASLYTS VPLSQGTGIT MIGERTNANG SRAFREAMLA GDWEKCVDIA KQQTRDGAHM LDLCVDYVGR DGREDMATLA SLLATSSTLP IMLDSTEPEV IRVGLEHLGG RSIVNSVNFE DGDGPESRYR RIMAMVQQHG AAVVALTIDE EGQARTAEHK IRIAERLIED ITGTYGLKES DIIVDCLTFP ISTGQEETRR DGIETIEAIR ELKKRHPEVH TTLGLSNISF GLNPAARQVL NSVFLHECIQ VGLDSAIAHS SKILPMNRID ERQREVALDM VYDRRAEGYD PLQEFMQLFE GVSAADAKDA RAEALAAMPL FERLAQRIID GDKNGLEEDL EAGMKEKKPI EIINEDLLNG MKTVGELFGS GQMQLPFVLQ SAETMKTAVA YLEPFMEDEA EATGEARAES KGRIVLATVK GDVHDIGKNL VDIIMSNNGY DVVNLGIKQP ISAMLEAAEK HNADAIGMSG LLVKSTVVMK DNLEEMNAAK ASHYPVMLGG AALTRTYVEN DLAEVYQGDV YYARDAFEGL SLMDELMAEQ RGEGADPDSP EAIEAARKKE ERRARNERSK RIAAERKAKA EPVEVPERSD VATDTPVATP PFWGTRIVKG LALAEYLPTL DERALFMGQW GLKATRGGEG PSYEELVETE GRPRFRYWID RLKAEGILDH TAIVYGYFPA VSEGDDVVIL ESPEPDAPER MRFSFPRQQR GRFLCIADFI RPREQAIAEG QVDVFPFQLV TMGDPIAQFA NKLFAANEYR DYLEVHGLGV QLTEAIAEYW HARIRSELQL TTGGTAADDD AEDKKKFFDL DYRGARFSFG YGSCPDLEDR IKMVELLQPE RIGVELSEEL QLHPEQSTDA FVLYHPEAKY FNV // ID Q8H825_ORYSJ Unreviewed; 329 AA. AC Q8H825; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 27-MAY-2015, entry version 69. DE SubName: Full=Homocysteine S-methyltransferase 1, putative, expressed {ECO:0000313|EMBL:ABF94697.1}; DE SubName: Full=Putative homocysteine S-methyltransferase-1 {ECO:0000313|EMBL:AAN05322.1}; GN Name=OJ1743A09.2 {ECO:0000313|EMBL:AAN05322.1}; GN OrderedLocusNames=LOC_Os03g12110 {ECO:0000313|EMBL:ABF94697.1}; GN ORFNames=OsJ_09954 {ECO:0000313|EMBL:EAZ26096.1}; 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 {ECO:0000313|Proteomes:UP000000763}; RN [1] {ECO:0000313|EMBL:AAN05322.1} RP NUCLEOTIDE SEQUENCE. RA Wing R.A., Yu Y., Soderlund C., Kim H.-R., Rambo T., Saski C., RA Currie J., Collura K.; RT "Rice Genomic Sequence."; RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ABF94697.1, ECO:0000313|Proteomes:UP000000763} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000000763}; RX PubMed=16109971; DOI=10.1101/gr.3869505; RG The rice chromosome 3 sequencing consortium; RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., RA Haas B., Wortman J., Pertea M., Jones K.M., Kim M., Overton L., RA Tsitrin T., Fadrosh D., Bera J., Weaver B., Jin S., Johri S., RA Reardon M., Webb K., Hill J., Moffat K., Tallon L., Van Aken S., RA Lewis M., Utterback T., Feldblyum T., Zismann V., Iobst S., Hsiao J., RA de Vazeille A.R., Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., RA Rambo T., Currie J., Collura K., Kernodle-Thompson S., Wei F., RA Kudrna K., Ammiraju J.S.S., Luo M., Goicoechea J.L., Wing R.A., RA Henry D., Oates R., Palmer M., Pries G., Saski C., Simmons J., RA Soderlund C., Nelson W., de la Bastide M., Spiegel L., Nascimento L., RA Huang E., Preston R., Zutavern T., Palmer L., O'Shaughnessy A., RA Dike S., McCombie W.R., Minx P., Cordum H., Wilson R., Jin W., RA Lee H.R., Jiang J., Jackson S.; RT "Sequence, annotation, and analysis of synteny between rice chromosome RT 3 and diverged grass species."; RL Genome Res. 15:1284-1291(2005). RN [3] {ECO:0000313|Proteomes:UP000000763} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000000763}; 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 [4] {ECO:0000313|EMBL:EAZ26096.1, ECO:0000313|Proteomes:UP000000763} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000000763}; 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] {ECO:0000313|EMBL:ABF94697.1} RP NUCLEOTIDE SEQUENCE. RA Buell R., Wing R.A., McCombie W.A., Ouyang S.; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000313|EMBL:EAZ26096.1} 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 [7] {ECO:0000313|Proteomes:UP000000763} RP GENOME REANNOTATION. RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000000763}; 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 [8] {ECO:0000313|EMBL:EAZ26096.1} 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AC105364; AAN05322.1; -; Genomic_DNA. DR EMBL; DP000009; ABF94697.1; -; Genomic_DNA. DR EMBL; CM000140; EAZ26096.1; -; Genomic_DNA. DR ProteinModelPortal; Q8H825; -. DR Gramene; Q8H825; -. DR InParanoid; Q8H825; -. DR OMA; AINDPLW; -. DR Proteomes; UP000000763; Chromosome 3. DR ExpressionAtlas; Q8H825; baseline. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000763}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:AAN05322.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000763}; KW Transferase {ECO:0000313|EMBL:AAN05322.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 236 236 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 303 303 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 329 AA; 35811 MW; 0F5D87D224C7CB1B CRC64; MAVAVEEIVR RAGGCAVIDG GFATQLEALG ADINDPLWSA ACLITKPHLI KEVHMQYLEA GADVIISSSY QATIPGFLAR GMLLEEAEGL LRRSIELALE ARDEFWKSTL RKSKPVYNRA LVAASIGSYG AYLADGSEYS GSYGEDITAE KLKDFHRRRL QVLASAGPDL IAFEAIPNKM EAQALVELLE EENIQVPSWI CFSSVDGKNL CSGESFAECL QFLNASDKVT IVGVNCTPPQ FIEGIIRELK KQTKKAIAVY PNSGEIWDGR AKRWLPAQCF GHKSFDALAK RWQEAGASLV GGCCRTTPST IRAVSKVLKG KTSYSATQI // ID Q8I585_PLAF7 Unreviewed; 581 AA. AC Q8I585; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 27-MAY-2015, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAN36411.1}; GN ORFNames=PFL1625w {ECO:0000313|EMBL:AAN36411.1}; OS Plasmodium falciparum (isolate 3D7). OC Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Plasmodium (Laverania). OX NCBI_TaxID=36329 {ECO:0000313|EMBL:AAN36411.1, ECO:0000313|Proteomes:UP000001450}; RN [1] {ECO:0000313|EMBL:AAN36411.1, ECO:0000313|Proteomes:UP000001450} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Isolate 3D7 {ECO:0000313|Proteomes:UP000001450}; 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., James K., RA Eisen J.A., Rutherford K., Salzberg S.L., Craig A., Kyes S., RA Chan M.-S., Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., RA Pertea M., Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., RA Martin D.M.A., Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., RA McFadden G.I., Cummings L.M., Subramanian G.M., Mungall C., RA Venter J.C., Carucci D.J., Hoffman S.L., Newbold C., Davis R.W., RA Fraser C.M., Barrell B.; RT "Genome sequence of the human malaria parasite Plasmodium RT falciparum."; RL Nature 419:498-511(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; AE014849; AAN36411.1; -; Genomic_DNA. DR RefSeq; XP_001350731.1; XM_001350695.1. DR ProteinModelPortal; Q8I585; -. DR IntAct; Q8I585; 1. DR MINT; MINT-1688889; -. DR EnsemblProtists; PFL1625w:mRNA; PFL1625w:pep; PFL1625w. DR GeneID; 811377; -. DR KEGG; pfa:PFL1625w; -. DR EuPathDB; PlasmoDB:PF3D7_1233700; -. DR HOGENOM; HOG000283439; -. DR InParanoid; Q8I585; -. DR Proteomes; UP000001450; Chromosome 12. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 4. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 4. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001450}; KW Reference proteome {ECO:0000313|Proteomes:UP000001450}. SQ SEQUENCE 581 AA; 68955 MW; B3FF6E9A0BD5D731 CRC64; MRKDLYTLDG GKISELGRLG YENFDFLSYE MNEENENNDN MISILENIHL SYLLGGCNII GTNTFQVNLY SFKKLGIDNG EEILNKYINI AYNSLLKYEE IKRKSKDDIN VLLNPRNKNI SVYDYLSSYH KIRKKFDILH EKDVSFNIDN YLKDIKIEQN IGHNKYRKFN KNRNNYISFS NGPYSSTFAD FSEYSGVMQK NKEDKNGEKK KKMKKNKEKK EEKKNKYIND NLCNFVDEKS QGKKKKNMSE YYQLDKNIIK NKNNIDRNIK KSINYKAYYK YSLYYDIQMN ISSVNSYGRE KYNPIEIVPK MKKKIQNVNC TNKDETNIIN THNNNNNDNI FFNKKLFNYG IEYYIDVSDQ EIISNCLFKL NTFCKNSDKL HLFSLTTFSN IREVLTFYNC IKYYGSTFNN KVIINFFCNS CKYVGCSKYS FFDIVSILLY LDSYNKYIKA IGLNCVNIEY VYDLFYPFQK YICPYNNINT NLYHSQNIQM NNIVKDVMKD LKKNRYINDF NFFCSPNKSL EVVSFDDQNG DVHFHNSANK TNHVYNYIEK WINVHVNGFG GCCYYNPYDI SLINYKINEL L // ID Q8JIY6_DANRE Unreviewed; 1263 AA. AC Q8JIY6; DT 01-OCT-2002, integrated into UniProtKB/TrEMBL. DT 01-OCT-2002, sequence version 1. DT 27-MAY-2015, entry version 100. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|EMBL:AAH45477.1}; DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AAM33342.1}; GN Name=mtr {ECO:0000313|EMBL:AAH45477.1, GN ECO:0000313|ZFIN:ZDB-GENE-031001-5}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|EMBL:AAM33342.1}; RN [1] {ECO:0000313|EMBL:AAM33342.1} RP NUCLEOTIDE SEQUENCE. RA Irwin M.S., Moser M.M., Carlson J.N., Gilroy H.H.III., Ellis A.R., RA Warren J.T.Jr.; RT "Molecular Genetic Analysis of Folate Metabolism in the Zebrafish."; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AAH45477.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=AB {ECO:0000313|EMBL:AAH45477.1}; RC TISSUE=Whole body {ECO:0000313|EMBL:AAH45477.1}; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; BC045477; AAH45477.1; -; mRNA. DR EMBL; AF506733; AAM33342.1; -; mRNA. DR RefSeq; NP_932338.1; NM_198072.1. DR UniGene; Dr.75737; -. DR ProteinModelPortal; Q8JIY6; -. DR SMR; Q8JIY6; 663-918, 924-1262. DR STRING; 7955.ENSDARP00000057160; -. DR GeneID; 378847; -. DR CTD; 4548; -. DR ZFIN; ZDB-GENE-031001-5; mtr. DR eggNOG; COG1410; -. DR HOVERGEN; HBG006347; -. DR PhylomeDB; Q8JIY6; -. DR NextBio; 20813844; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 2: Evidence at transcript level; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AAH45477.1}; KW Transferase {ECO:0000313|EMBL:AAH45477.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 258 258 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 321 321 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 783 783 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1263 AA; 139704 MW; 0F64BF9F2CF9608F CRC64; MPPTIHQSPA GRASSLRLEL TELLQQRILV LDGGMGTMIQ QRHLEEEEFR GQEFKDHPKS LKGNNDILSI TQPDVIYSIH KEYLEAGADI IETNTFSSTS IAQADYGMED LAYRLNKASA EVARRAADDV SAQTGCKRFV AGALGPTNKT LSVSPSVERP DYRNITFDEL VEAYAEQVKG LLDGGADVLL VETIFDTANA KAALFAIDRL FEESYEARPV LISGTIVDKS GRTLSGQTGE AFVISVSHAQ PLCIGLNCAL GASEMRPFIE AIGKSTSAFV ICYPNAGLPN TFGGYDETPD VTAAHLKEFA VDGLVNIVGG CCGTTPDHIR AIAESVRHVK PRVPPTDVYS DYMLLSGLEP FRIGPYTNFV NIGERCNVAG SRKFAKLIMA GNYEEALSIA KAQVEMGAQV LDINMDEGML DGAAAMSRFC NLIASEPDIC KVPLCIDSSN FSVIEAGLKC CQGKCIVNSI SLKEGEQDFL RRARQVRRYG AAVVVMAFDE DGQATETDQK VQICSRAYHL LIDQAGFNPN DIIFDPNILT IGTGMEEHSM YAINFIRATR IIKESLPGAR VSGGLSNLSF SFRGMEAIRE AMHGAFLYHA IKDGMDMGIV NAGNLPVYDD IDKELLLLCE NIIWNRDPDA TEKLLLYAQN NAKGGKKVVQ TDEWRTGSVE ERLEYALVKG IEKYVVEDTE EARAQTERYP RPLHVIEGPL MNGMKTVGDL FGAGKMFLPQ VIKSARVMKK AVGHLIPFME KEREEMMATS GCVEEVDPYQ GTVLLATVKG DVHDIGKNIV GVVLGCNNFR VIDLGVMIPC DRILREAIHN KADIIGLSGL ITPSLDEMIH VAKEMERLGL KIPLLIGGAT TSKTHTAVKI APRYSSPVVH VLDASRSVVV CSQLLDEGVR DDYFEEVQEE YEDIRQDHYD SLKDRRFLSL SRAREKGLHI DWFAQPKPVR PQFLGTHVFD TYDLRKLVDF IDWKPFFDVW QLRGKYPNRG YPKIFKDKTV GEGARRVHDD ALKLLNRLID SRGLQARGIV GFWAAQSDGD DIHLYTDDVT SPNTTPVATS HGLRQQAEKD SASSEPYLCV SDFVAPRSSG VQDYVGLFAV SVFGAEELSQ KFKKQGDDYR SIMVKALADR LAEAFAEELH VRVRRDLWGY SSEEDLPASD LHKLRYEGIR PAAGYPSQPD HSEKLTMWKL ADIQEKTGIS LTESLAMSPA ASVSGLYFSN PKSTYFAVGK ITKEQVEDYA LRKQMEVCEV ERWLGPILGY DTD // ID Q8KBD1_CHLTE Unreviewed; 1228 AA. AC Q8KBD1; DT 01-OCT-2002, integrated into UniProtKB/TrEMBL. DT 01-OCT-2002, sequence version 1. DT 27-MAY-2015, entry version 88. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AAM73077.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AAM73077.1}; GN Name=metH {ECO:0000313|EMBL:AAM73077.1}; GN OrderedLocusNames=CT1857 {ECO:0000313|EMBL:AAM73077.1}; OS Chlorobium tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / OS TLS). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobaculum. OX NCBI_TaxID=194439 {ECO:0000313|EMBL:AAM73077.1, ECO:0000313|Proteomes:UP000001007}; RN [1] {ECO:0000313|EMBL:AAM73077.1, ECO:0000313|Proteomes:UP000001007} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49652 / DSM 12025 / TLS RC {ECO:0000313|Proteomes:UP000001007}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AE006470; AAM73077.1; -; Genomic_DNA. DR RefSeq; NP_662735.1; NC_002932.3. DR RefSeq; WP_010933516.1; NC_002932.3. DR ProteinModelPortal; Q8KBD1; -. DR SMR; Q8KBD1; 648-895. DR STRING; 194439.CT1857; -. DR EnsemblBacteria; AAM73077; AAM73077; CT1857. DR GeneID; 1007840; -. DR KEGG; cte:CT1857; -. DR PATRIC; 21401565; VBIChlTep116050_1686. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CTEP194439:GHN0-1897-MONOMER; -. DR Proteomes; UP000001007; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001007}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AAM73077.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001007}; KW Transferase {ECO:0000313|EMBL:AAM73077.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1228 AA; 134894 MW; F24D1BBEE88B9560 CRC64; MNDNLYSLIE QRILVLDGAM GTMIQRHGLD EQDYRGERFA SHDHPLKGNN DLLVITRPDI IRSIHCDFLD AGADIIETCT FNANPISQSD YQLQDLTREL NVAAAKIARS AADEFTAKTP DKPRFVAGSI GPTNKTLSLS PDVNNPGFRA VTFQEMVDNY TAQLEGLHEG GVDLLLVETV FDTLNCKAAL YAIEEYAVKT GWQVPVMVSG TVVDASGRTL SGQTTEAFWI SISHMPSLLS VGLNCALGSK QMRPFIEALS NIAESYVSVY PNAGLPNEFG EYDDSPEYMA AQIAGFAESG FVNIVGGCCG TTPTHIRAIA EAVKTLPPRK RPANKHVLRL SGLEPLVVDE TTGFINVGER TNVTGSRKFA RLIKEANYDE ALSIARQQVE NGAQVIDVNL DEGMLDSEKV IVEFLNLIAS EPEIAKVPVM IDSSKWSVIE NGLRCTQGKS IVNSISLKEG EELFKERARK IMQYGAAAVV MAFDEQGQAD SLHRRIEICS RAYKILTEEV GFPPEDIIFD PNVLTVATGI DEHNNYALDF IESVRWIKQN LPHAKVSGGI SNVSFSFRGN EPVREAMHTA FLYHAIHAGL DMGIVNAAQL GIYEEIDPEL LVYVEDVLLN RRDDATERLV AFAETIRDGG EKAEAKNAEW RNAPVEERLK HALVKGIVDY IDEDTEEARQ LYPSPLEVIE GPLMNGMNHV GDLFAEGKMF LPQVVKSARV MKRSVAALIP YIEEEKSKNC DTSAKAKVLL ATVKGDVHDI GKNIVSVVLA CNNFDVIDIG VMMPCDKILE ALAEHKPDVL GLSGLITPSL EEMAHVAKEM ERLGMNIPLI IGGATTSKVH TAVKLAPCYP SGAVVHVLDA SRSVPVVSNL CNPAQRDSYI AALKDEQEAM RKSHAERMAA KKYVSLDAAR DNRLTIDWEA ETIDKPAQTG VTVLEDVTVG ALRPYIDWAP FFWSWELHGV YPQILEDEKV GEEATKLFND ATALLDRIDS EKLLGIKGVA GIFPANSIGD DIFVYADDER SIIRTVLHTL RQQGEKHGEA NLALADFVAP RESGVNDWIG CFTVTAGLGI QNLLDEFTAE NDDYHRIMTQ ALADRLAEAF AEMLHEKVRR ELWGYAPGEI LGNEELIAEK YRGIRPAPGY PACPDHTEKA IIFDLLNAEA ATGVTLTETF AMNPAASVCG LYFANPASKY FVLGKIGKDQ VEDYANRKGL EVAEAEKWLA PSLNYDPA // ID Q8KNI2_MICEC Unreviewed; 304 AA. AC Q8KNI2; DT 01-OCT-2002, integrated into UniProtKB/TrEMBL. DT 01-OCT-2002, sequence version 1. DT 01-OCT-2014, entry version 28. DE SubName: Full=CalE2 {ECO:0000313|EMBL:AAM94773.1}; GN Name=calE2 {ECO:0000313|EMBL:AAM94773.1}; OS Micromonospora echinospora (Micromonospora purpurea). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micromonosporineae; Micromonosporaceae; Micromonospora. OX NCBI_TaxID=1877 {ECO:0000313|EMBL:AAM94773.1}; RN [1] {ECO:0000313|EMBL:AAM94773.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NRRL 15839 {ECO:0000313|EMBL:AAM94773.1}; RX PubMed=12183629; DOI=10.1126/science.1072105; RA Ahlert J., Shepard E., Lomovskaya N., Zazopoulos E., Staffa A., RA Bachmann B.O., Huang K., Fonstein L., Czisny A., Whitwam R.E., RA Farnet C.M., Thorson J.S.; RT "The calicheamicin gene cluster and its iterative type I enediyne RT PKS."; RL Science 297:1173-1176(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; AF497482; AAM94773.1; -; Genomic_DNA. DR ProteinModelPortal; Q8KNI2; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; SQ SEQUENCE 304 AA; 31491 MW; B0D75081BDAFC45F CRC64; MDVPGAPTAG PLVLDGGLGT ELQRHGRSVS APWWTARCLL DAGGRRLVSR VHAAYVAAGA DVLTADTFRT TLRTAYRAGT DEATAAGLVR TAVTLARRAA DSTGAGRRVL VAASVAPVED CYRPDLVPGA AVLRREHGWL ADQLARAGVD LALVETMNTV REAVVATRAV REHGLPAWVS FVCTGDARLL SGEDLAAAAD AVRAAGAAAV LVNCTDPAGT ERALRRLRAA GPGLLGAYPN VEDRSGVPPA TPVDRYLPPG LTPDAFADLW AAWRPVGLRI VGGCCGTTPA HIAALRSRLA PRPG // ID Q8MIJ9_BOVIN Unreviewed; 133 AA. AC Q8MIJ9; DT 01-OCT-2002, integrated into UniProtKB/TrEMBL. DT 01-OCT-2002, sequence version 1. DT 29-OCT-2014, entry version 50. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AAM96905.1}; DE Flags: Fragment; GN Name=ms {ECO:0000313|EMBL:AAM96905.1}; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913 {ECO:0000313|EMBL:AAM96905.1}; RN [1] {ECO:0000313|EMBL:AAM96905.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Liver {ECO:0000313|EMBL:AAM96905.1}; RX PubMed=17582128; RA Graulet B., Matte J.J., Desrochers A., Doepel L., Palin M.F., RA Girard C.L.; RT "Effects of dietary supplements of folic acid and vitamin B12 on RT metabolism of dairy cows in early lactation."; RL J. Dairy Sci. 90:3442-3455(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; AY128710; AAM96905.1; -; mRNA. DR UniGene; Bt.47673; -. DR ProteinModelPortal; Q8MIJ9; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; FT NON_TER 1 1 {ECO:0000313|EMBL:AAM96905.1}. FT NON_TER 133 133 {ECO:0000313|EMBL:AAM96905.1}. SQ SEQUENCE 133 AA; 14628 MW; A74105B70D058581 CRC64; ERIMVLDGGM GTMIQRHKLS EEDFRGQEFK DHARPLKGNN DILSITQPNV IYQIHKEYLL AGADIIETNT FSSTSIAQAD YGLEHLAYRM NMCSAGVARK AAEDISLQTG IKRYVAGALG PTNKTLSVSP SVE // ID Q8MQN1_DROME Unreviewed; 326 AA. AC Q8MQN1; DT 01-OCT-2002, integrated into UniProtKB/TrEMBL. DT 01-OCT-2002, sequence version 1. DT 04-FEB-2015, entry version 51. DE SubName: Full=RE64786p {ECO:0000313|EMBL:AAM75078.1}; GN ORFNames=CG10621 {ECO:0000313|EMBL:AAM75078.1, GN ECO:0000313|FlyBase:FBgn0032726}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227; RN [1] {ECO:0000313|EMBL:AAM75078.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Berkeley {ECO:0000313|EMBL:AAM75078.1}; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R., Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.; RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY128485; AAM75078.1; -; mRNA. DR ProteinModelPortal; Q8MQN1; -. DR SMR; Q8MQN1; 3-316. DR STRING; 7227.FBpp0080732; -. DR PaxDb; Q8MQN1; -. DR PRIDE; Q8MQN1; -. DR FlyBase; FBgn0032726; CG10621. DR eggNOG; COG2040; -. DR OrthoDB; EOG7GQXW0; -. DR ChiTaRS; CG10621; fly. DR Bgee; Q8MQN1; -. DR ExpressionAtlas; Q8MQN1; differential. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IBA:GO_Central. DR GO; GO:0032259; P:methylation; IBA:GOC. DR GO; GO:0033528; P:S-methylmethionine cycle; IBA:GO_Central. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; SQ SEQUENCE 326 AA; 35909 MW; 5EBE04AC6B1F4686 CRC64; MGLTRVLVKD GGFGTQMTVH VGDSVDGDPL WSARFNATNP AAIISTHLDF LQNGADIILT NTYQSSVDGY MEYLELDEEQ SIELIKNTVR LAHIAKERYL TECYQAQLSV QEGYPLIIAS IGPFGAHLHD GSEYTGSYAD FVPAKEITDW HRVRIEACLE AGVDALAIET IPCQMEAEAL VEMLCDDYPD VKFWVAFQCK DENTLAHGET FADAANAIWD LLAERNAQDK CLAIGVNCVH PKFVTPLFKS LNGDREVGEQ IPLVVYPNSG EVYDVVNGWQ GREHCVPLAN YVPEWGNWGP RSLGDAVALM RGIYATSGRP FATGTN // ID Q8NQD1_CORGL Unreviewed; 1221 AA. AC Q8NQD1; DT 01-OCT-2002, integrated into UniProtKB/TrEMBL. DT 01-OCT-2002, sequence version 1. DT 27-MAY-2015, entry version 96. DE SubName: Full=Methionine synthase I, cobalamin-binding domain {ECO:0000313|EMBL:BAB98900.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:BAB98900.1}; GN OrderedLocusNames=Cgl1507 {ECO:0000313|EMBL:BAB98900.1}; 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 {ECO:0000313|Proteomes:UP000000582}; RN [1] {ECO:0000313|Proteomes:UP000000582} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 RC {ECO:0000313|Proteomes:UP000000582}; 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). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; BA000036; BAB98900.1; -; Genomic_DNA. DR RefSeq; NP_600723.1; NC_003450.3. DR RefSeq; WP_011014411.1; NC_003450.3. DR ProteinModelPortal; Q8NQD1; -. DR EnsemblBacteria; BAB98900; BAB98900; BAB98900. DR GeneID; 1019480; -. DR GeneID; 23501708; -. DR KEGG; cgl:NCgl1450; -. DR PATRIC; 21495057; VBICorGlu203724_1474. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR BioCyc; CGLU1204414-WGS:GSME-1449-MONOMER; -. DR Proteomes; UP000000582; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000582}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAB98900.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000582}; KW Transferase {ECO:0000313|EMBL:BAB98900.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 239 239 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 306 306 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 772 772 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1221 AA; 133407 MW; C2DF7B1F82341C45 CRC64; MSTSVTSPAH NNAHSSEFLD ALANHVLIGD GAMGTQLQGF DLDVEKDFLD LEGCNEILND TRPDVLRQIH RAYFEAGADL VETNTFGCNL PNLADYDIAD RCRELAYKGT AVAREVADEM GPGRNGMRRF VVGSLGPGTK LPSLGHAPYA DLRGHYKEAA LGIIDGGGDA FLIETAQDLL QVKAAVHGVQ DAMAELDTFL PIICHVTVET TGTMLMGSEI GAALTALQPL GIDMIGLNCA TGPDEMSEHL RYLSKHADIP VSVMPNAGLP VLGKNGAEYP LEAEDLAQAL AGFVSEYGLS MVGGCCGTTP EHIRAVRDAV VGVPEQETST LTKIPAGPVE QASREVEKED SVASLYTSVP LSQETGISMI GERTNSNGSK AFREAMLSGD WEKCVDIAKQ QTRDGAHMLD LCVDYVGRDG TADMATLAAL LATSSTLPIM IDSTEPEVIR TGLEHLGGRS IVNSVNFEDG DGPESRYQRI MKLVKQHGAA VVALTIDEEG QARTAEHKVR IAKRLIDDIT GSYGLDIKDI VVDCLTFPIS TGQEETRRDG IETIEAIREL KKLYPEIHTT LGLSNISFGL NPAARQVLNS VFLNECIEAG LDSAIAHSSK ILPMNRIDDR QREVALDMVY DRRTEDYDPL QEFMQLFEGV SAADAKDARA EQLAAMPLFE RLAQRIIDGD KNGLEDDLEA GMKEKSPIAI INEDLLNGMK TVGELFGSGQ MQLPFVLQSA ETMKTAVAYL EPFMEEEAEA TGSAQAEGKG KIVVATVKGD VHDIGKNLVD IILSNNGYDV VNLGIKQPLS AMLEAAEEHK ADVIGMSGLL VKSTVVMKEN LEEMNNAGAS NYPVILGGAA LTRTYVENDL NEVYTGEVYY ARDAFEGLRL MDEVMAEKRG EGLDPNSPEA IEQAKKKAER KARNERSRKI AAERKANAAP VIVPERSDVS TDTPTAAPPF WGTRIVKGLP LAEFLGNLDE RALFMGQWGL KSTRGNEGPS YEDLVETEGR PRLRYWLDRL KSEGILDHVA LVYGYFPAVA EGDDVVILES PDPHAAERMR FSFPRQQRGR FLCIADFIRP REQAVKDGQV DVMPFQLVTM GNPIADFANE LFAANEYREY LEVHGIGVQL TEALAEYWHS RVRSELKLND GGSVADFDPE DKTKFFDLDY RGARFSFGYG SCPDLEDRAK LVELLEPGRI GVELSEELQL HPEQSTDAFV LYHPEAKYFN V // ID Q8PAH1_XANCP Unreviewed; 379 AA. AC Q8PAH1; DT 01-OCT-2002, integrated into UniProtKB/TrEMBL. DT 01-OCT-2002, sequence version 1. DT 27-MAY-2015, entry version 68. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyl transferase {ECO:0000313|EMBL:AAM40808.1}; GN Name=metH1 {ECO:0000313|EMBL:AAM40808.1}; GN OrderedLocusNames=XCC1512 {ECO:0000313|EMBL:AAM40808.1}; 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 {ECO:0000313|EMBL:AAM40808.1, ECO:0000313|Proteomes:UP000001010}; RN [1] {ECO:0000313|EMBL:AAM40808.1, ECO:0000313|Proteomes:UP000001010} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33913 / NCPPB 528 / LMG 568 RC {ECO:0000313|Proteomes:UP000001010}; 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 ----------------------------------------------------------------------- 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; AAM40808.1; -; Genomic_DNA. DR RefSeq; NP_636884.1; NC_003902.1. DR RefSeq; WP_011036698.1; NC_003902.1. DR ProteinModelPortal; Q8PAH1; -. DR STRING; 190485.XCC1512; -. DR EnsemblBacteria; AAM40808; AAM40808; XCC1512. DR GeneID; 1001939; -. DR KEGG; xcc:XCC1512; -. DR PATRIC; 24073809; VBIXanCam115730_1620. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; XCAM190485:GIXZ-1510-MONOMER; -. DR Proteomes; UP000001010; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001010}; KW Reference proteome {ECO:0000313|Proteomes:UP000001010}; KW Transferase {ECO:0000313|EMBL:AAM40808.1}. SQ SEQUENCE 379 AA; 40447 MW; 991BF7BAA1179717 CRC64; MTHLPIPSAE SSIPFSLPWL HPERAAKLTA ALRERILIID GAMGTMIQRH DLQESDYRGT RFAEGYDSAQ GHVHGAGCDH APQGHDLKGN NDLLLLSSPE IIAGIHRAYL DAGADLLETN TFNATSVSQA DYHLEHLVYE LNKAGAQVAR ACCDAVEELT PQKPRFVIGV LGPTSRTASI SPDVNDPGYR NTSFDALRET YREAIDGLID GGADTLMVET IFDTLNAKAA LYAIEEVFEA RGGRLPVMIS GTITDASGRT LSGQTAEAFY ASVAHGKPLS VGLNCALGAK ELRPHVETLS QIADAYVSAH PNAGLPNAFG EYDETPAEMA ETLREFAKSG LLNLVGGCCG TTPDHIRAIA EAVADLPPRQ LPNALEQAA // ID Q8PAY2_XANCP Unreviewed; 347 AA. AC Q8PAY2; DT 01-OCT-2002, integrated into UniProtKB/TrEMBL. DT 01-OCT-2002, sequence version 1. DT 07-JAN-2015, entry version 56. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AAM40642.1}; GN Name=mmuM {ECO:0000313|EMBL:AAM40642.1}; GN OrderedLocusNames=XCC1344 {ECO:0000313|EMBL:AAM40642.1}; 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 {ECO:0000313|EMBL:AAM40642.1, ECO:0000313|Proteomes:UP000001010}; RN [1] {ECO:0000313|EMBL:AAM40642.1, ECO:0000313|Proteomes:UP000001010} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33913 / NCPPB 528 / LMG 568 RC {ECO:0000313|Proteomes:UP000001010}; 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 ----------------------------------------------------------------------- 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; AAM40642.1; -; Genomic_DNA. DR RefSeq; NP_636718.2; NC_003902.1. DR ProteinModelPortal; Q8PAY2; -. DR STRING; 190485.XCC1344; -. DR EnsemblBacteria; AAM40642; AAM40642; XCC1344. DR GeneID; 1001755; -. DR KEGG; xcc:XCC1344; -. DR PATRIC; 24073455; VBIXanCam115730_1444. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; XCAM190485:GIXZ-1342-MONOMER; -. DR Proteomes; UP000001010; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001010}; KW Methyltransferase {ECO:0000313|EMBL:AAM40642.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001010}; KW Transferase {ECO:0000313|EMBL:AAM40642.1}. SQ SEQUENCE 347 AA; 36640 MW; A76E097F0717C32F CRC64; MVRDSVRGAV LRRPCSDPKA CSPESASMTI VPRQPRVGAP FSDVLQRDAE VVLDGALATE LEQRGCDLND ALWSARVLME QPELIYQVHR DYFAAGAQCA ITASYQATPQ GFAARGLGLA QSQALIARSV ALAAQARADH LAAHPQAAPL WVAGSVGPYG AYLADGSEYR GDYALPVAQM LDFHRPRIAA LVDAGVDLLA CETLPSASEI TALRLLLEEF PQVHAWFSFT LRDAAHLSDG TPLAQVIPAL DACPQVVAVG INCIAIEQVT AALQSLAALT SLPLVVYPNS GEHYDASDKR WHAGTTVACS LATQRAQWHA AGARLIGGCC RTTPADIAAL VAARTAG // ID Q8PM72_XANAC Unreviewed; 363 AA. AC Q8PM72; DT 01-OCT-2002, integrated into UniProtKB/TrEMBL. DT 01-OCT-2002, sequence version 1. DT 27-MAY-2015, entry version 73. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyl transferase {ECO:0000313|EMBL:AAM36429.1}; GN Name=metH {ECO:0000313|EMBL:AAM36429.1}; GN OrderedLocusNames=XAC1560 {ECO:0000313|EMBL:AAM36429.1}; OS Xanthomonas axonopodis pv. citri (strain 306). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=190486 {ECO:0000313|EMBL:AAM36429.1, ECO:0000313|Proteomes:UP000000576}; RN [1] {ECO:0000313|EMBL:AAM36429.1, ECO:0000313|Proteomes:UP000000576} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=306 {ECO:0000313|EMBL:AAM36429.1, RC ECO:0000313|Proteomes:UP000000576}; 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 ----------------------------------------------------------------------- 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; AAM36429.1; -; Genomic_DNA. DR RefSeq; NP_641893.1; NC_003919.1. DR RefSeq; WP_011051004.1; NC_003919.1. DR ProteinModelPortal; Q8PM72; -. DR STRING; 190486.XAC1560; -. DR EnsemblBacteria; AAM36429; AAM36429; XAC1560. DR KEGG; xac:XAC1560; -. DR PATRIC; 24055119; VBIXanAxo33670_1639. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; XAXO190486:GH55-1560-MONOMER; -. DR Proteomes; UP000000576; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 2. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 2. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000576}; KW Transferase {ECO:0000313|EMBL:AAM36429.1}. SQ SEQUENCE 363 AA; 38818 MW; AD7B6BC84763AC6B CRC64; MPWLHPERAA KLTAALAERI LIIDGAMGTM IQRHDLQEPD YRGTRFADGY DSAHVHGPGC DHAHVPQGHD LKGNNDLLLL TRPEIIAGIH RAYLEAGADL LETNTFNATS VSQADYHLEH LVYELNKAGA QVARACCDDV EALTPHKPRF VIGVLGPTSR TASISPDVND PGYRNTSFDA LRATYREAIE GLIDGGADTL MVETIFDTLN AKAALYAIEE VFDARGGRLP VMVSGTITDA SGRTLSGQTA EAFYASVAHG RPLSIGLNCA LGARDLRPHV ETLAQIADTY VSAHPNAGLP NAFGEYDETP EEMAQTLREF AQAGLLNLVG GCCGTSPDHI RAIAEAVADL PPRQLPGAQE LAA // ID Q8PMN4_XANAC Unreviewed; 321 AA. AC Q8PMN4; DT 01-OCT-2002, integrated into UniProtKB/TrEMBL. DT 01-OCT-2002, sequence version 1. DT 27-MAY-2015, entry version 61. DE SubName: Full=Homocysteine S-methyltransferase {ECO:0000313|EMBL:AAM36263.1}; GN Name=mmuM {ECO:0000313|EMBL:AAM36263.1}; GN OrderedLocusNames=XAC1392 {ECO:0000313|EMBL:AAM36263.1}; OS Xanthomonas axonopodis pv. citri (strain 306). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=190486 {ECO:0000313|EMBL:AAM36263.1, ECO:0000313|Proteomes:UP000000576}; RN [1] {ECO:0000313|EMBL:AAM36263.1, ECO:0000313|Proteomes:UP000000576} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=306 {ECO:0000313|EMBL:AAM36263.1, RC ECO:0000313|Proteomes:UP000000576}; 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 ----------------------------------------------------------------------- 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; AAM36263.1; -; Genomic_DNA. DR RefSeq; NP_641727.1; NC_003919.1. DR RefSeq; WP_011050888.1; NC_003919.1. DR ProteinModelPortal; Q8PMN4; -. DR STRING; 190486.XAC1392; -. DR EnsemblBacteria; AAM36263; AAM36263; XAC1392. DR GeneID; 14852152; -. DR KEGG; xac:XAC1392; -. DR PATRIC; 24054781; VBIXanAxo33670_1471. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; ACETIPC; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; XAXO190486:GH55-1392-MONOMER; -. DR Proteomes; UP000000576; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000576}; KW Methyltransferase {ECO:0000313|EMBL:AAM36263.1}; KW Transferase {ECO:0000313|EMBL:AAM36263.1}. SQ SEQUENCE 321 AA; 34212 MW; 695495EC61083F9E CRC64; MTILPRQPRA NAPFSQALQH DGYVVLDGAL ATELEQRGCD LNDALWSARV LMEQPELIYQ VHRDYFAAGA QCAITASYQA TPLGFAARGL DVAQAQALIA RSVALAMQAR ADHLTLHPHA APLWVAGSVG PYGAYLADGS EYRGDYVLPI EQLMDFHRPR IAALAEAGVD LLACETLPSA SEIVALRQLL QHEFPQLHAW FSFTLRDAAH LSDGTPLAQV VPALDACAQV IAVGINCIAL DQATAALHSL SALTALPLVV YPNSGEHYDA SDKRWHAGRG AALTLADQHA HWLAAGARLI GGCCRTAPRD IAALAAARAA E // ID Q8R927_CALS4 Unreviewed; 803 AA. AC Q8R927; DT 01-JUN-2002, integrated into UniProtKB/TrEMBL. DT 01-JUN-2002, sequence version 1. DT 27-MAY-2015, entry version 81. DE SubName: Full=Methionine synthase I, cobalamin-binding domain protein {ECO:0000313|EMBL:AAM24995.1}; GN Name=MetH2 {ECO:0000313|EMBL:AAM24995.1}; GN OrderedLocusNames=TTE1803 {ECO:0000313|EMBL:AAM24995.1}; OS Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / OS JCM 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Caldanaerobacter. OX NCBI_TaxID=273068 {ECO:0000313|EMBL:AAM24995.1, ECO:0000313|Proteomes:UP000000555}; RN [1] {ECO:0000313|EMBL:AAM24995.1, ECO:0000313|Proteomes:UP000000555} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4 RC {ECO:0000313|Proteomes:UP000000555}; 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 ----------------------------------------------------------------------- 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; AAM24995.1; -; Genomic_DNA. DR RefSeq; NP_623391.1; NC_003869.1. DR RefSeq; WP_011025992.1; NC_003869.1. DR ProteinModelPortal; Q8R927; -. DR STRING; 273068.TTE1803; -. DR EnsemblBacteria; AAM24995; AAM24995; TTE1803. DR KEGG; tte:TTE1803; -. DR PATRIC; 23898355; VBITheTen82880_1815. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR Proteomes; UP000000555; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000555}; KW Reference proteome {ECO:0000313|Proteomes:UP000000555}. SQ SEQUENCE 803 AA; 87512 MW; E7C1B2F93CE6D93F CRC64; MVDIFKECEN RVVVFDGAMG TQLQERGLKA GECPEYINLK MPEVVFDIHK AYIEAGAEVI ETNTFGANRI KLAKYGLEDK VEEIVTKGVE IARKAAGDRP VALSVGPTGE LLAPFGDMTF DEAYEVFKEV VVAAEKAGAD IVIIETMSDM LEAKAAILAA KENTNMKVIC TMTFQEDGRT LMGSDPVTVV VSLQGLGLDA IGVNCSTGPD KMVKVVEKMA QVARIPIIAQ PNAGMPVIRD GKTVYDLKPE EFASFFPQLV EKGACIVGGC CGTTPYYIKL VKKAVENLKP KKLENKFTAL SSNTRTVFIG KEYPLRVIGE RINPTGKKKL SGALLSGDVN LAVEEALKQQ KCGAEILDVN VGVPGIEEEE MLPKVAFEVE KAVDLPLQLD STNVKAIEKA IRILRGRPII NSVNAKEESL KEVLPIVKKY GACVVGLTVG DKGLPKDRHE RVENARKILK KAEEYGIPKE DVIIDPVVLT VSSEQGAAIE TLEAMKIISE ELGVNTVVGL SNISFGLPER KLINSTFLAM AASHGLTAAI VNPCDESLMD TLRASMVLLN KDKGSENYLK VYGQRVKPKE EVIKRHEEDF SKKLYDQILE GKKSGVEEIV MALLEDNPPL SLVDEIIIPA LKEVGDRYEK GIYFLPQLLS SAEVVQSAFK LIKEKLPKGT ASKGKIILAT VEGDVHDIGK NIVKVLLENY GYEVIDLGKD VKGEVIVEEV KKTGAPLVGL SALMTTTLFN MEKIIKMLKE NTEAKVMVGG AVLTEEYAFK IGADYYGKTA QDAVKIADKF FLKNALVCKT CSF // ID Q8RGW4_FUSNN Unreviewed; 309 AA. AC Q8RGW4; DT 01-JUN-2002, integrated into UniProtKB/TrEMBL. DT 01-JUN-2002, sequence version 1. DT 27-MAY-2015, entry version 63. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AAL94369.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AAL94369.1}; GN OrderedLocusNames=FN0163 {ECO:0000313|EMBL:AAL94369.1}; 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 {ECO:0000313|EMBL:AAL94369.1, ECO:0000313|Proteomes:UP000002521}; RN [1] {ECO:0000313|EMBL:AAL94369.1, ECO:0000313|Proteomes:UP000002521} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131 RC {ECO:0000313|Proteomes:UP000002521}; 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; AAL94369.1; -; Genomic_DNA. DR RefSeq; NP_603070.1; NC_003454.1. DR RefSeq; WP_011016194.1; NC_003454.1. DR ProteinModelPortal; Q8RGW4; -. DR STRING; 190304.FN0163; -. DR EnsemblBacteria; AAL94369; AAL94369; FN0163. DR GeneID; 993060; -. DR KEGG; fnu:FN0163; -. DR PATRIC; 21950101; VBIFusNuc122357_0743. DR HOGENOM; HOG000265279; -. DR InParanoid; Q8RGW4; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6091CH; -. DR Proteomes; UP000002521; Chromosome. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002521}; KW Methyltransferase {ECO:0000313|EMBL:AAL94369.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002521}; KW Transferase {ECO:0000313|EMBL:AAL94369.1}. SQ SEQUENCE 309 AA; 34007 MW; 1BD43B1F2C9C2FA0 CRC64; MEERILVLDG AMGTVLQKYE LTLEDFNGAK GCYEILNETR PDIIFEVHKK YIEAGADIIE TNSFNCNAIS LKDYHLEDKV YDLAKKSAEI ARDAVKKSGK KVYVFGSVGP TNKGLSFSVG DVPFKRAVSF DEMKEVIKVQ VAGLIDGGVD GILLETVFDG LTAKVALLAI EEVFEEKNIK LPVSISATVN KQGKLSTGQS IESLMVDLDR DFVISFGFNC SFGAKNLVPL VIKIKELTTK FVSLHANAGL PNQNGEYEET AQKMRDDLLP LIENQAINIL GGCCGTDYEH IKLIAELVKG QKPRILPKR // ID Q8RK20_PSEPU Unreviewed; 392 AA. AC Q8RK20; DT 01-JUN-2002, integrated into UniProtKB/TrEMBL. DT 01-JUN-2002, sequence version 1. DT 27-MAY-2015, entry version 48. DE SubName: Full=Putative methionine synthase {ECO:0000313|EMBL:CAD29687.1}; DE Flags: Fragment; GN Name=metH {ECO:0000313|EMBL:CAD29687.1}; OS Pseudomonas putida (Arthrobacter siderocapsulatus). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=303 {ECO:0000313|EMBL:CAD29687.1}; RN [1] {ECO:0000313|EMBL:CAD29687.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=RH416 {ECO:0000313|EMBL:CAD29687.1}; RA von Wallbrunn A., Richnow H.H., Neumann G., Meinhardt F., RA Heipieper H.J.; RT "Studies on the enzymatic mechanism and genetic diversity of the cis- RT trans isomerase of unsaturated fatty acids in Pseudomonas strains."; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ441308; CAD29687.1; -; Genomic_DNA. DR ProteinModelPortal; Q8RK20; -. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; FT NON_TER 392 392 {ECO:0000313|EMBL:CAD29687.1}. SQ SEQUENCE 392 AA; 42707 MW; 5C14AFEF80388AE0 CRC64; MSDRSARLQA LQHALKERIL ILDGGMGTMI QSYRLEEHYY RGTRFADWPS DVKGNNDLLL LSRPDVIAAI EKAYLDAGAD ILETNAFNAT QISQADYAME SLVYELNVEG ARIARQVADA KTLETPDKPR FVAGVLGPTS RTCSISPDVN DPSYRNVTFD ELVENYVEAT RGLIEGGADL ILIETIFDTL NAKAAIFAVQ QVFEDDQVEL PIMISGTITD ASGRTLSGQT TEAFWNSVRH AKPISVGLNC ALGAKDLRPY LEELSTKADT HVSAHPNAGL PNAFGEYDET PAEMAAVVEE FAASGFLNII GGCCGTTPGH IQAIAEAVAK YKPREIPEIA KACRLSGLEP FTIDRQSLFV NVGERTNITG SAKFARLIRE ENYTEALEVA LQ // ID Q8VJP7_MYCTO Unreviewed; 814 AA. AC Q8VJP7; DT 01-MAR-2002, integrated into UniProtKB/TrEMBL. DT 01-MAR-2002, sequence version 1. DT 29-APR-2015, entry version 91. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|EMBL:AAK46467.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AAK46467.1}; GN Name=metH {ECO:0000313|EMBL:AAK46467.1}; GN OrderedLocusNames=MT2183 {ECO:0000313|EMBL:AAK46467.1}; OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=83331 {ECO:0000313|EMBL:AAK46467.1, ECO:0000313|Proteomes:UP000001020}; RN [1] {ECO:0000313|EMBL:AAK46467.1, ECO:0000313|Proteomes:UP000001020} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CDC 1551 / Oshkosh {ECO:0000313|Proteomes:UP000001020}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AE000516; AAK46467.1; -; Genomic_DNA. DR RefSeq; NP_336653.1; NC_002755.2. DR RefSeq; WP_010924493.1; NC_002755.2. DR ProteinModelPortal; Q8VJP7; -. DR SMR; Q8VJP7; 4-598, 615-814. DR STRING; 83331.MT2183; -. DR PRIDE; Q8VJP7; -. DR EnsemblBacteria; AAK46467; AAK46467; MT2183. DR KEGG; mtc:MT2183; -. DR PATRIC; 18126556; VBIMycTub22151_2391. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OrthoDB; EOG6091CH; -. DR Proteomes; UP000001020; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001020}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AAK46467.1}; KW Transferase {ECO:0000313|EMBL:AAK46467.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 210 210 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 276 276 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 277 277 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 721 721 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 814 AA; 86939 MW; 269DA22D32DA2A00 CRC64; MVGDGAMGTQ LQAADLTLDD FRGLEGCNEI LNETRPDVLE TIHRNYFEAG ADAVETNTFG CNLSNLGDYD IADRIRDLSQ KGTAIARRVA DELGSPDRKR YVLGSMGPGT KLPTLGHTEY AVIRDAYTEA ALGMLDGGAD AILVETCQDL LQLKAAVLGS RRAMTRAGRH IPVFAHVTVE TTGTMLLGSE IGAALTAVEP LGVDMIGLNC ATGPAEMSEH LRHLSRHARI PVSVMPNAGL PVLGAKGAEY PLLPDELAEA LAGFIAEFGL SLVGGCCGTT PAHIREVAAA VANIKRPERQ VSYEPSVSSL YTAIPFAQDA SVLVIGERTN ANGSKGFREA MIAEDYQKCL DIAKDQTRDG AHLLDLCVDY VGRDGVADMK ALASRLATSS TLPIMLDSTE TAVLQAGLEH LGGRCAINSV NYEDGDGPES RFAKTMALVA EHGAAVVALT IDEEGQARTA QKKVEIAERL INDITGNWGV DESSILIDTL TFTIATGQEE SRRDGIETIE AIRELKKRHP DVQTTLGLSN ISFGLNPAAR QVLNSVFLHE CQEAGLDSAI VHASKILPMN RIPEEQRNVA LDLVYDRRRE DYDPLQELMR LFEGVSAASS KEDRLAELAG LPLFERLAQR IVDGERNGLD ADLDEAMTQK PPLQIINEHL LAGMKTVGEL FGSGQMQLPF VLQSAEVMKA AVAYLEPHME RSDDDSGKGR IVLATVKGDV HDIGKNLVDI ILSNNGYEVV NIGIKQPIAT ILEVAEDKSA DVVGMSGLLV KSTANSASVG MPPNADVYPA AAVSCAAAAA VATVAAWVSQ YRNG // ID Q8X5Z8_ECO57 Unreviewed; 1227 AA. AC Q8X5Z8; Q7A950; DT 01-MAR-2002, integrated into UniProtKB/TrEMBL. DT 01-MAR-2002, sequence version 1. DT 27-MAY-2015, entry version 108. DE SubName: Full=B12-dependent homocysteine-N5-methyltetrahydrofolate transmethylase, repressor of metE and metF {ECO:0000313|EMBL:AAG59211.1}; GN Name=metH {ECO:0000313|EMBL:AAG59211.1}; GN OrderedLocusNames=Z5610 {ECO:0000313|EMBL:AAG59211.1}; OS Escherichia coli O157:H7. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83334 {ECO:0000313|Proteomes:UP000002519}; RN [1] {ECO:0000313|EMBL:AAG59211.1, ECO:0000313|Proteomes:UP000002519} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC RC {ECO:0000313|Proteomes:UP000002519}; 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). CC ----------------------------------------------------------------------- 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; AAG59211.1; -; Genomic_DNA. DR PIR; A98246; A98246. DR PIR; G86093; G86093. DR RefSeq; NP_312964.1; NC_002695.1. DR ProteinModelPortal; Q8X5Z8; -. DR SMR; Q8X5Z8; 651-1227. DR STRING; 155864.Z5610; -. DR EnsemblBacteria; AAG59211; AAG59211; Z5610. DR EnsemblBacteria; BAB38360; BAB38360; BAB38360. DR GeneID; 914852; -. DR KEGG; ece:Z5610; -. DR KEGG; ecs:ECs4937; -. DR PATRIC; 18359579; VBIEscCol44059_4926. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; ECOL386585:GJFA-4941-MONOMER; -. DR BioCyc; ECOO157:METH-MONOMER; -. DR Proteomes; UP000002519; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002519}; KW Methyltransferase {ECO:0000313|EMBL:AAG59211.1}; KW Transferase {ECO:0000313|EMBL:AAG59211.1}. SQ SEQUENCE 1227 AA; 136040 MW; 8FB5738E12303E7E CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV EDYARRKGMS VSDVERWLAP NLGYDAD // ID Q8XKH8_CLOPE Unreviewed; 279 AA. AC Q8XKH8; DT 01-MAR-2002, integrated into UniProtKB/TrEMBL. DT 01-MAR-2002, sequence version 1. DT 29-APR-2015, entry version 66. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:BAB81123.1}; GN OrderedLocusNames=CPE1417 {ECO:0000313|EMBL:BAB81123.1}; OS Clostridium perfringens (strain 13 / Type A). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=195102 {ECO:0000313|EMBL:BAB81123.1, ECO:0000313|Proteomes:UP000000818}; RN [1] {ECO:0000313|EMBL:BAB81123.1, ECO:0000313|Proteomes:UP000000818} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=13 / Type A {ECO:0000313|Proteomes:UP000000818}; 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; BAB81123.1; -; Genomic_DNA. DR RefSeq; NP_562333.1; NC_003366.1. DR RefSeq; WP_011010437.1; NC_003366.1. DR ProteinModelPortal; Q8XKH8; -. DR STRING; 195102.CPE1417; -. DR EnsemblBacteria; BAB81123; BAB81123; BAB81123. DR GeneID; 989727; -. DR KEGG; cpe:CPE1417; -. DR PATRIC; 19496783; VBICloPer59675_1487. DR HOGENOM; HOG000265278; -. DR OMA; GTNLFAM; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CPER195102:GJFM-1463-MONOMER; -. DR Proteomes; UP000000818; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000818}; KW Reference proteome {ECO:0000313|Proteomes:UP000000818}. SQ SEQUENCE 279 AA; 31047 MW; 9A53C3A7BEEB9D9E CRC64; MKNLNLKNGV IIADGAMGTR IMELGVNLKE TPSELLNIKK PELIEKIHRE YIESGANLIL SNTFMCNIIN AKRNNYNLEE IIEAGISIAK KACGYHGLVA LDIGPLSYYI EENDSSFKEI VYENTERIIN ASKDKFDLVI FETLGSLKEG EFAVKKAKTL TDKKVICSFT LAYKKDIPNF IKNMVSTLEP LGVDALGINC TGYEEILMAL DILKENTNLP IMIKANLGIP KKVGEELVYD KTLEEFKNLS KRALEKGVNI IGGCCGTTPE YIRAICNLK // ID Q8Y2P0_RALSO Unreviewed; 346 AA. AC Q8Y2P0; DT 01-MAR-2002, integrated into UniProtKB/TrEMBL. DT 01-MAR-2002, sequence version 1. DT 27-MAY-2015, entry version 71. DE SubName: Full=MetHa protein {ECO:0000313|EMBL:CAD13823.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAD13823.1}; GN Name=metHa {ECO:0000313|EMBL:CAD13823.1}; GN OrderedLocusNames=RSc0295 {ECO:0000313|EMBL:CAD13823.1}; OS Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=267608 {ECO:0000313|EMBL:CAD13823.1, ECO:0000313|Proteomes:UP000001436}; RN [1] {ECO:0000313|EMBL:CAD13823.1, ECO:0000313|Proteomes:UP000001436} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GMI1000 {ECO:0000313|EMBL:CAD13823.1, RC ECO:0000313|Proteomes:UP000001436}; 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; CAD13823.1; -; Genomic_DNA. DR RefSeq; NP_518416.1; NC_003295.1. DR RefSeq; WP_011000260.1; NC_003295.1. DR ProteinModelPortal; Q8Y2P0; -. DR STRING; 267608.RSc0295; -. DR EnsemblBacteria; CAD13823; CAD13823; RSc0295. DR GeneID; 1219098; -. DR KEGG; rso:RSc0295; -. DR PATRIC; 20259133; VBIRalSol70888_0301. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; RSOL267608:GCVU-296-MONOMER; -. DR Proteomes; UP000001436; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001436}; KW Methyltransferase {ECO:0000313|EMBL:CAD13823.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001436}; KW Transferase {ECO:0000313|EMBL:CAD13823.1}. SQ SEQUENCE 346 AA; 37555 MW; 788C1CC148509A34 CRC64; MTAPLPYTRA ANLPALLRER ILILDGAMGT MIQRYKLTEA QYRGERFASH PVDVKGNNEL LLLTRPEVIR EIHEQYLAAG ADLIETNTFG ATTVAQEDYK MAELAYEMNV VAARLAREAC DKYSTPDKPR FVAGAFGPTP KTASISPDVN DPGARNISFD QLRDAYYEQG KALLEGGADV FLVETIFDTL NAKAALFAID QLFEDSGERV PVMISGTVTD ASGRILSGQT VEAFWNSLRH AKPITFGLNC ALGAALMRPY IAELAKICDT AVSCYPNAGL PNPMSDTGFD ETPEVTSSLV DEFAAAGLVN LVGGCCGTTP EHIRAIAERV AQRKPRAWPG QYREAA // ID Q8Y6K6_LISMO Unreviewed; 617 AA. AC Q8Y6K6; DT 01-MAR-2002, integrated into UniProtKB/TrEMBL. DT 01-MAR-2002, sequence version 1. DT 27-MAY-2015, entry version 80. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=lmo1678 {ECO:0000313|EMBL:CAC99756.1}; OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e). OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=169963 {ECO:0000313|EMBL:CAC99756.1, ECO:0000313|Proteomes:UP000000817}; RN [1] {ECO:0000313|EMBL:CAC99756.1, ECO:0000313|Proteomes:UP000000817} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-679 / EGD-e {ECO:0000313|Proteomes:UP000000817}; 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., Portillo F.G., Garrido P., Gautier L., RA Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.M., RA Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., RA Maitournam A., Vicente J.M., Ng E., Nedjari H., Nordsiek G., RA Novella S., de Pablos B., Perez-Diaz J.C., Purcell R., Remmel B., RA Rose M., Schlueter T., Simoes N., Tierrez A., Vazquez-Boland J.A., RA Voss H., Wehland J., Cossart P.; RT "Comparative genomics of Listeria species."; RL Science 294:849-852(2001). CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL591980; CAC99756.1; -; Genomic_DNA. DR PIR; AF1284; AF1284. DR RefSeq; NP_465203.1; NC_003210.1. DR RefSeq; WP_003726093.1; NC_003210.1. DR ProteinModelPortal; Q8Y6K6; -. DR STRING; 169963.lmo1678; -. DR DNASU; 985643; -. DR EnsemblBacteria; CAC99756; CAC99756; CAC99756. DR GeneID; 985643; -. DR KEGG; lmo:lmo1678; -. DR PATRIC; 20312489; VBILisMon69206_1721. DR GenoList; LMO1678; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR PhylomeDB; Q8Y6K6; -. DR BioCyc; LMON169963:LMO1678-MONOMER; -. DR Proteomes; UP000000817; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000817}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000000817}. SQ SEQUENCE 617 AA; 68620 MW; B5D255AAB7E947EA CRC64; MNLRKDLSEK VLIADGAMGT LLYSYGVDRS FEELNLSHPE DIVAIHKAYI GAGADIIQTN TYGANYIKLA RYGLEDEVKR INQAAIRLAK EAARGTGTYI FGTIGGINGA VDARLPAAPL EEIKRSFREQ LYCFLLDGVD AILLETYYDL DELKTVLKIL RETTDLPVVA NVSMHEPGIL QNGKKLPDAL EELIALGADV VGINCRLGPY HMARALETVP LYDNAYLAVY PNASLPEMQE GKVIYQSDTD YFEHYGEVFR QEGARIIGGC CGTTPDHIRA LRKGLETTKP ILEKEVRPIL ELVPEEVEDV DSGERLLDKV KERLTILVEL DPPRTFDTTK FFEGAQALDE AGVDAITISD NSLATPRISN MALASILKHE YGIKPLIHLT TRDHNLVGMH SHVMGFHKLG LHDVLAITGD PTKVGDFPGA SSVFDLRSVE LVQLIKKFND GISYTGKSLK EKARFHVGAA FNPNVLNLEK AVRLIERKVE YGADYIITQP IYDVNKAILL KEALQKANID VPLFIGVMPL LSSRNAEFLH NEVPGIRLTD DVRERMREAE EHGHANEEGM AIARELVDAI CEHFQGIYII TPFLRYDLSI ELAKYAQNKQ QVQIGSK // ID Q8YEW8_BRUME Unreviewed; 1261 AA. AC Q8YEW8; DT 01-MAR-2002, integrated into UniProtKB/TrEMBL. DT 01-MAR-2002, sequence version 1. DT 29-APR-2015, entry version 98. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AAL52940.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AAL52940.1}; GN OrderedLocusNames=BMEI1759 {ECO:0000313|EMBL:AAL52940.1}; OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=224914 {ECO:0000313|EMBL:AAL52940.1, ECO:0000313|Proteomes:UP000000419}; RN [1] {ECO:0000313|EMBL:AAL52940.1, ECO:0000313|Proteomes:UP000000419} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=16M / ATCC 23456 / NCTC 10094 RC {ECO:0000313|Proteomes:UP000000419}; 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.C., 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). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AE008917; AAL52940.1; -; Genomic_DNA. DR PIR; AI3471; AI3471. DR RefSeq; NP_540676.1; NC_003317.1. DR RefSeq; WP_011005393.1; NC_003317.1. DR ProteinModelPortal; Q8YEW8; -. DR SMR; Q8YEW8; 673-921. DR STRING; 224914.BMEI1759; -. DR EnsemblBacteria; AAL52940; AAL52940; BMEI1759. DR KEGG; bme:BMEI1759; -. DR PATRIC; 17853924; VBIBruMel92729_1947. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; BMEL224914:GCJ0-1805-MONOMER; -. DR PRO; PR:Q8YEW8; -. DR Proteomes; UP000000419; Chromosome I. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000419}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AAL52940.1}; KW Transferase {ECO:0000313|EMBL:AAL52940.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 263 263 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 326 326 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 327 327 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 783 783 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1261 AA; 138668 MW; 816B9AE223736FD3 CRC64; MASSLDDLFG ATAAKPDGSE VLAALTQAAR ERILILDGAM GTQIQGLGFH EEHFRGDRFA TCDCQLQGNN DLLTLTQPKA IEEIHYAYAM AGADILETNT FSSTSIAQAD YGMEAMVYDL NRDGARLARR AALRAEQKDG RRRFVAGALG PTNRTASLSP DVNNPGFRAV TFDDVRIAYS EQIRGLIDGG SDIILIETIF DTLNAKAAVF ATEEVFAEKG VRLPVMISGT ITDLSGRTLS GQTPTAFWYS LRHARPFTIG LNCALGANAM RAHLDELSGI ADTFICAYPN AGLPNEFGQY DETPEAMAAQ IEGFARDGLV NVVGGCCGST PDHIRAIAQA VAKYEPRKPA KVPPLMRLSG LEPFTLTKDI PFVNIGERTN VTGSARFRKL VKAGDFAAAL DVARDQVANG AQIIDINMDE GLIDSEKAMV EFLNLIAAEP DIARVPIMLD SSKWEVIEAG LKCVQGKAVV NSISLKEGEE AFLHHARLVR AYGAAVVIMA FDETGQADTQ ARKIEICTRA YKILTEQVGF PPEDIIFDPN IFAVATGIEE HNNYGVDFIE ATREIVRTLP HVHISGGVSN LSFSFRGNEP VREAMHAVFL YHAIQAGMDM GIVNAGQLAV YDTIDAELRE ACEDVVLNRP TKTGESATER LLEIAERFRD SGSREARTQD LSWREWPVEK RLEHALVNGI TEYIEADTEE ARLAAERPLH VIEGPLMAGM NVVGDLFGSG KMFLPQVVKS ARVMKQAVAV LLPFMEEEKR LNGGEGRQSA GKVLMATVKG DVHDIGKNIV GVVLACNNYE IIDLGVMVPS QKILQVARDE KVDIIGLSGL ITPSLDEMAH VAAEMEREGF DIPLLIGGAT TSRVHTAVKI HSRYERGQAV YVVDASRAVG VVSNLLSPEG KQAYIDGLRN EYAKVAAAHA RNEAEKQRLP IARARANPHQ LDWENYEPVK PTFTGTKVFE TYDLAEIARY IDWTPFFQTW ELRGRYPAIL EDEKQGEAAR QLWADAQAML RKIIDEKWFT PRAVVGFWPA NAVGDDIRLF TDESRKEELA TLFTLRQQLT KRDGRPNVAM ADFVAPVESG KQDYVGGFVV TAGIGEIAIA ERFERANDDY SAILVKALAD RFAEAFAELM HERVRKEFWA YAPDEAFTPE ELISEPYKGI RPAPGYPAQP DHTEKTTLFR LLDATANTGV ELTESYAMWP GSSVSGLYIG HPESYYFGVA KVERDQVEDY ARRKDMDVEA VERWLTPILN YVPGASKDEA A // ID Q8YZZ6_NOSS1 Unreviewed; 1178 AA. AC Q8YZZ6; DT 01-MAR-2002, integrated into UniProtKB/TrEMBL. DT 01-MAR-2002, sequence version 1. DT 29-APR-2015, entry version 91. DE SubName: Full=5-methyltetrahydrofolate--homocysteine S-methyltransferase {ECO:0000313|EMBL:BAB72266.1}; GN OrderedLocusNames=alr0308 {ECO:0000313|EMBL:BAB72266.1}; OS Nostoc sp. (strain PCC 7120 / UTEX 2576). OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc. OX NCBI_TaxID=103690 {ECO:0000313|EMBL:BAB72266.1, ECO:0000313|Proteomes:UP000002483}; RN [1] {ECO:0000313|EMBL:BAB72266.1, ECO:0000313|Proteomes:UP000002483} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7120 / UTEX 2576 {ECO:0000313|Proteomes:UP000002483}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; BA000019; BAB72266.1; -; Genomic_DNA. DR PIR; AD1845; AD1845. DR RefSeq; NP_484352.1; NC_003272.1. DR RefSeq; WP_010994484.1; NC_003272.1. DR ProteinModelPortal; Q8YZZ6; -. DR STRING; 103690.alr0308; -. DR EnsemblBacteria; BAB72266; BAB72266; BAB72266. DR KEGG; ana:alr0308; -. DR PATRIC; 22770359; VBINosSp37423_0671. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR Proteomes; UP000002483; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002483}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAB72266.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002483}; KW Transferase {ECO:0000313|EMBL:BAB72266.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 228 228 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 294 294 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 295 295 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 737 737 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1178 AA; 130957 MW; CC193F86F6636BA5 CRC64; MTHPFLKRLH SPELPVIVFD GAMGTNLQTQ NLTAEDFGGV QYEGCNEYLV HTKPEAVAKV HRDFLAVGAD VIETDTFGAT SIVLAEYDLA DQTYYLNKKA AELAKSVAAE FSTPDKPRFV AGSIGPTTKL PTLGHIDFDT LKTCFAEQAE ALLDGGVDLL LVETCQDVLQ IKAALNGIEE VFGKRGERIP LMVSVTMESM GTMLVGSEIN AVLTILEPFP IDILGLNCAT GPDLMKPHIK YLAEHSPFVV SCIPNAGLPE NVGGQAHYRL TPMELRMALM HFVEDLGVQV IGGCCGTRPE HIQQLAEIAK DLKPKVRQPS LEPAAASIYS TQPYEQDNSF LIVGERLNAS GSKKCRDLLN AEDWDGLVSM ARSQVKEGAH ILDVNVDYVG RDGVRDMHEL VSRIVNNVTL PLMLDSTEWE KMEAGLKVAG GKCLLNSTNY EDGEPRFLKV LELAKKYGAG VVIGTIDEEG MARTAEKKFQ IAQRAYRQSV EYGIPPTEIF FDTLALPIST GIEEDRENGK ATIESISRIR KELPGCHVIL GVSNISFGLN SASRMVLNSV FLHEAMTAGM DAAIVSASKI LPLSKIEERH QEVCRQLIYD QRKFEGDICI YDPLTELTKL FEGVTTKRNK GVDESLPIEE RLKRHIIDGE RIGLEAQLTK ALEQYPPLEI INTFLLDGMK VVGELFGSGQ MQLPFVLQSA ETMKAAVAYL EPFMEKSESG NNAKGKVIIA TVKGDVHDIG KNLVDIILSN NGYKVINLGI KQPVENIIEA YNQHKADCIA MSGLLVKSTA FMKENLEVFN EKGINVPVIL GGAALTPKFV HKDCQNTYKG KVIYGKDAFS DLHFMDKLMP AKATGKWDNS LGFLDEVETE ETEPTNHKSP IPSPQSPVPS PQSPVPIDTR RSEAVAIDIP RPTPPFWGTQ LLQPSDISLE EIFWHMDLQA LIAGQWQFRK PKEQSKEEYQ AFLNEKVYPV LETWKQRIIA ENLLHPQVIY GYFPCQSEGN TLYVYETNSP NATEITQFEF PRQKSSKRLC IADFFAPKDS GIIDVFPMQA VTVGEIATEF AQKLFANNQY TDYLYFHGLA VQVAEALAEW THARIRRELG FGAEEPDNIR DILAQRYQGS RYSFGYPACP NIQDQFKQLD LLETSRINLY MDESEQLYPE QSTTAIITYH PVAKYFTA // ID Q8Z1V6_SALTI Unreviewed; 1227 AA. AC Q8Z1V6; Q7C5Q3; DT 01-MAR-2002, integrated into UniProtKB/TrEMBL. DT 01-MAR-2002, sequence version 1. DT 27-MAY-2015, entry version 101. DE SubName: Full=B12-dependent homocysteine-N5-methyltetrahydrofolate transmethylase {ECO:0000313|EMBL:CAD09193.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAD09193.1}; DE SubName: Full=MetH protein {ECO:0000313|EMBL:CEP54858.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CEP54858.1}; GN Name=metH {ECO:0000313|EMBL:CEP54858.1}; GN OrderedLocusNames=STY4405 {ECO:0000313|EMBL:CAD09193.1}; GN ORFNames=ERS163527_04280 {ECO:0000313|EMBL:CEV31166.1}, GN ERS163532_04133 {ECO:0000313|EMBL:CER03837.1}, GN ERS163535_04146 {ECO:0000313|EMBL:CET60944.1}, GN ERS163557_01860 {ECO:0000313|EMBL:CEU18636.1}, GN ERS163565_01807 {ECO:0000313|EMBL:CET45503.1}, GN ERS163587_02048 {ECO:0000313|EMBL:CEU00693.1}, GN ERS163590_02083 {ECO:0000313|EMBL:CER77976.1}, GN ERS207157_01750 {ECO:0000313|EMBL:CES58067.1}, GN ERS207180_01722 {ECO:0000313|EMBL:CER82150.1}, GN ERS223253_01529 {ECO:0000313|EMBL:CEQ52038.1}, GN ERS223257_01855 {ECO:0000313|EMBL:CEQ69349.1}, GN ERS223259_02213 {ECO:0000313|EMBL:CEQ87254.1}, GN ERS223263_01829 {ECO:0000313|EMBL:CEQ74463.1}, GN ERS223363_01677 {ECO:0000313|EMBL:CES67180.1}, GN ERS223402_01963 {ECO:0000313|EMBL:CET63996.1}, GN ERS223506_00880 {ECO:0000313|EMBL:CES73729.1}, GN ERS223509_01695 {ECO:0000313|EMBL:CES67453.1}, GN ERS223590_01905 {ECO:0000313|EMBL:CER92575.1}, GN ERS239527_04238 {ECO:0000313|EMBL:CEU44602.1}, GN ERS239550_01926 {ECO:0000313|EMBL:CES84503.1}, GN ERS239568_02121 {ECO:0000313|EMBL:CEU78556.1}, GN ERS239579_01885 {ECO:0000313|EMBL:CEU48213.1}, GN ERS239663_01684 {ECO:0000313|EMBL:CER96999.1}, GN ERS248915_01237 {ECO:0000313|EMBL:CER93589.1}, GN ERS248943_01715 {ECO:0000313|EMBL:CEU76198.1}, GN ERS248971_01707 {ECO:0000313|EMBL:CER12533.1}, GN ERS248991_01826 {ECO:0000313|EMBL:CEV30920.1}, GN ERS325052_04048 {ECO:0000313|EMBL:CEP54858.1}, GN ERS325134_02164 {ECO:0000313|EMBL:CES14252.1}, GN ERS325165_03934 {ECO:0000313|EMBL:CER61169.1}, GN ERS326214_01518 {ECO:0000313|EMBL:CET05054.1}, GN ERS326249_04020 {ECO:0000313|EMBL:CES14661.1}, GN ERS326384_04093 {ECO:0000313|EMBL:CES23804.1}, GN ERS326389_01720 {ECO:0000313|EMBL:CES18604.1}, GN ERS326407_03984 {ECO:0000313|EMBL:CER32403.1}, GN ERS326412_04070 {ECO:0000313|EMBL:CEU05827.1}, GN ERS326420_01520 {ECO:0000313|EMBL:CER50422.1}, GN ERS326422_01831 {ECO:0000313|EMBL:CEU05220.1}, GN ERS326491_03061 {ECO:0000313|EMBL:CEV03780.1}, GN ERS326513_02064 {ECO:0000313|EMBL:CEV16684.1}, GN ERS327363_01899 {ECO:0000313|EMBL:CEV18356.1}, GN ERS327392_04099 {ECO:0000313|EMBL:CER76083.1}, GN ERS330823_01658 {ECO:0000313|EMBL:CET20316.1}, GN ERS330826_01750 {ECO:0000313|EMBL:CEU52841.1}, GN ERS330884_02410 {ECO:0000313|EMBL:CET30039.1}, GN ERS330891_01263 {ECO:0000313|EMBL:CET09524.1}, GN ERS330892_04199 {ECO:0000313|EMBL:CET51765.1}, GN ERS330901_04065 {ECO:0000313|EMBL:CES41823.1}, GN ERS330902_04057 {ECO:0000313|EMBL:CEU25962.1}; OS Salmonella typhi. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=90370 {ECO:0000313|Proteomes:UP000000541}; RN [1] {ECO:0000313|EMBL:CAD09193.1, ECO:0000313|Proteomes:UP000000541} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CT18 {ECO:0000313|EMBL:CAD09193.1, RC ECO:0000313|Proteomes:UP000000541}; 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] {ECO:0000313|EMBL:CEP54858.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ERS325052 {ECO:0000313|EMBL:CEP54858.1}; RA Informatics Pathogen; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:CEQ52038.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=08-7714 {ECO:0000313|EMBL:CET30039.1}, RC 1007000 {ECO:0000313|EMBL:CEV18356.1}, RC 1022075 {ECO:0000313|EMBL:CER82150.1}, RC 1025691 {ECO:0000313|EMBL:CES58067.1}, RC 1650362 {ECO:0000313|EMBL:CES67180.1}, RC 3143/3 {ECO:0000313|EMBL:CER61169.1}, RC 3525/3 {ECO:0000313|EMBL:CES14252.1}, RC 62717 {ECO:0000313|EMBL:CER92575.1}, RC A122 {ECO:0000313|EMBL:CET63996.1}, RC A236 {ECO:0000313|EMBL:CEQ52038.1}, RC A240 {ECO:0000313|EMBL:CEQ69349.1}, RC A243 {ECO:0000313|EMBL:CEQ87254.1}, RC A247 {ECO:0000313|EMBL:CEQ74463.1}, RC A59307 {ECO:0000313|EMBL:CER76083.1}, RC E00-2756 {ECO:0000313|EMBL:CET20316.1}, RC E02-0530 {ECO:0000313|EMBL:CEU52841.1}, RC ERL021174 {ECO:0000313|EMBL:CER93589.1}, RC ERL07264 {ECO:0000313|EMBL:CEU76198.1}, RC ERL10320 {ECO:0000313|EMBL:CER12533.1}, RC ERL12680 {ECO:0000313|EMBL:CEV30920.1}, RC Gen-0001 {ECO:0000313|EMBL:CEU44602.1}, RC Gen-0024 {ECO:0000313|EMBL:CES84503.1}, RC Gen-0042 {ECO:0000313|EMBL:CEU78556.1}, RC Gen-0053 {ECO:0000313|EMBL:CEU48213.1}, RC IPC {ECO:0000313|EMBL:CEU25962.1}, IPCE {ECO:0000313|EMBL:CET09524.1}, RC IPCG {ECO:0000313|EMBL:CET51765.1}, RC IPCS {ECO:0000313|EMBL:CES41823.1}, RC LNT722 {ECO:0000313|EMBL:CES73729.1}, RC LNT899 {ECO:0000313|EMBL:CES67453.1}, RC MDUST114 {ECO:0000313|EMBL:CET05054.1}, RC MDUST14 {ECO:0000313|EMBL:CEV31166.1}, RC MDUST149 {ECO:0000313|EMBL:CES14661.1}, RC MDUST19 {ECO:0000313|EMBL:CER03837.1}, RC MDUST22 {ECO:0000313|EMBL:CET60944.1}, RC MDUST284 {ECO:0000313|EMBL:CES23804.1}, RC MDUST289 {ECO:0000313|EMBL:CES18604.1}, RC MDUST307 {ECO:0000313|EMBL:CER32403.1}, RC MDUST312 {ECO:0000313|EMBL:CEU05827.1}, RC MDUST320 {ECO:0000313|EMBL:CER50422.1}, RC MDUST322 {ECO:0000313|EMBL:CEU05220.1}, RC MDUST391 {ECO:0000313|EMBL:CEV03780.1}, RC MDUST413 {ECO:0000313|EMBL:CEV16684.1}, RC MDUST44 {ECO:0000313|EMBL:CEU18636.1}, RC MDUST52 {ECO:0000313|EMBL:CET45503.1}, RC MDUST74 {ECO:0000313|EMBL:CEU00693.1}, RC MDUST77 {ECO:0000313|EMBL:CER77976.1}, and RC UI2152 {ECO:0000313|EMBL:CER96999.1}; RA Informatics Pathogen; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AL513382; CAD09193.1; -; Genomic_DNA. DR EMBL; CELU01000022; CEP54858.1; -; Genomic_DNA. DR EMBL; CEWU01000006; CEQ52038.1; -; Genomic_DNA. DR EMBL; CEWY01000007; CEQ69349.1; -; Genomic_DNA. DR EMBL; CEXA01000007; CEQ74463.1; -; Genomic_DNA. DR EMBL; CEXF01000007; CEQ87254.1; -; Genomic_DNA. DR EMBL; CEXD01000024; CER03837.1; -; Genomic_DNA. DR EMBL; CEXH01000006; CER12533.1; -; Genomic_DNA. DR EMBL; CEXK01000023; CER32403.1; -; Genomic_DNA. DR EMBL; CEXP01000006; CER50422.1; -; Genomic_DNA. DR EMBL; CEXQ01000024; CER61169.1; -; Genomic_DNA. DR EMBL; CEXU01000023; CER76083.1; -; Genomic_DNA. DR EMBL; CEXV01000006; CER77976.1; -; Genomic_DNA. DR EMBL; CEXW01000006; CER82150.1; -; Genomic_DNA. DR EMBL; CEXY01000006; CER92575.1; -; Genomic_DNA. DR EMBL; CEXZ01000003; CER93589.1; -; Genomic_DNA. DR EMBL; CEYA01000006; CER96999.1; -; Genomic_DNA. DR EMBL; CEYD01000006; CES14252.1; -; Genomic_DNA. DR EMBL; CEYB01000023; CES14661.1; -; Genomic_DNA. DR EMBL; CEYF01000006; CES18604.1; -; Genomic_DNA. DR EMBL; CEYE01000023; CES23804.1; -; Genomic_DNA. DR EMBL; CEYI01000021; CES41823.1; -; Genomic_DNA. DR EMBL; CEYN01000006; CES58067.1; -; Genomic_DNA. DR EMBL; CEYQ01000006; CES67180.1; -; Genomic_DNA. DR EMBL; CEYP01000006; CES67453.1; -; Genomic_DNA. DR EMBL; CEYR01000002; CES73729.1; -; Genomic_DNA. DR EMBL; CEYT01000006; CES84503.1; -; Genomic_DNA. DR EMBL; CEYY01000005; CET05054.1; -; Genomic_DNA. DR EMBL; CEYZ01000003; CET09524.1; -; Genomic_DNA. DR EMBL; CEZB01000006; CET20316.1; -; Genomic_DNA. DR EMBL; CEZD01000008; CET30039.1; -; Genomic_DNA. DR EMBL; CEZF01000006; CET45503.1; -; Genomic_DNA. DR EMBL; CEZE01000021; CET51765.1; -; Genomic_DNA. DR EMBL; CEZG01000023; CET60944.1; -; Genomic_DNA. DR EMBL; CEZK01000006; CET63996.1; -; Genomic_DNA. DR EMBL; CEZS01000006; CEU00693.1; -; Genomic_DNA. DR EMBL; CEZU01000006; CEU05220.1; -; Genomic_DNA. DR EMBL; CEZO01000023; CEU05827.1; -; Genomic_DNA. DR EMBL; CEZX01000006; CEU18636.1; -; Genomic_DNA. DR EMBL; CEZT01000020; CEU25962.1; -; Genomic_DNA. DR EMBL; CEZY01000021; CEU44602.1; -; Genomic_DNA. DR EMBL; CFAD01000006; CEU48213.1; -; Genomic_DNA. DR EMBL; CFAE01000006; CEU52841.1; -; Genomic_DNA. DR EMBL; CFAM01000006; CEU76198.1; -; Genomic_DNA. DR EMBL; CFAL01000006; CEU78556.1; -; Genomic_DNA. DR EMBL; CFAP01000015; CEV03780.1; -; Genomic_DNA. DR EMBL; CFAS01000009; CEV16684.1; -; Genomic_DNA. DR EMBL; CFAU01000006; CEV18356.1; -; Genomic_DNA. DR EMBL; CFAV01000006; CEV30920.1; -; Genomic_DNA. DR EMBL; CFAT01000024; CEV31166.1; -; Genomic_DNA. DR RefSeq; NP_458507.1; NC_003198.1. DR ProteinModelPortal; Q8Z1V6; -. DR SMR; Q8Z1V6; 651-1227. DR STRING; 220341.STY4405; -. DR EnsemblBacteria; AAO71579; AAO71579; t4115. DR EnsemblBacteria; CAD09193; CAD09193; CAD09193. DR GeneID; 1250622; -. DR KEGG; sty:STY4405; -. DR PATRIC; 18547049; VBISalEnt120419_4504. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR Proteomes; UP000000541; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000541}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAD09193.1}; KW Transferase {ECO:0000313|EMBL:CAD09193.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 247 247 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 310 310 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 311 311 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 759 759 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1227 AA; 136019 MW; 5A8080F777214A56 CRC64; MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLHEEDFRGE RFADWPCDLK GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYRMESLS AEINYAAAKL ARACADEWTA RTPEKPRFVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKEEF EALGVDLPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE AGFLNIVGGC CGTTPEHIAA MSRAVAGLSP RQLPDIPVAC RLSGLEPLNI GDDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VESGAQIIDI NMDEGMLDAE AAMVRFLSLI AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVEAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRERKIEI CRRAYKILLE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG QLAIYDNLPA ELRDAVEDVI LNRRDDGTER LLDLAEKYRG SKTDEAASAQ QAEWRSWDVK KRLEYSLVKG ITEFIEQDTE EARQQAARPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EKGSSNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAREVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHARKKPR TPPVTLEAAR DNDLAFDWER YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KLLNPRGVVG LFPANRVGDD IEIYRDETRT HVLTVSHHLR QQTEKVGFAN YCLADFVAPK LSGKADYIGA FAVTGGLKED ALADAFEAQH DDYNKIMVKA IADRLAEAFA EYLHERVRKV YWGYAPNESL SNDELIRENY QGIRPAPGYP ACPEHTEKGT IWQLLDVEKH TGMKLTESFA MWPGASVSGW YFSHPESKYF AVAQIQRDQV TDYAFRKGMS VEDVERWLAP NLGYDAD // ID Q92AY2_LISIN Unreviewed; 617 AA. AC Q92AY2; DT 01-DEC-2001, integrated into UniProtKB/TrEMBL. DT 01-DEC-2001, sequence version 1. DT 29-APR-2015, entry version 79. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=lin1786 {ECO:0000313|EMBL:CAC97017.1}; OS Listeria innocua serovar 6a (strain CLIP 11262). OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=272626 {ECO:0000313|Proteomes:UP000002513}; RN [1] {ECO:0000313|EMBL:CAC97017.1, ECO:0000313|Proteomes:UP000002513} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CLIP 11262 {ECO:0000313|Proteomes:UP000002513}; 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., Portillo F.G., Garrido P., Gautier L., RA Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.M., RA Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., RA Maitournam A., Vicente J.M., Ng E., Nedjari H., Nordsiek G., RA Novella S., de Pablos B., Perez-Diaz J.C., Purcell R., Remmel B., RA Rose M., Schlueter T., Simoes N., Tierrez A., Vazquez-Boland J.A., RA Voss H., Wehland J., Cossart P.; RT "Comparative genomics of Listeria species."; RL Science 294:849-852(2001). CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL596169; CAC97017.1; -; Genomic_DNA. DR PIR; AI1655; AI1655. DR RefSeq; NP_471122.1; NC_003212.1. DR RefSeq; WP_010990953.1; NC_003212.1. DR ProteinModelPortal; Q92AY2; -. DR STRING; 272626.lin1786; -. DR EnsemblBacteria; CAC97017; CAC97017; CAC97017. DR KEGG; lin:lin1786; -. DR PATRIC; 20300329; VBILisInn102668_1831. DR GenoList; LIN1786; -. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR Proteomes; UP000002513; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002513}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 617 AA; 68650 MW; 1B043123A8B23FD8 CRC64; MNLRKDLSEK VLIADGAMGT LLYSYGVDRS FEELNLSHPE DIVAIHKAYI GAGADIIQTN TYGANYIKLA RYGLEDEVKR INQAAIRLAK EAARGTGTYI FGTIGGINGA VDARLPAAPL EEIKRSFREQ LYCFLLDGVD AILLETYYDL DELKTVLKIL RETTDLPVVA NVSMHESGIL QNGKKLPDAL EELIALGADV VGINCRLGPY HMARALETVP LYDKAYLAVY PNASLPEVQE GKVIYQSDTD YFEHYGEVFR QEGARIIGGC CGTTPDHIRA LRKGLESTKP VLEKEVRPIL ELVPEEVEDE ESGERLLDKV KERLTILVEL DPPRTFDTSK FFEGAKALDE AGVDAITISD NSLATPRISN MALASILKHE YGIKPLIHLT TRDHNLVGMH SHVMGFHKLG LHDVLAITGD PTKVGDFPGA SSVFDLRSVE LVQLIKKFND GISYTGKSLK EKARFHVGAA FNPNVLNLEK AVRLIERKVE YGADYIITQP IYDVNKAVLL KEALQKANID VPLFIGVMPL LSSRNAEFLH NEVPGIRLTD EVRERMREAE EHGHANEEGM AIARELVDAI CEHFQGIYII TPFLRYDLSI ELAKYVQNKQ QLQIASK // ID Q92LQ0_RHIME Unreviewed; 1257 AA. AC Q92LQ0; DT 01-DEC-2001, integrated into UniProtKB/TrEMBL. DT 01-DEC-2001, sequence version 1. DT 27-MAY-2015, entry version 88. DE SubName: Full=MetH protein {ECO:0000313|EMBL:CAC47560.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:CAC47560.1}; GN Name=metH {ECO:0000313|EMBL:CAC47560.1}; GN ORFNames=SMc03112 {ECO:0000313|EMBL:CAC47560.1}; 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 {ECO:0000313|EMBL:CAC47560.1, ECO:0000313|Proteomes:UP000001976}; RN [1] {ECO:0000313|EMBL:CAC47560.1, ECO:0000313|Proteomes:UP000001976} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1021 {ECO:0000313|EMBL:CAC47560.1, RC ECO:0000313|Proteomes:UP000001976}; 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] {ECO:0000313|Proteomes:UP000001976} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1021 {ECO:0000313|Proteomes:UP000001976}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AL591688; CAC47560.1; -; Genomic_DNA. DR RefSeq; NP_387087.1; NC_003047.1. DR RefSeq; WP_010970331.1; NC_003047.1. DR ProteinModelPortal; Q92LQ0; -. DR SMR; Q92LQ0; 668-1247. DR STRING; 266834.SMc03112; -. DR EnsemblBacteria; CAC47560; CAC47560; SMc03112. DR GeneID; 1234664; -. DR KEGG; sme:SMc03112; -. DR PATRIC; 23635566; VBISinMel96828_4507. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; SMEL266834:GJF6-3056-MONOMER; -. DR Proteomes; UP000001976; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001976}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:CAC47560.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001976}; KW Transferase {ECO:0000313|EMBL:CAC47560.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 262 262 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 325 325 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 326 326 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 779 779 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1257 AA; 138077 MW; DC4B8906DE121E60 CRC64; MSAADALFGN VSPKPDGSEV FRQLAQAAAE RILIMDGAMG TEIQQLGFVE DHFRGERFGG CACHQQGNND LLTLTQPKAI EDIHYHYAIA GADILETNTF SSTRIAQADY GMEDMVYDLN RDGARLARRA AKRAEAEDGR RRFVAGALGP TNRTASISPD VNNPGYRAVS FDDLRLAYAE QVRGLIDGGA DIILIETIFD TLNAKAAIFA TQEVFAEKGV RLPVMISGTI TDLSGRTLSG QTPTAFWYSV RHADPFTIGL NCALGANAMR AHIDELSAVA DTLVCAYPNA GLPNEFGRYD ESPEQMAAQV EGFARDGLVN IVGGCCGSTP AHIRAIAEAV AKYPPRRVPE IDRRMRLSGL EPFTLTDEIP FVNVGERTNV TGSAKFRKLI TAGDYAAALD VARDQVANGA QIIDVNMDEG LIDSKQVMVE FLNLVASEPD IARVPVMIDS SKWEVIEAGL KCVQGKALVN SISLKEGEAA FLHHARLVRA YGAAVVVMAF DEKGQADTKT RKVEICRRAY RLLTEEVGFP PEDIIFDPNI FAVATGIEEH NNYGVDFIEA THEIIAALPH VHVSGGVSNL SFSFRGNEPV REAMHAIFLY HAIQAGMDMG IVNAGQLAVY DAIDPELRET CEDVVLNRRA DSTERLLEIA ERYRGKGGSQ GKEKDLAWRE WPVEKRLEHA LVNGITEFIE ADTEEARLAA ERPLHVIEGP LMAGMNVVGD LFGSGKMFLP QVVKSARVMK QAVAVLLPHM EEEKRANGGG EARESAGKIL MATVKGDVHD IGKNIVGVVL ACNNYEIIDL GVMVPSAKIL EVAREQKVDI VGLSGLITPS LDEMAHVASE LEREGFDVPL LIGGATTSRV HTAVKINPRY SLGQTVYVTD ASRAVGVVSS LLSPEVRDSY KKTVRAEYLK VADAHARNEA EKRRLPLSQA RANAFRIDWD AHQPKVPSFL GTRVFEGWDL AELARYIDWT PFFQTWELKG VFPKILDDER QGAAARQLFE DAQAMVEKIV AEAWFAPKAV IGFWPAASMG DDVRLFADEV REAELATFFT LRQQMVKRDG RPNVALADFV APAASGKRDY VGGFVVTAGI EEVAIAERFE RANDDYSSIM VKALADRFAE AFAERMHEYV RKELWGYAPD EAFTPQELIA EPYAGIRPAP GYPAQPDHTE KETLFRLLDA EAAIGVRLTE SYAMWPGSSV SGLYVGHPDS YYFGVAKIER DQVEDYADRK RMSVREVERW LSPILNYVPM PETEAAE // ID Q92P25_RHIME Unreviewed; 337 AA. AC Q92P25; DT 01-DEC-2001, integrated into UniProtKB/TrEMBL. DT 01-DEC-2001, sequence version 1. DT 27-MAY-2015, entry version 67. DE SubName: Full=Bmt protein {ECO:0000313|EMBL:CAC46550.1}; DE EC=2.1.1.5 {ECO:0000313|EMBL:CAC46550.1}; GN Name=bmt {ECO:0000313|EMBL:CAC46550.1}; GN ORFNames=SMc04325 {ECO:0000313|EMBL:CAC46550.1}; 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 {ECO:0000313|EMBL:CAC46550.1, ECO:0000313|Proteomes:UP000001976}; RN [1] {ECO:0000313|EMBL:CAC46550.1, ECO:0000313|Proteomes:UP000001976} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1021 {ECO:0000313|EMBL:CAC46550.1, RC ECO:0000313|Proteomes:UP000001976}; 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] {ECO:0000313|Proteomes:UP000001976} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1021 {ECO:0000313|Proteomes:UP000001976}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505- CC 2}; CC ----------------------------------------------------------------------- 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; CAC46550.1; -; Genomic_DNA. DR RefSeq; NP_386077.1; NC_003047.1. DR RefSeq; WP_003530700.1; NC_003047.1. DR ProteinModelPortal; Q92P25; -. DR STRING; 266834.SMc04325; -. DR EnsemblBacteria; CAC46550; CAC46550; SMc04325. DR GeneID; 1233636; -. DR KEGG; sme:SMc04325; -. DR PATRIC; 23633365; VBISinMel96828_3421. DR HOGENOM; HOG000265278; -. DR KO; K00548; -. DR OMA; GTNLFAM; -. DR OrthoDB; EOG693GKH; -. DR BioCyc; SMEL266834:GJF6-2020-MONOMER; -. DR Proteomes; UP000001976; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001976}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2}; KW Methyltransferase {ECO:0000313|EMBL:CAC46550.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001976}; KW Transferase {ECO:0000313|EMBL:CAC46550.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 215 215 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 281 281 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. FT METAL 282 282 Zinc. {ECO:0000256|PIRSR:PIRSR037505-2}. SQ SEQUENCE 337 AA; 35069 MW; 121A703F6038BDD7 CRC64; MSVAAHALSD LLAQKGVLLA DGATGTSLFA MGLEAGEAPE IWNETKPDNI TKLHQDFVDA GADIILTNSF GGTRHRLKLH QAEDRVHQLN KRAAEIARAV ADKAPRKVIT AGSVGPTGEL LIPLGALSYE DAVAAFVEQI EGLKAGGAEV AWIETMSSPD EIRAAAEAAA KVGLPYVYTG SFDTAGKTMM GLHPKDIHGV AADIGEGPVA VGANCGVGAS DILSSLLDMT AASPEATIVV KGNCGIPEFR GSEIHYSGTP PLMAEYARLA VDAGAKIIGG CCGTSCNHLA AMRLAIDNHT RGERPTLETI VEKIGPLRNK SANEGPAAPA RERRRRA // ID Q93A68_9BACT Unreviewed; 612 AA. AC Q93A68; DT 01-DEC-2001, integrated into UniProtKB/TrEMBL. DT 01-DEC-2001, sequence version 1. DT 07-JAN-2015, entry version 54. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; OS uncultured bacterium. OC Bacteria; environmental samples. OX NCBI_TaxID=77133 {ECO:0000313|EMBL:AAL27409.1}; RN [1] {ECO:0000313|EMBL:AAL27409.1} RP NUCLEOTIDE SEQUENCE. RA Wilkinson D.E., Jeanicke T.J., Cowan D.A.; RT "Rapid extraction and purification of environmental DNA for molecular RT cloning and heterologous expression."; RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF429956; AAL27409.1; -; Genomic_DNA. DR ProteinModelPortal; Q93A68; -. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}. SQ SEQUENCE 612 AA; 66816 MW; 92F24B26375EE57A CRC64; MLIADGAIGT MLALRGVPTP YELANLLYPD TVRALHREYY EAGARLIETN TYTANRVRLF NLPERGSEAP PTYSLLEQFG SPEELVRRIN QEAVRLAREA VGADALVFGS VGPVGKPLEP IGETRLDEAE GAFREQMQAL LEAGVDGLIL ETFIDPRELE LAIRVARELA PDLPLIASKG FVEDGETLME GLPERFAHTV SALGVDAVGA NCVVGPQRML DIVRMMATGT ELPLSSMPTP GLPQLVRGQV VYDIHPDYFG RYAVRLVEAG AQIVGGCCGT TPDHIRAVAQ AVSRTPVKRR AGGIRAVVRE RKEEELPLAE PSRLSQILGK ERVIAVELDL PRGLKVQKVI EGARLLKEHG VHVIDISDGA RARLRMNVIA ISHLVQREAG IEVMMHFACR DRNLLAIQAD LLGAHALGIR NVLAITGDPA QIGDYPTATS VFDVDAIGLV RILRRFNEGR DLAGNTIGVR ANFTIAVAYN PLAPDPETER DRLRKKIEEG AHLVYTQPIF EMRVVEETAE LMNRLGVPWL VGVLPLRSAR HAEFMHNEVP GVSIPEPILR RMAEAPEEDA LAVGLEIARR FVAEAAPYAQ GVYLMPPAGS AQIALQVIEA IR // ID Q966F6_CAEEL Unreviewed; 304 AA. AC Q966F6; DT 01-DEC-2001, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 2. DT 01-APR-2015, entry version 79. DE SubName: Full=T13G4.4 {ECO:0000313|EMBL:CCD67540.1}; GN ORFNames=CELE_T13G4.4 {ECO:0000313|EMBL:CCD67540.1}, GN T13G4.4 {ECO:0000313|EMBL:CCD67540.1, ECO:0000313|WormBase:T13G4.4}; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CCD67540.1, ECO:0000313|Proteomes:UP000001940}; RN [1] {ECO:0000313|Proteomes:UP000001940} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2 {ECO:0000313|Proteomes:UP000001940}; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for RT investigating biology."; RL Science 282:2012-2018(1998). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX284606; CCD67540.1; -; Genomic_DNA. DR RefSeq; NP_508223.2; NM_075822.2. DR UniGene; Cel.27693; -. DR ProteinModelPortal; Q966F6; -. DR SMR; Q966F6; 2-296. DR STRING; 6239.T13G4.4; -. DR PaxDb; Q966F6; -. DR EnsemblMetazoa; T13G4.4.1; T13G4.4.1; WBGene00020491. DR EnsemblMetazoa; T13G4.4.2; T13G4.4.2; WBGene00020491. DR EnsemblMetazoa; T13G4.4.3; T13G4.4.3; WBGene00020491. DR GeneID; 188484; -. DR KEGG; cel:CELE_T13G4.4; -. DR UCSC; T13G4.4; c. elegans. DR CTD; 188484; -. DR WormBase; T13G4.4; CE44630; WBGene00020491; -. DR eggNOG; COG2040; -. DR GeneTree; ENSGT00510000049619; -. DR InParanoid; Q966F6; -. DR OMA; HWTFPAN; -. DR PhylomeDB; Q966F6; -. DR NextBio; 938976; -. DR Proteomes; UP000001940; Chromosome X. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IBA:GO_Central. DR GO; GO:0032259; P:methylation; IBA:GOC. DR GO; GO:0033528; P:S-methylmethionine cycle; IBA:GO_Central. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001940}; KW Reference proteome {ECO:0000313|Proteomes:UP000001940}. SQ SEQUENCE 304 AA; 34197 MW; 0EDF95F2BDCA5FFC CRC64; MVRLLDGSMS SQLLRFGYDC NQQENKPHWS FPANADMELM ENVYKSFLDL EVKVITSNTY HFGSTLDKTI PENAEKRELY EKYFEETCLK LCHLTTGSSD VEAWGSVGTL ATMYHDLSEY TGAYMDQSEA KKTAYDYFKI ILTLFHNRSS IRKLIFETIP SADEGSVALD VLQEFPEFEA VISFTFKEHG CLRHGEKITS VAQQMKQSPQ VLGIGINCTD PNNVLPALNE LQPFAFSEVF VYPNKGDSKF LEEGIDESNV FTKTLVTSWI EKGVTAIGGC CGVTNDQIKV LKPLLGKINT NQLL // ID Q97DX2_CLOAB Unreviewed; 314 AA. AC Q97DX2; DT 01-OCT-2001, integrated into UniProtKB/TrEMBL. DT 01-OCT-2001, sequence version 1. DT 27-MAY-2015, entry version 65. DE SubName: Full=Possible homocysteine S-methyltransferase {ECO:0000313|EMBL:AAK81280.1}; GN OrderedLocusNames=CA_C3348 {ECO:0000313|EMBL:AAK81280.1}; 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 {ECO:0000313|EMBL:AAK81280.1, ECO:0000313|Proteomes:UP000000814}; RN [1] {ECO:0000313|EMBL:AAK81280.1, ECO:0000313|Proteomes:UP000000814} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 RC {ECO:0000313|Proteomes:UP000000814}; 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; AAK81280.1; -; Genomic_DNA. DR PIR; E97311; E97311. DR RefSeq; NP_349940.1; NC_003030.1. DR RefSeq; WP_010966620.1; NC_003030.1. DR ProteinModelPortal; Q97DX2; -. DR STRING; 272562.CA_C3348; -. DR EnsemblBacteria; AAK81280; AAK81280; CA_C3348. DR GeneID; 1119530; -. DR KEGG; cac:CA_C3348; -. DR PATRIC; 32041131; VBICloAce74127_3529. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; YGRSVTK; -. DR OrthoDB; EOG6C019S; -. DR BioCyc; CACE272562:GJIH-3445-MONOMER; -. DR Proteomes; UP000000814; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000814}; KW Methyltransferase {ECO:0000313|EMBL:AAK81280.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000814}; KW Transferase {ECO:0000313|EMBL:AAK81280.1}. SQ SEQUENCE 314 AA; 34525 MW; C68FC2E88CE942D2 CRC64; MSNPIKSILD DFPVVILDGA LATELEKRGC NLNDSLWSAK ILANNPEIIE NVHYDYFVSG SDCAITSSYQ ATIDGFMKNG FPRDKAKDLI RNSVAIAKKA RDRFWGNPTN RRNRAKPFIA GSVGPYGAYL ADGSEYRGDY KIDENALIKF HKSNVKLLIE AGADILACET IPNLTEARAI VKLLEEFPGV YAWISFSCKN DYEISDGTPI FECAKVLNSC KNIAAIGVNC TSPKYINSLI KEIKKASDKP IIVYPNSGEE YDANTKTWHG ASSSNAFSIS AKEWFENGAS VIGGCCRTTP SDINATYKIL KNID // ID Q97LI3_CLOAB Unreviewed; 1212 AA. AC Q97LI3; DT 01-OCT-2001, integrated into UniProtKB/TrEMBL. DT 01-OCT-2001, sequence version 1. DT 27-MAY-2015, entry version 93. DE SubName: Full=Cobalamine-dependent methionine synthase I (Methyltransferase and cobalamine-binding domain) {ECO:0000313|EMBL:AAK78556.1}; GN Name=metH {ECO:0000313|EMBL:AAK78556.1}; GN OrderedLocusNames=CA_C0578 {ECO:0000313|EMBL:AAK78556.1}; 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 {ECO:0000313|EMBL:AAK78556.1, ECO:0000313|Proteomes:UP000000814}; RN [1] {ECO:0000313|EMBL:AAK78556.1, ECO:0000313|Proteomes:UP000000814} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 RC {ECO:0000313|Proteomes:UP000000814}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AE001437; AAK78556.1; -; Genomic_DNA. DR PIR; A96971; A96971. DR RefSeq; NP_347216.1; NC_003030.1. DR RefSeq; WP_010963898.1; NC_003030.1. DR ProteinModelPortal; Q97LI3; -. DR SMR; Q97LI3; 647-888. DR STRING; 272562.CA_C0578; -. DR DNASU; 1116761; -. DR EnsemblBacteria; AAK78556; AAK78556; CA_C0578. DR GeneID; 1116761; -. DR KEGG; cac:CA_C0578; -. DR PATRIC; 32035519; VBICloAce74127_0781. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; CACE272562:GJIH-619-MONOMER; -. DR Proteomes; UP000000814; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000814}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AAK78556.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000814}; KW Transferase {ECO:0000313|EMBL:AAK78556.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 244 244 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 307 307 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 756 756 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1212 AA; 135627 MW; 09D4EF087F93DCE4 CRC64; MNSSLKNLLN NKILVLDGAM GTCIQSFNLD EGDFKGSLSC TCHSNQKGNN DVLNLTKPEI IKEIHKRYLE AGADIIETNT FNATEISQKD YNMQDKIYDI NFKGAKLAKE ACTYYTKLNP NKPRFAAGSI GPTNRTASLS PDVENPGFRN VTFDELCNAY KHQIEALIDG GVDLLLIETI FDTLNARAAI FAAETVFENK KIKLPIIISG TIADKSGRIL SGQTLDAFAE SLKNENIIAI GLNCSFGAEE LIPFIKRLSE TQNRYISFHP NAGLPNSLGE YEELPEETAS IVKKLALEGH LNIVGGCCGT TPEHIRAISS VVKGISPRKV PNLEPKTIYS GLENIKIDKN SNFINIGERT NVAGSRKFAR LIREKNYEEA LTIARHQVEN GAQIIDINFD DALLDARSEM ETFLRLIASE PEISKVPVMI DSSNFEVLKV GLKSIQGKAI VNSISLKVGE EKFIEEAKFI KNFGAGVVVM AFDEEGQAAT YERKIEICKR AYTILTEKVE FPPENIIFDP NILSIATGIE EHDNYAVNYI KAVKWIKENL PYAKVSGGVS NLSFSFRGND AIRRAMHSVF LYHAINAGMD MGIVNPAMID LYDDIDKDLL EKVENVVLNK SSNASESLLE FAQTYKKTTE TLEKHEDEWR QKSPSERLSY ALVKGNVEFI EEDIEEARKE YTNALEIIEV PLMNGMKKVG KLFGEGKMFL PQVVKSARVM KKAVECLLPY INEEKSKNHN KSAGKVVFAT VKGDVHDIGK NIVSVVLSCN NFEVIDLGVM VPPETILETA KRENADIIAL SGLITPSLNE MAYVAEEMKR LNFDIPLMVG GAATSKTHTA LKLATKYKYV VHSTDASDAV TVAKNLMSEN KFTFLEKLNE EYSKIRETFS TNKIELISIQ NARKNRFTID WNKTKITEPK FVGIKKLQAV PINELRKYID WTFFFTSWDM GMNYPKIMKD PKYGAEAQKL FKDANEMLDL LQKENLITCN GVFGIFPANS VNDDIEIYTD KGTVTINTLR QQQILKDSDY KALSDYIAPK GIGIKDYIGG FIVTAGIGAK EYSDKLKKKC DDYGATMLKL ICDRLAEAFS ELLHLRVRKE YWGYSQDENL SLEKLLKGSY RGIKPAIGYP SIPDHSEKAK LFDLLLGKTS IGVELTESYM MNPTSSVCGL YFANERAKYF NINKIGKDQL EDYAVRSNKD INEIKKLLDT LL // ID Q98KX0_RHILO Unreviewed; 301 AA. AC Q98KX0; DT 01-OCT-2001, integrated into UniProtKB/TrEMBL. DT 01-OCT-2001, sequence version 1. DT 29-APR-2015, entry version 62. DE SubName: Full=Mlr1281 protein {ECO:0000313|EMBL:BAB48693.1}; GN OrderedLocusNames=mlr1281 {ECO:0000313|EMBL:BAB48693.1}; OS Rhizobium loti (strain MAFF303099) (Mesorhizobium loti). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=266835 {ECO:0000313|EMBL:BAB48693.1, ECO:0000313|Proteomes:UP000000552}; RN [1] {ECO:0000313|EMBL:BAB48693.1, ECO:0000313|Proteomes:UP000000552} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MAFF303099 {ECO:0000313|EMBL:BAB48693.1, RC ECO:0000313|Proteomes:UP000000552}; 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; BAB48693.1; -; Genomic_DNA. DR RefSeq; NP_102907.1; NC_002678.2. DR RefSeq; WP_010910047.1; NC_002678.2. DR ProteinModelPortal; Q98KX0; -. DR STRING; 266835.mlr1281; -. DR EnsemblBacteria; BAB48693; BAB48693; BAB48693. DR GeneID; 1225570; -. DR KEGG; mlo:mlr1281; -. DR PATRIC; 22476252; VBIMesLot2464_1038. DR HOGENOM; HOG000265278; -. DR OMA; PYVDVWL; -. DR OrthoDB; EOG6Q5NS7; -. DR BioCyc; MLOT266835:GJ9L-1025-MONOMER; -. DR Proteomes; UP000000552; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037505; Betaine_HMT; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000552}; KW Reference proteome {ECO:0000313|Proteomes:UP000000552}. SQ SEQUENCE 301 AA; 31953 MW; CA9FEA8C77684843 CRC64; MKNVILTDGG MGQELVRRSK SEPTPLWSAR VLIDEPDLVR DLHAEFIRAG ARVITINTYS ATPERLAREG AEDLFKPLQK RGIELARQAC DEAGEAAIAG CLSPLFGSYA PALTISYQET LDIYRRIVAE QADGVDLFLC ETMASSDEAR AAVTAASESG KPVWVSWTLA DHGTPRLRSG ETIAAAASAL DGLPIAARLL NCCRPETIAA ALPELIDLGG PVGAYANGFT STEALKHGGT VDVLHARHDL APDAYAEQAI GWVEAGADIV GGCCEVGPPH IAALRDRLQQ DSYEISGVLH A // ID Q98L18_RHILO Unreviewed; 340 AA. AC Q98L18; DT 01-OCT-2001, integrated into UniProtKB/TrEMBL. DT 01-OCT-2001, sequence version 1. DT 04-MAR-2015, entry version 61. DE SubName: Full=5-methyltetrahydrofolate S-homocysteine methyltransferase {ECO:0000313|EMBL:BAB48645.1}; GN OrderedLocusNames=mlr1220 {ECO:0000313|EMBL:BAB48645.1}; OS Rhizobium loti (strain MAFF303099) (Mesorhizobium loti). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=266835 {ECO:0000313|EMBL:BAB48645.1, ECO:0000313|Proteomes:UP000000552}; RN [1] {ECO:0000313|EMBL:BAB48645.1, ECO:0000313|Proteomes:UP000000552} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MAFF303099 {ECO:0000313|EMBL:BAB48645.1, RC ECO:0000313|Proteomes:UP000000552}; 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; BAB48645.1; -; Genomic_DNA. DR RefSeq; NP_102859.1; NC_002678.2. DR RefSeq; WP_010909999.1; NC_002678.2. DR ProteinModelPortal; Q98L18; -. DR STRING; 266835.mlr1220; -. DR EnsemblBacteria; BAB48645; BAB48645; BAB48645. DR GeneID; 1225522; -. DR KEGG; mlo:mlr1220; -. DR PATRIC; 22476150; VBIMesLot2464_0987. DR HOGENOM; HOG000265278; -. DR KO; K00548; -. DR OMA; GTNLFAM; -. DR OrthoDB; EOG693GKH; -. DR BioCyc; MLOT266835:GJ9L-977-MONOMER; -. DR Proteomes; UP000000552; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000552}; KW Methyltransferase {ECO:0000313|EMBL:BAB48645.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000552}; KW Transferase {ECO:0000313|EMBL:BAB48645.1}. SQ SEQUENCE 340 AA; 35719 MW; 12618499E8ECEC48 CRC64; MTTTNPIDAL LAEKGVLLAD GATGTNLFAM GLEAGEAPEL LNETAPDTIT NLHQNFVDAG ADIILTNSFG GTRHRLKLHH AQDRVHALNK RAAEIARAVA DKAGRKVIVA GSVGPTGELL VPLGAMTYDE AVDAFAEQIE GLKQGGAEVA WIETMSAPDE IRAAAEAAIR VGLPYTYTGS FDTAGRTMMG LLPKEIHGVV DGLSEAPLGV GANCGVGASD ILASLLDMTE AKPQATVIVK GNCGIPEFRG TEIHYSGTPE LMADYVRLAV DAGAKIVGGC CGTSFQHLAA MRKALDAHTK AGRPTVETIV ERIGPMRNKV ATENTAETSE ARRERRRSRA // ID Q9A6F6_CAUCR Unreviewed; 358 AA. AC Q9A6F6; DT 01-JUN-2001, integrated into UniProtKB/TrEMBL. DT 01-JUN-2001, sequence version 1. DT 27-MAY-2015, entry version 71. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AAK24109.1}; GN OrderedLocusNames=CC_2138 {ECO:0000313|EMBL:AAK24109.1}; OS Caulobacter crescentus (strain ATCC 19089 / CB15). OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Caulobacter. OX NCBI_TaxID=190650 {ECO:0000313|EMBL:AAK24109.1, ECO:0000313|Proteomes:UP000001816}; RN [1] {ECO:0000313|EMBL:AAK24109.1, ECO:0000313|Proteomes:UP000001816} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19089 / CB15 {ECO:0000313|Proteomes:UP000001816}; 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; AAK24109.1; -; Genomic_DNA. DR PIR; A87514; A87514. DR RefSeq; NP_420941.1; NC_002696.2. DR RefSeq; WP_010919999.1; NC_002696.2. DR ProteinModelPortal; Q9A6F6; -. DR SMR; Q9A6F6; 14-358. DR EnsemblBacteria; AAK24109; AAK24109; CC_2138. DR GeneID; 943063; -. DR KEGG; ccr:CC_2138; -. DR PATRIC; 21301294; VBICauCre124313_2158. DR HOGENOM; HOG000265279; -. DR KO; K00548; -. DR OMA; AQEDYKM; -. DR OrthoDB; EOG6H1PZ4; -. DR BioCyc; CAULO:CC2138-MONOMER; -. DR Proteomes; UP000001816; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001816}; KW Methyltransferase {ECO:0000313|EMBL:AAK24109.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001816}; KW Transferase {ECO:0000313|EMBL:AAK24109.1}. SQ SEQUENCE 358 AA; 39254 MW; 991DA5B41D57C68F CRC64; MTDLSIRANR VAALKAAAKE RILILDGSWG VMFQKKGLTE ADYRAERFAA YNGQMKGNND ILCLTRPDLV AELHDAYFSA GADISETNTF SGTTIAQADY HLGEQDVWDI NLEGAKIGRS VADRWNAQNP DRPKFIAGSM GPLNVMLSMS SDVNDPGARK VTFDQVYEAY RQQVDALYQG GVDLFLIETI TDTLNCKAAI KAILDWRDEG HEELPIWISG TITDRSGRTL SGQTAEAFWN SVKHAKPFAV GFNCALGADL MRPHIAEMAR IADTLVAAYP NAGLPNAMGQ YDEEPHETGH ALHEWAKDGL VNILGGCCGT TPDHIRHVAD EVRGVTPRQI PERPKAMRLA GLEPFELA // ID Q9AF90_PSEPU Unreviewed; 1237 AA. AC Q9AF90; DT 01-JUN-2001, integrated into UniProtKB/TrEMBL. DT 01-JUN-2001, sequence version 1. DT 01-APR-2015, entry version 67. DE SubName: Full=MetH {ECO:0000313|EMBL:AAK29461.1}; GN Name=metH {ECO:0000313|EMBL:AAK29461.1}; OS Pseudomonas putida (Arthrobacter siderocapsulatus). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=303 {ECO:0000313|EMBL:AAK29461.1}; RN [1] {ECO:0000313|EMBL:AAK29461.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DOT-T1E {ECO:0000313|EMBL:AAK29461.1}; RX PubMed=11479715; DOI=10.1007/s002030100293; RA Alaminos M., Ramos J.L.; RT "The methionine biosynthetic pathway from homoserine in Pseudomonas RT putida involves the metW, metX, metZ, metH and metE gene products."; RL Arch. Microbiol. 176:151-154(2001). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AF363276; AAK29461.1; -; Genomic_DNA. DR ProteinModelPortal; Q9AF90; -. DR SMR; Q9AF90; 656-1237. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 250 250 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 313 313 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 763 763 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1237 AA; 135647 MW; AC8E9FE5294C6210 CRC64; MSDRSARLQA LQNALKERIL ILDGGMGTMI QSYRLEEHDY RGTRFADWPS DVKGNNDLLL LSRPDVIAAI EKAYLDAGAD ILETNTFNAT QISQADYGME SLVYELNVEG ARIARQVADA KTLETPDKPR FVAGVLGPTS RTCSISPDVN DPGFRNVTFD ELVENYIEAT RGLIEGGADL ILIETIFDTL NAKAAIFAVQ QVFEDDNVEL PIMISGTITD ASGRTLSGQT TEAFWNSVRH AKPISVGLNC ALGAKDLRPY LEELATKADT HVSAHPNAGL PNAFGEYDET PAEMAAVVEE FAASGFLNII GGCLGTTPGH IQIQAIAEAV AKYKPREIPE IAKACRLSGL EPFTIDRQSL FVNVGERTNI TGSAKFARLI REENYTEALE VALQQVEAGA QVIDINMDEG MLDSQAAMVR FLNLIAGEPD ISRVPIMIDS SKWEVIEAGL KCIQGKGIVN SISMKEGVEQ FKHHARLCKR YGAAVVVMAF DEVGQADTAA RKKEICQRSY DILVNEVGFP PEDIIFDPNI FAVATGIEEH NNYAVDFIEA CAYIRDHLPH ALSSGGVSNV SFSFRGNNPV REAIHSVFLY HAIQNGLTMG IVNAGQLEIY DEIPAQLREK VEDVVLNRTP HGTDALLAIA DDYKGGGATK EVENEEWRSL PVEKRLEHAL VKGITAFIVE DTEECRQQCA RPIEVIEGPL MNGMNVVGDL FGAGKMFLPQ VVKSARVMKQ AVAHLIPFIE AEKGDKPEAK GKILMATVKG DVHDIGKNIF GVVLGCNGYD IVGPGVTVPA EKILQTAREQ KCDIIGLSGL ITPSLDEMVH VAREMQRQGF ELPLMIGGAT TSKAHTAVKI EPKYSNDAVI YVTDASRAVG VATQLLSKEL KPGFVEKTRL EYVDVRERTA NRSARTERLS YAQAIAAKPQ YDWASYQPAV PSFTGVKVLE DIDLRTLAEY IDWTPFFISW DLAGKFPRIL TDEVVGEAAT ALYKDAREML DKLIDEKLIS ARAVFGFWPA NQVADDDIEV YGEDGQALAT LHHLRQQTIK PDGKPNWSLA DFVAPKDSGV TDYVGGFITT AGIGAEEVAK AYQDKGDDYS SIMVKALADR LAEACAEWLH EQVRKEHWGY ARDEHLDNEA LIKEQYSGIR PAPGYPACPD HTEKETLFRL LDGTAIGETG PSGVYLTEHF AMFPAAAVSG WYFAHPQAKY FAVGKVDKDQ IERYSARKGQ DISVSERWLA PNLGYDS // ID Q9AJP7_9PSED Unreviewed; 284 AA. AC Q9AJP7; DT 01-JUN-2001, integrated into UniProtKB/TrEMBL. DT 01-JUN-2001, sequence version 1. DT 29-OCT-2014, entry version 38. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:BAB41103.1}; DE Flags: Fragment; GN Name=metH' {ECO:0000313|EMBL:BAB41103.1}; OS Pseudomonas psychrophila. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=122355 {ECO:0000313|EMBL:BAB41103.1}; RN [1] {ECO:0000313|EMBL:BAB41103.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=E-3 {ECO:0000313|EMBL:BAB41103.1}; RA Kusano T., Okuyama H.; RT "9-hexadecenoic acid cis-trans isomerase gene."; RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB041884; BAB41103.1; -; Genomic_DNA. DR ProteinModelPortal; Q9AJP7; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; FT NON_TER 284 284 {ECO:0000313|EMBL:BAB41103.1}. SQ SEQUENCE 284 AA; 30751 MW; 1A424EF80562DA9F CRC64; MSDRSARLQA LQQALKERIL ILDGGMGTMI QSYRLEEHDY RGTRFADWPS DVKGNNDLLI LSRPDVIGAI EKAYLDAGAD ILETNTFNAT QVSQADYGMQ ALAYELNVEG ARLARKVADA KTLETPDKPR FVAGVLGPTS RTCSLSPDVN NPGYRNVTFD ELVENYTEAT KGLIEGGSDL ILIETIFDTL NAKAAIFAVQ GVFEELGIEL PIMISGTITD ASGRTLSGQT TEAFWNSVSH AKPISVGLNC ALGASELRPY LEELSNKAST YVSAHPNAGL PNEF // ID Q9CBY5_MYCLE Unreviewed; 293 AA. AC Q9CBY5; DT 01-JUN-2001, integrated into UniProtKB/TrEMBL. DT 01-JUN-2001, sequence version 1. DT 01-APR-2015, entry version 62. DE SubName: Full=Possible transferase {ECO:0000313|EMBL:CAC30428.1}; GN OrderedLocusNames=ML1478 {ECO:0000313|EMBL:CAC30428.1}; OS Mycobacterium leprae (strain TN). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=272631 {ECO:0000313|Proteomes:UP000000806}; RN [1] {ECO:0000313|EMBL:CAC30428.1, ECO:0000313|Proteomes:UP000000806} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TN {ECO:0000313|EMBL:CAC30428.1, RC ECO:0000313|Proteomes:UP000000806}; 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., Ganier T., Churcher C., Harris D., RA Mungall K., 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., Oliver, 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL583922; CAC30428.1; -; Genomic_DNA. DR PIR; G87093; G87093. DR RefSeq; NP_302039.1; NC_002677.1. DR RefSeq; WP_010908360.1; NC_002677.1. DR ProteinModelPortal; Q9CBY5; -. DR STRING; 272631.ML1478; -. DR EnsemblBacteria; CAC30428; CAC30428; CAC30428. DR GeneID; 909506; -. DR KEGG; mle:ML1478; -. DR PATRIC; 18055674; VBIMycLep78757_2770. DR Leproma; ML1478; -. DR HOGENOM; HOG000265278; -. DR KO; K00547; -. DR OMA; YGRSVTK; -. DR OrthoDB; EOG6C019S; -. DR Proteomes; UP000000806; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000806}; KW Reference proteome {ECO:0000313|Proteomes:UP000000806}; KW Transferase {ECO:0000313|EMBL:CAC30428.1}. SQ SEQUENCE 293 AA; 30779 MW; F3A62A3305863139 CRC64; MGLAVHSESV LINDGGLATE LEARGNDLSD PLWSARLLTD APQEIVAVHV AYFRAGATIA TTVSYQASFE GFAARGIGRD QAIRLMRRSV ALASAARDEI SAGGLCVAAS VGPYGAALAD GSEYRGRYGL SVAALARWHR PRLEVLADAG ADVLALETIP DIDEAEALVD LVRSVGVPAW LSYTINGTRT RAGQPLAEAF AVAAGVPKIV AVGVNCCAPD DVLAAIQIAN IGKPIIVYPN SGERWDYRTW TGPRRFSAQL ALQWTAAGAR IVGGCCRVRP ADIAELTKAL ASR // ID Q9EWH3_STRCO Unreviewed; 1170 AA. AC Q9EWH3; DT 01-MAR-2001, integrated into UniProtKB/TrEMBL. DT 01-MAR-2001, sequence version 1. DT 27-MAY-2015, entry version 101. DE SubName: Full=Putative methionine synthase {ECO:0000313|EMBL:CAC18788.1}; GN OrderedLocusNames=SCO1657 {ECO:0000313|EMBL:CAC18788.1}; 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 {ECO:0000313|Proteomes:UP000001973}; RN [1] {ECO:0000313|EMBL:CAC18788.1, ECO:0000313|Proteomes:UP000001973} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-471 / A3(2) / M145 RC {ECO:0000313|Proteomes:UP000001973}; 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., Oliver K., O'Neil S., RA Rabbinowitsch E., Rajandream M.A., Rutherford K., Rutter S., RA Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., RA Warren T., Wietzorrek A., Woodward J., 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AL939109; CAC18788.1; -; Genomic_DNA. DR RefSeq; NP_625932.1; NC_003888.3. DR RefSeq; WP_011027904.1; NC_003888.3. DR ProteinModelPortal; Q9EWH3; -. DR STRING; 100226.SCO1657; -. DR EnsemblBacteria; CAC18788; CAC18788; CAC18788. DR GeneID; 1097088; -. DR KEGG; sco:SCO1657; -. DR PATRIC; 23732920; VBIStrCoe124346_1674. DR HOGENOM; HOG000251408; -. DR InParanoid; Q9EWH3; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR PhylomeDB; Q9EWH3; -. DR Proteomes; UP000001973; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001973}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001973}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 238 238 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 304 304 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 305 305 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 748 748 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1170 AA; 128291 MW; 3FAC689591C41851 CRC64; MASSPSTPPA DTRTRVSALR EALATRVVVA DGAMGTMLQA QNPTLDDFQQ LEGCNEVLNL TRPDIVRSVH EEYFAAGVDC VETNTFGANH SALGEYDIPE RVHELSEAGA RVAREVADEF GARDGRQRWV LGSMGPGTKL PTLGHAPYTV LRDAYQRNAE GLVAGGADAL LVETTQDLLQ TKASVLGARR ALDVLGLDLP LIVSVTVETT GTMLLGSEIG AALTALEPLG IDMIGLNCAT GPAEMSEHLR YLARHSRIPL TCMPNAGLPV LGKDGAHYPL TAPELADAHE TFVREYGLSL VGGCCGTTPE HLRQVVERVR DTAPTARDPR PEPGAASLYQ TVPFRQDTSY LAIGERTNAN GSKKFREAML DGRWDDCVEM ARDQIREGAH MLDLCVDYVG RDGVADMEEL AGRFATASTL PIVLDSTEVD VIRAGLEKLG GRAVINSVNY EDGAGPESRF ARVTKLAREH GAALIALTID EVGQARTAEK KVEIAERLID DLTGNWGIHE SDILVDCLTF TICTGQEESR KDGLATIEGI RELKRRHPDV QTTLGLSNIS FGLNPAARIL LNSVFLDECV KAGLDSAIVH ASKILPIARF DEEQVTTALD LIYDRRREGY DPLQKLMQLF EGATAKSLKA SKAEELAALP LEERLKRRII DGEKNGLEQD LDEALRERPA LEIVNDTLLD GMKVVGELFG SGQMQLPFVL QSAEVMKTAV AHLEPHMEKT DDDGKGTIVL ATVRGDVHDI GKNLVDIILS NNGYNVVNLG IKQPVSAILE AADEHRADVI GMSGLLVKST VIMKENLEEL NQRKLAADYP VILGGAALTR AYVEQDLHEI YDGEVRYARD AFEGLRLMDA LIGIKRGVPG AKLPELKQRR VRAATVEIDE RPEEGHVRSD VATDNPVPTP PFRGTRVVKG IQLKEYASWL DEGALFKGQW GLKQARTGEG PSYEELVESE GRPRLRGLLD RLQTDNLLEA AVVYGYFPCV SKDDDLIVLD DDGNERTRFT FPRQRRGRRL CLADFFRPEE SGETDVVGFQ VVTVGSRIGE ETARMFEANA YRDYLELHGL SVQLAEALAE YWHARVRSEL GFAGEDPAEM EDMFALKYRG ARFSLGYGAC PDLEDRAKIA ALLEPERIGV HLSEEFQLHP EQSTDAIVIH HPEAKYFNAR // ID Q9KCE1_BACHD Unreviewed; 1146 AA. AC Q9KCE1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 27-MAY-2015, entry version 95. DE SubName: Full=5-methyltetrahydrofolate S-homocysteine methyltransferase {ECO:0000313|EMBL:BAB05349.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:BAB05349.1}; GN Name=metH {ECO:0000313|EMBL:BAB05349.1}; GN OrderedLocusNames=BH1630 {ECO:0000313|EMBL:BAB05349.1}; 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 {ECO:0000313|EMBL:BAB05349.1, ECO:0000313|Proteomes:UP000001258}; RN [1] {ECO:0000313|EMBL:BAB05349.1, ECO:0000313|Proteomes:UP000001258} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125 RC {ECO:0000313|Proteomes:UP000001258}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; BA000004; BAB05349.1; -; Genomic_DNA. DR PIR; F83853; F83853. DR RefSeq; NP_242496.1; NC_002570.2. DR RefSeq; WP_010897793.1; NC_002570.2. DR ProteinModelPortal; Q9KCE1; -. DR STRING; 272558.BH1630; -. DR EnsemblBacteria; BAB05349; BAB05349; BAB05349. DR KEGG; bha:BH1630; -. DR PATRIC; 18940374; VBIBacHal18977_1700. DR HOGENOM; HOG000251408; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; BHAL272558:GJC5-1714-MONOMER; -. DR Proteomes; UP000001258; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001258}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:BAB05349.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001258}; KW Transferase {ECO:0000313|EMBL:BAB05349.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 227 227 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 290 290 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 291 291 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 724 724 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1146 AA; 126581 MW; ACCF52BAF5DD9A30 CRC64; MTKSLFEQQL ERKIVILDGA MGTMLQAANL TADDFGGEEY EGCNEYLNET APHVVEDIHR AYLEAGADVI ATNTFGATDI VLDDYDLGYK AEELNICAVK IAKRVAEEFS TPDWPRFVAG AMGPTTKSLS VTGGATFEQL IESYRQQATG LIKGGADILL LETSQDMRNV KAAYLGLSQA QKELEVKLPL IISGTIEPMG TTLAGQNIEA FYLSLEHMNP VVVGLNCATG PEFMRDHLRS LSDLATCSVS CYPNAGLPDE EGNYHESPES LAAKLAGFAE KGWLNMVGGC CGTTPDHIRA LLDVMKQFEP RQPKGDHPHS VSGIEPLLYD DSMRPLFVGE RTNVIGSRKF KRLIEEEKYE EASEIARSQV KKGAHVIDVC LADPDRDEME DMEEFLKFVI NKVKVPLMID STDEKVIEQA LTYSQGKAII NSINLEDGEE RFEKVVPLVH KYGAAVVVGT IDEEGMAITA EKKLAVAKRS YDLLVNKYNI RPSDIIFDPL VFPVGTGDEQ YIGSANETVE GIRRIKEELP ECLTILGVSN VSFGLPPVGR EVLNAAYLYH CTQAGLDYAI VNTEKLERYA SISDEEKELS RKLLFETTDE TLAEFTAFYR GKKAEKKVET SNLTLEERLA NYIVEGSKDG LTEDLDKALA KYDDPLDIIN GPLMNGMDEV GRLFNNNELI VAEVLQSAEV MKASVAHLEP HMEKKADDHG KGKIILATVK GDVHDIGKNL VEIILSNNGF RIVNLGIKVT SNELIEAVAR ENPDAIGLSG LLVKSAQQMV LTAQDLKQQQ ISIPILVGGA ALTRKFTNTK IAPEYDGLVV YAKDAMNGLE LANKLMKPDE REKLAVSLHE AKEQANSRTQ MGGGGTAVAV KPTRSHVSTT VPVAVPPDVK PHILRHHSIA HLEPYINMQM LLGRHLGLQG KVSRLLAEKD EKALELKEKV DALLTRVKEE QLMEAHGMYQ FFPAQSDGDD IVIYDQTGTN EIERFHFPRQ NKEPYLCLAD FLRPVSSGEM DYVGFLAVTA GKGIRELGEQ AKEAGDYLFS HLIQATALEM AEGFAERVHQ LMRDKWGFPD SADFTMEERF AAKYRGIRVS FGYPACPDLD DQAKLFKLLK PGKIGIELTE GFMMEPEASV TAMVFAHPEA RYFNVL // ID Q9KCE2_BACHD Unreviewed; 618 AA. AC Q9KCE2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 01-APR-2015, entry version 87. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=BH1629 {ECO:0000313|EMBL:BAB05348.1}; 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 {ECO:0000313|EMBL:BAB05348.1, ECO:0000313|Proteomes:UP000001258}; RN [1] {ECO:0000313|EMBL:BAB05348.1, ECO:0000313|Proteomes:UP000001258} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125 RC {ECO:0000313|Proteomes:UP000001258}; 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 -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- 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; BAB05348.1; -; Genomic_DNA. DR PIR; E83853; E83853. DR RefSeq; NP_242495.1; NC_002570.2. DR RefSeq; WP_010897792.1; NC_002570.2. DR ProteinModelPortal; Q9KCE2; -. DR STRING; 272558.BH1629; -. DR EnsemblBacteria; BAB05348; BAB05348; BAB05348. DR KEGG; bha:BH1629; -. DR PATRIC; 18940372; VBIBacHal18977_1699. DR HOGENOM; HOG000028409; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR BioCyc; BHAL272558:GJC5-1713-MONOMER; -. DR Proteomes; UP000001258; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001258}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000001258}. SQ SEQUENCE 618 AA; 68412 MW; 914D3EA1D8838D84 CRC64; MTNLVEALKT NILVGDGAMG TLLYEQGIDR CFEELNVTDP EKIVAAHVAY VEAGADVIQT NTYAANRMKL AKYQLDDQVL EINRAAVRLA RKAAKQETFV LGTIGGIRSV QFEEVEIQEV QDVFLEQMKA LVSEGVDGLL LETFYDLEEA KLAVSLARSL TDLPVIAHLS IAEIGVLQGG KLLEEAFAEL EGLGADLVGI NCRMGPYQML RSLETVQLLD RAYYSAYPNA SLPDYRDGRL YYHSNPEYFY EMGKRFVQQG VRLLGGCCGT TPEHVRAFAK VVKGLKPVVS KPVRLEIKET LSSTGQKTAR EPLAEKVKKQ PSIIVELDPP KNLAIDRFVE GAAALKNAGV DAVTMADNSL ASPRVDNLAL GAIIQQQVGA RPLVHVTCRD RNLIGLQSHL MGLHALGMTD LLAITGDPTK VGDFPGATSV YDVTSFQLIS LIKQLNEGIS FSGKELGQKA NFSVGAAFNP NVRHLERAVQ RMEKKIEAGA DYFMTQPIYN EKQIEDIYEA TKHIEKPIYI GIMPLINGRN AEFLHNEVPG IKLTDQIRER MARAGEDRQK GEREGLAIAK SLLDVATHYF NGIYLITPFL RYGMTVDLTH YVKETHHQIR QPERSVQK // ID Q9MYZ4_PIG Unreviewed; 163 AA. AC Q9MYZ4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 29-OCT-2014, entry version 47. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:AAF76901.1}; DE Flags: Fragment; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; OC Sus. OX NCBI_TaxID=9823 {ECO:0000313|EMBL:AAF76901.1}; RN [1] {ECO:0000313|EMBL:AAF76901.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Yorkshire X Landrace {ECO:0000313|EMBL:AAF76901.1}; RA Vallee M., Palin M.F., Guay F., Beaudry D., Blouin R., Laforest J.P., RA Lessard M., Matte J.; RT "Effect of folic acid supplement, breed and parity of sows on folate RT metabolism gene expression in early pregnancy."; RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF276463; AAF76901.1; -; mRNA. DR UniGene; Ssc.15975; -. DR ProteinModelPortal; Q9MYZ4; -. DR STRING; 9823.ENSSSCP00000010817; -. DR eggNOG; COG1410; -. DR HOGENOM; HOG000251409; -. DR SABIO-RK; Q9MYZ4; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; FT NON_TER 1 1 {ECO:0000313|EMBL:AAF76901.1}. FT NON_TER 163 163 {ECO:0000313|EMBL:AAF76901.1}. SQ SEQUENCE 163 AA; 17372 MW; 3F1B59D934CC3A69 CRC64; KCSAGVARKA AEEISLQTGI KRFVAGALGP TNKTLSVSPS VEKPDYRNIT FDELVEAYKE QAKGLLDGGV DILLIETIFD TANAKAALFA VQKLFEEEYA PRPIFISGTI VDKSGRTLSG QTGEAFVISV SHADPLCIGL NCALGAAEMR PFIEIIGKCT TAY // ID Q9R2M5_PSEPU Unreviewed; 109 AA. AC Q9R2M5; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 29-OCT-2014, entry version 40. DE SubName: Full=MetH {ECO:0000313|EMBL:AAD41254.1}; DE Flags: Fragment; GN Name=metH {ECO:0000313|EMBL:AAD41254.1}; OS Pseudomonas putida (Arthrobacter siderocapsulatus). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=303 {ECO:0000313|EMBL:AAD41254.1}; RN [1] {ECO:0000313|EMBL:AAD41254.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=2440 {ECO:0000313|EMBL:AAD41254.1}; RA Junker F., Ramos J.L.; RT "Involvement of the cis/trans isomerase CtiT1 in solvent resistance."; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AAD41251.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DOT-T1E {ECO:0000313|EMBL:AAD41251.1}; RX PubMed=10482510; RA Junker F., Ramos J.L.; RT "Involvement of the cis/trans isomerase Cti in solvent resistance of RT Pseudomonas putida DOT-T1E."; RL J. Bacteriol. 181:5693-5700(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF110738; AAD41251.1; -; Genomic_DNA. DR EMBL; AF110739; AAD41254.1; -; Genomic_DNA. DR ProteinModelPortal; Q9R2M5; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 4: Predicted; FT NON_TER 109 109 {ECO:0000313|EMBL:AAD41254.1}. SQ SEQUENCE 109 AA; 12227 MW; FA817BE63DE07212 CRC64; MSDRSARLQA LQNALKERIL ILDGGMGTMI QSYRLEEHDY RGTRFADWPS DVKGNNDLLL LSRPDVIAAI EKAYLDAGAD ILETNTFNAT QISQADYGME SLVYELNVE // ID Q9RA53_THETH Unreviewed; 1014 AA. AC Q9RA53; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 27-MAY-2015, entry version 72. DE SubName: Full=5-methyltetrahydrofolate (Homocysteine methyltransferase) {ECO:0000313|EMBL:BAA88674.1}; DE Flags: Fragment; GN Name=metH {ECO:0000313|EMBL:BAA88674.1}; OS Thermus thermophilus. OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; OC Thermus. OX NCBI_TaxID=274 {ECO:0000313|EMBL:BAA88674.1}; RN [1] {ECO:0000313|EMBL:BAA88674.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HB27 {ECO:0000313|EMBL:BAA88674.1}; RX PubMed=16232856; RA Kosuge T., Gao D., Hoshino T.; RT "Analysis of the methionine biosynthetic pathway in the extremely RT thermophilic eubacterium Thermus thermophilus."; RL J. Biosci. Bioeng. 90:271-279(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; AB029371; BAA88674.1; -; Genomic_DNA. DR ProteinModelPortal; Q9RA53; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000313|EMBL:BAA88674.1}; KW Transferase {ECO:0000313|EMBL:BAA88674.1}. FT NON_TER 1 1 {ECO:0000313|EMBL:BAA88674.1}. SQ SEQUENCE 1014 AA; 111276 MW; 4B33FEE1CA4EAF4C CRC64; RAYKEAARGL LKGGVDLILL ETAQDILQVR CAVLAVREAM AEVGREVPLQ VQVTFEATGT MLVGTDEQAA LAALESLPVD VVGMNCATGP DLMDSKVRYF AEHSTRFVSC LPNAGLPRNE GGRVVYDLTP EELAKWHLKF VAEYGVNAVG GCCGTGPEHI RKVAEAVKGL APKPRPESFP PQVASLYQAV SLKQEASLFL VGERLNATGS KRFREMLFAR DLEGILALAR EQVEEGAHAL DLSVAWTGRD ELEDLRWLLP HLATALTVPV MVDSTSPEAM ELALKYLPGR VLLNSANLED GLERFDRVAS LAKAHGAALV VLAIDEKGMA KTREEKVRVA LRMYERLTEH HGLRPEDLLF DLLTFPITQG DEESRPLAKE TLLAIEELRE RLPGVGFVLR VSNVSFGLKP RARRVLNSVF LDEARKRGLT AAIVDAGKIL PISQIPEEAY ALALDLIYDR RKEGFDPLLA FMAYFEAHKE DPGKREDAFL ALPLLERLKR RVVEGRKQGL EADLEEALKA GHKPLDLING PLLAGMKEVG DLFGAGKMQL PFVLQAAEVM KRAVAYLEPH MEKKGEGKGT LVLATVKGDV HDIGKNLVDI ILSNNGYRVV NLGIKVPIEE ILKAVEAHKP HAVGMSGLLV KSTLVMKENL EYMRDRGYTL PVILGGAALT RSYVEELKAI YPNVYYAEDA FEGLRLMEEL TGHAPPELTR KAPARPKREA PKVAPRARPV GEAPAVPRPP FFGVRVEEGL DLATIAHYVN KLALYRGQWG YSRKGFPGRR GRPWWSGRRS LSSRGSSRRR WRKGGLNPRS STASSPWPGR GGASRLLPRD GGGAGALPLP PAKGRGPEPR GLLPPPVCRA FGGRGGLDAQ GGLPGGGRDV LGVQLVTMGE APSRKAQALF ASGAYQDYLF VHGFSVEMTE ALAEYWHKRM RQMWGIAHKD ATEIQKLFQQ GYQGARYSFG YPACPDLADQ AKLDRLMGFH RVGVHLTENF QLEPEHATSA LVVHHPEARY FSVD // ID Q9RVQ6_DEIRA Unreviewed; 1258 AA. AC Q9RVQ6; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 27-MAY-2015, entry version 102. DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AAF10543.1}; GN OrderedLocusNames=DR_0966 {ECO:0000313|EMBL:AAF10543.1}; 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 {ECO:0000313|EMBL:AAF10543.1, ECO:0000313|Proteomes:UP000002524}; RN [1] {ECO:0000313|EMBL:AAF10543.1, ECO:0000313|Proteomes:UP000002524} 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 {ECO:0000313|Proteomes:UP000002524}; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 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; AE000513; AAF10543.1; -; Genomic_DNA. DR PIR; D75453; D75453. DR RefSeq; NP_294690.1; NC_001263.1. DR RefSeq; WP_010887611.1; NC_001263.1. DR ProteinModelPortal; Q9RVQ6; -. DR SMR; Q9RVQ6; 660-902. DR STRING; 243230.DR_0966; -. DR EnsemblBacteria; AAF10543; AAF10543; DR_0966. DR GeneID; 1799423; -. DR KEGG; dra:DR_0966; -. DR PATRIC; 21629502; VBIDeiRad64572_1153. DR HOGENOM; HOG000251409; -. DR InParanoid; Q9RVQ6; -. DR KO; K00548; -. DR OMA; DYNSIMV; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; DRAD243230:GH46-992-MONOMER; -. DR Proteomes; UP000002524; Chromosome I. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000002524}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:AAF10543.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002524}; KW Transferase {ECO:0000313|EMBL:AAF10543.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 259 259 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 322 322 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 323 323 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 768 768 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. SQ SEQUENCE 1258 AA; 136689 MW; B995A488159BD485 CRC64; MSHHPEASAS ANPSINHQPS TITEAARQRI LILDGAWGTQ LQRANLTEAD FRWDEADPTR MYRGNFDLLQ LTKPDVIRAV HRAYFEAGAD IASTNTFNST TISQADYGTE ALAYAMNREG ARLAREVADE FEARDGKKRW VAGSVGPTNR TATLSPDVER PEFRNVTYDD LVAAYSEAIT GLMEGGADLL LIETVFDTLN AKAALFAAQD VFAAQGRELP VMLSGTITDA SGRTLSGQTP EAFAVSTEHA GLFSLGLNCA LGADLLRPHL RAIAANTEAL VSVHPNAGLP NAFGEYDETP EHTAAVLADF AREGLVNIVG GCCGTTPEHI KAIAEAVKDI PPRQALQLPP YLRLSGLEAF TLTPETNFVN VGERTNVTGS PKFSKAILAG DYDAGLKIAR QQVTNGAQIV DINFDEGMLD GEGAMVKFLN LLAGEPDISR VPLMLDSSKW EILEAGLRRV QGKAVVNSIS LKDGEARFLE RARLLRRYGA AAVVMAFDEQ GQADNLARRR EILGRAYRLL TEQADFPPQD IIFDPNVLTV ATGIEEHDRY ALDFIEATRW IKENLPAAKV SGGISNVSFS FRGNNHVREA MHAVFLYHAI RAGLDMGIVN AGMLAVYEDI EPELREAVED VILARRPDAT ERLLTLADRY KDIKRESAAQ SAWRDLPVQE RLRHALVQGV ADHVDEDAEA AYQELGSPLA VIEGPLMDGM NVVGDLFGAG KMFLPQVVKS ARVMKKAVAY LTPYLEAEKA ESSSKGKVLL ATVKGDVHDI GKNIVGVVLA CNGYQVTDLG VMVPGEKILD EAERLGADVI GLSGLITPSL DEMVNVAREM TRRGVKTPLL IGGATTSRAH TAVKIDPAYD GTVVHVLDAS RAVTVTNDLL TDEAAYAGRV QGEYDTLRER HGERQVRLIA LAEARARAPQ LSAAVPPAPH DLGRQVVEQP IAELLPFIDW TPFFIAWEMK GIYPGILTDP LRGEEARKLF ADAQALLEQV IADGSLRARG VIGLWPAHGD DIVLDDAAMG RGETLDFETH ELAAGREPLP NMPRLHTLRQ QRDQTTPNTA LADFVAEGGD HIGAFATAIF GAEELAQQFE AQHDDYNSIL VKAVADRLAE AFAEKLHRDV RVRHWGYAEG EALDNTDLIK ERYQGIRPAP GYPAQPDHTE KRTLFELLDA ESIGLRLTES CAMTPAAAVS GLYFAHPEAR YFAVGRIGRD QVENYAARKG WTVQEAERWL GPLLAYSAGP GPEASQKALG AELTGAQS // ID Q9VJ31_DROME Unreviewed; 331 AA. AC Q9VJ31; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 27-MAY-2015, entry version 106. DE SubName: Full=CG10623 protein {ECO:0000313|EMBL:CAL25775.1}; DE SubName: Full=CG10623, isoform A {ECO:0000313|EMBL:AAF53726.1}; DE EC=2.1.1.- {ECO:0000313|EMBL:AAF53726.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:AAF53726.1}; DE SubName: Full=CG10623, isoform B {ECO:0000313|EMBL:AHN54587.1}; DE EC=2.1.1.- {ECO:0000313|EMBL:AHN54587.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:AHN54587.1}; DE SubName: Full=CG10623, isoform C {ECO:0000313|EMBL:AHN54588.1}; DE EC=2.1.1.- {ECO:0000313|EMBL:AHN54588.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:AHN54588.1}; DE SubName: Full=CG10623-PA {ECO:0000313|EMBL:CAR93715.1}; DE SubName: Full=GM29503p {ECO:0000313|EMBL:AAM50732.1}; GN ORFNames=CG10623 {ECO:0000313|EMBL:AAF53726.1, GN ECO:0000313|FlyBase:FBgn0032727}, GN Dmel_CG10623 {ECO:0000313|EMBL:AAF53726.1}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000313|EMBL:AAF53726.1, ECO:0000313|Proteomes:UP000000803}; RN [1] {ECO:0000313|EMBL:AAF53726.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., RA Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] {ECO:0000313|EMBL:AAF53726.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537568; RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A., RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A., RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R., RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J., RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C., RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.; RT "Finishing a whole-genome shotgun: release 3 of the Drosophila RT melanogaster euchromatic genome sequence."; RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002). RN [3] {ECO:0000313|EMBL:AAF53726.1, ECO:0000313|Proteomes:UP000000803} RP GENOME REANNOTATION. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] {ECO:0000313|EMBL:AAF53726.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537573; RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R., RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., RA Ashburner M., Celniker S.E.; RT "The transposable elements of the Drosophila melanogaster euchromatin: RT a genomics perspective."; RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002). RN [5] {ECO:0000313|EMBL:AAF53726.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537574; RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., RA Karpen G.H.; RT "Heterochromatic sequences in a Drosophila whole-genome shotgun RT assembly."; RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002). RN [6] {ECO:0000313|EMBL:AAM50732.1} RP NUCLEOTIDE SEQUENCE. RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R., Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.; RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000313|EMBL:AAF53726.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022; RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D., RA Ashburner M., Anxolabehere D.; RT "Combined evidence annotation of transposable elements in genome RT sequences."; RL PLoS Comput. Biol. 1:166-175(2005). RN [8] {ECO:0000313|EMBL:CAL25775.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ZBMEL131 {ECO:0000313|EMBL:CAL25775.1}, RC ZBMEL157 {ECO:0000313|EMBL:CAL25777.1}, RC ZBMEL191 {ECO:0000313|EMBL:CAL25779.1}, and RC ZBMEL229 {ECO:0000313|EMBL:CAL25780.1}; RX PubMed=16951084; DOI=10.1534/genetics.106.058008; RA Proeschel M., Zhang Z., Parsch J.; RT "Widespread adaptive evolution of Drosophila genes with sex-biased RT expression."; RL Genetics 174:893-900(2006). RN [9] {ECO:0000313|EMBL:AAF53726.1} RP NUCLEOTIDE SEQUENCE. RA Celniker S., Carlson J., Wan K., Frise E., Hoskins R., Park S., RA Svirskas R., Rubin G.; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. RN [10] {ECO:0000313|EMBL:AAF53726.1} RP NUCLEOTIDE SEQUENCE. RG Berkeley Drosophila Genome Project; RA Celniker S., Carlson J., Wan K., Pfeiffer B., Frise E., George R., RA Hoskins R., Stapleton M., Pacleb J., Park S., Svirskas R., Smith E., RA Yu C., Rubin G.; RT "Drosophila melanogaster release 4 sequence."; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. RN [11] {ECO:0000313|EMBL:AAF53726.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569856; DOI=10.1126/science.1139815; RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.; RT "The Release 5.1 annotation of Drosophila melanogaster RT heterochromatin."; RL Science 316:1586-1591(2007). RN [12] {ECO:0000313|EMBL:AAF53726.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569867; DOI=10.1126/science.1139816; RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M., RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A., RA Dimitri P., Karpen G.H., Celniker S.E.; RT "Sequence finishing and mapping of Drosophila melanogaster RT heterochromatin."; RL Science 316:1625-1628(2007). RN [13] {ECO:0000313|EMBL:CAR93715.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MEL15 {ECO:0000313|EMBL:CAR93715.1}, and RC MEL17 {ECO:0000313|EMBL:CAR93717.1}; RX PubMed=19126864; DOI=10.1093/molbev/msn297; RA Parsch J., Zhang Z., Baines J.F.; RT "The influence of demography and weak selection on the McDonald- RT Kreitman test: an empirical study in Drosophila."; RL Mol. Biol. Evol. 26:691-698(2009). RN [14] {ECO:0000313|EMBL:AAF53726.1} RP NUCLEOTIDE SEQUENCE. RG FlyBase; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. RN [15] {ECO:0000313|EMBL:CAL25775.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ZBMEL131 {ECO:0000313|EMBL:CAL25775.1}, RC ZBMEL157 {ECO:0000313|EMBL:CAL25777.1}, RC ZBMEL191 {ECO:0000313|EMBL:CAL25779.1}, and RC ZBMEL229 {ECO:0000313|EMBL:CAL25780.1}; RA Proeschel M., Zhang Z., Parsch J.; RT "Widespread adaptive evolution of Drosophila genes with sex-biased RT expression."; RL Genetics 0:0-0(0). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE014134; AAF53726.1; -; Genomic_DNA. DR EMBL; AY118872; AAM50732.1; -; mRNA. DR EMBL; AE014134; AHN54587.1; -; Genomic_DNA. DR EMBL; AE014134; AHN54588.1; -; Genomic_DNA. DR EMBL; AM294641; CAL25775.1; -; Genomic_DNA. DR EMBL; AM294643; CAL25777.1; -; Genomic_DNA. DR EMBL; AM294645; CAL25779.1; -; Genomic_DNA. DR EMBL; AM294646; CAL25780.1; -; Genomic_DNA. DR EMBL; FM245789; CAR93715.1; -; Genomic_DNA. DR EMBL; FM245791; CAR93717.1; -; Genomic_DNA. DR RefSeq; NP_001286073.1; NM_001299144.1. DR RefSeq; NP_001286074.1; NM_001299145.1. DR RefSeq; NP_609921.1; NM_136077.2. DR UniGene; Dm.13519; -. DR ProteinModelPortal; Q9VJ31; -. DR SMR; Q9VJ31; 48-331. DR MINT; MINT-923852; -. DR STRING; 7227.FBpp0080731; -. DR EnsemblMetazoa; FBtr0081190; FBpp0080731; FBgn0032727. DR EnsemblMetazoa; FBtr0344844; FBpp0311159; FBgn0032727. DR EnsemblMetazoa; FBtr0344845; FBpp0311160; FBgn0032727. DR GeneID; 35153; -. DR KEGG; dme:Dmel_CG10623; -. DR UCSC; CG10623-RA; d. melanogaster. DR FlyBase; FBgn0032727; CG10623. DR GeneTree; ENSGT00510000049619; -. DR OMA; SSVEGFM; -. DR OrthoDB; EOG7GQXW0; -. DR PhylomeDB; Q9VJ31; -. DR GenomeRNAi; 35153; -. DR NextBio; 792127; -. DR Proteomes; UP000000803; Chromosome 2L. DR ExpressionAtlas; Q9VJ31; differential. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IBA:GO_Central. DR GO; GO:0033528; P:S-methylmethionine cycle; IBA:GO_Central. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000000803}; KW Methyltransferase {ECO:0000313|EMBL:AAF53726.1}; KW Proteomics identification {ECO:0000213|PeptideAtlas:Q9VJ31}; KW Reference proteome {ECO:0000313|Proteomes:UP000000803}; KW Transferase {ECO:0000313|EMBL:AAF53726.1}. SQ SEQUENCE 331 AA; 36682 MW; CAE7E21C9E5BBFFD CRC64; MEVNQKWNWD TKPILVKCGG FSSQLAKNVT EKVDGDPLWG SRFDATNPEA VIQTHLDFLR NGADIILTNT YQSSVEGFVK YLGVTRERGV ELIQKSVQLA KQAKEQYLSE IGSEAESALP LIMGSIGPYG AYLHDGSEYT GNYADKMSKE ELRAWHKTRI EICLAAGVDG LALETLPCLM EAEAVTELVL DNFPDAKFWV SLQCMDEKHM ASGENFAEAA LSLWRLVQSR KAENRLLGIG LNCVNPLFVT PLLSSLTKVA GSDRIPLVVY SNRGEIYDVE QGDWTGTGEE VVKFVPEWIQ LGVRIVGGCC RVYPTDVLAI RKYVDGLNIK P // ID Q9VJ32_DROME Unreviewed; 331 AA. AC Q9VJ32; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 27-MAY-2015, entry version 113. DE SubName: Full=CG10621, isoform B {ECO:0000313|EMBL:AHN54585.1}; DE EC=2.1.1.- {ECO:0000313|EMBL:AHN54585.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:AHN54585.1}; DE SubName: Full=CG10621, isoform C {ECO:0000313|EMBL:AHN54586.1}; DE EC=2.1.1.- {ECO:0000313|EMBL:AHN54586.1}; DE EC=2.1.1.10 {ECO:0000313|EMBL:AHN54586.1}; DE SubName: Full=CG10621-PA {ECO:0000313|EMBL:AAF53725.1}; DE SubName: Full=FI01821p {ECO:0000313|EMBL:ABV82186.1}; GN ORFNames=CG10621 {ECO:0000313|EMBL:AAF53725.1, GN ECO:0000313|FlyBase:FBgn0032726}, GN Dmel_CG10621 {ECO:0000313|EMBL:AAF53725.1}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000313|EMBL:AAF53725.1, ECO:0000313|Proteomes:UP000000803}; RN [1] {ECO:0000313|EMBL:AAF53725.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., RA Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] {ECO:0000313|EMBL:AAF53725.1} RP NUCLEOTIDE SEQUENCE. RG Berkeley Drosophila Genome Project; RA Celniker S., Carlson J., Wan K., Pfeiffer B., Frise E., George R., RA Hoskins R., Stapleton M., Pacleb J., Park S., Svirskas R., Smith E., RA Yu C., Rubin G.; RT "Drosophila melanogaster release 4 sequence."; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:AAF53725.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537568; RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A., RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A., RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R., RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J., RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C., RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.; RT "Finishing a whole-genome shotgun: release 3 of the Drosophila RT melanogaster euchromatic genome sequence."; RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002). RN [4] {ECO:0000313|EMBL:AAF53725.1, ECO:0000313|Proteomes:UP000000803} RP GENOME REANNOTATION. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] {ECO:0000313|EMBL:AAF53725.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537573; RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R., RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., RA Ashburner M., Celniker S.E.; RT "The transposable elements of the Drosophila melanogaster euchromatin: RT a genomics perspective."; RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002). RN [6] {ECO:0000313|EMBL:AHN54585.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537574; RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., RA Karpen G.H.; RT "Heterochromatic sequences in a Drosophila whole-genome shotgun RT assembly."; RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002). RN [7] {ECO:0000313|EMBL:AHN54585.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022; RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D., RA Ashburner M., Anxolabehere D.; RT "Combined evidence annotation of transposable elements in genome RT sequences."; RL PLoS Comput. Biol. 1:166-175(2005). RN [8] {ECO:0000313|EMBL:AAF53725.1} RP NUCLEOTIDE SEQUENCE. RG FlyBase; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [9] {ECO:0000313|EMBL:AHN54585.1} RP NUCLEOTIDE SEQUENCE. RA Celniker S., Carlson J., Wan K., Frise E., Hoskins R., Park S., RA Svirskas R., Rubin G.; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. RN [10] {ECO:0000313|EMBL:AHN54585.1} RP NUCLEOTIDE SEQUENCE. RG Berkeley Drosophila Genome Project; RA Celniker S., Carlson J., Wan K., Pfeiffer B., Frise E., George R., RA Hoskins R., Stapleton M., Pacleb J., Park S., Svirskas R., Smith E., RA Yu C., Rubin G.; RT "Drosophila melanogaster release 4 sequence."; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. RN [11] {ECO:0000313|EMBL:AHN54585.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569856; DOI=10.1126/science.1139815; RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.; RT "The Release 5.1 annotation of Drosophila melanogaster RT heterochromatin."; RL Science 316:1586-1591(2007). RN [12] {ECO:0000313|EMBL:AHN54585.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569867; DOI=10.1126/science.1139816; RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M., RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A., RA Dimitri P., Karpen G.H., Celniker S.E.; RT "Sequence finishing and mapping of Drosophila melanogaster RT heterochromatin."; RL Science 316:1625-1628(2007). RN [13] {ECO:0000313|EMBL:ABV82186.1} RP NUCLEOTIDE SEQUENCE. RA Stapleton M., Carlson J., Frise E., Kapadia B., Park S., Wan K., RA Yu C., Celniker S.; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. RN [14] {ECO:0000313|EMBL:AHN54585.1} RP NUCLEOTIDE SEQUENCE. RG FlyBase; RL Submitted (JUL-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; AE003661; AAF53725.1; -; Genomic_DNA. DR EMBL; BT030804; ABV82186.1; -; mRNA. DR EMBL; AE014134; AHN54585.1; -; Genomic_DNA. DR EMBL; AE014134; AHN54586.1; -; Genomic_DNA. DR RefSeq; NP_001286071.1; NM_001299142.1. DR RefSeq; NP_001286072.1; NM_001299143.1. DR RefSeq; NP_609920.1; NM_136076.4. DR UniGene; Dm.10781; -. DR ProteinModelPortal; Q9VJ32; -. DR SMR; Q9VJ32; 4-330. DR MINT; MINT-853631; -. DR EnsemblMetazoa; FBtr0081191; FBpp0080732; FBgn0032726. DR EnsemblMetazoa; FBtr0342926; FBpp0309709; FBgn0032726. DR EnsemblMetazoa; FBtr0342927; FBpp0309710; FBgn0032726. DR GeneID; 35152; -. DR KEGG; dme:Dmel_CG10621; -. DR UCSC; CG10621-RA; d. melanogaster. DR FlyBase; FBgn0032726; CG10621. DR GeneTree; ENSGT00510000049619; -. DR KO; K00547; -. DR OMA; QCKDENT; -. DR PhylomeDB; Q9VJ32; -. DR ChiTaRS; CG10621; fly. DR GenomeRNAi; 35152; -. DR NextBio; 792122; -. DR Proteomes; UP000000803; Chromosome 2L. DR ExpressionAtlas; Q9VJ32; differential. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IBA:GO_Central. DR GO; GO:0033528; P:S-methylmethionine cycle; IBA:GO_Central. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Complete proteome {ECO:0000313|Proteomes:UP000000803}; KW Methyltransferase {ECO:0000313|EMBL:AHN54585.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000803}; KW Transferase {ECO:0000313|EMBL:AHN54585.1}. SQ SEQUENCE 331 AA; 36757 MW; 69860CA4C4D82371 CRC64; MGLTRVLVKD GGFGTQMTVH VGDSVDGDPL WSARFNATNP AAIISTHLDF LQNGADIILT NTYQSSVDGY MEYLELDEEQ SIELIKNTVR LAHIAKERYL TECYQAQLSV QEGYPLIIAS IGPFGAHLHD GSEYTGSYAD FVPAKEITDW HRVRIEACLE AGVDALAIET IPCQMEAEAL VEMLCDDYPD VKFWVAFQCK DENTLAHGET FADAANAIWD LLAERNAQDK CLAIGVNCVH PKFVTPLFKS LNGDREVGEQ IPLVVYPNSG EVYDVVNGWQ GREHCVPLAN YVPEWAQLGA KVIGGCCRTY ARDIRHIGEA IRDWNKLKKL S // ID Q9WYA5_THEMA Unreviewed; 768 AA. AC Q9WYA5; G4FHI2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 27-MAY-2015, entry version 106. DE SubName: Full=5-methyltetrahydrofolate S-homocysteine methyltransferase {ECO:0000313|EMBL:AAD35357.1}; DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AGL49192.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AGL49192.1}; GN OrderedLocusNames=TM_0268 {ECO:0000313|EMBL:AAD35357.1}; GN ORFNames=Tmari_0266 {ECO:0000313|EMBL:AGL49192.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35357.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35357.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099, and RC MSB8 {ECO:0000313|EMBL:AAD35357.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:1Q7M, ECO:0000213|PDB:1Q7Q, ECO:0000213|PDB:1Q7Z} RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-566, AND DISULFIDE BONDS. RX PubMed=14752199; DOI=10.1073/pnas.0308082100; RA Evans J.C., Huddler D.P., Hilgers M.T., Romanchuk G., Matthews R.G., RA Ludwig M.L.; RT "Structures of the N-terminal modules imply large domain motions RT during catalysis by methionine synthase."; RL Proc. Natl. Acad. Sci. U.S.A. 101:3729-3736(2004). RN [3] {ECO:0000213|PDB:3BOF, ECO:0000213|PDB:3BOL} RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-566 IN COMPLEX WITH ZINC. RX PubMed=18296644; DOI=10.1073/pnas.0709960105; RA Koutmos M., Pejchal R., Bomer T.M., Matthews R.G., Smith J.L., RA Ludwig M.L.; RT "Metal active site elasticity linked to activation of homocysteine in RT methionine synthases."; RL Proc. Natl. Acad. Sci. U.S.A. 105:3286-3291(2008). RN [4] {ECO:0000313|EMBL:AGL49192.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183, RC ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49192.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(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; AE000512; AAD35357.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49192.1; -; Genomic_DNA. DR PIR; B72397; B72397. DR RefSeq; NP_228081.1; NC_000853.1. DR RefSeq; WP_004082972.1; NC_023151.1. DR RefSeq; YP_007976617.1; NC_021214.1. DR RefSeq; YP_008990758.1; NC_023151.1. DR PDB; 1Q7M; X-ray; 2.10 A; A/B=1-566. DR PDB; 1Q7Q; X-ray; 3.10 A; A/B=1-566. DR PDB; 1Q7Z; X-ray; 1.70 A; A/B=1-566. DR PDB; 1Q85; X-ray; 2.00 A; A/B=1-566. DR PDB; 1Q8A; X-ray; 1.70 A; A/B=1-566. DR PDB; 1Q8J; X-ray; 1.90 A; A/B=1-566. DR PDB; 3BOF; X-ray; 1.70 A; A/B=1-566. DR PDB; 3BOL; X-ray; 1.85 A; A/B=1-566. DR PDBsum; 1Q7M; -. DR PDBsum; 1Q7Q; -. DR PDBsum; 1Q7Z; -. DR PDBsum; 1Q85; -. DR PDBsum; 1Q8A; -. DR PDBsum; 1Q8J; -. DR PDBsum; 3BOF; -. DR PDBsum; 3BOL; -. DR ProteinModelPortal; Q9WYA5; -. DR SMR; Q9WYA5; 1-565. DR STRING; 243274.TM0268; -. DR EnsemblBacteria; AAD35357; AAD35357; TM_0268. DR EnsemblBacteria; AGL49192; AGL49192; Tmari_0266. DR EnsemblBacteria; AHD17968; AHD17968; THEMA_03385. DR GeneID; 897179; -. DR KEGG; tma:TM0268; -. DR KEGG; tmi:THEMA_03385; -. DR KEGG; tmm:Tmari_0266; -. DR PATRIC; 23935413; VBITheMar51294_0272. DR KO; K00548; -. DR OMA; EPNAGKP; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; TMAR243274:GC6P-281-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Metal-binding; Methyltransferase {ECO:0000313|EMBL:AAD35357.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AAD35357.1}; Zinc. FT METAL 207 207 Zinc. FT METAL 234 234 Zinc. {ECO:0000213|PDB:3BOL}. FT METAL 272 272 Zinc. FT METAL 273 273 Zinc. FT DISULFID 207 272 {ECO:0000213|PDB:1Q7M, FT ECO:0000213|PDB:1Q7Q}. SQ SEQUENCE 768 AA; 85704 MW; 39E1A42EDE37A26C CRC64; MRNRREVSKL LSERVLLLDG AYGTEFMKYG YDDLPEELNI KAPDVVLKVH RSYIESGSDV ILTNTFGATR MKLRKHGLED KLDPIVRNAV RIARRAAGEK LVFGDIGPTG ELPYPLGSTL FEEFYENFRE TVEIMVEEGV DGIIFETFSD ILELKAAVLA AREVSRDVFL IAHMTFDEKG RSLTGTDPAN FAITFDELDI DALGINCSLG PEEILPIFQE LSQYTDKFLV VEPNAGKPIV ENGKTVYPLK PHDFAVHIDS YYELGVNIFG GCCGTTPEHV KLFRKVLGNR KPLQRKKKRI FAVSSPSKLV TFDHFVVIGE RINPAGRKKL WAEMQKGNEE IVIKEAKTQV EKGAEVLDVN FGIESQIDVR YVEKIVQTLP YVSNVPLSLD IQNVDLTERA LRAYPGRSLF NSAKVDEEEL EMKINLLKKY GGTLIVLLMG KDVPKSFEER KEYFEKALKI LERHDFSDRV IFDPGVLPLG AEGKPVEVLK TIEFISSKGF NTTVGLSNLS FGLPDRSYYN TAFLVLGISK GLSSAIMNPL DETLMKTLNA TLVILEKKEL PRAEVKEEKL VEIILSGNRS ELEKLVEDFL KEKDPLSVIE EHLRPAMERI GELYDKGKIF LPQLILAAQT VKPVFDKLTS MLPSDSQGET FVIATVKGDV HDIGKNIVAS VIRSSGYRVV DLGKDVDTSE IVEAVEKERP VALGLSAMMT TTVGRIKEVV EKLKEKNLKI PVIVGGASLN EKLAKELGAD YYAKNASEAV KILKSLGR // ID SAM4_YEAST Reviewed; 325 AA. AC Q08985; D6W397; DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 29-APR-2015, entry version 100. DE RecName: Full=Homocysteine S-methyltransferase 2; DE EC=2.1.1.10; DE AltName: Full=S-adenosylmethionine metabolism protein 4; DE AltName: Full=S-methylmethionine:homocysteine methyltransferase 2; DE Short=SMM:Hcy S-methyltransferase 2; GN Name=SAM4; OrderedLocusNames=YPL273W; 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 [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 [2] 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). RN [3] RP FUNCTION, AND INDUCTION. RX PubMed=11013242; DOI=10.1074/jbc.M005967200; RA Thomas D., Becker A., Surdin-Kerjan Y.; RT "Reverse methionine biosynthesis from S-adenosylmethionine in RT eukaryotic cells."; RL J. Biol. Chem. 275:40718-40724(2000). RN [4] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [5] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-138, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth RT phosphoproteome analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). CC -!- FUNCTION: Homocysteine S-methyltransferase involved in the CC conversion of S-adenosylmethionine (AdoMet) to methionine to CC control the methionine/AdoMet ratio. Converts also S- CC methylmethionine (SMM) to methionine. CC {ECO:0000269|PubMed:11013242}. CC -!- CATALYTIC ACTIVITY: S-methyl-L-methionine + L-homocysteine = 2 L- CC methionine. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00333}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. CC Nucleus {ECO:0000269|PubMed:14562095}. CC -!- INDUCTION: Up-regulated in response to high extracellular CC methionine. {ECO:0000269|PubMed:11013242}. CC -!- MISCELLANEOUS: Present with 60300 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z73629; CAA98009.1; -; Genomic_DNA. DR EMBL; BK006949; DAA11163.1; -; Genomic_DNA. DR PIR; S65306; S65306. DR RefSeq; NP_015050.1; NM_001184087.1. DR ProteinModelPortal; Q08985; -. DR SMR; Q08985; 15-315. DR BioGrid; 35940; 14. DR MINT; MINT-4505729; -. DR STRING; 4932.YPL273W; -. DR MaxQB; Q08985; -. DR PaxDb; Q08985; -. DR PeptideAtlas; Q08985; -. DR EnsemblFungi; YPL273W; YPL273W; YPL273W. DR GeneID; 855855; -. DR KEGG; sce:YPL273W; -. DR CYGD; YPL273w; -. DR EuPathDB; FungiDB:YPL273W; -. DR SGD; S000006194; SAM4. DR eggNOG; COG2040; -. DR GeneTree; ENSGT00510000049619; -. DR HOGENOM; HOG000066018; -. DR InParanoid; Q08985; -. DR KO; K00547; -. DR OMA; QCKDENT; -. DR OrthoDB; EOG7X9GHR; -. DR BioCyc; YEAST:YPL273W-MONOMER; -. DR NextBio; 980460; -. DR PRO; PR:Q08985; -. DR Proteomes; UP000002311; Chromosome XVI. DR Genevestigator; Q08985; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IDA:SGD. DR GO; GO:0050667; P:homocysteine metabolic process; IDA:SGD. DR GO; GO:0019284; P:L-methionine biosynthetic process from S-adenosylmethionine; IDA:SGD. DR GO; GO:0046498; P:S-adenosylhomocysteine metabolic process; IDA:SGD. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 1: Evidence at protein level; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; Metal-binding; KW Methionine biosynthesis; Methyltransferase; Nucleus; Phosphoprotein; KW Reference proteome; S-adenosyl-L-methionine; Transferase; Zinc. FT CHAIN 1 325 Homocysteine S-methyltransferase 2. FT /FTId=PRO_0000114619. FT DOMAIN 6 321 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 239 239 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 306 306 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 307 307 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT MOD_RES 138 138 Phosphothreonine. FT {ECO:0000269|PubMed:18407956}. SQ SEQUENCE 325 AA; 36669 MW; 54658C7B92A610F0 CRC64; MARLPLKQFL ADNPKKVLVL DGGQGTELEN RGIKVANPVW STIPFISESF WSDESSANRK IVKEMFNDFL NAGAEILMTT TYQTSYKSVS ENTPIRTLSE YNNLLNRIVD FSRNCIGEDK YLIGCIGPWG AHICREFTGD YGAEPENIDF YQYFKPQLEN FNKNDKLDLI GFETIPNIHE LKAILSWDES ILSRPFYIGL SVHEHGVLRD GTTMEEIAQV IKDLGDKINP NFSFLGINCV SFNQSPDILE SLHQALPNMA LLAYPNSGEV YDTEKKIWLP NSDKLNSWDT VVKQYISSGA RIIGGCCRTS PKDIQEISAA VKKYT // ID SMTA_ASTBI Reviewed; 338 AA. AC P56707; Q9ZRT7; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1999, sequence version 1. DT 01-APR-2015, entry version 51. DE RecName: Full=Selenocysteine methyltransferase; DE Short=SECYS-MT; DE Short=SECYS-methyltransferase; DE EC=2.1.1.280; GN Name=SMTA; OS Astragalus bisulcatus (Two-grooved milkvetch) (Phaca bisulcata). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; OC Galegeae; Astragalus. OX NCBI_TaxID=20406; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 80-100; 126-135; RP 170-184; 189-202; 214-232; 264-179 AND 282-300, IDENTIFICATION OF RP METHYL DONOR, AND TISSUE SPECIFICITY. RX PubMed=10026151; DOI=10.1074/jbc.274.9.5407; RA Neuhierl B., Thanbichler M., Lottspeich F., Boeck A.; RT "A family of S-methylmethionine-dependent thiol/selenol RT methyltransferases. Role in selenium tolerance and evolutionary RT relation."; RL J. Biol. Chem. 274:5407-5414(1999). RN [2] RP CATALYTIC ACTIVITY, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=8706715; DOI=10.1111/j.1432-1033.1996.0235u.x; RA Neuhierl B., Boeck A.; RT "On the mechanism of selenium tolerance in selenium-accumulating RT plants. Purification and characterization of a specific selenocysteine RT methyltransferase from cultured cells of Astragalus bisculatus."; RL Eur. J. Biochem. 239:235-238(1996). CC -!- FUNCTION: Catalyzes the methylation of selenocysteine with S- CC methylmethionine as donor. Does not methylate cysteine. CC -!- CATALYTIC ACTIVITY: S-methyl-L-methionine + L-selenocysteine = L- CC methionine + Se-methyl-L-selenocysteine. CC {ECO:0000269|PubMed:8706715}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00333}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.015 mM for S-adenosyl-L-methionine CC {ECO:0000269|PubMed:8706715}; CC KM=0.7 mM for L-selenocysteine {ECO:0000269|PubMed:8706715}; CC KM=0.35 mM for DL-selenohomocysteine CC {ECO:0000269|PubMed:8706715}; CC pH dependence: CC Optimum pH is 6.0. {ECO:0000269|PubMed:8706715}; CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8706715}. CC -!- TISSUE SPECIFICITY: Present in all tissues tested. CC {ECO:0000269|PubMed:10026151}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ131433; CAA10368.1; -; mRNA. DR PIR; T51940; T51940. DR ProteinModelPortal; P56707; -. DR BioCyc; MetaCyc:MONOMER-15257; -. DR BRENDA; 2.1.1.280; 557. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; Metal-binding; Methyltransferase; KW Transferase; Zinc. FT CHAIN 1 338 Selenocysteine methyltransferase. FT /FTId=PRO_0000114620. FT DOMAIN 1 327 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 245 245 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 312 312 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 313 313 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. SQ SEQUENCE 338 AA; 36714 MW; BDE604F49AFAF8A5 CRC64; MSSPLITDFL HQAGRAAVIA GGLGTELQRH GADLNDPLWS AKCLLSCPHL IRQVHLDYLE NGADIIITAS YQATIQGFKA KGFSDEEGEA LLRRSVEIAR EARDLYYQRC AESSSDNGDD SRILKQRPIL IAGSVGSYGA YLADGSEFSG NYGDAIKSET LKDFHRRKVQ ILADSGVDLL AFEAVPNKLE AQAYADLLEE ENIITPAWFA FTSKDGNNVV SGDSIEECGS IAESCDKVVA VGINCTPPRF IHDLILLLKK VTAKPIVIYP NSGETYDAIR KEWGQNSGVT DEDFVSYVDK WCESGASLVG GCCRTTPDTI RGIYKILSSG QSPTFSAK // ID SMTA_BRAOT Reviewed; 346 AA. AC Q4VNK0; DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 1. DT 01-APR-2015, entry version 26. DE RecName: Full=Selenocysteine Se-methyltransferase; DE Short=BoSMT; DE EC=2.1.1.280; GN Name=SMT; OS Brassica oleracea var. italica (Broccoli). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Brassiceae; OC Brassica. OX NCBI_TaxID=36774; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, RP BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION BY SELENATE AND SULFATE, RP ENZYME REGULATION, AND TISSUE SPECIFICITY. RC STRAIN=cv. Green comet; RX PubMed=15863700; DOI=10.1104/pp.104.056549; RA Lyi S.M., Heller L.I., Rutzke M., Welch R.M., Kochian L.V., Li L.; RT "Molecular and biochemical characterization of the selenocysteine Se- RT methyltransferase gene and Se-methylselenocysteine synthesis in RT broccoli."; RL Plant Physiol. 138:409-420(2005). RN [2] RP FUNCTION, AND CATALYTIC ACTIVITY. RC STRAIN=cv. Green comet; RX PubMed=17391716; DOI=10.1016/j.phytochem.2007.02.007; RA Lyi S.M., Zhou X., Kochian L.V., Li L.; RT "Biochemical and molecular characterization of the homocysteine S- RT methyltransferase from broccoli (Brassica oleracea var. italica)."; RL Phytochemistry 68:1112-1119(2007). CC -!- FUNCTION: Catalyzes the methylation of DL- and L-selenocysteine CC with S-methylmethionine as donor. Methylates also DL-homocysteine, CC DL- and L-cysteine in vitro. May be involved in selenium CC detoxification. {ECO:0000269|PubMed:15863700, CC ECO:0000269|PubMed:17391716}. CC -!- CATALYTIC ACTIVITY: S-methyl-L-methionine + L-selenocysteine = L- CC methionine + Se-methyl-L- selenocysteine. CC {ECO:0000269|PubMed:15863700, ECO:0000269|PubMed:17391716}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00333}; CC -!- ENZYME REGULATION: Inhibited by L-methionine. CC {ECO:0000269|PubMed:15863700}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 7.0. {ECO:0000269|PubMed:15863700}; CC -!- TISSUE SPECIFICITY: Expressed in roots, young leaves and florets, CC but not detected in plants not exposed to selenium. CC {ECO:0000269|PubMed:15863700}. CC -!- INDUCTION: Up-regulated by selenate, but not by selenite. Down- CC regulated by sulfate. {ECO:0000269|PubMed:15863700}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY817737; AAX20123.1; -; mRNA. DR BioCyc; MetaCyc:MONOMER-15249; -. DR BRENDA; 2.1.1.280; 947. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0016205; F:selenocysteine methyltransferase activity; IDA:UniProtKB. DR GO; GO:0032259; P:methylation; IDA:UniProtKB. DR GO; GO:0010269; P:response to selenium ion; IDA:UniProtKB. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 1: Evidence at protein level; KW Metal-binding; Methyltransferase; Transferase; Zinc. FT CHAIN 1 346 Selenocysteine Se-methyltransferase. FT /FTId=PRO_0000409375. FT DOMAIN 13 330 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT COMPBIAS 332 344 Ser-rich. FT METAL 248 248 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 315 315 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 316 316 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. SQ SEQUENCE 346 AA; 37863 MW; 50E11284D078FC8D CRC64; MVTGNTKAET FYSMKELLKE TGGYAIIDGG LATELERHGA DLNDPLWSAK CLLTSPHLIH TVHLDYLEAG ADIISSASYQ ATIQGFEAKG YSIEKSESLL RKSVEIACEA RSTYYDKCKD DDDKKILKKR PILVAASVGS YGAFLADGSE YSGIYGDLIT LETLKDFHRR RVQVLAESGA DIIAFETIPN KLEAQAFAEL LDEGVAKIPG WFSFNSKDGV NVVSGDSIKE CIAIAEACEK VVAVGINCTP PRFIEGLVLE IAKVTSKPIL VYPNSGERYD PERKEWVENT GVGNEDFVSY VEKWMDAGVS LLGGCCRTTP TTIRAIHKRL VSRRSLFSSS SSSSHH // ID YDM7_SCHPO Reviewed; 308 AA. AC P87138; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 29-APR-2015, entry version 77. DE RecName: Full=Uncharacterized protein C57A7.07c; GN ORFNames=SPAC57A7.07c; 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 [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 -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU329670; CAB08765.1; -; Genomic_DNA. DR PIR; T38947; T38947. DR RefSeq; NP_593374.1; NM_001018806.2. DR ProteinModelPortal; P87138; -. DR BioGrid; 278632; 5. DR STRING; 4896.SPAC57A7.07c-1; -. DR MaxQB; P87138; -. DR EnsemblFungi; SPAC57A7.07c.1; SPAC57A7.07c.1:pep; SPAC57A7.07c. DR GeneID; 2542156; -. DR KEGG; spo:SPAC57A7.07c; -. DR EuPathDB; FungiDB:SPAC57A7.07c; -. DR PomBase; SPAC57A7.07c; -. DR eggNOG; COG2040; -. DR InParanoid; P87138; -. DR OMA; EARELMW; -. DR OrthoDB; EOG79SF86; -. DR PhylomeDB; P87138; -. DR NextBio; 20803228; -. DR PRO; PR:P87138; -. DR Proteomes; UP000002485; Chromosome I. DR GO; GO:0005737; C:cytoplasm; ISO:PomBase. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; ISO:PomBase. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; ISO:PomBase. DR GO; GO:0033528; P:S-methylmethionine cycle; IBA:GO_Central. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome; Methyltransferase; Reference proteome; Transferase. FT CHAIN 1 308 Uncharacterized protein C57A7.07c. FT /FTId=PRO_0000114625. FT DOMAIN 1 307 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. SQ SEQUENCE 308 AA; 34542 MW; DC6AF257FC5262C3 CRC64; MLMLDGGSTA ILPKLPESIS ESRLWTSEAL VRYPEIVVKH HEEFLKVCDI ISTFTYQLDA SIYDEKVEGV PLKQVYANSI GLPVYAREHL GLPNKYIALC LGSHAATIPG CMEYKMIYDK PTDFEMLYNF HKNRIEAIQA SNPKAFEKID FIAFESLPHV TEAEVVCQLI QDMKGWSKRC WITCTCPERS TIERVSSIIS KILSINHDSI WGIGVNCFHL SLLEPIAKML SSLLPSNITA ILYPDGRGLY QNPDGTFSPG STDHPAPSPE EWSTITAKYS NLHNGNLILG GCCETNYNHL SLLREKTK // ID YITJ_BACSU Reviewed; 612 AA. AC O06745; Q796P9; DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 27-MAY-2015, entry version 95. DE RecName: Full=Bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase; DE Includes: DE RecName: Full=Homocysteine S-methyltransferase; DE EC=2.1.1.10; DE AltName: Full=S-methylmethionine:homocysteine methyltransferase; DE Includes: DE RecName: Full=5,10-methylenetetrahydrofolate reductase; DE EC=1.5.1.20; GN Name=yitJ; OrderedLocusNames=BSU11010; 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=9353932; RA Roche B., Autret S., Levine A., Vannier F., Medina N., Seror S.J.; RT "A Bacillus subtilis chromosome segment at the 100 degrees to 102 RT degrees position encoding 11 membrane proteins."; RL Microbiology 143:3309-3312(1997). 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 INDUCTION. RC STRAIN=168 / BR151; RX PubMed=10094622; DOI=10.1046/j.1365-2958.1998.01105.x; RA Grundy F.J., Henkin T.M.; RT "The S box regulon: a new global transcription termination control RT system for methionine and cysteine biosynthesis genes in Gram-positive RT bacteria."; RL Mol. Microbiol. 30:737-749(1998). CC -!- CATALYTIC ACTIVITY: S-methyl-L-methionine + L-homocysteine = 2 L- CC methionine. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00333}; CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC -!- INDUCTION: Induced by methionine starvation. CC {ECO:0000269|PubMed:10094622}. CC -!- SIMILARITY: In the C-terminal section; belongs to the CC methylenetetrahydrofolate reductase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y09476; CAA70665.1; -; Genomic_DNA. DR EMBL; AL009126; CAB12941.1; -; Genomic_DNA. DR PIR; C69840; C69840. DR RefSeq; NP_388982.1; NC_000964.3. DR RefSeq; WP_003245847.1; NZ_JNCM01000035.1. DR ProteinModelPortal; O06745; -. DR SMR; O06745; 2-393. DR STRING; 224308.BSU11010; -. DR PaxDb; O06745; -. DR EnsemblBacteria; CAB12941; CAB12941; BSU11010. DR GeneID; 939796; -. DR KEGG; bsu:BSU11010; -. DR PATRIC; 18973908; VBIBacSub10457_1148. DR GenoList; BSU11010; -. DR eggNOG; COG0685; -. DR HOGENOM; HOG000028409; -. DR InParanoid; O06745; -. DR KO; K00547; -. DR OMA; NEVPGIQ; -. DR OrthoDB; EOG6SNDP1; -. DR PhylomeDB; O06745; -. DR BioCyc; BSUB:BSU11010-MONOMER; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000001570; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02219; MTHFR; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 2: Evidence at transcript level; KW Amino-acid biosynthesis; Complete proteome; FAD; Flavoprotein; KW Metal-binding; Methionine biosynthesis; Methyltransferase; NAD; NADP; KW Oxidoreductase; Reference proteome; S-adenosyl-L-methionine; KW Transferase; Zinc. FT CHAIN 1 612 Bifunctional homocysteine S- FT methyltransferase/5,10- FT methylenetetrahydrofolate reductase. FT /FTId=PRO_0000379125. FT DOMAIN 1 280 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT REGION 1 280 Homocysteine S-methyltransferase. FT REGION 295 612 5,10-methylenetetrahydrofolate reductase. FT METAL 200 200 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 265 265 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. FT METAL 266 266 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. SQ SEQUENCE 612 AA; 67928 MW; A7B6FFC2E648F800 CRC64; MGLLEDLQRQ VLIGDGAMGT LLYSYGIDRC FEELNISKPE EIQRIHKAYV EAGANIIQTN TYGANYIKLS RHGLEDDIKK MNQEAVKIAR ASAGDAYVLG TMGGIRTFNK NAYSLDEIKR SFREQLYLLL HEEPDGLLLE TYYDLEEARE VLKIARKETD LPIMLNVSMH EQGVLQDGTP LSDALRSIAD LGADIVGINC RLGPYHMIEA LSEVPIFDDV FLSVYPNSSL PSLEEGRLVY ETDDTYFQNS ASEFRKQGAR IIGGCCGTTP NHIRAMAEAV GGLAPITEKE VKTRAKEFIS VHHERTEPGL DEIAAKKRSI IVELDPPKKL SFDKFLSAAA ELKEAGIDAL TLADNSLATP RISNVACGAL VKQQLDMRSL VHITCRDRNI IGLQSHLMGL DTLGLNDVLA ITGDPSKIGD FPGATSVYDL TSFDLIRLIK QFNEGLSLSG KPLGKKTNFS VAAAFNPNVR HLDKAVKRLE KKIDCGADYF VSQPVYSEQQ LVDIHNETKH LKTPIYIGIM PLTSSRNAEF IHNEIPGIKL SDTIREKMAH AGEDKEKQKA EGLAIARSLL DTACELFNGI YLITPFLRSD LTAELTSYIQ QKDEQRQNIF LH // ID YM99_YEAST Reviewed; 105 AA. AC Q04898; D6W0E8; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 29-APR-2015, entry version 82. DE RecName: Full=Putative uncharacterized protein YMR321C; GN OrderedLocusNames=YMR321C; ORFNames=YM9924.13C; 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 [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169872; RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., RA Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., RA Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome RT XIII."; RL Nature 387:90-93(1997). RN [2] 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 -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00333}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z54141; CAA90839.1; -; Genomic_DNA. DR EMBL; BK006946; DAA10222.1; -; Genomic_DNA. DR PIR; S69879; S69879. DR RefSeq; NP_014054.3; NM_001182834.3. DR ProteinModelPortal; Q04898; -. DR SMR; Q04898; 10-104. DR BioGrid; 35500; 1. DR STRING; 4932.YMR321C; -. DR EnsemblFungi; YMR321C; YMR321C; YMR321C. DR GeneID; 855371; -. DR KEGG; sce:YMR321C; -. DR CYGD; YMR321c; -. DR EuPathDB; FungiDB:YMR321C; -. DR SGD; S000004940; YMR321C. DR GeneTree; ENSGT00510000049619; -. DR InParanoid; Q04898; -. DR OrthoDB; EOG7X9GHR; -. DR BioCyc; YEAST:G3O-32984-MONOMER; -. DR NextBio; 979154; -. DR PRO; PR:Q04898; -. DR Proteomes; UP000002311; Chromosome XIII. DR Genevestigator; Q04898; -. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003726; S_MeTrfase. DR Pfam; PF02574; S-methyl_trans; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50970; HCY; 1. PE 3: Inferred from homology; KW Complete proteome; Methyltransferase; Reference proteome; Transferase. FT CHAIN 1 105 Putative uncharacterized protein YMR321C. FT /FTId=PRO_0000114626. FT DOMAIN 1 101 Hcy-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00333}. SQ SEQUENCE 105 AA; 11622 MW; 4A252F6A58DA6178 CRC64; MMDLGDKINP NLSFLGINCV SFNQSPDILE SLHQALPNMA LLAYPNSGEV YDTEKKIWLP NSDKLNSWDT VVKQYISSGA RIIGGCCRTS PKDIQEISAA VKKYT //